data_9FGE
# 
_entry.id   9FGE 
# 
_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   9FGE         pdb_00009fge 10.2210/pdb9fge/pdb 
WWPDB D_1292138814 ?            ?                   
# 
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 2025-01-15 
2 'Structure model' 1 1 2025-01-22 
3 'Structure model' 1 2 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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' '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 3 'Structure model' citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
3 3 'Structure model' '_citation.journal_volume'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FGE 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-23 
_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              andrea.mattevi@unipv.it 
_pdbx_contact_author.name_first         Andrea 
_pdbx_contact_author.name_last          Mattevi 
_pdbx_contact_author.name_mi            AM 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9523-7128 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Guerriere, T.B.' 1 0009-0003-3232-6822 
'Mattevi, A.'     2 0000-0002-9523-7128 
# 
_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            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1046 
_citation.page_last                 1060 
_citation.title                     
'Dehydrogenase versus oxidase function: the interplay between substrate binding and flavin microenvironment.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c05944 
_citation.pdbx_database_id_PubMed   39781101 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Guerriere, T.B.' 1  ? 
primary 'Vancheri, A.'    2  ? 
primary 'Ricotti, I.'     3  ? 
primary 'Serapian, S.A.'  4  ? 
primary 'Eggerichs, D.'   5  ? 
primary 'Tischler, D.'    6  ? 
primary 'Colombo, G.'     7  ? 
primary 'Mascotti, M.L.'  8  ? 
primary 'Fraaije, M.W.'   9  ? 
primary 'Mattevi, A.'     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 'FAD-binding oxidoreductase'    55207.992 2   ? ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'   785.550   2   ? ? ? ? 
3 non-polymer syn 4-hydroxy-3-methoxybenzaldehyde 152.147   2   ? ? ? ? 
4 non-polymer syn GLYCEROL                        92.094    2   ? ? ? ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'         106.120   1   ? ? ? ? 
6 water       nat water                           18.015    772 ? ? ? ? 
# 
_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       
;ADFAGAMKAFRGVVGAEWVFGDEEAVVPWSKTYIPDPAHQYKPVGAVCPQSVEEVQEIVRIANTYKQPLWTVSTGKNMGY
GMTAPATPGQVVLDLKRMNRILEVDADLGTCLLEPGVTYQQLKDYLEEHKIPLWIDVPDVGPIASPVGNTLDRGVGYTPY
GEHFMFQCGMEVCLPDGRLMRTGMGSIKGSTAWQAFKWGYGPYLDGLFTQSNFGIVTKMGLWLMPKPPVYKPFMVRHANM
EDVPKIIEAMRPLRVSNLVANCNLMMSASYQLAMFKRRNEIVPDGAPLDEASLKKAASANGLGMWNTYFALYGTEQTVAG
VEPIIRATLTASGGEVLTAAEMEGNPWFHHHQTLMQGGLNLDEVGLLRWRGAGGGLAWFAPVAAARGVEAERQTALAKEI
VEKHGFDYTAAYAIGWRDLHHIIALLFDKADPTQEQKADACYRELVTRFGAQGWASYRTGVNSMDLVAQQYGEVNRDFNR
TLKRAIDPNGILSPGKSGIHP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ADFAGAMKAFRGVVGAEWVFGDEEAVVPWSKTYIPDPAHQYKPVGAVCPQSVEEVQEIVRIANTYKQPLWTVSTGKNMGY
GMTAPATPGQVVLDLKRMNRILEVDADLGTCLLEPGVTYQQLKDYLEEHKIPLWIDVPDVGPIASPVGNTLDRGVGYTPY
GEHFMFQCGMEVCLPDGRLMRTGMGSIKGSTAWQAFKWGYGPYLDGLFTQSNFGIVTKMGLWLMPKPPVYKPFMVRHANM
EDVPKIIEAMRPLRVSNLVANCNLMMSASYQLAMFKRRNEIVPDGAPLDEASLKKAASANGLGMWNTYFALYGTEQTVAG
VEPIIRATLTASGGEVLTAAEMEGNPWFHHHQTLMQGGLNLDEVGLLRWRGAGGGLAWFAPVAAARGVEAERQTALAKEI
VEKHGFDYTAAYAIGWRDLHHIIALLFDKADPTQEQKADACYRELVTRFGAQGWASYRTGVNSMDLVAQQYGEVNRDFNR
TLKRAIDPNGILSPGKSGIHP
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE'   FAD 
3 4-hydroxy-3-methoxybenzaldehyde V55 
4 GLYCEROL                        GOL 
5 'DI(HYDROXYETHYL)ETHER'         PEG 
6 water                           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ASP n 
1 3   PHE n 
1 4   ALA n 
1 5   GLY n 
1 6   ALA n 
1 7   MET n 
1 8   LYS n 
1 9   ALA n 
1 10  PHE n 
1 11  ARG n 
1 12  GLY n 
1 13  VAL n 
1 14  VAL n 
1 15  GLY n 
1 16  ALA n 
1 17  GLU n 
1 18  TRP n 
1 19  VAL n 
1 20  PHE n 
1 21  GLY n 
1 22  ASP n 
1 23  GLU n 
1 24  GLU n 
1 25  ALA n 
1 26  VAL n 
1 27  VAL n 
1 28  PRO n 
1 29  TRP n 
1 30  SER n 
1 31  LYS n 
1 32  THR n 
1 33  TYR n 
1 34  ILE n 
1 35  PRO n 
1 36  ASP n 
1 37  PRO n 
1 38  ALA n 
1 39  HIS n 
1 40  GLN n 
1 41  TYR n 
1 42  LYS n 
1 43  PRO n 
1 44  VAL n 
1 45  GLY n 
1 46  ALA n 
1 47  VAL n 
1 48  CYS n 
1 49  PRO n 
1 50  GLN n 
1 51  SER n 
1 52  VAL n 
1 53  GLU n 
1 54  GLU n 
1 55  VAL n 
1 56  GLN n 
1 57  GLU n 
1 58  ILE n 
1 59  VAL n 
1 60  ARG n 
1 61  ILE n 
1 62  ALA n 
1 63  ASN n 
1 64  THR n 
1 65  TYR n 
1 66  LYS n 
1 67  GLN n 
1 68  PRO n 
1 69  LEU n 
1 70  TRP n 
1 71  THR n 
1 72  VAL n 
1 73  SER n 
1 74  THR n 
1 75  GLY n 
1 76  LYS n 
1 77  ASN n 
1 78  MET n 
1 79  GLY n 
1 80  TYR n 
1 81  GLY n 
1 82  MET n 
1 83  THR n 
1 84  ALA n 
1 85  PRO n 
1 86  ALA n 
1 87  THR n 
1 88  PRO n 
1 89  GLY n 
1 90  GLN n 
1 91  VAL n 
1 92  VAL n 
1 93  LEU n 
1 94  ASP n 
1 95  LEU n 
1 96  LYS n 
1 97  ARG n 
1 98  MET n 
1 99  ASN n 
1 100 ARG n 
1 101 ILE n 
1 102 LEU n 
1 103 GLU n 
1 104 VAL n 
1 105 ASP n 
1 106 ALA n 
1 107 ASP n 
1 108 LEU n 
1 109 GLY n 
1 110 THR n 
1 111 CYS n 
1 112 LEU n 
1 113 LEU n 
1 114 GLU n 
1 115 PRO n 
1 116 GLY n 
1 117 VAL n 
1 118 THR n 
1 119 TYR n 
1 120 GLN n 
1 121 GLN n 
1 122 LEU n 
1 123 LYS n 
1 124 ASP n 
1 125 TYR n 
1 126 LEU n 
1 127 GLU n 
1 128 GLU n 
1 129 HIS n 
1 130 LYS n 
1 131 ILE n 
1 132 PRO n 
1 133 LEU n 
1 134 TRP n 
1 135 ILE n 
1 136 ASP n 
1 137 VAL n 
1 138 PRO n 
1 139 ASP n 
1 140 VAL n 
1 141 GLY n 
1 142 PRO n 
1 143 ILE n 
1 144 ALA n 
1 145 SER n 
1 146 PRO n 
1 147 VAL n 
1 148 GLY n 
1 149 ASN n 
1 150 THR n 
1 151 LEU n 
1 152 ASP n 
1 153 ARG n 
1 154 GLY n 
1 155 VAL n 
1 156 GLY n 
1 157 TYR n 
1 158 THR n 
1 159 PRO n 
1 160 TYR n 
1 161 GLY n 
1 162 GLU n 
1 163 HIS n 
1 164 PHE n 
1 165 MET n 
1 166 PHE n 
1 167 GLN n 
1 168 CYS n 
1 169 GLY n 
1 170 MET n 
1 171 GLU n 
1 172 VAL n 
1 173 CYS n 
1 174 LEU n 
1 175 PRO n 
1 176 ASP n 
1 177 GLY n 
1 178 ARG n 
1 179 LEU n 
1 180 MET n 
1 181 ARG n 
1 182 THR n 
1 183 GLY n 
1 184 MET n 
1 185 GLY n 
1 186 SER n 
1 187 ILE n 
1 188 LYS n 
1 189 GLY n 
1 190 SER n 
1 191 THR n 
1 192 ALA n 
1 193 TRP n 
1 194 GLN n 
1 195 ALA n 
1 196 PHE n 
1 197 LYS n 
1 198 TRP n 
1 199 GLY n 
1 200 TYR n 
1 201 GLY n 
1 202 PRO n 
1 203 TYR n 
1 204 LEU n 
1 205 ASP n 
1 206 GLY n 
1 207 LEU n 
1 208 PHE n 
1 209 THR n 
1 210 GLN n 
1 211 SER n 
1 212 ASN n 
1 213 PHE n 
1 214 GLY n 
1 215 ILE n 
1 216 VAL n 
1 217 THR n 
1 218 LYS n 
1 219 MET n 
1 220 GLY n 
1 221 LEU n 
1 222 TRP n 
1 223 LEU n 
1 224 MET n 
1 225 PRO n 
1 226 LYS n 
1 227 PRO n 
1 228 PRO n 
1 229 VAL n 
1 230 TYR n 
1 231 LYS n 
1 232 PRO n 
1 233 PHE n 
1 234 MET n 
1 235 VAL n 
1 236 ARG n 
1 237 HIS n 
1 238 ALA n 
1 239 ASN n 
1 240 MET n 
1 241 GLU n 
1 242 ASP n 
1 243 VAL n 
1 244 PRO n 
1 245 LYS n 
1 246 ILE n 
1 247 ILE n 
1 248 GLU n 
1 249 ALA n 
1 250 MET n 
1 251 ARG n 
1 252 PRO n 
1 253 LEU n 
1 254 ARG n 
1 255 VAL n 
1 256 SER n 
1 257 ASN n 
1 258 LEU n 
1 259 VAL n 
1 260 ALA n 
1 261 ASN n 
1 262 CYS n 
1 263 ASN n 
1 264 LEU n 
1 265 MET n 
1 266 MET n 
1 267 SER n 
1 268 ALA n 
1 269 SER n 
1 270 TYR n 
1 271 GLN n 
1 272 LEU n 
1 273 ALA n 
1 274 MET n 
1 275 PHE n 
1 276 LYS n 
1 277 ARG n 
1 278 ARG n 
1 279 ASN n 
1 280 GLU n 
1 281 ILE n 
1 282 VAL n 
1 283 PRO n 
1 284 ASP n 
1 285 GLY n 
1 286 ALA n 
1 287 PRO n 
1 288 LEU n 
1 289 ASP n 
1 290 GLU n 
1 291 ALA n 
1 292 SER n 
1 293 LEU n 
1 294 LYS n 
1 295 LYS n 
1 296 ALA n 
1 297 ALA n 
1 298 SER n 
1 299 ALA n 
1 300 ASN n 
1 301 GLY n 
1 302 LEU n 
1 303 GLY n 
1 304 MET n 
1 305 TRP n 
1 306 ASN n 
1 307 THR n 
1 308 TYR n 
1 309 PHE n 
1 310 ALA n 
1 311 LEU n 
1 312 TYR n 
1 313 GLY n 
1 314 THR n 
1 315 GLU n 
1 316 GLN n 
1 317 THR n 
1 318 VAL n 
1 319 ALA n 
1 320 GLY n 
1 321 VAL n 
1 322 GLU n 
1 323 PRO n 
1 324 ILE n 
1 325 ILE n 
1 326 ARG n 
1 327 ALA n 
1 328 THR n 
1 329 LEU n 
1 330 THR n 
1 331 ALA n 
1 332 SER n 
1 333 GLY n 
1 334 GLY n 
1 335 GLU n 
1 336 VAL n 
1 337 LEU n 
1 338 THR n 
1 339 ALA n 
1 340 ALA n 
1 341 GLU n 
1 342 MET n 
1 343 GLU n 
1 344 GLY n 
1 345 ASN n 
1 346 PRO n 
1 347 TRP n 
1 348 PHE n 
1 349 HIS n 
1 350 HIS n 
1 351 HIS n 
1 352 GLN n 
1 353 THR n 
1 354 LEU n 
1 355 MET n 
1 356 GLN n 
1 357 GLY n 
1 358 GLY n 
1 359 LEU n 
1 360 ASN n 
1 361 LEU n 
1 362 ASP n 
1 363 GLU n 
1 364 VAL n 
1 365 GLY n 
1 366 LEU n 
1 367 LEU n 
1 368 ARG n 
1 369 TRP n 
1 370 ARG n 
1 371 GLY n 
1 372 ALA n 
1 373 GLY n 
1 374 GLY n 
1 375 GLY n 
1 376 LEU n 
1 377 ALA n 
1 378 TRP n 
1 379 PHE n 
1 380 ALA n 
1 381 PRO n 
1 382 VAL n 
1 383 ALA n 
1 384 ALA n 
1 385 ALA n 
1 386 ARG n 
1 387 GLY n 
1 388 VAL n 
1 389 GLU n 
1 390 ALA n 
1 391 GLU n 
1 392 ARG n 
1 393 GLN n 
1 394 THR n 
1 395 ALA n 
1 396 LEU n 
1 397 ALA n 
1 398 LYS n 
1 399 GLU n 
1 400 ILE n 
1 401 VAL n 
1 402 GLU n 
1 403 LYS n 
1 404 HIS n 
1 405 GLY n 
1 406 PHE n 
1 407 ASP n 
1 408 TYR n 
1 409 THR n 
1 410 ALA n 
1 411 ALA n 
1 412 TYR n 
1 413 ALA n 
1 414 ILE n 
1 415 GLY n 
1 416 TRP n 
1 417 ARG n 
1 418 ASP n 
1 419 LEU n 
1 420 HIS n 
1 421 HIS n 
1 422 ILE n 
1 423 ILE n 
1 424 ALA n 
1 425 LEU n 
1 426 LEU n 
1 427 PHE n 
1 428 ASP n 
1 429 LYS n 
1 430 ALA n 
1 431 ASP n 
1 432 PRO n 
1 433 THR n 
1 434 GLN n 
1 435 GLU n 
1 436 GLN n 
1 437 LYS n 
1 438 ALA n 
1 439 ASP n 
1 440 ALA n 
1 441 CYS n 
1 442 TYR n 
1 443 ARG n 
1 444 GLU n 
1 445 LEU n 
1 446 VAL n 
1 447 THR n 
1 448 ARG n 
1 449 PHE n 
1 450 GLY n 
1 451 ALA n 
1 452 GLN n 
1 453 GLY n 
1 454 TRP n 
1 455 ALA n 
1 456 SER n 
1 457 TYR n 
1 458 ARG n 
1 459 THR n 
1 460 GLY n 
1 461 VAL n 
1 462 ASN n 
1 463 SER n 
1 464 MET n 
1 465 ASP n 
1 466 LEU n 
1 467 VAL n 
1 468 ALA n 
1 469 GLN n 
1 470 GLN n 
1 471 TYR n 
1 472 GLY n 
1 473 GLU n 
1 474 VAL n 
1 475 ASN n 
1 476 ARG n 
1 477 ASP n 
1 478 PHE n 
1 479 ASN n 
1 480 ARG n 
1 481 THR n 
1 482 LEU n 
1 483 LYS n 
1 484 ARG n 
1 485 ALA n 
1 486 ILE n 
1 487 ASP n 
1 488 PRO n 
1 489 ASN n 
1 490 GLY n 
1 491 ILE n 
1 492 LEU n 
1 493 SER n 
1 494 PRO n 
1 495 GLY n 
1 496 LYS n 
1 497 SER n 
1 498 GLY n 
1 499 ILE n 
1 500 HIS n 
1 501 PRO 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                   501 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 EH199_11270 
_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      'Novosphingobium sp. 01WB02.4-10' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     530823 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
CYS 'L-peptide linking' y CYSTEINE                        ?                               'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE'   ?                               'C27 H33 N9 O15 P2' 785.550 
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'         ?                               'C4 H10 O3'         106.120 
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 
V55 non-polymer         . 4-hydroxy-3-methoxybenzaldehyde p-vanillin                      'C8 H8 O3'          152.147 
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   ALA 1   43  43  ALA ALA A . n 
A 1 2   ASP 2   44  44  ASP ASP A . n 
A 1 3   PHE 3   45  45  PHE PHE A . n 
A 1 4   ALA 4   46  46  ALA ALA A . n 
A 1 5   GLY 5   47  47  GLY GLY A . n 
A 1 6   ALA 6   48  48  ALA ALA A . n 
A 1 7   MET 7   49  49  MET MET A . n 
A 1 8   LYS 8   50  50  LYS LYS A . n 
A 1 9   ALA 9   51  51  ALA ALA A . n 
A 1 10  PHE 10  52  52  PHE PHE A . n 
A 1 11  ARG 11  53  53  ARG ARG A . n 
A 1 12  GLY 12  54  54  GLY GLY A . n 
A 1 13  VAL 13  55  55  VAL VAL A . n 
A 1 14  VAL 14  56  56  VAL VAL A . n 
A 1 15  GLY 15  57  57  GLY GLY A . n 
A 1 16  ALA 16  58  58  ALA ALA A . n 
A 1 17  GLU 17  59  59  GLU GLU A . n 
A 1 18  TRP 18  60  60  TRP TRP A . n 
A 1 19  VAL 19  61  61  VAL VAL A . n 
A 1 20  PHE 20  62  62  PHE PHE A . n 
A 1 21  GLY 21  63  63  GLY GLY A . n 
A 1 22  ASP 22  64  64  ASP ASP A . n 
A 1 23  GLU 23  65  65  GLU GLU A . n 
A 1 24  GLU 24  66  66  GLU GLU A . n 
A 1 25  ALA 25  67  67  ALA ALA A . n 
A 1 26  VAL 26  68  68  VAL VAL A . n 
A 1 27  VAL 27  69  69  VAL VAL A . n 
A 1 28  PRO 28  70  70  PRO PRO A . n 
A 1 29  TRP 29  71  71  TRP TRP A . n 
A 1 30  SER 30  72  72  SER SER A . n 
A 1 31  LYS 31  73  73  LYS LYS A . n 
A 1 32  THR 32  74  74  THR THR A . n 
A 1 33  TYR 33  75  75  TYR TYR A . n 
A 1 34  ILE 34  76  76  ILE ILE A . n 
A 1 35  PRO 35  77  77  PRO PRO A . n 
A 1 36  ASP 36  78  78  ASP ASP A . n 
A 1 37  PRO 37  79  79  PRO PRO A . n 
A 1 38  ALA 38  80  80  ALA ALA A . n 
A 1 39  HIS 39  81  81  HIS HIS A . n 
A 1 40  GLN 40  82  82  GLN GLN A . n 
A 1 41  TYR 41  83  83  TYR TYR A . n 
A 1 42  LYS 42  84  84  LYS LYS A . n 
A 1 43  PRO 43  85  85  PRO PRO A . n 
A 1 44  VAL 44  86  86  VAL VAL A . n 
A 1 45  GLY 45  87  87  GLY GLY A . n 
A 1 46  ALA 46  88  88  ALA ALA A . n 
A 1 47  VAL 47  89  89  VAL VAL A . n 
A 1 48  CYS 48  90  90  CYS CYS A . n 
A 1 49  PRO 49  91  91  PRO PRO A . n 
A 1 50  GLN 50  92  92  GLN GLN A . n 
A 1 51  SER 51  93  93  SER SER A . n 
A 1 52  VAL 52  94  94  VAL VAL A . n 
A 1 53  GLU 53  95  95  GLU GLU A . n 
A 1 54  GLU 54  96  96  GLU GLU A . n 
A 1 55  VAL 55  97  97  VAL VAL A . n 
A 1 56  GLN 56  98  98  GLN GLN A . n 
A 1 57  GLU 57  99  99  GLU GLU A . n 
A 1 58  ILE 58  100 100 ILE ILE A . n 
A 1 59  VAL 59  101 101 VAL VAL A . n 
A 1 60  ARG 60  102 102 ARG ARG A . n 
A 1 61  ILE 61  103 103 ILE ILE A . n 
A 1 62  ALA 62  104 104 ALA ALA A . n 
A 1 63  ASN 63  105 105 ASN ASN A . n 
A 1 64  THR 64  106 106 THR THR A . n 
A 1 65  TYR 65  107 107 TYR TYR A . n 
A 1 66  LYS 66  108 108 LYS LYS A . n 
A 1 67  GLN 67  109 109 GLN GLN A . n 
A 1 68  PRO 68  110 110 PRO PRO A . n 
A 1 69  LEU 69  111 111 LEU LEU A . n 
A 1 70  TRP 70  112 112 TRP TRP A . n 
A 1 71  THR 71  113 113 THR THR A . n 
A 1 72  VAL 72  114 114 VAL VAL A . n 
A 1 73  SER 73  115 115 SER SER A . n 
A 1 74  THR 74  116 116 THR THR A . n 
A 1 75  GLY 75  117 117 GLY GLY A . n 
A 1 76  LYS 76  118 118 LYS LYS A . n 
A 1 77  ASN 77  119 119 ASN ASN A . n 
A 1 78  MET 78  120 120 MET MET A . n 
A 1 79  GLY 79  121 121 GLY GLY A . n 
A 1 80  TYR 80  122 122 TYR TYR A . n 
A 1 81  GLY 81  123 123 GLY GLY A . n 
A 1 82  MET 82  124 124 MET MET A . n 
A 1 83  THR 83  125 125 THR THR A . n 
A 1 84  ALA 84  126 126 ALA ALA A . n 
A 1 85  PRO 85  127 127 PRO PRO A . n 
A 1 86  ALA 86  128 128 ALA ALA A . n 
A 1 87  THR 87  129 129 THR THR A . n 
A 1 88  PRO 88  130 130 PRO PRO A . n 
A 1 89  GLY 89  131 131 GLY GLY A . n 
A 1 90  GLN 90  132 132 GLN GLN A . n 
A 1 91  VAL 91  133 133 VAL VAL A . n 
A 1 92  VAL 92  134 134 VAL VAL A . n 
A 1 93  LEU 93  135 135 LEU LEU A . n 
A 1 94  ASP 94  136 136 ASP ASP A . n 
A 1 95  LEU 95  137 137 LEU LEU A . n 
A 1 96  LYS 96  138 138 LYS LYS A . n 
A 1 97  ARG 97  139 139 ARG ARG A . n 
A 1 98  MET 98  140 140 MET MET A . n 
A 1 99  ASN 99  141 141 ASN ASN A . n 
A 1 100 ARG 100 142 142 ARG ARG A . n 
A 1 101 ILE 101 143 143 ILE ILE A . n 
A 1 102 LEU 102 144 144 LEU LEU A . n 
A 1 103 GLU 103 145 145 GLU GLU A . n 
A 1 104 VAL 104 146 146 VAL VAL A . n 
A 1 105 ASP 105 147 147 ASP ASP A . n 
A 1 106 ALA 106 148 148 ALA ALA A . n 
A 1 107 ASP 107 149 149 ASP ASP A . n 
A 1 108 LEU 108 150 150 LEU LEU A . n 
A 1 109 GLY 109 151 151 GLY GLY A . n 
A 1 110 THR 110 152 152 THR THR A . n 
A 1 111 CYS 111 153 153 CYS CYS A . n 
A 1 112 LEU 112 154 154 LEU LEU A . n 
A 1 113 LEU 113 155 155 LEU LEU A . n 
A 1 114 GLU 114 156 156 GLU GLU A . n 
A 1 115 PRO 115 157 157 PRO PRO A . n 
A 1 116 GLY 116 158 158 GLY GLY A . n 
A 1 117 VAL 117 159 159 VAL VAL A . n 
A 1 118 THR 118 160 160 THR THR A . n 
A 1 119 TYR 119 161 161 TYR TYR A . n 
A 1 120 GLN 120 162 162 GLN GLN A . n 
A 1 121 GLN 121 163 163 GLN GLN A . n 
A 1 122 LEU 122 164 164 LEU LEU A . n 
A 1 123 LYS 123 165 165 LYS LYS A . n 
A 1 124 ASP 124 166 166 ASP ASP A . n 
A 1 125 TYR 125 167 167 TYR TYR A . n 
A 1 126 LEU 126 168 168 LEU LEU A . n 
A 1 127 GLU 127 169 169 GLU GLU A . n 
A 1 128 GLU 128 170 170 GLU GLU A . n 
A 1 129 HIS 129 171 171 HIS HIS A . n 
A 1 130 LYS 130 172 172 LYS LYS A . n 
A 1 131 ILE 131 173 173 ILE ILE A . n 
A 1 132 PRO 132 174 174 PRO PRO A . n 
A 1 133 LEU 133 175 175 LEU LEU A . n 
A 1 134 TRP 134 176 176 TRP TRP A . n 
A 1 135 ILE 135 177 177 ILE ILE A . n 
A 1 136 ASP 136 178 178 ASP ASP A . n 
A 1 137 VAL 137 179 179 VAL VAL A . n 
A 1 138 PRO 138 180 180 PRO PRO A . n 
A 1 139 ASP 139 181 181 ASP ASP A . n 
A 1 140 VAL 140 182 182 VAL VAL A . n 
A 1 141 GLY 141 183 183 GLY GLY A . n 
A 1 142 PRO 142 184 184 PRO PRO A . n 
A 1 143 ILE 143 185 185 ILE ILE A . n 
A 1 144 ALA 144 186 186 ALA ALA A . n 
A 1 145 SER 145 187 187 SER SER A . n 
A 1 146 PRO 146 188 188 PRO PRO A . n 
A 1 147 VAL 147 189 189 VAL VAL A . n 
A 1 148 GLY 148 190 190 GLY GLY A . n 
A 1 149 ASN 149 191 191 ASN ASN A . n 
A 1 150 THR 150 192 192 THR THR A . n 
A 1 151 LEU 151 193 193 LEU LEU A . n 
A 1 152 ASP 152 194 194 ASP ASP A . n 
A 1 153 ARG 153 195 195 ARG ARG A . n 
A 1 154 GLY 154 196 196 GLY GLY A . n 
A 1 155 VAL 155 197 197 VAL VAL A . n 
A 1 156 GLY 156 198 198 GLY GLY A . n 
A 1 157 TYR 157 199 199 TYR TYR A . n 
A 1 158 THR 158 200 200 THR THR A . n 
A 1 159 PRO 159 201 201 PRO PRO A . n 
A 1 160 TYR 160 202 202 TYR TYR A . n 
A 1 161 GLY 161 203 203 GLY GLY A . n 
A 1 162 GLU 162 204 204 GLU GLU A . n 
A 1 163 HIS 163 205 205 HIS HIS A . n 
A 1 164 PHE 164 206 206 PHE PHE A . n 
A 1 165 MET 165 207 207 MET MET A . n 
A 1 166 PHE 166 208 208 PHE PHE A . n 
A 1 167 GLN 167 209 209 GLN GLN A . n 
A 1 168 CYS 168 210 210 CYS CYS A . n 
A 1 169 GLY 169 211 211 GLY GLY A . n 
A 1 170 MET 170 212 212 MET MET A . n 
A 1 171 GLU 171 213 213 GLU GLU A . n 
A 1 172 VAL 172 214 214 VAL VAL A . n 
A 1 173 CYS 173 215 215 CYS CYS A . n 
A 1 174 LEU 174 216 216 LEU LEU A . n 
A 1 175 PRO 175 217 217 PRO PRO A . n 
A 1 176 ASP 176 218 218 ASP ASP A . n 
A 1 177 GLY 177 219 219 GLY GLY A . n 
A 1 178 ARG 178 220 220 ARG ARG A . n 
A 1 179 LEU 179 221 221 LEU LEU A . n 
A 1 180 MET 180 222 222 MET MET A . n 
A 1 181 ARG 181 223 223 ARG ARG A . n 
A 1 182 THR 182 224 224 THR THR A . n 
A 1 183 GLY 183 225 225 GLY GLY A . n 
A 1 184 MET 184 226 226 MET MET A . n 
A 1 185 GLY 185 227 227 GLY GLY A . n 
A 1 186 SER 186 228 228 SER SER A . n 
A 1 187 ILE 187 229 229 ILE ILE A . n 
A 1 188 LYS 188 230 230 LYS LYS A . n 
A 1 189 GLY 189 231 231 GLY GLY A . n 
A 1 190 SER 190 232 232 SER SER A . n 
A 1 191 THR 191 233 233 THR THR A . n 
A 1 192 ALA 192 234 234 ALA ALA A . n 
A 1 193 TRP 193 235 235 TRP TRP A . n 
A 1 194 GLN 194 236 236 GLN GLN A . n 
A 1 195 ALA 195 237 237 ALA ALA A . n 
A 1 196 PHE 196 238 238 PHE PHE A . n 
A 1 197 LYS 197 239 239 LYS LYS A . n 
A 1 198 TRP 198 240 240 TRP TRP A . n 
A 1 199 GLY 199 241 241 GLY GLY A . n 
A 1 200 TYR 200 242 242 TYR TYR A . n 
A 1 201 GLY 201 243 243 GLY GLY A . n 
A 1 202 PRO 202 244 244 PRO PRO A . n 
A 1 203 TYR 203 245 245 TYR TYR A . n 
A 1 204 LEU 204 246 246 LEU LEU A . n 
A 1 205 ASP 205 247 247 ASP ASP A . n 
A 1 206 GLY 206 248 248 GLY GLY A . n 
A 1 207 LEU 207 249 249 LEU LEU A . n 
A 1 208 PHE 208 250 250 PHE PHE A . n 
A 1 209 THR 209 251 251 THR THR A . n 
A 1 210 GLN 210 252 252 GLN GLN A . n 
A 1 211 SER 211 253 253 SER SER A . n 
A 1 212 ASN 212 254 254 ASN ASN A . n 
A 1 213 PHE 213 255 255 PHE PHE A . n 
A 1 214 GLY 214 256 256 GLY GLY A . n 
A 1 215 ILE 215 257 257 ILE ILE A . n 
A 1 216 VAL 216 258 258 VAL VAL A . n 
A 1 217 THR 217 259 259 THR THR A . n 
A 1 218 LYS 218 260 260 LYS LYS A . n 
A 1 219 MET 219 261 261 MET MET A . n 
A 1 220 GLY 220 262 262 GLY GLY A . n 
A 1 221 LEU 221 263 263 LEU LEU A . n 
A 1 222 TRP 222 264 264 TRP TRP A . n 
A 1 223 LEU 223 265 265 LEU LEU A . n 
A 1 224 MET 224 266 266 MET MET A . n 
A 1 225 PRO 225 267 267 PRO PRO A . n 
A 1 226 LYS 226 268 268 LYS LYS A . n 
A 1 227 PRO 227 269 269 PRO PRO A . n 
A 1 228 PRO 228 270 270 PRO PRO A . n 
A 1 229 VAL 229 271 271 VAL VAL A . n 
A 1 230 TYR 230 272 272 TYR TYR A . n 
A 1 231 LYS 231 273 273 LYS LYS A . n 
A 1 232 PRO 232 274 274 PRO PRO A . n 
A 1 233 PHE 233 275 275 PHE PHE A . n 
A 1 234 MET 234 276 276 MET MET A . n 
A 1 235 VAL 235 277 277 VAL VAL A . n 
A 1 236 ARG 236 278 278 ARG ARG A . n 
A 1 237 HIS 237 279 279 HIS HIS A . n 
A 1 238 ALA 238 280 280 ALA ALA A . n 
A 1 239 ASN 239 281 281 ASN ASN A . n 
A 1 240 MET 240 282 282 MET MET A . n 
A 1 241 GLU 241 283 283 GLU GLU A . n 
A 1 242 ASP 242 284 284 ASP ASP A . n 
A 1 243 VAL 243 285 285 VAL VAL A . n 
A 1 244 PRO 244 286 286 PRO PRO A . n 
A 1 245 LYS 245 287 287 LYS LYS A . n 
A 1 246 ILE 246 288 288 ILE ILE A . n 
A 1 247 ILE 247 289 289 ILE ILE A . n 
A 1 248 GLU 248 290 290 GLU GLU A . n 
A 1 249 ALA 249 291 291 ALA ALA A . n 
A 1 250 MET 250 292 292 MET MET A . n 
A 1 251 ARG 251 293 293 ARG ARG A . n 
A 1 252 PRO 252 294 294 PRO PRO A . n 
A 1 253 LEU 253 295 295 LEU LEU A . n 
A 1 254 ARG 254 296 296 ARG ARG A . n 
A 1 255 VAL 255 297 297 VAL VAL A . n 
A 1 256 SER 256 298 298 SER SER A . n 
A 1 257 ASN 257 299 299 ASN ASN A . n 
A 1 258 LEU 258 300 300 LEU LEU A . n 
A 1 259 VAL 259 301 301 VAL VAL A . n 
A 1 260 ALA 260 302 302 ALA ALA A . n 
A 1 261 ASN 261 303 303 ASN ASN A . n 
A 1 262 CYS 262 304 304 CYS CYS A . n 
A 1 263 ASN 263 305 305 ASN ASN A . n 
A 1 264 LEU 264 306 306 LEU LEU A . n 
A 1 265 MET 265 307 307 MET MET A . n 
A 1 266 MET 266 308 308 MET MET A . n 
A 1 267 SER 267 309 309 SER SER A . n 
A 1 268 ALA 268 310 310 ALA ALA A . n 
A 1 269 SER 269 311 311 SER SER A . n 
A 1 270 TYR 270 312 312 TYR TYR A . n 
A 1 271 GLN 271 313 313 GLN GLN A . n 
A 1 272 LEU 272 314 314 LEU LEU A . n 
A 1 273 ALA 273 315 315 ALA ALA A . n 
A 1 274 MET 274 316 316 MET MET A . n 
A 1 275 PHE 275 317 317 PHE PHE A . n 
A 1 276 LYS 276 318 318 LYS LYS A . n 
A 1 277 ARG 277 319 319 ARG ARG A . n 
A 1 278 ARG 278 320 320 ARG ARG A . n 
A 1 279 ASN 279 321 321 ASN ASN A . n 
A 1 280 GLU 280 322 322 GLU GLU A . n 
A 1 281 ILE 281 323 323 ILE ILE A . n 
A 1 282 VAL 282 324 324 VAL VAL A . n 
A 1 283 PRO 283 325 325 PRO PRO A . n 
A 1 284 ASP 284 326 326 ASP ASP A . n 
A 1 285 GLY 285 327 327 GLY GLY A . n 
A 1 286 ALA 286 328 328 ALA ALA A . n 
A 1 287 PRO 287 329 329 PRO PRO A . n 
A 1 288 LEU 288 330 330 LEU LEU A . n 
A 1 289 ASP 289 331 331 ASP ASP A . n 
A 1 290 GLU 290 332 332 GLU GLU A . n 
A 1 291 ALA 291 333 333 ALA ALA A . n 
A 1 292 SER 292 334 334 SER SER A . n 
A 1 293 LEU 293 335 335 LEU LEU A . n 
A 1 294 LYS 294 336 336 LYS LYS A . n 
A 1 295 LYS 295 337 337 LYS LYS A . n 
A 1 296 ALA 296 338 338 ALA ALA A . n 
A 1 297 ALA 297 339 339 ALA ALA A . n 
A 1 298 SER 298 340 340 SER SER A . n 
A 1 299 ALA 299 341 341 ALA ALA A . n 
A 1 300 ASN 300 342 342 ASN ASN A . n 
A 1 301 GLY 301 343 343 GLY GLY A . n 
A 1 302 LEU 302 344 344 LEU LEU A . n 
A 1 303 GLY 303 345 345 GLY GLY A . n 
A 1 304 MET 304 346 346 MET MET A . n 
A 1 305 TRP 305 347 347 TRP TRP A . n 
A 1 306 ASN 306 348 348 ASN ASN A . n 
A 1 307 THR 307 349 349 THR THR A . n 
A 1 308 TYR 308 350 350 TYR TYR A . n 
A 1 309 PHE 309 351 351 PHE PHE A . n 
A 1 310 ALA 310 352 352 ALA ALA A . n 
A 1 311 LEU 311 353 353 LEU LEU A . n 
A 1 312 TYR 312 354 354 TYR TYR A . n 
A 1 313 GLY 313 355 355 GLY GLY A . n 
A 1 314 THR 314 356 356 THR THR A . n 
A 1 315 GLU 315 357 357 GLU GLU A . n 
A 1 316 GLN 316 358 358 GLN GLN A . n 
A 1 317 THR 317 359 359 THR THR A . n 
A 1 318 VAL 318 360 360 VAL VAL A . n 
A 1 319 ALA 319 361 361 ALA ALA A . n 
A 1 320 GLY 320 362 362 GLY GLY A . n 
A 1 321 VAL 321 363 363 VAL VAL A . n 
A 1 322 GLU 322 364 364 GLU GLU A . n 
A 1 323 PRO 323 365 365 PRO PRO A . n 
A 1 324 ILE 324 366 366 ILE ILE A . n 
A 1 325 ILE 325 367 367 ILE ILE A . n 
A 1 326 ARG 326 368 368 ARG ARG A . n 
A 1 327 ALA 327 369 369 ALA ALA A . n 
A 1 328 THR 328 370 370 THR THR A . n 
A 1 329 LEU 329 371 371 LEU LEU A . n 
A 1 330 THR 330 372 372 THR THR A . n 
A 1 331 ALA 331 373 373 ALA ALA A . n 
A 1 332 SER 332 374 374 SER SER A . n 
A 1 333 GLY 333 375 375 GLY GLY A . n 
A 1 334 GLY 334 376 376 GLY GLY A . n 
A 1 335 GLU 335 377 377 GLU GLU A . n 
A 1 336 VAL 336 378 378 VAL VAL A . n 
A 1 337 LEU 337 379 379 LEU LEU A . n 
A 1 338 THR 338 380 380 THR THR A . n 
A 1 339 ALA 339 381 381 ALA ALA A . n 
A 1 340 ALA 340 382 382 ALA ALA A . n 
A 1 341 GLU 341 383 383 GLU GLU A . n 
A 1 342 MET 342 384 384 MET MET A . n 
A 1 343 GLU 343 385 385 GLU GLU A . n 
A 1 344 GLY 344 386 386 GLY GLY A . n 
A 1 345 ASN 345 387 387 ASN ASN A . n 
A 1 346 PRO 346 388 388 PRO PRO A . n 
A 1 347 TRP 347 389 389 TRP TRP A . n 
A 1 348 PHE 348 390 390 PHE PHE A . n 
A 1 349 HIS 349 391 391 HIS HIS A . n 
A 1 350 HIS 350 392 392 HIS HIS A . n 
A 1 351 HIS 351 393 393 HIS HIS A . n 
A 1 352 GLN 352 394 394 GLN GLN A . n 
A 1 353 THR 353 395 395 THR THR A . n 
A 1 354 LEU 354 396 396 LEU LEU A . n 
A 1 355 MET 355 397 397 MET MET A . n 
A 1 356 GLN 356 398 398 GLN GLN A . n 
A 1 357 GLY 357 399 399 GLY GLY A . n 
A 1 358 GLY 358 400 400 GLY GLY A . n 
A 1 359 LEU 359 401 401 LEU LEU A . n 
A 1 360 ASN 360 402 402 ASN ASN A . n 
A 1 361 LEU 361 403 403 LEU LEU A . n 
A 1 362 ASP 362 404 404 ASP ASP A . n 
A 1 363 GLU 363 405 405 GLU GLU A . n 
A 1 364 VAL 364 406 406 VAL VAL A . n 
A 1 365 GLY 365 407 407 GLY GLY A . n 
A 1 366 LEU 366 408 408 LEU LEU A . n 
A 1 367 LEU 367 409 409 LEU LEU A . n 
A 1 368 ARG 368 410 410 ARG ARG A . n 
A 1 369 TRP 369 411 411 TRP TRP A . n 
A 1 370 ARG 370 412 412 ARG ARG A . n 
A 1 371 GLY 371 413 413 GLY GLY A . n 
A 1 372 ALA 372 414 414 ALA ALA A . n 
A 1 373 GLY 373 415 415 GLY GLY A . n 
A 1 374 GLY 374 416 416 GLY GLY A . n 
A 1 375 GLY 375 417 417 GLY GLY A . n 
A 1 376 LEU 376 418 418 LEU LEU A . n 
A 1 377 ALA 377 419 419 ALA ALA A . n 
A 1 378 TRP 378 420 420 TRP TRP A . n 
A 1 379 PHE 379 421 421 PHE PHE A . n 
A 1 380 ALA 380 422 422 ALA ALA A . n 
A 1 381 PRO 381 423 423 PRO PRO A . n 
A 1 382 VAL 382 424 424 VAL VAL A . n 
A 1 383 ALA 383 425 425 ALA ALA A . n 
A 1 384 ALA 384 426 426 ALA ALA A . n 
A 1 385 ALA 385 427 427 ALA ALA A . n 
A 1 386 ARG 386 428 428 ARG ARG A . n 
A 1 387 GLY 387 429 429 GLY GLY A . n 
A 1 388 VAL 388 430 430 VAL VAL A . n 
A 1 389 GLU 389 431 431 GLU GLU A . n 
A 1 390 ALA 390 432 432 ALA ALA A . n 
A 1 391 GLU 391 433 433 GLU GLU A . n 
A 1 392 ARG 392 434 434 ARG ARG A . n 
A 1 393 GLN 393 435 435 GLN GLN A . n 
A 1 394 THR 394 436 436 THR THR A . n 
A 1 395 ALA 395 437 437 ALA ALA A . n 
A 1 396 LEU 396 438 438 LEU LEU A . n 
A 1 397 ALA 397 439 439 ALA ALA A . n 
A 1 398 LYS 398 440 440 LYS LYS A . n 
A 1 399 GLU 399 441 441 GLU GLU A . n 
A 1 400 ILE 400 442 442 ILE ILE A . n 
A 1 401 VAL 401 443 443 VAL VAL A . n 
A 1 402 GLU 402 444 444 GLU GLU A . n 
A 1 403 LYS 403 445 445 LYS LYS A . n 
A 1 404 HIS 404 446 446 HIS HIS A . n 
A 1 405 GLY 405 447 447 GLY GLY A . n 
A 1 406 PHE 406 448 448 PHE PHE A . n 
A 1 407 ASP 407 449 449 ASP ASP A . n 
A 1 408 TYR 408 450 450 TYR TYR A . n 
A 1 409 THR 409 451 451 THR THR A . n 
A 1 410 ALA 410 452 452 ALA ALA A . n 
A 1 411 ALA 411 453 453 ALA ALA A . n 
A 1 412 TYR 412 454 454 TYR TYR A . n 
A 1 413 ALA 413 455 455 ALA ALA A . n 
A 1 414 ILE 414 456 456 ILE ILE A . n 
A 1 415 GLY 415 457 457 GLY GLY A . n 
A 1 416 TRP 416 458 458 TRP TRP A . n 
A 1 417 ARG 417 459 459 ARG ARG A . n 
A 1 418 ASP 418 460 460 ASP ASP A . n 
A 1 419 LEU 419 461 461 LEU LEU A . n 
A 1 420 HIS 420 462 462 HIS HIS A . n 
A 1 421 HIS 421 463 463 HIS HIS A . n 
A 1 422 ILE 422 464 464 ILE ILE A . n 
A 1 423 ILE 423 465 465 ILE ILE A . n 
A 1 424 ALA 424 466 466 ALA ALA A . n 
A 1 425 LEU 425 467 467 LEU LEU A . n 
A 1 426 LEU 426 468 468 LEU LEU A . n 
A 1 427 PHE 427 469 469 PHE PHE A . n 
A 1 428 ASP 428 470 470 ASP ASP A . n 
A 1 429 LYS 429 471 471 LYS LYS A . n 
A 1 430 ALA 430 472 472 ALA ALA A . n 
A 1 431 ASP 431 473 473 ASP ASP A . n 
A 1 432 PRO 432 474 474 PRO PRO A . n 
A 1 433 THR 433 475 475 THR THR A . n 
A 1 434 GLN 434 476 476 GLN GLN A . n 
A 1 435 GLU 435 477 477 GLU GLU A . n 
A 1 436 GLN 436 478 478 GLN GLN A . n 
A 1 437 LYS 437 479 479 LYS LYS A . n 
A 1 438 ALA 438 480 480 ALA ALA A . n 
A 1 439 ASP 439 481 481 ASP ASP A . n 
A 1 440 ALA 440 482 482 ALA ALA A . n 
A 1 441 CYS 441 483 483 CYS CYS A . n 
A 1 442 TYR 442 484 484 TYR TYR A . n 
A 1 443 ARG 443 485 485 ARG ARG A . n 
A 1 444 GLU 444 486 486 GLU GLU A . n 
A 1 445 LEU 445 487 487 LEU LEU A . n 
A 1 446 VAL 446 488 488 VAL VAL A . n 
A 1 447 THR 447 489 489 THR THR A . n 
A 1 448 ARG 448 490 490 ARG ARG A . n 
A 1 449 PHE 449 491 491 PHE PHE A . n 
A 1 450 GLY 450 492 492 GLY GLY A . n 
A 1 451 ALA 451 493 493 ALA ALA A . n 
A 1 452 GLN 452 494 494 GLN GLN A . n 
A 1 453 GLY 453 495 495 GLY GLY A . n 
A 1 454 TRP 454 496 496 TRP TRP A . n 
A 1 455 ALA 455 497 497 ALA ALA A . n 
A 1 456 SER 456 498 498 SER SER A . n 
A 1 457 TYR 457 499 499 TYR TYR A . n 
A 1 458 ARG 458 500 500 ARG ARG A . n 
A 1 459 THR 459 501 501 THR THR A . n 
A 1 460 GLY 460 502 502 GLY GLY A . n 
A 1 461 VAL 461 503 503 VAL VAL A . n 
A 1 462 ASN 462 504 504 ASN ASN A . n 
A 1 463 SER 463 505 505 SER SER A . n 
A 1 464 MET 464 506 506 MET MET A . n 
A 1 465 ASP 465 507 507 ASP ASP A . n 
A 1 466 LEU 466 508 508 LEU LEU A . n 
A 1 467 VAL 467 509 509 VAL VAL A . n 
A 1 468 ALA 468 510 510 ALA ALA A . n 
A 1 469 GLN 469 511 511 GLN GLN A . n 
A 1 470 GLN 470 512 512 GLN GLN A . n 
A 1 471 TYR 471 513 513 TYR TYR A . n 
A 1 472 GLY 472 514 514 GLY GLY A . n 
A 1 473 GLU 473 515 515 GLU GLU A . n 
A 1 474 VAL 474 516 516 VAL VAL A . n 
A 1 475 ASN 475 517 517 ASN ASN A . n 
A 1 476 ARG 476 518 518 ARG ARG A . n 
A 1 477 ASP 477 519 519 ASP ASP A . n 
A 1 478 PHE 478 520 520 PHE PHE A . n 
A 1 479 ASN 479 521 521 ASN ASN A . n 
A 1 480 ARG 480 522 522 ARG ARG A . n 
A 1 481 THR 481 523 523 THR THR A . n 
A 1 482 LEU 482 524 524 LEU LEU A . n 
A 1 483 LYS 483 525 525 LYS LYS A . n 
A 1 484 ARG 484 526 526 ARG ARG A . n 
A 1 485 ALA 485 527 527 ALA ALA A . n 
A 1 486 ILE 486 528 528 ILE ILE A . n 
A 1 487 ASP 487 529 529 ASP ASP A . n 
A 1 488 PRO 488 530 530 PRO PRO A . n 
A 1 489 ASN 489 531 531 ASN ASN A . n 
A 1 490 GLY 490 532 532 GLY GLY A . n 
A 1 491 ILE 491 533 533 ILE ILE A . n 
A 1 492 LEU 492 534 534 LEU LEU A . n 
A 1 493 SER 493 535 535 SER SER A . n 
A 1 494 PRO 494 536 536 PRO PRO A . n 
A 1 495 GLY 495 537 537 GLY GLY A . n 
A 1 496 LYS 496 538 538 LYS LYS A . n 
A 1 497 SER 497 539 539 SER SER A . n 
A 1 498 GLY 498 540 540 GLY GLY A . n 
A 1 499 ILE 499 541 541 ILE ILE A . n 
A 1 500 HIS 500 542 542 HIS HIS A . n 
A 1 501 PRO 501 543 543 PRO PRO A . n 
B 1 1   ALA 1   43  43  ALA ALA B . n 
B 1 2   ASP 2   44  44  ASP ASP B . n 
B 1 3   PHE 3   45  45  PHE PHE B . n 
B 1 4   ALA 4   46  46  ALA ALA B . n 
B 1 5   GLY 5   47  47  GLY GLY B . n 
B 1 6   ALA 6   48  48  ALA ALA B . n 
B 1 7   MET 7   49  49  MET MET B . n 
B 1 8   LYS 8   50  50  LYS LYS B . n 
B 1 9   ALA 9   51  51  ALA ALA B . n 
B 1 10  PHE 10  52  52  PHE PHE B . n 
B 1 11  ARG 11  53  53  ARG ARG B . n 
B 1 12  GLY 12  54  54  GLY GLY B . n 
B 1 13  VAL 13  55  55  VAL VAL B . n 
B 1 14  VAL 14  56  56  VAL VAL B . n 
B 1 15  GLY 15  57  57  GLY GLY B . n 
B 1 16  ALA 16  58  58  ALA ALA B . n 
B 1 17  GLU 17  59  59  GLU GLU B . n 
B 1 18  TRP 18  60  60  TRP TRP B . n 
B 1 19  VAL 19  61  61  VAL VAL B . n 
B 1 20  PHE 20  62  62  PHE PHE B . n 
B 1 21  GLY 21  63  63  GLY GLY B . n 
B 1 22  ASP 22  64  64  ASP ASP B . n 
B 1 23  GLU 23  65  65  GLU GLU B . n 
B 1 24  GLU 24  66  66  GLU GLU B . n 
B 1 25  ALA 25  67  67  ALA ALA B . n 
B 1 26  VAL 26  68  68  VAL VAL B . n 
B 1 27  VAL 27  69  69  VAL VAL B . n 
B 1 28  PRO 28  70  70  PRO PRO B . n 
B 1 29  TRP 29  71  71  TRP TRP B . n 
B 1 30  SER 30  72  72  SER SER B . n 
B 1 31  LYS 31  73  73  LYS LYS B . n 
B 1 32  THR 32  74  74  THR THR B . n 
B 1 33  TYR 33  75  75  TYR TYR B . n 
B 1 34  ILE 34  76  76  ILE ILE B . n 
B 1 35  PRO 35  77  77  PRO PRO B . n 
B 1 36  ASP 36  78  78  ASP ASP B . n 
B 1 37  PRO 37  79  79  PRO PRO B . n 
B 1 38  ALA 38  80  80  ALA ALA B . n 
B 1 39  HIS 39  81  81  HIS HIS B . n 
B 1 40  GLN 40  82  82  GLN GLN B . n 
B 1 41  TYR 41  83  83  TYR TYR B . n 
B 1 42  LYS 42  84  84  LYS LYS B . n 
B 1 43  PRO 43  85  85  PRO PRO B . n 
B 1 44  VAL 44  86  86  VAL VAL B . n 
B 1 45  GLY 45  87  87  GLY GLY B . n 
B 1 46  ALA 46  88  88  ALA ALA B . n 
B 1 47  VAL 47  89  89  VAL VAL B . n 
B 1 48  CYS 48  90  90  CYS CYS B . n 
B 1 49  PRO 49  91  91  PRO PRO B . n 
B 1 50  GLN 50  92  92  GLN GLN B . n 
B 1 51  SER 51  93  93  SER SER B . n 
B 1 52  VAL 52  94  94  VAL VAL B . n 
B 1 53  GLU 53  95  95  GLU GLU B . n 
B 1 54  GLU 54  96  96  GLU GLU B . n 
B 1 55  VAL 55  97  97  VAL VAL B . n 
B 1 56  GLN 56  98  98  GLN GLN B . n 
B 1 57  GLU 57  99  99  GLU GLU B . n 
B 1 58  ILE 58  100 100 ILE ILE B . n 
B 1 59  VAL 59  101 101 VAL VAL B . n 
B 1 60  ARG 60  102 102 ARG ARG B . n 
B 1 61  ILE 61  103 103 ILE ILE B . n 
B 1 62  ALA 62  104 104 ALA ALA B . n 
B 1 63  ASN 63  105 105 ASN ASN B . n 
B 1 64  THR 64  106 106 THR THR B . n 
B 1 65  TYR 65  107 107 TYR TYR B . n 
B 1 66  LYS 66  108 108 LYS LYS B . n 
B 1 67  GLN 67  109 109 GLN GLN B . n 
B 1 68  PRO 68  110 110 PRO PRO B . n 
B 1 69  LEU 69  111 111 LEU LEU B . n 
B 1 70  TRP 70  112 112 TRP TRP B . n 
B 1 71  THR 71  113 113 THR THR B . n 
B 1 72  VAL 72  114 114 VAL VAL B . n 
B 1 73  SER 73  115 115 SER SER B . n 
B 1 74  THR 74  116 116 THR THR B . n 
B 1 75  GLY 75  117 117 GLY GLY B . n 
B 1 76  LYS 76  118 118 LYS LYS B . n 
B 1 77  ASN 77  119 119 ASN ASN B . n 
B 1 78  MET 78  120 120 MET MET B . n 
B 1 79  GLY 79  121 121 GLY GLY B . n 
B 1 80  TYR 80  122 122 TYR TYR B . n 
B 1 81  GLY 81  123 123 GLY GLY B . n 
B 1 82  MET 82  124 124 MET MET B . n 
B 1 83  THR 83  125 125 THR THR B . n 
B 1 84  ALA 84  126 126 ALA ALA B . n 
B 1 85  PRO 85  127 127 PRO PRO B . n 
B 1 86  ALA 86  128 128 ALA ALA B . n 
B 1 87  THR 87  129 129 THR THR B . n 
B 1 88  PRO 88  130 130 PRO PRO B . n 
B 1 89  GLY 89  131 131 GLY GLY B . n 
B 1 90  GLN 90  132 132 GLN GLN B . n 
B 1 91  VAL 91  133 133 VAL VAL B . n 
B 1 92  VAL 92  134 134 VAL VAL B . n 
B 1 93  LEU 93  135 135 LEU LEU B . n 
B 1 94  ASP 94  136 136 ASP ASP B . n 
B 1 95  LEU 95  137 137 LEU LEU B . n 
B 1 96  LYS 96  138 138 LYS LYS B . n 
B 1 97  ARG 97  139 139 ARG ARG B . n 
B 1 98  MET 98  140 140 MET MET B . n 
B 1 99  ASN 99  141 141 ASN ASN B . n 
B 1 100 ARG 100 142 142 ARG ARG B . n 
B 1 101 ILE 101 143 143 ILE ILE B . n 
B 1 102 LEU 102 144 144 LEU LEU B . n 
B 1 103 GLU 103 145 145 GLU GLU B . n 
B 1 104 VAL 104 146 146 VAL VAL B . n 
B 1 105 ASP 105 147 147 ASP ASP B . n 
B 1 106 ALA 106 148 148 ALA ALA B . n 
B 1 107 ASP 107 149 149 ASP ASP B . n 
B 1 108 LEU 108 150 150 LEU LEU B . n 
B 1 109 GLY 109 151 151 GLY GLY B . n 
B 1 110 THR 110 152 152 THR THR B . n 
B 1 111 CYS 111 153 153 CYS CYS B . n 
B 1 112 LEU 112 154 154 LEU LEU B . n 
B 1 113 LEU 113 155 155 LEU LEU B . n 
B 1 114 GLU 114 156 156 GLU GLU B . n 
B 1 115 PRO 115 157 157 PRO PRO B . n 
B 1 116 GLY 116 158 158 GLY GLY B . n 
B 1 117 VAL 117 159 159 VAL VAL B . n 
B 1 118 THR 118 160 160 THR THR B . n 
B 1 119 TYR 119 161 161 TYR TYR B . n 
B 1 120 GLN 120 162 162 GLN GLN B . n 
B 1 121 GLN 121 163 163 GLN GLN B . n 
B 1 122 LEU 122 164 164 LEU LEU B . n 
B 1 123 LYS 123 165 165 LYS LYS B . n 
B 1 124 ASP 124 166 166 ASP ASP B . n 
B 1 125 TYR 125 167 167 TYR TYR B . n 
B 1 126 LEU 126 168 168 LEU LEU B . n 
B 1 127 GLU 127 169 169 GLU GLU B . n 
B 1 128 GLU 128 170 170 GLU GLU B . n 
B 1 129 HIS 129 171 171 HIS HIS B . n 
B 1 130 LYS 130 172 172 LYS LYS B . n 
B 1 131 ILE 131 173 173 ILE ILE B . n 
B 1 132 PRO 132 174 174 PRO PRO B . n 
B 1 133 LEU 133 175 175 LEU LEU B . n 
B 1 134 TRP 134 176 176 TRP TRP B . n 
B 1 135 ILE 135 177 177 ILE ILE B . n 
B 1 136 ASP 136 178 178 ASP ASP B . n 
B 1 137 VAL 137 179 179 VAL VAL B . n 
B 1 138 PRO 138 180 180 PRO PRO B . n 
B 1 139 ASP 139 181 181 ASP ASP B . n 
B 1 140 VAL 140 182 182 VAL VAL B . n 
B 1 141 GLY 141 183 183 GLY GLY B . n 
B 1 142 PRO 142 184 184 PRO PRO B . n 
B 1 143 ILE 143 185 185 ILE ILE B . n 
B 1 144 ALA 144 186 186 ALA ALA B . n 
B 1 145 SER 145 187 187 SER SER B . n 
B 1 146 PRO 146 188 188 PRO PRO B . n 
B 1 147 VAL 147 189 189 VAL VAL B . n 
B 1 148 GLY 148 190 190 GLY GLY B . n 
B 1 149 ASN 149 191 191 ASN ASN B . n 
B 1 150 THR 150 192 192 THR THR B . n 
B 1 151 LEU 151 193 193 LEU LEU B . n 
B 1 152 ASP 152 194 194 ASP ASP B . n 
B 1 153 ARG 153 195 195 ARG ARG B . n 
B 1 154 GLY 154 196 196 GLY GLY B . n 
B 1 155 VAL 155 197 197 VAL VAL B . n 
B 1 156 GLY 156 198 198 GLY GLY B . n 
B 1 157 TYR 157 199 199 TYR TYR B . n 
B 1 158 THR 158 200 200 THR THR B . n 
B 1 159 PRO 159 201 201 PRO PRO B . n 
B 1 160 TYR 160 202 202 TYR TYR B . n 
B 1 161 GLY 161 203 203 GLY GLY B . n 
B 1 162 GLU 162 204 204 GLU GLU B . n 
B 1 163 HIS 163 205 205 HIS HIS B . n 
B 1 164 PHE 164 206 206 PHE PHE B . n 
B 1 165 MET 165 207 207 MET MET B . n 
B 1 166 PHE 166 208 208 PHE PHE B . n 
B 1 167 GLN 167 209 209 GLN GLN B . n 
B 1 168 CYS 168 210 210 CYS CYS B . n 
B 1 169 GLY 169 211 211 GLY GLY B . n 
B 1 170 MET 170 212 212 MET MET B . n 
B 1 171 GLU 171 213 213 GLU GLU B . n 
B 1 172 VAL 172 214 214 VAL VAL B . n 
B 1 173 CYS 173 215 215 CYS CYS B . n 
B 1 174 LEU 174 216 216 LEU LEU B . n 
B 1 175 PRO 175 217 217 PRO PRO B . n 
B 1 176 ASP 176 218 218 ASP ASP B . n 
B 1 177 GLY 177 219 219 GLY GLY B . n 
B 1 178 ARG 178 220 220 ARG ARG B . n 
B 1 179 LEU 179 221 221 LEU LEU B . n 
B 1 180 MET 180 222 222 MET MET B . n 
B 1 181 ARG 181 223 223 ARG ARG B . n 
B 1 182 THR 182 224 224 THR THR B . n 
B 1 183 GLY 183 225 225 GLY GLY B . n 
B 1 184 MET 184 226 226 MET MET B . n 
B 1 185 GLY 185 227 227 GLY GLY B . n 
B 1 186 SER 186 228 228 SER SER B . n 
B 1 187 ILE 187 229 229 ILE ILE B . n 
B 1 188 LYS 188 230 230 LYS LYS B . n 
B 1 189 GLY 189 231 231 GLY GLY B . n 
B 1 190 SER 190 232 232 SER SER B . n 
B 1 191 THR 191 233 233 THR THR B . n 
B 1 192 ALA 192 234 234 ALA ALA B . n 
B 1 193 TRP 193 235 235 TRP TRP B . n 
B 1 194 GLN 194 236 236 GLN GLN B . n 
B 1 195 ALA 195 237 237 ALA ALA B . n 
B 1 196 PHE 196 238 238 PHE PHE B . n 
B 1 197 LYS 197 239 239 LYS LYS B . n 
B 1 198 TRP 198 240 240 TRP TRP B . n 
B 1 199 GLY 199 241 241 GLY GLY B . n 
B 1 200 TYR 200 242 242 TYR TYR B . n 
B 1 201 GLY 201 243 243 GLY GLY B . n 
B 1 202 PRO 202 244 244 PRO PRO B . n 
B 1 203 TYR 203 245 245 TYR TYR B . n 
B 1 204 LEU 204 246 246 LEU LEU B . n 
B 1 205 ASP 205 247 247 ASP ASP B . n 
B 1 206 GLY 206 248 248 GLY GLY B . n 
B 1 207 LEU 207 249 249 LEU LEU B . n 
B 1 208 PHE 208 250 250 PHE PHE B . n 
B 1 209 THR 209 251 251 THR THR B . n 
B 1 210 GLN 210 252 252 GLN GLN B . n 
B 1 211 SER 211 253 253 SER SER B . n 
B 1 212 ASN 212 254 254 ASN ASN B . n 
B 1 213 PHE 213 255 255 PHE PHE B . n 
B 1 214 GLY 214 256 256 GLY GLY B . n 
B 1 215 ILE 215 257 257 ILE ILE B . n 
B 1 216 VAL 216 258 258 VAL VAL B . n 
B 1 217 THR 217 259 259 THR THR B . n 
B 1 218 LYS 218 260 260 LYS LYS B . n 
B 1 219 MET 219 261 261 MET MET B . n 
B 1 220 GLY 220 262 262 GLY GLY B . n 
B 1 221 LEU 221 263 263 LEU LEU B . n 
B 1 222 TRP 222 264 264 TRP TRP B . n 
B 1 223 LEU 223 265 265 LEU LEU B . n 
B 1 224 MET 224 266 266 MET MET B . n 
B 1 225 PRO 225 267 267 PRO PRO B . n 
B 1 226 LYS 226 268 268 LYS LYS B . n 
B 1 227 PRO 227 269 269 PRO PRO B . n 
B 1 228 PRO 228 270 270 PRO PRO B . n 
B 1 229 VAL 229 271 271 VAL VAL B . n 
B 1 230 TYR 230 272 272 TYR TYR B . n 
B 1 231 LYS 231 273 273 LYS LYS B . n 
B 1 232 PRO 232 274 274 PRO PRO B . n 
B 1 233 PHE 233 275 275 PHE PHE B . n 
B 1 234 MET 234 276 276 MET MET B . n 
B 1 235 VAL 235 277 277 VAL VAL B . n 
B 1 236 ARG 236 278 278 ARG ARG B . n 
B 1 237 HIS 237 279 279 HIS HIS B . n 
B 1 238 ALA 238 280 280 ALA ALA B . n 
B 1 239 ASN 239 281 281 ASN ASN B . n 
B 1 240 MET 240 282 282 MET MET B . n 
B 1 241 GLU 241 283 283 GLU GLU B . n 
B 1 242 ASP 242 284 284 ASP ASP B . n 
B 1 243 VAL 243 285 285 VAL VAL B . n 
B 1 244 PRO 244 286 286 PRO PRO B . n 
B 1 245 LYS 245 287 287 LYS LYS B . n 
B 1 246 ILE 246 288 288 ILE ILE B . n 
B 1 247 ILE 247 289 289 ILE ILE B . n 
B 1 248 GLU 248 290 290 GLU GLU B . n 
B 1 249 ALA 249 291 291 ALA ALA B . n 
B 1 250 MET 250 292 292 MET MET B . n 
B 1 251 ARG 251 293 293 ARG ARG B . n 
B 1 252 PRO 252 294 294 PRO PRO B . n 
B 1 253 LEU 253 295 295 LEU LEU B . n 
B 1 254 ARG 254 296 296 ARG ARG B . n 
B 1 255 VAL 255 297 297 VAL VAL B . n 
B 1 256 SER 256 298 298 SER SER B . n 
B 1 257 ASN 257 299 299 ASN ASN B . n 
B 1 258 LEU 258 300 300 LEU LEU B . n 
B 1 259 VAL 259 301 301 VAL VAL B . n 
B 1 260 ALA 260 302 302 ALA ALA B . n 
B 1 261 ASN 261 303 303 ASN ASN B . n 
B 1 262 CYS 262 304 304 CYS CYS B . n 
B 1 263 ASN 263 305 305 ASN ASN B . n 
B 1 264 LEU 264 306 306 LEU LEU B . n 
B 1 265 MET 265 307 307 MET MET B . n 
B 1 266 MET 266 308 308 MET MET B . n 
B 1 267 SER 267 309 309 SER SER B . n 
B 1 268 ALA 268 310 310 ALA ALA B . n 
B 1 269 SER 269 311 311 SER SER B . n 
B 1 270 TYR 270 312 312 TYR TYR B . n 
B 1 271 GLN 271 313 313 GLN GLN B . n 
B 1 272 LEU 272 314 314 LEU LEU B . n 
B 1 273 ALA 273 315 315 ALA ALA B . n 
B 1 274 MET 274 316 316 MET MET B . n 
B 1 275 PHE 275 317 317 PHE PHE B . n 
B 1 276 LYS 276 318 318 LYS LYS B . n 
B 1 277 ARG 277 319 319 ARG ARG B . n 
B 1 278 ARG 278 320 320 ARG ARG B . n 
B 1 279 ASN 279 321 321 ASN ASN B . n 
B 1 280 GLU 280 322 322 GLU GLU B . n 
B 1 281 ILE 281 323 323 ILE ILE B . n 
B 1 282 VAL 282 324 324 VAL VAL B . n 
B 1 283 PRO 283 325 325 PRO PRO B . n 
B 1 284 ASP 284 326 326 ASP ASP B . n 
B 1 285 GLY 285 327 327 GLY GLY B . n 
B 1 286 ALA 286 328 328 ALA ALA B . n 
B 1 287 PRO 287 329 329 PRO PRO B . n 
B 1 288 LEU 288 330 330 LEU LEU B . n 
B 1 289 ASP 289 331 331 ASP ASP B . n 
B 1 290 GLU 290 332 332 GLU GLU B . n 
B 1 291 ALA 291 333 333 ALA ALA B . n 
B 1 292 SER 292 334 334 SER SER B . n 
B 1 293 LEU 293 335 335 LEU LEU B . n 
B 1 294 LYS 294 336 336 LYS LYS B . n 
B 1 295 LYS 295 337 337 LYS LYS B . n 
B 1 296 ALA 296 338 338 ALA ALA B . n 
B 1 297 ALA 297 339 339 ALA ALA B . n 
B 1 298 SER 298 340 340 SER SER B . n 
B 1 299 ALA 299 341 341 ALA ALA B . n 
B 1 300 ASN 300 342 342 ASN ASN B . n 
B 1 301 GLY 301 343 343 GLY GLY B . n 
B 1 302 LEU 302 344 344 LEU LEU B . n 
B 1 303 GLY 303 345 345 GLY GLY B . n 
B 1 304 MET 304 346 346 MET MET B . n 
B 1 305 TRP 305 347 347 TRP TRP B . n 
B 1 306 ASN 306 348 348 ASN ASN B . n 
B 1 307 THR 307 349 349 THR THR B . n 
B 1 308 TYR 308 350 350 TYR TYR B . n 
B 1 309 PHE 309 351 351 PHE PHE B . n 
B 1 310 ALA 310 352 352 ALA ALA B . n 
B 1 311 LEU 311 353 353 LEU LEU B . n 
B 1 312 TYR 312 354 354 TYR TYR B . n 
B 1 313 GLY 313 355 355 GLY GLY B . n 
B 1 314 THR 314 356 356 THR THR B . n 
B 1 315 GLU 315 357 357 GLU GLU B . n 
B 1 316 GLN 316 358 358 GLN GLN B . n 
B 1 317 THR 317 359 359 THR THR B . n 
B 1 318 VAL 318 360 360 VAL VAL B . n 
B 1 319 ALA 319 361 361 ALA ALA B . n 
B 1 320 GLY 320 362 362 GLY GLY B . n 
B 1 321 VAL 321 363 363 VAL VAL B . n 
B 1 322 GLU 322 364 364 GLU GLU B . n 
B 1 323 PRO 323 365 365 PRO PRO B . n 
B 1 324 ILE 324 366 366 ILE ILE B . n 
B 1 325 ILE 325 367 367 ILE ILE B . n 
B 1 326 ARG 326 368 368 ARG ARG B . n 
B 1 327 ALA 327 369 369 ALA ALA B . n 
B 1 328 THR 328 370 370 THR THR B . n 
B 1 329 LEU 329 371 371 LEU LEU B . n 
B 1 330 THR 330 372 372 THR THR B . n 
B 1 331 ALA 331 373 373 ALA ALA B . n 
B 1 332 SER 332 374 374 SER SER B . n 
B 1 333 GLY 333 375 375 GLY GLY B . n 
B 1 334 GLY 334 376 376 GLY GLY B . n 
B 1 335 GLU 335 377 377 GLU GLU B . n 
B 1 336 VAL 336 378 378 VAL VAL B . n 
B 1 337 LEU 337 379 379 LEU LEU B . n 
B 1 338 THR 338 380 380 THR THR B . n 
B 1 339 ALA 339 381 381 ALA ALA B . n 
B 1 340 ALA 340 382 382 ALA ALA B . n 
B 1 341 GLU 341 383 383 GLU GLU B . n 
B 1 342 MET 342 384 384 MET MET B . n 
B 1 343 GLU 343 385 385 GLU GLU B . n 
B 1 344 GLY 344 386 386 GLY GLY B . n 
B 1 345 ASN 345 387 387 ASN ASN B . n 
B 1 346 PRO 346 388 388 PRO PRO B . n 
B 1 347 TRP 347 389 389 TRP TRP B . n 
B 1 348 PHE 348 390 390 PHE PHE B . n 
B 1 349 HIS 349 391 391 HIS HIS B . n 
B 1 350 HIS 350 392 392 HIS HIS B . n 
B 1 351 HIS 351 393 393 HIS HIS B . n 
B 1 352 GLN 352 394 394 GLN GLN B . n 
B 1 353 THR 353 395 395 THR THR B . n 
B 1 354 LEU 354 396 396 LEU LEU B . n 
B 1 355 MET 355 397 397 MET MET B . n 
B 1 356 GLN 356 398 398 GLN GLN B . n 
B 1 357 GLY 357 399 399 GLY GLY B . n 
B 1 358 GLY 358 400 400 GLY GLY B . n 
B 1 359 LEU 359 401 401 LEU LEU B . n 
B 1 360 ASN 360 402 402 ASN ASN B . n 
B 1 361 LEU 361 403 403 LEU LEU B . n 
B 1 362 ASP 362 404 404 ASP ASP B . n 
B 1 363 GLU 363 405 405 GLU GLU B . n 
B 1 364 VAL 364 406 406 VAL VAL B . n 
B 1 365 GLY 365 407 407 GLY GLY B . n 
B 1 366 LEU 366 408 408 LEU LEU B . n 
B 1 367 LEU 367 409 409 LEU LEU B . n 
B 1 368 ARG 368 410 410 ARG ARG B . n 
B 1 369 TRP 369 411 411 TRP TRP B . n 
B 1 370 ARG 370 412 412 ARG ARG B . n 
B 1 371 GLY 371 413 413 GLY GLY B . n 
B 1 372 ALA 372 414 414 ALA ALA B . n 
B 1 373 GLY 373 415 415 GLY GLY B . n 
B 1 374 GLY 374 416 416 GLY GLY B . n 
B 1 375 GLY 375 417 417 GLY GLY B . n 
B 1 376 LEU 376 418 418 LEU LEU B . n 
B 1 377 ALA 377 419 419 ALA ALA B . n 
B 1 378 TRP 378 420 420 TRP TRP B . n 
B 1 379 PHE 379 421 421 PHE PHE B . n 
B 1 380 ALA 380 422 422 ALA ALA B . n 
B 1 381 PRO 381 423 423 PRO PRO B . n 
B 1 382 VAL 382 424 424 VAL VAL B . n 
B 1 383 ALA 383 425 425 ALA ALA B . n 
B 1 384 ALA 384 426 426 ALA ALA B . n 
B 1 385 ALA 385 427 427 ALA ALA B . n 
B 1 386 ARG 386 428 428 ARG ARG B . n 
B 1 387 GLY 387 429 429 GLY GLY B . n 
B 1 388 VAL 388 430 430 VAL VAL B . n 
B 1 389 GLU 389 431 431 GLU GLU B . n 
B 1 390 ALA 390 432 432 ALA ALA B . n 
B 1 391 GLU 391 433 433 GLU GLU B . n 
B 1 392 ARG 392 434 434 ARG ARG B . n 
B 1 393 GLN 393 435 435 GLN GLN B . n 
B 1 394 THR 394 436 436 THR THR B . n 
B 1 395 ALA 395 437 437 ALA ALA B . n 
B 1 396 LEU 396 438 438 LEU LEU B . n 
B 1 397 ALA 397 439 439 ALA ALA B . n 
B 1 398 LYS 398 440 440 LYS LYS B . n 
B 1 399 GLU 399 441 441 GLU GLU B . n 
B 1 400 ILE 400 442 442 ILE ILE B . n 
B 1 401 VAL 401 443 443 VAL VAL B . n 
B 1 402 GLU 402 444 444 GLU GLU B . n 
B 1 403 LYS 403 445 445 LYS LYS B . n 
B 1 404 HIS 404 446 446 HIS HIS B . n 
B 1 405 GLY 405 447 447 GLY GLY B . n 
B 1 406 PHE 406 448 448 PHE PHE B . n 
B 1 407 ASP 407 449 449 ASP ASP B . n 
B 1 408 TYR 408 450 450 TYR TYR B . n 
B 1 409 THR 409 451 451 THR THR B . n 
B 1 410 ALA 410 452 452 ALA ALA B . n 
B 1 411 ALA 411 453 453 ALA ALA B . n 
B 1 412 TYR 412 454 454 TYR TYR B . n 
B 1 413 ALA 413 455 455 ALA ALA B . n 
B 1 414 ILE 414 456 456 ILE ILE B . n 
B 1 415 GLY 415 457 457 GLY GLY B . n 
B 1 416 TRP 416 458 458 TRP TRP B . n 
B 1 417 ARG 417 459 459 ARG ARG B . n 
B 1 418 ASP 418 460 460 ASP ASP B . n 
B 1 419 LEU 419 461 461 LEU LEU B . n 
B 1 420 HIS 420 462 462 HIS HIS B . n 
B 1 421 HIS 421 463 463 HIS HIS B . n 
B 1 422 ILE 422 464 464 ILE ILE B . n 
B 1 423 ILE 423 465 465 ILE ILE B . n 
B 1 424 ALA 424 466 466 ALA ALA B . n 
B 1 425 LEU 425 467 467 LEU LEU B . n 
B 1 426 LEU 426 468 468 LEU LEU B . n 
B 1 427 PHE 427 469 469 PHE PHE B . n 
B 1 428 ASP 428 470 470 ASP ASP B . n 
B 1 429 LYS 429 471 471 LYS LYS B . n 
B 1 430 ALA 430 472 472 ALA ALA B . n 
B 1 431 ASP 431 473 473 ASP ASP B . n 
B 1 432 PRO 432 474 474 PRO PRO B . n 
B 1 433 THR 433 475 475 THR THR B . n 
B 1 434 GLN 434 476 476 GLN GLN B . n 
B 1 435 GLU 435 477 477 GLU GLU B . n 
B 1 436 GLN 436 478 478 GLN GLN B . n 
B 1 437 LYS 437 479 479 LYS LYS B . n 
B 1 438 ALA 438 480 480 ALA ALA B . n 
B 1 439 ASP 439 481 481 ASP ASP B . n 
B 1 440 ALA 440 482 482 ALA ALA B . n 
B 1 441 CYS 441 483 483 CYS CYS B . n 
B 1 442 TYR 442 484 484 TYR TYR B . n 
B 1 443 ARG 443 485 485 ARG ARG B . n 
B 1 444 GLU 444 486 486 GLU GLU B . n 
B 1 445 LEU 445 487 487 LEU LEU B . n 
B 1 446 VAL 446 488 488 VAL VAL B . n 
B 1 447 THR 447 489 489 THR THR B . n 
B 1 448 ARG 448 490 490 ARG ARG B . n 
B 1 449 PHE 449 491 491 PHE PHE B . n 
B 1 450 GLY 450 492 492 GLY GLY B . n 
B 1 451 ALA 451 493 493 ALA ALA B . n 
B 1 452 GLN 452 494 494 GLN GLN B . n 
B 1 453 GLY 453 495 495 GLY GLY B . n 
B 1 454 TRP 454 496 496 TRP TRP B . n 
B 1 455 ALA 455 497 497 ALA ALA B . n 
B 1 456 SER 456 498 498 SER SER B . n 
B 1 457 TYR 457 499 499 TYR TYR B . n 
B 1 458 ARG 458 500 500 ARG ARG B . n 
B 1 459 THR 459 501 501 THR THR B . n 
B 1 460 GLY 460 502 502 GLY GLY B . n 
B 1 461 VAL 461 503 503 VAL VAL B . n 
B 1 462 ASN 462 504 504 ASN ASN B . n 
B 1 463 SER 463 505 505 SER SER B . n 
B 1 464 MET 464 506 506 MET MET B . n 
B 1 465 ASP 465 507 507 ASP ASP B . n 
B 1 466 LEU 466 508 508 LEU LEU B . n 
B 1 467 VAL 467 509 509 VAL VAL B . n 
B 1 468 ALA 468 510 510 ALA ALA B . n 
B 1 469 GLN 469 511 511 GLN GLN B . n 
B 1 470 GLN 470 512 512 GLN GLN B . n 
B 1 471 TYR 471 513 513 TYR TYR B . n 
B 1 472 GLY 472 514 514 GLY GLY B . n 
B 1 473 GLU 473 515 515 GLU GLU B . n 
B 1 474 VAL 474 516 516 VAL VAL B . n 
B 1 475 ASN 475 517 517 ASN ASN B . n 
B 1 476 ARG 476 518 518 ARG ARG B . n 
B 1 477 ASP 477 519 519 ASP ASP B . n 
B 1 478 PHE 478 520 520 PHE PHE B . n 
B 1 479 ASN 479 521 521 ASN ASN B . n 
B 1 480 ARG 480 522 522 ARG ARG B . n 
B 1 481 THR 481 523 523 THR THR B . n 
B 1 482 LEU 482 524 524 LEU LEU B . n 
B 1 483 LYS 483 525 525 LYS LYS B . n 
B 1 484 ARG 484 526 526 ARG ARG B . n 
B 1 485 ALA 485 527 527 ALA ALA B . n 
B 1 486 ILE 486 528 528 ILE ILE B . n 
B 1 487 ASP 487 529 529 ASP ASP B . n 
B 1 488 PRO 488 530 530 PRO PRO B . n 
B 1 489 ASN 489 531 531 ASN ASN B . n 
B 1 490 GLY 490 532 532 GLY GLY B . n 
B 1 491 ILE 491 533 533 ILE ILE B . n 
B 1 492 LEU 492 534 534 LEU LEU B . n 
B 1 493 SER 493 535 535 SER SER B . n 
B 1 494 PRO 494 536 536 PRO PRO B . n 
B 1 495 GLY 495 537 537 GLY GLY B . n 
B 1 496 LYS 496 538 538 LYS LYS B . n 
B 1 497 SER 497 539 539 SER SER B . n 
B 1 498 GLY 498 540 540 GLY GLY B . n 
B 1 499 ILE 499 541 541 ILE ILE B . n 
B 1 500 HIS 500 542 542 HIS HIS B . n 
B 1 501 PRO 501 543 543 PRO PRO B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        V55 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   V55 
_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 
C 2 FAD 1   601  601 FAD FAD A . 
D 3 V55 1   602  602 V55 V55 A . 
E 4 GOL 1   603  605 GOL GOL A . 
F 5 PEG 1   604  606 PEG PEG A . 
G 2 FAD 1   601  601 FAD FAD B . 
H 3 V55 1   602  602 V55 V55 B . 
I 4 GOL 1   603  607 GOL GOL B . 
J 6 HOH 1   701  675 HOH HOH A . 
J 6 HOH 2   702  590 HOH HOH A . 
J 6 HOH 3   703  724 HOH HOH A . 
J 6 HOH 4   704  707 HOH HOH A . 
J 6 HOH 5   705  436 HOH HOH A . 
J 6 HOH 6   706  529 HOH HOH A . 
J 6 HOH 7   707  685 HOH HOH A . 
J 6 HOH 8   708  643 HOH HOH A . 
J 6 HOH 9   709  532 HOH HOH A . 
J 6 HOH 10  710  698 HOH HOH A . 
J 6 HOH 11  711  772 HOH HOH A . 
J 6 HOH 12  712  121 HOH HOH A . 
J 6 HOH 13  713  148 HOH HOH A . 
J 6 HOH 14  714  405 HOH HOH A . 
J 6 HOH 15  715  264 HOH HOH A . 
J 6 HOH 16  716  750 HOH HOH A . 
J 6 HOH 17  717  517 HOH HOH A . 
J 6 HOH 18  718  282 HOH HOH A . 
J 6 HOH 19  719  134 HOH HOH A . 
J 6 HOH 20  720  267 HOH HOH A . 
J 6 HOH 21  721  586 HOH HOH A . 
J 6 HOH 22  722  482 HOH HOH A . 
J 6 HOH 23  723  570 HOH HOH A . 
J 6 HOH 24  724  261 HOH HOH A . 
J 6 HOH 25  725  182 HOH HOH A . 
J 6 HOH 26  726  537 HOH HOH A . 
J 6 HOH 27  727  695 HOH HOH A . 
J 6 HOH 28  728  659 HOH HOH A . 
J 6 HOH 29  729  646 HOH HOH A . 
J 6 HOH 30  730  221 HOH HOH A . 
J 6 HOH 31  731  379 HOH HOH A . 
J 6 HOH 32  732  196 HOH HOH A . 
J 6 HOH 33  733  478 HOH HOH A . 
J 6 HOH 34  734  731 HOH HOH A . 
J 6 HOH 35  735  605 HOH HOH A . 
J 6 HOH 36  736  350 HOH HOH A . 
J 6 HOH 37  737  306 HOH HOH A . 
J 6 HOH 38  738  400 HOH HOH A . 
J 6 HOH 39  739  736 HOH HOH A . 
J 6 HOH 40  740  316 HOH HOH A . 
J 6 HOH 41  741  771 HOH HOH A . 
J 6 HOH 42  742  363 HOH HOH A . 
J 6 HOH 43  743  99  HOH HOH A . 
J 6 HOH 44  744  305 HOH HOH A . 
J 6 HOH 45  745  279 HOH HOH A . 
J 6 HOH 46  746  271 HOH HOH A . 
J 6 HOH 47  747  185 HOH HOH A . 
J 6 HOH 48  748  239 HOH HOH A . 
J 6 HOH 49  749  62  HOH HOH A . 
J 6 HOH 50  750  275 HOH HOH A . 
J 6 HOH 51  751  387 HOH HOH A . 
J 6 HOH 52  752  413 HOH HOH A . 
J 6 HOH 53  753  181 HOH HOH A . 
J 6 HOH 54  754  609 HOH HOH A . 
J 6 HOH 55  755  342 HOH HOH A . 
J 6 HOH 56  756  416 HOH HOH A . 
J 6 HOH 57  757  394 HOH HOH A . 
J 6 HOH 58  758  748 HOH HOH A . 
J 6 HOH 59  759  490 HOH HOH A . 
J 6 HOH 60  760  149 HOH HOH A . 
J 6 HOH 61  761  25  HOH HOH A . 
J 6 HOH 62  762  3   HOH HOH A . 
J 6 HOH 63  763  592 HOH HOH A . 
J 6 HOH 64  764  606 HOH HOH A . 
J 6 HOH 65  765  183 HOH HOH A . 
J 6 HOH 66  766  423 HOH HOH A . 
J 6 HOH 67  767  312 HOH HOH A . 
J 6 HOH 68  768  738 HOH HOH A . 
J 6 HOH 69  769  203 HOH HOH A . 
J 6 HOH 70  770  101 HOH HOH A . 
J 6 HOH 71  771  340 HOH HOH A . 
J 6 HOH 72  772  351 HOH HOH A . 
J 6 HOH 73  773  746 HOH HOH A . 
J 6 HOH 74  774  339 HOH HOH A . 
J 6 HOH 75  775  488 HOH HOH A . 
J 6 HOH 76  776  479 HOH HOH A . 
J 6 HOH 77  777  213 HOH HOH A . 
J 6 HOH 78  778  48  HOH HOH A . 
J 6 HOH 79  779  573 HOH HOH A . 
J 6 HOH 80  780  190 HOH HOH A . 
J 6 HOH 81  781  747 HOH HOH A . 
J 6 HOH 82  782  656 HOH HOH A . 
J 6 HOH 83  783  308 HOH HOH A . 
J 6 HOH 84  784  325 HOH HOH A . 
J 6 HOH 85  785  702 HOH HOH A . 
J 6 HOH 86  786  449 HOH HOH A . 
J 6 HOH 87  787  31  HOH HOH A . 
J 6 HOH 88  788  390 HOH HOH A . 
J 6 HOH 89  789  361 HOH HOH A . 
J 6 HOH 90  790  311 HOH HOH A . 
J 6 HOH 91  791  331 HOH HOH A . 
J 6 HOH 92  792  557 HOH HOH A . 
J 6 HOH 93  793  542 HOH HOH A . 
J 6 HOH 94  794  751 HOH HOH A . 
J 6 HOH 95  795  137 HOH HOH A . 
J 6 HOH 96  796  538 HOH HOH A . 
J 6 HOH 97  797  654 HOH HOH A . 
J 6 HOH 98  798  429 HOH HOH A . 
J 6 HOH 99  799  177 HOH HOH A . 
J 6 HOH 100 800  539 HOH HOH A . 
J 6 HOH 101 801  166 HOH HOH A . 
J 6 HOH 102 802  208 HOH HOH A . 
J 6 HOH 103 803  69  HOH HOH A . 
J 6 HOH 104 804  332 HOH HOH A . 
J 6 HOH 105 805  531 HOH HOH A . 
J 6 HOH 106 806  138 HOH HOH A . 
J 6 HOH 107 807  483 HOH HOH A . 
J 6 HOH 108 808  481 HOH HOH A . 
J 6 HOH 109 809  397 HOH HOH A . 
J 6 HOH 110 810  74  HOH HOH A . 
J 6 HOH 111 811  286 HOH HOH A . 
J 6 HOH 112 812  109 HOH HOH A . 
J 6 HOH 113 813  425 HOH HOH A . 
J 6 HOH 114 814  186 HOH HOH A . 
J 6 HOH 115 815  35  HOH HOH A . 
J 6 HOH 116 816  132 HOH HOH A . 
J 6 HOH 117 817  144 HOH HOH A . 
J 6 HOH 118 818  749 HOH HOH A . 
J 6 HOH 119 819  153 HOH HOH A . 
J 6 HOH 120 820  38  HOH HOH A . 
J 6 HOH 121 821  197 HOH HOH A . 
J 6 HOH 122 822  377 HOH HOH A . 
J 6 HOH 123 823  376 HOH HOH A . 
J 6 HOH 124 824  15  HOH HOH A . 
J 6 HOH 125 825  441 HOH HOH A . 
J 6 HOH 126 826  83  HOH HOH A . 
J 6 HOH 127 827  272 HOH HOH A . 
J 6 HOH 128 828  314 HOH HOH A . 
J 6 HOH 129 829  164 HOH HOH A . 
J 6 HOH 130 830  73  HOH HOH A . 
J 6 HOH 131 831  556 HOH HOH A . 
J 6 HOH 132 832  460 HOH HOH A . 
J 6 HOH 133 833  318 HOH HOH A . 
J 6 HOH 134 834  295 HOH HOH A . 
J 6 HOH 135 835  770 HOH HOH A . 
J 6 HOH 136 836  56  HOH HOH A . 
J 6 HOH 137 837  354 HOH HOH A . 
J 6 HOH 138 838  22  HOH HOH A . 
J 6 HOH 139 839  422 HOH HOH A . 
J 6 HOH 140 840  206 HOH HOH A . 
J 6 HOH 141 841  10  HOH HOH A . 
J 6 HOH 142 842  597 HOH HOH A . 
J 6 HOH 143 843  86  HOH HOH A . 
J 6 HOH 144 844  106 HOH HOH A . 
J 6 HOH 145 845  330 HOH HOH A . 
J 6 HOH 146 846  366 HOH HOH A . 
J 6 HOH 147 847  9   HOH HOH A . 
J 6 HOH 148 848  432 HOH HOH A . 
J 6 HOH 149 849  336 HOH HOH A . 
J 6 HOH 150 850  326 HOH HOH A . 
J 6 HOH 151 851  111 HOH HOH A . 
J 6 HOH 152 852  362 HOH HOH A . 
J 6 HOH 153 853  59  HOH HOH A . 
J 6 HOH 154 854  356 HOH HOH A . 
J 6 HOH 155 855  52  HOH HOH A . 
J 6 HOH 156 856  159 HOH HOH A . 
J 6 HOH 157 857  252 HOH HOH A . 
J 6 HOH 158 858  359 HOH HOH A . 
J 6 HOH 159 859  16  HOH HOH A . 
J 6 HOH 160 860  216 HOH HOH A . 
J 6 HOH 161 861  578 HOH HOH A . 
J 6 HOH 162 862  165 HOH HOH A . 
J 6 HOH 163 863  210 HOH HOH A . 
J 6 HOH 164 864  180 HOH HOH A . 
J 6 HOH 165 865  130 HOH HOH A . 
J 6 HOH 166 866  167 HOH HOH A . 
J 6 HOH 167 867  269 HOH HOH A . 
J 6 HOH 168 868  158 HOH HOH A . 
J 6 HOH 169 869  638 HOH HOH A . 
J 6 HOH 170 870  95  HOH HOH A . 
J 6 HOH 171 871  226 HOH HOH A . 
J 6 HOH 172 872  561 HOH HOH A . 
J 6 HOH 173 873  637 HOH HOH A . 
J 6 HOH 174 874  580 HOH HOH A . 
J 6 HOH 175 875  648 HOH HOH A . 
J 6 HOH 176 876  6   HOH HOH A . 
J 6 HOH 177 877  77  HOH HOH A . 
J 6 HOH 178 878  100 HOH HOH A . 
J 6 HOH 179 879  346 HOH HOH A . 
J 6 HOH 180 880  450 HOH HOH A . 
J 6 HOH 181 881  110 HOH HOH A . 
J 6 HOH 182 882  369 HOH HOH A . 
J 6 HOH 183 883  57  HOH HOH A . 
J 6 HOH 184 884  80  HOH HOH A . 
J 6 HOH 185 885  41  HOH HOH A . 
J 6 HOH 186 886  20  HOH HOH A . 
J 6 HOH 187 887  486 HOH HOH A . 
J 6 HOH 188 888  575 HOH HOH A . 
J 6 HOH 189 889  211 HOH HOH A . 
J 6 HOH 190 890  92  HOH HOH A . 
J 6 HOH 191 891  79  HOH HOH A . 
J 6 HOH 192 892  232 HOH HOH A . 
J 6 HOH 193 893  514 HOH HOH A . 
J 6 HOH 194 894  407 HOH HOH A . 
J 6 HOH 195 895  75  HOH HOH A . 
J 6 HOH 196 896  12  HOH HOH A . 
J 6 HOH 197 897  188 HOH HOH A . 
J 6 HOH 198 898  382 HOH HOH A . 
J 6 HOH 199 899  552 HOH HOH A . 
J 6 HOH 200 900  119 HOH HOH A . 
J 6 HOH 201 901  117 HOH HOH A . 
J 6 HOH 202 902  11  HOH HOH A . 
J 6 HOH 203 903  112 HOH HOH A . 
J 6 HOH 204 904  729 HOH HOH A . 
J 6 HOH 205 905  526 HOH HOH A . 
J 6 HOH 206 906  227 HOH HOH A . 
J 6 HOH 207 907  642 HOH HOH A . 
J 6 HOH 208 908  424 HOH HOH A . 
J 6 HOH 209 909  120 HOH HOH A . 
J 6 HOH 210 910  600 HOH HOH A . 
J 6 HOH 211 911  129 HOH HOH A . 
J 6 HOH 212 912  147 HOH HOH A . 
J 6 HOH 213 913  21  HOH HOH A . 
J 6 HOH 214 914  555 HOH HOH A . 
J 6 HOH 215 915  191 HOH HOH A . 
J 6 HOH 216 916  294 HOH HOH A . 
J 6 HOH 217 917  489 HOH HOH A . 
J 6 HOH 218 918  610 HOH HOH A . 
J 6 HOH 219 919  402 HOH HOH A . 
J 6 HOH 220 920  222 HOH HOH A . 
J 6 HOH 221 921  4   HOH HOH A . 
J 6 HOH 222 922  781 HOH HOH A . 
J 6 HOH 223 923  54  HOH HOH A . 
J 6 HOH 224 924  292 HOH HOH A . 
J 6 HOH 225 925  303 HOH HOH A . 
J 6 HOH 226 926  93  HOH HOH A . 
J 6 HOH 227 927  201 HOH HOH A . 
J 6 HOH 228 928  141 HOH HOH A . 
J 6 HOH 229 929  457 HOH HOH A . 
J 6 HOH 230 930  527 HOH HOH A . 
J 6 HOH 231 931  82  HOH HOH A . 
J 6 HOH 232 932  284 HOH HOH A . 
J 6 HOH 233 933  55  HOH HOH A . 
J 6 HOH 234 934  477 HOH HOH A . 
J 6 HOH 235 935  87  HOH HOH A . 
J 6 HOH 236 936  758 HOH HOH A . 
J 6 HOH 237 937  89  HOH HOH A . 
J 6 HOH 238 938  581 HOH HOH A . 
J 6 HOH 239 939  139 HOH HOH A . 
J 6 HOH 240 940  151 HOH HOH A . 
J 6 HOH 241 941  50  HOH HOH A . 
J 6 HOH 242 942  266 HOH HOH A . 
J 6 HOH 243 943  611 HOH HOH A . 
J 6 HOH 244 944  415 HOH HOH A . 
J 6 HOH 245 945  473 HOH HOH A . 
J 6 HOH 246 946  739 HOH HOH A . 
J 6 HOH 247 947  176 HOH HOH A . 
J 6 HOH 248 948  178 HOH HOH A . 
J 6 HOH 249 949  94  HOH HOH A . 
J 6 HOH 250 950  91  HOH HOH A . 
J 6 HOH 251 951  711 HOH HOH A . 
J 6 HOH 252 952  315 HOH HOH A . 
J 6 HOH 253 953  499 HOH HOH A . 
J 6 HOH 254 954  194 HOH HOH A . 
J 6 HOH 255 955  378 HOH HOH A . 
J 6 HOH 256 956  353 HOH HOH A . 
J 6 HOH 257 957  371 HOH HOH A . 
J 6 HOH 258 958  666 HOH HOH A . 
J 6 HOH 259 959  163 HOH HOH A . 
J 6 HOH 260 960  338 HOH HOH A . 
J 6 HOH 261 961  44  HOH HOH A . 
J 6 HOH 262 962  501 HOH HOH A . 
J 6 HOH 263 963  281 HOH HOH A . 
J 6 HOH 264 964  558 HOH HOH A . 
J 6 HOH 265 965  735 HOH HOH A . 
J 6 HOH 266 966  263 HOH HOH A . 
J 6 HOH 267 967  458 HOH HOH A . 
J 6 HOH 268 968  84  HOH HOH A . 
J 6 HOH 269 969  474 HOH HOH A . 
J 6 HOH 270 970  584 HOH HOH A . 
J 6 HOH 271 971  37  HOH HOH A . 
J 6 HOH 272 972  773 HOH HOH A . 
J 6 HOH 273 973  317 HOH HOH A . 
J 6 HOH 274 974  375 HOH HOH A . 
J 6 HOH 275 975  192 HOH HOH A . 
J 6 HOH 276 976  304 HOH HOH A . 
J 6 HOH 277 977  632 HOH HOH A . 
J 6 HOH 278 978  635 HOH HOH A . 
J 6 HOH 279 979  372 HOH HOH A . 
J 6 HOH 280 980  674 HOH HOH A . 
J 6 HOH 281 981  229 HOH HOH A . 
J 6 HOH 282 982  470 HOH HOH A . 
J 6 HOH 283 983  225 HOH HOH A . 
J 6 HOH 284 984  636 HOH HOH A . 
J 6 HOH 285 985  492 HOH HOH A . 
J 6 HOH 286 986  122 HOH HOH A . 
J 6 HOH 287 987  708 HOH HOH A . 
J 6 HOH 288 988  491 HOH HOH A . 
J 6 HOH 289 989  285 HOH HOH A . 
J 6 HOH 290 990  498 HOH HOH A . 
J 6 HOH 291 991  146 HOH HOH A . 
J 6 HOH 292 992  193 HOH HOH A . 
J 6 HOH 293 993  515 HOH HOH A . 
J 6 HOH 294 994  560 HOH HOH A . 
J 6 HOH 295 995  428 HOH HOH A . 
J 6 HOH 296 996  540 HOH HOH A . 
J 6 HOH 297 997  741 HOH HOH A . 
J 6 HOH 298 998  126 HOH HOH A . 
J 6 HOH 299 999  554 HOH HOH A . 
J 6 HOH 300 1000 533 HOH HOH A . 
J 6 HOH 301 1001 310 HOH HOH A . 
J 6 HOH 302 1002 440 HOH HOH A . 
J 6 HOH 303 1003 421 HOH HOH A . 
J 6 HOH 304 1004 650 HOH HOH A . 
J 6 HOH 305 1005 172 HOH HOH A . 
J 6 HOH 306 1006 475 HOH HOH A . 
J 6 HOH 307 1007 96  HOH HOH A . 
J 6 HOH 308 1008 509 HOH HOH A . 
J 6 HOH 309 1009 651 HOH HOH A . 
J 6 HOH 310 1010 238 HOH HOH A . 
J 6 HOH 311 1011 1   HOH HOH A . 
J 6 HOH 312 1012 448 HOH HOH A . 
J 6 HOH 313 1013 195 HOH HOH A . 
J 6 HOH 314 1014 299 HOH HOH A . 
J 6 HOH 315 1015 494 HOH HOH A . 
J 6 HOH 316 1016 334 HOH HOH A . 
J 6 HOH 317 1017 550 HOH HOH A . 
J 6 HOH 318 1018 640 HOH HOH A . 
J 6 HOH 319 1019 631 HOH HOH A . 
J 6 HOH 320 1020 427 HOH HOH A . 
J 6 HOH 321 1021 725 HOH HOH A . 
J 6 HOH 322 1022 302 HOH HOH A . 
J 6 HOH 323 1023 777 HOH HOH A . 
J 6 HOH 324 1024 453 HOH HOH A . 
J 6 HOH 325 1025 680 HOH HOH A . 
J 6 HOH 326 1026 766 HOH HOH A . 
J 6 HOH 327 1027 677 HOH HOH A . 
J 6 HOH 328 1028 614 HOH HOH A . 
J 6 HOH 329 1029 791 HOH HOH A . 
J 6 HOH 330 1030 465 HOH HOH A . 
J 6 HOH 331 1031 150 HOH HOH A . 
J 6 HOH 332 1032 546 HOH HOH A . 
J 6 HOH 333 1033 383 HOH HOH A . 
J 6 HOH 334 1034 549 HOH HOH A . 
J 6 HOH 335 1035 320 HOH HOH A . 
J 6 HOH 336 1036 445 HOH HOH A . 
J 6 HOH 337 1037 661 HOH HOH A . 
J 6 HOH 338 1038 629 HOH HOH A . 
J 6 HOH 339 1039 401 HOH HOH A . 
J 6 HOH 340 1040 323 HOH HOH A . 
J 6 HOH 341 1041 785 HOH HOH A . 
J 6 HOH 342 1042 601 HOH HOH A . 
J 6 HOH 343 1043 617 HOH HOH A . 
J 6 HOH 344 1044 567 HOH HOH A . 
J 6 HOH 345 1045 170 HOH HOH A . 
J 6 HOH 346 1046 587 HOH HOH A . 
J 6 HOH 347 1047 668 HOH HOH A . 
J 6 HOH 348 1048 464 HOH HOH A . 
J 6 HOH 349 1049 291 HOH HOH A . 
J 6 HOH 350 1050 408 HOH HOH A . 
J 6 HOH 351 1051 576 HOH HOH A . 
J 6 HOH 352 1052 595 HOH HOH A . 
J 6 HOH 353 1053 684 HOH HOH A . 
J 6 HOH 354 1054 525 HOH HOH A . 
J 6 HOH 355 1055 476 HOH HOH A . 
J 6 HOH 356 1056 683 HOH HOH A . 
J 6 HOH 357 1057 717 HOH HOH A . 
J 6 HOH 358 1058 794 HOH HOH A . 
J 6 HOH 359 1059 395 HOH HOH A . 
J 6 HOH 360 1060 516 HOH HOH A . 
J 6 HOH 361 1061 386 HOH HOH A . 
J 6 HOH 362 1062 511 HOH HOH A . 
J 6 HOH 363 1063 755 HOH HOH A . 
J 6 HOH 364 1064 564 HOH HOH A . 
J 6 HOH 365 1065 349 HOH HOH A . 
J 6 HOH 366 1066 628 HOH HOH A . 
J 6 HOH 367 1067 582 HOH HOH A . 
J 6 HOH 368 1068 417 HOH HOH A . 
J 6 HOH 369 1069 681 HOH HOH A . 
J 6 HOH 370 1070 467 HOH HOH A . 
J 6 HOH 371 1071 721 HOH HOH A . 
J 6 HOH 372 1072 471 HOH HOH A . 
J 6 HOH 373 1073 669 HOH HOH A . 
J 6 HOH 374 1074 504 HOH HOH A . 
J 6 HOH 375 1075 585 HOH HOH A . 
J 6 HOH 376 1076 236 HOH HOH A . 
J 6 HOH 377 1077 534 HOH HOH A . 
J 6 HOH 378 1078 493 HOH HOH A . 
J 6 HOH 379 1079 410 HOH HOH A . 
J 6 HOH 380 1080 283 HOH HOH A . 
J 6 HOH 381 1081 693 HOH HOH A . 
K 6 HOH 1   701  764 HOH HOH B . 
K 6 HOH 2   702  704 HOH HOH B . 
K 6 HOH 3   703  406 HOH HOH B . 
K 6 HOH 4   704  645 HOH HOH B . 
K 6 HOH 5   705  487 HOH HOH B . 
K 6 HOH 6   706  443 HOH HOH B . 
K 6 HOH 7   707  653 HOH HOH B . 
K 6 HOH 8   708  767 HOH HOH B . 
K 6 HOH 9   709  665 HOH HOH B . 
K 6 HOH 10  710  701 HOH HOH B . 
K 6 HOH 11  711  404 HOH HOH B . 
K 6 HOH 12  712  524 HOH HOH B . 
K 6 HOH 13  713  733 HOH HOH B . 
K 6 HOH 14  714  105 HOH HOH B . 
K 6 HOH 15  715  90  HOH HOH B . 
K 6 HOH 16  716  345 HOH HOH B . 
K 6 HOH 17  717  173 HOH HOH B . 
K 6 HOH 18  718  782 HOH HOH B . 
K 6 HOH 19  719  396 HOH HOH B . 
K 6 HOH 20  720  246 HOH HOH B . 
K 6 HOH 21  721  171 HOH HOH B . 
K 6 HOH 22  722  219 HOH HOH B . 
K 6 HOH 23  723  253 HOH HOH B . 
K 6 HOH 24  724  355 HOH HOH B . 
K 6 HOH 25  725  329 HOH HOH B . 
K 6 HOH 26  726  679 HOH HOH B . 
K 6 HOH 27  727  274 HOH HOH B . 
K 6 HOH 28  728  187 HOH HOH B . 
K 6 HOH 29  729  594 HOH HOH B . 
K 6 HOH 30  730  374 HOH HOH B . 
K 6 HOH 31  731  131 HOH HOH B . 
K 6 HOH 32  732  774 HOH HOH B . 
K 6 HOH 33  733  463 HOH HOH B . 
K 6 HOH 34  734  510 HOH HOH B . 
K 6 HOH 35  735  287 HOH HOH B . 
K 6 HOH 36  736  503 HOH HOH B . 
K 6 HOH 37  737  591 HOH HOH B . 
K 6 HOH 38  738  381 HOH HOH B . 
K 6 HOH 39  739  430 HOH HOH B . 
K 6 HOH 40  740  352 HOH HOH B . 
K 6 HOH 41  741  528 HOH HOH B . 
K 6 HOH 42  742  485 HOH HOH B . 
K 6 HOH 43  743  136 HOH HOH B . 
K 6 HOH 44  744  155 HOH HOH B . 
K 6 HOH 45  745  522 HOH HOH B . 
K 6 HOH 46  746  776 HOH HOH B . 
K 6 HOH 47  747  78  HOH HOH B . 
K 6 HOH 48  748  545 HOH HOH B . 
K 6 HOH 49  749  365 HOH HOH B . 
K 6 HOH 50  750  273 HOH HOH B . 
K 6 HOH 51  751  603 HOH HOH B . 
K 6 HOH 52  752  290 HOH HOH B . 
K 6 HOH 53  753  88  HOH HOH B . 
K 6 HOH 54  754  472 HOH HOH B . 
K 6 HOH 55  755  360 HOH HOH B . 
K 6 HOH 56  756  64  HOH HOH B . 
K 6 HOH 57  757  322 HOH HOH B . 
K 6 HOH 58  758  728 HOH HOH B . 
K 6 HOH 59  759  33  HOH HOH B . 
K 6 HOH 60  760  162 HOH HOH B . 
K 6 HOH 61  761  175 HOH HOH B . 
K 6 HOH 62  762  391 HOH HOH B . 
K 6 HOH 63  763  388 HOH HOH B . 
K 6 HOH 64  764  411 HOH HOH B . 
K 6 HOH 65  765  293 HOH HOH B . 
K 6 HOH 66  766  752 HOH HOH B . 
K 6 HOH 67  767  168 HOH HOH B . 
K 6 HOH 68  768  198 HOH HOH B . 
K 6 HOH 69  769  446 HOH HOH B . 
K 6 HOH 70  770  495 HOH HOH B . 
K 6 HOH 71  771  468 HOH HOH B . 
K 6 HOH 72  772  270 HOH HOH B . 
K 6 HOH 73  773  689 HOH HOH B . 
K 6 HOH 74  774  604 HOH HOH B . 
K 6 HOH 75  775  358 HOH HOH B . 
K 6 HOH 76  776  276 HOH HOH B . 
K 6 HOH 77  777  319 HOH HOH B . 
K 6 HOH 78  778  367 HOH HOH B . 
K 6 HOH 79  779  128 HOH HOH B . 
K 6 HOH 80  780  189 HOH HOH B . 
K 6 HOH 81  781  480 HOH HOH B . 
K 6 HOH 82  782  24  HOH HOH B . 
K 6 HOH 83  783  434 HOH HOH B . 
K 6 HOH 84  784  572 HOH HOH B . 
K 6 HOH 85  785  47  HOH HOH B . 
K 6 HOH 86  786  452 HOH HOH B . 
K 6 HOH 87  787  250 HOH HOH B . 
K 6 HOH 88  788  243 HOH HOH B . 
K 6 HOH 89  789  277 HOH HOH B . 
K 6 HOH 90  790  71  HOH HOH B . 
K 6 HOH 91  791  19  HOH HOH B . 
K 6 HOH 92  792  762 HOH HOH B . 
K 6 HOH 93  793  280 HOH HOH B . 
K 6 HOH 94  794  431 HOH HOH B . 
K 6 HOH 95  795  742 HOH HOH B . 
K 6 HOH 96  796  209 HOH HOH B . 
K 6 HOH 97  797  536 HOH HOH B . 
K 6 HOH 98  798  779 HOH HOH B . 
K 6 HOH 99  799  237 HOH HOH B . 
K 6 HOH 100 800  321 HOH HOH B . 
K 6 HOH 101 801  215 HOH HOH B . 
K 6 HOH 102 802  333 HOH HOH B . 
K 6 HOH 103 803  444 HOH HOH B . 
K 6 HOH 104 804  256 HOH HOH B . 
K 6 HOH 105 805  341 HOH HOH B . 
K 6 HOH 106 806  563 HOH HOH B . 
K 6 HOH 107 807  641 HOH HOH B . 
K 6 HOH 108 808  68  HOH HOH B . 
K 6 HOH 109 809  548 HOH HOH B . 
K 6 HOH 110 810  743 HOH HOH B . 
K 6 HOH 111 811  241 HOH HOH B . 
K 6 HOH 112 812  753 HOH HOH B . 
K 6 HOH 113 813  7   HOH HOH B . 
K 6 HOH 114 814  228 HOH HOH B . 
K 6 HOH 115 815  652 HOH HOH B . 
K 6 HOH 116 816  60  HOH HOH B . 
K 6 HOH 117 817  125 HOH HOH B . 
K 6 HOH 118 818  98  HOH HOH B . 
K 6 HOH 119 819  553 HOH HOH B . 
K 6 HOH 120 820  13  HOH HOH B . 
K 6 HOH 121 821  438 HOH HOH B . 
K 6 HOH 122 822  224 HOH HOH B . 
K 6 HOH 123 823  97  HOH HOH B . 
K 6 HOH 124 824  745 HOH HOH B . 
K 6 HOH 125 825  298 HOH HOH B . 
K 6 HOH 126 826  212 HOH HOH B . 
K 6 HOH 127 827  223 HOH HOH B . 
K 6 HOH 128 828  32  HOH HOH B . 
K 6 HOH 129 829  392 HOH HOH B . 
K 6 HOH 130 830  81  HOH HOH B . 
K 6 HOH 131 831  157 HOH HOH B . 
K 6 HOH 132 832  217 HOH HOH B . 
K 6 HOH 133 833  14  HOH HOH B . 
K 6 HOH 134 834  714 HOH HOH B . 
K 6 HOH 135 835  257 HOH HOH B . 
K 6 HOH 136 836  574 HOH HOH B . 
K 6 HOH 137 837  719 HOH HOH B . 
K 6 HOH 138 838  76  HOH HOH B . 
K 6 HOH 139 839  142 HOH HOH B . 
K 6 HOH 140 840  409 HOH HOH B . 
K 6 HOH 141 841  716 HOH HOH B . 
K 6 HOH 142 842  730 HOH HOH B . 
K 6 HOH 143 843  399 HOH HOH B . 
K 6 HOH 144 844  506 HOH HOH B . 
K 6 HOH 145 845  36  HOH HOH B . 
K 6 HOH 146 846  518 HOH HOH B . 
K 6 HOH 147 847  459 HOH HOH B . 
K 6 HOH 148 848  114 HOH HOH B . 
K 6 HOH 149 849  145 HOH HOH B . 
K 6 HOH 150 850  43  HOH HOH B . 
K 6 HOH 151 851  34  HOH HOH B . 
K 6 HOH 152 852  67  HOH HOH B . 
K 6 HOH 153 853  200 HOH HOH B . 
K 6 HOH 154 854  598 HOH HOH B . 
K 6 HOH 155 855  278 HOH HOH B . 
K 6 HOH 156 856  179 HOH HOH B . 
K 6 HOH 157 857  520 HOH HOH B . 
K 6 HOH 158 858  27  HOH HOH B . 
K 6 HOH 159 859  727 HOH HOH B . 
K 6 HOH 160 860  713 HOH HOH B . 
K 6 HOH 161 861  327 HOH HOH B . 
K 6 HOH 162 862  300 HOH HOH B . 
K 6 HOH 163 863  107 HOH HOH B . 
K 6 HOH 164 864  118 HOH HOH B . 
K 6 HOH 165 865  389 HOH HOH B . 
K 6 HOH 166 866  30  HOH HOH B . 
K 6 HOH 167 867  309 HOH HOH B . 
K 6 HOH 168 868  116 HOH HOH B . 
K 6 HOH 169 869  248 HOH HOH B . 
K 6 HOH 170 870  135 HOH HOH B . 
K 6 HOH 171 871  154 HOH HOH B . 
K 6 HOH 172 872  53  HOH HOH B . 
K 6 HOH 173 873  577 HOH HOH B . 
K 6 HOH 174 874  599 HOH HOH B . 
K 6 HOH 175 875  156 HOH HOH B . 
K 6 HOH 176 876  174 HOH HOH B . 
K 6 HOH 177 877  103 HOH HOH B . 
K 6 HOH 178 878  344 HOH HOH B . 
K 6 HOH 179 879  65  HOH HOH B . 
K 6 HOH 180 880  513 HOH HOH B . 
K 6 HOH 181 881  235 HOH HOH B . 
K 6 HOH 182 882  454 HOH HOH B . 
K 6 HOH 183 883  8   HOH HOH B . 
K 6 HOH 184 884  5   HOH HOH B . 
K 6 HOH 185 885  39  HOH HOH B . 
K 6 HOH 186 886  547 HOH HOH B . 
K 6 HOH 187 887  17  HOH HOH B . 
K 6 HOH 188 888  469 HOH HOH B . 
K 6 HOH 189 889  220 HOH HOH B . 
K 6 HOH 190 890  104 HOH HOH B . 
K 6 HOH 191 891  108 HOH HOH B . 
K 6 HOH 192 892  780 HOH HOH B . 
K 6 HOH 193 893  255 HOH HOH B . 
K 6 HOH 194 894  259 HOH HOH B . 
K 6 HOH 195 895  61  HOH HOH B . 
K 6 HOH 196 896  58  HOH HOH B . 
K 6 HOH 197 897  521 HOH HOH B . 
K 6 HOH 198 898  23  HOH HOH B . 
K 6 HOH 199 899  18  HOH HOH B . 
K 6 HOH 200 900  519 HOH HOH B . 
K 6 HOH 201 901  744 HOH HOH B . 
K 6 HOH 202 902  385 HOH HOH B . 
K 6 HOH 203 903  260 HOH HOH B . 
K 6 HOH 204 904  70  HOH HOH B . 
K 6 HOH 205 905  433 HOH HOH B . 
K 6 HOH 206 906  123 HOH HOH B . 
K 6 HOH 207 907  113 HOH HOH B . 
K 6 HOH 208 908  664 HOH HOH B . 
K 6 HOH 209 909  569 HOH HOH B . 
K 6 HOH 210 910  740 HOH HOH B . 
K 6 HOH 211 911  258 HOH HOH B . 
K 6 HOH 212 912  63  HOH HOH B . 
K 6 HOH 213 913  102 HOH HOH B . 
K 6 HOH 214 914  541 HOH HOH B . 
K 6 HOH 215 915  757 HOH HOH B . 
K 6 HOH 216 916  435 HOH HOH B . 
K 6 HOH 217 917  40  HOH HOH B . 
K 6 HOH 218 918  589 HOH HOH B . 
K 6 HOH 219 919  364 HOH HOH B . 
K 6 HOH 220 920  184 HOH HOH B . 
K 6 HOH 221 921  462 HOH HOH B . 
K 6 HOH 222 922  214 HOH HOH B . 
K 6 HOH 223 923  709 HOH HOH B . 
K 6 HOH 224 924  265 HOH HOH B . 
K 6 HOH 225 925  169 HOH HOH B . 
K 6 HOH 226 926  115 HOH HOH B . 
K 6 HOH 227 927  202 HOH HOH B . 
K 6 HOH 228 928  42  HOH HOH B . 
K 6 HOH 229 929  160 HOH HOH B . 
K 6 HOH 230 930  307 HOH HOH B . 
K 6 HOH 231 931  602 HOH HOH B . 
K 6 HOH 232 932  231 HOH HOH B . 
K 6 HOH 233 933  505 HOH HOH B . 
K 6 HOH 234 934  204 HOH HOH B . 
K 6 HOH 235 935  335 HOH HOH B . 
K 6 HOH 236 936  671 HOH HOH B . 
K 6 HOH 237 937  368 HOH HOH B . 
K 6 HOH 238 938  384 HOH HOH B . 
K 6 HOH 239 939  28  HOH HOH B . 
K 6 HOH 240 940  442 HOH HOH B . 
K 6 HOH 241 941  268 HOH HOH B . 
K 6 HOH 242 942  288 HOH HOH B . 
K 6 HOH 243 943  143 HOH HOH B . 
K 6 HOH 244 944  234 HOH HOH B . 
K 6 HOH 245 945  508 HOH HOH B . 
K 6 HOH 246 946  262 HOH HOH B . 
K 6 HOH 247 947  124 HOH HOH B . 
K 6 HOH 248 948  583 HOH HOH B . 
K 6 HOH 249 949  29  HOH HOH B . 
K 6 HOH 250 950  496 HOH HOH B . 
K 6 HOH 251 951  127 HOH HOH B . 
K 6 HOH 252 952  596 HOH HOH B . 
K 6 HOH 253 953  530 HOH HOH B . 
K 6 HOH 254 954  313 HOH HOH B . 
K 6 HOH 255 955  763 HOH HOH B . 
K 6 HOH 256 956  678 HOH HOH B . 
K 6 HOH 257 957  414 HOH HOH B . 
K 6 HOH 258 958  199 HOH HOH B . 
K 6 HOH 259 959  49  HOH HOH B . 
K 6 HOH 260 960  26  HOH HOH B . 
K 6 HOH 261 961  712 HOH HOH B . 
K 6 HOH 262 962  398 HOH HOH B . 
K 6 HOH 263 963  568 HOH HOH B . 
K 6 HOH 264 964  296 HOH HOH B . 
K 6 HOH 265 965  85  HOH HOH B . 
K 6 HOH 266 966  571 HOH HOH B . 
K 6 HOH 267 967  45  HOH HOH B . 
K 6 HOH 268 968  140 HOH HOH B . 
K 6 HOH 269 969  566 HOH HOH B . 
K 6 HOH 270 970  152 HOH HOH B . 
K 6 HOH 271 971  795 HOH HOH B . 
K 6 HOH 272 972  696 HOH HOH B . 
K 6 HOH 273 973  551 HOH HOH B . 
K 6 HOH 274 974  412 HOH HOH B . 
K 6 HOH 275 975  244 HOH HOH B . 
K 6 HOH 276 976  688 HOH HOH B . 
K 6 HOH 277 977  230 HOH HOH B . 
K 6 HOH 278 978  370 HOH HOH B . 
K 6 HOH 279 979  420 HOH HOH B . 
K 6 HOH 280 980  161 HOH HOH B . 
K 6 HOH 281 981  247 HOH HOH B . 
K 6 HOH 282 982  218 HOH HOH B . 
K 6 HOH 283 983  759 HOH HOH B . 
K 6 HOH 284 984  734 HOH HOH B . 
K 6 HOH 285 985  466 HOH HOH B . 
K 6 HOH 286 986  393 HOH HOH B . 
K 6 HOH 287 987  249 HOH HOH B . 
K 6 HOH 288 988  240 HOH HOH B . 
K 6 HOH 289 989  348 HOH HOH B . 
K 6 HOH 290 990  461 HOH HOH B . 
K 6 HOH 291 991  343 HOH HOH B . 
K 6 HOH 292 992  324 HOH HOH B . 
K 6 HOH 293 993  51  HOH HOH B . 
K 6 HOH 294 994  254 HOH HOH B . 
K 6 HOH 295 995  245 HOH HOH B . 
K 6 HOH 296 996  46  HOH HOH B . 
K 6 HOH 297 997  133 HOH HOH B . 
K 6 HOH 298 998  205 HOH HOH B . 
K 6 HOH 299 999  705 HOH HOH B . 
K 6 HOH 300 1000 72  HOH HOH B . 
K 6 HOH 301 1001 544 HOH HOH B . 
K 6 HOH 302 1002 233 HOH HOH B . 
K 6 HOH 303 1003 543 HOH HOH B . 
K 6 HOH 304 1004 207 HOH HOH B . 
K 6 HOH 305 1005 66  HOH HOH B . 
K 6 HOH 306 1006 691 HOH HOH B . 
K 6 HOH 307 1007 451 HOH HOH B . 
K 6 HOH 308 1008 737 HOH HOH B . 
K 6 HOH 309 1009 455 HOH HOH B . 
K 6 HOH 310 1010 644 HOH HOH B . 
K 6 HOH 311 1011 380 HOH HOH B . 
K 6 HOH 312 1012 624 HOH HOH B . 
K 6 HOH 313 1013 2   HOH HOH B . 
K 6 HOH 314 1014 562 HOH HOH B . 
K 6 HOH 315 1015 289 HOH HOH B . 
K 6 HOH 316 1016 783 HOH HOH B . 
K 6 HOH 317 1017 686 HOH HOH B . 
K 6 HOH 318 1018 793 HOH HOH B . 
K 6 HOH 319 1019 627 HOH HOH B . 
K 6 HOH 320 1020 403 HOH HOH B . 
K 6 HOH 321 1021 723 HOH HOH B . 
K 6 HOH 322 1022 655 HOH HOH B . 
K 6 HOH 323 1023 593 HOH HOH B . 
K 6 HOH 324 1024 715 HOH HOH B . 
K 6 HOH 325 1025 787 HOH HOH B . 
K 6 HOH 326 1026 673 HOH HOH B . 
K 6 HOH 327 1027 687 HOH HOH B . 
K 6 HOH 328 1028 523 HOH HOH B . 
K 6 HOH 329 1029 690 HOH HOH B . 
K 6 HOH 330 1030 692 HOH HOH B . 
K 6 HOH 331 1031 790 HOH HOH B . 
K 6 HOH 332 1032 620 HOH HOH B . 
K 6 HOH 333 1033 786 HOH HOH B . 
K 6 HOH 334 1034 619 HOH HOH B . 
K 6 HOH 335 1035 607 HOH HOH B . 
K 6 HOH 336 1036 418 HOH HOH B . 
K 6 HOH 337 1037 347 HOH HOH B . 
K 6 HOH 338 1038 588 HOH HOH B . 
K 6 HOH 339 1039 301 HOH HOH B . 
K 6 HOH 340 1040 618 HOH HOH B . 
K 6 HOH 341 1041 670 HOH HOH B . 
K 6 HOH 342 1042 497 HOH HOH B . 
K 6 HOH 343 1043 699 HOH HOH B . 
K 6 HOH 344 1044 697 HOH HOH B . 
K 6 HOH 345 1045 769 HOH HOH B . 
K 6 HOH 346 1046 242 HOH HOH B . 
K 6 HOH 347 1047 507 HOH HOH B . 
K 6 HOH 348 1048 439 HOH HOH B . 
K 6 HOH 349 1049 616 HOH HOH B . 
K 6 HOH 350 1050 630 HOH HOH B . 
K 6 HOH 351 1051 357 HOH HOH B . 
K 6 HOH 352 1052 612 HOH HOH B . 
K 6 HOH 353 1053 251 HOH HOH B . 
K 6 HOH 354 1054 484 HOH HOH B . 
K 6 HOH 355 1055 608 HOH HOH B . 
K 6 HOH 356 1056 615 HOH HOH B . 
K 6 HOH 357 1057 788 HOH HOH B . 
K 6 HOH 358 1058 703 HOH HOH B . 
K 6 HOH 359 1059 694 HOH HOH B . 
K 6 HOH 360 1060 700 HOH HOH B . 
K 6 HOH 361 1061 626 HOH HOH B . 
K 6 HOH 362 1062 622 HOH HOH B . 
K 6 HOH 363 1063 621 HOH HOH B . 
K 6 HOH 364 1064 649 HOH HOH B . 
K 6 HOH 365 1065 447 HOH HOH B . 
K 6 HOH 366 1066 500 HOH HOH B . 
K 6 HOH 367 1067 565 HOH HOH B . 
K 6 HOH 368 1068 337 HOH HOH B . 
K 6 HOH 369 1069 512 HOH HOH B . 
K 6 HOH 370 1070 676 HOH HOH B . 
K 6 HOH 371 1071 579 HOH HOH B . 
K 6 HOH 372 1072 419 HOH HOH B . 
K 6 HOH 373 1073 682 HOH HOH B . 
K 6 HOH 374 1074 726 HOH HOH B . 
K 6 HOH 375 1075 559 HOH HOH B . 
K 6 HOH 376 1076 426 HOH HOH B . 
K 6 HOH 377 1077 328 HOH HOH B . 
K 6 HOH 378 1078 672 HOH HOH B . 
K 6 HOH 379 1079 789 HOH HOH B . 
K 6 HOH 380 1080 502 HOH HOH B . 
K 6 HOH 381 1081 623 HOH HOH B . 
K 6 HOH 382 1082 373 HOH HOH B . 
K 6 HOH 383 1083 625 HOH HOH B . 
K 6 HOH 384 1084 297 HOH HOH B . 
K 6 HOH 385 1085 720 HOH HOH B . 
K 6 HOH 386 1086 456 HOH HOH B . 
K 6 HOH 387 1087 768 HOH HOH B . 
K 6 HOH 388 1088 535 HOH HOH B . 
K 6 HOH 389 1089 613 HOH HOH B . 
K 6 HOH 390 1090 784 HOH HOH B . 
K 6 HOH 391 1091 718 HOH HOH B . 
# 
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 LEU 403 ? CG  ? A LEU 361 CG  
2  1 Y 1 A LEU 403 ? CD1 ? A LEU 361 CD1 
3  1 Y 1 A LEU 403 ? CD2 ? A LEU 361 CD2 
4  1 Y 1 A ASP 404 ? CG  ? A ASP 362 CG  
5  1 Y 1 A ASP 404 ? OD1 ? A ASP 362 OD1 
6  1 Y 1 A ASP 404 ? OD2 ? A ASP 362 OD2 
7  1 Y 1 A GLU 405 ? CG  ? A GLU 363 CG  
8  1 Y 1 A GLU 405 ? CD  ? A GLU 363 CD  
9  1 Y 1 A GLU 405 ? OE1 ? A GLU 363 OE1 
10 1 Y 1 A GLU 405 ? OE2 ? A GLU 363 OE2 
11 1 Y 1 B LEU 403 ? CG  ? B LEU 361 CG  
12 1 Y 1 B LEU 403 ? CD1 ? B LEU 361 CD1 
13 1 Y 1 B LEU 403 ? CD2 ? B LEU 361 CD2 
14 1 Y 1 B ASP 404 ? CG  ? B ASP 362 CG  
15 1 Y 1 B ASP 404 ? OD1 ? B ASP 362 OD1 
16 1 Y 1 B ASP 404 ? OD2 ? B ASP 362 OD2 
17 1 Y 1 B GLU 405 ? CG  ? B GLU 363 CG  
18 1 Y 1 B GLU 405 ? CD  ? B GLU 363 CD  
19 1 Y 1 B GLU 405 ? OE1 ? B GLU 363 OE1 
20 1 Y 1 B GLU 405 ? OE2 ? B GLU 363 OE2 
# 
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  ? ? ? 5.8.0405 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FGE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     91.326 
_cell.length_a_esd                 ? 
_cell.length_b                     97.824 
_cell.length_b_esd                 ? 
_cell.length_c                     129.607 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9FGE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 2 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FGE 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.62 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.08 
_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          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'PEG 20000 15%, 0.1 M MES' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.5 
# 
_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 R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-21 
_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   0.873128 
_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                        'ESRF BEAMLINE MASSIF-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.873128 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-3 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FGE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.60 
_reflns.d_resolution_low                               78.20 
_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                                     152440 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.02 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.158 
_reflns.pdbx_Rpim_I_all                                0.051 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.150 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.60 
_reflns_shell.d_res_low                                     1.63 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           67952 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7444 
_reflns_shell.percent_possible_obs                          99.3 
_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                               9.1 
_reflns_shell.pdbx_chi_squared                              1.01 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.562 
_reflns_shell.pdbx_Rpim_I_all                               0.504 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.793 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.476 
_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]                            -0.70 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.74 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.04 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               16.011 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.974 
_refine.correlation_coeff_Fo_to_Fc_free          0.965 
_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                                 9FGE 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.60 
_refine.ls_d_res_low                             78.20 
_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                     144823 
_refine.ls_number_reflns_R_free                  7529 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.49 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17650 
_refine.ls_R_factor_R_free                       0.20382 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17512 
_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                       0.080 
_refine.pdbx_overall_ESU_R_Free                  0.081 
_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                             1.633 
_refine.overall_SU_ML                            0.055 
_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                       1.60 
_refine_hist.d_res_low                        78.20 
_refine_hist.number_atoms_solvent             772 
_refine_hist.number_atoms_total               8659 
_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        7740 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         147 
_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  0.012  8100  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  7533  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.709  1.649  11023 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.579  1.566  17323 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.867  5.000  1000  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 7.739  5.000  52    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.274 10.000 1262  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.091  0.200  1172  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  9476  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1874  ? 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' ? 1.737  1.537  4006  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.737  1.537  4006  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.559  2.763  5004  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.559  2.763  5005  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.053  1.793  4094  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.053  1.794  4095  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.574  3.151  6020  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.680  16.50  9519  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.585  15.22  9328  ? 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                       1.600 
_refine_ls_shell.d_res_low                        1.642 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             541 
_refine_ls_shell.number_reflns_R_work             10574 
_refine_ls_shell.percent_reflns_obs               99.24 
_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                  0.290 
_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                  0.302 
# 
_struct.entry_id                     9FGE 
_struct.title                        'Vanillyl alcohol oxidase from Novosphingobium sp: T181D mutant in complex with vanillin' 
_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        9FGE 
_struct_keywords.text            'FAD, flavin, hydroxylase, alcohol, enzyme, FLAVOPROTEIN' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 6 ? 
K N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A3N9RU39_9SPHN 
_struct_ref.pdbx_db_accession          A0A3N9RU39 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ADFAGAMKAFRGVVGAEWVFGDEEAVVPWSKTYIPDPAHQYKPVGAVCPQSVEEVQEIVRIANTYKQPLWTVSTGKNMGY
GMTAPATPGQVVLDLKRMNRILEVDADLGTCLLEPGVTYQQLKDYLEEHKIPLWIDVPTVGPIASPVGNTLDRGVGYTPY
GEHFMFQCGMEVCLPDGRLMRTGMGSIKGSTAWQAFKWGYGPYLDGLFTQSNFGIVTKMGLWLMPKPPVYKPFMVRHANM
EDVPKIIEAMRPLRVSNLVANCNLMMSASYQLAMFKRRNEIVPDGAPLDEASLKKAASANGLGMWNTYFALYGTEQTVAG
VEPIIRATLTASGGEVLTAAEMEGNPWFHHHQTLMQGGLNLDEVGLLRWRGAGGGLAWFAPVAAARGVEAERQTALAKEI
VEKHGFDYTAAYAIGWRDLHHIIALLFDKADPTQEQKADACYRELVTRFGAQGWASYRTGVNSMDLVAQQYGEVNRDFNR
TLKRAIDPNGILSPGKSGIHP
;
_struct_ref.pdbx_align_begin           43 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9FGE A 1 ? 501 ? A0A3N9RU39 43 ? 543 ? 43 543 
2 1 9FGE B 1 ? 501 ? A0A3N9RU39 43 ? 543 ? 43 543 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9FGE ASP A 139 ? UNP A0A3N9RU39 THR 181 conflict 181 1 
2 9FGE ASP B 139 ? UNP A0A3N9RU39 THR 181 conflict 181 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 10950 ? 
1 MORE         -53   ? 
1 'SSA (A^2)'  32120 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_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 ASP A 2   ? GLY A 15  ? ASP A 44  GLY A 57  1 ? 14 
HELX_P HELX_P2  AA2 VAL A 26  ? SER A 30  ? VAL A 68  SER A 72  5 ? 5  
HELX_P HELX_P3  AA3 SER A 51  ? LYS A 66  ? SER A 93  LYS A 108 1 ? 16 
HELX_P HELX_P4  AA4 THR A 118 ? HIS A 129 ? THR A 160 HIS A 171 1 ? 12 
HELX_P HELX_P5  AA5 SER A 145 ? ASP A 152 ? SER A 187 ASP A 194 1 ? 8  
HELX_P HELX_P6  AA6 GLU A 162 ? MET A 165 ? GLU A 204 MET A 207 5 ? 4  
HELX_P HELX_P7  AA7 LEU A 204 ? THR A 209 ? LEU A 246 THR A 251 5 ? 6  
HELX_P HELX_P8  AA8 ASN A 239 ? GLU A 241 ? ASN A 281 GLU A 283 5 ? 3  
HELX_P HELX_P9  AA9 ASP A 242 ? SER A 256 ? ASP A 284 SER A 298 1 ? 15 
HELX_P HELX_P10 AB1 ALA A 268 ? LYS A 276 ? ALA A 310 LYS A 318 1 ? 9  
HELX_P HELX_P11 AB2 ARG A 277 ? ILE A 281 ? ARG A 319 ILE A 323 5 ? 5  
HELX_P HELX_P12 AB3 ASP A 289 ? ASN A 300 ? ASP A 331 ASN A 342 1 ? 12 
HELX_P HELX_P13 AB4 THR A 314 ? SER A 332 ? THR A 356 SER A 374 1 ? 19 
HELX_P HELX_P14 AB5 THR A 338 ? MET A 342 ? THR A 380 MET A 384 5 ? 5  
HELX_P HELX_P15 AB6 ASN A 345 ? MET A 355 ? ASN A 387 MET A 397 1 ? 11 
HELX_P HELX_P16 AB7 VAL A 364 ? TRP A 369 ? VAL A 406 TRP A 411 5 ? 6  
HELX_P HELX_P17 AB8 ARG A 386 ? HIS A 404 ? ARG A 428 HIS A 446 1 ? 19 
HELX_P HELX_P18 AB9 ASP A 431 ? GLN A 452 ? ASP A 473 GLN A 494 1 ? 22 
HELX_P HELX_P19 AC1 GLY A 460 ? ASN A 462 ? GLY A 502 ASN A 504 5 ? 3  
HELX_P HELX_P20 AC2 SER A 463 ? GLN A 469 ? SER A 505 GLN A 511 1 ? 7  
HELX_P HELX_P21 AC3 GLY A 472 ? ASP A 487 ? GLY A 514 ASP A 529 1 ? 16 
HELX_P HELX_P22 AC4 GLY A 495 ? ILE A 499 ? GLY A 537 ILE A 541 5 ? 5  
HELX_P HELX_P23 AC5 ASP B 2   ? GLY B 15  ? ASP B 44  GLY B 57  1 ? 14 
HELX_P HELX_P24 AC6 VAL B 26  ? SER B 30  ? VAL B 68  SER B 72  5 ? 5  
HELX_P HELX_P25 AC7 SER B 51  ? LYS B 66  ? SER B 93  LYS B 108 1 ? 16 
HELX_P HELX_P26 AC8 THR B 118 ? HIS B 129 ? THR B 160 HIS B 171 1 ? 12 
HELX_P HELX_P27 AC9 SER B 145 ? ASP B 152 ? SER B 187 ASP B 194 1 ? 8  
HELX_P HELX_P28 AD1 GLU B 162 ? MET B 165 ? GLU B 204 MET B 207 5 ? 4  
HELX_P HELX_P29 AD2 LEU B 204 ? THR B 209 ? LEU B 246 THR B 251 5 ? 6  
HELX_P HELX_P30 AD3 ASN B 239 ? GLU B 241 ? ASN B 281 GLU B 283 5 ? 3  
HELX_P HELX_P31 AD4 ASP B 242 ? SER B 256 ? ASP B 284 SER B 298 1 ? 15 
HELX_P HELX_P32 AD5 ALA B 268 ? LYS B 276 ? ALA B 310 LYS B 318 1 ? 9  
HELX_P HELX_P33 AD6 ARG B 277 ? ILE B 281 ? ARG B 319 ILE B 323 5 ? 5  
HELX_P HELX_P34 AD7 ASP B 289 ? ASN B 300 ? ASP B 331 ASN B 342 1 ? 12 
HELX_P HELX_P35 AD8 THR B 314 ? SER B 332 ? THR B 356 SER B 374 1 ? 19 
HELX_P HELX_P36 AD9 THR B 338 ? MET B 342 ? THR B 380 MET B 384 5 ? 5  
HELX_P HELX_P37 AE1 ASN B 345 ? MET B 355 ? ASN B 387 MET B 397 1 ? 11 
HELX_P HELX_P38 AE2 VAL B 364 ? TRP B 369 ? VAL B 406 TRP B 411 5 ? 6  
HELX_P HELX_P39 AE3 ARG B 386 ? HIS B 404 ? ARG B 428 HIS B 446 1 ? 19 
HELX_P HELX_P40 AE4 ASP B 431 ? GLN B 452 ? ASP B 473 GLN B 494 1 ? 22 
HELX_P HELX_P41 AE5 GLY B 460 ? ASN B 462 ? GLY B 502 ASN B 504 5 ? 3  
HELX_P HELX_P42 AE6 SER B 463 ? GLN B 469 ? SER B 505 GLN B 511 1 ? 7  
HELX_P HELX_P43 AE7 GLY B 472 ? ASP B 487 ? GLY B 514 ASP B 529 1 ? 16 
HELX_P HELX_P44 AE8 GLY B 495 ? ILE B 499 ? GLY B 537 ILE B 541 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 7 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 7 ? 
AB1 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AA9 6 7 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB1 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 19  ? PHE A 20  ? VAL A 61  PHE A 62  
AA1 2 GLY A 45  ? VAL A 47  ? GLY A 87  VAL A 89  
AA1 3 VAL A 91  ? ASP A 94  ? VAL A 133 ASP A 136 
AA1 4 LEU A 69  ? VAL A 72  ? LEU A 111 VAL A 114 
AA2 1 ILE A 101 ? ASP A 105 ? ILE A 143 ASP A 147 
AA2 2 THR A 110 ? LEU A 113 ? THR A 152 LEU A 155 
AA2 3 ILE A 215 ? TRP A 222 ? ILE A 257 TRP A 264 
AA2 4 GLN A 167 ? CYS A 173 ? GLN A 209 CYS A 215 
AA2 5 LEU A 179 ? ARG A 181 ? LEU A 221 ARG A 223 
AA3 1 LEU A 133 ? TRP A 134 ? LEU A 175 TRP A 176 
AA3 2 MET A 224 ? PRO A 225 ? MET A 266 PRO A 267 
AA4 1 GLU A 335 ? LEU A 337 ? GLU A 377 LEU A 379 
AA4 2 VAL A 229 ? HIS A 237 ? VAL A 271 HIS A 279 
AA4 3 TRP A 305 ? GLY A 313 ? TRP A 347 GLY A 355 
AA4 4 ASN A 263 ? SER A 267 ? ASN A 305 SER A 309 
AA4 5 THR A 409 ? ILE A 414 ? THR A 451 ILE A 456 
AA4 6 ASP A 418 ? ASP A 428 ? ASP A 460 ASP A 470 
AA4 7 GLY A 374 ? PHE A 379 ? GLY A 416 PHE A 421 
AA5 1 GLU A 335 ? LEU A 337 ? GLU A 377 LEU A 379 
AA5 2 VAL A 229 ? HIS A 237 ? VAL A 271 HIS A 279 
AA5 3 TRP A 305 ? GLY A 313 ? TRP A 347 GLY A 355 
AA5 4 ASN A 263 ? SER A 267 ? ASN A 305 SER A 309 
AA5 5 THR A 409 ? ILE A 414 ? THR A 451 ILE A 456 
AA5 6 ASP A 418 ? ASP A 428 ? ASP A 460 ASP A 470 
AA5 7 VAL A 382 ? ALA A 384 ? VAL A 424 ALA A 426 
AA6 1 VAL B 19  ? PHE B 20  ? VAL B 61  PHE B 62  
AA6 2 GLY B 45  ? VAL B 47  ? GLY B 87  VAL B 89  
AA6 3 VAL B 91  ? ASP B 94  ? VAL B 133 ASP B 136 
AA6 4 LEU B 69  ? VAL B 72  ? LEU B 111 VAL B 114 
AA7 1 ILE B 101 ? ASP B 105 ? ILE B 143 ASP B 147 
AA7 2 THR B 110 ? LEU B 113 ? THR B 152 LEU B 155 
AA7 3 ILE B 215 ? TRP B 222 ? ILE B 257 TRP B 264 
AA7 4 GLN B 167 ? CYS B 173 ? GLN B 209 CYS B 215 
AA7 5 LEU B 179 ? ARG B 181 ? LEU B 221 ARG B 223 
AA8 1 LEU B 133 ? TRP B 134 ? LEU B 175 TRP B 176 
AA8 2 MET B 224 ? PRO B 225 ? MET B 266 PRO B 267 
AA9 1 GLY B 334 ? LEU B 337 ? GLY B 376 LEU B 379 
AA9 2 VAL B 229 ? HIS B 237 ? VAL B 271 HIS B 279 
AA9 3 TRP B 305 ? GLY B 313 ? TRP B 347 GLY B 355 
AA9 4 ASN B 263 ? SER B 267 ? ASN B 305 SER B 309 
AA9 5 THR B 409 ? ILE B 414 ? THR B 451 ILE B 456 
AA9 6 ASP B 418 ? ASP B 428 ? ASP B 460 ASP B 470 
AA9 7 GLY B 374 ? PHE B 379 ? GLY B 416 PHE B 421 
AB1 1 GLY B 334 ? LEU B 337 ? GLY B 376 LEU B 379 
AB1 2 VAL B 229 ? HIS B 237 ? VAL B 271 HIS B 279 
AB1 3 TRP B 305 ? GLY B 313 ? TRP B 347 GLY B 355 
AB1 4 ASN B 263 ? SER B 267 ? ASN B 305 SER B 309 
AB1 5 THR B 409 ? ILE B 414 ? THR B 451 ILE B 456 
AB1 6 ASP B 418 ? ASP B 428 ? ASP B 460 ASP B 470 
AB1 7 VAL B 382 ? ALA B 384 ? VAL B 424 ALA B 426 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 20  ? N PHE A 62  O ALA A 46  ? O ALA A 88  
AA1 2 3 N GLY A 45  ? N GLY A 87  O VAL A 92  ? O VAL A 134 
AA1 3 4 O LEU A 93  ? O LEU A 135 N VAL A 72  ? N VAL A 114 
AA2 1 2 N ASP A 105 ? N ASP A 147 O THR A 110 ? O THR A 152 
AA2 2 3 N LEU A 113 ? N LEU A 155 O MET A 219 ? O MET A 261 
AA2 3 4 O ILE A 215 ? O ILE A 257 N CYS A 173 ? N CYS A 215 
AA2 4 5 N VAL A 172 ? N VAL A 214 O MET A 180 ? O MET A 222 
AA3 1 2 N TRP A 134 ? N TRP A 176 O MET A 224 ? O MET A 266 
AA4 1 2 O LEU A 337 ? O LEU A 379 N MET A 234 ? N MET A 276 
AA4 2 3 N PHE A 233 ? N PHE A 275 O PHE A 309 ? O PHE A 351 
AA4 3 4 O ASN A 306 ? O ASN A 348 N MET A 266 ? N MET A 308 
AA4 4 5 N ASN A 263 ? N ASN A 305 O ILE A 414 ? O ILE A 456 
AA4 5 6 N ALA A 413 ? N ALA A 455 O HIS A 420 ? O HIS A 462 
AA4 6 7 O LEU A 425 ? O LEU A 467 N ALA A 377 ? N ALA A 419 
AA5 1 2 O LEU A 337 ? O LEU A 379 N MET A 234 ? N MET A 276 
AA5 2 3 N PHE A 233 ? N PHE A 275 O PHE A 309 ? O PHE A 351 
AA5 3 4 O ASN A 306 ? O ASN A 348 N MET A 266 ? N MET A 308 
AA5 4 5 N ASN A 263 ? N ASN A 305 O ILE A 414 ? O ILE A 456 
AA5 5 6 N ALA A 413 ? N ALA A 455 O HIS A 420 ? O HIS A 462 
AA5 6 7 O LEU A 419 ? O LEU A 461 N ALA A 383 ? N ALA A 425 
AA6 1 2 N PHE B 20  ? N PHE B 62  O ALA B 46  ? O ALA B 88  
AA6 2 3 N GLY B 45  ? N GLY B 87  O VAL B 92  ? O VAL B 134 
AA6 3 4 O VAL B 91  ? O VAL B 133 N TRP B 70  ? N TRP B 112 
AA7 1 2 N ASP B 105 ? N ASP B 147 O THR B 110 ? O THR B 152 
AA7 2 3 N LEU B 113 ? N LEU B 155 O MET B 219 ? O MET B 261 
AA7 3 4 O ILE B 215 ? O ILE B 257 N CYS B 173 ? N CYS B 215 
AA7 4 5 N VAL B 172 ? N VAL B 214 O MET B 180 ? O MET B 222 
AA8 1 2 N TRP B 134 ? N TRP B 176 O MET B 224 ? O MET B 266 
AA9 1 2 O LEU B 337 ? O LEU B 379 N MET B 234 ? N MET B 276 
AA9 2 3 N VAL B 229 ? N VAL B 271 O GLY B 313 ? O GLY B 355 
AA9 3 4 O ASN B 306 ? O ASN B 348 N MET B 266 ? N MET B 308 
AA9 4 5 N MET B 265 ? N MET B 307 O TYR B 412 ? O TYR B 454 
AA9 5 6 N ALA B 413 ? N ALA B 455 O HIS B 420 ? O HIS B 462 
AA9 6 7 O ILE B 423 ? O ILE B 465 N PHE B 379 ? N PHE B 421 
AB1 1 2 O LEU B 337 ? O LEU B 379 N MET B 234 ? N MET B 276 
AB1 2 3 N VAL B 229 ? N VAL B 271 O GLY B 313 ? O GLY B 355 
AB1 3 4 O ASN B 306 ? O ASN B 348 N MET B 266 ? N MET B 308 
AB1 4 5 N MET B 265 ? N MET B 307 O TYR B 412 ? O TYR B 454 
AB1 5 6 N ALA B 413 ? N ALA B 455 O HIS B 420 ? O HIS B 462 
AB1 6 7 O LEU B 419 ? O LEU B 461 N ALA B 383 ? N ALA B 425 
# 
_pdbx_entry_details.entry_id                   9FGE 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE B ARG 278 ? ? CZ B ARG 278 ? ? NH1 B ARG 278 ? ? 123.35 120.30 3.05  0.50 N 
2 1 NE B ARG 320 ? ? CZ B ARG 320 ? ? NH2 B ARG 320 ? ? 117.21 120.30 -3.09 0.50 N 
# 
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 SER A 115 ? ? -94.74  -74.22  
2  1 LYS A 118 ? ? -107.03 43.36   
3  1 MET A 124 ? ? 52.95   -120.85 
4  1 TYR A 202 ? ? -99.06  33.88   
5  1 ASP A 404 ? ? -26.31  139.52  
6  1 GLU A 405 ? ? 149.94  81.81   
7  1 SER A 535 ? ? 37.92   57.06   
8  1 SER B 115 ? ? -95.49  -77.35  
9  1 LYS B 118 ? ? -107.52 41.83   
10 1 MET B 124 ? ? 56.36   -121.60 
11 1 TYR B 202 ? ? -94.58  32.76   
12 1 SER B 535 ? ? 30.33   61.66   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 278 ? ? 0.072 'SIDE CHAIN' 
2 1 ARG A 526 ? ? 0.093 'SIDE CHAIN' 
3 1 ARG B 278 ? ? 0.078 'SIDE CHAIN' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 1081 ? J HOH . 
2 1 B HOH 1091 ? K HOH . 
# 
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  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
GLN N      N N N 174 
GLN CA     C N S 175 
GLN C      C N N 176 
GLN O      O N N 177 
GLN CB     C N N 178 
GLN CG     C N N 179 
GLN CD     C N N 180 
GLN OE1    O N N 181 
GLN NE2    N N N 182 
GLN OXT    O N N 183 
GLN H      H N N 184 
GLN H2     H N N 185 
GLN HA     H N N 186 
GLN HB2    H N N 187 
GLN HB3    H N N 188 
GLN HG2    H N N 189 
GLN HG3    H N N 190 
GLN HE21   H N N 191 
GLN HE22   H N N 192 
GLN HXT    H N N 193 
GLU N      N N N 194 
GLU CA     C N S 195 
GLU C      C N N 196 
GLU O      O N N 197 
GLU CB     C N N 198 
GLU CG     C N N 199 
GLU CD     C N N 200 
GLU OE1    O N N 201 
GLU OE2    O N N 202 
GLU OXT    O N N 203 
GLU H      H N N 204 
GLU H2     H N N 205 
GLU HA     H N N 206 
GLU HB2    H N N 207 
GLU HB3    H N N 208 
GLU HG2    H N N 209 
GLU HG3    H N N 210 
GLU HE2    H N N 211 
GLU HXT    H N N 212 
GLY N      N N N 213 
GLY CA     C N N 214 
GLY C      C N N 215 
GLY O      O N N 216 
GLY OXT    O N N 217 
GLY H      H N N 218 
GLY H2     H N N 219 
GLY HA2    H N N 220 
GLY HA3    H N N 221 
GLY HXT    H N N 222 
GOL C1     C N N 223 
GOL O1     O N N 224 
GOL C2     C N N 225 
GOL O2     O N N 226 
GOL C3     C N N 227 
GOL O3     O N N 228 
GOL H11    H N N 229 
GOL H12    H N N 230 
GOL HO1    H N N 231 
GOL H2     H N N 232 
GOL HO2    H N N 233 
GOL H31    H N N 234 
GOL H32    H N N 235 
GOL HO3    H N N 236 
HIS N      N N N 237 
HIS CA     C N S 238 
HIS C      C N N 239 
HIS O      O N N 240 
HIS CB     C N N 241 
HIS CG     C Y N 242 
HIS ND1    N Y N 243 
HIS CD2    C Y N 244 
HIS CE1    C Y N 245 
HIS NE2    N Y N 246 
HIS OXT    O N N 247 
HIS H      H N N 248 
HIS H2     H N N 249 
HIS HA     H N N 250 
HIS HB2    H N N 251 
HIS HB3    H N N 252 
HIS HD1    H N N 253 
HIS HD2    H N N 254 
HIS HE1    H N N 255 
HIS HE2    H N N 256 
HIS HXT    H N N 257 
HOH O      O N N 258 
HOH H1     H N N 259 
HOH H2     H N N 260 
ILE N      N N N 261 
ILE CA     C N S 262 
ILE C      C N N 263 
ILE O      O N N 264 
ILE CB     C N S 265 
ILE CG1    C N N 266 
ILE CG2    C N N 267 
ILE CD1    C N N 268 
ILE OXT    O N N 269 
ILE H      H N N 270 
ILE H2     H N N 271 
ILE HA     H N N 272 
ILE HB     H N N 273 
ILE HG12   H N N 274 
ILE HG13   H N N 275 
ILE HG21   H N N 276 
ILE HG22   H N N 277 
ILE HG23   H N N 278 
ILE HD11   H N N 279 
ILE HD12   H N N 280 
ILE HD13   H N N 281 
ILE HXT    H N N 282 
LEU N      N N N 283 
LEU CA     C N S 284 
LEU C      C N N 285 
LEU O      O N N 286 
LEU CB     C N N 287 
LEU CG     C N N 288 
LEU CD1    C N N 289 
LEU CD2    C N N 290 
LEU OXT    O N N 291 
LEU H      H N N 292 
LEU H2     H N N 293 
LEU HA     H N N 294 
LEU HB2    H N N 295 
LEU HB3    H N N 296 
LEU HG     H N N 297 
LEU HD11   H N N 298 
LEU HD12   H N N 299 
LEU HD13   H N N 300 
LEU HD21   H N N 301 
LEU HD22   H N N 302 
LEU HD23   H N N 303 
LEU HXT    H N N 304 
LYS N      N N N 305 
LYS CA     C N S 306 
LYS C      C N N 307 
LYS O      O N N 308 
LYS CB     C N N 309 
LYS CG     C N N 310 
LYS CD     C N N 311 
LYS CE     C N N 312 
LYS NZ     N N N 313 
LYS OXT    O N N 314 
LYS H      H N N 315 
LYS H2     H N N 316 
LYS HA     H N N 317 
LYS HB2    H N N 318 
LYS HB3    H N N 319 
LYS HG2    H N N 320 
LYS HG3    H N N 321 
LYS HD2    H N N 322 
LYS HD3    H N N 323 
LYS HE2    H N N 324 
LYS HE3    H N N 325 
LYS HZ1    H N N 326 
LYS HZ2    H N N 327 
LYS HZ3    H N N 328 
LYS HXT    H N N 329 
MET N      N N N 330 
MET CA     C N S 331 
MET C      C N N 332 
MET O      O N N 333 
MET CB     C N N 334 
MET CG     C N N 335 
MET SD     S N N 336 
MET CE     C N N 337 
MET OXT    O N N 338 
MET H      H N N 339 
MET H2     H N N 340 
MET HA     H N N 341 
MET HB2    H N N 342 
MET HB3    H N N 343 
MET HG2    H N N 344 
MET HG3    H N N 345 
MET HE1    H N N 346 
MET HE2    H N N 347 
MET HE3    H N N 348 
MET HXT    H N N 349 
PEG C1     C N N 350 
PEG O1     O N N 351 
PEG C2     C N N 352 
PEG O2     O N N 353 
PEG C3     C N N 354 
PEG C4     C N N 355 
PEG O4     O N N 356 
PEG H11    H N N 357 
PEG H12    H N N 358 
PEG HO1    H N N 359 
PEG H21    H N N 360 
PEG H22    H N N 361 
PEG H31    H N N 362 
PEG H32    H N N 363 
PEG H41    H N N 364 
PEG H42    H N N 365 
PEG HO4    H N N 366 
PHE N      N N N 367 
PHE CA     C N S 368 
PHE C      C N N 369 
PHE O      O N N 370 
PHE CB     C N N 371 
PHE CG     C Y N 372 
PHE CD1    C Y N 373 
PHE CD2    C Y N 374 
PHE CE1    C Y N 375 
PHE CE2    C Y N 376 
PHE CZ     C Y N 377 
PHE OXT    O N N 378 
PHE H      H N N 379 
PHE H2     H N N 380 
PHE HA     H N N 381 
PHE HB2    H N N 382 
PHE HB3    H N N 383 
PHE HD1    H N N 384 
PHE HD2    H N N 385 
PHE HE1    H N N 386 
PHE HE2    H N N 387 
PHE HZ     H N N 388 
PHE HXT    H N N 389 
PRO N      N N N 390 
PRO CA     C N S 391 
PRO C      C N N 392 
PRO O      O N N 393 
PRO CB     C N N 394 
PRO CG     C N N 395 
PRO CD     C N N 396 
PRO OXT    O N N 397 
PRO H      H N N 398 
PRO HA     H N N 399 
PRO HB2    H N N 400 
PRO HB3    H N N 401 
PRO HG2    H N N 402 
PRO HG3    H N N 403 
PRO HD2    H N N 404 
PRO HD3    H N N 405 
PRO HXT    H N N 406 
SER N      N N N 407 
SER CA     C N S 408 
SER C      C N N 409 
SER O      O N N 410 
SER CB     C N N 411 
SER OG     O N N 412 
SER OXT    O N N 413 
SER H      H N N 414 
SER H2     H N N 415 
SER HA     H N N 416 
SER HB2    H N N 417 
SER HB3    H N N 418 
SER HG     H N N 419 
SER HXT    H N N 420 
THR N      N N N 421 
THR CA     C N S 422 
THR C      C N N 423 
THR O      O N N 424 
THR CB     C N R 425 
THR OG1    O N N 426 
THR CG2    C N N 427 
THR OXT    O N N 428 
THR H      H N N 429 
THR H2     H N N 430 
THR HA     H N N 431 
THR HB     H N N 432 
THR HG1    H N N 433 
THR HG21   H N N 434 
THR HG22   H N N 435 
THR HG23   H N N 436 
THR HXT    H N N 437 
TRP N      N N N 438 
TRP CA     C N S 439 
TRP C      C N N 440 
TRP O      O N N 441 
TRP CB     C N N 442 
TRP CG     C Y N 443 
TRP CD1    C Y N 444 
TRP CD2    C Y N 445 
TRP NE1    N Y N 446 
TRP CE2    C Y N 447 
TRP CE3    C Y N 448 
TRP CZ2    C Y N 449 
TRP CZ3    C Y N 450 
TRP CH2    C Y N 451 
TRP OXT    O N N 452 
TRP H      H N N 453 
TRP H2     H N N 454 
TRP HA     H N N 455 
TRP HB2    H N N 456 
TRP HB3    H N N 457 
TRP HD1    H N N 458 
TRP HE1    H N N 459 
TRP HE3    H N N 460 
TRP HZ2    H N N 461 
TRP HZ3    H N N 462 
TRP HH2    H N N 463 
TRP HXT    H N N 464 
TYR N      N N N 465 
TYR CA     C N S 466 
TYR C      C N N 467 
TYR O      O N N 468 
TYR CB     C N N 469 
TYR CG     C Y N 470 
TYR CD1    C Y N 471 
TYR CD2    C Y N 472 
TYR CE1    C Y N 473 
TYR CE2    C Y N 474 
TYR CZ     C Y N 475 
TYR OH     O N N 476 
TYR OXT    O N N 477 
TYR H      H N N 478 
TYR H2     H N N 479 
TYR HA     H N N 480 
TYR HB2    H N N 481 
TYR HB3    H N N 482 
TYR HD1    H N N 483 
TYR HD2    H N N 484 
TYR HE1    H N N 485 
TYR HE2    H N N 486 
TYR HH     H N N 487 
TYR HXT    H N N 488 
V55 CAI    C Y N 489 
V55 CAG    C Y N 490 
V55 CAK    C Y N 491 
V55 CAJ    C Y N 492 
V55 CAF    C Y N 493 
V55 OAB    O N N 494 
V55 CAE    C Y N 495 
V55 CAD    C N N 496 
V55 CAA    C N N 497 
V55 OAH    O N N 498 
V55 OAC    O N N 499 
V55 HAG    H N N 500 
V55 HAD    H N N 501 
V55 HAE    H N N 502 
V55 HAF    H N N 503 
V55 HAC    H N N 504 
V55 HAA1   H N N 505 
V55 HAA2   H N N 506 
V55 HAA3   H N N 507 
VAL N      N N N 508 
VAL CA     C N S 509 
VAL C      C N N 510 
VAL O      O N N 511 
VAL CB     C N N 512 
VAL CG1    C N N 513 
VAL CG2    C N N 514 
VAL OXT    O N N 515 
VAL H      H N N 516 
VAL H2     H N N 517 
VAL HA     H N N 518 
VAL HB     H N N 519 
VAL HG11   H N N 520 
VAL HG12   H N N 521 
VAL HG13   H N N 522 
VAL HG21   H N N 523 
VAL HG22   H N N 524 
VAL HG23   H N N 525 
VAL HXT    H N N 526 
# 
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  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
GOL C1    O1     sing N N 220 
GOL C1    C2     sing N N 221 
GOL C1    H11    sing N N 222 
GOL C1    H12    sing N N 223 
GOL O1    HO1    sing N N 224 
GOL C2    O2     sing N N 225 
GOL C2    C3     sing N N 226 
GOL C2    H2     sing N N 227 
GOL O2    HO2    sing N N 228 
GOL C3    O3     sing N N 229 
GOL C3    H31    sing N N 230 
GOL C3    H32    sing N N 231 
GOL O3    HO3    sing N N 232 
HIS N     CA     sing N N 233 
HIS N     H      sing N N 234 
HIS N     H2     sing N N 235 
HIS CA    C      sing N N 236 
HIS CA    CB     sing N N 237 
HIS CA    HA     sing N N 238 
HIS C     O      doub N N 239 
HIS C     OXT    sing N N 240 
HIS CB    CG     sing N N 241 
HIS CB    HB2    sing N N 242 
HIS CB    HB3    sing N N 243 
HIS CG    ND1    sing Y N 244 
HIS CG    CD2    doub Y N 245 
HIS ND1   CE1    doub Y N 246 
HIS ND1   HD1    sing N N 247 
HIS CD2   NE2    sing Y N 248 
HIS CD2   HD2    sing N N 249 
HIS CE1   NE2    sing Y N 250 
HIS CE1   HE1    sing N N 251 
HIS NE2   HE2    sing N N 252 
HIS OXT   HXT    sing N N 253 
HOH O     H1     sing N N 254 
HOH O     H2     sing N N 255 
ILE N     CA     sing N N 256 
ILE N     H      sing N N 257 
ILE N     H2     sing N N 258 
ILE CA    C      sing N N 259 
ILE CA    CB     sing N N 260 
ILE CA    HA     sing N N 261 
ILE C     O      doub N N 262 
ILE C     OXT    sing N N 263 
ILE CB    CG1    sing N N 264 
ILE CB    CG2    sing N N 265 
ILE CB    HB     sing N N 266 
ILE CG1   CD1    sing N N 267 
ILE CG1   HG12   sing N N 268 
ILE CG1   HG13   sing N N 269 
ILE CG2   HG21   sing N N 270 
ILE CG2   HG22   sing N N 271 
ILE CG2   HG23   sing N N 272 
ILE CD1   HD11   sing N N 273 
ILE CD1   HD12   sing N N 274 
ILE CD1   HD13   sing N N 275 
ILE OXT   HXT    sing N N 276 
LEU N     CA     sing N N 277 
LEU N     H      sing N N 278 
LEU N     H2     sing N N 279 
LEU CA    C      sing N N 280 
LEU CA    CB     sing N N 281 
LEU CA    HA     sing N N 282 
LEU C     O      doub N N 283 
LEU C     OXT    sing N N 284 
LEU CB    CG     sing N N 285 
LEU CB    HB2    sing N N 286 
LEU CB    HB3    sing N N 287 
LEU CG    CD1    sing N N 288 
LEU CG    CD2    sing N N 289 
LEU CG    HG     sing N N 290 
LEU CD1   HD11   sing N N 291 
LEU CD1   HD12   sing N N 292 
LEU CD1   HD13   sing N N 293 
LEU CD2   HD21   sing N N 294 
LEU CD2   HD22   sing N N 295 
LEU CD2   HD23   sing N N 296 
LEU OXT   HXT    sing N N 297 
LYS N     CA     sing N N 298 
LYS N     H      sing N N 299 
LYS N     H2     sing N N 300 
LYS CA    C      sing N N 301 
LYS CA    CB     sing N N 302 
LYS CA    HA     sing N N 303 
LYS C     O      doub N N 304 
LYS C     OXT    sing N N 305 
LYS CB    CG     sing N N 306 
LYS CB    HB2    sing N N 307 
LYS CB    HB3    sing N N 308 
LYS CG    CD     sing N N 309 
LYS CG    HG2    sing N N 310 
LYS CG    HG3    sing N N 311 
LYS CD    CE     sing N N 312 
LYS CD    HD2    sing N N 313 
LYS CD    HD3    sing N N 314 
LYS CE    NZ     sing N N 315 
LYS CE    HE2    sing N N 316 
LYS CE    HE3    sing N N 317 
LYS NZ    HZ1    sing N N 318 
LYS NZ    HZ2    sing N N 319 
LYS NZ    HZ3    sing N N 320 
LYS OXT   HXT    sing N N 321 
MET N     CA     sing N N 322 
MET N     H      sing N N 323 
MET N     H2     sing N N 324 
MET CA    C      sing N N 325 
MET CA    CB     sing N N 326 
MET CA    HA     sing N N 327 
MET C     O      doub N N 328 
MET C     OXT    sing N N 329 
MET CB    CG     sing N N 330 
MET CB    HB2    sing N N 331 
MET CB    HB3    sing N N 332 
MET CG    SD     sing N N 333 
MET CG    HG2    sing N N 334 
MET CG    HG3    sing N N 335 
MET SD    CE     sing N N 336 
MET CE    HE1    sing N N 337 
MET CE    HE2    sing N N 338 
MET CE    HE3    sing N N 339 
MET OXT   HXT    sing N N 340 
PEG C1    O1     sing N N 341 
PEG C1    C2     sing N N 342 
PEG C1    H11    sing N N 343 
PEG C1    H12    sing N N 344 
PEG O1    HO1    sing N N 345 
PEG C2    O2     sing N N 346 
PEG C2    H21    sing N N 347 
PEG C2    H22    sing N N 348 
PEG O2    C3     sing N N 349 
PEG C3    C4     sing N N 350 
PEG C3    H31    sing N N 351 
PEG C3    H32    sing N N 352 
PEG C4    O4     sing N N 353 
PEG C4    H41    sing N N 354 
PEG C4    H42    sing N N 355 
PEG O4    HO4    sing N N 356 
PHE N     CA     sing N N 357 
PHE N     H      sing N N 358 
PHE N     H2     sing N N 359 
PHE CA    C      sing N N 360 
PHE CA    CB     sing N N 361 
PHE CA    HA     sing N N 362 
PHE C     O      doub N N 363 
PHE C     OXT    sing N N 364 
PHE CB    CG     sing N N 365 
PHE CB    HB2    sing N N 366 
PHE CB    HB3    sing N N 367 
PHE CG    CD1    doub Y N 368 
PHE CG    CD2    sing Y N 369 
PHE CD1   CE1    sing Y N 370 
PHE CD1   HD1    sing N N 371 
PHE CD2   CE2    doub Y N 372 
PHE CD2   HD2    sing N N 373 
PHE CE1   CZ     doub Y N 374 
PHE CE1   HE1    sing N N 375 
PHE CE2   CZ     sing Y N 376 
PHE CE2   HE2    sing N N 377 
PHE CZ    HZ     sing N N 378 
PHE OXT   HXT    sing N N 379 
PRO N     CA     sing N N 380 
PRO N     CD     sing N N 381 
PRO N     H      sing N N 382 
PRO CA    C      sing N N 383 
PRO CA    CB     sing N N 384 
PRO CA    HA     sing N N 385 
PRO C     O      doub N N 386 
PRO C     OXT    sing N N 387 
PRO CB    CG     sing N N 388 
PRO CB    HB2    sing N N 389 
PRO CB    HB3    sing N N 390 
PRO CG    CD     sing N N 391 
PRO CG    HG2    sing N N 392 
PRO CG    HG3    sing N N 393 
PRO CD    HD2    sing N N 394 
PRO CD    HD3    sing N N 395 
PRO OXT   HXT    sing N N 396 
SER N     CA     sing N N 397 
SER N     H      sing N N 398 
SER N     H2     sing N N 399 
SER CA    C      sing N N 400 
SER CA    CB     sing N N 401 
SER CA    HA     sing N N 402 
SER C     O      doub N N 403 
SER C     OXT    sing N N 404 
SER CB    OG     sing N N 405 
SER CB    HB2    sing N N 406 
SER CB    HB3    sing N N 407 
SER OG    HG     sing N N 408 
SER OXT   HXT    sing N N 409 
THR N     CA     sing N N 410 
THR N     H      sing N N 411 
THR N     H2     sing N N 412 
THR CA    C      sing N N 413 
THR CA    CB     sing N N 414 
THR CA    HA     sing N N 415 
THR C     O      doub N N 416 
THR C     OXT    sing N N 417 
THR CB    OG1    sing N N 418 
THR CB    CG2    sing N N 419 
THR CB    HB     sing N N 420 
THR OG1   HG1    sing N N 421 
THR CG2   HG21   sing N N 422 
THR CG2   HG22   sing N N 423 
THR CG2   HG23   sing N N 424 
THR OXT   HXT    sing N N 425 
TRP N     CA     sing N N 426 
TRP N     H      sing N N 427 
TRP N     H2     sing N N 428 
TRP CA    C      sing N N 429 
TRP CA    CB     sing N N 430 
TRP CA    HA     sing N N 431 
TRP C     O      doub N N 432 
TRP C     OXT    sing N N 433 
TRP CB    CG     sing N N 434 
TRP CB    HB2    sing N N 435 
TRP CB    HB3    sing N N 436 
TRP CG    CD1    doub Y N 437 
TRP CG    CD2    sing Y N 438 
TRP CD1   NE1    sing Y N 439 
TRP CD1   HD1    sing N N 440 
TRP CD2   CE2    doub Y N 441 
TRP CD2   CE3    sing Y N 442 
TRP NE1   CE2    sing Y N 443 
TRP NE1   HE1    sing N N 444 
TRP CE2   CZ2    sing Y N 445 
TRP CE3   CZ3    doub Y N 446 
TRP CE3   HE3    sing N N 447 
TRP CZ2   CH2    doub Y N 448 
TRP CZ2   HZ2    sing N N 449 
TRP CZ3   CH2    sing Y N 450 
TRP CZ3   HZ3    sing N N 451 
TRP CH2   HH2    sing N N 452 
TRP OXT   HXT    sing N N 453 
TYR N     CA     sing N N 454 
TYR N     H      sing N N 455 
TYR N     H2     sing N N 456 
TYR CA    C      sing N N 457 
TYR CA    CB     sing N N 458 
TYR CA    HA     sing N N 459 
TYR C     O      doub N N 460 
TYR C     OXT    sing N N 461 
TYR CB    CG     sing N N 462 
TYR CB    HB2    sing N N 463 
TYR CB    HB3    sing N N 464 
TYR CG    CD1    doub Y N 465 
TYR CG    CD2    sing Y N 466 
TYR CD1   CE1    sing Y N 467 
TYR CD1   HD1    sing N N 468 
TYR CD2   CE2    doub Y N 469 
TYR CD2   HD2    sing N N 470 
TYR CE1   CZ     doub Y N 471 
TYR CE1   HE1    sing N N 472 
TYR CE2   CZ     sing Y N 473 
TYR CE2   HE2    sing N N 474 
TYR CZ    OH     sing N N 475 
TYR OH    HH     sing N N 476 
TYR OXT   HXT    sing N N 477 
V55 CAK   CAG    doub Y N 478 
V55 CAK   CAJ    sing Y N 479 
V55 CAK   OAH    sing N N 480 
V55 CAG   CAI    sing Y N 481 
V55 CAI   CAD    sing N N 482 
V55 CAI   CAE    doub Y N 483 
V55 CAD   OAB    doub N N 484 
V55 CAF   CAJ    doub Y N 485 
V55 CAF   CAE    sing Y N 486 
V55 CAJ   OAC    sing N N 487 
V55 CAA   OAH    sing N N 488 
V55 CAG   HAG    sing N N 489 
V55 CAD   HAD    sing N N 490 
V55 CAE   HAE    sing N N 491 
V55 CAF   HAF    sing N N 492 
V55 OAC   HAC    sing N N 493 
V55 CAA   HAA1   sing N N 494 
V55 CAA   HAA2   sing N N 495 
V55 CAA   HAA3   sing N N 496 
VAL N     CA     sing N N 497 
VAL N     H      sing N N 498 
VAL N     H2     sing N N 499 
VAL CA    C      sing N N 500 
VAL CA    CB     sing N N 501 
VAL CA    HA     sing N N 502 
VAL C     O      doub N N 503 
VAL C     OXT    sing N N 504 
VAL CB    CG1    sing N N 505 
VAL CB    CG2    sing N N 506 
VAL CB    HB     sing N N 507 
VAL CG1   HG11   sing N N 508 
VAL CG1   HG12   sing N N 509 
VAL CG1   HG13   sing N N 510 
VAL CG2   HG21   sing N N 511 
VAL CG2   HG22   sing N N 512 
VAL CG2   HG23   sing N N 513 
VAL OXT   HXT    sing N N 514 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             '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                    9FGE 
_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]   0.010950 
_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]   0.010222 
_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]   0.007716 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . ALA A 1 1   ? 10.195  18.394  65.954 1.00 28.94  ? 43   ALA A N     1 
ATOM   2    C CA    . ALA A 1 1   ? 10.754  19.505  65.139 1.00 24.97  ? 43   ALA A CA    1 
ATOM   3    C C     . ALA A 1 1   ? 10.641  20.852  65.881 1.00 25.57  ? 43   ALA A C     1 
ATOM   4    O O     . ALA A 1 1   ? 9.578   21.176  66.397 1.00 32.04  ? 43   ALA A O     1 
ATOM   5    C CB    . ALA A 1 1   ? 10.031  19.551  63.807 1.00 26.60  ? 43   ALA A CB    1 
ATOM   6    N N     . ASP A 1 2   ? 11.727  21.656  65.968 1.00 24.56  ? 44   ASP A N     1 
ATOM   7    C CA    . ASP A 1 2   ? 11.606  23.068  66.329 1.00 23.06  ? 44   ASP A CA    1 
ATOM   8    C C     . ASP A 1 2   ? 11.606  23.929  65.065 1.00 23.01  ? 44   ASP A C     1 
ATOM   9    O O     . ASP A 1 2   ? 12.638  24.395  64.564 1.00 19.40  ? 44   ASP A O     1 
ATOM   10   C CB    . ASP A 1 2   ? 12.703  23.479  67.295 1.00 24.66  ? 44   ASP A CB    1 
ATOM   11   C CG    . ASP A 1 2   ? 12.776  24.953  67.633 1.00 25.79  ? 44   ASP A CG    1 
ATOM   12   O OD1   . ASP A 1 2   ? 11.839  25.726  67.351 1.00 26.87  ? 44   ASP A OD1   1 
ATOM   13   O OD2   . ASP A 1 2   ? 13.806  25.319  68.163 1.00 28.96  ? 44   ASP A OD2   1 
ATOM   14   N N     . PHE A 1 3   ? 10.407  24.118  64.543 1.00 20.84  ? 45   PHE A N     1 
ATOM   15   C CA    . PHE A 1 3   ? 10.202  24.837  63.308 1.00 19.71  ? 45   PHE A CA    1 
ATOM   16   C C     . PHE A 1 3   ? 10.711  26.270  63.411 1.00 19.40  ? 45   PHE A C     1 
ATOM   17   O O     . PHE A 1 3   ? 11.461  26.707  62.553 1.00 18.04  ? 45   PHE A O     1 
ATOM   18   C CB    . PHE A 1 3   ? 8.730   24.765  62.916 1.00 19.00  ? 45   PHE A CB    1 
ATOM   19   C CG    . PHE A 1 3   ? 8.350   25.580  61.723 1.00 19.62  ? 45   PHE A CG    1 
ATOM   20   C CD1   . PHE A 1 3   ? 8.673   25.176  60.434 1.00 18.39  ? 45   PHE A CD1   1 
ATOM   21   C CD2   . PHE A 1 3   ? 7.735   26.807  61.880 1.00 20.59  ? 45   PHE A CD2   1 
ATOM   22   C CE1   . PHE A 1 3   ? 8.288   25.919  59.343 1.00 18.91  ? 45   PHE A CE1   1 
ATOM   23   C CE2   . PHE A 1 3   ? 7.382   27.560  60.786 1.00 20.69  ? 45   PHE A CE2   1 
ATOM   24   C CZ    . PHE A 1 3   ? 7.656   27.113  59.511 1.00 21.02  ? 45   PHE A CZ    1 
ATOM   25   N N     . ALA A 1 4   ? 10.305  27.005  64.449 1.00 20.02  ? 46   ALA A N     1 
ATOM   26   C CA    . ALA A 1 4   ? 10.644  28.410  64.518 1.00 19.41  ? 46   ALA A CA    1 
ATOM   27   C C     . ALA A 1 4   ? 12.164  28.597  64.632 1.00 17.58  ? 46   ALA A C     1 
ATOM   28   O O     . ALA A 1 4   ? 12.709  29.503  63.988 1.00 19.77  ? 46   ALA A O     1 
ATOM   29   C CB    . ALA A 1 4   ? 9.893   29.087  65.647 1.00 22.92  ? 46   ALA A CB    1 
ATOM   30   N N     . GLY A 1 5   ? 12.849  27.736  65.394 1.00 18.01  ? 47   GLY A N     1 
ATOM   31   C CA    . GLY A 1 5   ? 14.298  27.828  65.539 1.00 17.37  ? 47   GLY A CA    1 
ATOM   32   C C     . GLY A 1 5   ? 15.023  27.523  64.216 1.00 16.92  ? 47   GLY A C     1 
ATOM   33   O O     . GLY A 1 5   ? 16.008  28.157  63.855 1.00 15.92  ? 47   GLY A O     1 
ATOM   34   N N     . ALA A 1 6   ? 14.568  26.480  63.534 1.00 16.73  ? 48   ALA A N     1 
ATOM   35   C CA    . ALA A 1 6   ? 15.111  26.156  62.219 1.00 13.91  ? 48   ALA A CA    1 
ATOM   36   C C     . ALA A 1 6   ? 14.989  27.309  61.233 1.00 14.42  ? 48   ALA A C     1 
ATOM   37   O O     . ALA A 1 6   ? 15.971  27.646  60.580 1.00 14.89  ? 48   ALA A O     1 
ATOM   38   C CB    . ALA A 1 6   ? 14.419  24.921  61.686 1.00 13.07  ? 48   ALA A CB    1 
ATOM   39   N N     . MET A 1 7   ? 13.801  27.903  61.130 1.00 16.01  ? 49   MET A N     1 
ATOM   40   C CA    . MET A 1 7   ? 13.541  28.911  60.121 1.00 17.11  ? 49   MET A CA    1 
ATOM   41   C C     . MET A 1 7   ? 14.347  30.169  60.455 1.00 17.14  ? 49   MET A C     1 
ATOM   42   O O     . MET A 1 7   ? 14.924  30.803  59.574 1.00 16.12  ? 49   MET A O     1 
ATOM   43   C CB    . MET A 1 7   ? 12.030  29.201  60.058 1.00 18.36  ? 49   MET A CB    1 
ATOM   44   C CG    . MET A 1 7   ? 11.161  28.039  59.596 1.00 17.57  ? 49   MET A CG    1 
ATOM   45   S SD    . MET A 1 7   ? 11.613  27.383  57.982 1.00 19.86  ? 49   MET A SD    1 
ATOM   46   C CE    . MET A 1 7   ? 10.468  28.252  56.920 1.00 20.51  ? 49   MET A CE    1 
ATOM   47   N N     . LYS A 1 8   ? 14.515  30.468  61.748 1.00 16.35  ? 50   LYS A N     1 
ATOM   48   C CA    . LYS A 1 8   ? 15.356  31.615  62.076 1.00 17.93  ? 50   LYS A CA    1 
ATOM   49   C C     . LYS A 1 8   ? 16.808  31.384  61.665 1.00 15.95  ? 50   LYS A C     1 
ATOM   50   O O     . LYS A 1 8   ? 17.474  32.248  61.101 1.00 15.51  ? 50   LYS A O     1 
ATOM   51   C CB    . LYS A 1 8   ? 15.240  31.965  63.563 1.00 19.70  ? 50   LYS A CB    1 
ATOM   52   C CG    . LYS A 1 8   ? 16.223  33.024  64.011 1.00 23.13  ? 50   LYS A CG    1 
ATOM   53   C CD    . LYS A 1 8   ? 16.061  33.339  65.454 1.00 28.41  ? 50   LYS A CD    1 
ATOM   54   C CE    . LYS A 1 8   ? 17.026  34.403  65.911 1.00 34.78  ? 50   LYS A CE    1 
ATOM   55   N NZ    . LYS A 1 8   ? 16.688  34.814  67.299 1.00 41.21  ? 50   LYS A NZ    1 
ATOM   56   N N     . ALA A 1 9   ? 17.306  30.176  61.921 1.00 14.57  ? 51   ALA A N     1 
ATOM   57   C CA    . ALA A 1 9   ? 18.650  29.831  61.539 1.00 13.84  ? 51   ALA A CA    1 
ATOM   58   C C     . ALA A 1 9   ? 18.817  29.818  60.018 1.00 15.38  ? 51   ALA A C     1 
ATOM   59   O O     . ALA A 1 9   ? 19.851  30.281  59.524 1.00 14.92  ? 51   ALA A O     1 
ATOM   60   C CB    . ALA A 1 9   ? 19.007  28.492  62.161 1.00 14.66  ? 51   ALA A CB    1 
ATOM   61   N N     . PHE A 1 10  ? 17.806  29.318  59.290 1.00 14.54  ? 52   PHE A N     1 
ATOM   62   C CA    . PHE A 1 10  ? 17.857  29.339  57.822 1.00 14.75  ? 52   PHE A CA    1 
ATOM   63   C C     . PHE A 1 10  ? 17.939  30.771  57.266 1.00 15.36  ? 52   PHE A C     1 
ATOM   64   O O     . PHE A 1 10  ? 18.673  31.030  56.305 1.00 16.31  ? 52   PHE A O     1 
ATOM   65   C CB    . PHE A 1 10  ? 16.644  28.642  57.215 1.00 13.10  ? 52   PHE A CB    1 
ATOM   66   C CG    . PHE A 1 10  ? 16.471  27.147  57.408 1.00 12.81  ? 52   PHE A CG    1 
ATOM   67   C CD1   . PHE A 1 10  ? 17.502  26.283  57.660 1.00 11.75  ? 52   PHE A CD1   1 
ATOM   68   C CD2   . PHE A 1 10  ? 15.187  26.635  57.408 1.00 13.53  ? 52   PHE A CD2   1 
ATOM   69   C CE1   . PHE A 1 10  ? 17.268  24.931  57.821 1.00 14.30  ? 52   PHE A CE1   1 
ATOM   70   C CE2   . PHE A 1 10  ? 14.962  25.285  57.565 1.00 13.65  ? 52   PHE A CE2   1 
ATOM   71   C CZ    . PHE A 1 10  ? 16.002  24.440  57.798 1.00 12.52  ? 52   PHE A CZ    1 
ATOM   72   N N     . ARG A 1 11  ? 17.255  31.742  57.903 1.00 15.34  ? 53   ARG A N     1 
ATOM   73   C CA    . ARG A 1 11  ? 17.370  33.120  57.434 1.00 15.55  ? 53   ARG A CA    1 
ATOM   74   C C     . ARG A 1 11  ? 18.807  33.623  57.509 1.00 16.61  ? 53   ARG A C     1 
ATOM   75   O O     . ARG A 1 11  ? 19.228  34.393  56.648 1.00 17.82  ? 53   ARG A O     1 
ATOM   76   C CB    . ARG A 1 11  ? 16.434  34.044  58.225 1.00 17.64  ? 53   ARG A CB    1 
ATOM   77   C CG    . ARG A 1 11  ? 14.960  33.728  58.053 1.00 17.87  ? 53   ARG A CG    1 
ATOM   78   C CD    . ARG A 1 11  ? 14.018  34.612  58.884 1.00 20.46  ? 53   ARG A CD    1 
ATOM   79   N NE    . ARG A 1 11  ? 12.635  34.199  58.656 1.00 21.20  ? 53   ARG A NE    1 
ATOM   80   C CZ    . ARG A 1 11  ? 11.925  33.422  59.481 1.00 21.80  ? 53   ARG A CZ    1 
ATOM   81   N NH1   . ARG A 1 11  ? 12.329  33.169  60.719 1.00 22.72  ? 53   ARG A NH1   1 
ATOM   82   N NH2   . ARG A 1 11  ? 10.814  32.883  59.035 1.00 23.72  ? 53   ARG A NH2   1 
ATOM   83   N N     . GLY A 1 12  ? 19.554  33.196  58.535 1.00 15.19  ? 54   GLY A N     1 
ATOM   84   C CA    . GLY A 1 12  ? 20.947  33.528  58.721 1.00 16.40  ? 54   GLY A CA    1 
ATOM   85   C C     . GLY A 1 12  ? 21.838  32.948  57.630 1.00 17.09  ? 54   GLY A C     1 
ATOM   86   O O     . GLY A 1 12  ? 22.903  33.484  57.349 1.00 19.96  ? 54   GLY A O     1 
ATOM   87   N N     . VAL A 1 13  ? 21.403  31.833  57.008 1.00 14.68  ? 55   VAL A N     1 
ATOM   88   C CA    . VAL A 1 13  ? 22.185  31.215  55.954 1.00 14.53  ? 55   VAL A CA    1 
ATOM   89   C C     . VAL A 1 13  ? 21.901  31.859  54.603 1.00 15.41  ? 55   VAL A C     1 
ATOM   90   O O     . VAL A 1 13  ? 22.844  32.177  53.892 1.00 18.30  ? 55   VAL A O     1 
ATOM   91   C CB    . VAL A 1 13  ? 21.911  29.701  55.879 1.00 15.30  ? 55   VAL A CB    1 
ATOM   92   C CG1   . VAL A 1 13  ? 22.714  29.062  54.723 1.00 15.86  ? 55   VAL A CG1   1 
ATOM   93   C CG2   . VAL A 1 13  ? 22.255  28.990  57.187 1.00 16.81  ? 55   VAL A CG2   1 
ATOM   94   N N     . VAL A 1 14  ? 20.647  31.944  54.190 1.00 13.66  ? 56   VAL A N     1 
ATOM   95   C CA    . VAL A 1 14  ? 20.345  32.311  52.821 1.00 14.05  ? 56   VAL A CA    1 
ATOM   96   C C     . VAL A 1 14  ? 19.898  33.771  52.736 1.00 17.14  ? 56   VAL A C     1 
ATOM   97   O O     . VAL A 1 14  ? 19.753  34.263  51.632 1.00 17.85  ? 56   VAL A O     1 
ATOM   98   C CB    . VAL A 1 14  ? 19.296  31.367  52.202 1.00 14.18  ? 56   VAL A CB    1 
ATOM   99   C CG1   . VAL A 1 14  ? 19.860  29.939  52.075 1.00 14.12  ? 56   VAL A CG1   1 
ATOM   100  C CG2   . VAL A 1 14  ? 18.001  31.401  52.984 1.00 13.77  ? 56   VAL A CG2   1 
ATOM   101  N N     . GLY A 1 15  ? 19.597  34.401  53.870 1.00 16.73  ? 57   GLY A N     1 
ATOM   102  C CA    . GLY A 1 15  ? 18.931  35.701  53.869 1.00 18.89  ? 57   GLY A CA    1 
ATOM   103  C C     . GLY A 1 15  ? 17.421  35.563  54.080 1.00 18.63  ? 57   GLY A C     1 
ATOM   104  O O     . GLY A 1 15  ? 16.755  34.665  53.544 1.00 16.94  ? 57   GLY A O     1 
ATOM   105  N N     . ALA A 1 16  ? 16.818  36.505  54.817 1.00 18.07  ? 58   ALA A N     1 
ATOM   106  C CA    . ALA A 1 16  ? 15.404  36.424  55.115 1.00 18.02  ? 58   ALA A CA    1 
ATOM   107  C C     . ALA A 1 16  ? 14.528  36.384  53.860 1.00 17.23  ? 58   ALA A C     1 
ATOM   108  O O     . ALA A 1 16  ? 13.461  35.758  53.879 1.00 17.71  ? 58   ALA A O     1 
ATOM   109  C CB    . ALA A 1 16  ? 14.970  37.570  56.024 1.00 20.60  ? 58   ALA A CB    1 
ATOM   110  N N     . GLU A 1 17  ? 14.990  36.965  52.746 1.00 16.82  ? 59   GLU A N     1 
ATOM   111  C CA    . GLU A 1 17  ? 14.169  37.041  51.551 1.00 18.53  ? 59   GLU A CA    1 
ATOM   112  C C     . GLU A 1 17  ? 14.072  35.693  50.813 1.00 17.63  ? 59   GLU A C     1 
ATOM   113  O O     . GLU A 1 17  ? 13.216  35.566  49.910 1.00 17.83  ? 59   GLU A O     1 
ATOM   114  C CB    . GLU A 1 17  ? 14.660  38.121  50.578 1.00 20.38  ? 59   GLU A CB    1 
ATOM   115  C CG    . GLU A 1 17  ? 16.025  37.868  49.943 1.00 22.29  ? 59   GLU A CG    1 
ATOM   116  C CD    . GLU A 1 17  ? 17.293  38.226  50.699 1.00 26.24  ? 59   GLU A CD    1 
ATOM   117  O OE1   . GLU A 1 17  ? 17.245  38.396  51.952 1.00 27.44  ? 59   GLU A OE1   1 
ATOM   118  O OE2   . GLU A 1 17  ? 18.362  38.348  50.018 1.00 29.45  ? 59   GLU A OE2   1 
ATOM   119  N N     . TRP A 1 18  ? 14.823  34.678  51.277 1.00 17.27  ? 60   TRP A N     1 
ATOM   120  C CA    . TRP A 1 18  ? 14.818  33.360  50.629 1.00 14.27  ? 60   TRP A CA    1 
ATOM   121  C C     . TRP A 1 18  ? 14.276  32.291  51.567 1.00 15.11  ? 60   TRP A C     1 
ATOM   122  O O     . TRP A 1 18  ? 14.405  31.104  51.294 1.00 14.51  ? 60   TRP A O     1 
ATOM   123  C CB    . TRP A 1 18  ? 16.221  33.021  50.079 1.00 14.73  ? 60   TRP A CB    1 
ATOM   124  C CG    . TRP A 1 18  ? 16.624  33.918  48.952 1.00 16.17  ? 60   TRP A CG    1 
ATOM   125  C CD1   . TRP A 1 18  ? 17.635  34.841  48.959 1.00 19.20  ? 60   TRP A CD1   1 
ATOM   126  C CD2   . TRP A 1 18  ? 16.004  34.004  47.662 1.00 16.74  ? 60   TRP A CD2   1 
ATOM   127  N NE1   . TRP A 1 18  ? 17.677  35.470  47.748 1.00 19.32  ? 60   TRP A NE1   1 
ATOM   128  C CE2   . TRP A 1 18  ? 16.699  34.999  46.949 1.00 16.75  ? 60   TRP A CE2   1 
ATOM   129  C CE3   . TRP A 1 18  ? 14.919  33.355  47.075 1.00 18.56  ? 60   TRP A CE3   1 
ATOM   130  C CZ2   . TRP A 1 18  ? 16.377  35.327  45.642 1.00 20.40  ? 60   TRP A CZ2   1 
ATOM   131  C CZ3   . TRP A 1 18  ? 14.599  33.674  45.775 1.00 21.81  ? 60   TRP A CZ3   1 
ATOM   132  C CH2   . TRP A 1 18  ? 15.325  34.649  45.090 1.00 20.95  ? 60   TRP A CH2   1 
ATOM   133  N N     . VAL A 1 19  ? 13.679  32.714  52.695 1.00 15.69  ? 61   VAL A N     1 
ATOM   134  C CA    . VAL A 1 19  ? 12.952  31.832  53.597 1.00 14.62  ? 61   VAL A CA    1 
ATOM   135  C C     . VAL A 1 19  ? 11.473  32.227  53.584 1.00 17.26  ? 61   VAL A C     1 
ATOM   136  O O     . VAL A 1 19  ? 11.122  33.419  53.695 1.00 18.02  ? 61   VAL A O     1 
ATOM   137  C CB    . VAL A 1 19  ? 13.562  31.869  55.010 1.00 14.99  ? 61   VAL A CB    1 
ATOM   138  C CG1   . VAL A 1 19  ? 12.748  31.026  56.004 1.00 16.34  ? 61   VAL A CG1   1 
ATOM   139  C CG2   . VAL A 1 19  ? 15.052  31.434  54.976 1.00 14.53  ? 61   VAL A CG2   1 
ATOM   140  N N     . PHE A 1 20  ? 10.617  31.203  53.511 1.00 15.88  ? 62   PHE A N     1 
ATOM   141  C CA    . PHE A 1 20  ? 9.178   31.358  53.385 1.00 17.29  ? 62   PHE A CA    1 
ATOM   142  C C     . PHE A 1 20  ? 8.551   30.553  54.515 1.00 18.47  ? 62   PHE A C     1 
ATOM   143  O O     . PHE A 1 20  ? 8.556   29.318  54.453 1.00 17.00  ? 62   PHE A O     1 
ATOM   144  C CB    . PHE A 1 20  ? 8.789   30.946  51.960 1.00 15.88  ? 62   PHE A CB    1 
ATOM   145  C CG    . PHE A 1 20  ? 9.486   31.755  50.892 1.00 16.92  ? 62   PHE A CG    1 
ATOM   146  C CD1   . PHE A 1 20  ? 10.738  31.402  50.408 1.00 17.31  ? 62   PHE A CD1   1 
ATOM   147  C CD2   . PHE A 1 20  ? 8.900   32.926  50.414 1.00 18.93  ? 62   PHE A CD2   1 
ATOM   148  C CE1   . PHE A 1 20  ? 11.409  32.197  49.501 1.00 18.31  ? 62   PHE A CE1   1 
ATOM   149  C CE2   . PHE A 1 20  ? 9.556   33.698  49.460 1.00 19.02  ? 62   PHE A CE2   1 
ATOM   150  C CZ    . PHE A 1 20  ? 10.817  33.349  49.033 1.00 19.86  ? 62   PHE A CZ    1 
ATOM   151  N N     . GLY A 1 21  ? 8.024   31.227  55.552 1.00 19.66  ? 63   GLY A N     1 
ATOM   152  C CA    . GLY A 1 21  ? 7.868   30.596  56.863 1.00 19.70  ? 63   GLY A CA    1 
ATOM   153  C C     . GLY A 1 21  ? 6.479   30.687  57.496 1.00 23.56  ? 63   GLY A C     1 
ATOM   154  O O     . GLY A 1 21  ? 6.337   30.435  58.706 1.00 24.22  ? 63   GLY A O     1 
ATOM   155  N N     . ASP A 1 22  ? 5.452   30.950  56.685 1.00 24.43  ? 64   ASP A N     1 
ATOM   156  C CA    . ASP A 1 22  ? 4.079   30.855  57.172 1.00 29.47  ? 64   ASP A CA    1 
ATOM   157  C C     . ASP A 1 22  ? 3.135   30.464  56.037 1.00 28.17  ? 64   ASP A C     1 
ATOM   158  O O     . ASP A 1 22  ? 3.511   30.479  54.866 1.00 26.11  ? 64   ASP A O     1 
ATOM   159  C CB    . ASP A 1 22  ? 3.655   32.172  57.824 1.00 31.77  ? 64   ASP A CB    1 
ATOM   160  C CG    . ASP A 1 22  ? 3.793   33.355  56.896 1.00 34.03  ? 64   ASP A CG    1 
ATOM   161  O OD1   . ASP A 1 22  ? 3.164   33.342  55.816 1.00 32.96  ? 64   ASP A OD1   1 
ATOM   162  O OD2   . ASP A 1 22  ? 4.552   34.257  57.244 1.00 48.18  ? 64   ASP A OD2   1 
ATOM   163  N N     . GLU A 1 23  ? 1.867   30.215  56.381 1.00 31.70  ? 65   GLU A N     1 
ATOM   164  C CA    . GLU A 1 23  ? 0.911   29.676  55.421 1.00 32.21  ? 65   GLU A CA    1 
ATOM   165  C C     . GLU A 1 23  ? 0.835   30.527  54.149 1.00 31.38  ? 65   GLU A C     1 
ATOM   166  O O     . GLU A 1 23  ? 0.804   29.986  53.050 1.00 29.83  ? 65   GLU A O     1 
ATOM   167  C CB    . GLU A 1 23  ? -0.493  29.547  56.021 1.00 37.64  ? 65   GLU A CB    1 
ATOM   168  C CG    . GLU A 1 23  ? -1.466  28.888  55.039 1.00 44.54  ? 65   GLU A CG    1 
ATOM   169  C CD    . GLU A 1 23  ? -2.788  28.421  55.624 1.00 53.27  ? 65   GLU A CD    1 
ATOM   170  O OE1   . GLU A 1 23  ? -2.774  27.902  56.750 1.00 54.59  ? 65   GLU A OE1   1 
ATOM   171  O OE2   . GLU A 1 23  ? -3.819  28.538  54.930 1.00 61.99  ? 65   GLU A OE2   1 
ATOM   172  N N     . GLU A 1 24  ? 0.742   31.853  54.298 1.00 29.83  ? 66   GLU A N     1 
ATOM   173  C CA    . GLU A 1 24  ? 0.606   32.751  53.167 1.00 30.00  ? 66   GLU A CA    1 
ATOM   174  C C     . GLU A 1 24  ? 1.869   32.742  52.302 1.00 26.97  ? 66   GLU A C     1 
ATOM   175  O O     . GLU A 1 24  ? 1.786   32.772  51.080 1.00 25.52  ? 66   GLU A O     1 
ATOM   176  C CB    . GLU A 1 24  ? 0.331   34.167  53.671 1.00 37.90  ? 66   GLU A CB    1 
ATOM   177  C CG    . GLU A 1 24  ? 0.121   35.202  52.574 1.00 49.03  ? 66   GLU A CG    1 
ATOM   178  C CD    . GLU A 1 24  ? -0.289  36.575  53.107 1.00 67.62  ? 66   GLU A CD    1 
ATOM   179  O OE1   . GLU A 1 24  ? -0.358  36.757  54.365 1.00 59.64  ? 66   GLU A OE1   1 
ATOM   180  O OE2   . GLU A 1 24  ? -0.551  37.478  52.273 1.00 77.34  ? 66   GLU A OE2   1 
ATOM   181  N N     . ALA A 1 25  ? 3.043   32.782  52.944 1.00 22.13  ? 67   ALA A N     1 
ATOM   182  C CA    . ALA A 1 25  ? 4.295   32.845  52.210 1.00 20.40  ? 67   ALA A CA    1 
ATOM   183  C C     . ALA A 1 25  ? 4.551   31.529  51.434 1.00 18.11  ? 67   ALA A C     1 
ATOM   184  O O     . ALA A 1 25  ? 5.217   31.574  50.401 1.00 18.94  ? 67   ALA A O     1 
ATOM   185  C CB    . ALA A 1 25  ? 5.417   33.180  53.163 1.00 21.42  ? 67   ALA A CB    1 
ATOM   186  N N     . VAL A 1 26  ? 4.017   30.385  51.888 1.00 19.59  ? 68   VAL A N     1 
ATOM   187  C CA    . VAL A 1 26  ? 4.321   29.108  51.217 1.00 17.52  ? 68   VAL A CA    1 
ATOM   188  C C     . VAL A 1 26  ? 3.285   28.713  50.161 1.00 18.13  ? 68   VAL A C     1 
ATOM   189  O O     . VAL A 1 26  ? 3.398   27.655  49.527 1.00 16.33  ? 68   VAL A O     1 
ATOM   190  C CB    . VAL A 1 26  ? 4.513   27.931  52.196 1.00 21.01  ? 68   VAL A CB    1 
ATOM   191  C CG1   . VAL A 1 26  ? 5.530   28.278  53.245 1.00 26.96  ? 68   VAL A CG1   1 
ATOM   192  C CG2   . VAL A 1 26  ? 3.222   27.468  52.820 1.00 20.75  ? 68   VAL A CG2   1 
ATOM   193  N N     . VAL A 1 27  ? 2.288   29.575  49.904 1.00 18.44  ? 69   VAL A N     1 
ATOM   194  C CA    . VAL A 1 27  ? 1.314   29.346  48.850 1.00 18.92  ? 69   VAL A CA    1 
ATOM   195  C C     . VAL A 1 27  ? 1.986   28.945  47.531 1.00 18.07  ? 69   VAL A C     1 
ATOM   196  O O     . VAL A 1 27  ? 1.507   28.006  46.900 1.00 17.35  ? 69   VAL A O     1 
ATOM   197  C CB    . VAL A 1 27  ? 0.378   30.569  48.662 1.00 21.79  ? 69   VAL A CB    1 
ATOM   198  C CG1   . VAL A 1 27  ? -0.353  30.515  47.340 1.00 25.93  ? 69   VAL A CG1   1 
ATOM   199  C CG2   . VAL A 1 27  ? -0.609  30.667  49.813 1.00 22.37  ? 69   VAL A CG2   1 
ATOM   200  N N     . PRO A 1 28  ? 3.066   29.609  47.030 1.00 18.81  ? 70   PRO A N     1 
ATOM   201  C CA    . PRO A 1 28  ? 3.674   29.191  45.761 1.00 18.18  ? 70   PRO A CA    1 
ATOM   202  C C     . PRO A 1 28  ? 4.167   27.735  45.692 1.00 17.55  ? 70   PRO A C     1 
ATOM   203  O O     . PRO A 1 28  ? 4.439   27.231  44.601 1.00 17.43  ? 70   PRO A O     1 
ATOM   204  C CB    . PRO A 1 28  ? 4.823   30.166  45.544 1.00 19.17  ? 70   PRO A CB    1 
ATOM   205  C CG    . PRO A 1 28  ? 4.383   31.386  46.308 1.00 19.93  ? 70   PRO A CG    1 
ATOM   206  C CD    . PRO A 1 28  ? 3.685   30.843  47.544 1.00 18.28  ? 70   PRO A CD    1 
ATOM   207  N N     . TRP A 1 29  ? 4.298   27.078  46.849 1.00 14.16  ? 71   TRP A N     1 
ATOM   208  C CA    . TRP A 1 29  ? 4.779   25.692  46.914 1.00 13.18  ? 71   TRP A CA    1 
ATOM   209  C C     . TRP A 1 29  ? 3.645   24.701  47.204 1.00 14.00  ? 71   TRP A C     1 
ATOM   210  O O     . TRP A 1 29  ? 3.906   23.516  47.390 1.00 13.91  ? 71   TRP A O     1 
ATOM   211  C CB    . TRP A 1 29  ? 5.897   25.545  47.984 1.00 13.61  ? 71   TRP A CB    1 
ATOM   212  C CG    . TRP A 1 29  ? 7.181   26.201  47.584 1.00 14.31  ? 71   TRP A CG    1 
ATOM   213  C CD1   . TRP A 1 29  ? 8.229   25.625  46.911 1.00 14.60  ? 71   TRP A CD1   1 
ATOM   214  C CD2   . TRP A 1 29  ? 7.561   27.568  47.821 1.00 13.52  ? 71   TRP A CD2   1 
ATOM   215  N NE1   . TRP A 1 29  ? 9.219   26.550  46.696 1.00 16.48  ? 71   TRP A NE1   1 
ATOM   216  C CE2   . TRP A 1 29  ? 8.834   27.754  47.223 1.00 14.62  ? 71   TRP A CE2   1 
ATOM   217  C CE3   . TRP A 1 29  ? 6.926   28.653  48.429 1.00 14.52  ? 71   TRP A CE3   1 
ATOM   218  C CZ2   . TRP A 1 29  ? 9.495   28.982  47.241 1.00 15.97  ? 71   TRP A CZ2   1 
ATOM   219  C CZ3   . TRP A 1 29  ? 7.595   29.857  48.472 1.00 14.77  ? 71   TRP A CZ3   1 
ATOM   220  C CH2   . TRP A 1 29  ? 8.845   30.018  47.878 1.00 15.68  ? 71   TRP A CH2   1 
ATOM   221  N N     . SER A 1 30  ? 2.395   25.152  47.289 1.00 14.77  ? 72   SER A N     1 
ATOM   222  C CA    . SER A 1 30  ? 1.358   24.332  47.895 1.00 15.92  ? 72   SER A CA    1 
ATOM   223  C C     . SER A 1 30  ? 0.388   23.776  46.864 1.00 15.22  ? 72   SER A C     1 
ATOM   224  O O     . SER A 1 30  ? -0.345  22.882  47.239 1.00 17.87  ? 72   SER A O     1 
ATOM   225  C CB    . SER A 1 30  ? 0.619   25.104  48.970 1.00 19.05  ? 72   SER A CB    1 
ATOM   226  O OG    . SER A 1 30  ? 1.509   25.330  50.064 1.00 22.59  ? 72   SER A OG    1 
ATOM   227  N N     . LYS A 1 31  ? 0.340   24.266  45.618 1.00 15.07  ? 73   LYS A N     1 
ATOM   228  C CA    . LYS A 1 31  ? -0.678  23.782  44.682 1.00 16.31  ? 73   LYS A CA    1 
ATOM   229  C C     . LYS A 1 31  ? -0.257  22.411  44.127 1.00 14.17  ? 73   LYS A C     1 
ATOM   230  O O     . LYS A 1 31  ? 0.889   22.230  43.693 1.00 14.34  ? 73   LYS A O     1 
ATOM   231  C CB    . LYS A 1 31  ? -0.905  24.785  43.544 1.00 18.86  ? 73   LYS A CB    1 
ATOM   232  C CG    . LYS A 1 31  ? -2.101  24.492  42.640 1.00 23.82  ? 73   LYS A CG    1 
ATOM   233  C CD    . LYS A 1 31  ? -2.187  25.512  41.510 1.00 28.37  ? 73   LYS A CD    1 
ATOM   234  C CE    . LYS A 1 31  ? -3.332  25.316  40.538 1.00 34.76  ? 73   LYS A CE    1 
ATOM   235  N NZ    . LYS A 1 31  ? -4.612  25.306  41.269 1.00 42.35  ? 73   LYS A NZ    1 
ATOM   236  N N     . THR A 1 32  ? -1.230  21.482  44.046 1.00 12.88  ? 74   THR A N     1 
ATOM   237  C CA    . THR A 1 32  ? -1.015  20.170  43.437 1.00 11.93  ? 74   THR A CA    1 
ATOM   238  C C     . THR A 1 32  ? -2.208  19.865  42.534 1.00 12.16  ? 74   THR A C     1 
ATOM   239  O O     . THR A 1 32  ? -3.248  20.538  42.623 1.00 13.67  ? 74   THR A O     1 
ATOM   240  C CB    . THR A 1 32  ? -0.884  19.025  44.452 1.00 11.71  ? 74   THR A CB    1 
ATOM   241  O OG1   . THR A 1 32  ? -2.112  18.902  45.178 1.00 13.50  ? 74   THR A OG1   1 
ATOM   242  C CG2   . THR A 1 32  ? 0.273   19.194  45.412 1.00 12.00  ? 74   THR A CG2   1 
ATOM   243  N N     . TYR A 1 33  ? -2.063  18.820  41.749 1.00 11.90  ? 75   TYR A N     1 
ATOM   244  C CA    . TYR A 1 33  ? -3.083  18.383  40.793 1.00 13.16  ? 75   TYR A CA    1 
ATOM   245  C C     . TYR A 1 33  ? -3.590  17.002  41.166 1.00 12.05  ? 75   TYR A C     1 
ATOM   246  O O     . TYR A 1 33  ? -4.627  16.554  40.676 1.00 11.68  ? 75   TYR A O     1 
ATOM   247  C CB    . TYR A 1 33  ? -2.570  18.492  39.355 1.00 13.08  ? 75   TYR A CB    1 
ATOM   248  C CG    . TYR A 1 33  ? -2.101  19.884  39.051 1.00 13.52  ? 75   TYR A CG    1 
ATOM   249  C CD1   . TYR A 1 33  ? -2.984  20.879  38.712 1.00 14.88  ? 75   TYR A CD1   1 
ATOM   250  C CD2   . TYR A 1 33  ? -0.768  20.237  39.247 1.00 15.80  ? 75   TYR A CD2   1 
ATOM   251  C CE1   . TYR A 1 33  ? -2.554  22.185  38.549 1.00 16.75  ? 75   TYR A CE1   1 
ATOM   252  C CE2   . TYR A 1 33  ? -0.324  21.546  39.108 1.00 16.03  ? 75   TYR A CE2   1 
ATOM   253  C CZ    . TYR A 1 33  ? -1.228  22.523  38.730 1.00 19.19  ? 75   TYR A CZ    1 
ATOM   254  O OH    . TYR A 1 33  ? -0.841  23.861  38.599 1.00 19.84  ? 75   TYR A OH    1 
ATOM   255  N N     . ILE A 1 34  ? -2.829  16.290  42.005 1.00 11.80  ? 76   ILE A N     1 
ATOM   256  C CA    . ILE A 1 34  ? -3.255  15.012  42.521 1.00 10.80  ? 76   ILE A CA    1 
ATOM   257  C C     . ILE A 1 34  ? -4.472  15.194  43.442 1.00 11.91  ? 76   ILE A C     1 
ATOM   258  O O     . ILE A 1 34  ? -4.700  16.277  43.981 1.00 13.23  ? 76   ILE A O     1 
ATOM   259  C CB    . ILE A 1 34  ? -2.070  14.363  43.252 1.00 12.91  ? 76   ILE A CB    1 
ATOM   260  C CG1   . ILE A 1 34  ? -1.421  15.316  44.264 1.00 15.49  ? 76   ILE A CG1   1 
ATOM   261  C CG2   . ILE A 1 34  ? -1.079  13.785  42.232 1.00 14.85  ? 76   ILE A CG2   1 
ATOM   262  C CD1   . ILE A 1 34  ? -0.907  14.632  45.526 1.00 19.07  ? 76   ILE A CD1   1 
ATOM   263  N N     . PRO A 1 35  ? -5.272  14.135  43.670 1.00 13.22  ? 77   PRO A N     1 
ATOM   264  C CA    . PRO A 1 35  ? -6.407  14.242  44.578 1.00 13.89  ? 77   PRO A CA    1 
ATOM   265  C C     . PRO A 1 35  ? -5.895  14.318  46.019 1.00 15.42  ? 77   PRO A C     1 
ATOM   266  O O     . PRO A 1 35  ? -5.004  13.547  46.396 1.00 17.55  ? 77   PRO A O     1 
ATOM   267  C CB    . PRO A 1 35  ? -7.179  12.960  44.362 1.00 16.01  ? 77   PRO A CB    1 
ATOM   268  C CG    . PRO A 1 35  ? -6.242  12.010  43.700 1.00 15.33  ? 77   PRO A CG    1 
ATOM   269  C CD    . PRO A 1 35  ? -5.162  12.826  43.007 1.00 14.08  ? 77   PRO A CD    1 
ATOM   270  N N     . ASP A 1 36  ? -6.478  15.201  46.830 1.00 14.82  ? 78   ASP A N     1 
ATOM   271  C CA    . ASP A 1 36  ? -6.056  15.325  48.209 1.00 14.02  ? 78   ASP A CA    1 
ATOM   272  C C     . ASP A 1 36  ? -7.254  15.754  49.059 1.00 14.60  ? 78   ASP A C     1 
ATOM   273  O O     . ASP A 1 36  ? -7.280  16.889  49.502 1.00 16.44  ? 78   ASP A O     1 
ATOM   274  C CB    . ASP A 1 36  ? -4.896  16.311  48.328 1.00 15.25  ? 78   ASP A CB    1 
ATOM   275  C CG    . ASP A 1 36  ? -4.281  16.405  49.720 1.00 15.20  ? 78   ASP A CG    1 
ATOM   276  O OD1   . ASP A 1 36  ? -4.724  15.604  50.621 1.00 14.34  ? 78   ASP A OD1   1 
ATOM   277  O OD2   . ASP A 1 36  ? -3.387  17.284  49.902 1.00 14.75  ? 78   ASP A OD2   1 
ATOM   278  N N     . PRO A 1 37  ? -8.287  14.887  49.204 1.00 18.25  ? 79   PRO A N     1 
ATOM   279  C CA    . PRO A 1 37  ? -9.519  15.251  49.912 1.00 18.40  ? 79   PRO A CA    1 
ATOM   280  C C     . PRO A 1 37  ? -9.284  15.688  51.350 1.00 23.87  ? 79   PRO A C     1 
ATOM   281  O O     . PRO A 1 37  ? -9.942  16.619  51.805 1.00 28.46  ? 79   PRO A O     1 
ATOM   282  C CB    . PRO A 1 37  ? -10.382 13.980  49.841 1.00 18.95  ? 79   PRO A CB    1 
ATOM   283  C CG    . PRO A 1 37  ? -9.785  13.119  48.833 1.00 20.71  ? 79   PRO A CG    1 
ATOM   284  C CD    . PRO A 1 37  ? -8.341  13.534  48.648 1.00 18.02  ? 79   PRO A CD    1 
ATOM   285  N N     . ALA A 1 38  ? -8.254  15.144  52.010 1.00 23.11  ? 80   ALA A N     1 
ATOM   286  C CA    . ALA A 1 38  ? -7.975  15.554  53.384 1.00 26.79  ? 80   ALA A CA    1 
ATOM   287  C C     . ALA A 1 38  ? -7.082  16.795  53.466 1.00 26.72  ? 80   ALA A C     1 
ATOM   288  O O     . ALA A 1 38  ? -6.775  17.240  54.577 1.00 27.17  ? 80   ALA A O     1 
ATOM   289  C CB    . ALA A 1 38  ? -7.363  14.414  54.150 1.00 27.67  ? 80   ALA A CB    1 
ATOM   290  N N     . HIS A 1 39  ? -6.640  17.373  52.329 1.00 22.04  ? 81   HIS A N     1 
ATOM   291  C CA    . HIS A 1 39  ? -5.736  18.509  52.328 1.00 27.00  ? 81   HIS A CA    1 
ATOM   292  C C     . HIS A 1 39  ? -4.497  18.231  53.188 1.00 23.32  ? 81   HIS A C     1 
ATOM   293  O O     . HIS A 1 39  ? -4.065  19.094  53.936 1.00 26.47  ? 81   HIS A O     1 
ATOM   294  C CB    . HIS A 1 39  ? -6.453  19.805  52.739 1.00 33.61  ? 81   HIS A CB    1 
ATOM   295  C CG    . HIS A 1 39  ? -7.638  20.083  51.877 1.00 43.09  ? 81   HIS A CG    1 
ATOM   296  N ND1   . HIS A 1 39  ? -7.598  20.980  50.830 1.00 55.62  ? 81   HIS A ND1   1 
ATOM   297  C CD2   . HIS A 1 39  ? -8.857  19.533  51.850 1.00 50.91  ? 81   HIS A CD2   1 
ATOM   298  C CE1   . HIS A 1 39  ? -8.774  20.992  50.218 1.00 54.06  ? 81   HIS A CE1   1 
ATOM   299  N NE2   . HIS A 1 39  ? -9.550  20.106  50.812 1.00 55.26  ? 81   HIS A NE2   1 
ATOM   300  N N     . GLN A 1 40  ? -3.907  17.041  53.040 1.00 19.22  ? 82   GLN A N     1 
ATOM   301  C CA    . GLN A 1 40  ? -2.818  16.640  53.929 1.00 18.15  ? 82   GLN A CA    1 
ATOM   302  C C     . GLN A 1 40  ? -1.439  16.794  53.267 1.00 17.98  ? 82   GLN A C     1 
ATOM   303  O O     . GLN A 1 40  ? -0.436  16.697  53.968 1.00 19.47  ? 82   GLN A O     1 
ATOM   304  C CB    . GLN A 1 40  ? -3.037  15.214  54.441 1.00 21.89  ? 82   GLN A CB    1 
ATOM   305  C CG    . GLN A 1 40  ? -2.865  14.130  53.394 1.00 22.55  ? 82   GLN A CG    1 
ATOM   306  C CD    . GLN A 1 40  ? -3.252  12.744  53.869 1.00 28.73  ? 82   GLN A CD    1 
ATOM   307  O OE1   . GLN A 1 40  ? -2.654  12.199  54.796 1.00 34.06  ? 82   GLN A OE1   1 
ATOM   308  N NE2   . GLN A 1 40  ? -4.215  12.136  53.200 1.00 24.74  ? 82   GLN A NE2   1 
ATOM   309  N N     . TYR A 1 41  ? -1.346  16.930  51.943 1.00 15.09  ? 83   TYR A N     1 
ATOM   310  C CA    . TYR A 1 41  ? -0.042  17.063  51.271 1.00 14.90  ? 83   TYR A CA    1 
ATOM   311  C C     . TYR A 1 41  ? 0.274   18.545  51.040 1.00 14.05  ? 83   TYR A C     1 
ATOM   312  O O     . TYR A 1 41  ? -0.210  19.157  50.076 1.00 15.12  ? 83   TYR A O     1 
ATOM   313  C CB    . TYR A 1 41  ? 0.023   16.227  49.984 1.00 13.95  ? 83   TYR A CB    1 
ATOM   314  C CG    . TYR A 1 41  ? -0.277  14.767  50.258 1.00 13.97  ? 83   TYR A CG    1 
ATOM   315  C CD1   . TYR A 1 41  ? 0.610   13.976  50.983 1.00 14.32  ? 83   TYR A CD1   1 
ATOM   316  C CD2   . TYR A 1 41  ? -1.509  14.225  49.945 1.00 15.18  ? 83   TYR A CD2   1 
ATOM   317  C CE1   . TYR A 1 41  ? 0.314   12.687  51.349 1.00 15.07  ? 83   TYR A CE1   1 
ATOM   318  C CE2   . TYR A 1 41  ? -1.832  12.928  50.324 1.00 15.84  ? 83   TYR A CE2   1 
ATOM   319  C CZ    . TYR A 1 41  ? -0.928  12.169  51.049 1.00 16.21  ? 83   TYR A CZ    1 
ATOM   320  O OH    . TYR A 1 41  ? -1.281  10.891  51.370 1.00 17.52  ? 83   TYR A OH    1 
ATOM   321  N N     . LYS A 1 42  ? 1.026   19.123  51.994 1.00 13.90  ? 84   LYS A N     1 
ATOM   322  C CA    . LYS A 1 42  ? 1.271   20.552  52.021 1.00 15.77  ? 84   LYS A CA    1 
ATOM   323  C C     . LYS A 1 42  ? 2.544   20.842  52.795 1.00 12.97  ? 84   LYS A C     1 
ATOM   324  O O     . LYS A 1 42  ? 2.768   20.337  53.897 1.00 14.24  ? 84   LYS A O     1 
ATOM   325  C CB    . LYS A 1 42  ? 0.102   21.336  52.631 1.00 21.35  ? 84   LYS A CB    1 
ATOM   326  C CG    . LYS A 1 42  ? -0.159  21.121  54.105 1.00 30.96  ? 84   LYS A CG    1 
ATOM   327  C CD    . LYS A 1 42  ? -1.260  22.019  54.664 1.00 45.78  ? 84   LYS A CD    1 
ATOM   328  C CE    . LYS A 1 42  ? -2.646  21.645  54.180 1.00 60.67  ? 84   LYS A CE    1 
ATOM   329  N NZ    . LYS A 1 42  ? -3.501  22.844  53.962 1.00 69.16  ? 84   LYS A NZ    1 
ATOM   330  N N     . PRO A 1 43  ? 3.411   21.715  52.263 1.00 13.97  ? 85   PRO A N     1 
ATOM   331  C CA    . PRO A 1 43  ? 4.597   22.131  53.010 1.00 14.54  ? 85   PRO A CA    1 
ATOM   332  C C     . PRO A 1 43  ? 4.252   23.177  54.069 1.00 14.22  ? 85   PRO A C     1 
ATOM   333  O O     . PRO A 1 43  ? 3.233   23.886  53.953 1.00 15.23  ? 85   PRO A O     1 
ATOM   334  C CB    . PRO A 1 43  ? 5.446   22.714  51.888 1.00 15.65  ? 85   PRO A CB    1 
ATOM   335  C CG    . PRO A 1 43  ? 4.432   23.387  51.013 1.00 15.79  ? 85   PRO A CG    1 
ATOM   336  C CD    . PRO A 1 43  ? 3.249   22.442  50.989 1.00 16.39  ? 85   PRO A CD    1 
ATOM   337  N N     . VAL A 1 44  ? 5.116   23.296  55.088 1.00 14.18  ? 86   VAL A N     1 
ATOM   338  C CA    . VAL A 1 44  ? 4.968   24.331  56.107 1.00 15.49  ? 86   VAL A CA    1 
ATOM   339  C C     . VAL A 1 44  ? 5.953   25.472  55.923 1.00 16.24  ? 86   VAL A C     1 
ATOM   340  O O     . VAL A 1 44  ? 5.846   26.497  56.579 1.00 16.78  ? 86   VAL A O     1 
ATOM   341  C CB    . VAL A 1 44  ? 5.057   23.756  57.535 1.00 16.77  ? 86   VAL A CB    1 
ATOM   342  C CG1   . VAL A 1 44  ? 3.908   22.811  57.807 1.00 16.44  ? 86   VAL A CG1   1 
ATOM   343  C CG2   . VAL A 1 44  ? 6.399   23.082  57.853 1.00 15.72  ? 86   VAL A CG2   1 
ATOM   344  N N     . GLY A 1 45  ? 6.888   25.345  54.977 1.00 13.61  ? 87   GLY A N     1 
ATOM   345  C CA    . GLY A 1 45  ? 7.888   26.341  54.739 1.00 13.36  ? 87   GLY A CA    1 
ATOM   346  C C     . GLY A 1 45  ? 8.667   26.011  53.468 1.00 12.25  ? 87   GLY A C     1 
ATOM   347  O O     . GLY A 1 45  ? 8.468   24.969  52.846 1.00 13.48  ? 87   GLY A O     1 
ATOM   348  N N     . ALA A 1 46  ? 9.452   26.965  53.011 1.00 11.20  ? 88   ALA A N     1 
ATOM   349  C CA    . ALA A 1 46  ? 10.401  26.731  51.932 1.00 12.56  ? 88   ALA A CA    1 
ATOM   350  C C     . ALA A 1 46  ? 11.675  27.551  52.155 1.00 14.81  ? 88   ALA A C     1 
ATOM   351  O O     . ALA A 1 46  ? 11.654  28.619  52.786 1.00 13.04  ? 88   ALA A O     1 
ATOM   352  C CB    . ALA A 1 46  ? 9.792   27.042  50.601 1.00 12.66  ? 88   ALA A CB    1 
ATOM   353  N N     . VAL A 1 47  ? 12.813  27.020  51.660 1.00 11.94  ? 89   VAL A N     1 
ATOM   354  C CA    . VAL A 1 47  ? 14.093  27.695  51.727 1.00 13.28  ? 89   VAL A CA    1 
ATOM   355  C C     . VAL A 1 47  ? 14.797  27.510  50.390 1.00 14.38  ? 89   VAL A C     1 
ATOM   356  O O     . VAL A 1 47  ? 14.783  26.421  49.824 1.00 13.75  ? 89   VAL A O     1 
ATOM   357  C CB    . VAL A 1 47  ? 14.943  27.207  52.894 1.00 15.14  ? 89   VAL A CB    1 
ATOM   358  C CG1   . VAL A 1 47  ? 16.296  27.898  52.995 1.00 17.24  ? 89   VAL A CG1   1 
ATOM   359  C CG2   . VAL A 1 47  ? 14.192  27.219  54.201 1.00 24.21  ? 89   VAL A CG2   1 
ATOM   360  N N     . CYS A 1 48  ? 15.396  28.579  49.872 1.00 13.02  ? 90   CYS A N     1 
ATOM   361  C CA    . CYS A 1 48  ? 15.938  28.613  48.532 1.00 12.05  ? 90   CYS A CA    1 
ATOM   362  C C     . CYS A 1 48  ? 17.391  29.052  48.546 1.00 12.52  ? 90   CYS A C     1 
ATOM   363  O O     . CYS A 1 48  ? 17.719  30.238  48.327 1.00 13.76  ? 90   CYS A O     1 
ATOM   364  C CB    . CYS A 1 48  ? 15.172  29.561  47.622 1.00 14.86  ? 90   CYS A CB    1 
ATOM   365  S SG    . CYS A 1 48  ? 13.395  29.207  47.533 1.00 17.43  ? 90   CYS A SG    1 
ATOM   366  N N     . PRO A 1 49  ? 18.355  28.120  48.703 1.00 12.13  ? 91   PRO A N     1 
ATOM   367  C CA    . PRO A 1 49  ? 19.767  28.450  48.617 1.00 11.55  ? 91   PRO A CA    1 
ATOM   368  C C     . PRO A 1 49  ? 20.324  28.595  47.202 1.00 12.54  ? 91   PRO A C     1 
ATOM   369  O O     . PRO A 1 49  ? 19.764  28.043  46.235 1.00 12.22  ? 91   PRO A O     1 
ATOM   370  C CB    . PRO A 1 49  ? 20.472  27.293  49.327 1.00 12.03  ? 91   PRO A CB    1 
ATOM   371  C CG    . PRO A 1 49  ? 19.554  26.102  48.931 1.00 11.81  ? 91   PRO A CG    1 
ATOM   372  C CD    . PRO A 1 49  ? 18.148  26.688  48.973 1.00 11.52  ? 91   PRO A CD    1 
ATOM   373  N N     . GLN A 1 50  ? 21.461  29.317  47.115 1.00 12.55  ? 92   GLN A N     1 
ATOM   374  C CA    . GLN A 1 50  ? 22.143  29.486  45.836 1.00 14.22  ? 92   GLN A CA    1 
ATOM   375  C C     . GLN A 1 50  ? 23.496  28.774  45.755 1.00 14.25  ? 92   GLN A C     1 
ATOM   376  O O     . GLN A 1 50  ? 24.098  28.758  44.682 1.00 15.33  ? 92   GLN A O     1 
ATOM   377  C CB    . GLN A 1 50  ? 22.236  30.971  45.485 1.00 15.12  ? 92   GLN A CB    1 
ATOM   378  C CG    . GLN A 1 50  ? 22.973  31.836  46.493 1.00 16.64  ? 92   GLN A CG    1 
ATOM   379  C CD    . GLN A 1 50  ? 24.473  31.743  46.435 1.00 15.70  ? 92   GLN A CD    1 
ATOM   380  O OE1   . GLN A 1 50  ? 25.053  31.647  45.367 1.00 17.90  ? 92   GLN A OE1   1 
ATOM   381  N NE2   . GLN A 1 50  ? 25.146  31.817  47.573 1.00 16.83  ? 92   GLN A NE2   1 
ATOM   382  N N     . SER A 1 51  ? 24.014  28.231  46.868 1.00 13.35  ? 93   SER A N     1 
ATOM   383  C CA    . SER A 1 51  ? 25.293  27.553  46.833 1.00 13.92  ? 93   SER A CA    1 
ATOM   384  C C     . SER A 1 51  ? 25.240  26.225  47.571 1.00 11.38  ? 93   SER A C     1 
ATOM   385  O O     . SER A 1 51  ? 24.459  26.049  48.490 1.00 11.12  ? 93   SER A O     1 
ATOM   386  C CB    . SER A 1 51  ? 26.401  28.371  47.383 1.00 13.84  ? 93   SER A CB    1 
ATOM   387  O OG    . SER A 1 51  ? 26.270  28.517  48.806 1.00 14.78  ? 93   SER A OG    1 
ATOM   388  N N     . VAL A 1 52  ? 26.147  25.307  47.216 1.00 13.50  ? 94   VAL A N     1 
ATOM   389  C CA    . VAL A 1 52  ? 26.247  24.021  47.932 1.00 14.13  ? 94   VAL A CA    1 
ATOM   390  C C     . VAL A 1 52  ? 26.654  24.276  49.399 1.00 14.17  ? 94   VAL A C     1 
ATOM   391  O O     . VAL A 1 52  ? 26.201  23.578  50.296 1.00 13.24  ? 94   VAL A O     1 
ATOM   392  C CB    . VAL A 1 52  ? 27.206  23.088  47.163 1.00 17.34  ? 94   VAL A CB    1 
ATOM   393  C CG1   . VAL A 1 52  ? 28.626  23.652  47.151 1.00 18.97  ? 94   VAL A CG1   1 
ATOM   394  C CG2   . VAL A 1 52  ? 27.231  21.678  47.726 1.00 18.87  ? 94   VAL A CG2   1 
ATOM   395  N N     . GLU A 1 53  ? 27.480  25.283  49.689 1.00 12.91  ? 95   GLU A N     1 
ATOM   396  C CA    . GLU A 1 53  ? 27.848  25.568  51.071 1.00 14.34  ? 95   GLU A CA    1 
ATOM   397  C C     . GLU A 1 53  ? 26.622  25.962  51.908 1.00 14.09  ? 95   GLU A C     1 
ATOM   398  O O     . GLU A 1 53  ? 26.502  25.559  53.083 1.00 13.59  ? 95   GLU A O     1 
ATOM   399  C CB    . GLU A 1 53  ? 28.893  26.694  51.151 1.00 16.11  ? 95   GLU A CB    1 
ATOM   400  C CG    . GLU A 1 53  ? 30.257  26.303  50.550 1.00 18.89  ? 95   GLU A CG    1 
ATOM   401  C CD    . GLU A 1 53  ? 30.406  26.449  49.051 1.00 22.26  ? 95   GLU A CD    1 
ATOM   402  O OE1   . GLU A 1 53  ? 29.478  26.961  48.360 1.00 20.55  ? 95   GLU A OE1   1 
ATOM   403  O OE2   . GLU A 1 53  ? 31.489  26.001  48.553 1.00 28.70  ? 95   GLU A OE2   1 
ATOM   404  N N     . GLU A 1 54  ? 25.693  26.728  51.318 1.00 11.94  ? 96   GLU A N     1 
ATOM   405  C CA    . GLU A 1 54  ? 24.434  27.032  52.018 1.00 11.70  ? 96   GLU A CA    1 
ATOM   406  C C     . GLU A 1 54  ? 23.624  25.739  52.267 1.00 11.18  ? 96   GLU A C     1 
ATOM   407  O O     . GLU A 1 54  ? 23.012  25.562  53.349 1.00 11.24  ? 96   GLU A O     1 
ATOM   408  C CB    . GLU A 1 54  ? 23.608  28.070  51.254 1.00 12.69  ? 96   GLU A CB    1 
ATOM   409  C CG    . GLU A 1 54  ? 24.179  29.486  51.243 1.00 14.68  ? 96   GLU A CG    1 
ATOM   410  C CD    . GLU A 1 54  ? 23.490  30.405  50.262 1.00 16.26  ? 96   GLU A CD    1 
ATOM   411  O OE1   . GLU A 1 54  ? 22.636  29.964  49.503 1.00 16.10  ? 96   GLU A OE1   1 
ATOM   412  O OE2   . GLU A 1 54  ? 23.807  31.583  50.256 1.00 18.19  ? 96   GLU A OE2   1 
ATOM   413  N N     . VAL A 1 55  ? 23.601  24.831  51.268 1.00 10.52  ? 97   VAL A N     1 
ATOM   414  C CA    . VAL A 1 55  ? 22.904  23.554  51.446 1.00 10.60  ? 97   VAL A CA    1 
ATOM   415  C C     . VAL A 1 55  ? 23.446  22.828  52.663 1.00 11.40  ? 97   VAL A C     1 
ATOM   416  O O     . VAL A 1 55  ? 22.689  22.332  53.487 1.00 9.74   ? 97   VAL A O     1 
ATOM   417  C CB    . VAL A 1 55  ? 23.002  22.685  50.190 1.00 10.88  ? 97   VAL A CB    1 
ATOM   418  C CG1   . VAL A 1 55  ? 22.472  21.284  50.411 1.00 13.22  ? 97   VAL A CG1   1 
ATOM   419  C CG2   . VAL A 1 55  ? 22.242  23.314  49.028 1.00 12.30  ? 97   VAL A CG2   1 
ATOM   420  N N     . GLN A 1 56  ? 24.776  22.725  52.751 1.00 12.74  ? 98   GLN A N     1 
ATOM   421  C CA    . GLN A 1 56  ? 25.417  22.027  53.856 1.00 11.03  ? 98   GLN A CA    1 
ATOM   422  C C     . GLN A 1 56  ? 24.999  22.614  55.204 1.00 11.67  ? 98   GLN A C     1 
ATOM   423  O O     . GLN A 1 56  ? 24.711  21.846  56.127 1.00 11.44  ? 98   GLN A O     1 
ATOM   424  C CB    . GLN A 1 56  ? 26.930  22.069  53.686 1.00 12.34  ? 98   GLN A CB    1 
ATOM   425  C CG    . GLN A 1 56  ? 27.435  21.219  52.531 1.00 12.39  ? 98   GLN A CG    1 
ATOM   426  C CD    . GLN A 1 56  ? 28.934  21.348  52.416 1.00 13.91  ? 98   GLN A CD    1 
ATOM   427  O OE1   . GLN A 1 56  ? 29.451  22.268  51.759 1.00 18.12  ? 98   GLN A OE1   1 
ATOM   428  N NE2   . GLN A 1 56  ? 29.652  20.433  53.046 1.00 13.17  ? 98   GLN A NE2   1 
ATOM   429  N N     . GLU A 1 57  ? 24.995  23.945  55.286 1.00 12.11  ? 99   GLU A N     1 
ATOM   430  C CA    . GLU A 1 57  ? 24.625  24.603  56.535 1.00 13.91  ? 99   GLU A CA    1 
ATOM   431  C C     . GLU A 1 57  ? 23.158  24.332  56.860 1.00 12.91  ? 99   GLU A C     1 
ATOM   432  O O     . GLU A 1 57  ? 22.780  24.091  57.994 1.00 12.89  ? 99   GLU A O     1 
ATOM   433  C CB    . GLU A 1 57  ? 24.943  26.109  56.490 1.00 18.00  ? 99   GLU A CB    1 
ATOM   434  C CG    . GLU A 1 57  ? 24.794  26.771  57.851 1.00 24.85  ? 99   GLU A CG    1 
ATOM   435  C CD    . GLU A 1 57  ? 25.574  26.090  58.975 1.00 33.96  ? 99   GLU A CD    1 
ATOM   436  O OE1   . GLU A 1 57  ? 24.948  25.867  60.042 1.00 47.01  ? 99   GLU A OE1   1 
ATOM   437  O OE2   . GLU A 1 57  ? 26.784  25.706  58.762 1.00 29.55  ? 99   GLU A OE2   1 
ATOM   438  N N     . ILE A 1 58  ? 22.290  24.414  55.857 1.00 10.40  ? 100  ILE A N     1 
ATOM   439  C CA    . ILE A 1 58  ? 20.904  24.102  56.011 1.00 10.24  ? 100  ILE A CA    1 
ATOM   440  C C     . ILE A 1 58  ? 20.716  22.677  56.582 1.00 11.21  ? 100  ILE A C     1 
ATOM   441  O O     . ILE A 1 58  ? 19.902  22.462  57.486 1.00 11.02  ? 100  ILE A O     1 
ATOM   442  C CB    . ILE A 1 58  ? 20.160  24.326  54.675 1.00 10.59  ? 100  ILE A CB    1 
ATOM   443  C CG1   . ILE A 1 58  ? 20.015  25.828  54.350 1.00 10.52  ? 100  ILE A CG1   1 
ATOM   444  C CG2   . ILE A 1 58  ? 18.831  23.614  54.697 1.00 11.38  ? 100  ILE A CG2   1 
ATOM   445  C CD1   . ILE A 1 58  ? 19.706  26.174  52.886 1.00 11.68  ? 100  ILE A CD1   1 
ATOM   446  N N     . VAL A 1 59  ? 21.442  21.705  56.062 1.00 10.69  ? 101  VAL A N     1 
ATOM   447  C CA    . VAL A 1 59  ? 21.329  20.332  56.528 1.00 11.04  ? 101  VAL A CA    1 
ATOM   448  C C     . VAL A 1 59  ? 21.767  20.234  57.986 1.00 11.63  ? 101  VAL A C     1 
ATOM   449  O O     . VAL A 1 59  ? 21.161  19.472  58.742 1.00 11.38  ? 101  VAL A O     1 
ATOM   450  C CB    . VAL A 1 59  ? 22.088  19.389  55.553 1.00 9.97   ? 101  VAL A CB    1 
ATOM   451  C CG1   . VAL A 1 59  ? 22.246  17.983  56.088 1.00 13.60  ? 101  VAL A CG1   1 
ATOM   452  C CG2   . VAL A 1 59  ? 21.289  19.296  54.257 1.00 12.37  ? 101  VAL A CG2   1 
ATOM   453  N N     . ARG A 1 60  ? 22.826  20.949  58.366 1.00 11.53  ? 102  ARG A N     1 
ATOM   454  C CA    . ARG A 1 60  ? 23.322  20.878  59.726 1.00 11.57  ? 102  ARG A CA    1 
ATOM   455  C C     . ARG A 1 60  ? 22.227  21.409  60.655 1.00 12.71  ? 102  ARG A C     1 
ATOM   456  O O     . ARG A 1 60  ? 21.926  20.803  61.678 1.00 12.28  ? 102  ARG A O     1 
ATOM   457  C CB    . ARG A 1 60  ? 24.586  21.719  59.909 1.00 13.38  ? 102  ARG A CB    1 
ATOM   458  C CG    . ARG A 1 60  ? 25.841  21.098  59.309 1.00 16.63  ? 102  ARG A CG    1 
ATOM   459  C CD    . ARG A 1 60  ? 27.051  22.017  59.516 1.00 21.87  ? 102  ARG A CD    1 
ATOM   460  N NE    . ARG A 1 60  ? 28.081  21.639  58.562 1.00 28.14  ? 102  ARG A NE    1 
ATOM   461  C CZ    . ARG A 1 60  ? 28.482  22.317  57.492 1.00 24.41  ? 102  ARG A CZ    1 
ATOM   462  N NH1   . ARG A 1 60  ? 28.112  23.569  57.253 1.00 22.48  ? 102  ARG A NH1   1 
ATOM   463  N NH2   . ARG A 1 60  ? 29.325  21.721  56.683 1.00 27.89  ? 102  ARG A NH2   1 
ATOM   464  N N     . ILE A 1 61  ? 21.619  22.542  60.277 1.00 12.04  ? 103  ILE A N     1 
ATOM   465  C CA    . ILE A 1 61  ? 20.537  23.134  61.058 1.00 11.69  ? 103  ILE A CA    1 
ATOM   466  C C     . ILE A 1 61  ? 19.341  22.162  61.151 1.00 12.66  ? 103  ILE A C     1 
ATOM   467  O O     . ILE A 1 61  ? 18.689  22.010  62.204 1.00 12.67  ? 103  ILE A O     1 
ATOM   468  C CB    . ILE A 1 61  ? 20.106  24.487  60.438 1.00 12.99  ? 103  ILE A CB    1 
ATOM   469  C CG1   . ILE A 1 61  ? 21.201  25.527  60.618 1.00 13.63  ? 103  ILE A CG1   1 
ATOM   470  C CG2   . ILE A 1 61  ? 18.767  24.942  60.993 1.00 11.56  ? 103  ILE A CG2   1 
ATOM   471  C CD1   . ILE A 1 61  ? 21.110  26.619  59.571 1.00 14.56  ? 103  ILE A CD1   1 
ATOM   472  N N     . ALA A 1 62  ? 18.980  21.511  60.036 1.00 11.33  ? 104  ALA A N     1 
ATOM   473  C CA    . ALA A 1 62  ? 17.896  20.544  60.016 1.00 11.54  ? 104  ALA A CA    1 
ATOM   474  C C     . ALA A 1 62  ? 18.105  19.456  61.047 1.00 11.80  ? 104  ALA A C     1 
ATOM   475  O O     . ALA A 1 62  ? 17.159  19.049  61.778 1.00 12.47  ? 104  ALA A O     1 
ATOM   476  C CB    . ALA A 1 62  ? 17.690  19.982  58.608 1.00 12.98  ? 104  ALA A CB    1 
ATOM   477  N N     . ASN A 1 63  ? 19.345  19.020  61.170 1.00 12.01  ? 105  ASN A N     1 
ATOM   478  C CA    . ASN A 1 63  ? 19.673  17.994  62.162 1.00 12.69  ? 105  ASN A CA    1 
ATOM   479  C C     . ASN A 1 63  ? 19.498  18.537  63.585 1.00 12.36  ? 105  ASN A C     1 
ATOM   480  O O     . ASN A 1 63  ? 18.849  17.909  64.437 1.00 14.33  ? 105  ASN A O     1 
ATOM   481  C CB    . ASN A 1 63  ? 21.077  17.452  61.957 1.00 13.64  ? 105  ASN A CB    1 
ATOM   482  C CG    . ASN A 1 63  ? 21.130  16.407  60.850 1.00 15.22  ? 105  ASN A CG    1 
ATOM   483  O OD1   . ASN A 1 63  ? 20.709  15.263  61.029 1.00 13.47  ? 105  ASN A OD1   1 
ATOM   484  N ND2   . ASN A 1 63  ? 21.630  16.815  59.696 1.00 13.71  ? 105  ASN A ND2   1 
ATOM   485  N N     . THR A 1 64  ? 20.056  19.717  63.856 1.00 12.71  ? 106  THR A N     1 
ATOM   486  C CA    . THR A 1 64  ? 20.031  20.262  65.218 1.00 12.64  ? 106  THR A CA    1 
ATOM   487  C C     . THR A 1 64  ? 18.592  20.468  65.673 1.00 12.93  ? 106  THR A C     1 
ATOM   488  O O     . THR A 1 64  ? 18.290  20.218  66.840 1.00 16.13  ? 106  THR A O     1 
ATOM   489  C CB    . THR A 1 64  ? 20.838  21.556  65.298 1.00 13.49  ? 106  THR A CB    1 
ATOM   490  O OG1   . THR A 1 64  ? 22.185  21.234  64.918 1.00 14.78  ? 106  THR A OG1   1 
ATOM   491  C CG2   . THR A 1 64  ? 20.828  22.178  66.690 1.00 13.63  ? 106  THR A CG2   1 
ATOM   492  N N     . TYR A 1 65  ? 17.729  20.967  64.781 1.00 12.74  ? 107  TYR A N     1 
ATOM   493  C CA    . TYR A 1 65  ? 16.372  21.385  65.113 1.00 13.41  ? 107  TYR A CA    1 
ATOM   494  C C     . TYR A 1 65  ? 15.360  20.265  64.788 1.00 14.03  ? 107  TYR A C     1 
ATOM   495  O O     . TYR A 1 65  ? 14.145  20.454  64.957 1.00 15.71  ? 107  TYR A O     1 
ATOM   496  C CB    . TYR A 1 65  ? 16.080  22.716  64.419 1.00 13.93  ? 107  TYR A CB    1 
ATOM   497  C CG    . TYR A 1 65  ? 16.824  23.896  65.025 1.00 16.33  ? 107  TYR A CG    1 
ATOM   498  C CD1   . TYR A 1 65  ? 16.350  24.541  66.159 1.00 22.08  ? 107  TYR A CD1   1 
ATOM   499  C CD2   . TYR A 1 65  ? 18.053  24.297  64.546 1.00 17.46  ? 107  TYR A CD2   1 
ATOM   500  C CE1   . TYR A 1 65  ? 17.034  25.600  66.739 1.00 22.82  ? 107  TYR A CE1   1 
ATOM   501  C CE2   . TYR A 1 65  ? 18.753  25.352  65.109 1.00 20.79  ? 107  TYR A CE2   1 
ATOM   502  C CZ    . TYR A 1 65  ? 18.225  26.021  66.196 1.00 23.00  ? 107  TYR A CZ    1 
ATOM   503  O OH    . TYR A 1 65  ? 18.953  27.061  66.720 1.00 25.18  ? 107  TYR A OH    1 
ATOM   504  N N     . LYS A 1 66  ? 15.847  19.142  64.241 1.00 13.74  ? 108  LYS A N     1 
ATOM   505  C CA    . LYS A 1 66  ? 15.019  18.002  63.846 1.00 16.28  ? 108  LYS A CA    1 
ATOM   506  C C     . LYS A 1 66  ? 13.900  18.449  62.874 1.00 14.77  ? 108  LYS A C     1 
ATOM   507  O O     . LYS A 1 66  ? 12.762  17.975  62.971 1.00 17.04  ? 108  LYS A O     1 
ATOM   508  C CB    . LYS A 1 66  ? 14.515  17.260  65.099 1.00 19.52  ? 108  LYS A CB    1 
ATOM   509  C CG    . LYS A 1 66  ? 15.602  16.815  66.103 1.00 20.75  ? 108  LYS A CG    1 
ATOM   510  C CD    . LYS A 1 66  ? 16.718  15.871  65.488 1.00 22.67  ? 108  LYS A CD    1 
ATOM   511  C CE    . LYS A 1 66  ? 17.941  15.502  66.355 1.00 25.41  ? 108  LYS A CE    1 
ATOM   512  N NZ    . LYS A 1 66  ? 18.570  16.688  66.965 1.00 24.83  ? 108  LYS A NZ    1 
ATOM   513  N N     . GLN A 1 67  ? 14.221  19.313  61.888 1.00 12.47  ? 109  GLN A N     1 
ATOM   514  C CA    . GLN A 1 67  ? 13.257  19.859  60.963 1.00 11.27  ? 109  GLN A CA    1 
ATOM   515  C C     . GLN A 1 67  ? 13.464  19.227  59.589 1.00 11.58  ? 109  GLN A C     1 
ATOM   516  O O     . GLN A 1 67  ? 14.492  19.498  58.949 1.00 13.07  ? 109  GLN A O     1 
ATOM   517  C CB    . GLN A 1 67  ? 13.424  21.383  60.872 1.00 11.92  ? 109  GLN A CB    1 
ATOM   518  C CG    . GLN A 1 67  ? 12.594  22.005  59.776 1.00 12.87  ? 109  GLN A CG    1 
ATOM   519  C CD    . GLN A 1 67  ? 11.127  21.697  59.932 1.00 13.98  ? 109  GLN A CD    1 
ATOM   520  O OE1   . GLN A 1 67  ? 10.507  22.024  60.947 1.00 17.59  ? 109  GLN A OE1   1 
ATOM   521  N NE2   . GLN A 1 67  ? 10.527  20.979  58.989 1.00 14.20  ? 109  GLN A NE2   1 
ATOM   522  N N     . PRO A 1 68  ? 12.550  18.351  59.137 1.00 12.81  ? 110  PRO A N     1 
ATOM   523  C CA    . PRO A 1 68  ? 12.721  17.710  57.843 1.00 12.75  ? 110  PRO A CA    1 
ATOM   524  C C     . PRO A 1 68  ? 12.618  18.641  56.659 1.00 11.82  ? 110  PRO A C     1 
ATOM   525  O O     . PRO A 1 68  ? 11.902  19.656  56.707 1.00 12.99  ? 110  PRO A O     1 
ATOM   526  C CB    . PRO A 1 68  ? 11.629  16.639  57.767 1.00 13.04  ? 110  PRO A CB    1 
ATOM   527  C CG    . PRO A 1 68  ? 11.182  16.432  59.195 1.00 17.67  ? 110  PRO A CG    1 
ATOM   528  C CD    . PRO A 1 68  ? 11.415  17.771  59.878 1.00 13.61  ? 110  PRO A CD    1 
ATOM   529  N N     . LEU A 1 69  ? 13.382  18.268  55.611 1.00 10.76  ? 111  LEU A N     1 
ATOM   530  C CA    . LEU A 1 69  ? 13.481  18.989  54.339 1.00 10.88  ? 111  LEU A CA    1 
ATOM   531  C C     . LEU A 1 69  ? 12.973  18.120  53.190 1.00 11.26  ? 111  LEU A C     1 
ATOM   532  O O     . LEU A 1 69  ? 13.422  16.986  53.034 1.00 12.82  ? 111  LEU A O     1 
ATOM   533  C CB    . LEU A 1 69  ? 14.960  19.281  54.066 1.00 11.18  ? 111  LEU A CB    1 
ATOM   534  C CG    . LEU A 1 69  ? 15.658  20.119  55.130 1.00 12.07  ? 111  LEU A CG    1 
ATOM   535  C CD1   . LEU A 1 69  ? 17.157  20.134  54.962 1.00 13.83  ? 111  LEU A CD1   1 
ATOM   536  C CD2   . LEU A 1 69  ? 15.143  21.561  55.138 1.00 14.20  ? 111  LEU A CD2   1 
ATOM   537  N N     . TRP A 1 70  ? 12.127  18.674  52.324 1.00 10.95  ? 112  TRP A N     1 
ATOM   538  C CA    . TRP A 1 70  ? 11.694  17.956  51.121 1.00 10.27  ? 112  TRP A CA    1 
ATOM   539  C C     . TRP A 1 70  ? 12.397  18.604  49.946 1.00 11.47  ? 112  TRP A C     1 
ATOM   540  O O     . TRP A 1 70  ? 12.012  19.708  49.527 1.00 11.36  ? 112  TRP A O     1 
ATOM   541  C CB    . TRP A 1 70  ? 10.157  18.074  50.992 1.00 11.15  ? 112  TRP A CB    1 
ATOM   542  C CG    . TRP A 1 70  ? 9.542   17.320  49.857 1.00 9.84   ? 112  TRP A CG    1 
ATOM   543  C CD1   . TRP A 1 70  ? 9.296   17.781  48.597 1.00 11.46  ? 112  TRP A CD1   1 
ATOM   544  C CD2   . TRP A 1 70  ? 9.216   15.920  49.835 1.00 10.52  ? 112  TRP A CD2   1 
ATOM   545  N NE1   . TRP A 1 70  ? 8.805   16.783  47.797 1.00 11.94  ? 112  TRP A NE1   1 
ATOM   546  C CE2   . TRP A 1 70  ? 8.739   15.622  48.535 1.00 11.26  ? 112  TRP A CE2   1 
ATOM   547  C CE3   . TRP A 1 70  ? 9.238   14.884  50.772 1.00 10.99  ? 112  TRP A CE3   1 
ATOM   548  C CZ2   . TRP A 1 70  ? 8.327   14.339  48.159 1.00 11.65  ? 112  TRP A CZ2   1 
ATOM   549  C CZ3   . TRP A 1 70  ? 8.799   13.623  50.421 1.00 10.62  ? 112  TRP A CZ3   1 
ATOM   550  C CH2   . TRP A 1 70  ? 8.381   13.350  49.110 1.00 11.26  ? 112  TRP A CH2   1 
ATOM   551  N N     . THR A 1 71  ? 13.430  17.938  49.401 1.00 10.87  ? 113  THR A N     1 
ATOM   552  C CA    . THR A 1 71  ? 14.278  18.546  48.383 1.00 10.10  ? 113  THR A CA    1 
ATOM   553  C C     . THR A 1 71  ? 13.694  18.413  47.001 1.00 10.28  ? 113  THR A C     1 
ATOM   554  O O     . THR A 1 71  ? 13.282  17.305  46.610 1.00 11.09  ? 113  THR A O     1 
ATOM   555  C CB    . THR A 1 71  ? 15.688  17.934  48.440 1.00 12.28  ? 113  THR A CB    1 
ATOM   556  O OG1   . THR A 1 71  ? 16.200  18.090  49.772 1.00 11.96  ? 113  THR A OG1   1 
ATOM   557  C CG2   . THR A 1 71  ? 16.657  18.579  47.490 1.00 11.69  ? 113  THR A CG2   1 
ATOM   558  N N     . VAL A 1 72  ? 13.708  19.514  46.267 1.00 9.96   ? 114  VAL A N     1 
ATOM   559  C CA    . VAL A 1 72  ? 13.342  19.541  44.844 1.00 10.34  ? 114  VAL A CA    1 
ATOM   560  C C     . VAL A 1 72  ? 14.349  20.347  44.064 1.00 10.67  ? 114  VAL A C     1 
ATOM   561  O O     . VAL A 1 72  ? 15.074  21.161  44.634 1.00 11.48  ? 114  VAL A O     1 
ATOM   562  C CB    . VAL A 1 72  ? 11.921  20.099  44.690 1.00 10.37  ? 114  VAL A CB    1 
ATOM   563  C CG1   . VAL A 1 72  ? 10.931  19.354  45.586 1.00 10.72  ? 114  VAL A CG1   1 
ATOM   564  C CG2   . VAL A 1 72  ? 11.832  21.559  44.944 1.00 10.34  ? 114  VAL A CG2   1 
ATOM   565  N N     . SER A 1 73  ? 14.369  20.126  42.741 1.00 11.45  ? 115  SER A N     1 
ATOM   566  C CA    . SER A 1 73  ? 15.276  20.830  41.830 1.00 13.08  ? 115  SER A CA    1 
ATOM   567  C C     . SER A 1 73  ? 14.517  22.013  41.275 1.00 14.64  ? 115  SER A C     1 
ATOM   568  O O     . SER A 1 73  ? 14.843  23.123  41.663 1.00 19.92  ? 115  SER A O     1 
ATOM   569  C CB    . SER A 1 73  ? 15.811  19.949  40.749 1.00 12.61  ? 115  SER A CB    1 
ATOM   570  O OG    . SER A 1 73  ? 16.797  19.056  41.260 1.00 13.53  ? 115  SER A OG    1 
ATOM   571  N N     . THR A 1 74  ? 13.566  21.805  40.349 1.00 12.60  ? 116  THR A N     1 
ATOM   572  C CA    . THR A 1 74  ? 12.688  22.854  39.865 1.00 14.58  ? 116  THR A CA    1 
ATOM   573  C C     . THR A 1 74  ? 11.248  22.611  40.341 1.00 15.48  ? 116  THR A C     1 
ATOM   574  O O     . THR A 1 74  ? 10.399  23.494  40.186 1.00 15.83  ? 116  THR A O     1 
ATOM   575  C CB    . THR A 1 74  ? 12.759  23.041  38.350 1.00 15.06  ? 116  THR A CB    1 
ATOM   576  O OG1   . THR A 1 74  ? 12.768  21.829  37.618 1.00 13.77  ? 116  THR A OG1   1 
ATOM   577  C CG2   . THR A 1 74  ? 14.047  23.717  37.924 1.00 16.06  ? 116  THR A CG2   1 
ATOM   578  N N     . GLY A 1 75  ? 10.953  21.395  40.843 1.00 13.53  ? 117  GLY A N     1 
ATOM   579  C CA    . GLY A 1 75  ? 9.662   21.130  41.485 1.00 13.23  ? 117  GLY A CA    1 
ATOM   580  C C     . GLY A 1 75  ? 8.477   21.069  40.528 1.00 13.64  ? 117  GLY A C     1 
ATOM   581  O O     . GLY A 1 75  ? 7.356   21.381  40.939 1.00 17.49  ? 117  GLY A O     1 
ATOM   582  N N     . LYS A 1 76  ? 8.671   20.616  39.302 1.00 12.42  ? 118  LYS A N     1 
ATOM   583  C CA    . LYS A 1 76  ? 7.572   20.552  38.347 1.00 12.77  ? 118  LYS A CA    1 
ATOM   584  C C     . LYS A 1 76  ? 7.130   19.101  38.125 1.00 12.56  ? 118  LYS A C     1 
ATOM   585  O O     . LYS A 1 76  ? 6.747   18.729  37.023 1.00 12.86  ? 118  LYS A O     1 
ATOM   586  C CB    . LYS A 1 76  ? 7.995   21.218  37.039 1.00 14.93  ? 118  LYS A CB    1 
ATOM   587  C CG    . LYS A 1 76  ? 8.477   22.665  37.138 1.00 18.68  ? 118  LYS A CG    1 
ATOM   588  C CD    . LYS A 1 76  ? 7.576   23.549  37.946 1.00 22.42  ? 118  LYS A CD    1 
ATOM   589  C CE    . LYS A 1 76  ? 8.049   24.990  38.046 1.00 29.04  ? 118  LYS A CE    1 
ATOM   590  N NZ    . LYS A 1 76  ? 7.185   25.747  38.998 1.00 34.56  ? 118  LYS A NZ    1 
ATOM   591  N N     . ASN A 1 77  ? 7.029   18.344  39.229 1.00 11.94  ? 119  ASN A N     1 
ATOM   592  C CA    . ASN A 1 77  ? 6.595   16.951  39.230 1.00 11.91  ? 119  ASN A CA    1 
ATOM   593  C C     . ASN A 1 77  ? 5.067   16.905  39.136 1.00 11.21  ? 119  ASN A C     1 
ATOM   594  O O     . ASN A 1 77  ? 4.369   16.377  39.993 1.00 11.76  ? 119  ASN A O     1 
ATOM   595  C CB    . ASN A 1 77  ? 7.177   16.220  40.463 1.00 10.41  ? 119  ASN A CB    1 
ATOM   596  C CG    . ASN A 1 77  ? 7.657   14.828  40.128 1.00 13.03  ? 119  ASN A CG    1 
ATOM   597  O OD1   . ASN A 1 77  ? 7.780   14.475  38.946 1.00 12.65  ? 119  ASN A OD1   1 
ATOM   598  N ND2   . ASN A 1 77  ? 7.934   13.997  41.138 1.00 11.79  ? 119  ASN A ND2   1 
ATOM   599  N N     . MET A 1 78  ? 4.524   17.409  38.016 1.00 10.83  ? 120  MET A N     1 
ATOM   600  C CA    . MET A 1 78  ? 3.106   17.625  37.832 1.00 11.57  ? 120  MET A CA    1 
ATOM   601  C C     . MET A 1 78  ? 2.416   16.284  37.560 1.00 11.07  ? 120  MET A C     1 
ATOM   602  O O     . MET A 1 78  ? 2.839   15.551  36.686 1.00 11.54  ? 120  MET A O     1 
ATOM   603  C CB    . MET A 1 78  ? 2.870   18.600  36.675 1.00 13.89  ? 120  MET A CB    1 
ATOM   604  C CG    . MET A 1 78  ? 1.423   18.945  36.441 1.00 16.09  ? 120  MET A CG    1 
ATOM   605  S SD    . MET A 1 78  ? 1.225   20.213  35.111 1.00 19.73  ? 120  MET A SD    1 
ATOM   606  C CE    . MET A 1 78  ? 1.608   21.736  35.971 1.00 19.82  ? 120  MET A CE    1 
ATOM   607  N N     . GLY A 1 79  ? 1.397   16.005  38.378 1.00 10.29  ? 121  GLY A N     1 
ATOM   608  C CA    . GLY A 1 79  ? 0.713   14.727  38.412 1.00 10.89  ? 121  GLY A CA    1 
ATOM   609  C C     . GLY A 1 79  ? 1.345   13.741  39.386 1.00 10.43  ? 121  GLY A C     1 
ATOM   610  O O     . GLY A 1 79  ? 0.834   12.628  39.543 1.00 10.98  ? 121  GLY A O     1 
ATOM   611  N N     . TYR A 1 80  ? 2.455   14.161  40.018 1.00 11.42  ? 122  TYR A N     1 
ATOM   612  C CA    . TYR A 1 80  ? 3.158   13.337  40.996 1.00 10.36  ? 122  TYR A CA    1 
ATOM   613  C C     . TYR A 1 80  ? 3.367   14.083  42.324 1.00 11.74  ? 122  TYR A C     1 
ATOM   614  O O     . TYR A 1 80  ? 4.028   13.546  43.225 1.00 12.56  ? 122  TYR A O     1 
ATOM   615  C CB    . TYR A 1 80  ? 4.534   12.933  40.440 1.00 10.10  ? 122  TYR A CB    1 
ATOM   616  C CG    . TYR A 1 80  ? 4.559   11.869  39.371 1.00 9.49   ? 122  TYR A CG    1 
ATOM   617  C CD1   . TYR A 1 80  ? 3.920   10.661  39.514 1.00 8.91   ? 122  TYR A CD1   1 
ATOM   618  C CD2   . TYR A 1 80  ? 5.183   12.133  38.148 1.00 9.66   ? 122  TYR A CD2   1 
ATOM   619  C CE1   . TYR A 1 80  ? 3.984   9.712   38.488 1.00 9.04   ? 122  TYR A CE1   1 
ATOM   620  C CE2   . TYR A 1 80  ? 5.271   11.194  37.128 1.00 10.48  ? 122  TYR A CE2   1 
ATOM   621  C CZ    . TYR A 1 80  ? 4.661   9.965   37.309 1.00 9.35   ? 122  TYR A CZ    1 
ATOM   622  O OH    . TYR A 1 80  ? 4.694   8.982   36.323 1.00 11.10  ? 122  TYR A OH    1 
ATOM   623  N N     . GLY A 1 81  ? 2.763   15.264  42.469 1.00 10.92  ? 123  GLY A N     1 
ATOM   624  C CA    . GLY A 1 81  ? 2.798   15.996  43.731 1.00 10.72  ? 123  GLY A CA    1 
ATOM   625  C C     . GLY A 1 81  ? 3.401   17.392  43.697 1.00 11.12  ? 123  GLY A C     1 
ATOM   626  O O     . GLY A 1 81  ? 3.367   18.052  44.729 1.00 11.08  ? 123  GLY A O     1 
ATOM   627  N N     . MET A 1 82  ? 3.971   17.806  42.559 1.00 10.97  ? 124  MET A N     1 
ATOM   628  C CA    . MET A 1 82  ? 4.617   19.109  42.460 1.00 11.49  ? 124  MET A CA    1 
ATOM   629  C C     . MET A 1 82  ? 5.635   19.227  43.595 1.00 11.59  ? 124  MET A C     1 
ATOM   630  O O     . MET A 1 82  ? 6.530   18.378  43.696 1.00 11.99  ? 124  MET A O     1 
ATOM   631  C CB    . MET A 1 82  ? 3.587   20.245  42.432 1.00 12.49  ? 124  MET A CB    1 
ATOM   632  C CG    . MET A 1 82  ? 2.693   20.243  41.171 1.00 13.59  ? 124  MET A CG    1 
ATOM   633  S SD    . MET A 1 82  ? 3.544   20.498  39.632 1.00 14.22  ? 124  MET A SD    1 
ATOM   634  C CE    . MET A 1 82  ? 4.040   22.213  39.822 1.00 15.25  ? 124  MET A CE    1 
ATOM   635  N N     . THR A 1 83  ? 5.514   20.226  44.490 1.00 11.40  ? 125  THR A N     1 
ATOM   636  C CA    . THR A 1 83  ? 6.432   20.396  45.609 1.00 12.23  ? 125  THR A CA    1 
ATOM   637  C C     . THR A 1 83  ? 5.764   20.077  46.929 1.00 12.43  ? 125  THR A C     1 
ATOM   638  O O     . THR A 1 83  ? 6.301   20.468  47.972 1.00 13.21  ? 125  THR A O     1 
ATOM   639  C CB    . THR A 1 83  ? 7.093   21.796  45.657 1.00 12.85  ? 125  THR A CB    1 
ATOM   640  O OG1   . THR A 1 83  ? 6.090   22.819  45.695 1.00 14.69  ? 125  THR A OG1   1 
ATOM   641  C CG2   . THR A 1 83  ? 7.966   22.031  44.452 1.00 13.65  ? 125  THR A CG2   1 
ATOM   642  N N     . ALA A 1 84  ? 4.674   19.319  46.927 1.00 13.23  ? 126  ALA A N     1 
ATOM   643  C CA    . ALA A 1 84  ? 4.068   18.931  48.187 1.00 13.14  ? 126  ALA A CA    1 
ATOM   644  C C     . ALA A 1 84  ? 4.841   17.770  48.807 1.00 13.38  ? 126  ALA A C     1 
ATOM   645  O O     . ALA A 1 84  ? 5.064   16.781  48.118 1.00 13.19  ? 126  ALA A O     1 
ATOM   646  C CB    . ALA A 1 84  ? 2.646   18.534  47.972 1.00 14.13  ? 126  ALA A CB    1 
ATOM   647  N N     . PRO A 1 85  ? 5.216   17.830  50.108 1.00 12.31  ? 127  PRO A N     1 
ATOM   648  C CA    . PRO A 1 85  ? 5.863   16.676  50.749 1.00 11.98  ? 127  PRO A CA    1 
ATOM   649  C C     . PRO A 1 85  ? 4.920   15.509  51.029 1.00 12.29  ? 127  PRO A C     1 
ATOM   650  O O     . PRO A 1 85  ? 3.698   15.674  51.150 1.00 12.95  ? 127  PRO A O     1 
ATOM   651  C CB    . PRO A 1 85  ? 6.463   17.274  52.025 1.00 11.37  ? 127  PRO A CB    1 
ATOM   652  C CG    . PRO A 1 85  ? 6.499   18.757  51.774 1.00 12.68  ? 127  PRO A CG    1 
ATOM   653  C CD    . PRO A 1 85  ? 5.268   19.033  50.951 1.00 13.01  ? 127  PRO A CD    1 
ATOM   654  N N     . ALA A 1 86  ? 5.505   14.302  51.185 1.00 12.02  ? 128  ALA A N     1 
ATOM   655  C CA    . ALA A 1 86  ? 4.741   13.110  51.452 1.00 12.55  ? 128  ALA A CA    1 
ATOM   656  C C     . ALA A 1 86  ? 4.160   13.033  52.879 1.00 13.37  ? 128  ALA A C     1 
ATOM   657  O O     . ALA A 1 86  ? 3.155   12.317  53.069 1.00 13.91  ? 128  ALA A O     1 
ATOM   658  C CB    . ALA A 1 86  ? 5.593   11.880  51.109 1.00 13.69  ? 128  ALA A CB    1 
ATOM   659  N N     . THR A 1 87  ? 4.785   13.698  53.877 1.00 12.90  ? 129  THR A N     1 
ATOM   660  C CA    . THR A 1 87  ? 4.298   13.691  55.238 1.00 14.02  ? 129  THR A CA    1 
ATOM   661  C C     . THR A 1 87  ? 4.175   15.135  55.721 1.00 14.42  ? 129  THR A C     1 
ATOM   662  O O     . THR A 1 87  ? 4.828   16.033  55.209 1.00 13.49  ? 129  THR A O     1 
ATOM   663  C CB    . THR A 1 87  ? 5.183   12.871  56.199 1.00 14.46  ? 129  THR A CB    1 
ATOM   664  O OG1   . THR A 1 87  ? 6.412   13.564  56.465 1.00 14.53  ? 129  THR A OG1   1 
ATOM   665  C CG2   . THR A 1 87  ? 5.306   11.440  55.694 1.00 14.28  ? 129  THR A CG2   1 
ATOM   666  N N     . PRO A 1 88  ? 3.394   15.401  56.790 1.00 15.94  ? 130  PRO A N     1 
ATOM   667  C CA    . PRO A 1 88  ? 3.206   16.770  57.267 1.00 15.17  ? 130  PRO A CA    1 
ATOM   668  C C     . PRO A 1 88  ? 4.435   17.350  57.924 1.00 12.66  ? 130  PRO A C     1 
ATOM   669  O O     . PRO A 1 88  ? 5.309   16.638  58.462 1.00 15.63  ? 130  PRO A O     1 
ATOM   670  C CB    . PRO A 1 88  ? 2.082   16.645  58.330 1.00 17.21  ? 130  PRO A CB    1 
ATOM   671  C CG    . PRO A 1 88  ? 1.407   15.326  57.999 1.00 17.47  ? 130  PRO A CG    1 
ATOM   672  C CD    . PRO A 1 88  ? 2.503   14.433  57.459 1.00 17.60  ? 130  PRO A CD    1 
ATOM   673  N N     . GLY A 1 89  ? 4.507   18.664  57.897 1.00 13.29  ? 131  GLY A N     1 
ATOM   674  C CA    . GLY A 1 89  ? 5.475   19.358  58.718 1.00 14.00  ? 131  GLY A CA    1 
ATOM   675  C C     . GLY A 1 89  ? 6.857   19.592  58.093 1.00 13.44  ? 131  GLY A C     1 
ATOM   676  O O     . GLY A 1 89  ? 7.800   19.992  58.795 1.00 13.91  ? 131  GLY A O     1 
ATOM   677  N N     . GLN A 1 90  ? 6.973   19.370  56.784 1.00 12.28  ? 132  GLN A N     1 
ATOM   678  C CA    . GLN A 1 90  ? 8.252   19.506  56.103 1.00 11.77  ? 132  GLN A CA    1 
ATOM   679  C C     . GLN A 1 90  ? 8.417   20.890  55.447 1.00 11.90  ? 132  GLN A C     1 
ATOM   680  O O     . GLN A 1 90  ? 7.459   21.486  54.956 1.00 11.52  ? 132  GLN A O     1 
ATOM   681  C CB    . GLN A 1 90  ? 8.416   18.423  55.034 1.00 11.25  ? 132  GLN A CB    1 
ATOM   682  C CG    . GLN A 1 90  ? 8.230   16.997  55.556 1.00 12.15  ? 132  GLN A CG    1 
ATOM   683  C CD    . GLN A 1 90  ? 8.660   15.882  54.638 1.00 13.60  ? 132  GLN A CD    1 
ATOM   684  O OE1   . GLN A 1 90  ? 8.024   14.820  54.542 1.00 16.22  ? 132  GLN A OE1   1 
ATOM   685  N NE2   . GLN A 1 90  ? 9.718   16.150  53.901 1.00 10.71  ? 132  GLN A NE2   1 
ATOM   686  N N     . VAL A 1 91  ? 9.687   21.287  55.340 1.00 11.28  ? 133  VAL A N     1 
ATOM   687  C CA    . VAL A 1 91  ? 10.112  22.499  54.648 1.00 12.12  ? 133  VAL A CA    1 
ATOM   688  C C     . VAL A 1 91  ? 10.676  22.089  53.300 1.00 12.53  ? 133  VAL A C     1 
ATOM   689  O O     . VAL A 1 91  ? 11.575  21.247  53.257 1.00 12.92  ? 133  VAL A O     1 
ATOM   690  C CB    . VAL A 1 91  ? 11.142  23.264  55.494 1.00 11.74  ? 133  VAL A CB    1 
ATOM   691  C CG1   . VAL A 1 91  ? 11.829  24.420  54.750 1.00 12.18  ? 133  VAL A CG1   1 
ATOM   692  C CG2   . VAL A 1 91  ? 10.476  23.798  56.765 1.00 12.80  ? 133  VAL A CG2   1 
ATOM   693  N N     . VAL A 1 92  ? 10.212  22.734  52.232 1.00 12.48  ? 134  VAL A N     1 
ATOM   694  C CA    . VAL A 1 92  ? 10.748  22.439  50.912 1.00 12.10  ? 134  VAL A CA    1 
ATOM   695  C C     . VAL A 1 92  ? 12.136  23.067  50.815 1.00 12.71  ? 134  VAL A C     1 
ATOM   696  O O     . VAL A 1 92  ? 12.315  24.238  51.119 1.00 12.19  ? 134  VAL A O     1 
ATOM   697  C CB    . VAL A 1 92  ? 9.856   22.961  49.782 1.00 11.64  ? 134  VAL A CB    1 
ATOM   698  C CG1   . VAL A 1 92  ? 10.457  22.730  48.405 1.00 12.30  ? 134  VAL A CG1   1 
ATOM   699  C CG2   . VAL A 1 92  ? 8.458   22.409  49.869 1.00 12.21  ? 134  VAL A CG2   1 
ATOM   700  N N     . LEU A 1 93  ? 13.133  22.261  50.438 1.00 12.75  ? 135  LEU A N     1 
ATOM   701  C CA    . LEU A 1 93  ? 14.470  22.735  50.073 1.00 11.56  ? 135  LEU A CA    1 
ATOM   702  C C     . LEU A 1 93  ? 14.499  22.855  48.549 1.00 12.09  ? 135  LEU A C     1 
ATOM   703  O O     . LEU A 1 93  ? 14.560  21.853  47.813 1.00 11.23  ? 135  LEU A O     1 
ATOM   704  C CB    . LEU A 1 93  ? 15.522  21.748  50.588 1.00 11.77  ? 135  LEU A CB    1 
ATOM   705  C CG    . LEU A 1 93  ? 16.968  22.068  50.216 1.00 12.76  ? 135  LEU A CG    1 
ATOM   706  C CD1   . LEU A 1 93  ? 17.374  23.456  50.681 1.00 13.60  ? 135  LEU A CD1   1 
ATOM   707  C CD2   . LEU A 1 93  ? 17.911  21.010  50.723 1.00 13.22  ? 135  LEU A CD2   1 
ATOM   708  N N     . ASP A 1 94  ? 14.267  24.086  48.061 1.00 11.38  ? 136  ASP A N     1 
ATOM   709  C CA    . ASP A 1 94  ? 14.043  24.346  46.683 1.00 12.46  ? 136  ASP A CA    1 
ATOM   710  C C     . ASP A 1 94  ? 15.371  24.825  46.084 1.00 12.13  ? 136  ASP A C     1 
ATOM   711  O O     . ASP A 1 94  ? 15.885  25.897  46.453 1.00 12.58  ? 136  ASP A O     1 
ATOM   712  C CB    . ASP A 1 94  ? 13.010  25.461  46.549 1.00 13.22  ? 136  ASP A CB    1 
ATOM   713  C CG    . ASP A 1 94  ? 12.580  25.798  45.148 1.00 17.24  ? 136  ASP A CG    1 
ATOM   714  O OD1   . ASP A 1 94  ? 13.316  25.445  44.187 1.00 17.58  ? 136  ASP A OD1   1 
ATOM   715  O OD2   . ASP A 1 94  ? 11.425  26.388  45.025 1.00 18.43  ? 136  ASP A OD2   1 
ATOM   716  N N     . LEU A 1 95  ? 15.966  24.000  45.209 1.00 11.62  ? 137  LEU A N     1 
ATOM   717  C CA    . LEU A 1 95  ? 17.317  24.272  44.697 1.00 11.32  ? 137  LEU A CA    1 
ATOM   718  C C     . LEU A 1 95  ? 17.320  25.040  43.374 1.00 11.65  ? 137  LEU A C     1 
ATOM   719  O O     . LEU A 1 95  ? 18.340  25.054  42.693 1.00 12.01  ? 137  LEU A O     1 
ATOM   720  C CB    . LEU A 1 95  ? 18.055  22.923  44.608 1.00 10.82  ? 137  LEU A CB    1 
ATOM   721  C CG    . LEU A 1 95  ? 18.222  22.183  45.908 1.00 11.32  ? 137  LEU A CG    1 
ATOM   722  C CD1   . LEU A 1 95  ? 19.036  20.912  45.682 1.00 12.11  ? 137  LEU A CD1   1 
ATOM   723  C CD2   . LEU A 1 95  ? 18.921  23.050  46.950 1.00 11.28  ? 137  LEU A CD2   1 
ATOM   724  N N     . LYS A 1 96  ? 16.223  25.719  43.020 1.00 11.45  ? 138  LYS A N     1 
ATOM   725  C CA    . LYS A 1 96  ? 16.116  26.382  41.719 1.00 13.13  ? 138  LYS A CA    1 
ATOM   726  C C     . LYS A 1 96  ? 17.195  27.443  41.483 1.00 12.03  ? 138  LYS A C     1 
ATOM   727  O O     . LYS A 1 96  ? 17.493  27.700  40.315 1.00 12.60  ? 138  LYS A O     1 
ATOM   728  C CB    . LYS A 1 96  ? 14.753  27.053  41.517 1.00 13.55  ? 138  LYS A CB    1 
ATOM   729  C CG    . LYS A 1 96  ? 14.386  28.166  42.489 1.00 15.32  ? 138  LYS A CG    1 
ATOM   730  C CD    . LYS A 1 96  ? 13.004  28.729  42.215 1.00 19.01  ? 138  LYS A CD    1 
ATOM   731  C CE    . LYS A 1 96  ? 12.655  29.782  43.237 1.00 24.49  ? 138  LYS A CE    1 
ATOM   732  N NZ    . LYS A 1 96  ? 11.327  30.372  43.009 1.00 26.46  ? 138  LYS A NZ    1 
ATOM   733  N N     . ARG A 1 97  ? 17.701  28.100  42.526 1.00 10.73  ? 139  ARG A N     1 
ATOM   734  C CA    . ARG A 1 97  ? 18.744  29.127  42.366 1.00 11.38  ? 139  ARG A CA    1 
ATOM   735  C C     . ARG A 1 97  ? 20.123  28.537  42.093 1.00 11.98  ? 139  ARG A C     1 
ATOM   736  O O     . ARG A 1 97  ? 21.031  29.252  41.646 1.00 12.42  ? 139  ARG A O     1 
ATOM   737  C CB    . ARG A 1 97  ? 18.809  30.068  43.567 1.00 12.88  ? 139  ARG A CB    1 
ATOM   738  C CG    . ARG A 1 97  ? 17.504  30.812  43.820 1.00 14.35  ? 139  ARG A CG    1 
ATOM   739  C CD    . ARG A 1 97  ? 17.570  31.582  45.121 1.00 14.88  ? 139  ARG A CD    1 
ATOM   740  N NE    . ARG A 1 97  ? 18.546  32.650  45.077 1.00 15.39  ? 139  ARG A NE    1 
ATOM   741  C CZ    . ARG A 1 97  ? 19.353  33.016  46.071 1.00 14.61  ? 139  ARG A CZ    1 
ATOM   742  N NH1   . ARG A 1 97  ? 19.351  32.412  47.234 1.00 13.87  ? 139  ARG A NH1   1 
ATOM   743  N NH2   . ARG A 1 97  ? 20.173  34.053  45.899 1.00 17.06  ? 139  ARG A NH2   1 
ATOM   744  N N     . MET A 1 98  ? 20.282  27.221  42.316 1.00 11.53  ? 140  MET A N     1 
ATOM   745  C CA    . MET A 1 98  ? 21.535  26.548  42.031 1.00 12.60  ? 140  MET A CA    1 
ATOM   746  C C     . MET A 1 98  ? 21.460  26.092  40.582 1.00 11.62  ? 140  MET A C     1 
ATOM   747  O O     . MET A 1 98  ? 21.221  24.922  40.287 1.00 11.90  ? 140  MET A O     1 
ATOM   748  C CB    . MET A 1 98  ? 21.751  25.366  42.988 1.00 12.78  ? 140  MET A CB    1 
ATOM   749  C CG    . MET A 1 98  ? 22.152  25.807  44.384 1.00 14.30  ? 140  MET A CG    1 
ATOM   750  S SD    . MET A 1 98  ? 22.341  24.468  45.574 1.00 17.03  ? 140  MET A SD    1 
ATOM   751  C CE    . MET A 1 98  ? 23.767  23.629  44.908 1.00 12.68  ? 140  MET A CE    1 
ATOM   752  N N     . ASN A 1 99  ? 21.645  27.016  39.660 1.00 11.37  ? 141  ASN A N     1 
ATOM   753  C CA    . ASN A 1 99  ? 21.292  26.784  38.268 1.00 12.66  ? 141  ASN A CA    1 
ATOM   754  C C     . ASN A 1 99  ? 22.489  26.900  37.339 1.00 11.86  ? 141  ASN A C     1 
ATOM   755  O O     . ASN A 1 99  ? 22.359  27.363  36.202 1.00 11.58  ? 141  ASN A O     1 
ATOM   756  C CB    . ASN A 1 99  ? 20.202  27.705  37.765 1.00 13.43  ? 141  ASN A CB    1 
ATOM   757  C CG    . ASN A 1 99  ? 20.619  29.161  37.795 1.00 14.83  ? 141  ASN A CG    1 
ATOM   758  O OD1   . ASN A 1 99  ? 21.631  29.537  38.372 1.00 13.67  ? 141  ASN A OD1   1 
ATOM   759  N ND2   . ASN A 1 99  ? 19.823  29.962  37.135 1.00 19.15  ? 141  ASN A ND2   1 
ATOM   760  N N     . ARG A 1 100 ? 23.658  26.537  37.817 1.00 10.45  ? 142  ARG A N     1 
ATOM   761  C CA    . ARG A 1 100 ? 24.866  26.693  37.011 1.00 11.34  ? 142  ARG A CA    1 
ATOM   762  C C     . ARG A 1 100 ? 25.153  25.451  36.161 1.00 10.59  ? 142  ARG A C     1 
ATOM   763  O O     . ARG A 1 100 ? 25.142  24.310  36.634 1.00 10.57  ? 142  ARG A O     1 
ATOM   764  C CB    . ARG A 1 100 ? 26.053  26.961  37.935 1.00 11.97  ? 142  ARG A CB    1 
ATOM   765  C CG    . ARG A 1 100 ? 25.885  28.184  38.819 1.00 11.89  ? 142  ARG A CG    1 
ATOM   766  C CD    . ARG A 1 100 ? 26.922  28.235  39.922 1.00 12.71  ? 142  ARG A CD    1 
ATOM   767  N NE    . ARG A 1 100 ? 26.703  29.324  40.848 1.00 12.66  ? 142  ARG A NE    1 
ATOM   768  C CZ    . ARG A 1 100 ? 25.937  29.270  41.925 1.00 13.98  ? 142  ARG A CZ    1 
ATOM   769  N NH1   . ARG A 1 100 ? 25.310  28.151  42.240 1.00 13.49  ? 142  ARG A NH1   1 
ATOM   770  N NH2   . ARG A 1 100 ? 25.833  30.338  42.710 1.00 14.84  ? 142  ARG A NH2   1 
ATOM   771  N N     . ILE A 1 101 ? 25.448  25.696  34.882 1.00 9.85   ? 143  ILE A N     1 
ATOM   772  C CA    . ILE A 1 101 ? 26.035  24.693  34.007 1.00 10.95  ? 143  ILE A CA    1 
ATOM   773  C C     . ILE A 1 101 ? 27.530  24.716  34.278 1.00 12.36  ? 143  ILE A C     1 
ATOM   774  O O     . ILE A 1 101 ? 28.199  25.745  34.018 1.00 12.02  ? 143  ILE A O     1 
ATOM   775  C CB    . ILE A 1 101 ? 25.702  24.973  32.535 1.00 11.49  ? 143  ILE A CB    1 
ATOM   776  C CG1   . ILE A 1 101 ? 24.196  24.914  32.315 1.00 13.39  ? 143  ILE A CG1   1 
ATOM   777  C CG2   . ILE A 1 101 ? 26.464  24.050  31.607 1.00 11.23  ? 143  ILE A CG2   1 
ATOM   778  C CD1   . ILE A 1 101 ? 23.695  25.446  30.945 1.00 14.28  ? 143  ILE A CD1   1 
ATOM   779  N N     . LEU A 1 102 ? 28.007  23.638  34.891 1.00 11.21  ? 144  LEU A N     1 
ATOM   780  C CA    . LEU A 1 102 ? 29.393  23.605  35.327 1.00 12.45  ? 144  LEU A CA    1 
ATOM   781  C C     . LEU A 1 102 ? 30.358  23.255  34.207 1.00 14.45  ? 144  LEU A C     1 
ATOM   782  O O     . LEU A 1 102 ? 31.424  23.855  34.138 1.00 13.72  ? 144  LEU A O     1 
ATOM   783  C CB    . LEU A 1 102 ? 29.500  22.675  36.536 1.00 12.64  ? 144  LEU A CB    1 
ATOM   784  C CG    . LEU A 1 102 ? 28.696  23.143  37.743 1.00 12.40  ? 144  LEU A CG    1 
ATOM   785  C CD1   . LEU A 1 102 ? 28.765  22.105  38.834 1.00 12.97  ? 144  LEU A CD1   1 
ATOM   786  C CD2   . LEU A 1 102 ? 29.134  24.546  38.263 1.00 12.41  ? 144  LEU A CD2   1 
ATOM   787  N N     . GLU A 1 103 ? 30.049  22.222  33.406 1.00 13.03  ? 145  GLU A N     1 
ATOM   788  C CA    . GLU A 1 103 ? 30.921  21.824  32.324 1.00 13.64  ? 145  GLU A CA    1 
ATOM   789  C C     . GLU A 1 103 ? 30.041  21.289  31.212 1.00 13.81  ? 145  GLU A C     1 
ATOM   790  O O     . GLU A 1 103 ? 28.995  20.679  31.464 1.00 13.50  ? 145  GLU A O     1 
ATOM   791  C CB    . GLU A 1 103 ? 31.896  20.702  32.705 1.00 13.02  ? 145  GLU A CB    1 
ATOM   792  C CG    . GLU A 1 103 ? 32.698  20.946  33.956 1.00 15.32  ? 145  GLU A CG    1 
ATOM   793  C CD    . GLU A 1 103 ? 33.751  22.033  33.856 1.00 17.28  ? 145  GLU A CD    1 
ATOM   794  O OE1   . GLU A 1 103 ? 34.064  22.446  32.729 1.00 19.27  ? 145  GLU A OE1   1 
ATOM   795  O OE2   . GLU A 1 103 ? 34.242  22.472  34.945 1.00 20.28  ? 145  GLU A OE2   1 
ATOM   796  N N     . VAL A 1 104 ? 30.509  21.490  29.959 1.00 13.05  ? 146  VAL A N     1 
ATOM   797  C CA    . VAL A 1 104 ? 30.013  20.750  28.808 1.00 12.20  ? 146  VAL A CA    1 
ATOM   798  C C     . VAL A 1 104 ? 31.240  20.335  27.993 1.00 13.11  ? 146  VAL A C     1 
ATOM   799  O O     . VAL A 1 104 ? 32.054  21.173  27.610 1.00 15.08  ? 146  VAL A O     1 
ATOM   800  C CB    . VAL A 1 104 ? 29.033  21.554  27.938 1.00 12.71  ? 146  VAL A CB    1 
ATOM   801  C CG1   . VAL A 1 104 ? 28.660  20.771  26.676 1.00 14.15  ? 146  VAL A CG1   1 
ATOM   802  C CG2   . VAL A 1 104 ? 27.797  21.989  28.682 1.00 12.36  ? 146  VAL A CG2   1 
ATOM   803  N N     . ASP A 1 105 ? 31.388  19.035  27.776 1.00 13.70  ? 147  ASP A N     1 
ATOM   804  C CA    . ASP A 1 105 ? 32.523  18.460  27.084 1.00 14.72  ? 147  ASP A CA    1 
ATOM   805  C C     . ASP A 1 105 ? 32.037  18.061  25.710 1.00 14.56  ? 147  ASP A C     1 
ATOM   806  O O     . ASP A 1 105 ? 31.389  17.017  25.568 1.00 13.89  ? 147  ASP A O     1 
ATOM   807  C CB    . ASP A 1 105 ? 33.122  17.320  27.917 1.00 16.80  ? 147  ASP A CB    1 
ATOM   808  C CG    . ASP A 1 105 ? 34.324  16.568  27.349 1.00 21.78  ? 147  ASP A CG    1 
ATOM   809  O OD1   . ASP A 1 105 ? 34.599  16.696  26.119 1.00 20.66  ? 147  ASP A OD1   1 
ATOM   810  O OD2   . ASP A 1 105 ? 34.946  15.767  28.137 1.00 21.99  ? 147  ASP A OD2   1 
ATOM   811  N N     . ALA A 1 106 ? 32.419  18.865  24.677 1.00 14.73  ? 148  ALA A N     1 
ATOM   812  C CA    . ALA A 1 106 ? 31.910  18.625  23.346 1.00 16.69  ? 148  ALA A CA    1 
ATOM   813  C C     . ALA A 1 106 ? 32.409  17.302  22.762 1.00 16.68  ? 148  ALA A C     1 
ATOM   814  O O     . ALA A 1 106 ? 31.663  16.582  22.083 1.00 19.56  ? 148  ALA A O     1 
ATOM   815  C CB    . ALA A 1 106 ? 32.264  19.800  22.429 1.00 18.49  ? 148  ALA A CB    1 
ATOM   816  N N     . ASP A 1 107 ? 33.685  16.996  22.998 1.00 17.44  ? 149  ASP A N     1 
ATOM   817  C CA    . ASP A 1 107 ? 34.297  15.817  22.404 1.00 18.61  ? 149  ASP A CA    1 
ATOM   818  C C     . ASP A 1 107 ? 33.746  14.524  22.979 1.00 16.67  ? 149  ASP A C     1 
ATOM   819  O O     . ASP A 1 107 ? 33.468  13.602  22.229 1.00 17.12  ? 149  ASP A O     1 
ATOM   820  C CB    . ASP A 1 107 ? 35.798  15.797  22.693 1.00 22.39  ? 149  ASP A CB    1 
ATOM   821  C CG    . ASP A 1 107 ? 36.593  16.758  21.819 1.00 30.02  ? 149  ASP A CG    1 
ATOM   822  O OD1   . ASP A 1 107 ? 35.969  17.394  20.933 1.00 28.82  ? 149  ASP A OD1   1 
ATOM   823  O OD2   . ASP A 1 107 ? 37.833  16.809  22.020 1.00 30.34  ? 149  ASP A OD2   1 
ATOM   824  N N     . LEU A 1 108 ? 33.620  14.455  24.320 1.00 16.32  ? 150  LEU A N     1 
ATOM   825  C CA    . LEU A 1 108 ? 33.155  13.235  24.945 1.00 15.56  ? 150  LEU A CA    1 
ATOM   826  C C     . LEU A 1 108 ? 31.643  13.191  25.025 1.00 12.12  ? 150  LEU A C     1 
ATOM   827  O O     . LEU A 1 108 ? 31.088  12.141  25.343 1.00 13.76  ? 150  LEU A O     1 
ATOM   828  C CB    . LEU A 1 108 ? 33.732  13.085  26.365 1.00 17.18  ? 150  LEU A CB    1 
ATOM   829  C CG    . LEU A 1 108 ? 35.137  12.507  26.461 1.00 24.85  ? 150  LEU A CG    1 
ATOM   830  C CD1   . LEU A 1 108 ? 35.467  12.190  27.906 1.00 28.35  ? 150  LEU A CD1   1 
ATOM   831  C CD2   . LEU A 1 108 ? 35.257  11.265  25.588 1.00 25.69  ? 150  LEU A CD2   1 
ATOM   832  N N     . GLY A 1 109 ? 30.967  14.322  24.758 1.00 12.74  ? 151  GLY A N     1 
ATOM   833  C CA    . GLY A 1 109 ? 29.516  14.342  24.716 1.00 12.57  ? 151  GLY A CA    1 
ATOM   834  C C     . GLY A 1 109 ? 28.969  14.234  26.144 1.00 10.34  ? 151  GLY A C     1 
ATOM   835  O O     . GLY A 1 109 ? 28.197  13.311  26.406 1.00 11.76  ? 151  GLY A O     1 
ATOM   836  N N     . THR A 1 110 ? 29.356  15.166  27.024 1.00 11.26  ? 152  THR A N     1 
ATOM   837  C CA    . THR A 1 110 ? 28.941  15.094  28.421 1.00 10.52  ? 152  THR A CA    1 
ATOM   838  C C     . THR A 1 110 ? 28.664  16.501  28.931 1.00 10.64  ? 152  THR A C     1 
ATOM   839  O O     . THR A 1 110 ? 29.137  17.469  28.385 1.00 11.12  ? 152  THR A O     1 
ATOM   840  C CB    . THR A 1 110 ? 29.949  14.402  29.329 1.00 11.11  ? 152  THR A CB    1 
ATOM   841  O OG1   . THR A 1 110 ? 30.988  15.321  29.669 1.00 11.51  ? 152  THR A OG1   1 
ATOM   842  C CG2   . THR A 1 110 ? 30.498  13.113  28.752 1.00 11.56  ? 152  THR A CG2   1 
ATOM   843  N N     . CYS A 1 111 ? 27.999  16.562  30.091 1.00 10.79  ? 153  CYS A N     1 
ATOM   844  C CA    . CYS A 1 111 ? 27.908  17.809  30.846 1.00 10.93  ? 153  CYS A CA    1 
ATOM   845  C C     . CYS A 1 111 ? 27.868  17.502  32.345 1.00 10.63  ? 153  CYS A C     1 
ATOM   846  O O     . CYS A 1 111 ? 27.600  16.376  32.794 1.00 9.92   ? 153  CYS A O     1 
ATOM   847  C CB    . CYS A 1 111 ? 26.672  18.600  30.440 1.00 11.93  ? 153  CYS A CB    1 
ATOM   848  S SG    . CYS A 1 111 ? 25.064  17.834  30.750 1.00 12.58  ? 153  CYS A SG    1 
ATOM   849  N N     . LEU A 1 112 ? 28.043  18.548  33.126 1.00 10.19  ? 154  LEU A N     1 
ATOM   850  C CA    . LEU A 1 112 ? 27.939  18.508  34.587 1.00 8.61   ? 154  LEU A CA    1 
ATOM   851  C C     . LEU A 1 112 ? 27.062  19.699  34.982 1.00 10.53  ? 154  LEU A C     1 
ATOM   852  O O     . LEU A 1 112 ? 27.431  20.861  34.628 1.00 9.87   ? 154  LEU A O     1 
ATOM   853  C CB    . LEU A 1 112 ? 29.328  18.598  35.178 1.00 8.92   ? 154  LEU A CB    1 
ATOM   854  C CG    . LEU A 1 112 ? 29.407  18.634  36.682 1.00 10.10  ? 154  LEU A CG    1 
ATOM   855  C CD1   . LEU A 1 112 ? 28.926  17.336  37.235 1.00 9.28   ? 154  LEU A CD1   1 
ATOM   856  C CD2   . LEU A 1 112 ? 30.814  18.950  37.202 1.00 10.82  ? 154  LEU A CD2   1 
ATOM   857  N N     . LEU A 1 113 ? 25.983  19.419  35.771 1.00 10.07  ? 155  LEU A N     1 
ATOM   858  C CA    . LEU A 1 113 ? 24.910  20.364  36.002 1.00 9.93   ? 155  LEU A CA    1 
ATOM   859  C C     . LEU A 1 113 ? 24.586  20.493  37.478 1.00 11.12  ? 155  LEU A C     1 
ATOM   860  O O     . LEU A 1 113 ? 24.652  19.484  38.212 1.00 10.39  ? 155  LEU A O     1 
ATOM   861  C CB    . LEU A 1 113 ? 23.594  19.922  35.335 1.00 10.54  ? 155  LEU A CB    1 
ATOM   862  C CG    . LEU A 1 113 ? 23.667  19.560  33.852 1.00 11.62  ? 155  LEU A CG    1 
ATOM   863  C CD1   . LEU A 1 113 ? 22.331  19.082  33.317 1.00 12.31  ? 155  LEU A CD1   1 
ATOM   864  C CD2   . LEU A 1 113 ? 24.188  20.747  33.022 1.00 12.19  ? 155  LEU A CD2   1 
ATOM   865  N N     . GLU A 1 114 ? 24.214  21.699  37.880 1.00 9.80   ? 156  GLU A N     1 
ATOM   866  C CA    . GLU A 1 114 ? 23.542  21.907  39.161 1.00 10.10  ? 156  GLU A CA    1 
ATOM   867  C C     . GLU A 1 114 ? 22.036  21.639  39.037 1.00 9.27   ? 156  GLU A C     1 
ATOM   868  O O     . GLU A 1 114 ? 21.469  21.575  37.938 1.00 10.32  ? 156  GLU A O     1 
ATOM   869  C CB    . GLU A 1 114 ? 23.770  23.307  39.720 1.00 11.29  ? 156  GLU A CB    1 
ATOM   870  C CG    . GLU A 1 114 ? 25.219  23.541  40.147 1.00 12.81  ? 156  GLU A CG    1 
ATOM   871  C CD    . GLU A 1 114 ? 25.416  24.797  40.992 1.00 13.37  ? 156  GLU A CD    1 
ATOM   872  O OE1   . GLU A 1 114 ? 24.715  25.793  40.698 1.00 12.59  ? 156  GLU A OE1   1 
ATOM   873  O OE2   . GLU A 1 114 ? 26.191  24.783  41.948 1.00 15.53  ? 156  GLU A OE2   1 
ATOM   874  N N     . PRO A 1 115 ? 21.319  21.393  40.146 1.00 9.70   ? 157  PRO A N     1 
ATOM   875  C CA    . PRO A 1 115 ? 19.934  20.932  40.067 1.00 10.51  ? 157  PRO A CA    1 
ATOM   876  C C     . PRO A 1 115 ? 18.949  21.867  39.390 1.00 10.94  ? 157  PRO A C     1 
ATOM   877  O O     . PRO A 1 115 ? 18.016  21.457  38.715 1.00 11.65  ? 157  PRO A O     1 
ATOM   878  C CB    . PRO A 1 115 ? 19.580  20.721  41.552 1.00 11.57  ? 157  PRO A CB    1 
ATOM   879  C CG    . PRO A 1 115 ? 20.888  20.431  42.209 1.00 11.56  ? 157  PRO A CG    1 
ATOM   880  C CD    . PRO A 1 115 ? 21.857  21.364  41.530 1.00 10.42  ? 157  PRO A CD    1 
ATOM   881  N N     . GLY A 1 116 ? 19.190  23.157  39.554 1.00 9.83   ? 158  GLY A N     1 
ATOM   882  C CA    . GLY A 1 116 ? 18.336  24.205  39.024 1.00 10.14  ? 158  GLY A CA    1 
ATOM   883  C C     . GLY A 1 116 ? 18.468  24.478  37.534 1.00 9.53   ? 158  GLY A C     1 
ATOM   884  O O     . GLY A 1 116 ? 17.645  25.225  36.985 1.00 12.34  ? 158  GLY A O     1 
ATOM   885  N N     . VAL A 1 117 ? 19.467  23.924  36.881 1.00 9.60   ? 159  VAL A N     1 
ATOM   886  C CA    . VAL A 1 117 ? 19.547  24.030  35.427 1.00 9.79   ? 159  VAL A CA    1 
ATOM   887  C C     . VAL A 1 117 ? 18.263  23.467  34.805 1.00 11.50  ? 159  VAL A C     1 
ATOM   888  O O     . VAL A 1 117 ? 17.863  22.346  35.110 1.00 10.97  ? 159  VAL A O     1 
ATOM   889  C CB    . VAL A 1 117 ? 20.802  23.353  34.859 1.00 10.31  ? 159  VAL A CB    1 
ATOM   890  C CG1   . VAL A 1 117 ? 20.836  23.361  33.344 1.00 10.47  ? 159  VAL A CG1   1 
ATOM   891  C CG2   . VAL A 1 117 ? 22.092  23.922  35.416 1.00 11.64  ? 159  VAL A CG2   1 
ATOM   892  N N     . THR A 1 118 ? 17.649  24.229  33.891 1.00 11.25  ? 160  THR A N     1 
ATOM   893  C CA    . THR A 1 118 ? 16.483  23.773  33.183 1.00 10.72  ? 160  THR A CA    1 
ATOM   894  C C     . THR A 1 118 ? 16.850  23.179  31.828 1.00 10.98  ? 160  THR A C     1 
ATOM   895  O O     . THR A 1 118 ? 17.925  23.453  31.275 1.00 10.28  ? 160  THR A O     1 
ATOM   896  C CB    . THR A 1 118 ? 15.443  24.883  33.028 1.00 11.96  ? 160  THR A CB    1 
ATOM   897  O OG1   . THR A 1 118 ? 15.953  25.826  32.081 1.00 12.01  ? 160  THR A OG1   1 
ATOM   898  C CG2   . THR A 1 118 ? 15.073  25.532  34.346 1.00 11.45  ? 160  THR A CG2   1 
ATOM   899  N N     . TYR A 1 119 ? 15.928  22.419  31.232 1.00 11.91  ? 161  TYR A N     1 
ATOM   900  C CA    . TYR A 1 119 ? 16.145  21.895  29.896 1.00 11.94  ? 161  TYR A CA    1 
ATOM   901  C C     . TYR A 1 119 ? 16.318  23.064  28.916 1.00 13.09  ? 161  TYR A C     1 
ATOM   902  O O     . TYR A 1 119 ? 17.212  23.024  28.069 1.00 12.59  ? 161  TYR A O     1 
ATOM   903  C CB    . TYR A 1 119 ? 15.017  20.974  29.440 1.00 12.84  ? 161  TYR A CB    1 
ATOM   904  C CG    . TYR A 1 119 ? 15.078  19.596  30.070 1.00 11.92  ? 161  TYR A CG    1 
ATOM   905  C CD1   . TYR A 1 119 ? 15.947  18.617  29.622 1.00 11.71  ? 161  TYR A CD1   1 
ATOM   906  C CD2   . TYR A 1 119 ? 14.181  19.236  31.072 1.00 12.33  ? 161  TYR A CD2   1 
ATOM   907  C CE1   . TYR A 1 119 ? 16.002  17.346  30.192 1.00 13.07  ? 161  TYR A CE1   1 
ATOM   908  C CE2   . TYR A 1 119 ? 14.257  17.972  31.667 1.00 12.95  ? 161  TYR A CE2   1 
ATOM   909  C CZ    . TYR A 1 119 ? 15.163  17.040  31.218 1.00 13.11  ? 161  TYR A CZ    1 
ATOM   910  O OH    . TYR A 1 119 ? 15.108  15.771  31.794 1.00 17.08  ? 161  TYR A OH    1 
ATOM   911  N N     . GLN A 1 120 ? 15.506  24.111  29.076 1.00 14.27  ? 162  GLN A N     1 
ATOM   912  C CA    . GLN A 1 120 ? 15.580  25.268  28.189 1.00 16.52  ? 162  GLN A CA    1 
ATOM   913  C C     . GLN A 1 120 ? 16.965  25.912  28.271 1.00 14.65  ? 162  GLN A C     1 
ATOM   914  O O     . GLN A 1 120 ? 17.593  26.250  27.271 1.00 14.87  ? 162  GLN A O     1 
ATOM   915  C CB    . GLN A 1 120 ? 14.462  26.267  28.549 1.00 19.77  ? 162  GLN A CB    1 
ATOM   916  C CG    . GLN A 1 120 ? 14.598  27.617  27.854 1.00 26.73  ? 162  GLN A CG    1 
ATOM   917  C CD    . GLN A 1 120 ? 14.167  27.449  26.431 1.00 35.46  ? 162  GLN A CD    1 
ATOM   918  O OE1   . GLN A 1 120 ? 14.971  27.379  25.496 1.00 45.66  ? 162  GLN A OE1   1 
ATOM   919  N NE2   . GLN A 1 120 ? 12.861  27.298  26.280 1.00 38.91  ? 162  GLN A NE2   1 
ATOM   920  N N     . GLN A 1 121 ? 17.449  26.097  29.481 1.00 13.29  ? 163  GLN A N     1 
ATOM   921  C CA    . GLN A 1 121 ? 18.746  26.674  29.721 1.00 14.34  ? 163  GLN A CA    1 
ATOM   922  C C     . GLN A 1 121 ? 19.871  25.878  29.057 1.00 13.58  ? 163  GLN A C     1 
ATOM   923  O O     . GLN A 1 121 ? 20.803  26.419  28.460 1.00 14.11  ? 163  GLN A O     1 
ATOM   924  C CB    . GLN A 1 121 ? 18.864  26.743  31.233 1.00 16.58  ? 163  GLN A CB    1 
ATOM   925  C CG    . GLN A 1 121 ? 20.049  27.431  31.747 1.00 17.90  ? 163  GLN A CG    1 
ATOM   926  C CD    . GLN A 1 121 ? 20.055  27.476  33.262 1.00 18.65  ? 163  GLN A CD    1 
ATOM   927  O OE1   . GLN A 1 121 ? 19.121  27.092  34.021 1.00 17.28  ? 163  GLN A OE1   1 
ATOM   928  N NE2   . GLN A 1 121 ? 21.195  27.942  33.698 1.00 18.76  ? 163  GLN A NE2   1 
ATOM   929  N N     . LEU A 1 122 ? 19.828  24.551  29.180 1.00 11.77  ? 164  LEU A N     1 
ATOM   930  C CA    . LEU A 1 122 ? 20.855  23.689  28.627 1.00 10.95  ? 164  LEU A CA    1 
ATOM   931  C C     . LEU A 1 122 ? 20.796  23.737  27.102 1.00 12.13  ? 164  LEU A C     1 
ATOM   932  O O     . LEU A 1 122 ? 21.849  23.819  26.478 1.00 11.30  ? 164  LEU A O     1 
ATOM   933  C CB    . LEU A 1 122 ? 20.687  22.257  29.189 1.00 11.87  ? 164  LEU A CB    1 
ATOM   934  C CG    . LEU A 1 122 ? 21.720  21.237  28.741 1.00 13.12  ? 164  LEU A CG    1 
ATOM   935  C CD1   . LEU A 1 122 ? 23.183  21.712  29.006 1.00 14.17  ? 164  LEU A CD1   1 
ATOM   936  C CD2   . LEU A 1 122 ? 21.456  19.898  29.423 1.00 14.11  ? 164  LEU A CD2   1 
ATOM   937  N N     . LYS A 1 123 ? 19.610  23.605  26.514 1.00 11.44  ? 165  LYS A N     1 
ATOM   938  C CA    . LYS A 1 123 ? 19.479  23.680  25.074 1.00 11.80  ? 165  LYS A CA    1 
ATOM   939  C C     . LYS A 1 123 ? 19.986  25.033  24.572 1.00 12.44  ? 165  LYS A C     1 
ATOM   940  O O     . LYS A 1 123 ? 20.707  25.067  23.558 1.00 14.18  ? 165  LYS A O     1 
ATOM   941  C CB    . LYS A 1 123 ? 18.006  23.471  24.659 1.00 13.88  ? 165  LYS A CB    1 
ATOM   942  C CG    . LYS A 1 123 ? 17.759  23.467  23.153 1.00 15.46  ? 165  LYS A CG    1 
ATOM   943  C CD    . LYS A 1 123 ? 18.471  22.343  22.423 1.00 16.45  ? 165  LYS A CD    1 
ATOM   944  C CE    . LYS A 1 123 ? 18.079  22.187  20.975 1.00 17.92  ? 165  LYS A CE    1 
ATOM   945  N NZ    . LYS A 1 123 ? 18.811  21.098  20.286 1.00 18.70  ? 165  LYS A NZ    1 
ATOM   946  N N     . ASP A 1 124 ? 19.619  26.129  25.252 1.00 12.84  ? 166  ASP A N     1 
ATOM   947  C CA    . ASP A 1 124 ? 20.123  27.459  24.852 1.00 14.93  ? 166  ASP A CA    1 
ATOM   948  C C     . ASP A 1 124 ? 21.655  27.531  24.907 1.00 16.07  ? 166  ASP A C     1 
ATOM   949  O O     . ASP A 1 124 ? 22.320  28.107  24.014 1.00 15.94  ? 166  ASP A O     1 
ATOM   950  C CB    . ASP A 1 124 ? 19.546  28.576  25.715 1.00 16.93  ? 166  ASP A CB    1 
ATOM   951  C CG    . ASP A 1 124 ? 18.082  28.904  25.458 1.00 19.27  ? 166  ASP A CG    1 
ATOM   952  O OD1   . ASP A 1 124 ? 17.491  28.330  24.501 1.00 20.96  ? 166  ASP A OD1   1 
ATOM   953  O OD2   . ASP A 1 124 ? 17.521  29.634  26.290 1.00 23.28  ? 166  ASP A OD2   1 
ATOM   954  N N     . TYR A 1 125 ? 22.238  26.982  25.955 1.00 13.69  ? 167  TYR A N     1 
ATOM   955  C CA    . TYR A 1 125 ? 23.687  26.942  26.132 1.00 14.33  ? 167  TYR A CA    1 
ATOM   956  C C     . TYR A 1 125 ? 24.341  26.212  24.971 1.00 16.28  ? 167  TYR A C     1 
ATOM   957  O O     . TYR A 1 125 ? 25.298  26.694  24.353 1.00 15.28  ? 167  TYR A O     1 
ATOM   958  C CB    . TYR A 1 125 ? 24.034  26.320  27.490 1.00 16.66  ? 167  TYR A CB    1 
ATOM   959  C CG    . TYR A 1 125 ? 25.491  26.338  27.858 1.00 16.78  ? 167  TYR A CG    1 
ATOM   960  C CD1   . TYR A 1 125 ? 26.396  25.422  27.375 1.00 19.42  ? 167  TYR A CD1   1 
ATOM   961  C CD2   . TYR A 1 125 ? 25.918  27.309  28.739 1.00 22.64  ? 167  TYR A CD2   1 
ATOM   962  C CE1   . TYR A 1 125 ? 27.739  25.477  27.750 1.00 23.10  ? 167  TYR A CE1   1 
ATOM   963  C CE2   . TYR A 1 125 ? 27.228  27.357  29.155 1.00 25.59  ? 167  TYR A CE2   1 
ATOM   964  C CZ    . TYR A 1 125 ? 28.131  26.454  28.651 1.00 23.13  ? 167  TYR A CZ    1 
ATOM   965  O OH    . TYR A 1 125 ? 29.399  26.608  29.146 1.00 32.32  ? 167  TYR A OH    1 
ATOM   966  N N     . LEU A 1 126 ? 23.826  25.036  24.625 1.00 12.87  ? 168  LEU A N     1 
ATOM   967  C CA    . LEU A 1 126 ? 24.398  24.304  23.515 1.00 13.58  ? 168  LEU A CA    1 
ATOM   968  C C     . LEU A 1 126 ? 24.303  25.093  22.206 1.00 14.64  ? 168  LEU A C     1 
ATOM   969  O O     . LEU A 1 126 ? 25.258  25.094  21.415 1.00 15.28  ? 168  LEU A O     1 
ATOM   970  C CB    . LEU A 1 126 ? 23.673  22.952  23.421 1.00 14.77  ? 168  LEU A CB    1 
ATOM   971  C CG    . LEU A 1 126 ? 23.910  21.990  24.600 1.00 14.28  ? 168  LEU A CG    1 
ATOM   972  C CD1   . LEU A 1 126 ? 23.019  20.735  24.498 1.00 14.53  ? 168  LEU A CD1   1 
ATOM   973  C CD2   . LEU A 1 126 ? 25.340  21.518  24.695 1.00 13.72  ? 168  LEU A CD2   1 
ATOM   974  N N     . GLU A 1 127 ? 23.138  25.669  21.938 1.00 14.99  ? 169  GLU A N     1 
ATOM   975  C CA    . GLU A 1 127 ? 22.949  26.373  20.681 1.00 16.90  ? 169  GLU A CA    1 
ATOM   976  C C     . GLU A 1 127 ? 23.832  27.619  20.619 1.00 15.87  ? 169  GLU A C     1 
ATOM   977  O O     . GLU A 1 127 ? 24.411  27.905  19.565 1.00 18.13  ? 169  GLU A O     1 
ATOM   978  C CB    . GLU A 1 127 ? 21.484  26.764  20.483 1.00 20.67  ? 169  GLU A CB    1 
ATOM   979  C CG    . GLU A 1 127 ? 20.620  25.521  20.424 1.00 28.90  ? 169  GLU A CG    1 
ATOM   980  C CD    . GLU A 1 127 ? 19.229  25.606  19.816 1.00 45.02  ? 169  GLU A CD    1 
ATOM   981  O OE1   . GLU A 1 127 ? 18.361  26.348  20.372 1.00 61.44  ? 169  GLU A OE1   1 
ATOM   982  O OE2   . GLU A 1 127 ? 19.003  24.875  18.814 1.00 55.56  ? 169  GLU A OE2   1 
ATOM   983  N N     . GLU A 1 128 ? 23.900  28.384  21.704 1.00 14.82  ? 170  GLU A N     1 
ATOM   984  C CA    . GLU A 1 128 ? 24.655  29.632  21.743 1.00 16.21  ? 170  GLU A CA    1 
ATOM   985  C C     . GLU A 1 128 ? 26.153  29.389  21.523 1.00 17.54  ? 170  GLU A C     1 
ATOM   986  O O     . GLU A 1 128 ? 26.863  30.290  21.019 1.00 19.80  ? 170  GLU A O     1 
ATOM   987  C CB    . GLU A 1 128 ? 24.451  30.347  23.083 1.00 18.50  ? 170  GLU A CB    1 
ATOM   988  C CG    . GLU A 1 128 ? 23.074  30.920  23.205 1.00 22.03  ? 170  GLU A CG    1 
ATOM   989  C CD    . GLU A 1 128 ? 22.685  31.382  24.601 1.00 24.31  ? 170  GLU A CD    1 
ATOM   990  O OE1   . GLU A 1 128 ? 23.529  31.330  25.541 1.00 30.25  ? 170  GLU A OE1   1 
ATOM   991  O OE2   . GLU A 1 128 ? 21.527  31.724  24.729 1.00 34.26  ? 170  GLU A OE2   1 
ATOM   992  N N     . HIS A 1 129 ? 26.658  28.223  21.945 1.00 14.65  ? 171  HIS A N     1 
ATOM   993  C CA    . HIS A 1 129 ? 28.053  27.878  21.811 1.00 15.10  ? 171  HIS A CA    1 
ATOM   994  C C     . HIS A 1 129 ? 28.292  27.006  20.568 1.00 15.00  ? 171  HIS A C     1 
ATOM   995  O O     . HIS A 1 129 ? 29.418  26.547  20.358 1.00 17.66  ? 171  HIS A O     1 
ATOM   996  C CB    . HIS A 1 129 ? 28.615  27.228  23.083 1.00 13.58  ? 171  HIS A CB    1 
ATOM   997  C CG    . HIS A 1 129 ? 28.503  28.074  24.305 1.00 15.44  ? 171  HIS A CG    1 
ATOM   998  N ND1   . HIS A 1 129 ? 27.370  28.237  25.085 1.00 14.85  ? 171  HIS A ND1   1 
ATOM   999  C CD2   . HIS A 1 129 ? 29.434  28.856  24.860 1.00 17.61  ? 171  HIS A CD2   1 
ATOM   1000 C CE1   . HIS A 1 129 ? 27.628  29.110  26.057 1.00 15.50  ? 171  HIS A CE1   1 
ATOM   1001 N NE2   . HIS A 1 129 ? 28.867  29.522  25.923 1.00 18.68  ? 171  HIS A NE2   1 
ATOM   1002 N N     . LYS A 1 130 ? 27.251  26.794  19.731 1.00 14.85  ? 172  LYS A N     1 
ATOM   1003 C CA    . LYS A 1 130 ? 27.330  25.962  18.538 1.00 16.94  ? 172  LYS A CA    1 
ATOM   1004 C C     . LYS A 1 130 ? 27.913  24.577  18.807 1.00 16.90  ? 172  LYS A C     1 
ATOM   1005 O O     . LYS A 1 130 ? 28.723  24.062  18.032 1.00 18.49  ? 172  LYS A O     1 
ATOM   1006 C CB    . LYS A 1 130 ? 28.187  26.614  17.438 1.00 20.22  ? 172  LYS A CB    1 
ATOM   1007 C CG    . LYS A 1 130 ? 27.822  28.061  17.169 1.00 25.85  ? 172  LYS A CG    1 
ATOM   1008 C CD    . LYS A 1 130 ? 26.545  28.294  16.457 1.00 31.08  ? 172  LYS A CD    1 
ATOM   1009 C CE    . LYS A 1 130 ? 26.496  29.694  15.875 1.00 41.52  ? 172  LYS A CE    1 
ATOM   1010 N NZ    . LYS A 1 130 ? 25.113  30.075  15.512 1.00 48.18  ? 172  LYS A NZ    1 
ATOM   1011 N N     . ILE A 1 131 ? 27.509  23.961  19.915 1.00 14.83  ? 173  ILE A N     1 
ATOM   1012 C CA    . ILE A 1 131 ? 27.956  22.618  20.282 1.00 14.73  ? 173  ILE A CA    1 
ATOM   1013 C C     . ILE A 1 131 ? 26.991  21.590  19.729 1.00 13.33  ? 173  ILE A C     1 
ATOM   1014 O O     . ILE A 1 131 ? 25.779  21.682  20.012 1.00 15.03  ? 173  ILE A O     1 
ATOM   1015 C CB    . ILE A 1 131 ? 28.042  22.537  21.798 1.00 14.62  ? 173  ILE A CB    1 
ATOM   1016 C CG1   . ILE A 1 131 ? 29.077  23.511  22.363 1.00 17.27  ? 173  ILE A CG1   1 
ATOM   1017 C CG2   . ILE A 1 131 ? 28.348  21.125  22.285 1.00 15.74  ? 173  ILE A CG2   1 
ATOM   1018 C CD1   . ILE A 1 131 ? 29.011  23.643  23.862 1.00 17.81  ? 173  ILE A CD1   1 
ATOM   1019 N N     . PRO A 1 132 ? 27.445  20.697  18.823 1.00 14.67  ? 174  PRO A N     1 
ATOM   1020 C CA    . PRO A 1 132 ? 26.561  19.787  18.125 1.00 14.22  ? 174  PRO A CA    1 
ATOM   1021 C C     . PRO A 1 132 ? 26.171  18.556  18.979 1.00 14.61  ? 174  PRO A C     1 
ATOM   1022 O O     . PRO A 1 132 ? 26.418  17.412  18.580 1.00 15.10  ? 174  PRO A O     1 
ATOM   1023 C CB    . PRO A 1 132 ? 27.447  19.371  16.931 1.00 17.22  ? 174  PRO A CB    1 
ATOM   1024 C CG    . PRO A 1 132 ? 28.830  19.353  17.498 1.00 17.14  ? 174  PRO A CG    1 
ATOM   1025 C CD    . PRO A 1 132 ? 28.843  20.606  18.353 1.00 18.57  ? 174  PRO A CD    1 
ATOM   1026 N N     . LEU A 1 133 ? 25.585  18.831  20.149 1.00 12.85  ? 175  LEU A N     1 
ATOM   1027 C CA    . LEU A 1 133 ? 25.000  17.818  21.023 1.00 12.38  ? 175  LEU A CA    1 
ATOM   1028 C C     . LEU A 1 133 ? 23.509  18.142  21.177 1.00 13.78  ? 175  LEU A C     1 
ATOM   1029 O O     . LEU A 1 133 ? 23.075  19.311  21.233 1.00 14.36  ? 175  LEU A O     1 
ATOM   1030 C CB    . LEU A 1 133 ? 25.696  17.845  22.392 1.00 11.60  ? 175  LEU A CB    1 
ATOM   1031 C CG    . LEU A 1 133 ? 27.199  17.553  22.416 1.00 11.15  ? 175  LEU A CG    1 
ATOM   1032 C CD1   . LEU A 1 133 ? 27.787  17.825  23.807 1.00 11.43  ? 175  LEU A CD1   1 
ATOM   1033 C CD2   . LEU A 1 133 ? 27.477  16.117  22.048 1.00 11.44  ? 175  LEU A CD2   1 
ATOM   1034 N N     . TRP A 1 134 ? 22.737  17.083  21.427 1.00 13.50  ? 176  TRP A N     1 
ATOM   1035 C CA    . TRP A 1 134 ? 21.319  17.202  21.732 1.00 13.61  ? 176  TRP A CA    1 
ATOM   1036 C C     . TRP A 1 134 ? 21.059  16.864  23.199 1.00 13.32  ? 176  TRP A C     1 
ATOM   1037 O O     . TRP A 1 134 ? 21.874  16.238  23.874 1.00 14.15  ? 176  TRP A O     1 
ATOM   1038 C CB    . TRP A 1 134 ? 20.566  16.230  20.855 1.00 14.59  ? 176  TRP A CB    1 
ATOM   1039 C CG    . TRP A 1 134 ? 20.178  16.747  19.508 1.00 16.25  ? 176  TRP A CG    1 
ATOM   1040 C CD1   . TRP A 1 134 ? 20.459  17.961  18.956 1.00 18.04  ? 176  TRP A CD1   1 
ATOM   1041 C CD2   . TRP A 1 134 ? 19.476  16.000  18.517 1.00 19.08  ? 176  TRP A CD2   1 
ATOM   1042 N NE1   . TRP A 1 134 ? 19.930  18.025  17.696 1.00 21.06  ? 176  TRP A NE1   1 
ATOM   1043 C CE2   . TRP A 1 134 ? 19.339  16.844  17.406 1.00 19.91  ? 176  TRP A CE2   1 
ATOM   1044 C CE3   . TRP A 1 134 ? 18.972  14.707  18.484 1.00 21.88  ? 176  TRP A CE3   1 
ATOM   1045 C CZ2   . TRP A 1 134 ? 18.678  16.423  16.245 1.00 25.68  ? 176  TRP A CZ2   1 
ATOM   1046 C CZ3   . TRP A 1 134 ? 18.301  14.310  17.351 1.00 24.85  ? 176  TRP A CZ3   1 
ATOM   1047 C CH2   . TRP A 1 134 ? 18.196  15.142  16.261 1.00 21.53  ? 176  TRP A CH2   1 
ATOM   1048 N N     . ILE A 1 135 ? 19.918  17.332  23.681 1.00 12.35  ? 177  ILE A N     1 
ATOM   1049 C CA    . ILE A 1 135 ? 19.358  16.929  24.958 1.00 12.66  ? 177  ILE A CA    1 
ATOM   1050 C C     . ILE A 1 135 ? 18.225  15.937  24.721 1.00 12.61  ? 177  ILE A C     1 
ATOM   1051 O O     . ILE A 1 135 ? 17.798  15.665  23.589 1.00 13.24  ? 177  ILE A O     1 
ATOM   1052 C CB    . ILE A 1 135 ? 18.875  18.131  25.782 1.00 12.62  ? 177  ILE A CB    1 
ATOM   1053 C CG1   . ILE A 1 135 ? 17.815  18.965  25.022 1.00 12.04  ? 177  ILE A CG1   1 
ATOM   1054 C CG2   . ILE A 1 135 ? 20.076  18.916  26.249 1.00 15.99  ? 177  ILE A CG2   1 
ATOM   1055 C CD1   . ILE A 1 135 ? 17.101  20.006  25.898 1.00 13.63  ? 177  ILE A CD1   1 
ATOM   1056 N N     . ASP A 1 136 ? 17.730  15.346  25.814 1.00 11.94  ? 178  ASP A N     1 
ATOM   1057 C CA    . ASP A 1 136 ? 16.635  14.418  25.763 1.00 11.98  ? 178  ASP A CA    1 
ATOM   1058 C C     . ASP A 1 136 ? 15.608  14.871  26.801 1.00 11.98  ? 178  ASP A C     1 
ATOM   1059 O O     . ASP A 1 136 ? 15.933  14.932  27.986 1.00 12.50  ? 178  ASP A O     1 
ATOM   1060 C CB    . ASP A 1 136 ? 17.162  12.993  25.949 1.00 13.34  ? 178  ASP A CB    1 
ATOM   1061 C CG    . ASP A 1 136 ? 16.062  11.959  25.793 1.00 12.81  ? 178  ASP A CG    1 
ATOM   1062 O OD1   . ASP A 1 136 ? 15.099  12.007  26.630 1.00 12.72  ? 178  ASP A OD1   1 
ATOM   1063 O OD2   . ASP A 1 136 ? 16.129  11.178  24.802 1.00 12.45  ? 178  ASP A OD2   1 
ATOM   1064 N N     . VAL A 1 137 ? 14.429  15.283  26.320 1.00 13.05  ? 179  VAL A N     1 
ATOM   1065 C CA    . VAL A 1 137 ? 13.479  16.010  27.150 1.00 13.84  ? 179  VAL A CA    1 
ATOM   1066 C C     . VAL A 1 137 ? 12.235  15.182  27.395 1.00 12.84  ? 179  VAL A C     1 
ATOM   1067 O O     . VAL A 1 137 ? 11.690  14.523  26.523 1.00 12.93  ? 179  VAL A O     1 
ATOM   1068 C CB    . VAL A 1 137 ? 13.070  17.375  26.562 1.00 15.96  ? 179  VAL A CB    1 
ATOM   1069 C CG1   . VAL A 1 137 ? 14.240  18.284  26.395 1.00 17.64  ? 179  VAL A CG1   1 
ATOM   1070 C CG2   . VAL A 1 137 ? 12.323  17.252  25.250 1.00 16.08  ? 179  VAL A CG2   1 
ATOM   1071 N N     . PRO A 1 138 ? 11.678  15.230  28.610 1.00 13.35  ? 180  PRO A N     1 
ATOM   1072 C CA    . PRO A 1 138 ? 10.323  14.745  28.843 1.00 13.30  ? 180  PRO A CA    1 
ATOM   1073 C C     . PRO A 1 138 ? 9.328   15.676  28.141 1.00 14.40  ? 180  PRO A C     1 
ATOM   1074 O O     . PRO A 1 138 ? 9.676   16.796  27.782 1.00 14.71  ? 180  PRO A O     1 
ATOM   1075 C CB    . PRO A 1 138 ? 10.213  14.794  30.362 1.00 14.15  ? 180  PRO A CB    1 
ATOM   1076 C CG    . PRO A 1 138 ? 11.084  16.012  30.726 1.00 14.04  ? 180  PRO A CG    1 
ATOM   1077 C CD    . PRO A 1 138 ? 12.239  15.969  29.746 1.00 13.62  ? 180  PRO A CD    1 
ATOM   1078 N N     . ASP A 1 139 ? 8.074   15.244  28.012 1.00 14.57  ? 181  ASP A N     1 
ATOM   1079 C CA    . ASP A 1 139 ? 7.022   16.015  27.373 1.00 16.85  ? 181  ASP A CA    1 
ATOM   1080 C C     . ASP A 1 139 ? 6.400   17.029  28.339 1.00 18.54  ? 181  ASP A C     1 
ATOM   1081 O O     . ASP A 1 139 ? 5.217   17.018  28.605 1.00 23.52  ? 181  ASP A O     1 
ATOM   1082 C CB    . ASP A 1 139 ? 5.965   15.061  26.849 1.00 17.47  ? 181  ASP A CB    1 
ATOM   1083 C CG    . ASP A 1 139 ? 4.982   15.687  25.868 1.00 19.82  ? 181  ASP A CG    1 
ATOM   1084 O OD1   . ASP A 1 139 ? 5.189   16.841  25.515 1.00 22.02  ? 181  ASP A OD1   1 
ATOM   1085 O OD2   . ASP A 1 139 ? 4.020   14.989  25.528 1.00 22.08  ? 181  ASP A OD2   1 
ATOM   1086 N N     . VAL A 1 140 ? 7.186   17.974  28.772 1.00 21.76  ? 182  VAL A N     1 
ATOM   1087 C CA    . VAL A 1 140 ? 6.784   18.969  29.751 1.00 26.14  ? 182  VAL A CA    1 
ATOM   1088 C C     . VAL A 1 140 ? 6.752   20.359  29.145 1.00 37.05  ? 182  VAL A C     1 
ATOM   1089 O O     . VAL A 1 140 ? 7.130   20.594  27.992 1.00 40.68  ? 182  VAL A O     1 
ATOM   1090 C CB    . VAL A 1 140 ? 7.802   19.016  30.891 1.00 29.97  ? 182  VAL A CB    1 
ATOM   1091 C CG1   . VAL A 1 140 ? 7.814   17.700  31.651 1.00 28.07  ? 182  VAL A CG1   1 
ATOM   1092 C CG2   . VAL A 1 140 ? 9.161   19.429  30.351 1.00 29.60  ? 182  VAL A CG2   1 
ATOM   1093 N N     . GLY A 1 141 ? 6.378   21.284  30.017 1.00 31.24  ? 183  GLY A N     1 
ATOM   1094 C CA    . GLY A 1 141 ? 6.209   22.674  29.667 1.00 45.62  ? 183  GLY A CA    1 
ATOM   1095 C C     . GLY A 1 141 ? 7.545   23.388  29.773 1.00 46.14  ? 183  GLY A C     1 
ATOM   1096 O O     . GLY A 1 141 ? 8.612   22.766  29.669 1.00 42.64  ? 183  GLY A O     1 
ATOM   1097 N N     . PRO A 1 142 ? 7.510   24.715  30.017 1.00 42.83  ? 184  PRO A N     1 
ATOM   1098 C CA    . PRO A 1 142 ? 8.709   25.530  29.860 1.00 38.79  ? 184  PRO A CA    1 
ATOM   1099 C C     . PRO A 1 142 ? 9.786   25.236  30.907 1.00 31.69  ? 184  PRO A C     1 
ATOM   1100 O O     . PRO A 1 142 ? 10.963  25.432  30.624 1.00 33.09  ? 184  PRO A O     1 
ATOM   1101 C CB    . PRO A 1 142 ? 8.184   26.986  29.937 1.00 39.25  ? 184  PRO A CB    1 
ATOM   1102 C CG    . PRO A 1 142 ? 6.860   26.889  30.685 1.00 41.49  ? 184  PRO A CG    1 
ATOM   1103 C CD    . PRO A 1 142 ? 6.323   25.492  30.415 1.00 43.49  ? 184  PRO A CD    1 
ATOM   1104 N N     . ILE A 1 143 ? 9.399   24.768  32.106 1.00 26.51  ? 185  ILE A N     1 
ATOM   1105 C CA    . ILE A 1 143 ? 10.367  24.577  33.176 1.00 24.97  ? 185  ILE A CA    1 
ATOM   1106 C C     . ILE A 1 143 ? 10.368  23.119  33.629 1.00 20.29  ? 185  ILE A C     1 
ATOM   1107 O O     . ILE A 1 143 ? 9.360   22.605  34.085 1.00 17.93  ? 185  ILE A O     1 
ATOM   1108 C CB    . ILE A 1 143 ? 10.081  25.500  34.371 1.00 25.70  ? 185  ILE A CB    1 
ATOM   1109 C CG1   . ILE A 1 143 ? 10.072  26.968  33.933 1.00 30.72  ? 185  ILE A CG1   1 
ATOM   1110 C CG2   . ILE A 1 143 ? 11.054  25.226  35.526 1.00 26.99  ? 185  ILE A CG2   1 
ATOM   1111 C CD1   . ILE A 1 143 ? 9.789   27.957  35.067 1.00 34.86  ? 185  ILE A CD1   1 
ATOM   1112 N N     . ALA A 1 144 ? 11.526  22.473  33.534 1.00 16.64  ? 186  ALA A N     1 
ATOM   1113 C CA    . ALA A 1 144 ? 11.781  21.173  34.144 1.00 14.27  ? 186  ALA A CA    1 
ATOM   1114 C C     . ALA A 1 144 ? 13.302  21.007  34.214 1.00 12.48  ? 186  ALA A C     1 
ATOM   1115 O O     . ALA A 1 144 ? 14.019  21.779  33.595 1.00 12.27  ? 186  ALA A O     1 
ATOM   1116 C CB    . ALA A 1 144 ? 11.123  20.086  33.355 1.00 15.05  ? 186  ALA A CB    1 
ATOM   1117 N N     . SER A 1 145 ? 13.812  20.030  34.959 1.00 11.33  ? 187  SER A N     1 
ATOM   1118 C CA    . SER A 1 145 ? 15.223  19.944  35.320 1.00 10.55  ? 187  SER A CA    1 
ATOM   1119 C C     . SER A 1 145 ? 15.802  18.618  34.862 1.00 11.68  ? 187  SER A C     1 
ATOM   1120 O O     . SER A 1 145 ? 15.252  17.587  35.252 1.00 11.83  ? 187  SER A O     1 
ATOM   1121 C CB    . SER A 1 145 ? 15.333  19.994  36.877 1.00 10.55  ? 187  SER A CB    1 
ATOM   1122 O OG    . SER A 1 145 ? 16.642  19.574  37.285 1.00 12.43  ? 187  SER A OG    1 
ATOM   1123 N N     . PRO A 1 146 ? 16.898  18.556  34.070 1.00 10.78  ? 188  PRO A N     1 
ATOM   1124 C CA    . PRO A 1 146 ? 17.540  17.275  33.836 1.00 12.58  ? 188  PRO A CA    1 
ATOM   1125 C C     . PRO A 1 146 ? 17.897  16.569  35.105 1.00 10.25  ? 188  PRO A C     1 
ATOM   1126 O O     . PRO A 1 146 ? 17.753  15.339  35.198 1.00 12.17  ? 188  PRO A O     1 
ATOM   1127 C CB    . PRO A 1 146 ? 18.826  17.600  33.034 1.00 12.94  ? 188  PRO A CB    1 
ATOM   1128 C CG    . PRO A 1 146 ? 18.675  19.006  32.597 1.00 13.91  ? 188  PRO A CG    1 
ATOM   1129 C CD    . PRO A 1 146 ? 17.506  19.625  33.305 1.00 11.43  ? 188  PRO A CD    1 
ATOM   1130 N N     . VAL A 1 147 ? 18.324  17.284  36.127 1.00 10.32  ? 189  VAL A N     1 
ATOM   1131 C CA    . VAL A 1 147 ? 18.691  16.622  37.368 1.00 10.43  ? 189  VAL A CA    1 
ATOM   1132 C C     . VAL A 1 147 ? 17.471  16.042  38.111 1.00 9.76   ? 189  VAL A C     1 
ATOM   1133 O O     . VAL A 1 147 ? 17.391  14.823  38.369 1.00 10.61  ? 189  VAL A O     1 
ATOM   1134 C CB    . VAL A 1 147 ? 19.461  17.556  38.301 1.00 11.34  ? 189  VAL A CB    1 
ATOM   1135 C CG1   . VAL A 1 147 ? 19.548  16.992  39.678 1.00 11.97  ? 189  VAL A CG1   1 
ATOM   1136 C CG2   . VAL A 1 147 ? 20.790  17.909  37.695 1.00 12.87  ? 189  VAL A CG2   1 
ATOM   1137 N N     . GLY A 1 148 ? 16.429  16.845  38.286 1.00 10.61  ? 190  GLY A N     1 
ATOM   1138 C CA    . GLY A 1 148 ? 15.251  16.393  39.007 1.00 10.21  ? 190  GLY A CA    1 
ATOM   1139 C C     . GLY A 1 148 ? 14.582  15.201  38.308 1.00 10.76  ? 190  GLY A C     1 
ATOM   1140 O O     . GLY A 1 148 ? 14.149  14.194  38.909 1.00 10.29  ? 190  GLY A O     1 
ATOM   1141 N N     . ASN A 1 149 ? 14.468  15.330  36.986 1.00 10.69  ? 191  ASN A N     1 
ATOM   1142 C CA    . ASN A 1 149 ? 13.814  14.297  36.191 1.00 10.46  ? 191  ASN A CA    1 
ATOM   1143 C C     . ASN A 1 149 ? 14.602  12.990  36.258 1.00 10.80  ? 191  ASN A C     1 
ATOM   1144 O O     . ASN A 1 149 ? 14.041  11.938  36.473 1.00 11.50  ? 191  ASN A O     1 
ATOM   1145 C CB    . ASN A 1 149 ? 13.613  14.796  34.764 1.00 9.19   ? 191  ASN A CB    1 
ATOM   1146 C CG    . ASN A 1 149 ? 12.847  13.769  33.945 1.00 10.37  ? 191  ASN A CG    1 
ATOM   1147 O OD1   . ASN A 1 149 ? 11.606  13.876  33.746 1.00 12.87  ? 191  ASN A OD1   1 
ATOM   1148 N ND2   . ASN A 1 149 ? 13.560  12.776  33.487 1.00 10.33  ? 191  ASN A ND2   1 
ATOM   1149 N N     . THR A 1 150 ? 15.921  13.054  36.046 1.00 10.29  ? 192  THR A N     1 
ATOM   1150 C CA    . THR A 1 150 ? 16.768  11.894  36.122 1.00 9.10   ? 192  THR A CA    1 
ATOM   1151 C C     . THR A 1 150 ? 16.689  11.215  37.483 1.00 9.43   ? 192  THR A C     1 
ATOM   1152 O O     . THR A 1 150 ? 16.713  9.985   37.561 1.00 10.04  ? 192  THR A O     1 
ATOM   1153 C CB    . THR A 1 150 ? 18.194  12.230  35.693 1.00 9.28   ? 192  THR A CB    1 
ATOM   1154 O OG1   . THR A 1 150 ? 18.147  12.806  34.360 1.00 11.30  ? 192  THR A OG1   1 
ATOM   1155 C CG2   . THR A 1 150 ? 19.079  11.019  35.676 1.00 11.76  ? 192  THR A CG2   1 
ATOM   1156 N N     . LEU A 1 151 ? 16.629  11.998  38.529 1.00 10.01  ? 193  LEU A N     1 
ATOM   1157 C CA    . LEU A 1 151 ? 16.606  11.432  39.872 1.00 11.91  ? 193  LEU A CA    1 
ATOM   1158 C C     . LEU A 1 151 ? 15.282  10.740  40.189 1.00 12.45  ? 193  LEU A C     1 
ATOM   1159 O O     . LEU A 1 151 ? 15.312  9.736   40.928 1.00 13.99  ? 193  LEU A O     1 
ATOM   1160 C CB    . LEU A 1 151 ? 16.923  12.486  40.939 1.00 12.56  ? 193  LEU A CB    1 
ATOM   1161 C CG    . LEU A 1 151 ? 18.321  13.101  40.895 1.00 12.58  ? 193  LEU A CG    1 
ATOM   1162 C CD1   . LEU A 1 151 ? 18.475  14.162  41.985 1.00 13.04  ? 193  LEU A CD1   1 
ATOM   1163 C CD2   . LEU A 1 151 ? 19.390  12.035  41.017 1.00 13.93  ? 193  LEU A CD2   1 
ATOM   1164 N N     . ASP A 1 152 ? 14.191  11.104  39.523 1.00 10.75  ? 194  ASP A N     1 
ATOM   1165 C CA    . ASP A 1 152 ? 12.958  10.342  39.650 1.00 11.60  ? 194  ASP A CA    1 
ATOM   1166 C C     . ASP A 1 152 ? 12.885  9.233   38.586 1.00 10.47  ? 194  ASP A C     1 
ATOM   1167 O O     . ASP A 1 152 ? 11.823  8.619   38.438 1.00 9.83   ? 194  ASP A O     1 
ATOM   1168 C CB    . ASP A 1 152 ? 11.757  11.290  39.606 1.00 13.98  ? 194  ASP A CB    1 
ATOM   1169 C CG    . ASP A 1 152 ? 10.768  11.011  40.750 1.00 15.70  ? 194  ASP A CG    1 
ATOM   1170 O OD1   . ASP A 1 152 ? 11.246  10.555  41.792 1.00 14.72  ? 194  ASP A OD1   1 
ATOM   1171 O OD2   . ASP A 1 152 ? 9.554   11.333  40.611 1.00 13.20  ? 194  ASP A OD2   1 
ATOM   1172 N N     . ARG A 1 153 ? 13.972  9.027   37.828 1.00 10.11  ? 195  ARG A N     1 
ATOM   1173 C CA    . ARG A 1 153 ? 14.083  8.092   36.693 1.00 8.96   ? 195  ARG A CA    1 
ATOM   1174 C C     . ARG A 1 153 ? 13.001  8.321   35.646 1.00 9.91   ? 195  ARG A C     1 
ATOM   1175 O O     . ARG A 1 153 ? 12.414  7.354   35.116 1.00 9.70   ? 195  ARG A O     1 
ATOM   1176 C CB    . ARG A 1 153 ? 14.128  6.633   37.133 1.00 9.07   ? 195  ARG A CB    1 
ATOM   1177 C CG    . ARG A 1 153 ? 15.195  6.422   38.210 1.00 9.73   ? 195  ARG A CG    1 
ATOM   1178 C CD    . ARG A 1 153 ? 15.487  4.978   38.571 1.00 10.63  ? 195  ARG A CD    1 
ATOM   1179 N NE    . ARG A 1 153 ? 14.359  4.379   39.260 1.00 10.81  ? 195  ARG A NE    1 
ATOM   1180 C CZ    . ARG A 1 153 ? 14.302  4.070   40.553 1.00 9.67   ? 195  ARG A CZ    1 
ATOM   1181 N NH1   . ARG A 1 153 ? 15.310  4.325   41.357 1.00 9.30   ? 195  ARG A NH1   1 
ATOM   1182 N NH2   . ARG A 1 153 ? 13.198  3.540   41.044 1.00 8.67   ? 195  ARG A NH2   1 
ATOM   1183 N N     . GLY A 1 154 ? 12.915  9.562   35.209 1.00 9.22   ? 196  GLY A N     1 
ATOM   1184 C CA    . GLY A 1 154 ? 12.030  9.884   34.103 1.00 10.43  ? 196  GLY A CA    1 
ATOM   1185 C C     . GLY A 1 154 ? 12.616  9.555   32.741 1.00 10.62  ? 196  GLY A C     1 
ATOM   1186 O O     . GLY A 1 154 ? 13.704  8.969   32.556 1.00 9.68   ? 196  GLY A O     1 
ATOM   1187 N N     . VAL A 1 155 ? 11.798  9.906   31.740 1.00 10.58  ? 197  VAL A N     1 
ATOM   1188 C CA    . VAL A 1 155 ? 11.909  9.366   30.406 1.00 12.03  ? 197  VAL A CA    1 
ATOM   1189 C C     . VAL A 1 155 ? 11.685  10.454  29.353 1.00 11.37  ? 197  VAL A C     1 
ATOM   1190 O O     . VAL A 1 155 ? 10.786  11.288  29.537 1.00 11.06  ? 197  VAL A O     1 
ATOM   1191 C CB    . VAL A 1 155 ? 10.885  8.235   30.264 1.00 13.84  ? 197  VAL A CB    1 
ATOM   1192 C CG1   . VAL A 1 155 ? 10.815  7.757   28.823 1.00 15.13  ? 197  VAL A CG1   1 
ATOM   1193 C CG2   . VAL A 1 155 ? 11.230  7.094   31.220 1.00 13.69  ? 197  VAL A CG2   1 
ATOM   1194 N N     . GLY A 1 156 ? 12.464  10.351  28.267 1.00 11.28  ? 198  GLY A N     1 
ATOM   1195 C CA    . GLY A 1 156 ? 12.290  11.160  27.073 1.00 11.30  ? 198  GLY A CA    1 
ATOM   1196 C C     . GLY A 1 156 ? 12.339  10.286  25.822 1.00 12.16  ? 198  GLY A C     1 
ATOM   1197 O O     . GLY A 1 156 ? 12.295  9.057   25.960 1.00 11.22  ? 198  GLY A O     1 
ATOM   1198 N N     . TYR A 1 157 ? 12.505  10.934  24.648 1.00 11.14  ? 199  TYR A N     1 
ATOM   1199 C CA    . TYR A 1 157 ? 12.053  10.297  23.408 1.00 10.43  ? 199  TYR A CA    1 
ATOM   1200 C C     . TYR A 1 157 ? 13.118  10.293  22.309 1.00 12.19  ? 199  TYR A C     1 
ATOM   1201 O O     . TYR A 1 157 ? 12.741  10.144  21.144 1.00 13.16  ? 199  TYR A O     1 
ATOM   1202 C CB    . TYR A 1 157 ? 10.693  10.894  22.995 1.00 11.35  ? 199  TYR A CB    1 
ATOM   1203 C CG    . TYR A 1 157 ? 9.726   10.764  24.144 1.00 10.58  ? 199  TYR A CG    1 
ATOM   1204 C CD1   . TYR A 1 157 ? 9.394   9.506   24.608 1.00 10.15  ? 199  TYR A CD1   1 
ATOM   1205 C CD2   . TYR A 1 157 ? 9.364   11.853  24.923 1.00 11.56  ? 199  TYR A CD2   1 
ATOM   1206 C CE1   . TYR A 1 157 ? 8.699   9.320   25.800 1.00 10.50  ? 199  TYR A CE1   1 
ATOM   1207 C CE2   . TYR A 1 157 ? 8.623   11.678  26.094 1.00 11.76  ? 199  TYR A CE2   1 
ATOM   1208 C CZ    . TYR A 1 157 ? 8.284   10.410  26.526 1.00 10.97  ? 199  TYR A CZ    1 
ATOM   1209 O OH    . TYR A 1 157 ? 7.614   10.250  27.729 1.00 11.97  ? 199  TYR A OH    1 
ATOM   1210 N N     . THR A 1 158 ? 14.400  10.459  22.661 1.00 10.76  ? 200  THR A N     1 
ATOM   1211 C CA    . THR A 1 158 ? 15.511  10.193  21.743 1.00 12.10  ? 200  THR A CA    1 
ATOM   1212 C C     . THR A 1 158 ? 16.117  8.821   22.101 1.00 11.30  ? 200  THR A C     1 
ATOM   1213 O O     . THR A 1 158 ? 15.691  8.136   23.034 1.00 11.16  ? 200  THR A O     1 
ATOM   1214 C CB    . THR A 1 158 ? 16.516  11.371  21.712 1.00 12.10  ? 200  THR A CB    1 
ATOM   1215 O OG1   . THR A 1 158 ? 17.444  11.191  22.804 1.00 12.07  ? 200  THR A OG1   1 
ATOM   1216 C CG2   . THR A 1 158 ? 15.830  12.727  21.822 1.00 13.87  ? 200  THR A CG2   1 
ATOM   1217 N N     . PRO A 1 159 ? 17.208  8.392   21.428 1.00 12.19  ? 201  PRO A N     1 
ATOM   1218 C CA    . PRO A 1 159 ? 17.942  7.203   21.868 1.00 12.52  ? 201  PRO A CA    1 
ATOM   1219 C C     . PRO A 1 159 ? 18.489  7.321   23.281 1.00 11.40  ? 201  PRO A C     1 
ATOM   1220 O O     . PRO A 1 159 ? 18.792  6.289   23.893 1.00 12.27  ? 201  PRO A O     1 
ATOM   1221 C CB    . PRO A 1 159 ? 19.047  7.047   20.829 1.00 12.63  ? 201  PRO A CB    1 
ATOM   1222 C CG    . PRO A 1 159 ? 18.453  7.700   19.616 1.00 13.04  ? 201  PRO A CG    1 
ATOM   1223 C CD    . PRO A 1 159 ? 17.749  8.927   20.160 1.00 12.65  ? 201  PRO A CD    1 
ATOM   1224 N N     . TYR A 1 160 ? 18.579  8.532   23.818 1.00 10.70  ? 202  TYR A N     1 
ATOM   1225 C CA    . TYR A 1 160 ? 19.004  8.744   25.208 1.00 11.18  ? 202  TYR A CA    1 
ATOM   1226 C C     . TYR A 1 160 ? 17.789  8.957   26.122 1.00 11.03  ? 202  TYR A C     1 
ATOM   1227 O O     . TYR A 1 160 ? 17.908  9.557   27.222 1.00 12.10  ? 202  TYR A O     1 
ATOM   1228 C CB    . TYR A 1 160 ? 19.974  9.932   25.300 1.00 11.01  ? 202  TYR A CB    1 
ATOM   1229 C CG    . TYR A 1 160 ? 21.414  9.662   24.875 1.00 11.90  ? 202  TYR A CG    1 
ATOM   1230 C CD1   . TYR A 1 160 ? 21.751  8.807   23.839 1.00 12.14  ? 202  TYR A CD1   1 
ATOM   1231 C CD2   . TYR A 1 160 ? 22.467  10.326  25.508 1.00 11.01  ? 202  TYR A CD2   1 
ATOM   1232 C CE1   . TYR A 1 160 ? 23.079  8.623   23.426 1.00 11.38  ? 202  TYR A CE1   1 
ATOM   1233 C CE2   . TYR A 1 160 ? 23.781  10.207  25.072 1.00 11.29  ? 202  TYR A CE2   1 
ATOM   1234 C CZ    . TYR A 1 160 ? 24.097  9.352   24.040 1.00 13.75  ? 202  TYR A CZ    1 
ATOM   1235 O OH    . TYR A 1 160 ? 25.399  9.174   23.672 1.00 13.09  ? 202  TYR A OH    1 
ATOM   1236 N N     . GLY A 1 161 ? 16.674  8.278   25.804 1.00 9.95   ? 203  GLY A N     1 
ATOM   1237 C CA    . GLY A 1 161 ? 15.430  8.561   26.520 1.00 10.28  ? 203  GLY A CA    1 
ATOM   1238 C C     . GLY A 1 161 ? 15.343  7.962   27.919 1.00 10.23  ? 203  GLY A C     1 
ATOM   1239 O O     . GLY A 1 161 ? 14.563  8.465   28.706 1.00 10.73  ? 203  GLY A O     1 
ATOM   1240 N N     . GLU A 1 162 ? 16.049  6.867   28.201 1.00 11.59  ? 204  GLU A N     1 
ATOM   1241 C CA    . GLU A 1 162 ? 16.018  6.273   29.539 1.00 10.96  ? 204  GLU A CA    1 
ATOM   1242 C C     . GLU A 1 162 ? 17.028  7.025   30.407 1.00 10.81  ? 204  GLU A C     1 
ATOM   1243 O O     . GLU A 1 162 ? 18.197  6.683   30.522 1.00 11.73  ? 204  GLU A O     1 
ATOM   1244 C CB    . GLU A 1 162 ? 16.274  4.775   29.475 1.00 11.98  ? 204  GLU A CB    1 
ATOM   1245 C CG    . GLU A 1 162 ? 16.058  4.091   30.826 1.00 15.19  ? 204  GLU A CG    1 
ATOM   1246 C CD    . GLU A 1 162 ? 14.648  4.152   31.377 1.00 15.47  ? 204  GLU A CD    1 
ATOM   1247 O OE1   . GLU A 1 162 ? 13.652  3.842   30.625 1.00 15.35  ? 204  GLU A OE1   1 
ATOM   1248 O OE2   . GLU A 1 162 ? 14.499  4.483   32.584 1.00 14.66  ? 204  GLU A OE2   1 
ATOM   1249 N N     . HIS A 1 163 ? 16.601  8.162   30.977 1.00 11.38  ? 205  HIS A N     1 
ATOM   1250 C CA    . HIS A 1 163 ? 17.507  9.162   31.521 1.00 10.46  ? 205  HIS A CA    1 
ATOM   1251 C C     . HIS A 1 163 ? 18.541  8.631   32.516 1.00 10.16  ? 205  HIS A C     1 
ATOM   1252 O O     . HIS A 1 163 ? 19.741  8.941   32.410 1.00 10.05  ? 205  HIS A O     1 
ATOM   1253 C CB    . HIS A 1 163 ? 16.715  10.323  32.120 1.00 12.09  ? 205  HIS A CB    1 
ATOM   1254 C CG    . HIS A 1 163 ? 15.946  11.119  31.115 1.00 11.27  ? 205  HIS A CG    1 
ATOM   1255 N ND1   . HIS A 1 163 ? 14.944  12.031  31.393 1.00 10.95  ? 205  HIS A ND1   1 
ATOM   1256 C CD2   . HIS A 1 163 ? 16.123  11.149  29.795 1.00 12.69  ? 205  HIS A CD2   1 
ATOM   1257 C CE1   . HIS A 1 163 ? 14.503  12.524  30.267 1.00 12.79  ? 205  HIS A CE1   1 
ATOM   1258 N NE2   . HIS A 1 163 ? 15.229  12.054  29.291 1.00 12.25  ? 205  HIS A NE2   1 
ATOM   1259 N N     . PHE A 1 164 ? 18.122  7.779   33.461 1.00 10.47  ? 206  PHE A N     1 
ATOM   1260 C CA    . PHE A 1 164 ? 19.065  7.300   34.448 1.00 10.43  ? 206  PHE A CA    1 
ATOM   1261 C C     . PHE A 1 164 ? 20.205  6.492   33.806 1.00 11.23  ? 206  PHE A C     1 
ATOM   1262 O O     . PHE A 1 164 ? 21.317  6.472   34.351 1.00 11.43  ? 206  PHE A O     1 
ATOM   1263 C CB    . PHE A 1 164 ? 18.349  6.585   35.599 1.00 10.27  ? 206  PHE A CB    1 
ATOM   1264 C CG    . PHE A 1 164 ? 19.261  6.104   36.701 1.00 12.32  ? 206  PHE A CG    1 
ATOM   1265 C CD1   . PHE A 1 164 ? 20.227  6.918   37.277 1.00 13.74  ? 206  PHE A CD1   1 
ATOM   1266 C CD2   . PHE A 1 164 ? 19.140  4.813   37.162 1.00 13.16  ? 206  PHE A CD2   1 
ATOM   1267 C CE1   . PHE A 1 164 ? 21.100  6.418   38.245 1.00 13.22  ? 206  PHE A CE1   1 
ATOM   1268 C CE2   . PHE A 1 164 ? 19.942  4.351   38.197 1.00 14.69  ? 206  PHE A CE2   1 
ATOM   1269 C CZ    . PHE A 1 164 ? 20.944  5.141   38.715 1.00 13.74  ? 206  PHE A CZ    1 
ATOM   1270 N N     . MET A 1 165 ? 19.987  5.822   32.657 1.00 11.09  ? 207  MET A N     1 
ATOM   1271 C CA    . MET A 1 165 ? 21.063  5.104   32.000 1.00 13.87  ? 207  MET A CA    1 
ATOM   1272 C C     . MET A 1 165 ? 22.220  6.017   31.596 1.00 13.21  ? 207  MET A C     1 
ATOM   1273 O O     . MET A 1 165 ? 23.356  5.547   31.539 1.00 15.62  ? 207  MET A O     1 
ATOM   1274 C CB    . MET A 1 165 ? 20.572  4.382   30.743 1.00 16.96  ? 207  MET A CB    1 
ATOM   1275 C CG    . MET A 1 165 ? 19.791  3.201   31.079 1.00 25.79  ? 207  MET A CG    1 
ATOM   1276 S SD    . MET A 1 165 ? 20.771  1.727   31.600 1.00 45.31  ? 207  MET A SD    1 
ATOM   1277 C CE    . MET A 1 165 ? 22.450  2.098   31.102 1.00 33.99  ? 207  MET A CE    1 
ATOM   1278 N N     . PHE A 1 166 ? 21.933  7.309   31.380 1.00 10.51  ? 208  PHE A N     1 
ATOM   1279 C CA    . PHE A 1 166 ? 22.878  8.253   30.812 1.00 11.55  ? 208  PHE A CA    1 
ATOM   1280 C C     . PHE A 1 166 ? 23.491  9.174   31.866 1.00 9.10   ? 208  PHE A C     1 
ATOM   1281 O O     . PHE A 1 166 ? 24.292  10.031  31.552 1.00 11.76  ? 208  PHE A O     1 
ATOM   1282 C CB    . PHE A 1 166 ? 22.190  8.982   29.639 1.00 13.00  ? 208  PHE A CB    1 
ATOM   1283 C CG    . PHE A 1 166 ? 21.861  8.033   28.534 1.00 14.11  ? 208  PHE A CG    1 
ATOM   1284 C CD1   . PHE A 1 166 ? 22.848  7.615   27.641 1.00 14.23  ? 208  PHE A CD1   1 
ATOM   1285 C CD2   . PHE A 1 166 ? 20.592  7.465   28.451 1.00 15.98  ? 208  PHE A CD2   1 
ATOM   1286 C CE1   . PHE A 1 166 ? 22.549  6.669   26.678 1.00 15.56  ? 208  PHE A CE1   1 
ATOM   1287 C CE2   . PHE A 1 166 ? 20.342  6.446   27.541 1.00 15.44  ? 208  PHE A CE2   1 
ATOM   1288 C CZ    . PHE A 1 166 ? 21.312  6.075   26.651 1.00 15.69  ? 208  PHE A CZ    1 
ATOM   1289 N N     . GLN A 1 167 ? 23.096  9.034   33.138 1.00 9.55   ? 209  GLN A N     1 
ATOM   1290 C CA    . GLN A 1 167 ? 23.715  9.728   34.257 1.00 9.74   ? 209  GLN A CA    1 
ATOM   1291 C C     . GLN A 1 167 ? 25.096  9.150   34.516 1.00 9.19   ? 209  GLN A C     1 
ATOM   1292 O O     . GLN A 1 167 ? 25.308  7.938   34.435 1.00 8.89   ? 209  GLN A O     1 
ATOM   1293 C CB    . GLN A 1 167 ? 22.764  9.642   35.463 1.00 10.22  ? 209  GLN A CB    1 
ATOM   1294 C CG    . GLN A 1 167 ? 23.274  10.336  36.726 1.00 11.16  ? 209  GLN A CG    1 
ATOM   1295 C CD    . GLN A 1 167 ? 24.053  9.433   37.653 1.00 11.25  ? 209  GLN A CD    1 
ATOM   1296 O OE1   . GLN A 1 167 ? 23.799  8.238   37.691 1.00 12.65  ? 209  GLN A OE1   1 
ATOM   1297 N NE2   . GLN A 1 167 ? 25.062  9.943   38.326 1.00 10.68  ? 209  GLN A NE2   1 
ATOM   1298 N N     . CYS A 1 168 ? 26.058  10.011  34.833 1.00 8.81   ? 210  CYS A N     1 
ATOM   1299 C CA    . CYS A 1 168 ? 27.427  9.582   35.054 1.00 8.49   ? 210  CYS A CA    1 
ATOM   1300 C C     . CYS A 1 168 ? 28.119  10.543  36.021 1.00 9.95   ? 210  CYS A C     1 
ATOM   1301 O O     . CYS A 1 168 ? 28.450  11.661  35.662 1.00 10.21  ? 210  CYS A O     1 
ATOM   1302 C CB    . CYS A 1 168 ? 28.218  9.470   33.744 1.00 8.79   ? 210  CYS A CB    1 
ATOM   1303 S SG    . CYS A 1 168 ? 29.826  8.653   33.909 1.00 10.18  ? 210  CYS A SG    1 
ATOM   1304 N N     . GLY A 1 169 ? 28.280  10.076  37.268 1.00 9.37   ? 211  GLY A N     1 
ATOM   1305 C CA    . GLY A 1 169 ? 28.786  10.879  38.383 1.00 10.38  ? 211  GLY A CA    1 
ATOM   1306 C C     . GLY A 1 169 ? 27.751  11.811  39.018 1.00 10.41  ? 211  GLY A C     1 
ATOM   1307 O O     . GLY A 1 169 ? 26.889  12.376  38.336 1.00 10.18  ? 211  GLY A O     1 
ATOM   1308 N N     . MET A 1 170 ? 27.831  11.935  40.348 1.00 9.45   ? 212  MET A N     1 
ATOM   1309 C CA    . MET A 1 170 ? 27.058  12.933  41.048 1.00 9.83   ? 212  MET A CA    1 
ATOM   1310 C C     . MET A 1 170 ? 27.790  13.335  42.310 1.00 10.16  ? 212  MET A C     1 
ATOM   1311 O O     . MET A 1 170 ? 28.615  12.593  42.868 1.00 9.47   ? 212  MET A O     1 
ATOM   1312 C CB    . MET A 1 170 ? 25.634  12.509  41.412 1.00 9.97   ? 212  MET A CB    1 
ATOM   1313 C CG    . MET A 1 170 ? 25.596  11.241  42.224 1.00 11.81  ? 212  MET A CG    1 
ATOM   1314 S SD    . MET A 1 170 ? 23.908  10.756  42.828 1.00 13.19  ? 212  MET A SD    1 
ATOM   1315 C CE    . MET A 1 170 ? 23.023  10.489  41.315 1.00 13.75  ? 212  MET A CE    1 
ATOM   1316 N N     . GLU A 1 171 ? 27.456  14.540  42.769 1.00 9.99   ? 213  GLU A N     1 
ATOM   1317 C CA    . GLU A 1 171 ? 27.848  14.966  44.122 1.00 9.24   ? 213  GLU A CA    1 
ATOM   1318 C C     . GLU A 1 171 ? 26.585  14.979  44.983 1.00 9.48   ? 213  GLU A C     1 
ATOM   1319 O O     . GLU A 1 171 ? 25.557  15.478  44.557 1.00 9.73   ? 213  GLU A O     1 
ATOM   1320 C CB    . GLU A 1 171 ? 28.514  16.350  44.093 1.00 9.59   ? 213  GLU A CB    1 
ATOM   1321 C CG    . GLU A 1 171 ? 28.974  16.867  45.473 1.00 11.22  ? 213  GLU A CG    1 
ATOM   1322 C CD    . GLU A 1 171 ? 29.544  18.274  45.365 1.00 12.50  ? 213  GLU A CD    1 
ATOM   1323 O OE1   . GLU A 1 171 ? 28.745  19.239  45.236 1.00 13.95  ? 213  GLU A OE1   1 
ATOM   1324 O OE2   . GLU A 1 171 ? 30.779  18.382  45.318 1.00 15.19  ? 213  GLU A OE2   1 
ATOM   1325 N N     . VAL A 1 172 ? 26.695  14.443  46.207 1.00 10.45  ? 214  VAL A N     1 
ATOM   1326 C CA    . VAL A 1 172 ? 25.589  14.338  47.147 1.00 11.65  ? 214  VAL A CA    1 
ATOM   1327 C C     . VAL A 1 172 ? 26.010  15.018  48.436 1.00 11.89  ? 214  VAL A C     1 
ATOM   1328 O O     . VAL A 1 172 ? 27.107  14.791  48.958 1.00 13.56  ? 214  VAL A O     1 
ATOM   1329 C CB    . VAL A 1 172 ? 25.254  12.853  47.427 1.00 14.02  ? 214  VAL A CB    1 
ATOM   1330 C CG1   . VAL A 1 172 ? 24.072  12.730  48.333 1.00 15.20  ? 214  VAL A CG1   1 
ATOM   1331 C CG2   . VAL A 1 172 ? 25.015  12.092  46.110 1.00 14.44  ? 214  VAL A CG2   1 
ATOM   1332 N N     . CYS A 1 173 ? 25.115  15.848  48.973 1.00 10.13  ? 215  CYS A N     1 
ATOM   1333 C CA    . CYS A 1 173 ? 25.207  16.243  50.367 1.00 10.36  ? 215  CYS A CA    1 
ATOM   1334 C C     . CYS A 1 173 ? 24.479  15.179  51.174 1.00 9.82   ? 215  CYS A C     1 
ATOM   1335 O O     . CYS A 1 173 ? 23.268  15.001  51.022 1.00 10.30  ? 215  CYS A O     1 
ATOM   1336 C CB    . CYS A 1 173 ? 24.582  17.620  50.559 1.00 11.29  ? 215  CYS A CB    1 
ATOM   1337 S SG    . CYS A 1 173 ? 24.713  18.198  52.292 1.00 12.04  ? 215  CYS A SG    1 
ATOM   1338 N N     . LEU A 1 174 ? 25.228  14.461  52.016 1.00 10.26  ? 216  LEU A N     1 
ATOM   1339 C CA    . LEU A 1 174 ? 24.668  13.361  52.788 1.00 9.61   ? 216  LEU A CA    1 
ATOM   1340 C C     . LEU A 1 174 ? 23.910  14.022  53.956 1.00 9.98   ? 216  LEU A C     1 
ATOM   1341 O O     . LEU A 1 174 ? 24.019  15.221  54.244 1.00 10.21  ? 216  LEU A O     1 
ATOM   1342 C CB    . LEU A 1 174 ? 25.816  12.529  53.372 1.00 11.84  ? 216  LEU A CB    1 
ATOM   1343 C CG    . LEU A 1 174 ? 26.599  11.769  52.291 1.00 13.36  ? 216  LEU A CG    1 
ATOM   1344 C CD1   . LEU A 1 174 ? 27.821  11.038  52.855 1.00 15.72  ? 216  LEU A CD1   1 
ATOM   1345 C CD2   . LEU A 1 174 ? 25.670  10.827  51.554 1.00 14.67  ? 216  LEU A CD2   1 
ATOM   1346 N N     . PRO A 1 175 ? 23.095  13.274  54.697 1.00 10.50  ? 217  PRO A N     1 
ATOM   1347 C CA    . PRO A 1 175 ? 22.289  13.879  55.754 1.00 11.11  ? 217  PRO A CA    1 
ATOM   1348 C C     . PRO A 1 175 ? 23.069  14.515  56.906 1.00 13.69  ? 217  PRO A C     1 
ATOM   1349 O O     . PRO A 1 175 ? 22.476  15.275  57.673 1.00 14.06  ? 217  PRO A O     1 
ATOM   1350 C CB    . PRO A 1 175 ? 21.510  12.671  56.308 1.00 10.13  ? 217  PRO A CB    1 
ATOM   1351 C CG    . PRO A 1 175 ? 21.376  11.751  55.137 1.00 10.70  ? 217  PRO A CG    1 
ATOM   1352 C CD    . PRO A 1 175 ? 22.682  11.898  54.388 1.00 10.83  ? 217  PRO A CD    1 
ATOM   1353 N N     . ASP A 1 176 ? 24.350  14.176  57.056 1.00 13.54  ? 218  ASP A N     1 
ATOM   1354 C CA    . ASP A 1 176 ? 25.171  14.836  58.060 1.00 16.88  ? 218  ASP A CA    1 
ATOM   1355 C C     . ASP A 1 176 ? 25.827  16.124  57.556 1.00 16.72  ? 218  ASP A C     1 
ATOM   1356 O O     . ASP A 1 176 ? 26.547  16.768  58.335 1.00 17.13  ? 218  ASP A O     1 
ATOM   1357 C CB    . ASP A 1 176 ? 26.262  13.908  58.586 1.00 19.52  ? 218  ASP A CB    1 
ATOM   1358 C CG    . ASP A 1 176 ? 27.331  13.492  57.588 1.00 21.55  ? 218  ASP A CG    1 
ATOM   1359 O OD1   . ASP A 1 176 ? 27.196  13.762  56.407 1.00 20.48  ? 218  ASP A OD1   1 
ATOM   1360 O OD2   . ASP A 1 176 ? 28.331  12.911  58.032 1.00 27.12  ? 218  ASP A OD2   1 
ATOM   1361 N N     . GLY A 1 177 ? 25.570  16.525  56.302 1.00 12.56  ? 219  GLY A N     1 
ATOM   1362 C CA    . GLY A 1 177 ? 26.163  17.740  55.766 1.00 12.68  ? 219  GLY A CA    1 
ATOM   1363 C C     . GLY A 1 177 ? 27.507  17.553  55.049 1.00 13.36  ? 219  GLY A C     1 
ATOM   1364 O O     . GLY A 1 177 ? 28.039  18.537  54.531 1.00 15.28  ? 219  GLY A O     1 
ATOM   1365 N N     . ARG A 1 178 ? 28.058  16.321  54.986 1.00 12.64  ? 220  ARG A N     1 
ATOM   1366 C CA    . ARG A 1 178 ? 29.277  16.057  54.244 1.00 12.15  ? 220  ARG A CA    1 
ATOM   1367 C C     . ARG A 1 178 ? 28.962  15.824  52.764 1.00 11.38  ? 220  ARG A C     1 
ATOM   1368 O O     . ARG A 1 178 ? 27.885  15.339  52.442 1.00 12.70  ? 220  ARG A O     1 
ATOM   1369 C CB    . ARG A 1 178 ? 30.028  14.868  54.836 1.00 15.44  ? 220  ARG A CB    1 
ATOM   1370 C CG    . ARG A 1 178 ? 30.651  15.135  56.198 1.00 18.99  ? 220  ARG A CG    1 
ATOM   1371 C CD    . ARG A 1 178 ? 31.556  14.006  56.675 1.00 22.04  ? 220  ARG A CD    1 
ATOM   1372 N NE    . ARG A 1 178 ? 30.839  12.755  56.765 1.00 25.35  ? 220  ARG A NE    1 
ATOM   1373 C CZ    . ARG A 1 178 ? 31.413  11.534  56.793 1.00 29.25  ? 220  ARG A CZ    1 
ATOM   1374 N NH1   . ARG A 1 178 ? 32.733  11.407  56.798 1.00 24.48  ? 220  ARG A NH1   1 
ATOM   1375 N NH2   . ARG A 1 178 ? 30.643  10.453  56.748 1.00 29.44  ? 220  ARG A NH2   1 
ATOM   1376 N N     . LEU A 1 179 ? 29.816  16.325  51.892 1.00 11.22  ? 221  LEU A N     1 
ATOM   1377 C CA    . LEU A 1 179 ? 29.710  16.046  50.461 1.00 11.31  ? 221  LEU A CA    1 
ATOM   1378 C C     . LEU A 1 179 ? 30.442  14.765  50.087 1.00 11.58  ? 221  LEU A C     1 
ATOM   1379 O O     . LEU A 1 179 ? 31.518  14.470  50.600 1.00 13.22  ? 221  LEU A O     1 
ATOM   1380 C CB    . LEU A 1 179 ? 30.298  17.217  49.672 1.00 12.21  ? 221  LEU A CB    1 
ATOM   1381 C CG    . LEU A 1 179 ? 29.660  18.572  49.923 1.00 12.99  ? 221  LEU A CG    1 
ATOM   1382 C CD1   . LEU A 1 179 ? 30.339  19.650  49.064 1.00 15.27  ? 221  LEU A CD1   1 
ATOM   1383 C CD2   . LEU A 1 179 ? 28.180  18.538  49.669 1.00 14.33  ? 221  LEU A CD2   1 
ATOM   1384 N N     . MET A 1 180 ? 29.853  14.021  49.160 1.00 9.87   ? 222  MET A N     1 
ATOM   1385 C CA    . MET A 1 180 ? 30.410  12.772  48.654 1.00 9.73   ? 222  MET A CA    1 
ATOM   1386 C C     . MET A 1 180 ? 30.242  12.770  47.127 1.00 11.07  ? 222  MET A C     1 
ATOM   1387 O O     . MET A 1 180 ? 29.141  13.011  46.626 1.00 11.37  ? 222  MET A O     1 
ATOM   1388 C CB    . MET A 1 180 ? 29.726  11.551  49.265 1.00 10.68  ? 222  MET A CB    1 
ATOM   1389 C CG    . MET A 1 180 ? 30.329  10.264  48.815 1.00 11.38  ? 222  MET A CG    1 
ATOM   1390 S SD    . MET A 1 180 ? 29.568  8.816   49.575 1.00 12.53  ? 222  MET A SD    1 
ATOM   1391 C CE    . MET A 1 180 ? 28.009  8.714   48.706 1.00 12.71  ? 222  MET A CE    1 
ATOM   1392 N N     . ARG A 1 181 ? 31.327  12.511  46.360 1.00 9.78   ? 223  ARG A N     1 
ATOM   1393 C CA    . ARG A 1 181 ? 31.240  12.408  44.913 1.00 9.36   ? 223  ARG A CA    1 
ATOM   1394 C C     . ARG A 1 181 ? 31.317  10.927  44.533 1.00 9.70   ? 223  ARG A C     1 
ATOM   1395 O O     . ARG A 1 181 ? 32.155  10.146  45.037 1.00 10.27  ? 223  ARG A O     1 
ATOM   1396 C CB    . ARG A 1 181 ? 32.356  13.189  44.226 1.00 10.77  ? 223  ARG A CB    1 
ATOM   1397 C CG    . ARG A 1 181 ? 32.201  14.687  44.423 1.00 11.99  ? 223  ARG A CG    1 
ATOM   1398 C CD    . ARG A 1 181 ? 33.201  15.493  43.643 1.00 12.48  ? 223  ARG A CD    1 
ATOM   1399 N NE    . ARG A 1 181 ? 32.869  16.894  43.816 1.00 14.25  ? 223  ARG A NE    1 
ATOM   1400 C CZ    . ARG A 1 181 ? 33.325  17.893  43.066 1.00 15.61  ? 223  ARG A CZ    1 
ATOM   1401 N NH1   . ARG A 1 181 ? 34.247  17.678  42.145 1.00 15.66  ? 223  ARG A NH1   1 
ATOM   1402 N NH2   . ARG A 1 181 ? 32.823  19.114  43.231 1.00 15.78  ? 223  ARG A NH2   1 
ATOM   1403 N N     . THR A 1 182 ? 30.419  10.507  43.651 1.00 9.05   ? 224  THR A N     1 
ATOM   1404 C CA    . THR A 1 182 ? 30.334  9.107   43.223 1.00 9.31   ? 224  THR A CA    1 
ATOM   1405 C C     . THR A 1 182 ? 31.268  8.866   42.035 1.00 11.40  ? 224  THR A C     1 
ATOM   1406 O O     . THR A 1 182 ? 31.774  9.807   41.413 1.00 11.13  ? 224  THR A O     1 
ATOM   1407 C CB    . THR A 1 182 ? 28.886  8.722   42.848 1.00 10.76  ? 224  THR A CB    1 
ATOM   1408 O OG1   . THR A 1 182 ? 28.538  9.451   41.660 1.00 10.68  ? 224  THR A OG1   1 
ATOM   1409 C CG2   . THR A 1 182 ? 27.932  9.026   43.991 1.00 10.82  ? 224  THR A CG2   1 
ATOM   1410 N N     . GLY A 1 183 ? 31.432  7.579   41.706 1.00 12.08  ? 225  GLY A N     1 
ATOM   1411 C CA    . GLY A 1 183 ? 32.153  7.156   40.512 1.00 12.15  ? 225  GLY A CA    1 
ATOM   1412 C C     . GLY A 1 183 ? 33.642  7.479   40.671 1.00 11.05  ? 225  GLY A C     1 
ATOM   1413 O O     . GLY A 1 183 ? 34.296  7.089   41.630 1.00 11.63  ? 225  GLY A O     1 
ATOM   1414 N N     . MET A 1 184 ? 34.193  8.211   39.690 1.00 11.30  ? 226  MET A N     1 
ATOM   1415 C CA    . MET A 1 184 ? 35.585  8.598   39.752 1.00 12.50  ? 226  MET A CA    1 
ATOM   1416 C C     . MET A 1 184 ? 35.773  9.956   40.447 1.00 13.48  ? 226  MET A C     1 
ATOM   1417 O O     . MET A 1 184 ? 36.905  10.435  40.619 1.00 14.41  ? 226  MET A O     1 
ATOM   1418 C CB    . MET A 1 184 ? 36.147  8.688   38.335 1.00 13.03  ? 226  MET A CB    1 
ATOM   1419 C CG    . MET A 1 184 ? 35.970  7.418   37.539 1.00 12.93  ? 226  MET A CG    1 
ATOM   1420 S SD    . MET A 1 184 ? 36.549  5.931   38.405 1.00 14.87  ? 226  MET A SD    1 
ATOM   1421 C CE    . MET A 1 184 ? 38.290  6.257   38.293 1.00 14.31  ? 226  MET A CE    1 
ATOM   1422 N N     . GLY A 1 185 ? 34.678  10.602  40.846 1.00 11.06  ? 227  GLY A N     1 
ATOM   1423 C CA    . GLY A 1 185 ? 34.716  12.013  41.257 1.00 11.19  ? 227  GLY A CA    1 
ATOM   1424 C C     . GLY A 1 185 ? 35.409  12.305  42.591 1.00 13.50  ? 227  GLY A C     1 
ATOM   1425 O O     . GLY A 1 185 ? 35.829  13.451  42.837 1.00 14.84  ? 227  GLY A O     1 
ATOM   1426 N N     . SER A 1 186 ? 35.592  11.277  43.419 1.00 12.98  ? 228  SER A N     1 
ATOM   1427 C CA    . SER A 1 186 ? 36.219  11.497  44.715 1.00 14.00  ? 228  SER A CA    1 
ATOM   1428 C C     . SER A 1 186 ? 37.745  11.455  44.602 1.00 16.91  ? 228  SER A C     1 
ATOM   1429 O O     . SER A 1 186 ? 38.416  11.616  45.604 1.00 18.18  ? 228  SER A O     1 
ATOM   1430 C CB    . SER A 1 186 ? 35.716  10.521  45.731 1.00 14.44  ? 228  SER A CB    1 
ATOM   1431 O OG    . SER A 1 186 ? 36.147  9.178   45.487 1.00 13.83  ? 228  SER A OG    1 
ATOM   1432 N N     . ILE A 1 187 ? 38.289  11.173  43.422 1.00 17.32  ? 229  ILE A N     1 
ATOM   1433 C CA    . ILE A 1 187 ? 39.726  11.250  43.190 1.00 20.75  ? 229  ILE A CA    1 
ATOM   1434 C C     . ILE A 1 187 ? 40.055  12.705  42.840 1.00 24.40  ? 229  ILE A C     1 
ATOM   1435 O O     . ILE A 1 187 ? 39.519  13.227  41.873 1.00 21.03  ? 229  ILE A O     1 
ATOM   1436 C CB    . ILE A 1 187 ? 40.125  10.300  42.047 1.00 21.79  ? 229  ILE A CB    1 
ATOM   1437 C CG1   . ILE A 1 187 ? 39.588  8.859   42.108 1.00 23.15  ? 229  ILE A CG1   1 
ATOM   1438 C CG2   . ILE A 1 187 ? 41.635  10.307  41.865 1.00 24.87  ? 229  ILE A CG2   1 
ATOM   1439 C CD1   . ILE A 1 187 ? 40.350  7.950   42.934 1.00 27.44  ? 229  ILE A CD1   1 
ATOM   1440 N N     . LYS A 1 188 ? 40.950  13.391  43.574 1.00 25.21  ? 230  LYS A N     1 
ATOM   1441 C CA    . LYS A 1 188 ? 41.086  14.827  43.355 1.00 31.40  ? 230  LYS A CA    1 
ATOM   1442 C C     . LYS A 1 188 ? 41.556  15.107  41.922 1.00 26.01  ? 230  LYS A C     1 
ATOM   1443 O O     . LYS A 1 188 ? 42.453  14.434  41.467 1.00 27.25  ? 230  LYS A O     1 
ATOM   1444 C CB    . LYS A 1 188 ? 42.062  15.430  44.375 1.00 41.68  ? 230  LYS A CB    1 
ATOM   1445 C CG    . LYS A 1 188 ? 42.029  16.956  44.462 1.00 52.53  ? 230  LYS A CG    1 
ATOM   1446 C CD    . LYS A 1 188 ? 43.015  17.528  45.489 1.00 62.33  ? 230  LYS A CD    1 
ATOM   1447 C CE    . LYS A 1 188 ? 42.822  19.004  45.786 1.00 66.84  ? 230  LYS A CE    1 
ATOM   1448 N NZ    . LYS A 1 188 ? 43.321  19.855  44.679 1.00 70.37  ? 230  LYS A NZ    1 
ATOM   1449 N N     . GLY A 1 189 ? 40.891  16.051  41.235 1.00 35.49  ? 231  GLY A N     1 
ATOM   1450 C CA    . GLY A 1 189 ? 41.203  16.383  39.843 1.00 39.04  ? 231  GLY A CA    1 
ATOM   1451 C C     . GLY A 1 189 ? 41.132  15.181  38.892 1.00 41.19  ? 231  GLY A C     1 
ATOM   1452 O O     . GLY A 1 189 ? 41.941  15.014  37.952 1.00 36.90  ? 231  GLY A O     1 
ATOM   1453 N N     . SER A 1 190 ? 40.177  14.286  39.170 1.00 35.39  ? 232  SER A N     1 
ATOM   1454 C CA    . SER A 1 190 ? 39.842  13.272  38.183 1.00 23.70  ? 232  SER A CA    1 
ATOM   1455 C C     . SER A 1 190 ? 39.263  13.994  36.971 1.00 18.51  ? 232  SER A C     1 
ATOM   1456 O O     . SER A 1 190 ? 38.422  14.883  37.085 1.00 20.19  ? 232  SER A O     1 
ATOM   1457 C CB    . SER A 1 190 ? 38.861  12.253  38.717 1.00 20.18  ? 232  SER A CB    1 
ATOM   1458 O OG    . SER A 1 190 ? 38.381  11.421  37.670 1.00 17.40  ? 232  SER A OG    1 
ATOM   1459 N N     . THR A 1 191 ? 39.684  13.535  35.805 1.00 15.20  ? 233  THR A N     1 
ATOM   1460 C CA    . THR A 1 191 ? 39.130  13.985  34.549 1.00 15.38  ? 233  THR A CA    1 
ATOM   1461 C C     . THR A 1 191 ? 38.131  12.966  33.992 1.00 13.96  ? 233  THR A C     1 
ATOM   1462 O O     . THR A 1 191 ? 37.647  13.136  32.862 1.00 14.47  ? 233  THR A O     1 
ATOM   1463 C CB    . THR A 1 191 ? 40.266  14.316  33.571 1.00 18.17  ? 233  THR A CB    1 
ATOM   1464 O OG1   . THR A 1 191 ? 40.977  13.113  33.310 1.00 20.05  ? 233  THR A OG1   1 
ATOM   1465 C CG2   . THR A 1 191 ? 41.184  15.368  34.147 1.00 21.74  ? 233  THR A CG2   1 
ATOM   1466 N N     . ALA A 1 192 ? 37.737  11.962  34.782 1.00 12.30  ? 234  ALA A N     1 
ATOM   1467 C CA    . ALA A 1 192 ? 36.924  10.863  34.274 1.00 11.39  ? 234  ALA A CA    1 
ATOM   1468 C C     . ALA A 1 192 ? 35.550  10.788  34.976 1.00 10.02  ? 234  ALA A C     1 
ATOM   1469 O O     . ALA A 1 192 ? 34.837  9.788   34.852 1.00 11.25  ? 234  ALA A O     1 
ATOM   1470 C CB    . ALA A 1 192 ? 37.647  9.540   34.452 1.00 11.67  ? 234  ALA A CB    1 
ATOM   1471 N N     . TRP A 1 193 ? 35.140  11.856  35.663 1.00 10.18  ? 235  TRP A N     1 
ATOM   1472 C CA    . TRP A 1 193 ? 33.901  11.806  36.452 1.00 9.95   ? 235  TRP A CA    1 
ATOM   1473 C C     . TRP A 1 193 ? 32.696  11.572  35.550 1.00 10.93  ? 235  TRP A C     1 
ATOM   1474 O O     . TRP A 1 193 ? 31.734  10.891  35.980 1.00 10.62  ? 235  TRP A O     1 
ATOM   1475 C CB    . TRP A 1 193 ? 33.749  13.097  37.271 1.00 10.14  ? 235  TRP A CB    1 
ATOM   1476 C CG    . TRP A 1 193 ? 32.760  13.042  38.404 1.00 9.90   ? 235  TRP A CG    1 
ATOM   1477 C CD1   . TRP A 1 193 ? 32.226  11.955  39.025 1.00 10.41  ? 235  TRP A CD1   1 
ATOM   1478 C CD2   . TRP A 1 193 ? 32.262  14.196  39.090 1.00 10.57  ? 235  TRP A CD2   1 
ATOM   1479 N NE1   . TRP A 1 193 ? 31.402  12.361  40.050 1.00 10.73  ? 235  TRP A NE1   1 
ATOM   1480 C CE2   . TRP A 1 193 ? 31.467  13.732  40.161 1.00 10.81  ? 235  TRP A CE2   1 
ATOM   1481 C CE3   . TRP A 1 193 ? 32.487  15.575  38.943 1.00 12.79  ? 235  TRP A CE3   1 
ATOM   1482 C CZ2   . TRP A 1 193 ? 30.775  14.625  40.980 1.00 11.73  ? 235  TRP A CZ2   1 
ATOM   1483 C CZ3   . TRP A 1 193 ? 31.859  16.438  39.804 1.00 11.29  ? 235  TRP A CZ3   1 
ATOM   1484 C CH2   . TRP A 1 193 ? 31.024  15.967  40.800 1.00 10.90  ? 235  TRP A CH2   1 
ATOM   1485 N N     . GLN A 1 194 ? 32.710  12.171  34.347 1.00 10.11  ? 236  GLN A N     1 
ATOM   1486 C CA    . GLN A 1 194 ? 31.628  12.006  33.399 1.00 10.39  ? 236  GLN A CA    1 
ATOM   1487 C C     . GLN A 1 194 ? 31.958  10.992  32.317 1.00 10.86  ? 236  GLN A C     1 
ATOM   1488 O O     . GLN A 1 194 ? 31.236  10.926  31.323 1.00 12.31  ? 236  GLN A O     1 
ATOM   1489 C CB    . GLN A 1 194 ? 31.208  13.370  32.822 1.00 10.72  ? 236  GLN A CB    1 
ATOM   1490 C CG    . GLN A 1 194 ? 30.165  14.065  33.690 1.00 12.48  ? 236  GLN A CG    1 
ATOM   1491 C CD    . GLN A 1 194 ? 30.744  14.520  34.986 1.00 12.30  ? 236  GLN A CD    1 
ATOM   1492 O OE1   . GLN A 1 194 ? 31.498  15.489  35.009 1.00 15.92  ? 236  GLN A OE1   1 
ATOM   1493 N NE2   . GLN A 1 194 ? 30.328  13.919  36.088 1.00 11.46  ? 236  GLN A NE2   1 
ATOM   1494 N N     . ALA A 1 195 ? 32.978  10.139  32.528 1.00 11.27  ? 237  ALA A N     1 
ATOM   1495 C CA    . ALA A 1 195 ? 33.416  9.197   31.504 1.00 11.58  ? 237  ALA A CA    1 
ATOM   1496 C C     . ALA A 1 195 ? 33.075  7.753   31.904 1.00 11.95  ? 237  ALA A C     1 
ATOM   1497 O O     . ALA A 1 195 ? 32.737  6.957   31.028 1.00 10.91  ? 237  ALA A O     1 
ATOM   1498 C CB    . ALA A 1 195 ? 34.892  9.363   31.264 1.00 12.76  ? 237  ALA A CB    1 
ATOM   1499 N N     . PHE A 1 196 ? 33.180  7.403   33.198 1.00 12.61  ? 238  PHE A N     1 
ATOM   1500 C CA    . PHE A 1 196 ? 33.039  6.026   33.657 1.00 11.63  ? 238  PHE A CA    1 
ATOM   1501 C C     . PHE A 1 196 ? 32.027  5.978   34.788 1.00 11.96  ? 238  PHE A C     1 
ATOM   1502 O O     . PHE A 1 196 ? 32.264  6.539   35.820 1.00 12.34  ? 238  PHE A O     1 
ATOM   1503 C CB    . PHE A 1 196 ? 34.384  5.465   34.134 1.00 11.69  ? 238  PHE A CB    1 
ATOM   1504 C CG    . PHE A 1 196 ? 34.339  4.053   34.600 1.00 10.86  ? 238  PHE A CG    1 
ATOM   1505 C CD1   . PHE A 1 196 ? 33.899  3.042   33.739 1.00 12.76  ? 238  PHE A CD1   1 
ATOM   1506 C CD2   . PHE A 1 196 ? 34.690  3.700   35.893 1.00 11.59  ? 238  PHE A CD2   1 
ATOM   1507 C CE1   . PHE A 1 196 ? 33.802  1.719   34.169 1.00 13.28  ? 238  PHE A CE1   1 
ATOM   1508 C CE2   . PHE A 1 196 ? 34.613  2.380   36.318 1.00 12.35  ? 238  PHE A CE2   1 
ATOM   1509 C CZ    . PHE A 1 196 ? 34.210  1.388   35.453 1.00 12.17  ? 238  PHE A CZ    1 
ATOM   1510 N N     . LYS A 1 197 ? 30.944  5.198   34.620 1.00 11.37  ? 239  LYS A N     1 
ATOM   1511 C CA    . LYS A 1 197 ? 29.819  5.267   35.564 1.00 11.73  ? 239  LYS A CA    1 
ATOM   1512 C C     . LYS A 1 197 ? 30.127  4.670   36.937 1.00 11.39  ? 239  LYS A C     1 
ATOM   1513 O O     . LYS A 1 197 ? 29.654  5.189   37.958 1.00 11.96  ? 239  LYS A O     1 
ATOM   1514 C CB    . LYS A 1 197 ? 28.546  4.552   35.074 1.00 14.84  ? 239  LYS A CB    1 
ATOM   1515 C CG    . LYS A 1 197 ? 27.921  5.132   33.816 1.00 16.76  ? 239  LYS A CG    1 
ATOM   1516 C CD    . LYS A 1 197 ? 26.711  4.376   33.293 1.00 16.16  ? 239  LYS A CD    1 
ATOM   1517 C CE    . LYS A 1 197 ? 25.561  4.157   34.266 1.00 15.46  ? 239  LYS A CE    1 
ATOM   1518 N NZ    . LYS A 1 197 ? 24.518  5.224   34.234 1.00 17.54  ? 239  LYS A NZ    1 
ATOM   1519 N N     . TRP A 1 198 ? 30.809  3.526   36.991 1.00 11.05  ? 240  TRP A N     1 
ATOM   1520 C CA    . TRP A 1 198 ? 30.645  2.641   38.142 1.00 11.28  ? 240  TRP A CA    1 
ATOM   1521 C C     . TRP A 1 198 ? 31.572  2.955   39.316 1.00 12.17  ? 240  TRP A C     1 
ATOM   1522 O O     . TRP A 1 198 ? 31.243  2.613   40.468 1.00 13.91  ? 240  TRP A O     1 
ATOM   1523 C CB    . TRP A 1 198 ? 30.922  1.189   37.750 1.00 12.00  ? 240  TRP A CB    1 
ATOM   1524 C CG    . TRP A 1 198 ? 30.265  0.682   36.514 1.00 11.68  ? 240  TRP A CG    1 
ATOM   1525 C CD1   . TRP A 1 198 ? 30.891  -0.032  35.534 1.00 13.12  ? 240  TRP A CD1   1 
ATOM   1526 C CD2   . TRP A 1 198 ? 28.881  0.755   36.160 1.00 12.17  ? 240  TRP A CD2   1 
ATOM   1527 N NE1   . TRP A 1 198 ? 30.007  -0.418  34.605 1.00 12.61  ? 240  TRP A NE1   1 
ATOM   1528 C CE2   . TRP A 1 198 ? 28.755  0.045   34.946 1.00 11.90  ? 240  TRP A CE2   1 
ATOM   1529 C CE3   . TRP A 1 198 ? 27.748  1.345   36.729 1.00 13.11  ? 240  TRP A CE3   1 
ATOM   1530 C CZ2   . TRP A 1 198 ? 27.550  -0.015  34.257 1.00 13.28  ? 240  TRP A CZ2   1 
ATOM   1531 C CZ3   . TRP A 1 198 ? 26.531  1.237   36.083 1.00 13.37  ? 240  TRP A CZ3   1 
ATOM   1532 C CH2   . TRP A 1 198 ? 26.438  0.565   34.859 1.00 13.55  ? 240  TRP A CH2   1 
ATOM   1533 N N     . GLY A 1 199 ? 32.745  3.511   39.020 1.00 12.25  ? 241  GLY A N     1 
ATOM   1534 C CA    . GLY A 1 199 ? 33.812  3.587   40.004 1.00 11.08  ? 241  GLY A CA    1 
ATOM   1535 C C     . GLY A 1 199 ? 34.267  2.221   40.529 1.00 10.97  ? 241  GLY A C     1 
ATOM   1536 O O     . GLY A 1 199 ? 34.346  1.267   39.768 1.00 12.91  ? 241  GLY A O     1 
ATOM   1537 N N     . TYR A 1 200 ? 34.629  2.179   41.816 1.00 10.36  ? 242  TYR A N     1 
ATOM   1538 C CA    . TYR A 1 200 ? 35.290  1.070   42.486 1.00 10.59  ? 242  TYR A CA    1 
ATOM   1539 C C     . TYR A 1 200 ? 34.483  0.733   43.737 1.00 10.72  ? 242  TYR A C     1 
ATOM   1540 O O     . TYR A 1 200 ? 34.066  1.618   44.505 1.00 11.52  ? 242  TYR A O     1 
ATOM   1541 C CB    . TYR A 1 200 ? 36.728  1.410   42.888 1.00 11.48  ? 242  TYR A CB    1 
ATOM   1542 C CG    . TYR A 1 200 ? 37.429  0.444   43.795 1.00 9.91   ? 242  TYR A CG    1 
ATOM   1543 C CD1   . TYR A 1 200 ? 37.763  -0.828  43.343 1.00 12.11  ? 242  TYR A CD1   1 
ATOM   1544 C CD2   . TYR A 1 200 ? 37.672  0.744   45.113 1.00 10.58  ? 242  TYR A CD2   1 
ATOM   1545 C CE1   . TYR A 1 200 ? 38.399  -1.733  44.182 1.00 12.43  ? 242  TYR A CE1   1 
ATOM   1546 C CE2   . TYR A 1 200 ? 38.248  -0.166  45.969 1.00 10.13  ? 242  TYR A CE2   1 
ATOM   1547 C CZ    . TYR A 1 200 ? 38.634  -1.409  45.503 1.00 10.56  ? 242  TYR A CZ    1 
ATOM   1548 O OH    . TYR A 1 200 ? 39.298  -2.286  46.366 1.00 11.53  ? 242  TYR A OH    1 
ATOM   1549 N N     . GLY A 1 201 ? 34.226  -0.573  43.939 1.00 8.78   ? 243  GLY A N     1 
ATOM   1550 C CA    . GLY A 1 201 ? 33.406  -0.907  45.121 1.00 9.68   ? 243  GLY A CA    1 
ATOM   1551 C C     . GLY A 1 201 ? 31.927  -0.760  44.799 1.00 9.43   ? 243  GLY A C     1 
ATOM   1552 O O     . GLY A 1 201 ? 31.548  -0.577  43.651 1.00 9.16   ? 243  GLY A O     1 
ATOM   1553 N N     . PRO A 1 202 ? 31.035  -0.793  45.817 1.00 10.28  ? 244  PRO A N     1 
ATOM   1554 C CA    . PRO A 1 202 ? 29.594  -0.770  45.592 1.00 9.82   ? 244  PRO A CA    1 
ATOM   1555 C C     . PRO A 1 202 ? 29.210  0.450   44.753 1.00 10.50  ? 244  PRO A C     1 
ATOM   1556 O O     . PRO A 1 202 ? 29.747  1.538   44.968 1.00 10.45  ? 244  PRO A O     1 
ATOM   1557 C CB    . PRO A 1 202 ? 29.001  -0.696  47.015 1.00 11.28  ? 244  PRO A CB    1 
ATOM   1558 C CG    . PRO A 1 202 ? 30.084  -1.115  47.967 1.00 13.14  ? 244  PRO A CG    1 
ATOM   1559 C CD    . PRO A 1 202 ? 31.401  -1.013  47.238 1.00 11.48  ? 244  PRO A CD    1 
ATOM   1560 N N     . TYR A 1 203 ? 28.318  0.245   43.768 1.00 10.35  ? 245  TYR A N     1 
ATOM   1561 C CA    . TYR A 1 203 ? 27.815  1.290   42.896 1.00 9.96   ? 245  TYR A CA    1 
ATOM   1562 C C     . TYR A 1 203 ? 26.680  2.013   43.611 1.00 11.97  ? 245  TYR A C     1 
ATOM   1563 O O     . TYR A 1 203 ? 25.649  1.391   43.910 1.00 11.86  ? 245  TYR A O     1 
ATOM   1564 C CB    . TYR A 1 203 ? 27.276  0.697   41.599 1.00 9.12   ? 245  TYR A CB    1 
ATOM   1565 C CG    . TYR A 1 203 ? 26.535  1.652   40.714 1.00 10.84  ? 245  TYR A CG    1 
ATOM   1566 C CD1   . TYR A 1 203 ? 27.143  2.779   40.233 1.00 9.53   ? 245  TYR A CD1   1 
ATOM   1567 C CD2   . TYR A 1 203 ? 25.213  1.458   40.395 1.00 14.56  ? 245  TYR A CD2   1 
ATOM   1568 C CE1   . TYR A 1 203 ? 26.498  3.657   39.395 1.00 10.69  ? 245  TYR A CE1   1 
ATOM   1569 C CE2   . TYR A 1 203 ? 24.542  2.335   39.555 1.00 16.05  ? 245  TYR A CE2   1 
ATOM   1570 C CZ    . TYR A 1 203 ? 25.196  3.428   39.021 1.00 14.42  ? 245  TYR A CZ    1 
ATOM   1571 O OH    . TYR A 1 203 ? 24.484  4.256   38.155 1.00 13.85  ? 245  TYR A OH    1 
ATOM   1572 N N     . LEU A 1 204 ? 26.904  3.296   43.939 1.00 11.62  ? 246  LEU A N     1 
ATOM   1573 C CA    . LEU A 1 204 ? 26.036  3.996   44.900 1.00 12.79  ? 246  LEU A CA    1 
ATOM   1574 C C     . LEU A 1 204 ? 25.012  4.926   44.254 1.00 11.57  ? 246  LEU A C     1 
ATOM   1575 O O     . LEU A 1 204 ? 24.087  5.321   44.948 1.00 11.10  ? 246  LEU A O     1 
ATOM   1576 C CB    . LEU A 1 204 ? 26.880  4.836   45.849 1.00 13.44  ? 246  LEU A CB    1 
ATOM   1577 C CG    . LEU A 1 204 ? 27.954  4.107   46.666 1.00 14.40  ? 246  LEU A CG    1 
ATOM   1578 C CD1   . LEU A 1 204 ? 28.716  5.082   47.536 1.00 15.36  ? 246  LEU A CD1   1 
ATOM   1579 C CD2   . LEU A 1 204 ? 27.363  2.995   47.470 1.00 15.74  ? 246  LEU A CD2   1 
ATOM   1580 N N     . ASP A 1 205 ? 25.132  5.313   42.976 1.00 11.79  ? 247  ASP A N     1 
ATOM   1581 C CA    . ASP A 1 205 ? 24.364  6.409   42.446 1.00 12.46  ? 247  ASP A CA    1 
ATOM   1582 C C     . ASP A 1 205 ? 22.886  6.071   42.501 1.00 12.40  ? 247  ASP A C     1 
ATOM   1583 O O     . ASP A 1 205 ? 22.069  6.980   42.702 1.00 10.64  ? 247  ASP A O     1 
ATOM   1584 C CB    . ASP A 1 205 ? 24.762  6.785   41.015 1.00 11.57  ? 247  ASP A CB    1 
ATOM   1585 C CG    . ASP A 1 205 ? 26.220  7.175   40.877 1.00 11.33  ? 247  ASP A CG    1 
ATOM   1586 O OD1   . ASP A 1 205 ? 27.075  6.393   41.268 1.00 13.60  ? 247  ASP A OD1   1 
ATOM   1587 O OD2   . ASP A 1 205 ? 26.494  8.260   40.389 1.00 13.31  ? 247  ASP A OD2   1 
ATOM   1588 N N     . GLY A 1 206 ? 22.535  4.805   42.297 1.00 11.72  ? 248  GLY A N     1 
ATOM   1589 C CA    . GLY A 1 206 ? 21.133  4.418   42.339 1.00 12.33  ? 248  GLY A CA    1 
ATOM   1590 C C     . GLY A 1 206 ? 20.426  4.611   43.689 1.00 11.63  ? 248  GLY A C     1 
ATOM   1591 O O     . GLY A 1 206 ? 19.179  4.775   43.747 1.00 10.85  ? 248  GLY A O     1 
ATOM   1592 N N     . LEU A 1 207 ? 21.202  4.628   44.792 1.00 11.79  ? 249  LEU A N     1 
ATOM   1593 C CA    . LEU A 1 207 ? 20.645  4.903   46.100 1.00 13.62  ? 249  LEU A CA    1 
ATOM   1594 C C     . LEU A 1 207 ? 20.056  6.294   46.203 1.00 12.60  ? 249  LEU A C     1 
ATOM   1595 O O     . LEU A 1 207 ? 19.302  6.555   47.139 1.00 14.43  ? 249  LEU A O     1 
ATOM   1596 C CB    . LEU A 1 207 ? 21.713  4.834   47.201 1.00 17.01  ? 249  LEU A CB    1 
ATOM   1597 C CG    . LEU A 1 207 ? 22.282  3.474   47.475 1.00 21.57  ? 249  LEU A CG    1 
ATOM   1598 C CD1   . LEU A 1 207 ? 23.298  3.600   48.595 1.00 18.89  ? 249  LEU A CD1   1 
ATOM   1599 C CD2   . LEU A 1 207 ? 21.184  2.503   47.845 1.00 25.28  ? 249  LEU A CD2   1 
ATOM   1600 N N     . PHE A 1 208 ? 20.459  7.202   45.329 1.00 10.44  ? 250  PHE A N     1 
ATOM   1601 C CA    . PHE A 1 208 ? 20.019  8.596   45.384 1.00 10.64  ? 250  PHE A CA    1 
ATOM   1602 C C     . PHE A 1 208 ? 18.947  8.858   44.321 1.00 12.52  ? 250  PHE A C     1 
ATOM   1603 O O     . PHE A 1 208 ? 18.619  10.037  44.100 1.00 14.32  ? 250  PHE A O     1 
ATOM   1604 C CB    . PHE A 1 208 ? 21.215  9.572   45.287 1.00 11.85  ? 250  PHE A CB    1 
ATOM   1605 C CG    . PHE A 1 208 ? 22.243  9.248   46.347 1.00 10.35  ? 250  PHE A CG    1 
ATOM   1606 C CD1   . PHE A 1 208 ? 21.938  9.565   47.661 1.00 11.84  ? 250  PHE A CD1   1 
ATOM   1607 C CD2   . PHE A 1 208 ? 23.426  8.569   46.114 1.00 10.39  ? 250  PHE A CD2   1 
ATOM   1608 C CE1   . PHE A 1 208 ? 22.786  9.213   48.685 1.00 10.91  ? 250  PHE A CE1   1 
ATOM   1609 C CE2   . PHE A 1 208 ? 24.333  8.277   47.143 1.00 11.41  ? 250  PHE A CE2   1 
ATOM   1610 C CZ    . PHE A 1 208 ? 23.986  8.566   48.441 1.00 11.72  ? 250  PHE A CZ    1 
ATOM   1611 N N     . THR A 1 209 ? 18.396  7.799   43.679 1.00 10.27  ? 251  THR A N     1 
ATOM   1612 C CA    . THR A 1 209 ? 17.278  7.959   42.757 1.00 10.58  ? 251  THR A CA    1 
ATOM   1613 C C     . THR A 1 209 ? 16.027  7.401   43.444 1.00 9.83   ? 251  THR A C     1 
ATOM   1614 O O     . THR A 1 209 ? 16.066  6.354   44.163 1.00 9.25   ? 251  THR A O     1 
ATOM   1615 C CB    . THR A 1 209 ? 17.525  7.283   41.403 1.00 9.59   ? 251  THR A CB    1 
ATOM   1616 O OG1   . THR A 1 209 ? 17.664  5.856   41.593 1.00 11.54  ? 251  THR A OG1   1 
ATOM   1617 C CG2   . THR A 1 209 ? 18.763  7.831   40.731 1.00 11.99  ? 251  THR A CG2   1 
ATOM   1618 N N     . GLN A 1 210 ? 14.913  8.125   43.251 1.00 9.53   ? 252  GLN A N     1 
ATOM   1619 C CA    . GLN A 1 210 ? 13.638  7.880   43.951 1.00 9.56   ? 252  GLN A CA    1 
ATOM   1620 C C     . GLN A 1 210 ? 13.851  7.563   45.427 1.00 9.71   ? 252  GLN A C     1 
ATOM   1621 O O     . GLN A 1 210 ? 13.308  6.590   45.952 1.00 10.71  ? 252  GLN A O     1 
ATOM   1622 C CB    . GLN A 1 210 ? 12.793  6.773   43.297 1.00 10.05  ? 252  GLN A CB    1 
ATOM   1623 C CG    . GLN A 1 210 ? 12.311  7.109   41.884 1.00 10.42  ? 252  GLN A CG    1 
ATOM   1624 C CD    . GLN A 1 210 ? 11.217  6.200   41.376 1.00 11.53  ? 252  GLN A CD    1 
ATOM   1625 O OE1   . GLN A 1 210 ? 10.675  5.370   42.100 1.00 10.68  ? 252  GLN A OE1   1 
ATOM   1626 N NE2   . GLN A 1 210 ? 10.903  6.303   40.096 1.00 10.94  ? 252  GLN A NE2   1 
ATOM   1627 N N     . SER A 1 211 ? 14.601  8.430   46.093 1.00 10.01  ? 253  SER A N     1 
ATOM   1628 C CA    . SER A 1 211 ? 15.001  8.116   47.446 1.00 10.93  ? 253  SER A CA    1 
ATOM   1629 C C     . SER A 1 211 ? 15.093  9.401   48.304 1.00 11.31  ? 253  SER A C     1 
ATOM   1630 O O     . SER A 1 211 ? 14.871  10.533  47.835 1.00 11.76  ? 253  SER A O     1 
ATOM   1631 C CB    . SER A 1 211 ? 16.253  7.317   47.409 1.00 18.55  ? 253  SER A CB    1 
ATOM   1632 O OG    . SER A 1 211 ? 17.343  8.091   47.705 1.00 24.57  ? 253  SER A OG    1 
ATOM   1633 N N     . ASN A 1 212 ? 15.366  9.167   49.591 1.00 11.49  ? 254  ASN A N     1 
ATOM   1634 C CA    . ASN A 1 212 ? 15.536  10.224  50.607 1.00 9.22   ? 254  ASN A CA    1 
ATOM   1635 C C     . ASN A 1 212 ? 16.838  10.000  51.371 1.00 10.02  ? 254  ASN A C     1 
ATOM   1636 O O     . ASN A 1 212 ? 16.906  10.248  52.589 1.00 11.11  ? 254  ASN A O     1 
ATOM   1637 C CB    . ASN A 1 212 ? 14.321  10.318  51.489 1.00 10.24  ? 254  ASN A CB    1 
ATOM   1638 C CG    . ASN A 1 212 ? 13.941  9.029   52.204 1.00 10.78  ? 254  ASN A CG    1 
ATOM   1639 O OD1   . ASN A 1 212 ? 14.594  7.983   52.056 1.00 11.55  ? 254  ASN A OD1   1 
ATOM   1640 N ND2   . ASN A 1 212 ? 12.814  9.063   52.888 1.00 10.90  ? 254  ASN A ND2   1 
ATOM   1641 N N     . PHE A 1 213 ? 17.863  9.556   50.650 1.00 9.45   ? 255  PHE A N     1 
ATOM   1642 C CA    . PHE A 1 213 ? 19.134  9.271   51.299 1.00 10.47  ? 255  PHE A CA    1 
ATOM   1643 C C     . PHE A 1 213 ? 20.166  10.381  51.121 1.00 10.19  ? 255  PHE A C     1 
ATOM   1644 O O     . PHE A 1 213 ? 21.189  10.358  51.808 1.00 11.93  ? 255  PHE A O     1 
ATOM   1645 C CB    . PHE A 1 213 ? 19.701  7.946   50.796 1.00 10.41  ? 255  PHE A CB    1 
ATOM   1646 C CG    . PHE A 1 213 ? 18.821  6.718   50.994 1.00 10.01  ? 255  PHE A CG    1 
ATOM   1647 C CD1   . PHE A 1 213 ? 17.810  6.622   51.958 1.00 10.59  ? 255  PHE A CD1   1 
ATOM   1648 C CD2   . PHE A 1 213 ? 19.031  5.601   50.225 1.00 10.53  ? 255  PHE A CD2   1 
ATOM   1649 C CE1   . PHE A 1 213 ? 17.074  5.443   52.157 1.00 10.24  ? 255  PHE A CE1   1 
ATOM   1650 C CE2   . PHE A 1 213 ? 18.293  4.428   50.442 1.00 9.66   ? 255  PHE A CE2   1 
ATOM   1651 C CZ    . PHE A 1 213 ? 17.277  4.391   51.329 1.00 10.01  ? 255  PHE A CZ    1 
ATOM   1652 N N     . GLY A 1 214 ? 19.909  11.380  50.270 1.00 10.44  ? 256  GLY A N     1 
ATOM   1653 C CA    . GLY A 1 214 ? 20.902  12.386  49.990 1.00 10.23  ? 256  GLY A CA    1 
ATOM   1654 C C     . GLY A 1 214 ? 20.283  13.508  49.177 1.00 10.19  ? 256  GLY A C     1 
ATOM   1655 O O     . GLY A 1 214 ? 19.235  13.329  48.588 1.00 11.30  ? 256  GLY A O     1 
ATOM   1656 N N     . ILE A 1 215 ? 20.934  14.664  49.211 1.00 8.98   ? 257  ILE A N     1 
ATOM   1657 C CA    . ILE A 1 215 ? 20.597  15.816  48.386 1.00 8.99   ? 257  ILE A CA    1 
ATOM   1658 C C     . ILE A 1 215 ? 21.651  15.903  47.282 1.00 9.11   ? 257  ILE A C     1 
ATOM   1659 O O     . ILE A 1 215 ? 22.841  16.111  47.564 1.00 9.54   ? 257  ILE A O     1 
ATOM   1660 C CB    . ILE A 1 215 ? 20.597  17.115  49.195 1.00 10.33  ? 257  ILE A CB    1 
ATOM   1661 C CG1   . ILE A 1 215 ? 19.520  17.089  50.279 1.00 11.20  ? 257  ILE A CG1   1 
ATOM   1662 C CG2   . ILE A 1 215 ? 20.454  18.324  48.288 1.00 11.43  ? 257  ILE A CG2   1 
ATOM   1663 C CD1   . ILE A 1 215 ? 19.766  18.072  51.410 1.00 12.41  ? 257  ILE A CD1   1 
ATOM   1664 N N     . VAL A 1 216 ? 21.230  15.728  46.036 1.00 9.41   ? 258  VAL A N     1 
ATOM   1665 C CA    . VAL A 1 216 ? 22.142  15.796  44.900 1.00 10.91  ? 258  VAL A CA    1 
ATOM   1666 C C     . VAL A 1 216 ? 22.393  17.279  44.591 1.00 10.03  ? 258  VAL A C     1 
ATOM   1667 O O     . VAL A 1 216 ? 21.453  18.036  44.346 1.00 11.41  ? 258  VAL A O     1 
ATOM   1668 C CB    . VAL A 1 216 ? 21.560  15.016  43.706 1.00 10.78  ? 258  VAL A CB    1 
ATOM   1669 C CG1   . VAL A 1 216 ? 22.398  15.202  42.434 1.00 11.72  ? 258  VAL A CG1   1 
ATOM   1670 C CG2   . VAL A 1 216 ? 21.379  13.492  44.020 1.00 11.16  ? 258  VAL A CG2   1 
ATOM   1671 N N     . THR A 1 217 ? 23.679  17.666  44.596 1.00 9.61   ? 259  THR A N     1 
ATOM   1672 C CA    . THR A 1 217 ? 24.116  19.017  44.388 1.00 9.65   ? 259  THR A CA    1 
ATOM   1673 C C     . THR A 1 217 ? 24.772  19.209  43.033 1.00 10.70  ? 259  THR A C     1 
ATOM   1674 O O     . THR A 1 217 ? 24.850  20.342  42.570 1.00 10.39  ? 259  THR A O     1 
ATOM   1675 C CB    . THR A 1 217 ? 25.065  19.416  45.514 1.00 10.62  ? 259  THR A CB    1 
ATOM   1676 O OG1   . THR A 1 217 ? 26.162  18.479  45.549 1.00 11.38  ? 259  THR A OG1   1 
ATOM   1677 C CG2   . THR A 1 217 ? 24.294  19.480  46.817 1.00 11.97  ? 259  THR A CG2   1 
ATOM   1678 N N     . LYS A 1 218 ? 25.217  18.136  42.384 1.00 9.63   ? 260  LYS A N     1 
ATOM   1679 C CA    . LYS A 1 218 ? 25.800  18.214  41.048 1.00 9.59   ? 260  LYS A CA    1 
ATOM   1680 C C     . LYS A 1 218 ? 25.557  16.872  40.382 1.00 9.83   ? 260  LYS A C     1 
ATOM   1681 O O     . LYS A 1 218 ? 25.652  15.852  41.050 1.00 10.18  ? 260  LYS A O     1 
ATOM   1682 C CB    . LYS A 1 218 ? 27.323  18.413  41.078 1.00 10.10  ? 260  LYS A CB    1 
ATOM   1683 C CG    . LYS A 1 218 ? 27.849  19.705  41.717 1.00 10.07  ? 260  LYS A CG    1 
ATOM   1684 C CD    . LYS A 1 218 ? 29.370  19.767  41.885 1.00 10.93  ? 260  LYS A CD    1 
ATOM   1685 C CE    . LYS A 1 218 ? 29.858  21.136  42.360 1.00 12.15  ? 260  LYS A CE    1 
ATOM   1686 N NZ    . LYS A 1 218 ? 29.223  21.527  43.659 1.00 13.36  ? 260  LYS A NZ    1 
ATOM   1687 N N     . MET A 1 219 ? 25.293  16.830  39.067 1.00 9.87   ? 261  MET A N     1 
ATOM   1688 C CA    . MET A 1 219 ? 25.060  15.569  38.371 1.00 9.96   ? 261  MET A CA    1 
ATOM   1689 C C     . MET A 1 219 ? 25.627  15.626  36.970 1.00 9.61   ? 261  MET A C     1 
ATOM   1690 O O     . MET A 1 219 ? 25.427  16.615  36.277 1.00 10.22  ? 261  MET A O     1 
ATOM   1691 C CB    . MET A 1 219 ? 23.577  15.253  38.242 1.00 10.99  ? 261  MET A CB    1 
ATOM   1692 C CG    . MET A 1 219 ? 23.274  13.845  37.829 1.00 11.90  ? 261  MET A CG    1 
ATOM   1693 S SD    . MET A 1 219 ? 21.484  13.573  37.443 1.00 12.47  ? 261  MET A SD    1 
ATOM   1694 C CE    . MET A 1 219 ? 21.459  14.162  35.761 1.00 14.36  ? 261  MET A CE    1 
ATOM   1695 N N     . GLY A 1 220 ? 26.309  14.566  36.578 1.00 9.40   ? 262  GLY A N     1 
ATOM   1696 C CA    . GLY A 1 220 ? 26.843  14.439  35.233 1.00 9.08   ? 262  GLY A CA    1 
ATOM   1697 C C     . GLY A 1 220 ? 25.859  13.688  34.358 1.00 10.81  ? 262  GLY A C     1 
ATOM   1698 O O     . GLY A 1 220 ? 25.120  12.809  34.785 1.00 9.83   ? 262  GLY A O     1 
ATOM   1699 N N     . LEU A 1 221 ? 25.858  14.026  33.072 1.00 10.12  ? 263  LEU A N     1 
ATOM   1700 C CA    . LEU A 1 221 ? 24.897  13.495  32.145 1.00 11.83  ? 263  LEU A CA    1 
ATOM   1701 C C     . LEU A 1 221 ? 25.581  13.309  30.795 1.00 11.58  ? 263  LEU A C     1 
ATOM   1702 O O     . LEU A 1 221 ? 26.257  14.210  30.285 1.00 12.58  ? 263  LEU A O     1 
ATOM   1703 C CB    . LEU A 1 221 ? 23.693  14.441  32.070 1.00 15.01  ? 263  LEU A CB    1 
ATOM   1704 C CG    . LEU A 1 221 ? 22.566  14.045  31.138 1.00 18.43  ? 263  LEU A CG    1 
ATOM   1705 C CD1   . LEU A 1 221 ? 21.993  12.688  31.494 1.00 20.28  ? 263  LEU A CD1   1 
ATOM   1706 C CD2   . LEU A 1 221 ? 21.464  15.079  31.200 1.00 19.12  ? 263  LEU A CD2   1 
ATOM   1707 N N     . TRP A 1 222 ? 25.380  12.179  30.192 1.00 9.60   ? 264  TRP A N     1 
ATOM   1708 C CA    . TRP A 1 222 ? 25.811  11.996  28.794 1.00 9.72   ? 264  TRP A CA    1 
ATOM   1709 C C     . TRP A 1 222 ? 24.817  12.621  27.810 1.00 10.40  ? 264  TRP A C     1 
ATOM   1710 O O     . TRP A 1 222 ? 23.630  12.532  28.014 1.00 10.82  ? 264  TRP A O     1 
ATOM   1711 C CB    . TRP A 1 222 ? 25.998  10.507  28.478 1.00 10.42  ? 264  TRP A CB    1 
ATOM   1712 C CG    . TRP A 1 222 ? 27.118  9.865   29.235 1.00 10.29  ? 264  TRP A CG    1 
ATOM   1713 C CD1   . TRP A 1 222 ? 28.108  10.491  29.960 1.00 10.22  ? 264  TRP A CD1   1 
ATOM   1714 C CD2   . TRP A 1 222 ? 27.319  8.445   29.393 1.00 12.12  ? 264  TRP A CD2   1 
ATOM   1715 N NE1   . TRP A 1 222 ? 28.956  9.520   30.462 1.00 10.75  ? 264  TRP A NE1   1 
ATOM   1716 C CE2   . TRP A 1 222 ? 28.492  8.278   30.157 1.00 11.32  ? 264  TRP A CE2   1 
ATOM   1717 C CE3   . TRP A 1 222 ? 26.648  7.292   28.913 1.00 14.10  ? 264  TRP A CE3   1 
ATOM   1718 C CZ2   . TRP A 1 222 ? 28.995  7.003   30.470 1.00 15.18  ? 264  TRP A CZ2   1 
ATOM   1719 C CZ3   . TRP A 1 222 ? 27.119  6.047   29.265 1.00 19.65  ? 264  TRP A CZ3   1 
ATOM   1720 C CH2   . TRP A 1 222 ? 28.275  5.902   30.035 1.00 19.40  ? 264  TRP A CH2   1 
ATOM   1721 N N     . LEU A 1 223 ? 25.312  13.233  26.710 1.00 10.28  ? 265  LEU A N     1 
ATOM   1722 C CA    . LEU A 1 223 ? 24.506  13.886  25.687 1.00 10.53  ? 265  LEU A CA    1 
ATOM   1723 C C     . LEU A 1 223 ? 24.816  13.271  24.328 1.00 10.70  ? 265  LEU A C     1 
ATOM   1724 O O     . LEU A 1 223 ? 25.967  13.057  23.966 1.00 12.56  ? 265  LEU A O     1 
ATOM   1725 C CB    . LEU A 1 223 ? 24.873  15.390  25.652 1.00 10.95  ? 265  LEU A CB    1 
ATOM   1726 C CG    . LEU A 1 223 ? 24.622  16.182  26.944 1.00 11.18  ? 265  LEU A CG    1 
ATOM   1727 C CD1   . LEU A 1 223 ? 25.169  17.607  26.831 1.00 12.59  ? 265  LEU A CD1   1 
ATOM   1728 C CD2   . LEU A 1 223 ? 23.164  16.201  27.292 1.00 12.63  ? 265  LEU A CD2   1 
ATOM   1729 N N     . MET A 1 224 ? 23.771  13.128  23.517 1.00 11.49  ? 266  MET A N     1 
ATOM   1730 C CA    . MET A 1 224 ? 23.885  12.454  22.231 1.00 12.51  ? 266  MET A CA    1 
ATOM   1731 C C     . MET A 1 224 ? 24.396  13.426  21.174 1.00 13.14  ? 266  MET A C     1 
ATOM   1732 O O     . MET A 1 224 ? 23.871  14.535  21.047 1.00 11.61  ? 266  MET A O     1 
ATOM   1733 C CB    . MET A 1 224 ? 22.536  11.893  21.766 1.00 12.51  ? 266  MET A CB    1 
ATOM   1734 C CG    . MET A 1 224 ? 22.649  11.090  20.497 1.00 14.76  ? 266  MET A CG    1 
ATOM   1735 S SD    . MET A 1 224 ? 21.008  10.466  20.034 1.00 17.66  ? 266  MET A SD    1 
ATOM   1736 C CE    . MET A 1 224 ? 20.333  11.925  19.280 1.00 23.41  ? 266  MET A CE    1 
ATOM   1737 N N     . PRO A 1 225 ? 25.414  13.039  20.381 1.00 11.98  ? 267  PRO A N     1 
ATOM   1738 C CA    . PRO A 1 225 ? 25.805  13.821  19.230 1.00 13.25  ? 267  PRO A CA    1 
ATOM   1739 C C     . PRO A 1 225 ? 24.642  14.050  18.263 1.00 14.65  ? 267  PRO A C     1 
ATOM   1740 O O     . PRO A 1 225 ? 23.844  13.151  17.968 1.00 13.93  ? 267  PRO A O     1 
ATOM   1741 C CB    . PRO A 1 225 ? 26.889  12.970  18.576 1.00 13.21  ? 267  PRO A CB    1 
ATOM   1742 C CG    . PRO A 1 225 ? 27.486  12.194  19.719 1.00 14.31  ? 267  PRO A CG    1 
ATOM   1743 C CD    . PRO A 1 225 ? 26.286  11.872  20.592 1.00 13.20  ? 267  PRO A CD    1 
ATOM   1744 N N     . LYS A 1 226 ? 24.524  15.286  17.786 1.00 15.80  ? 268  LYS A N     1 
ATOM   1745 C CA    . LYS A 1 226 ? 23.544  15.598  16.752 1.00 16.64  ? 268  LYS A CA    1 
ATOM   1746 C C     . LYS A 1 226 ? 23.856  14.776  15.508 1.00 17.29  ? 268  LYS A C     1 
ATOM   1747 O O     . LYS A 1 226 ? 24.965  14.824  14.977 1.00 18.61  ? 268  LYS A O     1 
ATOM   1748 C CB    . LYS A 1 226 ? 23.602  17.099  16.492 1.00 20.02  ? 268  LYS A CB    1 
ATOM   1749 C CG    . LYS A 1 226 ? 22.831  17.656  15.307 1.00 27.27  ? 268  LYS A CG    1 
ATOM   1750 C CD    . LYS A 1 226 ? 23.391  19.067  15.073 1.00 36.03  ? 268  LYS A CD    1 
ATOM   1751 C CE    . LYS A 1 226 ? 22.401  20.095  14.591 1.00 46.12  ? 268  LYS A CE    1 
ATOM   1752 N NZ    . LYS A 1 226 ? 21.922  19.747  13.241 1.00 51.05  ? 268  LYS A NZ    1 
ATOM   1753 N N     . PRO A 1 227 ? 22.887  14.005  15.009 1.00 16.72  ? 269  PRO A N     1 
ATOM   1754 C CA    . PRO A 1 227 ? 23.101  13.174  13.825 1.00 18.31  ? 269  PRO A CA    1 
ATOM   1755 C C     . PRO A 1 227 ? 22.999  14.000  12.546 1.00 19.58  ? 269  PRO A C     1 
ATOM   1756 O O     . PRO A 1 227 ? 22.339  15.027  12.502 1.00 19.79  ? 269  PRO A O     1 
ATOM   1757 C CB    . PRO A 1 227 ? 21.961  12.178  13.957 1.00 20.31  ? 269  PRO A CB    1 
ATOM   1758 C CG    . PRO A 1 227 ? 20.858  13.014  14.515 1.00 19.51  ? 269  PRO A CG    1 
ATOM   1759 C CD    . PRO A 1 227 ? 21.525  13.886  15.555 1.00 16.63  ? 269  PRO A CD    1 
ATOM   1760 N N     . PRO A 1 228 ? 23.694  13.597  11.475 1.00 22.89  ? 270  PRO A N     1 
ATOM   1761 C CA    . PRO A 1 228 ? 23.527  14.278  10.180 1.00 24.40  ? 270  PRO A CA    1 
ATOM   1762 C C     . PRO A 1 228 ? 22.090  14.272  9.660  1.00 21.82  ? 270  PRO A C     1 
ATOM   1763 O O     . PRO A 1 228 ? 21.628  15.269  9.086  1.00 22.87  ? 270  PRO A O     1 
ATOM   1764 C CB    . PRO A 1 228 ? 24.464  13.491  9.250  1.00 24.73  ? 270  PRO A CB    1 
ATOM   1765 C CG    . PRO A 1 228 ? 25.504  12.834  10.174 1.00 27.54  ? 270  PRO A CG    1 
ATOM   1766 C CD    . PRO A 1 228 ? 24.781  12.607  11.493 1.00 27.20  ? 270  PRO A CD    1 
ATOM   1767 N N     . VAL A 1 229 ? 21.422  13.141  9.861  1.00 20.90  ? 271  VAL A N     1 
ATOM   1768 C CA    . VAL A 1 229 ? 20.035  12.956  9.477  1.00 20.94  ? 271  VAL A CA    1 
ATOM   1769 C C     . VAL A 1 229 ? 19.168  12.529  10.678 1.00 17.88  ? 271  VAL A C     1 
ATOM   1770 O O     . VAL A 1 229 ? 19.505  11.590  11.395 1.00 17.87  ? 271  VAL A O     1 
ATOM   1771 C CB    . VAL A 1 229 ? 19.936  11.946  8.323  1.00 21.93  ? 271  VAL A CB    1 
ATOM   1772 C CG1   . VAL A 1 229 ? 18.508  11.641  7.949  1.00 22.24  ? 271  VAL A CG1   1 
ATOM   1773 C CG2   . VAL A 1 229 ? 20.724  12.482  7.131  1.00 23.18  ? 271  VAL A CG2   1 
ATOM   1774 N N     . TYR A 1 230 ? 18.021  13.208  10.778 1.00 17.65  ? 272  TYR A N     1 
ATOM   1775 C CA    . TYR A 1 230 ? 16.941  12.904  11.720 1.00 16.01  ? 272  TYR A CA    1 
ATOM   1776 C C     . TYR A 1 230 ? 15.643  12.737  10.921 1.00 16.89  ? 272  TYR A C     1 
ATOM   1777 O O     . TYR A 1 230 ? 15.239  13.638  10.173 1.00 17.71  ? 272  TYR A O     1 
ATOM   1778 C CB    . TYR A 1 230 ? 16.747  14.087  12.672 1.00 17.10  ? 272  TYR A CB    1 
ATOM   1779 C CG    . TYR A 1 230 ? 15.482  14.050  13.484 1.00 16.47  ? 272  TYR A CG    1 
ATOM   1780 C CD1   . TYR A 1 230 ? 15.234  12.978  14.353 1.00 17.13  ? 272  TYR A CD1   1 
ATOM   1781 C CD2   . TYR A 1 230 ? 14.525  15.042  13.378 1.00 14.35  ? 272  TYR A CD2   1 
ATOM   1782 C CE1   . TYR A 1 230 ? 14.070  12.913  15.117 1.00 15.66  ? 272  TYR A CE1   1 
ATOM   1783 C CE2   . TYR A 1 230 ? 13.360  14.993  14.115 1.00 15.59  ? 272  TYR A CE2   1 
ATOM   1784 C CZ    . TYR A 1 230 ? 13.123  13.915  14.972 1.00 14.45  ? 272  TYR A CZ    1 
ATOM   1785 O OH    . TYR A 1 230 ? 11.941  13.941  15.695 1.00 15.61  ? 272  TYR A OH    1 
ATOM   1786 N N     . LYS A 1 231 ? 15.013  11.591  11.061 1.00 15.76  ? 273  LYS A N     1 
ATOM   1787 C CA    . LYS A 1 231 ? 13.806  11.266  10.315 1.00 15.71  ? 273  LYS A CA    1 
ATOM   1788 C C     . LYS A 1 231 ? 12.707  10.771  11.243 1.00 15.25  ? 273  LYS A C     1 
ATOM   1789 O O     . LYS A 1 231 ? 12.782  9.649   11.714 1.00 16.13  ? 273  LYS A O     1 
ATOM   1790 C CB    . LYS A 1 231 ? 14.069  10.222  9.252  1.00 17.64  ? 273  LYS A CB    1 
ATOM   1791 C CG    . LYS A 1 231 ? 12.859  10.013  8.358  1.00 19.65  ? 273  LYS A CG    1 
ATOM   1792 C CD    . LYS A 1 231 ? 13.138  9.165   7.136  1.00 21.73  ? 273  LYS A CD    1 
ATOM   1793 C CE    . LYS A 1 231 ? 12.005  9.200   6.127  1.00 21.37  ? 273  LYS A CE    1 
ATOM   1794 N NZ    . LYS A 1 231 ? 12.356  8.368   4.951  1.00 23.95  ? 273  LYS A NZ    1 
ATOM   1795 N N     . PRO A 1 232 ? 11.704  11.608  11.565 1.00 14.18  ? 274  PRO A N     1 
ATOM   1796 C CA    . PRO A 1 232 ? 10.586  11.206  12.434 1.00 14.93  ? 274  PRO A CA    1 
ATOM   1797 C C     . PRO A 1 232 ? 9.448   10.502  11.698 1.00 15.20  ? 274  PRO A C     1 
ATOM   1798 O O     . PRO A 1 232 ? 9.235   10.771  10.517 1.00 15.23  ? 274  PRO A O     1 
ATOM   1799 C CB    . PRO A 1 232 ? 10.113  12.544  12.994 1.00 15.21  ? 274  PRO A CB    1 
ATOM   1800 C CG    . PRO A 1 232 ? 10.421  13.556  11.910 1.00 16.78  ? 274  PRO A CG    1 
ATOM   1801 C CD    . PRO A 1 232 ? 11.675  13.048  11.268 1.00 15.34  ? 274  PRO A CD    1 
ATOM   1802 N N     . PHE A 1 233 ? 8.781   9.585   12.389 1.00 14.54  ? 275  PHE A N     1 
ATOM   1803 C CA    . PHE A 1 233 ? 7.681   8.797   11.852 1.00 15.13  ? 275  PHE A CA    1 
ATOM   1804 C C     . PHE A 1 233 ? 6.532   8.732   12.846 1.00 17.24  ? 275  PHE A C     1 
ATOM   1805 O O     . PHE A 1 233 ? 6.710   8.810   14.078 1.00 14.70  ? 275  PHE A O     1 
ATOM   1806 C CB    . PHE A 1 233 ? 8.084   7.353   11.581 1.00 16.78  ? 275  PHE A CB    1 
ATOM   1807 C CG    . PHE A 1 233 ? 9.187   7.126   10.583 1.00 17.32  ? 275  PHE A CG    1 
ATOM   1808 C CD1   . PHE A 1 233 ? 10.508  7.370   10.916 1.00 17.27  ? 275  PHE A CD1   1 
ATOM   1809 C CD2   . PHE A 1 233 ? 8.872   6.724   9.285  1.00 19.15  ? 275  PHE A CD2   1 
ATOM   1810 C CE1   . PHE A 1 233 ? 11.518  7.087   10.024 1.00 18.14  ? 275  PHE A CE1   1 
ATOM   1811 C CE2   . PHE A 1 233 ? 9.883   6.458   8.386  1.00 18.61  ? 275  PHE A CE2   1 
ATOM   1812 C CZ    . PHE A 1 233 ? 11.195  6.663   8.743  1.00 19.64  ? 275  PHE A CZ    1 
ATOM   1813 N N     . MET A 1 234 ? 5.327   8.599   12.281 1.00 17.89  ? 276  MET A N     1 
ATOM   1814 C CA    . MET A 1 234 ? 4.111   8.279   13.023 1.00 18.33  ? 276  MET A CA    1 
ATOM   1815 C C     . MET A 1 234 ? 3.507   6.995   12.454 1.00 18.41  ? 276  MET A C     1 
ATOM   1816 O O     . MET A 1 234 ? 3.455   6.863   11.244 1.00 21.09  ? 276  MET A O     1 
ATOM   1817 C CB    . MET A 1 234 ? 3.116   9.429   12.880 1.00 17.98  ? 276  MET A CB    1 
ATOM   1818 C CG    . MET A 1 234 ? 1.706   9.131   13.330 1.00 23.86  ? 276  MET A CG    1 
ATOM   1819 S SD    . MET A 1 234 ? 0.717   10.675  13.052 1.00 32.04  ? 276  MET A SD    1 
ATOM   1820 C CE    . MET A 1 234 ? -0.948  10.117  13.448 1.00 24.78  ? 276  MET A CE    1 
ATOM   1821 N N     . VAL A 1 235 ? 3.071   6.066   13.309 1.00 16.64  ? 277  VAL A N     1 
ATOM   1822 C CA    . VAL A 1 235 ? 2.336   4.901   12.865 1.00 16.44  ? 277  VAL A CA    1 
ATOM   1823 C C     . VAL A 1 235 ? 0.913   5.036   13.382 1.00 17.15  ? 277  VAL A C     1 
ATOM   1824 O O     . VAL A 1 235 ? 0.679   5.115   14.586 1.00 16.11  ? 277  VAL A O     1 
ATOM   1825 C CB    . VAL A 1 235 ? 2.950   3.587   13.333 1.00 21.62  ? 277  VAL A CB    1 
ATOM   1826 C CG1   . VAL A 1 235 ? 2.377   2.412   12.579 1.00 21.01  ? 277  VAL A CG1   1 
ATOM   1827 C CG2   . VAL A 1 235 ? 4.432   3.615   13.190 1.00 26.69  ? 277  VAL A CG2   1 
ATOM   1828 N N     . ARG A 1 236 ? -0.053  4.923   12.474 1.00 15.83  ? 278  ARG A N     1 
ATOM   1829 C CA    . ARG A 1 236 ? -1.446  5.041   12.822 1.00 17.33  ? 278  ARG A CA    1 
ATOM   1830 C C     . ARG A 1 236 ? -2.095  3.659   12.800 1.00 17.33  ? 278  ARG A C     1 
ATOM   1831 O O     . ARG A 1 236 ? -2.004  2.949   11.783 1.00 17.55  ? 278  ARG A O     1 
ATOM   1832 C CB    . ARG A 1 236 ? -2.044  6.040   11.814 1.00 21.09  ? 278  ARG A CB    1 
ATOM   1833 C CG    . ARG A 1 236 ? -3.539  6.234   11.872 1.00 25.71  ? 278  ARG A CG    1 
ATOM   1834 C CD    . ARG A 1 236 ? -3.903  7.565   11.179 1.00 27.45  ? 278  ARG A CD    1 
ATOM   1835 N NE    . ARG A 1 236 ? -3.591  7.514   9.763  1.00 28.02  ? 278  ARG A NE    1 
ATOM   1836 C CZ    . ARG A 1 236 ? -3.650  8.530   8.887  1.00 28.88  ? 278  ARG A CZ    1 
ATOM   1837 N NH1   . ARG A 1 236 ? -3.653  9.797   9.271  1.00 23.58  ? 278  ARG A NH1   1 
ATOM   1838 N NH2   . ARG A 1 236 ? -3.609  8.246   7.590  1.00 27.23  ? 278  ARG A NH2   1 
ATOM   1839 N N     . HIS A 1 237 ? -2.740  3.280   13.915 1.00 15.25  ? 279  HIS A N     1 
ATOM   1840 C CA    . HIS A 1 237 ? -3.516  2.063   14.015 1.00 15.17  ? 279  HIS A CA    1 
ATOM   1841 C C     . HIS A 1 237 ? -4.977  2.444   14.187 1.00 15.33  ? 279  HIS A C     1 
ATOM   1842 O O     . HIS A 1 237 ? -5.292  3.337   14.949 1.00 18.09  ? 279  HIS A O     1 
ATOM   1843 C CB    . HIS A 1 237 ? -2.996  1.126   15.118 1.00 15.16  ? 279  HIS A CB    1 
ATOM   1844 C CG    . HIS A 1 237 ? -1.774  0.346   14.744 1.00 14.82  ? 279  HIS A CG    1 
ATOM   1845 N ND1   . HIS A 1 237 ? -0.478  0.814   14.815 1.00 14.77  ? 279  HIS A ND1   1 
ATOM   1846 C CD2   . HIS A 1 237 ? -1.681  -0.934  14.330 1.00 17.42  ? 279  HIS A CD2   1 
ATOM   1847 C CE1   . HIS A 1 237 ? 0.371   -0.141  14.435 1.00 15.68  ? 279  HIS A CE1   1 
ATOM   1848 N NE2   . HIS A 1 237 ? -0.354  -1.225  14.150 1.00 16.96  ? 279  HIS A NE2   1 
ATOM   1849 N N     . ALA A 1 238 ? -5.885  1.727   13.517 1.00 19.31  ? 280  ALA A N     1 
ATOM   1850 C CA    . ALA A 1 238 ? -7.265  2.191   13.382 1.00 20.00  ? 280  ALA A CA    1 
ATOM   1851 C C     . ALA A 1 238 ? -8.156  1.836   14.566 1.00 22.74  ? 280  ALA A C     1 
ATOM   1852 O O     . ALA A 1 238 ? -9.131  2.541   14.801 1.00 23.28  ? 280  ALA A O     1 
ATOM   1853 C CB    . ALA A 1 238 ? -7.846  1.637   12.078 1.00 18.63  ? 280  ALA A CB    1 
ATOM   1854 N N     . ASN A 1 239 ? -7.825  0.790   15.345 1.00 19.28  ? 281  ASN A N     1 
ATOM   1855 C CA    . ASN A 1 239 ? -8.759  0.234   16.300 1.00 19.20  ? 281  ASN A CA    1 
ATOM   1856 C C     . ASN A 1 239 ? -8.214  0.264   17.735 1.00 20.69  ? 281  ASN A C     1 
ATOM   1857 O O     . ASN A 1 239 ? -7.022  -0.022  17.945 1.00 18.75  ? 281  ASN A O     1 
ATOM   1858 C CB    . ASN A 1 239 ? -9.082  -1.239  15.984 1.00 24.79  ? 281  ASN A CB    1 
ATOM   1859 C CG    . ASN A 1 239 ? -9.209  -1.570  14.499 1.00 32.90  ? 281  ASN A CG    1 
ATOM   1860 O OD1   . ASN A 1 239 ? -8.418  -2.342  13.931 1.00 37.69  ? 281  ASN A OD1   1 
ATOM   1861 N ND2   . ASN A 1 239 ? -10.213 -0.994  13.861 1.00 25.88  ? 281  ASN A ND2   1 
ATOM   1862 N N     . MET A 1 240 ? -9.126  0.481   18.709 1.00 19.17  ? 282  MET A N     1 
ATOM   1863 C CA    . MET A 1 240 ? -8.789  0.382   20.126 1.00 20.60  ? 282  MET A CA    1 
ATOM   1864 C C     . MET A 1 240 ? -8.151  -0.971  20.442 1.00 21.37  ? 282  MET A C     1 
ATOM   1865 O O     . MET A 1 240 ? -7.245  -1.062  21.277 1.00 19.21  ? 282  MET A O     1 
ATOM   1866 C CB    . MET A 1 240 ? -10.022 0.582   21.028 1.00 22.64  ? 282  MET A CB    1 
ATOM   1867 C CG    . MET A 1 240 ? -9.799  0.312   22.535 1.00 25.19  ? 282  MET A CG    1 
ATOM   1868 S SD    . MET A 1 240 ? -8.570  1.334   23.482 1.00 27.37  ? 282  MET A SD    1 
ATOM   1869 C CE    . MET A 1 240 ? -9.548  2.779   23.914 1.00 30.08  ? 282  MET A CE    1 
ATOM   1870 N N     . GLU A 1 241 ? -8.632  -2.038  19.792 1.00 21.65  ? 283  GLU A N     1 
ATOM   1871 C CA    . GLU A 1 241 ? -8.169  -3.373  20.130 1.00 23.03  ? 283  GLU A CA    1 
ATOM   1872 C C     . GLU A 1 241 ? -6.819  -3.718  19.494 1.00 19.89  ? 283  GLU A C     1 
ATOM   1873 O O     . GLU A 1 241 ? -6.322  -4.832  19.680 1.00 20.01  ? 283  GLU A O     1 
ATOM   1874 C CB    . GLU A 1 241 ? -9.246  -4.409  19.806 1.00 26.48  ? 283  GLU A CB    1 
ATOM   1875 C CG    . GLU A 1 241 ? -9.596  -4.496  18.347 1.00 30.28  ? 283  GLU A CG    1 
ATOM   1876 C CD    . GLU A 1 241 ? -10.676 -3.535  17.838 1.00 38.13  ? 283  GLU A CD    1 
ATOM   1877 O OE1   . GLU A 1 241 ? -11.014 -2.479  18.515 1.00 30.12  ? 283  GLU A OE1   1 
ATOM   1878 O OE2   . GLU A 1 241 ? -11.193 -3.841  16.721 1.00 46.54  ? 283  GLU A OE2   1 
ATOM   1879 N N     . ASP A 1 242 ? -6.189  -2.809  18.739 1.00 18.73  ? 284  ASP A N     1 
ATOM   1880 C CA    . ASP A 1 242 ? -4.906  -3.078  18.103 1.00 18.03  ? 284  ASP A CA    1 
ATOM   1881 C C     . ASP A 1 242 ? -3.733  -3.143  19.112 1.00 18.48  ? 284  ASP A C     1 
ATOM   1882 O O     . ASP A 1 242 ? -2.629  -3.546  18.732 1.00 18.51  ? 284  ASP A O     1 
ATOM   1883 C CB    . ASP A 1 242 ? -4.584  -2.050  17.021 1.00 18.76  ? 284  ASP A CB    1 
ATOM   1884 C CG    . ASP A 1 242 ? -5.439  -2.200  15.760 1.00 24.30  ? 284  ASP A CG    1 
ATOM   1885 O OD1   . ASP A 1 242 ? -6.032  -3.272  15.621 1.00 24.99  ? 284  ASP A OD1   1 
ATOM   1886 O OD2   . ASP A 1 242 ? -5.559  -1.224  15.009 1.00 20.55  ? 284  ASP A OD2   1 
ATOM   1887 N N     . VAL A 1 243 ? -3.965  -2.743  20.356 1.00 17.09  ? 285  VAL A N     1 
ATOM   1888 C CA    . VAL A 1 243 ? -2.911  -2.698  21.380 1.00 17.17  ? 285  VAL A CA    1 
ATOM   1889 C C     . VAL A 1 243 ? -1.931  -3.869  21.245 1.00 16.53  ? 285  VAL A C     1 
ATOM   1890 O O     . VAL A 1 243 ? -0.745  -3.610  21.070 1.00 17.00  ? 285  VAL A O     1 
ATOM   1891 C CB    . VAL A 1 243 ? -3.471  -2.591  22.802 1.00 17.97  ? 285  VAL A CB    1 
ATOM   1892 C CG1   . VAL A 1 243 ? -2.426  -2.843  23.888 1.00 17.64  ? 285  VAL A CG1   1 
ATOM   1893 C CG2   . VAL A 1 243 ? -4.096  -1.226  23.051 1.00 18.66  ? 285  VAL A CG2   1 
ATOM   1894 N N     . PRO A 1 244 ? -2.320  -5.163  21.416 1.00 17.46  ? 286  PRO A N     1 
ATOM   1895 C CA    . PRO A 1 244 ? -1.343  -6.249  21.448 1.00 17.17  ? 286  PRO A CA    1 
ATOM   1896 C C     . PRO A 1 244 ? -0.535  -6.333  20.167 1.00 16.98  ? 286  PRO A C     1 
ATOM   1897 O O     . PRO A 1 244 ? 0.650   -6.660  20.233 1.00 15.42  ? 286  PRO A O     1 
ATOM   1898 C CB    . PRO A 1 244 ? -2.150  -7.536  21.670 1.00 18.95  ? 286  PRO A CB    1 
ATOM   1899 C CG    . PRO A 1 244 ? -3.542  -7.174  21.206 1.00 17.46  ? 286  PRO A CG    1 
ATOM   1900 C CD    . PRO A 1 244 ? -3.680  -5.697  21.610 1.00 17.21  ? 286  PRO A CD    1 
ATOM   1901 N N     . LYS A 1 245 ? -1.149  -6.058  18.992 1.00 15.70  ? 287  LYS A N     1 
ATOM   1902 C CA    . LYS A 1 245 ? -0.403  -6.189  17.760 1.00 15.24  ? 287  LYS A CA    1 
ATOM   1903 C C     . LYS A 1 245 ? 0.681   -5.111  17.626 1.00 15.19  ? 287  LYS A C     1 
ATOM   1904 O O     . LYS A 1 245 ? 1.717   -5.362  17.022 1.00 14.29  ? 287  LYS A O     1 
ATOM   1905 C CB    . LYS A 1 245 ? -1.332  -6.085  16.545 1.00 21.61  ? 287  LYS A CB    1 
ATOM   1906 C CG    . LYS A 1 245 ? -2.455  -7.111  16.416 1.00 26.45  ? 287  LYS A CG    1 
ATOM   1907 C CD    . LYS A 1 245 ? -3.204  -6.917  15.062 1.00 31.59  ? 287  LYS A CD    1 
ATOM   1908 C CE    . LYS A 1 245 ? -3.864  -5.547  14.976 1.00 40.65  ? 287  LYS A CE    1 
ATOM   1909 N NZ    . LYS A 1 245 ? -4.077  -5.015  13.593 1.00 46.82  ? 287  LYS A NZ    1 
ATOM   1910 N N     . ILE A 1 246 ? 0.444   -3.896  18.170 1.00 15.44  ? 288  ILE A N     1 
ATOM   1911 C CA    . ILE A 1 246 ? 1.417   -2.807  18.121 1.00 14.29  ? 288  ILE A CA    1 
ATOM   1912 C C     . ILE A 1 246 ? 2.665   -3.168  18.930 1.00 14.83  ? 288  ILE A C     1 
ATOM   1913 O O     . ILE A 1 246 ? 3.816   -3.015  18.485 1.00 15.74  ? 288  ILE A O     1 
ATOM   1914 C CB    . ILE A 1 246 ? 0.817   -1.479  18.604 1.00 15.25  ? 288  ILE A CB    1 
ATOM   1915 C CG1   . ILE A 1 246 ? -0.463  -1.108  17.828 1.00 16.31  ? 288  ILE A CG1   1 
ATOM   1916 C CG2   . ILE A 1 246 ? 1.862   -0.389  18.537 1.00 18.65  ? 288  ILE A CG2   1 
ATOM   1917 C CD1   . ILE A 1 246 ? -1.306  0.056   18.424 1.00 15.85  ? 288  ILE A CD1   1 
ATOM   1918 N N     . ILE A 1 247 ? 2.422   -3.664  20.144 1.00 14.18  ? 289  ILE A N     1 
ATOM   1919 C CA    . ILE A 1 247 ? 3.539   -4.035  21.011 1.00 14.95  ? 289  ILE A CA    1 
ATOM   1920 C C     . ILE A 1 247 ? 4.310   -5.198  20.381 1.00 15.11  ? 289  ILE A C     1 
ATOM   1921 O O     . ILE A 1 247 ? 5.526   -5.170  20.371 1.00 14.57  ? 289  ILE A O     1 
ATOM   1922 C CB    . ILE A 1 247 ? 3.034   -4.373  22.429 1.00 14.73  ? 289  ILE A CB    1 
ATOM   1923 C CG1   . ILE A 1 247 ? 2.327   -3.200  23.129 1.00 15.55  ? 289  ILE A CG1   1 
ATOM   1924 C CG2   . ILE A 1 247 ? 4.164   -4.941  23.311 1.00 16.28  ? 289  ILE A CG2   1 
ATOM   1925 C CD1   . ILE A 1 247 ? 3.084   -1.943  23.223 1.00 16.24  ? 289  ILE A CD1   1 
ATOM   1926 N N     . GLU A 1 248 ? 3.617   -6.214  19.849 1.00 14.78  ? 290  GLU A N     1 
ATOM   1927 C CA    . GLU A 1 248 ? 4.302   -7.357  19.241 1.00 15.66  ? 290  GLU A CA    1 
ATOM   1928 C C     . GLU A 1 248 ? 5.104   -6.950  18.019 1.00 16.40  ? 290  GLU A C     1 
ATOM   1929 O O     . GLU A 1 248 ? 6.130   -7.586  17.763 1.00 20.34  ? 290  GLU A O     1 
ATOM   1930 C CB    . GLU A 1 248 ? 3.330   -8.483  18.881 1.00 13.63  ? 290  GLU A CB    1 
ATOM   1931 C CG    . GLU A 1 248 ? 2.844   -9.206  20.148 1.00 14.91  ? 290  GLU A CG    1 
ATOM   1932 C CD    . GLU A 1 248 ? 3.994   -9.778  20.993 1.00 17.27  ? 290  GLU A CD    1 
ATOM   1933 O OE1   . GLU A 1 248 ? 4.903   -10.499 20.408 1.00 18.39  ? 290  GLU A OE1   1 
ATOM   1934 O OE2   . GLU A 1 248 ? 4.059   -9.523  22.220 1.00 17.82  ? 290  GLU A OE2   1 
ATOM   1935 N N     . ALA A 1 249 ? 4.647   -5.916  17.283 1.00 15.87  ? 291  ALA A N     1 
ATOM   1936 C CA    . ALA A 1 249 ? 5.408   -5.416  16.138 1.00 16.08  ? 291  ALA A CA    1 
ATOM   1937 C C     . ALA A 1 249 ? 6.644   -4.626  16.580 1.00 14.49  ? 291  ALA A C     1 
ATOM   1938 O O     . ALA A 1 249 ? 7.708   -4.694  15.997 1.00 15.72  ? 291  ALA A O     1 
ATOM   1939 C CB    . ALA A 1 249 ? 4.497   -4.579  15.233 1.00 16.77  ? 291  ALA A CB    1 
ATOM   1940 N N     . MET A 1 250 ? 6.480   -3.759  17.574 1.00 15.19  ? 292  MET A N     1 
ATOM   1941 C CA    . MET A 1 250 ? 7.574   -2.891  17.949 1.00 15.16  ? 292  MET A CA    1 
ATOM   1942 C C     . MET A 1 250 ? 8.658   -3.665  18.700 1.00 15.18  ? 292  MET A C     1 
ATOM   1943 O O     . MET A 1 250 ? 9.834   -3.294  18.583 1.00 15.08  ? 292  MET A O     1 
ATOM   1944 C CB    . MET A 1 250 ? 7.076   -1.760  18.849 1.00 17.00  ? 292  MET A CB    1 
ATOM   1945 C CG    . MET A 1 250 ? 6.201   -0.750  18.111 1.00 17.76  ? 292  MET A CG    1 
ATOM   1946 S SD    . MET A 1 250 ? 7.074   0.205   16.861 1.00 19.08  ? 292  MET A SD    1 
ATOM   1947 C CE    . MET A 1 250 ? 8.150   1.233   17.877 1.00 23.67  ? 292  MET A CE    1 
ATOM   1948 N N     . ARG A 1 251 ? 8.244   -4.650  19.523 1.00 15.88  ? 293  ARG A N     1 
ATOM   1949 C CA    . ARG A 1 251 ? 9.160   -5.369  20.409 1.00 16.14  ? 293  ARG A CA    1 
ATOM   1950 C C     . ARG A 1 251 ? 10.388  -5.863  19.646 1.00 15.30  ? 293  ARG A C     1 
ATOM   1951 O O     . ARG A 1 251 ? 11.534  -5.590  20.029 1.00 14.74  ? 293  ARG A O     1 
ATOM   1952 C CB    . ARG A 1 251 ? 8.459   -6.520  21.135 1.00 16.28  ? 293  ARG A CB    1 
ATOM   1953 C CG    . ARG A 1 251 ? 9.365   -7.265  22.107 1.00 18.27  ? 293  ARG A CG    1 
ATOM   1954 C CD    . ARG A 1 251 ? 9.889   -8.569  21.586 1.00 20.03  ? 293  ARG A CD    1 
ATOM   1955 N NE    . ARG A 1 251 ? 8.855   -9.557  21.324 1.00 21.24  ? 293  ARG A NE    1 
ATOM   1956 C CZ    . ARG A 1 251 ? 8.864   -10.395 20.284 1.00 21.58  ? 293  ARG A CZ    1 
ATOM   1957 N NH1   . ARG A 1 251 ? 7.765   -11.040 20.011 1.00 24.51  ? 293  ARG A NH1   1 
ATOM   1958 N NH2   . ARG A 1 251 ? 9.937   -10.572 19.530 1.00 21.96  ? 293  ARG A NH2   1 
ATOM   1959 N N     . PRO A 1 252 ? 10.246  -6.625  18.525 1.00 14.95  ? 294  PRO A N     1 
ATOM   1960 C CA    . PRO A 1 252 ? 11.450  -7.088  17.838 1.00 16.40  ? 294  PRO A CA    1 
ATOM   1961 C C     . PRO A 1 252 ? 12.345  -5.963  17.322 1.00 15.93  ? 294  PRO A C     1 
ATOM   1962 O O     . PRO A 1 252 ? 13.576  -6.110  17.270 1.00 17.25  ? 294  PRO A O     1 
ATOM   1963 C CB    . PRO A 1 252 ? 10.933  -7.971  16.675 1.00 17.32  ? 294  PRO A CB    1 
ATOM   1964 C CG    . PRO A 1 252 ? 9.481   -7.530  16.530 1.00 17.64  ? 294  PRO A CG    1 
ATOM   1965 C CD    . PRO A 1 252 ? 9.001   -7.116  17.914 1.00 17.35  ? 294  PRO A CD    1 
ATOM   1966 N N     . LEU A 1 253 ? 11.736  -4.846  16.878 1.00 15.62  ? 295  LEU A N     1 
ATOM   1967 C CA    . LEU A 1 253 ? 12.481  -3.713  16.363 1.00 13.90  ? 295  LEU A CA    1 
ATOM   1968 C C     . LEU A 1 253 ? 13.308  -3.067  17.465 1.00 15.73  ? 295  LEU A C     1 
ATOM   1969 O O     . LEU A 1 253 ? 14.429  -2.656  17.205 1.00 17.58  ? 295  LEU A O     1 
ATOM   1970 C CB    . LEU A 1 253 ? 11.521  -2.671  15.776 1.00 15.03  ? 295  LEU A CB    1 
ATOM   1971 C CG    . LEU A 1 253 ? 10.629  -3.161  14.645 1.00 16.04  ? 295  LEU A CG    1 
ATOM   1972 C CD1   . LEU A 1 253 ? 9.735   -2.011  14.156 1.00 17.10  ? 295  LEU A CD1   1 
ATOM   1973 C CD2   . LEU A 1 253 ? 11.455  -3.724  13.510 1.00 17.98  ? 295  LEU A CD2   1 
ATOM   1974 N N     . ARG A 1 254 ? 12.789  -3.084  18.700 1.00 14.65  ? 296  ARG A N     1 
ATOM   1975 C CA    . ARG A 1 254 ? 13.509  -2.506  19.831 1.00 15.40  ? 296  ARG A CA    1 
ATOM   1976 C C     . ARG A 1 254 ? 14.524  -3.499  20.413 1.00 14.82  ? 296  ARG A C     1 
ATOM   1977 O O     . ARG A 1 254 ? 15.647  -3.112  20.672 1.00 18.48  ? 296  ARG A O     1 
ATOM   1978 C CB    . ARG A 1 254 ? 12.572  -2.056  20.944 1.00 16.37  ? 296  ARG A CB    1 
ATOM   1979 C CG    . ARG A 1 254 ? 11.601  -0.953  20.569 1.00 16.39  ? 296  ARG A CG    1 
ATOM   1980 C CD    . ARG A 1 254 ? 12.268  0.302   20.060 1.00 18.27  ? 296  ARG A CD    1 
ATOM   1981 N NE    . ARG A 1 254 ? 13.261  0.719   21.066 1.00 19.41  ? 296  ARG A NE    1 
ATOM   1982 C CZ    . ARG A 1 254 ? 12.910  1.297   22.200 1.00 20.61  ? 296  ARG A CZ    1 
ATOM   1983 N NH1   . ARG A 1 254 ? 11.677  1.718   22.353 1.00 20.65  ? 296  ARG A NH1   1 
ATOM   1984 N NH2   . ARG A 1 254 ? 13.801  1.490   23.147 1.00 21.47  ? 296  ARG A NH2   1 
ATOM   1985 N N     . VAL A 1 255 ? 14.156  -4.759  20.605 1.00 14.84  ? 297  VAL A N     1 
ATOM   1986 C CA    . VAL A 1 255 ? 15.118  -5.724  21.147 1.00 15.37  ? 297  VAL A CA    1 
ATOM   1987 C C     . VAL A 1 255 ? 16.345  -5.799  20.235 1.00 18.81  ? 297  VAL A C     1 
ATOM   1988 O O     . VAL A 1 255 ? 17.464  -5.880  20.735 1.00 20.39  ? 297  VAL A O     1 
ATOM   1989 C CB    . VAL A 1 255 ? 14.455  -7.086  21.428 1.00 18.69  ? 297  VAL A CB    1 
ATOM   1990 C CG1   . VAL A 1 255 ? 15.466  -8.175  21.784 1.00 18.96  ? 297  VAL A CG1   1 
ATOM   1991 C CG2   . VAL A 1 255 ? 13.389  -7.006  22.516 1.00 18.10  ? 297  VAL A CG2   1 
ATOM   1992 N N     . SER A 1 256 ? 16.167  -5.754  18.896 1.00 18.65  ? 298  SER A N     1 
ATOM   1993 C CA    . SER A 1 256 ? 17.298  -5.777  17.963 1.00 19.63  ? 298  SER A CA    1 
ATOM   1994 C C     . SER A 1 256 ? 17.868  -4.395  17.700 1.00 20.36  ? 298  SER A C     1 
ATOM   1995 O O     . SER A 1 256 ? 18.810  -4.277  16.925 1.00 22.10  ? 298  SER A O     1 
ATOM   1996 C CB    . SER A 1 256 ? 16.973  -6.388  16.622 1.00 22.30  ? 298  SER A CB    1 
ATOM   1997 O OG    . SER A 1 256 ? 16.795  -7.786  16.762 1.00 28.54  ? 298  SER A OG    1 
ATOM   1998 N N     . ASN A 1 257 ? 17.287  -3.362  18.295 1.00 20.55  ? 299  ASN A N     1 
ATOM   1999 C CA    . ASN A 1 257 ? 17.780  -2.005  18.185 1.00 21.57  ? 299  ASN A CA    1 
ATOM   2000 C C     . ASN A 1 257 ? 17.817  -1.493  16.736 1.00 21.78  ? 299  ASN A C     1 
ATOM   2001 O O     . ASN A 1 257 ? 18.650  -0.667  16.393 1.00 23.39  ? 299  ASN A O     1 
ATOM   2002 C CB    . ASN A 1 257 ? 19.120  -1.869  18.934 1.00 27.04  ? 299  ASN A CB    1 
ATOM   2003 C CG    . ASN A 1 257 ? 19.373  -0.437  19.363 1.00 28.20  ? 299  ASN A CG    1 
ATOM   2004 O OD1   . ASN A 1 257 ? 18.508  0.219   19.942 1.00 30.58  ? 299  ASN A OD1   1 
ATOM   2005 N ND2   . ASN A 1 257 ? 20.556  0.068   19.089 1.00 34.90  ? 299  ASN A ND2   1 
ATOM   2006 N N     . LEU A 1 258 ? 16.835  -1.868  15.901 1.00 18.40  ? 300  LEU A N     1 
ATOM   2007 C CA    . LEU A 1 258 ? 16.590  -1.176  14.638 1.00 16.92  ? 300  LEU A CA    1 
ATOM   2008 C C     . LEU A 1 258 ? 15.941  0.189   14.873 1.00 16.86  ? 300  LEU A C     1 
ATOM   2009 O O     . LEU A 1 258 ? 16.105  1.084   14.048 1.00 16.86  ? 300  LEU A O     1 
ATOM   2010 C CB    . LEU A 1 258 ? 15.645  -1.990  13.753 1.00 20.12  ? 300  LEU A CB    1 
ATOM   2011 C CG    . LEU A 1 258 ? 16.241  -3.221  13.055 1.00 25.27  ? 300  LEU A CG    1 
ATOM   2012 C CD1   . LEU A 1 258 ? 16.324  -4.415  13.958 1.00 26.48  ? 300  LEU A CD1   1 
ATOM   2013 C CD2   . LEU A 1 258 ? 15.426  -3.586  11.826 1.00 28.52  ? 300  LEU A CD2   1 
ATOM   2014 N N     . VAL A 1 259 ? 15.133  0.279   15.947 1.00 16.58  ? 301  VAL A N     1 
ATOM   2015 C CA    . VAL A 1 259 ? 14.601  1.520   16.480 1.00 16.71  ? 301  VAL A CA    1 
ATOM   2016 C C     . VAL A 1 259 ? 15.171  1.657   17.891 1.00 14.22  ? 301  VAL A C     1 
ATOM   2017 O O     . VAL A 1 259 ? 15.154  0.680   18.646 1.00 15.43  ? 301  VAL A O     1 
ATOM   2018 C CB    . VAL A 1 259 ? 13.057  1.568   16.476 1.00 16.35  ? 301  VAL A CB    1 
ATOM   2019 C CG1   . VAL A 1 259 ? 12.506  2.800   17.193 1.00 16.89  ? 301  VAL A CG1   1 
ATOM   2020 C CG2   . VAL A 1 259 ? 12.471  1.479   15.053 1.00 16.47  ? 301  VAL A CG2   1 
ATOM   2021 N N     . ALA A 1 260 ? 15.700  2.843   18.201 1.00 15.20  ? 302  ALA A N     1 
ATOM   2022 C CA    . ALA A 1 260 ? 16.459  3.010   19.450 1.00 15.79  ? 302  ALA A CA    1 
ATOM   2023 C C     . ALA A 1 260 ? 15.855  4.016   20.414 1.00 16.40  ? 302  ALA A C     1 
ATOM   2024 O O     . ALA A 1 260 ? 16.242  3.991   21.600 1.00 15.69  ? 302  ALA A O     1 
ATOM   2025 C CB    . ALA A 1 260 ? 17.893  3.392   19.203 1.00 18.31  ? 302  ALA A CB    1 
ATOM   2026 N N     . ASN A 1 261 ? 14.973  4.893   19.912 1.00 14.93  ? 303  ASN A N     1 
ATOM   2027 C CA    . ASN A 1 261 ? 14.383  5.895   20.792 1.00 14.51  ? 303  ASN A CA    1 
ATOM   2028 C C     . ASN A 1 261 ? 13.184  5.300   21.526 1.00 13.60  ? 303  ASN A C     1 
ATOM   2029 O O     . ASN A 1 261 ? 12.483  4.453   21.029 1.00 12.08  ? 303  ASN A O     1 
ATOM   2030 C CB    . ASN A 1 261 ? 14.027  7.215   20.106 1.00 13.29  ? 303  ASN A CB    1 
ATOM   2031 C CG    . ASN A 1 261 ? 12.914  7.159   19.089 1.00 14.96  ? 303  ASN A CG    1 
ATOM   2032 O OD1   . ASN A 1 261 ? 12.792  6.203   18.318 1.00 15.24  ? 303  ASN A OD1   1 
ATOM   2033 N ND2   . ASN A 1 261 ? 12.099  8.198   19.111 1.00 12.44  ? 303  ASN A ND2   1 
ATOM   2034 N N     . CYS A 1 262 ? 12.905  5.824   22.711 1.00 13.57  ? 304  CYS A N     1 
ATOM   2035 C CA    . CYS A 1 262 ? 11.689  5.478   23.409 1.00 12.44  ? 304  CYS A CA    1 
ATOM   2036 C C     . CYS A 1 262 ? 10.478  5.950   22.586 1.00 12.80  ? 304  CYS A C     1 
ATOM   2037 O O     . CYS A 1 262 ? 10.474  7.091   22.091 1.00 12.57  ? 304  CYS A O     1 
ATOM   2038 C CB    . CYS A 1 262 ? 11.739  6.091   24.806 1.00 13.01  ? 304  CYS A CB    1 
ATOM   2039 S SG    . CYS A 1 262 ? 10.227  5.809   25.750 1.00 17.27  ? 304  CYS A SG    1 
ATOM   2040 N N     . ASN A 1 263 ? 9.476   5.066   22.396 1.00 12.88  ? 305  ASN A N     1 
ATOM   2041 C CA    . ASN A 1 263 ? 8.349   5.317   21.483 1.00 13.86  ? 305  ASN A CA    1 
ATOM   2042 C C     . ASN A 1 263 ? 7.065   5.538   22.260 1.00 14.59  ? 305  ASN A C     1 
ATOM   2043 O O     . ASN A 1 263 ? 6.623   4.646   22.970 1.00 14.80  ? 305  ASN A O     1 
ATOM   2044 C CB    . ASN A 1 263 ? 8.135   4.084   20.578 1.00 12.89  ? 305  ASN A CB    1 
ATOM   2045 C CG    . ASN A 1 263 ? 9.451   3.634   20.009 1.00 13.62  ? 305  ASN A CG    1 
ATOM   2046 O OD1   . ASN A 1 263 ? 9.864   2.508   20.251 1.00 15.89  ? 305  ASN A OD1   1 
ATOM   2047 N ND2   . ASN A 1 263 ? 10.162  4.536   19.356 1.00 15.42  ? 305  ASN A ND2   1 
ATOM   2048 N N     . LEU A 1 264 ? 6.475   6.719   22.155 1.00 13.66  ? 306  LEU A N     1 
ATOM   2049 C CA    . LEU A 1 264 ? 5.156   6.960   22.728 1.00 12.84  ? 306  LEU A CA    1 
ATOM   2050 C C     . LEU A 1 264 ? 4.095   6.398   21.785 1.00 13.32  ? 306  LEU A C     1 
ATOM   2051 O O     . LEU A 1 264 ? 4.013   6.815   20.643 1.00 13.20  ? 306  LEU A O     1 
ATOM   2052 C CB    . LEU A 1 264 ? 4.941   8.464   22.947 1.00 13.45  ? 306  LEU A CB    1 
ATOM   2053 C CG    . LEU A 1 264 ? 5.648   9.046   24.166 1.00 13.53  ? 306  LEU A CG    1 
ATOM   2054 C CD1   . LEU A 1 264 ? 5.482   10.561  24.237 1.00 15.58  ? 306  LEU A CD1   1 
ATOM   2055 C CD2   . LEU A 1 264 ? 5.145   8.398   25.439 1.00 14.31  ? 306  LEU A CD2   1 
ATOM   2056 N N     . MET A 1 265 ? 3.343   5.434   22.330 1.00 13.26  ? 307  MET A N     1 
ATOM   2057 C CA    . MET A 1 265 ? 2.152   4.869   21.728 1.00 12.89  ? 307  MET A CA    1 
ATOM   2058 C C     . MET A 1 265 ? 0.954   5.519   22.421 1.00 14.05  ? 307  MET A C     1 
ATOM   2059 O O     . MET A 1 265 ? 0.613   5.160   23.549 1.00 11.91  ? 307  MET A O     1 
ATOM   2060 C CB    . MET A 1 265 ? 2.176   3.354   21.928 1.00 14.08  ? 307  MET A CB    1 
ATOM   2061 C CG    . MET A 1 265 ? 0.916   2.622   21.607 1.00 14.80  ? 307  MET A CG    1 
ATOM   2062 S SD    . MET A 1 265 ? 1.145   0.836   22.018 1.00 17.06  ? 307  MET A SD    1 
ATOM   2063 C CE    . MET A 1 265 ? -0.563  0.385   22.285 1.00 17.63  ? 307  MET A CE    1 
ATOM   2064 N N     . MET A 1 266 ? 0.325   6.488   21.734 1.00 13.44  ? 308  MET A N     1 
ATOM   2065 C CA    . MET A 1 266 ? -0.625  7.392   22.345 1.00 13.61  ? 308  MET A CA    1 
ATOM   2066 C C     . MET A 1 266 ? -2.057  6.959   22.034 1.00 12.79  ? 308  MET A C     1 
ATOM   2067 O O     . MET A 1 266 ? -2.404  6.716   20.873 1.00 13.01  ? 308  MET A O     1 
ATOM   2068 C CB    . MET A 1 266 ? -0.401  8.782   21.734 1.00 14.24  ? 308  MET A CB    1 
ATOM   2069 C CG    . MET A 1 266 ? 0.994   9.316   21.811 1.00 14.74  ? 308  MET A CG    1 
ATOM   2070 S SD    . MET A 1 266 ? 1.505   9.682   23.480 1.00 17.88  ? 308  MET A SD    1 
ATOM   2071 C CE    . MET A 1 266 ? 0.211   10.815  23.952 1.00 18.57  ? 308  MET A CE    1 
ATOM   2072 N N     . SER A 1 267 ? -2.912  6.959   23.046 1.00 12.82  ? 309  SER A N     1 
ATOM   2073 C CA    . SER A 1 267 ? -4.335  6.764   22.812 1.00 11.51  ? 309  SER A CA    1 
ATOM   2074 C C     . SER A 1 267 ? -4.963  8.025   22.191 1.00 11.80  ? 309  SER A C     1 
ATOM   2075 O O     . SER A 1 267 ? -4.597  9.157   22.460 1.00 13.73  ? 309  SER A O     1 
ATOM   2076 C CB    . SER A 1 267 ? -5.070  6.370   24.047 1.00 12.78  ? 309  SER A CB    1 
ATOM   2077 O OG    . SER A 1 267 ? -5.261  7.445   24.936 1.00 13.25  ? 309  SER A OG    1 
ATOM   2078 N N     . ALA A 1 268 ? -5.998  7.817   21.382 1.00 13.30  ? 310  ALA A N     1 
ATOM   2079 C CA    . ALA A 1 268 ? -6.697  8.929   20.781 1.00 13.96  ? 310  ALA A CA    1 
ATOM   2080 C C     . ALA A 1 268 ? -7.256  9.811   21.877 1.00 12.96  ? 310  ALA A C     1 
ATOM   2081 O O     . ALA A 1 268 ? -7.265  11.028  21.724 1.00 13.55  ? 310  ALA A O     1 
ATOM   2082 C CB    . ALA A 1 268 ? -7.805  8.392   19.880 1.00 14.06  ? 310  ALA A CB    1 
ATOM   2083 N N     . SER A 1 269 ? -7.780  9.214   22.938 1.00 13.66  ? 311  SER A N     1 
ATOM   2084 C CA    . SER A 1 269 ? -8.375  10.014  23.996 1.00 14.41  ? 311  SER A CA    1 
ATOM   2085 C C     . SER A 1 269 ? -7.367  10.985  24.617 1.00 14.62  ? 311  SER A C     1 
ATOM   2086 O O     . SER A 1 269 ? -7.673  12.179  24.818 1.00 14.00  ? 311  SER A O     1 
ATOM   2087 C CB    . SER A 1 269 ? -9.045  9.157   25.016 1.00 14.86  ? 311  SER A CB    1 
ATOM   2088 O OG    . SER A 1 269 ? -8.092  8.288   25.619 1.00 15.32  ? 311  SER A OG    1 
ATOM   2089 N N     . TYR A 1 270 ? -6.157  10.494  24.924 1.00 14.87  ? 312  TYR A N     1 
ATOM   2090 C CA    . TYR A 1 270 ? -5.103  11.365  25.410 1.00 12.94  ? 312  TYR A CA    1 
ATOM   2091 C C     . TYR A 1 270 ? -4.759  12.475  24.427 1.00 13.34  ? 312  TYR A C     1 
ATOM   2092 O O     . TYR A 1 270 ? -4.691  13.665  24.772 1.00 12.66  ? 312  TYR A O     1 
ATOM   2093 C CB    . TYR A 1 270 ? -3.846  10.550  25.785 1.00 13.01  ? 312  TYR A CB    1 
ATOM   2094 C CG    . TYR A 1 270 ? -2.761  11.350  26.477 1.00 13.97  ? 312  TYR A CG    1 
ATOM   2095 C CD1   . TYR A 1 270 ? -1.965  12.262  25.805 1.00 14.79  ? 312  TYR A CD1   1 
ATOM   2096 C CD2   . TYR A 1 270 ? -2.532  11.183  27.832 1.00 18.43  ? 312  TYR A CD2   1 
ATOM   2097 C CE1   . TYR A 1 270 ? -0.985  13.001  26.443 1.00 14.78  ? 312  TYR A CE1   1 
ATOM   2098 C CE2   . TYR A 1 270 ? -1.556  11.917  28.481 1.00 19.86  ? 312  TYR A CE2   1 
ATOM   2099 C CZ    . TYR A 1 270 ? -0.779  12.824  27.791 1.00 19.47  ? 312  TYR A CZ    1 
ATOM   2100 O OH    . TYR A 1 270 ? 0.256   13.559  28.391 1.00 18.81  ? 312  TYR A OH    1 
ATOM   2101 N N     . GLN A 1 271 ? -4.553  12.101  23.151 1.00 13.44  ? 313  GLN A N     1 
ATOM   2102 C CA    . GLN A 1 271 ? -4.209  13.085  22.160 1.00 13.22  ? 313  GLN A CA    1 
ATOM   2103 C C     . GLN A 1 271 ? -5.297  14.162  22.078 1.00 14.33  ? 313  GLN A C     1 
ATOM   2104 O O     . GLN A 1 271 ? -4.948  15.340  21.988 1.00 14.13  ? 313  GLN A O     1 
ATOM   2105 C CB    . GLN A 1 271 ? -3.914  12.389  20.836 1.00 13.40  ? 313  GLN A CB    1 
ATOM   2106 C CG    . GLN A 1 271 ? -2.734  11.460  20.974 1.00 15.19  ? 313  GLN A CG    1 
ATOM   2107 C CD    . GLN A 1 271 ? -2.279  10.974  19.646 1.00 15.95  ? 313  GLN A CD    1 
ATOM   2108 O OE1   . GLN A 1 271 ? -2.945  10.150  19.059 1.00 18.41  ? 313  GLN A OE1   1 
ATOM   2109 N NE2   . GLN A 1 271 ? -1.146  11.483  19.195 1.00 16.18  ? 313  GLN A NE2   1 
ATOM   2110 N N     . LEU A 1 272 ? -6.564  13.761  22.029 1.00 14.32  ? 314  LEU A N     1 
ATOM   2111 C CA    . LEU A 1 272 ? -7.611  14.771  21.945 1.00 14.57  ? 314  LEU A CA    1 
ATOM   2112 C C     . LEU A 1 272 ? -7.586  15.654  23.179 1.00 14.93  ? 314  LEU A C     1 
ATOM   2113 O O     . LEU A 1 272 ? -7.811  16.854  23.057 1.00 15.08  ? 314  LEU A O     1 
ATOM   2114 C CB    . LEU A 1 272 ? -8.965  14.093  21.702 1.00 16.18  ? 314  LEU A CB    1 
ATOM   2115 C CG    . LEU A 1 272 ? -9.131  13.399  20.358 1.00 17.28  ? 314  LEU A CG    1 
ATOM   2116 C CD1   . LEU A 1 272 ? -10.342 12.470  20.361 1.00 19.56  ? 314  LEU A CD1   1 
ATOM   2117 C CD2   . LEU A 1 272 ? -9.202  14.422  19.198 1.00 17.24  ? 314  LEU A CD2   1 
ATOM   2118 N N     . ALA A 1 273 ? -7.334  15.065  24.353 1.00 14.55  ? 315  ALA A N     1 
ATOM   2119 C CA    . ALA A 1 273 ? -7.358  15.818  25.613 1.00 14.25  ? 315  ALA A CA    1 
ATOM   2120 C C     . ALA A 1 273 ? -6.273  16.889  25.654 1.00 15.94  ? 315  ALA A C     1 
ATOM   2121 O O     . ALA A 1 273 ? -6.372  17.880  26.409 1.00 17.05  ? 315  ALA A O     1 
ATOM   2122 C CB    . ALA A 1 273 ? -7.255  14.899  26.820 1.00 14.08  ? 315  ALA A CB    1 
ATOM   2123 N N     . MET A 1 274 ? -5.202  16.709  24.877 1.00 15.00  ? 316  MET A N     1 
ATOM   2124 C CA    . MET A 1 274 ? -4.138  17.699  24.858 1.00 16.62  ? 316  MET A CA    1 
ATOM   2125 C C     . MET A 1 274 ? -4.640  19.059  24.350 1.00 17.91  ? 316  MET A C     1 
ATOM   2126 O O     . MET A 1 274 ? -4.078  20.092  24.727 1.00 21.50  ? 316  MET A O     1 
ATOM   2127 C CB    . MET A 1 274 ? -3.015  17.211  23.939 1.00 15.96  ? 316  MET A CB    1 
ATOM   2128 C CG    . MET A 1 274 ? -2.232  16.057  24.501 1.00 17.33  ? 316  MET A CG    1 
ATOM   2129 S SD    . MET A 1 274 ? -1.138  15.271  23.243 1.00 19.26  ? 316  MET A SD    1 
ATOM   2130 C CE    . MET A 1 274 ? 0.022   16.588  22.916 1.00 19.82  ? 316  MET A CE    1 
ATOM   2131 N N     . PHE A 1 275 ? -5.563  19.039  23.381 1.00 16.47  ? 317  PHE A N     1 
ATOM   2132 C CA    . PHE A 1 275 ? -5.958  20.275  22.701 1.00 20.03  ? 317  PHE A CA    1 
ATOM   2133 C C     . PHE A 1 275 ? -7.461  20.570  22.815 1.00 22.08  ? 317  PHE A C     1 
ATOM   2134 O O     . PHE A 1 275 ? -7.905  21.628  22.392 1.00 22.30  ? 317  PHE A O     1 
ATOM   2135 C CB    . PHE A 1 275 ? -5.520  20.246  21.234 1.00 20.08  ? 317  PHE A CB    1 
ATOM   2136 C CG    . PHE A 1 275 ? -4.028  20.148  21.025 1.00 22.40  ? 317  PHE A CG    1 
ATOM   2137 C CD1   . PHE A 1 275 ? -3.169  21.071  21.606 1.00 26.36  ? 317  PHE A CD1   1 
ATOM   2138 C CD2   . PHE A 1 275 ? -3.469  19.114  20.304 1.00 22.43  ? 317  PHE A CD2   1 
ATOM   2139 C CE1   . PHE A 1 275 ? -1.794  20.990  21.419 1.00 27.14  ? 317  PHE A CE1   1 
ATOM   2140 C CE2   . PHE A 1 275 ? -2.093  19.034  20.105 1.00 24.73  ? 317  PHE A CE2   1 
ATOM   2141 C CZ    . PHE A 1 275 ? -1.255  19.980  20.651 1.00 25.31  ? 317  PHE A CZ    1 
ATOM   2142 N N     . LYS A 1 276 ? -8.273  19.653  23.339 1.00 19.57  ? 318  LYS A N     1 
ATOM   2143 C CA    . LYS A 1 276 ? -9.715  19.821  23.381 1.00 18.62  ? 318  LYS A CA    1 
ATOM   2144 C C     . LYS A 1 276 ? -10.211 19.449  24.776 1.00 18.61  ? 318  LYS A C     1 
ATOM   2145 O O     . LYS A 1 276 ? -9.568  18.677  25.482 1.00 19.15  ? 318  LYS A O     1 
ATOM   2146 C CB    . LYS A 1 276 ? -10.392 18.882  22.387 1.00 19.76  ? 318  LYS A CB    1 
ATOM   2147 C CG    . LYS A 1 276 ? -9.902  19.043  20.961 1.00 24.20  ? 318  LYS A CG    1 
ATOM   2148 C CD    . LYS A 1 276 ? -10.643 18.214  20.002 1.00 28.47  ? 318  LYS A CD    1 
ATOM   2149 C CE    . LYS A 1 276 ? -10.369 18.548  18.547 1.00 34.57  ? 318  LYS A CE    1 
ATOM   2150 N NZ    . LYS A 1 276 ? -10.881 19.891  18.179 1.00 39.20  ? 318  LYS A NZ    1 
ATOM   2151 N N     . ARG A 1 277 ? -11.343 20.011  25.172 1.00 15.17  ? 319  ARG A N     1 
ATOM   2152 C CA    . ARG A 1 277 ? -12.014 19.624  26.407 1.00 15.64  ? 319  ARG A CA    1 
ATOM   2153 C C     . ARG A 1 277 ? -12.998 18.506  26.094 1.00 13.18  ? 319  ARG A C     1 
ATOM   2154 O O     . ARG A 1 277 ? -13.453 18.368  24.954 1.00 13.30  ? 319  ARG A O     1 
ATOM   2155 C CB    . ARG A 1 277 ? -12.722 20.850  27.008 1.00 16.67  ? 319  ARG A CB    1 
ATOM   2156 C CG    . ARG A 1 277 ? -11.763 22.005  27.287 1.00 17.22  ? 319  ARG A CG    1 
ATOM   2157 C CD    . ARG A 1 277 ? -12.460 23.136  27.981 1.00 17.10  ? 319  ARG A CD    1 
ATOM   2158 N NE    . ARG A 1 277 ? -11.542 24.233  28.166 1.00 18.92  ? 319  ARG A NE    1 
ATOM   2159 C CZ    . ARG A 1 277 ? -11.903 25.392  28.694 1.00 21.29  ? 319  ARG A CZ    1 
ATOM   2160 N NH1   . ARG A 1 277 ? -13.129 25.530  29.160 1.00 19.63  ? 319  ARG A NH1   1 
ATOM   2161 N NH2   . ARG A 1 277 ? -11.020 26.368  28.813 1.00 23.27  ? 319  ARG A NH2   1 
ATOM   2162 N N     . ARG A 1 278 ? -13.321 17.729  27.127 1.00 12.58  ? 320  ARG A N     1 
ATOM   2163 C CA    . ARG A 1 278 ? -14.143 16.529  26.961 1.00 12.80  ? 320  ARG A CA    1 
ATOM   2164 C C     . ARG A 1 278 ? -15.491 16.881  26.315 1.00 13.56  ? 320  ARG A C     1 
ATOM   2165 O O     . ARG A 1 278 ? -15.999 16.138  25.476 1.00 13.13  ? 320  ARG A O     1 
ATOM   2166 C CB    . ARG A 1 278 ? -14.364 15.872  28.328 1.00 11.48  ? 320  ARG A CB    1 
ATOM   2167 C CG    . ARG A 1 278 ? -14.932 14.469  28.210 1.00 12.34  ? 320  ARG A CG    1 
ATOM   2168 C CD    . ARG A 1 278 ? -15.355 13.989  29.531 1.00 11.64  ? 320  ARG A CD    1 
ATOM   2169 N NE    . ARG A 1 278 ? -15.685 12.585  29.553 1.00 13.65  ? 320  ARG A NE    1 
ATOM   2170 C CZ    . ARG A 1 278 ? -16.906 12.075  29.411 1.00 15.54  ? 320  ARG A CZ    1 
ATOM   2171 N NH1   . ARG A 1 278 ? -17.967 12.874  29.292 1.00 15.22  ? 320  ARG A NH1   1 
ATOM   2172 N NH2   . ARG A 1 278 ? -17.025 10.749  29.274 1.00 15.79  ? 320  ARG A NH2   1 
ATOM   2173 N N     . ASN A 1 279 ? -16.041 18.040  26.701 1.00 11.74  ? 321  ASN A N     1 
ATOM   2174 C CA    . ASN A 1 279 ? -17.359 18.429  26.206 1.00 13.78  ? 321  ASN A CA    1 
ATOM   2175 C C     . ASN A 1 279 ? -17.350 18.945  24.769 1.00 15.52  ? 321  ASN A C     1 
ATOM   2176 O O     . ASN A 1 279 ? -18.433 19.302  24.260 1.00 14.97  ? 321  ASN A O     1 
ATOM   2177 C CB    . ASN A 1 279 ? -18.045 19.374  27.189 1.00 14.32  ? 321  ASN A CB    1 
ATOM   2178 C CG    . ASN A 1 279 ? -17.373 20.727  27.294 1.00 12.70  ? 321  ASN A CG    1 
ATOM   2179 O OD1   . ASN A 1 279 ? -16.494 21.105  26.529 1.00 14.14  ? 321  ASN A OD1   1 
ATOM   2180 N ND2   . ASN A 1 279 ? -17.752 21.449  28.331 1.00 15.95  ? 321  ASN A ND2   1 
ATOM   2181 N N     . GLU A 1 280 ? -16.187 18.970  24.111 1.00 14.88  ? 322  GLU A N     1 
ATOM   2182 C CA    . GLU A 1 280 ? -16.127 19.147  22.668 1.00 16.78  ? 322  GLU A CA    1 
ATOM   2183 C C     . GLU A 1 280 ? -16.302 17.813  21.945 1.00 17.52  ? 322  GLU A C     1 
ATOM   2184 O O     . GLU A 1 280 ? -16.436 17.773  20.714 1.00 18.35  ? 322  GLU A O     1 
ATOM   2185 C CB    . GLU A 1 280 ? -14.814 19.818  22.287 1.00 18.98  ? 322  GLU A CB    1 
ATOM   2186 C CG    . GLU A 1 280 ? -14.627 21.248  22.833 1.00 19.23  ? 322  GLU A CG    1 
ATOM   2187 C CD    . GLU A 1 280 ? -13.181 21.684  22.589 1.00 24.05  ? 322  GLU A CD    1 
ATOM   2188 O OE1   . GLU A 1 280 ? -12.675 21.559  21.419 1.00 29.14  ? 322  GLU A OE1   1 
ATOM   2189 O OE2   . GLU A 1 280 ? -12.504 22.080  23.531 1.00 22.78  ? 322  GLU A OE2   1 
ATOM   2190 N N     . ILE A 1 281 ? -16.222 16.706  22.680 1.00 15.85  ? 323  ILE A N     1 
ATOM   2191 C CA    . ILE A 1 281 ? -16.229 15.379  22.077 1.00 17.27  ? 323  ILE A CA    1 
ATOM   2192 C C     . ILE A 1 281 ? -17.526 14.629  22.409 1.00 16.85  ? 323  ILE A C     1 
ATOM   2193 O O     . ILE A 1 281 ? -18.158 14.061  21.506 1.00 19.21  ? 323  ILE A O     1 
ATOM   2194 C CB    . ILE A 1 281 ? -15.015 14.559  22.557 1.00 19.31  ? 323  ILE A CB    1 
ATOM   2195 C CG1   . ILE A 1 281 ? -13.693 15.340  22.503 1.00 22.43  ? 323  ILE A CG1   1 
ATOM   2196 C CG2   . ILE A 1 281 ? -14.922 13.245  21.782 1.00 21.02  ? 323  ILE A CG2   1 
ATOM   2197 C CD1   . ILE A 1 281 ? -13.247 15.753  21.159 1.00 25.09  ? 323  ILE A CD1   1 
ATOM   2198 N N     . VAL A 1 282 ? -17.892 14.568  23.693 1.00 14.37  ? 324  VAL A N     1 
ATOM   2199 C CA    . VAL A 1 282 ? -19.120 13.942  24.127 1.00 14.57  ? 324  VAL A CA    1 
ATOM   2200 C C     . VAL A 1 282 ? -19.782 14.807  25.182 1.00 15.71  ? 324  VAL A C     1 
ATOM   2201 O O     . VAL A 1 282 ? -19.110 15.553  25.876 1.00 14.33  ? 324  VAL A O     1 
ATOM   2202 C CB    . VAL A 1 282 ? -18.938 12.507  24.666 1.00 15.30  ? 324  VAL A CB    1 
ATOM   2203 C CG1   . VAL A 1 282 ? -18.478 11.535  23.607 1.00 17.13  ? 324  VAL A CG1   1 
ATOM   2204 C CG2   . VAL A 1 282 ? -18.003 12.511  25.860 1.00 15.27  ? 324  VAL A CG2   1 
ATOM   2205 N N     . PRO A 1 283 ? -21.119 14.716  25.362 1.00 17.81  ? 325  PRO A N     1 
ATOM   2206 C CA    . PRO A 1 283 ? -21.786 15.397  26.480 1.00 19.25  ? 325  PRO A CA    1 
ATOM   2207 C C     . PRO A 1 283 ? -21.302 14.957  27.852 1.00 18.57  ? 325  PRO A C     1 
ATOM   2208 O O     . PRO A 1 283 ? -20.898 13.809  28.049 1.00 18.63  ? 325  PRO A O     1 
ATOM   2209 C CB    . PRO A 1 283 ? -23.276 15.038  26.344 1.00 21.59  ? 325  PRO A CB    1 
ATOM   2210 C CG    . PRO A 1 283 ? -23.417 14.541  24.933 1.00 22.12  ? 325  PRO A CG    1 
ATOM   2211 C CD    . PRO A 1 283 ? -22.066 14.002  24.485 1.00 20.17  ? 325  PRO A CD    1 
ATOM   2212 N N     . ASP A 1 284 ? -21.315 15.904  28.803 1.00 19.09  ? 326  ASP A N     1 
ATOM   2213 C CA    . ASP A 1 284 ? -21.074 15.550  30.180 1.00 21.21  ? 326  ASP A CA    1 
ATOM   2214 C C     . ASP A 1 284 ? -22.103 14.500  30.554 1.00 25.25  ? 326  ASP A C     1 
ATOM   2215 O O     . ASP A 1 284 ? -23.252 14.549  30.126 1.00 28.01  ? 326  ASP A O     1 
ATOM   2216 C CB    . ASP A 1 284 ? -21.201 16.743  31.122 1.00 22.26  ? 326  ASP A CB    1 
ATOM   2217 C CG    . ASP A 1 284 ? -20.113 17.782  30.976 1.00 20.21  ? 326  ASP A CG    1 
ATOM   2218 O OD1   . ASP A 1 284 ? -19.064 17.512  30.330 1.00 20.64  ? 326  ASP A OD1   1 
ATOM   2219 O OD2   . ASP A 1 284 ? -20.343 18.931  31.434 1.00 25.25  ? 326  ASP A OD2   1 
ATOM   2220 N N     . GLY A 1 285 ? -21.679 13.502  31.295 1.00 27.43  ? 327  GLY A N     1 
ATOM   2221 C CA    . GLY A 1 285 ? -22.682 12.504  31.626 1.00 25.36  ? 327  GLY A CA    1 
ATOM   2222 C C     . GLY A 1 285 ? -22.695 11.320  30.676 1.00 23.02  ? 327  GLY A C     1 
ATOM   2223 O O     . GLY A 1 285 ? -23.221 10.283  31.052 1.00 26.96  ? 327  GLY A O     1 
ATOM   2224 N N     . ALA A 1 286 ? -22.187 11.466  29.458 1.00 18.64  ? 328  ALA A N     1 
ATOM   2225 C CA    . ALA A 1 286 ? -22.107 10.372  28.525 1.00 17.50  ? 328  ALA A CA    1 
ATOM   2226 C C     . ALA A 1 286 ? -20.726 9.746   28.586 1.00 17.98  ? 328  ALA A C     1 
ATOM   2227 O O     . ALA A 1 286 ? -19.774 10.387  28.971 1.00 16.90  ? 328  ALA A O     1 
ATOM   2228 C CB    . ALA A 1 286 ? -22.382 10.812  27.122 1.00 18.90  ? 328  ALA A CB    1 
ATOM   2229 N N     . PRO A 1 287 ? -20.600 8.447   28.284 1.00 17.12  ? 329  PRO A N     1 
ATOM   2230 C CA    . PRO A 1 287 ? -19.287 7.804   28.213 1.00 20.20  ? 329  PRO A CA    1 
ATOM   2231 C C     . PRO A 1 287 ? -18.473 8.321   27.028 1.00 17.14  ? 329  PRO A C     1 
ATOM   2232 O O     . PRO A 1 287 ? -19.018 8.837   26.055 1.00 18.32  ? 329  PRO A O     1 
ATOM   2233 C CB    . PRO A 1 287 ? -19.607 6.296   28.075 1.00 21.94  ? 329  PRO A CB    1 
ATOM   2234 C CG    . PRO A 1 287 ? -21.047 6.246   27.587 1.00 25.20  ? 329  PRO A CG    1 
ATOM   2235 C CD    . PRO A 1 287 ? -21.714 7.512   28.097 1.00 22.78  ? 329  PRO A CD    1 
ATOM   2236 N N     . LEU A 1 288 ? -17.145 8.192   27.141 1.00 18.17  ? 330  LEU A N     1 
ATOM   2237 C CA    . LEU A 1 288 ? -16.267 8.539   26.002 1.00 17.81  ? 330  LEU A CA    1 
ATOM   2238 C C     . LEU A 1 288 ? -16.269 7.310   25.093 1.00 19.58  ? 330  LEU A C     1 
ATOM   2239 O O     . LEU A 1 288 ? -15.326 6.524   25.146 1.00 19.43  ? 330  LEU A O     1 
ATOM   2240 C CB    . LEU A 1 288 ? -14.867 8.884   26.518 1.00 18.80  ? 330  LEU A CB    1 
ATOM   2241 C CG    . LEU A 1 288 ? -13.923 9.566   25.534 1.00 18.74  ? 330  LEU A CG    1 
ATOM   2242 C CD1   . LEU A 1 288 ? -14.449 10.941  25.157 1.00 20.15  ? 330  LEU A CD1   1 
ATOM   2243 C CD2   . LEU A 1 288 ? -12.529 9.675   26.135 1.00 18.37  ? 330  LEU A CD2   1 
ATOM   2244 N N     . ASP A 1 289 ? -17.331 7.164   24.316 1.00 19.42  ? 331  ASP A N     1 
ATOM   2245 C CA    . ASP A 1 289 ? -17.497 5.974   23.445 1.00 19.78  ? 331  ASP A CA    1 
ATOM   2246 C C     . ASP A 1 289 ? -16.491 5.941   22.286 1.00 19.88  ? 331  ASP A C     1 
ATOM   2247 O O     . ASP A 1 289 ? -16.046 6.988   21.856 1.00 18.32  ? 331  ASP A O     1 
ATOM   2248 C CB    . ASP A 1 289 ? -18.937 5.870   22.950 1.00 19.62  ? 331  ASP A CB    1 
ATOM   2249 C CG    . ASP A 1 289 ? -19.298 6.940   21.946 1.00 21.75  ? 331  ASP A CG    1 
ATOM   2250 O OD1   . ASP A 1 289 ? -19.573 8.062   22.381 1.00 22.68  ? 331  ASP A OD1   1 
ATOM   2251 O OD2   . ASP A 1 289 ? -19.287 6.632   20.748 1.00 23.74  ? 331  ASP A OD2   1 
ATOM   2252 N N     . GLU A 1 290 ? -16.189 4.726   21.815 1.00 20.62  ? 332  GLU A N     1 
ATOM   2253 C CA    . GLU A 1 290 ? -15.163 4.552   20.754 1.00 22.88  ? 332  GLU A CA    1 
ATOM   2254 C C     . GLU A 1 290 ? -15.616 5.109   19.397 1.00 21.70  ? 332  GLU A C     1 
ATOM   2255 O O     . GLU A 1 290 ? -14.763 5.513   18.635 1.00 19.97  ? 332  GLU A O     1 
ATOM   2256 C CB    . GLU A 1 290 ? -14.757 3.078   20.648 1.00 30.33  ? 332  GLU A CB    1 
ATOM   2257 C CG    . GLU A 1 290 ? -13.865 2.668   21.806 1.00 40.58  ? 332  GLU A CG    1 
ATOM   2258 C CD    . GLU A 1 290 ? -13.417 1.220   21.885 1.00 45.79  ? 332  GLU A CD    1 
ATOM   2259 O OE1   . GLU A 1 290 ? -13.541 0.502   20.880 1.00 45.34  ? 332  GLU A OE1   1 
ATOM   2260 O OE2   . GLU A 1 290 ? -12.935 0.826   22.958 1.00 35.56  ? 332  GLU A OE2   1 
ATOM   2261 N N     . ALA A 1 291 ? -16.910 5.096   19.122 1.00 20.80  ? 333  ALA A N     1 
ATOM   2262 C CA    . ALA A 1 291 ? -17.350 5.703   17.847 1.00 21.40  ? 333  ALA A CA    1 
ATOM   2263 C C     . ALA A 1 291 ? -17.064 7.208   17.850 1.00 17.87  ? 333  ALA A C     1 
ATOM   2264 O O     . ALA A 1 291 ? -16.571 7.725   16.864 1.00 18.79  ? 333  ALA A O     1 
ATOM   2265 C CB    . ALA A 1 291 ? -18.807 5.420   17.610 1.00 23.20  ? 333  ALA A CB    1 
ATOM   2266 N N     . SER A 1 292 ? -17.400 7.852   18.962 1.00 18.09  ? 334  SER A N     1 
ATOM   2267 C CA    . SER A 1 292 ? -17.177 9.311   19.047 1.00 19.77  ? 334  SER A CA    1 
ATOM   2268 C C     . SER A 1 292 ? -15.665 9.576   19.002 1.00 19.08  ? 334  SER A C     1 
ATOM   2269 O O     . SER A 1 292 ? -15.256 10.514  18.327 1.00 19.33  ? 334  SER A O     1 
ATOM   2270 C CB    . SER A 1 292 ? -17.830 9.896   20.281 1.00 21.40  ? 334  SER A CB    1 
ATOM   2271 O OG    . SER A 1 292 ? -19.216 9.624   20.316 1.00 21.02  ? 334  SER A OG    1 
ATOM   2272 N N     . LEU A 1 293 ? -14.880 8.742   19.703 1.00 17.52  ? 335  LEU A N     1 
ATOM   2273 C CA    . LEU A 1 293 ? -13.436 8.913   19.679 1.00 17.25  ? 335  LEU A CA    1 
ATOM   2274 C C     . LEU A 1 293 ? -12.893 8.708   18.292 1.00 16.37  ? 335  LEU A C     1 
ATOM   2275 O O     . LEU A 1 293 ? -12.052 9.493   17.824 1.00 18.05  ? 335  LEU A O     1 
ATOM   2276 C CB    . LEU A 1 293 ? -12.727 7.929   20.627 1.00 18.99  ? 335  LEU A CB    1 
ATOM   2277 C CG    . LEU A 1 293 ? -12.761 8.324   22.083 1.00 21.34  ? 335  LEU A CG    1 
ATOM   2278 C CD1   . LEU A 1 293 ? -12.247 7.198   22.956 1.00 23.18  ? 335  LEU A CD1   1 
ATOM   2279 C CD2   . LEU A 1 293 ? -11.927 9.605   22.274 1.00 21.83  ? 335  LEU A CD2   1 
ATOM   2280 N N     . LYS A 1 294 ? -13.338 7.634   17.624 1.00 17.65  ? 336  LYS A N     1 
ATOM   2281 C CA    . LYS A 1 294 ? -12.838 7.354   16.294 1.00 19.20  ? 336  LYS A CA    1 
ATOM   2282 C C     . LYS A 1 294 ? -13.159 8.498   15.327 1.00 19.58  ? 336  LYS A C     1 
ATOM   2283 O O     . LYS A 1 294 ? -12.353 8.850   14.474 1.00 22.03  ? 336  LYS A O     1 
ATOM   2284 C CB    . LYS A 1 294 ? -13.411 6.026   15.806 1.00 23.90  ? 336  LYS A CB    1 
ATOM   2285 C CG    . LYS A 1 294 ? -12.812 5.516   14.510 1.00 34.43  ? 336  LYS A CG    1 
ATOM   2286 C CD    . LYS A 1 294 ? -13.361 4.158   14.088 1.00 41.15  ? 336  LYS A CD    1 
ATOM   2287 C CE    . LYS A 1 294 ? -12.491 2.986   14.454 1.00 44.29  ? 336  LYS A CE    1 
ATOM   2288 N NZ    . LYS A 1 294 ? -12.689 2.606   15.871 1.00 55.42  ? 336  LYS A NZ    1 
ATOM   2289 N N     . LYS A 1 295 ? -14.384 9.022   15.374 1.00 19.52  ? 337  LYS A N     1 
ATOM   2290 C CA    . LYS A 1 295 ? -14.809 10.081  14.460 1.00 21.42  ? 337  LYS A CA    1 
ATOM   2291 C C     . LYS A 1 295 ? -13.979 11.349  14.655 1.00 19.19  ? 337  LYS A C     1 
ATOM   2292 O O     . LYS A 1 295 ? -13.472 11.949  13.700 1.00 18.89  ? 337  LYS A O     1 
ATOM   2293 C CB    . LYS A 1 295 ? -16.287 10.399  14.699 1.00 23.90  ? 337  LYS A CB    1 
ATOM   2294 C CG    . LYS A 1 295 ? -16.847 11.583  13.904 1.00 30.61  ? 337  LYS A CG    1 
ATOM   2295 C CD    . LYS A 1 295 ? -18.343 11.764  14.116 1.00 36.39  ? 337  LYS A CD    1 
ATOM   2296 C CE    . LYS A 1 295 ? -18.851 13.165  13.847 1.00 45.10  ? 337  LYS A CE    1 
ATOM   2297 N NZ    . LYS A 1 295 ? -20.209 13.331  14.429 1.00 49.38  ? 337  LYS A NZ    1 
ATOM   2298 N N     . ALA A 1 296 ? -13.790 11.709  15.927 1.00 19.34  ? 338  ALA A N     1 
ATOM   2299 C CA    . ALA A 1 296 ? -12.992 12.869  16.310 1.00 18.11  ? 338  ALA A CA    1 
ATOM   2300 C C     . ALA A 1 296 ? -11.523 12.699  15.950 1.00 16.95  ? 338  ALA A C     1 
ATOM   2301 O O     . ALA A 1 296 ? -10.865 13.617  15.462 1.00 17.95  ? 338  ALA A O     1 
ATOM   2302 C CB    . ALA A 1 296 ? -13.144 13.092  17.783 1.00 18.20  ? 338  ALA A CB    1 
ATOM   2303 N N     . ALA A 1 297 ? -10.982 11.501  16.229 1.00 17.56  ? 339  ALA A N     1 
ATOM   2304 C CA    . ALA A 1 297 ? -9.597  11.230  15.873 1.00 17.72  ? 339  ALA A CA    1 
ATOM   2305 C C     . ALA A 1 297 ? -9.387  11.286  14.366 1.00 17.75  ? 339  ALA A C     1 
ATOM   2306 O O     . ALA A 1 297 ? -8.463  11.960  13.899 1.00 17.72  ? 339  ALA A O     1 
ATOM   2307 C CB    . ALA A 1 297 ? -9.191  9.893   16.477 1.00 18.73  ? 339  ALA A CB    1 
ATOM   2308 N N     . SER A 1 298 ? -10.289 10.632  13.608 1.00 20.46  ? 340  SER A N     1 
ATOM   2309 C CA    . SER A 1 298 ? -10.189 10.564  12.141 1.00 21.19  ? 340  SER A CA    1 
ATOM   2310 C C     . SER A 1 298 ? -10.233 11.970  11.541 1.00 20.54  ? 340  SER A C     1 
ATOM   2311 O O     . SER A 1 298 ? -9.465  12.278  10.634 1.00 21.72  ? 340  SER A O     1 
ATOM   2312 C CB    . SER A 1 298 ? -11.279 9.691   11.581 1.00 24.15  ? 340  SER A CB    1 
ATOM   2313 O OG    . SER A 1 298 ? -11.019 8.314   11.813 1.00 25.82  ? 340  SER A OG    1 
ATOM   2314 N N     . ALA A 1 299 ? -11.099 12.837  12.071 1.00 20.43  ? 341  ALA A N     1 
ATOM   2315 C CA    . ALA A 1 299 ? -11.211 14.213  11.606 1.00 21.91  ? 341  ALA A CA    1 
ATOM   2316 C C     . ALA A 1 299 ? -9.920  15.007  11.822 1.00 24.44  ? 341  ALA A C     1 
ATOM   2317 O O     . ALA A 1 299 ? -9.733  16.057  11.209 1.00 22.60  ? 341  ALA A O     1 
ATOM   2318 C CB    . ALA A 1 299 ? -12.379 14.900  12.275 1.00 22.79  ? 341  ALA A CB    1 
ATOM   2319 N N     . ASN A 1 300 ? -9.021  14.512  12.695 1.00 21.14  ? 342  ASN A N     1 
ATOM   2320 C CA    . ASN A 1 300 ? -7.779  15.185  13.041 1.00 21.58  ? 342  ASN A CA    1 
ATOM   2321 C C     . ASN A 1 300 ? -6.559  14.418  12.519 1.00 21.15  ? 342  ASN A C     1 
ATOM   2322 O O     . ASN A 1 300 ? -5.421  14.715  12.913 1.00 20.39  ? 342  ASN A O     1 
ATOM   2323 C CB    . ASN A 1 300 ? -7.747  15.363  14.556 1.00 21.56  ? 342  ASN A CB    1 
ATOM   2324 C CG    . ASN A 1 300 ? -8.582  16.537  14.995 1.00 22.24  ? 342  ASN A CG    1 
ATOM   2325 O OD1   . ASN A 1 300 ? -8.193  17.672  14.740 1.00 25.65  ? 342  ASN A OD1   1 
ATOM   2326 N ND2   . ASN A 1 300 ? -9.741  16.275  15.564 1.00 23.20  ? 342  ASN A ND2   1 
ATOM   2327 N N     . GLY A 1 301 ? -6.788  13.418  11.652 1.00 19.74  ? 343  GLY A N     1 
ATOM   2328 C CA    . GLY A 1 301 ? -5.726  12.619  11.055 1.00 19.83  ? 343  GLY A CA    1 
ATOM   2329 C C     . GLY A 1 301 ? -5.062  11.634  12.034 1.00 18.11  ? 343  GLY A C     1 
ATOM   2330 O O     . GLY A 1 301 ? -3.955  11.186  11.776 1.00 22.12  ? 343  GLY A O     1 
ATOM   2331 N N     . LEU A 1 302 ? -5.779  11.257  13.094 1.00 17.25  ? 344  LEU A N     1 
ATOM   2332 C CA    . LEU A 1 302 ? -5.301  10.291  14.077 1.00 16.49  ? 344  LEU A CA    1 
ATOM   2333 C C     . LEU A 1 302 ? -6.058  8.983   13.972 1.00 19.10  ? 344  LEU A C     1 
ATOM   2334 O O     . LEU A 1 302 ? -7.267  8.953   13.720 1.00 18.45  ? 344  LEU A O     1 
ATOM   2335 C CB    . LEU A 1 302 ? -5.513  10.835  15.485 1.00 15.83  ? 344  LEU A CB    1 
ATOM   2336 C CG    . LEU A 1 302 ? -4.864  12.164  15.797 1.00 17.18  ? 344  LEU A CG    1 
ATOM   2337 C CD1   . LEU A 1 302 ? -5.299  12.652  17.166 1.00 17.29  ? 344  LEU A CD1   1 
ATOM   2338 C CD2   . LEU A 1 302 ? -3.355  12.065  15.739 1.00 17.93  ? 344  LEU A CD2   1 
ATOM   2339 N N     . GLY A 1 303 ? -5.329  7.903   14.310 1.00 16.72  ? 345  GLY A N     1 
ATOM   2340 C CA    . GLY A 1 303 ? -5.905  6.599   14.568 1.00 16.29  ? 345  GLY A CA    1 
ATOM   2341 C C     . GLY A 1 303 ? -6.349  6.491   16.007 1.00 15.66  ? 345  GLY A C     1 
ATOM   2342 O O     . GLY A 1 303 ? -6.255  7.461   16.776 1.00 16.65  ? 345  GLY A O     1 
ATOM   2343 N N     . MET A 1 304 ? -6.806  5.301   16.392 1.00 15.32  ? 346  MET A N     1 
ATOM   2344 C CA    . MET A 1 304 ? -7.166  5.101   17.780 1.00 14.80  ? 346  MET A CA    1 
ATOM   2345 C C     . MET A 1 304 ? -5.904  4.918   18.647 1.00 14.65  ? 346  MET A C     1 
ATOM   2346 O O     . MET A 1 304 ? -5.973  5.187   19.855 1.00 15.39  ? 346  MET A O     1 
ATOM   2347 C CB    . MET A 1 304 ? -8.115  3.916   17.945 1.00 16.96  ? 346  MET A CB    1 
ATOM   2348 C CG    . MET A 1 304 ? -9.528  4.257   17.420 1.00 17.05  ? 346  MET A CG    1 
ATOM   2349 S SD    . MET A 1 304 ? -10.358 5.450   18.507 1.00 21.16  ? 346  MET A SD    1 
ATOM   2350 C CE    . MET A 1 304 ? -10.720 4.440   19.937 1.00 24.29  ? 346  MET A CE    1 
ATOM   2351 N N     . TRP A 1 305 ? -4.787  4.498   18.035 1.00 14.17  ? 347  TRP A N     1 
ATOM   2352 C CA    . TRP A 1 305 ? -3.479  4.497   18.697 1.00 12.98  ? 347  TRP A CA    1 
ATOM   2353 C C     . TRP A 1 305 ? -2.505  5.084   17.690 1.00 14.56  ? 347  TRP A C     1 
ATOM   2354 O O     . TRP A 1 305 ? -2.561  4.763   16.502 1.00 16.68  ? 347  TRP A O     1 
ATOM   2355 C CB    . TRP A 1 305 ? -3.053  3.081   19.098 1.00 13.59  ? 347  TRP A CB    1 
ATOM   2356 C CG    . TRP A 1 305 ? -3.841  2.509   20.223 1.00 13.47  ? 347  TRP A CG    1 
ATOM   2357 C CD1   . TRP A 1 305 ? -4.933  1.710   20.133 1.00 13.96  ? 347  TRP A CD1   1 
ATOM   2358 C CD2   . TRP A 1 305 ? -3.671  2.792   21.628 1.00 14.62  ? 347  TRP A CD2   1 
ATOM   2359 N NE1   . TRP A 1 305 ? -5.436  1.463   21.378 1.00 15.12  ? 347  TRP A NE1   1 
ATOM   2360 C CE2   . TRP A 1 305 ? -4.649  2.070   22.323 1.00 14.41  ? 347  TRP A CE2   1 
ATOM   2361 C CE3   . TRP A 1 305 ? -2.705  3.496   22.353 1.00 15.10  ? 347  TRP A CE3   1 
ATOM   2362 C CZ2   . TRP A 1 305 ? -4.725  2.044   23.721 1.00 16.68  ? 347  TRP A CZ2   1 
ATOM   2363 C CZ3   . TRP A 1 305 ? -2.767  3.465   23.725 1.00 14.01  ? 347  TRP A CZ3   1 
ATOM   2364 C CH2   . TRP A 1 305 ? -3.770  2.771   24.397 1.00 15.53  ? 347  TRP A CH2   1 
ATOM   2365 N N     . ASN A 1 306 ? -1.590  5.949   18.159 1.00 13.86  ? 348  ASN A N     1 
ATOM   2366 C CA    . ASN A 1 306 ? -0.674  6.627   17.250 1.00 13.29  ? 348  ASN A CA    1 
ATOM   2367 C C     . ASN A 1 306 ? 0.712   6.534   17.889 1.00 13.80  ? 348  ASN A C     1 
ATOM   2368 O O     . ASN A 1 306 ? 0.863   6.965   19.048 1.00 12.68  ? 348  ASN A O     1 
ATOM   2369 C CB    . ASN A 1 306 ? -1.104  8.081   17.062 1.00 14.76  ? 348  ASN A CB    1 
ATOM   2370 C CG    . ASN A 1 306 ? -2.487  8.141   16.427 1.00 15.60  ? 348  ASN A CG    1 
ATOM   2371 O OD1   . ASN A 1 306 ? -2.629  7.832   15.235 1.00 18.87  ? 348  ASN A OD1   1 
ATOM   2372 N ND2   . ASN A 1 306 ? -3.489  8.257   17.264 1.00 16.19  ? 348  ASN A ND2   1 
ATOM   2373 N N     . THR A 1 307 ? 1.650   5.877   17.200 1.00 13.06  ? 349  THR A N     1 
ATOM   2374 C CA    . THR A 1 307 ? 2.917   5.538   17.838 1.00 13.16  ? 349  THR A CA    1 
ATOM   2375 C C     . THR A 1 307 ? 4.024   6.281   17.111 1.00 14.77  ? 349  THR A C     1 
ATOM   2376 O O     . THR A 1 307 ? 4.054   6.281   15.881 1.00 16.02  ? 349  THR A O     1 
ATOM   2377 C CB    . THR A 1 307 ? 3.162   4.034   17.851 1.00 13.91  ? 349  THR A CB    1 
ATOM   2378 O OG1   . THR A 1 307 ? 2.067   3.417   18.495 1.00 14.62  ? 349  THR A OG1   1 
ATOM   2379 C CG2   . THR A 1 307 ? 4.468   3.655   18.502 1.00 14.73  ? 349  THR A CG2   1 
ATOM   2380 N N     . TYR A 1 308 ? 4.938   6.911   17.871 1.00 13.84  ? 350  TYR A N     1 
ATOM   2381 C CA    . TYR A 1 308 ? 5.922   7.810   17.332 1.00 13.29  ? 350  TYR A CA    1 
ATOM   2382 C C     . TYR A 1 308 ? 7.318   7.210   17.514 1.00 12.44  ? 350  TYR A C     1 
ATOM   2383 O O     . TYR A 1 308 ? 7.709   6.861   18.626 1.00 13.70  ? 350  TYR A O     1 
ATOM   2384 C CB    . TYR A 1 308 ? 5.754   9.205   17.959 1.00 14.44  ? 350  TYR A CB    1 
ATOM   2385 C CG    . TYR A 1 308 ? 4.424   9.803   17.635 1.00 13.70  ? 350  TYR A CG    1 
ATOM   2386 C CD1   . TYR A 1 308 ? 3.314   9.518   18.398 1.00 13.57  ? 350  TYR A CD1   1 
ATOM   2387 C CD2   . TYR A 1 308 ? 4.232   10.562  16.493 1.00 14.40  ? 350  TYR A CD2   1 
ATOM   2388 C CE1   . TYR A 1 308 ? 2.069   10.030  18.106 1.00 14.19  ? 350  TYR A CE1   1 
ATOM   2389 C CE2   . TYR A 1 308 ? 2.982   11.080  16.179 1.00 15.73  ? 350  TYR A CE2   1 
ATOM   2390 C CZ    . TYR A 1 308 ? 1.884   10.770  16.948 1.00 15.55  ? 350  TYR A CZ    1 
ATOM   2391 O OH    . TYR A 1 308 ? 0.616   11.301  16.690 1.00 15.04  ? 350  TYR A OH    1 
ATOM   2392 N N     . PHE A 1 309 ? 8.099   7.166   16.431 1.00 12.86  ? 351  PHE A N     1 
ATOM   2393 C CA    . PHE A 1 309 ? 9.489   6.738   16.474 1.00 12.39  ? 351  PHE A CA    1 
ATOM   2394 C C     . PHE A 1 309 ? 10.304  7.576   15.512 1.00 13.68  ? 351  PHE A C     1 
ATOM   2395 O O     . PHE A 1 309 ? 9.755   8.302   14.686 1.00 14.47  ? 351  PHE A O     1 
ATOM   2396 C CB    . PHE A 1 309 ? 9.635   5.245   16.198 1.00 13.96  ? 351  PHE A CB    1 
ATOM   2397 C CG    . PHE A 1 309 ? 9.323   4.816   14.785 1.00 16.37  ? 351  PHE A CG    1 
ATOM   2398 C CD1   . PHE A 1 309 ? 8.044   4.519   14.371 1.00 16.89  ? 351  PHE A CD1   1 
ATOM   2399 C CD2   . PHE A 1 309 ? 10.344  4.749   13.864 1.00 17.75  ? 351  PHE A CD2   1 
ATOM   2400 C CE1   . PHE A 1 309 ? 7.803   4.151   13.051 1.00 18.21  ? 351  PHE A CE1   1 
ATOM   2401 C CE2   . PHE A 1 309 ? 10.093  4.425   12.538 1.00 19.43  ? 351  PHE A CE2   1 
ATOM   2402 C CZ    . PHE A 1 309 ? 8.826   4.116   12.157 1.00 15.98  ? 351  PHE A CZ    1 
ATOM   2403 N N     . ALA A 1 310 ? 11.629  7.498   15.623 1.00 13.54  ? 352  ALA A N     1 
ATOM   2404 C CA    . ALA A 1 310 ? 12.489  8.198   14.695 1.00 13.98  ? 352  ALA A CA    1 
ATOM   2405 C C     . ALA A 1 310 ? 13.719  7.358   14.385 1.00 15.18  ? 352  ALA A C     1 
ATOM   2406 O O     . ALA A 1 310 ? 14.044  6.428   15.119 1.00 14.18  ? 352  ALA A O     1 
ATOM   2407 C CB    . ALA A 1 310 ? 12.873  9.513   15.224 1.00 14.94  ? 352  ALA A CB    1 
ATOM   2408 N N     . LEU A 1 311 ? 14.345  7.717   13.256 1.00 16.63  ? 353  LEU A N     1 
ATOM   2409 C CA    . LEU A 1 311 ? 15.630  7.166   12.817 1.00 17.44  ? 353  LEU A CA    1 
ATOM   2410 C C     . LEU A 1 311 ? 16.667  8.285   12.784 1.00 17.01  ? 353  LEU A C     1 
ATOM   2411 O O     . LEU A 1 311 ? 16.378  9.450   12.482 1.00 16.30  ? 353  LEU A O     1 
ATOM   2412 C CB    . LEU A 1 311 ? 15.435  6.481   11.439 1.00 16.80  ? 353  LEU A CB    1 
ATOM   2413 C CG    . LEU A 1 311 ? 14.598  5.213   11.492 1.00 18.63  ? 353  LEU A CG    1 
ATOM   2414 C CD1   . LEU A 1 311 ? 14.387  4.642   10.091 1.00 17.89  ? 353  LEU A CD1   1 
ATOM   2415 C CD2   . LEU A 1 311 ? 15.169  4.172   12.440 1.00 21.26  ? 353  LEU A CD2   1 
ATOM   2416 N N     . TYR A 1 312 ? 17.902  7.920   13.179 1.00 16.88  ? 354  TYR A N     1 
ATOM   2417 C CA    . TYR A 1 312 ? 18.979  8.866   13.371 1.00 16.59  ? 354  TYR A CA    1 
ATOM   2418 C C     . TYR A 1 312 ? 20.254  8.295   12.742 1.00 17.75  ? 354  TYR A C     1 
ATOM   2419 O O     . TYR A 1 312 ? 20.602  7.132   12.986 1.00 19.29  ? 354  TYR A O     1 
ATOM   2420 C CB    . TYR A 1 312 ? 19.251  9.119   14.863 1.00 15.84  ? 354  TYR A CB    1 
ATOM   2421 C CG    . TYR A 1 312 ? 18.042  9.388   15.735 1.00 14.07  ? 354  TYR A CG    1 
ATOM   2422 C CD1   . TYR A 1 312 ? 17.247  8.354   16.185 1.00 13.43  ? 354  TYR A CD1   1 
ATOM   2423 C CD2   . TYR A 1 312 ? 17.696  10.671  16.102 1.00 15.14  ? 354  TYR A CD2   1 
ATOM   2424 C CE1   . TYR A 1 312 ? 16.123  8.601   16.969 1.00 12.53  ? 354  TYR A CE1   1 
ATOM   2425 C CE2   . TYR A 1 312 ? 16.601  10.941  16.923 1.00 14.31  ? 354  TYR A CE2   1 
ATOM   2426 C CZ    . TYR A 1 312 ? 15.814  9.889   17.370 1.00 12.32  ? 354  TYR A CZ    1 
ATOM   2427 O OH    . TYR A 1 312 ? 14.741  10.080  18.195 1.00 11.68  ? 354  TYR A OH    1 
ATOM   2428 N N     . GLY A 1 313 ? 20.944  9.106   11.948 1.00 19.24  ? 355  GLY A N     1 
ATOM   2429 C CA    . GLY A 1 313 ? 22.246  8.706   11.420 1.00 20.83  ? 355  GLY A CA    1 
ATOM   2430 C C     . GLY A 1 313 ? 22.511  9.403   10.089 1.00 20.61  ? 355  GLY A C     1 
ATOM   2431 O O     . GLY A 1 313 ? 22.572  10.633  10.035 1.00 23.14  ? 355  GLY A O     1 
ATOM   2432 N N     . THR A 1 314 ? 22.676  8.613   9.032  1.00 26.69  ? 356  THR A N     1 
ATOM   2433 C CA    . THR A 1 314 ? 22.812  9.176   7.693  1.00 26.38  ? 356  THR A CA    1 
ATOM   2434 C C     . THR A 1 314 ? 21.703  8.663   6.794  1.00 26.41  ? 356  THR A C     1 
ATOM   2435 O O     . THR A 1 314 ? 21.007  7.719   7.159  1.00 23.99  ? 356  THR A O     1 
ATOM   2436 C CB    . THR A 1 314 ? 24.144  8.809   7.040  1.00 27.16  ? 356  THR A CB    1 
ATOM   2437 O OG1   . THR A 1 314 ? 24.158  7.388   6.822  1.00 23.39  ? 356  THR A OG1   1 
ATOM   2438 C CG2   . THR A 1 314 ? 25.303  9.286   7.887  1.00 28.20  ? 356  THR A CG2   1 
ATOM   2439 N N     . GLU A 1 315 ? 21.609  9.250   5.590  1.00 27.80  ? 357  GLU A N     1 
ATOM   2440 C CA    . GLU A 1 315 ? 20.642  8.771   4.613  1.00 28.83  ? 357  GLU A CA    1 
ATOM   2441 C C     . GLU A 1 315 ? 20.876  7.270   4.426  1.00 25.30  ? 357  GLU A C     1 
ATOM   2442 O O     . GLU A 1 315 ? 19.937  6.501   4.287  1.00 26.12  ? 357  GLU A O     1 
ATOM   2443 C CB    . GLU A 1 315 ? 20.742  9.549   3.291  1.00 34.94  ? 357  GLU A CB    1 
ATOM   2444 C CG    . GLU A 1 315 ? 20.511  11.055  3.416  1.00 42.32  ? 357  GLU A CG    1 
ATOM   2445 C CD    . GLU A 1 315 ? 21.718  11.930  3.780  1.00 58.52  ? 357  GLU A CD    1 
ATOM   2446 O OE1   . GLU A 1 315 ? 22.683  11.431  4.445  1.00 56.75  ? 357  GLU A OE1   1 
ATOM   2447 O OE2   . GLU A 1 315 ? 21.716  13.138  3.385  1.00 65.42  ? 357  GLU A OE2   1 
ATOM   2448 N N     . GLN A 1 316 ? 22.134  6.834   4.467  1.00 25.01  ? 358  GLN A N     1 
ATOM   2449 C CA    . GLN A 1 316 ? 22.416  5.438   4.188  1.00 29.99  ? 358  GLN A CA    1 
ATOM   2450 C C     . GLN A 1 316 ? 22.043  4.534   5.373  1.00 25.87  ? 358  GLN A C     1 
ATOM   2451 O O     . GLN A 1 316 ? 21.457  3.486   5.163  1.00 23.85  ? 358  GLN A O     1 
ATOM   2452 C CB    . GLN A 1 316 ? 23.860  5.276   3.719  1.00 37.57  ? 358  GLN A CB    1 
ATOM   2453 C CG    . GLN A 1 316 ? 23.983  4.135   2.733  1.00 44.88  ? 358  GLN A CG    1 
ATOM   2454 C CD    . GLN A 1 316 ? 25.364  4.030   2.142  1.00 54.11  ? 358  GLN A CD    1 
ATOM   2455 O OE1   . GLN A 1 316 ? 25.973  5.030   1.766  1.00 61.93  ? 358  GLN A OE1   1 
ATOM   2456 N NE2   . GLN A 1 316 ? 25.867  2.807   2.072  1.00 58.63  ? 358  GLN A NE2   1 
ATOM   2457 N N     . THR A 1 317 ? 22.363  4.912   6.621  1.00 25.78  ? 359  THR A N     1 
ATOM   2458 C CA    . THR A 1 317 ? 22.012  4.073   7.759  1.00 23.89  ? 359  THR A CA    1 
ATOM   2459 C C     . THR A 1 317 ? 20.490  4.035   7.920  1.00 22.08  ? 359  THR A C     1 
ATOM   2460 O O     . THR A 1 317 ? 19.933  2.961   8.198  1.00 23.87  ? 359  THR A O     1 
ATOM   2461 C CB    . THR A 1 317 ? 22.709  4.494   9.072  1.00 24.88  ? 359  THR A CB    1 
ATOM   2462 O OG1   . THR A 1 317 ? 22.210  5.733   9.558  1.00 22.59  ? 359  THR A OG1   1 
ATOM   2463 C CG2   . THR A 1 317 ? 24.203  4.634   8.890  1.00 28.37  ? 359  THR A CG2   1 
ATOM   2464 N N     . VAL A 1 318 ? 19.822  5.178   7.683  1.00 22.57  ? 360  VAL A N     1 
ATOM   2465 C CA    . VAL A 1 318 ? 18.362  5.250   7.735  1.00 21.67  ? 360  VAL A CA    1 
ATOM   2466 C C     . VAL A 1 318 ? 17.757  4.281   6.706  1.00 24.05  ? 360  VAL A C     1 
ATOM   2467 O O     . VAL A 1 318 ? 16.892  3.481   7.049  1.00 24.19  ? 360  VAL A O     1 
ATOM   2468 C CB    . VAL A 1 318 ? 17.850  6.691   7.558  1.00 23.75  ? 360  VAL A CB    1 
ATOM   2469 C CG1   . VAL A 1 318 ? 16.361  6.736   7.288  1.00 24.70  ? 360  VAL A CG1   1 
ATOM   2470 C CG2   . VAL A 1 318 ? 18.216  7.571   8.745  1.00 25.88  ? 360  VAL A CG2   1 
ATOM   2471 N N     . ALA A 1 319 ? 18.290  4.278   5.471  1.00 25.07  ? 361  ALA A N     1 
ATOM   2472 C CA    . ALA A 1 319 ? 17.797  3.399   4.421  1.00 24.33  ? 361  ALA A CA    1 
ATOM   2473 C C     . ALA A 1 319 ? 18.059  1.923   4.706  1.00 26.45  ? 361  ALA A C     1 
ATOM   2474 O O     . ALA A 1 319 ? 17.330  1.090   4.174  1.00 28.37  ? 361  ALA A O     1 
ATOM   2475 C CB    . ALA A 1 319 ? 18.364  3.802   3.070  1.00 23.54  ? 361  ALA A CB    1 
ATOM   2476 N N     . GLY A 1 320 ? 19.065  1.587   5.545  1.00 24.78  ? 362  GLY A N     1 
ATOM   2477 C CA    . GLY A 1 320 ? 19.333  0.208   5.937  1.00 24.61  ? 362  GLY A CA    1 
ATOM   2478 C C     . GLY A 1 320 ? 18.226  -0.437  6.774  1.00 26.13  ? 362  GLY A C     1 
ATOM   2479 O O     . GLY A 1 320 ? 18.057  -1.667  6.781  1.00 25.32  ? 362  GLY A O     1 
ATOM   2480 N N     . VAL A 1 321 ? 17.490  0.382   7.545  1.00 22.51  ? 363  VAL A N     1 
ATOM   2481 C CA    . VAL A 1 321 ? 16.524  -0.205  8.460  1.00 20.27  ? 363  VAL A CA    1 
ATOM   2482 C C     . VAL A 1 321 ? 15.084  0.179   8.126  1.00 17.94  ? 363  VAL A C     1 
ATOM   2483 O O     . VAL A 1 321 ? 14.165  -0.557  8.518  1.00 19.50  ? 363  VAL A O     1 
ATOM   2484 C CB    . VAL A 1 321 ? 16.876  0.134   9.915  1.00 20.18  ? 363  VAL A CB    1 
ATOM   2485 C CG1   . VAL A 1 321 ? 18.187  -0.528  10.312 1.00 23.58  ? 363  VAL A CG1   1 
ATOM   2486 C CG2   . VAL A 1 321 ? 16.910  1.625   10.177 1.00 20.91  ? 363  VAL A CG2   1 
ATOM   2487 N N     . GLU A 1 322 ? 14.878  1.267   7.390  1.00 18.92  ? 364  GLU A N     1 
ATOM   2488 C CA    . GLU A 1 322 ? 13.525  1.792   7.189  1.00 19.68  ? 364  GLU A CA    1 
ATOM   2489 C C     . GLU A 1 322 ? 12.637  0.763   6.491  1.00 23.29  ? 364  GLU A C     1 
ATOM   2490 O O     . GLU A 1 322 ? 11.494  0.554   6.894  1.00 19.16  ? 364  GLU A O     1 
ATOM   2491 C CB    . GLU A 1 322 ? 13.517  3.164   6.514  1.00 20.36  ? 364  GLU A CB    1 
ATOM   2492 C CG    . GLU A 1 322 ? 12.135  3.670   6.216  1.00 20.44  ? 364  GLU A CG    1 
ATOM   2493 C CD    . GLU A 1 322 ? 12.042  5.044   5.595  1.00 21.41  ? 364  GLU A CD    1 
ATOM   2494 O OE1   . GLU A 1 322 ? 13.058  5.768   5.579  1.00 21.79  ? 364  GLU A OE1   1 
ATOM   2495 O OE2   . GLU A 1 322 ? 10.922  5.391   5.139  1.00 23.43  ? 364  GLU A OE2   1 
ATOM   2496 N N     . PRO A 1 323 ? 13.092  0.057   5.443  1.00 20.47  ? 365  PRO A N     1 
ATOM   2497 C CA    . PRO A 1 323 ? 12.234  -0.957  4.845  1.00 23.67  ? 365  PRO A CA    1 
ATOM   2498 C C     . PRO A 1 323 ? 11.731  -2.055  5.771  1.00 22.16  ? 365  PRO A C     1 
ATOM   2499 O O     . PRO A 1 323 ? 10.561  -2.399  5.668  1.00 21.61  ? 365  PRO A O     1 
ATOM   2500 C CB    . PRO A 1 323 ? 13.119  -1.574  3.735  1.00 21.96  ? 365  PRO A CB    1 
ATOM   2501 C CG    . PRO A 1 323 ? 14.075  -0.438  3.387  1.00 23.18  ? 365  PRO A CG    1 
ATOM   2502 C CD    . PRO A 1 323 ? 14.374  0.242   4.720  1.00 22.75  ? 365  PRO A CD    1 
ATOM   2503 N N     . ILE A 1 324 ? 12.604  -2.620  6.637  1.00 20.77  ? 366  ILE A N     1 
ATOM   2504 C CA    . ILE A 1 324 ? 12.195  -3.693  7.530  1.00 21.83  ? 366  ILE A CA    1 
ATOM   2505 C C     . ILE A 1 324 ? 11.186  -3.150  8.539  1.00 19.21  ? 366  ILE A C     1 
ATOM   2506 O O     . ILE A 1 324 ? 10.251  -3.828  8.917  1.00 19.05  ? 366  ILE A O     1 
ATOM   2507 C CB    . ILE A 1 324 ? 13.388  -4.328  8.276  1.00 26.71  ? 366  ILE A CB    1 
ATOM   2508 C CG1   . ILE A 1 324 ? 14.413  -4.923  7.312  1.00 31.97  ? 366  ILE A CG1   1 
ATOM   2509 C CG2   . ILE A 1 324 ? 12.896  -5.370  9.265  1.00 28.34  ? 366  ILE A CG2   1 
ATOM   2510 C CD1   . ILE A 1 324 ? 15.762  -5.226  7.943  1.00 35.53  ? 366  ILE A CD1   1 
ATOM   2511 N N     . ILE A 1 325 ? 11.426  -1.930  9.040  1.00 18.34  ? 367  ILE A N     1 
ATOM   2512 C CA    . ILE A 1 325 ? 10.522  -1.316  10.006 1.00 17.68  ? 367  ILE A CA    1 
ATOM   2513 C C     . ILE A 1 325 ? 9.137   -1.125  9.394  1.00 17.88  ? 367  ILE A C     1 
ATOM   2514 O O     . ILE A 1 325 ? 8.123   -1.489  9.989  1.00 17.28  ? 367  ILE A O     1 
ATOM   2515 C CB    . ILE A 1 325 ? 11.129  -0.002  10.528 1.00 17.21  ? 367  ILE A CB    1 
ATOM   2516 C CG1   . ILE A 1 325 ? 12.407  -0.250  11.346 1.00 17.16  ? 367  ILE A CG1   1 
ATOM   2517 C CG2   . ILE A 1 325 ? 10.100  0.798   11.303 1.00 17.35  ? 367  ILE A CG2   1 
ATOM   2518 C CD1   . ILE A 1 325 ? 13.248  0.961   11.525 1.00 16.95  ? 367  ILE A CD1   1 
ATOM   2519 N N     . ARG A 1 326 ? 9.097   -0.577  8.192  1.00 17.99  ? 368  ARG A N     1 
ATOM   2520 C CA    . ARG A 1 326 ? 7.833   -0.387  7.479  1.00 19.00  ? 368  ARG A CA    1 
ATOM   2521 C C     . ARG A 1 326 ? 7.103   -1.711  7.268  1.00 19.59  ? 368  ARG A C     1 
ATOM   2522 O O     . ARG A 1 326 ? 5.910   -1.810  7.534  1.00 20.66  ? 368  ARG A O     1 
ATOM   2523 C CB    . ARG A 1 326 ? 8.067   0.299   6.133  1.00 20.35  ? 368  ARG A CB    1 
ATOM   2524 C CG    . ARG A 1 326 ? 8.334   1.786   6.226  1.00 22.31  ? 368  ARG A CG    1 
ATOM   2525 C CD    . ARG A 1 326 ? 8.349   2.420   4.855  1.00 22.04  ? 368  ARG A CD    1 
ATOM   2526 N NE    . ARG A 1 326 ? 8.553   3.844   4.978  1.00 21.72  ? 368  ARG A NE    1 
ATOM   2527 C CZ    . ARG A 1 326 ? 7.597   4.762   4.923  1.00 20.57  ? 368  ARG A CZ    1 
ATOM   2528 N NH1   . ARG A 1 326 ? 6.341   4.408   4.895  1.00 20.31  ? 368  ARG A NH1   1 
ATOM   2529 N NH2   . ARG A 1 326 ? 7.903   6.040   4.968  1.00 21.28  ? 368  ARG A NH2   1 
ATOM   2530 N N     . ALA A 1 327 ? 7.815   -2.760  6.826  1.00 21.06  ? 369  ALA A N     1 
ATOM   2531 C CA    . ALA A 1 327 ? 7.170   -4.049  6.616  1.00 21.86  ? 369  ALA A CA    1 
ATOM   2532 C C     . ALA A 1 327 ? 6.533   -4.633  7.883  1.00 21.21  ? 369  ALA A C     1 
ATOM   2533 O O     . ALA A 1 327 ? 5.418   -5.169  7.837  1.00 23.74  ? 369  ALA A O     1 
ATOM   2534 C CB    . ALA A 1 327 ? 8.141   -5.018  5.981  1.00 20.26  ? 369  ALA A CB    1 
ATOM   2535 N N     . THR A 1 328 ? 7.267   -4.579  9.003  1.00 19.86  ? 370  THR A N     1 
ATOM   2536 C CA    . THR A 1 328 ? 6.859   -5.145  10.279 1.00 20.73  ? 370  THR A CA    1 
ATOM   2537 C C     . THR A 1 328 ? 5.619   -4.398  10.770 1.00 20.67  ? 370  THR A C     1 
ATOM   2538 O O     . THR A 1 328 ? 4.662   -5.018  11.235 1.00 21.68  ? 370  THR A O     1 
ATOM   2539 C CB    . THR A 1 328 ? 8.005   -5.032  11.306 1.00 21.29  ? 370  THR A CB    1 
ATOM   2540 O OG1   . THR A 1 328 ? 9.165   -5.746  10.889 1.00 24.66  ? 370  THR A OG1   1 
ATOM   2541 C CG2   . THR A 1 328 ? 7.629   -5.555  12.671 1.00 23.14  ? 370  THR A CG2   1 
ATOM   2542 N N     . LEU A 1 329 ? 5.637   -3.057  10.647 1.00 18.89  ? 371  LEU A N     1 
ATOM   2543 C CA    . LEU A 1 329 ? 4.539   -2.276  11.186 1.00 18.78  ? 371  LEU A CA    1 
ATOM   2544 C C     . LEU A 1 329 ? 3.311   -2.333  10.266 1.00 18.91  ? 371  LEU A C     1 
ATOM   2545 O O     . LEU A 1 329 ? 2.181   -2.413  10.755 1.00 20.12  ? 371  LEU A O     1 
ATOM   2546 C CB    . LEU A 1 329 ? 5.020   -0.850  11.418 1.00 18.49  ? 371  LEU A CB    1 
ATOM   2547 C CG    . LEU A 1 329 ? 5.961   -0.692  12.609 1.00 20.49  ? 371  LEU A CG    1 
ATOM   2548 C CD1   . LEU A 1 329 ? 6.547   0.703   12.630 1.00 20.69  ? 371  LEU A CD1   1 
ATOM   2549 C CD2   . LEU A 1 329 ? 5.211   -0.959  13.889 1.00 23.17  ? 371  LEU A CD2   1 
ATOM   2550 N N     . THR A 1 330 ? 3.527   -2.341  8.938  1.00 19.75  ? 372  THR A N     1 
ATOM   2551 C CA    . THR A 1 330 ? 2.387   -2.446  8.038  1.00 20.18  ? 372  THR A CA    1 
ATOM   2552 C C     . THR A 1 330 ? 1.684   -3.794  8.267  1.00 24.14  ? 372  THR A C     1 
ATOM   2553 O O     . THR A 1 330 ? 0.440   -3.856  8.279  1.00 22.41  ? 372  THR A O     1 
ATOM   2554 C CB    . THR A 1 330 ? 2.810   -2.227  6.575  1.00 22.98  ? 372  THR A CB    1 
ATOM   2555 O OG1   . THR A 1 330 ? 3.371   -0.912  6.483  1.00 23.87  ? 372  THR A OG1   1 
ATOM   2556 C CG2   . THR A 1 330 ? 1.664   -2.348  5.590  1.00 26.85  ? 372  THR A CG2   1 
ATOM   2557 N N     . ALA A 1 331 ? 2.459   -4.861  8.509  1.00 21.84  ? 373  ALA A N     1 
ATOM   2558 C CA    . ALA A 1 331 ? 1.896   -6.201  8.671  1.00 22.08  ? 373  ALA A CA    1 
ATOM   2559 C C     . ALA A 1 331 ? 1.018   -6.246  9.925  1.00 22.75  ? 373  ALA A C     1 
ATOM   2560 O O     . ALA A 1 331 ? 0.062   -7.011  9.974  1.00 22.84  ? 373  ALA A O     1 
ATOM   2561 C CB    . ALA A 1 331 ? 2.974   -7.277  8.680  1.00 22.43  ? 373  ALA A CB    1 
ATOM   2562 N N     . SER A 1 332 ? 1.252   -5.332  10.897 1.00 18.91  ? 374  SER A N     1 
ATOM   2563 C CA    . SER A 1 332 ? 0.456   -5.263  12.101 1.00 19.68  ? 374  SER A CA    1 
ATOM   2564 C C     . SER A 1 332 ? -0.815  -4.435  11.923 1.00 20.37  ? 374  SER A C     1 
ATOM   2565 O O     . SER A 1 332 ? -1.477  -4.181  12.917 1.00 20.45  ? 374  SER A O     1 
ATOM   2566 C CB    . SER A 1 332 ? 1.241   -4.684  13.292 1.00 19.03  ? 374  SER A CB    1 
ATOM   2567 O OG    . SER A 1 332 ? 1.467   -3.285  13.135 1.00 17.14  ? 374  SER A OG    1 
ATOM   2568 N N     . GLY A 1 333 ? -1.117  -3.939  10.716 1.00 21.45  ? 375  GLY A N     1 
ATOM   2569 C CA    . GLY A 1 333 ? -2.256  -3.044  10.544 1.00 22.50  ? 375  GLY A CA    1 
ATOM   2570 C C     . GLY A 1 333 ? -1.943  -1.559  10.687 1.00 21.36  ? 375  GLY A C     1 
ATOM   2571 O O     . GLY A 1 333 ? -2.845  -0.717  10.763 1.00 21.97  ? 375  GLY A O     1 
ATOM   2572 N N     . GLY A 1 334 ? -0.662  -1.198  10.756 1.00 18.36  ? 376  GLY A N     1 
ATOM   2573 C CA    . GLY A 1 334 ? -0.311  0.202   10.952 1.00 19.50  ? 376  GLY A CA    1 
ATOM   2574 C C     . GLY A 1 334 ? -0.025  0.892   9.617  1.00 22.29  ? 376  GLY A C     1 
ATOM   2575 O O     . GLY A 1 334 ? 0.471   0.257   8.685  1.00 25.78  ? 376  GLY A O     1 
ATOM   2576 N N     . GLU A 1 335 ? -0.297  2.188   9.555  1.00 19.05  ? 377  GLU A N     1 
ATOM   2577 C CA    . GLU A 1 335 ? 0.055   3.005   8.422  1.00 20.24  ? 377  GLU A CA    1 
ATOM   2578 C C     . GLU A 1 335 ? 1.212   3.883   8.859  1.00 18.77  ? 377  GLU A C     1 
ATOM   2579 O O     . GLU A 1 335 ? 1.042   4.678   9.783  1.00 20.21  ? 377  GLU A O     1 
ATOM   2580 C CB    . GLU A 1 335 ? -1.156  3.843   8.000  1.00 24.87  ? 377  GLU A CB    1 
ATOM   2581 C CG    . GLU A 1 335 ? -0.922  4.633   6.724  1.00 31.26  ? 377  GLU A CG    1 
ATOM   2582 C CD    . GLU A 1 335 ? -2.101  5.455   6.211  1.00 36.88  ? 377  GLU A CD    1 
ATOM   2583 O OE1   . GLU A 1 335 ? -3.095  5.634   6.955  1.00 37.08  ? 377  GLU A OE1   1 
ATOM   2584 O OE2   . GLU A 1 335 ? -1.988  5.955   5.075  1.00 44.41  ? 377  GLU A OE2   1 
ATOM   2585 N N     . VAL A 1 336 ? 2.361   3.756   8.187  1.00 16.94  ? 378  VAL A N     1 
ATOM   2586 C CA    . VAL A 1 336 ? 3.562   4.475   8.574  1.00 18.31  ? 378  VAL A CA    1 
ATOM   2587 C C     . VAL A 1 336 ? 3.648   5.767   7.770  1.00 20.66  ? 378  VAL A C     1 
ATOM   2588 O O     . VAL A 1 336 ? 3.683   5.735   6.539  1.00 21.60  ? 378  VAL A O     1 
ATOM   2589 C CB    . VAL A 1 336 ? 4.798   3.609   8.367  1.00 17.52  ? 378  VAL A CB    1 
ATOM   2590 C CG1   . VAL A 1 336 ? 6.056   4.330   8.768  1.00 19.01  ? 378  VAL A CG1   1 
ATOM   2591 C CG2   . VAL A 1 336 ? 4.687   2.277   9.093  1.00 18.57  ? 378  VAL A CG2   1 
ATOM   2592 N N     . LEU A 1 337 ? 3.762   6.893   8.479  1.00 17.76  ? 379  LEU A N     1 
ATOM   2593 C CA    . LEU A 1 337 ? 3.646   8.225   7.911  1.00 20.34  ? 379  LEU A CA    1 
ATOM   2594 C C     . LEU A 1 337 ? 4.874   9.044   8.299  1.00 21.34  ? 379  LEU A C     1 
ATOM   2595 O O     . LEU A 1 337 ? 5.415   8.880   9.405  1.00 18.69  ? 379  LEU A O     1 
ATOM   2596 C CB    . LEU A 1 337 ? 2.355   8.887   8.424  1.00 23.11  ? 379  LEU A CB    1 
ATOM   2597 C CG    . LEU A 1 337 ? 1.062   8.138   8.078  1.00 28.02  ? 379  LEU A CG    1 
ATOM   2598 C CD1   . LEU A 1 337 ? -0.037  8.456   9.081  1.00 31.96  ? 379  LEU A CD1   1 
ATOM   2599 C CD2   . LEU A 1 337 ? 0.594   8.466   6.655  1.00 29.05  ? 379  LEU A CD2   1 
ATOM   2600 N N     . THR A 1 338 ? 5.276   9.943   7.388  1.00 19.30  ? 380  THR A N     1 
ATOM   2601 C CA    . THR A 1 338 ? 6.413   10.822  7.579  1.00 19.17  ? 380  THR A CA    1 
ATOM   2602 C C     . THR A 1 338 ? 5.936   12.279  7.541  1.00 18.80  ? 380  THR A C     1 
ATOM   2603 O O     . THR A 1 338 ? 4.749   12.529  7.408  1.00 19.40  ? 380  THR A O     1 
ATOM   2604 C CB    . THR A 1 338 ? 7.474   10.527  6.523  1.00 26.34  ? 380  THR A CB    1 
ATOM   2605 O OG1   . THR A 1 338 ? 6.874   10.910  5.287  1.00 26.27  ? 380  THR A OG1   1 
ATOM   2606 C CG2   . THR A 1 338 ? 7.858   9.066   6.511  1.00 29.14  ? 380  THR A CG2   1 
ATOM   2607 N N     . ALA A 1 339 ? 6.869   13.224  7.720  1.00 20.33  ? 381  ALA A N     1 
ATOM   2608 C CA    . ALA A 1 339 ? 6.570   14.649  7.839  1.00 20.54  ? 381  ALA A CA    1 
ATOM   2609 C C     . ALA A 1 339 ? 5.846   15.173  6.605  1.00 25.55  ? 381  ALA A C     1 
ATOM   2610 O O     . ALA A 1 339 ? 4.956   16.029  6.727  1.00 26.62  ? 381  ALA A O     1 
ATOM   2611 C CB    . ALA A 1 339 ? 7.826   15.424  8.098  1.00 23.16  ? 381  ALA A CB    1 
ATOM   2612 N N     . ALA A 1 340 ? 6.169   14.580  5.444  1.00 29.18  ? 382  ALA A N     1 
ATOM   2613 C CA    . ALA A 1 340 ? 5.597   15.014  4.176  1.00 31.42  ? 382  ALA A CA    1 
ATOM   2614 C C     . ALA A 1 340 ? 4.106   14.699  4.106  1.00 31.13  ? 382  ALA A C     1 
ATOM   2615 O O     . ALA A 1 340 ? 3.362   15.361  3.390  1.00 34.90  ? 382  ALA A O     1 
ATOM   2616 C CB    . ALA A 1 340 ? 6.350   14.380  3.036  1.00 34.85  ? 382  ALA A CB    1 
ATOM   2617 N N     . GLU A 1 341 ? 3.648   13.701  4.865  1.00 25.61  ? 383  GLU A N     1 
ATOM   2618 C CA    . GLU A 1 341 ? 2.250   13.335  4.868  1.00 25.35  ? 383  GLU A CA    1 
ATOM   2619 C C     . GLU A 1 341 ? 1.516   14.025  6.005  1.00 28.01  ? 383  GLU A C     1 
ATOM   2620 O O     . GLU A 1 341 ? 0.316   13.961  6.018  1.00 33.14  ? 383  GLU A O     1 
ATOM   2621 C CB    . GLU A 1 341 ? 2.039   11.827  5.056  1.00 28.51  ? 383  GLU A CB    1 
ATOM   2622 C CG    . GLU A 1 341 ? 2.258   10.995  3.807  1.00 30.80  ? 383  GLU A CG    1 
ATOM   2623 C CD    . GLU A 1 341 ? 3.622   10.359  3.678  1.00 37.78  ? 383  GLU A CD    1 
ATOM   2624 O OE1   . GLU A 1 341 ? 4.002   9.546   4.556  1.00 34.14  ? 383  GLU A OE1   1 
ATOM   2625 O OE2   . GLU A 1 341 ? 4.320   10.715  2.716  1.00 47.92  ? 383  GLU A OE2   1 
ATOM   2626 N N     . MET A 1 342 ? 2.213   14.581  7.005  1.00 26.64  ? 384  MET A N     1 
ATOM   2627 C CA    . MET A 1 342 ? 1.528   15.016  8.224  1.00 25.98  ? 384  MET A CA    1 
ATOM   2628 C C     . MET A 1 342 ? 1.679   16.532  8.408  1.00 30.89  ? 384  MET A C     1 
ATOM   2629 O O     . MET A 1 342 ? 1.589   17.065  9.523  1.00 27.95  ? 384  MET A O     1 
ATOM   2630 C CB    . MET A 1 342 ? 2.108   14.226  9.402  1.00 26.39  ? 384  MET A CB    1 
ATOM   2631 C CG    . MET A 1 342 ? 1.807   12.735  9.281  1.00 28.80  ? 384  MET A CG    1 
ATOM   2632 S SD    . MET A 1 342 ? 0.029   12.404  9.001  1.00 40.86  ? 384  MET A SD    1 
ATOM   2633 C CE    . MET A 1 342 ? -0.520  13.132  10.546 1.00 25.18  ? 384  MET A CE    1 
ATOM   2634 N N     . GLU A 1 343 ? 1.792   17.255  7.278  1.00 32.33  ? 385  GLU A N     1 
ATOM   2635 C CA    . GLU A 1 343 ? 1.984   18.695  7.303  1.00 34.38  ? 385  GLU A CA    1 
ATOM   2636 C C     . GLU A 1 343 ? 0.777   19.358  7.940  1.00 29.81  ? 385  GLU A C     1 
ATOM   2637 O O     . GLU A 1 343 ? -0.374  19.053  7.613  1.00 32.09  ? 385  GLU A O     1 
ATOM   2638 C CB    . GLU A 1 343 ? 2.243   19.263  5.905  1.00 43.85  ? 385  GLU A CB    1 
ATOM   2639 C CG    . GLU A 1 343 ? 3.552   18.743  5.321  1.00 53.68  ? 385  GLU A CG    1 
ATOM   2640 C CD    . GLU A 1 343 ? 3.957   19.323  3.977  1.00 66.26  ? 385  GLU A CD    1 
ATOM   2641 O OE1   . GLU A 1 343 ? 3.263   20.259  3.520  1.00 73.79  ? 385  GLU A OE1   1 
ATOM   2642 O OE2   . GLU A 1 343 ? 4.960   18.835  3.390  1.00 65.78  ? 385  GLU A OE2   1 
ATOM   2643 N N     . GLY A 1 344 ? 1.062   20.190  8.939  1.00 28.54  ? 386  GLY A N     1 
ATOM   2644 C CA    . GLY A 1 344 ? 0.017   20.891  9.649  1.00 30.56  ? 386  GLY A CA    1 
ATOM   2645 C C     . GLY A 1 344 ? -0.633  20.036  10.732 1.00 28.99  ? 386  GLY A C     1 
ATOM   2646 O O     . GLY A 1 344 ? -1.614  20.462  11.351 1.00 27.49  ? 386  GLY A O     1 
ATOM   2647 N N     . ASN A 1 345 ? -0.149  18.796  10.931 1.00 23.04  ? 387  ASN A N     1 
ATOM   2648 C CA    . ASN A 1 345 ? -0.775  17.972  11.961 1.00 19.81  ? 387  ASN A CA    1 
ATOM   2649 C C     . ASN A 1 345 ? -0.099  18.291  13.280 1.00 18.46  ? 387  ASN A C     1 
ATOM   2650 O O     . ASN A 1 345 ? 1.105   18.113  13.357 1.00 18.13  ? 387  ASN A O     1 
ATOM   2651 C CB    . ASN A 1 345 ? -0.658  16.484  11.675 1.00 19.97  ? 387  ASN A CB    1 
ATOM   2652 C CG    . ASN A 1 345 ? -1.400  15.671  12.712 1.00 22.25  ? 387  ASN A CG    1 
ATOM   2653 O OD1   . ASN A 1 345 ? -0.937  15.515  13.848 1.00 21.22  ? 387  ASN A OD1   1 
ATOM   2654 N ND2   . ASN A 1 345 ? -2.542  15.122  12.343 1.00 22.59  ? 387  ASN A ND2   1 
ATOM   2655 N N     . PRO A 1 346 ? -0.791  18.881  14.276 1.00 17.91  ? 388  PRO A N     1 
ATOM   2656 C CA    . PRO A 1 346 ? -0.122  19.388  15.474 1.00 17.77  ? 388  PRO A CA    1 
ATOM   2657 C C     . PRO A 1 346 ? 0.419   18.267  16.369 1.00 16.54  ? 388  PRO A C     1 
ATOM   2658 O O     . PRO A 1 346 ? 1.390   18.503  17.071 1.00 16.81  ? 388  PRO A O     1 
ATOM   2659 C CB    . PRO A 1 346 ? -1.185  20.204  16.204 1.00 19.06  ? 388  PRO A CB    1 
ATOM   2660 C CG    . PRO A 1 346 ? -2.487  19.600  15.750 1.00 20.71  ? 388  PRO A CG    1 
ATOM   2661 C CD    . PRO A 1 346 ? -2.237  19.163  14.318 1.00 19.89  ? 388  PRO A CD    1 
ATOM   2662 N N     . TRP A 1 347 ? -0.166  17.067  16.293 1.00 15.84  ? 389  TRP A N     1 
ATOM   2663 C CA    . TRP A 1 347 ? 0.356   15.944  17.054 1.00 15.52  ? 389  TRP A CA    1 
ATOM   2664 C C     . TRP A 1 347 ? 1.675   15.458  16.449 1.00 16.16  ? 389  TRP A C     1 
ATOM   2665 O O     . TRP A 1 347 ? 2.670   15.220  17.160 1.00 14.35  ? 389  TRP A O     1 
ATOM   2666 C CB    . TRP A 1 347 ? -0.668  14.825  17.157 1.00 15.87  ? 389  TRP A CB    1 
ATOM   2667 C CG    . TRP A 1 347 ? -1.849  15.203  17.994 1.00 16.92  ? 389  TRP A CG    1 
ATOM   2668 C CD1   . TRP A 1 347 ? -1.958  15.148  19.356 1.00 15.60  ? 389  TRP A CD1   1 
ATOM   2669 C CD2   . TRP A 1 347 ? -3.049  15.837  17.524 1.00 15.84  ? 389  TRP A CD2   1 
ATOM   2670 N NE1   . TRP A 1 347 ? -3.170  15.634  19.749 1.00 16.51  ? 389  TRP A NE1   1 
ATOM   2671 C CE2   . TRP A 1 347 ? -3.870  16.056  18.638 1.00 16.86  ? 389  TRP A CE2   1 
ATOM   2672 C CE3   . TRP A 1 347 ? -3.531  16.166  16.254 1.00 18.09  ? 389  TRP A CE3   1 
ATOM   2673 C CZ2   . TRP A 1 347 ? -5.148  16.598  18.528 1.00 18.50  ? 389  TRP A CZ2   1 
ATOM   2674 C CZ3   . TRP A 1 347 ? -4.767  16.748  16.151 1.00 18.98  ? 389  TRP A CZ3   1 
ATOM   2675 C CH2   . TRP A 1 347 ? -5.573  16.949  17.266 1.00 18.31  ? 389  TRP A CH2   1 
ATOM   2676 N N     . PHE A 1 348 ? 1.736   15.327  15.121 1.00 15.92  ? 390  PHE A N     1 
ATOM   2677 C CA    . PHE A 1 348 ? 3.002   14.991  14.485 1.00 16.01  ? 390  PHE A CA    1 
ATOM   2678 C C     . PHE A 1 348 ? 4.095   16.007  14.829 1.00 14.79  ? 390  PHE A C     1 
ATOM   2679 O O     . PHE A 1 348 ? 5.230   15.633  15.132 1.00 15.77  ? 390  PHE A O     1 
ATOM   2680 C CB    . PHE A 1 348 ? 2.871   14.871  12.963 1.00 16.79  ? 390  PHE A CB    1 
ATOM   2681 C CG    . PHE A 1 348 ? 4.089   14.259  12.322 1.00 17.11  ? 390  PHE A CG    1 
ATOM   2682 C CD1   . PHE A 1 348 ? 5.176   15.041  11.972 1.00 16.80  ? 390  PHE A CD1   1 
ATOM   2683 C CD2   . PHE A 1 348 ? 4.163   12.895  12.118 1.00 17.19  ? 390  PHE A CD2   1 
ATOM   2684 C CE1   . PHE A 1 348 ? 6.306   14.480  11.414 1.00 16.80  ? 390  PHE A CE1   1 
ATOM   2685 C CE2   . PHE A 1 348 ? 5.287   12.326  11.537 1.00 16.89  ? 390  PHE A CE2   1 
ATOM   2686 C CZ    . PHE A 1 348 ? 6.377   13.111  11.235 1.00 16.73  ? 390  PHE A CZ    1 
ATOM   2687 N N     . HIS A 1 349 ? 3.755   17.303  14.824 1.00 15.16  ? 391  HIS A N     1 
ATOM   2688 C CA    . HIS A 1 349 ? 4.711   18.340  15.115 1.00 16.90  ? 391  HIS A CA    1 
ATOM   2689 C C     . HIS A 1 349 ? 5.192   18.213  16.564 1.00 14.84  ? 391  HIS A C     1 
ATOM   2690 O O     . HIS A 1 349 ? 6.387   18.329  16.836 1.00 15.97  ? 391  HIS A O     1 
ATOM   2691 C CB    . HIS A 1 349 ? 4.106   19.716  14.847 1.00 19.39  ? 391  HIS A CB    1 
ATOM   2692 C CG    . HIS A 1 349 ? 5.069   20.810  15.171 1.00 22.50  ? 391  HIS A CG    1 
ATOM   2693 N ND1   . HIS A 1 349 ? 6.181   21.074  14.399 1.00 26.33  ? 391  HIS A ND1   1 
ATOM   2694 C CD2   . HIS A 1 349 ? 5.132   21.632  16.226 1.00 26.37  ? 391  HIS A CD2   1 
ATOM   2695 C CE1   . HIS A 1 349 ? 6.867   22.066  14.955 1.00 27.70  ? 391  HIS A CE1   1 
ATOM   2696 N NE2   . HIS A 1 349 ? 6.247   22.410  16.066 1.00 29.76  ? 391  HIS A NE2   1 
ATOM   2697 N N     . HIS A 1 350 ? 4.245   17.957  17.468 1.00 16.52  ? 392  HIS A N     1 
ATOM   2698 C CA    . HIS A 1 350 ? 4.554   17.730  18.875 1.00 15.48  ? 392  HIS A CA    1 
ATOM   2699 C C     . HIS A 1 350 ? 5.615   16.634  19.083 1.00 15.14  ? 392  HIS A C     1 
ATOM   2700 O O     . HIS A 1 350 ? 6.629   16.841  19.773 1.00 15.77  ? 392  HIS A O     1 
ATOM   2701 C CB    . HIS A 1 350 ? 3.241   17.477  19.625 1.00 16.97  ? 392  HIS A CB    1 
ATOM   2702 C CG    . HIS A 1 350 ? 3.408   17.393  21.112 1.00 18.55  ? 392  HIS A CG    1 
ATOM   2703 N ND1   . HIS A 1 350 ? 3.336   18.523  21.887 1.00 20.85  ? 392  HIS A ND1   1 
ATOM   2704 C CD2   . HIS A 1 350 ? 3.594   16.347  21.954 1.00 20.03  ? 392  HIS A CD2   1 
ATOM   2705 C CE1   . HIS A 1 350 ? 3.500   18.178  23.169 1.00 22.32  ? 392  HIS A CE1   1 
ATOM   2706 N NE2   . HIS A 1 350 ? 3.691   16.883  23.227 1.00 19.36  ? 392  HIS A NE2   1 
ATOM   2707 N N     . HIS A 1 351 ? 5.445   15.499  18.430 1.00 13.66  ? 393  HIS A N     1 
ATOM   2708 C CA    . HIS A 1 351 ? 6.349   14.380  18.608 1.00 14.27  ? 393  HIS A CA    1 
ATOM   2709 C C     . HIS A 1 351 ? 7.642   14.536  17.812 1.00 15.34  ? 393  HIS A C     1 
ATOM   2710 O O     . HIS A 1 351 ? 8.687   14.112  18.273 1.00 15.79  ? 393  HIS A O     1 
ATOM   2711 C CB    . HIS A 1 351 ? 5.615   13.071  18.322 1.00 14.75  ? 393  HIS A CB    1 
ATOM   2712 C CG    . HIS A 1 351 ? 4.636   12.696  19.352 1.00 15.27  ? 393  HIS A CG    1 
ATOM   2713 N ND1   . HIS A 1 351 ? 3.272   12.910  19.383 1.00 18.17  ? 393  HIS A ND1   1 
ATOM   2714 C CD2   . HIS A 1 351 ? 4.955   12.102  20.512 1.00 14.04  ? 393  HIS A CD2   1 
ATOM   2715 C CE1   . HIS A 1 351 ? 2.798   12.456  20.541 1.00 14.51  ? 393  HIS A CE1   1 
ATOM   2716 N NE2   . HIS A 1 351 ? 3.799   11.958  21.210 1.00 16.91  ? 393  HIS A NE2   1 
ATOM   2717 N N     . GLN A 1 352 ? 7.581   15.150  16.612 1.00 15.98  ? 394  GLN A N     1 
ATOM   2718 C CA    . GLN A 1 352 ? 8.775   15.472  15.829 1.00 17.63  ? 394  GLN A CA    1 
ATOM   2719 C C     . GLN A 1 352 ? 9.711   16.346  16.672 1.00 16.03  ? 394  GLN A C     1 
ATOM   2720 O O     . GLN A 1 352 ? 10.923  16.171  16.601 1.00 15.84  ? 394  GLN A O     1 
ATOM   2721 C CB    . GLN A 1 352 ? 8.424   16.227  14.539 1.00 22.70  ? 394  GLN A CB    1 
ATOM   2722 C CG    . GLN A 1 352 ? 9.562   17.138  14.062 1.00 31.05  ? 394  GLN A CG    1 
ATOM   2723 C CD    . GLN A 1 352 ? 9.173   17.905  12.834 1.00 42.36  ? 394  GLN A CD    1 
ATOM   2724 O OE1   . GLN A 1 352 ? 8.984   19.115  12.915 1.00 56.72  ? 394  GLN A OE1   1 
ATOM   2725 N NE2   . GLN A 1 352 ? 9.029   17.203  11.711 1.00 40.47  ? 394  GLN A NE2   1 
ATOM   2726 N N     . THR A 1 353 ? 9.130   17.240  17.481 1.00 13.99  ? 395  THR A N     1 
ATOM   2727 C CA    . THR A 1 353 ? 9.910   18.095  18.369 1.00 15.11  ? 395  THR A CA    1 
ATOM   2728 C C     . THR A 1 353 ? 10.541  17.215  19.457 1.00 13.60  ? 395  THR A C     1 
ATOM   2729 O O     . THR A 1 353 ? 11.727  17.316  19.736 1.00 13.77  ? 395  THR A O     1 
ATOM   2730 C CB    . THR A 1 353 ? 9.048   19.235  18.921 1.00 17.22  ? 395  THR A CB    1 
ATOM   2731 O OG1   . THR A 1 353 ? 8.627   20.059  17.820 1.00 18.19  ? 395  THR A OG1   1 
ATOM   2732 C CG2   . THR A 1 353 ? 9.829   20.113  19.862 1.00 17.63  ? 395  THR A CG2   1 
ATOM   2733 N N     . LEU A 1 354 ? 9.724   16.433  20.142 1.00 13.58  ? 396  LEU A N     1 
ATOM   2734 C CA    . LEU A 1 354 ? 10.217  15.624  21.255 1.00 14.99  ? 396  LEU A CA    1 
ATOM   2735 C C     . LEU A 1 354 ? 11.348  14.709  20.824 1.00 13.70  ? 396  LEU A C     1 
ATOM   2736 O O     . LEU A 1 354 ? 12.318  14.517  21.574 1.00 13.04  ? 396  LEU A O     1 
ATOM   2737 C CB    . LEU A 1 354 ? 9.103   14.755  21.843 1.00 14.88  ? 396  LEU A CB    1 
ATOM   2738 C CG    . LEU A 1 354 ? 8.027   15.436  22.680 1.00 17.39  ? 396  LEU A CG    1 
ATOM   2739 C CD1   . LEU A 1 354 ? 6.931   14.410  23.033 1.00 17.52  ? 396  LEU A CD1   1 
ATOM   2740 C CD2   . LEU A 1 354 ? 8.643   16.093  23.930 1.00 17.14  ? 396  LEU A CD2   1 
ATOM   2741 N N     . MET A 1 355 ? 11.195  14.083  19.649 1.00 14.32  ? 397  MET A N     1 
ATOM   2742 C CA    . MET A 1 355 ? 12.116  13.004  19.292 1.00 14.38  ? 397  MET A CA    1 
ATOM   2743 C C     . MET A 1 355 ? 13.468  13.549  18.770 1.00 12.47  ? 397  MET A C     1 
ATOM   2744 O O     . MET A 1 355 ? 14.399  12.791  18.487 1.00 12.73  ? 397  MET A O     1 
ATOM   2745 C CB    . MET A 1 355 ? 11.437  12.045  18.312 1.00 15.33  ? 397  MET A CB    1 
ATOM   2746 C CG    . MET A 1 355 ? 10.248  11.311  18.937 1.00 14.56  ? 397  MET A CG    1 
ATOM   2747 S SD    . MET A 1 355 ? 9.521   10.063  17.780 1.00 14.12  ? 397  MET A SD    1 
ATOM   2748 C CE    . MET A 1 355 ? 9.037   11.070  16.377 1.00 15.77  ? 397  MET A CE    1 
ATOM   2749 N N     . GLN A 1 356 ? 13.628  14.870  18.705 1.00 13.67  ? 398  GLN A N     1 
ATOM   2750 C CA    . GLN A 1 356 ? 14.950  15.489  18.488 1.00 14.74  ? 398  GLN A CA    1 
ATOM   2751 C C     . GLN A 1 356 ? 15.432  16.263  19.722 1.00 14.53  ? 398  GLN A C     1 
ATOM   2752 O O     . GLN A 1 356 ? 16.344  17.082  19.629 1.00 15.90  ? 398  GLN A O     1 
ATOM   2753 C CB    . GLN A 1 356 ? 14.995  16.340  17.222 1.00 18.00  ? 398  GLN A CB    1 
ATOM   2754 C CG    . GLN A 1 356 ? 13.988  17.457  17.180 1.00 17.94  ? 398  GLN A CG    1 
ATOM   2755 C CD    . GLN A 1 356 ? 14.136  18.269  15.915 1.00 22.98  ? 398  GLN A CD    1 
ATOM   2756 O OE1   . GLN A 1 356 ? 15.213  18.734  15.576 1.00 26.49  ? 398  GLN A OE1   1 
ATOM   2757 N NE2   . GLN A 1 356 ? 13.045  18.479  15.227 1.00 20.49  ? 398  GLN A NE2   1 
ATOM   2758 N N     . GLY A 1 357 ? 14.725  16.074  20.839 1.00 14.96  ? 399  GLY A N     1 
ATOM   2759 C CA    . GLY A 1 357 ? 15.029  16.787  22.077 1.00 14.96  ? 399  GLY A CA    1 
ATOM   2760 C C     . GLY A 1 357 ? 14.773  18.285  21.993 1.00 17.29  ? 399  GLY A C     1 
ATOM   2761 O O     . GLY A 1 357 ? 15.519  19.080  22.574 1.00 16.15  ? 399  GLY A O     1 
ATOM   2762 N N     . GLY A 1 358 ? 13.717  18.671  21.273 1.00 18.02  ? 400  GLY A N     1 
ATOM   2763 C CA    . GLY A 1 358 ? 13.340  20.070  21.157 1.00 19.48  ? 400  GLY A CA    1 
ATOM   2764 C C     . GLY A 1 358 ? 12.394  20.488  22.287 1.00 20.10  ? 400  GLY A C     1 
ATOM   2765 O O     . GLY A 1 358 ? 11.698  19.667  22.849 1.00 20.49  ? 400  GLY A O     1 
ATOM   2766 N N     . LEU A 1 359 ? 12.273  21.806  22.513 1.00 25.82  ? 401  LEU A N     1 
ATOM   2767 C CA    . LEU A 1 359 ? 11.387  22.318  23.551 1.00 28.78  ? 401  LEU A CA    1 
ATOM   2768 C C     . LEU A 1 359 ? 10.003  22.596  22.946 1.00 28.57  ? 401  LEU A C     1 
ATOM   2769 O O     . LEU A 1 359 ? 9.969   23.261  21.932 1.00 27.48  ? 401  LEU A O     1 
ATOM   2770 C CB    . LEU A 1 359 ? 12.034  23.617  24.056 1.00 34.31  ? 401  LEU A CB    1 
ATOM   2771 C CG    . LEU A 1 359 ? 13.537  23.569  24.354 1.00 37.38  ? 401  LEU A CG    1 
ATOM   2772 C CD1   . LEU A 1 359 ? 14.109  24.967  24.505 1.00 41.26  ? 401  LEU A CD1   1 
ATOM   2773 C CD2   . LEU A 1 359 ? 13.783  22.782  25.620 1.00 37.64  ? 401  LEU A CD2   1 
ATOM   2774 N N     . ASN A 1 360 ? 8.888   22.056  23.476 1.00 37.41  ? 402  ASN A N     1 
ATOM   2775 C CA    . ASN A 1 360 ? 7.570   22.337  22.886 1.00 42.88  ? 402  ASN A CA    1 
ATOM   2776 C C     . ASN A 1 360 ? 7.003   23.617  23.509 1.00 49.16  ? 402  ASN A C     1 
ATOM   2777 O O     . ASN A 1 360 ? 7.501   24.080  24.533 1.00 45.17  ? 402  ASN A O     1 
ATOM   2778 C CB    . ASN A 1 360 ? 6.545   21.181  22.953 1.00 38.56  ? 402  ASN A CB    1 
ATOM   2779 C CG    . ASN A 1 360 ? 6.524   20.255  21.732 1.00 36.68  ? 402  ASN A CG    1 
ATOM   2780 O OD1   . ASN A 1 360 ? 6.267   20.671  20.594 1.00 33.47  ? 402  ASN A OD1   1 
ATOM   2781 N ND2   . ASN A 1 360 ? 6.768   18.967  21.937 1.00 27.10  ? 402  ASN A ND2   1 
ATOM   2782 N N     . LEU A 1 361 ? 5.958   24.176  22.865 1.00 59.54  ? 403  LEU A N     1 
ATOM   2783 C CA    . LEU A 1 361 ? 5.336   25.443  23.244 1.00 63.71  ? 403  LEU A CA    1 
ATOM   2784 C C     . LEU A 1 361 ? 4.393   25.244  24.436 1.00 65.72  ? 403  LEU A C     1 
ATOM   2785 O O     . LEU A 1 361 ? 3.289   24.719  24.268 1.00 67.12  ? 403  LEU A O     1 
ATOM   2786 C CB    . LEU A 1 361 ? 4.564   26.007  22.040 1.00 56.87  ? 403  LEU A CB    1 
ATOM   2787 N N     . ASP A 1 362 ? 4.831   25.714  25.620 1.00 67.68  ? 404  ASP A N     1 
ATOM   2788 C CA    . ASP A 1 362 ? 4.094   25.651  26.880 1.00 77.99  ? 404  ASP A CA    1 
ATOM   2789 C C     . ASP A 1 362 ? 2.583   25.602  26.636 1.00 79.83  ? 404  ASP A C     1 
ATOM   2790 O O     . ASP A 1 362 ? 2.077   26.304  25.765 1.00 102.68 ? 404  ASP A O     1 
ATOM   2791 C CB    . ASP A 1 362 ? 4.446   26.863  27.755 1.00 72.83  ? 404  ASP A CB    1 
ATOM   2792 N N     . GLU A 1 363 ? 1.851   24.782  27.405 1.00 71.83  ? 405  GLU A N     1 
ATOM   2793 C CA    . GLU A 1 363 ? 0.397   24.738  27.298 1.00 61.20  ? 405  GLU A CA    1 
ATOM   2794 C C     . GLU A 1 363 ? -0.133  23.349  27.646 1.00 53.30  ? 405  GLU A C     1 
ATOM   2795 O O     . GLU A 1 363 ? -0.428  22.586  26.723 1.00 60.53  ? 405  GLU A O     1 
ATOM   2796 C CB    . GLU A 1 363 ? -0.066  25.047  25.867 1.00 62.97  ? 405  GLU A CB    1 
ATOM   2797 N N     . VAL A 1 364 ? -0.288  23.036  28.950 1.00 46.10  ? 406  VAL A N     1 
ATOM   2798 C CA    . VAL A 1 364 ? -0.770  21.717  29.373 1.00 41.10  ? 406  VAL A CA    1 
ATOM   2799 C C     . VAL A 1 364 ? -2.307  21.665  29.295 1.00 37.08  ? 406  VAL A C     1 
ATOM   2800 O O     . VAL A 1 364 ? -2.985  21.743  30.345 1.00 33.53  ? 406  VAL A O     1 
ATOM   2801 C CB    . VAL A 1 364 ? -0.261  21.280  30.774 1.00 39.60  ? 406  VAL A CB    1 
ATOM   2802 C CG1   . VAL A 1 364 ? -0.579  19.812  31.025 1.00 37.27  ? 406  VAL A CG1   1 
ATOM   2803 C CG2   . VAL A 1 364 ? 1.226   21.506  30.992 1.00 39.82  ? 406  VAL A CG2   1 
ATOM   2804 N N     . GLY A 1 365 ? -2.840  21.438  28.068 1.00 29.91  ? 407  GLY A N     1 
ATOM   2805 C CA    . GLY A 1 365 ? -4.271  21.218  27.828 1.00 27.17  ? 407  GLY A CA    1 
ATOM   2806 C C     . GLY A 1 365 ? -4.925  20.140  28.710 1.00 22.06  ? 407  GLY A C     1 
ATOM   2807 O O     . GLY A 1 365 ? -6.110  20.230  29.038 1.00 20.05  ? 407  GLY A O     1 
ATOM   2808 N N     . LEU A 1 366 ? -4.136  19.141  29.126 1.00 19.85  ? 408  LEU A N     1 
ATOM   2809 C CA    . LEU A 1 366 ? -4.663  18.008  29.891 1.00 22.04  ? 408  LEU A CA    1 
ATOM   2810 C C     . LEU A 1 366 ? -5.375  18.476  31.161 1.00 20.77  ? 408  LEU A C     1 
ATOM   2811 O O     . LEU A 1 366 ? -6.299  17.808  31.651 1.00 21.77  ? 408  LEU A O     1 
ATOM   2812 C CB    . LEU A 1 366 ? -3.541  17.075  30.346 1.00 23.67  ? 408  LEU A CB    1 
ATOM   2813 C CG    . LEU A 1 366 ? -3.017  16.013  29.404 1.00 29.46  ? 408  LEU A CG    1 
ATOM   2814 C CD1   . LEU A 1 366 ? -2.400  14.893  30.254 1.00 31.25  ? 408  LEU A CD1   1 
ATOM   2815 C CD2   . LEU A 1 366 ? -4.089  15.456  28.467 1.00 25.60  ? 408  LEU A CD2   1 
ATOM   2816 N N     . LEU A 1 367 ? -4.944  19.614  31.718 1.00 17.71  ? 409  LEU A N     1 
ATOM   2817 C CA    . LEU A 1 367 ? -5.547  20.093  32.952 1.00 17.70  ? 409  LEU A CA    1 
ATOM   2818 C C     . LEU A 1 367 ? -6.935  20.701  32.778 1.00 17.89  ? 409  LEU A C     1 
ATOM   2819 O O     . LEU A 1 367 ? -7.504  21.116  33.786 1.00 18.65  ? 409  LEU A O     1 
ATOM   2820 C CB    . LEU A 1 367 ? -4.634  21.141  33.568 1.00 21.50  ? 409  LEU A CB    1 
ATOM   2821 C CG    . LEU A 1 367 ? -3.308  20.619  34.106 1.00 25.77  ? 409  LEU A CG    1 
ATOM   2822 C CD1   . LEU A 1 367 ? -2.455  21.795  34.557 1.00 27.88  ? 409  LEU A CD1   1 
ATOM   2823 C CD2   . LEU A 1 367 ? -3.543  19.675  35.248 1.00 26.36  ? 409  LEU A CD2   1 
ATOM   2824 N N     . ARG A 1 368 ? -7.473  20.802  31.559 1.00 14.11  ? 410  ARG A N     1 
ATOM   2825 C CA    . ARG A 1 368 ? -8.810  21.323  31.395 1.00 16.78  ? 410  ARG A CA    1 
ATOM   2826 C C     . ARG A 1 368 ? -9.845  20.340  30.837 1.00 19.92  ? 410  ARG A C     1 
ATOM   2827 O O     . ARG A 1 368 ? -10.951 20.756  30.431 1.00 22.38  ? 410  ARG A O     1 
ATOM   2828 C CB    . ARG A 1 368 ? -8.762  22.596  30.524 1.00 19.26  ? 410  ARG A CB    1 
ATOM   2829 C CG    . ARG A 1 368 ? -8.084  23.801  31.180 1.00 24.30  ? 410  ARG A CG    1 
ATOM   2830 C CD    . ARG A 1 368 ? -8.651  24.289  32.515 1.00 26.90  ? 410  ARG A CD    1 
ATOM   2831 N NE    . ARG A 1 368 ? -10.070 24.622  32.446 1.00 31.96  ? 410  ARG A NE    1 
ATOM   2832 C CZ    . ARG A 1 368 ? -10.564 25.870  32.329 1.00 29.45  ? 410  ARG A CZ    1 
ATOM   2833 N NH1   . ARG A 1 368 ? -9.750  26.906  32.324 1.00 29.78  ? 410  ARG A NH1   1 
ATOM   2834 N NH2   . ARG A 1 368 ? -11.866 26.067  32.246 1.00 28.96  ? 410  ARG A NH2   1 
ATOM   2835 N N     . TRP A 1 369 ? -9.601  19.039  30.937 1.00 15.15  ? 411  TRP A N     1 
ATOM   2836 C CA    . TRP A 1 369 ? -10.439 18.032  30.288 1.00 13.85  ? 411  TRP A CA    1 
ATOM   2837 C C     . TRP A 1 369 ? -11.891 18.032  30.754 1.00 14.05  ? 411  TRP A C     1 
ATOM   2838 O O     . TRP A 1 369 ? -12.788 18.076  29.902 1.00 14.33  ? 411  TRP A O     1 
ATOM   2839 C CB    . TRP A 1 369 ? -9.769  16.672  30.471 1.00 13.59  ? 411  TRP A CB    1 
ATOM   2840 C CG    . TRP A 1 369 ? -10.485 15.500  29.880 1.00 12.26  ? 411  TRP A CG    1 
ATOM   2841 C CD1   . TRP A 1 369 ? -10.903 14.395  30.531 1.00 13.34  ? 411  TRP A CD1   1 
ATOM   2842 C CD2   . TRP A 1 369 ? -10.692 15.224  28.480 1.00 12.73  ? 411  TRP A CD2   1 
ATOM   2843 N NE1   . TRP A 1 369 ? -11.393 13.456  29.651 1.00 14.72  ? 411  TRP A NE1   1 
ATOM   2844 C CE2   . TRP A 1 369 ? -11.281 13.937  28.390 1.00 12.90  ? 411  TRP A CE2   1 
ATOM   2845 C CE3   . TRP A 1 369 ? -10.477 15.934  27.299 1.00 13.10  ? 411  TRP A CE3   1 
ATOM   2846 C CZ2   . TRP A 1 369 ? -11.612 13.380  27.159 1.00 13.63  ? 411  TRP A CZ2   1 
ATOM   2847 C CZ3   . TRP A 1 369 ? -10.819 15.379  26.078 1.00 13.82  ? 411  TRP A CZ3   1 
ATOM   2848 C CH2   . TRP A 1 369 ? -11.393 14.121  26.019 1.00 15.28  ? 411  TRP A CH2   1 
ATOM   2849 N N     . ARG A 1 370 ? -12.116 17.815  32.054 1.00 14.35  ? 412  ARG A N     1 
ATOM   2850 C CA    . ARG A 1 370 ? -13.441 17.529  32.612 1.00 16.71  ? 412  ARG A CA    1 
ATOM   2851 C C     . ARG A 1 370 ? -13.852 18.676  33.524 1.00 16.55  ? 412  ARG A C     1 
ATOM   2852 O O     . ARG A 1 370 ? -13.107 19.040  34.443 1.00 15.79  ? 412  ARG A O     1 
ATOM   2853 C CB    . ARG A 1 370 ? -13.506 16.284  33.529 1.00 20.33  ? 412  ARG A CB    1 
ATOM   2854 C CG    . ARG A 1 370 ? -13.634 14.950  32.833 1.00 26.12  ? 412  ARG A CG    1 
ATOM   2855 C CD    . ARG A 1 370 ? -13.739 13.771  33.799 1.00 21.89  ? 412  ARG A CD    1 
ATOM   2856 N NE    . ARG A 1 370 ? -14.011 12.544  33.028 1.00 32.26  ? 412  ARG A NE    1 
ATOM   2857 C CZ    . ARG A 1 370 ? -15.190 11.958  32.938 1.00 32.15  ? 412  ARG A CZ    1 
ATOM   2858 N NH1   . ARG A 1 370 ? -16.294 12.595  33.305 1.00 34.64  ? 412  ARG A NH1   1 
ATOM   2859 N NH2   . ARG A 1 370 ? -15.282 10.754  32.419 1.00 37.09  ? 412  ARG A NH2   1 
ATOM   2860 N N     . GLY A 1 371 ? -15.046 19.245  33.287 1.00 15.58  ? 413  GLY A N     1 
ATOM   2861 C CA    . GLY A 1 371 ? -15.598 20.241  34.189 1.00 17.17  ? 413  GLY A CA    1 
ATOM   2862 C C     . GLY A 1 371 ? -14.677 21.433  34.307 1.00 15.06  ? 413  GLY A C     1 
ATOM   2863 O O     . GLY A 1 371 ? -14.161 21.953  33.313 1.00 18.16  ? 413  GLY A O     1 
ATOM   2864 N N     . ALA A 1 372 ? -14.399 21.852  35.538 1.00 16.21  ? 414  ALA A N     1 
ATOM   2865 C CA    . ALA A 1 372 ? -13.488 22.955  35.801 1.00 15.90  ? 414  ALA A CA    1 
ATOM   2866 C C     . ALA A 1 372 ? -12.003 22.569  35.667 1.00 17.64  ? 414  ALA A C     1 
ATOM   2867 O O     . ALA A 1 372 ? -11.138 23.437  35.696 1.00 19.70  ? 414  ALA A O     1 
ATOM   2868 C CB    . ALA A 1 372 ? -13.768 23.481  37.194 1.00 17.86  ? 414  ALA A CB    1 
ATOM   2869 N N     . GLY A 1 373 ? -11.704 21.281  35.484 1.00 14.23  ? 415  GLY A N     1 
ATOM   2870 C CA    . GLY A 1 373 ? -10.351 20.783  35.309 1.00 14.89  ? 415  GLY A CA    1 
ATOM   2871 C C     . GLY A 1 373 ? -9.552  20.779  36.615 1.00 14.00  ? 415  GLY A C     1 
ATOM   2872 O O     . GLY A 1 373 ? -10.136 20.797  37.709 1.00 14.95  ? 415  GLY A O     1 
ATOM   2873 N N     . GLY A 1 374 ? -8.235  20.748  36.455 1.00 13.54  ? 416  GLY A N     1 
ATOM   2874 C CA    . GLY A 1 374 ? -7.306  20.894  37.572 1.00 13.28  ? 416  GLY A CA    1 
ATOM   2875 C C     . GLY A 1 374 ? -6.912  19.604  38.304 1.00 14.01  ? 416  GLY A C     1 
ATOM   2876 O O     . GLY A 1 374 ? -6.126  19.666  39.242 1.00 14.57  ? 416  GLY A O     1 
ATOM   2877 N N     . GLY A 1 375 ? -7.437  18.465  37.874 1.00 13.41  ? 417  GLY A N     1 
ATOM   2878 C CA    . GLY A 1 375 ? -7.168  17.168  38.479 1.00 12.84  ? 417  GLY A CA    1 
ATOM   2879 C C     . GLY A 1 375 ? -6.387  16.286  37.522 1.00 11.20  ? 417  GLY A C     1 
ATOM   2880 O O     . GLY A 1 375 ? -6.815  16.048  36.388 1.00 12.39  ? 417  GLY A O     1 
ATOM   2881 N N     . LEU A 1 376 ? -5.170  15.908  37.942 1.00 12.32  ? 418  LEU A N     1 
ATOM   2882 C CA    . LEU A 1 376 ? -4.337  14.966  37.192 1.00 11.85  ? 418  LEU A CA    1 
ATOM   2883 C C     . LEU A 1 376 ? -3.461  14.189  38.165 1.00 12.11  ? 418  LEU A C     1 
ATOM   2884 O O     . LEU A 1 376 ? -2.703  14.779  38.932 1.00 11.70  ? 418  LEU A O     1 
ATOM   2885 C CB    . LEU A 1 376 ? -3.416  15.700  36.224 1.00 13.93  ? 418  LEU A CB    1 
ATOM   2886 C CG    . LEU A 1 376 ? -2.217  14.892  35.663 1.00 16.31  ? 418  LEU A CG    1 
ATOM   2887 C CD1   . LEU A 1 376 ? -2.679  13.899  34.655 1.00 16.61  ? 418  LEU A CD1   1 
ATOM   2888 C CD2   . LEU A 1 376 ? -1.169  15.783  35.031 1.00 18.97  ? 418  LEU A CD2   1 
ATOM   2889 N N     . ALA A 1 377 ? -3.577  12.866  38.083 1.00 10.98  ? 419  ALA A N     1 
ATOM   2890 C CA    . ALA A 1 377 ? -2.647  11.975  38.761 1.00 11.27  ? 419  ALA A CA    1 
ATOM   2891 C C     . ALA A 1 377 ? -2.210  10.928  37.727 1.00 10.47  ? 419  ALA A C     1 
ATOM   2892 O O     . ALA A 1 377 ? -3.043  10.323  37.035 1.00 11.50  ? 419  ALA A O     1 
ATOM   2893 C CB    . ALA A 1 377 ? -3.298  11.317  39.973 1.00 12.20  ? 419  ALA A CB    1 
ATOM   2894 N N     . TRP A 1 378 ? -0.885  10.720  37.632 1.00 10.00  ? 420  TRP A N     1 
ATOM   2895 C CA    . TRP A 1 378 ? -0.348  9.606   36.868 1.00 9.73   ? 420  TRP A CA    1 
ATOM   2896 C C     . TRP A 1 378 ? -0.377  8.322   37.676 1.00 10.15  ? 420  TRP A C     1 
ATOM   2897 O O     . TRP A 1 378 ? 0.142   8.324   38.820 1.00 12.83  ? 420  TRP A O     1 
ATOM   2898 C CB    . TRP A 1 378 ? 1.094   9.880   36.421 1.00 9.73   ? 420  TRP A CB    1 
ATOM   2899 C CG    . TRP A 1 378 ? 1.282   11.179  35.693 1.00 10.21  ? 420  TRP A CG    1 
ATOM   2900 C CD1   . TRP A 1 378 ? 1.924   12.305  36.125 1.00 11.74  ? 420  TRP A CD1   1 
ATOM   2901 C CD2   . TRP A 1 378 ? 0.852   11.443  34.343 1.00 11.74  ? 420  TRP A CD2   1 
ATOM   2902 N NE1   . TRP A 1 378 ? 1.885   13.260  35.161 1.00 13.05  ? 420  TRP A NE1   1 
ATOM   2903 C CE2   . TRP A 1 378 ? 1.250   12.767  34.051 1.00 11.87  ? 420  TRP A CE2   1 
ATOM   2904 C CE3   . TRP A 1 378 ? 0.182   10.692  33.377 1.00 12.12  ? 420  TRP A CE3   1 
ATOM   2905 C CZ2   . TRP A 1 378 ? 0.972   13.369  32.841 1.00 12.14  ? 420  TRP A CZ2   1 
ATOM   2906 C CZ3   . TRP A 1 378 ? -0.057  11.287  32.158 1.00 12.80  ? 420  TRP A CZ3   1 
ATOM   2907 C CH2   . TRP A 1 378 ? 0.347   12.586  31.893 1.00 12.14  ? 420  TRP A CH2   1 
ATOM   2908 N N     . PHE A 1 379 ? -0.889  7.266   37.011 1.00 10.86  ? 421  PHE A N     1 
ATOM   2909 C CA    . PHE A 1 379 ? -0.778  5.878   37.443 1.00 9.67   ? 421  PHE A CA    1 
ATOM   2910 C C     . PHE A 1 379 ? 0.098   5.202   36.403 1.00 10.94  ? 421  PHE A C     1 
ATOM   2911 O O     . PHE A 1 379 ? -0.243  5.258   35.221 1.00 11.75  ? 421  PHE A O     1 
ATOM   2912 C CB    . PHE A 1 379 ? -2.143  5.220   37.613 1.00 10.15  ? 421  PHE A CB    1 
ATOM   2913 C CG    . PHE A 1 379 ? -2.001  3.760   37.982 1.00 11.16  ? 421  PHE A CG    1 
ATOM   2914 C CD1   . PHE A 1 379 ? -1.225  3.392   39.052 1.00 12.03  ? 421  PHE A CD1   1 
ATOM   2915 C CD2   . PHE A 1 379 ? -2.571  2.766   37.205 1.00 11.62  ? 421  PHE A CD2   1 
ATOM   2916 C CE1   . PHE A 1 379 ? -1.062  2.052   39.349 1.00 14.20  ? 421  PHE A CE1   1 
ATOM   2917 C CE2   . PHE A 1 379 ? -2.436  1.417   37.532 1.00 12.75  ? 421  PHE A CE2   1 
ATOM   2918 C CZ    . PHE A 1 379 ? -1.689  1.072   38.626 1.00 12.17  ? 421  PHE A CZ    1 
ATOM   2919 N N     . ALA A 1 380 ? 1.276   4.732   36.807 1.00 9.47   ? 422  ALA A N     1 
ATOM   2920 C CA    . ALA A 1 380 ? 2.356   4.437   35.858 1.00 10.51  ? 422  ALA A CA    1 
ATOM   2921 C C     . ALA A 1 380 ? 2.905   3.020   36.055 1.00 10.61  ? 422  ALA A C     1 
ATOM   2922 O O     . ALA A 1 380 ? 4.111   2.855   36.327 1.00 10.64  ? 422  ALA A O     1 
ATOM   2923 C CB    . ALA A 1 380 ? 3.432   5.489   35.947 1.00 10.89  ? 422  ALA A CB    1 
ATOM   2924 N N     . PRO A 1 381 ? 2.061   1.980   35.879 1.00 10.88  ? 423  PRO A N     1 
ATOM   2925 C CA    . PRO A 1 381 ? 2.535   0.591   35.961 1.00 10.70  ? 423  PRO A CA    1 
ATOM   2926 C C     . PRO A 1 381 ? 3.485   0.187   34.842 1.00 12.40  ? 423  PRO A C     1 
ATOM   2927 O O     . PRO A 1 381 ? 3.403   0.664   33.708 1.00 12.24  ? 423  PRO A O     1 
ATOM   2928 C CB    . PRO A 1 381 ? 1.229   -0.242  36.010 1.00 11.08  ? 423  PRO A CB    1 
ATOM   2929 C CG    . PRO A 1 381 ? 0.259   0.620   35.148 1.00 10.59  ? 423  PRO A CG    1 
ATOM   2930 C CD    . PRO A 1 381 ? 0.612   2.050   35.563 1.00 10.82  ? 423  PRO A CD    1 
ATOM   2931 N N     . VAL A 1 382 ? 4.401   -0.715  35.186 1.00 12.70  ? 424  VAL A N     1 
ATOM   2932 C CA    . VAL A 1 382 ? 5.348   -1.360  34.287 1.00 12.48  ? 424  VAL A CA    1 
ATOM   2933 C C     . VAL A 1 382 ? 4.689   -2.598  33.679 1.00 12.14  ? 424  VAL A C     1 
ATOM   2934 O O     . VAL A 1 382 ? 3.927   -3.305  34.328 1.00 13.90  ? 424  VAL A O     1 
ATOM   2935 C CB    . VAL A 1 382 ? 6.579   -1.779  35.113 1.00 13.69  ? 424  VAL A CB    1 
ATOM   2936 C CG1   . VAL A 1 382 ? 7.567   -2.561  34.275 1.00 15.05  ? 424  VAL A CG1   1 
ATOM   2937 C CG2   . VAL A 1 382 ? 7.238   -0.551  35.728 1.00 14.06  ? 424  VAL A CG2   1 
ATOM   2938 N N     . ALA A 1 383 ? 5.062   -2.899  32.446 1.00 13.84  ? 425  ALA A N     1 
ATOM   2939 C CA    . ALA A 1 383 ? 4.799   -4.180  31.834 1.00 14.44  ? 425  ALA A CA    1 
ATOM   2940 C C     . ALA A 1 383 ? 6.052   -4.650  31.093 1.00 14.10  ? 425  ALA A C     1 
ATOM   2941 O O     . ALA A 1 383 ? 6.843   -3.835  30.638 1.00 14.74  ? 425  ALA A O     1 
ATOM   2942 C CB    . ALA A 1 383 ? 3.648   -3.993  30.882 1.00 14.84  ? 425  ALA A CB    1 
ATOM   2943 N N     . ALA A 1 384 ? 6.241   -5.958  30.991 1.00 11.35  ? 426  ALA A N     1 
ATOM   2944 C CA    . ALA A 1 384 ? 7.143   -6.485  29.969 1.00 13.02  ? 426  ALA A CA    1 
ATOM   2945 C C     . ALA A 1 384 ? 6.596   -6.117  28.603 1.00 11.96  ? 426  ALA A C     1 
ATOM   2946 O O     . ALA A 1 384 ? 5.381   -6.022  28.440 1.00 13.40  ? 426  ALA A O     1 
ATOM   2947 C CB    . ALA A 1 384 ? 7.294   -7.990  30.095 1.00 15.00  ? 426  ALA A CB    1 
ATOM   2948 N N     . ALA A 1 385 ? 7.469   -5.970  27.618 1.00 12.29  ? 427  ALA A N     1 
ATOM   2949 C CA    . ALA A 1 385 ? 7.081   -5.631  26.260 1.00 12.53  ? 427  ALA A CA    1 
ATOM   2950 C C     . ALA A 1 385 ? 6.451   -6.858  25.576 1.00 12.68  ? 427  ALA A C     1 
ATOM   2951 O O     . ALA A 1 385 ? 7.013   -7.368  24.620 1.00 13.12  ? 427  ALA A O     1 
ATOM   2952 C CB    . ALA A 1 385 ? 8.259   -5.093  25.495 1.00 13.95  ? 427  ALA A CB    1 
ATOM   2953 N N     . ARG A 1 386 ? 5.276   -7.246  26.039 1.00 12.80  ? 428  ARG A N     1 
ATOM   2954 C CA    . ARG A 1 386 ? 4.472   -8.337  25.493 1.00 15.14  ? 428  ARG A CA    1 
ATOM   2955 C C     . ARG A 1 386 ? 3.040   -7.838  25.220 1.00 14.69  ? 428  ARG A C     1 
ATOM   2956 O O     . ARG A 1 386 ? 2.411   -7.208  26.062 1.00 13.55  ? 428  ARG A O     1 
ATOM   2957 C CB    . ARG A 1 386 ? 4.413   -9.522  26.466 1.00 15.54  ? 428  ARG A CB    1 
ATOM   2958 C CG    . ARG A 1 386 ? 5.781   -10.117 26.817 1.00 16.16  ? 428  ARG A CG    1 
ATOM   2959 C CD    . ARG A 1 386 ? 5.640   -11.256 27.823 1.00 16.31  ? 428  ARG A CD    1 
ATOM   2960 N NE    . ARG A 1 386 ? 6.966   -11.709 28.225 1.00 19.81  ? 428  ARG A NE    1 
ATOM   2961 C CZ    . ARG A 1 386 ? 7.388   -11.738 29.480 1.00 18.42  ? 428  ARG A CZ    1 
ATOM   2962 N NH1   . ARG A 1 386 ? 6.645   -11.294 30.477 1.00 19.29  ? 428  ARG A NH1   1 
ATOM   2963 N NH2   . ARG A 1 386 ? 8.577   -12.250 29.725 1.00 21.91  ? 428  ARG A NH2   1 
ATOM   2964 N N     . GLY A 1 387 ? 2.551   -8.083  23.982 1.00 14.66  ? 429  GLY A N     1 
ATOM   2965 C CA    . GLY A 1 387 ? 1.215   -7.639  23.641 1.00 14.82  ? 429  GLY A CA    1 
ATOM   2966 C C     . GLY A 1 387 ? 0.152   -8.047  24.655 1.00 13.90  ? 429  GLY A C     1 
ATOM   2967 O O     . GLY A 1 387 ? -0.741  -7.262  24.951 1.00 15.89  ? 429  GLY A O     1 
ATOM   2968 N N     . VAL A 1 388 ? 0.178   -9.305  25.151 1.00 15.04  ? 430  VAL A N     1 
ATOM   2969 C CA    . VAL A 1 388 ? -0.866  -9.800  26.036 1.00 16.79  ? 430  VAL A CA    1 
ATOM   2970 C C     . VAL A 1 388 ? -0.907  -9.024  27.350 1.00 16.07  ? 430  VAL A C     1 
ATOM   2971 O O     . VAL A 1 388 ? -1.981  -8.786  27.910 1.00 16.39  ? 430  VAL A O     1 
ATOM   2972 C CB    . VAL A 1 388 ? -0.726  -11.291 26.357 1.00 21.01  ? 430  VAL A CB    1 
ATOM   2973 C CG1   . VAL A 1 388 ? 0.522   -11.567 27.165 1.00 20.54  ? 430  VAL A CG1   1 
ATOM   2974 C CG2   . VAL A 1 388 ? -1.951  -11.772 27.119 1.00 25.05  ? 430  VAL A CG2   1 
ATOM   2975 N N     . GLU A 1 389 ? 0.264   -8.577  27.816 1.00 16.69  ? 431  GLU A N     1 
ATOM   2976 C CA    . GLU A 1 389 ? 0.326   -7.775  29.030 1.00 15.06  ? 431  GLU A CA    1 
ATOM   2977 C C     . GLU A 1 389 ? -0.327  -6.421  28.789 1.00 14.47  ? 431  GLU A C     1 
ATOM   2978 O O     . GLU A 1 389 ? -1.066  -5.947  29.665 1.00 14.23  ? 431  GLU A O     1 
ATOM   2979 C CB    . GLU A 1 389 ? 1.776   -7.599  29.503 1.00 19.49  ? 431  GLU A CB    1 
ATOM   2980 C CG    . GLU A 1 389 ? 2.326   -8.870  30.108 1.00 24.08  ? 431  GLU A CG    1 
ATOM   2981 C CD    . GLU A 1 389 ? 3.648   -8.805  30.865 1.00 30.16  ? 431  GLU A CD    1 
ATOM   2982 O OE1   . GLU A 1 389 ? 3.949   -7.761  31.530 1.00 30.17  ? 431  GLU A OE1   1 
ATOM   2983 O OE2   . GLU A 1 389 ? 4.331   -9.866  30.883 1.00 29.87  ? 431  GLU A OE2   1 
ATOM   2984 N N     . ALA A 1 390 ? 0.014   -5.780  27.671 1.00 13.34  ? 432  ALA A N     1 
ATOM   2985 C CA    . ALA A 1 390 ? -0.597  -4.478  27.369 1.00 13.16  ? 432  ALA A CA    1 
ATOM   2986 C C     . ALA A 1 390 ? -2.111  -4.608  27.177 1.00 14.21  ? 432  ALA A C     1 
ATOM   2987 O O     . ALA A 1 390 ? -2.906  -3.824  27.699 1.00 14.54  ? 432  ALA A O     1 
ATOM   2988 C CB    . ALA A 1 390 ? 0.076   -3.878  26.187 1.00 12.35  ? 432  ALA A CB    1 
ATOM   2989 N N     . GLU A 1 391 ? -2.527  -5.670  26.479 1.00 17.08  ? 433  GLU A N     1 
ATOM   2990 C CA    . GLU A 1 391 ? -3.953  -5.913  26.320 1.00 16.31  ? 433  GLU A CA    1 
ATOM   2991 C C     . GLU A 1 391 ? -4.677  -5.986  27.642 1.00 15.46  ? 433  GLU A C     1 
ATOM   2992 O O     . GLU A 1 391 ? -5.754  -5.368  27.865 1.00 16.45  ? 433  GLU A O     1 
ATOM   2993 C CB    . GLU A 1 391 ? -4.143  -7.228  25.546 1.00 18.40  ? 433  GLU A CB    1 
ATOM   2994 C CG    . GLU A 1 391 ? -5.559  -7.510  25.135 1.00 22.40  ? 433  GLU A CG    1 
ATOM   2995 C CD    . GLU A 1 391 ? -5.655  -8.618  24.079 1.00 29.10  ? 433  GLU A CD    1 
ATOM   2996 O OE1   . GLU A 1 391 ? -4.972  -9.643  24.244 1.00 32.00  ? 433  GLU A OE1   1 
ATOM   2997 O OE2   . GLU A 1 391 ? -6.389  -8.434  23.087 1.00 36.48  ? 433  GLU A OE2   1 
ATOM   2998 N N     . ARG A 1 392 ? -4.118  -6.769  28.566 1.00 14.82  ? 434  ARG A N     1 
ATOM   2999 C CA    . ARG A 1 392 ? -4.780  -6.995  29.827 1.00 14.36  ? 434  ARG A CA    1 
ATOM   3000 C C     . ARG A 1 392 ? -4.740  -5.731  30.698 1.00 14.31  ? 434  ARG A C     1 
ATOM   3001 O O     . ARG A 1 392 ? -5.699  -5.451  31.423 1.00 13.90  ? 434  ARG A O     1 
ATOM   3002 C CB    . ARG A 1 392 ? -4.200  -8.183  30.596 1.00 16.11  ? 434  ARG A CB    1 
ATOM   3003 C CG    . ARG A 1 392 ? -4.382  -9.538  29.902 1.00 18.15  ? 434  ARG A CG    1 
ATOM   3004 C CD    . ARG A 1 392 ? -3.568  -10.560 30.678 1.00 18.66  ? 434  ARG A CD    1 
ATOM   3005 N NE    . ARG A 1 392 ? -4.146  -10.705 32.004 1.00 27.60  ? 434  ARG A NE    1 
ATOM   3006 C CZ    . ARG A 1 392 ? -3.512  -10.869 33.174 1.00 26.79  ? 434  ARG A CZ    1 
ATOM   3007 N NH1   . ARG A 1 392 ? -2.257  -11.263 33.227 1.00 27.36  ? 434  ARG A NH1   1 
ATOM   3008 N NH2   . ARG A 1 392 ? -4.201  -10.763 34.310 1.00 31.15  ? 434  ARG A NH2   1 
ATOM   3009 N N     . GLN A 1 393 ? -3.626  -4.994  30.678 1.00 13.04  ? 435  GLN A N     1 
ATOM   3010 C CA    . GLN A 1 393 ? -3.544  -3.787  31.516 1.00 13.02  ? 435  GLN A CA    1 
ATOM   3011 C C     . GLN A 1 393 ? -4.479  -2.675  31.009 1.00 12.48  ? 435  GLN A C     1 
ATOM   3012 O O     . GLN A 1 393 ? -5.112  -2.023  31.824 1.00 13.60  ? 435  GLN A O     1 
ATOM   3013 C CB    . GLN A 1 393 ? -2.139  -3.185  31.570 1.00 12.85  ? 435  GLN A CB    1 
ATOM   3014 C CG    . GLN A 1 393 ? -1.128  -4.012  32.348 1.00 13.09  ? 435  GLN A CG    1 
ATOM   3015 C CD    . GLN A 1 393 ? 0.121   -3.238  32.726 1.00 12.83  ? 435  GLN A CD    1 
ATOM   3016 O OE1   . GLN A 1 393 ? 0.270   -2.049  32.432 1.00 13.77  ? 435  GLN A OE1   1 
ATOM   3017 N NE2   . GLN A 1 393 ? 1.080   -3.908  33.345 1.00 12.96  ? 435  GLN A NE2   1 
ATOM   3018 N N     . THR A 1 394 ? -4.575  -2.541  29.691 1.00 14.38  ? 436  THR A N     1 
ATOM   3019 C CA    . THR A 1 394 ? -5.518  -1.604  29.112 1.00 13.68  ? 436  THR A CA    1 
ATOM   3020 C C     . THR A 1 394 ? -6.917  -1.988  29.584 1.00 13.04  ? 436  THR A C     1 
ATOM   3021 O O     . THR A 1 394 ? -7.694  -1.130  29.996 1.00 14.12  ? 436  THR A O     1 
ATOM   3022 C CB    . THR A 1 394 ? -5.310  -1.480  27.603 1.00 15.67  ? 436  THR A CB    1 
ATOM   3023 O OG1   . THR A 1 394 ? -4.107  -0.729  27.348 1.00 13.92  ? 436  THR A OG1   1 
ATOM   3024 C CG2   . THR A 1 394 ? -6.458  -0.762  26.915 1.00 16.19  ? 436  THR A CG2   1 
ATOM   3025 N N     . ALA A 1 395 ? -7.292  -3.271  29.455 1.00 14.85  ? 437  ALA A N     1 
ATOM   3026 C CA    . ALA A 1 395 ? -8.642  -3.676  29.799 1.00 14.73  ? 437  ALA A CA    1 
ATOM   3027 C C     . ALA A 1 395 ? -8.953  -3.410  31.260 1.00 15.64  ? 437  ALA A C     1 
ATOM   3028 O O     . ALA A 1 395 ? -10.064 -2.974  31.610 1.00 15.68  ? 437  ALA A O     1 
ATOM   3029 C CB    . ALA A 1 395 ? -8.852  -5.143  29.467 1.00 16.26  ? 437  ALA A CB    1 
ATOM   3030 N N     . LEU A 1 396 ? -8.003  -3.707  32.175 1.00 14.17  ? 438  LEU A N     1 
ATOM   3031 C CA    . LEU A 1 396 ? -8.288  -3.557  33.591 1.00 13.63  ? 438  LEU A CA    1 
ATOM   3032 C C     . LEU A 1 396 ? -8.360  -2.061  33.970 1.00 13.49  ? 438  LEU A C     1 
ATOM   3033 O O     . LEU A 1 396 ? -9.187  -1.637  34.778 1.00 14.60  ? 438  LEU A O     1 
ATOM   3034 C CB    . LEU A 1 396 ? -7.195  -4.282  34.405 1.00 14.29  ? 438  LEU A CB    1 
ATOM   3035 C CG    . LEU A 1 396 ? -7.377  -4.215  35.915 1.00 15.39  ? 438  LEU A CG    1 
ATOM   3036 C CD1   . LEU A 1 396 ? -8.712  -4.797  36.349 1.00 15.94  ? 438  LEU A CD1   1 
ATOM   3037 C CD2   . LEU A 1 396 ? -6.259  -4.974  36.617 1.00 15.78  ? 438  LEU A CD2   1 
ATOM   3038 N N     . ALA A 1 397 ? -7.432  -1.261  33.453 1.00 13.62  ? 439  ALA A N     1 
ATOM   3039 C CA    . ALA A 1 397 ? -7.431  0.180   33.706 1.00 14.24  ? 439  ALA A CA    1 
ATOM   3040 C C     . ALA A 1 397 ? -8.743  0.794   33.235 1.00 14.29  ? 439  ALA A C     1 
ATOM   3041 O O     . ALA A 1 397 ? -9.356  1.564   33.972 1.00 14.09  ? 439  ALA A O     1 
ATOM   3042 C CB    . ALA A 1 397 ? -6.267  0.854   33.017 1.00 15.77  ? 439  ALA A CB    1 
ATOM   3043 N N     . LYS A 1 398 ? -9.177  0.451   32.020 1.00 15.44  ? 440  LYS A N     1 
ATOM   3044 C CA    . LYS A 1 398 ? -10.430 1.025   31.513 1.00 17.65  ? 440  LYS A CA    1 
ATOM   3045 C C     . LYS A 1 398 ? -11.623 0.643   32.392 1.00 16.32  ? 440  LYS A C     1 
ATOM   3046 O O     . LYS A 1 398 ? -12.518 1.466   32.694 1.00 19.24  ? 440  LYS A O     1 
ATOM   3047 C CB    . LYS A 1 398 ? -10.729 0.531   30.101 1.00 20.92  ? 440  LYS A CB    1 
ATOM   3048 C CG    . LYS A 1 398 ? -9.836  0.974   28.993 1.00 28.15  ? 440  LYS A CG    1 
ATOM   3049 C CD    . LYS A 1 398 ? -10.285 0.387   27.656 1.00 36.73  ? 440  LYS A CD    1 
ATOM   3050 C CE    . LYS A 1 398 ? -11.772 0.528   27.416 1.00 43.76  ? 440  LYS A CE    1 
ATOM   3051 N NZ    . LYS A 1 398 ? -12.114 0.071   26.053 1.00 55.71  ? 440  LYS A NZ    1 
ATOM   3052 N N     . GLU A 1 399 ? -11.667 -0.634  32.815 1.00 15.74  ? 441  GLU A N     1 
ATOM   3053 C CA    . GLU A 1 399 ? -12.725 -1.125  33.689 1.00 16.87  ? 441  GLU A CA    1 
ATOM   3054 C C     . GLU A 1 399 ? -12.771 -0.287  34.962 1.00 15.69  ? 441  GLU A C     1 
ATOM   3055 O O     . GLU A 1 399 ? -13.829 0.138   35.425 1.00 14.94  ? 441  GLU A O     1 
ATOM   3056 C CB    . GLU A 1 399 ? -12.525 -2.602  34.023 1.00 20.07  ? 441  GLU A CB    1 
ATOM   3057 C CG    . GLU A 1 399 ? -13.521 -3.151  35.011 1.00 24.69  ? 441  GLU A CG    1 
ATOM   3058 C CD    . GLU A 1 399 ? -13.283 -4.592  35.475 1.00 28.38  ? 441  GLU A CD    1 
ATOM   3059 O OE1   . GLU A 1 399 ? -12.678 -5.374  34.758 1.00 32.13  ? 441  GLU A OE1   1 
ATOM   3060 O OE2   . GLU A 1 399 ? -13.601 -4.879  36.621 1.00 33.39  ? 441  GLU A OE2   1 
ATOM   3061 N N     . ILE A 1 400 ? -11.601 -0.066  35.572 1.00 13.82  ? 442  ILE A N     1 
ATOM   3062 C CA    . ILE A 1 400 ? -11.579 0.618   36.848 1.00 13.56  ? 442  ILE A CA    1 
ATOM   3063 C C     . ILE A 1 400 ? -11.900 2.098   36.700 1.00 13.13  ? 442  ILE A C     1 
ATOM   3064 O O     . ILE A 1 400 ? -12.679 2.647   37.483 1.00 14.62  ? 442  ILE A O     1 
ATOM   3065 C CB    . ILE A 1 400 ? -10.229 0.369   37.537 1.00 14.78  ? 442  ILE A CB    1 
ATOM   3066 C CG1   . ILE A 1 400 ? -10.039 -1.118  37.796 1.00 15.00  ? 442  ILE A CG1   1 
ATOM   3067 C CG2   . ILE A 1 400 ? -10.074 1.162   38.798 1.00 14.12  ? 442  ILE A CG2   1 
ATOM   3068 C CD1   . ILE A 1 400 ? -8.634  -1.428  38.300 1.00 15.70  ? 442  ILE A CD1   1 
ATOM   3069 N N     . VAL A 1 401 ? -11.294 2.775   35.713 1.00 14.12  ? 443  VAL A N     1 
ATOM   3070 C CA    . VAL A 1 401 ? -11.543 4.195   35.633 1.00 14.28  ? 443  VAL A CA    1 
ATOM   3071 C C     . VAL A 1 401 ? -13.019 4.413   35.289 1.00 15.64  ? 443  VAL A C     1 
ATOM   3072 O O     . VAL A 1 401 ? -13.617 5.353   35.829 1.00 14.87  ? 443  VAL A O     1 
ATOM   3073 C CB    . VAL A 1 401 ? -10.595 4.959   34.690 1.00 14.18  ? 443  VAL A CB    1 
ATOM   3074 C CG1   . VAL A 1 401 ? -9.152  4.902   35.191 1.00 14.04  ? 443  VAL A CG1   1 
ATOM   3075 C CG2   . VAL A 1 401 ? -10.713 4.489   33.246 1.00 14.05  ? 443  VAL A CG2   1 
ATOM   3076 N N     . GLU A 1 402 ? -13.590 3.563   34.443 1.00 14.72  ? 444  GLU A N     1 
ATOM   3077 C CA    . GLU A 1 402 ? -14.948 3.839   33.968 1.00 18.22  ? 444  GLU A CA    1 
ATOM   3078 C C     . GLU A 1 402 ? -15.921 3.529   35.100 1.00 17.18  ? 444  GLU A C     1 
ATOM   3079 O O     . GLU A 1 402 ? -16.896 4.216   35.283 1.00 18.75  ? 444  GLU A O     1 
ATOM   3080 C CB    . GLU A 1 402 ? -15.220 3.104   32.656 1.00 19.98  ? 444  GLU A CB    1 
ATOM   3081 C CG    . GLU A 1 402 ? -14.522 3.732   31.448 1.00 25.22  ? 444  GLU A CG    1 
ATOM   3082 C CD    . GLU A 1 402 ? -14.583 2.937   30.154 1.00 31.03  ? 444  GLU A CD    1 
ATOM   3083 O OE1   . GLU A 1 402 ? -15.358 1.952   30.069 1.00 28.83  ? 444  GLU A OE1   1 
ATOM   3084 O OE2   . GLU A 1 402 ? -13.741 3.198   29.287 1.00 39.50  ? 444  GLU A OE2   1 
ATOM   3085 N N     . LYS A 1 403 ? -15.633 2.524   35.928 1.00 18.06  ? 445  LYS A N     1 
ATOM   3086 C CA    . LYS A 1 403 ? -16.480 2.232   37.086 1.00 19.03  ? 445  LYS A CA    1 
ATOM   3087 C C     . LYS A 1 403 ? -16.621 3.434   38.046 1.00 21.26  ? 445  LYS A C     1 
ATOM   3088 O O     . LYS A 1 403 ? -17.677 3.595   38.670 1.00 18.20  ? 445  LYS A O     1 
ATOM   3089 C CB    . LYS A 1 403 ? -15.908 1.009   37.805 1.00 22.42  ? 445  LYS A CB    1 
ATOM   3090 C CG    . LYS A 1 403 ? -16.177 0.857   39.287 1.00 27.95  ? 445  LYS A CG    1 
ATOM   3091 C CD    . LYS A 1 403 ? -15.391 -0.305  39.886 1.00 27.19  ? 445  LYS A CD    1 
ATOM   3092 C CE    . LYS A 1 403 ? -15.749 -0.525  41.334 1.00 29.99  ? 445  LYS A CE    1 
ATOM   3093 N NZ    . LYS A 1 403 ? -15.005 -1.662  41.925 1.00 31.33  ? 445  LYS A NZ    1 
ATOM   3094 N N     . HIS A 1 404 ? -15.589 4.292   38.161 1.00 16.13  ? 446  HIS A N     1 
ATOM   3095 C CA    . HIS A 1 404 ? -15.576 5.461   39.023 1.00 16.44  ? 446  HIS A CA    1 
ATOM   3096 C C     . HIS A 1 404 ? -16.001 6.751   38.303 1.00 14.99  ? 446  HIS A C     1 
ATOM   3097 O O     . HIS A 1 404 ? -15.995 7.832   38.889 1.00 14.33  ? 446  HIS A O     1 
ATOM   3098 C CB    . HIS A 1 404 ? -14.157 5.596   39.628 1.00 16.45  ? 446  HIS A CB    1 
ATOM   3099 C CG    . HIS A 1 404 ? -13.859 4.606   40.728 1.00 16.30  ? 446  HIS A CG    1 
ATOM   3100 N ND1   . HIS A 1 404 ? -13.325 3.332   40.587 1.00 18.99  ? 446  HIS A ND1   1 
ATOM   3101 C CD2   . HIS A 1 404 ? -14.119 4.767   42.021 1.00 15.15  ? 446  HIS A CD2   1 
ATOM   3102 C CE1   . HIS A 1 404 ? -13.234 2.775   41.815 1.00 15.68  ? 446  HIS A CE1   1 
ATOM   3103 N NE2   . HIS A 1 404 ? -13.677 3.658   42.687 1.00 21.36  ? 446  HIS A NE2   1 
ATOM   3104 N N     . GLY A 1 405 ? -16.382 6.618   37.031 1.00 16.23  ? 447  GLY A N     1 
ATOM   3105 C CA    . GLY A 1 405 ? -16.913 7.707   36.232 1.00 18.12  ? 447  GLY A CA    1 
ATOM   3106 C C     . GLY A 1 405 ? -15.841 8.524   35.514 1.00 16.61  ? 447  GLY A C     1 
ATOM   3107 O O     . GLY A 1 405 ? -16.105 9.652   35.096 1.00 17.30  ? 447  GLY A O     1 
ATOM   3108 N N     . PHE A 1 406 ? -14.669 7.934   35.295 1.00 14.64  ? 448  PHE A N     1 
ATOM   3109 C CA    . PHE A 1 406 ? -13.593 8.619   34.605 1.00 13.45  ? 448  PHE A CA    1 
ATOM   3110 C C     . PHE A 1 406 ? -13.315 7.950   33.273 1.00 14.16  ? 448  PHE A C     1 
ATOM   3111 O O     . PHE A 1 406 ? -13.859 6.886   32.962 1.00 16.29  ? 448  PHE A O     1 
ATOM   3112 C CB    . PHE A 1 406 ? -12.354 8.681   35.506 1.00 13.57  ? 448  PHE A CB    1 
ATOM   3113 C CG    . PHE A 1 406 ? -12.585 9.430   36.785 1.00 13.11  ? 448  PHE A CG    1 
ATOM   3114 C CD1   . PHE A 1 406 ? -12.790 10.802  36.771 1.00 13.54  ? 448  PHE A CD1   1 
ATOM   3115 C CD2   . PHE A 1 406 ? -12.654 8.752   37.999 1.00 13.60  ? 448  PHE A CD2   1 
ATOM   3116 C CE1   . PHE A 1 406 ? -13.074 11.470  37.947 1.00 13.42  ? 448  PHE A CE1   1 
ATOM   3117 C CE2   . PHE A 1 406 ? -12.976 9.423   39.170 1.00 13.75  ? 448  PHE A CE2   1 
ATOM   3118 C CZ    . PHE A 1 406 ? -13.162 10.782  39.143 1.00 13.58  ? 448  PHE A CZ    1 
ATOM   3119 N N     . ASP A 1 407 ? -12.431 8.575   32.489 1.00 12.67  ? 449  ASP A N     1 
ATOM   3120 C CA    . ASP A 1 407 ? -12.066 8.077   31.187 1.00 12.83  ? 449  ASP A CA    1 
ATOM   3121 C C     . ASP A 1 407 ? -10.682 7.422   31.192 1.00 12.36  ? 449  ASP A C     1 
ATOM   3122 O O     . ASP A 1 407 ? -9.834  7.770   32.007 1.00 12.38  ? 449  ASP A O     1 
ATOM   3123 C CB    . ASP A 1 407 ? -12.028 9.176   30.131 1.00 14.10  ? 449  ASP A CB    1 
ATOM   3124 C CG    . ASP A 1 407 ? -13.321 9.979   30.021 1.00 15.82  ? 449  ASP A CG    1 
ATOM   3125 O OD1   . ASP A 1 407 ? -14.413 9.375   30.144 1.00 15.59  ? 449  ASP A OD1   1 
ATOM   3126 O OD2   . ASP A 1 407 ? -13.212 11.227  29.823 1.00 16.43  ? 449  ASP A OD2   1 
ATOM   3127 N N     . TYR A 1 408 ? -10.477 6.524   30.238 1.00 12.37  ? 450  TYR A N     1 
ATOM   3128 C CA    . TYR A 1 408 ? -9.162  5.997   29.915 1.00 12.55  ? 450  TYR A CA    1 
ATOM   3129 C C     . TYR A 1 408 ? -8.446  6.893   28.905 1.00 12.15  ? 450  TYR A C     1 
ATOM   3130 O O     . TYR A 1 408 ? -8.813  6.954   27.736 1.00 13.44  ? 450  TYR A O     1 
ATOM   3131 C CB    . TYR A 1 408 ? -9.222  4.554   29.386 1.00 12.95  ? 450  TYR A CB    1 
ATOM   3132 C CG    . TYR A 1 408 ? -7.892  3.907   29.092 1.00 13.57  ? 450  TYR A CG    1 
ATOM   3133 C CD1   . TYR A 1 408 ? -7.028  3.504   30.121 1.00 14.20  ? 450  TYR A CD1   1 
ATOM   3134 C CD2   . TYR A 1 408 ? -7.491  3.655   27.788 1.00 13.36  ? 450  TYR A CD2   1 
ATOM   3135 C CE1   . TYR A 1 408 ? -5.819  2.863   29.842 1.00 13.08  ? 450  TYR A CE1   1 
ATOM   3136 C CE2   . TYR A 1 408 ? -6.286  3.026   27.482 1.00 13.13  ? 450  TYR A CE2   1 
ATOM   3137 C CZ    . TYR A 1 408 ? -5.447  2.620   28.519 1.00 12.68  ? 450  TYR A CZ    1 
ATOM   3138 O OH    . TYR A 1 408 ? -4.274  2.021   28.139 1.00 11.38  ? 450  TYR A OH    1 
ATOM   3139 N N     . THR A 1 409 ? -7.402  7.565   29.416 1.00 12.03  ? 451  THR A N     1 
ATOM   3140 C CA    . THR A 1 409 ? -6.538  8.480   28.677 1.00 11.42  ? 451  THR A CA    1 
ATOM   3141 C C     . THR A 1 409 ? -5.085  8.101   28.993 1.00 12.21  ? 451  THR A C     1 
ATOM   3142 O O     . THR A 1 409 ? -4.636  8.342   30.116 1.00 12.27  ? 451  THR A O     1 
ATOM   3143 C CB    . THR A 1 409 ? -6.805  9.943   29.043 1.00 11.81  ? 451  THR A CB    1 
ATOM   3144 O OG1   . THR A 1 409 ? -6.896  10.128  30.449 1.00 12.49  ? 451  THR A OG1   1 
ATOM   3145 C CG2   . THR A 1 409 ? -8.116  10.459  28.478 1.00 12.88  ? 451  THR A CG2   1 
ATOM   3146 N N     . ALA A 1 410 ? -4.403  7.492   28.020 1.00 12.31  ? 452  ALA A N     1 
ATOM   3147 C CA    . ALA A 1 410 ? -3.173  6.780   28.347 1.00 12.80  ? 452  ALA A CA    1 
ATOM   3148 C C     . ALA A 1 410 ? -2.222  6.749   27.179 1.00 14.31  ? 452  ALA A C     1 
ATOM   3149 O O     . ALA A 1 410 ? -2.553  6.993   26.010 1.00 12.46  ? 452  ALA A O     1 
ATOM   3150 C CB    . ALA A 1 410 ? -3.482  5.399   28.811 1.00 13.85  ? 452  ALA A CB    1 
ATOM   3151 N N     . ALA A 1 411 ? -0.961  6.499   27.539 1.00 13.10  ? 453  ALA A N     1 
ATOM   3152 C CA    . ALA A 1 411 ? 0.041   6.168   26.536 1.00 13.28  ? 453  ALA A CA    1 
ATOM   3153 C C     . ALA A 1 411 ? 0.912   5.045   27.070 1.00 14.90  ? 453  ALA A C     1 
ATOM   3154 O O     . ALA A 1 411 ? 1.015   4.880   28.281 1.00 15.71  ? 453  ALA A O     1 
ATOM   3155 C CB    . ALA A 1 411 ? 0.883   7.377   26.224 1.00 14.71  ? 453  ALA A CB    1 
ATOM   3156 N N     . TYR A 1 412 ? 1.544   4.309   26.160 1.00 13.45  ? 454  TYR A N     1 
ATOM   3157 C CA    . TYR A 1 412 ? 2.636   3.419   26.497 1.00 13.38  ? 454  TYR A CA    1 
ATOM   3158 C C     . TYR A 1 412 ? 3.938   4.036   26.014 1.00 12.91  ? 454  TYR A C     1 
ATOM   3159 O O     . TYR A 1 412 ? 4.064   4.413   24.867 1.00 14.65  ? 454  TYR A O     1 
ATOM   3160 C CB    . TYR A 1 412 ? 2.465   2.062   25.829 1.00 13.40  ? 454  TYR A CB    1 
ATOM   3161 C CG    . TYR A 1 412 ? 1.412   1.199   26.456 1.00 12.57  ? 454  TYR A CG    1 
ATOM   3162 C CD1   . TYR A 1 412 ? 1.695   0.346   27.513 1.00 11.83  ? 454  TYR A CD1   1 
ATOM   3163 C CD2   . TYR A 1 412 ? 0.114   1.191   25.992 1.00 12.68  ? 454  TYR A CD2   1 
ATOM   3164 C CE1   . TYR A 1 412 ? 0.747   -0.488  28.069 1.00 9.99   ? 454  TYR A CE1   1 
ATOM   3165 C CE2   . TYR A 1 412 ? -0.862  0.398   26.578 1.00 12.81  ? 454  TYR A CE2   1 
ATOM   3166 C CZ    . TYR A 1 412 ? -0.549  -0.507  27.571 1.00 12.13  ? 454  TYR A CZ    1 
ATOM   3167 O OH    . TYR A 1 412 ? -1.525  -1.289  28.151 1.00 13.22  ? 454  TYR A OH    1 
ATOM   3168 N N     . ALA A 1 413 ? 4.915   4.161   26.924 1.00 12.27  ? 455  ALA A N     1 
ATOM   3169 C CA    . ALA A 1 413 ? 6.264   4.503   26.543 1.00 11.96  ? 455  ALA A CA    1 
ATOM   3170 C C     . ALA A 1 413 ? 7.025   3.196   26.350 1.00 13.21  ? 455  ALA A C     1 
ATOM   3171 O O     . ALA A 1 413 ? 7.332   2.503   27.327 1.00 12.45  ? 455  ALA A O     1 
ATOM   3172 C CB    . ALA A 1 413 ? 6.946   5.354   27.612 1.00 10.90  ? 455  ALA A CB    1 
ATOM   3173 N N     . ILE A 1 414 ? 7.286   2.864   25.087 1.00 14.48  ? 456  ILE A N     1 
ATOM   3174 C CA    . ILE A 1 414 ? 7.874   1.570   24.752 1.00 13.33  ? 456  ILE A CA    1 
ATOM   3175 C C     . ILE A 1 414 ? 9.384   1.672   24.928 1.00 12.79  ? 456  ILE A C     1 
ATOM   3176 O O     . ILE A 1 414 ? 10.031  2.539   24.316 1.00 12.82  ? 456  ILE A O     1 
ATOM   3177 C CB    . ILE A 1 414 ? 7.523   1.182   23.300 1.00 14.27  ? 456  ILE A CB    1 
ATOM   3178 C CG1   . ILE A 1 414 ? 6.004   1.189   23.067 1.00 14.48  ? 456  ILE A CG1   1 
ATOM   3179 C CG2   . ILE A 1 414 ? 8.142   -0.177  22.941 1.00 13.82  ? 456  ILE A CG2   1 
ATOM   3180 C CD1   . ILE A 1 414 ? 5.587   0.931   21.667 1.00 15.46  ? 456  ILE A CD1   1 
ATOM   3181 N N     . GLY A 1 415 ? 9.927   0.763   25.755 1.00 9.80   ? 457  GLY A N     1 
ATOM   3182 C CA    . GLY A 1 415 ? 11.341  0.703   25.987 1.00 11.61  ? 457  GLY A CA    1 
ATOM   3183 C C     . GLY A 1 415 ? 11.982  -0.492  25.310 1.00 13.20  ? 457  GLY A C     1 
ATOM   3184 O O     . GLY A 1 415 ? 11.427  -1.071  24.373 1.00 16.07  ? 457  GLY A O     1 
ATOM   3185 N N     . TRP A 1 416 ? 13.163  -0.841  25.809 1.00 12.76  ? 458  TRP A N     1 
ATOM   3186 C CA    . TRP A 1 416 ? 13.962  -1.853  25.174 1.00 13.22  ? 458  TRP A CA    1 
ATOM   3187 C C     . TRP A 1 416 ? 13.270  -3.194  25.338 1.00 13.98  ? 458  TRP A C     1 
ATOM   3188 O O     . TRP A 1 416 ? 13.048  -3.875  24.345 1.00 17.11  ? 458  TRP A O     1 
ATOM   3189 C CB    . TRP A 1 416 ? 15.371  -1.891  25.802 1.00 14.89  ? 458  TRP A CB    1 
ATOM   3190 C CG    . TRP A 1 416 ? 16.436  -2.450  24.900 1.00 18.02  ? 458  TRP A CG    1 
ATOM   3191 C CD1   . TRP A 1 416 ? 16.253  -3.208  23.781 1.00 18.81  ? 458  TRP A CD1   1 
ATOM   3192 C CD2   . TRP A 1 416 ? 17.852  -2.243  24.995 1.00 20.60  ? 458  TRP A CD2   1 
ATOM   3193 N NE1   . TRP A 1 416 ? 17.459  -3.505  23.189 1.00 18.30  ? 458  TRP A NE1   1 
ATOM   3194 C CE2   . TRP A 1 416 ? 18.455  -2.953  23.925 1.00 19.62  ? 458  TRP A CE2   1 
ATOM   3195 C CE3   . TRP A 1 416 ? 18.659  -1.578  25.919 1.00 25.51  ? 458  TRP A CE3   1 
ATOM   3196 C CZ2   . TRP A 1 416 ? 19.821  -2.955  23.713 1.00 23.38  ? 458  TRP A CZ2   1 
ATOM   3197 C CZ3   . TRP A 1 416 ? 20.021  -1.596  25.718 1.00 27.15  ? 458  TRP A CZ3   1 
ATOM   3198 C CH2   . TRP A 1 416 ? 20.586  -2.282  24.643 1.00 25.20  ? 458  TRP A CH2   1 
ATOM   3199 N N     . ARG A 1 417 ? 12.977  -3.576  26.583 1.00 13.68  ? 459  ARG A N     1 
ATOM   3200 C CA    . ARG A 1 417 ? 12.293  -4.815  26.897 1.00 12.89  ? 459  ARG A CA    1 
ATOM   3201 C C     . ARG A 1 417 ? 11.074  -4.570  27.784 1.00 11.24  ? 459  ARG A C     1 
ATOM   3202 O O     . ARG A 1 417 ? 10.418  -5.548  28.162 1.00 11.06  ? 459  ARG A O     1 
ATOM   3203 C CB    . ARG A 1 417 ? 13.263  -5.796  27.564 1.00 15.40  ? 459  ARG A CB    1 
ATOM   3204 C CG    . ARG A 1 417 ? 14.304  -6.262  26.557 1.00 17.47  ? 459  ARG A CG    1 
ATOM   3205 C CD    . ARG A 1 417 ? 15.559  -6.777  27.113 1.00 18.05  ? 459  ARG A CD    1 
ATOM   3206 N NE    . ARG A 1 417 ? 16.287  -7.560  26.139 1.00 15.04  ? 459  ARG A NE    1 
ATOM   3207 C CZ    . ARG A 1 417 ? 17.408  -7.202  25.525 1.00 12.63  ? 459  ARG A CZ    1 
ATOM   3208 N NH1   . ARG A 1 417 ? 17.836  -5.938  25.498 1.00 13.51  ? 459  ARG A NH1   1 
ATOM   3209 N NH2   . ARG A 1 417 ? 18.099  -8.105  24.877 1.00 10.70  ? 459  ARG A NH2   1 
ATOM   3210 N N     . ASP A 1 418 ? 10.769  -3.285  28.063 1.00 11.14  ? 460  ASP A N     1 
ATOM   3211 C CA    . ASP A 1 418 ? 9.725   -2.908  28.970 1.00 11.46  ? 460  ASP A CA    1 
ATOM   3212 C C     . ASP A 1 418 ? 8.744   -1.943  28.312 1.00 11.85  ? 460  ASP A C     1 
ATOM   3213 O O     . ASP A 1 418 ? 9.071   -1.293  27.308 1.00 13.65  ? 460  ASP A O     1 
ATOM   3214 C CB    . ASP A 1 418 ? 10.280  -2.168  30.212 1.00 14.50  ? 460  ASP A CB    1 
ATOM   3215 C CG    . ASP A 1 418 ? 10.701  -0.723  29.913 1.00 17.38  ? 460  ASP A CG    1 
ATOM   3216 O OD1   . ASP A 1 418 ? 11.788  -0.535  29.398 1.00 17.38  ? 460  ASP A OD1   1 
ATOM   3217 O OD2   . ASP A 1 418 ? 9.813   0.239   30.037 1.00 22.51  ? 460  ASP A OD2   1 
ATOM   3218 N N     . LEU A 1 419 ? 7.590   -1.775  28.964 1.00 13.20  ? 461  LEU A N     1 
ATOM   3219 C CA    . LEU A 1 419 ? 6.682   -0.661  28.691 1.00 13.46  ? 461  LEU A CA    1 
ATOM   3220 C C     . LEU A 1 419 ? 6.441   0.087   29.988 1.00 12.37  ? 461  LEU A C     1 
ATOM   3221 O O     . LEU A 1 419 ? 6.276   -0.587  31.012 1.00 13.82  ? 461  LEU A O     1 
ATOM   3222 C CB    . LEU A 1 419 ? 5.322   -1.172  28.224 1.00 15.29  ? 461  LEU A CB    1 
ATOM   3223 C CG    . LEU A 1 419 ? 5.304   -2.315  27.221 1.00 16.05  ? 461  LEU A CG    1 
ATOM   3224 C CD1   . LEU A 1 419 ? 3.875   -2.839  26.996 1.00 14.92  ? 461  LEU A CD1   1 
ATOM   3225 C CD2   . LEU A 1 419 ? 5.959   -1.853  25.944 1.00 17.64  ? 461  LEU A CD2   1 
ATOM   3226 N N     . HIS A 1 420 ? 6.472   1.438   29.942 1.00 12.31  ? 462  HIS A N     1 
ATOM   3227 C CA    . HIS A 1 420 ? 5.862   2.231   31.004 1.00 12.61  ? 462  HIS A CA    1 
ATOM   3228 C C     . HIS A 1 420 ? 4.430   2.539   30.535 1.00 11.37  ? 462  HIS A C     1 
ATOM   3229 O O     . HIS A 1 420 ? 4.277   3.283   29.544 1.00 13.05  ? 462  HIS A O     1 
ATOM   3230 C CB    . HIS A 1 420 ? 6.577   3.554   31.282 1.00 12.60  ? 462  HIS A CB    1 
ATOM   3231 C CG    . HIS A 1 420 ? 7.974   3.486   31.756 1.00 16.37  ? 462  HIS A CG    1 
ATOM   3232 N ND1   . HIS A 1 420 ? 8.909   2.585   31.279 1.00 21.73  ? 462  HIS A ND1   1 
ATOM   3233 C CD2   . HIS A 1 420 ? 8.626   4.259   32.665 1.00 14.48  ? 462  HIS A CD2   1 
ATOM   3234 C CE1   . HIS A 1 420 ? 10.091  2.807   31.918 1.00 20.92  ? 462  HIS A CE1   1 
ATOM   3235 N NE2   . HIS A 1 420 ? 9.946   3.864   32.733 1.00 14.57  ? 462  HIS A NE2   1 
ATOM   3236 N N     . HIS A 1 421 ? 3.421   1.941   31.172 1.00 10.97  ? 463  HIS A N     1 
ATOM   3237 C CA    . HIS A 1 421 ? 2.029   2.231   30.839 1.00 11.06  ? 463  HIS A CA    1 
ATOM   3238 C C     . HIS A 1 421 ? 1.587   3.483   31.588 1.00 10.50  ? 463  HIS A C     1 
ATOM   3239 O O     . HIS A 1 421 ? 1.368   3.406   32.797 1.00 13.71  ? 463  HIS A O     1 
ATOM   3240 C CB    . HIS A 1 421 ? 1.130   1.062   31.252 1.00 10.72  ? 463  HIS A CB    1 
ATOM   3241 C CG    . HIS A 1 421 ? -0.268  1.156   30.787 1.00 10.51  ? 463  HIS A CG    1 
ATOM   3242 N ND1   . HIS A 1 421 ? -1.112  0.133   31.156 1.00 13.16  ? 463  HIS A ND1   1 
ATOM   3243 C CD2   . HIS A 1 421 ? -0.985  1.998   30.067 1.00 12.66  ? 463  HIS A CD2   1 
ATOM   3244 C CE1   . HIS A 1 421 ? -2.328  0.383   30.615 1.00 13.78  ? 463  HIS A CE1   1 
ATOM   3245 N NE2   . HIS A 1 421 ? -2.266  1.519   29.941 1.00 12.95  ? 463  HIS A NE2   1 
ATOM   3246 N N     . ILE A 1 422 ? 1.532   4.648   30.918 1.00 11.54  ? 464  ILE A N     1 
ATOM   3247 C CA    . ILE A 1 422 ? 1.257   5.934   31.572 1.00 12.71  ? 464  ILE A CA    1 
ATOM   3248 C C     . ILE A 1 422 ? -0.225  6.291   31.490 1.00 12.20  ? 464  ILE A C     1 
ATOM   3249 O O     . ILE A 1 422 ? -0.724  6.594   30.407 1.00 13.87  ? 464  ILE A O     1 
ATOM   3250 C CB    . ILE A 1 422 ? 2.135   7.027   30.960 1.00 12.62  ? 464  ILE A CB    1 
ATOM   3251 C CG1   . ILE A 1 422 ? 3.624   6.634   30.999 1.00 13.50  ? 464  ILE A CG1   1 
ATOM   3252 C CG2   . ILE A 1 422 ? 1.872   8.380   31.621 1.00 13.82  ? 464  ILE A CG2   1 
ATOM   3253 C CD1   . ILE A 1 422 ? 4.151   6.369   32.375 1.00 13.54  ? 464  ILE A CD1   1 
ATOM   3254 N N     . ILE A 1 423 ? -0.915  6.209   32.612 1.00 11.81  ? 465  ILE A N     1 
ATOM   3255 C CA    . ILE A 1 423 ? -2.361  6.416   32.668 1.00 13.20  ? 465  ILE A CA    1 
ATOM   3256 C C     . ILE A 1 423 ? -2.642  7.747   33.372 1.00 13.21  ? 465  ILE A C     1 
ATOM   3257 O O     . ILE A 1 423 ? -2.271  7.952   34.532 1.00 10.74  ? 465  ILE A O     1 
ATOM   3258 C CB    . ILE A 1 423 ? -3.048  5.212   33.358 1.00 12.51  ? 465  ILE A CB    1 
ATOM   3259 C CG1   . ILE A 1 423 ? -2.829  3.881   32.622 1.00 12.59  ? 465  ILE A CG1   1 
ATOM   3260 C CG2   . ILE A 1 423 ? -4.536  5.455   33.604 1.00 14.42  ? 465  ILE A CG2   1 
ATOM   3261 C CD1   . ILE A 1 423 ? -2.978  2.661   33.493 1.00 13.05  ? 465  ILE A CD1   1 
ATOM   3262 N N     . ALA A 1 424 ? -3.195  8.712   32.624 1.00 11.88  ? 466  ALA A N     1 
ATOM   3263 C CA    . ALA A 1 424 ? -3.563  9.979   33.216 1.00 12.84  ? 466  ALA A CA    1 
ATOM   3264 C C     . ALA A 1 424 ? -4.969  9.830   33.773 1.00 11.82  ? 466  ALA A C     1 
ATOM   3265 O O     . ALA A 1 424 ? -5.918  9.636   32.999 1.00 12.18  ? 466  ALA A O     1 
ATOM   3266 C CB    . ALA A 1 424 ? -3.548  11.088  32.187 1.00 13.24  ? 466  ALA A CB    1 
ATOM   3267 N N     . LEU A 1 425 ? -5.122  10.004  35.080 1.00 11.77  ? 467  LEU A N     1 
ATOM   3268 C CA    . LEU A 1 425 ? -6.430  10.099  35.724 1.00 12.28  ? 467  LEU A CA    1 
ATOM   3269 C C     . LEU A 1 425 ? -6.818  11.562  35.785 1.00 12.16  ? 467  LEU A C     1 
ATOM   3270 O O     . LEU A 1 425 ? -6.264  12.327  36.557 1.00 12.97  ? 467  LEU A O     1 
ATOM   3271 C CB    . LEU A 1 425 ? -6.419  9.468   37.113 1.00 12.76  ? 467  LEU A CB    1 
ATOM   3272 C CG    . LEU A 1 425 ? -7.779  9.422   37.794 1.00 13.74  ? 467  LEU A CG    1 
ATOM   3273 C CD1   . LEU A 1 425 ? -8.759  8.659   36.926 1.00 15.63  ? 467  LEU A CD1   1 
ATOM   3274 C CD2   . LEU A 1 425 ? -7.693  8.804   39.185 1.00 14.33  ? 467  LEU A CD2   1 
ATOM   3275 N N     . LEU A 1 426 ? -7.684  11.968  34.824 1.00 11.59  ? 468  LEU A N     1 
ATOM   3276 C CA    . LEU A 1 426 ? -8.077  13.358  34.664 1.00 12.13  ? 468  LEU A CA    1 
ATOM   3277 C C     . LEU A 1 426 ? -9.428  13.587  35.365 1.00 13.70  ? 468  LEU A C     1 
ATOM   3278 O O     . LEU A 1 426 ? -10.369 12.781  35.167 1.00 14.08  ? 468  LEU A O     1 
ATOM   3279 C CB    . LEU A 1 426 ? -8.194  13.674  33.167 1.00 12.52  ? 468  LEU A CB    1 
ATOM   3280 C CG    . LEU A 1 426 ? -6.912  13.456  32.356 1.00 13.49  ? 468  LEU A CG    1 
ATOM   3281 C CD1   . LEU A 1 426 ? -7.163  13.671  30.876 1.00 14.86  ? 468  LEU A CD1   1 
ATOM   3282 C CD2   . LEU A 1 426 ? -5.795  14.393  32.824 1.00 13.31  ? 468  LEU A CD2   1 
ATOM   3283 N N     . PHE A 1 427 ? -9.493  14.664  36.183 1.00 12.62  ? 469  PHE A N     1 
ATOM   3284 C CA    . PHE A 1 427 ? -10.700 14.914  36.954 1.00 12.61  ? 469  PHE A CA    1 
ATOM   3285 C C     . PHE A 1 427 ? -10.876 16.402  37.208 1.00 12.90  ? 469  PHE A C     1 
ATOM   3286 O O     . PHE A 1 427 ? -9.984  17.201  36.960 1.00 12.85  ? 469  PHE A O     1 
ATOM   3287 C CB    . PHE A 1 427 ? -10.753 14.054  38.225 1.00 13.18  ? 469  PHE A CB    1 
ATOM   3288 C CG    . PHE A 1 427 ? -9.675  14.355  39.221 1.00 12.41  ? 469  PHE A CG    1 
ATOM   3289 C CD1   . PHE A 1 427 ? -8.407  13.828  39.026 1.00 13.13  ? 469  PHE A CD1   1 
ATOM   3290 C CD2   . PHE A 1 427 ? -9.900  15.201  40.302 1.00 12.24  ? 469  PHE A CD2   1 
ATOM   3291 C CE1   . PHE A 1 427 ? -7.382  14.108  39.926 1.00 12.60  ? 469  PHE A CE1   1 
ATOM   3292 C CE2   . PHE A 1 427 ? -8.885  15.454  41.201 1.00 13.06  ? 469  PHE A CE2   1 
ATOM   3293 C CZ    . PHE A 1 427 ? -7.626  14.924  40.980 1.00 12.78  ? 469  PHE A CZ    1 
ATOM   3294 N N     . ASP A 1 428 ? -12.110 16.740  37.652 1.00 12.90  ? 470  ASP A N     1 
ATOM   3295 C CA    . ASP A 1 428 ? -12.440 18.088  38.107 1.00 14.36  ? 470  ASP A CA    1 
ATOM   3296 C C     . ASP A 1 428 ? -12.104 18.233  39.596 1.00 12.91  ? 470  ASP A C     1 
ATOM   3297 O O     . ASP A 1 428 ? -12.863 17.813  40.494 1.00 13.51  ? 470  ASP A O     1 
ATOM   3298 C CB    . ASP A 1 428 ? -13.908 18.349  37.760 1.00 13.60  ? 470  ASP A CB    1 
ATOM   3299 C CG    . ASP A 1 428 ? -14.369 19.750  38.130 1.00 17.39  ? 470  ASP A CG    1 
ATOM   3300 O OD1   . ASP A 1 428 ? -13.618 20.469  38.843 1.00 16.27  ? 470  ASP A OD1   1 
ATOM   3301 O OD2   . ASP A 1 428 ? -15.496 20.116  37.642 1.00 17.95  ? 470  ASP A OD2   1 
ATOM   3302 N N     . LYS A 1 429 ? -10.912 18.775  39.879 1.00 13.35  ? 471  LYS A N     1 
ATOM   3303 C CA    . LYS A 1 429 ? -10.459 18.831  41.265 1.00 13.20  ? 471  LYS A CA    1 
ATOM   3304 C C     . LYS A 1 429 ? -11.263 19.834  42.097 1.00 16.10  ? 471  LYS A C     1 
ATOM   3305 O O     . LYS A 1 429 ? -11.314 19.709  43.325 1.00 17.46  ? 471  LYS A O     1 
ATOM   3306 C CB    . LYS A 1 429 ? -8.962  19.113  41.326 1.00 14.50  ? 471  LYS A CB    1 
ATOM   3307 C CG    . LYS A 1 429 ? -8.383  19.085  42.742 1.00 14.01  ? 471  LYS A CG    1 
ATOM   3308 C CD    . LYS A 1 429 ? -6.874  19.018  42.827 1.00 15.46  ? 471  LYS A CD    1 
ATOM   3309 C CE    . LYS A 1 429 ? -6.411  19.163  44.271 1.00 14.60  ? 471  LYS A CE    1 
ATOM   3310 N NZ    . LYS A 1 429 ? -4.941  18.980  44.420 1.00 14.83  ? 471  LYS A NZ    1 
ATOM   3311 N N     . ALA A 1 430 ? -11.822 20.852  41.429 1.00 14.80  ? 472  ALA A N     1 
ATOM   3312 C CA    . ALA A 1 430 ? -12.580 21.896  42.123 1.00 16.03  ? 472  ALA A CA    1 
ATOM   3313 C C     . ALA A 1 430 ? -13.931 21.387  42.600 1.00 17.02  ? 472  ALA A C     1 
ATOM   3314 O O     . ALA A 1 430 ? -14.602 22.077  43.378 1.00 20.29  ? 472  ALA A O     1 
ATOM   3315 C CB    . ALA A 1 430 ? -12.748 23.071  41.188 1.00 16.35  ? 472  ALA A CB    1 
ATOM   3316 N N     . ASP A 1 431 ? -14.339 20.190  42.172 1.00 16.36  ? 473  ASP A N     1 
ATOM   3317 C CA    . ASP A 1 431 ? -15.561 19.564  42.655 1.00 16.37  ? 473  ASP A CA    1 
ATOM   3318 C C     . ASP A 1 431 ? -15.168 18.531  43.695 1.00 17.45  ? 473  ASP A C     1 
ATOM   3319 O O     . ASP A 1 431 ? -14.588 17.489  43.357 1.00 15.73  ? 473  ASP A O     1 
ATOM   3320 C CB    . ASP A 1 431 ? -16.395 18.962  41.538 1.00 16.73  ? 473  ASP A CB    1 
ATOM   3321 C CG    . ASP A 1 431 ? -17.639 18.221  41.972 1.00 20.02  ? 473  ASP A CG    1 
ATOM   3322 O OD1   . ASP A 1 431 ? -17.699 17.756  43.101 1.00 20.48  ? 473  ASP A OD1   1 
ATOM   3323 O OD2   . ASP A 1 431 ? -18.562 18.133  41.146 1.00 27.94  ? 473  ASP A OD2   1 
ATOM   3324 N N     . PRO A 1 432 ? -15.416 18.810  44.988 1.00 18.86  ? 474  PRO A N     1 
ATOM   3325 C CA    . PRO A 1 432 ? -14.888 17.940  46.046 1.00 18.10  ? 474  PRO A CA    1 
ATOM   3326 C C     . PRO A 1 432 ? -15.350 16.490  45.964 1.00 17.83  ? 474  PRO A C     1 
ATOM   3327 O O     . PRO A 1 432 ? -14.598 15.568  46.323 1.00 18.41  ? 474  PRO A O     1 
ATOM   3328 C CB    . PRO A 1 432 ? -15.389 18.551  47.373 1.00 21.36  ? 474  PRO A CB    1 
ATOM   3329 C CG    . PRO A 1 432 ? -16.047 19.851  47.011 1.00 20.89  ? 474  PRO A CG    1 
ATOM   3330 C CD    . PRO A 1 432 ? -16.113 19.992  45.512 1.00 18.80  ? 474  PRO A CD    1 
ATOM   3331 N N     . THR A 1 433 ? -16.542 16.235  45.406 1.00 15.72  ? 475  THR A N     1 
ATOM   3332 C CA    . THR A 1 433 ? -17.013 14.881  45.201 1.00 17.05  ? 475  THR A CA    1 
ATOM   3333 C C     . THR A 1 433 ? -16.172 14.172  44.138 1.00 17.04  ? 475  THR A C     1 
ATOM   3334 O O     . THR A 1 433 ? -15.825 13.010  44.287 1.00 16.80  ? 475  THR A O     1 
ATOM   3335 C CB    . THR A 1 433 ? -18.501 14.852  44.802 1.00 22.74  ? 475  THR A CB    1 
ATOM   3336 O OG1   . THR A 1 433 ? -19.225 15.488  45.860 1.00 24.18  ? 475  THR A OG1   1 
ATOM   3337 C CG2   . THR A 1 433 ? -19.013 13.445  44.617 1.00 23.80  ? 475  THR A CG2   1 
ATOM   3338 N N     . GLN A 1 434 ? -15.852 14.888  43.059 1.00 13.69  ? 476  GLN A N     1 
ATOM   3339 C CA    . GLN A 1 434 ? -15.046 14.349  41.991 1.00 13.34  ? 476  GLN A CA    1 
ATOM   3340 C C     . GLN A 1 434 ? -13.619 14.083  42.473 1.00 13.68  ? 476  GLN A C     1 
ATOM   3341 O O     . GLN A 1 434 ? -13.071 13.037  42.107 1.00 14.76  ? 476  GLN A O     1 
ATOM   3342 C CB    . GLN A 1 434 ? -15.040 15.259  40.770 1.00 14.28  ? 476  GLN A CB    1 
ATOM   3343 C CG    . GLN A 1 434 ? -16.356 15.270  40.012 1.00 16.49  ? 476  GLN A CG    1 
ATOM   3344 C CD    . GLN A 1 434 ? -16.766 13.925  39.486 1.00 17.72  ? 476  GLN A CD    1 
ATOM   3345 O OE1   . GLN A 1 434 ? -16.006 13.244  38.798 1.00 17.42  ? 476  GLN A OE1   1 
ATOM   3346 N NE2   . GLN A 1 434 ? -17.969 13.515  39.855 1.00 21.57  ? 476  GLN A NE2   1 
ATOM   3347 N N     . GLU A 1 435 ? -13.110 14.921  43.372 1.00 13.98  ? 477  GLU A N     1 
ATOM   3348 C CA    . GLU A 1 435 ? -11.765 14.697  43.902 1.00 13.33  ? 477  GLU A CA    1 
ATOM   3349 C C     . GLU A 1 435 ? -11.783 13.443  44.769 1.00 14.01  ? 477  GLU A C     1 
ATOM   3350 O O     . GLU A 1 435 ? -10.889 12.606  44.674 1.00 12.85  ? 477  GLU A O     1 
ATOM   3351 C CB    . GLU A 1 435 ? -11.323 15.923  44.693 1.00 13.94  ? 477  GLU A CB    1 
ATOM   3352 C CG    . GLU A 1 435 ? -9.997  15.737  45.402 1.00 15.61  ? 477  GLU A CG    1 
ATOM   3353 C CD    . GLU A 1 435 ? -9.573  16.904  46.264 1.00 17.91  ? 477  GLU A CD    1 
ATOM   3354 O OE1   . GLU A 1 435 ? -10.475 17.523  46.896 1.00 19.14  ? 477  GLU A OE1   1 
ATOM   3355 O OE2   . GLU A 1 435 ? -8.389  17.231  46.282 1.00 17.62  ? 477  GLU A OE2   1 
ATOM   3356 N N     . GLN A 1 436 ? -12.834 13.268  45.573 1.00 15.77  ? 478  GLN A N     1 
ATOM   3357 C CA    . GLN A 1 436 ? -12.969 12.069  46.400 1.00 16.09  ? 478  GLN A CA    1 
ATOM   3358 C C     . GLN A 1 436 ? -13.073 10.819  45.540 1.00 15.13  ? 478  GLN A C     1 
ATOM   3359 O O     . GLN A 1 436 ? -12.438 9.792   45.842 1.00 15.38  ? 478  GLN A O     1 
ATOM   3360 C CB    . GLN A 1 436 ? -14.170 12.167  47.358 1.00 21.24  ? 478  GLN A CB    1 
ATOM   3361 C CG    . GLN A 1 436 ? -13.900 12.900  48.643 1.00 29.48  ? 478  GLN A CG    1 
ATOM   3362 C CD    . GLN A 1 436 ? -15.126 13.422  49.376 1.00 40.79  ? 478  GLN A CD    1 
ATOM   3363 O OE1   . GLN A 1 436 ? -16.265 13.361  48.912 1.00 44.59  ? 478  GLN A OE1   1 
ATOM   3364 N NE2   . GLN A 1 436 ? -14.884 14.001  50.538 1.00 47.75  ? 478  GLN A NE2   1 
ATOM   3365 N N     . LYS A 1 437 ? -13.884 10.853  44.477 1.00 14.18  ? 479  LYS A N     1 
ATOM   3366 C CA    . LYS A 1 437 ? -14.001 9.705   43.590 1.00 13.79  ? 479  LYS A CA    1 
ATOM   3367 C C     . LYS A 1 437 ? -12.665 9.376   42.926 1.00 13.58  ? 479  LYS A C     1 
ATOM   3368 O O     . LYS A 1 437 ? -12.397 8.201   42.633 1.00 14.26  ? 479  LYS A O     1 
ATOM   3369 C CB    . LYS A 1 437 ? -15.115 9.896   42.547 1.00 15.65  ? 479  LYS A CB    1 
ATOM   3370 C CG    . LYS A 1 437 ? -16.509 9.842   43.159 1.00 15.70  ? 479  LYS A CG    1 
ATOM   3371 C CD    . LYS A 1 437 ? -17.577 10.283  42.178 1.00 20.07  ? 479  LYS A CD    1 
ATOM   3372 C CE    . LYS A 1 437 ? -17.780 9.309   41.050 1.00 26.37  ? 479  LYS A CE    1 
ATOM   3373 N NZ    . LYS A 1 437 ? -17.807 7.927   41.545 1.00 32.23  ? 479  LYS A NZ    1 
ATOM   3374 N N     . ALA A 1 438 ? -11.898 10.394  42.506 1.00 13.78  ? 480  ALA A N     1 
ATOM   3375 C CA    . ALA A 1 438 ? -10.606 10.147  41.857 1.00 13.82  ? 480  ALA A CA    1 
ATOM   3376 C C     . ALA A 1 438 ? -9.651  9.463   42.855 1.00 13.09  ? 480  ALA A C     1 
ATOM   3377 O O     . ALA A 1 438 ? -8.894  8.568   42.442 1.00 14.42  ? 480  ALA A O     1 
ATOM   3378 C CB    . ALA A 1 438 ? -9.997  11.406  41.274 1.00 14.47  ? 480  ALA A CB    1 
ATOM   3379 N N     . ASP A 1 439 ? -9.667  9.922   44.115 1.00 13.62  ? 481  ASP A N     1 
ATOM   3380 C CA    . ASP A 1 439 ? -8.858  9.304   45.148 1.00 14.36  ? 481  ASP A CA    1 
ATOM   3381 C C     . ASP A 1 439 ? -9.215  7.819   45.241 1.00 14.43  ? 481  ASP A C     1 
ATOM   3382 O O     . ASP A 1 439 ? -8.313  6.987   45.330 1.00 14.30  ? 481  ASP A O     1 
ATOM   3383 C CB    . ASP A 1 439 ? -9.061  10.046  46.469 1.00 16.21  ? 481  ASP A CB    1 
ATOM   3384 C CG    . ASP A 1 439 ? -7.948  9.827   47.468 1.00 22.66  ? 481  ASP A CG    1 
ATOM   3385 O OD1   . ASP A 1 439 ? -6.743  9.993   47.069 1.00 20.64  ? 481  ASP A OD1   1 
ATOM   3386 O OD2   . ASP A 1 439 ? -8.303  9.543   48.635 1.00 25.03  ? 481  ASP A OD2   1 
ATOM   3387 N N     . ALA A 1 440 ? -10.523 7.486   45.267 1.00 11.96  ? 482  ALA A N     1 
ATOM   3388 C CA    . ALA A 1 440 ? -10.937 6.097   45.416 1.00 14.51  ? 482  ALA A CA    1 
ATOM   3389 C C     . ALA A 1 440 ? -10.548 5.297   44.185 1.00 13.18  ? 482  ALA A C     1 
ATOM   3390 O O     . ALA A 1 440 ? -10.157 4.144   44.267 1.00 13.58  ? 482  ALA A O     1 
ATOM   3391 C CB    . ALA A 1 440 ? -12.454 6.000   45.695 1.00 14.54  ? 482  ALA A CB    1 
ATOM   3392 N N     . CYS A 1 441 ? -10.741 5.865   42.994 1.00 13.07  ? 483  CYS A N     1 
ATOM   3393 C CA    . CYS A 1 441 ? -10.351 5.216   41.757 1.00 11.88  ? 483  CYS A CA    1 
ATOM   3394 C C     . CYS A 1 441 ? -8.845  4.884   41.750 1.00 13.34  ? 483  CYS A C     1 
ATOM   3395 O O     . CYS A 1 441 ? -8.446  3.758   41.416 1.00 14.57  ? 483  CYS A O     1 
ATOM   3396 C CB    . CYS A 1 441 ? -10.663 6.185   40.620 1.00 12.98  ? 483  CYS A CB    1 
ATOM   3397 S SG    . CYS A 1 441 ? -10.300 5.509   38.993 1.00 14.75  ? 483  CYS A SG    1 
ATOM   3398 N N     . TYR A 1 442 ? -8.027  5.877   42.161 1.00 12.88  ? 484  TYR A N     1 
ATOM   3399 C CA    . TYR A 1 442 ? -6.571  5.713   42.159 1.00 12.69  ? 484  TYR A CA    1 
ATOM   3400 C C     . TYR A 1 442 ? -6.197  4.523   43.052 1.00 13.07  ? 484  TYR A C     1 
ATOM   3401 O O     . TYR A 1 442 ? -5.374  3.682   42.687 1.00 13.37  ? 484  TYR A O     1 
ATOM   3402 C CB    . TYR A 1 442 ? -5.836  6.998   42.546 1.00 12.26  ? 484  TYR A CB    1 
ATOM   3403 C CG    . TYR A 1 442 ? -4.384  6.979   42.129 1.00 13.03  ? 484  TYR A CG    1 
ATOM   3404 C CD1   . TYR A 1 442 ? -3.431  6.280   42.862 1.00 11.67  ? 484  TYR A CD1   1 
ATOM   3405 C CD2   . TYR A 1 442 ? -3.970  7.577   40.947 1.00 12.21  ? 484  TYR A CD2   1 
ATOM   3406 C CE1   . TYR A 1 442 ? -2.133  6.153   42.410 1.00 11.00  ? 484  TYR A CE1   1 
ATOM   3407 C CE2   . TYR A 1 442 ? -2.641  7.543   40.531 1.00 11.73  ? 484  TYR A CE2   1 
ATOM   3408 C CZ    . TYR A 1 442 ? -1.713  6.818   41.274 1.00 11.84  ? 484  TYR A CZ    1 
ATOM   3409 O OH    . TYR A 1 442 ? -0.396  6.747   40.822 1.00 11.12  ? 484  TYR A OH    1 
ATOM   3410 N N     . ARG A 1 443 ? -6.784  4.476   44.246 1.00 13.44  ? 485  ARG A N     1 
ATOM   3411 C CA    . ARG A 1 443 ? -6.472  3.391   45.159 1.00 14.14  ? 485  ARG A CA    1 
ATOM   3412 C C     . ARG A 1 443 ? -6.813  2.039   44.538 1.00 14.23  ? 485  ARG A C     1 
ATOM   3413 O O     . ARG A 1 443 ? -6.065  1.063   44.682 1.00 13.56  ? 485  ARG A O     1 
ATOM   3414 C CB    . ARG A 1 443 ? -7.226  3.603   46.468 1.00 15.74  ? 485  ARG A CB    1 
ATOM   3415 C CG    . ARG A 1 443 ? -7.147  2.429   47.425 1.00 22.13  ? 485  ARG A CG    1 
ATOM   3416 C CD    . ARG A 1 443 ? -8.037  2.661   48.627 1.00 26.16  ? 485  ARG A CD    1 
ATOM   3417 N NE    . ARG A 1 443 ? -7.319  3.483   49.567 1.00 32.36  ? 485  ARG A NE    1 
ATOM   3418 C CZ    . ARG A 1 443 ? -6.263  3.066   50.279 1.00 37.99  ? 485  ARG A CZ    1 
ATOM   3419 N NH1   . ARG A 1 443 ? -5.943  1.784   50.331 1.00 37.58  ? 485  ARG A NH1   1 
ATOM   3420 N NH2   . ARG A 1 443 ? -5.535  3.947   50.943 1.00 41.57  ? 485  ARG A NH2   1 
ATOM   3421 N N     . GLU A 1 444 ? -7.963  1.944   43.868 1.00 12.43  ? 486  GLU A N     1 
ATOM   3422 C CA    . GLU A 1 444 ? -8.385  0.718   43.217 1.00 12.99  ? 486  GLU A CA    1 
ATOM   3423 C C     . GLU A 1 444 ? -7.431  0.341   42.088 1.00 11.66  ? 486  GLU A C     1 
ATOM   3424 O O     . GLU A 1 444 ? -7.097  -0.837  41.892 1.00 12.97  ? 486  GLU A O     1 
ATOM   3425 C CB    . GLU A 1 444 ? -9.862  0.778   42.720 1.00 13.27  ? 486  GLU A CB    1 
ATOM   3426 C CG    . GLU A 1 444 ? -10.297 -0.517  42.064 1.00 14.30  ? 486  GLU A CG    1 
ATOM   3427 C CD    . GLU A 1 444 ? -11.802 -0.704  41.876 1.00 17.88  ? 486  GLU A CD    1 
ATOM   3428 O OE1   . GLU A 1 444 ? -12.546 0.124   42.393 1.00 18.47  ? 486  GLU A OE1   1 
ATOM   3429 O OE2   . GLU A 1 444 ? -12.209 -1.647  41.221 1.00 22.02  ? 486  GLU A OE2   1 
ATOM   3430 N N     . LEU A 1 445 ? -6.920  1.314   41.334 1.00 11.87  ? 487  LEU A N     1 
ATOM   3431 C CA    . LEU A 1 445 ? -5.956  1.025   40.277 1.00 12.48  ? 487  LEU A CA    1 
ATOM   3432 C C     . LEU A 1 445 ? -4.728  0.363   40.901 1.00 11.69  ? 487  LEU A C     1 
ATOM   3433 O O     . LEU A 1 445 ? -4.306  -0.695  40.416 1.00 12.19  ? 487  LEU A O     1 
ATOM   3434 C CB    . LEU A 1 445 ? -5.529  2.324   39.583 1.00 12.95  ? 487  LEU A CB    1 
ATOM   3435 C CG    . LEU A 1 445 ? -6.521  2.870   38.548 1.00 13.43  ? 487  LEU A CG    1 
ATOM   3436 C CD1   . LEU A 1 445 ? -6.143  4.290   38.082 1.00 15.16  ? 487  LEU A CD1   1 
ATOM   3437 C CD2   . LEU A 1 445 ? -6.636  1.944   37.360 1.00 14.35  ? 487  LEU A CD2   1 
ATOM   3438 N N     . VAL A 1 446 ? -4.170  0.981   41.945 1.00 11.18  ? 488  VAL A N     1 
ATOM   3439 C CA    . VAL A 1 446 ? -2.928  0.444   42.505 1.00 11.94  ? 488  VAL A CA    1 
ATOM   3440 C C     . VAL A 1 446 ? -3.166  -0.994  43.046 1.00 11.83  ? 488  VAL A C     1 
ATOM   3441 O O     . VAL A 1 446 ? -2.385  -1.912  42.795 1.00 11.73  ? 488  VAL A O     1 
ATOM   3442 C CB    . VAL A 1 446 ? -2.345  1.363   43.583 1.00 12.53  ? 488  VAL A CB    1 
ATOM   3443 C CG1   . VAL A 1 446 ? -1.145  0.720   44.298 1.00 12.40  ? 488  VAL A CG1   1 
ATOM   3444 C CG2   . VAL A 1 446 ? -1.986  2.752   43.035 1.00 12.06  ? 488  VAL A CG2   1 
ATOM   3445 N N     . THR A 1 447 ? -4.252  -1.169  43.788 1.00 12.41  ? 489  THR A N     1 
ATOM   3446 C CA    . THR A 1 447 ? -4.517  -2.410  44.533 1.00 13.56  ? 489  THR A CA    1 
ATOM   3447 C C     . THR A 1 447 ? -4.805  -3.544  43.553 1.00 13.07  ? 489  THR A C     1 
ATOM   3448 O O     . THR A 1 447 ? -4.254  -4.641  43.647 1.00 14.28  ? 489  THR A O     1 
ATOM   3449 C CB    . THR A 1 447 ? -5.677  -2.174  45.528 1.00 16.11  ? 489  THR A CB    1 
ATOM   3450 O OG1   . THR A 1 447 ? -5.185  -1.151  46.412 1.00 21.78  ? 489  THR A OG1   1 
ATOM   3451 C CG2   . THR A 1 447 ? -6.003  -3.406  46.332 1.00 22.29  ? 489  THR A CG2   1 
ATOM   3452 N N     . ARG A 1 448 ? -5.682  -3.301  42.573 1.00 13.23  ? 490  ARG A N     1 
ATOM   3453 C CA    . ARG A 1 448 ? -6.058  -4.345  41.625 1.00 13.81  ? 490  ARG A CA    1 
ATOM   3454 C C     . ARG A 1 448 ? -4.935  -4.674  40.656 1.00 12.83  ? 490  ARG A C     1 
ATOM   3455 O O     . ARG A 1 448 ? -4.737  -5.842  40.304 1.00 12.75  ? 490  ARG A O     1 
ATOM   3456 C CB    . ARG A 1 448 ? -7.396  -4.048  40.960 1.00 13.41  ? 490  ARG A CB    1 
ATOM   3457 C CG    . ARG A 1 448 ? -8.558  -4.206  41.949 1.00 15.89  ? 490  ARG A CG    1 
ATOM   3458 C CD    . ARG A 1 448 ? -9.892  -4.007  41.287 1.00 19.70  ? 490  ARG A CD    1 
ATOM   3459 N NE    . ARG A 1 448 ? -10.201 -5.048  40.313 1.00 20.67  ? 490  ARG A NE    1 
ATOM   3460 C CZ    . ARG A 1 448 ? -11.130 -4.925  39.382 1.00 20.51  ? 490  ARG A CZ    1 
ATOM   3461 N NH1   . ARG A 1 448 ? -11.892 -3.850  39.354 1.00 20.80  ? 490  ARG A NH1   1 
ATOM   3462 N NH2   . ARG A 1 448 ? -11.305 -5.889  38.494 1.00 22.90  ? 490  ARG A NH2   1 
ATOM   3463 N N     . PHE A 1 449 ? -4.154  -3.678  40.204 1.00 13.52  ? 491  PHE A N     1 
ATOM   3464 C CA    . PHE A 1 449 ? -2.985  -3.996  39.391 1.00 12.94  ? 491  PHE A CA    1 
ATOM   3465 C C     . PHE A 1 449 ? -1.997  -4.877  40.175 1.00 11.43  ? 491  PHE A C     1 
ATOM   3466 O O     . PHE A 1 449 ? -1.464  -5.828  39.623 1.00 12.28  ? 491  PHE A O     1 
ATOM   3467 C CB    . PHE A 1 449 ? -2.332  -2.704  38.866 1.00 13.18  ? 491  PHE A CB    1 
ATOM   3468 C CG    . PHE A 1 449 ? -2.844  -2.294  37.506 1.00 11.21  ? 491  PHE A CG    1 
ATOM   3469 C CD1   . PHE A 1 449 ? -4.181  -1.984  37.320 1.00 12.31  ? 491  PHE A CD1   1 
ATOM   3470 C CD2   . PHE A 1 449 ? -2.009  -2.206  36.430 1.00 11.51  ? 491  PHE A CD2   1 
ATOM   3471 C CE1   . PHE A 1 449 ? -4.641  -1.565  36.087 1.00 12.75  ? 491  PHE A CE1   1 
ATOM   3472 C CE2   . PHE A 1 449 ? -2.458  -1.803  35.189 1.00 12.30  ? 491  PHE A CE2   1 
ATOM   3473 C CZ    . PHE A 1 449 ? -3.795  -1.521  35.007 1.00 11.49  ? 491  PHE A CZ    1 
ATOM   3474 N N     . GLY A 1 450 ? -1.788  -4.543  41.440 1.00 12.20  ? 492  GLY A N     1 
ATOM   3475 C CA    . GLY A 1 450 ? -0.829  -5.251  42.292 1.00 13.71  ? 492  GLY A CA    1 
ATOM   3476 C C     . GLY A 1 450 ? -1.222  -6.723  42.418 1.00 14.64  ? 492  GLY A C     1 
ATOM   3477 O O     . GLY A 1 450 ? -0.355  -7.589  42.311 1.00 15.40  ? 492  GLY A O     1 
ATOM   3478 N N     . ALA A 1 451 ? -2.527  -6.960  42.586 1.00 12.66  ? 493  ALA A N     1 
ATOM   3479 C CA    . ALA A 1 451 ? -3.038  -8.336  42.644 1.00 14.43  ? 493  ALA A CA    1 
ATOM   3480 C C     . ALA A 1 451 ? -2.808  -9.151  41.366 1.00 15.42  ? 493  ALA A C     1 
ATOM   3481 O O     . ALA A 1 451 ? -2.788  -10.373 41.429 1.00 17.33  ? 493  ALA A O     1 
ATOM   3482 C CB    . ALA A 1 451 ? -4.504  -8.343  43.046 1.00 16.13  ? 493  ALA A CB    1 
ATOM   3483 N N     . GLN A 1 452 ? -2.673  -8.534  40.180 1.00 15.79  ? 494  GLN A N     1 
ATOM   3484 C CA    . GLN A 1 452 ? -2.341  -9.181  38.923 1.00 15.56  ? 494  GLN A CA    1 
ATOM   3485 C C     . GLN A 1 452 ? -0.825  -9.197  38.660 1.00 14.73  ? 494  GLN A C     1 
ATOM   3486 O O     . GLN A 1 452 ? -0.383  -9.638  37.594 1.00 15.86  ? 494  GLN A O     1 
ATOM   3487 C CB    . GLN A 1 452 ? -3.007  -8.439  37.747 1.00 16.28  ? 494  GLN A CB    1 
ATOM   3488 C CG    . GLN A 1 452 ? -4.527  -8.453  37.853 1.00 19.42  ? 494  GLN A CG    1 
ATOM   3489 C CD    . GLN A 1 452 ? -5.084  -9.858  37.968 1.00 19.81  ? 494  GLN A CD    1 
ATOM   3490 O OE1   . GLN A 1 452 ? -4.687  -10.736 37.220 1.00 23.74  ? 494  GLN A OE1   1 
ATOM   3491 N NE2   . GLN A 1 452 ? -5.963  -10.089 38.933 1.00 21.72  ? 494  GLN A NE2   1 
ATOM   3492 N N     . GLY A 1 453 ? -0.014  -8.748  39.625 1.00 13.89  ? 495  GLY A N     1 
ATOM   3493 C CA    . GLY A 1 453 ? 1.425   -8.802  39.504 1.00 13.59  ? 495  GLY A CA    1 
ATOM   3494 C C     . GLY A 1 453 ? 2.088   -7.556  38.873 1.00 15.54  ? 495  GLY A C     1 
ATOM   3495 O O     . GLY A 1 453 ? 3.256   -7.614  38.477 1.00 15.53  ? 495  GLY A O     1 
ATOM   3496 N N     . TRP A 1 454 ? 1.369   -6.411  38.836 1.00 12.63  ? 496  TRP A N     1 
ATOM   3497 C CA    . TRP A 1 454 ? 1.836   -5.189  38.204 1.00 12.54  ? 496  TRP A CA    1 
ATOM   3498 C C     . TRP A 1 454 ? 1.923   -4.052  39.212 1.00 11.80  ? 496  TRP A C     1 
ATOM   3499 O O     . TRP A 1 454 ? 1.033   -3.837  40.039 1.00 14.06  ? 496  TRP A O     1 
ATOM   3500 C CB    . TRP A 1 454 ? 0.859   -4.788  37.096 1.00 12.37  ? 496  TRP A CB    1 
ATOM   3501 C CG    . TRP A 1 454 ? 0.626   -5.810  36.040 1.00 12.56  ? 496  TRP A CG    1 
ATOM   3502 C CD1   . TRP A 1 454 ? 1.574   -6.500  35.347 1.00 15.50  ? 496  TRP A CD1   1 
ATOM   3503 C CD2   . TRP A 1 454 ? -0.633  -6.129  35.424 1.00 14.62  ? 496  TRP A CD2   1 
ATOM   3504 N NE1   . TRP A 1 454 ? 0.973   -7.331  34.436 1.00 16.08  ? 496  TRP A NE1   1 
ATOM   3505 C CE2   . TRP A 1 454 ? -0.361  -7.106  34.444 1.00 16.08  ? 496  TRP A CE2   1 
ATOM   3506 C CE3   . TRP A 1 454 ? -1.962  -5.799  35.673 1.00 14.30  ? 496  TRP A CE3   1 
ATOM   3507 C CZ2   . TRP A 1 454 ? -1.376  -7.697  33.698 1.00 15.76  ? 496  TRP A CZ2   1 
ATOM   3508 C CZ3   . TRP A 1 454 ? -2.961  -6.356  34.912 1.00 15.51  ? 496  TRP A CZ3   1 
ATOM   3509 C CH2   . TRP A 1 454 ? -2.663  -7.299  33.943 1.00 17.10  ? 496  TRP A CH2   1 
ATOM   3510 N N     . ALA A 1 455 ? 2.987   -3.252  39.101 1.00 12.54  ? 497  ALA A N     1 
ATOM   3511 C CA    . ALA A 1 455 ? 3.149   -2.131  39.995 1.00 10.67  ? 497  ALA A CA    1 
ATOM   3512 C C     . ALA A 1 455 ? 3.936   -1.022  39.260 1.00 10.19  ? 497  ALA A C     1 
ATOM   3513 O O     . ALA A 1 455 ? 4.510   -1.209  38.180 1.00 9.32   ? 497  ALA A O     1 
ATOM   3514 C CB    . ALA A 1 455 ? 3.777   -2.495  41.318 1.00 12.50  ? 497  ALA A CB    1 
ATOM   3515 N N     . SER A 1 456 ? 3.941   0.161   39.867 1.00 10.38  ? 498  SER A N     1 
ATOM   3516 C CA    . SER A 1 456 ? 4.380   1.393   39.281 1.00 10.48  ? 498  SER A CA    1 
ATOM   3517 C C     . SER A 1 456 ? 5.884   1.523   39.227 1.00 10.82  ? 498  SER A C     1 
ATOM   3518 O O     . SER A 1 456 ? 6.574   1.107   40.153 1.00 10.24  ? 498  SER A O     1 
ATOM   3519 C CB    . SER A 1 456 ? 3.783   2.554   40.054 1.00 11.97  ? 498  SER A CB    1 
ATOM   3520 O OG    . SER A 1 456 ? 2.357   2.531   39.975 1.00 12.31  ? 498  SER A OG    1 
ATOM   3521 N N     . TYR A 1 457 ? 6.352   2.226   38.179 1.00 10.25  ? 499  TYR A N     1 
ATOM   3522 C CA    . TYR A 1 457 ? 7.752   2.685   38.067 1.00 11.30  ? 499  TYR A CA    1 
ATOM   3523 C C     . TYR A 1 457 ? 8.022   3.932   38.887 1.00 11.70  ? 499  TYR A C     1 
ATOM   3524 O O     . TYR A 1 457 ? 9.181   4.216   39.177 1.00 11.49  ? 499  TYR A O     1 
ATOM   3525 C CB    . TYR A 1 457 ? 8.187   2.931   36.611 1.00 11.41  ? 499  TYR A CB    1 
ATOM   3526 C CG    . TYR A 1 457 ? 8.174   4.330   36.014 1.00 11.03  ? 499  TYR A CG    1 
ATOM   3527 C CD1   . TYR A 1 457 ? 7.003   4.944   35.629 1.00 11.12  ? 499  TYR A CD1   1 
ATOM   3528 C CD2   . TYR A 1 457 ? 9.348   5.066   35.928 1.00 9.70   ? 499  TYR A CD2   1 
ATOM   3529 C CE1   . TYR A 1 457 ? 6.987   6.245   35.145 1.00 10.70  ? 499  TYR A CE1   1 
ATOM   3530 C CE2   . TYR A 1 457 ? 9.357   6.343   35.423 1.00 10.65  ? 499  TYR A CE2   1 
ATOM   3531 C CZ    . TYR A 1 457 ? 8.180   6.945   35.040 1.00 10.48  ? 499  TYR A CZ    1 
ATOM   3532 O OH    . TYR A 1 457 ? 8.282   8.243   34.576 1.00 10.90  ? 499  TYR A OH    1 
ATOM   3533 N N     . ARG A 1 458 ? 6.962   4.687   39.215 1.00 11.18  ? 500  ARG A N     1 
ATOM   3534 C CA    . ARG A 1 458 ? 7.004   6.055   39.731 1.00 10.35  ? 500  ARG A CA    1 
ATOM   3535 C C     . ARG A 1 458 ? 5.578   6.360   40.191 1.00 10.77  ? 500  ARG A C     1 
ATOM   3536 O O     . ARG A 1 458 ? 4.596   5.934   39.564 1.00 9.81   ? 500  ARG A O     1 
ATOM   3537 C CB    . ARG A 1 458 ? 7.456   6.987   38.615 1.00 9.33   ? 500  ARG A CB    1 
ATOM   3538 C CG    . ARG A 1 458 ? 7.786   8.438   38.980 1.00 9.14   ? 500  ARG A CG    1 
ATOM   3539 C CD    . ARG A 1 458 ? 8.303   9.122   37.744 1.00 10.00  ? 500  ARG A CD    1 
ATOM   3540 N NE    . ARG A 1 458 ? 8.593   10.526  37.966 1.00 10.66  ? 500  ARG A NE    1 
ATOM   3541 C CZ    . ARG A 1 458 ? 8.906   11.339  36.982 1.00 9.85   ? 500  ARG A CZ    1 
ATOM   3542 N NH1   . ARG A 1 458 ? 8.962   10.890  35.746 1.00 11.70  ? 500  ARG A NH1   1 
ATOM   3543 N NH2   . ARG A 1 458 ? 9.224   12.586  37.241 1.00 10.07  ? 500  ARG A NH2   1 
ATOM   3544 N N     . THR A 1 459 ? 5.444   7.111   41.273 1.00 10.83  ? 501  THR A N     1 
ATOM   3545 C CA    . THR A 1 459 ? 4.131   7.493   41.730 1.00 10.52  ? 501  THR A CA    1 
ATOM   3546 C C     . THR A 1 459 ? 4.155   8.811   42.493 1.00 9.50   ? 501  THR A C     1 
ATOM   3547 O O     . THR A 1 459 ? 5.234   9.388   42.767 1.00 10.07  ? 501  THR A O     1 
ATOM   3548 C CB    . THR A 1 459 ? 3.508   6.385   42.592 1.00 11.04  ? 501  THR A CB    1 
ATOM   3549 O OG1   . THR A 1 459 ? 2.098   6.538   42.441 1.00 11.74  ? 501  THR A OG1   1 
ATOM   3550 C CG2   . THR A 1 459 ? 3.900   6.481   44.048 1.00 11.55  ? 501  THR A CG2   1 
ATOM   3551 N N     . GLY A 1 460 ? 2.952   9.363   42.701 1.00 9.15   ? 502  GLY A N     1 
ATOM   3552 C CA    . GLY A 1 460 ? 2.831   10.637  43.409 1.00 8.83   ? 502  GLY A CA    1 
ATOM   3553 C C     . GLY A 1 460 ? 2.805   10.538  44.923 1.00 10.68  ? 502  GLY A C     1 
ATOM   3554 O O     . GLY A 1 460 ? 2.643   9.447   45.463 1.00 10.45  ? 502  GLY A O     1 
ATOM   3555 N N     . VAL A 1 461 ? 2.977   11.691  45.603 1.00 11.65  ? 503  VAL A N     1 
ATOM   3556 C CA    . VAL A 1 461 ? 3.205   11.670  47.043 1.00 12.43  ? 503  VAL A CA    1 
ATOM   3557 C C     . VAL A 1 461 ? 2.033   11.052  47.782 1.00 15.01  ? 503  VAL A C     1 
ATOM   3558 O O     . VAL A 1 461 ? 2.251   10.467  48.839 1.00 16.21  ? 503  VAL A O     1 
ATOM   3559 C CB    . VAL A 1 461 ? 3.521   13.070  47.635 1.00 12.20  ? 503  VAL A CB    1 
ATOM   3560 C CG1   . VAL A 1 461 ? 4.837   13.609  47.096 1.00 12.21  ? 503  VAL A CG1   1 
ATOM   3561 C CG2   . VAL A 1 461 ? 2.406   14.057  47.355 1.00 13.20  ? 503  VAL A CG2   1 
ATOM   3562 N N     . ASN A 1 462 ? 0.819   11.162  47.230 1.00 13.99  ? 504  ASN A N     1 
ATOM   3563 C CA    . ASN A 1 462 ? -0.377  10.636  47.872 1.00 15.19  ? 504  ASN A CA    1 
ATOM   3564 C C     . ASN A 1 462 ? -0.478  9.115   47.809 1.00 13.86  ? 504  ASN A C     1 
ATOM   3565 O O     . ASN A 1 462 ? -1.334  8.535   48.489 1.00 16.87  ? 504  ASN A O     1 
ATOM   3566 C CB    . ASN A 1 462 ? -1.606  11.321  47.300 1.00 17.68  ? 504  ASN A CB    1 
ATOM   3567 C CG    . ASN A 1 462 ? -1.794  11.041  45.833 1.00 18.92  ? 504  ASN A CG    1 
ATOM   3568 O OD1   . ASN A 1 462 ? -0.876  11.231  45.021 1.00 16.12  ? 504  ASN A OD1   1 
ATOM   3569 N ND2   . ASN A 1 462 ? -2.946  10.514  45.468 1.00 24.10  ? 504  ASN A ND2   1 
ATOM   3570 N N     . SER A 1 463 ? 0.308   8.456   46.951 1.00 11.48  ? 505  SER A N     1 
ATOM   3571 C CA    . SER A 1 463 ? 0.225   7.006   46.781 1.00 11.39  ? 505  SER A CA    1 
ATOM   3572 C C     . SER A 1 463 ? 1.551   6.302   47.099 1.00 10.17  ? 505  SER A C     1 
ATOM   3573 O O     . SER A 1 463 ? 1.662   5.139   46.814 1.00 10.38  ? 505  SER A O     1 
ATOM   3574 C CB    . SER A 1 463 ? -0.305  6.604   45.404 1.00 12.67  ? 505  SER A CB    1 
ATOM   3575 O OG    . SER A 1 463 ? 0.506   7.147   44.346 1.00 14.54  ? 505  SER A OG    1 
ATOM   3576 N N     . MET A 1 464 ? 2.593   7.013   47.547 1.00 11.76  ? 506  MET A N     1 
ATOM   3577 C CA    . MET A 1 464 ? 3.911   6.397   47.669 1.00 11.14  ? 506  MET A CA    1 
ATOM   3578 C C     . MET A 1 464 ? 3.884   5.233   48.666 1.00 12.13  ? 506  MET A C     1 
ATOM   3579 O O     . MET A 1 464 ? 4.594   4.245   48.478 1.00 11.11  ? 506  MET A O     1 
ATOM   3580 C CB    . MET A 1 464 ? 4.921   7.448   48.116 1.00 11.13  ? 506  MET A CB    1 
ATOM   3581 C CG    . MET A 1 464 ? 5.396   8.332   46.982 1.00 10.67  ? 506  MET A CG    1 
ATOM   3582 S SD    . MET A 1 464 ? 6.435   9.727   47.501 1.00 11.31  ? 506  MET A SD    1 
ATOM   3583 C CE    . MET A 1 464 ? 6.657   10.571  45.914 1.00 12.69  ? 506  MET A CE    1 
ATOM   3584 N N     . ASP A 1 465 ? 3.096   5.335   49.748 1.00 12.43  ? 507  ASP A N     1 
ATOM   3585 C CA    . ASP A 1 465 ? 3.009   4.215   50.686 1.00 12.23  ? 507  ASP A CA    1 
ATOM   3586 C C     . ASP A 1 465 ? 2.257   3.030   50.104 1.00 12.12  ? 507  ASP A C     1 
ATOM   3587 O O     . ASP A 1 465 ? 2.691   1.902   50.255 1.00 12.40  ? 507  ASP A O     1 
ATOM   3588 C CB    . ASP A 1 465 ? 2.276   4.577   51.979 1.00 14.87  ? 507  ASP A CB    1 
ATOM   3589 C CG    . ASP A 1 465 ? 3.045   5.451   52.951 1.00 20.75  ? 507  ASP A CG    1 
ATOM   3590 O OD1   . ASP A 1 465 ? 4.251   5.655   52.769 1.00 18.81  ? 507  ASP A OD1   1 
ATOM   3591 O OD2   . ASP A 1 465 ? 2.398   5.953   53.891 1.00 24.10  ? 507  ASP A OD2   1 
ATOM   3592 N N     . LEU A 1 466 ? 1.142   3.274   49.415 1.00 12.13  ? 508  LEU A N     1 
ATOM   3593 C CA    . LEU A 1 466 ? 0.336   2.209   48.825 1.00 11.59  ? 508  LEU A CA    1 
ATOM   3594 C C     . LEU A 1 466 ? 1.102   1.491   47.705 1.00 11.31  ? 508  LEU A C     1 
ATOM   3595 O O     . LEU A 1 466 ? 1.041   0.273   47.575 1.00 12.83  ? 508  LEU A O     1 
ATOM   3596 C CB    . LEU A 1 466 ? -1.001  2.801   48.340 1.00 12.53  ? 508  LEU A CB    1 
ATOM   3597 C CG    . LEU A 1 466 ? -1.974  1.759   47.804 1.00 13.13  ? 508  LEU A CG    1 
ATOM   3598 C CD1   . LEU A 1 466 ? -2.349  0.726   48.859 1.00 16.86  ? 508  LEU A CD1   1 
ATOM   3599 C CD2   . LEU A 1 466 ? -3.203  2.421   47.183 1.00 15.78  ? 508  LEU A CD2   1 
ATOM   3600 N N     . VAL A 1 467 ? 1.869   2.229   46.906 1.00 11.99  ? 509  VAL A N     1 
ATOM   3601 C CA    . VAL A 1 467 ? 2.702   1.585   45.897 1.00 11.73  ? 509  VAL A CA    1 
ATOM   3602 C C     . VAL A 1 467 ? 3.793   0.757   46.581 1.00 10.19  ? 509  VAL A C     1 
ATOM   3603 O O     . VAL A 1 467 ? 4.025   -0.367  46.164 1.00 11.13  ? 509  VAL A O     1 
ATOM   3604 C CB    . VAL A 1 467 ? 3.248   2.597   44.889 1.00 10.93  ? 509  VAL A CB    1 
ATOM   3605 C CG1   . VAL A 1 467 ? 4.289   1.972   44.013 1.00 11.08  ? 509  VAL A CG1   1 
ATOM   3606 C CG2   . VAL A 1 467 ? 2.106   3.124   44.024 1.00 12.31  ? 509  VAL A CG2   1 
ATOM   3607 N N     . ALA A 1 468 ? 4.401   1.271   47.641 1.00 9.61   ? 510  ALA A N     1 
ATOM   3608 C CA    . ALA A 1 468 ? 5.462   0.526   48.313 1.00 11.10  ? 510  ALA A CA    1 
ATOM   3609 C C     . ALA A 1 468 ? 4.879   -0.801  48.782 1.00 11.01  ? 510  ALA A C     1 
ATOM   3610 O O     . ALA A 1 468 ? 5.620   -1.799  48.826 1.00 12.74  ? 510  ALA A O     1 
ATOM   3611 C CB    . ALA A 1 468 ? 6.042   1.344   49.426 1.00 10.68  ? 510  ALA A CB    1 
ATOM   3612 N N     . GLN A 1 469 ? 3.612   -0.786  49.217 1.00 13.12  ? 511  GLN A N     1 
ATOM   3613 C CA    . GLN A 1 469 ? 2.969   -1.997  49.752 1.00 14.32  ? 511  GLN A CA    1 
ATOM   3614 C C     . GLN A 1 469 ? 2.822   -3.075  48.700 1.00 13.91  ? 511  GLN A C     1 
ATOM   3615 O O     . GLN A 1 469 ? 2.591   -4.218  49.075 1.00 14.77  ? 511  GLN A O     1 
ATOM   3616 C CB    . GLN A 1 469 ? 1.609   -1.663  50.357 1.00 14.67  ? 511  GLN A CB    1 
ATOM   3617 C CG    . GLN A 1 469 ? 1.740   -0.879  51.664 1.00 18.59  ? 511  GLN A CG    1 
ATOM   3618 C CD    . GLN A 1 469 ? 0.385   -0.348  52.113 1.00 24.95  ? 511  GLN A CD    1 
ATOM   3619 O OE1   . GLN A 1 469 ? -0.629  -1.035  52.075 1.00 36.32  ? 511  GLN A OE1   1 
ATOM   3620 N NE2   . GLN A 1 469 ? 0.326   0.915   52.480 1.00 31.58  ? 511  GLN A NE2   1 
ATOM   3621 N N     . GLN A 1 470 ? 2.845   -2.749  47.390 1.00 11.64  ? 512  GLN A N     1 
ATOM   3622 C CA    . GLN A 1 470 ? 2.762   -3.715  46.302 1.00 11.02  ? 512  GLN A CA    1 
ATOM   3623 C C     . GLN A 1 470 ? 4.065   -4.528  46.222 1.00 11.81  ? 512  GLN A C     1 
ATOM   3624 O O     . GLN A 1 470 ? 4.046   -5.668  45.735 1.00 13.13  ? 512  GLN A O     1 
ATOM   3625 C CB    . GLN A 1 470 ? 2.422   -3.090  44.967 1.00 12.70  ? 512  GLN A CB    1 
ATOM   3626 C CG    . GLN A 1 470 ? 1.185   -2.198  45.002 1.00 12.64  ? 512  GLN A CG    1 
ATOM   3627 C CD    . GLN A 1 470 ? 0.024   -2.825  45.749 1.00 13.01  ? 512  GLN A CD    1 
ATOM   3628 O OE1   . GLN A 1 470 ? -0.378  -3.936  45.415 1.00 14.20  ? 512  GLN A OE1   1 
ATOM   3629 N NE2   . GLN A 1 470 ? -0.499  -2.161  46.767 1.00 13.58  ? 512  GLN A NE2   1 
ATOM   3630 N N     . TYR A 1 471 ? 5.204   -3.942  46.612 1.00 12.20  ? 513  TYR A N     1 
ATOM   3631 C CA    . TYR A 1 471 ? 6.506   -4.575  46.479 1.00 12.15  ? 513  TYR A CA    1 
ATOM   3632 C C     . TYR A 1 471 ? 6.777   -5.341  47.788 1.00 12.75  ? 513  TYR A C     1 
ATOM   3633 O O     . TYR A 1 471 ? 5.946   -5.244  48.705 1.00 13.30  ? 513  TYR A O     1 
ATOM   3634 C CB    . TYR A 1 471 ? 7.569   -3.499  46.178 1.00 12.52  ? 513  TYR A CB    1 
ATOM   3635 C CG    . TYR A 1 471 ? 7.483   -2.895  44.812 1.00 11.68  ? 513  TYR A CG    1 
ATOM   3636 C CD1   . TYR A 1 471 ? 6.690   -1.765  44.555 1.00 11.57  ? 513  TYR A CD1   1 
ATOM   3637 C CD2   . TYR A 1 471 ? 8.212   -3.426  43.772 1.00 11.66  ? 513  TYR A CD2   1 
ATOM   3638 C CE1   . TYR A 1 471 ? 6.618   -1.252  43.275 1.00 11.45  ? 513  TYR A CE1   1 
ATOM   3639 C CE2   . TYR A 1 471 ? 8.139   -2.925  42.483 1.00 12.10  ? 513  TYR A CE2   1 
ATOM   3640 C CZ    . TYR A 1 471 ? 7.354   -1.812  42.252 1.00 12.20  ? 513  TYR A CZ    1 
ATOM   3641 O OH    . TYR A 1 471 ? 7.343   -1.364  40.965 1.00 12.75  ? 513  TYR A OH    1 
ATOM   3642 N N     . GLY A 1 472 ? 7.905   -6.078  47.884 1.00 12.55  ? 514  GLY A N     1 
ATOM   3643 C CA    . GLY A 1 472 ? 8.123   -7.036  48.969 1.00 12.09  ? 514  GLY A CA    1 
ATOM   3644 C C     . GLY A 1 472 ? 8.279   -6.372  50.335 1.00 14.00  ? 514  GLY A C     1 
ATOM   3645 O O     . GLY A 1 472 ? 8.827   -5.274  50.480 1.00 12.32  ? 514  GLY A O     1 
ATOM   3646 N N     . GLU A 1 473 ? 7.859   -7.095  51.367 1.00 13.36  ? 515  GLU A N     1 
ATOM   3647 C CA    . GLU A 1 473 ? 8.089   -6.651  52.740 1.00 15.28  ? 515  GLU A CA    1 
ATOM   3648 C C     . GLU A 1 473 ? 9.577   -6.600  53.077 1.00 13.21  ? 515  GLU A C     1 
ATOM   3649 O O     . GLU A 1 473 ? 9.992   -5.690  53.799 1.00 12.20  ? 515  GLU A O     1 
ATOM   3650 C CB    . GLU A 1 473 ? 7.414   -7.583  53.749 1.00 21.17  ? 515  GLU A CB    1 
ATOM   3651 C CG    . GLU A 1 473 ? 5.908   -7.542  53.670 1.00 33.05  ? 515  GLU A CG    1 
ATOM   3652 C CD    . GLU A 1 473 ? 5.211   -8.148  54.877 1.00 45.75  ? 515  GLU A CD    1 
ATOM   3653 O OE1   . GLU A 1 473 ? 5.902   -8.820  55.686 1.00 51.10  ? 515  GLU A OE1   1 
ATOM   3654 O OE2   . GLU A 1 473 ? 3.996   -7.903  55.026 1.00 57.84  ? 515  GLU A OE2   1 
ATOM   3655 N N     . VAL A 1 474 ? 10.392  -7.552  52.578 1.00 10.53  ? 516  VAL A N     1 
ATOM   3656 C CA    . VAL A 1 474 ? 11.817  -7.502  52.840 1.00 11.94  ? 516  VAL A CA    1 
ATOM   3657 C C     . VAL A 1 474 ? 12.418  -6.238  52.219 1.00 11.68  ? 516  VAL A C     1 
ATOM   3658 O O     . VAL A 1 474 ? 13.258  -5.627  52.849 1.00 12.25  ? 516  VAL A O     1 
ATOM   3659 C CB    . VAL A 1 474 ? 12.563  -8.752  52.326 1.00 13.71  ? 516  VAL A CB    1 
ATOM   3660 C CG1   . VAL A 1 474 ? 14.058  -8.695  52.541 1.00 13.68  ? 516  VAL A CG1   1 
ATOM   3661 C CG2   . VAL A 1 474 ? 12.061  -10.010 53.040 1.00 15.45  ? 516  VAL A CG2   1 
ATOM   3662 N N     . ASN A 1 475 ? 11.945  -5.852  51.019 1.00 10.56  ? 517  ASN A N     1 
ATOM   3663 C CA    . ASN A 1 475 ? 12.445  -4.655  50.367 1.00 10.66  ? 517  ASN A CA    1 
ATOM   3664 C C     . ASN A 1 475 ? 12.157  -3.432  51.231 1.00 11.02  ? 517  ASN A C     1 
ATOM   3665 O O     . ASN A 1 475 ? 12.994  -2.533  51.419 1.00 11.62  ? 517  ASN A O     1 
ATOM   3666 C CB    . ASN A 1 475 ? 11.854  -4.494  48.973 1.00 10.55  ? 517  ASN A CB    1 
ATOM   3667 C CG    . ASN A 1 475 ? 12.164  -5.633  48.035 1.00 11.38  ? 517  ASN A CG    1 
ATOM   3668 O OD1   . ASN A 1 475 ? 12.937  -5.483  47.044 1.00 14.54  ? 517  ASN A OD1   1 
ATOM   3669 N ND2   . ASN A 1 475 ? 11.606  -6.769  48.361 1.00 8.60   ? 517  ASN A ND2   1 
ATOM   3670 N N     . ARG A 1 476 ? 10.914  -3.386  51.744 1.00 11.67  ? 518  ARG A N     1 
ATOM   3671 C CA    . ARG A 1 476 ? 10.497  -2.267  52.593 1.00 12.15  ? 518  ARG A CA    1 
ATOM   3672 C C     . ARG A 1 476 ? 11.409  -2.196  53.818 1.00 11.94  ? 518  ARG A C     1 
ATOM   3673 O O     . ARG A 1 476 ? 11.907  -1.123  54.198 1.00 11.23  ? 518  ARG A O     1 
ATOM   3674 C CB    . ARG A 1 476 ? 9.019   -2.453  52.971 1.00 14.72  ? 518  ARG A CB    1 
ATOM   3675 C CG    . ARG A 1 476 ? 8.260   -1.249  53.482 1.00 16.59  ? 518  ARG A CG    1 
ATOM   3676 C CD    . ARG A 1 476 ? 7.651   -0.479  52.319 1.00 19.44  ? 518  ARG A CD    1 
ATOM   3677 N NE    . ARG A 1 476 ? 7.135   0.815   52.792 1.00 21.40  ? 518  ARG A NE    1 
ATOM   3678 C CZ    . ARG A 1 476 ? 5.872   1.066   53.130 1.00 20.76  ? 518  ARG A CZ    1 
ATOM   3679 N NH1   . ARG A 1 476 ? 4.929   0.120   53.094 1.00 23.28  ? 518  ARG A NH1   1 
ATOM   3680 N NH2   . ARG A 1 476 ? 5.539   2.288   53.474 1.00 19.92  ? 518  ARG A NH2   1 
ATOM   3681 N N     . ASP A 1 477 ? 11.660  -3.344  54.448 1.00 12.33  ? 519  ASP A N     1 
ATOM   3682 C CA    . ASP A 1 477 ? 12.521  -3.356  55.630 1.00 14.42  ? 519  ASP A CA    1 
ATOM   3683 C C     . ASP A 1 477 ? 13.958  -2.943  55.328 1.00 13.29  ? 519  ASP A C     1 
ATOM   3684 O O     . ASP A 1 477 ? 14.609  -2.211  56.079 1.00 13.66  ? 519  ASP A O     1 
ATOM   3685 C CB    . ASP A 1 477 ? 12.582  -4.759  56.256 1.00 14.99  ? 519  ASP A CB    1 
ATOM   3686 C CG    . ASP A 1 477 ? 11.312  -5.209  56.952 1.00 24.05  ? 519  ASP A CG    1 
ATOM   3687 O OD1   . ASP A 1 477 ? 10.447  -4.355  57.184 1.00 24.52  ? 519  ASP A OD1   1 
ATOM   3688 O OD2   . ASP A 1 477 ? 11.183  -6.456  57.211 1.00 26.83  ? 519  ASP A OD2   1 
ATOM   3689 N N     . PHE A 1 478 ? 14.509  -3.454  54.211 1.00 11.82  ? 520  PHE A N     1 
ATOM   3690 C CA    . PHE A 1 478 ? 15.859  -3.129  53.830 1.00 11.03  ? 520  PHE A CA    1 
ATOM   3691 C C     . PHE A 1 478 ? 16.004  -1.619  53.545 1.00 12.27  ? 520  PHE A C     1 
ATOM   3692 O O     . PHE A 1 478 ? 16.955  -0.992  53.989 1.00 11.86  ? 520  PHE A O     1 
ATOM   3693 C CB    . PHE A 1 478 ? 16.230  -3.943  52.573 1.00 12.59  ? 520  PHE A CB    1 
ATOM   3694 C CG    . PHE A 1 478 ? 17.670  -3.836  52.175 1.00 13.06  ? 520  PHE A CG    1 
ATOM   3695 C CD1   . PHE A 1 478 ? 18.632  -4.562  52.852 1.00 15.16  ? 520  PHE A CD1   1 
ATOM   3696 C CD2   . PHE A 1 478 ? 18.088  -2.996  51.172 1.00 13.93  ? 520  PHE A CD2   1 
ATOM   3697 C CE1   . PHE A 1 478 ? 19.958  -4.500  52.450 1.00 14.67  ? 520  PHE A CE1   1 
ATOM   3698 C CE2   . PHE A 1 478 ? 19.418  -2.923  50.785 1.00 15.83  ? 520  PHE A CE2   1 
ATOM   3699 C CZ    . PHE A 1 478 ? 20.347  -3.684  51.448 1.00 13.05  ? 520  PHE A CZ    1 
ATOM   3700 N N     . ASN A 1 479 ? 15.032  -1.013  52.853 1.00 10.97  ? 521  ASN A N     1 
ATOM   3701 C CA    . ASN A 1 479 ? 15.071  0.423   52.609 1.00 11.43  ? 521  ASN A CA    1 
ATOM   3702 C C     . ASN A 1 479 ? 15.069  1.176   53.946 1.00 11.56  ? 521  ASN A C     1 
ATOM   3703 O O     . ASN A 1 479 ? 15.715  2.230   54.067 1.00 11.99  ? 521  ASN A O     1 
ATOM   3704 C CB    . ASN A 1 479 ? 13.932  0.842   51.687 1.00 12.53  ? 521  ASN A CB    1 
ATOM   3705 C CG    . ASN A 1 479 ? 14.208  0.548   50.235 1.00 15.28  ? 521  ASN A CG    1 
ATOM   3706 O OD1   . ASN A 1 479 ? 15.344  0.501   49.811 1.00 19.96  ? 521  ASN A OD1   1 
ATOM   3707 N ND2   . ASN A 1 479 ? 13.168  0.435   49.442 1.00 18.39  ? 521  ASN A ND2   1 
ATOM   3708 N N     . ARG A 1 480 ? 14.310  0.684   54.924 1.00 11.66  ? 522  ARG A N     1 
ATOM   3709 C CA    . ARG A 1 480 ? 14.227  1.362   56.206 1.00 13.45  ? 522  ARG A CA    1 
ATOM   3710 C C     . ARG A 1 480 ? 15.539  1.198   56.958 1.00 12.75  ? 522  ARG A C     1 
ATOM   3711 O O     . ARG A 1 480 ? 15.966  2.120   57.640 1.00 14.31  ? 522  ARG A O     1 
ATOM   3712 C CB    . ARG A 1 480 ? 13.009  0.887   57.006 1.00 17.12  ? 522  ARG A CB    1 
ATOM   3713 C CG    . ARG A 1 480 ? 12.678  1.728   58.226 1.00 24.81  ? 522  ARG A CG    1 
ATOM   3714 C CD    . ARG A 1 480 ? 11.319  1.318   58.769 1.00 27.52  ? 522  ARG A CD    1 
ATOM   3715 N NE    . ARG A 1 480 ? 10.643  2.489   59.337 1.00 38.51  ? 522  ARG A NE    1 
ATOM   3716 C CZ    . ARG A 1 480 ? 9.544   2.440   60.096 1.00 39.29  ? 522  ARG A CZ    1 
ATOM   3717 N NH1   . ARG A 1 480 ? 9.054   1.270   60.484 1.00 42.00  ? 522  ARG A NH1   1 
ATOM   3718 N NH2   . ARG A 1 480 ? 8.957   3.559   60.489 1.00 34.43  ? 522  ARG A NH2   1 
ATOM   3719 N N     . THR A 1 481 ? 16.193  0.038   56.852 1.00 12.85  ? 523  THR A N     1 
ATOM   3720 C CA    . THR A 1 481 ? 17.493  -0.129  57.485 1.00 12.90  ? 523  THR A CA    1 
ATOM   3721 C C     . THR A 1 481 ? 18.469  0.890   56.909 1.00 12.30  ? 523  THR A C     1 
ATOM   3722 O O     . THR A 1 481 ? 19.199  1.524   57.674 1.00 13.93  ? 523  THR A O     1 
ATOM   3723 C CB    . THR A 1 481 ? 18.061  -1.544  57.287 1.00 16.74  ? 523  THR A CB    1 
ATOM   3724 O OG1   . THR A 1 481 ? 17.132  -2.409  57.942 1.00 17.93  ? 523  THR A OG1   1 
ATOM   3725 C CG2   . THR A 1 481 ? 19.475  -1.708  57.813 1.00 18.03  ? 523  THR A CG2   1 
ATOM   3726 N N     . LEU A 1 482 ? 18.503  1.037   55.579 1.00 12.03  ? 524  LEU A N     1 
ATOM   3727 C CA    . LEU A 1 482 ? 19.386  1.991   54.924 1.00 12.64  ? 524  LEU A CA    1 
ATOM   3728 C C     . LEU A 1 482 ? 19.051  3.410   55.396 1.00 12.22  ? 524  LEU A C     1 
ATOM   3729 O O     . LEU A 1 482 ? 19.977  4.188   55.676 1.00 12.20  ? 524  LEU A O     1 
ATOM   3730 C CB    . LEU A 1 482 ? 19.262  1.942   53.404 1.00 15.17  ? 524  LEU A CB    1 
ATOM   3731 C CG    . LEU A 1 482 ? 19.719  0.668   52.676 1.00 18.32  ? 524  LEU A CG    1 
ATOM   3732 C CD1   . LEU A 1 482 ? 19.412  0.750   51.175 1.00 18.72  ? 524  LEU A CD1   1 
ATOM   3733 C CD2   . LEU A 1 482 ? 21.192  0.353   52.948 1.00 22.22  ? 524  LEU A CD2   1 
ATOM   3734 N N     . LYS A 1 483 ? 17.742  3.752   55.429 1.00 11.11  ? 525  LYS A N     1 
ATOM   3735 C CA    . LYS A 1 483 ? 17.337  5.114   55.802 1.00 11.65  ? 525  LYS A CA    1 
ATOM   3736 C C     . LYS A 1 483 ? 17.882  5.476   57.190 1.00 11.75  ? 525  LYS A C     1 
ATOM   3737 O O     . LYS A 1 483 ? 18.312  6.592   57.501 1.00 11.80  ? 525  LYS A O     1 
ATOM   3738 C CB    . LYS A 1 483 ? 15.800  5.189   55.780 1.00 12.83  ? 525  LYS A CB    1 
ATOM   3739 C CG    . LYS A 1 483 ? 15.201  6.521   56.235 1.00 12.87  ? 525  LYS A CG    1 
ATOM   3740 C CD    . LYS A 1 483 ? 15.713  7.657   55.401 1.00 12.24  ? 525  LYS A CD    1 
ATOM   3741 C CE    . LYS A 1 483 ? 14.976  8.928   55.714 1.00 12.99  ? 525  LYS A CE    1 
ATOM   3742 N NZ    . LYS A 1 483 ? 15.487  10.057  54.894 1.00 13.93  ? 525  LYS A NZ    1 
ATOM   3743 N N     . ARG A 1 484 ? 17.668  4.556   58.128 1.00 13.47  ? 526  ARG A N     1 
ATOM   3744 C CA    . ARG A 1 484 ? 18.029  4.796   59.518 1.00 14.20  ? 526  ARG A CA    1 
ATOM   3745 C C     . ARG A 1 484 ? 19.527  4.899   59.699 1.00 15.06  ? 526  ARG A C     1 
ATOM   3746 O O     . ARG A 1 484 ? 19.985  5.697   60.547 1.00 15.67  ? 526  ARG A O     1 
ATOM   3747 C CB    . ARG A 1 484 ? 17.455  3.734   60.435 1.00 17.00  ? 526  ARG A CB    1 
ATOM   3748 C CG    . ARG A 1 484 ? 15.984  3.965   60.730 1.00 20.03  ? 526  ARG A CG    1 
ATOM   3749 C CD    . ARG A 1 484 ? 15.321  2.849   61.494 1.00 26.43  ? 526  ARG A CD    1 
ATOM   3750 N NE    . ARG A 1 484 ? 13.915  3.212   61.586 1.00 30.45  ? 526  ARG A NE    1 
ATOM   3751 C CZ    . ARG A 1 484 ? 12.960  2.455   62.127 1.00 38.73  ? 526  ARG A CZ    1 
ATOM   3752 N NH1   . ARG A 1 484 ? 13.111  1.145   62.207 1.00 40.79  ? 526  ARG A NH1   1 
ATOM   3753 N NH2   . ARG A 1 484 ? 11.811  3.006   62.478 1.00 35.02  ? 526  ARG A NH2   1 
ATOM   3754 N N     . ALA A 1 485 ? 20.289  4.212   58.842 1.00 13.54  ? 527  ALA A N     1 
ATOM   3755 C CA    . ALA A 1 485 ? 21.735  4.251   58.965 1.00 14.64  ? 527  ALA A CA    1 
ATOM   3756 C C     . ALA A 1 485 ? 22.296  5.521   58.333 1.00 13.26  ? 527  ALA A C     1 
ATOM   3757 O O     . ALA A 1 485 ? 23.254  6.072   58.853 1.00 15.43  ? 527  ALA A O     1 
ATOM   3758 C CB    . ALA A 1 485 ? 22.352  3.041   58.326 1.00 14.17  ? 527  ALA A CB    1 
ATOM   3759 N N     . ILE A 1 486 ? 21.746  5.922   57.170 1.00 11.97  ? 528  ILE A N     1 
ATOM   3760 C CA    . ILE A 1 486 ? 22.235  7.046   56.395 1.00 12.35  ? 528  ILE A CA    1 
ATOM   3761 C C     . ILE A 1 486 ? 21.749  8.379   56.957 1.00 12.95  ? 528  ILE A C     1 
ATOM   3762 O O     . ILE A 1 486 ? 22.531  9.363   56.975 1.00 11.39  ? 528  ILE A O     1 
ATOM   3763 C CB    . ILE A 1 486 ? 21.851  6.856   54.906 1.00 12.42  ? 528  ILE A CB    1 
ATOM   3764 C CG1   . ILE A 1 486 ? 22.498  5.619   54.312 1.00 14.46  ? 528  ILE A CG1   1 
ATOM   3765 C CG2   . ILE A 1 486 ? 22.280  8.054   54.115 1.00 13.35  ? 528  ILE A CG2   1 
ATOM   3766 C CD1   . ILE A 1 486 ? 21.903  5.180   52.977 1.00 15.43  ? 528  ILE A CD1   1 
ATOM   3767 N N     . ASP A 1 487 ? 20.490  8.383   57.461 1.00 10.39  ? 529  ASP A N     1 
ATOM   3768 C CA    . ASP A 1 487 ? 19.834  9.596   57.941 1.00 11.33  ? 529  ASP A CA    1 
ATOM   3769 C C     . ASP A 1 487 ? 19.245  9.363   59.323 1.00 10.88  ? 529  ASP A C     1 
ATOM   3770 O O     . ASP A 1 487 ? 18.020  9.211   59.494 1.00 10.93  ? 529  ASP A O     1 
ATOM   3771 C CB    . ASP A 1 487 ? 18.754  10.033  56.969 1.00 10.72  ? 529  ASP A CB    1 
ATOM   3772 C CG    . ASP A 1 487 ? 17.989  11.299  57.280 1.00 11.13  ? 529  ASP A CG    1 
ATOM   3773 O OD1   . ASP A 1 487 ? 18.431  12.102  58.182 1.00 11.83  ? 529  ASP A OD1   1 
ATOM   3774 O OD2   . ASP A 1 487 ? 16.974  11.515  56.585 1.00 10.19  ? 529  ASP A OD2   1 
ATOM   3775 N N     . PRO A 1 488 ? 20.097  9.359   60.361 1.00 12.36  ? 530  PRO A N     1 
ATOM   3776 C CA    . PRO A 1 488 ? 19.612  8.928   61.665 1.00 14.00  ? 530  PRO A CA    1 
ATOM   3777 C C     . PRO A 1 488 ? 18.536  9.811   62.237 1.00 14.03  ? 530  PRO A C     1 
ATOM   3778 O O     . PRO A 1 488 ? 17.748  9.327   63.059 1.00 15.07  ? 530  PRO A O     1 
ATOM   3779 C CB    . PRO A 1 488 ? 20.854  8.905   62.578 1.00 14.88  ? 530  PRO A CB    1 
ATOM   3780 C CG    . PRO A 1 488 ? 22.014  9.046   61.683 1.00 18.03  ? 530  PRO A CG    1 
ATOM   3781 C CD    . PRO A 1 488 ? 21.544  9.511   60.319 1.00 13.59  ? 530  PRO A CD    1 
ATOM   3782 N N     . ASN A 1 489 ? 18.557  11.118  61.919 1.00 13.06  ? 531  ASN A N     1 
ATOM   3783 C CA    . ASN A 1 489 ? 17.551  12.018  62.445 1.00 11.72  ? 531  ASN A CA    1 
ATOM   3784 C C     . ASN A 1 489 ? 16.290  12.062  61.576 1.00 11.75  ? 531  ASN A C     1 
ATOM   3785 O O     . ASN A 1 489 ? 15.343  12.777  61.892 1.00 14.17  ? 531  ASN A O     1 
ATOM   3786 C CB    . ASN A 1 489 ? 18.113  13.416  62.643 1.00 13.62  ? 531  ASN A CB    1 
ATOM   3787 C CG    . ASN A 1 489 ? 19.175  13.466  63.712 1.00 12.30  ? 531  ASN A CG    1 
ATOM   3788 O OD1   . ASN A 1 489 ? 20.218  14.144  63.607 1.00 13.88  ? 531  ASN A OD1   1 
ATOM   3789 N ND2   . ASN A 1 489 ? 18.808  12.822  64.780 1.00 12.24  ? 531  ASN A ND2   1 
ATOM   3790 N N     . GLY A 1 490 ? 16.287  11.391  60.407 1.00 11.51  ? 532  GLY A N     1 
ATOM   3791 C CA    . GLY A 1 490 ? 15.149  11.386  59.521 1.00 12.02  ? 532  GLY A CA    1 
ATOM   3792 C C     . GLY A 1 490 ? 14.755  12.776  59.001 1.00 12.00  ? 532  GLY A C     1 
ATOM   3793 O O     . GLY A 1 490 ? 13.544  13.095  58.855 1.00 14.09  ? 532  GLY A O     1 
ATOM   3794 N N     . ILE A 1 491 ? 15.782  13.550  58.636 1.00 11.64  ? 533  ILE A N     1 
ATOM   3795 C CA    . ILE A 1 491 ? 15.475  14.909  58.213 1.00 12.11  ? 533  ILE A CA    1 
ATOM   3796 C C     . ILE A 1 491 ? 15.417  15.067  56.680 1.00 12.63  ? 533  ILE A C     1 
ATOM   3797 O O     . ILE A 1 491 ? 15.209  16.181  56.223 1.00 12.71  ? 533  ILE A O     1 
ATOM   3798 C CB    . ILE A 1 491 ? 16.352  15.953  58.930 1.00 13.64  ? 533  ILE A CB    1 
ATOM   3799 C CG1   . ILE A 1 491 ? 17.840  15.630  58.932 1.00 14.72  ? 533  ILE A CG1   1 
ATOM   3800 C CG2   . ILE A 1 491 ? 15.850  16.125  60.367 1.00 14.11  ? 533  ILE A CG2   1 
ATOM   3801 C CD1   . ILE A 1 491 ? 18.464  15.686  57.585 1.00 15.05  ? 533  ILE A CD1   1 
ATOM   3802 N N     . LEU A 1 492 ? 15.683  14.031  55.875 1.00 10.65  ? 534  LEU A N     1 
ATOM   3803 C CA    . LEU A 1 492 ? 15.518  14.143  54.423 1.00 9.86   ? 534  LEU A CA    1 
ATOM   3804 C C     . LEU A 1 492 ? 14.245  13.445  53.955 1.00 10.50  ? 534  LEU A C     1 
ATOM   3805 O O     . LEU A 1 492 ? 14.040  12.218  54.096 1.00 13.09  ? 534  LEU A O     1 
ATOM   3806 C CB    . LEU A 1 492 ? 16.691  13.569  53.631 1.00 11.22  ? 534  LEU A CB    1 
ATOM   3807 C CG    . LEU A 1 492 ? 18.052  14.232  53.845 1.00 11.37  ? 534  LEU A CG    1 
ATOM   3808 C CD1   . LEU A 1 492 ? 19.035  13.721  52.764 1.00 12.89  ? 534  LEU A CD1   1 
ATOM   3809 C CD2   . LEU A 1 492 ? 17.963  15.755  53.852 1.00 11.23  ? 534  LEU A CD2   1 
ATOM   3810 N N     . SER A 1 493 ? 13.344  14.241  53.413 1.00 10.74  ? 535  SER A N     1 
ATOM   3811 C CA    . SER A 1 493 ? 12.153  13.789  52.679 1.00 9.87   ? 535  SER A CA    1 
ATOM   3812 C C     . SER A 1 493 ? 11.494  12.550  53.258 1.00 10.83  ? 535  SER A C     1 
ATOM   3813 O O     . SER A 1 493 ? 11.241  11.570  52.563 1.00 9.82   ? 535  SER A O     1 
ATOM   3814 C CB    . SER A 1 493 ? 12.440  13.581  51.225 1.00 10.83  ? 535  SER A CB    1 
ATOM   3815 O OG    . SER A 1 493 ? 12.821  14.844  50.605 1.00 12.30  ? 535  SER A OG    1 
ATOM   3816 N N     . PRO A 1 494 ? 11.085  12.568  54.542 1.00 10.84  ? 536  PRO A N     1 
ATOM   3817 C CA    . PRO A 1 494 ? 10.364  11.418  55.070 1.00 13.34  ? 536  PRO A CA    1 
ATOM   3818 C C     . PRO A 1 494 ? 9.137   11.067  54.217 1.00 11.40  ? 536  PRO A C     1 
ATOM   3819 O O     . PRO A 1 494 ? 8.408   11.936  53.732 1.00 13.16  ? 536  PRO A O     1 
ATOM   3820 C CB    . PRO A 1 494 ? 9.973   11.836  56.500 1.00 14.93  ? 536  PRO A CB    1 
ATOM   3821 C CG    . PRO A 1 494 ? 10.529  13.184  56.755 1.00 14.76  ? 536  PRO A CG    1 
ATOM   3822 C CD    . PRO A 1 494 ? 11.239  13.661  55.512 1.00 14.18  ? 536  PRO A CD    1 
ATOM   3823 N N     . GLY A 1 495 ? 8.907   9.756   54.039 1.00 11.25  ? 537  GLY A N     1 
ATOM   3824 C CA    . GLY A 1 495 ? 7.822   9.220   53.243 1.00 11.53  ? 537  GLY A CA    1 
ATOM   3825 C C     . GLY A 1 495 ? 8.097   9.119   51.747 1.00 11.22  ? 537  GLY A C     1 
ATOM   3826 O O     . GLY A 1 495 ? 7.303   8.481   51.049 1.00 11.62  ? 537  GLY A O     1 
ATOM   3827 N N     . LYS A 1 496 ? 9.180   9.696   51.244 1.00 9.72   ? 538  LYS A N     1 
ATOM   3828 C CA    . LYS A 1 496 ? 9.515   9.528   49.846 1.00 10.05  ? 538  LYS A CA    1 
ATOM   3829 C C     . LYS A 1 496 ? 9.618   8.018   49.563 1.00 10.10  ? 538  LYS A C     1 
ATOM   3830 O O     . LYS A 1 496 ? 10.294  7.315   50.279 1.00 10.11  ? 538  LYS A O     1 
ATOM   3831 C CB    . LYS A 1 496 ? 10.818  10.225  49.468 1.00 10.88  ? 538  LYS A CB    1 
ATOM   3832 C CG    . LYS A 1 496 ? 11.360  9.939   48.066 1.00 11.65  ? 538  LYS A CG    1 
ATOM   3833 C CD    . LYS A 1 496 ? 10.442  10.462  46.954 1.00 11.53  ? 538  LYS A CD    1 
ATOM   3834 C CE    . LYS A 1 496 ? 11.080  10.279  45.576 1.00 12.53  ? 538  LYS A CE    1 
ATOM   3835 N NZ    . LYS A 1 496 ? 10.112  10.488  44.445 1.00 12.04  ? 538  LYS A NZ    1 
ATOM   3836 N N     . SER A 1 497 ? 8.951   7.541   48.506 1.00 9.83   ? 539  SER A N     1 
ATOM   3837 C CA    . SER A 1 497 ? 8.971   6.117   48.099 1.00 9.64   ? 539  SER A CA    1 
ATOM   3838 C C     . SER A 1 497 ? 8.482   5.186   49.209 1.00 9.81   ? 539  SER A C     1 
ATOM   3839 O O     . SER A 1 497 ? 8.819   4.016   49.242 1.00 10.88  ? 539  SER A O     1 
ATOM   3840 C CB    . SER A 1 497 ? 10.324  5.680   47.579 1.00 10.19  ? 539  SER A CB    1 
ATOM   3841 O OG    . SER A 1 497 ? 10.674  6.475   46.446 1.00 10.83  ? 539  SER A OG    1 
ATOM   3842 N N     . GLY A 1 498 ? 7.663   5.710   50.125 1.00 10.24  ? 540  GLY A N     1 
ATOM   3843 C CA    . GLY A 1 498 ? 7.166   4.957   51.260 1.00 10.86  ? 540  GLY A CA    1 
ATOM   3844 C C     . GLY A 1 498 ? 8.217   4.614   52.305 1.00 12.41  ? 540  GLY A C     1 
ATOM   3845 O O     . GLY A 1 498 ? 7.934   3.763   53.155 1.00 11.50  ? 540  GLY A O     1 
ATOM   3846 N N     . ILE A 1 499 ? 9.331   5.346   52.289 1.00 11.17  ? 541  ILE A N     1 
ATOM   3847 C CA    . ILE A 1 499 ? 10.420  5.177   53.265 1.00 10.96  ? 541  ILE A CA    1 
ATOM   3848 C C     . ILE A 1 499 ? 10.296  6.169   54.424 1.00 11.88  ? 541  ILE A C     1 
ATOM   3849 O O     . ILE A 1 499 ? 10.573  7.368   54.284 1.00 11.55  ? 541  ILE A O     1 
ATOM   3850 C CB    . ILE A 1 499 ? 11.774  5.358   52.573 1.00 11.88  ? 541  ILE A CB    1 
ATOM   3851 C CG1   . ILE A 1 499 ? 11.927  4.390   51.396 1.00 11.04  ? 541  ILE A CG1   1 
ATOM   3852 C CG2   . ILE A 1 499 ? 12.910  5.140   53.567 1.00 13.82  ? 541  ILE A CG2   1 
ATOM   3853 C CD1   . ILE A 1 499 ? 13.146  4.630   50.530 1.00 11.78  ? 541  ILE A CD1   1 
ATOM   3854 N N     . HIS A 1 500 ? 10.044  5.646   55.587 1.00 12.95  ? 542  HIS A N     1 
ATOM   3855 C CA    . HIS A 1 500 ? 9.817   6.453   56.764 1.00 13.62  ? 542  HIS A CA    1 
ATOM   3856 C C     . HIS A 1 500 ? 10.905  6.183   57.810 1.00 16.86  ? 542  HIS A C     1 
ATOM   3857 O O     . HIS A 1 500 ? 11.237  5.029   58.091 1.00 18.82  ? 542  HIS A O     1 
ATOM   3858 C CB    . HIS A 1 500 ? 8.456   6.035   57.324 1.00 15.72  ? 542  HIS A CB    1 
ATOM   3859 C CG    . HIS A 1 500 ? 7.289   6.511   56.509 1.00 15.05  ? 542  HIS A CG    1 
ATOM   3860 N ND1   . HIS A 1 500 ? 6.596   5.709   55.610 1.00 20.61  ? 542  HIS A ND1   1 
ATOM   3861 C CD2   . HIS A 1 500 ? 6.677   7.727   56.511 1.00 13.68  ? 542  HIS A CD2   1 
ATOM   3862 C CE1   . HIS A 1 500 ? 5.627   6.439   55.084 1.00 16.05  ? 542  HIS A CE1   1 
ATOM   3863 N NE2   . HIS A 1 500 ? 5.653   7.654   55.638 1.00 18.02  ? 542  HIS A NE2   1 
ATOM   3864 N N     . PRO A 1 501 ? 11.414  7.235   58.475 1.00 19.38  ? 543  PRO A N     1 
ATOM   3865 C CA    . PRO A 1 501 ? 12.291  7.076   59.645 1.00 22.04  ? 543  PRO A CA    1 
ATOM   3866 C C     . PRO A 1 501 ? 11.602  6.240   60.723 1.00 24.23  ? 543  PRO A C     1 
ATOM   3867 O O     . PRO A 1 501 ? 10.377  6.319   60.791 1.00 27.74  ? 543  PRO A O     1 
ATOM   3868 C CB    . PRO A 1 501 ? 12.440  8.489   60.225 1.00 24.70  ? 543  PRO A CB    1 
ATOM   3869 C CG    . PRO A 1 501 ? 12.101  9.403   59.079 1.00 27.50  ? 543  PRO A CG    1 
ATOM   3870 C CD    . PRO A 1 501 ? 11.102  8.648   58.207 1.00 22.63  ? 543  PRO A CD    1 
ATOM   3871 N N     . ALA B 1 1   ? 35.366  -15.751 65.889 1.00 29.18  ? 43   ALA B N     1 
ATOM   3872 C CA    . ALA B 1 1   ? 34.867  -16.907 65.101 1.00 27.47  ? 43   ALA B CA    1 
ATOM   3873 C C     . ALA B 1 1   ? 35.019  -18.199 65.905 1.00 29.17  ? 43   ALA B C     1 
ATOM   3874 O O     . ALA B 1 1   ? 36.065  -18.461 66.487 1.00 33.99  ? 43   ALA B O     1 
ATOM   3875 C CB    . ALA B 1 1   ? 35.610  -17.054 63.790 1.00 28.69  ? 43   ALA B CB    1 
ATOM   3876 N N     . ASP B 1 2   ? 33.986  -19.043 65.894 1.00 25.23  ? 44   ASP B N     1 
ATOM   3877 C CA    . ASP B 1 2   ? 34.141  -20.428 66.290 1.00 24.96  ? 44   ASP B CA    1 
ATOM   3878 C C     . ASP B 1 2   ? 34.108  -21.342 65.061 1.00 21.51  ? 44   ASP B C     1 
ATOM   3879 O O     . ASP B 1 2   ? 33.067  -21.813 64.602 1.00 20.54  ? 44   ASP B O     1 
ATOM   3880 C CB    . ASP B 1 2   ? 33.076  -20.784 67.287 1.00 25.21  ? 44   ASP B CB    1 
ATOM   3881 C CG    . ASP B 1 2   ? 33.050  -22.248 67.667 1.00 29.53  ? 44   ASP B CG    1 
ATOM   3882 O OD1   . ASP B 1 2   ? 34.007  -23.014 67.357 1.00 28.20  ? 44   ASP B OD1   1 
ATOM   3883 O OD2   . ASP B 1 2   ? 32.029  -22.609 68.262 1.00 30.11  ? 44   ASP B OD2   1 
ATOM   3884 N N     . PHE B 1 3   ? 35.298  -21.576 64.534 1.00 21.81  ? 45   PHE B N     1 
ATOM   3885 C CA    . PHE B 1 3   ? 35.464  -22.282 63.285 1.00 20.05  ? 45   PHE B CA    1 
ATOM   3886 C C     . PHE B 1 3   ? 34.957  -23.721 63.391 1.00 19.47  ? 45   PHE B C     1 
ATOM   3887 O O     . PHE B 1 3   ? 34.237  -24.156 62.511 1.00 16.81  ? 45   PHE B O     1 
ATOM   3888 C CB    . PHE B 1 3   ? 36.929  -22.203 62.858 1.00 19.53  ? 45   PHE B CB    1 
ATOM   3889 C CG    . PHE B 1 3   ? 37.310  -22.978 61.630 1.00 17.11  ? 45   PHE B CG    1 
ATOM   3890 C CD1   . PHE B 1 3   ? 37.034  -22.511 60.346 1.00 18.21  ? 45   PHE B CD1   1 
ATOM   3891 C CD2   . PHE B 1 3   ? 37.864  -24.239 61.761 1.00 17.56  ? 45   PHE B CD2   1 
ATOM   3892 C CE1   . PHE B 1 3   ? 37.460  -23.211 59.226 1.00 17.02  ? 45   PHE B CE1   1 
ATOM   3893 C CE2   . PHE B 1 3   ? 38.208  -24.972 60.652 1.00 18.10  ? 45   PHE B CE2   1 
ATOM   3894 C CZ    . PHE B 1 3   ? 38.024  -24.457 59.381 1.00 18.82  ? 45   PHE B CZ    1 
ATOM   3895 N N     . ALA B 1 4   ? 35.347  -24.470 64.426 1.00 21.33  ? 46   ALA B N     1 
ATOM   3896 C CA    . ALA B 1 4   ? 34.967  -25.871 64.525 1.00 21.29  ? 46   ALA B CA    1 
ATOM   3897 C C     . ALA B 1 4   ? 33.446  -26.045 64.627 1.00 19.05  ? 46   ALA B C     1 
ATOM   3898 O O     . ALA B 1 4   ? 32.885  -26.949 63.989 1.00 17.49  ? 46   ALA B O     1 
ATOM   3899 C CB    . ALA B 1 4   ? 35.655  -26.525 65.688 1.00 23.73  ? 46   ALA B CB    1 
ATOM   3900 N N     . GLY B 1 5   ? 32.784  -25.156 65.376 1.00 16.61  ? 47   GLY B N     1 
ATOM   3901 C CA    . GLY B 1 5   ? 31.337  -25.245 65.543 1.00 16.37  ? 47   GLY B CA    1 
ATOM   3902 C C     . GLY B 1 5   ? 30.631  -24.925 64.225 1.00 15.48  ? 47   GLY B C     1 
ATOM   3903 O O     . GLY B 1 5   ? 29.689  -25.599 63.837 1.00 14.92  ? 47   GLY B O     1 
ATOM   3904 N N     . ALA B 1 6   ? 31.120  -23.885 63.523 1.00 16.27  ? 48   ALA B N     1 
ATOM   3905 C CA    . ALA B 1 6   ? 30.566  -23.514 62.229 1.00 14.45  ? 48   ALA B CA    1 
ATOM   3906 C C     . ALA B 1 6   ? 30.682  -24.672 61.223 1.00 13.21  ? 48   ALA B C     1 
ATOM   3907 O O     . ALA B 1 6   ? 29.699  -25.035 60.560 1.00 14.19  ? 48   ALA B O     1 
ATOM   3908 C CB    . ALA B 1 6   ? 31.264  -22.245 61.717 1.00 13.22  ? 48   ALA B CB    1 
ATOM   3909 N N     . MET B 1 7   ? 31.876  -25.264 61.093 1.00 14.92  ? 49   MET B N     1 
ATOM   3910 C CA    . MET B 1 7   ? 32.106  -26.294 60.092 1.00 15.44  ? 49   MET B CA    1 
ATOM   3911 C C     . MET B 1 7   ? 31.303  -27.553 60.418 1.00 15.62  ? 49   MET B C     1 
ATOM   3912 O O     . MET B 1 7   ? 30.730  -28.197 59.530 1.00 14.48  ? 49   MET B O     1 
ATOM   3913 C CB    . MET B 1 7   ? 33.615  -26.606 59.985 1.00 17.85  ? 49   MET B CB    1 
ATOM   3914 C CG    . MET B 1 7   ? 34.440  -25.372 59.567 1.00 19.10  ? 49   MET B CG    1 
ATOM   3915 S SD    . MET B 1 7   ? 34.025  -24.752 57.903 1.00 19.39  ? 49   MET B SD    1 
ATOM   3916 C CE    . MET B 1 7   ? 35.094  -25.772 56.891 1.00 21.54  ? 49   MET B CE    1 
ATOM   3917 N N     . LYS B 1 8   ? 31.153  -27.877 61.700 1.00 13.52  ? 50   LYS B N     1 
ATOM   3918 C CA    . LYS B 1 8   ? 30.311  -29.011 62.050 1.00 14.97  ? 50   LYS B CA    1 
ATOM   3919 C C     . LYS B 1 8   ? 28.849  -28.796 61.618 1.00 15.31  ? 50   LYS B C     1 
ATOM   3920 O O     . LYS B 1 8   ? 28.222  -29.683 61.024 1.00 15.02  ? 50   LYS B O     1 
ATOM   3921 C CB    . LYS B 1 8   ? 30.403  -29.325 63.552 1.00 16.26  ? 50   LYS B CB    1 
ATOM   3922 C CG    . LYS B 1 8   ? 29.571  -30.521 63.949 1.00 17.69  ? 50   LYS B CG    1 
ATOM   3923 C CD    . LYS B 1 8   ? 29.525  -30.724 65.436 1.00 25.29  ? 50   LYS B CD    1 
ATOM   3924 C CE    . LYS B 1 8   ? 28.648  -31.899 65.817 1.00 27.80  ? 50   LYS B CE    1 
ATOM   3925 N NZ    . LYS B 1 8   ? 28.885  -32.259 67.238 1.00 34.51  ? 50   LYS B NZ    1 
ATOM   3926 N N     . ALA B 1 9   ? 28.324  -27.585 61.867 1.00 14.92  ? 51   ALA B N     1 
ATOM   3927 C CA    . ALA B 1 9   ? 26.964  -27.233 61.482 1.00 13.93  ? 51   ALA B CA    1 
ATOM   3928 C C     . ALA B 1 9   ? 26.822  -27.204 59.977 1.00 14.24  ? 51   ALA B C     1 
ATOM   3929 O O     . ALA B 1 9   ? 25.771  -27.622 59.475 1.00 15.11  ? 51   ALA B O     1 
ATOM   3930 C CB    . ALA B 1 9   ? 26.585  -25.894 62.128 1.00 15.36  ? 51   ALA B CB    1 
ATOM   3931 N N     . PHE B 1 10  ? 27.864  -26.715 59.254 1.00 13.29  ? 52   PHE B N     1 
ATOM   3932 C CA    . PHE B 1 10  ? 27.825  -26.762 57.795 1.00 13.04  ? 52   PHE B CA    1 
ATOM   3933 C C     . PHE B 1 10  ? 27.707  -28.197 57.261 1.00 14.32  ? 52   PHE B C     1 
ATOM   3934 O O     . PHE B 1 10  ? 26.979  -28.418 56.278 1.00 14.32  ? 52   PHE B O     1 
ATOM   3935 C CB    . PHE B 1 10  ? 29.031  -26.064 57.159 1.00 12.74  ? 52   PHE B CB    1 
ATOM   3936 C CG    . PHE B 1 10  ? 29.205  -24.570 57.374 1.00 13.41  ? 52   PHE B CG    1 
ATOM   3937 C CD1   . PHE B 1 10  ? 28.127  -23.748 57.671 1.00 12.31  ? 52   PHE B CD1   1 
ATOM   3938 C CD2   . PHE B 1 10  ? 30.470  -24.014 57.360 1.00 13.75  ? 52   PHE B CD2   1 
ATOM   3939 C CE1   . PHE B 1 10  ? 28.316  -22.400 57.927 1.00 12.71  ? 52   PHE B CE1   1 
ATOM   3940 C CE2   . PHE B 1 10  ? 30.647  -22.647 57.577 1.00 14.64  ? 52   PHE B CE2   1 
ATOM   3941 C CZ    . PHE B 1 10  ? 29.572  -21.849 57.834 1.00 12.76  ? 52   PHE B CZ    1 
ATOM   3942 N N     . ARG B 1 11  ? 28.449  -29.164 57.814 1.00 14.69  ? 53   ARG B N     1 
ATOM   3943 C CA    . ARG B 1 11  ? 28.314  -30.540 57.336 1.00 15.93  ? 53   ARG B CA    1 
ATOM   3944 C C     . ARG B 1 11  ? 26.862  -31.040 57.433 1.00 15.67  ? 53   ARG B C     1 
ATOM   3945 O O     . ARG B 1 11  ? 26.387  -31.813 56.591 1.00 18.21  ? 53   ARG B O     1 
ATOM   3946 C CB    . ARG B 1 11  ? 29.248  -31.479 58.108 1.00 17.22  ? 53   ARG B CB    1 
ATOM   3947 C CG    . ARG B 1 11  ? 30.715  -31.103 58.029 1.00 17.57  ? 53   ARG B CG    1 
ATOM   3948 C CD    . ARG B 1 11  ? 31.629  -32.007 58.875 1.00 21.07  ? 53   ARG B CD    1 
ATOM   3949 N NE    . ARG B 1 11  ? 32.992  -31.593 58.640 1.00 22.42  ? 53   ARG B NE    1 
ATOM   3950 C CZ    . ARG B 1 11  ? 33.721  -30.823 59.455 1.00 23.19  ? 53   ARG B CZ    1 
ATOM   3951 N NH1   . ARG B 1 11  ? 33.342  -30.588 60.698 1.00 24.22  ? 53   ARG B NH1   1 
ATOM   3952 N NH2   . ARG B 1 11  ? 34.814  -30.268 58.986 1.00 24.24  ? 53   ARG B NH2   1 
ATOM   3953 N N     . GLY B 1 12  ? 26.131  -30.573 58.445 1.00 14.79  ? 54   GLY B N     1 
ATOM   3954 C CA    . GLY B 1 12  ? 24.748  -30.915 58.643 1.00 15.69  ? 54   GLY B CA    1 
ATOM   3955 C C     . GLY B 1 12  ? 23.840  -30.377 57.544 1.00 16.70  ? 54   GLY B C     1 
ATOM   3956 O O     . GLY B 1 12  ? 22.802  -30.973 57.261 1.00 19.13  ? 54   GLY B O     1 
ATOM   3957 N N     . VAL B 1 13  ? 24.247  -29.246 56.940 1.00 15.01  ? 55   VAL B N     1 
ATOM   3958 C CA    . VAL B 1 13  ? 23.468  -28.604 55.897 1.00 14.10  ? 55   VAL B CA    1 
ATOM   3959 C C     . VAL B 1 13  ? 23.757  -29.240 54.542 1.00 15.55  ? 55   VAL B C     1 
ATOM   3960 O O     . VAL B 1 13  ? 22.811  -29.575 53.828 1.00 17.12  ? 55   VAL B O     1 
ATOM   3961 C CB    . VAL B 1 13  ? 23.727  -27.087 55.867 1.00 12.86  ? 55   VAL B CB    1 
ATOM   3962 C CG1   . VAL B 1 13  ? 22.954  -26.431 54.715 1.00 15.11  ? 55   VAL B CG1   1 
ATOM   3963 C CG2   . VAL B 1 13  ? 23.325  -26.460 57.197 1.00 15.96  ? 55   VAL B CG2   1 
ATOM   3964 N N     . VAL B 1 14  ? 25.030  -29.310 54.149 1.00 13.22  ? 56   VAL B N     1 
ATOM   3965 C CA    . VAL B 1 14  ? 25.358  -29.721 52.793 1.00 14.68  ? 56   VAL B CA    1 
ATOM   3966 C C     . VAL B 1 14  ? 25.819  -31.183 52.690 1.00 16.09  ? 56   VAL B C     1 
ATOM   3967 O O     . VAL B 1 14  ? 25.982  -31.679 51.576 1.00 17.87  ? 56   VAL B O     1 
ATOM   3968 C CB    . VAL B 1 14  ? 26.399  -28.786 52.177 1.00 14.03  ? 56   VAL B CB    1 
ATOM   3969 C CG1   . VAL B 1 14  ? 25.818  -27.375 52.075 1.00 15.24  ? 56   VAL B CG1   1 
ATOM   3970 C CG2   . VAL B 1 14  ? 27.726  -28.841 52.915 1.00 14.17  ? 56   VAL B CG2   1 
ATOM   3971 N N     . GLY B 1 15  ? 26.093  -31.826 53.824 1.00 15.52  ? 57   GLY B N     1 
ATOM   3972 C CA    . GLY B 1 15  ? 26.816  -33.099 53.817 1.00 18.70  ? 57   GLY B CA    1 
ATOM   3973 C C     . GLY B 1 15  ? 28.312  -32.916 54.043 1.00 18.41  ? 57   GLY B C     1 
ATOM   3974 O O     . GLY B 1 15  ? 28.946  -32.013 53.481 1.00 16.26  ? 57   GLY B O     1 
ATOM   3975 N N     . ALA B 1 16  ? 28.927  -33.871 54.769 1.00 18.19  ? 58   ALA B N     1 
ATOM   3976 C CA    . ALA B 1 16  ? 30.340  -33.831 55.053 1.00 16.76  ? 58   ALA B CA    1 
ATOM   3977 C C     . ALA B 1 16  ? 31.192  -33.759 53.799 1.00 16.57  ? 58   ALA B C     1 
ATOM   3978 O O     . ALA B 1 16  ? 32.277  -33.171 53.822 1.00 17.86  ? 58   ALA B O     1 
ATOM   3979 C CB    . ALA B 1 16  ? 30.722  -35.025 55.899 1.00 19.76  ? 58   ALA B CB    1 
ATOM   3980 N N     . GLU B 1 17  ? 30.706  -34.359 52.705 1.00 15.77  ? 59   GLU B N     1 
ATOM   3981 C CA    . GLU B 1 17  ? 31.516  -34.466 51.511 1.00 15.18  ? 59   GLU B CA    1 
ATOM   3982 C C     . GLU B 1 17  ? 31.612  -33.122 50.775 1.00 17.02  ? 59   GLU B C     1 
ATOM   3983 O O     . GLU B 1 17  ? 32.460  -32.992 49.871 1.00 17.38  ? 59   GLU B O     1 
ATOM   3984 C CB    . GLU B 1 17  ? 31.008  -35.567 50.572 1.00 16.75  ? 59   GLU B CB    1 
ATOM   3985 C CG    . GLU B 1 17  ? 29.684  -35.299 49.886 1.00 18.32  ? 59   GLU B CG    1 
ATOM   3986 C CD    . GLU B 1 17  ? 28.394  -35.592 50.628 1.00 24.66  ? 59   GLU B CD    1 
ATOM   3987 O OE1   . GLU B 1 17  ? 28.430  -35.771 51.876 1.00 27.36  ? 59   GLU B OE1   1 
ATOM   3988 O OE2   . GLU B 1 17  ? 27.323  -35.689 49.948 1.00 32.93  ? 59   GLU B OE2   1 
ATOM   3989 N N     . TRP B 1 18  ? 30.844  -32.109 51.204 1.00 17.94  ? 60   TRP B N     1 
ATOM   3990 C CA    . TRP B 1 18  ? 30.867  -30.785 50.569 1.00 14.68  ? 60   TRP B CA    1 
ATOM   3991 C C     . TRP B 1 18  ? 31.394  -29.699 51.507 1.00 15.86  ? 60   TRP B C     1 
ATOM   3992 O O     . TRP B 1 18  ? 31.248  -28.480 51.263 1.00 15.59  ? 60   TRP B O     1 
ATOM   3993 C CB    . TRP B 1 18  ? 29.480  -30.453 50.031 1.00 16.06  ? 60   TRP B CB    1 
ATOM   3994 C CG    . TRP B 1 18  ? 29.094  -31.313 48.874 1.00 15.42  ? 60   TRP B CG    1 
ATOM   3995 C CD1   . TRP B 1 18  ? 28.065  -32.203 48.842 1.00 16.76  ? 60   TRP B CD1   1 
ATOM   3996 C CD2   . TRP B 1 18  ? 29.747  -31.396 47.610 1.00 17.13  ? 60   TRP B CD2   1 
ATOM   3997 N NE1   . TRP B 1 18  ? 28.045  -32.853 47.654 1.00 18.70  ? 60   TRP B NE1   1 
ATOM   3998 C CE2   . TRP B 1 18  ? 29.043  -32.366 46.870 1.00 17.78  ? 60   TRP B CE2   1 
ATOM   3999 C CE3   . TRP B 1 18  ? 30.815  -30.721 47.024 1.00 20.46  ? 60   TRP B CE3   1 
ATOM   4000 C CZ2   . TRP B 1 18  ? 29.385  -32.660 45.558 1.00 20.81  ? 60   TRP B CZ2   1 
ATOM   4001 C CZ3   . TRP B 1 18  ? 31.156  -31.023 45.723 1.00 21.89  ? 60   TRP B CZ3   1 
ATOM   4002 C CH2   . TRP B 1 18  ? 30.439  -31.983 45.019 1.00 20.60  ? 60   TRP B CH2   1 
ATOM   4003 N N     . VAL B 1 19  ? 31.990  -30.113 52.622 1.00 15.06  ? 61   VAL B N     1 
ATOM   4004 C CA    . VAL B 1 19  ? 32.720  -29.235 53.537 1.00 14.99  ? 61   VAL B CA    1 
ATOM   4005 C C     . VAL B 1 19  ? 34.190  -29.636 53.557 1.00 18.48  ? 61   VAL B C     1 
ATOM   4006 O O     . VAL B 1 19  ? 34.520  -30.830 53.643 1.00 17.80  ? 61   VAL B O     1 
ATOM   4007 C CB    . VAL B 1 19  ? 32.117  -29.269 54.944 1.00 15.06  ? 61   VAL B CB    1 
ATOM   4008 C CG1   . VAL B 1 19  ? 32.899  -28.405 55.918 1.00 15.47  ? 61   VAL B CG1   1 
ATOM   4009 C CG2   . VAL B 1 19  ? 30.648  -28.860 54.964 1.00 15.94  ? 61   VAL B CG2   1 
ATOM   4010 N N     . PHE B 1 20  ? 35.059  -28.618 53.460 1.00 17.74  ? 62   PHE B N     1 
ATOM   4011 C CA    . PHE B 1 20  ? 36.502  -28.777 53.329 1.00 15.80  ? 62   PHE B CA    1 
ATOM   4012 C C     . PHE B 1 20  ? 37.117  -27.956 54.444 1.00 18.47  ? 62   PHE B C     1 
ATOM   4013 O O     . PHE B 1 20  ? 37.090  -26.725 54.412 1.00 15.90  ? 62   PHE B O     1 
ATOM   4014 C CB    . PHE B 1 20  ? 36.915  -28.330 51.923 1.00 16.30  ? 62   PHE B CB    1 
ATOM   4015 C CG    . PHE B 1 20  ? 36.191  -29.132 50.870 1.00 15.27  ? 62   PHE B CG    1 
ATOM   4016 C CD1   . PHE B 1 20  ? 34.939  -28.740 50.410 1.00 16.23  ? 62   PHE B CD1   1 
ATOM   4017 C CD2   . PHE B 1 20  ? 36.751  -30.309 50.385 1.00 16.16  ? 62   PHE B CD2   1 
ATOM   4018 C CE1   . PHE B 1 20  ? 34.259  -29.510 49.495 1.00 16.72  ? 62   PHE B CE1   1 
ATOM   4019 C CE2   . PHE B 1 20  ? 36.077  -31.067 49.439 1.00 18.43  ? 62   PHE B CE2   1 
ATOM   4020 C CZ    . PHE B 1 20  ? 34.825  -30.684 49.029 1.00 18.48  ? 62   PHE B CZ    1 
ATOM   4021 N N     . GLY B 1 21  ? 37.670  -28.620 55.460 1.00 17.86  ? 63   GLY B N     1 
ATOM   4022 C CA    . GLY B 1 21  ? 37.811  -27.979 56.761 1.00 20.89  ? 63   GLY B CA    1 
ATOM   4023 C C     . GLY B 1 21  ? 39.194  -28.096 57.396 1.00 22.90  ? 63   GLY B C     1 
ATOM   4024 O O     . GLY B 1 21  ? 39.323  -27.855 58.606 1.00 22.66  ? 63   GLY B O     1 
ATOM   4025 N N     . ASP B 1 22  ? 40.214  -28.371 56.581 1.00 22.47  ? 64   ASP B N     1 
ATOM   4026 C CA    . ASP B 1 22  ? 41.584  -28.273 57.093 1.00 29.51  ? 64   ASP B CA    1 
ATOM   4027 C C     . ASP B 1 22  ? 42.545  -27.863 55.984 1.00 28.35  ? 64   ASP B C     1 
ATOM   4028 O O     . ASP B 1 22  ? 42.179  -27.823 54.815 1.00 28.32  ? 64   ASP B O     1 
ATOM   4029 C CB    . ASP B 1 22  ? 42.030  -29.560 57.793 1.00 30.63  ? 64   ASP B CB    1 
ATOM   4030 C CG    . ASP B 1 22  ? 41.893  -30.817 56.967 1.00 33.81  ? 64   ASP B CG    1 
ATOM   4031 O OD1   . ASP B 1 22  ? 42.327  -30.838 55.794 1.00 32.66  ? 64   ASP B OD1   1 
ATOM   4032 O OD2   . ASP B 1 22  ? 41.396  -31.784 57.520 1.00 47.15  ? 64   ASP B OD2   1 
ATOM   4033 N N     . GLU B 1 23  ? 43.803  -27.609 56.348 1.00 30.39  ? 65   GLU B N     1 
ATOM   4034 C CA    . GLU B 1 23  ? 44.774  -27.065 55.404 1.00 31.39  ? 65   GLU B CA    1 
ATOM   4035 C C     . GLU B 1 23  ? 44.875  -27.912 54.135 1.00 29.32  ? 65   GLU B C     1 
ATOM   4036 O O     . GLU B 1 23  ? 44.893  -27.372 53.026 1.00 30.27  ? 65   GLU B O     1 
ATOM   4037 C CB    . GLU B 1 23  ? 46.172  -26.941 56.018 1.00 37.86  ? 65   GLU B CB    1 
ATOM   4038 C CG    . GLU B 1 23  ? 47.185  -26.375 55.022 1.00 46.20  ? 65   GLU B CG    1 
ATOM   4039 C CD    . GLU B 1 23  ? 48.534  -25.964 55.595 1.00 56.13  ? 65   GLU B CD    1 
ATOM   4040 O OE1   . GLU B 1 23  ? 48.553  -25.401 56.705 1.00 56.43  ? 65   GLU B OE1   1 
ATOM   4041 O OE2   . GLU B 1 23  ? 49.557  -26.160 54.902 1.00 65.17  ? 65   GLU B OE2   1 
ATOM   4042 N N     . GLU B 1 24  ? 44.947  -29.238 54.288 1.00 28.08  ? 66   GLU B N     1 
ATOM   4043 C CA    . GLU B 1 24  ? 45.064  -30.141 53.153 1.00 28.70  ? 66   GLU B CA    1 
ATOM   4044 C C     . GLU B 1 24  ? 43.803  -30.120 52.285 1.00 25.06  ? 66   GLU B C     1 
ATOM   4045 O O     . GLU B 1 24  ? 43.868  -30.182 51.060 1.00 25.69  ? 66   GLU B O     1 
ATOM   4046 C CB    . GLU B 1 24  ? 45.325  -31.566 53.642 1.00 35.68  ? 66   GLU B CB    1 
ATOM   4047 C CG    . GLU B 1 24  ? 45.333  -32.616 52.539 1.00 42.80  ? 66   GLU B CG    1 
ATOM   4048 C CD    . GLU B 1 24  ? 45.440  -34.048 53.048 1.00 59.45  ? 66   GLU B CD    1 
ATOM   4049 O OE1   . GLU B 1 24  ? 45.419  -34.248 54.289 1.00 61.34  ? 66   GLU B OE1   1 
ATOM   4050 O OE2   . GLU B 1 24  ? 45.543  -34.970 52.208 1.00 70.44  ? 66   GLU B OE2   1 
ATOM   4051 N N     . ALA B 1 25  ? 42.634  -30.115 52.919 1.00 21.57  ? 67   ALA B N     1 
ATOM   4052 C CA    . ALA B 1 25  ? 41.401  -30.234 52.168 1.00 18.65  ? 67   ALA B CA    1 
ATOM   4053 C C     . ALA B 1 25  ? 41.112  -28.915 51.398 1.00 18.03  ? 67   ALA B C     1 
ATOM   4054 O O     . ALA B 1 25  ? 40.431  -28.963 50.363 1.00 18.85  ? 67   ALA B O     1 
ATOM   4055 C CB    . ALA B 1 25  ? 40.282  -30.617 53.095 1.00 21.14  ? 67   ALA B CB    1 
ATOM   4056 N N     . VAL B 1 26  ? 41.639  -27.771 51.860 1.00 18.96  ? 68   VAL B N     1 
ATOM   4057 C CA    . VAL B 1 26  ? 41.330  -26.480 51.229 1.00 16.86  ? 68   VAL B CA    1 
ATOM   4058 C C     . VAL B 1 26  ? 42.371  -26.095 50.165 1.00 19.27  ? 68   VAL B C     1 
ATOM   4059 O O     . VAL B 1 26  ? 42.264  -25.050 49.524 1.00 16.17  ? 68   VAL B O     1 
ATOM   4060 C CB    . VAL B 1 26  ? 41.103  -25.377 52.288 1.00 22.35  ? 68   VAL B CB    1 
ATOM   4061 C CG1   . VAL B 1 26  ? 42.394  -24.733 52.748 1.00 21.70  ? 68   VAL B CG1   1 
ATOM   4062 C CG2   . VAL B 1 26  ? 40.152  -24.331 51.748 1.00 24.17  ? 68   VAL B CG2   1 
ATOM   4063 N N     . VAL B 1 27  ? 43.366  -26.968 49.879 1.00 18.53  ? 69   VAL B N     1 
ATOM   4064 C CA    . VAL B 1 27  ? 44.358  -26.718 48.840 1.00 18.86  ? 69   VAL B CA    1 
ATOM   4065 C C     . VAL B 1 27  ? 43.714  -26.318 47.513 1.00 19.31  ? 69   VAL B C     1 
ATOM   4066 O O     . VAL B 1 27  ? 44.180  -25.387 46.831 1.00 19.16  ? 69   VAL B O     1 
ATOM   4067 C CB    . VAL B 1 27  ? 45.303  -27.934 48.684 1.00 21.18  ? 69   VAL B CB    1 
ATOM   4068 C CG1   . VAL B 1 27  ? 45.950  -27.986 47.309 1.00 24.34  ? 69   VAL B CG1   1 
ATOM   4069 C CG2   . VAL B 1 27  ? 46.332  -27.948 49.798 1.00 22.42  ? 69   VAL B CG2   1 
ATOM   4070 N N     . PRO B 1 28  ? 42.604  -26.948 47.063 1.00 18.19  ? 70   PRO B N     1 
ATOM   4071 C CA    . PRO B 1 28  ? 42.019  -26.549 45.775 1.00 18.23  ? 70   PRO B CA    1 
ATOM   4072 C C     . PRO B 1 28  ? 41.513  -25.092 45.709 1.00 17.44  ? 70   PRO B C     1 
ATOM   4073 O O     . PRO B 1 28  ? 41.294  -24.599 44.614 1.00 18.45  ? 70   PRO B O     1 
ATOM   4074 C CB    . PRO B 1 28  ? 40.932  -27.593 45.541 1.00 18.61  ? 70   PRO B CB    1 
ATOM   4075 C CG    . PRO B 1 28  ? 41.376  -28.777 46.347 1.00 19.89  ? 70   PRO B CG    1 
ATOM   4076 C CD    . PRO B 1 28  ? 41.990  -28.168 47.582 1.00 19.22  ? 70   PRO B CD    1 
ATOM   4077 N N     . TRP B 1 29  ? 41.350  -24.413 46.867 1.00 14.80  ? 71   TRP B N     1 
ATOM   4078 C CA    . TRP B 1 29  ? 40.842  -23.026 46.902 1.00 12.86  ? 71   TRP B CA    1 
ATOM   4079 C C     . TRP B 1 29  ? 41.977  -22.042 47.196 1.00 13.63  ? 71   TRP B C     1 
ATOM   4080 O O     . TRP B 1 29  ? 41.735  -20.854 47.423 1.00 14.79  ? 71   TRP B O     1 
ATOM   4081 C CB    . TRP B 1 29  ? 39.703  -22.910 47.949 1.00 10.98  ? 71   TRP B CB    1 
ATOM   4082 C CG    . TRP B 1 29  ? 38.447  -23.585 47.559 1.00 13.40  ? 71   TRP B CG    1 
ATOM   4083 C CD1   . TRP B 1 29  ? 37.400  -23.031 46.887 1.00 13.15  ? 71   TRP B CD1   1 
ATOM   4084 C CD2   . TRP B 1 29  ? 38.104  -24.964 47.774 1.00 13.46  ? 71   TRP B CD2   1 
ATOM   4085 N NE1   . TRP B 1 29  ? 36.417  -23.962 46.679 1.00 15.11  ? 71   TRP B NE1   1 
ATOM   4086 C CE2   . TRP B 1 29  ? 36.805  -25.148 47.233 1.00 14.53  ? 71   TRP B CE2   1 
ATOM   4087 C CE3   . TRP B 1 29  ? 38.759  -26.031 48.390 1.00 14.90  ? 71   TRP B CE3   1 
ATOM   4088 C CZ2   . TRP B 1 29  ? 36.173  -26.383 47.239 1.00 15.77  ? 71   TRP B CZ2   1 
ATOM   4089 C CZ3   . TRP B 1 29  ? 38.113  -27.244 48.417 1.00 15.74  ? 71   TRP B CZ3   1 
ATOM   4090 C CH2   . TRP B 1 29  ? 36.853  -27.412 47.847 1.00 15.29  ? 71   TRP B CH2   1 
ATOM   4091 N N     . SER B 1 30  ? 43.240  -22.525 47.263 1.00 13.67  ? 72   SER B N     1 
ATOM   4092 C CA    . SER B 1 30  ? 44.316  -21.755 47.845 1.00 14.36  ? 72   SER B CA    1 
ATOM   4093 C C     . SER B 1 30  ? 45.292  -21.194 46.813 1.00 13.91  ? 72   SER B C     1 
ATOM   4094 O O     . SER B 1 30  ? 45.982  -20.266 47.199 1.00 17.70  ? 72   SER B O     1 
ATOM   4095 C CB    . SER B 1 30  ? 45.068  -22.537 48.907 1.00 17.60  ? 72   SER B CB    1 
ATOM   4096 O OG    . SER B 1 30  ? 44.189  -22.765 50.008 1.00 22.37  ? 72   SER B OG    1 
ATOM   4097 N N     . LYS B 1 31  ? 45.338  -21.656 45.557 1.00 13.36  ? 73   LYS B N     1 
ATOM   4098 C CA    . LYS B 1 31  ? 46.380  -21.200 44.642 1.00 14.03  ? 73   LYS B CA    1 
ATOM   4099 C C     . LYS B 1 31  ? 45.969  -19.813 44.073 1.00 14.05  ? 73   LYS B C     1 
ATOM   4100 O O     . LYS B 1 31  ? 44.806  -19.627 43.661 1.00 13.02  ? 73   LYS B O     1 
ATOM   4101 C CB    . LYS B 1 31  ? 46.600  -22.209 43.515 1.00 17.53  ? 73   LYS B CB    1 
ATOM   4102 C CG    . LYS B 1 31  ? 47.711  -21.821 42.529 1.00 21.76  ? 73   LYS B CG    1 
ATOM   4103 C CD    . LYS B 1 31  ? 48.532  -23.003 42.116 1.00 29.19  ? 73   LYS B CD    1 
ATOM   4104 C CE    . LYS B 1 31  ? 49.665  -22.634 41.181 1.00 37.31  ? 73   LYS B CE    1 
ATOM   4105 N NZ    . LYS B 1 31  ? 49.149  -22.537 39.802 1.00 44.86  ? 73   LYS B NZ    1 
ATOM   4106 N N     . THR B 1 32  ? 46.908  -18.847 44.078 1.00 12.75  ? 74   THR B N     1 
ATOM   4107 C CA    . THR B 1 32  ? 46.721  -17.543 43.462 1.00 13.27  ? 74   THR B CA    1 
ATOM   4108 C C     . THR B 1 32  ? 47.895  -17.215 42.555 1.00 12.89  ? 74   THR B C     1 
ATOM   4109 O O     . THR B 1 32  ? 48.918  -17.895 42.585 1.00 13.33  ? 74   THR B O     1 
ATOM   4110 C CB    . THR B 1 32  ? 46.603  -16.420 44.486 1.00 13.53  ? 74   THR B CB    1 
ATOM   4111 O OG1   . THR B 1 32  ? 47.836  -16.296 45.195 1.00 13.38  ? 74   THR B OG1   1 
ATOM   4112 C CG2   . THR B 1 32  ? 45.460  -16.650 45.438 1.00 14.18  ? 74   THR B CG2   1 
ATOM   4113 N N     . TYR B 1 33  ? 47.700  -16.217 41.708 1.00 11.42  ? 75   TYR B N     1 
ATOM   4114 C CA    . TYR B 1 33  ? 48.732  -15.763 40.772 1.00 12.82  ? 75   TYR B CA    1 
ATOM   4115 C C     . TYR B 1 33  ? 49.221  -14.370 41.132 1.00 11.85  ? 75   TYR B C     1 
ATOM   4116 O O     . TYR B 1 33  ? 50.282  -13.961 40.667 1.00 12.00  ? 75   TYR B O     1 
ATOM   4117 C CB    . TYR B 1 33  ? 48.222  -15.819 39.332 1.00 13.17  ? 75   TYR B CB    1 
ATOM   4118 C CG    . TYR B 1 33  ? 47.755  -17.219 39.020 1.00 13.03  ? 75   TYR B CG    1 
ATOM   4119 C CD1   . TYR B 1 33  ? 48.634  -18.193 38.673 1.00 15.85  ? 75   TYR B CD1   1 
ATOM   4120 C CD2   . TYR B 1 33  ? 46.420  -17.571 39.224 1.00 13.76  ? 75   TYR B CD2   1 
ATOM   4121 C CE1   . TYR B 1 33  ? 48.210  -19.501 38.465 1.00 16.99  ? 75   TYR B CE1   1 
ATOM   4122 C CE2   . TYR B 1 33  ? 45.984  -18.884 39.078 1.00 14.96  ? 75   TYR B CE2   1 
ATOM   4123 C CZ    . TYR B 1 33  ? 46.897  -19.854 38.692 1.00 19.47  ? 75   TYR B CZ    1 
ATOM   4124 O OH    . TYR B 1 33  ? 46.510  -21.172 38.509 1.00 19.94  ? 75   TYR B OH    1 
ATOM   4125 N N     . ILE B 1 34  ? 48.478  -13.641 42.011 1.00 12.36  ? 76   ILE B N     1 
ATOM   4126 C CA    . ILE B 1 34  ? 48.924  -12.353 42.511 1.00 11.79  ? 76   ILE B CA    1 
ATOM   4127 C C     . ILE B 1 34  ? 50.142  -12.534 43.417 1.00 11.99  ? 76   ILE B C     1 
ATOM   4128 O O     . ILE B 1 34  ? 50.375  -13.593 43.978 1.00 12.36  ? 76   ILE B O     1 
ATOM   4129 C CB    . ILE B 1 34  ? 47.775  -11.662 43.296 1.00 12.64  ? 76   ILE B CB    1 
ATOM   4130 C CG1   . ILE B 1 34  ? 47.186  -12.620 44.343 1.00 14.89  ? 76   ILE B CG1   1 
ATOM   4131 C CG2   . ILE B 1 34  ? 46.699  -11.153 42.339 1.00 13.86  ? 76   ILE B CG2   1 
ATOM   4132 C CD1   . ILE B 1 34  ? 46.628  -12.010 45.600 1.00 17.64  ? 76   ILE B CD1   1 
ATOM   4133 N N     . PRO B 1 35  ? 50.971  -11.494 43.590 1.00 13.15  ? 77   PRO B N     1 
ATOM   4134 C CA    . PRO B 1 35  ? 52.095  -11.590 44.542 1.00 13.63  ? 77   PRO B CA    1 
ATOM   4135 C C     . PRO B 1 35  ? 51.572  -11.654 45.977 1.00 14.10  ? 77   PRO B C     1 
ATOM   4136 O O     . PRO B 1 35  ? 50.637  -10.902 46.312 1.00 14.93  ? 77   PRO B O     1 
ATOM   4137 C CB    . PRO B 1 35  ? 52.894  -10.308 44.275 1.00 15.39  ? 77   PRO B CB    1 
ATOM   4138 C CG    . PRO B 1 35  ? 51.910  -9.385  43.689 1.00 15.14  ? 77   PRO B CG    1 
ATOM   4139 C CD    . PRO B 1 35  ? 50.910  -10.197 42.908 1.00 13.83  ? 77   PRO B CD    1 
ATOM   4140 N N     . ASP B 1 36  ? 52.156  -12.551 46.810 1.00 12.80  ? 78   ASP B N     1 
ATOM   4141 C CA    . ASP B 1 36  ? 51.721  -12.702 48.185 1.00 13.40  ? 78   ASP B CA    1 
ATOM   4142 C C     . ASP B 1 36  ? 52.920  -13.128 49.035 1.00 14.85  ? 78   ASP B C     1 
ATOM   4143 O O     . ASP B 1 36  ? 52.953  -14.255 49.496 1.00 15.98  ? 78   ASP B O     1 
ATOM   4144 C CB    . ASP B 1 36  ? 50.598  -13.718 48.316 1.00 13.44  ? 78   ASP B CB    1 
ATOM   4145 C CG    . ASP B 1 36  ? 49.961  -13.776 49.694 1.00 14.45  ? 78   ASP B CG    1 
ATOM   4146 O OD1   . ASP B 1 36  ? 50.392  -12.955 50.585 1.00 14.53  ? 78   ASP B OD1   1 
ATOM   4147 O OD2   . ASP B 1 36  ? 49.065  -14.650 49.860 1.00 15.44  ? 78   ASP B OD2   1 
ATOM   4148 N N     . PRO B 1 37  ? 53.964  -12.277 49.125 1.00 15.60  ? 79   PRO B N     1 
ATOM   4149 C CA    . PRO B 1 37  ? 55.194  -12.663 49.824 1.00 18.42  ? 79   PRO B CA    1 
ATOM   4150 C C     . PRO B 1 37  ? 54.967  -13.118 51.268 1.00 24.01  ? 79   PRO B C     1 
ATOM   4151 O O     . PRO B 1 37  ? 55.670  -14.010 51.732 1.00 29.47  ? 79   PRO B O     1 
ATOM   4152 C CB    . PRO B 1 37  ? 56.082  -11.416 49.725 1.00 18.20  ? 79   PRO B CB    1 
ATOM   4153 C CG    . PRO B 1 37  ? 55.406  -10.412 48.867 1.00 19.93  ? 79   PRO B CG    1 
ATOM   4154 C CD    . PRO B 1 37  ? 53.995  -10.900 48.611 1.00 16.32  ? 79   PRO B CD    1 
ATOM   4155 N N     . ALA B 1 38  ? 53.953  -12.580 51.962 1.00 22.80  ? 80   ALA B N     1 
ATOM   4156 C CA    . ALA B 1 38  ? 53.721  -12.988 53.343 1.00 26.54  ? 80   ALA B CA    1 
ATOM   4157 C C     . ALA B 1 38  ? 52.792  -14.202 53.450 1.00 25.86  ? 80   ALA B C     1 
ATOM   4158 O O     . ALA B 1 38  ? 52.492  -14.628 54.564 1.00 26.60  ? 80   ALA B O     1 
ATOM   4159 C CB    . ALA B 1 38  ? 53.209  -11.818 54.130 1.00 27.34  ? 80   ALA B CB    1 
ATOM   4160 N N     . HIS B 1 39  ? 52.315  -14.774 52.323 1.00 21.71  ? 81   HIS B N     1 
ATOM   4161 C CA    . HIS B 1 39  ? 51.411  -15.910 52.299 1.00 25.95  ? 81   HIS B CA    1 
ATOM   4162 C C     . HIS B 1 39  ? 50.164  -15.649 53.165 1.00 22.55  ? 81   HIS B C     1 
ATOM   4163 O O     . HIS B 1 39  ? 49.696  -16.550 53.844 1.00 25.91  ? 81   HIS B O     1 
ATOM   4164 C CB    . HIS B 1 39  ? 52.132  -17.207 52.707 1.00 34.05  ? 81   HIS B CB    1 
ATOM   4165 C CG    . HIS B 1 39  ? 53.363  -17.465 51.899 1.00 40.29  ? 81   HIS B CG    1 
ATOM   4166 N ND1   . HIS B 1 39  ? 53.318  -18.192 50.729 1.00 53.43  ? 81   HIS B ND1   1 
ATOM   4167 C CD2   . HIS B 1 39  ? 54.624  -17.039 52.029 1.00 47.08  ? 81   HIS B CD2   1 
ATOM   4168 C CE1   . HIS B 1 39  ? 54.525  -18.219 50.181 1.00 50.03  ? 81   HIS B CE1   1 
ATOM   4169 N NE2   . HIS B 1 39  ? 55.337  -17.520 50.950 1.00 54.78  ? 81   HIS B NE2   1 
ATOM   4170 N N     . GLN B 1 40  ? 49.590  -14.449 53.051 1.00 18.41  ? 82   GLN B N     1 
ATOM   4171 C CA    . GLN B 1 40  ? 48.486  -14.026 53.909 1.00 18.37  ? 82   GLN B CA    1 
ATOM   4172 C C     . GLN B 1 40  ? 47.115  -14.150 53.229 1.00 17.30  ? 82   GLN B C     1 
ATOM   4173 O O     . GLN B 1 40  ? 46.117  -14.080 53.944 1.00 19.80  ? 82   GLN B O     1 
ATOM   4174 C CB    . GLN B 1 40  ? 48.732  -12.596 54.389 1.00 20.51  ? 82   GLN B CB    1 
ATOM   4175 C CG    . GLN B 1 40  ? 48.478  -11.504 53.371 1.00 23.18  ? 82   GLN B CG    1 
ATOM   4176 C CD    . GLN B 1 40  ? 48.854  -10.144 53.907 1.00 28.49  ? 82   GLN B CD    1 
ATOM   4177 O OE1   . GLN B 1 40  ? 48.273  -9.667  54.882 1.00 33.23  ? 82   GLN B OE1   1 
ATOM   4178 N NE2   . GLN B 1 40  ? 49.832  -9.507  53.279 1.00 26.60  ? 82   GLN B NE2   1 
ATOM   4179 N N     . TYR B 1 41  ? 47.029  -14.294 51.898 1.00 14.90  ? 83   TYR B N     1 
ATOM   4180 C CA    . TYR B 1 41  ? 45.733  -14.468 51.230 1.00 13.98  ? 83   TYR B CA    1 
ATOM   4181 C C     . TYR B 1 41  ? 45.408  -15.952 50.999 1.00 13.13  ? 83   TYR B C     1 
ATOM   4182 O O     . TYR B 1 41  ? 45.871  -16.625 50.076 1.00 15.74  ? 83   TYR B O     1 
ATOM   4183 C CB    . TYR B 1 41  ? 45.662  -13.614 49.961 1.00 12.86  ? 83   TYR B CB    1 
ATOM   4184 C CG    . TYR B 1 41  ? 45.956  -12.166 50.256 1.00 13.70  ? 83   TYR B CG    1 
ATOM   4185 C CD1   . TYR B 1 41  ? 45.062  -11.354 50.936 1.00 14.95  ? 83   TYR B CD1   1 
ATOM   4186 C CD2   . TYR B 1 41  ? 47.189  -11.617 49.932 1.00 15.61  ? 83   TYR B CD2   1 
ATOM   4187 C CE1   . TYR B 1 41  ? 45.375  -10.054 51.267 1.00 14.35  ? 83   TYR B CE1   1 
ATOM   4188 C CE2   . TYR B 1 41  ? 47.530  -10.316 50.285 1.00 15.89  ? 83   TYR B CE2   1 
ATOM   4189 C CZ    . TYR B 1 41  ? 46.623  -9.530  50.973 1.00 15.31  ? 83   TYR B CZ    1 
ATOM   4190 O OH    . TYR B 1 41  ? 46.901  -8.199  51.262 1.00 17.65  ? 83   TYR B OH    1 
ATOM   4191 N N     . LYS B 1 42  ? 44.631  -16.495 51.923 1.00 14.41  ? 84   LYS B N     1 
ATOM   4192 C CA    . LYS B 1 42  ? 44.345  -17.922 51.921 1.00 16.02  ? 84   LYS B CA    1 
ATOM   4193 C C     . LYS B 1 42  ? 43.107  -18.219 52.747 1.00 13.79  ? 84   LYS B C     1 
ATOM   4194 O O     . LYS B 1 42  ? 42.938  -17.717 53.854 1.00 14.57  ? 84   LYS B O     1 
ATOM   4195 C CB    . LYS B 1 42  ? 45.536  -18.757 52.410 1.00 22.85  ? 84   LYS B CB    1 
ATOM   4196 C CG    . LYS B 1 42  ? 45.934  -18.681 53.864 1.00 27.87  ? 84   LYS B CG    1 
ATOM   4197 C CD    . LYS B 1 42  ? 47.044  -19.684 54.166 1.00 38.51  ? 84   LYS B CD    1 
ATOM   4198 C CE    . LYS B 1 42  ? 48.413  -19.256 53.668 1.00 48.34  ? 84   LYS B CE    1 
ATOM   4199 N NZ    . LYS B 1 42  ? 49.329  -20.399 53.377 1.00 51.55  ? 84   LYS B NZ    1 
ATOM   4200 N N     . PRO B 1 43  ? 42.203  -19.066 52.230 1.00 14.62  ? 85   PRO B N     1 
ATOM   4201 C CA    . PRO B 1 43  ? 41.033  -19.494 53.015 1.00 13.52  ? 85   PRO B CA    1 
ATOM   4202 C C     . PRO B 1 43  ? 41.382  -20.590 54.022 1.00 13.80  ? 85   PRO B C     1 
ATOM   4203 O O     . PRO B 1 43  ? 42.419  -21.243 53.884 1.00 14.53  ? 85   PRO B O     1 
ATOM   4204 C CB    . PRO B 1 43  ? 40.103  -20.051 51.926 1.00 15.57  ? 85   PRO B CB    1 
ATOM   4205 C CG    . PRO B 1 43  ? 41.087  -20.666 50.947 1.00 16.08  ? 85   PRO B CG    1 
ATOM   4206 C CD    . PRO B 1 43  ? 42.331  -19.804 50.965 1.00 16.17  ? 85   PRO B CD    1 
ATOM   4207 N N     . VAL B 1 44  ? 40.530  -20.759 55.036 1.00 12.80  ? 86   VAL B N     1 
ATOM   4208 C CA    . VAL B 1 44  ? 40.717  -21.755 56.077 1.00 14.99  ? 86   VAL B CA    1 
ATOM   4209 C C     . VAL B 1 44  ? 39.714  -22.898 55.903 1.00 15.02  ? 86   VAL B C     1 
ATOM   4210 O O     . VAL B 1 44  ? 39.834  -23.924 56.566 1.00 16.18  ? 86   VAL B O     1 
ATOM   4211 C CB    . VAL B 1 44  ? 40.669  -21.154 57.506 1.00 15.73  ? 86   VAL B CB    1 
ATOM   4212 C CG1   . VAL B 1 44  ? 41.801  -20.188 57.734 1.00 16.72  ? 86   VAL B CG1   1 
ATOM   4213 C CG2   . VAL B 1 44  ? 39.307  -20.484 57.800 1.00 15.41  ? 86   VAL B CG2   1 
ATOM   4214 N N     . GLY B 1 45  ? 38.789  -22.790 54.929 1.00 13.32  ? 87   GLY B N     1 
ATOM   4215 C CA    . GLY B 1 45  ? 37.798  -23.812 54.696 1.00 11.83  ? 87   GLY B CA    1 
ATOM   4216 C C     . GLY B 1 45  ? 36.997  -23.438 53.435 1.00 11.68  ? 87   GLY B C     1 
ATOM   4217 O O     . GLY B 1 45  ? 37.184  -22.351 52.868 1.00 11.85  ? 87   GLY B O     1 
ATOM   4218 N N     . ALA B 1 46  ? 36.198  -24.386 52.953 1.00 12.63  ? 88   ALA B N     1 
ATOM   4219 C CA    . ALA B 1 46  ? 35.263  -24.162 51.851 1.00 13.61  ? 88   ALA B CA    1 
ATOM   4220 C C     . ALA B 1 46  ? 33.992  -24.953 52.107 1.00 15.22  ? 88   ALA B C     1 
ATOM   4221 O O     . ALA B 1 46  ? 34.023  -26.019 52.738 1.00 14.03  ? 88   ALA B O     1 
ATOM   4222 C CB    . ALA B 1 46  ? 35.801  -24.527 50.484 1.00 13.78  ? 88   ALA B CB    1 
ATOM   4223 N N     . VAL B 1 47  ? 32.854  -24.400 51.614 1.00 12.25  ? 89   VAL B N     1 
ATOM   4224 C CA    . VAL B 1 47  ? 31.588  -25.095 51.671 1.00 14.38  ? 89   VAL B CA    1 
ATOM   4225 C C     . VAL B 1 47  ? 30.895  -24.899 50.338 1.00 13.44  ? 89   VAL B C     1 
ATOM   4226 O O     . VAL B 1 47  ? 30.852  -23.792 49.819 1.00 12.86  ? 89   VAL B O     1 
ATOM   4227 C CB    . VAL B 1 47  ? 30.720  -24.620 52.835 1.00 15.80  ? 89   VAL B CB    1 
ATOM   4228 C CG1   . VAL B 1 47  ? 29.395  -25.341 52.912 1.00 17.00  ? 89   VAL B CG1   1 
ATOM   4229 C CG2   . VAL B 1 47  ? 31.465  -24.710 54.134 1.00 22.40  ? 89   VAL B CG2   1 
ATOM   4230 N N     . CYS B 1 48  ? 30.308  -25.979 49.820 1.00 12.51  ? 90   CYS B N     1 
ATOM   4231 C CA    . CYS B 1 48  ? 29.763  -26.017 48.480 1.00 11.93  ? 90   CYS B CA    1 
ATOM   4232 C C     . CYS B 1 48  ? 28.297  -26.443 48.484 1.00 12.90  ? 90   CYS B C     1 
ATOM   4233 O O     . CYS B 1 48  ? 27.960  -27.622 48.242 1.00 12.83  ? 90   CYS B O     1 
ATOM   4234 C CB    . CYS B 1 48  ? 30.537  -26.994 47.619 1.00 14.51  ? 90   CYS B CB    1 
ATOM   4235 S SG    . CYS B 1 48  ? 32.273  -26.592 47.450 1.00 17.51  ? 90   CYS B SG    1 
ATOM   4236 N N     . PRO B 1 49  ? 27.340  -25.509 48.666 1.00 11.69  ? 91   PRO B N     1 
ATOM   4237 C CA    . PRO B 1 49  ? 25.924  -25.828 48.600 1.00 11.92  ? 91   PRO B CA    1 
ATOM   4238 C C     . PRO B 1 49  ? 25.379  -25.995 47.189 1.00 13.40  ? 91   PRO B C     1 
ATOM   4239 O O     . PRO B 1 49  ? 25.954  -25.453 46.259 1.00 14.22  ? 91   PRO B O     1 
ATOM   4240 C CB    . PRO B 1 49  ? 25.247  -24.632 49.259 1.00 12.96  ? 91   PRO B CB    1 
ATOM   4241 C CG    . PRO B 1 49  ? 26.155  -23.476 48.848 1.00 11.61  ? 91   PRO B CG    1 
ATOM   4242 C CD    . PRO B 1 49  ? 27.554  -24.072 48.959 1.00 11.80  ? 91   PRO B CD    1 
ATOM   4243 N N     . GLN B 1 50  ? 24.231  -26.694 47.073 1.00 12.12  ? 92   GLN B N     1 
ATOM   4244 C CA    . GLN B 1 50  ? 23.555  -26.904 45.778 1.00 11.27  ? 92   GLN B CA    1 
ATOM   4245 C C     . GLN B 1 50  ? 22.217  -26.191 45.690 1.00 13.16  ? 92   GLN B C     1 
ATOM   4246 O O     . GLN B 1 50  ? 21.616  -26.179 44.627 1.00 13.81  ? 92   GLN B O     1 
ATOM   4247 C CB    . GLN B 1 50  ? 23.444  -28.374 45.426 1.00 14.18  ? 92   GLN B CB    1 
ATOM   4248 C CG    . GLN B 1 50  ? 22.681  -29.236 46.428 1.00 15.76  ? 92   GLN B CG    1 
ATOM   4249 C CD    . GLN B 1 50  ? 21.186  -29.118 46.368 1.00 15.39  ? 92   GLN B CD    1 
ATOM   4250 O OE1   . GLN B 1 50  ? 20.622  -29.068 45.294 1.00 18.01  ? 92   GLN B OE1   1 
ATOM   4251 N NE2   . GLN B 1 50  ? 20.519  -29.134 47.522 1.00 16.00  ? 92   GLN B NE2   1 
ATOM   4252 N N     . SER B 1 51  ? 21.720  -25.581 46.785 1.00 12.13  ? 93   SER B N     1 
ATOM   4253 C CA    . SER B 1 51  ? 20.441  -24.889 46.743 1.00 12.67  ? 93   SER B CA    1 
ATOM   4254 C C     . SER B 1 51  ? 20.495  -23.581 47.533 1.00 11.96  ? 93   SER B C     1 
ATOM   4255 O O     . SER B 1 51  ? 21.266  -23.438 48.478 1.00 11.03  ? 93   SER B O     1 
ATOM   4256 C CB    . SER B 1 51  ? 19.298  -25.693 47.267 1.00 13.41  ? 93   SER B CB    1 
ATOM   4257 O OG    . SER B 1 51  ? 19.480  -25.922 48.665 1.00 14.98  ? 93   SER B OG    1 
ATOM   4258 N N     . VAL B 1 52  ? 19.545  -22.711 47.199 1.00 13.79  ? 94   VAL B N     1 
ATOM   4259 C CA    . VAL B 1 52  ? 19.407  -21.430 47.869 1.00 13.85  ? 94   VAL B CA    1 
ATOM   4260 C C     . VAL B 1 52  ? 19.024  -21.663 49.333 1.00 12.37  ? 94   VAL B C     1 
ATOM   4261 O O     . VAL B 1 52  ? 19.482  -20.936 50.205 1.00 11.60  ? 94   VAL B O     1 
ATOM   4262 C CB    . VAL B 1 52  ? 18.418  -20.527 47.097 1.00 15.75  ? 94   VAL B CB    1 
ATOM   4263 C CG1   . VAL B 1 52  ? 17.006  -21.091 47.147 1.00 16.58  ? 94   VAL B CG1   1 
ATOM   4264 C CG2   . VAL B 1 52  ? 18.456  -19.112 47.653 1.00 16.29  ? 94   VAL B CG2   1 
ATOM   4265 N N     . GLU B 1 53  ? 18.211  -22.693 49.624 1.00 12.92  ? 95   GLU B N     1 
ATOM   4266 C CA    . GLU B 1 53  ? 17.828  -22.994 50.997 1.00 14.56  ? 95   GLU B CA    1 
ATOM   4267 C C     . GLU B 1 53  ? 19.050  -23.384 51.833 1.00 13.41  ? 95   GLU B C     1 
ATOM   4268 O O     . GLU B 1 53  ? 19.169  -22.961 53.000 1.00 12.61  ? 95   GLU B O     1 
ATOM   4269 C CB    . GLU B 1 53  ? 16.803  -24.147 51.053 1.00 17.34  ? 95   GLU B CB    1 
ATOM   4270 C CG    . GLU B 1 53  ? 15.457  -23.767 50.431 1.00 19.76  ? 95   GLU B CG    1 
ATOM   4271 C CD    . GLU B 1 53  ? 15.316  -23.825 48.927 1.00 22.88  ? 95   GLU B CD    1 
ATOM   4272 O OE1   . GLU B 1 53  ? 16.228  -24.306 48.216 1.00 19.64  ? 95   GLU B OE1   1 
ATOM   4273 O OE2   . GLU B 1 53  ? 14.261  -23.317 48.447 1.00 27.74  ? 95   GLU B OE2   1 
ATOM   4274 N N     . GLU B 1 54  ? 19.977  -24.147 51.224 1.00 10.79  ? 96   GLU B N     1 
ATOM   4275 C CA    . GLU B 1 54  ? 21.264  -24.456 51.887 1.00 10.89  ? 96   GLU B CA    1 
ATOM   4276 C C     . GLU B 1 54  ? 22.065  -23.165 52.164 1.00 10.55  ? 96   GLU B C     1 
ATOM   4277 O O     . GLU B 1 54  ? 22.655  -22.972 53.252 1.00 11.83  ? 96   GLU B O     1 
ATOM   4278 C CB    . GLU B 1 54  ? 22.108  -25.485 51.114 1.00 12.05  ? 96   GLU B CB    1 
ATOM   4279 C CG    . GLU B 1 54  ? 21.563  -26.916 51.173 1.00 13.29  ? 96   GLU B CG    1 
ATOM   4280 C CD    . GLU B 1 54  ? 22.265  -27.839 50.229 1.00 14.79  ? 96   GLU B CD    1 
ATOM   4281 O OE1   . GLU B 1 54  ? 23.104  -27.394 49.447 1.00 16.55  ? 96   GLU B OE1   1 
ATOM   4282 O OE2   . GLU B 1 54  ? 21.885  -29.010 50.178 1.00 20.14  ? 96   GLU B OE2   1 
ATOM   4283 N N     . VAL B 1 55  ? 22.122  -22.263 51.181 1.00 10.36  ? 97   VAL B N     1 
ATOM   4284 C CA    . VAL B 1 55  ? 22.807  -20.982 51.363 1.00 10.82  ? 97   VAL B CA    1 
ATOM   4285 C C     . VAL B 1 55  ? 22.218  -20.276 52.562 1.00 11.18  ? 97   VAL B C     1 
ATOM   4286 O O     . VAL B 1 55  ? 22.961  -19.734 53.404 1.00 10.58  ? 97   VAL B O     1 
ATOM   4287 C CB    . VAL B 1 55  ? 22.685  -20.087 50.110 1.00 11.55  ? 97   VAL B CB    1 
ATOM   4288 C CG1   . VAL B 1 55  ? 23.222  -18.677 50.362 1.00 12.41  ? 97   VAL B CG1   1 
ATOM   4289 C CG2   . VAL B 1 55  ? 23.422  -20.717 48.948 1.00 12.28  ? 97   VAL B CG2   1 
ATOM   4290 N N     . GLN B 1 56  ? 20.890  -20.259 52.636 1.00 9.92   ? 98   GLN B N     1 
ATOM   4291 C CA    . GLN B 1 56  ? 20.297  -19.459 53.717 1.00 10.52  ? 98   GLN B CA    1 
ATOM   4292 C C     . GLN B 1 56  ? 20.662  -20.040 55.101 1.00 11.43  ? 98   GLN B C     1 
ATOM   4293 O O     . GLN B 1 56  ? 20.942  -19.323 56.084 1.00 11.44  ? 98   GLN B O     1 
ATOM   4294 C CB    . GLN B 1 56  ? 18.765  -19.400 53.600 1.00 11.46  ? 98   GLN B CB    1 
ATOM   4295 C CG    . GLN B 1 56  ? 18.217  -18.554 52.447 1.00 11.54  ? 98   GLN B CG    1 
ATOM   4296 C CD    . GLN B 1 56  ? 16.716  -18.713 52.376 1.00 12.58  ? 98   GLN B CD    1 
ATOM   4297 O OE1   . GLN B 1 56  ? 16.182  -19.637 51.760 1.00 17.19  ? 98   GLN B OE1   1 
ATOM   4298 N NE2   . GLN B 1 56  ? 15.994  -17.822 52.990 1.00 14.37  ? 98   GLN B NE2   1 
ATOM   4299 N N     . GLU B 1 57  ? 20.651  -21.366 55.187 1.00 12.08  ? 99   GLU B N     1 
ATOM   4300 C CA    . GLU B 1 57  ? 20.994  -22.039 56.443 1.00 13.30  ? 99   GLU B CA    1 
ATOM   4301 C C     . GLU B 1 57  ? 22.443  -21.777 56.802 1.00 11.35  ? 99   GLU B C     1 
ATOM   4302 O O     . GLU B 1 57  ? 22.781  -21.526 57.957 1.00 12.08  ? 99   GLU B O     1 
ATOM   4303 C CB    . GLU B 1 57  ? 20.826  -23.567 56.313 1.00 17.23  ? 99   GLU B CB    1 
ATOM   4304 C CG    . GLU B 1 57  ? 19.474  -24.130 56.569 1.00 30.28  ? 99   GLU B CG    1 
ATOM   4305 C CD    . GLU B 1 57  ? 19.615  -25.625 56.882 1.00 36.69  ? 99   GLU B CD    1 
ATOM   4306 O OE1   . GLU B 1 57  ? 19.787  -26.393 55.910 1.00 47.92  ? 99   GLU B OE1   1 
ATOM   4307 O OE2   . GLU B 1 57  ? 19.716  -25.985 58.080 1.00 41.13  ? 99   GLU B OE2   1 
ATOM   4308 N N     . ILE B 1 58  ? 23.330  -21.849 55.804 1.00 8.79   ? 100  ILE B N     1 
ATOM   4309 C CA    . ILE B 1 58  ? 24.736  -21.550 55.985 1.00 9.93   ? 100  ILE B CA    1 
ATOM   4310 C C     . ILE B 1 58  ? 24.902  -20.130 56.551 1.00 10.59  ? 100  ILE B C     1 
ATOM   4311 O O     . ILE B 1 58  ? 25.728  -19.894 57.440 1.00 11.21  ? 100  ILE B O     1 
ATOM   4312 C CB    . ILE B 1 58  ? 25.491  -21.759 54.655 1.00 9.61   ? 100  ILE B CB    1 
ATOM   4313 C CG1   . ILE B 1 58  ? 25.721  -23.249 54.359 1.00 10.39  ? 100  ILE B CG1   1 
ATOM   4314 C CG2   . ILE B 1 58  ? 26.824  -21.019 54.697 1.00 11.23  ? 100  ILE B CG2   1 
ATOM   4315 C CD1   . ILE B 1 58  ? 26.047  -23.533 52.897 1.00 11.07  ? 100  ILE B CD1   1 
ATOM   4316 N N     . VAL B 1 59  ? 24.202  -19.161 55.973 1.00 11.42  ? 101  VAL B N     1 
ATOM   4317 C CA    . VAL B 1 59  ? 24.285  -17.787 56.461 1.00 11.49  ? 101  VAL B CA    1 
ATOM   4318 C C     . VAL B 1 59  ? 23.810  -17.675 57.899 1.00 10.01  ? 101  VAL B C     1 
ATOM   4319 O O     . VAL B 1 59  ? 24.464  -16.964 58.711 1.00 11.04  ? 101  VAL B O     1 
ATOM   4320 C CB    . VAL B 1 59  ? 23.587  -16.779 55.521 1.00 11.29  ? 101  VAL B CB    1 
ATOM   4321 C CG1   . VAL B 1 59  ? 23.543  -15.396 56.143 1.00 13.05  ? 101  VAL B CG1   1 
ATOM   4322 C CG2   . VAL B 1 59  ? 24.336  -16.723 54.210 1.00 13.25  ? 101  VAL B CG2   1 
ATOM   4323 N N     . ARG B 1 60  ? 22.736  -18.344 58.277 1.00 10.67  ? 102  ARG B N     1 
ATOM   4324 C CA    . ARG B 1 60  ? 22.279  -18.306 59.674 1.00 11.27  ? 102  ARG B CA    1 
ATOM   4325 C C     . ARG B 1 60  ? 23.375  -18.842 60.592 1.00 12.78  ? 102  ARG B C     1 
ATOM   4326 O O     . ARG B 1 60  ? 23.677  -18.232 61.631 1.00 11.81  ? 102  ARG B O     1 
ATOM   4327 C CB    . ARG B 1 60  ? 20.988  -19.102 59.880 1.00 14.36  ? 102  ARG B CB    1 
ATOM   4328 C CG    . ARG B 1 60  ? 19.803  -18.451 59.172 1.00 17.71  ? 102  ARG B CG    1 
ATOM   4329 C CD    . ARG B 1 60  ? 18.592  -19.357 59.293 1.00 23.83  ? 102  ARG B CD    1 
ATOM   4330 N NE    . ARG B 1 60  ? 17.631  -18.927 58.297 1.00 32.73  ? 102  ARG B NE    1 
ATOM   4331 C CZ    . ARG B 1 60  ? 17.128  -19.678 57.329 1.00 32.14  ? 102  ARG B CZ    1 
ATOM   4332 N NH1   . ARG B 1 60  ? 17.490  -20.939 57.187 1.00 27.00  ? 102  ARG B NH1   1 
ATOM   4333 N NH2   . ARG B 1 60  ? 16.263  -19.126 56.495 1.00 38.94  ? 102  ARG B NH2   1 
ATOM   4334 N N     . ILE B 1 61  ? 24.020  -19.943 60.195 1.00 11.77  ? 103  ILE B N     1 
ATOM   4335 C CA    . ILE B 1 61  ? 25.039  -20.550 61.046 1.00 12.95  ? 103  ILE B CA    1 
ATOM   4336 C C     . ILE B 1 61  ? 26.251  -19.622 61.139 1.00 11.79  ? 103  ILE B C     1 
ATOM   4337 O O     . ILE B 1 61  ? 26.908  -19.484 62.185 1.00 11.98  ? 103  ILE B O     1 
ATOM   4338 C CB    . ILE B 1 61  ? 25.436  -21.926 60.481 1.00 12.51  ? 103  ILE B CB    1 
ATOM   4339 C CG1   . ILE B 1 61  ? 24.357  -22.982 60.695 1.00 14.68  ? 103  ILE B CG1   1 
ATOM   4340 C CG2   . ILE B 1 61  ? 26.787  -22.377 61.013 1.00 12.19  ? 103  ILE B CG2   1 
ATOM   4341 C CD1   . ILE B 1 61  ? 24.411  -24.096 59.669 1.00 15.28  ? 103  ILE B CD1   1 
ATOM   4342 N N     . ALA B 1 62  ? 26.624  -19.006 60.024 1.00 10.77  ? 104  ALA B N     1 
ATOM   4343 C CA    . ALA B 1 62  ? 27.749  -18.076 59.996 1.00 11.64  ? 104  ALA B CA    1 
ATOM   4344 C C     . ALA B 1 62  ? 27.556  -16.948 61.017 1.00 11.34  ? 104  ALA B C     1 
ATOM   4345 O O     . ALA B 1 62  ? 28.484  -16.570 61.758 1.00 13.19  ? 104  ALA B O     1 
ATOM   4346 C CB    . ALA B 1 62  ? 27.985  -17.580 58.592 1.00 11.40  ? 104  ALA B CB    1 
ATOM   4347 N N     . ASN B 1 63  ? 26.334  -16.426 61.142 1.00 10.73  ? 105  ASN B N     1 
ATOM   4348 C CA    . ASN B 1 63  ? 26.014  -15.424 62.149 1.00 10.82  ? 105  ASN B CA    1 
ATOM   4349 C C     . ASN B 1 63  ? 26.188  -15.967 63.576 1.00 9.84   ? 105  ASN B C     1 
ATOM   4350 O O     . ASN B 1 63  ? 26.830  -15.355 64.435 1.00 11.40  ? 105  ASN B O     1 
ATOM   4351 C CB    . ASN B 1 63  ? 24.618  -14.862 61.895 1.00 11.91  ? 105  ASN B CB    1 
ATOM   4352 C CG    . ASN B 1 63  ? 24.639  -13.839 60.771 1.00 12.47  ? 105  ASN B CG    1 
ATOM   4353 O OD1   . ASN B 1 63  ? 25.035  -12.682 60.930 1.00 12.89  ? 105  ASN B OD1   1 
ATOM   4354 N ND2   . ASN B 1 63  ? 24.157  -14.222 59.594 1.00 13.79  ? 105  ASN B ND2   1 
ATOM   4355 N N     . THR B 1 64  ? 25.587  -17.133 63.800 1.00 9.81   ? 106  THR B N     1 
ATOM   4356 C CA    . THR B 1 64  ? 25.635  -17.755 65.141 1.00 10.56  ? 106  THR B CA    1 
ATOM   4357 C C     . THR B 1 64  ? 27.064  -17.933 65.624 1.00 11.98  ? 106  THR B C     1 
ATOM   4358 O O     . THR B 1 64  ? 27.350  -17.663 66.775 1.00 13.34  ? 106  THR B O     1 
ATOM   4359 C CB    . THR B 1 64  ? 24.845  -19.069 65.150 1.00 12.94  ? 106  THR B CB    1 
ATOM   4360 O OG1   . THR B 1 64  ? 23.468  -18.732 64.912 1.00 13.53  ? 106  THR B OG1   1 
ATOM   4361 C CG2   . THR B 1 64  ? 24.970  -19.857 66.437 1.00 13.66  ? 106  THR B CG2   1 
ATOM   4362 N N     . TYR B 1 65  ? 27.968  -18.378 64.735 1.00 11.53  ? 107  TYR B N     1 
ATOM   4363 C CA    . TYR B 1 65  ? 29.335  -18.705 65.100 1.00 12.79  ? 107  TYR B CA    1 
ATOM   4364 C C     . TYR B 1 65  ? 30.329  -17.594 64.727 1.00 14.52  ? 107  TYR B C     1 
ATOM   4365 O O     . TYR B 1 65  ? 31.522  -17.750 64.938 1.00 17.01  ? 107  TYR B O     1 
ATOM   4366 C CB    . TYR B 1 65  ? 29.706  -20.032 64.420 1.00 14.03  ? 107  TYR B CB    1 
ATOM   4367 C CG    . TYR B 1 65  ? 29.045  -21.250 65.005 1.00 15.06  ? 107  TYR B CG    1 
ATOM   4368 C CD1   . TYR B 1 65  ? 29.476  -21.742 66.221 1.00 20.35  ? 107  TYR B CD1   1 
ATOM   4369 C CD2   . TYR B 1 65  ? 27.899  -21.788 64.476 1.00 17.87  ? 107  TYR B CD2   1 
ATOM   4370 C CE1   . TYR B 1 65  ? 28.832  -22.802 66.835 1.00 20.06  ? 107  TYR B CE1   1 
ATOM   4371 C CE2   . TYR B 1 65  ? 27.247  -22.873 65.073 1.00 19.15  ? 107  TYR B CE2   1 
ATOM   4372 C CZ    . TYR B 1 65  ? 27.699  -23.335 66.284 1.00 20.95  ? 107  TYR B CZ    1 
ATOM   4373 O OH    . TYR B 1 65  ? 27.157  -24.426 66.910 1.00 23.43  ? 107  TYR B OH    1 
ATOM   4374 N N     . LYS B 1 66  ? 29.850  -16.479 64.174 1.00 13.29  ? 108  LYS B N     1 
ATOM   4375 C CA    . LYS B 1 66  ? 30.659  -15.331 63.767 1.00 15.71  ? 108  LYS B CA    1 
ATOM   4376 C C     . LYS B 1 66  ? 31.788  -15.787 62.825 1.00 15.35  ? 108  LYS B C     1 
ATOM   4377 O O     . LYS B 1 66  ? 32.927  -15.306 62.894 1.00 15.62  ? 108  LYS B O     1 
ATOM   4378 C CB    . LYS B 1 66  ? 31.156  -14.563 65.000 1.00 17.99  ? 108  LYS B CB    1 
ATOM   4379 C CG    . LYS B 1 66  ? 30.086  -14.245 66.050 1.00 20.60  ? 108  LYS B CG    1 
ATOM   4380 C CD    . LYS B 1 66  ? 28.963  -13.337 65.565 1.00 25.03  ? 108  LYS B CD    1 
ATOM   4381 C CE    . LYS B 1 66  ? 27.870  -13.018 66.596 1.00 27.16  ? 108  LYS B CE    1 
ATOM   4382 N NZ    . LYS B 1 66  ? 26.877  -14.095 66.895 1.00 21.10  ? 108  LYS B NZ    1 
ATOM   4383 N N     . GLN B 1 67  ? 31.459  -16.666 61.875 1.00 13.43  ? 109  GLN B N     1 
ATOM   4384 C CA    . GLN B 1 67  ? 32.417  -17.211 60.933 1.00 11.83  ? 109  GLN B CA    1 
ATOM   4385 C C     . GLN B 1 67  ? 32.209  -16.586 59.551 1.00 12.38  ? 109  GLN B C     1 
ATOM   4386 O O     . GLN B 1 67  ? 31.191  -16.857 58.908 1.00 13.59  ? 109  GLN B O     1 
ATOM   4387 C CB    . GLN B 1 67  ? 32.239  -18.719 60.807 1.00 12.01  ? 109  GLN B CB    1 
ATOM   4388 C CG    . GLN B 1 67  ? 33.075  -19.384 59.729 1.00 12.46  ? 109  GLN B CG    1 
ATOM   4389 C CD    . GLN B 1 67  ? 34.553  -19.112 59.887 1.00 14.28  ? 109  GLN B CD    1 
ATOM   4390 O OE1   . GLN B 1 67  ? 35.159  -19.414 60.921 1.00 16.66  ? 109  GLN B OE1   1 
ATOM   4391 N NE2   . GLN B 1 67  ? 35.142  -18.387 58.957 1.00 12.49  ? 109  GLN B NE2   1 
ATOM   4392 N N     . PRO B 1 68  ? 33.129  -15.733 59.096 1.00 11.77  ? 110  PRO B N     1 
ATOM   4393 C CA    . PRO B 1 68  ? 32.977  -15.087 57.797 1.00 12.87  ? 110  PRO B CA    1 
ATOM   4394 C C     . PRO B 1 68  ? 33.092  -16.015 56.615 1.00 11.50  ? 110  PRO B C     1 
ATOM   4395 O O     . PRO B 1 68  ? 33.792  -17.031 56.672 1.00 11.76  ? 110  PRO B O     1 
ATOM   4396 C CB    . PRO B 1 68  ? 34.108  -14.054 57.711 1.00 14.73  ? 110  PRO B CB    1 
ATOM   4397 C CG    . PRO B 1 68  ? 34.502  -13.837 59.141 1.00 17.84  ? 110  PRO B CG    1 
ATOM   4398 C CD    . PRO B 1 68  ? 34.209  -15.124 59.899 1.00 13.32  ? 110  PRO B CD    1 
ATOM   4399 N N     . LEU B 1 69  ? 32.324  -15.670 55.571 1.00 10.76  ? 111  LEU B N     1 
ATOM   4400 C CA    . LEU B 1 69  ? 32.192  -16.413 54.312 1.00 10.82  ? 111  LEU B CA    1 
ATOM   4401 C C     . LEU B 1 69  ? 32.719  -15.533 53.201 1.00 11.43  ? 111  LEU B C     1 
ATOM   4402 O O     . LEU B 1 69  ? 32.249  -14.403 53.083 1.00 12.65  ? 111  LEU B O     1 
ATOM   4403 C CB    . LEU B 1 69  ? 30.706  -16.630 54.043 1.00 11.56  ? 111  LEU B CB    1 
ATOM   4404 C CG    . LEU B 1 69  ? 29.998  -17.458 55.102 1.00 13.43  ? 111  LEU B CG    1 
ATOM   4405 C CD1   . LEU B 1 69  ? 28.516  -17.537 54.873 1.00 15.15  ? 111  LEU B CD1   1 
ATOM   4406 C CD2   . LEU B 1 69  ? 30.556  -18.881 55.162 1.00 16.23  ? 111  LEU B CD2   1 
ATOM   4407 N N     . TRP B 1 70  ? 33.538  -16.095 52.333 1.00 9.91   ? 112  TRP B N     1 
ATOM   4408 C CA    . TRP B 1 70  ? 33.979  -15.396 51.119 1.00 9.84   ? 112  TRP B CA    1 
ATOM   4409 C C     . TRP B 1 70  ? 33.292  -16.005 49.907 1.00 9.95   ? 112  TRP B C     1 
ATOM   4410 O O     . TRP B 1 70  ? 33.652  -17.104 49.501 1.00 11.09  ? 112  TRP B O     1 
ATOM   4411 C CB    . TRP B 1 70  ? 35.516  -15.482 50.996 1.00 9.90   ? 112  TRP B CB    1 
ATOM   4412 C CG    . TRP B 1 70  ? 36.106  -14.693 49.864 1.00 10.53  ? 112  TRP B CG    1 
ATOM   4413 C CD1   . TRP B 1 70  ? 36.395  -15.202 48.623 1.00 11.66  ? 112  TRP B CD1   1 
ATOM   4414 C CD2   . TRP B 1 70  ? 36.421  -13.283 49.824 1.00 10.15  ? 112  TRP B CD2   1 
ATOM   4415 N NE1   . TRP B 1 70  ? 36.842  -14.185 47.809 1.00 12.01  ? 112  TRP B NE1   1 
ATOM   4416 C CE2   . TRP B 1 70  ? 36.926  -13.018 48.536 1.00 11.16  ? 112  TRP B CE2   1 
ATOM   4417 C CE3   . TRP B 1 70  ? 36.428  -12.236 50.754 1.00 9.78   ? 112  TRP B CE3   1 
ATOM   4418 C CZ2   . TRP B 1 70  ? 37.303  -11.753 48.112 1.00 11.18  ? 112  TRP B CZ2   1 
ATOM   4419 C CZ3   . TRP B 1 70  ? 36.839  -10.982 50.333 1.00 11.81  ? 112  TRP B CZ3   1 
ATOM   4420 C CH2   . TRP B 1 70  ? 37.250  -10.726 49.014 1.00 11.35  ? 112  TRP B CH2   1 
ATOM   4421 N N     . THR B 1 71  ? 32.264  -15.338 49.360 1.00 10.09  ? 113  THR B N     1 
ATOM   4422 C CA    . THR B 1 71  ? 31.376  -15.910 48.355 1.00 10.54  ? 113  THR B CA    1 
ATOM   4423 C C     . THR B 1 71  ? 31.940  -15.754 46.966 1.00 10.46  ? 113  THR B C     1 
ATOM   4424 O O     . THR B 1 71  ? 32.374  -14.666 46.598 1.00 10.90  ? 113  THR B O     1 
ATOM   4425 C CB    . THR B 1 71  ? 29.967  -15.314 48.417 1.00 11.73  ? 113  THR B CB    1 
ATOM   4426 O OG1   . THR B 1 71  ? 29.463  -15.562 49.737 1.00 12.29  ? 113  THR B OG1   1 
ATOM   4427 C CG2   . THR B 1 71  ? 29.003  -15.925 47.426 1.00 11.85  ? 113  THR B CG2   1 
ATOM   4428 N N     . VAL B 1 72  ? 31.953  -16.876 46.230 1.00 10.22  ? 114  VAL B N     1 
ATOM   4429 C CA    . VAL B 1 72  ? 32.298  -16.894 44.811 1.00 10.77  ? 114  VAL B CA    1 
ATOM   4430 C C     . VAL B 1 72  ? 31.279  -17.706 44.036 1.00 10.53  ? 114  VAL B C     1 
ATOM   4431 O O     . VAL B 1 72  ? 30.502  -18.469 44.595 1.00 10.99  ? 114  VAL B O     1 
ATOM   4432 C CB    . VAL B 1 72  ? 33.707  -17.438 44.647 1.00 10.56  ? 114  VAL B CB    1 
ATOM   4433 C CG1   . VAL B 1 72  ? 34.691  -16.686 45.523 1.00 10.54  ? 114  VAL B CG1   1 
ATOM   4434 C CG2   . VAL B 1 72  ? 33.787  -18.915 44.906 1.00 11.65  ? 114  VAL B CG2   1 
ATOM   4435 N N     . SER B 1 73  ? 31.287  -17.480 42.739 1.00 12.55  ? 115  SER B N     1 
ATOM   4436 C CA    . SER B 1 73  ? 30.417  -18.197 41.814 1.00 13.12  ? 115  SER B CA    1 
ATOM   4437 C C     . SER B 1 73  ? 31.205  -19.372 41.237 1.00 15.49  ? 115  SER B C     1 
ATOM   4438 O O     . SER B 1 73  ? 30.916  -20.504 41.608 1.00 20.74  ? 115  SER B O     1 
ATOM   4439 C CB    . SER B 1 73  ? 29.835  -17.304 40.735 1.00 12.90  ? 115  SER B CB    1 
ATOM   4440 O OG    . SER B 1 73  ? 28.883  -16.402 41.268 1.00 14.27  ? 115  SER B OG    1 
ATOM   4441 N N     . THR B 1 74  ? 32.113  -19.170 40.275 1.00 11.80  ? 116  THR B N     1 
ATOM   4442 C CA    . THR B 1 74  ? 33.001  -20.231 39.825 1.00 14.33  ? 116  THR B CA    1 
ATOM   4443 C C     . THR B 1 74  ? 34.386  -19.997 40.380 1.00 13.41  ? 116  THR B C     1 
ATOM   4444 O O     . THR B 1 74  ? 35.254  -20.856 40.299 1.00 14.84  ? 116  THR B O     1 
ATOM   4445 C CB    . THR B 1 74  ? 32.933  -20.398 38.308 1.00 13.96  ? 116  THR B CB    1 
ATOM   4446 O OG1   . THR B 1 74  ? 32.905  -19.161 37.617 1.00 14.70  ? 116  THR B OG1   1 
ATOM   4447 C CG2   . THR B 1 74  ? 31.660  -21.132 37.895 1.00 15.18  ? 116  THR B CG2   1 
ATOM   4448 N N     . GLY B 1 75  ? 34.662  -18.756 40.861 1.00 13.01  ? 117  GLY B N     1 
ATOM   4449 C CA    . GLY B 1 75  ? 35.980  -18.506 41.463 1.00 13.00  ? 117  GLY B CA    1 
ATOM   4450 C C     . GLY B 1 75  ? 37.174  -18.443 40.498 1.00 13.81  ? 117  GLY B C     1 
ATOM   4451 O O     . GLY B 1 75  ? 38.334  -18.753 40.864 1.00 16.38  ? 117  GLY B O     1 
ATOM   4452 N N     . LYS B 1 76  ? 36.996  -17.972 39.283 1.00 12.67  ? 118  LYS B N     1 
ATOM   4453 C CA    . LYS B 1 76  ? 38.098  -17.943 38.338 1.00 14.14  ? 118  LYS B CA    1 
ATOM   4454 C C     . LYS B 1 76  ? 38.577  -16.512 38.133 1.00 11.93  ? 118  LYS B C     1 
ATOM   4455 O O     . LYS B 1 76  ? 38.902  -16.112 36.998 1.00 11.71  ? 118  LYS B O     1 
ATOM   4456 C CB    . LYS B 1 76  ? 37.627  -18.612 37.047 1.00 14.68  ? 118  LYS B CB    1 
ATOM   4457 C CG    . LYS B 1 76  ? 37.114  -20.045 37.212 1.00 18.20  ? 118  LYS B CG    1 
ATOM   4458 C CD    . LYS B 1 76  ? 38.174  -20.977 37.780 1.00 22.70  ? 118  LYS B CD    1 
ATOM   4459 C CE    . LYS B 1 76  ? 37.815  -22.446 37.693 1.00 30.93  ? 118  LYS B CE    1 
ATOM   4460 N NZ    . LYS B 1 76  ? 37.755  -23.090 39.017 1.00 35.13  ? 118  LYS B NZ    1 
ATOM   4461 N N     . ASN B 1 77  ? 38.666  -15.746 39.225 1.00 12.00  ? 119  ASN B N     1 
ATOM   4462 C CA    . ASN B 1 77  ? 39.095  -14.351 39.190 1.00 11.04  ? 119  ASN B CA    1 
ATOM   4463 C C     . ASN B 1 77  ? 40.624  -14.301 39.108 1.00 10.41  ? 119  ASN B C     1 
ATOM   4464 O O     . ASN B 1 77  ? 41.317  -13.765 39.954 1.00 10.12  ? 119  ASN B O     1 
ATOM   4465 C CB    . ASN B 1 77  ? 38.487  -13.586 40.367 1.00 10.98  ? 119  ASN B CB    1 
ATOM   4466 C CG    . ASN B 1 77  ? 38.022  -12.180 40.059 1.00 11.90  ? 119  ASN B CG    1 
ATOM   4467 O OD1   . ASN B 1 77  ? 37.869  -11.758 38.913 1.00 11.35  ? 119  ASN B OD1   1 
ATOM   4468 N ND2   . ASN B 1 77  ? 37.719  -11.422 41.109 1.00 13.51  ? 119  ASN B ND2   1 
ATOM   4469 N N     . MET B 1 78  ? 41.131  -14.775 37.975 1.00 10.33  ? 120  MET B N     1 
ATOM   4470 C CA    . MET B 1 78  ? 42.559  -14.988 37.792 1.00 11.20  ? 120  MET B CA    1 
ATOM   4471 C C     . MET B 1 78  ? 43.252  -13.638 37.532 1.00 10.83  ? 120  MET B C     1 
ATOM   4472 O O     . MET B 1 78  ? 42.833  -12.892 36.656 1.00 11.54  ? 120  MET B O     1 
ATOM   4473 C CB    . MET B 1 78  ? 42.791  -15.958 36.627 1.00 14.49  ? 120  MET B CB    1 
ATOM   4474 C CG    . MET B 1 78  ? 44.242  -16.233 36.354 1.00 16.66  ? 120  MET B CG    1 
ATOM   4475 S SD    . MET B 1 78  ? 44.446  -17.583 35.094 1.00 20.35  ? 120  MET B SD    1 
ATOM   4476 C CE    . MET B 1 78  ? 43.931  -19.033 36.003 1.00 23.25  ? 120  MET B CE    1 
ATOM   4477 N N     . GLY B 1 79  ? 44.281  -13.341 38.333 1.00 9.79   ? 121  GLY B N     1 
ATOM   4478 C CA    . GLY B 1 79  ? 44.940  -12.056 38.408 1.00 11.29  ? 121  GLY B CA    1 
ATOM   4479 C C     . GLY B 1 79  ? 44.322  -11.067 39.379 1.00 10.31  ? 121  GLY B C     1 
ATOM   4480 O O     . GLY B 1 79  ? 44.835  -9.977  39.558 1.00 10.67  ? 121  GLY B O     1 
ATOM   4481 N N     . TYR B 1 80  ? 43.223  -11.491 40.009 1.00 10.37  ? 122  TYR B N     1 
ATOM   4482 C CA    . TYR B 1 80  ? 42.479  -10.702 40.999 1.00 10.02  ? 122  TYR B CA    1 
ATOM   4483 C C     . TYR B 1 80  ? 42.354  -11.447 42.337 1.00 9.97   ? 122  TYR B C     1 
ATOM   4484 O O     . TYR B 1 80  ? 41.652  -10.979 43.225 1.00 11.23  ? 122  TYR B O     1 
ATOM   4485 C CB    . TYR B 1 80  ? 41.096  -10.296 40.461 1.00 11.13  ? 122  TYR B CB    1 
ATOM   4486 C CG    . TYR B 1 80  ? 41.070  -9.251  39.347 1.00 10.61  ? 122  TYR B CG    1 
ATOM   4487 C CD1   . TYR B 1 80  ? 41.669  -8.025  39.475 1.00 10.34  ? 122  TYR B CD1   1 
ATOM   4488 C CD2   . TYR B 1 80  ? 40.430  -9.507  38.111 1.00 11.58  ? 122  TYR B CD2   1 
ATOM   4489 C CE1   . TYR B 1 80  ? 41.631  -7.062  38.465 1.00 9.88   ? 122  TYR B CE1   1 
ATOM   4490 C CE2   . TYR B 1 80  ? 40.366  -8.553  37.090 1.00 11.27  ? 122  TYR B CE2   1 
ATOM   4491 C CZ    . TYR B 1 80  ? 40.998  -7.321  37.256 1.00 10.51  ? 122  TYR B CZ    1 
ATOM   4492 O OH    . TYR B 1 80  ? 40.969  -6.297  36.296 1.00 11.12  ? 122  TYR B OH    1 
ATOM   4493 N N     . GLY B 1 81  ? 42.966  -12.617 42.470 1.00 9.89   ? 123  GLY B N     1 
ATOM   4494 C CA    . GLY B 1 81  ? 42.909  -13.368 43.703 1.00 9.73   ? 123  GLY B CA    1 
ATOM   4495 C C     . GLY B 1 81  ? 42.285  -14.748 43.654 1.00 11.41  ? 123  GLY B C     1 
ATOM   4496 O O     . GLY B 1 81  ? 42.302  -15.401 44.699 1.00 11.13  ? 123  GLY B O     1 
ATOM   4497 N N     . MET B 1 82  ? 41.706  -15.172 42.533 1.00 11.24  ? 124  MET B N     1 
ATOM   4498 C CA    . MET B 1 82  ? 41.094  -16.502 42.464 1.00 11.53  ? 124  MET B CA    1 
ATOM   4499 C C     . MET B 1 82  ? 40.027  -16.646 43.576 1.00 12.06  ? 124  MET B C     1 
ATOM   4500 O O     . MET B 1 82  ? 39.132  -15.788 43.690 1.00 12.35  ? 124  MET B O     1 
ATOM   4501 C CB    . MET B 1 82  ? 42.177  -17.598 42.431 1.00 12.26  ? 124  MET B CB    1 
ATOM   4502 C CG    . MET B 1 82  ? 43.016  -17.616 41.140 1.00 14.40  ? 124  MET B CG    1 
ATOM   4503 S SD    . MET B 1 82  ? 42.130  -17.872 39.609 1.00 14.13  ? 124  MET B SD    1 
ATOM   4504 C CE    . MET B 1 82  ? 41.479  -19.519 39.807 1.00 12.45  ? 124  MET B CE    1 
ATOM   4505 N N     . THR B 1 83  ? 40.165  -17.627 44.463 1.00 11.66  ? 125  THR B N     1 
ATOM   4506 C CA    . THR B 1 83  ? 39.244  -17.764 45.587 1.00 12.84  ? 125  THR B CA    1 
ATOM   4507 C C     . THR B 1 83  ? 39.883  -17.411 46.912 1.00 12.90  ? 125  THR B C     1 
ATOM   4508 O O     . THR B 1 83  ? 39.360  -17.828 47.960 1.00 13.31  ? 125  THR B O     1 
ATOM   4509 C CB    . THR B 1 83  ? 38.598  -19.160 45.635 1.00 12.19  ? 125  THR B CB    1 
ATOM   4510 O OG1   . THR B 1 83  ? 39.587  -20.171 45.659 1.00 13.11  ? 125  THR B OG1   1 
ATOM   4511 C CG2   . THR B 1 83  ? 37.734  -19.396 44.426 1.00 13.98  ? 125  THR B CG2   1 
ATOM   4512 N N     . ALA B 1 84  ? 40.947  -16.618 46.919 1.00 11.50  ? 126  ALA B N     1 
ATOM   4513 C CA    . ALA B 1 84  ? 41.576  -16.298 48.174 1.00 12.53  ? 126  ALA B CA    1 
ATOM   4514 C C     . ALA B 1 84  ? 40.852  -15.123 48.804 1.00 12.57  ? 126  ALA B C     1 
ATOM   4515 O O     . ALA B 1 84  ? 40.662  -14.111 48.107 1.00 12.25  ? 126  ALA B O     1 
ATOM   4516 C CB    . ALA B 1 84  ? 43.006  -15.930 47.966 1.00 12.78  ? 126  ALA B CB    1 
ATOM   4517 N N     . PRO B 1 85  ? 40.454  -15.202 50.100 1.00 12.33  ? 127  PRO B N     1 
ATOM   4518 C CA    . PRO B 1 85  ? 39.810  -14.061 50.739 1.00 11.76  ? 127  PRO B CA    1 
ATOM   4519 C C     . PRO B 1 85  ? 40.726  -12.888 51.054 1.00 13.66  ? 127  PRO B C     1 
ATOM   4520 O O     . PRO B 1 85  ? 41.937  -13.029 51.132 1.00 12.53  ? 127  PRO B O     1 
ATOM   4521 C CB    . PRO B 1 85  ? 39.220  -14.671 52.013 1.00 11.88  ? 127  PRO B CB    1 
ATOM   4522 C CG    . PRO B 1 85  ? 39.139  -16.151 51.716 1.00 13.08  ? 127  PRO B CG    1 
ATOM   4523 C CD    . PRO B 1 85  ? 40.415  -16.415 50.964 1.00 11.43  ? 127  PRO B CD    1 
ATOM   4524 N N     . ALA B 1 86  ? 40.129  -11.691 51.188 1.00 13.47  ? 128  ALA B N     1 
ATOM   4525 C CA    . ALA B 1 86  ? 40.909  -10.512 51.480 1.00 11.72  ? 128  ALA B CA    1 
ATOM   4526 C C     . ALA B 1 86  ? 41.478  -10.435 52.885 1.00 13.48  ? 128  ALA B C     1 
ATOM   4527 O O     . ALA B 1 86  ? 42.454  -9.691  53.078 1.00 15.12  ? 128  ALA B O     1 
ATOM   4528 C CB    . ALA B 1 86  ? 40.070  -9.283  51.197 1.00 13.69  ? 128  ALA B CB    1 
ATOM   4529 N N     . THR B 1 87  ? 40.878  -11.112 53.859 1.00 12.53  ? 129  THR B N     1 
ATOM   4530 C CA    . THR B 1 87  ? 41.404  -11.062 55.216 1.00 13.17  ? 129  THR B CA    1 
ATOM   4531 C C     . THR B 1 87  ? 41.497  -12.504 55.702 1.00 13.55  ? 129  THR B C     1 
ATOM   4532 O O     . THR B 1 87  ? 40.845  -13.411 55.176 1.00 12.16  ? 129  THR B O     1 
ATOM   4533 C CB    . THR B 1 87  ? 40.517  -10.209 56.142 1.00 13.56  ? 129  THR B CB    1 
ATOM   4534 O OG1   . THR B 1 87  ? 39.281  -10.853 56.431 1.00 14.05  ? 129  THR B OG1   1 
ATOM   4535 C CG2   . THR B 1 87  ? 40.256  -8.826  55.604 1.00 13.50  ? 129  THR B CG2   1 
ATOM   4536 N N     . PRO B 1 88  ? 42.249  -12.751 56.799 1.00 14.93  ? 130  PRO B N     1 
ATOM   4537 C CA    . PRO B 1 88  ? 42.465  -14.116 57.273 1.00 15.33  ? 130  PRO B CA    1 
ATOM   4538 C C     . PRO B 1 88  ? 41.246  -14.732 57.917 1.00 13.38  ? 130  PRO B C     1 
ATOM   4539 O O     . PRO B 1 88  ? 40.383  -14.015 58.437 1.00 15.61  ? 130  PRO B O     1 
ATOM   4540 C CB    . PRO B 1 88  ? 43.570  -13.949 58.341 1.00 16.58  ? 130  PRO B CB    1 
ATOM   4541 C CG    . PRO B 1 88  ? 44.252  -12.646 57.926 1.00 17.26  ? 130  PRO B CG    1 
ATOM   4542 C CD    . PRO B 1 88  ? 43.098  -11.764 57.487 1.00 16.09  ? 130  PRO B CD    1 
ATOM   4543 N N     . GLY B 1 89  ? 41.189  -16.059 57.872 1.00 13.45  ? 131  GLY B N     1 
ATOM   4544 C CA    . GLY B 1 89  ? 40.247  -16.786 58.693 1.00 12.82  ? 131  GLY B CA    1 
ATOM   4545 C C     . GLY B 1 89  ? 38.869  -16.960 58.042 1.00 13.13  ? 131  GLY B C     1 
ATOM   4546 O O     . GLY B 1 89  ? 37.909  -17.295 58.733 1.00 14.29  ? 131  GLY B O     1 
ATOM   4547 N N     . GLN B 1 90  ? 38.750  -16.719 56.732 1.00 11.29  ? 132  GLN B N     1 
ATOM   4548 C CA    . GLN B 1 90  ? 37.455  -16.891 56.062 1.00 12.05  ? 132  GLN B CA    1 
ATOM   4549 C C     . GLN B 1 90  ? 37.261  -18.269 55.380 1.00 12.85  ? 132  GLN B C     1 
ATOM   4550 O O     . GLN B 1 90  ? 38.219  -18.906 54.962 1.00 12.45  ? 132  GLN B O     1 
ATOM   4551 C CB    . GLN B 1 90  ? 37.281  -15.830 54.982 1.00 12.04  ? 132  GLN B CB    1 
ATOM   4552 C CG    . GLN B 1 90  ? 37.456  -14.398 55.484 1.00 11.40  ? 132  GLN B CG    1 
ATOM   4553 C CD    . GLN B 1 90  ? 37.014  -13.294 54.534 1.00 12.19  ? 132  GLN B CD    1 
ATOM   4554 O OE1   . GLN B 1 90  ? 37.586  -12.197 54.428 1.00 15.45  ? 132  GLN B OE1   1 
ATOM   4555 N NE2   . GLN B 1 90  ? 35.938  -13.538 53.878 1.00 9.25   ? 132  GLN B NE2   1 
ATOM   4556 N N     . VAL B 1 91  ? 35.981  -18.685 55.272 1.00 11.28  ? 133  VAL B N     1 
ATOM   4557 C CA    . VAL B 1 91  ? 35.586  -19.895 54.583 1.00 11.61  ? 133  VAL B CA    1 
ATOM   4558 C C     . VAL B 1 91  ? 35.009  -19.507 53.242 1.00 11.04  ? 133  VAL B C     1 
ATOM   4559 O O     . VAL B 1 91  ? 34.119  -18.638 53.182 1.00 11.49  ? 133  VAL B O     1 
ATOM   4560 C CB    . VAL B 1 91  ? 34.570  -20.688 55.428 1.00 10.85  ? 133  VAL B CB    1 
ATOM   4561 C CG1   . VAL B 1 91  ? 33.900  -21.815 54.660 1.00 10.62  ? 133  VAL B CG1   1 
ATOM   4562 C CG2   . VAL B 1 91  ? 35.184  -21.210 56.740 1.00 11.98  ? 133  VAL B CG2   1 
ATOM   4563 N N     . VAL B 1 92  ? 35.493  -20.161 52.169 1.00 9.89   ? 134  VAL B N     1 
ATOM   4564 C CA    . VAL B 1 92  ? 34.947  -19.866 50.867 1.00 11.05  ? 134  VAL B CA    1 
ATOM   4565 C C     . VAL B 1 92  ? 33.556  -20.445 50.793 1.00 10.74  ? 134  VAL B C     1 
ATOM   4566 O O     . VAL B 1 92  ? 33.350  -21.599 51.116 1.00 12.34  ? 134  VAL B O     1 
ATOM   4567 C CB    . VAL B 1 92  ? 35.844  -20.362 49.728 1.00 11.16  ? 134  VAL B CB    1 
ATOM   4568 C CG1   . VAL B 1 92  ? 35.235  -20.093 48.364 1.00 12.89  ? 134  VAL B CG1   1 
ATOM   4569 C CG2   . VAL B 1 92  ? 37.209  -19.812 49.807 1.00 12.73  ? 134  VAL B CG2   1 
ATOM   4570 N N     . LEU B 1 93  ? 32.583  -19.624 50.364 1.00 11.55  ? 135  LEU B N     1 
ATOM   4571 C CA    . LEU B 1 93  ? 31.234  -20.067 50.055 1.00 12.12  ? 135  LEU B CA    1 
ATOM   4572 C C     . LEU B 1 93  ? 31.179  -20.202 48.533 1.00 10.91  ? 135  LEU B C     1 
ATOM   4573 O O     . LEU B 1 93  ? 31.118  -19.218 47.785 1.00 10.81  ? 135  LEU B O     1 
ATOM   4574 C CB    . LEU B 1 93  ? 30.161  -19.087 50.626 1.00 11.17  ? 135  LEU B CB    1 
ATOM   4575 C CG    . LEU B 1 93  ? 28.735  -19.424 50.184 1.00 14.09  ? 135  LEU B CG    1 
ATOM   4576 C CD1   . LEU B 1 93  ? 28.323  -20.795 50.627 1.00 14.28  ? 135  LEU B CD1   1 
ATOM   4577 C CD2   . LEU B 1 93  ? 27.747  -18.397 50.662 1.00 14.81  ? 135  LEU B CD2   1 
ATOM   4578 N N     . ASP B 1 94  ? 31.369  -21.433 48.055 1.00 9.91   ? 136  ASP B N     1 
ATOM   4579 C CA    . ASP B 1 94  ? 31.619  -21.708 46.646 1.00 11.22  ? 136  ASP B CA    1 
ATOM   4580 C C     . ASP B 1 94  ? 30.317  -22.187 46.026 1.00 11.48  ? 136  ASP B C     1 
ATOM   4581 O O     . ASP B 1 94  ? 29.790  -23.233 46.425 1.00 12.00  ? 136  ASP B O     1 
ATOM   4582 C CB    . ASP B 1 94  ? 32.641  -22.826 46.516 1.00 13.21  ? 136  ASP B CB    1 
ATOM   4583 C CG    . ASP B 1 94  ? 33.100  -23.117 45.113 1.00 16.26  ? 136  ASP B CG    1 
ATOM   4584 O OD1   . ASP B 1 94  ? 32.354  -22.756 44.167 1.00 18.19  ? 136  ASP B OD1   1 
ATOM   4585 O OD2   . ASP B 1 94  ? 34.188  -23.773 44.986 1.00 18.02  ? 136  ASP B OD2   1 
ATOM   4586 N N     . LEU B 1 95  ? 29.711  -21.394 45.142 1.00 10.14  ? 137  LEU B N     1 
ATOM   4587 C CA    . LEU B 1 95  ? 28.360  -21.654 44.628 1.00 10.39  ? 137  LEU B CA    1 
ATOM   4588 C C     . LEU B 1 95  ? 28.377  -22.387 43.290 1.00 11.47  ? 137  LEU B C     1 
ATOM   4589 O O     . LEU B 1 95  ? 27.346  -22.408 42.622 1.00 11.28  ? 137  LEU B O     1 
ATOM   4590 C CB    . LEU B 1 95  ? 27.595  -20.319 44.490 1.00 10.30  ? 137  LEU B CB    1 
ATOM   4591 C CG    . LEU B 1 95  ? 27.493  -19.519 45.783 1.00 11.01  ? 137  LEU B CG    1 
ATOM   4592 C CD1   . LEU B 1 95  ? 26.695  -18.277 45.560 1.00 11.14  ? 137  LEU B CD1   1 
ATOM   4593 C CD2   . LEU B 1 95  ? 26.881  -20.338 46.929 1.00 12.21  ? 137  LEU B CD2   1 
ATOM   4594 N N     . LYS B 1 96  ? 29.456  -23.092 42.968 1.00 11.27  ? 138  LYS B N     1 
ATOM   4595 C CA    . LYS B 1 96  ? 29.588  -23.748 41.677 1.00 12.13  ? 138  LYS B CA    1 
ATOM   4596 C C     . LYS B 1 96  ? 28.525  -24.818 41.438 1.00 11.51  ? 138  LYS B C     1 
ATOM   4597 O O     . LYS B 1 96  ? 28.173  -25.036 40.291 1.00 12.29  ? 138  LYS B O     1 
ATOM   4598 C CB    . LYS B 1 96  ? 30.941  -24.411 41.460 1.00 12.70  ? 138  LYS B CB    1 
ATOM   4599 C CG    . LYS B 1 96  ? 31.275  -25.530 42.421 1.00 14.80  ? 138  LYS B CG    1 
ATOM   4600 C CD    . LYS B 1 96  ? 32.671  -26.052 42.215 1.00 18.41  ? 138  LYS B CD    1 
ATOM   4601 C CE    . LYS B 1 96  ? 32.988  -27.185 43.166 1.00 22.53  ? 138  LYS B CE    1 
ATOM   4602 N NZ    . LYS B 1 96  ? 34.319  -27.745 42.831 1.00 23.97  ? 138  LYS B NZ    1 
ATOM   4603 N N     . ARG B 1 97  ? 27.985  -25.459 42.463 1.00 11.33  ? 139  ARG B N     1 
ATOM   4604 C CA    . ARG B 1 97  ? 26.971  -26.491 42.245 1.00 13.37  ? 139  ARG B CA    1 
ATOM   4605 C C     . ARG B 1 97  ? 25.570  -25.898 42.027 1.00 13.15  ? 139  ARG B C     1 
ATOM   4606 O O     . ARG B 1 97  ? 24.659  -26.629 41.616 1.00 12.98  ? 139  ARG B O     1 
ATOM   4607 C CB    . ARG B 1 97  ? 26.930  -27.491 43.394 1.00 12.87  ? 139  ARG B CB    1 
ATOM   4608 C CG    . ARG B 1 97  ? 28.247  -28.165 43.708 1.00 13.53  ? 139  ARG B CG    1 
ATOM   4609 C CD    . ARG B 1 97  ? 28.132  -28.880 45.058 1.00 14.88  ? 139  ARG B CD    1 
ATOM   4610 N NE    . ARG B 1 97  ? 27.196  -30.000 45.025 1.00 15.77  ? 139  ARG B NE    1 
ATOM   4611 C CZ    . ARG B 1 97  ? 26.391  -30.392 46.018 1.00 13.75  ? 139  ARG B CZ    1 
ATOM   4612 N NH1   . ARG B 1 97  ? 26.353  -29.799 47.180 1.00 16.08  ? 139  ARG B NH1   1 
ATOM   4613 N NH2   . ARG B 1 97  ? 25.581  -31.405 45.838 1.00 17.32  ? 139  ARG B NH2   1 
ATOM   4614 N N     . MET B 1 98  ? 25.370  -24.590 42.296 1.00 12.85  ? 140  MET B N     1 
ATOM   4615 C CA    . MET B 1 98  ? 24.118  -23.927 41.970 1.00 12.33  ? 140  MET B CA    1 
ATOM   4616 C C     . MET B 1 98  ? 24.223  -23.465 40.526 1.00 12.03  ? 140  MET B C     1 
ATOM   4617 O O     . MET B 1 98  ? 24.476  -22.281 40.240 1.00 12.32  ? 140  MET B O     1 
ATOM   4618 C CB    . MET B 1 98  ? 23.891  -22.756 42.933 1.00 12.46  ? 140  MET B CB    1 
ATOM   4619 C CG    . MET B 1 98  ? 23.500  -23.195 44.314 1.00 14.82  ? 140  MET B CG    1 
ATOM   4620 S SD    . MET B 1 98  ? 23.309  -21.844 45.517 1.00 17.67  ? 140  MET B SD    1 
ATOM   4621 C CE    . MET B 1 98  ? 21.925  -20.947 44.813 1.00 14.14  ? 140  MET B CE    1 
ATOM   4622 N N     . ASN B 1 99  ? 24.030  -24.388 39.608 1.00 10.65  ? 141  ASN B N     1 
ATOM   4623 C CA    . ASN B 1 99  ? 24.341  -24.158 38.205 1.00 9.61   ? 141  ASN B CA    1 
ATOM   4624 C C     . ASN B 1 99  ? 23.151  -24.250 37.290 1.00 11.55  ? 141  ASN B C     1 
ATOM   4625 O O     . ASN B 1 99  ? 23.298  -24.705 36.156 1.00 12.93  ? 141  ASN B O     1 
ATOM   4626 C CB    . ASN B 1 99  ? 25.457  -25.038 37.721 1.00 12.37  ? 141  ASN B CB    1 
ATOM   4627 C CG    . ASN B 1 99  ? 25.053  -26.494 37.716 1.00 14.14  ? 141  ASN B CG    1 
ATOM   4628 O OD1   . ASN B 1 99  ? 24.042  -26.909 38.305 1.00 14.17  ? 141  ASN B OD1   1 
ATOM   4629 N ND2   . ASN B 1 99  ? 25.916  -27.249 37.082 1.00 18.39  ? 141  ASN B ND2   1 
ATOM   4630 N N     . ARG B 1 100 ? 21.967  -23.913 37.784 1.00 11.27  ? 142  ARG B N     1 
ATOM   4631 C CA    . ARG B 1 100 ? 20.758  -24.043 37.006 1.00 11.71  ? 142  ARG B CA    1 
ATOM   4632 C C     . ARG B 1 100 ? 20.507  -22.827 36.121 1.00 10.22  ? 142  ARG B C     1 
ATOM   4633 O O     . ARG B 1 100 ? 20.524  -21.661 36.555 1.00 11.77  ? 142  ARG B O     1 
ATOM   4634 C CB    . ARG B 1 100 ? 19.588  -24.302 37.950 1.00 11.60  ? 142  ARG B CB    1 
ATOM   4635 C CG    . ARG B 1 100 ? 19.750  -25.551 38.791 1.00 12.06  ? 142  ARG B CG    1 
ATOM   4636 C CD    . ARG B 1 100 ? 18.735  -25.581 39.914 1.00 12.32  ? 142  ARG B CD    1 
ATOM   4637 N NE    . ARG B 1 100 ? 18.931  -26.692 40.815 1.00 13.75  ? 142  ARG B NE    1 
ATOM   4638 C CZ    . ARG B 1 100 ? 19.733  -26.673 41.834 1.00 14.36  ? 142  ARG B CZ    1 
ATOM   4639 N NH1   . ARG B 1 100 ? 20.368  -25.549 42.161 1.00 14.08  ? 142  ARG B NH1   1 
ATOM   4640 N NH2   . ARG B 1 100 ? 19.823  -27.729 42.604 1.00 15.09  ? 142  ARG B NH2   1 
ATOM   4641 N N     . ILE B 1 101 ? 20.227  -23.095 34.842 1.00 12.04  ? 143  ILE B N     1 
ATOM   4642 C CA    . ILE B 1 101 ? 19.642  -22.076 33.977 1.00 11.36  ? 143  ILE B CA    1 
ATOM   4643 C C     . ILE B 1 101 ? 18.152  -22.101 34.275 1.00 12.40  ? 143  ILE B C     1 
ATOM   4644 O O     . ILE B 1 101 ? 17.488  -23.130 34.056 1.00 12.92  ? 143  ILE B O     1 
ATOM   4645 C CB    . ILE B 1 101 ? 19.924  -22.344 32.492 1.00 11.61  ? 143  ILE B CB    1 
ATOM   4646 C CG1   . ILE B 1 101 ? 21.432  -22.347 32.269 1.00 12.17  ? 143  ILE B CG1   1 
ATOM   4647 C CG2   . ILE B 1 101 ? 19.184  -21.383 31.561 1.00 11.90  ? 143  ILE B CG2   1 
ATOM   4648 C CD1   . ILE B 1 101 ? 21.928  -22.778 30.904 1.00 12.65  ? 143  ILE B CD1   1 
ATOM   4649 N N     . LEU B 1 102 ? 17.633  -21.029 34.846 1.00 9.78   ? 144  LEU B N     1 
ATOM   4650 C CA    . LEU B 1 102 ? 16.264  -21.005 35.312 1.00 10.42  ? 144  LEU B CA    1 
ATOM   4651 C C     . LEU B 1 102 ? 15.301  -20.602 34.204 1.00 12.65  ? 144  LEU B C     1 
ATOM   4652 O O     . LEU B 1 102 ? 14.215  -21.189 34.109 1.00 14.63  ? 144  LEU B O     1 
ATOM   4653 C CB    . LEU B 1 102 ? 16.176  -20.048 36.513 1.00 11.92  ? 144  LEU B CB    1 
ATOM   4654 C CG    . LEU B 1 102 ? 17.014  -20.459 37.687 1.00 13.20  ? 144  LEU B CG    1 
ATOM   4655 C CD1   . LEU B 1 102 ? 16.967  -19.426 38.788 1.00 13.88  ? 144  LEU B CD1   1 
ATOM   4656 C CD2   . LEU B 1 102 ? 16.576  -21.821 38.256 1.00 15.78  ? 144  LEU B CD2   1 
ATOM   4657 N N     . GLU B 1 103 ? 15.635  -19.584 33.395 1.00 11.55  ? 145  GLU B N     1 
ATOM   4658 C CA    . GLU B 1 103 ? 14.754  -19.196 32.297 1.00 12.87  ? 145  GLU B CA    1 
ATOM   4659 C C     . GLU B 1 103 ? 15.618  -18.644 31.162 1.00 13.92  ? 145  GLU B C     1 
ATOM   4660 O O     . GLU B 1 103 ? 16.686  -18.058 31.399 1.00 11.70  ? 145  GLU B O     1 
ATOM   4661 C CB    . GLU B 1 103 ? 13.795  -18.061 32.682 1.00 14.38  ? 145  GLU B CB    1 
ATOM   4662 C CG    . GLU B 1 103 ? 12.982  -18.270 33.935 1.00 17.00  ? 145  GLU B CG    1 
ATOM   4663 C CD    . GLU B 1 103 ? 11.941  -19.368 33.862 1.00 18.40  ? 145  GLU B CD    1 
ATOM   4664 O OE1   . GLU B 1 103 ? 11.604  -19.760 32.740 1.00 20.44  ? 145  GLU B OE1   1 
ATOM   4665 O OE2   . GLU B 1 103 ? 11.454  -19.811 34.963 1.00 19.42  ? 145  GLU B OE2   1 
ATOM   4666 N N     . VAL B 1 104 ? 15.105  -18.768 29.920 1.00 12.17  ? 146  VAL B N     1 
ATOM   4667 C CA    . VAL B 1 104 ? 15.605  -18.046 28.772 1.00 13.61  ? 146  VAL B CA    1 
ATOM   4668 C C     . VAL B 1 104 ? 14.379  -17.683 27.950 1.00 13.90  ? 146  VAL B C     1 
ATOM   4669 O O     . VAL B 1 104 ? 13.579  -18.554 27.585 1.00 14.62  ? 146  VAL B O     1 
ATOM   4670 C CB    . VAL B 1 104 ? 16.548  -18.873 27.893 1.00 13.67  ? 146  VAL B CB    1 
ATOM   4671 C CG1   . VAL B 1 104 ? 16.918  -18.093 26.636 1.00 13.57  ? 146  VAL B CG1   1 
ATOM   4672 C CG2   . VAL B 1 104 ? 17.758  -19.368 28.650 1.00 14.81  ? 146  VAL B CG2   1 
ATOM   4673 N N     . ASP B 1 105 ? 14.240  -16.381 27.736 1.00 12.85  ? 147  ASP B N     1 
ATOM   4674 C CA    . ASP B 1 105 ? 13.125  -15.774 27.040 1.00 14.96  ? 147  ASP B CA    1 
ATOM   4675 C C     . ASP B 1 105 ? 13.636  -15.377 25.663 1.00 14.16  ? 147  ASP B C     1 
ATOM   4676 O O     . ASP B 1 105 ? 14.343  -14.395 25.527 1.00 12.38  ? 147  ASP B O     1 
ATOM   4677 C CB    . ASP B 1 105 ? 12.541  -14.644 27.896 1.00 16.02  ? 147  ASP B CB    1 
ATOM   4678 C CG    . ASP B 1 105 ? 11.337  -13.908 27.334 1.00 21.65  ? 147  ASP B CG    1 
ATOM   4679 O OD1   . ASP B 1 105 ? 11.037  -14.063 26.129 1.00 19.32  ? 147  ASP B OD1   1 
ATOM   4680 O OD2   . ASP B 1 105 ? 10.738  -13.102 28.123 1.00 21.12  ? 147  ASP B OD2   1 
ATOM   4681 N N     . ALA B 1 106 ? 13.265  -16.168 24.654 1.00 14.23  ? 148  ALA B N     1 
ATOM   4682 C CA    . ALA B 1 106 ? 13.757  -15.929 23.306 1.00 15.93  ? 148  ALA B CA    1 
ATOM   4683 C C     . ALA B 1 106 ? 13.243  -14.608 22.731 1.00 15.98  ? 148  ALA B C     1 
ATOM   4684 O O     . ALA B 1 106 ? 13.970  -13.922 22.009 1.00 19.04  ? 148  ALA B O     1 
ATOM   4685 C CB    . ALA B 1 106 ? 13.372  -17.096 22.417 1.00 18.55  ? 148  ALA B CB    1 
ATOM   4686 N N     . ASP B 1 107 ? 11.964  -14.293 22.989 1.00 17.65  ? 149  ASP B N     1 
ATOM   4687 C CA    . ASP B 1 107 ? 11.344  -13.123 22.375 1.00 17.68  ? 149  ASP B CA    1 
ATOM   4688 C C     . ASP B 1 107 ? 11.893  -11.827 22.971 1.00 16.60  ? 149  ASP B C     1 
ATOM   4689 O O     . ASP B 1 107 ? 12.172  -10.894 22.220 1.00 17.22  ? 149  ASP B O     1 
ATOM   4690 C CB    . ASP B 1 107 ? 9.828   -13.091 22.602 1.00 21.21  ? 149  ASP B CB    1 
ATOM   4691 C CG    . ASP B 1 107 ? 9.020   -14.119 21.819 1.00 27.30  ? 149  ASP B CG    1 
ATOM   4692 O OD1   . ASP B 1 107 ? 9.605   -14.736 20.953 1.00 26.96  ? 149  ASP B OD1   1 
ATOM   4693 O OD2   . ASP B 1 107 ? 7.779   -14.230 22.080 1.00 26.94  ? 149  ASP B OD2   1 
ATOM   4694 N N     . LEU B 1 108 ? 12.032  -11.763 24.315 1.00 15.46  ? 150  LEU B N     1 
ATOM   4695 C CA    . LEU B 1 108 ? 12.540  -10.557 24.937 1.00 16.93  ? 150  LEU B CA    1 
ATOM   4696 C C     . LEU B 1 108 ? 14.068  -10.540 24.986 1.00 14.06  ? 150  LEU B C     1 
ATOM   4697 O O     . LEU B 1 108 ? 14.645  -9.512  25.292 1.00 15.12  ? 150  LEU B O     1 
ATOM   4698 C CB    . LEU B 1 108 ? 11.997  -10.372 26.357 1.00 16.28  ? 150  LEU B CB    1 
ATOM   4699 C CG    . LEU B 1 108 ? 10.545  -9.954  26.471 1.00 24.15  ? 150  LEU B CG    1 
ATOM   4700 C CD1   . LEU B 1 108 ? 10.300  -9.639  27.927 1.00 25.66  ? 150  LEU B CD1   1 
ATOM   4701 C CD2   . LEU B 1 108 ? 10.249  -8.761  25.567 1.00 24.39  ? 150  LEU B CD2   1 
ATOM   4702 N N     . GLY B 1 109 ? 14.735  -11.675 24.709 1.00 14.00  ? 151  GLY B N     1 
ATOM   4703 C CA    . GLY B 1 109 ? 16.179  -11.692 24.687 1.00 13.03  ? 151  GLY B CA    1 
ATOM   4704 C C     . GLY B 1 109 ? 16.727  -11.590 26.105 1.00 11.66  ? 151  GLY B C     1 
ATOM   4705 O O     . GLY B 1 109 ? 17.490  -10.669 26.416 1.00 10.84  ? 151  GLY B O     1 
ATOM   4706 N N     . THR B 1 110 ? 16.275  -12.501 26.981 1.00 11.10  ? 152  THR B N     1 
ATOM   4707 C CA    . THR B 1 110 ? 16.709  -12.441 28.379 1.00 10.50  ? 152  THR B CA    1 
ATOM   4708 C C     . THR B 1 110 ? 16.973  -13.833 28.924 1.00 10.52  ? 152  THR B C     1 
ATOM   4709 O O     . THR B 1 110 ? 16.527  -14.830 28.359 1.00 10.81  ? 152  THR B O     1 
ATOM   4710 C CB    . THR B 1 110 ? 15.715  -11.738 29.329 1.00 12.47  ? 152  THR B CB    1 
ATOM   4711 O OG1   . THR B 1 110 ? 14.618  -12.596 29.631 1.00 12.11  ? 152  THR B OG1   1 
ATOM   4712 C CG2   . THR B 1 110 ? 15.189  -10.428 28.769 1.00 12.07  ? 152  THR B CG2   1 
ATOM   4713 N N     . CYS B 1 111 ? 17.648  -13.889 30.087 1.00 9.47   ? 153  CYS B N     1 
ATOM   4714 C CA    . CYS B 1 111 ? 17.777  -15.159 30.813 1.00 10.46  ? 153  CYS B CA    1 
ATOM   4715 C C     . CYS B 1 111 ? 17.839  -14.868 32.315 1.00 11.53  ? 153  CYS B C     1 
ATOM   4716 O O     . CYS B 1 111 ? 18.057  -13.734 32.768 1.00 10.39  ? 153  CYS B O     1 
ATOM   4717 C CB    . CYS B 1 111 ? 19.008  -15.979 30.407 1.00 11.98  ? 153  CYS B CB    1 
ATOM   4718 S SG    . CYS B 1 111 ? 20.591  -15.181 30.694 1.00 12.61  ? 153  CYS B SG    1 
ATOM   4719 N N     . LEU B 1 112 ? 17.651  -15.928 33.102 1.00 10.18  ? 154  LEU B N     1 
ATOM   4720 C CA    . LEU B 1 112 ? 17.741  -15.902 34.560 1.00 9.63   ? 154  LEU B CA    1 
ATOM   4721 C C     . LEU B 1 112 ? 18.623  -17.074 34.994 1.00 9.20   ? 154  LEU B C     1 
ATOM   4722 O O     . LEU B 1 112 ? 18.308  -18.219 34.640 1.00 9.85   ? 154  LEU B O     1 
ATOM   4723 C CB    . LEU B 1 112 ? 16.337  -16.013 35.146 1.00 11.15  ? 154  LEU B CB    1 
ATOM   4724 C CG    . LEU B 1 112 ? 16.256  -16.036 36.655 1.00 10.66  ? 154  LEU B CG    1 
ATOM   4725 C CD1   . LEU B 1 112 ? 16.695  -14.710 37.225 1.00 10.98  ? 154  LEU B CD1   1 
ATOM   4726 C CD2   . LEU B 1 112 ? 14.854  -16.346 37.141 1.00 10.96  ? 154  LEU B CD2   1 
ATOM   4727 N N     . LEU B 1 113 ? 19.672  -16.802 35.754 1.00 10.36  ? 155  LEU B N     1 
ATOM   4728 C CA    . LEU B 1 113 ? 20.757  -17.737 35.999 1.00 11.10  ? 155  LEU B CA    1 
ATOM   4729 C C     . LEU B 1 113 ? 21.050  -17.868 37.488 1.00 11.34  ? 155  LEU B C     1 
ATOM   4730 O O     . LEU B 1 113 ? 21.033  -16.863 38.180 1.00 12.36  ? 155  LEU B O     1 
ATOM   4731 C CB    . LEU B 1 113 ? 22.072  -17.292 35.330 1.00 10.70  ? 155  LEU B CB    1 
ATOM   4732 C CG    . LEU B 1 113 ? 22.003  -16.931 33.842 1.00 11.03  ? 155  LEU B CG    1 
ATOM   4733 C CD1   . LEU B 1 113 ? 23.330  -16.404 33.329 1.00 10.80  ? 155  LEU B CD1   1 
ATOM   4734 C CD2   . LEU B 1 113 ? 21.501  -18.099 32.978 1.00 11.78  ? 155  LEU B CD2   1 
ATOM   4735 N N     . GLU B 1 114 ? 21.426  -19.079 37.906 1.00 11.23  ? 156  GLU B N     1 
ATOM   4736 C CA    . GLU B 1 114 ? 22.111  -19.254 39.170 1.00 11.28  ? 156  GLU B CA    1 
ATOM   4737 C C     . GLU B 1 114 ? 23.613  -18.989 39.004 1.00 9.95   ? 156  GLU B C     1 
ATOM   4738 O O     . GLU B 1 114 ? 24.186  -18.958 37.907 1.00 10.21  ? 156  GLU B O     1 
ATOM   4739 C CB    . GLU B 1 114 ? 21.879  -20.651 39.739 1.00 11.68  ? 156  GLU B CB    1 
ATOM   4740 C CG    . GLU B 1 114 ? 20.427  -20.885 40.199 1.00 13.35  ? 156  GLU B CG    1 
ATOM   4741 C CD    . GLU B 1 114 ? 20.242  -22.171 40.991 1.00 14.77  ? 156  GLU B CD    1 
ATOM   4742 O OE1   . GLU B 1 114 ? 20.935  -23.169 40.647 1.00 11.89  ? 156  GLU B OE1   1 
ATOM   4743 O OE2   . GLU B 1 114 ? 19.454  -22.177 41.954 1.00 17.37  ? 156  GLU B OE2   1 
ATOM   4744 N N     . PRO B 1 115 ? 24.340  -18.762 40.106 1.00 10.49  ? 157  PRO B N     1 
ATOM   4745 C CA    . PRO B 1 115 ? 25.734  -18.325 40.009 1.00 10.65  ? 157  PRO B CA    1 
ATOM   4746 C C     . PRO B 1 115 ? 26.721  -19.254 39.335 1.00 10.64  ? 157  PRO B C     1 
ATOM   4747 O O     . PRO B 1 115 ? 27.708  -18.841 38.688 1.00 11.95  ? 157  PRO B O     1 
ATOM   4748 C CB    . PRO B 1 115 ? 26.084  -18.044 41.487 1.00 11.34  ? 157  PRO B CB    1 
ATOM   4749 C CG    . PRO B 1 115 ? 24.790  -17.745 42.116 1.00 11.89  ? 157  PRO B CG    1 
ATOM   4750 C CD    . PRO B 1 115 ? 23.808  -18.719 41.489 1.00 11.74  ? 157  PRO B CD    1 
ATOM   4751 N N     . GLY B 1 116 ? 26.462  -20.532 39.505 1.00 9.70   ? 158  GLY B N     1 
ATOM   4752 C CA    . GLY B 1 116 ? 27.331  -21.579 39.000 1.00 10.03  ? 158  GLY B CA    1 
ATOM   4753 C C     . GLY B 1 116 ? 27.222  -21.837 37.514 1.00 9.20   ? 158  GLY B C     1 
ATOM   4754 O O     . GLY B 1 116 ? 28.065  -22.566 36.990 1.00 11.32  ? 158  GLY B O     1 
ATOM   4755 N N     . VAL B 1 117 ? 26.212  -21.266 36.835 1.00 11.02  ? 159  VAL B N     1 
ATOM   4756 C CA    . VAL B 1 117 ? 26.116  -21.385 35.389 1.00 10.48  ? 159  VAL B CA    1 
ATOM   4757 C C     . VAL B 1 117 ? 27.402  -20.806 34.778 1.00 12.07  ? 159  VAL B C     1 
ATOM   4758 O O     . VAL B 1 117 ? 27.795  -19.663 35.099 1.00 10.43  ? 159  VAL B O     1 
ATOM   4759 C CB    . VAL B 1 117 ? 24.860  -20.706 34.829 1.00 10.77  ? 159  VAL B CB    1 
ATOM   4760 C CG1   . VAL B 1 117 ? 24.846  -20.744 33.306 1.00 11.99  ? 159  VAL B CG1   1 
ATOM   4761 C CG2   . VAL B 1 117 ? 23.547  -21.267 35.392 1.00 12.44  ? 159  VAL B CG2   1 
ATOM   4762 N N     . THR B 1 118 ? 28.053  -21.572 33.894 1.00 10.53  ? 160  THR B N     1 
ATOM   4763 C CA    . THR B 1 118 ? 29.204  -21.089 33.163 1.00 10.95  ? 160  THR B CA    1 
ATOM   4764 C C     . THR B 1 118 ? 28.855  -20.527 31.791 1.00 10.64  ? 160  THR B C     1 
ATOM   4765 O O     . THR B 1 118 ? 27.788  -20.829 31.233 1.00 10.50  ? 160  THR B O     1 
ATOM   4766 C CB    . THR B 1 118 ? 30.241  -22.201 33.004 1.00 11.09  ? 160  THR B CB    1 
ATOM   4767 O OG1   . THR B 1 118 ? 29.737  -23.154 32.064 1.00 11.62  ? 160  THR B OG1   1 
ATOM   4768 C CG2   . THR B 1 118 ? 30.569  -22.850 34.350 1.00 11.53  ? 160  THR B CG2   1 
ATOM   4769 N N     . TYR B 1 119 ? 29.776  -19.743 31.194 1.00 11.59  ? 161  TYR B N     1 
ATOM   4770 C CA    . TYR B 1 119 ? 29.533  -19.254 29.864 1.00 11.89  ? 161  TYR B CA    1 
ATOM   4771 C C     . TYR B 1 119 ? 29.349  -20.425 28.907 1.00 13.19  ? 161  TYR B C     1 
ATOM   4772 O O     . TYR B 1 119 ? 28.466  -20.358 28.022 1.00 12.37  ? 161  TYR B O     1 
ATOM   4773 C CB    . TYR B 1 119 ? 30.635  -18.312 29.408 1.00 12.41  ? 161  TYR B CB    1 
ATOM   4774 C CG    . TYR B 1 119 ? 30.573  -16.961 30.071 1.00 12.62  ? 161  TYR B CG    1 
ATOM   4775 C CD1   . TYR B 1 119 ? 29.698  -15.975 29.615 1.00 13.78  ? 161  TYR B CD1   1 
ATOM   4776 C CD2   . TYR B 1 119 ? 31.454  -16.620 31.089 1.00 12.64  ? 161  TYR B CD2   1 
ATOM   4777 C CE1   . TYR B 1 119 ? 29.675  -14.693 30.158 1.00 15.05  ? 161  TYR B CE1   1 
ATOM   4778 C CE2   . TYR B 1 119 ? 31.412  -15.339 31.637 1.00 13.30  ? 161  TYR B CE2   1 
ATOM   4779 C CZ    . TYR B 1 119 ? 30.523  -14.403 31.193 1.00 13.64  ? 161  TYR B CZ    1 
ATOM   4780 O OH    . TYR B 1 119 ? 30.578  -13.138 31.781 1.00 18.50  ? 161  TYR B OH    1 
ATOM   4781 N N     . GLN B 1 120 ? 30.149  -21.477 29.101 1.00 14.42  ? 162  GLN B N     1 
ATOM   4782 C CA    . GLN B 1 120 ? 30.097  -22.631 28.193 1.00 17.12  ? 162  GLN B CA    1 
ATOM   4783 C C     . GLN B 1 120 ? 28.704  -23.250 28.238 1.00 14.69  ? 162  GLN B C     1 
ATOM   4784 O O     . GLN B 1 120 ? 28.080  -23.583 27.212 1.00 14.93  ? 162  GLN B O     1 
ATOM   4785 C CB    . GLN B 1 120 ? 31.167  -23.678 28.576 1.00 19.87  ? 162  GLN B CB    1 
ATOM   4786 C CG    . GLN B 1 120 ? 31.055  -24.988 27.799 1.00 27.75  ? 162  GLN B CG    1 
ATOM   4787 C CD    . GLN B 1 120 ? 31.535  -24.793 26.392 1.00 36.58  ? 162  GLN B CD    1 
ATOM   4788 O OE1   . GLN B 1 120 ? 30.761  -24.690 25.440 1.00 46.51  ? 162  GLN B OE1   1 
ATOM   4789 N NE2   . GLN B 1 120 ? 32.844  -24.666 26.261 1.00 37.09  ? 162  GLN B NE2   1 
ATOM   4790 N N     . GLN B 1 121 ? 28.229  -23.448 29.462 1.00 13.39  ? 163  GLN B N     1 
ATOM   4791 C CA    . GLN B 1 121 ? 26.925  -24.022 29.694 1.00 14.97  ? 163  GLN B CA    1 
ATOM   4792 C C     . GLN B 1 121 ? 25.804  -23.226 29.031 1.00 15.35  ? 163  GLN B C     1 
ATOM   4793 O O     . GLN B 1 121 ? 24.868  -23.774 28.442 1.00 15.25  ? 163  GLN B O     1 
ATOM   4794 C CB    . GLN B 1 121 ? 26.819  -24.051 31.202 1.00 16.37  ? 163  GLN B CB    1 
ATOM   4795 C CG    . GLN B 1 121 ? 25.652  -24.787 31.709 1.00 17.56  ? 163  GLN B CG    1 
ATOM   4796 C CD    . GLN B 1 121 ? 25.644  -24.835 33.223 1.00 18.20  ? 163  GLN B CD    1 
ATOM   4797 O OE1   . GLN B 1 121 ? 26.551  -24.416 33.979 1.00 17.90  ? 163  GLN B OE1   1 
ATOM   4798 N NE2   . GLN B 1 121 ? 24.515  -25.335 33.649 1.00 18.20  ? 163  GLN B NE2   1 
ATOM   4799 N N     . LEU B 1 122 ? 25.839  -21.893 29.188 1.00 11.73  ? 164  LEU B N     1 
ATOM   4800 C CA    . LEU B 1 122 ? 24.806  -21.061 28.615 1.00 11.40  ? 164  LEU B CA    1 
ATOM   4801 C C     . LEU B 1 122 ? 24.886  -21.097 27.091 1.00 12.06  ? 164  LEU B C     1 
ATOM   4802 O O     . LEU B 1 122 ? 23.839  -21.177 26.444 1.00 11.74  ? 164  LEU B O     1 
ATOM   4803 C CB    . LEU B 1 122 ? 24.924  -19.654 29.216 1.00 11.73  ? 164  LEU B CB    1 
ATOM   4804 C CG    . LEU B 1 122 ? 23.879  -18.645 28.763 1.00 14.08  ? 164  LEU B CG    1 
ATOM   4805 C CD1   . LEU B 1 122 ? 22.432  -19.116 29.031 1.00 14.83  ? 164  LEU B CD1   1 
ATOM   4806 C CD2   . LEU B 1 122 ? 24.173  -17.300 29.410 1.00 14.42  ? 164  LEU B CD2   1 
ATOM   4807 N N     . LYS B 1 123 ? 26.087  -20.987 26.510 1.00 11.29  ? 165  LYS B N     1 
ATOM   4808 C CA    . LYS B 1 123 ? 26.214  -21.044 25.069 1.00 12.83  ? 165  LYS B CA    1 
ATOM   4809 C C     . LYS B 1 123 ? 25.665  -22.387 24.552 1.00 13.41  ? 165  LYS B C     1 
ATOM   4810 O O     . LYS B 1 123 ? 24.897  -22.395 23.589 1.00 13.62  ? 165  LYS B O     1 
ATOM   4811 C CB    . LYS B 1 123 ? 27.685  -20.924 24.646 1.00 14.24  ? 165  LYS B CB    1 
ATOM   4812 C CG    . LYS B 1 123 ? 27.889  -20.825 23.133 1.00 15.70  ? 165  LYS B CG    1 
ATOM   4813 C CD    . LYS B 1 123 ? 27.178  -19.683 22.446 1.00 17.05  ? 165  LYS B CD    1 
ATOM   4814 C CE    . LYS B 1 123 ? 27.580  -19.553 20.991 1.00 18.62  ? 165  LYS B CE    1 
ATOM   4815 N NZ    . LYS B 1 123 ? 26.874  -18.472 20.266 1.00 20.96  ? 165  LYS B NZ    1 
ATOM   4816 N N     . ASP B 1 124 ? 26.043  -23.499 25.203 1.00 13.60  ? 166  ASP B N     1 
ATOM   4817 C CA    . ASP B 1 124 ? 25.535  -24.836 24.812 1.00 15.82  ? 166  ASP B CA    1 
ATOM   4818 C C     . ASP B 1 124 ? 24.003  -24.875 24.857 1.00 16.27  ? 166  ASP B C     1 
ATOM   4819 O O     . ASP B 1 124 ? 23.339  -25.443 23.974 1.00 15.85  ? 166  ASP B O     1 
ATOM   4820 C CB    . ASP B 1 124 ? 26.094  -25.960 25.689 1.00 16.37  ? 166  ASP B CB    1 
ATOM   4821 C CG    . ASP B 1 124 ? 27.563  -26.262 25.430 1.00 19.43  ? 166  ASP B CG    1 
ATOM   4822 O OD1   . ASP B 1 124 ? 28.127  -25.729 24.461 1.00 22.32  ? 166  ASP B OD1   1 
ATOM   4823 O OD2   . ASP B 1 124 ? 28.152  -26.972 26.245 1.00 23.70  ? 166  ASP B OD2   1 
ATOM   4824 N N     . TYR B 1 125 ? 23.426  -24.311 25.921 1.00 13.93  ? 167  TYR B N     1 
ATOM   4825 C CA    . TYR B 1 125 ? 21.974  -24.305 26.103 1.00 14.57  ? 167  TYR B CA    1 
ATOM   4826 C C     . TYR B 1 125 ? 21.304  -23.586 24.935 1.00 15.51  ? 167  TYR B C     1 
ATOM   4827 O O     . TYR B 1 125 ? 20.314  -24.050 24.356 1.00 14.64  ? 167  TYR B O     1 
ATOM   4828 C CB    . TYR B 1 125 ? 21.603  -23.632 27.423 1.00 17.38  ? 167  TYR B CB    1 
ATOM   4829 C CG    . TYR B 1 125 ? 20.149  -23.681 27.791 1.00 17.95  ? 167  TYR B CG    1 
ATOM   4830 C CD1   . TYR B 1 125 ? 19.243  -22.758 27.314 1.00 20.14  ? 167  TYR B CD1   1 
ATOM   4831 C CD2   . TYR B 1 125 ? 19.713  -24.653 28.691 1.00 21.28  ? 167  TYR B CD2   1 
ATOM   4832 C CE1   . TYR B 1 125 ? 17.894  -22.831 27.651 1.00 23.82  ? 167  TYR B CE1   1 
ATOM   4833 C CE2   . TYR B 1 125 ? 18.389  -24.697 29.084 1.00 24.05  ? 167  TYR B CE2   1 
ATOM   4834 C CZ    . TYR B 1 125 ? 17.489  -23.790 28.572 1.00 21.98  ? 167  TYR B CZ    1 
ATOM   4835 O OH    . TYR B 1 125 ? 16.168  -23.855 28.981 1.00 34.12  ? 167  TYR B OH    1 
ATOM   4836 N N     . LEU B 1 126 ? 21.829  -22.398 24.574 1.00 12.66  ? 168  LEU B N     1 
ATOM   4837 C CA    . LEU B 1 126 ? 21.271  -21.655 23.455 1.00 12.41  ? 168  LEU B CA    1 
ATOM   4838 C C     . LEU B 1 126 ? 21.355  -22.447 22.140 1.00 14.13  ? 168  LEU B C     1 
ATOM   4839 O O     . LEU B 1 126 ? 20.380  -22.465 21.382 1.00 15.39  ? 168  LEU B O     1 
ATOM   4840 C CB    . LEU B 1 126 ? 21.977  -20.305 23.360 1.00 13.20  ? 168  LEU B CB    1 
ATOM   4841 C CG    . LEU B 1 126 ? 21.740  -19.394 24.577 1.00 13.34  ? 168  LEU B CG    1 
ATOM   4842 C CD1   . LEU B 1 126 ? 22.671  -18.178 24.442 1.00 13.69  ? 168  LEU B CD1   1 
ATOM   4843 C CD2   . LEU B 1 126 ? 20.307  -18.897 24.711 1.00 16.03  ? 168  LEU B CD2   1 
ATOM   4844 N N     . GLU B 1 127 ? 22.531  -22.977 21.844 1.00 15.05  ? 169  GLU B N     1 
ATOM   4845 C CA    . GLU B 1 127 ? 22.754  -23.740 20.629 1.00 16.18  ? 169  GLU B CA    1 
ATOM   4846 C C     . GLU B 1 127 ? 21.843  -24.968 20.579 1.00 16.68  ? 169  GLU B C     1 
ATOM   4847 O O     . GLU B 1 127 ? 21.257  -25.285 19.527 1.00 17.89  ? 169  GLU B O     1 
ATOM   4848 C CB    . GLU B 1 127 ? 24.227  -24.139 20.545 1.00 16.82  ? 169  GLU B CB    1 
ATOM   4849 C CG    . GLU B 1 127 ? 25.129  -22.944 20.255 1.00 22.21  ? 169  GLU B CG    1 
ATOM   4850 C CD    . GLU B 1 127 ? 25.011  -22.317 18.870 1.00 34.97  ? 169  GLU B CD    1 
ATOM   4851 O OE1   . GLU B 1 127 ? 25.403  -21.113 18.711 1.00 41.01  ? 169  GLU B OE1   1 
ATOM   4852 O OE2   . GLU B 1 127 ? 24.545  -23.039 17.935 1.00 37.73  ? 169  GLU B OE2   1 
ATOM   4853 N N     . GLU B 1 128 ? 21.762  -25.705 21.670 1.00 15.63  ? 170  GLU B N     1 
ATOM   4854 C CA    . GLU B 1 128 ? 21.021  -26.963 21.686 1.00 18.00  ? 170  GLU B CA    1 
ATOM   4855 C C     . GLU B 1 128 ? 19.530  -26.722 21.484 1.00 18.71  ? 170  GLU B C     1 
ATOM   4856 O O     . GLU B 1 128 ? 18.836  -27.599 20.931 1.00 20.51  ? 170  GLU B O     1 
ATOM   4857 C CB    . GLU B 1 128 ? 21.215  -27.651 23.030 1.00 19.80  ? 170  GLU B CB    1 
ATOM   4858 C CG    . GLU B 1 128 ? 22.539  -28.349 23.101 1.00 24.04  ? 170  GLU B CG    1 
ATOM   4859 C CD    . GLU B 1 128 ? 22.843  -28.782 24.536 1.00 28.36  ? 170  GLU B CD    1 
ATOM   4860 O OE1   . GLU B 1 128 ? 21.938  -28.715 25.407 1.00 32.45  ? 170  GLU B OE1   1 
ATOM   4861 O OE2   . GLU B 1 128 ? 23.957  -29.180 24.768 1.00 35.27  ? 170  GLU B OE2   1 
ATOM   4862 N N     . HIS B 1 129 ? 19.024  -25.563 21.947 1.00 14.08  ? 171  HIS B N     1 
ATOM   4863 C CA    . HIS B 1 129 ? 17.629  -25.192 21.791 1.00 14.94  ? 171  HIS B CA    1 
ATOM   4864 C C     . HIS B 1 129 ? 17.375  -24.377 20.530 1.00 14.89  ? 171  HIS B C     1 
ATOM   4865 O O     . HIS B 1 129 ? 16.246  -23.870 20.345 1.00 16.55  ? 171  HIS B O     1 
ATOM   4866 C CB    . HIS B 1 129 ? 17.087  -24.488 23.044 1.00 14.78  ? 171  HIS B CB    1 
ATOM   4867 C CG    . HIS B 1 129 ? 17.154  -25.399 24.247 1.00 15.26  ? 171  HIS B CG    1 
ATOM   4868 N ND1   . HIS B 1 129 ? 18.271  -25.578 25.056 1.00 14.81  ? 171  HIS B ND1   1 
ATOM   4869 C CD2   . HIS B 1 129 ? 16.224  -26.245 24.749 1.00 17.91  ? 171  HIS B CD2   1 
ATOM   4870 C CE1   . HIS B 1 129 ? 17.999  -26.458 26.007 1.00 16.62  ? 171  HIS B CE1   1 
ATOM   4871 N NE2   . HIS B 1 129 ? 16.769  -26.895 25.831 1.00 17.26  ? 171  HIS B NE2   1 
ATOM   4872 N N     . LYS B 1 130 ? 18.411  -24.127 19.717 1.00 14.67  ? 172  LYS B N     1 
ATOM   4873 C CA    . LYS B 1 130 ? 18.308  -23.307 18.511 1.00 15.84  ? 172  LYS B CA    1 
ATOM   4874 C C     . LYS B 1 130 ? 17.734  -21.930 18.778 1.00 18.11  ? 172  LYS B C     1 
ATOM   4875 O O     . LYS B 1 130 ? 16.909  -21.410 18.005 1.00 18.37  ? 172  LYS B O     1 
ATOM   4876 C CB    . LYS B 1 130 ? 17.437  -23.977 17.438 1.00 20.27  ? 172  LYS B CB    1 
ATOM   4877 C CG    . LYS B 1 130 ? 17.804  -25.434 17.222 1.00 26.68  ? 172  LYS B CG    1 
ATOM   4878 C CD    . LYS B 1 130 ? 19.077  -25.670 16.477 1.00 31.61  ? 172  LYS B CD    1 
ATOM   4879 C CE    . LYS B 1 130 ? 19.061  -27.063 15.873 1.00 43.49  ? 172  LYS B CE    1 
ATOM   4880 N NZ    . LYS B 1 130 ? 20.371  -27.439 15.294 1.00 50.28  ? 172  LYS B NZ    1 
ATOM   4881 N N     . ILE B 1 131 ? 18.170  -21.343 19.891 1.00 14.97  ? 173  ILE B N     1 
ATOM   4882 C CA    . ILE B 1 131 ? 17.712  -20.019 20.262 1.00 15.01  ? 173  ILE B CA    1 
ATOM   4883 C C     . ILE B 1 131 ? 18.667  -18.983 19.699 1.00 15.50  ? 173  ILE B C     1 
ATOM   4884 O O     . ILE B 1 131 ? 19.869  -18.999 20.054 1.00 14.84  ? 173  ILE B O     1 
ATOM   4885 C CB    . ILE B 1 131 ? 17.643  -19.898 21.779 1.00 15.68  ? 173  ILE B CB    1 
ATOM   4886 C CG1   . ILE B 1 131 ? 16.622  -20.871 22.385 1.00 18.49  ? 173  ILE B CG1   1 
ATOM   4887 C CG2   . ILE B 1 131 ? 17.346  -18.479 22.180 1.00 15.48  ? 173  ILE B CG2   1 
ATOM   4888 C CD1   . ILE B 1 131 ? 16.771  -21.062 23.842 1.00 17.79  ? 173  ILE B CD1   1 
ATOM   4889 N N     . PRO B 1 132 ? 18.183  -18.076 18.825 1.00 17.29  ? 174  PRO B N     1 
ATOM   4890 C CA    . PRO B 1 132 ? 19.042  -17.131 18.119 1.00 16.33  ? 174  PRO B CA    1 
ATOM   4891 C C     . PRO B 1 132 ? 19.461  -15.912 18.956 1.00 14.91  ? 174  PRO B C     1 
ATOM   4892 O O     . PRO B 1 132 ? 19.231  -14.770 18.572 1.00 15.65  ? 174  PRO B O     1 
ATOM   4893 C CB    . PRO B 1 132 ? 18.171  -16.734 16.918 1.00 18.39  ? 174  PRO B CB    1 
ATOM   4894 C CG    . PRO B 1 132 ? 16.792  -16.782 17.467 1.00 17.62  ? 174  PRO B CG    1 
ATOM   4895 C CD    . PRO B 1 132 ? 16.773  -17.990 18.396 1.00 18.23  ? 174  PRO B CD    1 
ATOM   4896 N N     . LEU B 1 133 ? 20.092  -16.193 20.100 1.00 12.76  ? 175  LEU B N     1 
ATOM   4897 C CA    . LEU B 1 133 ? 20.672  -15.207 20.978 1.00 13.04  ? 175  LEU B CA    1 
ATOM   4898 C C     . LEU B 1 133 ? 22.152  -15.536 21.154 1.00 14.73  ? 175  LEU B C     1 
ATOM   4899 O O     . LEU B 1 133 ? 22.536  -16.713 21.158 1.00 13.75  ? 175  LEU B O     1 
ATOM   4900 C CB    . LEU B 1 133 ? 19.983  -15.204 22.364 1.00 12.11  ? 175  LEU B CB    1 
ATOM   4901 C CG    . LEU B 1 133 ? 18.481  -14.868 22.416 1.00 11.59  ? 175  LEU B CG    1 
ATOM   4902 C CD1   . LEU B 1 133 ? 17.850  -15.138 23.781 1.00 11.72  ? 175  LEU B CD1   1 
ATOM   4903 C CD2   . LEU B 1 133 ? 18.275  -13.422 21.997 1.00 12.07  ? 175  LEU B CD2   1 
ATOM   4904 N N     . TRP B 1 134 ? 22.940  -14.483 21.432 1.00 12.73  ? 176  TRP B N     1 
ATOM   4905 C CA    . TRP B 1 134 ? 24.360  -14.574 21.704 1.00 12.79  ? 176  TRP B CA    1 
ATOM   4906 C C     . TRP B 1 134 ? 24.587  -14.247 23.176 1.00 13.57  ? 176  TRP B C     1 
ATOM   4907 O O     . TRP B 1 134 ? 23.752  -13.606 23.831 1.00 13.87  ? 176  TRP B O     1 
ATOM   4908 C CB    . TRP B 1 134 ? 25.117  -13.572 20.809 1.00 14.71  ? 176  TRP B CB    1 
ATOM   4909 C CG    . TRP B 1 134 ? 25.483  -14.075 19.471 1.00 15.74  ? 176  TRP B CG    1 
ATOM   4910 C CD1   . TRP B 1 134 ? 25.228  -15.302 18.950 1.00 18.15  ? 176  TRP B CD1   1 
ATOM   4911 C CD2   . TRP B 1 134 ? 26.196  -13.342 18.476 1.00 19.28  ? 176  TRP B CD2   1 
ATOM   4912 N NE1   . TRP B 1 134 ? 25.736  -15.377 17.677 1.00 21.15  ? 176  TRP B NE1   1 
ATOM   4913 C CE2   . TRP B 1 134 ? 26.333  -14.199 17.367 1.00 20.06  ? 176  TRP B CE2   1 
ATOM   4914 C CE3   . TRP B 1 134 ? 26.710  -12.050 18.430 1.00 22.38  ? 176  TRP B CE3   1 
ATOM   4915 C CZ2   . TRP B 1 134 ? 27.001  -13.796 16.204 1.00 24.75  ? 176  TRP B CZ2   1 
ATOM   4916 C CZ3   . TRP B 1 134 ? 27.359  -11.656 17.275 1.00 23.05  ? 176  TRP B CZ3   1 
ATOM   4917 C CH2   . TRP B 1 134 ? 27.496  -12.513 16.201 1.00 19.31  ? 176  TRP B CH2   1 
ATOM   4918 N N     . ILE B 1 135 ? 25.754  -14.677 23.655 1.00 12.41  ? 177  ILE B N     1 
ATOM   4919 C CA    . ILE B 1 135 ? 26.318  -14.291 24.935 1.00 12.75  ? 177  ILE B CA    1 
ATOM   4920 C C     . ILE B 1 135 ? 27.440  -13.293 24.702 1.00 12.98  ? 177  ILE B C     1 
ATOM   4921 O O     . ILE B 1 135 ? 27.883  -13.085 23.561 1.00 13.56  ? 177  ILE B O     1 
ATOM   4922 C CB    . ILE B 1 135 ? 26.801  -15.518 25.727 1.00 13.10  ? 177  ILE B CB    1 
ATOM   4923 C CG1   . ILE B 1 135 ? 27.894  -16.291 24.993 1.00 12.17  ? 177  ILE B CG1   1 
ATOM   4924 C CG2   . ILE B 1 135 ? 25.614  -16.413 26.079 1.00 16.16  ? 177  ILE B CG2   1 
ATOM   4925 C CD1   . ILE B 1 135 ? 28.585  -17.367 25.842 1.00 11.84  ? 177  ILE B CD1   1 
ATOM   4926 N N     . ASP B 1 136 ? 27.928  -12.690 25.790 1.00 12.87  ? 178  ASP B N     1 
ATOM   4927 C CA    . ASP B 1 136 ? 29.048  -11.770 25.727 1.00 11.76  ? 178  ASP B CA    1 
ATOM   4928 C C     . ASP B 1 136 ? 30.073  -12.220 26.761 1.00 11.01  ? 178  ASP B C     1 
ATOM   4929 O O     . ASP B 1 136 ? 29.733  -12.301 27.946 1.00 12.47  ? 178  ASP B O     1 
ATOM   4930 C CB    . ASP B 1 136 ? 28.560  -10.358 25.905 1.00 11.77  ? 178  ASP B CB    1 
ATOM   4931 C CG    . ASP B 1 136 ? 29.647  -9.305  25.746 1.00 12.90  ? 178  ASP B CG    1 
ATOM   4932 O OD1   . ASP B 1 136 ? 30.567  -9.286  26.649 1.00 14.03  ? 178  ASP B OD1   1 
ATOM   4933 O OD2   . ASP B 1 136 ? 29.544  -8.508  24.777 1.00 13.62  ? 178  ASP B OD2   1 
ATOM   4934 N N     . VAL B 1 137 ? 31.248  -12.639 26.288 1.00 12.17  ? 179  VAL B N     1 
ATOM   4935 C CA    . VAL B 1 137 ? 32.183  -13.395 27.119 1.00 14.50  ? 179  VAL B CA    1 
ATOM   4936 C C     . VAL B 1 137 ? 33.424  -12.571 27.358 1.00 13.58  ? 179  VAL B C     1 
ATOM   4937 O O     . VAL B 1 137 ? 33.905  -11.874 26.455 1.00 11.36  ? 179  VAL B O     1 
ATOM   4938 C CB    . VAL B 1 137 ? 32.594  -14.740 26.486 1.00 16.40  ? 179  VAL B CB    1 
ATOM   4939 C CG1   . VAL B 1 137 ? 31.364  -15.570 26.313 1.00 18.98  ? 179  VAL B CG1   1 
ATOM   4940 C CG2   . VAL B 1 137 ? 33.328  -14.542 25.152 1.00 15.57  ? 179  VAL B CG2   1 
ATOM   4941 N N     . PRO B 1 138 ? 33.989  -12.630 28.573 1.00 12.83  ? 180  PRO B N     1 
ATOM   4942 C CA    . PRO B 1 138 ? 35.345  -12.111 28.794 1.00 13.40  ? 180  PRO B CA    1 
ATOM   4943 C C     . PRO B 1 138 ? 36.357  -13.056 28.138 1.00 13.20  ? 180  PRO B C     1 
ATOM   4944 O O     . PRO B 1 138 ? 35.996  -14.160 27.756 1.00 15.58  ? 180  PRO B O     1 
ATOM   4945 C CB    . PRO B 1 138 ? 35.440  -12.097 30.324 1.00 14.15  ? 180  PRO B CB    1 
ATOM   4946 C CG    . PRO B 1 138 ? 34.625  -13.366 30.701 1.00 15.79  ? 180  PRO B CG    1 
ATOM   4947 C CD    . PRO B 1 138 ? 33.474  -13.398 29.707 1.00 13.74  ? 180  PRO B CD    1 
ATOM   4948 N N     . ASP B 1 139 ? 37.610  -12.640 27.997 1.00 13.20  ? 181  ASP B N     1 
ATOM   4949 C CA    . ASP B 1 139 ? 38.659  -13.393 27.355 1.00 16.37  ? 181  ASP B CA    1 
ATOM   4950 C C     . ASP B 1 139 ? 39.302  -14.381 28.326 1.00 18.26  ? 181  ASP B C     1 
ATOM   4951 O O     . ASP B 1 139 ? 40.505  -14.341 28.587 1.00 23.92  ? 181  ASP B O     1 
ATOM   4952 C CB    . ASP B 1 139 ? 39.700  -12.424 26.814 1.00 17.36  ? 181  ASP B CB    1 
ATOM   4953 C CG    . ASP B 1 139 ? 40.657  -13.074 25.827 1.00 21.19  ? 181  ASP B CG    1 
ATOM   4954 O OD1   . ASP B 1 139 ? 40.415  -14.217 25.459 1.00 21.72  ? 181  ASP B OD1   1 
ATOM   4955 O OD2   . ASP B 1 139 ? 41.609  -12.405 25.455 1.00 22.49  ? 181  ASP B OD2   1 
ATOM   4956 N N     . VAL B 1 140 ? 38.494  -15.291 28.815 1.00 18.41  ? 182  VAL B N     1 
ATOM   4957 C CA    . VAL B 1 140 ? 38.887  -16.301 29.786 1.00 28.29  ? 182  VAL B CA    1 
ATOM   4958 C C     . VAL B 1 140 ? 38.911  -17.691 29.148 1.00 37.57  ? 182  VAL B C     1 
ATOM   4959 O O     . VAL B 1 140 ? 38.462  -17.922 28.004 1.00 39.95  ? 182  VAL B O     1 
ATOM   4960 C CB    . VAL B 1 140 ? 37.847  -16.334 30.909 1.00 31.64  ? 182  VAL B CB    1 
ATOM   4961 C CG1   . VAL B 1 140 ? 37.702  -14.991 31.608 1.00 28.99  ? 182  VAL B CG1   1 
ATOM   4962 C CG2   . VAL B 1 140 ? 36.521  -16.830 30.333 1.00 29.39  ? 182  VAL B CG2   1 
ATOM   4963 N N     . GLY B 1 141 ? 39.357  -18.648 29.963 1.00 35.09  ? 183  GLY B N     1 
ATOM   4964 C CA    . GLY B 1 141 ? 39.498  -20.022 29.520 1.00 45.00  ? 183  GLY B CA    1 
ATOM   4965 C C     . GLY B 1 141 ? 38.178  -20.749 29.690 1.00 42.17  ? 183  GLY B C     1 
ATOM   4966 O O     . GLY B 1 141 ? 37.113  -20.131 29.659 1.00 39.34  ? 183  GLY B O     1 
ATOM   4967 N N     . PRO B 1 142 ? 38.195  -22.074 29.932 1.00 36.94  ? 184  PRO B N     1 
ATOM   4968 C CA    . PRO B 1 142 ? 36.968  -22.853 29.801 1.00 33.67  ? 184  PRO B CA    1 
ATOM   4969 C C     . PRO B 1 142 ? 35.874  -22.604 30.838 1.00 30.17  ? 184  PRO B C     1 
ATOM   4970 O O     . PRO B 1 142 ? 34.714  -22.882 30.550 1.00 33.43  ? 184  PRO B O     1 
ATOM   4971 C CB    . PRO B 1 142 ? 37.464  -24.322 29.872 1.00 36.91  ? 184  PRO B CB    1 
ATOM   4972 C CG    . PRO B 1 142 ? 38.794  -24.248 30.601 1.00 37.09  ? 184  PRO B CG    1 
ATOM   4973 C CD    . PRO B 1 142 ? 39.378  -22.895 30.247 1.00 38.46  ? 184  PRO B CD    1 
ATOM   4974 N N     . ILE B 1 143 ? 36.222  -22.107 32.037 1.00 26.15  ? 185  ILE B N     1 
ATOM   4975 C CA    . ILE B 1 143 ? 35.258  -21.950 33.121 1.00 24.40  ? 185  ILE B CA    1 
ATOM   4976 C C     . ILE B 1 143 ? 35.270  -20.499 33.620 1.00 22.13  ? 185  ILE B C     1 
ATOM   4977 O O     . ILE B 1 143 ? 36.284  -19.988 34.071 1.00 19.81  ? 185  ILE B O     1 
ATOM   4978 C CB    . ILE B 1 143 ? 35.568  -22.904 34.279 1.00 26.27  ? 185  ILE B CB    1 
ATOM   4979 C CG1   . ILE B 1 143 ? 35.426  -24.365 33.847 1.00 30.50  ? 185  ILE B CG1   1 
ATOM   4980 C CG2   . ILE B 1 143 ? 34.713  -22.560 35.502 1.00 27.43  ? 185  ILE B CG2   1 
ATOM   4981 C CD1   . ILE B 1 143 ? 36.124  -25.331 34.757 1.00 31.26  ? 185  ILE B CD1   1 
ATOM   4982 N N     . ALA B 1 144 ? 34.113  -19.857 33.535 1.00 17.22  ? 186  ALA B N     1 
ATOM   4983 C CA    . ALA B 1 144 ? 33.868  -18.546 34.126 1.00 15.17  ? 186  ALA B CA    1 
ATOM   4984 C C     . ALA B 1 144 ? 32.356  -18.372 34.191 1.00 12.59  ? 186  ALA B C     1 
ATOM   4985 O O     . ALA B 1 144 ? 31.626  -19.124 33.534 1.00 12.41  ? 186  ALA B O     1 
ATOM   4986 C CB    . ALA B 1 144 ? 34.513  -17.428 33.349 1.00 15.45  ? 186  ALA B CB    1 
ATOM   4987 N N     . SER B 1 145 ? 31.863  -17.402 34.957 1.00 10.47  ? 187  SER B N     1 
ATOM   4988 C CA    . SER B 1 145 ? 30.460  -17.308 35.318 1.00 11.44  ? 187  SER B CA    1 
ATOM   4989 C C     . SER B 1 145 ? 29.879  -15.974 34.867 1.00 10.97  ? 187  SER B C     1 
ATOM   4990 O O     . SER B 1 145 ? 30.396  -14.945 35.288 1.00 11.78  ? 187  SER B O     1 
ATOM   4991 C CB    . SER B 1 145 ? 30.351  -17.402 36.850 1.00 12.18  ? 187  SER B CB    1 
ATOM   4992 O OG    . SER B 1 145 ? 29.078  -16.911 37.314 1.00 14.13  ? 187  SER B OG    1 
ATOM   4993 N N     . PRO B 1 146 ? 28.774  -15.926 34.079 1.00 11.14  ? 188  PRO B N     1 
ATOM   4994 C CA    . PRO B 1 146 ? 28.103  -14.659 33.847 1.00 11.77  ? 188  PRO B CA    1 
ATOM   4995 C C     . PRO B 1 146 ? 27.749  -13.897 35.117 1.00 11.97  ? 188  PRO B C     1 
ATOM   4996 O O     . PRO B 1 146 ? 27.892  -12.666 35.173 1.00 11.69  ? 188  PRO B O     1 
ATOM   4997 C CB    . PRO B 1 146 ? 26.839  -15.043 33.046 1.00 13.27  ? 188  PRO B CB    1 
ATOM   4998 C CG    . PRO B 1 146 ? 27.019  -16.437 32.597 1.00 13.48  ? 188  PRO B CG    1 
ATOM   4999 C CD    . PRO B 1 146 ? 28.237  -17.017 33.245 1.00 12.06  ? 188  PRO B CD    1 
ATOM   5000 N N     . VAL B 1 147 ? 27.325  -14.628 36.125 1.00 9.62   ? 189  VAL B N     1 
ATOM   5001 C CA    . VAL B 1 147 ? 26.980  -13.976 37.371 1.00 10.25  ? 189  VAL B CA    1 
ATOM   5002 C C     . VAL B 1 147 ? 28.277  -13.406 37.996 1.00 9.93   ? 189  VAL B C     1 
ATOM   5003 O O     . VAL B 1 147 ? 28.287  -12.220 38.342 1.00 10.54  ? 189  VAL B O     1 
ATOM   5004 C CB    . VAL B 1 147 ? 26.184  -14.923 38.297 1.00 10.50  ? 189  VAL B CB    1 
ATOM   5005 C CG1   . VAL B 1 147 ? 26.048  -14.318 39.687 1.00 12.06  ? 189  VAL B CG1   1 
ATOM   5006 C CG2   . VAL B 1 147 ? 24.840  -15.322 37.657 1.00 12.76  ? 189  VAL B CG2   1 
ATOM   5007 N N     . GLY B 1 148 ? 29.290  -14.239 38.266 1.00 9.90   ? 190  GLY B N     1 
ATOM   5008 C CA    . GLY B 1 148 ? 30.460  -13.768 39.018 1.00 10.28  ? 190  GLY B CA    1 
ATOM   5009 C C     . GLY B 1 148 ? 31.120  -12.574 38.290 1.00 11.42  ? 190  GLY B C     1 
ATOM   5010 O O     . GLY B 1 148 ? 31.499  -11.566 38.848 1.00 10.13  ? 190  GLY B O     1 
ATOM   5011 N N     . ASN B 1 149 ? 31.246  -12.686 36.980 1.00 10.38  ? 191  ASN B N     1 
ATOM   5012 C CA    . ASN B 1 149 ? 31.902  -11.638 36.208 1.00 10.58  ? 191  ASN B CA    1 
ATOM   5013 C C     . ASN B 1 149 ? 31.081  -10.365 36.268 1.00 9.51   ? 191  ASN B C     1 
ATOM   5014 O O     . ASN B 1 149 ? 31.633  -9.290  36.506 1.00 10.34  ? 191  ASN B O     1 
ATOM   5015 C CB    . ASN B 1 149 ? 32.111  -12.168 34.801 1.00 10.70  ? 191  ASN B CB    1 
ATOM   5016 C CG    . ASN B 1 149 ? 32.835  -11.159 33.912 1.00 12.96  ? 191  ASN B CG    1 
ATOM   5017 O OD1   . ASN B 1 149 ? 34.068  -11.258 33.746 1.00 13.34  ? 191  ASN B OD1   1 
ATOM   5018 N ND2   . ASN B 1 149 ? 32.110  -10.164 33.460 1.00 10.30  ? 191  ASN B ND2   1 
ATOM   5019 N N     . THR B 1 150 ? 29.758  -10.466 36.071 1.00 8.86   ? 192  THR B N     1 
ATOM   5020 C CA    . THR B 1 150 ? 28.909  -9.281  36.081 1.00 8.81   ? 192  THR B CA    1 
ATOM   5021 C C     . THR B 1 150 ? 28.954  -8.592  37.443 1.00 10.11  ? 192  THR B C     1 
ATOM   5022 O O     . THR B 1 150 ? 29.038  -7.346  37.504 1.00 10.28  ? 192  THR B O     1 
ATOM   5023 C CB    . THR B 1 150 ? 27.483  -9.605  35.617 1.00 9.80   ? 192  THR B CB    1 
ATOM   5024 O OG1   . THR B 1 150 ? 27.444  -10.204 34.307 1.00 10.90  ? 192  THR B OG1   1 
ATOM   5025 C CG2   . THR B 1 150 ? 26.585  -8.398  35.746 1.00 12.40  ? 192  THR B CG2   1 
ATOM   5026 N N     . LEU B 1 151 ? 29.004  -9.387  38.527 1.00 10.56  ? 193  LEU B N     1 
ATOM   5027 C CA    . LEU B 1 151 ? 29.058  -8.790  39.858 1.00 10.94  ? 193  LEU B CA    1 
ATOM   5028 C C     . LEU B 1 151 ? 30.375  -8.064  40.189 1.00 12.18  ? 193  LEU B C     1 
ATOM   5029 O O     . LEU B 1 151 ? 30.367  -7.068  40.970 1.00 13.09  ? 193  LEU B O     1 
ATOM   5030 C CB    . LEU B 1 151 ? 28.747  -9.837  40.940 1.00 10.90  ? 193  LEU B CB    1 
ATOM   5031 C CG    . LEU B 1 151 ? 27.341  -10.443 40.863 1.00 11.54  ? 193  LEU B CG    1 
ATOM   5032 C CD1   . LEU B 1 151 ? 27.228  -11.518 41.930 1.00 13.81  ? 193  LEU B CD1   1 
ATOM   5033 C CD2   . LEU B 1 151 ? 26.267  -9.372  41.050 1.00 13.34  ? 193  LEU B CD2   1 
ATOM   5034 N N     . ASP B 1 152 ? 31.469  -8.430  39.529 1.00 11.33  ? 194  ASP B N     1 
ATOM   5035 C CA    . ASP B 1 152 ? 32.702  -7.684  39.626 1.00 11.04  ? 194  ASP B CA    1 
ATOM   5036 C C     . ASP B 1 152 ? 32.797  -6.600  38.543 1.00 9.50   ? 194  ASP B C     1 
ATOM   5037 O O     . ASP B 1 152 ? 33.843  -5.986  38.407 1.00 7.95   ? 194  ASP B O     1 
ATOM   5038 C CB    . ASP B 1 152 ? 33.910  -8.634  39.630 1.00 11.15  ? 194  ASP B CB    1 
ATOM   5039 C CG    . ASP B 1 152 ? 34.915  -8.426  40.758 1.00 12.62  ? 194  ASP B CG    1 
ATOM   5040 O OD1   . ASP B 1 152 ? 34.497  -7.949  41.866 1.00 12.23  ? 194  ASP B OD1   1 
ATOM   5041 O OD2   . ASP B 1 152 ? 36.129  -8.727  40.541 1.00 13.08  ? 194  ASP B OD2   1 
ATOM   5042 N N     . ARG B 1 153 ? 31.727  -6.416  37.745 1.00 9.50   ? 195  ARG B N     1 
ATOM   5043 C CA    . ARG B 1 153 ? 31.597  -5.437  36.678 1.00 8.79   ? 195  ARG B CA    1 
ATOM   5044 C C     . ARG B 1 153 ? 32.640  -5.642  35.587 1.00 9.61   ? 195  ARG B C     1 
ATOM   5045 O O     . ARG B 1 153 ? 33.226  -4.698  35.065 1.00 9.22   ? 195  ARG B O     1 
ATOM   5046 C CB    . ARG B 1 153 ? 31.559  -4.029  37.260 1.00 8.76   ? 195  ARG B CB    1 
ATOM   5047 C CG    . ARG B 1 153 ? 30.425  -3.821  38.228 1.00 8.61   ? 195  ARG B CG    1 
ATOM   5048 C CD    . ARG B 1 153 ? 30.216  -2.370  38.566 1.00 8.74   ? 195  ARG B CD    1 
ATOM   5049 N NE    . ARG B 1 153 ? 31.349  -1.775  39.257 1.00 10.05  ? 195  ARG B NE    1 
ATOM   5050 C CZ    . ARG B 1 153 ? 31.386  -1.457  40.546 1.00 9.35   ? 195  ARG B CZ    1 
ATOM   5051 N NH1   . ARG B 1 153 ? 30.386  -1.714  41.364 1.00 10.71  ? 195  ARG B NH1   1 
ATOM   5052 N NH2   . ARG B 1 153 ? 32.458  -0.885  41.036 1.00 9.22   ? 195  ARG B NH2   1 
ATOM   5053 N N     . GLY B 1 154 ? 32.773  -6.912  35.191 1.00 8.89   ? 196  GLY B N     1 
ATOM   5054 C CA    . GLY B 1 154 ? 33.608  -7.323  34.080 1.00 8.34   ? 196  GLY B CA    1 
ATOM   5055 C C     . GLY B 1 154 ? 33.050  -6.924  32.727 1.00 10.46  ? 196  GLY B C     1 
ATOM   5056 O O     . GLY B 1 154 ? 31.963  -6.365  32.570 1.00 10.27  ? 196  GLY B O     1 
ATOM   5057 N N     . VAL B 1 155 ? 33.853  -7.278  31.698 1.00 10.48  ? 197  VAL B N     1 
ATOM   5058 C CA    . VAL B 1 155 ? 33.766  -6.713  30.365 1.00 11.43  ? 197  VAL B CA    1 
ATOM   5059 C C     . VAL B 1 155 ? 33.982  -7.794  29.315 1.00 10.89  ? 197  VAL B C     1 
ATOM   5060 O O     . VAL B 1 155 ? 34.900  -8.619  29.475 1.00 11.36  ? 197  VAL B O     1 
ATOM   5061 C CB    . VAL B 1 155 ? 34.812  -5.601  30.235 1.00 13.54  ? 197  VAL B CB    1 
ATOM   5062 C CG1   . VAL B 1 155 ? 35.000  -5.140  28.785 1.00 14.43  ? 197  VAL B CG1   1 
ATOM   5063 C CG2   . VAL B 1 155 ? 34.482  -4.484  31.213 1.00 13.70  ? 197  VAL B CG2   1 
ATOM   5064 N N     . GLY B 1 156 ? 33.159  -7.726  28.249 1.00 10.87  ? 198  GLY B N     1 
ATOM   5065 C CA    . GLY B 1 156 ? 33.423  -8.483  27.043 1.00 10.84  ? 198  GLY B CA    1 
ATOM   5066 C C     . GLY B 1 156 ? 33.309  -7.615  25.789 1.00 11.67  ? 198  GLY B C     1 
ATOM   5067 O O     . GLY B 1 156 ? 33.339  -6.386  25.862 1.00 11.38  ? 198  GLY B O     1 
ATOM   5068 N N     . TYR B 1 157 ? 33.183  -8.297  24.636 1.00 11.53  ? 199  TYR B N     1 
ATOM   5069 C CA    . TYR B 1 157 ? 33.632  -7.723  23.371 1.00 10.86  ? 199  TYR B CA    1 
ATOM   5070 C C     . TYR B 1 157 ? 32.562  -7.740  22.270 1.00 12.46  ? 199  TYR B C     1 
ATOM   5071 O O     . TYR B 1 157 ? 32.940  -7.576  21.101 1.00 10.88  ? 199  TYR B O     1 
ATOM   5072 C CB    . TYR B 1 157 ? 35.011  -8.277  22.962 1.00 11.77  ? 199  TYR B CB    1 
ATOM   5073 C CG    . TYR B 1 157 ? 35.965  -8.122  24.112 1.00 11.71  ? 199  TYR B CG    1 
ATOM   5074 C CD1   . TYR B 1 157 ? 36.292  -6.868  24.585 1.00 11.25  ? 199  TYR B CD1   1 
ATOM   5075 C CD2   . TYR B 1 157 ? 36.274  -9.211  24.912 1.00 11.90  ? 199  TYR B CD2   1 
ATOM   5076 C CE1   . TYR B 1 157 ? 36.997  -6.691  25.778 1.00 11.38  ? 199  TYR B CE1   1 
ATOM   5077 C CE2   . TYR B 1 157 ? 37.027  -9.050  26.070 1.00 11.62  ? 199  TYR B CE2   1 
ATOM   5078 C CZ    . TYR B 1 157 ? 37.388  -7.788  26.514 1.00 10.66  ? 199  TYR B CZ    1 
ATOM   5079 O OH    . TYR B 1 157 ? 38.096  -7.677  27.716 1.00 11.76  ? 199  TYR B OH    1 
ATOM   5080 N N     . THR B 1 158 ? 31.280  -7.766  22.641 1.00 11.21  ? 200  THR B N     1 
ATOM   5081 C CA    . THR B 1 158 ? 30.173  -7.545  21.710 1.00 12.18  ? 200  THR B CA    1 
ATOM   5082 C C     . THR B 1 158 ? 29.550  -6.202  22.047 1.00 10.91  ? 200  THR B C     1 
ATOM   5083 O O     . THR B 1 158 ? 29.965  -5.485  22.999 1.00 10.98  ? 200  THR B O     1 
ATOM   5084 C CB    . THR B 1 158 ? 29.192  -8.748  21.650 1.00 12.84  ? 200  THR B CB    1 
ATOM   5085 O OG1   . THR B 1 158 ? 28.244  -8.591  22.718 1.00 11.95  ? 200  THR B OG1   1 
ATOM   5086 C CG2   . THR B 1 158 ? 29.836  -10.121 21.755 1.00 14.35  ? 200  THR B CG2   1 
ATOM   5087 N N     . PRO B 1 159 ? 28.471  -5.775  21.376 1.00 12.10  ? 201  PRO B N     1 
ATOM   5088 C CA    . PRO B 1 159 ? 27.743  -4.592  21.856 1.00 11.60  ? 201  PRO B CA    1 
ATOM   5089 C C     . PRO B 1 159 ? 27.216  -4.674  23.289 1.00 10.42  ? 201  PRO B C     1 
ATOM   5090 O O     . PRO B 1 159 ? 26.872  -3.630  23.848 1.00 11.89  ? 201  PRO B O     1 
ATOM   5091 C CB    . PRO B 1 159 ? 26.593  -4.485  20.857 1.00 12.39  ? 201  PRO B CB    1 
ATOM   5092 C CG    . PRO B 1 159 ? 27.183  -5.105  19.576 1.00 12.64  ? 201  PRO B CG    1 
ATOM   5093 C CD    . PRO B 1 159 ? 27.913  -6.313  20.108 1.00 12.28  ? 201  PRO B CD    1 
ATOM   5094 N N     . TYR B 1 160 ? 27.084  -5.897  23.819 1.00 10.61  ? 202  TYR B N     1 
ATOM   5095 C CA    . TYR B 1 160 ? 26.667  -6.130  25.205 1.00 10.87  ? 202  TYR B CA    1 
ATOM   5096 C C     . TYR B 1 160 ? 27.900  -6.296  26.117 1.00 11.10  ? 202  TYR B C     1 
ATOM   5097 O O     . TYR B 1 160 ? 27.794  -6.923  27.191 1.00 11.64  ? 202  TYR B O     1 
ATOM   5098 C CB    . TYR B 1 160 ? 25.693  -7.312  25.277 1.00 10.69  ? 202  TYR B CB    1 
ATOM   5099 C CG    . TYR B 1 160 ? 24.253  -7.056  24.859 1.00 10.69  ? 202  TYR B CG    1 
ATOM   5100 C CD1   . TYR B 1 160 ? 23.901  -6.204  23.820 1.00 12.90  ? 202  TYR B CD1   1 
ATOM   5101 C CD2   . TYR B 1 160 ? 23.206  -7.708  25.508 1.00 10.96  ? 202  TYR B CD2   1 
ATOM   5102 C CE1   . TYR B 1 160 ? 22.588  -6.032  23.407 1.00 12.79  ? 202  TYR B CE1   1 
ATOM   5103 C CE2   . TYR B 1 160 ? 21.893  -7.553  25.093 1.00 11.23  ? 202  TYR B CE2   1 
ATOM   5104 C CZ    . TYR B 1 160 ? 21.571  -6.703  24.065 1.00 12.80  ? 202  TYR B CZ    1 
ATOM   5105 O OH    . TYR B 1 160 ? 20.263  -6.523  23.700 1.00 13.00  ? 202  TYR B OH    1 
ATOM   5106 N N     . GLY B 1 161 ? 28.997  -5.595  25.795 1.00 11.02  ? 203  GLY B N     1 
ATOM   5107 C CA    . GLY B 1 161 ? 30.246  -5.857  26.485 1.00 9.95   ? 203  GLY B CA    1 
ATOM   5108 C C     . GLY B 1 161 ? 30.315  -5.285  27.889 1.00 10.45  ? 203  GLY B C     1 
ATOM   5109 O O     . GLY B 1 161 ? 31.082  -5.830  28.696 1.00 10.88  ? 203  GLY B O     1 
ATOM   5110 N N     . GLU B 1 162 ? 29.637  -4.167  28.151 1.00 11.27  ? 204  GLU B N     1 
ATOM   5111 C CA    . GLU B 1 162 ? 29.665  -3.604  29.504 1.00 11.16  ? 204  GLU B CA    1 
ATOM   5112 C C     . GLU B 1 162 ? 28.653  -4.353  30.370 1.00 10.67  ? 204  GLU B C     1 
ATOM   5113 O O     . GLU B 1 162 ? 27.485  -3.982  30.480 1.00 11.69  ? 204  GLU B O     1 
ATOM   5114 C CB    . GLU B 1 162 ? 29.439  -2.103  29.471 1.00 11.04  ? 204  GLU B CB    1 
ATOM   5115 C CG    . GLU B 1 162 ? 29.610  -1.441  30.821 1.00 13.70  ? 204  GLU B CG    1 
ATOM   5116 C CD    . GLU B 1 162 ? 30.999  -1.499  31.409 1.00 13.94  ? 204  GLU B CD    1 
ATOM   5117 O OE1   . GLU B 1 162 ? 32.012  -1.234  30.655 1.00 16.83  ? 204  GLU B OE1   1 
ATOM   5118 O OE2   . GLU B 1 162 ? 31.117  -1.919  32.560 1.00 12.53  ? 204  GLU B OE2   1 
ATOM   5119 N N     . HIS B 1 163 ? 29.086  -5.510  30.927 1.00 11.16  ? 205  HIS B N     1 
ATOM   5120 C CA    . HIS B 1 163 ? 28.188  -6.517  31.486 1.00 10.37  ? 205  HIS B CA    1 
ATOM   5121 C C     . HIS B 1 163 ? 27.141  -6.001  32.479 1.00 10.71  ? 205  HIS B C     1 
ATOM   5122 O O     . HIS B 1 163 ? 25.955  -6.291  32.356 1.00 11.16  ? 205  HIS B O     1 
ATOM   5123 C CB    . HIS B 1 163 ? 28.965  -7.690  32.076 1.00 11.22  ? 205  HIS B CB    1 
ATOM   5124 C CG    . HIS B 1 163 ? 29.748  -8.459  31.110 1.00 11.64  ? 205  HIS B CG    1 
ATOM   5125 N ND1   . HIS B 1 163 ? 30.736  -9.396  31.397 1.00 12.02  ? 205  HIS B ND1   1 
ATOM   5126 C CD2   . HIS B 1 163 ? 29.572  -8.461  29.760 1.00 12.02  ? 205  HIS B CD2   1 
ATOM   5127 C CE1   . HIS B 1 163 ? 31.160  -9.894  30.251 1.00 12.40  ? 205  HIS B CE1   1 
ATOM   5128 N NE2   . HIS B 1 163 ? 30.439  -9.380  29.262 1.00 12.86  ? 205  HIS B NE2   1 
ATOM   5129 N N     . PHE B 1 164 ? 27.521  -5.157  33.427 1.00 9.90   ? 206  PHE B N     1 
ATOM   5130 C CA    . PHE B 1 164 ? 26.574  -4.702  34.440 1.00 10.08  ? 206  PHE B CA    1 
ATOM   5131 C C     . PHE B 1 164 ? 25.460  -3.855  33.799 1.00 11.05  ? 206  PHE B C     1 
ATOM   5132 O O     . PHE B 1 164 ? 24.342  -3.817  34.321 1.00 12.07  ? 206  PHE B O     1 
ATOM   5133 C CB    . PHE B 1 164 ? 27.281  -3.968  35.594 1.00 11.08  ? 206  PHE B CB    1 
ATOM   5134 C CG    . PHE B 1 164 ? 26.388  -3.488  36.701 1.00 11.65  ? 206  PHE B CG    1 
ATOM   5135 C CD1   . PHE B 1 164 ? 25.414  -4.305  37.262 1.00 12.52  ? 206  PHE B CD1   1 
ATOM   5136 C CD2   . PHE B 1 164 ? 26.497  -2.182  37.177 1.00 12.87  ? 206  PHE B CD2   1 
ATOM   5137 C CE1   . PHE B 1 164 ? 24.539  -3.813  38.235 1.00 13.14  ? 206  PHE B CE1   1 
ATOM   5138 C CE2   . PHE B 1 164 ? 25.662  -1.705  38.202 1.00 14.54  ? 206  PHE B CE2   1 
ATOM   5139 C CZ    . PHE B 1 164 ? 24.695  -2.522  38.730 1.00 13.72  ? 206  PHE B CZ    1 
ATOM   5140 N N     . MET B 1 165 ? 25.690  -3.205  32.645 1.00 11.19  ? 207  MET B N     1 
ATOM   5141 C CA    . MET B 1 165 ? 24.604  -2.473  32.023 1.00 13.43  ? 207  MET B CA    1 
ATOM   5142 C C     . MET B 1 165 ? 23.456  -3.406  31.630 1.00 13.93  ? 207  MET B C     1 
ATOM   5143 O O     . MET B 1 165 ? 22.331  -2.939  31.522 1.00 15.10  ? 207  MET B O     1 
ATOM   5144 C CB    . MET B 1 165 ? 25.042  -1.764  30.736 1.00 16.98  ? 207  MET B CB    1 
ATOM   5145 C CG    . MET B 1 165 ? 25.905  -0.584  30.940 1.00 25.11  ? 207  MET B CG    1 
ATOM   5146 S SD    . MET B 1 165 ? 26.177  0.353   29.361 1.00 40.44  ? 207  MET B SD    1 
ATOM   5147 C CE    . MET B 1 165 ? 27.175  1.766   29.866 1.00 48.00  ? 207  MET B CE    1 
ATOM   5148 N N     . PHE B 1 166 ? 23.734  -4.679  31.360 1.00 10.42  ? 208  PHE B N     1 
ATOM   5149 C CA    . PHE B 1 166 ? 22.762  -5.609  30.803 1.00 11.67  ? 208  PHE B CA    1 
ATOM   5150 C C     . PHE B 1 166 ? 22.188  -6.548  31.857 1.00 10.56  ? 208  PHE B C     1 
ATOM   5151 O O     . PHE B 1 166 ? 21.388  -7.424  31.560 1.00 12.89  ? 208  PHE B O     1 
ATOM   5152 C CB    . PHE B 1 166 ? 23.434  -6.368  29.632 1.00 12.70  ? 208  PHE B CB    1 
ATOM   5153 C CG    . PHE B 1 166 ? 23.813  -5.429  28.535 1.00 14.13  ? 208  PHE B CG    1 
ATOM   5154 C CD1   . PHE B 1 166 ? 22.861  -5.029  27.592 1.00 14.99  ? 208  PHE B CD1   1 
ATOM   5155 C CD2   . PHE B 1 166 ? 25.074  -4.830  28.489 1.00 15.78  ? 208  PHE B CD2   1 
ATOM   5156 C CE1   . PHE B 1 166 ? 23.153  -4.055  26.648 1.00 15.52  ? 208  PHE B CE1   1 
ATOM   5157 C CE2   . PHE B 1 166 ? 25.325  -3.814  27.567 1.00 14.79  ? 208  PHE B CE2   1 
ATOM   5158 C CZ    . PHE B 1 166 ? 24.383  -3.462  26.637 1.00 16.35  ? 208  PHE B CZ    1 
ATOM   5159 N N     . GLN B 1 167 ? 22.590  -6.385  33.124 1.00 9.67   ? 209  GLN B N     1 
ATOM   5160 C CA    . GLN B 1 167 ? 21.963  -7.099  34.215 1.00 10.03  ? 209  GLN B CA    1 
ATOM   5161 C C     . GLN B 1 167 ? 20.567  -6.538  34.460 1.00 9.16   ? 209  GLN B C     1 
ATOM   5162 O O     . GLN B 1 167 ? 20.351  -5.331  34.388 1.00 10.65  ? 209  GLN B O     1 
ATOM   5163 C CB    . GLN B 1 167 ? 22.871  -6.949  35.452 1.00 9.60   ? 209  GLN B CB    1 
ATOM   5164 C CG    . GLN B 1 167 ? 22.355  -7.628  36.696 1.00 10.82  ? 209  GLN B CG    1 
ATOM   5165 C CD    . GLN B 1 167 ? 21.596  -6.713  37.622 1.00 10.78  ? 209  GLN B CD    1 
ATOM   5166 O OE1   . GLN B 1 167 ? 21.872  -5.524  37.697 1.00 15.57  ? 209  GLN B OE1   1 
ATOM   5167 N NE2   . GLN B 1 167 ? 20.632  -7.251  38.301 1.00 10.66  ? 209  GLN B NE2   1 
ATOM   5168 N N     . CYS B 1 168 ? 19.625  -7.386  34.808 1.00 9.68   ? 210  CYS B N     1 
ATOM   5169 C CA    . CYS B 1 168 ? 18.249  -6.978  35.069 1.00 9.36   ? 210  CYS B CA    1 
ATOM   5170 C C     . CYS B 1 168 ? 17.551  -7.934  36.028 1.00 10.68  ? 210  CYS B C     1 
ATOM   5171 O O     . CYS B 1 168 ? 17.197  -9.039  35.638 1.00 10.68  ? 210  CYS B O     1 
ATOM   5172 C CB    . CYS B 1 168 ? 17.456  -6.888  33.758 1.00 9.64   ? 210  CYS B CB    1 
ATOM   5173 S SG    . CYS B 1 168 ? 15.866  -6.003  33.905 1.00 10.54  ? 210  CYS B SG    1 
ATOM   5174 N N     . GLY B 1 169 ? 17.363  -7.459  37.265 1.00 10.63  ? 211  GLY B N     1 
ATOM   5175 C CA    . GLY B 1 169 ? 16.784  -8.244  38.344 1.00 10.38  ? 211  GLY B CA    1 
ATOM   5176 C C     . GLY B 1 169 ? 17.858  -9.144  38.987 1.00 10.88  ? 211  GLY B C     1 
ATOM   5177 O O     . GLY B 1 169 ? 18.700  -9.725  38.294 1.00 10.50  ? 211  GLY B O     1 
ATOM   5178 N N     . MET B 1 170 ? 17.837  -9.241  40.312 1.00 10.13  ? 212  MET B N     1 
ATOM   5179 C CA    . MET B 1 170 ? 18.639  -10.223 41.013 1.00 10.51  ? 212  MET B CA    1 
ATOM   5180 C C     . MET B 1 170 ? 17.878  -10.657 42.277 1.00 10.22  ? 212  MET B C     1 
ATOM   5181 O O     . MET B 1 170 ? 17.024  -9.946  42.823 1.00 9.31   ? 212  MET B O     1 
ATOM   5182 C CB    . MET B 1 170 ? 20.047  -9.720  41.334 1.00 10.41  ? 212  MET B CB    1 
ATOM   5183 C CG    . MET B 1 170 ? 20.077  -8.547  42.253 1.00 11.40  ? 212  MET B CG    1 
ATOM   5184 S SD    . MET B 1 170 ? 21.746  -8.134  42.806 1.00 13.21  ? 212  MET B SD    1 
ATOM   5185 C CE    . MET B 1 170 ? 22.671  -7.801  41.331 1.00 13.20  ? 212  MET B CE    1 
ATOM   5186 N N     . GLU B 1 171 ? 18.186  -11.874 42.755 1.00 10.54  ? 213  GLU B N     1 
ATOM   5187 C CA    . GLU B 1 171 ? 17.822  -12.298 44.098 1.00 8.60   ? 213  GLU B CA    1 
ATOM   5188 C C     . GLU B 1 171 ? 19.082  -12.358 44.949 1.00 8.88   ? 213  GLU B C     1 
ATOM   5189 O O     . GLU B 1 171 ? 20.136  -12.830 44.504 1.00 10.00  ? 213  GLU B O     1 
ATOM   5190 C CB    . GLU B 1 171 ? 17.198  -13.691 44.090 1.00 9.97   ? 213  GLU B CB    1 
ATOM   5191 C CG    . GLU B 1 171 ? 16.724  -14.222 45.445 1.00 10.56  ? 213  GLU B CG    1 
ATOM   5192 C CD    . GLU B 1 171 ? 16.148  -15.630 45.320 1.00 12.75  ? 213  GLU B CD    1 
ATOM   5193 O OE1   . GLU B 1 171 ? 16.934  -16.616 45.167 1.00 12.97  ? 213  GLU B OE1   1 
ATOM   5194 O OE2   . GLU B 1 171 ? 14.896  -15.716 45.227 1.00 15.39  ? 213  GLU B OE2   1 
ATOM   5195 N N     . VAL B 1 172 ? 18.964  -11.841 46.175 1.00 9.59   ? 214  VAL B N     1 
ATOM   5196 C CA    . VAL B 1 172 ? 20.082  -11.761 47.105 1.00 10.64  ? 214  VAL B CA    1 
ATOM   5197 C C     . VAL B 1 172 ? 19.663  -12.404 48.413 1.00 11.41  ? 214  VAL B C     1 
ATOM   5198 O O     . VAL B 1 172 ? 18.552  -12.176 48.914 1.00 13.02  ? 214  VAL B O     1 
ATOM   5199 C CB    . VAL B 1 172 ? 20.434  -10.284 47.364 1.00 13.72  ? 214  VAL B CB    1 
ATOM   5200 C CG1   . VAL B 1 172 ? 21.578  -10.156 48.317 1.00 15.35  ? 214  VAL B CG1   1 
ATOM   5201 C CG2   . VAL B 1 172 ? 20.742  -9.544  46.057 1.00 15.25  ? 214  VAL B CG2   1 
ATOM   5202 N N     . CYS B 1 173 ? 20.544  -13.236 48.972 1.00 10.42  ? 215  CYS B N     1 
ATOM   5203 C CA    . CYS B 1 173 ? 20.465  -13.617 50.375 1.00 10.76  ? 215  CYS B CA    1 
ATOM   5204 C C     . CYS B 1 173 ? 21.190  -12.537 51.171 1.00 10.45  ? 215  CYS B C     1 
ATOM   5205 O O     . CYS B 1 173 ? 22.406  -12.348 51.009 1.00 10.47  ? 215  CYS B O     1 
ATOM   5206 C CB    . CYS B 1 173 ? 21.083  -15.012 50.571 1.00 11.65  ? 215  CYS B CB    1 
ATOM   5207 S SG    . CYS B 1 173 ? 20.982  -15.627 52.293 1.00 12.76  ? 215  CYS B SG    1 
ATOM   5208 N N     . LEU B 1 174 ? 20.428  -11.806 51.999 1.00 10.09  ? 216  LEU B N     1 
ATOM   5209 C CA    . LEU B 1 174 ? 20.982  -10.776 52.885 1.00 10.92  ? 216  LEU B CA    1 
ATOM   5210 C C     . LEU B 1 174 ? 21.764  -11.429 54.018 1.00 10.89  ? 216  LEU B C     1 
ATOM   5211 O O     . LEU B 1 174 ? 21.659  -12.650 54.237 1.00 10.56  ? 216  LEU B O     1 
ATOM   5212 C CB    . LEU B 1 174 ? 19.840  -9.926  53.401 1.00 10.93  ? 216  LEU B CB    1 
ATOM   5213 C CG    . LEU B 1 174 ? 19.087  -9.214  52.281 1.00 12.78  ? 216  LEU B CG    1 
ATOM   5214 C CD1   . LEU B 1 174 ? 17.842  -8.573  52.854 1.00 14.27  ? 216  LEU B CD1   1 
ATOM   5215 C CD2   . LEU B 1 174 ? 19.983  -8.208  51.566 1.00 13.49  ? 216  LEU B CD2   1 
ATOM   5216 N N     . PRO B 1 175 ? 22.601  -10.651 54.712 1.00 10.58  ? 217  PRO B N     1 
ATOM   5217 C CA    . PRO B 1 175 ? 23.390  -11.208 55.811 1.00 13.19  ? 217  PRO B CA    1 
ATOM   5218 C C     . PRO B 1 175 ? 22.608  -11.878 56.913 1.00 12.80  ? 217  PRO B C     1 
ATOM   5219 O O     . PRO B 1 175 ? 23.212  -12.651 57.595 1.00 15.28  ? 217  PRO B O     1 
ATOM   5220 C CB    . PRO B 1 175 ? 24.099  -9.957  56.325 1.00 12.89  ? 217  PRO B CB    1 
ATOM   5221 C CG    . PRO B 1 175 ? 24.350  -9.187  55.078 1.00 11.12  ? 217  PRO B CG    1 
ATOM   5222 C CD    . PRO B 1 175 ? 23.011  -9.268  54.406 1.00 11.05  ? 217  PRO B CD    1 
ATOM   5223 N N     . ASP B 1 176 ? 21.310  -11.587 57.058 1.00 13.07  ? 218  ASP B N     1 
ATOM   5224 C CA    . ASP B 1 176 ? 20.487  -12.232 58.087 1.00 16.63  ? 218  ASP B CA    1 
ATOM   5225 C C     . ASP B 1 176 ? 19.850  -13.538 57.588 1.00 16.99  ? 218  ASP B C     1 
ATOM   5226 O O     . ASP B 1 176 ? 19.057  -14.146 58.307 1.00 19.95  ? 218  ASP B O     1 
ATOM   5227 C CB    . ASP B 1 176 ? 19.391  -11.301 58.587 1.00 19.28  ? 218  ASP B CB    1 
ATOM   5228 C CG    . ASP B 1 176 ? 18.327  -10.879 57.578 1.00 22.14  ? 218  ASP B CG    1 
ATOM   5229 O OD1   . ASP B 1 176 ? 18.435  -11.206 56.400 1.00 20.30  ? 218  ASP B OD1   1 
ATOM   5230 O OD2   . ASP B 1 176 ? 17.395  -10.171 57.965 1.00 28.42  ? 218  ASP B OD2   1 
ATOM   5231 N N     . GLY B 1 177 ? 20.046  -13.904 56.320 1.00 13.44  ? 219  GLY B N     1 
ATOM   5232 C CA    . GLY B 1 177 ? 19.489  -15.131 55.793 1.00 12.89  ? 219  GLY B CA    1 
ATOM   5233 C C     . GLY B 1 177 ? 18.166  -14.979 55.048 1.00 12.27  ? 219  GLY B C     1 
ATOM   5234 O O     . GLY B 1 177 ? 17.660  -15.968 54.526 1.00 13.51  ? 219  GLY B O     1 
ATOM   5235 N N     . ARG B 1 178 ? 17.585  -13.762 55.000 1.00 12.35  ? 220  ARG B N     1 
ATOM   5236 C CA    . ARG B 1 178 ? 16.384  -13.523 54.203 1.00 11.96  ? 220  ARG B CA    1 
ATOM   5237 C C     . ARG B 1 178 ? 16.717  -13.309 52.727 1.00 11.41  ? 220  ARG B C     1 
ATOM   5238 O O     . ARG B 1 178 ? 17.741  -12.726 52.423 1.00 13.18  ? 220  ARG B O     1 
ATOM   5239 C CB    . ARG B 1 178 ? 15.676  -12.291 54.773 1.00 14.72  ? 220  ARG B CB    1 
ATOM   5240 C CG    . ARG B 1 178 ? 15.098  -12.550 56.163 1.00 17.19  ? 220  ARG B CG    1 
ATOM   5241 C CD    . ARG B 1 178 ? 14.150  -11.430 56.587 1.00 21.37  ? 220  ARG B CD    1 
ATOM   5242 N NE    . ARG B 1 178 ? 14.843  -10.149 56.608 1.00 23.94  ? 220  ARG B NE    1 
ATOM   5243 C CZ    . ARG B 1 178 ? 14.243  -8.954  56.666 1.00 27.98  ? 220  ARG B CZ    1 
ATOM   5244 N NH1   . ARG B 1 178 ? 12.929  -8.868  56.683 1.00 25.48  ? 220  ARG B NH1   1 
ATOM   5245 N NH2   . ARG B 1 178 ? 14.971  -7.853  56.605 1.00 24.19  ? 220  ARG B NH2   1 
ATOM   5246 N N     . LEU B 1 179 ? 15.817  -13.698 51.841 1.00 11.83  ? 221  LEU B N     1 
ATOM   5247 C CA    . LEU B 1 179 ? 15.991  -13.463 50.413 1.00 11.11  ? 221  LEU B CA    1 
ATOM   5248 C C     . LEU B 1 179 ? 15.278  -12.159 50.062 1.00 11.02  ? 221  LEU B C     1 
ATOM   5249 O O     . LEU B 1 179 ? 14.169  -11.890 50.534 1.00 12.85  ? 221  LEU B O     1 
ATOM   5250 C CB    . LEU B 1 179 ? 15.417  -14.618 49.597 1.00 11.67  ? 221  LEU B CB    1 
ATOM   5251 C CG    . LEU B 1 179 ? 16.047  -15.992 49.846 1.00 12.67  ? 221  LEU B CG    1 
ATOM   5252 C CD1   . LEU B 1 179 ? 15.401  -17.043 48.988 1.00 13.69  ? 221  LEU B CD1   1 
ATOM   5253 C CD2   . LEU B 1 179 ? 17.534  -15.956 49.596 1.00 13.76  ? 221  LEU B CD2   1 
ATOM   5254 N N     . MET B 1 180 ? 15.921  -11.384 49.229 1.00 7.72   ? 222  MET B N     1 
ATOM   5255 C CA    . MET B 1 180 ? 15.307  -10.193 48.616 1.00 9.06   ? 222  MET B CA    1 
ATOM   5256 C C     . MET B 1 180 ? 15.463  -10.204 47.092 1.00 10.12  ? 222  MET B C     1 
ATOM   5257 O O     . MET B 1 180 ? 16.566  -10.398 46.554 1.00 9.73   ? 222  MET B O     1 
ATOM   5258 C CB    . MET B 1 180 ? 15.968  -8.957  49.222 1.00 10.10  ? 222  MET B CB    1 
ATOM   5259 C CG    . MET B 1 180 ? 15.356  -7.637  48.800 1.00 10.88  ? 222  MET B CG    1 
ATOM   5260 S SD    . MET B 1 180 ? 16.104  -6.203  49.588 1.00 13.17  ? 222  MET B SD    1 
ATOM   5261 C CE    . MET B 1 180 ? 17.623  -6.071  48.648 1.00 13.31  ? 222  MET B CE    1 
ATOM   5262 N N     . ARG B 1 181 ? 14.351  -9.912  46.357 1.00 9.78   ? 223  ARG B N     1 
ATOM   5263 C CA    . ARG B 1 181 ? 14.412  -9.758  44.901 1.00 9.15   ? 223  ARG B CA    1 
ATOM   5264 C C     . ARG B 1 181 ? 14.330  -8.293  44.502 1.00 9.27   ? 223  ARG B C     1 
ATOM   5265 O O     . ARG B 1 181 ? 13.485  -7.546  45.010 1.00 11.21  ? 223  ARG B O     1 
ATOM   5266 C CB    . ARG B 1 181 ? 13.309  -10.580 44.240 1.00 9.58   ? 223  ARG B CB    1 
ATOM   5267 C CG    . ARG B 1 181 ? 13.455  -12.095 44.474 1.00 10.89  ? 223  ARG B CG    1 
ATOM   5268 C CD    . ARG B 1 181 ? 12.482  -12.880 43.621 1.00 12.86  ? 223  ARG B CD    1 
ATOM   5269 N NE    . ARG B 1 181 ? 12.832  -14.297 43.740 1.00 15.26  ? 223  ARG B NE    1 
ATOM   5270 C CZ    . ARG B 1 181 ? 12.304  -15.273 43.027 1.00 16.20  ? 223  ARG B CZ    1 
ATOM   5271 N NH1   . ARG B 1 181 ? 11.391  -15.016 42.110 1.00 14.86  ? 223  ARG B NH1   1 
ATOM   5272 N NH2   . ARG B 1 181 ? 12.784  -16.504 43.184 1.00 18.20  ? 223  ARG B NH2   1 
ATOM   5273 N N     . THR B 1 182 ? 15.234  -7.877  43.642 1.00 10.01  ? 224  THR B N     1 
ATOM   5274 C CA    . THR B 1 182 ? 15.318  -6.491  43.222 1.00 10.46  ? 224  THR B CA    1 
ATOM   5275 C C     . THR B 1 182 ? 14.368  -6.261  42.047 1.00 12.11  ? 224  THR B C     1 
ATOM   5276 O O     . THR B 1 182 ? 13.846  -7.184  41.398 1.00 10.71  ? 224  THR B O     1 
ATOM   5277 C CB    . THR B 1 182 ? 16.753  -6.115  42.846 1.00 11.25  ? 224  THR B CB    1 
ATOM   5278 O OG1   . THR B 1 182 ? 17.127  -6.821  41.656 1.00 10.74  ? 224  THR B OG1   1 
ATOM   5279 C CG2   . THR B 1 182 ? 17.772  -6.291  43.961 1.00 10.51  ? 224  THR B CG2   1 
ATOM   5280 N N     . GLY B 1 183 ? 14.256  -4.982  41.674 1.00 11.72  ? 225  GLY B N     1 
ATOM   5281 C CA    . GLY B 1 183 ? 13.487  -4.566  40.519 1.00 12.40  ? 225  GLY B CA    1 
ATOM   5282 C C     . GLY B 1 183 ? 11.981  -4.853  40.690 1.00 11.44  ? 225  GLY B C     1 
ATOM   5283 O O     . GLY B 1 183 ? 11.329  -4.531  41.697 1.00 11.20  ? 225  GLY B O     1 
ATOM   5284 N N     . MET B 1 184 ? 11.475  -5.632  39.717 1.00 12.38  ? 226  MET B N     1 
ATOM   5285 C CA    . MET B 1 184 ? 10.075  -6.017  39.735 1.00 12.83  ? 226  MET B CA    1 
ATOM   5286 C C     . MET B 1 184 ? 9.882   -7.380  40.397 1.00 12.84  ? 226  MET B C     1 
ATOM   5287 O O     . MET B 1 184 ? 8.750   -7.824  40.623 1.00 14.18  ? 226  MET B O     1 
ATOM   5288 C CB    . MET B 1 184 ? 9.509   -6.054  38.319 1.00 13.27  ? 226  MET B CB    1 
ATOM   5289 C CG    . MET B 1 184 ? 9.692   -4.767  37.537 1.00 13.73  ? 226  MET B CG    1 
ATOM   5290 S SD    . MET B 1 184 ? 9.120   -3.291  38.399 1.00 14.61  ? 226  MET B SD    1 
ATOM   5291 C CE    . MET B 1 184 ? 7.352   -3.501  38.347 1.00 15.12  ? 226  MET B CE    1 
ATOM   5292 N N     . GLY B 1 185 ? 10.981  -8.038  40.811 1.00 11.00  ? 227  GLY B N     1 
ATOM   5293 C CA    . GLY B 1 185 ? 10.969  -9.442  41.242 1.00 10.01  ? 227  GLY B CA    1 
ATOM   5294 C C     . GLY B 1 185 ? 10.240  -9.700  42.566 1.00 12.50  ? 227  GLY B C     1 
ATOM   5295 O O     . GLY B 1 185 ? 9.842   -10.844 42.824 1.00 14.37  ? 227  GLY B O     1 
ATOM   5296 N N     . SER B 1 186 ? 10.047  -8.659  43.408 1.00 13.21  ? 228  SER B N     1 
ATOM   5297 C CA    . SER B 1 186 ? 9.431   -8.873  44.716 1.00 13.31  ? 228  SER B CA    1 
ATOM   5298 C C     . SER B 1 186 ? 7.900   -8.825  44.644 1.00 16.06  ? 228  SER B C     1 
ATOM   5299 O O     . SER B 1 186 ? 7.248   -9.001  45.679 1.00 17.49  ? 228  SER B O     1 
ATOM   5300 C CB    . SER B 1 186 ? 9.967   -7.913  45.722 1.00 13.98  ? 228  SER B CB    1 
ATOM   5301 O OG    . SER B 1 186 ? 9.487   -6.578  45.465 1.00 13.84  ? 228  SER B OG    1 
ATOM   5302 N N     . ILE B 1 187 ? 7.362   -8.612  43.450 1.00 17.33  ? 229  ILE B N     1 
ATOM   5303 C CA    . ILE B 1 187 ? 5.923   -8.713  43.194 1.00 20.52  ? 229  ILE B CA    1 
ATOM   5304 C C     . ILE B 1 187 ? 5.616   -10.164 42.810 1.00 22.86  ? 229  ILE B C     1 
ATOM   5305 O O     . ILE B 1 187 ? 6.187   -10.669 41.872 1.00 22.67  ? 229  ILE B O     1 
ATOM   5306 C CB    . ILE B 1 187 ? 5.538   -7.743  42.073 1.00 21.85  ? 229  ILE B CB    1 
ATOM   5307 C CG1   . ILE B 1 187 ? 6.075   -6.318  42.260 1.00 25.48  ? 229  ILE B CG1   1 
ATOM   5308 C CG2   . ILE B 1 187 ? 4.037   -7.805  41.792 1.00 23.49  ? 229  ILE B CG2   1 
ATOM   5309 C CD1   . ILE B 1 187 ? 5.174   -5.334  42.826 1.00 33.62  ? 229  ILE B CD1   1 
ATOM   5310 N N     . LYS B 1 188 ? 4.737   -10.878 43.532 1.00 24.45  ? 230  LYS B N     1 
ATOM   5311 C CA    . LYS B 1 188 ? 4.642   -12.322 43.333 1.00 29.94  ? 230  LYS B CA    1 
ATOM   5312 C C     . LYS B 1 188 ? 4.183   -12.614 41.902 1.00 25.44  ? 230  LYS B C     1 
ATOM   5313 O O     . LYS B 1 188 ? 3.264   -11.982 41.440 1.00 26.97  ? 230  LYS B O     1 
ATOM   5314 C CB    . LYS B 1 188 ? 3.658   -12.926 44.354 1.00 37.81  ? 230  LYS B CB    1 
ATOM   5315 C CG    . LYS B 1 188 ? 3.415   -14.427 44.235 1.00 44.84  ? 230  LYS B CG    1 
ATOM   5316 C CD    . LYS B 1 188 ? 4.676   -15.264 44.137 1.00 52.62  ? 230  LYS B CD    1 
ATOM   5317 C CE    . LYS B 1 188 ? 4.372   -16.731 43.914 1.00 62.51  ? 230  LYS B CE    1 
ATOM   5318 N NZ    . LYS B 1 188 ? 5.586   -17.485 43.521 1.00 69.33  ? 230  LYS B NZ    1 
ATOM   5319 N N     . GLY B 1 189 ? 4.861   -13.532 41.201 1.00 34.74  ? 231  GLY B N     1 
ATOM   5320 C CA    . GLY B 1 189 ? 4.495   -13.849 39.821 1.00 38.56  ? 231  GLY B CA    1 
ATOM   5321 C C     . GLY B 1 189 ? 4.525   -12.616 38.904 1.00 44.52  ? 231  GLY B C     1 
ATOM   5322 O O     . GLY B 1 189 ? 3.631   -12.395 38.064 1.00 36.92  ? 231  GLY B O     1 
ATOM   5323 N N     . SER B 1 190 ? 5.537   -11.759 39.144 1.00 36.62  ? 232  SER B N     1 
ATOM   5324 C CA    . SER B 1 190 ? 5.845   -10.699 38.200 1.00 24.94  ? 232  SER B CA    1 
ATOM   5325 C C     . SER B 1 190 ? 6.391   -11.387 36.961 1.00 18.52  ? 232  SER B C     1 
ATOM   5326 O O     . SER B 1 190 ? 7.219   -12.275 37.055 1.00 19.11  ? 232  SER B O     1 
ATOM   5327 C CB    . SER B 1 190 ? 6.849   -9.694  38.739 1.00 20.01  ? 232  SER B CB    1 
ATOM   5328 O OG    . SER B 1 190 ? 7.273   -8.807  37.695 1.00 16.51  ? 232  SER B OG    1 
ATOM   5329 N N     . THR B 1 191 ? 5.994   -10.896 35.805 1.00 14.94  ? 233  THR B N     1 
ATOM   5330 C CA    . THR B 1 191 ? 6.542   -11.371 34.558 1.00 15.33  ? 233  THR B CA    1 
ATOM   5331 C C     . THR B 1 191 ? 7.526   -10.344 33.987 1.00 15.08  ? 233  THR B C     1 
ATOM   5332 O O     . THR B 1 191 ? 7.975   -10.481 32.849 1.00 13.98  ? 233  THR B O     1 
ATOM   5333 C CB    . THR B 1 191 ? 5.402   -11.734 33.600 1.00 17.50  ? 233  THR B CB    1 
ATOM   5334 O OG1   . THR B 1 191 ? 4.695   -10.529 33.291 1.00 18.03  ? 233  THR B OG1   1 
ATOM   5335 C CG2   . THR B 1 191 ? 4.539   -12.819 34.208 1.00 18.17  ? 233  THR B CG2   1 
ATOM   5336 N N     . ALA B 1 192 ? 7.927   -9.347  34.787 1.00 12.63  ? 234  ALA B N     1 
ATOM   5337 C CA    . ALA B 1 192 ? 8.740   -8.242  34.264 1.00 11.53  ? 234  ALA B CA    1 
ATOM   5338 C C     . ALA B 1 192 ? 10.123  -8.154  34.954 1.00 10.40  ? 234  ALA B C     1 
ATOM   5339 O O     . ALA B 1 192 ? 10.872  -7.168  34.841 1.00 9.83   ? 234  ALA B O     1 
ATOM   5340 C CB    . ALA B 1 192 ? 7.984   -6.964  34.412 1.00 12.61  ? 234  ALA B CB    1 
ATOM   5341 N N     . TRP B 1 193 ? 10.521  -9.228  35.640 1.00 11.12  ? 235  TRP B N     1 
ATOM   5342 C CA    . TRP B 1 193 ? 11.762  -9.177  36.435 1.00 9.86   ? 235  TRP B CA    1 
ATOM   5343 C C     . TRP B 1 193 ? 12.996  -8.968  35.554 1.00 9.70   ? 235  TRP B C     1 
ATOM   5344 O O     . TRP B 1 193 ? 13.916  -8.276  35.995 1.00 10.43  ? 235  TRP B O     1 
ATOM   5345 C CB    . TRP B 1 193 ? 11.940  -10.480 37.230 1.00 10.33  ? 235  TRP B CB    1 
ATOM   5346 C CG    . TRP B 1 193 ? 12.896  -10.462 38.382 1.00 10.81  ? 235  TRP B CG    1 
ATOM   5347 C CD1   . TRP B 1 193 ? 13.444  -9.377  38.985 1.00 10.83  ? 235  TRP B CD1   1 
ATOM   5348 C CD2   . TRP B 1 193 ? 13.416  -11.609 39.063 1.00 10.76  ? 235  TRP B CD2   1 
ATOM   5349 N NE1   . TRP B 1 193 ? 14.210  -9.767  40.063 1.00 10.15  ? 235  TRP B NE1   1 
ATOM   5350 C CE2   . TRP B 1 193 ? 14.213  -11.130 40.118 1.00 11.51  ? 235  TRP B CE2   1 
ATOM   5351 C CE3   . TRP B 1 193 ? 13.215  -12.992 38.927 1.00 13.36  ? 235  TRP B CE3   1 
ATOM   5352 C CZ2   . TRP B 1 193 ? 14.817  -12.014 41.019 1.00 11.77  ? 235  TRP B CZ2   1 
ATOM   5353 C CZ3   . TRP B 1 193 ? 13.850  -13.861 39.788 1.00 11.54  ? 235  TRP B CZ3   1 
ATOM   5354 C CH2   . TRP B 1 193 ? 14.640  -13.356 40.829 1.00 12.04  ? 235  TRP B CH2   1 
ATOM   5355 N N     . GLN B 1 194 ? 12.976  -9.504  34.321 1.00 10.87  ? 236  GLN B N     1 
ATOM   5356 C CA    . GLN B 1 194 ? 14.068  -9.348  33.375 1.00 10.95  ? 236  GLN B CA    1 
ATOM   5357 C C     . GLN B 1 194 ? 13.717  -8.331  32.294 1.00 11.21  ? 236  GLN B C     1 
ATOM   5358 O O     . GLN B 1 194 ? 14.417  -8.257  31.276 1.00 11.69  ? 236  GLN B O     1 
ATOM   5359 C CB    . GLN B 1 194 ? 14.543  -10.697 32.806 1.00 10.03  ? 236  GLN B CB    1 
ATOM   5360 C CG    . GLN B 1 194 ? 15.593  -11.381 33.744 1.00 8.05   ? 236  GLN B CG    1 
ATOM   5361 C CD    . GLN B 1 194 ? 14.940  -11.905 34.971 1.00 11.47  ? 236  GLN B CD    1 
ATOM   5362 O OE1   . GLN B 1 194 ? 14.178  -12.879 34.993 1.00 15.44  ? 236  GLN B OE1   1 
ATOM   5363 N NE2   . GLN B 1 194 ? 15.279  -11.294 36.084 1.00 10.82  ? 236  GLN B NE2   1 
ATOM   5364 N N     . ALA B 1 195 ? 12.693  -7.514  32.531 1.00 11.06  ? 237  ALA B N     1 
ATOM   5365 C CA    . ALA B 1 195 ? 12.239  -6.545  31.546 1.00 11.33  ? 237  ALA B CA    1 
ATOM   5366 C C     . ALA B 1 195 ? 12.587  -5.109  31.932 1.00 12.00  ? 237  ALA B C     1 
ATOM   5367 O O     . ALA B 1 195 ? 12.923  -4.310  31.056 1.00 10.57  ? 237  ALA B O     1 
ATOM   5368 C CB    . ALA B 1 195 ? 10.774  -6.713  31.280 1.00 12.79  ? 237  ALA B CB    1 
ATOM   5369 N N     . PHE B 1 196 ? 12.451  -4.761  33.220 1.00 10.93  ? 238  PHE B N     1 
ATOM   5370 C CA    . PHE B 1 196 ? 12.616  -3.375  33.654 1.00 10.96  ? 238  PHE B CA    1 
ATOM   5371 C C     . PHE B 1 196 ? 13.638  -3.342  34.779 1.00 10.71  ? 238  PHE B C     1 
ATOM   5372 O O     . PHE B 1 196 ? 13.407  -3.962  35.811 1.00 11.93  ? 238  PHE B O     1 
ATOM   5373 C CB    . PHE B 1 196 ? 11.281  -2.804  34.102 1.00 10.78  ? 238  PHE B CB    1 
ATOM   5374 C CG    . PHE B 1 196 ? 11.344  -1.386  34.592 1.00 10.38  ? 238  PHE B CG    1 
ATOM   5375 C CD1   . PHE B 1 196 ? 11.838  -0.417  33.773 1.00 10.86  ? 238  PHE B CD1   1 
ATOM   5376 C CD2   . PHE B 1 196 ? 10.977  -1.031  35.892 1.00 10.28  ? 238  PHE B CD2   1 
ATOM   5377 C CE1   . PHE B 1 196 ? 11.856  0.920   34.185 1.00 13.14  ? 238  PHE B CE1   1 
ATOM   5378 C CE2   . PHE B 1 196 ? 11.075  0.283   36.322 1.00 11.50  ? 238  PHE B CE2   1 
ATOM   5379 C CZ    . PHE B 1 196 ? 11.495  1.273   35.468 1.00 11.91  ? 238  PHE B CZ    1 
ATOM   5380 N N     . LYS B 1 197 ? 14.715  -2.550  34.630 1.00 11.12  ? 239  LYS B N     1 
ATOM   5381 C CA    . LYS B 1 197 ? 15.810  -2.665  35.578 1.00 11.42  ? 239  LYS B CA    1 
ATOM   5382 C C     . LYS B 1 197 ? 15.507  -2.054  36.940 1.00 12.24  ? 239  LYS B C     1 
ATOM   5383 O O     . LYS B 1 197 ? 15.975  -2.535  37.967 1.00 12.68  ? 239  LYS B O     1 
ATOM   5384 C CB    . LYS B 1 197 ? 17.075  -1.996  35.047 1.00 12.40  ? 239  LYS B CB    1 
ATOM   5385 C CG    . LYS B 1 197 ? 17.828  -2.677  33.931 1.00 14.42  ? 239  LYS B CG    1 
ATOM   5386 C CD    . LYS B 1 197 ? 18.896  -1.803  33.279 1.00 14.96  ? 239  LYS B CD    1 
ATOM   5387 C CE    . LYS B 1 197 ? 20.110  -1.522  34.158 1.00 16.19  ? 239  LYS B CE    1 
ATOM   5388 N NZ    . LYS B 1 197 ? 21.112  -2.642  34.226 1.00 16.73  ? 239  LYS B NZ    1 
ATOM   5389 N N     . TRP B 1 198 ? 14.856  -0.899  36.984 1.00 10.42  ? 240  TRP B N     1 
ATOM   5390 C CA    . TRP B 1 198 ? 15.027  -0.038  38.161 1.00 10.78  ? 240  TRP B CA    1 
ATOM   5391 C C     . TRP B 1 198 ? 14.107  -0.382  39.305 1.00 10.74  ? 240  TRP B C     1 
ATOM   5392 O O     . TRP B 1 198 ? 14.459  -0.053  40.444 1.00 13.96  ? 240  TRP B O     1 
ATOM   5393 C CB    . TRP B 1 198 ? 14.757  1.436   37.808 1.00 10.08  ? 240  TRP B CB    1 
ATOM   5394 C CG    . TRP B 1 198 ? 15.396  1.946   36.554 1.00 10.41  ? 240  TRP B CG    1 
ATOM   5395 C CD1   . TRP B 1 198 ? 14.785  2.687   35.603 1.00 12.14  ? 240  TRP B CD1   1 
ATOM   5396 C CD2   . TRP B 1 198 ? 16.774  1.854   36.165 1.00 11.56  ? 240  TRP B CD2   1 
ATOM   5397 N NE1   . TRP B 1 198 ? 15.656  3.027   34.614 1.00 12.91  ? 240  TRP B NE1   1 
ATOM   5398 C CE2   . TRP B 1 198 ? 16.912  2.562   34.941 1.00 12.12  ? 240  TRP B CE2   1 
ATOM   5399 C CE3   . TRP B 1 198 ? 17.916  1.294   36.735 1.00 12.98  ? 240  TRP B CE3   1 
ATOM   5400 C CZ2   . TRP B 1 198 ? 18.116  2.591   34.214 1.00 13.44  ? 240  TRP B CZ2   1 
ATOM   5401 C CZ3   . TRP B 1 198 ? 19.113  1.358   36.067 1.00 12.35  ? 240  TRP B CZ3   1 
ATOM   5402 C CH2   . TRP B 1 198 ? 19.213  2.023   34.826 1.00 12.87  ? 240  TRP B CH2   1 
ATOM   5403 N N     . GLY B 1 199 ? 12.911  -0.882  39.045 1.00 11.19  ? 241  GLY B N     1 
ATOM   5404 C CA    . GLY B 1 199 ? 11.859  -0.986  40.058 1.00 10.15  ? 241  GLY B CA    1 
ATOM   5405 C C     . GLY B 1 199 ? 11.381  0.368   40.596 1.00 10.42  ? 241  GLY B C     1 
ATOM   5406 O O     . GLY B 1 199 ? 11.313  1.313   39.821 1.00 10.71  ? 241  GLY B O     1 
ATOM   5407 N N     . TYR B 1 200 ? 10.978  0.374   41.883 1.00 9.36   ? 242  TYR B N     1 
ATOM   5408 C CA    . TYR B 1 200 ? 10.369  1.539   42.517 1.00 10.74  ? 242  TYR B CA    1 
ATOM   5409 C C     . TYR B 1 200 ? 11.198  1.883   43.751 1.00 9.79   ? 242  TYR B C     1 
ATOM   5410 O O     . TYR B 1 200 ? 11.588  0.964   44.478 1.00 11.56  ? 242  TYR B O     1 
ATOM   5411 C CB    . TYR B 1 200 ? 8.904   1.273   42.872 1.00 11.33  ? 242  TYR B CB    1 
ATOM   5412 C CG    . TYR B 1 200 ? 8.212   2.254   43.776 1.00 11.08  ? 242  TYR B CG    1 
ATOM   5413 C CD1   . TYR B 1 200 ? 7.866   3.519   43.352 1.00 11.81  ? 242  TYR B CD1   1 
ATOM   5414 C CD2   . TYR B 1 200 ? 8.065   1.990   45.130 1.00 10.64  ? 242  TYR B CD2   1 
ATOM   5415 C CE1   . TYR B 1 200 ? 7.253   4.421   44.204 1.00 11.76  ? 242  TYR B CE1   1 
ATOM   5416 C CE2   . TYR B 1 200 ? 7.410   2.874   45.983 1.00 10.25  ? 242  TYR B CE2   1 
ATOM   5417 C CZ    . TYR B 1 200 ? 7.030   4.121   45.529 1.00 10.97  ? 242  TYR B CZ    1 
ATOM   5418 O OH    . TYR B 1 200 ? 6.337   4.917   46.440 1.00 11.39  ? 242  TYR B OH    1 
ATOM   5419 N N     . GLY B 1 201 ? 11.404  3.198   43.998 1.00 9.17   ? 243  GLY B N     1 
ATOM   5420 C CA    . GLY B 1 201 ? 12.247  3.580   45.125 1.00 9.79   ? 243  GLY B CA    1 
ATOM   5421 C C     . GLY B 1 201 ? 13.730  3.357   44.798 1.00 9.26   ? 243  GLY B C     1 
ATOM   5422 O O     . GLY B 1 201 ? 14.167  3.169   43.649 1.00 8.01   ? 243  GLY B O     1 
ATOM   5423 N N     . PRO B 1 202 ? 14.628  3.403   45.835 1.00 9.07   ? 244  PRO B N     1 
ATOM   5424 C CA    . PRO B 1 202 ? 16.061  3.397   45.578 1.00 9.85   ? 244  PRO B CA    1 
ATOM   5425 C C     . PRO B 1 202 ? 16.462  2.199   44.717 1.00 10.45  ? 244  PRO B C     1 
ATOM   5426 O O     . PRO B 1 202 ? 15.924  1.083   44.904 1.00 10.61  ? 244  PRO B O     1 
ATOM   5427 C CB    . PRO B 1 202 ? 16.672  3.345   47.008 1.00 10.81  ? 244  PRO B CB    1 
ATOM   5428 C CG    . PRO B 1 202 ? 15.572  3.749   47.975 1.00 12.43  ? 244  PRO B CG    1 
ATOM   5429 C CD    . PRO B 1 202 ? 14.275  3.551   47.247 1.00 11.12  ? 244  PRO B CD    1 
ATOM   5430 N N     . TYR B 1 203 ? 17.387  2.415   43.761 1.00 10.60  ? 245  TYR B N     1 
ATOM   5431 C CA    . TYR B 1 203 ? 17.889  1.348   42.920 1.00 11.26  ? 245  TYR B CA    1 
ATOM   5432 C C     . TYR B 1 203 ? 19.029  0.646   43.650 1.00 12.19  ? 245  TYR B C     1 
ATOM   5433 O O     . TYR B 1 203 ? 20.052  1.279   43.906 1.00 11.73  ? 245  TYR B O     1 
ATOM   5434 C CB    . TYR B 1 203 ? 18.329  1.928   41.587 1.00 11.45  ? 245  TYR B CB    1 
ATOM   5435 C CG    . TYR B 1 203 ? 19.073  0.951   40.712 1.00 12.61  ? 245  TYR B CG    1 
ATOM   5436 C CD1   . TYR B 1 203 ? 18.457  -0.167  40.203 1.00 11.31  ? 245  TYR B CD1   1 
ATOM   5437 C CD2   . TYR B 1 203 ? 20.395  1.150   40.402 1.00 14.57  ? 245  TYR B CD2   1 
ATOM   5438 C CE1   . TYR B 1 203 ? 19.131  -1.031  39.359 1.00 10.75  ? 245  TYR B CE1   1 
ATOM   5439 C CE2   . TYR B 1 203 ? 21.087  0.287   39.557 1.00 15.37  ? 245  TYR B CE2   1 
ATOM   5440 C CZ    . TYR B 1 203 ? 20.431  -0.775  39.002 1.00 13.59  ? 245  TYR B CZ    1 
ATOM   5441 O OH    . TYR B 1 203 ? 21.195  -1.562  38.162 1.00 15.22  ? 245  TYR B OH    1 
ATOM   5442 N N     . LEU B 1 204 ? 18.845  -0.643  43.927 1.00 10.49  ? 246  LEU B N     1 
ATOM   5443 C CA    . LEU B 1 204 ? 19.670  -1.369  44.891 1.00 13.35  ? 246  LEU B CA    1 
ATOM   5444 C C     . LEU B 1 204 ? 20.689  -2.307  44.225 1.00 12.32  ? 246  LEU B C     1 
ATOM   5445 O O     . LEU B 1 204 ? 21.623  -2.693  44.904 1.00 10.24  ? 246  LEU B O     1 
ATOM   5446 C CB    . LEU B 1 204 ? 18.802  -2.208  45.852 1.00 13.95  ? 246  LEU B CB    1 
ATOM   5447 C CG    . LEU B 1 204 ? 17.686  -1.475  46.642 1.00 14.82  ? 246  LEU B CG    1 
ATOM   5448 C CD1   . LEU B 1 204 ? 16.890  -2.420  47.502 1.00 15.08  ? 246  LEU B CD1   1 
ATOM   5449 C CD2   . LEU B 1 204 ? 18.272  -0.378  47.466 1.00 15.82  ? 246  LEU B CD2   1 
ATOM   5450 N N     . ASP B 1 205 ? 20.516  -2.727  42.957 1.00 11.72  ? 247  ASP B N     1 
ATOM   5451 C CA    . ASP B 1 205 ? 21.318  -3.826  42.396 1.00 11.79  ? 247  ASP B CA    1 
ATOM   5452 C C     . ASP B 1 205 ? 22.811  -3.479  42.503 1.00 11.95  ? 247  ASP B C     1 
ATOM   5453 O O     . ASP B 1 205 ? 23.638  -4.369  42.695 1.00 10.97  ? 247  ASP B O     1 
ATOM   5454 C CB    . ASP B 1 205 ? 20.888  -4.160  40.965 1.00 11.13  ? 247  ASP B CB    1 
ATOM   5455 C CG    . ASP B 1 205 ? 19.411  -4.500  40.833 1.00 10.19  ? 247  ASP B CG    1 
ATOM   5456 O OD1   . ASP B 1 205 ? 18.565  -3.673  41.336 1.00 11.45  ? 247  ASP B OD1   1 
ATOM   5457 O OD2   . ASP B 1 205 ? 19.131  -5.615  40.319 1.00 13.89  ? 247  ASP B OD2   1 
ATOM   5458 N N     . GLY B 1 206 ? 23.163  -2.197  42.301 1.00 12.47  ? 248  GLY B N     1 
ATOM   5459 C CA    . GLY B 1 206 ? 24.566  -1.818  42.340 1.00 13.55  ? 248  GLY B CA    1 
ATOM   5460 C C     . GLY B 1 206 ? 25.262  -1.998  43.690 1.00 12.61  ? 248  GLY B C     1 
ATOM   5461 O O     . GLY B 1 206 ? 26.497  -2.144  43.751 1.00 10.91  ? 248  GLY B O     1 
ATOM   5462 N N     . LEU B 1 207 ? 24.487  -2.000  44.780 1.00 12.73  ? 249  LEU B N     1 
ATOM   5463 C CA    . LEU B 1 207 ? 25.014  -2.278  46.098 1.00 13.78  ? 249  LEU B CA    1 
ATOM   5464 C C     . LEU B 1 207 ? 25.611  -3.666  46.187 1.00 12.84  ? 249  LEU B C     1 
ATOM   5465 O O     . LEU B 1 207 ? 26.358  -3.939  47.126 1.00 15.84  ? 249  LEU B O     1 
ATOM   5466 C CB    . LEU B 1 207 ? 23.929  -2.240  47.184 1.00 18.74  ? 249  LEU B CB    1 
ATOM   5467 C CG    . LEU B 1 207 ? 23.440  -0.876  47.609 1.00 24.90  ? 249  LEU B CG    1 
ATOM   5468 C CD1   . LEU B 1 207 ? 22.448  -1.072  48.721 1.00 24.35  ? 249  LEU B CD1   1 
ATOM   5469 C CD2   . LEU B 1 207 ? 24.609  0.002   48.049 1.00 26.80  ? 249  LEU B CD2   1 
ATOM   5470 N N     . PHE B 1 208 ? 25.194  -4.591  45.308 1.00 11.58  ? 250  PHE B N     1 
ATOM   5471 C CA    . PHE B 1 208 ? 25.650  -5.971  45.376 1.00 10.52  ? 250  PHE B CA    1 
ATOM   5472 C C     . PHE B 1 208 ? 26.717  -6.265  44.315 1.00 12.30  ? 250  PHE B C     1 
ATOM   5473 O O     . PHE B 1 208 ? 26.978  -7.449  44.038 1.00 12.60  ? 250  PHE B O     1 
ATOM   5474 C CB    . PHE B 1 208 ? 24.434  -6.927  45.282 1.00 10.53  ? 250  PHE B CB    1 
ATOM   5475 C CG    . PHE B 1 208 ? 23.423  -6.624  46.366 1.00 9.83   ? 250  PHE B CG    1 
ATOM   5476 C CD1   . PHE B 1 208 ? 23.743  -6.898  47.675 1.00 10.35  ? 250  PHE B CD1   1 
ATOM   5477 C CD2   . PHE B 1 208 ? 22.233  -5.948  46.116 1.00 9.13   ? 250  PHE B CD2   1 
ATOM   5478 C CE1   . PHE B 1 208 ? 22.850  -6.588  48.690 1.00 10.82  ? 250  PHE B CE1   1 
ATOM   5479 C CE2   . PHE B 1 208 ? 21.348  -5.635  47.135 1.00 10.89  ? 250  PHE B CE2   1 
ATOM   5480 C CZ    . PHE B 1 208 ? 21.674  -5.957  48.426 1.00 10.83  ? 250  PHE B CZ    1 
ATOM   5481 N N     . THR B 1 209 ? 27.310  -5.204  43.717 1.00 10.90  ? 251  THR B N     1 
ATOM   5482 C CA    . THR B 1 209 ? 28.405  -5.322  42.791 1.00 10.55  ? 251  THR B CA    1 
ATOM   5483 C C     . THR B 1 209 ? 29.654  -4.788  43.460 1.00 10.26  ? 251  THR B C     1 
ATOM   5484 O O     . THR B 1 209 ? 29.617  -3.788  44.224 1.00 9.74   ? 251  THR B O     1 
ATOM   5485 C CB    . THR B 1 209 ? 28.087  -4.640  41.450 1.00 9.98   ? 251  THR B CB    1 
ATOM   5486 O OG1   . THR B 1 209 ? 27.950  -3.222  41.611 1.00 12.49  ? 251  THR B OG1   1 
ATOM   5487 C CG2   . THR B 1 209 ? 26.854  -5.216  40.806 1.00 12.76  ? 251  THR B CG2   1 
ATOM   5488 N N     . GLN B 1 210 ? 30.762  -5.526  43.254 1.00 8.73   ? 252  GLN B N     1 
ATOM   5489 C CA    . GLN B 1 210 ? 32.021  -5.295  43.944 1.00 8.66   ? 252  GLN B CA    1 
ATOM   5490 C C     . GLN B 1 210 ? 31.810  -4.968  45.411 1.00 10.10  ? 252  GLN B C     1 
ATOM   5491 O O     . GLN B 1 210 ? 32.349  -3.980  45.942 1.00 10.33  ? 252  GLN B O     1 
ATOM   5492 C CB    . GLN B 1 210 ? 32.848  -4.164  43.322 1.00 9.63   ? 252  GLN B CB    1 
ATOM   5493 C CG    . GLN B 1 210 ? 33.342  -4.487  41.921 1.00 9.80   ? 252  GLN B CG    1 
ATOM   5494 C CD    . GLN B 1 210 ? 34.411  -3.570  41.383 1.00 9.77   ? 252  GLN B CD    1 
ATOM   5495 O OE1   . GLN B 1 210 ? 35.025  -2.798  42.115 1.00 9.29   ? 252  GLN B OE1   1 
ATOM   5496 N NE2   . GLN B 1 210 ? 34.686  -3.723  40.086 1.00 8.38   ? 252  GLN B NE2   1 
ATOM   5497 N N     . SER B 1 211 ? 31.054  -5.828  46.073 1.00 9.46   ? 253  SER B N     1 
ATOM   5498 C CA    . SER B 1 211 ? 30.685  -5.505  47.445 1.00 12.93  ? 253  SER B CA    1 
ATOM   5499 C C     . SER B 1 211 ? 30.537  -6.743  48.297 1.00 11.50  ? 253  SER B C     1 
ATOM   5500 O O     . SER B 1 211 ? 30.762  -7.861  47.845 1.00 11.29  ? 253  SER B O     1 
ATOM   5501 C CB    . SER B 1 211 ? 29.450  -4.689  47.496 1.00 20.57  ? 253  SER B CB    1 
ATOM   5502 O OG    . SER B 1 211 ? 28.419  -5.575  47.344 1.00 24.97  ? 253  SER B OG    1 
ATOM   5503 N N     . ASN B 1 212 ? 30.274  -6.483  49.577 1.00 10.49  ? 254  ASN B N     1 
ATOM   5504 C CA    . ASN B 1 212 ? 30.111  -7.556  50.558 1.00 9.70   ? 254  ASN B CA    1 
ATOM   5505 C C     . ASN B 1 212 ? 28.818  -7.337  51.351 1.00 8.91   ? 254  ASN B C     1 
ATOM   5506 O O     . ASN B 1 212 ? 28.764  -7.633  52.568 1.00 9.93   ? 254  ASN B O     1 
ATOM   5507 C CB    . ASN B 1 212 ? 31.360  -7.685  51.423 1.00 10.30  ? 254  ASN B CB    1 
ATOM   5508 C CG    . ASN B 1 212 ? 31.734  -6.408  52.164 1.00 10.53  ? 254  ASN B CG    1 
ATOM   5509 O OD1   . ASN B 1 212 ? 31.064  -5.380  52.080 1.00 11.37  ? 254  ASN B OD1   1 
ATOM   5510 N ND2   . ASN B 1 212 ? 32.864  -6.445  52.859 1.00 11.77  ? 254  ASN B ND2   1 
ATOM   5511 N N     . PHE B 1 213 ? 27.755  -6.927  50.655 1.00 8.96   ? 255  PHE B N     1 
ATOM   5512 C CA    . PHE B 1 213 ? 26.505  -6.618  51.323 1.00 10.04  ? 255  PHE B CA    1 
ATOM   5513 C C     . PHE B 1 213 ? 25.463  -7.724  51.149 1.00 10.72  ? 255  PHE B C     1 
ATOM   5514 O O     . PHE B 1 213 ? 24.429  -7.729  51.832 1.00 12.29  ? 255  PHE B O     1 
ATOM   5515 C CB    . PHE B 1 213 ? 25.943  -5.296  50.796 1.00 10.82  ? 255  PHE B CB    1 
ATOM   5516 C CG    . PHE B 1 213 ? 26.818  -4.082  51.008 1.00 10.30  ? 255  PHE B CG    1 
ATOM   5517 C CD1   . PHE B 1 213 ? 27.788  -4.029  52.008 1.00 11.36  ? 255  PHE B CD1   1 
ATOM   5518 C CD2   . PHE B 1 213 ? 26.608  -2.944  50.268 1.00 13.17  ? 255  PHE B CD2   1 
ATOM   5519 C CE1   . PHE B 1 213 ? 28.565  -2.904  52.168 1.00 11.81  ? 255  PHE B CE1   1 
ATOM   5520 C CE2   . PHE B 1 213 ? 27.364  -1.800  50.466 1.00 12.44  ? 255  PHE B CE2   1 
ATOM   5521 C CZ    . PHE B 1 213 ? 28.327  -1.776  51.420 1.00 11.56  ? 255  PHE B CZ    1 
ATOM   5522 N N     . GLY B 1 214 ? 25.746  -8.679  50.268 1.00 10.85  ? 256  GLY B N     1 
ATOM   5523 C CA    . GLY B 1 214 ? 24.806  -9.771  50.078 1.00 10.91  ? 256  GLY B CA    1 
ATOM   5524 C C     . GLY B 1 214 ? 25.409  -10.878 49.243 1.00 10.06  ? 256  GLY B C     1 
ATOM   5525 O O     . GLY B 1 214 ? 26.426  -10.664 48.618 1.00 11.67  ? 256  GLY B O     1 
ATOM   5526 N N     . ILE B 1 215 ? 24.742  -12.032 49.227 1.00 9.29   ? 257  ILE B N     1 
ATOM   5527 C CA    . ILE B 1 215 ? 25.080  -13.171 48.384 1.00 9.74   ? 257  ILE B CA    1 
ATOM   5528 C C     . ILE B 1 215 ? 24.050  -13.251 47.264 1.00 9.55   ? 257  ILE B C     1 
ATOM   5529 O O     . ILE B 1 215 ? 22.864  -13.469 47.530 1.00 10.34  ? 257  ILE B O     1 
ATOM   5530 C CB    . ILE B 1 215 ? 25.055  -14.454 49.235 1.00 10.81  ? 257  ILE B CB    1 
ATOM   5531 C CG1   . ILE B 1 215 ? 26.111  -14.367 50.330 1.00 10.25  ? 257  ILE B CG1   1 
ATOM   5532 C CG2   . ILE B 1 215 ? 25.273  -15.682 48.355 1.00 12.05  ? 257  ILE B CG2   1 
ATOM   5533 C CD1   . ILE B 1 215 ? 25.868  -15.401 51.430 1.00 11.68  ? 257  ILE B CD1   1 
ATOM   5534 N N     . VAL B 1 216 ? 24.488  -13.092 46.011 1.00 9.85   ? 258  VAL B N     1 
ATOM   5535 C CA    . VAL B 1 216 ? 23.578  -13.172 44.886 1.00 9.96   ? 258  VAL B CA    1 
ATOM   5536 C C     . VAL B 1 216 ? 23.295  -14.651 44.598 1.00 9.72   ? 258  VAL B C     1 
ATOM   5537 O O     . VAL B 1 216 ? 24.206  -15.441 44.340 1.00 10.76  ? 258  VAL B O     1 
ATOM   5538 C CB    . VAL B 1 216 ? 24.162  -12.429 43.685 1.00 10.16  ? 258  VAL B CB    1 
ATOM   5539 C CG1   . VAL B 1 216 ? 23.301  -12.606 42.440 1.00 11.65  ? 258  VAL B CG1   1 
ATOM   5540 C CG2   . VAL B 1 216 ? 24.317  -10.945 44.002 1.00 11.54  ? 258  VAL B CG2   1 
ATOM   5541 N N     . THR B 1 217 ? 21.997  -14.995 44.580 1.00 9.43   ? 259  THR B N     1 
ATOM   5542 C CA    . THR B 1 217 ? 21.576  -16.363 44.356 1.00 9.69   ? 259  THR B CA    1 
ATOM   5543 C C     . THR B 1 217 ? 20.913  -16.582 43.008 1.00 9.68   ? 259  THR B C     1 
ATOM   5544 O O     . THR B 1 217 ? 20.864  -17.742 42.555 1.00 10.20  ? 259  THR B O     1 
ATOM   5545 C CB    . THR B 1 217 ? 20.612  -16.789 45.459 1.00 11.20  ? 259  THR B CB    1 
ATOM   5546 O OG1   . THR B 1 217 ? 19.514  -15.864 45.552 1.00 11.90  ? 259  THR B OG1   1 
ATOM   5547 C CG2   . THR B 1 217 ? 21.354  -16.863 46.770 1.00 12.18  ? 259  THR B CG2   1 
ATOM   5548 N N     . LYS B 1 218 ? 20.467  -15.500 42.362 1.00 9.14   ? 260  LYS B N     1 
ATOM   5549 C CA    . LYS B 1 218 ? 19.862  -15.552 41.045 1.00 7.97   ? 260  LYS B CA    1 
ATOM   5550 C C     . LYS B 1 218 ? 20.125  -14.209 40.378 1.00 8.83   ? 260  LYS B C     1 
ATOM   5551 O O     . LYS B 1 218 ? 20.041  -13.174 41.037 1.00 9.93   ? 260  LYS B O     1 
ATOM   5552 C CB    . LYS B 1 218 ? 18.353  -15.762 41.083 1.00 8.55   ? 260  LYS B CB    1 
ATOM   5553 C CG    . LYS B 1 218 ? 17.849  -17.054 41.750 1.00 10.01  ? 260  LYS B CG    1 
ATOM   5554 C CD    . LYS B 1 218 ? 16.320  -17.184 41.810 1.00 11.92  ? 260  LYS B CD    1 
ATOM   5555 C CE    . LYS B 1 218 ? 15.826  -18.524 42.368 1.00 13.20  ? 260  LYS B CE    1 
ATOM   5556 N NZ    . LYS B 1 218 ? 16.469  -18.888 43.675 1.00 12.77  ? 260  LYS B NZ    1 
ATOM   5557 N N     . MET B 1 219 ? 20.397  -14.183 39.065 1.00 9.28   ? 261  MET B N     1 
ATOM   5558 C CA    . MET B 1 219 ? 20.572  -12.900 38.392 1.00 7.88   ? 261  MET B CA    1 
ATOM   5559 C C     . MET B 1 219 ? 20.005  -12.973 36.986 1.00 9.15   ? 261  MET B C     1 
ATOM   5560 O O     . MET B 1 219 ? 20.239  -13.945 36.274 1.00 9.38   ? 261  MET B O     1 
ATOM   5561 C CB    . MET B 1 219 ? 22.053  -12.576 38.263 1.00 9.13   ? 261  MET B CB    1 
ATOM   5562 C CG    . MET B 1 219 ? 22.354  -11.162 37.777 1.00 9.07   ? 261  MET B CG    1 
ATOM   5563 S SD    . MET B 1 219 ? 24.175  -10.931 37.414 1.00 12.46  ? 261  MET B SD    1 
ATOM   5564 C CE    . MET B 1 219 ? 24.182  -11.549 35.739 1.00 14.02  ? 261  MET B CE    1 
ATOM   5565 N N     . GLY B 1 220 ? 19.353  -11.899 36.563 1.00 8.62   ? 262  GLY B N     1 
ATOM   5566 C CA    . GLY B 1 220 ? 18.824  -11.836 35.201 1.00 8.61   ? 262  GLY B CA    1 
ATOM   5567 C C     . GLY B 1 220 ? 19.840  -11.082 34.334 1.00 9.56   ? 262  GLY B C     1 
ATOM   5568 O O     . GLY B 1 220 ? 20.567  -10.208 34.791 1.00 8.97   ? 262  GLY B O     1 
ATOM   5569 N N     . LEU B 1 221 ? 19.840  -11.387 33.030 1.00 10.46  ? 263  LEU B N     1 
ATOM   5570 C CA    . LEU B 1 221 ? 20.777  -10.836 32.084 1.00 11.94  ? 263  LEU B CA    1 
ATOM   5571 C C     . LEU B 1 221 ? 20.084  -10.701 30.736 1.00 11.88  ? 263  LEU B C     1 
ATOM   5572 O O     . LEU B 1 221 ? 19.429  -11.611 30.254 1.00 12.68  ? 263  LEU B O     1 
ATOM   5573 C CB    . LEU B 1 221 ? 22.000  -11.766 32.006 1.00 12.69  ? 263  LEU B CB    1 
ATOM   5574 C CG    . LEU B 1 221 ? 23.126  -11.330 31.097 1.00 15.91  ? 263  LEU B CG    1 
ATOM   5575 C CD1   . LEU B 1 221 ? 23.727  -9.993  31.492 1.00 14.98  ? 263  LEU B CD1   1 
ATOM   5576 C CD2   . LEU B 1 221 ? 24.197  -12.405 31.176 1.00 17.93  ? 263  LEU B CD2   1 
ATOM   5577 N N     . TRP B 1 222 ? 20.240  -9.544  30.110 1.00 10.68  ? 264  TRP B N     1 
ATOM   5578 C CA    . TRP B 1 222 ? 19.821  -9.376  28.736 1.00 9.49   ? 264  TRP B CA    1 
ATOM   5579 C C     . TRP B 1 222 ? 20.841  -9.976  27.773 1.00 10.51  ? 264  TRP B C     1 
ATOM   5580 O O     . TRP B 1 222 ? 22.048  -9.893  27.995 1.00 10.70  ? 264  TRP B O     1 
ATOM   5581 C CB    . TRP B 1 222 ? 19.658  -7.886  28.472 1.00 10.23  ? 264  TRP B CB    1 
ATOM   5582 C CG    . TRP B 1 222 ? 18.546  -7.247  29.239 1.00 10.17  ? 264  TRP B CG    1 
ATOM   5583 C CD1   . TRP B 1 222 ? 17.526  -7.847  29.920 1.00 9.97   ? 264  TRP B CD1   1 
ATOM   5584 C CD2   . TRP B 1 222 ? 18.330  -5.827  29.370 1.00 12.26  ? 264  TRP B CD2   1 
ATOM   5585 N NE1   . TRP B 1 222 ? 16.682  -6.891  30.423 1.00 10.36  ? 264  TRP B NE1   1 
ATOM   5586 C CE2   . TRP B 1 222 ? 17.151  -5.649  30.116 1.00 11.96  ? 264  TRP B CE2   1 
ATOM   5587 C CE3   . TRP B 1 222 ? 19.044  -4.696  28.943 1.00 15.73  ? 264  TRP B CE3   1 
ATOM   5588 C CZ2   . TRP B 1 222 ? 16.666  -4.384  30.426 1.00 15.44  ? 264  TRP B CZ2   1 
ATOM   5589 C CZ3   . TRP B 1 222 ? 18.604  -3.443  29.307 1.00 18.28  ? 264  TRP B CZ3   1 
ATOM   5590 C CH2   . TRP B 1 222 ? 17.428  -3.299  30.046 1.00 19.22  ? 264  TRP B CH2   1 
ATOM   5591 N N     . LEU B 1 223 ? 20.326  -10.610 26.703 1.00 10.46  ? 265  LEU B N     1 
ATOM   5592 C CA    . LEU B 1 223 ? 21.140  -11.243 25.681 1.00 11.00  ? 265  LEU B CA    1 
ATOM   5593 C C     . LEU B 1 223 ? 20.845  -10.618 24.323 1.00 11.15  ? 265  LEU B C     1 
ATOM   5594 O O     . LEU B 1 223 ? 19.682  -10.388 23.965 1.00 12.53  ? 265  LEU B O     1 
ATOM   5595 C CB    . LEU B 1 223 ? 20.793  -12.751 25.625 1.00 11.47  ? 265  LEU B CB    1 
ATOM   5596 C CG    . LEU B 1 223 ? 21.029  -13.571 26.910 1.00 11.83  ? 265  LEU B CG    1 
ATOM   5597 C CD1   . LEU B 1 223 ? 20.492  -15.019 26.776 1.00 12.72  ? 265  LEU B CD1   1 
ATOM   5598 C CD2   . LEU B 1 223 ? 22.495  -13.569 27.290 1.00 13.01  ? 265  LEU B CD2   1 
ATOM   5599 N N     . MET B 1 224 ? 21.886  -10.505 23.503 1.00 12.04  ? 266  MET B N     1 
ATOM   5600 C CA    . MET B 1 224 ? 21.763  -9.834  22.227 1.00 12.15  ? 266  MET B CA    1 
ATOM   5601 C C     . MET B 1 224 ? 21.229  -10.805 21.185 1.00 12.02  ? 266  MET B C     1 
ATOM   5602 O O     . MET B 1 224 ? 21.758  -11.911 21.048 1.00 12.01  ? 266  MET B O     1 
ATOM   5603 C CB    . MET B 1 224 ? 23.120  -9.280  21.770 1.00 13.42  ? 266  MET B CB    1 
ATOM   5604 C CG    . MET B 1 224 ? 23.004  -8.454  20.483 1.00 15.04  ? 266  MET B CG    1 
ATOM   5605 S SD    . MET B 1 224 ? 24.649  -7.814  20.009 1.00 17.95  ? 266  MET B SD    1 
ATOM   5606 C CE    . MET B 1 224 ? 25.254  -9.295  19.233 1.00 25.68  ? 266  MET B CE    1 
ATOM   5607 N N     . PRO B 1 225 ? 20.218  -10.406 20.384 1.00 12.58  ? 267  PRO B N     1 
ATOM   5608 C CA    . PRO B 1 225 ? 19.851  -11.180 19.204 1.00 13.64  ? 267  PRO B CA    1 
ATOM   5609 C C     . PRO B 1 225 ? 21.029  -11.429 18.266 1.00 15.12  ? 267  PRO B C     1 
ATOM   5610 O O     . PRO B 1 225 ? 21.798  -10.519 17.951 1.00 14.32  ? 267  PRO B O     1 
ATOM   5611 C CB    . PRO B 1 225 ? 18.760  -10.326 18.546 1.00 14.55  ? 267  PRO B CB    1 
ATOM   5612 C CG    . PRO B 1 225 ? 18.185  -9.526  19.678 1.00 13.47  ? 267  PRO B CG    1 
ATOM   5613 C CD    . PRO B 1 225 ? 19.360  -9.227  20.592 1.00 13.45  ? 267  PRO B CD    1 
ATOM   5614 N N     . LYS B 1 226 ? 21.105  -12.662 17.736 1.00 15.76  ? 268  LYS B N     1 
ATOM   5615 C CA    . LYS B 1 226 ? 22.101  -12.963 16.723 1.00 16.87  ? 268  LYS B CA    1 
ATOM   5616 C C     . LYS B 1 226 ? 21.806  -12.120 15.477 1.00 17.25  ? 268  LYS B C     1 
ATOM   5617 O O     . LYS B 1 226 ? 20.695  -12.164 14.964 1.00 20.18  ? 268  LYS B O     1 
ATOM   5618 C CB    . LYS B 1 226 ? 22.065  -14.458 16.436 1.00 19.49  ? 268  LYS B CB    1 
ATOM   5619 C CG    . LYS B 1 226 ? 22.852  -14.992 15.241 1.00 29.54  ? 268  LYS B CG    1 
ATOM   5620 C CD    . LYS B 1 226 ? 22.669  -16.532 15.190 1.00 32.52  ? 268  LYS B CD    1 
ATOM   5621 C CE    . LYS B 1 226 ? 23.459  -17.201 14.084 1.00 43.48  ? 268  LYS B CE    1 
ATOM   5622 N NZ    . LYS B 1 226 ? 22.953  -16.805 12.747 1.00 47.11  ? 268  LYS B NZ    1 
ATOM   5623 N N     . PRO B 1 227 ? 22.763  -11.350 14.943 1.00 16.55  ? 269  PRO B N     1 
ATOM   5624 C CA    . PRO B 1 227 ? 22.538  -10.521 13.765 1.00 19.21  ? 269  PRO B CA    1 
ATOM   5625 C C     . PRO B 1 227 ? 22.673  -11.334 12.479 1.00 20.97  ? 269  PRO B C     1 
ATOM   5626 O O     . PRO B 1 227 ? 23.320  -12.368 12.448 1.00 20.82  ? 269  PRO B O     1 
ATOM   5627 C CB    . PRO B 1 227 ? 23.674  -9.518  13.855 1.00 20.69  ? 269  PRO B CB    1 
ATOM   5628 C CG    . PRO B 1 227 ? 24.774  -10.349 14.395 1.00 19.90  ? 269  PRO B CG    1 
ATOM   5629 C CD    . PRO B 1 227 ? 24.124  -11.201 15.461 1.00 17.65  ? 269  PRO B CD    1 
ATOM   5630 N N     . PRO B 1 228 ? 21.944  -10.963 11.423 1.00 24.35  ? 270  PRO B N     1 
ATOM   5631 C CA    . PRO B 1 228 ? 22.099  -11.648 10.131 1.00 25.11  ? 270  PRO B CA    1 
ATOM   5632 C C     . PRO B 1 228 ? 23.544  -11.648 9.646  1.00 20.93  ? 270  PRO B C     1 
ATOM   5633 O O     . PRO B 1 228 ? 24.026  -12.681 9.161  1.00 24.75  ? 270  PRO B O     1 
ATOM   5634 C CB    . PRO B 1 228 ? 21.171  -10.842 9.207  1.00 25.56  ? 270  PRO B CB    1 
ATOM   5635 C CG    . PRO B 1 228 ? 20.142  -10.190 10.125 1.00 28.01  ? 270  PRO B CG    1 
ATOM   5636 C CD    . PRO B 1 228 ? 20.853  -9.981  11.453 1.00 29.04  ? 270  PRO B CD    1 
ATOM   5637 N N     . VAL B 1 229 ? 24.231  -10.532 9.866  1.00 21.01  ? 271  VAL B N     1 
ATOM   5638 C CA    . VAL B 1 229 ? 25.626  -10.370 9.476  1.00 23.60  ? 271  VAL B CA    1 
ATOM   5639 C C     . VAL B 1 229 ? 26.486  -9.875  10.650 1.00 19.30  ? 271  VAL B C     1 
ATOM   5640 O O     . VAL B 1 229 ? 26.155  -8.901  11.339 1.00 19.21  ? 271  VAL B O     1 
ATOM   5641 C CB    . VAL B 1 229 ? 25.763  -9.453  8.249  1.00 23.10  ? 271  VAL B CB    1 
ATOM   5642 C CG1   . VAL B 1 229 ? 27.221  -9.203  7.853  1.00 24.23  ? 271  VAL B CG1   1 
ATOM   5643 C CG2   . VAL B 1 229 ? 24.928  -10.071 7.115  1.00 22.25  ? 271  VAL B CG2   1 
ATOM   5644 N N     . TYR B 1 230 ? 27.636  -10.550 10.747 1.00 18.97  ? 272  TYR B N     1 
ATOM   5645 C CA    . TYR B 1 230 ? 28.711  -10.250 11.691 1.00 16.93  ? 272  TYR B CA    1 
ATOM   5646 C C     . TYR B 1 230 ? 30.002  -10.056 10.887 1.00 16.95  ? 272  TYR B C     1 
ATOM   5647 O O     . TYR B 1 230 ? 30.415  -10.985 10.198 1.00 19.33  ? 272  TYR B O     1 
ATOM   5648 C CB    . TYR B 1 230 ? 28.927  -11.452 12.625 1.00 16.64  ? 272  TYR B CB    1 
ATOM   5649 C CG    . TYR B 1 230 ? 30.204  -11.418 13.424 1.00 17.03  ? 272  TYR B CG    1 
ATOM   5650 C CD1   . TYR B 1 230 ? 30.461  -10.321 14.236 1.00 18.59  ? 272  TYR B CD1   1 
ATOM   5651 C CD2   . TYR B 1 230 ? 31.136  -12.435 13.374 1.00 14.93  ? 272  TYR B CD2   1 
ATOM   5652 C CE1   . TYR B 1 230 ? 31.647  -10.205 14.952 1.00 16.55  ? 272  TYR B CE1   1 
ATOM   5653 C CE2   . TYR B 1 230 ? 32.280  -12.383 14.142 1.00 15.29  ? 272  TYR B CE2   1 
ATOM   5654 C CZ    . TYR B 1 230 ? 32.551  -11.257 14.895 1.00 15.38  ? 272  TYR B CZ    1 
ATOM   5655 O OH    . TYR B 1 230 ? 33.710  -11.265 15.593 1.00 16.42  ? 272  TYR B OH    1 
ATOM   5656 N N     . LYS B 1 231 ? 30.644  -8.918  11.037 1.00 15.15  ? 273  LYS B N     1 
ATOM   5657 C CA    . LYS B 1 231 ? 31.845  -8.603  10.281 1.00 17.52  ? 273  LYS B CA    1 
ATOM   5658 C C     . LYS B 1 231 ? 32.949  -8.125  11.218 1.00 15.94  ? 273  LYS B C     1 
ATOM   5659 O O     . LYS B 1 231 ? 32.915  -6.999  11.698 1.00 16.51  ? 273  LYS B O     1 
ATOM   5660 C CB    . LYS B 1 231 ? 31.592  -7.556  9.204  1.00 17.59  ? 273  LYS B CB    1 
ATOM   5661 C CG    . LYS B 1 231 ? 32.769  -7.412  8.242  1.00 20.10  ? 273  LYS B CG    1 
ATOM   5662 C CD    . LYS B 1 231 ? 32.524  -6.487  7.034  1.00 22.28  ? 273  LYS B CD    1 
ATOM   5663 C CE    . LYS B 1 231 ? 33.701  -6.500  6.075  1.00 22.91  ? 273  LYS B CE    1 
ATOM   5664 N NZ    . LYS B 1 231 ? 33.385  -5.710  4.865  1.00 25.26  ? 273  LYS B NZ    1 
ATOM   5665 N N     . PRO B 1 232 ? 33.932  -8.988  11.535 1.00 15.39  ? 274  PRO B N     1 
ATOM   5666 C CA    . PRO B 1 232 ? 35.053  -8.567  12.382 1.00 15.47  ? 274  PRO B CA    1 
ATOM   5667 C C     . PRO B 1 232 ? 36.180  -7.834  11.661 1.00 14.85  ? 274  PRO B C     1 
ATOM   5668 O O     . PRO B 1 232 ? 36.435  -8.119  10.488 1.00 16.97  ? 274  PRO B O     1 
ATOM   5669 C CB    . PRO B 1 232 ? 35.553  -9.901  12.922 1.00 14.92  ? 274  PRO B CB    1 
ATOM   5670 C CG    . PRO B 1 232 ? 35.291  -10.885 11.800 1.00 17.07  ? 274  PRO B CG    1 
ATOM   5671 C CD    . PRO B 1 232 ? 34.014  -10.407 11.176 1.00 16.16  ? 274  PRO B CD    1 
ATOM   5672 N N     . PHE B 1 233 ? 36.859  -6.947  12.371 1.00 14.07  ? 275  PHE B N     1 
ATOM   5673 C CA    . PHE B 1 233 ? 37.957  -6.186  11.827 1.00 15.52  ? 275  PHE B CA    1 
ATOM   5674 C C     . PHE B 1 233 ? 39.121  -6.138  12.815 1.00 17.47  ? 275  PHE B C     1 
ATOM   5675 O O     . PHE B 1 233 ? 38.936  -6.218  14.042 1.00 15.20  ? 275  PHE B O     1 
ATOM   5676 C CB    . PHE B 1 233 ? 37.575  -4.727  11.555 1.00 17.31  ? 275  PHE B CB    1 
ATOM   5677 C CG    . PHE B 1 233 ? 36.489  -4.485  10.550 1.00 16.48  ? 275  PHE B CG    1 
ATOM   5678 C CD1   . PHE B 1 233 ? 35.155  -4.718  10.861 1.00 17.86  ? 275  PHE B CD1   1 
ATOM   5679 C CD2   . PHE B 1 233 ? 36.815  -4.077  9.265  1.00 18.29  ? 275  PHE B CD2   1 
ATOM   5680 C CE1   . PHE B 1 233 ? 34.156  -4.498  9.926  1.00 19.69  ? 275  PHE B CE1   1 
ATOM   5681 C CE2   . PHE B 1 233 ? 35.814  -3.822  8.347  1.00 19.24  ? 275  PHE B CE2   1 
ATOM   5682 C CZ    . PHE B 1 233 ? 34.494  -4.046  8.669  1.00 21.02  ? 275  PHE B CZ    1 
ATOM   5683 N N     . MET B 1 234 ? 40.326  -5.915  12.262 1.00 17.09  ? 276  MET B N     1 
ATOM   5684 C CA    . MET B 1 234 ? 41.547  -5.628  13.022 1.00 18.60  ? 276  MET B CA    1 
ATOM   5685 C C     . MET B 1 234 ? 42.176  -4.355  12.437 1.00 19.84  ? 276  MET B C     1 
ATOM   5686 O O     . MET B 1 234 ? 42.200  -4.166  11.214 1.00 20.59  ? 276  MET B O     1 
ATOM   5687 C CB    . MET B 1 234 ? 42.550  -6.778  12.901 1.00 19.81  ? 276  MET B CB    1 
ATOM   5688 C CG    . MET B 1 234 ? 43.958  -6.438  13.286 1.00 27.47  ? 276  MET B CG    1 
ATOM   5689 S SD    . MET B 1 234 ? 44.958  -7.943  12.985 1.00 33.15  ? 276  MET B SD    1 
ATOM   5690 C CE    . MET B 1 234 ? 46.632  -7.341  13.208 1.00 29.48  ? 276  MET B CE    1 
ATOM   5691 N N     . VAL B 1 235 ? 42.586  -3.429  13.299 1.00 16.39  ? 277  VAL B N     1 
ATOM   5692 C CA    . VAL B 1 235 ? 43.301  -2.246  12.870 1.00 18.36  ? 277  VAL B CA    1 
ATOM   5693 C C     . VAL B 1 235 ? 44.726  -2.378  13.378 1.00 19.47  ? 277  VAL B C     1 
ATOM   5694 O O     . VAL B 1 235 ? 44.964  -2.505  14.572 1.00 16.62  ? 277  VAL B O     1 
ATOM   5695 C CB    . VAL B 1 235 ? 42.707  -0.911  13.370 1.00 23.11  ? 277  VAL B CB    1 
ATOM   5696 C CG1   . VAL B 1 235 ? 43.255  0.245   12.544 1.00 22.84  ? 277  VAL B CG1   1 
ATOM   5697 C CG2   . VAL B 1 235 ? 41.212  -0.948  13.380 1.00 29.64  ? 277  VAL B CG2   1 
ATOM   5698 N N     . ARG B 1 236 ? 45.685  -2.293  12.441 1.00 17.99  ? 278  ARG B N     1 
ATOM   5699 C CA    . ARG B 1 236 ? 47.092  -2.396  12.772 1.00 18.36  ? 278  ARG B CA    1 
ATOM   5700 C C     . ARG B 1 236 ? 47.729  -1.007  12.741 1.00 16.80  ? 278  ARG B C     1 
ATOM   5701 O O     . ARG B 1 236 ? 47.643  -0.304  11.713 1.00 17.17  ? 278  ARG B O     1 
ATOM   5702 C CB    . ARG B 1 236 ? 47.672  -3.410  11.770 1.00 23.01  ? 278  ARG B CB    1 
ATOM   5703 C CG    . ARG B 1 236 ? 49.152  -3.666  11.878 1.00 27.44  ? 278  ARG B CG    1 
ATOM   5704 C CD    . ARG B 1 236 ? 49.510  -4.971  11.150 1.00 27.36  ? 278  ARG B CD    1 
ATOM   5705 N NE    . ARG B 1 236 ? 49.268  -4.890  9.727  1.00 26.85  ? 278  ARG B NE    1 
ATOM   5706 C CZ    . ARG B 1 236 ? 49.360  -5.889  8.842  1.00 26.95  ? 278  ARG B CZ    1 
ATOM   5707 N NH1   . ARG B 1 236 ? 49.325  -7.168  9.182  1.00 23.84  ? 278  ARG B NH1   1 
ATOM   5708 N NH2   . ARG B 1 236 ? 49.418  -5.572  7.565  1.00 29.00  ? 278  ARG B NH2   1 
ATOM   5709 N N     . HIS B 1 237 ? 48.385  -0.637  13.851 1.00 15.22  ? 279  HIS B N     1 
ATOM   5710 C CA    . HIS B 1 237 ? 49.173  0.578   13.983 1.00 16.01  ? 279  HIS B CA    1 
ATOM   5711 C C     . HIS B 1 237 ? 50.638  0.191   14.198 1.00 17.22  ? 279  HIS B C     1 
ATOM   5712 O O     . HIS B 1 237 ? 50.988  -0.706  15.008 1.00 17.34  ? 279  HIS B O     1 
ATOM   5713 C CB    . HIS B 1 237 ? 48.648  1.492   15.103 1.00 16.22  ? 279  HIS B CB    1 
ATOM   5714 C CG    . HIS B 1 237 ? 47.455  2.287   14.731 1.00 15.84  ? 279  HIS B CG    1 
ATOM   5715 N ND1   . HIS B 1 237 ? 46.165  1.825   14.793 1.00 15.77  ? 279  HIS B ND1   1 
ATOM   5716 C CD2   . HIS B 1 237 ? 47.368  3.584   14.351 1.00 17.93  ? 279  HIS B CD2   1 
ATOM   5717 C CE1   . HIS B 1 237 ? 45.338  2.779   14.362 1.00 17.41  ? 279  HIS B CE1   1 
ATOM   5718 N NE2   . HIS B 1 237 ? 46.052  3.863   14.091 1.00 17.73  ? 279  HIS B NE2   1 
ATOM   5719 N N     . ALA B 1 238 ? 51.530  0.909   13.483 1.00 18.79  ? 280  ALA B N     1 
ATOM   5720 C CA    . ALA B 1 238 ? 52.922  0.482   13.360 1.00 20.52  ? 280  ALA B CA    1 
ATOM   5721 C C     . ALA B 1 238 ? 53.804  0.787   14.567 1.00 21.68  ? 280  ALA B C     1 
ATOM   5722 O O     . ALA B 1 238 ? 54.766  0.043   14.798 1.00 22.67  ? 280  ALA B O     1 
ATOM   5723 C CB    . ALA B 1 238 ? 53.526  1.100   12.099 1.00 18.95  ? 280  ALA B CB    1 
ATOM   5724 N N     . ASN B 1 239 ? 53.473  1.828   15.366 1.00 19.42  ? 281  ASN B N     1 
ATOM   5725 C CA    . ASN B 1 239 ? 54.394  2.420   16.307 1.00 19.86  ? 281  ASN B CA    1 
ATOM   5726 C C     . ASN B 1 239 ? 53.854  2.388   17.743 1.00 20.30  ? 281  ASN B C     1 
ATOM   5727 O O     . ASN B 1 239 ? 52.672  2.678   17.957 1.00 18.64  ? 281  ASN B O     1 
ATOM   5728 C CB    . ASN B 1 239 ? 54.644  3.894   15.940 1.00 23.82  ? 281  ASN B CB    1 
ATOM   5729 C CG    . ASN B 1 239 ? 54.850  4.132   14.454 1.00 31.02  ? 281  ASN B CG    1 
ATOM   5730 O OD1   . ASN B 1 239 ? 54.048  4.806   13.776 1.00 35.07  ? 281  ASN B OD1   1 
ATOM   5731 N ND2   . ASN B 1 239 ? 55.944  3.592   13.956 1.00 24.87  ? 281  ASN B ND2   1 
ATOM   5732 N N     . MET B 1 240 ? 54.741  2.130   18.715 1.00 18.46  ? 282  MET B N     1 
ATOM   5733 C CA    . MET B 1 240 ? 54.436  2.239   20.134 1.00 20.50  ? 282  MET B CA    1 
ATOM   5734 C C     . MET B 1 240 ? 53.794  3.595   20.427 1.00 20.89  ? 282  MET B C     1 
ATOM   5735 O O     . MET B 1 240 ? 52.838  3.676   21.209 1.00 19.80  ? 282  MET B O     1 
ATOM   5736 C CB    . MET B 1 240 ? 55.680  2.061   21.025 1.00 22.90  ? 282  MET B CB    1 
ATOM   5737 C CG    . MET B 1 240 ? 55.454  2.367   22.525 1.00 24.80  ? 282  MET B CG    1 
ATOM   5738 S SD    . MET B 1 240 ? 54.246  1.304   23.480 1.00 30.19  ? 282  MET B SD    1 
ATOM   5739 C CE    . MET B 1 240 ? 55.238  -0.159  23.792 1.00 32.04  ? 282  MET B CE    1 
ATOM   5740 N N     . GLU B 1 241 ? 54.275  4.657   19.755 1.00 20.61  ? 283  GLU B N     1 
ATOM   5741 C CA    . GLU B 1 241 ? 53.815  5.998   20.088 1.00 22.54  ? 283  GLU B CA    1 
ATOM   5742 C C     . GLU B 1 241 ? 52.460  6.360   19.473 1.00 20.22  ? 283  GLU B C     1 
ATOM   5743 O O     . GLU B 1 241 ? 51.985  7.486   19.672 1.00 18.99  ? 283  GLU B O     1 
ATOM   5744 C CB    . GLU B 1 241 ? 54.908  7.018   19.753 1.00 28.93  ? 283  GLU B CB    1 
ATOM   5745 C CG    . GLU B 1 241 ? 55.212  7.111   18.284 1.00 33.19  ? 283  GLU B CG    1 
ATOM   5746 C CD    . GLU B 1 241 ? 56.298  6.177   17.775 1.00 38.96  ? 283  GLU B CD    1 
ATOM   5747 O OE1   . GLU B 1 241 ? 56.695  5.163   18.496 1.00 30.57  ? 283  GLU B OE1   1 
ATOM   5748 O OE2   . GLU B 1 241 ? 56.769  6.486   16.643 1.00 49.30  ? 283  GLU B OE2   1 
ATOM   5749 N N     . ASP B 1 242 ? 51.806  5.460   18.726 1.00 18.23  ? 284  ASP B N     1 
ATOM   5750 C CA    . ASP B 1 242 ? 50.530  5.744   18.088 1.00 18.00  ? 284  ASP B CA    1 
ATOM   5751 C C     . ASP B 1 242 ? 49.366  5.829   19.104 1.00 17.26  ? 284  ASP B C     1 
ATOM   5752 O O     . ASP B 1 242 ? 48.254  6.214   18.711 1.00 17.77  ? 284  ASP B O     1 
ATOM   5753 C CB    . ASP B 1 242 ? 50.183  4.709   17.018 1.00 18.37  ? 284  ASP B CB    1 
ATOM   5754 C CG    . ASP B 1 242 ? 51.061  4.801   15.764 1.00 23.10  ? 284  ASP B CG    1 
ATOM   5755 O OD1   . ASP B 1 242 ? 51.684  5.871   15.592 1.00 24.53  ? 284  ASP B OD1   1 
ATOM   5756 O OD2   . ASP B 1 242 ? 51.166  3.792   15.019 1.00 21.60  ? 284  ASP B OD2   1 
ATOM   5757 N N     . VAL B 1 243 ? 49.588  5.414   20.362 1.00 18.87  ? 285  VAL B N     1 
ATOM   5758 C CA    . VAL B 1 243 ? 48.501  5.323   21.351 1.00 17.17  ? 285  VAL B CA    1 
ATOM   5759 C C     . VAL B 1 243 ? 47.508  6.484   21.212 1.00 16.32  ? 285  VAL B C     1 
ATOM   5760 O O     . VAL B 1 243 ? 46.319  6.250   21.060 1.00 16.30  ? 285  VAL B O     1 
ATOM   5761 C CB    . VAL B 1 243 ? 49.075  5.250   22.773 1.00 17.77  ? 285  VAL B CB    1 
ATOM   5762 C CG1   . VAL B 1 243 ? 48.025  5.524   23.856 1.00 17.82  ? 285  VAL B CG1   1 
ATOM   5763 C CG2   . VAL B 1 243 ? 49.719  3.899   23.056 1.00 17.91  ? 285  VAL B CG2   1 
ATOM   5764 N N     . PRO B 1 244 ? 47.915  7.775   21.354 1.00 18.03  ? 286  PRO B N     1 
ATOM   5765 C CA    . PRO B 1 244 ? 46.932  8.850   21.413 1.00 17.28  ? 286  PRO B CA    1 
ATOM   5766 C C     . PRO B 1 244 ? 46.129  8.976   20.135 1.00 18.37  ? 286  PRO B C     1 
ATOM   5767 O O     . PRO B 1 244 ? 44.944  9.279   20.179 1.00 15.57  ? 286  PRO B O     1 
ATOM   5768 C CB    . PRO B 1 244 ? 47.776  10.081  21.731 1.00 18.81  ? 286  PRO B CB    1 
ATOM   5769 C CG    . PRO B 1 244 ? 49.181  9.712   21.245 1.00 17.84  ? 286  PRO B CG    1 
ATOM   5770 C CD    . PRO B 1 244 ? 49.278  8.257   21.658 1.00 17.48  ? 286  PRO B CD    1 
ATOM   5771 N N     . LYS B 1 245 ? 46.758  8.726   18.973 1.00 16.95  ? 287  LYS B N     1 
ATOM   5772 C CA    . LYS B 1 245 ? 46.027  8.825   17.725 1.00 16.61  ? 287  LYS B CA    1 
ATOM   5773 C C     . LYS B 1 245 ? 44.950  7.750   17.589 1.00 15.45  ? 287  LYS B C     1 
ATOM   5774 O O     . LYS B 1 245 ? 43.904  7.995   16.999 1.00 14.76  ? 287  LYS B O     1 
ATOM   5775 C CB    . LYS B 1 245 ? 46.989  8.669   16.537 1.00 21.40  ? 287  LYS B CB    1 
ATOM   5776 C CG    . LYS B 1 245 ? 48.084  9.724   16.416 1.00 26.20  ? 287  LYS B CG    1 
ATOM   5777 C CD    . LYS B 1 245 ? 48.890  9.552   15.083 1.00 30.57  ? 287  LYS B CD    1 
ATOM   5778 C CE    . LYS B 1 245 ? 49.655  8.245   15.010 1.00 39.30  ? 287  LYS B CE    1 
ATOM   5779 N NZ    . LYS B 1 245 ? 49.772  7.668   13.631 1.00 44.31  ? 287  LYS B NZ    1 
ATOM   5780 N N     . ILE B 1 246 ? 45.203  6.548   18.139 1.00 15.31  ? 288  ILE B N     1 
ATOM   5781 C CA    . ILE B 1 246 ? 44.235  5.471   18.089 1.00 13.43  ? 288  ILE B CA    1 
ATOM   5782 C C     . ILE B 1 246 ? 43.013  5.846   18.936 1.00 13.01  ? 288  ILE B C     1 
ATOM   5783 O O     . ILE B 1 246 ? 41.886  5.654   18.510 1.00 13.63  ? 288  ILE B O     1 
ATOM   5784 C CB    . ILE B 1 246 ? 44.853  4.142   18.570 1.00 15.28  ? 288  ILE B CB    1 
ATOM   5785 C CG1   . ILE B 1 246 ? 46.108  3.737   17.783 1.00 14.76  ? 288  ILE B CG1   1 
ATOM   5786 C CG2   . ILE B 1 246 ? 43.835  3.036   18.526 1.00 16.27  ? 288  ILE B CG2   1 
ATOM   5787 C CD1   . ILE B 1 246 ? 46.954  2.722   18.530 1.00 15.48  ? 288  ILE B CD1   1 
ATOM   5788 N N     . ILE B 1 247 ? 43.242  6.355   20.151 1.00 12.71  ? 289  ILE B N     1 
ATOM   5789 C CA    . ILE B 1 247 ? 42.116  6.689   21.029 1.00 14.38  ? 289  ILE B CA    1 
ATOM   5790 C C     . ILE B 1 247 ? 41.321  7.827   20.382 1.00 14.42  ? 289  ILE B C     1 
ATOM   5791 O O     . ILE B 1 247 ? 40.109  7.789   20.386 1.00 13.85  ? 289  ILE B O     1 
ATOM   5792 C CB    . ILE B 1 247 ? 42.597  7.032   22.453 1.00 13.66  ? 289  ILE B CB    1 
ATOM   5793 C CG1   . ILE B 1 247 ? 43.339  5.880   23.153 1.00 15.52  ? 289  ILE B CG1   1 
ATOM   5794 C CG2   . ILE B 1 247 ? 41.449  7.570   23.318 1.00 15.76  ? 289  ILE B CG2   1 
ATOM   5795 C CD1   . ILE B 1 247 ? 42.553  4.624   23.287 1.00 15.96  ? 289  ILE B CD1   1 
ATOM   5796 N N     . GLU B 1 248 ? 42.012  8.834   19.845 1.00 14.91  ? 290  GLU B N     1 
ATOM   5797 C CA    . GLU B 1 248 ? 41.336  9.983   19.248 1.00 15.35  ? 290  GLU B CA    1 
ATOM   5798 C C     . GLU B 1 248 ? 40.538  9.598   18.015 1.00 15.81  ? 290  GLU B C     1 
ATOM   5799 O O     . GLU B 1 248 ? 39.523  10.229  17.735 1.00 18.38  ? 290  GLU B O     1 
ATOM   5800 C CB    . GLU B 1 248 ? 42.328  11.110  18.929 1.00 16.74  ? 290  GLU B CB    1 
ATOM   5801 C CG    . GLU B 1 248 ? 42.737  11.893  20.172 1.00 18.92  ? 290  GLU B CG    1 
ATOM   5802 C CD    . GLU B 1 248 ? 41.569  12.444  20.996 1.00 20.92  ? 290  GLU B CD    1 
ATOM   5803 O OE1   . GLU B 1 248 ? 40.725  13.149  20.402 1.00 22.60  ? 290  GLU B OE1   1 
ATOM   5804 O OE2   . GLU B 1 248 ? 41.492  12.191  22.214 1.00 19.69  ? 290  GLU B OE2   1 
ATOM   5805 N N     . ALA B 1 249 ? 40.956  8.565   17.268 1.00 15.83  ? 291  ALA B N     1 
ATOM   5806 C CA    . ALA B 1 249 ? 40.199  8.085   16.116 1.00 16.35  ? 291  ALA B CA    1 
ATOM   5807 C C     . ALA B 1 249 ? 39.009  7.222   16.521 1.00 15.06  ? 291  ALA B C     1 
ATOM   5808 O O     . ALA B 1 249 ? 37.939  7.286   15.904 1.00 16.88  ? 291  ALA B O     1 
ATOM   5809 C CB    . ALA B 1 249 ? 41.097  7.282   15.174 1.00 19.87  ? 291  ALA B CB    1 
ATOM   5810 N N     . MET B 1 250 ? 39.170  6.413   17.572 1.00 16.23  ? 292  MET B N     1 
ATOM   5811 C CA    . MET B 1 250 ? 38.086  5.533   17.958 1.00 16.54  ? 292  MET B CA    1 
ATOM   5812 C C     . MET B 1 250 ? 36.993  6.294   18.718 1.00 15.49  ? 292  MET B C     1 
ATOM   5813 O O     . MET B 1 250 ? 35.833  5.913   18.582 1.00 15.63  ? 292  MET B O     1 
ATOM   5814 C CB    . MET B 1 250 ? 38.596  4.390   18.841 1.00 17.70  ? 292  MET B CB    1 
ATOM   5815 C CG    . MET B 1 250 ? 39.415  3.340   18.067 1.00 19.84  ? 292  MET B CG    1 
ATOM   5816 S SD    . MET B 1 250 ? 38.544  2.380   16.778 1.00 19.24  ? 292  MET B SD    1 
ATOM   5817 C CE    . MET B 1 250 ? 37.384  1.461   17.813 1.00 22.07  ? 292  MET B CE    1 
ATOM   5818 N N     . ARG B 1 251 ? 37.380  7.310   19.528 1.00 16.40  ? 293  ARG B N     1 
ATOM   5819 C CA    . ARG B 1 251 ? 36.443  7.995   20.404 1.00 16.67  ? 293  ARG B CA    1 
ATOM   5820 C C     . ARG B 1 251 ? 35.239  8.471   19.602 1.00 16.10  ? 293  ARG B C     1 
ATOM   5821 O O     . ARG B 1 251 ? 34.111  8.164   19.934 1.00 15.81  ? 293  ARG B O     1 
ATOM   5822 C CB    . ARG B 1 251 ? 37.127  9.125   21.177 1.00 16.40  ? 293  ARG B CB    1 
ATOM   5823 C CG    . ARG B 1 251 ? 36.215  9.868   22.161 1.00 18.65  ? 293  ARG B CG    1 
ATOM   5824 C CD    . ARG B 1 251 ? 35.753  11.224  21.674 1.00 21.57  ? 293  ARG B CD    1 
ATOM   5825 N NE    . ARG B 1 251 ? 36.822  12.154  21.361 1.00 21.05  ? 293  ARG B NE    1 
ATOM   5826 C CZ    . ARG B 1 251 ? 36.847  12.999  20.322 1.00 25.15  ? 293  ARG B CZ    1 
ATOM   5827 N NH1   . ARG B 1 251 ? 35.805  13.190  19.518 1.00 23.53  ? 293  ARG B NH1   1 
ATOM   5828 N NH2   . ARG B 1 251 ? 37.923  13.732  20.131 1.00 26.57  ? 293  ARG B NH2   1 
ATOM   5829 N N     . PRO B 1 252 ? 35.368  9.260   18.500 1.00 15.80  ? 294  PRO B N     1 
ATOM   5830 C CA    . PRO B 1 252 ? 34.151  9.725   17.833 1.00 17.46  ? 294  PRO B CA    1 
ATOM   5831 C C     . PRO B 1 252 ? 33.267  8.612   17.275 1.00 16.89  ? 294  PRO B C     1 
ATOM   5832 O O     . PRO B 1 252 ? 32.041  8.724   17.173 1.00 17.90  ? 294  PRO B O     1 
ATOM   5833 C CB    . PRO B 1 252 ? 34.661  10.650  16.704 1.00 19.28  ? 294  PRO B CB    1 
ATOM   5834 C CG    . PRO B 1 252 ? 36.114  10.251  16.529 1.00 19.34  ? 294  PRO B CG    1 
ATOM   5835 C CD    . PRO B 1 252 ? 36.612  9.737   17.875 1.00 17.40  ? 294  PRO B CD    1 
ATOM   5836 N N     . LEU B 1 253 ? 33.896  7.514   16.810 1.00 15.88  ? 295  LEU B N     1 
ATOM   5837 C CA    . LEU B 1 253 ? 33.179  6.354   16.316 1.00 15.33  ? 295  LEU B CA    1 
ATOM   5838 C C     . LEU B 1 253 ? 32.352  5.713   17.436 1.00 15.56  ? 295  LEU B C     1 
ATOM   5839 O O     . LEU B 1 253 ? 31.257  5.277   17.167 1.00 16.32  ? 295  LEU B O     1 
ATOM   5840 C CB    . LEU B 1 253 ? 34.145  5.298   15.758 1.00 15.33  ? 295  LEU B CB    1 
ATOM   5841 C CG    . LEU B 1 253 ? 35.030  5.787   14.600 1.00 17.19  ? 295  LEU B CG    1 
ATOM   5842 C CD1   . LEU B 1 253 ? 35.935  4.647   14.094 1.00 17.98  ? 295  LEU B CD1   1 
ATOM   5843 C CD2   . LEU B 1 253 ? 34.197  6.345   13.478 1.00 17.62  ? 295  LEU B CD2   1 
ATOM   5844 N N     . ARG B 1 254 ? 32.895  5.679   18.655 1.00 15.81  ? 296  ARG B N     1 
ATOM   5845 C CA    . ARG B 1 254 ? 32.184  5.129   19.804 1.00 17.38  ? 296  ARG B CA    1 
ATOM   5846 C C     . ARG B 1 254 ? 31.142  6.135   20.358 1.00 18.03  ? 296  ARG B C     1 
ATOM   5847 O O     . ARG B 1 254 ? 30.031  5.739   20.681 1.00 19.24  ? 296  ARG B O     1 
ATOM   5848 C CB    . ARG B 1 254 ? 33.192  4.682   20.860 1.00 16.17  ? 296  ARG B CB    1 
ATOM   5849 C CG    . ARG B 1 254 ? 34.115  3.533   20.440 1.00 16.21  ? 296  ARG B CG    1 
ATOM   5850 C CD    . ARG B 1 254 ? 33.389  2.296   19.972 1.00 16.86  ? 296  ARG B CD    1 
ATOM   5851 N NE    . ARG B 1 254 ? 32.379  1.861   20.966 1.00 20.81  ? 296  ARG B NE    1 
ATOM   5852 C CZ    . ARG B 1 254 ? 32.685  1.283   22.129 1.00 23.06  ? 296  ARG B CZ    1 
ATOM   5853 N NH1   . ARG B 1 254 ? 33.924  0.944   22.375 1.00 23.29  ? 296  ARG B NH1   1 
ATOM   5854 N NH2   . ARG B 1 254 ? 31.769  1.094   23.067 1.00 25.04  ? 296  ARG B NH2   1 
ATOM   5855 N N     . VAL B 1 255 ? 31.494  7.410   20.532 1.00 17.62  ? 297  VAL B N     1 
ATOM   5856 C CA    . VAL B 1 255 ? 30.546  8.378   21.087 1.00 17.68  ? 297  VAL B CA    1 
ATOM   5857 C C     . VAL B 1 255 ? 29.304  8.451   20.195 1.00 20.39  ? 297  VAL B C     1 
ATOM   5858 O O     . VAL B 1 255 ? 28.182  8.533   20.713 1.00 22.48  ? 297  VAL B O     1 
ATOM   5859 C CB    . VAL B 1 255 ? 31.194  9.737   21.390 1.00 21.59  ? 297  VAL B CB    1 
ATOM   5860 C CG1   . VAL B 1 255 ? 30.184  10.780  21.845 1.00 22.13  ? 297  VAL B CG1   1 
ATOM   5861 C CG2   . VAL B 1 255 ? 32.266  9.611   22.462 1.00 21.88  ? 297  VAL B CG2   1 
ATOM   5862 N N     . SER B 1 256 ? 29.479  8.402   18.858 1.00 20.29  ? 298  SER B N     1 
ATOM   5863 C CA    . SER B 1 256 ? 28.355  8.425   17.915 1.00 20.38  ? 298  SER B CA    1 
ATOM   5864 C C     . SER B 1 256 ? 27.781  7.046   17.647 1.00 22.07  ? 298  SER B C     1 
ATOM   5865 O O     . SER B 1 256 ? 26.822  6.897   16.895 1.00 25.43  ? 298  SER B O     1 
ATOM   5866 C CB    . SER B 1 256 ? 28.744  9.057   16.609 1.00 22.26  ? 298  SER B CB    1 
ATOM   5867 O OG    . SER B 1 256 ? 28.844  10.453  16.783 1.00 28.68  ? 298  SER B OG    1 
ATOM   5868 N N     . ASN B 1 257 ? 28.379  6.022   18.243 1.00 23.89  ? 299  ASN B N     1 
ATOM   5869 C CA    . ASN B 1 257 ? 27.887  4.662   18.136 1.00 25.66  ? 299  ASN B CA    1 
ATOM   5870 C C     . ASN B 1 257 ? 27.886  4.125   16.701 1.00 24.77  ? 299  ASN B C     1 
ATOM   5871 O O     . ASN B 1 257 ? 27.077  3.283   16.360 1.00 26.23  ? 299  ASN B O     1 
ATOM   5872 C CB    . ASN B 1 257 ? 26.522  4.544   18.838 1.00 32.64  ? 299  ASN B CB    1 
ATOM   5873 C CG    . ASN B 1 257 ? 26.234  3.126   19.280 1.00 33.70  ? 299  ASN B CG    1 
ATOM   5874 O OD1   . ASN B 1 257 ? 27.091  2.461   19.875 1.00 33.26  ? 299  ASN B OD1   1 
ATOM   5875 N ND2   . ASN B 1 257 ? 25.049  2.651   18.951 1.00 39.22  ? 299  ASN B ND2   1 
ATOM   5876 N N     . LEU B 1 258 ? 28.865  4.502   15.871 1.00 20.93  ? 300  LEU B N     1 
ATOM   5877 C CA    . LEU B 1 258 ? 29.082  3.811   14.604 1.00 20.02  ? 300  LEU B CA    1 
ATOM   5878 C C     . LEU B 1 258 ? 29.726  2.440   14.821 1.00 17.62  ? 300  LEU B C     1 
ATOM   5879 O O     . LEU B 1 258 ? 29.566  1.561   13.985 1.00 17.31  ? 300  LEU B O     1 
ATOM   5880 C CB    . LEU B 1 258 ? 30.021  4.602   13.688 1.00 22.46  ? 300  LEU B CB    1 
ATOM   5881 C CG    . LEU B 1 258 ? 29.392  5.756   12.911 1.00 29.12  ? 300  LEU B CG    1 
ATOM   5882 C CD1   . LEU B 1 258 ? 29.162  6.929   13.811 1.00 30.56  ? 300  LEU B CD1   1 
ATOM   5883 C CD2   . LEU B 1 258 ? 30.282  6.138   11.732 1.00 30.58  ? 300  LEU B CD2   1 
ATOM   5884 N N     . VAL B 1 259 ? 30.536  2.347   15.894 1.00 16.80  ? 301  VAL B N     1 
ATOM   5885 C CA    . VAL B 1 259 ? 31.062  1.100   16.423 1.00 17.10  ? 301  VAL B CA    1 
ATOM   5886 C C     . VAL B 1 259 ? 30.493  0.954   17.826 1.00 14.75  ? 301  VAL B C     1 
ATOM   5887 O O     . VAL B 1 259 ? 30.536  1.932   18.578 1.00 15.69  ? 301  VAL B O     1 
ATOM   5888 C CB    . VAL B 1 259 ? 32.603  1.083   16.439 1.00 15.68  ? 301  VAL B CB    1 
ATOM   5889 C CG1   . VAL B 1 259 ? 33.125  -0.145  17.168 1.00 16.85  ? 301  VAL B CG1   1 
ATOM   5890 C CG2   . VAL B 1 259 ? 33.170  1.182   15.036 1.00 17.44  ? 301  VAL B CG2   1 
ATOM   5891 N N     . ALA B 1 260 ? 29.931  -0.227  18.130 1.00 15.73  ? 302  ALA B N     1 
ATOM   5892 C CA    . ALA B 1 260 ? 29.160  -0.381  19.366 1.00 16.77  ? 302  ALA B CA    1 
ATOM   5893 C C     . ALA B 1 260 ? 29.746  -1.424  20.322 1.00 16.78  ? 302  ALA B C     1 
ATOM   5894 O O     . ALA B 1 260 ? 29.359  -1.468  21.493 1.00 17.82  ? 302  ALA B O     1 
ATOM   5895 C CB    . ALA B 1 260 ? 27.732  -0.708  19.011 1.00 19.93  ? 302  ALA B CB    1 
ATOM   5896 N N     . ASN B 1 261 ? 30.689  -2.261  19.856 1.00 14.67  ? 303  ASN B N     1 
ATOM   5897 C CA    . ASN B 1 261 ? 31.319  -3.245  20.756 1.00 14.00  ? 303  ASN B CA    1 
ATOM   5898 C C     . ASN B 1 261 ? 32.511  -2.653  21.473 1.00 15.31  ? 303  ASN B C     1 
ATOM   5899 O O     . ASN B 1 261 ? 33.200  -1.747  20.958 1.00 14.89  ? 303  ASN B O     1 
ATOM   5900 C CB    . ASN B 1 261 ? 31.646  -4.574  20.076 1.00 12.41  ? 303  ASN B CB    1 
ATOM   5901 C CG    . ASN B 1 261 ? 32.744  -4.523  19.056 1.00 13.59  ? 303  ASN B CG    1 
ATOM   5902 O OD1   . ASN B 1 261 ? 32.833  -3.570  18.289 1.00 14.64  ? 303  ASN B OD1   1 
ATOM   5903 N ND2   . ASN B 1 261 ? 33.546  -5.565  19.013 1.00 12.87  ? 303  ASN B ND2   1 
ATOM   5904 N N     . CYS B 1 262 ? 32.779  -3.213  22.669 1.00 14.52  ? 304  CYS B N     1 
ATOM   5905 C CA    . CYS B 1 262 ? 33.996  -2.876  23.394 1.00 14.89  ? 304  CYS B CA    1 
ATOM   5906 C C     . CYS B 1 262 ? 35.202  -3.353  22.574 1.00 14.10  ? 304  CYS B C     1 
ATOM   5907 O O     . CYS B 1 262 ? 35.158  -4.478  22.072 1.00 13.26  ? 304  CYS B O     1 
ATOM   5908 C CB    . CYS B 1 262 ? 33.965  -3.471  24.809 1.00 14.91  ? 304  CYS B CB    1 
ATOM   5909 S SG    . CYS B 1 262 ? 35.467  -3.192  25.748 1.00 16.31  ? 304  CYS B SG    1 
ATOM   5910 N N     . ASN B 1 263 ? 36.202  -2.460  22.378 1.00 13.87  ? 305  ASN B N     1 
ATOM   5911 C CA    . ASN B 1 263 ? 37.318  -2.716  21.462 1.00 15.15  ? 305  ASN B CA    1 
ATOM   5912 C C     . ASN B 1 263 ? 38.587  -2.915  22.267 1.00 15.39  ? 305  ASN B C     1 
ATOM   5913 O O     . ASN B 1 263 ? 39.024  -2.014  22.939 1.00 15.28  ? 305  ASN B O     1 
ATOM   5914 C CB    . ASN B 1 263 ? 37.555  -1.511  20.538 1.00 14.38  ? 305  ASN B CB    1 
ATOM   5915 C CG    . ASN B 1 263 ? 36.235  -1.037  19.989 1.00 15.21  ? 305  ASN B CG    1 
ATOM   5916 O OD1   . ASN B 1 263 ? 35.779  0.060   20.312 1.00 17.36  ? 305  ASN B OD1   1 
ATOM   5917 N ND2   . ASN B 1 263 ? 35.547  -1.930  19.307 1.00 14.88  ? 305  ASN B ND2   1 
ATOM   5918 N N     . LEU B 1 264 ? 39.202  -4.077  22.150 1.00 14.09  ? 306  LEU B N     1 
ATOM   5919 C CA    . LEU B 1 264 ? 40.512  -4.312  22.725 1.00 13.71  ? 306  LEU B CA    1 
ATOM   5920 C C     . LEU B 1 264 ? 41.564  -3.763  21.769 1.00 14.15  ? 306  LEU B C     1 
ATOM   5921 O O     . LEU B 1 264 ? 41.642  -4.193  20.611 1.00 14.14  ? 306  LEU B O     1 
ATOM   5922 C CB    . LEU B 1 264 ? 40.720  -5.815  22.905 1.00 12.93  ? 306  LEU B CB    1 
ATOM   5923 C CG    . LEU B 1 264 ? 40.001  -6.403  24.116 1.00 13.12  ? 306  LEU B CG    1 
ATOM   5924 C CD1   . LEU B 1 264 ? 40.141  -7.905  24.164 1.00 14.91  ? 306  LEU B CD1   1 
ATOM   5925 C CD2   . LEU B 1 264 ? 40.519  -5.772  25.398 1.00 14.27  ? 306  LEU B CD2   1 
ATOM   5926 N N     . MET B 1 265 ? 42.330  -2.821  22.322 1.00 13.43  ? 307  MET B N     1 
ATOM   5927 C CA    . MET B 1 265 ? 43.493  -2.235  21.709 1.00 13.37  ? 307  MET B CA    1 
ATOM   5928 C C     . MET B 1 265 ? 44.684  -2.896  22.397 1.00 12.10  ? 307  MET B C     1 
ATOM   5929 O O     . MET B 1 265 ? 45.080  -2.513  23.506 1.00 13.70  ? 307  MET B O     1 
ATOM   5930 C CB    . MET B 1 265 ? 43.474  -0.723  21.937 1.00 14.50  ? 307  MET B CB    1 
ATOM   5931 C CG    . MET B 1 265 ? 44.728  0.001   21.627 1.00 14.19  ? 307  MET B CG    1 
ATOM   5932 S SD    . MET B 1 265 ? 44.488  1.801   22.018 1.00 17.36  ? 307  MET B SD    1 
ATOM   5933 C CE    . MET B 1 265 ? 46.171  2.359   22.245 1.00 18.65  ? 307  MET B CE    1 
ATOM   5934 N N     . MET B 1 266 ? 45.274  -3.857  21.721 1.00 12.85  ? 308  MET B N     1 
ATOM   5935 C CA    . MET B 1 266 ? 46.246  -4.757  22.331 1.00 13.82  ? 308  MET B CA    1 
ATOM   5936 C C     . MET B 1 266 ? 47.683  -4.337  22.002 1.00 13.06  ? 308  MET B C     1 
ATOM   5937 O O     . MET B 1 266 ? 48.012  -4.112  20.832 1.00 13.53  ? 308  MET B O     1 
ATOM   5938 C CB    . MET B 1 266 ? 46.044  -6.162  21.764 1.00 14.84  ? 308  MET B CB    1 
ATOM   5939 C CG    . MET B 1 266 ? 44.632  -6.688  21.776 1.00 16.05  ? 308  MET B CG    1 
ATOM   5940 S SD    . MET B 1 266 ? 44.140  -7.056  23.460 1.00 17.68  ? 308  MET B SD    1 
ATOM   5941 C CE    . MET B 1 266 ? 45.481  -8.089  23.976 1.00 16.73  ? 308  MET B CE    1 
ATOM   5942 N N     . SER B 1 267 ? 48.535  -4.291  23.006 1.00 12.26  ? 309  SER B N     1 
ATOM   5943 C CA    . SER B 1 267 ? 49.959  -4.082  22.762 1.00 12.79  ? 309  SER B CA    1 
ATOM   5944 C C     . SER B 1 267 ? 50.587  -5.333  22.165 1.00 12.40  ? 309  SER B C     1 
ATOM   5945 O O     . SER B 1 267 ? 50.236  -6.467  22.513 1.00 14.01  ? 309  SER B O     1 
ATOM   5946 C CB    . SER B 1 267 ? 50.749  -3.683  23.998 1.00 13.29  ? 309  SER B CB    1 
ATOM   5947 O OG    . SER B 1 267 ? 50.964  -4.759  24.911 1.00 14.34  ? 309  SER B OG    1 
ATOM   5948 N N     . ALA B 1 268 ? 51.618  -5.119  21.326 1.00 12.48  ? 310  ALA B N     1 
ATOM   5949 C CA    . ALA B 1 268 ? 52.323  -6.257  20.748 1.00 12.49  ? 310  ALA B CA    1 
ATOM   5950 C C     . ALA B 1 268 ? 52.910  -7.137  21.832 1.00 11.92  ? 310  ALA B C     1 
ATOM   5951 O O     . ALA B 1 268 ? 52.886  -8.363  21.669 1.00 13.28  ? 310  ALA B O     1 
ATOM   5952 C CB    . ALA B 1 268 ? 53.410  -5.778  19.827 1.00 13.68  ? 310  ALA B CB    1 
ATOM   5953 N N     . SER B 1 269 ? 53.427  -6.557  22.918 1.00 12.52  ? 311  SER B N     1 
ATOM   5954 C CA    . SER B 1 269 ? 54.054  -7.371  23.949 1.00 13.38  ? 311  SER B CA    1 
ATOM   5955 C C     . SER B 1 269 ? 53.046  -8.340  24.583 1.00 13.46  ? 311  SER B C     1 
ATOM   5956 O O     . SER B 1 269 ? 53.327  -9.542  24.783 1.00 13.99  ? 311  SER B O     1 
ATOM   5957 C CB    . SER B 1 269 ? 54.704  -6.495  24.951 1.00 13.97  ? 311  SER B CB    1 
ATOM   5958 O OG    . SER B 1 269 ? 53.740  -5.693  25.619 1.00 13.43  ? 311  SER B OG    1 
ATOM   5959 N N     . TYR B 1 270 ? 51.827  -7.831  24.861 1.00 13.93  ? 312  TYR B N     1 
ATOM   5960 C CA    . TYR B 1 270 ? 50.802  -8.704  25.416 1.00 13.82  ? 312  TYR B CA    1 
ATOM   5961 C C     . TYR B 1 270 ? 50.477  -9.798  24.428 1.00 11.90  ? 312  TYR B C     1 
ATOM   5962 O O     . TYR B 1 270 ? 50.389  -10.971 24.782 1.00 12.71  ? 312  TYR B O     1 
ATOM   5963 C CB    . TYR B 1 270 ? 49.530  -7.925  25.797 1.00 14.21  ? 312  TYR B CB    1 
ATOM   5964 C CG    . TYR B 1 270 ? 48.456  -8.760  26.462 1.00 13.95  ? 312  TYR B CG    1 
ATOM   5965 C CD1   . TYR B 1 270 ? 47.691  -9.658  25.775 1.00 13.85  ? 312  TYR B CD1   1 
ATOM   5966 C CD2   . TYR B 1 270 ? 48.212  -8.616  27.799 1.00 19.98  ? 312  TYR B CD2   1 
ATOM   5967 C CE1   . TYR B 1 270 ? 46.666  -10.372 26.371 1.00 16.06  ? 312  TYR B CE1   1 
ATOM   5968 C CE2   . TYR B 1 270 ? 47.167  -9.280  28.404 1.00 19.51  ? 312  TYR B CE2   1 
ATOM   5969 C CZ    . TYR B 1 270 ? 46.403  -10.172 27.698 1.00 19.16  ? 312  TYR B CZ    1 
ATOM   5970 O OH    . TYR B 1 270 ? 45.409  -10.941 28.328 1.00 18.65  ? 312  TYR B OH    1 
ATOM   5971 N N     . GLN B 1 271 ? 50.223  -9.420  23.147 1.00 10.53  ? 313  GLN B N     1 
ATOM   5972 C CA    . GLN B 1 271 ? 49.865  -10.408 22.157 1.00 11.83  ? 313  GLN B CA    1 
ATOM   5973 C C     . GLN B 1 271 ? 50.909  -11.499 22.067 1.00 12.79  ? 313  GLN B C     1 
ATOM   5974 O O     . GLN B 1 271 ? 50.534  -12.678 21.998 1.00 13.89  ? 313  GLN B O     1 
ATOM   5975 C CB    . GLN B 1 271 ? 49.563  -9.750  20.815 1.00 12.86  ? 313  GLN B CB    1 
ATOM   5976 C CG    . GLN B 1 271 ? 48.311  -8.902  20.915 1.00 13.45  ? 313  GLN B CG    1 
ATOM   5977 C CD    . GLN B 1 271 ? 47.966  -8.357  19.567 1.00 16.34  ? 313  GLN B CD    1 
ATOM   5978 O OE1   . GLN B 1 271 ? 48.679  -7.523  19.013 1.00 18.61  ? 313  GLN B OE1   1 
ATOM   5979 N NE2   . GLN B 1 271 ? 46.833  -8.826  19.090 1.00 16.36  ? 313  GLN B NE2   1 
ATOM   5980 N N     . LEU B 1 272 ? 52.186  -11.130 21.955 1.00 14.60  ? 314  LEU B N     1 
ATOM   5981 C CA    . LEU B 1 272 ? 53.250  -12.141 21.917 1.00 14.65  ? 314  LEU B CA    1 
ATOM   5982 C C     . LEU B 1 272 ? 53.284  -13.041 23.146 1.00 16.10  ? 314  LEU B C     1 
ATOM   5983 O O     . LEU B 1 272 ? 53.479  -14.247 23.019 1.00 16.28  ? 314  LEU B O     1 
ATOM   5984 C CB    . LEU B 1 272 ? 54.599  -11.441 21.696 1.00 17.00  ? 314  LEU B CB    1 
ATOM   5985 C CG    . LEU B 1 272 ? 54.735  -10.744 20.344 1.00 18.38  ? 314  LEU B CG    1 
ATOM   5986 C CD1   . LEU B 1 272 ? 55.958  -9.824  20.335 1.00 19.97  ? 314  LEU B CD1   1 
ATOM   5987 C CD2   . LEU B 1 272 ? 54.821  -11.750 19.192 1.00 18.79  ? 314  LEU B CD2   1 
ATOM   5988 N N     . ALA B 1 273 ? 53.030  -12.474 24.315 1.00 15.04  ? 315  ALA B N     1 
ATOM   5989 C CA    . ALA B 1 273 ? 53.024  -13.195 25.573 1.00 14.94  ? 315  ALA B CA    1 
ATOM   5990 C C     . ALA B 1 273 ? 51.931  -14.244 25.624 1.00 17.10  ? 315  ALA B C     1 
ATOM   5991 O O     . ALA B 1 273 ? 52.040  -15.220 26.386 1.00 16.67  ? 315  ALA B O     1 
ATOM   5992 C CB    . ALA B 1 273 ? 52.901  -12.267 26.746 1.00 14.64  ? 315  ALA B CB    1 
ATOM   5993 N N     . MET B 1 274 ? 50.866  -14.038 24.869 1.00 14.74  ? 316  MET B N     1 
ATOM   5994 C CA    . MET B 1 274 ? 49.808  -15.033 24.812 1.00 16.20  ? 316  MET B CA    1 
ATOM   5995 C C     . MET B 1 274 ? 50.327  -16.368 24.327 1.00 15.97  ? 316  MET B C     1 
ATOM   5996 O O     . MET B 1 274 ? 49.756  -17.386 24.712 1.00 20.11  ? 316  MET B O     1 
ATOM   5997 C CB    . MET B 1 274 ? 48.678  -14.570 23.883 1.00 16.23  ? 316  MET B CB    1 
ATOM   5998 C CG    . MET B 1 274 ? 47.888  -13.441 24.448 1.00 16.39  ? 316  MET B CG    1 
ATOM   5999 S SD    . MET B 1 274 ? 46.793  -12.623 23.218 1.00 19.20  ? 316  MET B SD    1 
ATOM   6000 C CE    . MET B 1 274 ? 45.657  -13.945 22.840 1.00 20.84  ? 316  MET B CE    1 
ATOM   6001 N N     . PHE B 1 275 ? 51.243  -16.350 23.349 1.00 17.25  ? 317  PHE B N     1 
ATOM   6002 C CA    . PHE B 1 275 ? 51.627  -17.602 22.696 1.00 20.91  ? 317  PHE B CA    1 
ATOM   6003 C C     . PHE B 1 275 ? 53.125  -17.925 22.805 1.00 23.07  ? 317  PHE B C     1 
ATOM   6004 O O     . PHE B 1 275 ? 53.544  -19.043 22.478 1.00 21.05  ? 317  PHE B O     1 
ATOM   6005 C CB    . PHE B 1 275 ? 51.182  -17.612 21.239 1.00 21.47  ? 317  PHE B CB    1 
ATOM   6006 C CG    . PHE B 1 275 ? 49.690  -17.517 21.032 1.00 24.44  ? 317  PHE B CG    1 
ATOM   6007 C CD1   . PHE B 1 275 ? 48.830  -18.443 21.596 1.00 26.70  ? 317  PHE B CD1   1 
ATOM   6008 C CD2   . PHE B 1 275 ? 49.146  -16.496 20.279 1.00 23.24  ? 317  PHE B CD2   1 
ATOM   6009 C CE1   . PHE B 1 275 ? 47.460  -18.363 21.389 1.00 28.94  ? 317  PHE B CE1   1 
ATOM   6010 C CE2   . PHE B 1 275 ? 47.778  -16.420 20.055 1.00 24.50  ? 317  PHE B CE2   1 
ATOM   6011 C CZ    . PHE B 1 275 ? 46.936  -17.357 20.601 1.00 25.57  ? 317  PHE B CZ    1 
ATOM   6012 N N     . LYS B 1 276 ? 53.937  -16.998 23.323 1.00 19.18  ? 318  LYS B N     1 
ATOM   6013 C CA    . LYS B 1 276 ? 55.379  -17.149 23.365 1.00 18.83  ? 318  LYS B CA    1 
ATOM   6014 C C     . LYS B 1 276 ? 55.869  -16.776 24.760 1.00 19.30  ? 318  LYS B C     1 
ATOM   6015 O O     . LYS B 1 276 ? 55.194  -16.023 25.463 1.00 19.65  ? 318  LYS B O     1 
ATOM   6016 C CB    . LYS B 1 276 ? 56.035  -16.198 22.370 1.00 19.53  ? 318  LYS B CB    1 
ATOM   6017 C CG    . LYS B 1 276 ? 55.541  -16.371 20.937 1.00 23.40  ? 318  LYS B CG    1 
ATOM   6018 C CD    . LYS B 1 276 ? 56.289  -15.500 20.014 1.00 29.34  ? 318  LYS B CD    1 
ATOM   6019 C CE    . LYS B 1 276 ? 55.954  -15.715 18.547 1.00 35.17  ? 318  LYS B CE    1 
ATOM   6020 N NZ    . LYS B 1 276 ? 56.418  -17.036 18.054 1.00 38.71  ? 318  LYS B NZ    1 
ATOM   6021 N N     . ARG B 1 277 ? 56.989  -17.359 25.168 1.00 15.22  ? 319  ARG B N     1 
ATOM   6022 C CA    . ARG B 1 277 ? 57.672  -16.965 26.379 1.00 15.19  ? 319  ARG B CA    1 
ATOM   6023 C C     . ARG B 1 277 ? 58.671  -15.863 26.075 1.00 13.26  ? 319  ARG B C     1 
ATOM   6024 O O     . ARG B 1 277 ? 59.108  -15.705 24.933 1.00 12.97  ? 319  ARG B O     1 
ATOM   6025 C CB    . ARG B 1 277 ? 58.373  -18.188 26.978 1.00 16.71  ? 319  ARG B CB    1 
ATOM   6026 C CG    . ARG B 1 277 ? 57.389  -19.311 27.268 1.00 17.61  ? 319  ARG B CG    1 
ATOM   6027 C CD    . ARG B 1 277 ? 58.104  -20.469 27.912 1.00 18.15  ? 319  ARG B CD    1 
ATOM   6028 N NE    . ARG B 1 277 ? 57.193  -21.573 28.145 1.00 18.05  ? 319  ARG B NE    1 
ATOM   6029 C CZ    . ARG B 1 277 ? 57.563  -22.738 28.653 1.00 20.68  ? 319  ARG B CZ    1 
ATOM   6030 N NH1   . ARG B 1 277 ? 58.802  -22.901 29.082 1.00 19.75  ? 319  ARG B NH1   1 
ATOM   6031 N NH2   . ARG B 1 277 ? 56.673  -23.705 28.776 1.00 22.72  ? 319  ARG B NH2   1 
ATOM   6032 N N     . ARG B 1 278 ? 59.023  -15.096 27.112 1.00 12.76  ? 320  ARG B N     1 
ATOM   6033 C CA    . ARG B 1 278 ? 59.830  -13.889 26.921 1.00 12.81  ? 320  ARG B CA    1 
ATOM   6034 C C     . ARG B 1 278 ? 61.167  -14.242 26.267 1.00 13.50  ? 320  ARG B C     1 
ATOM   6035 O O     . ARG B 1 278 ? 61.664  -13.493 25.440 1.00 13.57  ? 320  ARG B O     1 
ATOM   6036 C CB    . ARG B 1 278 ? 60.052  -13.203 28.279 1.00 11.63  ? 320  ARG B CB    1 
ATOM   6037 C CG    . ARG B 1 278 ? 60.666  -11.816 28.144 1.00 13.00  ? 320  ARG B CG    1 
ATOM   6038 C CD    . ARG B 1 278 ? 60.996  -11.340 29.518 1.00 12.41  ? 320  ARG B CD    1 
ATOM   6039 N NE    . ARG B 1 278 ? 61.329  -9.917  29.547 1.00 11.75  ? 320  ARG B NE    1 
ATOM   6040 C CZ    . ARG B 1 278 ? 62.544  -9.419  29.379 1.00 15.89  ? 320  ARG B CZ    1 
ATOM   6041 N NH1   . ARG B 1 278 ? 63.623  -10.211 29.259 1.00 14.92  ? 320  ARG B NH1   1 
ATOM   6042 N NH2   . ARG B 1 278 ? 62.659  -8.085  29.338 1.00 16.57  ? 320  ARG B NH2   1 
ATOM   6043 N N     . ASN B 1 279 ? 61.769  -15.385 26.651 1.00 13.48  ? 321  ASN B N     1 
ATOM   6044 C CA    . ASN B 1 279 ? 63.084  -15.775 26.137 1.00 13.29  ? 321  ASN B CA    1 
ATOM   6045 C C     . ASN B 1 279 ? 63.035  -16.325 24.715 1.00 16.10  ? 321  ASN B C     1 
ATOM   6046 O O     . ASN B 1 279 ? 64.092  -16.719 24.166 1.00 14.65  ? 321  ASN B O     1 
ATOM   6047 C CB    . ASN B 1 279 ? 63.763  -16.698 27.134 1.00 13.19  ? 321  ASN B CB    1 
ATOM   6048 C CG    . ASN B 1 279 ? 63.047  -18.028 27.272 1.00 12.65  ? 321  ASN B CG    1 
ATOM   6049 O OD1   . ASN B 1 279 ? 62.163  -18.410 26.492 1.00 14.80  ? 321  ASN B OD1   1 
ATOM   6050 N ND2   . ASN B 1 279 ? 63.436  -18.717 28.322 1.00 14.12  ? 321  ASN B ND2   1 
ATOM   6051 N N     . GLU B 1 280 ? 61.848  -16.309 24.087 1.00 14.92  ? 322  GLU B N     1 
ATOM   6052 C CA    . GLU B 1 280 ? 61.789  -16.526 22.661 1.00 17.55  ? 322  GLU B CA    1 
ATOM   6053 C C     . GLU B 1 280 ? 61.948  -15.195 21.919 1.00 17.65  ? 322  GLU B C     1 
ATOM   6054 O O     . GLU B 1 280 ? 62.038  -15.172 20.702 1.00 20.01  ? 322  GLU B O     1 
ATOM   6055 C CB    . GLU B 1 280 ? 60.469  -17.177 22.306 1.00 18.83  ? 322  GLU B CB    1 
ATOM   6056 C CG    . GLU B 1 280 ? 60.301  -18.585 22.827 1.00 20.82  ? 322  GLU B CG    1 
ATOM   6057 C CD    . GLU B 1 280 ? 58.880  -19.029 22.543 1.00 24.77  ? 322  GLU B CD    1 
ATOM   6058 O OE1   . GLU B 1 280 ? 58.403  -18.871 21.383 1.00 29.93  ? 322  GLU B OE1   1 
ATOM   6059 O OE2   . GLU B 1 280 ? 58.208  -19.439 23.458 1.00 22.43  ? 322  GLU B OE2   1 
ATOM   6060 N N     . ILE B 1 281 ? 61.895  -14.086 22.639 1.00 15.78  ? 323  ILE B N     1 
ATOM   6061 C CA    . ILE B 1 281 ? 61.875  -12.742 22.048 1.00 17.87  ? 323  ILE B CA    1 
ATOM   6062 C C     . ILE B 1 281 ? 63.181  -11.993 22.357 1.00 17.42  ? 323  ILE B C     1 
ATOM   6063 O O     . ILE B 1 281 ? 63.797  -11.428 21.454 1.00 20.35  ? 323  ILE B O     1 
ATOM   6064 C CB    . ILE B 1 281 ? 60.676  -11.894 22.543 1.00 19.39  ? 323  ILE B CB    1 
ATOM   6065 C CG1   . ILE B 1 281 ? 59.339  -12.651 22.494 1.00 22.16  ? 323  ILE B CG1   1 
ATOM   6066 C CG2   . ILE B 1 281 ? 60.615  -10.549 21.782 1.00 20.09  ? 323  ILE B CG2   1 
ATOM   6067 C CD1   . ILE B 1 281 ? 58.903  -13.029 21.166 1.00 23.17  ? 323  ILE B CD1   1 
ATOM   6068 N N     . VAL B 1 282 ? 63.585  -11.936 23.634 1.00 14.87  ? 324  VAL B N     1 
ATOM   6069 C CA    . VAL B 1 282 ? 64.827  -11.275 24.028 1.00 15.60  ? 324  VAL B CA    1 
ATOM   6070 C C     . VAL B 1 282 ? 65.454  -12.123 25.107 1.00 16.09  ? 324  VAL B C     1 
ATOM   6071 O O     . VAL B 1 282 ? 64.763  -12.864 25.799 1.00 15.01  ? 324  VAL B O     1 
ATOM   6072 C CB    . VAL B 1 282 ? 64.639  -9.828  24.561 1.00 16.29  ? 324  VAL B CB    1 
ATOM   6073 C CG1   . VAL B 1 282 ? 64.114  -8.854  23.505 1.00 17.50  ? 324  VAL B CG1   1 
ATOM   6074 C CG2   . VAL B 1 282 ? 63.752  -9.813  25.804 1.00 17.67  ? 324  VAL B CG2   1 
ATOM   6075 N N     . PRO B 1 283 ? 66.784  -12.023 25.332 1.00 17.54  ? 325  PRO B N     1 
ATOM   6076 C CA    . PRO B 1 283 ? 67.407  -12.717 26.474 1.00 19.12  ? 325  PRO B CA    1 
ATOM   6077 C C     . PRO B 1 283 ? 66.946  -12.256 27.857 1.00 17.30  ? 325  PRO B C     1 
ATOM   6078 O O     . PRO B 1 283 ? 66.507  -11.119 28.072 1.00 16.49  ? 325  PRO B O     1 
ATOM   6079 C CB    . PRO B 1 283 ? 68.920  -12.501 26.287 1.00 20.46  ? 325  PRO B CB    1 
ATOM   6080 C CG    . PRO B 1 283 ? 69.069  -11.918 24.906 1.00 24.04  ? 325  PRO B CG    1 
ATOM   6081 C CD    . PRO B 1 283 ? 67.739  -11.303 24.487 1.00 18.68  ? 325  PRO B CD    1 
ATOM   6082 N N     . ASP B 1 284 ? 66.967  -13.210 28.795 1.00 17.64  ? 326  ASP B N     1 
ATOM   6083 C CA    . ASP B 1 284 ? 66.722  -12.902 30.177 1.00 21.62  ? 326  ASP B CA    1 
ATOM   6084 C C     . ASP B 1 284 ? 67.756  -11.861 30.546 1.00 25.25  ? 326  ASP B C     1 
ATOM   6085 O O     . ASP B 1 284 ? 68.895  -11.915 30.087 1.00 28.72  ? 326  ASP B O     1 
ATOM   6086 C CB    . ASP B 1 284 ? 66.875  -14.117 31.089 1.00 22.93  ? 326  ASP B CB    1 
ATOM   6087 C CG    . ASP B 1 284 ? 65.783  -15.154 30.951 1.00 23.02  ? 326  ASP B CG    1 
ATOM   6088 O OD1   . ASP B 1 284 ? 64.757  -14.883 30.272 1.00 20.84  ? 326  ASP B OD1   1 
ATOM   6089 O OD2   . ASP B 1 284 ? 66.024  -16.289 31.432 1.00 26.54  ? 326  ASP B OD2   1 
ATOM   6090 N N     . GLY B 1 285 ? 67.340  -10.875 31.300 1.00 24.76  ? 327  GLY B N     1 
ATOM   6091 C CA    . GLY B 1 285 ? 68.336  -9.866  31.633 1.00 25.73  ? 327  GLY B CA    1 
ATOM   6092 C C     . GLY B 1 285 ? 68.361  -8.683  30.675 1.00 22.87  ? 327  GLY B C     1 
ATOM   6093 O O     . GLY B 1 285 ? 68.903  -7.650  31.050 1.00 28.12  ? 327  GLY B O     1 
ATOM   6094 N N     . ALA B 1 286 ? 67.847  -8.820  29.451 1.00 19.30  ? 328  ALA B N     1 
ATOM   6095 C CA    . ALA B 1 286 ? 67.774  -7.716  28.516 1.00 18.14  ? 328  ALA B CA    1 
ATOM   6096 C C     . ALA B 1 286 ? 66.375  -7.095  28.594 1.00 18.95  ? 328  ALA B C     1 
ATOM   6097 O O     . ALA B 1 286 ? 65.405  -7.780  28.878 1.00 18.82  ? 328  ALA B O     1 
ATOM   6098 C CB    . ALA B 1 286 ? 68.072  -8.175  27.120 1.00 20.15  ? 328  ALA B CB    1 
ATOM   6099 N N     . PRO B 1 287 ? 66.231  -5.784  28.299 1.00 18.31  ? 329  PRO B N     1 
ATOM   6100 C CA    . PRO B 1 287 ? 64.914  -5.184  28.176 1.00 18.59  ? 329  PRO B CA    1 
ATOM   6101 C C     . PRO B 1 287 ? 64.127  -5.693  26.976 1.00 16.79  ? 329  PRO B C     1 
ATOM   6102 O O     . PRO B 1 287 ? 64.678  -6.163  25.967 1.00 16.73  ? 329  PRO B O     1 
ATOM   6103 C CB    . PRO B 1 287 ? 65.191  -3.673  28.015 1.00 19.20  ? 329  PRO B CB    1 
ATOM   6104 C CG    . PRO B 1 287 ? 66.620  -3.571  27.532 1.00 23.03  ? 329  PRO B CG    1 
ATOM   6105 C CD    . PRO B 1 287 ? 67.328  -4.840  27.983 1.00 21.54  ? 329  PRO B CD    1 
ATOM   6106 N N     . LEU B 1 288 ? 62.793  -5.561  27.075 1.00 16.12  ? 330  LEU B N     1 
ATOM   6107 C CA    . LEU B 1 288 ? 61.923  -5.894  25.968 1.00 17.57  ? 330  LEU B CA    1 
ATOM   6108 C C     . LEU B 1 288 ? 61.904  -4.679  25.054 1.00 18.64  ? 330  LEU B C     1 
ATOM   6109 O O     . LEU B 1 288 ? 60.982  -3.871  25.099 1.00 18.41  ? 330  LEU B O     1 
ATOM   6110 C CB    . LEU B 1 288 ? 60.524  -6.246  26.505 1.00 17.23  ? 330  LEU B CB    1 
ATOM   6111 C CG    . LEU B 1 288 ? 59.585  -6.939  25.526 1.00 18.63  ? 330  LEU B CG    1 
ATOM   6112 C CD1   . LEU B 1 288 ? 60.077  -8.345  25.173 1.00 19.26  ? 330  LEU B CD1   1 
ATOM   6113 C CD2   . LEU B 1 288 ? 58.191  -7.023  26.150 1.00 18.91  ? 330  LEU B CD2   1 
ATOM   6114 N N     . ASP B 1 289 ? 62.957  -4.527  24.248 1.00 18.67  ? 331  ASP B N     1 
ATOM   6115 C CA    . ASP B 1 289 ? 63.158  -3.289  23.489 1.00 20.53  ? 331  ASP B CA    1 
ATOM   6116 C C     . ASP B 1 289 ? 62.200  -3.210  22.304 1.00 20.96  ? 331  ASP B C     1 
ATOM   6117 O O     . ASP B 1 289 ? 61.764  -4.226  21.779 1.00 18.12  ? 331  ASP B O     1 
ATOM   6118 C CB    . ASP B 1 289 ? 64.608  -3.136  23.019 1.00 19.99  ? 331  ASP B CB    1 
ATOM   6119 C CG    . ASP B 1 289 ? 64.998  -4.184  22.007 1.00 22.32  ? 331  ASP B CG    1 
ATOM   6120 O OD1   . ASP B 1 289 ? 65.207  -5.344  22.407 1.00 22.44  ? 331  ASP B OD1   1 
ATOM   6121 O OD2   . ASP B 1 289 ? 64.967  -3.873  20.815 1.00 23.75  ? 331  ASP B OD2   1 
ATOM   6122 N N     . GLU B 1 290 ? 61.884  -1.977  21.869 1.00 21.00  ? 332  GLU B N     1 
ATOM   6123 C CA    . GLU B 1 290 ? 60.871  -1.788  20.840 1.00 22.07  ? 332  GLU B CA    1 
ATOM   6124 C C     . GLU B 1 290 ? 61.295  -2.379  19.499 1.00 20.53  ? 332  GLU B C     1 
ATOM   6125 O O     . GLU B 1 290 ? 60.443  -2.872  18.773 1.00 21.80  ? 332  GLU B O     1 
ATOM   6126 C CB    . GLU B 1 290 ? 60.472  -0.307  20.709 1.00 26.75  ? 332  GLU B CB    1 
ATOM   6127 C CG    . GLU B 1 290 ? 59.565  0.100   21.871 1.00 34.39  ? 332  GLU B CG    1 
ATOM   6128 C CD    . GLU B 1 290 ? 59.043  1.528   21.913 1.00 39.52  ? 332  GLU B CD    1 
ATOM   6129 O OE1   . GLU B 1 290 ? 59.197  2.248   20.906 1.00 37.12  ? 332  GLU B OE1   1 
ATOM   6130 O OE2   . GLU B 1 290 ? 58.543  1.914   22.987 1.00 45.91  ? 332  GLU B OE2   1 
ATOM   6131 N N     . ALA B 1 291 ? 62.587  -2.356  19.157 1.00 21.22  ? 333  ALA B N     1 
ATOM   6132 C CA    . ALA B 1 291 ? 63.009  -2.958  17.890 1.00 21.62  ? 333  ALA B CA    1 
ATOM   6133 C C     . ALA B 1 291 ? 62.780  -4.477  17.884 1.00 18.64  ? 333  ALA B C     1 
ATOM   6134 O O     . ALA B 1 291 ? 62.277  -5.001  16.887 1.00 20.00  ? 333  ALA B O     1 
ATOM   6135 C CB    . ALA B 1 291 ? 64.462  -2.637  17.580 1.00 23.07  ? 333  ALA B CB    1 
ATOM   6136 N N     . SER B 1 292 ? 63.083  -5.166  18.996 1.00 18.52  ? 334  SER B N     1 
ATOM   6137 C CA    . SER B 1 292 ? 62.841  -6.607  19.071 1.00 19.84  ? 334  SER B CA    1 
ATOM   6138 C C     . SER B 1 292 ? 61.339  -6.893  19.000 1.00 19.74  ? 334  SER B C     1 
ATOM   6139 O O     . SER B 1 292 ? 60.919  -7.874  18.404 1.00 17.46  ? 334  SER B O     1 
ATOM   6140 C CB    . SER B 1 292 ? 63.431  -7.231  20.301 1.00 19.44  ? 334  SER B CB    1 
ATOM   6141 O OG    . SER B 1 292 ? 64.826  -6.984  20.385 1.00 19.95  ? 334  SER B OG    1 
ATOM   6142 N N     . LEU B 1 293 ? 60.525  -6.049  19.673 1.00 17.67  ? 335  LEU B N     1 
ATOM   6143 C CA    . LEU B 1 293 ? 59.090  -6.260  19.646 1.00 18.97  ? 335  LEU B CA    1 
ATOM   6144 C C     . LEU B 1 293 ? 58.557  -6.068  18.249 1.00 18.26  ? 335  LEU B C     1 
ATOM   6145 O O     . LEU B 1 293 ? 57.723  -6.847  17.798 1.00 17.83  ? 335  LEU B O     1 
ATOM   6146 C CB    . LEU B 1 293 ? 58.372  -5.284  20.591 1.00 19.82  ? 335  LEU B CB    1 
ATOM   6147 C CG    . LEU B 1 293 ? 58.382  -5.675  22.048 1.00 21.70  ? 335  LEU B CG    1 
ATOM   6148 C CD1   . LEU B 1 293 ? 57.876  -4.526  22.891 1.00 22.56  ? 335  LEU B CD1   1 
ATOM   6149 C CD2   . LEU B 1 293 ? 57.511  -6.945  22.256 1.00 22.47  ? 335  LEU B CD2   1 
ATOM   6150 N N     . LYS B 1 294 ? 58.992  -4.981  17.580 1.00 18.92  ? 336  LYS B N     1 
ATOM   6151 C CA    . LYS B 1 294 ? 58.490  -4.677  16.247 1.00 21.09  ? 336  LYS B CA    1 
ATOM   6152 C C     . LYS B 1 294 ? 58.830  -5.801  15.267 1.00 19.00  ? 336  LYS B C     1 
ATOM   6153 O O     . LYS B 1 294 ? 58.024  -6.199  14.449 1.00 21.34  ? 336  LYS B O     1 
ATOM   6154 C CB    . LYS B 1 294 ? 59.082  -3.346  15.777 1.00 27.90  ? 336  LYS B CB    1 
ATOM   6155 C CG    . LYS B 1 294 ? 58.338  -2.648  14.648 1.00 36.86  ? 336  LYS B CG    1 
ATOM   6156 C CD    . LYS B 1 294 ? 58.765  -1.187  14.514 1.00 41.39  ? 336  LYS B CD    1 
ATOM   6157 C CE    . LYS B 1 294 ? 58.155  -0.516  13.306 1.00 47.26  ? 336  LYS B CE    1 
ATOM   6158 N NZ    . LYS B 1 294 ? 58.711  0.844   13.113 1.00 48.98  ? 336  LYS B NZ    1 
ATOM   6159 N N     . LYS B 1 295 ? 60.047  -6.330  15.351 1.00 19.53  ? 337  LYS B N     1 
ATOM   6160 C CA    . LYS B 1 295 ? 60.473  -7.410  14.460 1.00 20.95  ? 337  LYS B CA    1 
ATOM   6161 C C     . LYS B 1 295 ? 59.658  -8.689  14.671 1.00 18.50  ? 337  LYS B C     1 
ATOM   6162 O O     . LYS B 1 295 ? 59.190  -9.314  13.712 1.00 20.16  ? 337  LYS B O     1 
ATOM   6163 C CB    . LYS B 1 295 ? 61.956  -7.717  14.683 1.00 23.64  ? 337  LYS B CB    1 
ATOM   6164 C CG    . LYS B 1 295 ? 62.491  -8.933  13.939 1.00 28.41  ? 337  LYS B CG    1 
ATOM   6165 C CD    . LYS B 1 295 ? 63.989  -9.077  14.081 1.00 36.77  ? 337  LYS B CD    1 
ATOM   6166 C CE    . LYS B 1 295 ? 64.537  -10.365 13.506 1.00 43.04  ? 337  LYS B CE    1 
ATOM   6167 N NZ    . LYS B 1 295 ? 65.875  -10.627 14.091 1.00 47.92  ? 337  LYS B NZ    1 
ATOM   6168 N N     . ALA B 1 296 ? 59.413  -9.017  15.930 1.00 17.12  ? 338  ALA B N     1 
ATOM   6169 C CA    . ALA B 1 296 ? 58.665  -10.206 16.312 1.00 16.65  ? 338  ALA B CA    1 
ATOM   6170 C C     . ALA B 1 296 ? 57.185  -10.037 15.939 1.00 17.41  ? 338  ALA B C     1 
ATOM   6171 O O     . ALA B 1 296 ? 56.546  -10.947 15.395 1.00 17.65  ? 338  ALA B O     1 
ATOM   6172 C CB    . ALA B 1 296 ? 58.880  -10.468 17.781 1.00 16.23  ? 338  ALA B CB    1 
ATOM   6173 N N     . ALA B 1 297 ? 56.632  -8.838  16.178 1.00 16.94  ? 339  ALA B N     1 
ATOM   6174 C CA    . ALA B 1 297 ? 55.244  -8.577  15.835 1.00 18.09  ? 339  ALA B CA    1 
ATOM   6175 C C     . ALA B 1 297 ? 55.062  -8.636  14.306 1.00 18.65  ? 339  ALA B C     1 
ATOM   6176 O O     . ALA B 1 297 ? 54.145  -9.313  13.807 1.00 17.90  ? 339  ALA B O     1 
ATOM   6177 C CB    . ALA B 1 297 ? 54.831  -7.256  16.485 1.00 17.20  ? 339  ALA B CB    1 
ATOM   6178 N N     . SER B 1 298 ? 55.932  -7.933  13.559 1.00 19.41  ? 340  SER B N     1 
ATOM   6179 C CA    . SER B 1 298 ? 55.859  -7.948  12.093 1.00 21.00  ? 340  SER B CA    1 
ATOM   6180 C C     . SER B 1 298 ? 55.914  -9.350  11.481 1.00 19.53  ? 340  SER B C     1 
ATOM   6181 O O     . SER B 1 298 ? 55.189  -9.608  10.518 1.00 21.33  ? 340  SER B O     1 
ATOM   6182 C CB    . SER B 1 298 ? 56.903  -7.090  11.489 1.00 24.06  ? 340  SER B CB    1 
ATOM   6183 O OG    . SER B 1 298 ? 56.650  -5.734  11.806 1.00 27.99  ? 340  SER B OG    1 
ATOM   6184 N N     . ALA B 1 299 ? 56.749  -10.243 12.032 1.00 19.60  ? 341  ALA B N     1 
ATOM   6185 C CA    . ALA B 1 299 ? 56.869  -11.602 11.537 1.00 20.53  ? 341  ALA B CA    1 
ATOM   6186 C C     . ALA B 1 299 ? 55.587  -12.395 11.779 1.00 23.76  ? 341  ALA B C     1 
ATOM   6187 O O     . ALA B 1 299 ? 55.376  -13.433 11.168 1.00 24.25  ? 341  ALA B O     1 
ATOM   6188 C CB    . ALA B 1 299 ? 58.024  -12.293 12.191 1.00 20.43  ? 341  ALA B CB    1 
ATOM   6189 N N     . ASN B 1 300 ? 54.714  -11.862 12.655 1.00 21.89  ? 342  ASN B N     1 
ATOM   6190 C CA    . ASN B 1 300 ? 53.453  -12.474 12.999 1.00 21.58  ? 342  ASN B CA    1 
ATOM   6191 C C     . ASN B 1 300 ? 52.246  -11.705 12.455 1.00 21.32  ? 342  ASN B C     1 
ATOM   6192 O O     . ASN B 1 300 ? 51.125  -12.025 12.841 1.00 22.62  ? 342  ASN B O     1 
ATOM   6193 C CB    . ASN B 1 300 ? 53.407  -12.650 14.514 1.00 20.69  ? 342  ASN B CB    1 
ATOM   6194 C CG    . ASN B 1 300 ? 54.232  -13.853 14.932 1.00 21.66  ? 342  ASN B CG    1 
ATOM   6195 O OD1   . ASN B 1 300 ? 53.850  -14.982 14.647 1.00 24.06  ? 342  ASN B OD1   1 
ATOM   6196 N ND2   . ASN B 1 300 ? 55.391  -13.631 15.518 1.00 21.97  ? 342  ASN B ND2   1 
ATOM   6197 N N     . GLY B 1 301 ? 52.460  -10.695 11.597 1.00 20.51  ? 343  GLY B N     1 
ATOM   6198 C CA    . GLY B 1 301 ? 51.368  -9.915  11.043 1.00 19.54  ? 343  GLY B CA    1 
ATOM   6199 C C     . GLY B 1 301 ? 50.715  -8.933  12.030 1.00 19.73  ? 343  GLY B C     1 
ATOM   6200 O O     . GLY B 1 301 ? 49.597  -8.486  11.777 1.00 22.10  ? 343  GLY B O     1 
ATOM   6201 N N     . LEU B 1 302 ? 51.449  -8.576  13.077 1.00 17.97  ? 344  LEU B N     1 
ATOM   6202 C CA    . LEU B 1 302 ? 50.981  -7.633  14.090 1.00 17.69  ? 344  LEU B CA    1 
ATOM   6203 C C     . LEU B 1 302 ? 51.734  -6.318  14.011 1.00 18.76  ? 344  LEU B C     1 
ATOM   6204 O O     . LEU B 1 302 ? 52.927  -6.261  13.677 1.00 17.60  ? 344  LEU B O     1 
ATOM   6205 C CB    . LEU B 1 302 ? 51.204  -8.206  15.488 1.00 17.57  ? 344  LEU B CB    1 
ATOM   6206 C CG    . LEU B 1 302 ? 50.543  -9.549  15.737 1.00 18.35  ? 344  LEU B CG    1 
ATOM   6207 C CD1   . LEU B 1 302 ? 51.011  -10.104 17.065 1.00 16.87  ? 344  LEU B CD1   1 
ATOM   6208 C CD2   . LEU B 1 302 ? 49.012  -9.456  15.668 1.00 19.06  ? 344  LEU B CD2   1 
ATOM   6209 N N     . GLY B 1 303 ? 51.003  -5.250  14.341 1.00 15.25  ? 345  GLY B N     1 
ATOM   6210 C CA    . GLY B 1 303 ? 51.573  -3.936  14.535 1.00 15.17  ? 345  GLY B CA    1 
ATOM   6211 C C     . GLY B 1 303 ? 52.044  -3.826  15.978 1.00 15.47  ? 345  GLY B C     1 
ATOM   6212 O O     . GLY B 1 303 ? 51.944  -4.795  16.738 1.00 15.78  ? 345  GLY B O     1 
ATOM   6213 N N     . MET B 1 304 ? 52.469  -2.638  16.404 1.00 15.27  ? 346  MET B N     1 
ATOM   6214 C CA    . MET B 1 304 ? 52.824  -2.447  17.788 1.00 14.19  ? 346  MET B CA    1 
ATOM   6215 C C     . MET B 1 304 ? 51.560  -2.263  18.641 1.00 14.32  ? 346  MET B C     1 
ATOM   6216 O O     . MET B 1 304 ? 51.614  -2.540  19.846 1.00 14.47  ? 346  MET B O     1 
ATOM   6217 C CB    . MET B 1 304 ? 53.765  -1.240  17.931 1.00 17.28  ? 346  MET B CB    1 
ATOM   6218 C CG    . MET B 1 304 ? 55.189  -1.578  17.421 1.00 17.97  ? 346  MET B CG    1 
ATOM   6219 S SD    . MET B 1 304 ? 55.982  -2.815  18.502 1.00 21.07  ? 346  MET B SD    1 
ATOM   6220 C CE    . MET B 1 304 ? 56.406  -1.814  19.917 1.00 22.36  ? 346  MET B CE    1 
ATOM   6221 N N     . TRP B 1 305 ? 50.448  -1.845  18.016 1.00 13.81  ? 347  TRP B N     1 
ATOM   6222 C CA    . TRP B 1 305 ? 49.142  -1.811  18.652 1.00 13.54  ? 347  TRP B CA    1 
ATOM   6223 C C     . TRP B 1 305 ? 48.153  -2.406  17.661 1.00 14.64  ? 347  TRP B C     1 
ATOM   6224 O O     . TRP B 1 305 ? 48.187  -2.088  16.481 1.00 16.85  ? 347  TRP B O     1 
ATOM   6225 C CB    . TRP B 1 305 ? 48.729  -0.393  19.067 1.00 14.41  ? 347  TRP B CB    1 
ATOM   6226 C CG    . TRP B 1 305 ? 49.519  0.101   20.216 1.00 12.09  ? 347  TRP B CG    1 
ATOM   6227 C CD1   . TRP B 1 305 ? 50.575  0.941   20.142 1.00 13.20  ? 347  TRP B CD1   1 
ATOM   6228 C CD2   . TRP B 1 305 ? 49.244  -0.084  21.610 1.00 13.10  ? 347  TRP B CD2   1 
ATOM   6229 N NE1   . TRP B 1 305 ? 51.056  1.206   21.397 1.00 14.64  ? 347  TRP B NE1   1 
ATOM   6230 C CE2   . TRP B 1 305 ? 50.267  0.562   22.317 1.00 13.77  ? 347  TRP B CE2   1 
ATOM   6231 C CE3   . TRP B 1 305 ? 48.336  -0.852  22.317 1.00 13.31  ? 347  TRP B CE3   1 
ATOM   6232 C CZ2   . TRP B 1 305 ? 50.323  0.577   23.705 1.00 15.02  ? 347  TRP B CZ2   1 
ATOM   6233 C CZ3   . TRP B 1 305 ? 48.367  -0.794  23.688 1.00 13.39  ? 347  TRP B CZ3   1 
ATOM   6234 C CH2   . TRP B 1 305 ? 49.340  -0.104  24.370 1.00 15.15  ? 347  TRP B CH2   1 
ATOM   6235 N N     . ASN B 1 306 ? 47.260  -3.271  18.144 1.00 13.54  ? 348  ASN B N     1 
ATOM   6236 C CA    . ASN B 1 306 ? 46.349  -3.964  17.261 1.00 13.95  ? 348  ASN B CA    1 
ATOM   6237 C C     . ASN B 1 306 ? 44.968  -3.878  17.900 1.00 13.82  ? 348  ASN B C     1 
ATOM   6238 O O     . ASN B 1 306 ? 44.794  -4.356  19.033 1.00 13.94  ? 348  ASN B O     1 
ATOM   6239 C CB    . ASN B 1 306 ? 46.750  -5.418  17.021 1.00 14.72  ? 348  ASN B CB    1 
ATOM   6240 C CG    . ASN B 1 306 ? 48.130  -5.473  16.380 1.00 15.67  ? 348  ASN B CG    1 
ATOM   6241 O OD1   . ASN B 1 306 ? 48.272  -5.165  15.188 1.00 19.12  ? 348  ASN B OD1   1 
ATOM   6242 N ND2   . ASN B 1 306 ? 49.142  -5.594  17.207 1.00 15.89  ? 348  ASN B ND2   1 
ATOM   6243 N N     . THR B 1 307 ? 44.027  -3.222  17.197 1.00 13.64  ? 349  THR B N     1 
ATOM   6244 C CA    . THR B 1 307 ? 42.741  -2.878  17.812 1.00 13.09  ? 349  THR B CA    1 
ATOM   6245 C C     . THR B 1 307 ? 41.627  -3.626  17.075 1.00 14.19  ? 349  THR B C     1 
ATOM   6246 O O     . THR B 1 307 ? 41.564  -3.669  15.837 1.00 15.61  ? 349  THR B O     1 
ATOM   6247 C CB    . THR B 1 307 ? 42.531  -1.356  17.823 1.00 14.06  ? 349  THR B CB    1 
ATOM   6248 O OG1   . THR B 1 307 ? 43.630  -0.712  18.470 1.00 14.82  ? 349  THR B OG1   1 
ATOM   6249 C CG2   . THR B 1 307 ? 41.225  -0.971  18.498 1.00 14.62  ? 349  THR B CG2   1 
ATOM   6250 N N     . TYR B 1 308 ? 40.739  -4.261  17.841 1.00 14.09  ? 350  TYR B N     1 
ATOM   6251 C CA    . TYR B 1 308 ? 39.752  -5.164  17.289 1.00 14.13  ? 350  TYR B CA    1 
ATOM   6252 C C     . TYR B 1 308 ? 38.347  -4.598  17.499 1.00 13.32  ? 350  TYR B C     1 
ATOM   6253 O O     . TYR B 1 308 ? 37.953  -4.238  18.609 1.00 13.96  ? 350  TYR B O     1 
ATOM   6254 C CB    . TYR B 1 308 ? 39.934  -6.569  17.864 1.00 14.02  ? 350  TYR B CB    1 
ATOM   6255 C CG    . TYR B 1 308 ? 41.272  -7.147  17.574 1.00 13.73  ? 350  TYR B CG    1 
ATOM   6256 C CD1   . TYR B 1 308 ? 42.352  -6.859  18.379 1.00 13.18  ? 350  TYR B CD1   1 
ATOM   6257 C CD2   . TYR B 1 308 ? 41.456  -7.970  16.459 1.00 13.94  ? 350  TYR B CD2   1 
ATOM   6258 C CE1   . TYR B 1 308 ? 43.589  -7.379  18.123 1.00 14.73  ? 350  TYR B CE1   1 
ATOM   6259 C CE2   . TYR B 1 308 ? 42.716  -8.445  16.148 1.00 15.77  ? 350  TYR B CE2   1 
ATOM   6260 C CZ    . TYR B 1 308 ? 43.774  -8.188  17.005 1.00 14.21  ? 350  TYR B CZ    1 
ATOM   6261 O OH    . TYR B 1 308 ? 45.017  -8.674  16.722 1.00 15.90  ? 350  TYR B OH    1 
ATOM   6262 N N     . PHE B 1 309 ? 37.564  -4.553  16.409 1.00 15.08  ? 351  PHE B N     1 
ATOM   6263 C CA    . PHE B 1 309 ? 36.190  -4.056  16.454 1.00 14.72  ? 351  PHE B CA    1 
ATOM   6264 C C     . PHE B 1 309 ? 35.367  -4.895  15.498 1.00 14.53  ? 351  PHE B C     1 
ATOM   6265 O O     . PHE B 1 309 ? 35.904  -5.636  14.674 1.00 15.34  ? 351  PHE B O     1 
ATOM   6266 C CB    . PHE B 1 309 ? 36.107  -2.544  16.171 1.00 14.82  ? 351  PHE B CB    1 
ATOM   6267 C CG    . PHE B 1 309 ? 36.368  -2.139  14.741 1.00 17.22  ? 351  PHE B CG    1 
ATOM   6268 C CD1   . PHE B 1 309 ? 35.335  -2.102  13.825 1.00 17.86  ? 351  PHE B CD1   1 
ATOM   6269 C CD2   . PHE B 1 309 ? 37.634  -1.829  14.315 1.00 17.81  ? 351  PHE B CD2   1 
ATOM   6270 C CE1   . PHE B 1 309 ? 35.553  -1.761  12.501 1.00 20.22  ? 351  PHE B CE1   1 
ATOM   6271 C CE2   . PHE B 1 309 ? 37.854  -1.453  12.989 1.00 19.65  ? 351  PHE B CE2   1 
ATOM   6272 C CZ    . PHE B 1 309 ? 36.815  -1.414  12.098 1.00 18.75  ? 351  PHE B CZ    1 
ATOM   6273 N N     . ALA B 1 310 ? 34.040  -4.789  15.586 1.00 14.07  ? 352  ALA B N     1 
ATOM   6274 C CA    . ALA B 1 310 ? 33.199  -5.508  14.653 1.00 14.19  ? 352  ALA B CA    1 
ATOM   6275 C C     . ALA B 1 310 ? 31.963  -4.677  14.347 1.00 15.10  ? 352  ALA B C     1 
ATOM   6276 O O     . ALA B 1 310 ? 31.657  -3.745  15.095 1.00 16.40  ? 352  ALA B O     1 
ATOM   6277 C CB    . ALA B 1 310 ? 32.793  -6.831  15.231 1.00 15.49  ? 352  ALA B CB    1 
ATOM   6278 N N     . LEU B 1 311 ? 31.306  -5.070  13.235 1.00 16.56  ? 353  LEU B N     1 
ATOM   6279 C CA    . LEU B 1 311 ? 30.013  -4.529  12.821 1.00 18.00  ? 353  LEU B CA    1 
ATOM   6280 C C     . LEU B 1 311 ? 28.983  -5.648  12.775 1.00 17.15  ? 353  LEU B C     1 
ATOM   6281 O O     . LEU B 1 311 ? 29.304  -6.818  12.461 1.00 17.13  ? 353  LEU B O     1 
ATOM   6282 C CB    . LEU B 1 311 ? 30.173  -3.827  11.455 1.00 19.21  ? 353  LEU B CB    1 
ATOM   6283 C CG    . LEU B 1 311 ? 31.036  -2.576  11.491 1.00 20.86  ? 353  LEU B CG    1 
ATOM   6284 C CD1   . LEU B 1 311 ? 31.227  -1.965  10.099 1.00 20.95  ? 353  LEU B CD1   1 
ATOM   6285 C CD2   . LEU B 1 311 ? 30.517  -1.544  12.447 1.00 21.24  ? 353  LEU B CD2   1 
ATOM   6286 N N     . TYR B 1 312 ? 27.740  -5.266  13.149 1.00 16.67  ? 354  TYR B N     1 
ATOM   6287 C CA    . TYR B 1 312 ? 26.666  -6.211  13.345 1.00 16.68  ? 354  TYR B CA    1 
ATOM   6288 C C     . TYR B 1 312 ? 25.395  -5.662  12.687 1.00 17.56  ? 354  TYR B C     1 
ATOM   6289 O O     . TYR B 1 312 ? 25.098  -4.484  12.872 1.00 18.89  ? 354  TYR B O     1 
ATOM   6290 C CB    . TYR B 1 312 ? 26.371  -6.442  14.834 1.00 16.24  ? 354  TYR B CB    1 
ATOM   6291 C CG    . TYR B 1 312 ? 27.588  -6.721  15.688 1.00 15.72  ? 354  TYR B CG    1 
ATOM   6292 C CD1   . TYR B 1 312 ? 28.357  -5.677  16.154 1.00 14.50  ? 354  TYR B CD1   1 
ATOM   6293 C CD2   . TYR B 1 312 ? 27.963  -8.006  16.024 1.00 16.56  ? 354  TYR B CD2   1 
ATOM   6294 C CE1   . TYR B 1 312 ? 29.473  -5.928  16.933 1.00 13.65  ? 354  TYR B CE1   1 
ATOM   6295 C CE2   . TYR B 1 312 ? 29.075  -8.268  16.810 1.00 14.17  ? 354  TYR B CE2   1 
ATOM   6296 C CZ    . TYR B 1 312 ? 29.821  -7.219  17.283 1.00 12.82  ? 354  TYR B CZ    1 
ATOM   6297 O OH    . TYR B 1 312 ? 30.913  -7.434  18.103 1.00 12.89  ? 354  TYR B OH    1 
ATOM   6298 N N     . GLY B 1 313 ? 24.719  -6.512  11.923 1.00 19.50  ? 355  GLY B N     1 
ATOM   6299 C CA    . GLY B 1 313 ? 23.460  -6.136  11.274 1.00 20.72  ? 355  GLY B CA    1 
ATOM   6300 C C     . GLY B 1 313 ? 23.177  -6.909  9.984  1.00 20.12  ? 355  GLY B C     1 
ATOM   6301 O O     . GLY B 1 313 ? 23.163  -8.134  9.927  1.00 20.96  ? 355  GLY B O     1 
ATOM   6302 N N     . THR B 1 314 ? 22.966  -6.145  8.912  1.00 26.51  ? 356  THR B N     1 
ATOM   6303 C CA    . THR B 1 314 ? 22.855  -6.688  7.574  1.00 28.48  ? 356  THR B CA    1 
ATOM   6304 C C     . THR B 1 314 ? 23.986  -6.154  6.720  1.00 30.39  ? 356  THR B C     1 
ATOM   6305 O O     . THR B 1 314 ? 24.689  -5.220  7.122  1.00 26.80  ? 356  THR B O     1 
ATOM   6306 C CB    . THR B 1 314 ? 21.531  -6.263  6.926  1.00 30.18  ? 356  THR B CB    1 
ATOM   6307 O OG1   . THR B 1 314 ? 21.558  -4.837  6.768  1.00 29.05  ? 356  THR B OG1   1 
ATOM   6308 C CG2   . THR B 1 314 ? 20.327  -6.689  7.745  1.00 28.88  ? 356  THR B CG2   1 
ATOM   6309 N N     . GLU B 1 315 ? 24.062  -6.676  5.498  1.00 27.79  ? 357  GLU B N     1 
ATOM   6310 C CA    . GLU B 1 315 ? 25.083  -6.240  4.565  1.00 30.72  ? 357  GLU B CA    1 
ATOM   6311 C C     . GLU B 1 315 ? 24.905  -4.734  4.350  1.00 30.15  ? 357  GLU B C     1 
ATOM   6312 O O     . GLU B 1 315 ? 25.870  -3.980  4.263  1.00 27.45  ? 357  GLU B O     1 
ATOM   6313 C CB    . GLU B 1 315 ? 24.996  -7.101  3.300  1.00 36.40  ? 357  GLU B CB    1 
ATOM   6314 C CG    . GLU B 1 315 ? 25.176  -8.599  3.564  1.00 43.91  ? 357  GLU B CG    1 
ATOM   6315 C CD    . GLU B 1 315 ? 23.958  -9.460  3.936  1.00 54.95  ? 357  GLU B CD    1 
ATOM   6316 O OE1   . GLU B 1 315 ? 22.897  -8.932  4.431  1.00 45.25  ? 357  GLU B OE1   1 
ATOM   6317 O OE2   . GLU B 1 315 ? 24.049  -10.708 3.719  1.00 67.63  ? 357  GLU B OE2   1 
ATOM   6318 N N     . GLN B 1 316 ? 23.649  -4.267  4.376  1.00 29.23  ? 358  GLN B N     1 
ATOM   6319 C CA    . GLN B 1 316 ? 23.370  -2.869  4.091  1.00 32.02  ? 358  GLN B CA    1 
ATOM   6320 C C     . GLN B 1 316 ? 23.679  -1.957  5.287  1.00 28.73  ? 358  GLN B C     1 
ATOM   6321 O O     . GLN B 1 316 ? 24.248  -0.882  5.081  1.00 26.68  ? 358  GLN B O     1 
ATOM   6322 C CB    . GLN B 1 316 ? 21.952  -2.676  3.539  1.00 35.58  ? 358  GLN B CB    1 
ATOM   6323 C CG    . GLN B 1 316 ? 21.882  -1.463  2.620  1.00 39.87  ? 358  GLN B CG    1 
ATOM   6324 C CD    . GLN B 1 316 ? 20.523  -1.265  1.990  1.00 43.21  ? 358  GLN B CD    1 
ATOM   6325 O OE1   . GLN B 1 316 ? 19.970  -2.173  1.372  1.00 54.66  ? 358  GLN B OE1   1 
ATOM   6326 N NE2   . GLN B 1 316 ? 19.975  -0.071  2.134  1.00 40.92  ? 358  GLN B NE2   1 
ATOM   6327 N N     . THR B 1 317 ? 23.336  -2.357  6.528  1.00 27.84  ? 359  THR B N     1 
ATOM   6328 C CA    . THR B 1 317 ? 23.689  -1.547  7.693  1.00 27.62  ? 359  THR B CA    1 
ATOM   6329 C C     . THR B 1 317 ? 25.210  -1.481  7.856  1.00 23.80  ? 359  THR B C     1 
ATOM   6330 O O     . THR B 1 317 ? 25.740  -0.413  8.167  1.00 24.94  ? 359  THR B O     1 
ATOM   6331 C CB    . THR B 1 317 ? 23.018  -2.022  8.999  1.00 28.68  ? 359  THR B CB    1 
ATOM   6332 O OG1   . THR B 1 317 ? 23.551  -3.291  9.349  1.00 26.73  ? 359  THR B OG1   1 
ATOM   6333 C CG2   . THR B 1 317 ? 21.515  -2.106  8.866  1.00 30.94  ? 359  THR B CG2   1 
ATOM   6334 N N     . VAL B 1 318 ? 25.924  -2.580  7.592  1.00 24.44  ? 360  VAL B N     1 
ATOM   6335 C CA    . VAL B 1 318 ? 27.383  -2.586  7.685  1.00 23.87  ? 360  VAL B CA    1 
ATOM   6336 C C     . VAL B 1 318 ? 27.968  -1.597  6.662  1.00 24.12  ? 360  VAL B C     1 
ATOM   6337 O O     . VAL B 1 318 ? 28.792  -0.761  7.023  1.00 23.16  ? 360  VAL B O     1 
ATOM   6338 C CB    . VAL B 1 318 ? 27.937  -4.007  7.513  1.00 23.60  ? 360  VAL B CB    1 
ATOM   6339 C CG1   . VAL B 1 318 ? 29.452  -4.042  7.340  1.00 24.98  ? 360  VAL B CG1   1 
ATOM   6340 C CG2   . VAL B 1 318 ? 27.484  -4.906  8.668  1.00 26.54  ? 360  VAL B CG2   1 
ATOM   6341 N N     . ALA B 1 319 ? 27.496  -1.659  5.399  1.00 25.68  ? 361  ALA B N     1 
ATOM   6342 C CA    . ALA B 1 319 ? 27.944  -0.751  4.345  1.00 24.80  ? 361  ALA B CA    1 
ATOM   6343 C C     . ALA B 1 319 ? 27.661  0.723   4.656  1.00 25.16  ? 361  ALA B C     1 
ATOM   6344 O O     . ALA B 1 319 ? 28.361  1.598   4.152  1.00 30.21  ? 361  ALA B O     1 
ATOM   6345 C CB    . ALA B 1 319 ? 27.331  -1.146  3.028  1.00 25.13  ? 361  ALA B CB    1 
ATOM   6346 N N     . GLY B 1 320 ? 26.644  1.009   5.487  1.00 22.33  ? 362  GLY B N     1 
ATOM   6347 C CA    . GLY B 1 320 ? 26.345  2.360   5.917  1.00 24.54  ? 362  GLY B CA    1 
ATOM   6348 C C     . GLY B 1 320 ? 27.450  3.016   6.747  1.00 24.87  ? 362  GLY B C     1 
ATOM   6349 O O     . GLY B 1 320 ? 27.532  4.240   6.776  1.00 26.21  ? 362  GLY B O     1 
ATOM   6350 N N     . VAL B 1 321 ? 28.279  2.230   7.466  1.00 24.55  ? 363  VAL B N     1 
ATOM   6351 C CA    . VAL B 1 321 ? 29.209  2.841   8.400  1.00 22.68  ? 363  VAL B CA    1 
ATOM   6352 C C     . VAL B 1 321 ? 30.667  2.482   8.085  1.00 19.07  ? 363  VAL B C     1 
ATOM   6353 O O     . VAL B 1 321 ? 31.570  3.235   8.462  1.00 20.56  ? 363  VAL B O     1 
ATOM   6354 C CB    . VAL B 1 321 ? 28.819  2.524   9.853  1.00 21.97  ? 363  VAL B CB    1 
ATOM   6355 C CG1   . VAL B 1 321 ? 27.500  3.183   10.224 1.00 24.61  ? 363  VAL B CG1   1 
ATOM   6356 C CG2   . VAL B 1 321 ? 28.791  1.038   10.128 1.00 22.49  ? 363  VAL B CG2   1 
ATOM   6357 N N     . GLU B 1 322 ? 30.892  1.401   7.351  1.00 20.81  ? 364  GLU B N     1 
ATOM   6358 C CA    . GLU B 1 322 ? 32.234  0.883   7.154  1.00 22.29  ? 364  GLU B CA    1 
ATOM   6359 C C     . GLU B 1 322 ? 33.098  1.917   6.446  1.00 25.00  ? 364  GLU B C     1 
ATOM   6360 O O     . GLU B 1 322 ? 34.257  2.083   6.811  1.00 19.86  ? 364  GLU B O     1 
ATOM   6361 C CB    . GLU B 1 322 ? 32.222  -0.433  6.396  1.00 21.72  ? 364  GLU B CB    1 
ATOM   6362 C CG    . GLU B 1 322 ? 33.589  -1.007  6.137  1.00 22.02  ? 364  GLU B CG    1 
ATOM   6363 C CD    . GLU B 1 322 ? 33.607  -2.383  5.506  1.00 22.37  ? 364  GLU B CD    1 
ATOM   6364 O OE1   . GLU B 1 322 ? 32.594  -3.107  5.544  1.00 22.21  ? 364  GLU B OE1   1 
ATOM   6365 O OE2   . GLU B 1 322 ? 34.690  -2.755  4.995  1.00 24.83  ? 364  GLU B OE2   1 
ATOM   6366 N N     . PRO B 1 323 ? 32.625  2.620   5.390  1.00 24.65  ? 365  PRO B N     1 
ATOM   6367 C CA    . PRO B 1 323 ? 33.490  3.617   4.755  1.00 24.04  ? 365  PRO B CA    1 
ATOM   6368 C C     . PRO B 1 323 ? 33.998  4.728   5.672  1.00 22.87  ? 365  PRO B C     1 
ATOM   6369 O O     . PRO B 1 323 ? 35.170  5.107   5.586  1.00 22.46  ? 365  PRO B O     1 
ATOM   6370 C CB    . PRO B 1 323 ? 32.589  4.190   3.628  1.00 24.65  ? 365  PRO B CB    1 
ATOM   6371 C CG    . PRO B 1 323 ? 31.640  3.041   3.316  1.00 26.01  ? 365  PRO B CG    1 
ATOM   6372 C CD    . PRO B 1 323 ? 31.331  2.441   4.686  1.00 25.26  ? 365  PRO B CD    1 
ATOM   6373 N N     . ILE B 1 324 ? 33.122  5.284   6.528  1.00 21.16  ? 366  ILE B N     1 
ATOM   6374 C CA    . ILE B 1 324 ? 33.502  6.321   7.462  1.00 22.15  ? 366  ILE B CA    1 
ATOM   6375 C C     . ILE B 1 324 ? 34.494  5.768   8.478  1.00 21.48  ? 366  ILE B C     1 
ATOM   6376 O O     . ILE B 1 324 ? 35.410  6.466   8.876  1.00 19.64  ? 366  ILE B O     1 
ATOM   6377 C CB    . ILE B 1 324 ? 32.276  6.924   8.170  1.00 26.92  ? 366  ILE B CB    1 
ATOM   6378 C CG1   . ILE B 1 324 ? 31.377  7.661   7.171  1.00 31.64  ? 366  ILE B CG1   1 
ATOM   6379 C CG2   . ILE B 1 324 ? 32.711  7.845   9.298  1.00 28.81  ? 366  ILE B CG2   1 
ATOM   6380 C CD1   . ILE B 1 324 ? 30.111  8.228   7.787  1.00 33.60  ? 366  ILE B CD1   1 
ATOM   6381 N N     . ILE B 1 325 ? 34.254  4.536   8.943  1.00 20.13  ? 367  ILE B N     1 
ATOM   6382 C CA    . ILE B 1 325 ? 35.142  3.946   9.937  1.00 19.23  ? 367  ILE B CA    1 
ATOM   6383 C C     . ILE B 1 325 ? 36.524  3.784   9.315  1.00 18.66  ? 367  ILE B C     1 
ATOM   6384 O O     . ILE B 1 325 ? 37.521  4.169   9.909  1.00 18.11  ? 367  ILE B O     1 
ATOM   6385 C CB    . ILE B 1 325 ? 34.562  2.623   10.472 1.00 19.62  ? 367  ILE B CB    1 
ATOM   6386 C CG1   . ILE B 1 325 ? 33.327  2.871   11.351 1.00 19.89  ? 367  ILE B CG1   1 
ATOM   6387 C CG2   . ILE B 1 325 ? 35.595  1.814   11.234 1.00 21.01  ? 367  ILE B CG2   1 
ATOM   6388 C CD1   . ILE B 1 325 ? 32.426  1.656   11.472 1.00 19.36  ? 367  ILE B CD1   1 
ATOM   6389 N N     . ARG B 1 326 ? 36.567  3.191   8.128  1.00 18.31  ? 368  ARG B N     1 
ATOM   6390 C CA    . ARG B 1 326 ? 37.832  3.019   7.421  1.00 21.17  ? 368  ARG B CA    1 
ATOM   6391 C C     . ARG B 1 326 ? 38.549  4.361   7.223  1.00 23.19  ? 368  ARG B C     1 
ATOM   6392 O O     . ARG B 1 326 ? 39.754  4.468   7.468  1.00 21.43  ? 368  ARG B O     1 
ATOM   6393 C CB    . ARG B 1 326 ? 37.630  2.279   6.108  1.00 18.76  ? 368  ARG B CB    1 
ATOM   6394 C CG    . ARG B 1 326 ? 37.363  0.795   6.252  1.00 21.43  ? 368  ARG B CG    1 
ATOM   6395 C CD    . ARG B 1 326 ? 37.286  0.195   4.864  1.00 22.81  ? 368  ARG B CD    1 
ATOM   6396 N NE    . ARG B 1 326 ? 37.108  -1.233  4.934  1.00 20.66  ? 368  ARG B NE    1 
ATOM   6397 C CZ    . ARG B 1 326 ? 38.071  -2.140  4.912  1.00 21.62  ? 368  ARG B CZ    1 
ATOM   6398 N NH1   . ARG B 1 326 ? 39.332  -1.783  4.857  1.00 21.35  ? 368  ARG B NH1   1 
ATOM   6399 N NH2   . ARG B 1 326 ? 37.748  -3.419  4.954  1.00 23.77  ? 368  ARG B NH2   1 
ATOM   6400 N N     . ALA B 1 327 ? 37.842  5.404   6.763  1.00 22.69  ? 369  ALA B N     1 
ATOM   6401 C CA    . ALA B 1 327 ? 38.509  6.683   6.548  1.00 23.33  ? 369  ALA B CA    1 
ATOM   6402 C C     . ALA B 1 327 ? 39.113  7.281   7.829  1.00 22.56  ? 369  ALA B C     1 
ATOM   6403 O O     . ALA B 1 327 ? 40.237  7.798   7.797  1.00 23.24  ? 369  ALA B O     1 
ATOM   6404 C CB    . ALA B 1 327 ? 37.540  7.630   5.846  1.00 24.17  ? 369  ALA B CB    1 
ATOM   6405 N N     . THR B 1 328 ? 38.360  7.253   8.950  1.00 21.03  ? 370  THR B N     1 
ATOM   6406 C CA    . THR B 1 328 ? 38.776  7.772   10.238 1.00 21.84  ? 370  THR B CA    1 
ATOM   6407 C C     . THR B 1 328 ? 40.027  7.011   10.683 1.00 21.54  ? 370  THR B C     1 
ATOM   6408 O O     . THR B 1 328 ? 41.004  7.613   11.105 1.00 20.38  ? 370  THR B O     1 
ATOM   6409 C CB    . THR B 1 328 ? 37.631  7.669   11.270 1.00 23.56  ? 370  THR B CB    1 
ATOM   6410 O OG1   . THR B 1 328 ? 36.482  8.388   10.812 1.00 27.21  ? 370  THR B OG1   1 
ATOM   6411 C CG2   . THR B 1 328 ? 37.960  8.242   12.625 1.00 24.56  ? 370  THR B CG2   1 
ATOM   6412 N N     . LEU B 1 329 ? 40.003  5.685   10.572 1.00 19.54  ? 371  LEU B N     1 
ATOM   6413 C CA    . LEU B 1 329 ? 41.107  4.911   11.139 1.00 18.48  ? 371  LEU B CA    1 
ATOM   6414 C C     . LEU B 1 329 ? 42.361  4.973   10.244 1.00 18.82  ? 371  LEU B C     1 
ATOM   6415 O O     . LEU B 1 329 ? 43.482  5.037   10.747 1.00 19.51  ? 371  LEU B O     1 
ATOM   6416 C CB    . LEU B 1 329 ? 40.643  3.475   11.384 1.00 18.41  ? 371  LEU B CB    1 
ATOM   6417 C CG    . LEU B 1 329 ? 39.677  3.329   12.553 1.00 20.64  ? 371  LEU B CG    1 
ATOM   6418 C CD1   . LEU B 1 329 ? 39.092  1.936   12.555 1.00 20.64  ? 371  LEU B CD1   1 
ATOM   6419 C CD2   . LEU B 1 329 ? 40.392  3.629   13.850 1.00 23.44  ? 371  LEU B CD2   1 
ATOM   6420 N N     . THR B 1 330 ? 42.194  5.000   8.907  1.00 19.59  ? 372  THR B N     1 
ATOM   6421 C CA    . THR B 1 330 ? 43.324  5.121   8.000  1.00 21.73  ? 372  THR B CA    1 
ATOM   6422 C C     . THR B 1 330 ? 44.015  6.471   8.207  1.00 23.53  ? 372  THR B C     1 
ATOM   6423 O O     . THR B 1 330 ? 45.252  6.526   8.204  1.00 21.59  ? 372  THR B O     1 
ATOM   6424 C CB    . THR B 1 330 ? 42.915  4.848   6.543  1.00 22.42  ? 372  THR B CB    1 
ATOM   6425 O OG1   . THR B 1 330 ? 42.377  3.522   6.404  1.00 24.00  ? 372  THR B OG1   1 
ATOM   6426 C CG2   . THR B 1 330 ? 44.090  4.889   5.586  1.00 27.39  ? 372  THR B CG2   1 
ATOM   6427 N N     . ALA B 1 331 ? 43.233  7.531   8.439  1.00 21.51  ? 373  ALA B N     1 
ATOM   6428 C CA    . ALA B 1 331 ? 43.791  8.861   8.640  1.00 21.96  ? 373  ALA B CA    1 
ATOM   6429 C C     . ALA B 1 331 ? 44.659  8.884   9.893  1.00 21.84  ? 373  ALA B C     1 
ATOM   6430 O O     . ALA B 1 331 ? 45.586  9.676   9.987  1.00 22.57  ? 373  ALA B O     1 
ATOM   6431 C CB    . ALA B 1 331 ? 42.705  9.901   8.685  1.00 23.46  ? 373  ALA B CB    1 
ATOM   6432 N N     . SER B 1 332 ? 44.404  7.960   10.840 1.00 20.73  ? 374  SER B N     1 
ATOM   6433 C CA    . SER B 1 332 ? 45.164  7.885   12.061 1.00 21.04  ? 374  SER B CA    1 
ATOM   6434 C C     . SER B 1 332 ? 46.421  7.020   11.927 1.00 20.70  ? 374  SER B C     1 
ATOM   6435 O O     . SER B 1 332 ? 47.088  6.805   12.924 1.00 20.76  ? 374  SER B O     1 
ATOM   6436 C CB    . SER B 1 332 ? 44.311  7.361   13.199 1.00 22.38  ? 374  SER B CB    1 
ATOM   6437 O OG    . SER B 1 332 ? 44.188  5.945   13.147 1.00 17.30  ? 374  SER B OG    1 
ATOM   6438 N N     . GLY B 1 333 ? 46.715  6.524   10.720 1.00 20.92  ? 375  GLY B N     1 
ATOM   6439 C CA    . GLY B 1 333 ? 47.874  5.681   10.489 1.00 20.82  ? 375  GLY B CA    1 
ATOM   6440 C C     . GLY B 1 333 ? 47.587  4.202   10.660 1.00 21.33  ? 375  GLY B C     1 
ATOM   6441 O O     . GLY B 1 333 ? 48.512  3.398   10.791 1.00 21.25  ? 375  GLY B O     1 
ATOM   6442 N N     . GLY B 1 334 ? 46.303  3.843   10.698 1.00 18.79  ? 376  GLY B N     1 
ATOM   6443 C CA    . GLY B 1 334 ? 45.940  2.444   10.905 1.00 20.86  ? 376  GLY B CA    1 
ATOM   6444 C C     . GLY B 1 334 ? 45.705  1.750   9.568  1.00 22.03  ? 376  GLY B C     1 
ATOM   6445 O O     . GLY B 1 334 ? 45.217  2.355   8.613  1.00 24.39  ? 376  GLY B O     1 
ATOM   6446 N N     . GLU B 1 335 ? 45.972  0.460   9.524  1.00 19.49  ? 377  GLU B N     1 
ATOM   6447 C CA    . GLU B 1 335 ? 45.637  -0.353  8.388  1.00 19.89  ? 377  GLU B CA    1 
ATOM   6448 C C     . GLU B 1 335 ? 44.460  -1.225  8.819  1.00 19.47  ? 377  GLU B C     1 
ATOM   6449 O O     . GLU B 1 335 ? 44.600  -2.016  9.756  1.00 20.00  ? 377  GLU B O     1 
ATOM   6450 C CB    . GLU B 1 335 ? 46.851  -1.185  7.965  1.00 25.04  ? 377  GLU B CB    1 
ATOM   6451 C CG    . GLU B 1 335 ? 46.567  -2.031  6.736  1.00 28.22  ? 377  GLU B CG    1 
ATOM   6452 C CD    . GLU B 1 335 ? 47.757  -2.784  6.165  1.00 33.86  ? 377  GLU B CD    1 
ATOM   6453 O OE1   . GLU B 1 335 ? 48.767  -2.927  6.873  1.00 34.66  ? 377  GLU B OE1   1 
ATOM   6454 O OE2   . GLU B 1 335 ? 47.633  -3.250  5.021  1.00 43.04  ? 377  GLU B OE2   1 
ATOM   6455 N N     . VAL B 1 336 ? 43.304  -1.058  8.174  1.00 18.45  ? 378  VAL B N     1 
ATOM   6456 C CA    . VAL B 1 336 ? 42.118  -1.824  8.541  1.00 18.38  ? 378  VAL B CA    1 
ATOM   6457 C C     . VAL B 1 336 ? 42.030  -3.134  7.756  1.00 20.55  ? 378  VAL B C     1 
ATOM   6458 O O     . VAL B 1 336 ? 42.015  -3.132  6.523  1.00 20.51  ? 378  VAL B O     1 
ATOM   6459 C CB    . VAL B 1 336 ? 40.881  -0.940  8.327  1.00 18.58  ? 378  VAL B CB    1 
ATOM   6460 C CG1   . VAL B 1 336 ? 39.580  -1.661  8.643  1.00 20.57  ? 378  VAL B CG1   1 
ATOM   6461 C CG2   . VAL B 1 336 ? 41.025  0.355   9.093  1.00 18.75  ? 378  VAL B CG2   1 
ATOM   6462 N N     . LEU B 1 337 ? 41.951  -4.262  8.473  1.00 17.50  ? 379  LEU B N     1 
ATOM   6463 C CA    . LEU B 1 337 ? 42.010  -5.594  7.892  1.00 18.55  ? 379  LEU B CA    1 
ATOM   6464 C C     . LEU B 1 337 ? 40.785  -6.420  8.295  1.00 19.75  ? 379  LEU B C     1 
ATOM   6465 O O     . LEU B 1 337 ? 40.219  -6.243  9.371  1.00 20.23  ? 379  LEU B O     1 
ATOM   6466 C CB    . LEU B 1 337 ? 43.308  -6.284  8.333  1.00 18.42  ? 379  LEU B CB    1 
ATOM   6467 C CG    . LEU B 1 337 ? 44.591  -5.508  8.012  1.00 24.17  ? 379  LEU B CG    1 
ATOM   6468 C CD1   . LEU B 1 337 ? 45.682  -5.754  9.037  1.00 26.56  ? 379  LEU B CD1   1 
ATOM   6469 C CD2   . LEU B 1 337 ? 45.092  -5.861  6.628  1.00 27.88  ? 379  LEU B CD2   1 
ATOM   6470 N N     . THR B 1 338 ? 40.401  -7.345  7.406  1.00 20.46  ? 380  THR B N     1 
ATOM   6471 C CA    . THR B 1 338 ? 39.256  -8.230  7.545  1.00 19.32  ? 380  THR B CA    1 
ATOM   6472 C C     . THR B 1 338 ? 39.719  -9.676  7.488  1.00 18.34  ? 380  THR B C     1 
ATOM   6473 O O     . THR B 1 338 ? 40.900  -9.928  7.358  1.00 20.42  ? 380  THR B O     1 
ATOM   6474 C CB    . THR B 1 338 ? 38.173  -7.906  6.499  1.00 26.17  ? 380  THR B CB    1 
ATOM   6475 O OG1   . THR B 1 338 ? 38.658  -8.237  5.195  1.00 25.35  ? 380  THR B OG1   1 
ATOM   6476 C CG2   . THR B 1 338 ? 37.778  -6.445  6.544  1.00 29.13  ? 380  THR B CG2   1 
ATOM   6477 N N     . ALA B 1 339 ? 38.789  -10.613 7.681  1.00 19.92  ? 381  ALA B N     1 
ATOM   6478 C CA    . ALA B 1 339 ? 39.107  -12.036 7.800  1.00 22.07  ? 381  ALA B CA    1 
ATOM   6479 C C     . ALA B 1 339 ? 39.852  -12.534 6.581  1.00 27.27  ? 381  ALA B C     1 
ATOM   6480 O O     . ALA B 1 339 ? 40.750  -13.349 6.721  1.00 28.03  ? 381  ALA B O     1 
ATOM   6481 C CB    . ALA B 1 339 ? 37.874  -12.840 8.004  1.00 24.25  ? 381  ALA B CB    1 
ATOM   6482 N N     . ALA B 1 340 ? 39.502  -11.980 5.409  1.00 29.95  ? 382  ALA B N     1 
ATOM   6483 C CA    . ALA B 1 340 ? 40.070  -12.428 4.145  1.00 33.29  ? 382  ALA B CA    1 
ATOM   6484 C C     . ALA B 1 340 ? 41.563  -12.133 4.061  1.00 31.83  ? 382  ALA B C     1 
ATOM   6485 O O     . ALA B 1 340 ? 42.278  -12.814 3.334  1.00 32.56  ? 382  ALA B O     1 
ATOM   6486 C CB    . ALA B 1 340 ? 39.340  -11.760 3.008  1.00 37.85  ? 382  ALA B CB    1 
ATOM   6487 N N     . GLU B 1 341 ? 42.027  -11.101 4.770  1.00 28.72  ? 383  GLU B N     1 
ATOM   6488 C CA    . GLU B 1 341 ? 43.426  -10.742 4.812  1.00 27.22  ? 383  GLU B CA    1 
ATOM   6489 C C     . GLU B 1 341 ? 44.132  -11.403 5.982  1.00 27.77  ? 383  GLU B C     1 
ATOM   6490 O O     . GLU B 1 341 ? 45.345  -11.356 6.032  1.00 35.11  ? 383  GLU B O     1 
ATOM   6491 C CB    . GLU B 1 341 ? 43.661  -9.242  5.021  1.00 31.02  ? 383  GLU B CB    1 
ATOM   6492 C CG    . GLU B 1 341 ? 43.391  -8.384  3.812  1.00 33.67  ? 383  GLU B CG    1 
ATOM   6493 C CD    . GLU B 1 341 ? 42.001  -7.805  3.743  1.00 41.23  ? 383  GLU B CD    1 
ATOM   6494 O OE1   . GLU B 1 341 ? 41.605  -7.044  4.691  1.00 34.62  ? 383  GLU B OE1   1 
ATOM   6495 O OE2   . GLU B 1 341 ? 41.315  -8.115  2.740  1.00 49.27  ? 383  GLU B OE2   1 
ATOM   6496 N N     . MET B 1 342 ? 43.404  -11.939 6.964  1.00 27.15  ? 384  MET B N     1 
ATOM   6497 C CA    . MET B 1 342 ? 44.080  -12.370 8.180  1.00 26.37  ? 384  MET B CA    1 
ATOM   6498 C C     . MET B 1 342 ? 43.970  -13.887 8.334  1.00 30.36  ? 384  MET B C     1 
ATOM   6499 O O     . MET B 1 342 ? 44.073  -14.426 9.433  1.00 26.71  ? 384  MET B O     1 
ATOM   6500 C CB    . MET B 1 342 ? 43.502  -11.596 9.362  1.00 26.87  ? 384  MET B CB    1 
ATOM   6501 C CG    . MET B 1 342 ? 43.846  -10.130 9.291  1.00 31.14  ? 384  MET B CG    1 
ATOM   6502 S SD    . MET B 1 342 ? 45.623  -9.815  8.969  1.00 42.47  ? 384  MET B SD    1 
ATOM   6503 C CE    . MET B 1 342 ? 46.244  -10.491 10.504 1.00 26.04  ? 384  MET B CE    1 
ATOM   6504 N N     . GLU B 1 343 ? 43.884  -14.610 7.198  1.00 32.21  ? 385  GLU B N     1 
ATOM   6505 C CA    . GLU B 1 343 ? 43.700  -16.053 7.255  1.00 34.63  ? 385  GLU B CA    1 
ATOM   6506 C C     . GLU B 1 343 ? 44.914  -16.682 7.904  1.00 33.10  ? 385  GLU B C     1 
ATOM   6507 O O     . GLU B 1 343 ? 46.052  -16.348 7.565  1.00 36.49  ? 385  GLU B O     1 
ATOM   6508 C CB    . GLU B 1 343 ? 43.502  -16.684 5.879  1.00 41.75  ? 385  GLU B CB    1 
ATOM   6509 C CG    . GLU B 1 343 ? 42.181  -16.271 5.266  1.00 46.18  ? 385  GLU B CG    1 
ATOM   6510 C CD    . GLU B 1 343 ? 41.705  -17.164 4.142  1.00 55.52  ? 385  GLU B CD    1 
ATOM   6511 O OE1   . GLU B 1 343 ? 42.538  -17.942 3.621  1.00 58.19  ? 385  GLU B OE1   1 
ATOM   6512 O OE2   . GLU B 1 343 ? 40.496  -17.102 3.824  1.00 60.29  ? 385  GLU B OE2   1 
ATOM   6513 N N     . GLY B 1 344 ? 44.647  -17.531 8.890  1.00 29.19  ? 386  GLY B N     1 
ATOM   6514 C CA    . GLY B 1 344 ? 45.710  -18.213 9.600  1.00 31.70  ? 386  GLY B CA    1 
ATOM   6515 C C     . GLY B 1 344 ? 46.343  -17.369 10.702 1.00 29.61  ? 386  GLY B C     1 
ATOM   6516 O O     . GLY B 1 344 ? 47.213  -17.848 11.428 1.00 30.04  ? 386  GLY B O     1 
ATOM   6517 N N     . ASN B 1 345 ? 45.897  -16.117 10.868 1.00 22.05  ? 387  ASN B N     1 
ATOM   6518 C CA    . ASN B 1 345 ? 46.487  -15.334 11.942 1.00 19.70  ? 387  ASN B CA    1 
ATOM   6519 C C     . ASN B 1 345 ? 45.787  -15.666 13.254 1.00 18.59  ? 387  ASN B C     1 
ATOM   6520 O O     . ASN B 1 345 ? 44.603  -15.411 13.368 1.00 18.37  ? 387  ASN B O     1 
ATOM   6521 C CB    . ASN B 1 345 ? 46.374  -13.838 11.659 1.00 19.64  ? 387  ASN B CB    1 
ATOM   6522 C CG    . ASN B 1 345 ? 47.084  -13.030 12.719 1.00 21.96  ? 387  ASN B CG    1 
ATOM   6523 O OD1   . ASN B 1 345 ? 46.602  -12.877 13.835 1.00 19.70  ? 387  ASN B OD1   1 
ATOM   6524 N ND2   . ASN B 1 345 ? 48.229  -12.470 12.371 1.00 23.20  ? 387  ASN B ND2   1 
ATOM   6525 N N     . PRO B 1 346 ? 46.470  -16.247 14.265 1.00 18.48  ? 388  PRO B N     1 
ATOM   6526 C CA    . PRO B 1 346 ? 45.783  -16.760 15.458 1.00 17.52  ? 388  PRO B CA    1 
ATOM   6527 C C     . PRO B 1 346 ? 45.216  -15.646 16.337 1.00 17.67  ? 388  PRO B C     1 
ATOM   6528 O O     . PRO B 1 346 ? 44.268  -15.914 17.064 1.00 17.17  ? 388  PRO B O     1 
ATOM   6529 C CB    . PRO B 1 346 ? 46.845  -17.522 16.250 1.00 18.95  ? 388  PRO B CB    1 
ATOM   6530 C CG    . PRO B 1 346 ? 48.140  -16.866 15.806 1.00 19.96  ? 388  PRO B CG    1 
ATOM   6531 C CD    . PRO B 1 346 ? 47.917  -16.534 14.334 1.00 20.30  ? 388  PRO B CD    1 
ATOM   6532 N N     . TRP B 1 347 ? 45.800  -14.446 16.280 1.00 16.36  ? 389  TRP B N     1 
ATOM   6533 C CA    . TRP B 1 347 ? 45.276  -13.338 17.049 1.00 16.16  ? 389  TRP B CA    1 
ATOM   6534 C C     . TRP B 1 347 ? 43.969  -12.865 16.436 1.00 17.08  ? 389  TRP B C     1 
ATOM   6535 O O     . TRP B 1 347 ? 43.022  -12.590 17.168 1.00 17.18  ? 389  TRP B O     1 
ATOM   6536 C CB    . TRP B 1 347 ? 46.288  -12.198 17.194 1.00 16.44  ? 389  TRP B CB    1 
ATOM   6537 C CG    . TRP B 1 347 ? 47.533  -12.579 17.938 1.00 17.00  ? 389  TRP B CG    1 
ATOM   6538 C CD1   . TRP B 1 347 ? 47.667  -12.546 19.291 1.00 15.76  ? 389  TRP B CD1   1 
ATOM   6539 C CD2   . TRP B 1 347 ? 48.731  -13.215 17.442 1.00 16.57  ? 389  TRP B CD2   1 
ATOM   6540 N NE1   . TRP B 1 347 ? 48.870  -13.030 19.669 1.00 16.13  ? 389  TRP B NE1   1 
ATOM   6541 C CE2   . TRP B 1 347 ? 49.570  -13.411 18.557 1.00 17.01  ? 389  TRP B CE2   1 
ATOM   6542 C CE3   . TRP B 1 347 ? 49.216  -13.573 16.180 1.00 17.93  ? 389  TRP B CE3   1 
ATOM   6543 C CZ2   . TRP B 1 347 ? 50.841  -13.976 18.459 1.00 18.32  ? 389  TRP B CZ2   1 
ATOM   6544 C CZ3   . TRP B 1 347 ? 50.473  -14.136 16.073 1.00 18.65  ? 389  TRP B CZ3   1 
ATOM   6545 C CH2   . TRP B 1 347 ? 51.275  -14.346 17.196 1.00 19.60  ? 389  TRP B CH2   1 
ATOM   6546 N N     . PHE B 1 348 ? 43.910  -12.737 15.096 1.00 16.50  ? 390  PHE B N     1 
ATOM   6547 C CA    . PHE B 1 348 ? 42.669  -12.342 14.457 1.00 16.15  ? 390  PHE B CA    1 
ATOM   6548 C C     . PHE B 1 348 ? 41.570  -13.352 14.801 1.00 15.64  ? 390  PHE B C     1 
ATOM   6549 O O     . PHE B 1 348 ? 40.437  -12.980 15.114 1.00 16.88  ? 390  PHE B O     1 
ATOM   6550 C CB    . PHE B 1 348 ? 42.794  -12.185 12.942 1.00 14.97  ? 390  PHE B CB    1 
ATOM   6551 C CG    . PHE B 1 348 ? 41.574  -11.580 12.314 1.00 15.55  ? 390  PHE B CG    1 
ATOM   6552 C CD1   . PHE B 1 348 ? 40.490  -12.356 11.963 1.00 16.33  ? 390  PHE B CD1   1 
ATOM   6553 C CD2   . PHE B 1 348 ? 41.514  -10.219 12.109 1.00 17.41  ? 390  PHE B CD2   1 
ATOM   6554 C CE1   . PHE B 1 348 ? 39.357  -11.788 11.399 1.00 16.89  ? 390  PHE B CE1   1 
ATOM   6555 C CE2   . PHE B 1 348 ? 40.380  -9.654  11.538 1.00 18.14  ? 390  PHE B CE2   1 
ATOM   6556 C CZ    . PHE B 1 348 ? 39.305  -10.436 11.218 1.00 17.22  ? 390  PHE B CZ    1 
ATOM   6557 N N     . HIS B 1 349 ? 41.905  -14.637 14.785 1.00 14.48  ? 391  HIS B N     1 
ATOM   6558 C CA    . HIS B 1 349 ? 40.960  -15.695 15.077 1.00 17.70  ? 391  HIS B CA    1 
ATOM   6559 C C     . HIS B 1 349 ? 40.474  -15.561 16.530 1.00 15.66  ? 391  HIS B C     1 
ATOM   6560 O O     . HIS B 1 349 ? 39.279  -15.655 16.799 1.00 16.88  ? 391  HIS B O     1 
ATOM   6561 C CB    . HIS B 1 349 ? 41.553  -17.078 14.793 1.00 19.54  ? 391  HIS B CB    1 
ATOM   6562 C CG    . HIS B 1 349 ? 40.564  -18.161 15.108 1.00 20.78  ? 391  HIS B CG    1 
ATOM   6563 N ND1   . HIS B 1 349 ? 39.450  -18.416 14.333 1.00 25.04  ? 391  HIS B ND1   1 
ATOM   6564 C CD2   . HIS B 1 349 ? 40.494  -18.972 16.141 1.00 24.25  ? 391  HIS B CD2   1 
ATOM   6565 C CE1   . HIS B 1 349 ? 38.744  -19.390 14.887 1.00 25.99  ? 391  HIS B CE1   1 
ATOM   6566 N NE2   . HIS B 1 349 ? 39.374  -19.754 15.988 1.00 28.82  ? 391  HIS B NE2   1 
ATOM   6567 N N     . HIS B 1 350 ? 41.414  -15.312 17.443 1.00 14.54  ? 392  HIS B N     1 
ATOM   6568 C CA    . HIS B 1 350 ? 41.089  -15.125 18.853 1.00 14.88  ? 392  HIS B CA    1 
ATOM   6569 C C     . HIS B 1 350 ? 40.046  -13.999 19.057 1.00 15.09  ? 392  HIS B C     1 
ATOM   6570 O O     . HIS B 1 350 ? 39.031  -14.186 19.770 1.00 16.55  ? 392  HIS B O     1 
ATOM   6571 C CB    . HIS B 1 350 ? 42.412  -14.886 19.581 1.00 15.45  ? 392  HIS B CB    1 
ATOM   6572 C CG    . HIS B 1 350 ? 42.264  -14.724 21.047 1.00 16.82  ? 392  HIS B CG    1 
ATOM   6573 N ND1   . HIS B 1 350 ? 42.337  -15.834 21.839 1.00 21.24  ? 392  HIS B ND1   1 
ATOM   6574 C CD2   . HIS B 1 350 ? 42.086  -13.661 21.870 1.00 19.17  ? 392  HIS B CD2   1 
ATOM   6575 C CE1   . HIS B 1 350 ? 42.183  -15.455 23.113 1.00 22.43  ? 392  HIS B CE1   1 
ATOM   6576 N NE2   . HIS B 1 350 ? 42.005  -14.158 23.155 1.00 19.31  ? 392  HIS B NE2   1 
ATOM   6577 N N     . HIS B 1 351 ? 40.232  -12.864 18.384 1.00 13.73  ? 393  HIS B N     1 
ATOM   6578 C CA    . HIS B 1 351 ? 39.353  -11.732 18.566 1.00 13.98  ? 393  HIS B CA    1 
ATOM   6579 C C     . HIS B 1 351 ? 38.058  -11.922 17.788 1.00 14.77  ? 393  HIS B C     1 
ATOM   6580 O O     . HIS B 1 351 ? 36.994  -11.491 18.214 1.00 15.11  ? 393  HIS B O     1 
ATOM   6581 C CB    . HIS B 1 351 ? 40.076  -10.422 18.202 1.00 15.68  ? 393  HIS B CB    1 
ATOM   6582 C CG    . HIS B 1 351 ? 41.026  -10.077 19.289 1.00 16.09  ? 393  HIS B CG    1 
ATOM   6583 N ND1   . HIS B 1 351 ? 42.391  -10.307 19.363 1.00 18.33  ? 393  HIS B ND1   1 
ATOM   6584 C CD2   . HIS B 1 351 ? 40.687  -9.450  20.424 1.00 13.13  ? 393  HIS B CD2   1 
ATOM   6585 C CE1   . HIS B 1 351 ? 42.818  -9.854  20.552 1.00 13.82  ? 393  HIS B CE1   1 
ATOM   6586 N NE2   . HIS B 1 351 ? 41.787  -9.284  21.147 1.00 15.57  ? 393  HIS B NE2   1 
ATOM   6587 N N     . GLN B 1 352 ? 38.137  -12.509 16.583 1.00 15.32  ? 394  GLN B N     1 
ATOM   6588 C CA    . GLN B 1 352 ? 36.925  -12.790 15.819 1.00 17.51  ? 394  GLN B CA    1 
ATOM   6589 C C     . GLN B 1 352 ? 35.988  -13.688 16.643 1.00 16.96  ? 394  GLN B C     1 
ATOM   6590 O O     . GLN B 1 352 ? 34.760  -13.554 16.576 1.00 17.38  ? 394  GLN B O     1 
ATOM   6591 C CB    . GLN B 1 352 ? 37.243  -13.476 14.483 1.00 22.80  ? 394  GLN B CB    1 
ATOM   6592 C CG    . GLN B 1 352 ? 36.142  -14.445 14.023 1.00 32.06  ? 394  GLN B CG    1 
ATOM   6593 C CD    . GLN B 1 352 ? 36.419  -15.103 12.702 1.00 43.95  ? 394  GLN B CD    1 
ATOM   6594 O OE1   . GLN B 1 352 ? 36.549  -16.322 12.663 1.00 57.32  ? 394  GLN B OE1   1 
ATOM   6595 N NE2   . GLN B 1 352 ? 36.503  -14.321 11.625 1.00 42.34  ? 394  GLN B NE2   1 
ATOM   6596 N N     . THR B 1 353 ? 36.549  -14.625 17.407 1.00 15.20  ? 395  THR B N     1 
ATOM   6597 C CA    . THR B 1 353 ? 35.742  -15.429 18.315 1.00 16.49  ? 395  THR B CA    1 
ATOM   6598 C C     . THR B 1 353 ? 35.104  -14.553 19.398 1.00 13.73  ? 395  THR B C     1 
ATOM   6599 O O     . THR B 1 353 ? 33.903  -14.706 19.683 1.00 15.32  ? 395  THR B O     1 
ATOM   6600 C CB    . THR B 1 353 ? 36.577  -16.556 18.928 1.00 17.59  ? 395  THR B CB    1 
ATOM   6601 O OG1   . THR B 1 353 ? 37.067  -17.349 17.858 1.00 17.50  ? 395  THR B OG1   1 
ATOM   6602 C CG2   . THR B 1 353 ? 35.781  -17.432 19.860 1.00 19.09  ? 395  THR B CG2   1 
ATOM   6603 N N     . LEU B 1 354 ? 35.914  -13.797 20.117 1.00 13.63  ? 396  LEU B N     1 
ATOM   6604 C CA    . LEU B 1 354 ? 35.432  -12.981 21.231 1.00 14.52  ? 396  LEU B CA    1 
ATOM   6605 C C     . LEU B 1 354 ? 34.308  -12.049 20.803 1.00 13.81  ? 396  LEU B C     1 
ATOM   6606 O O     . LEU B 1 354 ? 33.366  -11.863 21.557 1.00 13.17  ? 396  LEU B O     1 
ATOM   6607 C CB    . LEU B 1 354 ? 36.559  -12.112 21.785 1.00 14.07  ? 396  LEU B CB    1 
ATOM   6608 C CG    . LEU B 1 354 ? 37.618  -12.784 22.649 1.00 15.22  ? 396  LEU B CG    1 
ATOM   6609 C CD1   . LEU B 1 354 ? 38.702  -11.755 22.995 1.00 15.34  ? 396  LEU B CD1   1 
ATOM   6610 C CD2   . LEU B 1 354 ? 36.992  -13.386 23.912 1.00 15.77  ? 396  LEU B CD2   1 
ATOM   6611 N N     . MET B 1 355 ? 34.430  -11.428 19.600 1.00 13.85  ? 397  MET B N     1 
ATOM   6612 C CA    . MET B 1 355 ? 33.499  -10.374 19.215 1.00 12.73  ? 397  MET B CA    1 
ATOM   6613 C C     . MET B 1 355 ? 32.151  -10.908 18.714 1.00 13.65  ? 397  MET B C     1 
ATOM   6614 O O     . MET B 1 355 ? 31.222  -10.120 18.516 1.00 13.28  ? 397  MET B O     1 
ATOM   6615 C CB    . MET B 1 355 ? 34.119  -9.377  18.209 1.00 14.41  ? 397  MET B CB    1 
ATOM   6616 C CG    . MET B 1 355 ? 35.356  -8.663  18.792 1.00 14.31  ? 397  MET B CG    1 
ATOM   6617 S SD    . MET B 1 355 ? 36.141  -7.425  17.737 1.00 14.30  ? 397  MET B SD    1 
ATOM   6618 C CE    . MET B 1 355 ? 36.552  -8.458  16.327 1.00 16.01  ? 397  MET B CE    1 
ATOM   6619 N N     . GLN B 1 356 ? 31.982  -12.230 18.641 1.00 13.13  ? 398  GLN B N     1 
ATOM   6620 C CA    . GLN B 1 356 ? 30.682  -12.846 18.424 1.00 13.10  ? 398  GLN B CA    1 
ATOM   6621 C C     . GLN B 1 356 ? 30.240  -13.631 19.670 1.00 14.83  ? 398  GLN B C     1 
ATOM   6622 O O     . GLN B 1 356 ? 29.343  -14.477 19.611 1.00 17.17  ? 398  GLN B O     1 
ATOM   6623 C CB    . GLN B 1 356 ? 30.667  -13.684 17.149 1.00 17.90  ? 398  GLN B CB    1 
ATOM   6624 C CG    . GLN B 1 356 ? 31.649  -14.837 17.130 1.00 18.50  ? 398  GLN B CG    1 
ATOM   6625 C CD    . GLN B 1 356 ? 31.513  -15.626 15.843 1.00 22.11  ? 398  GLN B CD    1 
ATOM   6626 O OE1   . GLN B 1 356 ? 30.429  -16.061 15.487 1.00 28.40  ? 398  GLN B OE1   1 
ATOM   6627 N NE2   . GLN B 1 356 ? 32.617  -15.931 15.204 1.00 21.35  ? 398  GLN B NE2   1 
ATOM   6628 N N     . GLY B 1 357 ? 30.953  -13.438 20.782 1.00 15.09  ? 399  GLY B N     1 
ATOM   6629 C CA    . GLY B 1 357 ? 30.617  -14.099 22.049 1.00 16.15  ? 399  GLY B CA    1 
ATOM   6630 C C     . GLY B 1 357 ? 30.850  -15.610 21.970 1.00 15.96  ? 399  GLY B C     1 
ATOM   6631 O O     . GLY B 1 357 ? 30.112  -16.413 22.542 1.00 16.48  ? 399  GLY B O     1 
ATOM   6632 N N     . GLY B 1 358 ? 31.926  -15.986 21.270 1.00 16.85  ? 400  GLY B N     1 
ATOM   6633 C CA    . GLY B 1 358 ? 32.379  -17.357 21.151 1.00 18.72  ? 400  GLY B CA    1 
ATOM   6634 C C     . GLY B 1 358 ? 33.356  -17.747 22.251 1.00 19.58  ? 400  GLY B C     1 
ATOM   6635 O O     . GLY B 1 358 ? 34.029  -16.917 22.804 1.00 24.68  ? 400  GLY B O     1 
ATOM   6636 N N     . LEU B 1 359 ? 33.454  -19.055 22.546 1.00 29.19  ? 401  LEU B N     1 
ATOM   6637 C CA    . LEU B 1 359 ? 34.367  -19.502 23.594 1.00 34.35  ? 401  LEU B CA    1 
ATOM   6638 C C     . LEU B 1 359 ? 35.718  -19.854 22.974 1.00 33.68  ? 401  LEU B C     1 
ATOM   6639 O O     . LEU B 1 359 ? 35.707  -20.627 22.034 1.00 26.11  ? 401  LEU B O     1 
ATOM   6640 C CB    . LEU B 1 359 ? 33.737  -20.744 24.228 1.00 42.87  ? 401  LEU B CB    1 
ATOM   6641 C CG    . LEU B 1 359 ? 32.354  -20.516 24.844 1.00 47.51  ? 401  LEU B CG    1 
ATOM   6642 C CD1   . LEU B 1 359 ? 31.548  -21.800 24.783 1.00 48.54  ? 401  LEU B CD1   1 
ATOM   6643 C CD2   . LEU B 1 359 ? 32.502  -20.004 26.278 1.00 45.74  ? 401  LEU B CD2   1 
ATOM   6644 N N     . ASN B 1 360 ? 36.833  -19.264 23.445 1.00 39.55  ? 402  ASN B N     1 
ATOM   6645 C CA    . ASN B 1 360 ? 38.150  -19.665 22.959 1.00 44.11  ? 402  ASN B CA    1 
ATOM   6646 C C     . ASN B 1 360 ? 38.538  -20.893 23.786 1.00 51.50  ? 402  ASN B C     1 
ATOM   6647 O O     . ASN B 1 360 ? 38.375  -20.909 25.009 1.00 48.59  ? 402  ASN B O     1 
ATOM   6648 C CB    . ASN B 1 360 ? 39.214  -18.542 22.933 1.00 41.74  ? 402  ASN B CB    1 
ATOM   6649 C CG    . ASN B 1 360 ? 39.144  -17.603 21.721 1.00 42.29  ? 402  ASN B CG    1 
ATOM   6650 O OD1   . ASN B 1 360 ? 39.369  -17.995 20.567 1.00 38.20  ? 402  ASN B OD1   1 
ATOM   6651 N ND2   . ASN B 1 360 ? 38.837  -16.332 21.945 1.00 30.08  ? 402  ASN B ND2   1 
ATOM   6652 N N     . LEU B 1 361 ? 38.937  -21.968 23.096 1.00 62.94  ? 403  LEU B N     1 
ATOM   6653 C CA    . LEU B 1 361 ? 39.477  -23.148 23.752 1.00 70.78  ? 403  LEU B CA    1 
ATOM   6654 C C     . LEU B 1 361 ? 40.996  -23.012 23.704 1.00 81.79  ? 403  LEU B C     1 
ATOM   6655 O O     . LEU B 1 361 ? 41.608  -23.199 22.649 1.00 83.34  ? 403  LEU B O     1 
ATOM   6656 C CB    . LEU B 1 361 ? 38.984  -24.419 23.045 1.00 68.38  ? 403  LEU B CB    1 
ATOM   6657 N N     . ASP B 1 362 ? 41.587  -22.610 24.837 1.00 71.24  ? 404  ASP B N     1 
ATOM   6658 C CA    . ASP B 1 362 ? 43.019  -22.361 24.898 1.00 70.62  ? 404  ASP B CA    1 
ATOM   6659 C C     . ASP B 1 362 ? 43.439  -22.313 26.371 1.00 69.60  ? 404  ASP B C     1 
ATOM   6660 O O     . ASP B 1 362 ? 42.626  -22.020 27.251 1.00 60.33  ? 404  ASP B O     1 
ATOM   6661 C CB    . ASP B 1 362 ? 43.403  -21.106 24.096 1.00 60.50  ? 404  ASP B CB    1 
ATOM   6662 N N     . GLU B 1 363 ? 44.710  -22.654 26.628 1.00 62.45  ? 405  GLU B N     1 
ATOM   6663 C CA    . GLU B 1 363 ? 45.329  -22.440 27.927 1.00 57.51  ? 405  GLU B CA    1 
ATOM   6664 C C     . GLU B 1 363 ? 45.761  -20.973 27.983 1.00 50.27  ? 405  GLU B C     1 
ATOM   6665 O O     . GLU B 1 363 ? 45.809  -20.294 26.956 1.00 50.47  ? 405  GLU B O     1 
ATOM   6666 C CB    . GLU B 1 363 ? 46.485  -23.429 28.150 1.00 53.59  ? 405  GLU B CB    1 
ATOM   6667 N N     . VAL B 1 364 ? 46.060  -20.504 29.199 1.00 46.33  ? 406  VAL B N     1 
ATOM   6668 C CA    . VAL B 1 364 ? 46.498  -19.139 29.439 1.00 38.76  ? 406  VAL B CA    1 
ATOM   6669 C C     . VAL B 1 364 ? 48.032  -19.080 29.341 1.00 35.51  ? 406  VAL B C     1 
ATOM   6670 O O     . VAL B 1 364 ? 48.765  -19.207 30.352 1.00 29.21  ? 406  VAL B O     1 
ATOM   6671 C CB    . VAL B 1 364 ? 45.936  -18.608 30.779 1.00 39.00  ? 406  VAL B CB    1 
ATOM   6672 C CG1   . VAL B 1 364 ? 46.219  -17.126 30.941 1.00 36.75  ? 406  VAL B CG1   1 
ATOM   6673 C CG2   . VAL B 1 364 ? 44.439  -18.865 30.902 1.00 37.66  ? 406  VAL B CG2   1 
ATOM   6674 N N     . GLY B 1 365 ? 48.496  -18.827 28.103 1.00 30.22  ? 407  GLY B N     1 
ATOM   6675 C CA    . GLY B 1 365 ? 49.902  -18.575 27.820 1.00 26.35  ? 407  GLY B CA    1 
ATOM   6676 C C     . GLY B 1 365 ? 50.562  -17.515 28.703 1.00 21.71  ? 407  GLY B C     1 
ATOM   6677 O O     . GLY B 1 365 ? 51.760  -17.604 28.992 1.00 19.70  ? 407  GLY B O     1 
ATOM   6678 N N     . LEU B 1 366 ? 49.793  -16.483 29.092 1.00 20.14  ? 408  LEU B N     1 
ATOM   6679 C CA    . LEU B 1 366 ? 50.360  -15.388 29.866 1.00 22.12  ? 408  LEU B CA    1 
ATOM   6680 C C     . LEU B 1 366 ? 51.068  -15.876 31.133 1.00 20.80  ? 408  LEU B C     1 
ATOM   6681 O O     . LEU B 1 366 ? 51.976  -15.214 31.647 1.00 21.86  ? 408  LEU B O     1 
ATOM   6682 C CB    . LEU B 1 366 ? 49.270  -14.438 30.351 1.00 23.71  ? 408  LEU B CB    1 
ATOM   6683 C CG    . LEU B 1 366 ? 48.682  -13.404 29.408 1.00 29.22  ? 408  LEU B CG    1 
ATOM   6684 C CD1   . LEU B 1 366 ? 48.040  -12.310 30.268 1.00 27.40  ? 408  LEU B CD1   1 
ATOM   6685 C CD2   . LEU B 1 366 ? 49.693  -12.815 28.444 1.00 26.05  ? 408  LEU B CD2   1 
ATOM   6686 N N     . LEU B 1 367 ? 50.615  -17.002 31.696 1.00 16.78  ? 409  LEU B N     1 
ATOM   6687 C CA    . LEU B 1 367 ? 51.225  -17.443 32.941 1.00 16.90  ? 409  LEU B CA    1 
ATOM   6688 C C     . LEU B 1 367 ? 52.613  -18.044 32.748 1.00 18.16  ? 409  LEU B C     1 
ATOM   6689 O O     . LEU B 1 367 ? 53.178  -18.496 33.741 1.00 19.46  ? 409  LEU B O     1 
ATOM   6690 C CB    . LEU B 1 367 ? 50.313  -18.489 33.586 1.00 20.20  ? 409  LEU B CB    1 
ATOM   6691 C CG    . LEU B 1 367 ? 48.937  -17.996 34.025 1.00 24.79  ? 409  LEU B CG    1 
ATOM   6692 C CD1   . LEU B 1 367 ? 48.091  -19.153 34.540 1.00 28.98  ? 409  LEU B CD1   1 
ATOM   6693 C CD2   . LEU B 1 367 ? 49.071  -16.963 35.096 1.00 25.31  ? 409  LEU B CD2   1 
ATOM   6694 N N     . ARG B 1 368 ? 53.156  -18.110 31.525 1.00 14.32  ? 410  ARG B N     1 
ATOM   6695 C CA    . ARG B 1 368 ? 54.495  -18.632 31.363 1.00 17.31  ? 410  ARG B CA    1 
ATOM   6696 C C     . ARG B 1 368 ? 55.511  -17.657 30.779 1.00 19.11  ? 410  ARG B C     1 
ATOM   6697 O O     . ARG B 1 368 ? 56.606  -18.068 30.351 1.00 19.97  ? 410  ARG B O     1 
ATOM   6698 C CB    . ARG B 1 368 ? 54.480  -19.884 30.477 1.00 18.88  ? 410  ARG B CB    1 
ATOM   6699 C CG    . ARG B 1 368 ? 53.729  -21.061 31.101 1.00 24.38  ? 410  ARG B CG    1 
ATOM   6700 C CD    . ARG B 1 368 ? 54.221  -21.561 32.451 1.00 27.17  ? 410  ARG B CD    1 
ATOM   6701 N NE    . ARG B 1 368 ? 55.631  -21.932 32.413 1.00 29.63  ? 410  ARG B NE    1 
ATOM   6702 C CZ    . ARG B 1 368 ? 56.051  -23.196 32.262 1.00 31.68  ? 410  ARG B CZ    1 
ATOM   6703 N NH1   . ARG B 1 368 ? 55.167  -24.173 32.168 1.00 29.79  ? 410  ARG B NH1   1 
ATOM   6704 N NH2   . ARG B 1 368 ? 57.337  -23.480 32.215 1.00 28.01  ? 410  ARG B NH2   1 
ATOM   6705 N N     . TRP B 1 369 ? 55.284  -16.374 30.920 1.00 14.21  ? 411  TRP B N     1 
ATOM   6706 C CA    . TRP B 1 369 ? 56.123  -15.393 30.241 1.00 14.16  ? 411  TRP B CA    1 
ATOM   6707 C C     . TRP B 1 369 ? 57.586  -15.375 30.694 1.00 14.64  ? 411  TRP B C     1 
ATOM   6708 O O     . TRP B 1 369 ? 58.459  -15.450 29.833 1.00 15.74  ? 411  TRP B O     1 
ATOM   6709 C CB    . TRP B 1 369 ? 55.460  -14.032 30.416 1.00 13.44  ? 411  TRP B CB    1 
ATOM   6710 C CG    . TRP B 1 369 ? 56.129  -12.843 29.798 1.00 13.48  ? 411  TRP B CG    1 
ATOM   6711 C CD1   . TRP B 1 369 ? 56.620  -11.759 30.443 1.00 12.90  ? 411  TRP B CD1   1 
ATOM   6712 C CD2   . TRP B 1 369 ? 56.366  -12.590 28.410 1.00 12.95  ? 411  TRP B CD2   1 
ATOM   6713 N NE1   . TRP B 1 369 ? 57.066  -10.827 29.558 1.00 14.13  ? 411  TRP B NE1   1 
ATOM   6714 C CE2   . TRP B 1 369 ? 56.955  -11.311 28.316 1.00 13.78  ? 411  TRP B CE2   1 
ATOM   6715 C CE3   . TRP B 1 369 ? 56.107  -13.293 27.237 1.00 13.37  ? 411  TRP B CE3   1 
ATOM   6716 C CZ2   . TRP B 1 369 ? 57.258  -10.728 27.096 1.00 14.04  ? 411  TRP B CZ2   1 
ATOM   6717 C CZ3   . TRP B 1 369 ? 56.454  -12.728 26.026 1.00 13.78  ? 411  TRP B CZ3   1 
ATOM   6718 C CH2   . TRP B 1 369 ? 57.017  -11.464 25.973 1.00 15.64  ? 411  TRP B CH2   1 
ATOM   6719 N N     . ARG B 1 370 ? 57.845  -15.197 31.997 1.00 15.41  ? 412  ARG B N     1 
ATOM   6720 C CA    . ARG B 1 370 ? 59.156  -14.901 32.564 1.00 15.84  ? 412  ARG B CA    1 
ATOM   6721 C C     . ARG B 1 370 ? 59.546  -16.049 33.478 1.00 15.13  ? 412  ARG B C     1 
ATOM   6722 O O     . ARG B 1 370 ? 58.809  -16.404 34.383 1.00 14.56  ? 412  ARG B O     1 
ATOM   6723 C CB    . ARG B 1 370 ? 59.179  -13.652 33.478 1.00 21.28  ? 412  ARG B CB    1 
ATOM   6724 C CG    . ARG B 1 370 ? 59.247  -12.308 32.780 1.00 25.97  ? 412  ARG B CG    1 
ATOM   6725 C CD    . ARG B 1 370 ? 59.364  -11.141 33.758 1.00 22.88  ? 412  ARG B CD    1 
ATOM   6726 N NE    . ARG B 1 370 ? 59.610  -9.868  33.031 1.00 28.30  ? 412  ARG B NE    1 
ATOM   6727 C CZ    . ARG B 1 370 ? 60.788  -9.287  32.942 1.00 30.23  ? 412  ARG B CZ    1 
ATOM   6728 N NH1   . ARG B 1 370 ? 61.872  -9.881  33.419 1.00 33.33  ? 412  ARG B NH1   1 
ATOM   6729 N NH2   . ARG B 1 370 ? 60.915  -8.144  32.306 1.00 35.21  ? 412  ARG B NH2   1 
ATOM   6730 N N     . GLY B 1 371 ? 60.731  -16.611 33.260 1.00 14.51  ? 413  GLY B N     1 
ATOM   6731 C CA    . GLY B 1 371 ? 61.270  -17.618 34.166 1.00 15.48  ? 413  GLY B CA    1 
ATOM   6732 C C     . GLY B 1 371 ? 60.333  -18.810 34.254 1.00 14.84  ? 413  GLY B C     1 
ATOM   6733 O O     . GLY B 1 371 ? 59.798  -19.287 33.242 1.00 17.83  ? 413  GLY B O     1 
ATOM   6734 N N     . ALA B 1 372 ? 60.076  -19.241 35.501 1.00 15.49  ? 414  ALA B N     1 
ATOM   6735 C CA    . ALA B 1 372 ? 59.155  -20.323 35.817 1.00 16.59  ? 414  ALA B CA    1 
ATOM   6736 C C     . ALA B 1 372 ? 57.677  -19.911 35.678 1.00 17.93  ? 414  ALA B C     1 
ATOM   6737 O O     . ALA B 1 372 ? 56.806  -20.773 35.667 1.00 20.10  ? 414  ALA B O     1 
ATOM   6738 C CB    . ALA B 1 372 ? 59.458  -20.846 37.209 1.00 15.79  ? 414  ALA B CB    1 
ATOM   6739 N N     . GLY B 1 373 ? 57.397  -18.611 35.469 1.00 15.57  ? 415  GLY B N     1 
ATOM   6740 C CA    . GLY B 1 373 ? 56.053  -18.104 35.281 1.00 15.05  ? 415  GLY B CA    1 
ATOM   6741 C C     . GLY B 1 373 ? 55.255  -18.072 36.580 1.00 14.23  ? 415  GLY B C     1 
ATOM   6742 O O     . GLY B 1 373 ? 55.849  -18.141 37.656 1.00 16.24  ? 415  GLY B O     1 
ATOM   6743 N N     . GLY B 1 374 ? 53.926  -18.092 36.432 1.00 13.83  ? 416  GLY B N     1 
ATOM   6744 C CA    . GLY B 1 374 ? 52.981  -18.276 37.534 1.00 14.04  ? 416  GLY B CA    1 
ATOM   6745 C C     . GLY B 1 374 ? 52.569  -16.992 38.275 1.00 15.33  ? 416  GLY B C     1 
ATOM   6746 O O     . GLY B 1 374 ? 51.798  -17.070 39.232 1.00 13.09  ? 416  GLY B O     1 
ATOM   6747 N N     . GLY B 1 375 ? 53.103  -15.844 37.853 1.00 13.73  ? 417  GLY B N     1 
ATOM   6748 C CA    . GLY B 1 375 ? 52.823  -14.537 38.446 1.00 12.93  ? 417  GLY B CA    1 
ATOM   6749 C C     . GLY B 1 375 ? 52.036  -13.654 37.481 1.00 12.57  ? 417  GLY B C     1 
ATOM   6750 O O     . GLY B 1 375 ? 52.449  -13.419 36.330 1.00 12.78  ? 417  GLY B O     1 
ATOM   6751 N N     . LEU B 1 376 ? 50.829  -13.265 37.919 1.00 12.33  ? 418  LEU B N     1 
ATOM   6752 C CA    . LEU B 1 376 ? 49.962  -12.351 37.165 1.00 12.05  ? 418  LEU B CA    1 
ATOM   6753 C C     . LEU B 1 376 ? 49.120  -11.530 38.155 1.00 11.66  ? 418  LEU B C     1 
ATOM   6754 O O     . LEU B 1 376 ? 48.367  -12.094 38.962 1.00 11.85  ? 418  LEU B O     1 
ATOM   6755 C CB    . LEU B 1 376 ? 48.994  -13.098 36.262 1.00 14.26  ? 418  LEU B CB    1 
ATOM   6756 C CG    . LEU B 1 376 ? 47.837  -12.247 35.662 1.00 16.93  ? 418  LEU B CG    1 
ATOM   6757 C CD1   . LEU B 1 376 ? 48.290  -11.141 34.714 1.00 16.90  ? 418  LEU B CD1   1 
ATOM   6758 C CD2   . LEU B 1 376 ? 46.819  -13.132 34.979 1.00 19.99  ? 418  LEU B CD2   1 
ATOM   6759 N N     . ALA B 1 377 ? 49.213  -10.214 38.037 1.00 11.35  ? 419  ALA B N     1 
ATOM   6760 C CA    . ALA B 1 377 ? 48.299  -9.321  38.746 1.00 12.03  ? 419  ALA B CA    1 
ATOM   6761 C C     . ALA B 1 377 ? 47.845  -8.247  37.771 1.00 10.39  ? 419  ALA B C     1 
ATOM   6762 O O     . ALA B 1 377 ? 48.671  -7.683  37.069 1.00 11.25  ? 419  ALA B O     1 
ATOM   6763 C CB    . ALA B 1 377 ? 48.948  -8.665  39.929 1.00 12.56  ? 419  ALA B CB    1 
ATOM   6764 N N     . TRP B 1 378 ? 46.521  -8.113  37.605 1.00 9.80   ? 420  TRP B N     1 
ATOM   6765 C CA    . TRP B 1 378 ? 45.965  -7.023  36.833 1.00 10.35  ? 420  TRP B CA    1 
ATOM   6766 C C     . TRP B 1 378 ? 46.041  -5.709  37.602 1.00 10.78  ? 420  TRP B C     1 
ATOM   6767 O O     . TRP B 1 378 ? 45.575  -5.641  38.744 1.00 12.96  ? 420  TRP B O     1 
ATOM   6768 C CB    . TRP B 1 378 ? 44.522  -7.309  36.481 1.00 8.93   ? 420  TRP B CB    1 
ATOM   6769 C CG    . TRP B 1 378 ? 44.363  -8.567  35.683 1.00 10.86  ? 420  TRP B CG    1 
ATOM   6770 C CD1   . TRP B 1 378 ? 43.715  -9.682  36.105 1.00 11.56  ? 420  TRP B CD1   1 
ATOM   6771 C CD2   . TRP B 1 378 ? 44.824  -8.824  34.341 1.00 10.64  ? 420  TRP B CD2   1 
ATOM   6772 N NE1   . TRP B 1 378 ? 43.751  -10.631 35.130 1.00 12.64  ? 420  TRP B NE1   1 
ATOM   6773 C CE2   . TRP B 1 378 ? 44.428  -10.145 34.031 1.00 11.82  ? 420  TRP B CE2   1 
ATOM   6774 C CE3   . TRP B 1 378 ? 45.462  -8.073  33.346 1.00 11.92  ? 420  TRP B CE3   1 
ATOM   6775 C CZ2   . TRP B 1 378 ? 44.698  -10.751 32.802 1.00 12.21  ? 420  TRP B CZ2   1 
ATOM   6776 C CZ3   . TRP B 1 378 ? 45.733  -8.675  32.129 1.00 11.76  ? 420  TRP B CZ3   1 
ATOM   6777 C CH2   . TRP B 1 378 ? 45.310  -9.969  31.846 1.00 12.71  ? 420  TRP B CH2   1 
ATOM   6778 N N     . PHE B 1 379 ? 46.565  -4.672  36.953 1.00 10.46  ? 421  PHE B N     1 
ATOM   6779 C CA    . PHE B 1 379 ? 46.445  -3.290  37.376 1.00 10.63  ? 421  PHE B CA    1 
ATOM   6780 C C     . PHE B 1 379 ? 45.553  -2.621  36.343 1.00 10.71  ? 421  PHE B C     1 
ATOM   6781 O O     . PHE B 1 379 ? 45.860  -2.626  35.167 1.00 10.29  ? 421  PHE B O     1 
ATOM   6782 C CB    . PHE B 1 379 ? 47.797  -2.589  37.577 1.00 11.57  ? 421  PHE B CB    1 
ATOM   6783 C CG    . PHE B 1 379 ? 47.641  -1.126  37.932 1.00 11.38  ? 421  PHE B CG    1 
ATOM   6784 C CD1   . PHE B 1 379 ? 46.895  -0.750  39.034 1.00 11.75  ? 421  PHE B CD1   1 
ATOM   6785 C CD2   . PHE B 1 379 ? 48.244  -0.152  37.184 1.00 10.81  ? 421  PHE B CD2   1 
ATOM   6786 C CE1   . PHE B 1 379 ? 46.694  0.597   39.291 1.00 12.44  ? 421  PHE B CE1   1 
ATOM   6787 C CE2   . PHE B 1 379 ? 48.121  1.191   37.515 1.00 12.28  ? 421  PHE B CE2   1 
ATOM   6788 C CZ    . PHE B 1 379 ? 47.340  1.548   38.565 1.00 12.28  ? 421  PHE B CZ    1 
ATOM   6789 N N     . ALA B 1 380 ? 44.377  -2.159  36.751 1.00 9.59   ? 422  ALA B N     1 
ATOM   6790 C CA    . ALA B 1 380 ? 43.312  -1.825  35.820 1.00 10.73  ? 422  ALA B CA    1 
ATOM   6791 C C     . ALA B 1 380 ? 42.780  -0.409  36.055 1.00 10.75  ? 422  ALA B C     1 
ATOM   6792 O O     . ALA B 1 380 ? 41.573  -0.210  36.304 1.00 10.40  ? 422  ALA B O     1 
ATOM   6793 C CB    . ALA B 1 380 ? 42.219  -2.844  35.973 1.00 10.83  ? 422  ALA B CB    1 
ATOM   6794 N N     . PRO B 1 381 ? 43.625  0.642   35.900 1.00 11.16  ? 423  PRO B N     1 
ATOM   6795 C CA    . PRO B 1 381 ? 43.150  2.033   35.972 1.00 10.51  ? 423  PRO B CA    1 
ATOM   6796 C C     . PRO B 1 381 ? 42.182  2.449   34.868 1.00 12.41  ? 423  PRO B C     1 
ATOM   6797 O O     . PRO B 1 381 ? 42.242  1.976   33.740 1.00 12.14  ? 423  PRO B O     1 
ATOM   6798 C CB    . PRO B 1 381 ? 44.464  2.860   35.929 1.00 11.13  ? 423  PRO B CB    1 
ATOM   6799 C CG    . PRO B 1 381 ? 45.387  1.960   35.057 1.00 11.34  ? 423  PRO B CG    1 
ATOM   6800 C CD    . PRO B 1 381 ? 45.078  0.566   35.579 1.00 11.33  ? 423  PRO B CD    1 
ATOM   6801 N N     . VAL B 1 382 ? 41.251  3.339   35.210 1.00 11.67  ? 424  VAL B N     1 
ATOM   6802 C CA    . VAL B 1 382 ? 40.313  3.985   34.287 1.00 12.08  ? 424  VAL B CA    1 
ATOM   6803 C C     . VAL B 1 382 ? 40.968  5.214   33.687 1.00 11.68  ? 424  VAL B C     1 
ATOM   6804 O O     . VAL B 1 382 ? 41.726  5.883   34.368 1.00 12.20  ? 424  VAL B O     1 
ATOM   6805 C CB    . VAL B 1 382 ? 39.044  4.423   35.074 1.00 13.72  ? 424  VAL B CB    1 
ATOM   6806 C CG1   . VAL B 1 382 ? 38.028  5.149   34.238 1.00 15.99  ? 424  VAL B CG1   1 
ATOM   6807 C CG2   . VAL B 1 382 ? 38.424  3.206   35.736 1.00 16.40  ? 424  VAL B CG2   1 
ATOM   6808 N N     . ALA B 1 383 ? 40.615  5.518   32.435 1.00 13.07  ? 425  ALA B N     1 
ATOM   6809 C CA    . ALA B 1 383 ? 40.837  6.830   31.840 1.00 15.07  ? 425  ALA B CA    1 
ATOM   6810 C C     . ALA B 1 383 ? 39.570  7.278   31.137 1.00 13.80  ? 425  ALA B C     1 
ATOM   6811 O O     . ALA B 1 383 ? 38.785  6.450   30.696 1.00 14.13  ? 425  ALA B O     1 
ATOM   6812 C CB    . ALA B 1 383 ? 41.954  6.743   30.847 1.00 15.22  ? 425  ALA B CB    1 
ATOM   6813 N N     . ALA B 1 384 ? 39.399  8.589   30.974 1.00 13.20  ? 426  ALA B N     1 
ATOM   6814 C CA    . ALA B 1 384 ? 38.486  9.068   29.956 1.00 12.25  ? 426  ALA B CA    1 
ATOM   6815 C C     . ALA B 1 384 ? 39.047  8.743   28.583 1.00 11.65  ? 426  ALA B C     1 
ATOM   6816 O O     . ALA B 1 384 ? 40.258  8.587   28.431 1.00 12.56  ? 426  ALA B O     1 
ATOM   6817 C CB    . ALA B 1 384 ? 38.300  10.579  30.027 1.00 14.44  ? 426  ALA B CB    1 
ATOM   6818 N N     . ALA B 1 385 ? 38.168  8.656   27.602 1.00 11.56  ? 427  ALA B N     1 
ATOM   6819 C CA    . ALA B 1 385 ? 38.569  8.277   26.248 1.00 12.16  ? 427  ALA B CA    1 
ATOM   6820 C C     . ALA B 1 385 ? 39.185  9.500   25.534 1.00 13.29  ? 427  ALA B C     1 
ATOM   6821 O O     . ALA B 1 385 ? 38.621  10.022  24.574 1.00 13.13  ? 427  ALA B O     1 
ATOM   6822 C CB    . ALA B 1 385 ? 37.412  7.718   25.474 1.00 12.62  ? 427  ALA B CB    1 
ATOM   6823 N N     . ARG B 1 386 ? 40.361  9.892   26.028 1.00 14.17  ? 428  ARG B N     1 
ATOM   6824 C CA    . ARG B 1 386 ? 41.141  10.989  25.481 1.00 14.49  ? 428  ARG B CA    1 
ATOM   6825 C C     . ARG B 1 386 ? 42.566  10.476  25.205 1.00 14.99  ? 428  ARG B C     1 
ATOM   6826 O O     . ARG B 1 386 ? 43.207  9.877   26.069 1.00 12.97  ? 428  ARG B O     1 
ATOM   6827 C CB    . ARG B 1 386 ? 41.187  12.174  26.445 1.00 16.24  ? 428  ARG B CB    1 
ATOM   6828 C CG    . ARG B 1 386 ? 39.827  12.762  26.818 1.00 17.40  ? 428  ARG B CG    1 
ATOM   6829 C CD    . ARG B 1 386 ? 39.989  13.981  27.703 1.00 18.71  ? 428  ARG B CD    1 
ATOM   6830 N NE    . ARG B 1 386 ? 38.693  14.485  28.167 1.00 21.52  ? 428  ARG B NE    1 
ATOM   6831 C CZ    . ARG B 1 386 ? 38.237  14.386  29.418 1.00 19.78  ? 428  ARG B CZ    1 
ATOM   6832 N NH1   . ARG B 1 386 ? 38.992  13.933  30.392 1.00 21.50  ? 428  ARG B NH1   1 
ATOM   6833 N NH2   . ARG B 1 386 ? 37.036  14.838  29.715 1.00 21.90  ? 428  ARG B NH2   1 
ATOM   6834 N N     . GLY B 1 387 ? 43.071  10.761  23.990 1.00 14.74  ? 429  GLY B N     1 
ATOM   6835 C CA    . GLY B 1 387 ? 44.401  10.325  23.608 1.00 14.40  ? 429  GLY B CA    1 
ATOM   6836 C C     . GLY B 1 387 ? 45.472  10.719  24.619 1.00 14.28  ? 429  GLY B C     1 
ATOM   6837 O O     . GLY B 1 387 ? 46.375  9.928   24.918 1.00 15.26  ? 429  GLY B O     1 
ATOM   6838 N N     . VAL B 1 388 ? 45.437  11.980  25.104 1.00 15.71  ? 430  VAL B N     1 
ATOM   6839 C CA    . VAL B 1 388 ? 46.485  12.446  26.003 1.00 17.36  ? 430  VAL B CA    1 
ATOM   6840 C C     . VAL B 1 388 ? 46.524  11.616  27.296 1.00 16.67  ? 430  VAL B C     1 
ATOM   6841 O O     . VAL B 1 388 ? 47.580  11.400  27.904 1.00 16.06  ? 430  VAL B O     1 
ATOM   6842 C CB    . VAL B 1 388 ? 46.363  13.947  26.332 1.00 21.01  ? 430  VAL B CB    1 
ATOM   6843 C CG1   . VAL B 1 388 ? 45.080  14.309  27.067 1.00 23.32  ? 430  VAL B CG1   1 
ATOM   6844 C CG2   . VAL B 1 388 ? 47.542  14.439  27.156 1.00 24.68  ? 430  VAL B CG2   1 
ATOM   6845 N N     . GLU B 1 389 ? 45.357  11.173  27.787 1.00 16.82  ? 431  GLU B N     1 
ATOM   6846 C CA    . GLU B 1 389 ? 45.350  10.388  29.015 1.00 15.33  ? 431  GLU B CA    1 
ATOM   6847 C C     . GLU B 1 389 ? 45.976  9.015   28.800 1.00 14.22  ? 431  GLU B C     1 
ATOM   6848 O O     . GLU B 1 389 ? 46.727  8.559   29.670 1.00 14.62  ? 431  GLU B O     1 
ATOM   6849 C CB    . GLU B 1 389 ? 43.922  10.185  29.554 1.00 18.53  ? 431  GLU B CB    1 
ATOM   6850 C CG    . GLU B 1 389 ? 43.305  11.492  29.976 1.00 23.33  ? 431  GLU B CG    1 
ATOM   6851 C CD    . GLU B 1 389 ? 42.032  11.448  30.811 1.00 31.02  ? 431  GLU B CD    1 
ATOM   6852 O OE1   . GLU B 1 389 ? 41.738  10.384  31.445 1.00 29.68  ? 431  GLU B OE1   1 
ATOM   6853 O OE2   . GLU B 1 389 ? 41.327  12.515  30.827 1.00 30.63  ? 431  GLU B OE2   1 
ATOM   6854 N N     . ALA B 1 390 ? 45.641  8.368   27.676 1.00 13.69  ? 432  ALA B N     1 
ATOM   6855 C CA    . ALA B 1 390 ? 46.236  7.051   27.365 1.00 14.51  ? 432  ALA B CA    1 
ATOM   6856 C C     . ALA B 1 390 ? 47.747  7.207   27.184 1.00 14.99  ? 432  ALA B C     1 
ATOM   6857 O O     . ALA B 1 390 ? 48.546  6.433   27.705 1.00 14.59  ? 432  ALA B O     1 
ATOM   6858 C CB    . ALA B 1 390 ? 45.598  6.487   26.130 1.00 15.09  ? 432  ALA B CB    1 
ATOM   6859 N N     . GLU B 1 391 ? 48.165  8.286   26.502 1.00 16.49  ? 433  GLU B N     1 
ATOM   6860 C CA    . GLU B 1 391 ? 49.591  8.513   26.292 1.00 15.54  ? 433  GLU B CA    1 
ATOM   6861 C C     . GLU B 1 391 ? 50.324  8.609   27.620 1.00 15.84  ? 433  GLU B C     1 
ATOM   6862 O O     . GLU B 1 391 ? 51.384  7.982   27.838 1.00 15.66  ? 433  GLU B O     1 
ATOM   6863 C CB    . GLU B 1 391 ? 49.779  9.792   25.466 1.00 17.63  ? 433  GLU B CB    1 
ATOM   6864 C CG    . GLU B 1 391 ? 51.215  10.154  25.156 1.00 20.86  ? 433  GLU B CG    1 
ATOM   6865 C CD    . GLU B 1 391 ? 51.262  11.282  24.117 1.00 27.21  ? 433  GLU B CD    1 
ATOM   6866 O OE1   . GLU B 1 391 ? 50.523  12.283  24.285 1.00 30.62  ? 433  GLU B OE1   1 
ATOM   6867 O OE2   . GLU B 1 391 ? 51.990  11.133  23.111 1.00 37.48  ? 433  GLU B OE2   1 
ATOM   6868 N N     . ARG B 1 392 ? 49.759  9.399   28.548 1.00 14.08  ? 434  ARG B N     1 
ATOM   6869 C CA    . ARG B 1 392 ? 50.392  9.623   29.830 1.00 13.45  ? 434  ARG B CA    1 
ATOM   6870 C C     . ARG B 1 392 ? 50.351  8.377   30.727 1.00 13.51  ? 434  ARG B C     1 
ATOM   6871 O O     . ARG B 1 392 ? 51.336  8.099   31.426 1.00 13.28  ? 434  ARG B O     1 
ATOM   6872 C CB    . ARG B 1 392 ? 49.769  10.823  30.558 1.00 16.40  ? 434  ARG B CB    1 
ATOM   6873 C CG    . ARG B 1 392 ? 50.037  12.193  29.929 1.00 19.38  ? 434  ARG B CG    1 
ATOM   6874 C CD    . ARG B 1 392 ? 49.303  13.278  30.724 1.00 20.87  ? 434  ARG B CD    1 
ATOM   6875 N NE    . ARG B 1 392 ? 49.843  13.358  32.086 1.00 25.91  ? 434  ARG B NE    1 
ATOM   6876 C CZ    . ARG B 1 392 ? 49.184  13.509  33.240 1.00 27.47  ? 434  ARG B CZ    1 
ATOM   6877 N NH1   . ARG B 1 392 ? 47.923  13.870  33.251 1.00 26.63  ? 434  ARG B NH1   1 
ATOM   6878 N NH2   . ARG B 1 392 ? 49.845  13.383  34.387 1.00 31.06  ? 434  ARG B NH2   1 
ATOM   6879 N N     . GLN B 1 393 ? 49.262  7.612   30.680 1.00 12.55  ? 435  GLN B N     1 
ATOM   6880 C CA    . GLN B 1 393 ? 49.167  6.397   31.503 1.00 12.73  ? 435  GLN B CA    1 
ATOM   6881 C C     . GLN B 1 393 ? 50.106  5.306   30.995 1.00 12.41  ? 435  GLN B C     1 
ATOM   6882 O O     . GLN B 1 393 ? 50.764  4.665   31.784 1.00 13.88  ? 435  GLN B O     1 
ATOM   6883 C CB    . GLN B 1 393 ? 47.755  5.819   31.547 1.00 13.01  ? 435  GLN B CB    1 
ATOM   6884 C CG    . GLN B 1 393 ? 46.789  6.656   32.353 1.00 13.87  ? 435  GLN B CG    1 
ATOM   6885 C CD    . GLN B 1 393 ? 45.541  5.880   32.708 1.00 12.59  ? 435  GLN B CD    1 
ATOM   6886 O OE1   . GLN B 1 393 ? 45.400  4.708   32.367 1.00 14.78  ? 435  GLN B OE1   1 
ATOM   6887 N NE2   . GLN B 1 393 ? 44.587  6.534   33.364 1.00 12.76  ? 435  GLN B NE2   1 
ATOM   6888 N N     . THR B 1 394 ? 50.219  5.170   29.694 1.00 13.55  ? 436  THR B N     1 
ATOM   6889 C CA    . THR B 1 394 ? 51.160  4.207   29.139 1.00 12.96  ? 436  THR B CA    1 
ATOM   6890 C C     . THR B 1 394 ? 52.582  4.588   29.534 1.00 13.69  ? 436  THR B C     1 
ATOM   6891 O O     . THR B 1 394 ? 53.349  3.725   29.993 1.00 15.27  ? 436  THR B O     1 
ATOM   6892 C CB    . THR B 1 394 ? 50.950  4.080   27.634 1.00 15.55  ? 436  THR B CB    1 
ATOM   6893 O OG1   . THR B 1 394 ? 49.763  3.337   27.338 1.00 13.82  ? 436  THR B OG1   1 
ATOM   6894 C CG2   . THR B 1 394 ? 52.100  3.366   26.949 1.00 16.30  ? 436  THR B CG2   1 
ATOM   6895 N N     . ALA B 1 395 ? 52.944  5.893   29.423 1.00 15.14  ? 437  ALA B N     1 
ATOM   6896 C CA    . ALA B 1 395 ? 54.290  6.331   29.783 1.00 14.70  ? 437  ALA B CA    1 
ATOM   6897 C C     . ALA B 1 395 ? 54.586  6.069   31.248 1.00 15.42  ? 437  ALA B C     1 
ATOM   6898 O O     . ALA B 1 395 ? 55.678  5.604   31.634 1.00 16.86  ? 437  ALA B O     1 
ATOM   6899 C CB    . ALA B 1 395 ? 54.472  7.788   29.423 1.00 15.26  ? 437  ALA B CB    1 
ATOM   6900 N N     . LEU B 1 396 ? 53.610  6.355   32.135 1.00 14.02  ? 438  LEU B N     1 
ATOM   6901 C CA    . LEU B 1 396 ? 53.862  6.194   33.546 1.00 14.41  ? 438  LEU B CA    1 
ATOM   6902 C C     . LEU B 1 396 ? 53.968  4.709   33.917 1.00 13.19  ? 438  LEU B C     1 
ATOM   6903 O O     . LEU B 1 396 ? 54.845  4.331   34.689 1.00 13.52  ? 438  LEU B O     1 
ATOM   6904 C CB    . LEU B 1 396 ? 52.778  6.899   34.385 1.00 15.37  ? 438  LEU B CB    1 
ATOM   6905 C CG    . LEU B 1 396 ? 52.985  6.826   35.891 1.00 16.70  ? 438  LEU B CG    1 
ATOM   6906 C CD1   . LEU B 1 396 ? 54.329  7.391   36.356 1.00 16.77  ? 438  LEU B CD1   1 
ATOM   6907 C CD2   . LEU B 1 396 ? 51.885  7.592   36.621 1.00 16.31  ? 438  LEU B CD2   1 
ATOM   6908 N N     . ALA B 1 397 ? 53.068  3.882   33.386 1.00 13.12  ? 439  ALA B N     1 
ATOM   6909 C CA    . ALA B 1 397 ? 53.073  2.461   33.712 1.00 13.08  ? 439  ALA B CA    1 
ATOM   6910 C C     . ALA B 1 397 ? 54.364  1.808   33.217 1.00 14.07  ? 439  ALA B C     1 
ATOM   6911 O O     . ALA B 1 397 ? 54.984  1.065   33.936 1.00 13.17  ? 439  ALA B O     1 
ATOM   6912 C CB    . ALA B 1 397 ? 51.873  1.755   33.099 1.00 14.82  ? 439  ALA B CB    1 
ATOM   6913 N N     . LYS B 1 398 ? 54.783  2.145   31.994 1.00 16.52  ? 440  LYS B N     1 
ATOM   6914 C CA    . LYS B 1 398 ? 56.063  1.680   31.452 1.00 18.63  ? 440  LYS B CA    1 
ATOM   6915 C C     . LYS B 1 398 ? 57.244  2.040   32.350 1.00 16.75  ? 440  LYS B C     1 
ATOM   6916 O O     . LYS B 1 398 ? 58.097  1.193   32.664 1.00 17.86  ? 440  LYS B O     1 
ATOM   6917 C CB    . LYS B 1 398 ? 56.336  2.304   30.077 1.00 23.31  ? 440  LYS B CB    1 
ATOM   6918 C CG    . LYS B 1 398 ? 55.586  1.711   28.916 1.00 29.71  ? 440  LYS B CG    1 
ATOM   6919 C CD    . LYS B 1 398 ? 56.062  2.212   27.546 1.00 34.93  ? 440  LYS B CD    1 
ATOM   6920 C CE    . LYS B 1 398 ? 57.541  2.002   27.338 1.00 42.10  ? 440  LYS B CE    1 
ATOM   6921 N NZ    . LYS B 1 398 ? 57.896  2.181   25.914 1.00 59.74  ? 440  LYS B NZ    1 
ATOM   6922 N N     . GLU B 1 399 ? 57.332  3.310   32.742 1.00 16.15  ? 441  GLU B N     1 
ATOM   6923 C CA    . GLU B 1 399 ? 58.356  3.770   33.649 1.00 16.44  ? 441  GLU B CA    1 
ATOM   6924 C C     . GLU B 1 399 ? 58.390  2.896   34.898 1.00 15.96  ? 441  GLU B C     1 
ATOM   6925 O O     . GLU B 1 399 ? 59.472  2.495   35.333 1.00 18.58  ? 441  GLU B O     1 
ATOM   6926 C CB    . GLU B 1 399 ? 58.171  5.244   33.998 1.00 19.69  ? 441  GLU B CB    1 
ATOM   6927 C CG    . GLU B 1 399 ? 59.165  5.757   35.018 1.00 24.16  ? 441  GLU B CG    1 
ATOM   6928 C CD    . GLU B 1 399 ? 58.879  7.193   35.439 1.00 29.97  ? 441  GLU B CD    1 
ATOM   6929 O OE1   . GLU B 1 399 ? 58.225  7.928   34.659 1.00 33.14  ? 441  GLU B OE1   1 
ATOM   6930 O OE2   . GLU B 1 399 ? 59.231  7.535   36.568 1.00 32.56  ? 441  GLU B OE2   1 
ATOM   6931 N N     . ILE B 1 400 ? 57.225  2.677   35.518 1.00 13.48  ? 442  ILE B N     1 
ATOM   6932 C CA    . ILE B 1 400 ? 57.196  2.007   36.796 1.00 14.20  ? 442  ILE B CA    1 
ATOM   6933 C C     . ILE B 1 400 ? 57.537  0.532   36.644 1.00 13.69  ? 442  ILE B C     1 
ATOM   6934 O O     . ILE B 1 400 ? 58.325  0.026   37.422 1.00 15.46  ? 442  ILE B O     1 
ATOM   6935 C CB    . ILE B 1 400 ? 55.852  2.226   37.513 1.00 13.86  ? 442  ILE B CB    1 
ATOM   6936 C CG1   . ILE B 1 400 ? 55.683  3.706   37.859 1.00 12.81  ? 442  ILE B CG1   1 
ATOM   6937 C CG2   . ILE B 1 400 ? 55.723  1.334   38.731 1.00 14.32  ? 442  ILE B CG2   1 
ATOM   6938 C CD1   . ILE B 1 400 ? 54.255  4.078   38.260 1.00 13.71  ? 442  ILE B CD1   1 
ATOM   6939 N N     . VAL B 1 401 ? 56.916  -0.181  35.700 1.00 13.28  ? 443  VAL B N     1 
ATOM   6940 C CA    . VAL B 1 401 ? 57.193  -1.619  35.610 1.00 14.18  ? 443  VAL B CA    1 
ATOM   6941 C C     . VAL B 1 401 ? 58.677  -1.829  35.241 1.00 14.91  ? 443  VAL B C     1 
ATOM   6942 O O     . VAL B 1 401 ? 59.305  -2.742  35.760 1.00 14.05  ? 443  VAL B O     1 
ATOM   6943 C CB    . VAL B 1 401 ? 56.251  -2.344  34.656 1.00 13.25  ? 443  VAL B CB    1 
ATOM   6944 C CG1   . VAL B 1 401 ? 54.803  -2.203  35.133 1.00 13.37  ? 443  VAL B CG1   1 
ATOM   6945 C CG2   . VAL B 1 401 ? 56.419  -1.906  33.201 1.00 12.15  ? 443  VAL B CG2   1 
ATOM   6946 N N     . GLU B 1 402 ? 59.235  -0.966  34.413 1.00 17.32  ? 444  GLU B N     1 
ATOM   6947 C CA    . GLU B 1 402 ? 60.618  -1.191  33.955 1.00 18.49  ? 444  GLU B CA    1 
ATOM   6948 C C     . GLU B 1 402 ? 61.598  -0.869  35.083 1.00 19.20  ? 444  GLU B C     1 
ATOM   6949 O O     . GLU B 1 402 ? 62.578  -1.580  35.260 1.00 19.16  ? 444  GLU B O     1 
ATOM   6950 C CB    . GLU B 1 402 ? 60.865  -0.471  32.630 1.00 20.12  ? 444  GLU B CB    1 
ATOM   6951 C CG    . GLU B 1 402 ? 60.102  -1.090  31.462 1.00 23.73  ? 444  GLU B CG    1 
ATOM   6952 C CD    . GLU B 1 402 ? 60.208  -0.316  30.160 1.00 31.51  ? 444  GLU B CD    1 
ATOM   6953 O OE1   . GLU B 1 402 ? 61.019  0.611   30.108 1.00 32.47  ? 444  GLU B OE1   1 
ATOM   6954 O OE2   . GLU B 1 402 ? 59.381  -0.553  29.243 1.00 40.98  ? 444  GLU B OE2   1 
ATOM   6955 N N     . LYS B 1 403 ? 61.306  0.150   35.907 1.00 18.55  ? 445  LYS B N     1 
ATOM   6956 C CA    . LYS B 1 403 ? 62.077  0.433   37.109 1.00 20.27  ? 445  LYS B CA    1 
ATOM   6957 C C     . LYS B 1 403 ? 62.266  -0.801  37.999 1.00 21.18  ? 445  LYS B C     1 
ATOM   6958 O O     . LYS B 1 403 ? 63.336  -0.945  38.628 1.00 18.21  ? 445  LYS B O     1 
ATOM   6959 C CB    . LYS B 1 403 ? 61.373  1.567   37.867 1.00 23.71  ? 445  LYS B CB    1 
ATOM   6960 C CG    . LYS B 1 403 ? 61.812  1.812   39.301 1.00 29.26  ? 445  LYS B CG    1 
ATOM   6961 C CD    . LYS B 1 403 ? 61.121  3.022   39.895 1.00 27.97  ? 445  LYS B CD    1 
ATOM   6962 C CE    . LYS B 1 403 ? 61.434  3.157   41.360 1.00 30.57  ? 445  LYS B CE    1 
ATOM   6963 N NZ    . LYS B 1 403 ? 60.758  4.355   41.903 1.00 32.07  ? 445  LYS B NZ    1 
ATOM   6964 N N     . HIS B 1 404 ? 61.203  -1.631  38.130 1.00 16.74  ? 446  HIS B N     1 
ATOM   6965 C CA    . HIS B 1 404 ? 61.189  -2.790  39.001 1.00 16.98  ? 446  HIS B CA    1 
ATOM   6966 C C     . HIS B 1 404 ? 61.645  -4.056  38.276 1.00 14.08  ? 446  HIS B C     1 
ATOM   6967 O O     . HIS B 1 404 ? 61.674  -5.115  38.864 1.00 17.73  ? 446  HIS B O     1 
ATOM   6968 C CB    . HIS B 1 404 ? 59.803  -2.981  39.642 1.00 16.65  ? 446  HIS B CB    1 
ATOM   6969 C CG    . HIS B 1 404 ? 59.504  -1.974  40.700 1.00 16.76  ? 446  HIS B CG    1 
ATOM   6970 N ND1   . HIS B 1 404 ? 58.967  -0.718  40.505 1.00 19.31  ? 446  HIS B ND1   1 
ATOM   6971 C CD2   . HIS B 1 404 ? 59.742  -2.084  42.018 1.00 15.66  ? 446  HIS B CD2   1 
ATOM   6972 C CE1   . HIS B 1 404 ? 58.879  -0.104  41.680 1.00 15.52  ? 446  HIS B CE1   1 
ATOM   6973 N NE2   . HIS B 1 404 ? 59.366  -0.906  42.601 1.00 21.59  ? 446  HIS B NE2   1 
ATOM   6974 N N     . GLY B 1 405 ? 62.006  -3.961  37.005 1.00 14.99  ? 447  GLY B N     1 
ATOM   6975 C CA    . GLY B 1 405 ? 62.536  -5.080  36.268 1.00 16.10  ? 447  GLY B CA    1 
ATOM   6976 C C     . GLY B 1 405 ? 61.491  -5.886  35.506 1.00 14.31  ? 447  GLY B C     1 
ATOM   6977 O O     . GLY B 1 405 ? 61.804  -6.988  35.065 1.00 16.09  ? 447  GLY B O     1 
ATOM   6978 N N     . PHE B 1 406 ? 60.313  -5.321  35.268 1.00 13.81  ? 448  PHE B N     1 
ATOM   6979 C CA    . PHE B 1 406 ? 59.221  -5.994  34.569 1.00 12.30  ? 448  PHE B CA    1 
ATOM   6980 C C     . PHE B 1 406 ? 58.905  -5.295  33.256 1.00 13.89  ? 448  PHE B C     1 
ATOM   6981 O O     . PHE B 1 406 ? 59.442  -4.235  32.968 1.00 16.21  ? 448  PHE B O     1 
ATOM   6982 C CB    . PHE B 1 406 ? 57.972  -6.062  35.460 1.00 13.40  ? 448  PHE B CB    1 
ATOM   6983 C CG    . PHE B 1 406 ? 58.228  -6.803  36.737 1.00 14.18  ? 448  PHE B CG    1 
ATOM   6984 C CD1   . PHE B 1 406 ? 58.500  -8.162  36.724 1.00 14.59  ? 448  PHE B CD1   1 
ATOM   6985 C CD2   . PHE B 1 406 ? 58.340  -6.118  37.924 1.00 12.54  ? 448  PHE B CD2   1 
ATOM   6986 C CE1   . PHE B 1 406 ? 58.779  -8.827  37.912 1.00 14.53  ? 448  PHE B CE1   1 
ATOM   6987 C CE2   . PHE B 1 406 ? 58.617  -6.794  39.104 1.00 14.34  ? 448  PHE B CE2   1 
ATOM   6988 C CZ    . PHE B 1 406 ? 58.871  -8.145  39.092 1.00 13.65  ? 448  PHE B CZ    1 
ATOM   6989 N N     . ASP B 1 407 ? 58.078  -5.932  32.428 1.00 12.76  ? 449  ASP B N     1 
ATOM   6990 C CA    . ASP B 1 407 ? 57.714  -5.437  31.118 1.00 13.68  ? 449  ASP B CA    1 
ATOM   6991 C C     . ASP B 1 407 ? 56.336  -4.763  31.142 1.00 12.03  ? 449  ASP B C     1 
ATOM   6992 O O     . ASP B 1 407 ? 55.501  -5.108  31.963 1.00 12.27  ? 449  ASP B O     1 
ATOM   6993 C CB    . ASP B 1 407 ? 57.694  -6.529  30.068 1.00 13.69  ? 449  ASP B CB    1 
ATOM   6994 C CG    . ASP B 1 407 ? 58.987  -7.334  29.964 1.00 17.04  ? 449  ASP B CG    1 
ATOM   6995 O OD1   . ASP B 1 407 ? 60.076  -6.726  30.087 1.00 15.91  ? 449  ASP B OD1   1 
ATOM   6996 O OD2   . ASP B 1 407 ? 58.853  -8.571  29.801 1.00 16.51  ? 449  ASP B OD2   1 
ATOM   6997 N N     . TYR B 1 408 ? 56.133  -3.848  30.196 1.00 12.19  ? 450  TYR B N     1 
ATOM   6998 C CA    . TYR B 1 408 ? 54.812  -3.332  29.875 1.00 12.36  ? 450  TYR B CA    1 
ATOM   6999 C C     . TYR B 1 408 ? 54.086  -4.244  28.895 1.00 12.19  ? 450  TYR B C     1 
ATOM   7000 O O     . TYR B 1 408 ? 54.462  -4.303  27.745 1.00 14.24  ? 450  TYR B O     1 
ATOM   7001 C CB    . TYR B 1 408 ? 54.885  -1.904  29.343 1.00 13.04  ? 450  TYR B CB    1 
ATOM   7002 C CG    . TYR B 1 408 ? 53.554  -1.268  29.059 1.00 12.58  ? 450  TYR B CG    1 
ATOM   7003 C CD1   . TYR B 1 408 ? 52.702  -0.885  30.078 1.00 12.00  ? 450  TYR B CD1   1 
ATOM   7004 C CD2   . TYR B 1 408 ? 53.158  -0.999  27.755 1.00 13.72  ? 450  TYR B CD2   1 
ATOM   7005 C CE1   . TYR B 1 408 ? 51.513  -0.235  29.797 1.00 12.87  ? 450  TYR B CE1   1 
ATOM   7006 C CE2   . TYR B 1 408 ? 51.934  -0.405  27.442 1.00 14.37  ? 450  TYR B CE2   1 
ATOM   7007 C CZ    . TYR B 1 408 ? 51.108  0.013   28.482 1.00 14.17  ? 450  TYR B CZ    1 
ATOM   7008 O OH    . TYR B 1 408 ? 49.924  0.670   28.157 1.00 13.45  ? 450  TYR B OH    1 
ATOM   7009 N N     . THR B 1 409 ? 53.049  -4.921  29.408 1.00 12.12  ? 451  THR B N     1 
ATOM   7010 C CA    . THR B 1 409 ? 52.195  -5.835  28.667 1.00 12.56  ? 451  THR B CA    1 
ATOM   7011 C C     . THR B 1 409 ? 50.757  -5.463  28.988 1.00 11.82  ? 451  THR B C     1 
ATOM   7012 O O     . THR B 1 409 ? 50.281  -5.721  30.103 1.00 12.31  ? 451  THR B O     1 
ATOM   7013 C CB    . THR B 1 409 ? 52.497  -7.305  29.027 1.00 13.23  ? 451  THR B CB    1 
ATOM   7014 O OG1   . THR B 1 409 ? 52.569  -7.487  30.428 1.00 13.19  ? 451  THR B OG1   1 
ATOM   7015 C CG2   . THR B 1 409 ? 53.795  -7.820  28.459 1.00 15.47  ? 451  THR B CG2   1 
ATOM   7016 N N     . ALA B 1 410 ? 50.072  -4.848  28.033 1.00 10.43  ? 452  ALA B N     1 
ATOM   7017 C CA    . ALA B 1 410 ? 48.836  -4.170  28.325 1.00 11.55  ? 452  ALA B CA    1 
ATOM   7018 C C     . ALA B 1 410 ? 47.886  -4.149  27.142 1.00 13.12  ? 452  ALA B C     1 
ATOM   7019 O O     . ALA B 1 410 ? 48.241  -4.385  25.981 1.00 13.57  ? 452  ALA B O     1 
ATOM   7020 C CB    . ALA B 1 410 ? 49.122  -2.767  28.777 1.00 13.09  ? 452  ALA B CB    1 
ATOM   7021 N N     . ALA B 1 411 ? 46.628  -3.811  27.463 1.00 12.89  ? 453  ALA B N     1 
ATOM   7022 C CA    . ALA B 1 411 ? 45.641  -3.494  26.448 1.00 12.22  ? 453  ALA B CA    1 
ATOM   7023 C C     . ALA B 1 411 ? 44.778  -2.378  27.000 1.00 14.44  ? 453  ALA B C     1 
ATOM   7024 O O     . ALA B 1 411 ? 44.692  -2.218  28.196 1.00 13.67  ? 453  ALA B O     1 
ATOM   7025 C CB    . ALA B 1 411 ? 44.752  -4.644  26.158 1.00 14.31  ? 453  ALA B CB    1 
ATOM   7026 N N     . TYR B 1 412 ? 44.093  -1.661  26.103 1.00 12.85  ? 454  TYR B N     1 
ATOM   7027 C CA    . TYR B 1 412 ? 43.009  -0.779  26.474 1.00 13.13  ? 454  TYR B CA    1 
ATOM   7028 C C     . TYR B 1 412 ? 41.712  -1.409  25.994 1.00 13.31  ? 454  TYR B C     1 
ATOM   7029 O O     . TYR B 1 412 ? 41.609  -1.809  24.827 1.00 14.17  ? 454  TYR B O     1 
ATOM   7030 C CB    . TYR B 1 412 ? 43.192  0.576   25.795 1.00 13.47  ? 454  TYR B CB    1 
ATOM   7031 C CG    . TYR B 1 412 ? 44.258  1.435   26.427 1.00 13.12  ? 454  TYR B CG    1 
ATOM   7032 C CD1   . TYR B 1 412 ? 43.943  2.311   27.456 1.00 12.75  ? 454  TYR B CD1   1 
ATOM   7033 C CD2   . TYR B 1 412 ? 45.575  1.429   25.982 1.00 13.03  ? 454  TYR B CD2   1 
ATOM   7034 C CE1   . TYR B 1 412 ? 44.904  3.134   28.022 1.00 11.87  ? 454  TYR B CE1   1 
ATOM   7035 C CE2   . TYR B 1 412 ? 46.559  2.208   26.588 1.00 13.34  ? 454  TYR B CE2   1 
ATOM   7036 C CZ    . TYR B 1 412 ? 46.199  3.151   27.534 1.00 12.18  ? 454  TYR B CZ    1 
ATOM   7037 O OH    . TYR B 1 412 ? 47.147  3.911   28.149 1.00 14.72  ? 454  TYR B OH    1 
ATOM   7038 N N     . ALA B 1 413 ? 40.719  -1.528  26.901 1.00 12.99  ? 455  ALA B N     1 
ATOM   7039 C CA    . ALA B 1 413 ? 39.376  -1.869  26.502 1.00 12.86  ? 455  ALA B CA    1 
ATOM   7040 C C     . ALA B 1 413 ? 38.624  -0.555  26.333 1.00 13.17  ? 455  ALA B C     1 
ATOM   7041 O O     . ALA B 1 413 ? 38.323  0.155   27.307 1.00 14.11  ? 455  ALA B O     1 
ATOM   7042 C CB    . ALA B 1 413 ? 38.727  -2.741  27.559 1.00 13.18  ? 455  ALA B CB    1 
ATOM   7043 N N     . ILE B 1 414 ? 38.382  -0.217  25.071 1.00 14.32  ? 456  ILE B N     1 
ATOM   7044 C CA    . ILE B 1 414 ? 37.765  1.051   24.726 1.00 14.40  ? 456  ILE B CA    1 
ATOM   7045 C C     . ILE B 1 414 ? 36.258  0.925   24.900 1.00 13.09  ? 456  ILE B C     1 
ATOM   7046 O O     . ILE B 1 414 ? 35.619  0.086   24.261 1.00 14.84  ? 456  ILE B O     1 
ATOM   7047 C CB    . ILE B 1 414 ? 38.121  1.446   23.282 1.00 14.91  ? 456  ILE B CB    1 
ATOM   7048 C CG1   . ILE B 1 414 ? 39.637  1.476   23.066 1.00 15.22  ? 456  ILE B CG1   1 
ATOM   7049 C CG2   . ILE B 1 414 ? 37.483  2.801   22.953 1.00 15.71  ? 456  ILE B CG2   1 
ATOM   7050 C CD1   . ILE B 1 414 ? 40.087  1.751   21.625 1.00 17.41  ? 456  ILE B CD1   1 
ATOM   7051 N N     . GLY B 1 415 ? 35.711  1.813   25.741 1.00 12.44  ? 457  GLY B N     1 
ATOM   7052 C CA    . GLY B 1 415 ? 34.285  1.923   25.991 1.00 13.24  ? 457  GLY B CA    1 
ATOM   7053 C C     . GLY B 1 415 ? 33.657  3.132   25.307 1.00 15.03  ? 457  GLY B C     1 
ATOM   7054 O O     . GLY B 1 415 ? 34.220  3.684   24.363 1.00 15.61  ? 457  GLY B O     1 
ATOM   7055 N N     . TRP B 1 416 ? 32.447  3.474   25.753 1.00 14.35  ? 458  TRP B N     1 
ATOM   7056 C CA    . TRP B 1 416 ? 31.673  4.530   25.134 1.00 15.48  ? 458  TRP B CA    1 
ATOM   7057 C C     . TRP B 1 416 ? 32.374  5.884   25.305 1.00 15.54  ? 458  TRP B C     1 
ATOM   7058 O O     . TRP B 1 416 ? 32.653  6.550   24.312 1.00 17.93  ? 458  TRP B O     1 
ATOM   7059 C CB    . TRP B 1 416 ? 30.268  4.549   25.782 1.00 17.44  ? 458  TRP B CB    1 
ATOM   7060 C CG    . TRP B 1 416 ? 29.211  5.120   24.889 1.00 19.90  ? 458  TRP B CG    1 
ATOM   7061 C CD1   . TRP B 1 416 ? 29.370  5.892   23.769 1.00 21.49  ? 458  TRP B CD1   1 
ATOM   7062 C CD2   . TRP B 1 416 ? 27.800  4.947   25.043 1.00 19.61  ? 458  TRP B CD2   1 
ATOM   7063 N NE1   . TRP B 1 416 ? 28.149  6.160   23.185 1.00 19.89  ? 458  TRP B NE1   1 
ATOM   7064 C CE2   . TRP B 1 416 ? 27.167  5.619   23.976 1.00 20.03  ? 458  TRP B CE2   1 
ATOM   7065 C CE3   . TRP B 1 416 ? 27.027  4.216   25.952 1.00 26.36  ? 458  TRP B CE3   1 
ATOM   7066 C CZ2   . TRP B 1 416 ? 25.785  5.579   23.782 1.00 23.47  ? 458  TRP B CZ2   1 
ATOM   7067 C CZ3   . TRP B 1 416 ? 25.654  4.229   25.791 1.00 29.39  ? 458  TRP B CZ3   1 
ATOM   7068 C CH2   . TRP B 1 416 ? 25.049  4.890   24.714 1.00 27.85  ? 458  TRP B CH2   1 
ATOM   7069 N N     . ARG B 1 417 ? 32.676  6.260   26.558 1.00 13.77  ? 459  ARG B N     1 
ATOM   7070 C CA    . ARG B 1 417 ? 33.369  7.489   26.883 1.00 13.11  ? 459  ARG B CA    1 
ATOM   7071 C C     . ARG B 1 417 ? 34.592  7.215   27.762 1.00 11.49  ? 459  ARG B C     1 
ATOM   7072 O O     . ARG B 1 417 ? 35.256  8.171   28.165 1.00 11.28  ? 459  ARG B O     1 
ATOM   7073 C CB    . ARG B 1 417 ? 32.399  8.437   27.601 1.00 14.06  ? 459  ARG B CB    1 
ATOM   7074 C CG    . ARG B 1 417 ? 31.328  8.927   26.636 1.00 16.74  ? 459  ARG B CG    1 
ATOM   7075 C CD    . ARG B 1 417 ? 30.099  9.494   27.217 1.00 16.70  ? 459  ARG B CD    1 
ATOM   7076 N NE    . ARG B 1 417 ? 29.360  10.229  26.238 1.00 15.43  ? 459  ARG B NE    1 
ATOM   7077 C CZ    . ARG B 1 417 ? 28.283  9.832   25.571 1.00 13.72  ? 459  ARG B CZ    1 
ATOM   7078 N NH1   . ARG B 1 417 ? 27.861  8.566   25.598 1.00 13.70  ? 459  ARG B NH1   1 
ATOM   7079 N NH2   . ARG B 1 417 ? 27.572  10.735  24.901 1.00 11.25  ? 459  ARG B NH2   1 
ATOM   7080 N N     . ASP B 1 418 ? 34.862  5.930   28.064 1.00 11.17  ? 460  ASP B N     1 
ATOM   7081 C CA    . ASP B 1 418 ? 35.915  5.547   28.980 1.00 12.64  ? 460  ASP B CA    1 
ATOM   7082 C C     . ASP B 1 418 ? 36.906  4.577   28.325 1.00 12.21  ? 460  ASP B C     1 
ATOM   7083 O O     . ASP B 1 418 ? 36.581  3.943   27.326 1.00 15.22  ? 460  ASP B O     1 
ATOM   7084 C CB    . ASP B 1 418 ? 35.351  4.812   30.206 1.00 14.63  ? 460  ASP B CB    1 
ATOM   7085 C CG    . ASP B 1 418 ? 34.968  3.363   29.910 1.00 20.15  ? 460  ASP B CG    1 
ATOM   7086 O OD1   . ASP B 1 418 ? 33.865  3.162   29.399 1.00 18.56  ? 460  ASP B OD1   1 
ATOM   7087 O OD2   . ASP B 1 418 ? 35.867  2.430   30.059 1.00 24.51  ? 460  ASP B OD2   1 
ATOM   7088 N N     . LEU B 1 419 ? 38.053  4.390   28.991 1.00 13.31  ? 461  LEU B N     1 
ATOM   7089 C CA    . LEU B 1 419 ? 38.947  3.271   28.701 1.00 12.53  ? 461  LEU B CA    1 
ATOM   7090 C C     . LEU B 1 419 ? 39.179  2.538   30.015 1.00 13.75  ? 461  LEU B C     1 
ATOM   7091 O O     . LEU B 1 419 ? 39.389  3.187   31.029 1.00 12.27  ? 461  LEU B O     1 
ATOM   7092 C CB    . LEU B 1 419 ? 40.301  3.760   28.222 1.00 12.18  ? 461  LEU B CB    1 
ATOM   7093 C CG    . LEU B 1 419 ? 40.299  4.894   27.191 1.00 14.37  ? 461  LEU B CG    1 
ATOM   7094 C CD1   . LEU B 1 419 ? 41.711  5.459   26.993 1.00 14.76  ? 461  LEU B CD1   1 
ATOM   7095 C CD2   . LEU B 1 419 ? 39.684  4.445   25.885 1.00 13.51  ? 461  LEU B CD2   1 
ATOM   7096 N N     . HIS B 1 420 ? 39.178  1.210   29.958 1.00 12.32  ? 462  HIS B N     1 
ATOM   7097 C CA    . HIS B 1 420 ? 39.794  0.377   30.985 1.00 14.16  ? 462  HIS B CA    1 
ATOM   7098 C C     . HIS B 1 420 ? 41.217  0.081   30.476 1.00 13.01  ? 462  HIS B C     1 
ATOM   7099 O O     . HIS B 1 420 ? 41.393  -0.639  29.490 1.00 13.30  ? 462  HIS B O     1 
ATOM   7100 C CB    . HIS B 1 420 ? 39.081  -0.969  31.204 1.00 13.60  ? 462  HIS B CB    1 
ATOM   7101 C CG    . HIS B 1 420 ? 37.654  -0.901  31.718 1.00 16.79  ? 462  HIS B CG    1 
ATOM   7102 N ND1   . HIS B 1 420 ? 36.690  -0.028  31.243 1.00 22.58  ? 462  HIS B ND1   1 
ATOM   7103 C CD2   . HIS B 1 420 ? 37.024  -1.634  32.665 1.00 15.03  ? 462  HIS B CD2   1 
ATOM   7104 C CE1   . HIS B 1 420 ? 35.530  -0.238  31.892 1.00 20.21  ? 462  HIS B CE1   1 
ATOM   7105 N NE2   . HIS B 1 420 ? 35.698  -1.266  32.713 1.00 14.57  ? 462  HIS B NE2   1 
ATOM   7106 N N     . HIS B 1 421 ? 42.212  0.626   31.155 1.00 11.59  ? 463  HIS B N     1 
ATOM   7107 C CA    . HIS B 1 421 ? 43.602  0.339   30.822 1.00 12.89  ? 463  HIS B CA    1 
ATOM   7108 C C     . HIS B 1 421 ? 44.061  -0.892  31.598 1.00 12.23  ? 463  HIS B C     1 
ATOM   7109 O O     . HIS B 1 421 ? 44.331  -0.794  32.815 1.00 13.26  ? 463  HIS B O     1 
ATOM   7110 C CB    . HIS B 1 421 ? 44.459  1.558   31.190 1.00 12.06  ? 463  HIS B CB    1 
ATOM   7111 C CG    . HIS B 1 421 ? 45.861  1.505   30.766 1.00 12.40  ? 463  HIS B CG    1 
ATOM   7112 N ND1   . HIS B 1 421 ? 46.734  2.522   31.107 1.00 14.09  ? 463  HIS B ND1   1 
ATOM   7113 C CD2   . HIS B 1 421 ? 46.585  0.591   30.063 1.00 14.17  ? 463  HIS B CD2   1 
ATOM   7114 C CE1   . HIS B 1 421 ? 47.965  2.249   30.571 1.00 13.87  ? 463  HIS B CE1   1 
ATOM   7115 N NE2   . HIS B 1 421 ? 47.893  1.089   29.931 1.00 12.72  ? 463  HIS B NE2   1 
ATOM   7116 N N     . ILE B 1 422 ? 44.123  -2.043  30.912 1.00 11.41  ? 464  ILE B N     1 
ATOM   7117 C CA    . ILE B 1 422 ? 44.416  -3.344  31.537 1.00 10.95  ? 464  ILE B CA    1 
ATOM   7118 C C     . ILE B 1 422 ? 45.905  -3.642  31.436 1.00 11.86  ? 464  ILE B C     1 
ATOM   7119 O O     . ILE B 1 422 ? 46.373  -3.961  30.368 1.00 13.37  ? 464  ILE B O     1 
ATOM   7120 C CB    . ILE B 1 422 ? 43.563  -4.476  30.934 1.00 11.55  ? 464  ILE B CB    1 
ATOM   7121 C CG1   . ILE B 1 422 ? 42.074  -4.129  30.943 1.00 11.69  ? 464  ILE B CG1   1 
ATOM   7122 C CG2   . ILE B 1 422 ? 43.853  -5.815  31.610 1.00 13.05  ? 464  ILE B CG2   1 
ATOM   7123 C CD1   . ILE B 1 422 ? 41.492  -3.819  32.299 1.00 13.67  ? 464  ILE B CD1   1 
ATOM   7124 N N     . ILE B 1 423 ? 46.595  -3.577  32.589 1.00 11.97  ? 465  ILE B N     1 
ATOM   7125 C CA    . ILE B 1 423 ? 48.032  -3.814  32.656 1.00 12.38  ? 465  ILE B CA    1 
ATOM   7126 C C     . ILE B 1 423 ? 48.315  -5.127  33.378 1.00 11.84  ? 465  ILE B C     1 
ATOM   7127 O O     . ILE B 1 423 ? 47.919  -5.291  34.530 1.00 11.81  ? 465  ILE B O     1 
ATOM   7128 C CB    . ILE B 1 423 ? 48.711  -2.626  33.346 1.00 13.12  ? 465  ILE B CB    1 
ATOM   7129 C CG1   . ILE B 1 423 ? 48.470  -1.333  32.572 1.00 13.25  ? 465  ILE B CG1   1 
ATOM   7130 C CG2   . ILE B 1 423 ? 50.201  -2.889  33.574 1.00 13.75  ? 465  ILE B CG2   1 
ATOM   7131 C CD1   . ILE B 1 423 ? 48.636  -0.100  33.431 1.00 13.09  ? 465  ILE B CD1   1 
ATOM   7132 N N     . ALA B 1 424 ? 48.825  -6.113  32.640 1.00 12.20  ? 466  ALA B N     1 
ATOM   7133 C CA    . ALA B 1 424 ? 49.202  -7.397  33.211 1.00 12.70  ? 466  ALA B CA    1 
ATOM   7134 C C     . ALA B 1 424 ? 50.612  -7.243  33.745 1.00 12.40  ? 466  ALA B C     1 
ATOM   7135 O O     . ALA B 1 424 ? 51.554  -7.004  32.959 1.00 12.37  ? 466  ALA B O     1 
ATOM   7136 C CB    . ALA B 1 424 ? 49.175  -8.497  32.177 1.00 14.93  ? 466  ALA B CB    1 
ATOM   7137 N N     . LEU B 1 425 ? 50.776  -7.387  35.055 1.00 11.68  ? 467  LEU B N     1 
ATOM   7138 C CA    . LEU B 1 425 ? 52.094  -7.440  35.690 1.00 12.21  ? 467  LEU B CA    1 
ATOM   7139 C C     . LEU B 1 425 ? 52.511  -8.910  35.776 1.00 12.32  ? 467  LEU B C     1 
ATOM   7140 O O     . LEU B 1 425 ? 51.971  -9.677  36.574 1.00 12.18  ? 467  LEU B O     1 
ATOM   7141 C CB    . LEU B 1 425 ? 52.091  -6.836  37.087 1.00 11.98  ? 467  LEU B CB    1 
ATOM   7142 C CG    . LEU B 1 425 ? 53.455  -6.794  37.745 1.00 13.31  ? 467  LEU B CG    1 
ATOM   7143 C CD1   . LEU B 1 425 ? 54.435  -5.987  36.908 1.00 14.68  ? 467  LEU B CD1   1 
ATOM   7144 C CD2   . LEU B 1 425 ? 53.337  -6.171  39.138 1.00 15.11  ? 467  LEU B CD2   1 
ATOM   7145 N N     . LEU B 1 426 ? 53.362  -9.315  34.833 1.00 11.55  ? 468  LEU B N     1 
ATOM   7146 C CA    . LEU B 1 426 ? 53.763  -10.700 34.670 1.00 12.72  ? 468  LEU B CA    1 
ATOM   7147 C C     . LEU B 1 426 ? 55.120  -10.929 35.335 1.00 14.89  ? 468  LEU B C     1 
ATOM   7148 O O     . LEU B 1 426 ? 56.063  -10.149 35.130 1.00 14.29  ? 468  LEU B O     1 
ATOM   7149 C CB    . LEU B 1 426 ? 53.871  -11.032 33.174 1.00 11.83  ? 468  LEU B CB    1 
ATOM   7150 C CG    . LEU B 1 426 ? 52.602  -10.812 32.342 1.00 12.83  ? 468  LEU B CG    1 
ATOM   7151 C CD1   . LEU B 1 426 ? 52.830  -11.102 30.866 1.00 14.50  ? 468  LEU B CD1   1 
ATOM   7152 C CD2   . LEU B 1 426 ? 51.504  -11.766 32.843 1.00 12.89  ? 468  LEU B CD2   1 
ATOM   7153 N N     . PHE B 1 427 ? 55.192  -11.991 36.161 1.00 13.24  ? 469  PHE B N     1 
ATOM   7154 C CA    . PHE B 1 427 ? 56.418  -12.249 36.894 1.00 12.71  ? 469  PHE B CA    1 
ATOM   7155 C C     . PHE B 1 427 ? 56.578  -13.746 37.163 1.00 12.40  ? 469  PHE B C     1 
ATOM   7156 O O     . PHE B 1 427 ? 55.656  -14.531 36.954 1.00 12.86  ? 469  PHE B O     1 
ATOM   7157 C CB    . PHE B 1 427 ? 56.442  -11.420 38.183 1.00 12.98  ? 469  PHE B CB    1 
ATOM   7158 C CG    . PHE B 1 427 ? 55.342  -11.718 39.172 1.00 12.25  ? 469  PHE B CG    1 
ATOM   7159 C CD1   . PHE B 1 427 ? 54.049  -11.219 39.007 1.00 11.52  ? 469  PHE B CD1   1 
ATOM   7160 C CD2   . PHE B 1 427 ? 55.589  -12.554 40.253 1.00 11.95  ? 469  PHE B CD2   1 
ATOM   7161 C CE1   . PHE B 1 427 ? 53.050  -11.528 39.911 1.00 10.91  ? 469  PHE B CE1   1 
ATOM   7162 C CE2   . PHE B 1 427 ? 54.580  -12.875 41.156 1.00 13.77  ? 469  PHE B CE2   1 
ATOM   7163 C CZ    . PHE B 1 427 ? 53.311  -12.363 40.975 1.00 12.70  ? 469  PHE B CZ    1 
ATOM   7164 N N     . ASP B 1 428 ? 57.781  -14.097 37.638 1.00 12.25  ? 470  ASP B N     1 
ATOM   7165 C CA    . ASP B 1 428 ? 58.072  -15.455 38.097 1.00 12.97  ? 470  ASP B CA    1 
ATOM   7166 C C     . ASP B 1 428 ? 57.748  -15.613 39.577 1.00 12.69  ? 470  ASP B C     1 
ATOM   7167 O O     . ASP B 1 428 ? 58.528  -15.197 40.440 1.00 13.55  ? 470  ASP B O     1 
ATOM   7168 C CB    . ASP B 1 428 ? 59.533  -15.747 37.790 1.00 13.97  ? 470  ASP B CB    1 
ATOM   7169 C CG    . ASP B 1 428 ? 59.982  -17.159 38.134 1.00 17.21  ? 470  ASP B CG    1 
ATOM   7170 O OD1   . ASP B 1 428 ? 59.242  -17.864 38.860 1.00 16.65  ? 470  ASP B OD1   1 
ATOM   7171 O OD2   . ASP B 1 428 ? 61.083  -17.516 37.628 1.00 16.80  ? 470  ASP B OD2   1 
ATOM   7172 N N     . LYS B 1 429 ? 56.580  -16.189 39.872 1.00 14.03  ? 471  LYS B N     1 
ATOM   7173 C CA    . LYS B 1 429 ? 56.128  -16.219 41.253 1.00 13.30  ? 471  LYS B CA    1 
ATOM   7174 C C     . LYS B 1 429 ? 56.924  -17.226 42.079 1.00 16.78  ? 471  LYS B C     1 
ATOM   7175 O O     . LYS B 1 429 ? 56.985  -17.095 43.311 1.00 15.98  ? 471  LYS B O     1 
ATOM   7176 C CB    . LYS B 1 429 ? 54.630  -16.514 41.316 1.00 14.05  ? 471  LYS B CB    1 
ATOM   7177 C CG    . LYS B 1 429 ? 54.057  -16.456 42.726 1.00 13.41  ? 471  LYS B CG    1 
ATOM   7178 C CD    . LYS B 1 429 ? 52.550  -16.420 42.810 1.00 15.26  ? 471  LYS B CD    1 
ATOM   7179 C CE    . LYS B 1 429 ? 52.082  -16.592 44.247 1.00 13.20  ? 471  LYS B CE    1 
ATOM   7180 N NZ    . LYS B 1 429 ? 50.622  -16.385 44.376 1.00 14.45  ? 471  LYS B NZ    1 
ATOM   7181 N N     . ALA B 1 430 ? 57.523  -18.219 41.388 1.00 14.70  ? 472  ALA B N     1 
ATOM   7182 C CA    . ALA B 1 430 ? 58.261  -19.291 42.043 1.00 15.95  ? 472  ALA B CA    1 
ATOM   7183 C C     . ALA B 1 430 ? 59.621  -18.802 42.546 1.00 16.78  ? 472  ALA B C     1 
ATOM   7184 O O     . ALA B 1 430 ? 60.271  -19.519 43.342 1.00 18.36  ? 472  ALA B O     1 
ATOM   7185 C CB    . ALA B 1 430 ? 58.384  -20.445 41.072 1.00 15.31  ? 472  ALA B CB    1 
ATOM   7186 N N     . ASP B 1 431 ? 60.044  -17.588 42.120 1.00 16.65  ? 473  ASP B N     1 
ATOM   7187 C CA    . ASP B 1 431 ? 61.251  -16.970 42.625 1.00 15.08  ? 473  ASP B CA    1 
ATOM   7188 C C     . ASP B 1 431 ? 60.852  -15.953 43.683 1.00 16.30  ? 473  ASP B C     1 
ATOM   7189 O O     . ASP B 1 431 ? 60.260  -14.912 43.349 1.00 16.19  ? 473  ASP B O     1 
ATOM   7190 C CB    . ASP B 1 431 ? 62.042  -16.310 41.502 1.00 16.71  ? 473  ASP B CB    1 
ATOM   7191 C CG    . ASP B 1 431 ? 63.279  -15.540 41.930 1.00 19.97  ? 473  ASP B CG    1 
ATOM   7192 O OD1   . ASP B 1 431 ? 63.329  -15.073 43.099 1.00 21.76  ? 473  ASP B OD1   1 
ATOM   7193 O OD2   . ASP B 1 431 ? 64.221  -15.446 41.098 1.00 23.15  ? 473  ASP B OD2   1 
ATOM   7194 N N     . PRO B 1 432 ? 61.117  -16.189 44.974 1.00 16.41  ? 474  PRO B N     1 
ATOM   7195 C CA    . PRO B 1 432 ? 60.581  -15.296 46.004 1.00 17.37  ? 474  PRO B CA    1 
ATOM   7196 C C     . PRO B 1 432 ? 61.044  -13.856 45.914 1.00 17.27  ? 474  PRO B C     1 
ATOM   7197 O O     . PRO B 1 432 ? 60.293  -12.956 46.324 1.00 17.62  ? 474  PRO B O     1 
ATOM   7198 C CB    . PRO B 1 432 ? 61.010  -15.848 47.372 1.00 20.58  ? 474  PRO B CB    1 
ATOM   7199 C CG    . PRO B 1 432 ? 61.759  -17.116 47.056 1.00 21.27  ? 474  PRO B CG    1 
ATOM   7200 C CD    . PRO B 1 432 ? 61.786  -17.364 45.565 1.00 18.67  ? 474  PRO B CD    1 
ATOM   7201 N N     . THR B 1 433 ? 62.224  -13.612 45.337 1.00 14.53  ? 475  THR B N     1 
ATOM   7202 C CA    . THR B 1 433 ? 62.716  -12.261 45.131 1.00 17.86  ? 475  THR B CA    1 
ATOM   7203 C C     . THR B 1 433 ? 61.897  -11.550 44.064 1.00 16.78  ? 475  THR B C     1 
ATOM   7204 O O     . THR B 1 433 ? 61.570  -10.351 44.218 1.00 18.11  ? 475  THR B O     1 
ATOM   7205 C CB    . THR B 1 433 ? 64.206  -12.236 44.735 1.00 21.71  ? 475  THR B CB    1 
ATOM   7206 O OG1   . THR B 1 433 ? 64.935  -12.855 45.799 1.00 22.84  ? 475  THR B OG1   1 
ATOM   7207 C CG2   . THR B 1 433 ? 64.704  -10.819 44.549 1.00 24.27  ? 475  THR B CG2   1 
ATOM   7208 N N     . GLN B 1 434 ? 61.534  -12.280 43.005 1.00 13.68  ? 476  GLN B N     1 
ATOM   7209 C CA    . GLN B 1 434 ? 60.708  -11.695 41.966 1.00 14.20  ? 476  GLN B CA    1 
ATOM   7210 C C     . GLN B 1 434 ? 59.284  -11.414 42.488 1.00 14.14  ? 476  GLN B C     1 
ATOM   7211 O O     . GLN B 1 434 ? 58.676  -10.404 42.141 1.00 14.57  ? 476  GLN B O     1 
ATOM   7212 C CB    . GLN B 1 434 ? 60.661  -12.586 40.727 1.00 14.62  ? 476  GLN B CB    1 
ATOM   7213 C CG    . GLN B 1 434 ? 61.954  -12.627 39.910 1.00 16.10  ? 476  GLN B CG    1 
ATOM   7214 C CD    . GLN B 1 434 ? 62.370  -11.278 39.396 1.00 18.69  ? 476  GLN B CD    1 
ATOM   7215 O OE1   . GLN B 1 434 ? 61.614  -10.588 38.729 1.00 15.79  ? 476  GLN B OE1   1 
ATOM   7216 N NE2   . GLN B 1 434 ? 63.598  -10.895 39.727 1.00 23.87  ? 476  GLN B NE2   1 
ATOM   7217 N N     . GLU B 1 435 ? 58.775  -12.289 43.343 1.00 13.49  ? 477  GLU B N     1 
ATOM   7218 C CA    . GLU B 1 435 ? 57.444  -12.066 43.901 1.00 15.06  ? 477  GLU B CA    1 
ATOM   7219 C C     . GLU B 1 435 ? 57.467  -10.799 44.749 1.00 15.25  ? 477  GLU B C     1 
ATOM   7220 O O     . GLU B 1 435 ? 56.516  -10.036 44.745 1.00 13.30  ? 477  GLU B O     1 
ATOM   7221 C CB    . GLU B 1 435 ? 56.986  -13.282 44.692 1.00 15.81  ? 477  GLU B CB    1 
ATOM   7222 C CG    . GLU B 1 435 ? 55.644  -13.098 45.377 1.00 17.43  ? 477  GLU B CG    1 
ATOM   7223 C CD    . GLU B 1 435 ? 55.235  -14.288 46.240 1.00 17.77  ? 477  GLU B CD    1 
ATOM   7224 O OE1   . GLU B 1 435 ? 56.115  -14.878 46.936 1.00 18.68  ? 477  GLU B OE1   1 
ATOM   7225 O OE2   . GLU B 1 435 ? 54.050  -14.664 46.240 1.00 18.62  ? 477  GLU B OE2   1 
ATOM   7226 N N     . GLN B 1 436 ? 58.522  -10.619 45.560 1.00 15.27  ? 478  GLN B N     1 
ATOM   7227 C CA    . GLN B 1 436 ? 58.654  -9.405  46.372 1.00 16.11  ? 478  GLN B CA    1 
ATOM   7228 C C     . GLN B 1 436 ? 58.718  -8.171  45.501 1.00 13.83  ? 478  GLN B C     1 
ATOM   7229 O O     . GLN B 1 436 ? 58.097  -7.123  45.790 1.00 15.50  ? 478  GLN B O     1 
ATOM   7230 C CB    . GLN B 1 436 ? 59.873  -9.495  47.309 1.00 18.90  ? 478  GLN B CB    1 
ATOM   7231 C CG    . GLN B 1 436 ? 59.660  -10.354 48.537 1.00 27.92  ? 478  GLN B CG    1 
ATOM   7232 C CD    . GLN B 1 436 ? 60.919  -10.825 49.250 1.00 38.15  ? 478  GLN B CD    1 
ATOM   7233 O OE1   . GLN B 1 436 ? 62.056  -10.649 48.811 1.00 41.73  ? 478  GLN B OE1   1 
ATOM   7234 N NE2   . GLN B 1 436 ? 60.721  -11.482 50.378 1.00 48.08  ? 478  GLN B NE2   1 
ATOM   7235 N N     . LYS B 1 437 ? 59.535  -8.206  44.451 1.00 13.62  ? 479  LYS B N     1 
ATOM   7236 C CA    . LYS B 1 437 ? 59.663  -7.076  43.538 1.00 15.10  ? 479  LYS B CA    1 
ATOM   7237 C C     . LYS B 1 437 ? 58.317  -6.757  42.880 1.00 14.46  ? 479  LYS B C     1 
ATOM   7238 O O     . LYS B 1 437 ? 58.040  -5.591  42.634 1.00 14.76  ? 479  LYS B O     1 
ATOM   7239 C CB    . LYS B 1 437 ? 60.746  -7.316  42.485 1.00 16.13  ? 479  LYS B CB    1 
ATOM   7240 C CG    . LYS B 1 437 ? 62.163  -7.227  43.077 1.00 17.40  ? 479  LYS B CG    1 
ATOM   7241 C CD    . LYS B 1 437 ? 63.261  -7.590  42.086 1.00 20.20  ? 479  LYS B CD    1 
ATOM   7242 C CE    . LYS B 1 437 ? 63.405  -6.604  40.966 1.00 28.01  ? 479  LYS B CE    1 
ATOM   7243 N NZ    . LYS B 1 437 ? 63.555  -5.245  41.502 1.00 33.41  ? 479  LYS B NZ    1 
ATOM   7244 N N     . ALA B 1 438 ? 57.539  -7.773  42.486 1.00 13.27  ? 480  ALA B N     1 
ATOM   7245 C CA    . ALA B 1 438 ? 56.265  -7.510  41.807 1.00 11.68  ? 480  ALA B CA    1 
ATOM   7246 C C     . ALA B 1 438 ? 55.291  -6.841  42.801 1.00 13.01  ? 480  ALA B C     1 
ATOM   7247 O O     . ALA B 1 438 ? 54.517  -5.983  42.386 1.00 14.54  ? 480  ALA B O     1 
ATOM   7248 C CB    . ALA B 1 438 ? 55.716  -8.784  41.233 1.00 13.16  ? 480  ALA B CB    1 
ATOM   7249 N N     . ASP B 1 439 ? 55.378  -7.241  44.078 1.00 12.53  ? 481  ASP B N     1 
ATOM   7250 C CA    . ASP B 1 439 ? 54.550  -6.649  45.128 1.00 14.85  ? 481  ASP B CA    1 
ATOM   7251 C C     . ASP B 1 439 ? 54.877  -5.151  45.241 1.00 14.52  ? 481  ASP B C     1 
ATOM   7252 O O     . ASP B 1 439 ? 53.968  -4.326  45.281 1.00 15.08  ? 481  ASP B O     1 
ATOM   7253 C CB    . ASP B 1 439 ? 54.758  -7.404  46.445 1.00 17.11  ? 481  ASP B CB    1 
ATOM   7254 C CG    . ASP B 1 439 ? 53.658  -7.160  47.466 1.00 23.02  ? 481  ASP B CG    1 
ATOM   7255 O OD1   . ASP B 1 439 ? 52.487  -7.373  47.111 1.00 22.26  ? 481  ASP B OD1   1 
ATOM   7256 O OD2   . ASP B 1 439 ? 53.982  -6.726  48.576 1.00 30.72  ? 481  ASP B OD2   1 
ATOM   7257 N N     . ALA B 1 440 ? 56.174  -4.809  45.347 1.00 12.63  ? 482  ALA B N     1 
ATOM   7258 C CA    . ALA B 1 440 ? 56.608  -3.415  45.421 1.00 13.34  ? 482  ALA B CA    1 
ATOM   7259 C C     . ALA B 1 440 ? 56.197  -2.637  44.178 1.00 13.20  ? 482  ALA B C     1 
ATOM   7260 O O     . ALA B 1 440 ? 55.816  -1.458  44.238 1.00 13.65  ? 482  ALA B O     1 
ATOM   7261 C CB    . ALA B 1 440 ? 58.115  -3.389  45.628 1.00 13.30  ? 482  ALA B CB    1 
ATOM   7262 N N     . CYS B 1 441 ? 56.312  -3.267  42.996 1.00 12.38  ? 483  CYS B N     1 
ATOM   7263 C CA    . CYS B 1 441 ? 55.984  -2.610  41.766 1.00 12.31  ? 483  CYS B CA    1 
ATOM   7264 C C     . CYS B 1 441 ? 54.490  -2.268  41.729 1.00 12.64  ? 483  CYS B C     1 
ATOM   7265 O O     . CYS B 1 441 ? 54.092  -1.154  41.332 1.00 12.91  ? 483  CYS B O     1 
ATOM   7266 C CB    . CYS B 1 441 ? 56.361  -3.546  40.605 1.00 13.45  ? 483  CYS B CB    1 
ATOM   7267 S SG    . CYS B 1 441 ? 55.943  -2.901  38.964 1.00 15.31  ? 483  CYS B SG    1 
ATOM   7268 N N     . TYR B 1 442 ? 53.665  -3.246  42.149 1.00 12.27  ? 484  TYR B N     1 
ATOM   7269 C CA    . TYR B 1 442 ? 52.239  -3.044  42.106 1.00 12.87  ? 484  TYR B CA    1 
ATOM   7270 C C     . TYR B 1 442 ? 51.840  -1.883  43.030 1.00 12.94  ? 484  TYR B C     1 
ATOM   7271 O O     . TYR B 1 442 ? 51.017  -1.048  42.646 1.00 12.87  ? 484  TYR B O     1 
ATOM   7272 C CB    . TYR B 1 442 ? 51.500  -4.336  42.439 1.00 12.14  ? 484  TYR B CB    1 
ATOM   7273 C CG    . TYR B 1 442 ? 50.039  -4.282  42.052 1.00 11.83  ? 484  TYR B CG    1 
ATOM   7274 C CD1   . TYR B 1 442 ? 49.088  -3.632  42.813 1.00 10.46  ? 484  TYR B CD1   1 
ATOM   7275 C CD2   . TYR B 1 442 ? 49.620  -4.911  40.897 1.00 12.16  ? 484  TYR B CD2   1 
ATOM   7276 C CE1   . TYR B 1 442 ? 47.790  -3.512  42.368 1.00 10.75  ? 484  TYR B CE1   1 
ATOM   7277 C CE2   . TYR B 1 442 ? 48.301  -4.872  40.482 1.00 11.16  ? 484  TYR B CE2   1 
ATOM   7278 C CZ    . TYR B 1 442 ? 47.377  -4.165  41.227 1.00 10.91  ? 484  TYR B CZ    1 
ATOM   7279 O OH    . TYR B 1 442 ? 46.044  -4.115  40.797 1.00 10.72  ? 484  TYR B OH    1 
ATOM   7280 N N     . ARG B 1 443 ? 52.425  -1.826  44.230 1.00 13.32  ? 485  ARG B N     1 
ATOM   7281 C CA    . ARG B 1 443 ? 52.147  -0.741  45.157 1.00 13.34  ? 485  ARG B CA    1 
ATOM   7282 C C     . ARG B 1 443 ? 52.466  0.597   44.492 1.00 14.30  ? 485  ARG B C     1 
ATOM   7283 O O     . ARG B 1 443 ? 51.731  1.586   44.634 1.00 13.76  ? 485  ARG B O     1 
ATOM   7284 C CB    . ARG B 1 443 ? 52.954  -0.916  46.438 1.00 15.53  ? 485  ARG B CB    1 
ATOM   7285 C CG    . ARG B 1 443 ? 52.838  0.242   47.415 1.00 21.29  ? 485  ARG B CG    1 
ATOM   7286 C CD    . ARG B 1 443 ? 53.647  0.014   48.691 1.00 24.19  ? 485  ARG B CD    1 
ATOM   7287 N NE    . ARG B 1 443 ? 52.879  -0.800  49.614 1.00 30.31  ? 485  ARG B NE    1 
ATOM   7288 C CZ    . ARG B 1 443 ? 51.828  -0.358  50.319 1.00 34.54  ? 485  ARG B CZ    1 
ATOM   7289 N NH1   . ARG B 1 443 ? 51.535  0.929   50.381 1.00 36.49  ? 485  ARG B NH1   1 
ATOM   7290 N NH2   . ARG B 1 443 ? 51.076  -1.216  50.977 1.00 39.74  ? 485  ARG B NH2   1 
ATOM   7291 N N     . GLU B 1 444 ? 53.620  0.681   43.810 1.00 13.18  ? 486  GLU B N     1 
ATOM   7292 C CA    . GLU B 1 444 ? 54.028  1.918   43.182 1.00 13.45  ? 486  GLU B CA    1 
ATOM   7293 C C     . GLU B 1 444 ? 53.050  2.311   42.069 1.00 13.05  ? 486  GLU B C     1 
ATOM   7294 O O     . GLU B 1 444 ? 52.729  3.479   41.890 1.00 12.67  ? 486  GLU B O     1 
ATOM   7295 C CB    . GLU B 1 444 ? 55.483  1.831   42.648 1.00 14.64  ? 486  GLU B CB    1 
ATOM   7296 C CG    . GLU B 1 444 ? 55.979  3.178   42.139 1.00 15.33  ? 486  GLU B CG    1 
ATOM   7297 C CD    . GLU B 1 444 ? 57.487  3.322   41.880 1.00 19.70  ? 486  GLU B CD    1 
ATOM   7298 O OE1   . GLU B 1 444 ? 58.249  2.502   42.351 1.00 18.84  ? 486  GLU B OE1   1 
ATOM   7299 O OE2   . GLU B 1 444 ? 57.872  4.266   41.210 1.00 20.35  ? 486  GLU B OE2   1 
ATOM   7300 N N     . LEU B 1 445 ? 52.616  1.354   41.235 1.00 11.65  ? 487  LEU B N     1 
ATOM   7301 C CA    . LEU B 1 445 ? 51.617  1.627   40.218 1.00 11.95  ? 487  LEU B CA    1 
ATOM   7302 C C     . LEU B 1 445 ? 50.389  2.289   40.835 1.00 11.14  ? 487  LEU B C     1 
ATOM   7303 O O     . LEU B 1 445 ? 49.971  3.351   40.380 1.00 11.12  ? 487  LEU B O     1 
ATOM   7304 C CB    . LEU B 1 445 ? 51.214  0.316   39.540 1.00 13.25  ? 487  LEU B CB    1 
ATOM   7305 C CG    . LEU B 1 445 ? 52.202  -0.213  38.493 1.00 13.47  ? 487  LEU B CG    1 
ATOM   7306 C CD1   . LEU B 1 445 ? 51.797  -1.640  38.077 1.00 14.62  ? 487  LEU B CD1   1 
ATOM   7307 C CD2   . LEU B 1 445 ? 52.326  0.706   37.301 1.00 14.60  ? 487  LEU B CD2   1 
ATOM   7308 N N     . VAL B 1 446 ? 49.799  1.654   41.845 1.00 12.46  ? 488  VAL B N     1 
ATOM   7309 C CA    . VAL B 1 446 ? 48.588  2.188   42.464 1.00 11.83  ? 488  VAL B CA    1 
ATOM   7310 C C     . VAL B 1 446 ? 48.832  3.615   43.014 1.00 11.50  ? 488  VAL B C     1 
ATOM   7311 O O     . VAL B 1 446 ? 48.052  4.514   42.730 1.00 10.54  ? 488  VAL B O     1 
ATOM   7312 C CB    . VAL B 1 446 ? 48.052  1.253   43.558 1.00 11.04  ? 488  VAL B CB    1 
ATOM   7313 C CG1   . VAL B 1 446 ? 46.839  1.865   44.284 1.00 11.09  ? 488  VAL B CG1   1 
ATOM   7314 C CG2   . VAL B 1 446 ? 47.756  -0.143  42.998 1.00 10.62  ? 488  VAL B CG2   1 
ATOM   7315 N N     . THR B 1 447 ? 49.915  3.795   43.776 1.00 12.63  ? 489  THR B N     1 
ATOM   7316 C CA    . THR B 1 447 ? 50.192  5.044   44.493 1.00 13.79  ? 489  THR B CA    1 
ATOM   7317 C C     . THR B 1 447 ? 50.435  6.132   43.484 1.00 11.89  ? 489  THR B C     1 
ATOM   7318 O O     . THR B 1 447 ? 49.917  7.272   43.623 1.00 13.77  ? 489  THR B O     1 
ATOM   7319 C CB    . THR B 1 447 ? 51.319  4.826   45.528 1.00 16.22  ? 489  THR B CB    1 
ATOM   7320 O OG1   . THR B 1 447 ? 50.855  3.795   46.423 1.00 20.78  ? 489  THR B OG1   1 
ATOM   7321 C CG2   . THR B 1 447 ? 51.648  6.042   46.352 1.00 22.11  ? 489  THR B CG2   1 
ATOM   7322 N N     . ARG B 1 448 ? 51.332  5.910   42.530 1.00 12.69  ? 490  ARG B N     1 
ATOM   7323 C CA    . ARG B 1 448 ? 51.709  6.989   41.632 1.00 12.89  ? 490  ARG B CA    1 
ATOM   7324 C C     . ARG B 1 448 ? 50.602  7.302   40.625 1.00 12.62  ? 490  ARG B C     1 
ATOM   7325 O O     . ARG B 1 448 ? 50.447  8.467   40.264 1.00 13.96  ? 490  ARG B O     1 
ATOM   7326 C CB    . ARG B 1 448 ? 53.055  6.745   40.923 1.00 13.46  ? 490  ARG B CB    1 
ATOM   7327 C CG    . ARG B 1 448 ? 54.224  6.764   41.907 1.00 15.66  ? 490  ARG B CG    1 
ATOM   7328 C CD    . ARG B 1 448 ? 55.560  6.568   41.232 1.00 19.60  ? 490  ARG B CD    1 
ATOM   7329 N NE    . ARG B 1 448 ? 55.895  7.625   40.284 1.00 21.54  ? 490  ARG B NE    1 
ATOM   7330 C CZ    . ARG B 1 448 ? 56.830  7.505   39.355 1.00 19.86  ? 490  ARG B CZ    1 
ATOM   7331 N NH1   . ARG B 1 448 ? 57.602  6.425   39.313 1.00 20.99  ? 490  ARG B NH1   1 
ATOM   7332 N NH2   . ARG B 1 448 ? 57.021  8.486   38.491 1.00 21.66  ? 490  ARG B NH2   1 
ATOM   7333 N N     . PHE B 1 449 ? 49.811  6.317   40.167 1.00 11.89  ? 491  PHE B N     1 
ATOM   7334 C CA    . PHE B 1 449 ? 48.638  6.647   39.371 1.00 12.18  ? 491  PHE B CA    1 
ATOM   7335 C C     . PHE B 1 449 ? 47.662  7.522   40.173 1.00 11.09  ? 491  PHE B C     1 
ATOM   7336 O O     . PHE B 1 449 ? 47.114  8.466   39.627 1.00 12.09  ? 491  PHE B O     1 
ATOM   7337 C CB    . PHE B 1 449 ? 47.984  5.381   38.839 1.00 13.53  ? 491  PHE B CB    1 
ATOM   7338 C CG    . PHE B 1 449 ? 48.506  4.958   37.498 1.00 12.14  ? 491  PHE B CG    1 
ATOM   7339 C CD1   . PHE B 1 449 ? 49.843  4.638   37.283 1.00 14.33  ? 491  PHE B CD1   1 
ATOM   7340 C CD2   . PHE B 1 449 ? 47.645  4.836   36.434 1.00 12.97  ? 491  PHE B CD2   1 
ATOM   7341 C CE1   . PHE B 1 449 ? 50.269  4.203   36.035 1.00 13.39  ? 491  PHE B CE1   1 
ATOM   7342 C CE2   . PHE B 1 449 ? 48.082  4.440   35.181 1.00 14.58  ? 491  PHE B CE2   1 
ATOM   7343 C CZ    . PHE B 1 449 ? 49.393  4.129   34.970 1.00 13.10  ? 491  PHE B CZ    1 
ATOM   7344 N N     . GLY B 1 450 ? 47.480  7.174   41.426 1.00 12.26  ? 492  GLY B N     1 
ATOM   7345 C CA    . GLY B 1 450 ? 46.496  7.874   42.259 1.00 15.14  ? 492  GLY B CA    1 
ATOM   7346 C C     . GLY B 1 450 ? 46.878  9.350   42.381 1.00 15.94  ? 492  GLY B C     1 
ATOM   7347 O O     . GLY B 1 450 ? 46.038  10.247  42.326 1.00 15.99  ? 492  GLY B O     1 
ATOM   7348 N N     . ALA B 1 451 ? 48.183  9.588   42.514 1.00 16.89  ? 493  ALA B N     1 
ATOM   7349 C CA    . ALA B 1 451 ? 48.688  10.958  42.630 1.00 16.08  ? 493  ALA B CA    1 
ATOM   7350 C C     . ALA B 1 451 ? 48.495  11.768  41.347 1.00 16.01  ? 493  ALA B C     1 
ATOM   7351 O O     . ALA B 1 451 ? 48.498  13.004  41.387 1.00 17.20  ? 493  ALA B O     1 
ATOM   7352 C CB    . ALA B 1 451 ? 50.121  10.912  43.079 1.00 17.38  ? 493  ALA B CB    1 
ATOM   7353 N N     . GLN B 1 452 ? 48.280  11.141  40.188 1.00 15.58  ? 494  GLN B N     1 
ATOM   7354 C CA    . GLN B 1 452 ? 47.960  11.838  38.960 1.00 15.12  ? 494  GLN B CA    1 
ATOM   7355 C C     . GLN B 1 452 ? 46.450  11.854  38.687 1.00 14.06  ? 494  GLN B C     1 
ATOM   7356 O O     . GLN B 1 452 ? 46.014  12.287  37.622 1.00 16.56  ? 494  GLN B O     1 
ATOM   7357 C CB    . GLN B 1 452 ? 48.627  11.153  37.756 1.00 15.94  ? 494  GLN B CB    1 
ATOM   7358 C CG    . GLN B 1 452 ? 50.146  11.128  37.846 1.00 19.07  ? 494  GLN B CG    1 
ATOM   7359 C CD    . GLN B 1 452 ? 50.710  12.529  37.950 1.00 20.47  ? 494  GLN B CD    1 
ATOM   7360 O OE1   . GLN B 1 452 ? 50.367  13.400  37.161 1.00 22.52  ? 494  GLN B OE1   1 
ATOM   7361 N NE2   . GLN B 1 452 ? 51.576  12.750  38.930 1.00 21.09  ? 494  GLN B NE2   1 
ATOM   7362 N N     . GLY B 1 453 ? 45.652  11.343  39.616 1.00 14.40  ? 495  GLY B N     1 
ATOM   7363 C CA    . GLY B 1 453 ? 44.204  11.384  39.478 1.00 14.37  ? 495  GLY B CA    1 
ATOM   7364 C C     . GLY B 1 453 ? 43.539  10.145  38.841 1.00 14.19  ? 495  GLY B C     1 
ATOM   7365 O O     . GLY B 1 453 ? 42.369  10.199  38.402 1.00 14.29  ? 495  GLY B O     1 
ATOM   7366 N N     . TRP B 1 454 ? 44.282  9.022   38.805 1.00 12.44  ? 496  TRP B N     1 
ATOM   7367 C CA    . TRP B 1 454 ? 43.847  7.796   38.155 1.00 12.32  ? 496  TRP B CA    1 
ATOM   7368 C C     . TRP B 1 454 ? 43.755  6.648   39.156 1.00 12.33  ? 496  TRP B C     1 
ATOM   7369 O O     . TRP B 1 454 ? 44.659  6.437   39.958 1.00 13.10  ? 496  TRP B O     1 
ATOM   7370 C CB    . TRP B 1 454 ? 44.831  7.424   37.040 1.00 11.89  ? 496  TRP B CB    1 
ATOM   7371 C CG    . TRP B 1 454 ? 45.043  8.465   35.980 1.00 13.80  ? 496  TRP B CG    1 
ATOM   7372 C CD1   . TRP B 1 454 ? 44.109  9.206   35.319 1.00 15.55  ? 496  TRP B CD1   1 
ATOM   7373 C CD2   . TRP B 1 454 ? 46.304  8.787   35.381 1.00 14.26  ? 496  TRP B CD2   1 
ATOM   7374 N NE1   . TRP B 1 454 ? 44.715  10.039  34.401 1.00 15.85  ? 496  TRP B NE1   1 
ATOM   7375 C CE2   . TRP B 1 454 ? 46.054  9.787   34.409 1.00 17.43  ? 496  TRP B CE2   1 
ATOM   7376 C CE3   . TRP B 1 454 ? 47.611  8.397   35.640 1.00 15.31  ? 496  TRP B CE3   1 
ATOM   7377 C CZ2   . TRP B 1 454 ? 47.079  10.351  33.652 1.00 15.97  ? 496  TRP B CZ2   1 
ATOM   7378 C CZ3   . TRP B 1 454 ? 48.620  8.905   34.855 1.00 16.47  ? 496  TRP B CZ3   1 
ATOM   7379 C CH2   . TRP B 1 454 ? 48.353  9.890   33.898 1.00 17.88  ? 496  TRP B CH2   1 
ATOM   7380 N N     . ALA B 1 455 ? 42.667  5.858   39.045 1.00 11.38  ? 497  ALA B N     1 
ATOM   7381 C CA    . ALA B 1 455 ? 42.500  4.727   39.931 1.00 11.85  ? 497  ALA B CA    1 
ATOM   7382 C C     . ALA B 1 455 ? 41.714  3.627   39.213 1.00 10.17  ? 497  ALA B C     1 
ATOM   7383 O O     . ALA B 1 455 ? 41.133  3.831   38.141 1.00 10.34  ? 497  ALA B O     1 
ATOM   7384 C CB    . ALA B 1 455 ? 41.856  5.124   41.236 1.00 12.56  ? 497  ALA B CB    1 
ATOM   7385 N N     . SER B 1 456 ? 41.743  2.455   39.848 1.00 10.62  ? 498  SER B N     1 
ATOM   7386 C CA    . SER B 1 456 ? 41.300  1.208   39.253 1.00 11.65  ? 498  SER B CA    1 
ATOM   7387 C C     . SER B 1 456 ? 39.774  1.063   39.216 1.00 10.74  ? 498  SER B C     1 
ATOM   7388 O O     . SER B 1 456 ? 39.063  1.472   40.162 1.00 11.06  ? 498  SER B O     1 
ATOM   7389 C CB    . SER B 1 456 ? 41.913  0.052   40.021 1.00 12.83  ? 498  SER B CB    1 
ATOM   7390 O OG    . SER B 1 456 ? 43.324  0.102   39.952 1.00 13.72  ? 498  SER B OG    1 
ATOM   7391 N N     . TYR B 1 457 ? 39.289  0.380   38.163 1.00 10.44  ? 499  TYR B N     1 
ATOM   7392 C CA    . TYR B 1 457 ? 37.891  -0.046  38.028 1.00 10.55  ? 499  TYR B CA    1 
ATOM   7393 C C     . TYR B 1 457 ? 37.651  -1.319  38.851 1.00 11.19  ? 499  TYR B C     1 
ATOM   7394 O O     . TYR B 1 457 ? 36.507  -1.622  39.163 1.00 10.06  ? 499  TYR B O     1 
ATOM   7395 C CB    . TYR B 1 457 ? 37.453  -0.286  36.568 1.00 9.97   ? 499  TYR B CB    1 
ATOM   7396 C CG    . TYR B 1 457 ? 37.468  -1.697  36.019 1.00 10.14  ? 499  TYR B CG    1 
ATOM   7397 C CD1   . TYR B 1 457 ? 38.648  -2.297  35.633 1.00 9.79   ? 499  TYR B CD1   1 
ATOM   7398 C CD2   . TYR B 1 457 ? 36.304  -2.433  35.925 1.00 11.15  ? 499  TYR B CD2   1 
ATOM   7399 C CE1   . TYR B 1 457 ? 38.668  -3.597  35.127 1.00 10.71  ? 499  TYR B CE1   1 
ATOM   7400 C CE2   . TYR B 1 457 ? 36.287  -3.731  35.435 1.00 10.08  ? 499  TYR B CE2   1 
ATOM   7401 C CZ    . TYR B 1 457 ? 37.474  -4.309  35.010 1.00 10.82  ? 499  TYR B CZ    1 
ATOM   7402 O OH    . TYR B 1 457 ? 37.426  -5.591  34.515 1.00 10.56  ? 499  TYR B OH    1 
ATOM   7403 N N     . ARG B 1 458 ? 38.712  -2.083  39.156 1.00 10.18  ? 500  ARG B N     1 
ATOM   7404 C CA    . ARG B 1 458 ? 38.633  -3.431  39.700 1.00 9.65   ? 500  ARG B CA    1 
ATOM   7405 C C     . ARG B 1 458 ? 40.030  -3.744  40.190 1.00 9.89   ? 500  ARG B C     1 
ATOM   7406 O O     . ARG B 1 458 ? 41.013  -3.340  39.560 1.00 10.50  ? 500  ARG B O     1 
ATOM   7407 C CB    . ARG B 1 458 ? 38.246  -4.375  38.557 1.00 9.77   ? 500  ARG B CB    1 
ATOM   7408 C CG    . ARG B 1 458 ? 37.850  -5.794  38.966 1.00 10.62  ? 500  ARG B CG    1 
ATOM   7409 C CD    . ARG B 1 458 ? 37.337  -6.437  37.713 1.00 11.35  ? 500  ARG B CD    1 
ATOM   7410 N NE    . ARG B 1 458 ? 37.049  -7.856  37.944 1.00 11.88  ? 500  ARG B NE    1 
ATOM   7411 C CZ    . ARG B 1 458 ? 36.804  -8.695  36.960 1.00 11.15  ? 500  ARG B CZ    1 
ATOM   7412 N NH1   . ARG B 1 458 ? 36.673  -8.196  35.743 1.00 10.81  ? 500  ARG B NH1   1 
ATOM   7413 N NH2   . ARG B 1 458 ? 36.494  -9.959  37.202 1.00 11.41  ? 500  ARG B NH2   1 
ATOM   7414 N N     . THR B 1 459 ? 40.172  -4.460  41.291 1.00 10.00  ? 501  THR B N     1 
ATOM   7415 C CA    . THR B 1 459 ? 41.502  -4.882  41.678 1.00 9.82   ? 501  THR B CA    1 
ATOM   7416 C C     . THR B 1 459 ? 41.478  -6.203  42.436 1.00 9.39   ? 501  THR B C     1 
ATOM   7417 O O     . THR B 1 459 ? 40.408  -6.741  42.768 1.00 10.10  ? 501  THR B O     1 
ATOM   7418 C CB    . THR B 1 459 ? 42.166  -3.806  42.553 1.00 10.28  ? 501  THR B CB    1 
ATOM   7419 O OG1   . THR B 1 459 ? 43.580  -3.858  42.377 1.00 11.21  ? 501  THR B OG1   1 
ATOM   7420 C CG2   . THR B 1 459 ? 41.737  -3.913  44.010 1.00 9.81   ? 501  THR B CG2   1 
ATOM   7421 N N     . GLY B 1 460 ? 42.670  -6.729  42.705 1.00 10.91  ? 502  GLY B N     1 
ATOM   7422 C CA    . GLY B 1 460 ? 42.778  -8.011  43.381 1.00 10.80  ? 502  GLY B CA    1 
ATOM   7423 C C     . GLY B 1 460 ? 42.845  -7.928  44.908 1.00 11.19  ? 502  GLY B C     1 
ATOM   7424 O O     . GLY B 1 460 ? 43.021  -6.833  45.472 1.00 11.56  ? 502  GLY B O     1 
ATOM   7425 N N     . VAL B 1 461 ? 42.678  -9.081  45.578 1.00 11.87  ? 503  VAL B N     1 
ATOM   7426 C CA    . VAL B 1 461 ? 42.430  -9.043  47.020 1.00 11.97  ? 503  VAL B CA    1 
ATOM   7427 C C     . VAL B 1 461 ? 43.603  -8.424  47.743 1.00 15.15  ? 503  VAL B C     1 
ATOM   7428 O O     . VAL B 1 461 ? 43.392  -7.838  48.822 1.00 17.00  ? 503  VAL B O     1 
ATOM   7429 C CB    . VAL B 1 461 ? 42.112  -10.423 47.601 1.00 12.61  ? 503  VAL B CB    1 
ATOM   7430 C CG1   . VAL B 1 461 ? 40.777  -10.920 47.065 1.00 12.58  ? 503  VAL B CG1   1 
ATOM   7431 C CG2   . VAL B 1 461 ? 43.211  -11.435 47.330 1.00 14.19  ? 503  VAL B CG2   1 
ATOM   7432 N N     . ASN B 1 462 ? 44.792  -8.528  47.195 1.00 13.48  ? 504  ASN B N     1 
ATOM   7433 C CA    . ASN B 1 462 ? 45.977  -8.015  47.868 1.00 14.58  ? 504  ASN B CA    1 
ATOM   7434 C C     . ASN B 1 462 ? 46.122  -6.494  47.798 1.00 13.83  ? 504  ASN B C     1 
ATOM   7435 O O     . ASN B 1 462 ? 46.958  -5.905  48.472 1.00 15.74  ? 504  ASN B O     1 
ATOM   7436 C CB    . ASN B 1 462 ? 47.225  -8.677  47.313 1.00 18.08  ? 504  ASN B CB    1 
ATOM   7437 C CG    . ASN B 1 462 ? 47.399  -8.403  45.846 1.00 18.39  ? 504  ASN B CG    1 
ATOM   7438 O OD1   . ASN B 1 462 ? 46.483  -8.614  45.040 1.00 15.91  ? 504  ASN B OD1   1 
ATOM   7439 N ND2   . ASN B 1 462 ? 48.570  -7.927  45.471 1.00 22.61  ? 504  ASN B ND2   1 
ATOM   7440 N N     . SER B 1 463 ? 45.350  -5.836  46.925 1.00 11.84  ? 505  SER B N     1 
ATOM   7441 C CA    . SER B 1 463 ? 45.448  -4.397  46.786 1.00 11.96  ? 505  SER B CA    1 
ATOM   7442 C C     . SER B 1 463 ? 44.112  -3.714  47.064 1.00 12.12  ? 505  SER B C     1 
ATOM   7443 O O     . SER B 1 463 ? 43.974  -2.530  46.766 1.00 10.26  ? 505  SER B O     1 
ATOM   7444 C CB    . SER B 1 463 ? 45.990  -4.004  45.413 1.00 13.42  ? 505  SER B CB    1 
ATOM   7445 O OG    . SER B 1 463 ? 45.161  -4.524  44.376 1.00 14.55  ? 505  SER B OG    1 
ATOM   7446 N N     . MET B 1 464 ? 43.087  -4.428  47.566 1.00 11.54  ? 506  MET B N     1 
ATOM   7447 C CA    . MET B 1 464 ? 41.762  -3.784  47.683 1.00 10.53  ? 506  MET B CA    1 
ATOM   7448 C C     . MET B 1 464 ? 41.776  -2.610  48.681 1.00 10.86  ? 506  MET B C     1 
ATOM   7449 O O     . MET B 1 464 ? 41.069  -1.609  48.508 1.00 9.34   ? 506  MET B O     1 
ATOM   7450 C CB    . MET B 1 464 ? 40.723  -4.805  48.083 1.00 11.04  ? 506  MET B CB    1 
ATOM   7451 C CG    . MET B 1 464 ? 40.215  -5.636  46.949 1.00 11.57  ? 506  MET B CG    1 
ATOM   7452 S SD    . MET B 1 464 ? 39.244  -7.105  47.471 1.00 11.51  ? 506  MET B SD    1 
ATOM   7453 C CE    . MET B 1 464 ? 39.035  -7.856  45.893 1.00 11.27  ? 506  MET B CE    1 
ATOM   7454 N N     . ASP B 1 465 ? 42.584  -2.712  49.732 1.00 11.67  ? 507  ASP B N     1 
ATOM   7455 C CA    . ASP B 1 465 ? 42.651  -1.617  50.671 1.00 12.76  ? 507  ASP B CA    1 
ATOM   7456 C C     . ASP B 1 465 ? 43.375  -0.430  50.053 1.00 11.81  ? 507  ASP B C     1 
ATOM   7457 O O     . ASP B 1 465 ? 42.936  0.724   50.174 1.00 12.45  ? 507  ASP B O     1 
ATOM   7458 C CB    . ASP B 1 465 ? 43.395  -2.019  51.934 1.00 13.72  ? 507  ASP B CB    1 
ATOM   7459 C CG    . ASP B 1 465 ? 42.626  -2.866  52.926 1.00 18.67  ? 507  ASP B CG    1 
ATOM   7460 O OD1   . ASP B 1 465 ? 41.385  -3.022  52.793 1.00 18.05  ? 507  ASP B OD1   1 
ATOM   7461 O OD2   . ASP B 1 465 ? 43.291  -3.363  53.886 1.00 21.99  ? 507  ASP B OD2   1 
ATOM   7462 N N     . LEU B 1 466 ? 44.527  -0.685  49.444 1.00 12.11  ? 508  LEU B N     1 
ATOM   7463 C CA    . LEU B 1 466 ? 45.314  0.392   48.842 1.00 11.84  ? 508  LEU B CA    1 
ATOM   7464 C C     . LEU B 1 466 ? 44.565  1.115   47.715 1.00 11.13  ? 508  LEU B C     1 
ATOM   7465 O O     . LEU B 1 466 ? 44.647  2.338   47.613 1.00 11.86  ? 508  LEU B O     1 
ATOM   7466 C CB    . LEU B 1 466 ? 46.635  -0.170  48.295 1.00 13.89  ? 508  LEU B CB    1 
ATOM   7467 C CG    . LEU B 1 466 ? 47.628  0.885   47.785 1.00 14.94  ? 508  LEU B CG    1 
ATOM   7468 C CD1   . LEU B 1 466 ? 48.057  1.847   48.879 1.00 17.18  ? 508  LEU B CD1   1 
ATOM   7469 C CD2   . LEU B 1 466 ? 48.830  0.205   47.152 1.00 15.97  ? 508  LEU B CD2   1 
ATOM   7470 N N     . VAL B 1 467 ? 43.785  0.395   46.903 1.00 10.87  ? 509  VAL B N     1 
ATOM   7471 C CA    . VAL B 1 467 ? 42.944  1.056   45.916 1.00 9.99   ? 509  VAL B CA    1 
ATOM   7472 C C     . VAL B 1 467 ? 41.821  1.881   46.550 1.00 10.03  ? 509  VAL B C     1 
ATOM   7473 O O     . VAL B 1 467 ? 41.628  3.011   46.121 1.00 10.49  ? 509  VAL B O     1 
ATOM   7474 C CB    . VAL B 1 467 ? 42.422  0.029   44.919 1.00 10.45  ? 509  VAL B CB    1 
ATOM   7475 C CG1   . VAL B 1 467 ? 41.325  0.560   44.015 1.00 11.15  ? 509  VAL B CG1   1 
ATOM   7476 C CG2   . VAL B 1 467 ? 43.582  -0.476  44.091 1.00 12.02  ? 509  VAL B CG2   1 
ATOM   7477 N N     . ALA B 1 468 ? 41.156  1.367   47.604 1.00 11.42  ? 510  ALA B N     1 
ATOM   7478 C CA    . ALA B 1 468 ? 40.149  2.130   48.373 1.00 10.80  ? 510  ALA B CA    1 
ATOM   7479 C C     . ALA B 1 468 ? 40.739  3.440   48.860 1.00 12.96  ? 510  ALA B C     1 
ATOM   7480 O O     . ALA B 1 468 ? 40.043  4.450   48.848 1.00 13.42  ? 510  ALA B O     1 
ATOM   7481 C CB    . ALA B 1 468 ? 39.621  1.290   49.476 1.00 12.15  ? 510  ALA B CB    1 
ATOM   7482 N N     . GLN B 1 469 ? 42.014  3.408   49.294 1.00 12.27  ? 511  GLN B N     1 
ATOM   7483 C CA    . GLN B 1 469 ? 42.690  4.610   49.775 1.00 13.87  ? 511  GLN B CA    1 
ATOM   7484 C C     . GLN B 1 469 ? 42.848  5.675   48.704 1.00 12.56  ? 511  GLN B C     1 
ATOM   7485 O O     . GLN B 1 469 ? 43.087  6.823   49.049 1.00 14.76  ? 511  GLN B O     1 
ATOM   7486 C CB    . GLN B 1 469 ? 44.051  4.253   50.363 1.00 15.11  ? 511  GLN B CB    1 
ATOM   7487 C CG    . GLN B 1 469 ? 43.928  3.511   51.678 1.00 19.04  ? 511  GLN B CG    1 
ATOM   7488 C CD    . GLN B 1 469 ? 45.274  2.967   52.110 1.00 26.34  ? 511  GLN B CD    1 
ATOM   7489 O OE1   . GLN B 1 469 ? 46.299  3.636   51.996 1.00 34.80  ? 511  GLN B OE1   1 
ATOM   7490 N NE2   . GLN B 1 469 ? 45.289  1.720   52.546 1.00 30.21  ? 511  GLN B NE2   1 
ATOM   7491 N N     . GLN B 1 470 ? 42.782  5.350   47.420 1.00 11.74  ? 512  GLN B N     1 
ATOM   7492 C CA    . GLN B 1 470 ? 42.881  6.341   46.354 1.00 12.00  ? 512  GLN B CA    1 
ATOM   7493 C C     . GLN B 1 470 ? 41.571  7.134   46.167 1.00 12.83  ? 512  GLN B C     1 
ATOM   7494 O O     . GLN B 1 470 ? 41.612  8.266   45.639 1.00 14.31  ? 512  GLN B O     1 
ATOM   7495 C CB    . GLN B 1 470 ? 43.237  5.724   45.009 1.00 13.30  ? 512  GLN B CB    1 
ATOM   7496 C CG    . GLN B 1 470 ? 44.454  4.824   45.066 1.00 12.75  ? 512  GLN B CG    1 
ATOM   7497 C CD    . GLN B 1 470 ? 45.636  5.459   45.777 1.00 12.77  ? 512  GLN B CD    1 
ATOM   7498 O OE1   . GLN B 1 470 ? 46.031  6.565   45.427 1.00 15.68  ? 512  GLN B OE1   1 
ATOM   7499 N NE2   . GLN B 1 470 ? 46.182  4.800   46.783 1.00 13.80  ? 512  GLN B NE2   1 
ATOM   7500 N N     . TYR B 1 471 ? 40.437  6.548   46.590 1.00 12.48  ? 513  TYR B N     1 
ATOM   7501 C CA    . TYR B 1 471 ? 39.134  7.181   46.476 1.00 12.49  ? 513  TYR B CA    1 
ATOM   7502 C C     . TYR B 1 471 ? 38.839  7.938   47.778 1.00 12.63  ? 513  TYR B C     1 
ATOM   7503 O O     . TYR B 1 471 ? 39.671  7.907   48.710 1.00 13.29  ? 513  TYR B O     1 
ATOM   7504 C CB    . TYR B 1 471 ? 38.089  6.116   46.148 1.00 12.12  ? 513  TYR B CB    1 
ATOM   7505 C CG    . TYR B 1 471 ? 38.214  5.530   44.770 1.00 11.95  ? 513  TYR B CG    1 
ATOM   7506 C CD1   . TYR B 1 471 ? 38.975  4.374   44.504 1.00 11.28  ? 513  TYR B CD1   1 
ATOM   7507 C CD2   . TYR B 1 471 ? 37.467  6.052   43.753 1.00 11.95  ? 513  TYR B CD2   1 
ATOM   7508 C CE1   . TYR B 1 471 ? 39.064  3.864   43.209 1.00 10.97  ? 513  TYR B CE1   1 
ATOM   7509 C CE2   . TYR B 1 471 ? 37.524  5.528   42.465 1.00 11.11  ? 513  TYR B CE2   1 
ATOM   7510 C CZ    . TYR B 1 471 ? 38.310  4.418   42.206 1.00 11.09  ? 513  TYR B CZ    1 
ATOM   7511 O OH    . TYR B 1 471 ? 38.364  3.953   40.940 1.00 11.59  ? 513  TYR B OH    1 
ATOM   7512 N N     . GLY B 1 472 ? 37.683  8.625   47.884 1.00 12.22  ? 514  GLY B N     1 
ATOM   7513 C CA    . GLY B 1 472 ? 37.499  9.594   48.968 1.00 12.04  ? 514  GLY B CA    1 
ATOM   7514 C C     . GLY B 1 472 ? 37.349  8.946   50.346 1.00 12.41  ? 514  GLY B C     1 
ATOM   7515 O O     . GLY B 1 472 ? 36.844  7.825   50.503 1.00 12.42  ? 514  GLY B O     1 
ATOM   7516 N N     . GLU B 1 473 ? 37.776  9.693   51.363 1.00 13.08  ? 515  GLU B N     1 
ATOM   7517 C CA    . GLU B 1 473 ? 37.551  9.277   52.750 1.00 15.37  ? 515  GLU B CA    1 
ATOM   7518 C C     . GLU B 1 473 ? 36.063  9.193   53.093 1.00 13.20  ? 515  GLU B C     1 
ATOM   7519 O O     . GLU B 1 473 ? 35.647  8.298   53.830 1.00 11.97  ? 515  GLU B O     1 
ATOM   7520 C CB    . GLU B 1 473 ? 38.238  10.246  53.719 1.00 20.20  ? 515  GLU B CB    1 
ATOM   7521 C CG    . GLU B 1 473 ? 37.941  9.959   55.194 1.00 34.26  ? 515  GLU B CG    1 
ATOM   7522 C CD    . GLU B 1 473 ? 38.376  8.605   55.762 1.00 51.67  ? 515  GLU B CD    1 
ATOM   7523 O OE1   . GLU B 1 473 ? 39.591  8.431   56.018 1.00 72.82  ? 515  GLU B OE1   1 
ATOM   7524 O OE2   . GLU B 1 473 ? 37.504  7.713   55.981 1.00 56.43  ? 515  GLU B OE2   1 
ATOM   7525 N N     . VAL B 1 474 ? 35.248  10.131  52.585 1.00 11.79  ? 516  VAL B N     1 
ATOM   7526 C CA    . VAL B 1 474 ? 33.807  10.097  52.848 1.00 11.61  ? 516  VAL B CA    1 
ATOM   7527 C C     . VAL B 1 474 ? 33.201  8.835   52.216 1.00 10.54  ? 516  VAL B C     1 
ATOM   7528 O O     . VAL B 1 474 ? 32.363  8.203   52.828 1.00 11.78  ? 516  VAL B O     1 
ATOM   7529 C CB    . VAL B 1 474 ? 33.091  11.378  52.383 1.00 12.94  ? 516  VAL B CB    1 
ATOM   7530 C CG1   . VAL B 1 474 ? 31.589  11.316  52.606 1.00 13.35  ? 516  VAL B CG1   1 
ATOM   7531 C CG2   . VAL B 1 474 ? 33.656  12.574  53.129 1.00 16.31  ? 516  VAL B CG2   1 
ATOM   7532 N N     . ASN B 1 475 ? 33.680  8.440   51.031 1.00 10.59  ? 517  ASN B N     1 
ATOM   7533 C CA    . ASN B 1 475 ? 33.186  7.236   50.368 1.00 11.27  ? 517  ASN B CA    1 
ATOM   7534 C C     . ASN B 1 475 ? 33.466  6.031   51.261 1.00 10.66  ? 517  ASN B C     1 
ATOM   7535 O O     . ASN B 1 475 ? 32.614  5.162   51.474 1.00 11.71  ? 517  ASN B O     1 
ATOM   7536 C CB    . ASN B 1 475 ? 33.803  7.046   48.960 1.00 11.07  ? 517  ASN B CB    1 
ATOM   7537 C CG    . ASN B 1 475 ? 33.494  8.206   48.045 1.00 12.79  ? 517  ASN B CG    1 
ATOM   7538 O OD1   . ASN B 1 475 ? 32.683  8.092   47.087 1.00 15.91  ? 517  ASN B OD1   1 
ATOM   7539 N ND2   . ASN B 1 475 ? 34.045  9.356   48.388 1.00 9.17   ? 517  ASN B ND2   1 
ATOM   7540 N N     . ARG B 1 476 ? 34.704  5.985   51.764 1.00 10.91  ? 518  ARG B N     1 
ATOM   7541 C CA    . ARG B 1 476 ? 35.092  4.860   52.604 1.00 10.97  ? 518  ARG B CA    1 
ATOM   7542 C C     . ARG B 1 476 ? 34.174  4.797   53.824 1.00 11.91  ? 518  ARG B C     1 
ATOM   7543 O O     . ARG B 1 476 ? 33.764  3.708   54.260 1.00 12.69  ? 518  ARG B O     1 
ATOM   7544 C CB    . ARG B 1 476 ? 36.565  5.020   52.949 1.00 15.84  ? 518  ARG B CB    1 
ATOM   7545 C CG    . ARG B 1 476 ? 37.269  3.816   53.523 1.00 19.98  ? 518  ARG B CG    1 
ATOM   7546 C CD    . ARG B 1 476 ? 38.040  3.101   52.424 1.00 22.79  ? 518  ARG B CD    1 
ATOM   7547 N NE    . ARG B 1 476 ? 38.506  1.775   52.859 1.00 24.19  ? 518  ARG B NE    1 
ATOM   7548 C CZ    . ARG B 1 476 ? 39.771  1.543   53.184 1.00 21.41  ? 518  ARG B CZ    1 
ATOM   7549 N NH1   . ARG B 1 476 ? 40.184  0.314   53.440 1.00 19.10  ? 518  ARG B NH1   1 
ATOM   7550 N NH2   . ARG B 1 476 ? 40.629  2.566   53.187 1.00 24.22  ? 518  ARG B NH2   1 
ATOM   7551 N N     . ASP B 1 477 ? 33.935  5.941   54.493 1.00 11.89  ? 519  ASP B N     1 
ATOM   7552 C CA    . ASP B 1 477 ? 33.075  5.988   55.678 1.00 13.45  ? 519  ASP B CA    1 
ATOM   7553 C C     . ASP B 1 477 ? 31.648  5.555   55.370 1.00 12.31  ? 519  ASP B C     1 
ATOM   7554 O O     . ASP B 1 477 ? 31.005  4.868   56.156 1.00 12.58  ? 519  ASP B O     1 
ATOM   7555 C CB    . ASP B 1 477 ? 33.023  7.411   56.248 1.00 15.44  ? 519  ASP B CB    1 
ATOM   7556 C CG    . ASP B 1 477 ? 34.297  7.901   56.910 1.00 22.18  ? 519  ASP B CG    1 
ATOM   7557 O OD1   . ASP B 1 477 ? 35.174  7.054   57.174 1.00 24.90  ? 519  ASP B OD1   1 
ATOM   7558 O OD2   . ASP B 1 477 ? 34.383  9.146   57.166 1.00 25.05  ? 519  ASP B OD2   1 
ATOM   7559 N N     . PHE B 1 478 ? 31.109  6.045   54.248 1.00 11.43  ? 520  PHE B N     1 
ATOM   7560 C CA    . PHE B 1 478 ? 29.766  5.720   53.841 1.00 11.97  ? 520  PHE B CA    1 
ATOM   7561 C C     . PHE B 1 478 ? 29.613  4.211   53.626 1.00 11.54  ? 520  PHE B C     1 
ATOM   7562 O O     . PHE B 1 478 ? 28.651  3.604   54.103 1.00 11.93  ? 520  PHE B O     1 
ATOM   7563 C CB    . PHE B 1 478 ? 29.428  6.444   52.540 1.00 12.94  ? 520  PHE B CB    1 
ATOM   7564 C CG    . PHE B 1 478 ? 27.986  6.337   52.151 1.00 13.22  ? 520  PHE B CG    1 
ATOM   7565 C CD1   . PHE B 1 478 ? 27.033  7.132   52.778 1.00 16.50  ? 520  PHE B CD1   1 
ATOM   7566 C CD2   . PHE B 1 478 ? 27.582  5.464   51.166 1.00 15.33  ? 520  PHE B CD2   1 
ATOM   7567 C CE1   . PHE B 1 478 ? 25.706  7.036   52.408 1.00 16.81  ? 520  PHE B CE1   1 
ATOM   7568 C CE2   . PHE B 1 478 ? 26.247  5.385   50.802 1.00 17.09  ? 520  PHE B CE2   1 
ATOM   7569 C CZ    . PHE B 1 478 ? 25.330  6.204   51.397 1.00 15.26  ? 520  PHE B CZ    1 
ATOM   7570 N N     . ASN B 1 479 ? 30.562  3.600   52.908 1.00 11.64  ? 521  ASN B N     1 
ATOM   7571 C CA    . ASN B 1 479 ? 30.552  2.157   52.690 1.00 12.71  ? 521  ASN B CA    1 
ATOM   7572 C C     . ASN B 1 479 ? 30.654  1.403   54.021 1.00 13.15  ? 521  ASN B C     1 
ATOM   7573 O O     . ASN B 1 479 ? 29.969  0.408   54.159 1.00 11.56  ? 521  ASN B O     1 
ATOM   7574 C CB    . ASN B 1 479 ? 31.675  1.746   51.751 1.00 13.57  ? 521  ASN B CB    1 
ATOM   7575 C CG    . ASN B 1 479 ? 31.397  2.022   50.284 1.00 15.88  ? 521  ASN B CG    1 
ATOM   7576 O OD1   . ASN B 1 479 ? 30.259  2.124   49.869 1.00 23.19  ? 521  ASN B OD1   1 
ATOM   7577 N ND2   . ASN B 1 479 ? 32.442  2.082   49.498 1.00 19.17  ? 521  ASN B ND2   1 
ATOM   7578 N N     . ARG B 1 480 ? 31.380  1.933   55.012 1.00 12.97  ? 522  ARG B N     1 
ATOM   7579 C CA    . ARG B 1 480 ? 31.471  1.252   56.293 1.00 14.80  ? 522  ARG B CA    1 
ATOM   7580 C C     . ARG B 1 480 ? 30.156  1.364   57.064 1.00 14.16  ? 522  ARG B C     1 
ATOM   7581 O O     . ARG B 1 480 ? 29.695  0.405   57.714 1.00 13.79  ? 522  ARG B O     1 
ATOM   7582 C CB    . ARG B 1 480 ? 32.628  1.788   57.130 1.00 19.35  ? 522  ARG B CB    1 
ATOM   7583 C CG    . ARG B 1 480 ? 32.888  0.955   58.383 1.00 27.71  ? 522  ARG B CG    1 
ATOM   7584 C CD    . ARG B 1 480 ? 34.236  1.253   59.032 1.00 39.54  ? 522  ARG B CD    1 
ATOM   7585 N NE    . ARG B 1 480 ? 34.414  2.676   59.288 1.00 55.79  ? 522  ARG B NE    1 
ATOM   7586 C CZ    . ARG B 1 480 ? 35.097  3.543   58.524 1.00 61.15  ? 522  ARG B CZ    1 
ATOM   7587 N NH1   . ARG B 1 480 ? 35.825  3.143   57.491 1.00 60.43  ? 522  ARG B NH1   1 
ATOM   7588 N NH2   . ARG B 1 480 ? 35.043  4.833   58.812 1.00 55.63  ? 522  ARG B NH2   1 
ATOM   7589 N N     . THR B 1 481 ? 29.507  2.519   56.959 1.00 13.05  ? 523  THR B N     1 
ATOM   7590 C CA    . THR B 1 481 ? 28.190  2.706   57.565 1.00 13.74  ? 523  THR B CA    1 
ATOM   7591 C C     . THR B 1 481 ? 27.164  1.716   56.997 1.00 13.43  ? 523  THR B C     1 
ATOM   7592 O O     . THR B 1 481 ? 26.383  1.096   57.756 1.00 14.96  ? 523  THR B O     1 
ATOM   7593 C CB    . THR B 1 481 ? 27.675  4.139   57.350 1.00 15.81  ? 523  THR B CB    1 
ATOM   7594 O OG1   . THR B 1 481 ? 28.525  4.993   58.105 1.00 18.19  ? 523  THR B OG1   1 
ATOM   7595 C CG2   . THR B 1 481 ? 26.239  4.299   57.812 1.00 17.98  ? 523  THR B CG2   1 
ATOM   7596 N N     . LEU B 1 482 ? 27.167  1.536   55.678 1.00 12.39  ? 524  LEU B N     1 
ATOM   7597 C CA    . LEU B 1 482 ? 26.277  0.579   55.062 1.00 14.27  ? 524  LEU B CA    1 
ATOM   7598 C C     . LEU B 1 482 ? 26.623  -0.820  55.546 1.00 13.87  ? 524  LEU B C     1 
ATOM   7599 O O     . LEU B 1 482 ? 25.721  -1.605  55.834 1.00 13.39  ? 524  LEU B O     1 
ATOM   7600 C CB    . LEU B 1 482 ? 26.391  0.627   53.544 1.00 15.47  ? 524  LEU B CB    1 
ATOM   7601 C CG    . LEU B 1 482 ? 25.938  1.902   52.855 1.00 18.31  ? 524  LEU B CG    1 
ATOM   7602 C CD1   . LEU B 1 482 ? 26.062  1.747   51.376 1.00 19.98  ? 524  LEU B CD1   1 
ATOM   7603 C CD2   . LEU B 1 482 ? 24.534  2.278   53.270 1.00 22.42  ? 524  LEU B CD2   1 
ATOM   7604 N N     . LYS B 1 483 ? 27.926  -1.133  55.575 1.00 12.51  ? 525  LYS B N     1 
ATOM   7605 C CA    . LYS B 1 483 ? 28.345  -2.493  55.928 1.00 12.73  ? 525  LYS B CA    1 
ATOM   7606 C C     . LYS B 1 483 ? 27.836  -2.873  57.303 1.00 12.28  ? 525  LYS B C     1 
ATOM   7607 O O     . LYS B 1 483 ? 27.278  -3.974  57.534 1.00 12.48  ? 525  LYS B O     1 
ATOM   7608 C CB    . LYS B 1 483 ? 29.867  -2.604  56.008 1.00 12.56  ? 525  LYS B CB    1 
ATOM   7609 C CG    . LYS B 1 483 ? 30.430  -3.986  56.330 1.00 13.17  ? 525  LYS B CG    1 
ATOM   7610 C CD    . LYS B 1 483 ? 29.950  -5.059  55.402 1.00 13.16  ? 525  LYS B CD    1 
ATOM   7611 C CE    . LYS B 1 483 ? 30.781  -6.298  55.656 1.00 12.64  ? 525  LYS B CE    1 
ATOM   7612 N NZ    . LYS B 1 483 ? 30.230  -7.477  54.968 1.00 12.61  ? 525  LYS B NZ    1 
ATOM   7613 N N     . ARG B 1 484 ? 28.052  -1.986  58.252 1.00 14.21  ? 526  ARG B N     1 
ATOM   7614 C CA    . ARG B 1 484 ? 27.695  -2.302  59.632 1.00 15.72  ? 526  ARG B CA    1 
ATOM   7615 C C     . ARG B 1 484 ? 26.176  -2.406  59.789 1.00 14.66  ? 526  ARG B C     1 
ATOM   7616 O O     . ARG B 1 484 ? 25.707  -3.187  60.612 1.00 15.17  ? 526  ARG B O     1 
ATOM   7617 C CB    . ARG B 1 484 ? 28.275  -1.267  60.594 1.00 17.71  ? 526  ARG B CB    1 
ATOM   7618 C CG    . ARG B 1 484 ? 29.779  -1.364  60.736 1.00 21.64  ? 526  ARG B CG    1 
ATOM   7619 C CD    . ARG B 1 484 ? 30.310  -0.281  61.661 1.00 28.05  ? 526  ARG B CD    1 
ATOM   7620 N NE    . ARG B 1 484 ? 31.743  -0.460  61.728 1.00 33.74  ? 526  ARG B NE    1 
ATOM   7621 C CZ    . ARG B 1 484 ? 32.557  0.165   62.574 1.00 41.72  ? 526  ARG B CZ    1 
ATOM   7622 N NH1   . ARG B 1 484 ? 32.094  1.088   63.403 1.00 43.63  ? 526  ARG B NH1   1 
ATOM   7623 N NH2   . ARG B 1 484 ? 33.833  -0.175  62.597 1.00 39.25  ? 526  ARG B NH2   1 
ATOM   7624 N N     . ALA B 1 485 ? 25.411  -1.623  59.012 1.00 14.60  ? 527  ALA B N     1 
ATOM   7625 C CA    . ALA B 1 485 ? 23.946  -1.658  59.096 1.00 15.60  ? 527  ALA B CA    1 
ATOM   7626 C C     . ALA B 1 485 ? 23.379  -2.933  58.442 1.00 15.29  ? 527  ALA B C     1 
ATOM   7627 O O     . ALA B 1 485 ? 22.439  -3.543  58.958 1.00 17.21  ? 527  ALA B O     1 
ATOM   7628 C CB    . ALA B 1 485 ? 23.352  -0.412  58.458 1.00 17.22  ? 527  ALA B CB    1 
ATOM   7629 N N     . ILE B 1 486 ? 23.936  -3.312  57.284 1.00 12.98  ? 528  ILE B N     1 
ATOM   7630 C CA    . ILE B 1 486 ? 23.461  -4.426  56.466 1.00 13.36  ? 528  ILE B CA    1 
ATOM   7631 C C     . ILE B 1 486 ? 23.948  -5.772  57.024 1.00 12.00  ? 528  ILE B C     1 
ATOM   7632 O O     . ILE B 1 486 ? 23.157  -6.749  56.988 1.00 13.50  ? 528  ILE B O     1 
ATOM   7633 C CB    . ILE B 1 486 ? 23.848  -4.222  54.978 1.00 12.88  ? 528  ILE B CB    1 
ATOM   7634 C CG1   . ILE B 1 486 ? 23.226  -2.932  54.411 1.00 14.40  ? 528  ILE B CG1   1 
ATOM   7635 C CG2   . ILE B 1 486 ? 23.479  -5.430  54.135 1.00 13.46  ? 528  ILE B CG2   1 
ATOM   7636 C CD1   . ILE B 1 486 ? 23.805  -2.571  53.075 1.00 14.37  ? 528  ILE B CD1   1 
ATOM   7637 N N     . ASP B 1 487 ? 25.202  -5.799  57.530 1.00 11.10  ? 529  ASP B N     1 
ATOM   7638 C CA    . ASP B 1 487 ? 25.835  -7.025  58.005 1.00 9.95   ? 529  ASP B CA    1 
ATOM   7639 C C     . ASP B 1 487 ? 26.437  -6.814  59.365 1.00 11.20  ? 529  ASP B C     1 
ATOM   7640 O O     . ASP B 1 487 ? 27.646  -6.673  59.540 1.00 11.95  ? 529  ASP B O     1 
ATOM   7641 C CB    . ASP B 1 487 ? 26.942  -7.425  57.034 1.00 10.33  ? 529  ASP B CB    1 
ATOM   7642 C CG    . ASP B 1 487 ? 27.674  -8.723  57.246 1.00 10.06  ? 529  ASP B CG    1 
ATOM   7643 O OD1   . ASP B 1 487 ? 27.272  -9.499  58.149 1.00 10.45  ? 529  ASP B OD1   1 
ATOM   7644 O OD2   . ASP B 1 487 ? 28.719  -8.905  56.590 1.00 11.28  ? 529  ASP B OD2   1 
ATOM   7645 N N     . PRO B 1 488 ? 25.585  -6.760  60.390 1.00 14.01  ? 530  PRO B N     1 
ATOM   7646 C CA    . PRO B 1 488 ? 26.074  -6.366  61.716 1.00 15.16  ? 530  PRO B CA    1 
ATOM   7647 C C     . PRO B 1 488 ? 27.137  -7.272  62.310 1.00 14.94  ? 530  PRO B C     1 
ATOM   7648 O O     . PRO B 1 488 ? 27.964  -6.801  63.104 1.00 15.50  ? 530  PRO B O     1 
ATOM   7649 C CB    . PRO B 1 488 ? 24.802  -6.379  62.585 1.00 16.38  ? 530  PRO B CB    1 
ATOM   7650 C CG    . PRO B 1 488 ? 23.655  -6.342  61.659 1.00 20.57  ? 530  PRO B CG    1 
ATOM   7651 C CD    . PRO B 1 488 ? 24.118  -6.830  60.303 1.00 15.47  ? 530  PRO B CD    1 
ATOM   7652 N N     . ASN B 1 489 ? 27.133  -8.564  61.963 1.00 12.83  ? 531  ASN B N     1 
ATOM   7653 C CA    . ASN B 1 489 ? 28.143  -9.493  62.471 1.00 12.72  ? 531  ASN B CA    1 
ATOM   7654 C C     . ASN B 1 489 ? 29.408  -9.536  61.589 1.00 13.04  ? 531  ASN B C     1 
ATOM   7655 O O     . ASN B 1 489 ? 30.393  -10.225 61.904 1.00 13.65  ? 531  ASN B O     1 
ATOM   7656 C CB    . ASN B 1 489 ? 27.596  -10.917 62.708 1.00 14.71  ? 531  ASN B CB    1 
ATOM   7657 C CG    . ASN B 1 489 ? 26.509  -10.955 63.773 1.00 17.15  ? 531  ASN B CG    1 
ATOM   7658 O OD1   . ASN B 1 489 ? 25.420  -11.541 63.603 1.00 17.77  ? 531  ASN B OD1   1 
ATOM   7659 N ND2   . ASN B 1 489 ? 26.807  -10.271 64.859 1.00 16.53  ? 531  ASN B ND2   1 
ATOM   7660 N N     . GLY B 1 490 ? 29.394  -8.830  60.440 1.00 12.99  ? 532  GLY B N     1 
ATOM   7661 C CA    . GLY B 1 490 ? 30.551  -8.780  59.571 1.00 12.23  ? 532  GLY B CA    1 
ATOM   7662 C C     . GLY B 1 490 ? 30.916  -10.155 58.988 1.00 12.13  ? 532  GLY B C     1 
ATOM   7663 O O     . GLY B 1 490 ? 32.115  -10.456 58.794 1.00 13.78  ? 532  GLY B O     1 
ATOM   7664 N N     . ILE B 1 491 ? 29.904  -10.946 58.644 1.00 11.53  ? 533  ILE B N     1 
ATOM   7665 C CA    . ILE B 1 491 ? 30.172  -12.304 58.176 1.00 12.06  ? 533  ILE B CA    1 
ATOM   7666 C C     . ILE B 1 491 ? 30.261  -12.438 56.651 1.00 12.65  ? 533  ILE B C     1 
ATOM   7667 O O     . ILE B 1 491 ? 30.547  -13.543 56.206 1.00 13.91  ? 533  ILE B O     1 
ATOM   7668 C CB    . ILE B 1 491 ? 29.285  -13.375 58.858 1.00 13.83  ? 533  ILE B CB    1 
ATOM   7669 C CG1   . ILE B 1 491 ? 27.799  -13.063 58.830 1.00 16.26  ? 533  ILE B CG1   1 
ATOM   7670 C CG2   . ILE B 1 491 ? 29.737  -13.614 60.289 1.00 13.40  ? 533  ILE B CG2   1 
ATOM   7671 C CD1   . ILE B 1 491 ? 27.194  -13.154 57.444 1.00 16.28  ? 533  ILE B CD1   1 
ATOM   7672 N N     . LEU B 1 492 ? 30.029  -11.390 55.857 1.00 10.81  ? 534  LEU B N     1 
ATOM   7673 C CA    . LEU B 1 492 ? 30.177  -11.533 54.400 1.00 10.97  ? 534  LEU B CA    1 
ATOM   7674 C C     . LEU B 1 492 ? 31.456  -10.839 53.912 1.00 10.53  ? 534  LEU B C     1 
ATOM   7675 O O     . LEU B 1 492 ? 31.626  -9.614  54.090 1.00 11.82  ? 534  LEU B O     1 
ATOM   7676 C CB    . LEU B 1 492 ? 28.990  -10.979 53.614 1.00 11.10  ? 534  LEU B CB    1 
ATOM   7677 C CG    . LEU B 1 492 ? 27.617  -11.603 53.846 1.00 10.71  ? 534  LEU B CG    1 
ATOM   7678 C CD1   . LEU B 1 492 ? 26.603  -11.078 52.807 1.00 12.09  ? 534  LEU B CD1   1 
ATOM   7679 C CD2   . LEU B 1 492 ? 27.673  -13.114 53.829 1.00 10.95  ? 534  LEU B CD2   1 
ATOM   7680 N N     . SER B 1 493 ? 32.340  -11.662 53.325 1.00 9.88   ? 535  SER B N     1 
ATOM   7681 C CA    . SER B 1 493 ? 33.556  -11.236 52.666 1.00 9.63   ? 535  SER B CA    1 
ATOM   7682 C C     . SER B 1 493 ? 34.193  -9.960  53.233 1.00 9.76   ? 535  SER B C     1 
ATOM   7683 O O     . SER B 1 493 ? 34.377  -8.958  52.539 1.00 9.58   ? 535  SER B O     1 
ATOM   7684 C CB    . SER B 1 493 ? 33.235  -11.008 51.187 1.00 10.95  ? 535  SER B CB    1 
ATOM   7685 O OG    . SER B 1 493 ? 32.825  -12.237 50.569 1.00 11.55  ? 535  SER B OG    1 
ATOM   7686 N N     . PRO B 1 494 ? 34.615  -9.941  54.509 1.00 9.66   ? 536  PRO B N     1 
ATOM   7687 C CA    . PRO B 1 494 ? 35.283  -8.772  55.073 1.00 11.51  ? 536  PRO B CA    1 
ATOM   7688 C C     . PRO B 1 494 ? 36.532  -8.436  54.255 1.00 11.71  ? 536  PRO B C     1 
ATOM   7689 O O     . PRO B 1 494 ? 37.250  -9.323  53.762 1.00 11.81  ? 536  PRO B O     1 
ATOM   7690 C CB    . PRO B 1 494 ? 35.639  -9.161  56.520 1.00 11.69  ? 536  PRO B CB    1 
ATOM   7691 C CG    . PRO B 1 494 ? 35.203  -10.569 56.711 1.00 12.74  ? 536  PRO B CG    1 
ATOM   7692 C CD    . PRO B 1 494 ? 34.403  -11.009 55.504 1.00 11.79  ? 536  PRO B CD    1 
ATOM   7693 N N     . GLY B 1 495 ? 36.694  -7.111  54.010 1.00 10.79  ? 537  GLY B N     1 
ATOM   7694 C CA    . GLY B 1 495 ? 37.801  -6.581  53.221 1.00 10.01  ? 537  GLY B CA    1 
ATOM   7695 C C     . GLY B 1 495 ? 37.565  -6.503  51.728 1.00 10.68  ? 537  GLY B C     1 
ATOM   7696 O O     . GLY B 1 495 ? 38.356  -5.848  51.025 1.00 11.59  ? 537  GLY B O     1 
ATOM   7697 N N     . LYS B 1 496 ? 36.484  -7.078  51.219 1.00 9.83   ? 538  LYS B N     1 
ATOM   7698 C CA    . LYS B 1 496 ? 36.179  -6.881  49.788 1.00 9.82   ? 538  LYS B CA    1 
ATOM   7699 C C     . LYS B 1 496 ? 36.040  -5.378  49.501 1.00 10.85  ? 538  LYS B C     1 
ATOM   7700 O O     . LYS B 1 496 ? 35.390  -4.671  50.252 1.00 9.73   ? 538  LYS B O     1 
ATOM   7701 C CB    . LYS B 1 496 ? 34.869  -7.569  49.443 1.00 11.14  ? 538  LYS B CB    1 
ATOM   7702 C CG    . LYS B 1 496 ? 34.329  -7.353  48.037 1.00 12.24  ? 538  LYS B CG    1 
ATOM   7703 C CD    . LYS B 1 496 ? 35.215  -7.892  46.959 1.00 11.50  ? 538  LYS B CD    1 
ATOM   7704 C CE    . LYS B 1 496 ? 34.608  -7.637  45.578 1.00 12.04  ? 538  LYS B CE    1 
ATOM   7705 N NZ    . LYS B 1 496 ? 35.590  -7.887  44.474 1.00 12.48  ? 538  LYS B NZ    1 
ATOM   7706 N N     . SER B 1 497 ? 36.704  -4.891  48.449 1.00 9.72   ? 539  SER B N     1 
ATOM   7707 C CA    . SER B 1 497 ? 36.673  -3.463  48.102 1.00 10.10  ? 539  SER B CA    1 
ATOM   7708 C C     . SER B 1 497 ? 37.162  -2.566  49.230 1.00 10.37  ? 539  SER B C     1 
ATOM   7709 O O     . SER B 1 497 ? 36.849  -1.376  49.243 1.00 10.67  ? 539  SER B O     1 
ATOM   7710 C CB    . SER B 1 497 ? 35.317  -3.051  47.597 1.00 11.01  ? 539  SER B CB    1 
ATOM   7711 O OG    . SER B 1 497 ? 34.973  -3.823  46.445 1.00 11.03  ? 539  SER B OG    1 
ATOM   7712 N N     . GLY B 1 498 ? 38.012  -3.100  50.128 1.00 10.97  ? 540  GLY B N     1 
ATOM   7713 C CA    . GLY B 1 498 ? 38.503  -2.341  51.268 1.00 11.52  ? 540  GLY B CA    1 
ATOM   7714 C C     . GLY B 1 498 ? 37.456  -2.049  52.333 1.00 11.75  ? 540  GLY B C     1 
ATOM   7715 O O     . GLY B 1 498 ? 37.648  -1.151  53.146 1.00 13.59  ? 540  GLY B O     1 
ATOM   7716 N N     . ILE B 1 499 ? 36.317  -2.738  52.285 1.00 10.95  ? 541  ILE B N     1 
ATOM   7717 C CA    . ILE B 1 499 ? 35.220  -2.527  53.234 1.00 10.73  ? 541  ILE B CA    1 
ATOM   7718 C C     . ILE B 1 499 ? 35.362  -3.502  54.381 1.00 12.78  ? 541  ILE B C     1 
ATOM   7719 O O     . ILE B 1 499 ? 35.118  -4.689  54.186 1.00 14.02  ? 541  ILE B O     1 
ATOM   7720 C CB    . ILE B 1 499 ? 33.864  -2.687  52.541 1.00 11.42  ? 541  ILE B CB    1 
ATOM   7721 C CG1   . ILE B 1 499 ? 33.735  -1.802  51.316 1.00 12.15  ? 541  ILE B CG1   1 
ATOM   7722 C CG2   . ILE B 1 499 ? 32.713  -2.464  53.507 1.00 13.03  ? 541  ILE B CG2   1 
ATOM   7723 C CD1   . ILE B 1 499 ? 32.477  -2.043  50.509 1.00 12.94  ? 541  ILE B CD1   1 
ATOM   7724 N N     . HIS B 1 500 ? 35.666  -2.982  55.575 1.00 13.62  ? 542  HIS B N     1 
ATOM   7725 C CA    . HIS B 1 500 ? 35.868  -3.801  56.765 1.00 15.44  ? 542  HIS B CA    1 
ATOM   7726 C C     . HIS B 1 500 ? 34.776  -3.543  57.812 1.00 17.82  ? 542  HIS B C     1 
ATOM   7727 O O     . HIS B 1 500 ? 34.415  -2.401  58.052 1.00 20.32  ? 542  HIS B O     1 
ATOM   7728 C CB    . HIS B 1 500 ? 37.214  -3.428  57.367 1.00 15.78  ? 542  HIS B CB    1 
ATOM   7729 C CG    . HIS B 1 500 ? 38.361  -3.877  56.516 1.00 15.30  ? 542  HIS B CG    1 
ATOM   7730 N ND1   . HIS B 1 500 ? 39.003  -3.119  55.568 1.00 18.61  ? 542  HIS B ND1   1 
ATOM   7731 C CD2   . HIS B 1 500 ? 38.958  -5.070  56.517 1.00 13.71  ? 542  HIS B CD2   1 
ATOM   7732 C CE1   . HIS B 1 500 ? 39.957  -3.871  55.006 1.00 15.18  ? 542  HIS B CE1   1 
ATOM   7733 N NE2   . HIS B 1 500 ? 39.960  -5.039  55.593 1.00 18.46  ? 542  HIS B NE2   1 
ATOM   7734 N N     . PRO B 1 501 ? 34.268  -4.579  58.484 1.00 18.74  ? 543  PRO B N     1 
ATOM   7735 C CA    . PRO B 1 501 ? 33.445  -4.374  59.677 1.00 23.16  ? 543  PRO B CA    1 
ATOM   7736 C C     . PRO B 1 501 ? 34.171  -3.578  60.776 1.00 26.04  ? 543  PRO B C     1 
ATOM   7737 O O     . PRO B 1 501 ? 35.413  -3.616  60.799 1.00 27.16  ? 543  PRO B O     1 
ATOM   7738 C CB    . PRO B 1 501 ? 33.190  -5.785  60.237 1.00 24.39  ? 543  PRO B CB    1 
ATOM   7739 C CG    . PRO B 1 501 ? 33.557  -6.725  59.140 1.00 24.53  ? 543  PRO B CG    1 
ATOM   7740 C CD    . PRO B 1 501 ? 34.523  -5.995  58.212 1.00 21.92  ? 543  PRO B CD    1 
HETATM 7741 P PA    . FAD C 2 .   ? 11.651  17.834  40.382 1.00 11.04  ? 601  FAD A PA    1 
HETATM 7742 O O1A   . FAD C 2 .   ? 10.178  17.987  40.659 1.00 9.93   ? 601  FAD A O1A   1 
HETATM 7743 O O2A   . FAD C 2 .   ? 12.548  18.949  40.851 1.00 12.42  ? 601  FAD A O2A   1 
HETATM 7744 O O5B   . FAD C 2 .   ? 12.203  16.473  40.976 1.00 11.22  ? 601  FAD A O5B   1 
HETATM 7745 C C5B   . FAD C 2 .   ? 11.460  15.240  41.032 1.00 11.26  ? 601  FAD A C5B   1 
HETATM 7746 C C4B   . FAD C 2 .   ? 11.748  14.546  42.358 1.00 11.89  ? 601  FAD A C4B   1 
HETATM 7747 O O4B   . FAD C 2 .   ? 13.152  14.158  42.468 1.00 12.74  ? 601  FAD A O4B   1 
HETATM 7748 C C3B   . FAD C 2 .   ? 11.487  15.406  43.596 1.00 11.74  ? 601  FAD A C3B   1 
HETATM 7749 O O3B   . FAD C 2 .   ? 10.117  15.458  43.941 1.00 14.46  ? 601  FAD A O3B   1 
HETATM 7750 C C2B   . FAD C 2 .   ? 12.410  14.759  44.624 1.00 12.56  ? 601  FAD A C2B   1 
HETATM 7751 O O2B   . FAD C 2 .   ? 11.885  13.557  45.143 1.00 17.30  ? 601  FAD A O2B   1 
HETATM 7752 C C1B   . FAD C 2 .   ? 13.617  14.378  43.811 1.00 12.27  ? 601  FAD A C1B   1 
HETATM 7753 N N9A   . FAD C 2 .   ? 14.646  15.385  43.748 1.00 12.53  ? 601  FAD A N9A   1 
HETATM 7754 C C8A   . FAD C 2 .   ? 14.719  16.447  42.809 1.00 13.00  ? 601  FAD A C8A   1 
HETATM 7755 N N7A   . FAD C 2 .   ? 15.835  17.152  42.929 1.00 11.46  ? 601  FAD A N7A   1 
HETATM 7756 C C5A   . FAD C 2 .   ? 16.554  16.470  43.902 1.00 11.43  ? 601  FAD A C5A   1 
HETATM 7757 C C6A   . FAD C 2 .   ? 17.832  16.714  44.436 1.00 10.41  ? 601  FAD A C6A   1 
HETATM 7758 N N6A   . FAD C 2 .   ? 18.605  17.684  44.000 1.00 10.42  ? 601  FAD A N6A   1 
HETATM 7759 N N1A   . FAD C 2 .   ? 18.294  15.891  45.426 1.00 10.28  ? 601  FAD A N1A   1 
HETATM 7760 C C2A   . FAD C 2 .   ? 17.489  14.866  45.763 1.00 12.16  ? 601  FAD A C2A   1 
HETATM 7761 N N3A   . FAD C 2 .   ? 16.238  14.561  45.368 1.00 11.79  ? 601  FAD A N3A   1 
HETATM 7762 C C4A   . FAD C 2 .   ? 15.800  15.446  44.464 1.00 10.58  ? 601  FAD A C4A   1 
HETATM 7763 N N1    . FAD C 2 .   ? 7.854   13.013  33.081 1.00 11.51  ? 601  FAD A N1    1 
HETATM 7764 C C2    . FAD C 2 .   ? 8.705   12.270  32.354 1.00 10.84  ? 601  FAD A C2    1 
HETATM 7765 O O2    . FAD C 2 .   ? 9.684   11.706  32.896 1.00 11.42  ? 601  FAD A O2    1 
HETATM 7766 N N3    . FAD C 2 .   ? 8.528   12.048  30.988 1.00 10.23  ? 601  FAD A N3    1 
HETATM 7767 C C4    . FAD C 2 .   ? 7.533   12.688  30.275 1.00 12.45  ? 601  FAD A C4    1 
HETATM 7768 O O4    . FAD C 2 .   ? 7.485   12.548  29.031 1.00 11.02  ? 601  FAD A O4    1 
HETATM 7769 C C4X   . FAD C 2 .   ? 6.606   13.448  31.033 1.00 12.18  ? 601  FAD A C4X   1 
HETATM 7770 N N5    . FAD C 2 .   ? 5.586   14.058  30.412 1.00 13.40  ? 601  FAD A N5    1 
HETATM 7771 C C5X   . FAD C 2 .   ? 4.732   14.816  31.171 1.00 11.36  ? 601  FAD A C5X   1 
HETATM 7772 C C6    . FAD C 2 .   ? 3.587   15.361  30.527 1.00 12.18  ? 601  FAD A C6    1 
HETATM 7773 C C7    . FAD C 2 .   ? 2.675   16.119  31.209 1.00 12.24  ? 601  FAD A C7    1 
HETATM 7774 C C7M   . FAD C 2 .   ? 1.503   16.686  30.463 1.00 13.25  ? 601  FAD A C7M   1 
HETATM 7775 C C8    . FAD C 2 .   ? 2.854   16.312  32.590 1.00 11.86  ? 601  FAD A C8    1 
HETATM 7776 C C8M   . FAD C 2 .   ? 1.865   17.119  33.382 1.00 14.13  ? 601  FAD A C8M   1 
HETATM 7777 C C9    . FAD C 2 .   ? 3.941   15.746  33.251 1.00 11.32  ? 601  FAD A C9    1 
HETATM 7778 C C9A   . FAD C 2 .   ? 4.893   14.985  32.557 1.00 11.40  ? 601  FAD A C9A   1 
HETATM 7779 N N10   . FAD C 2 .   ? 6.008   14.408  33.168 1.00 10.43  ? 601  FAD A N10   1 
HETATM 7780 C C10   . FAD C 2 .   ? 6.841   13.566  32.457 1.00 10.84  ? 601  FAD A C10   1 
HETATM 7781 C "C1'" . FAD C 2 .   ? 6.142   14.452  34.646 1.00 11.37  ? 601  FAD A "C1'" 1 
HETATM 7782 C "C2'" . FAD C 2 .   ? 6.971   15.596  35.233 1.00 10.62  ? 601  FAD A "C2'" 1 
HETATM 7783 O "O2'" . FAD C 2 .   ? 6.333   16.835  34.933 1.00 11.98  ? 601  FAD A "O2'" 1 
HETATM 7784 C "C3'" . FAD C 2 .   ? 8.419   15.601  34.727 1.00 11.54  ? 601  FAD A "C3'" 1 
HETATM 7785 O "O3'" . FAD C 2 .   ? 9.002   14.343  34.986 1.00 11.62  ? 601  FAD A "O3'" 1 
HETATM 7786 C "C4'" . FAD C 2 .   ? 9.297   16.715  35.287 1.00 11.26  ? 601  FAD A "C4'" 1 
HETATM 7787 O "O4'" . FAD C 2 .   ? 10.555  16.744  34.574 1.00 12.58  ? 601  FAD A "O4'" 1 
HETATM 7788 C "C5'" . FAD C 2 .   ? 9.544   16.550  36.774 1.00 11.50  ? 601  FAD A "C5'" 1 
HETATM 7789 O "O5'" . FAD C 2 .   ? 9.730   17.826  37.442 1.00 11.39  ? 601  FAD A "O5'" 1 
HETATM 7790 P P     . FAD C 2 .   ? 11.196  18.451  37.611 1.00 10.85  ? 601  FAD A P     1 
HETATM 7791 O O1P   . FAD C 2 .   ? 12.060  18.176  36.409 1.00 10.92  ? 601  FAD A O1P   1 
HETATM 7792 O O2P   . FAD C 2 .   ? 11.029  19.873  38.065 1.00 10.77  ? 601  FAD A O2P   1 
HETATM 7793 O O3P   . FAD C 2 .   ? 11.885  17.641  38.794 1.00 10.34  ? 601  FAD A O3P   1 
HETATM 7794 C CAI   . V55 D 3 .   ? 4.404   11.040  30.736 1.00 17.20  ? 602  V55 A CAI   1 
HETATM 7795 C CAG   . V55 D 3 .   ? 5.390   10.051  30.613 1.00 16.22  ? 602  V55 A CAG   1 
HETATM 7796 C CAK   . V55 D 3 .   ? 5.955   9.511   31.752 1.00 15.28  ? 602  V55 A CAK   1 
HETATM 7797 C CAJ   . V55 D 3 .   ? 5.495   9.880   33.000 1.00 12.69  ? 602  V55 A CAJ   1 
HETATM 7798 C CAF   . V55 D 3 .   ? 4.480   10.811  33.109 1.00 14.50  ? 602  V55 A CAF   1 
HETATM 7799 O OAB   . V55 D 3 .   ? 4.062   11.419  28.421 1.00 34.26  ? 602  V55 A OAB   1 
HETATM 7800 C CAE   . V55 D 3 .   ? 3.977   11.419  31.990 1.00 16.17  ? 602  V55 A CAE   1 
HETATM 7801 C CAD   . V55 D 3 .   ? 3.789   11.670  29.549 1.00 25.75  ? 602  V55 A CAD   1 
HETATM 7802 C CAA   . V55 D 3 .   ? 7.308   7.965   30.583 1.00 15.37  ? 602  V55 A CAA   1 
HETATM 7803 O OAH   . V55 D 3 .   ? 6.912   8.541   31.820 1.00 13.00  ? 602  V55 A OAH   1 
HETATM 7804 O OAC   . V55 D 3 .   ? 6.022   9.324   34.153 1.00 12.14  ? 602  V55 A OAC   1 
HETATM 7805 C C1    . GOL E 4 .   ? 7.653   28.497  43.587 1.00 37.84  ? 603  GOL A C1    1 
HETATM 7806 O O1    . GOL E 4 .   ? 8.140   29.806  43.351 1.00 40.10  ? 603  GOL A O1    1 
HETATM 7807 C C2    . GOL E 4 .   ? 8.606   27.498  42.998 1.00 36.49  ? 603  GOL A C2    1 
HETATM 7808 O O2    . GOL E 4 .   ? 9.926   27.862  43.427 1.00 30.69  ? 603  GOL A O2    1 
HETATM 7809 C C3    . GOL E 4 .   ? 8.248   26.083  43.388 1.00 39.56  ? 603  GOL A C3    1 
HETATM 7810 O O3    . GOL E 4 .   ? 8.925   25.118  42.587 1.00 37.58  ? 603  GOL A O3    1 
HETATM 7811 C C1    . PEG F 5 .   ? 9.660   -0.307  47.793 1.00 35.05  ? 604  PEG A C1    1 
HETATM 7812 O O1    . PEG F 5 .   ? 9.939   -0.678  49.155 1.00 34.13  ? 604  PEG A O1    1 
HETATM 7813 C C2    . PEG F 5 .   ? 10.770  -0.654  46.775 1.00 34.09  ? 604  PEG A C2    1 
HETATM 7814 O O2    . PEG F 5 .   ? 10.661  -1.999  46.290 1.00 32.91  ? 604  PEG A O2    1 
HETATM 7815 C C3    . PEG F 5 .   ? 11.348  -2.303  45.086 1.00 38.87  ? 604  PEG A C3    1 
HETATM 7816 C C4    . PEG F 5 .   ? 12.782  -2.084  45.260 1.00 33.57  ? 604  PEG A C4    1 
HETATM 7817 O O4    . PEG F 5 .   ? 13.287  -2.656  46.446 1.00 19.55  ? 604  PEG A O4    1 
HETATM 7818 P PA    . FAD G 2 .   ? 34.016  -15.200 40.367 1.00 11.32  ? 601  FAD B PA    1 
HETATM 7819 O O1A   . FAD G 2 .   ? 35.480  -15.307 40.681 1.00 12.11  ? 601  FAD B O1A   1 
HETATM 7820 O O2A   . FAD G 2 .   ? 33.112  -16.311 40.831 1.00 11.56  ? 601  FAD B O2A   1 
HETATM 7821 O O5B   . FAD G 2 .   ? 33.451  -13.837 40.968 1.00 11.02  ? 601  FAD B O5B   1 
HETATM 7822 C C5B   . FAD G 2 .   ? 34.212  -12.619 41.049 1.00 11.96  ? 601  FAD B C5B   1 
HETATM 7823 C C4B   . FAD G 2 .   ? 33.930  -11.924 42.353 1.00 13.24  ? 601  FAD B C4B   1 
HETATM 7824 O O4B   . FAD G 2 .   ? 32.539  -11.514 42.440 1.00 12.77  ? 601  FAD B O4B   1 
HETATM 7825 C C3B   . FAD G 2 .   ? 34.195  -12.791 43.583 1.00 12.73  ? 601  FAD B C3B   1 
HETATM 7826 O O3B   . FAD G 2 .   ? 35.559  -12.823 43.981 1.00 13.70  ? 601  FAD B O3B   1 
HETATM 7827 C C2B   . FAD G 2 .   ? 33.292  -12.133 44.626 1.00 15.17  ? 601  FAD B C2B   1 
HETATM 7828 O O2B   . FAD G 2 .   ? 33.818  -10.933 45.161 1.00 17.92  ? 601  FAD B O2B   1 
HETATM 7829 C C1B   . FAD G 2 .   ? 32.105  -11.711 43.797 1.00 12.97  ? 601  FAD B C1B   1 
HETATM 7830 N N9A   . FAD G 2 .   ? 31.025  -12.724 43.710 1.00 12.66  ? 601  FAD B N9A   1 
HETATM 7831 C C8A   . FAD G 2 .   ? 31.002  -13.794 42.833 1.00 11.15  ? 601  FAD B C8A   1 
HETATM 7832 N N7A   . FAD G 2 .   ? 29.870  -14.474 42.895 1.00 10.35  ? 601  FAD B N7A   1 
HETATM 7833 C C5A   . FAD G 2 .   ? 29.151  -13.859 43.927 1.00 10.98  ? 601  FAD B C5A   1 
HETATM 7834 C C6A   . FAD G 2 .   ? 27.842  -14.059 44.387 1.00 11.05  ? 601  FAD B C6A   1 
HETATM 7835 N N6A   . FAD G 2 .   ? 27.060  -15.043 43.947 1.00 10.25  ? 601  FAD B N6A   1 
HETATM 7836 N N1A   . FAD G 2 .   ? 27.399  -13.235 45.380 1.00 10.74  ? 601  FAD B N1A   1 
HETATM 7837 C C2A   . FAD G 2 .   ? 28.204  -12.215 45.750 1.00 11.67  ? 601  FAD B C2A   1 
HETATM 7838 N N3A   . FAD G 2 .   ? 29.442  -11.907 45.353 1.00 12.74  ? 601  FAD B N3A   1 
HETATM 7839 C C4A   . FAD G 2 .   ? 29.868  -12.800 44.455 1.00 10.68  ? 601  FAD B C4A   1 
HETATM 7840 N N1    . FAD G 2 .   ? 37.824  -10.371 33.058 1.00 10.18  ? 601  FAD B N1    1 
HETATM 7841 C C2    . FAD G 2 .   ? 36.972  -9.625  32.330 1.00 9.57   ? 601  FAD B C2    1 
HETATM 7842 O O2    . FAD G 2 .   ? 35.987  -9.061  32.869 1.00 10.93  ? 601  FAD B O2    1 
HETATM 7843 N N3    . FAD G 2 .   ? 37.152  -9.426  30.975 1.00 9.64   ? 601  FAD B N3    1 
HETATM 7844 C C4    . FAD G 2 .   ? 38.160  -10.056 30.291 1.00 11.59  ? 601  FAD B C4    1 
HETATM 7845 O O4    . FAD G 2 .   ? 38.202  -9.915  29.049 1.00 12.72  ? 601  FAD B O4    1 
HETATM 7846 C C4X   . FAD G 2 .   ? 39.062  -10.852 31.032 1.00 11.03  ? 601  FAD B C4X   1 
HETATM 7847 N N5    . FAD G 2 .   ? 40.071  -11.452 30.387 1.00 13.82  ? 601  FAD B N5    1 
HETATM 7848 C C5X   . FAD G 2 .   ? 40.927  -12.204 31.150 1.00 12.36  ? 601  FAD B C5X   1 
HETATM 7849 C C6    . FAD G 2 .   ? 42.073  -12.734 30.509 1.00 11.89  ? 601  FAD B C6    1 
HETATM 7850 C C7    . FAD G 2 .   ? 42.981  -13.502 31.193 1.00 12.83  ? 601  FAD B C7    1 
HETATM 7851 C C7M   . FAD G 2 .   ? 44.167  -14.080 30.475 1.00 14.53  ? 601  FAD B C7M   1 
HETATM 7852 C C8    . FAD G 2 .   ? 42.824  -13.677 32.587 1.00 12.69  ? 601  FAD B C8    1 
HETATM 7853 C C8M   . FAD G 2 .   ? 43.815  -14.487 33.382 1.00 13.81  ? 601  FAD B C8M   1 
HETATM 7854 C C9    . FAD G 2 .   ? 41.713  -13.160 33.222 1.00 11.40  ? 601  FAD B C9    1 
HETATM 7855 C C9A   . FAD G 2 .   ? 40.782  -12.373 32.541 1.00 11.98  ? 601  FAD B C9A   1 
HETATM 7856 N N10   . FAD G 2 .   ? 39.677  -11.794 33.172 1.00 10.25  ? 601  FAD B N10   1 
HETATM 7857 C C10   . FAD G 2 .   ? 38.816  -10.986 32.431 1.00 10.23  ? 601  FAD B C10   1 
HETATM 7858 C "C1'" . FAD G 2 .   ? 39.526  -11.820 34.631 1.00 10.34  ? 601  FAD B "C1'" 1 
HETATM 7859 C "C2'" . FAD G 2 .   ? 38.661  -12.935 35.235 1.00 10.56  ? 601  FAD B "C2'" 1 
HETATM 7860 O "O2'" . FAD G 2 .   ? 39.313  -14.186 34.948 1.00 12.70  ? 601  FAD B "O2'" 1 
HETATM 7861 C "C3'" . FAD G 2 .   ? 37.215  -12.941 34.742 1.00 11.01  ? 601  FAD B "C3'" 1 
HETATM 7862 O "O3'" . FAD G 2 .   ? 36.653  -11.670 34.993 1.00 10.66  ? 601  FAD B "O3'" 1 
HETATM 7863 C "C4'" . FAD G 2 .   ? 36.350  -14.065 35.290 1.00 10.40  ? 601  FAD B "C4'" 1 
HETATM 7864 O "O4'" . FAD G 2 .   ? 35.095  -14.120 34.569 1.00 11.75  ? 601  FAD B "O4'" 1 
HETATM 7865 C "C5'" . FAD G 2 .   ? 36.110  -13.894 36.768 1.00 10.23  ? 601  FAD B "C5'" 1 
HETATM 7866 O "O5'" . FAD G 2 .   ? 35.945  -15.208 37.396 1.00 9.98   ? 601  FAD B "O5'" 1 
HETATM 7867 P P     . FAD G 2 .   ? 34.467  -15.798 37.602 1.00 11.04  ? 601  FAD B P     1 
HETATM 7868 O O1P   . FAD G 2 .   ? 33.618  -15.524 36.405 1.00 10.24  ? 601  FAD B O1P   1 
HETATM 7869 O O2P   . FAD G 2 .   ? 34.637  -17.207 38.053 1.00 10.58  ? 601  FAD B O2P   1 
HETATM 7870 O O3P   . FAD G 2 .   ? 33.808  -14.974 38.796 1.00 10.79  ? 601  FAD B O3P   1 
HETATM 7871 C CAI   . V55 H 3 .   ? 41.276  -8.425  30.737 1.00 16.08  ? 602  V55 B CAI   1 
HETATM 7872 C CAG   . V55 H 3 .   ? 40.291  -7.437  30.605 1.00 14.85  ? 602  V55 B CAG   1 
HETATM 7873 C CAK   . V55 H 3 .   ? 39.715  -6.898  31.732 1.00 12.94  ? 602  V55 B CAK   1 
HETATM 7874 C CAJ   . V55 H 3 .   ? 40.156  -7.291  32.999 1.00 12.42  ? 602  V55 B CAJ   1 
HETATM 7875 C CAF   . V55 H 3 .   ? 41.157  -8.230  33.118 1.00 14.25  ? 602  V55 B CAF   1 
HETATM 7876 O OAB   . V55 H 3 .   ? 41.695  -8.714  28.436 1.00 34.49  ? 602  V55 B OAB   1 
HETATM 7877 C CAE   . V55 H 3 .   ? 41.678  -8.821  31.995 1.00 14.56  ? 602  V55 B CAE   1 
HETATM 7878 C CAD   . V55 H 3 .   ? 41.910  -9.030  29.560 1.00 25.85  ? 602  V55 B CAD   1 
HETATM 7879 C CAA   . V55 H 3 .   ? 38.308  -5.380  30.561 1.00 18.76  ? 602  V55 B CAA   1 
HETATM 7880 O OAH   . V55 H 3 .   ? 38.752  -5.941  31.780 1.00 13.78  ? 602  V55 B OAH   1 
HETATM 7881 O OAC   . V55 H 3 .   ? 39.612  -6.722  34.120 1.00 13.81  ? 602  V55 B OAC   1 
HETATM 7882 C C1    . GOL I 4 .   ? 37.474  -23.870 42.499 1.00 44.09  ? 603  GOL B C1    1 
HETATM 7883 O O1    . GOL I 4 .   ? 36.771  -22.644 42.703 1.00 37.50  ? 603  GOL B O1    1 
HETATM 7884 C C2    . GOL I 4 .   ? 37.137  -24.861 43.584 1.00 37.53  ? 603  GOL B C2    1 
HETATM 7885 O O2    . GOL I 4 .   ? 35.787  -25.306 43.403 1.00 32.19  ? 603  GOL B O2    1 
HETATM 7886 C C3    . GOL I 4 .   ? 38.101  -26.022 43.658 1.00 38.16  ? 603  GOL B C3    1 
HETATM 7887 O O3    . GOL I 4 .   ? 37.484  -27.252 43.311 1.00 39.54  ? 603  GOL B O3    1 
HETATM 7888 O O     . HOH J 6 .   ? -4.222  4.825   8.814  1.00 33.96  ? 701  HOH A O     1 
HETATM 7889 O O     . HOH J 6 .   ? 21.145  25.509  18.128 1.00 34.86  ? 702  HOH A O     1 
HETATM 7890 O O     . HOH J 6 .   ? 43.732  16.147  36.909 1.00 37.42  ? 703  HOH A O     1 
HETATM 7891 O O     . HOH J 6 .   ? -14.048 25.123  32.630 1.00 37.60  ? 704  HOH A O     1 
HETATM 7892 O O     . HOH J 6 .   ? -14.999 -3.698  38.208 1.00 35.60  ? 705  HOH A O     1 
HETATM 7893 O O     . HOH J 6 .   ? 16.986  14.275  32.235 1.00 35.00  ? 706  HOH A O     1 
HETATM 7894 O O     . HOH J 6 .   ? -1.491  20.650  25.679 1.00 38.82  ? 707  HOH A O     1 
HETATM 7895 O O     . HOH J 6 .   ? -11.886 22.999  32.208 1.00 23.28  ? 708  HOH A O     1 
HETATM 7896 O O     . HOH J 6 .   ? -19.631 18.460  44.431 1.00 35.66  ? 709  HOH A O     1 
HETATM 7897 O O     . HOH J 6 .   ? -17.342 18.567  37.113 1.00 34.59  ? 710  HOH A O     1 
HETATM 7898 O O     . HOH J 6 .   ? 2.702   12.616  26.738 1.00 46.46  ? 711  HOH A O     1 
HETATM 7899 O O     . HOH J 6 .   ? 6.966   24.078  41.462 1.00 21.81  ? 712  HOH A O     1 
HETATM 7900 O O     . HOH J 6 .   ? 31.502  2.887   42.927 1.00 21.57  ? 713  HOH A O     1 
HETATM 7901 O O     . HOH J 6 .   ? -0.634  21.942  49.534 1.00 26.95  ? 714  HOH A O     1 
HETATM 7902 O O     . HOH J 6 .   ? 39.931  9.462   37.625 1.00 23.63  ? 715  HOH A O     1 
HETATM 7903 O O     . HOH J 6 .   ? -13.124 20.506  19.092 1.00 41.20  ? 716  HOH A O     1 
HETATM 7904 O O     . HOH J 6 .   ? -12.097 19.897  45.693 1.00 34.38  ? 717  HOH A O     1 
HETATM 7905 O O     . HOH J 6 .   ? 28.480  25.439  60.593 1.00 26.55  ? 718  HOH A O     1 
HETATM 7906 O O     . HOH J 6 .   ? 25.614  6.241   37.069 1.00 17.15  ? 719  HOH A O     1 
HETATM 7907 O O     . HOH J 6 .   ? -7.048  -6.222  22.046 1.00 28.76  ? 720  HOH A O     1 
HETATM 7908 O O     . HOH J 6 .   ? 24.174  29.840  27.492 1.00 37.10  ? 721  HOH A O     1 
HETATM 7909 O O     . HOH J 6 .   ? 24.546  5.608   60.995 1.00 28.42  ? 722  HOH A O     1 
HETATM 7910 O O     . HOH J 6 .   ? 14.534  -8.644  17.568 1.00 40.52  ? 723  HOH A O     1 
HETATM 7911 O O     . HOH J 6 .   ? -8.052  19.588  27.513 1.00 26.76  ? 724  HOH A O     1 
HETATM 7912 O O     . HOH J 6 .   ? -20.288 20.775  29.669 1.00 24.95  ? 725  HOH A O     1 
HETATM 7913 O O     . HOH J 6 .   ? -22.505 19.689  32.564 1.00 28.38  ? 726  HOH A O     1 
HETATM 7914 O O     . HOH J 6 .   ? -13.807 23.224  45.527 1.00 31.45  ? 727  HOH A O     1 
HETATM 7915 O O     . HOH J 6 .   ? 24.326  0.922   2.913  1.00 28.29  ? 728  HOH A O     1 
HETATM 7916 O O     . HOH J 6 .   ? -3.739  9.909   43.092 1.00 24.69  ? 729  HOH A O     1 
HETATM 7917 O O     . HOH J 6 .   ? 34.269  8.650   43.801 1.00 14.64  ? 730  HOH A O     1 
HETATM 7918 O O     . HOH J 6 .   ? 8.534   8.113   60.595 1.00 28.47  ? 731  HOH A O     1 
HETATM 7919 O O     . HOH J 6 .   ? 11.578  12.831  60.506 1.00 26.15  ? 732  HOH A O     1 
HETATM 7920 O O     . HOH J 6 .   ? 5.429   7.401   4.384  1.00 31.09  ? 733  HOH A O     1 
HETATM 7921 O O     . HOH J 6 .   ? 12.930  23.752  30.625 1.00 18.24  ? 734  HOH A O     1 
HETATM 7922 O O     . HOH J 6 .   ? 5.164   14.206  59.347 1.00 35.52  ? 735  HOH A O     1 
HETATM 7923 O O     . HOH J 6 .   ? 19.994  -5.541  21.194 1.00 21.15  ? 736  HOH A O     1 
HETATM 7924 O O     . HOH J 6 .   ? 9.217   -2.200  3.458  1.00 26.40  ? 737  HOH A O     1 
HETATM 7925 O O     . HOH J 6 .   ? 33.813  16.652  35.235 1.00 25.44  ? 738  HOH A O     1 
HETATM 7926 O O     . HOH J 6 .   ? 11.049  21.863  29.799 1.00 36.89  ? 739  HOH A O     1 
HETATM 7927 O O     . HOH J 6 .   ? -14.500 11.942  11.308 1.00 27.25  ? 740  HOH A O     1 
HETATM 7928 O O     . HOH J 6 .   ? 42.306  12.436  45.582 1.00 34.81  ? 741  HOH A O     1 
HETATM 7929 O O     . HOH J 6 .   ? 23.642  22.977  19.273 1.00 33.34  ? 742  HOH A O     1 
HETATM 7930 O O     . HOH J 6 .   ? 9.197   17.760  43.136 1.00 14.88  ? 743  HOH A O     1 
HETATM 7931 O O     . HOH J 6 .   ? 31.820  22.583  50.712 1.00 26.51  ? 744  HOH A O     1 
HETATM 7932 O O     . HOH J 6 .   ? 5.560   -6.760  37.597 1.00 23.54  ? 745  HOH A O     1 
HETATM 7933 O O     . HOH J 6 .   ? 29.497  5.534   40.808 1.00 17.37  ? 746  HOH A O     1 
HETATM 7934 O O     . HOH J 6 .   ? 9.564   12.341  8.457  1.00 24.78  ? 747  HOH A O     1 
HETATM 7935 O O     . HOH J 6 .   ? -5.726  13.227  51.026 1.00 24.30  ? 748  HOH A O     1 
HETATM 7936 O O     . HOH J 6 .   ? 17.231  27.854  45.363 1.00 12.32  ? 749  HOH A O     1 
HETATM 7937 O O     . HOH J 6 .   ? -4.967  11.548  48.198 1.00 20.66  ? 750  HOH A O     1 
HETATM 7938 O O     . HOH J 6 .   ? 4.579   -7.554  11.877 1.00 27.63  ? 751  HOH A O     1 
HETATM 7939 O O     . HOH J 6 .   ? 14.795  28.167  31.900 1.00 26.85  ? 752  HOH A O     1 
HETATM 7940 O O     . HOH J 6 .   ? 12.847  14.951  47.986 1.00 17.06  ? 753  HOH A O     1 
HETATM 7941 O O     . HOH J 6 .   ? 31.654  25.331  46.024 1.00 32.05  ? 754  HOH A O     1 
HETATM 7942 O O     . HOH J 6 .   ? 11.567  25.131  42.258 1.00 25.17  ? 755  HOH A O     1 
HETATM 7943 O O     . HOH J 6 .   ? 27.704  30.414  49.915 1.00 27.60  ? 756  HOH A O     1 
HETATM 7944 O O     . HOH J 6 .   ? 3.358   -12.220 30.250 1.00 30.56  ? 757  HOH A O     1 
HETATM 7945 O O     . HOH J 6 .   ? -6.741  -5.790  15.835 1.00 38.58  ? 758  HOH A O     1 
HETATM 7946 O O     . HOH J 6 .   ? 1.328   24.709  39.810 1.00 28.30  ? 759  HOH A O     1 
HETATM 7947 O O     . HOH J 6 .   ? 16.109  27.097  38.005 1.00 14.15  ? 760  HOH A O     1 
HETATM 7948 O O     . HOH J 6 .   ? 14.970  13.131  47.430 1.00 13.76  ? 761  HOH A O     1 
HETATM 7949 O O     . HOH J 6 .   ? -4.991  8.403   45.912 1.00 24.18  ? 762  HOH A O     1 
HETATM 7950 O O     . HOH J 6 .   ? 4.380   -5.821  5.504  1.00 35.72  ? 763  HOH A O     1 
HETATM 7951 O O     . HOH J 6 .   ? -11.757 1.147   17.859 1.00 34.26  ? 764  HOH A O     1 
HETATM 7952 O O     . HOH J 6 .   ? -21.189 8.769   24.559 1.00 20.86  ? 765  HOH A O     1 
HETATM 7953 O O     . HOH J 6 .   ? -12.255 -3.260  30.168 1.00 26.22  ? 766  HOH A O     1 
HETATM 7954 O O     . HOH J 6 .   ? 4.616   -11.965 18.230 1.00 28.25  ? 767  HOH A O     1 
HETATM 7955 O O     . HOH J 6 .   ? 21.572  2.055   2.945  1.00 34.78  ? 768  HOH A O     1 
HETATM 7956 O O     . HOH J 6 .   ? 24.186  10.780  16.853 1.00 27.95  ? 769  HOH A O     1 
HETATM 7957 O O     . HOH J 6 .   ? -15.580 7.091   29.507 1.00 19.80  ? 770  HOH A O     1 
HETATM 7958 O O     . HOH J 6 .   ? 1.267   25.434  54.804 1.00 37.48  ? 771  HOH A O     1 
HETATM 7959 O O     . HOH J 6 .   ? 6.570   -9.843  16.457 1.00 29.80  ? 772  HOH A O     1 
HETATM 7960 O O     . HOH J 6 .   ? 19.280  39.329  53.360 1.00 41.76  ? 773  HOH A O     1 
HETATM 7961 O O     . HOH J 6 .   ? 22.130  30.646  60.819 1.00 22.02  ? 774  HOH A O     1 
HETATM 7962 O O     . HOH J 6 .   ? 2.588   20.788  20.738 1.00 31.89  ? 775  HOH A O     1 
HETATM 7963 O O     . HOH J 6 .   ? -10.252 23.438  23.855 1.00 34.22  ? 776  HOH A O     1 
HETATM 7964 O O     . HOH J 6 .   ? 17.476  29.494  65.618 1.00 21.72  ? 777  HOH A O     1 
HETATM 7965 O O     . HOH J 6 .   ? 15.538  15.800  50.948 1.00 12.15  ? 778  HOH A O     1 
HETATM 7966 O O     . HOH J 6 .   ? 20.926  31.773  40.807 1.00 30.13  ? 779  HOH A O     1 
HETATM 7967 O O     . HOH J 6 .   ? -15.721 23.648  26.645 1.00 22.56  ? 780  HOH A O     1 
HETATM 7968 O O     . HOH J 6 .   ? -0.194  5.469   54.263 1.00 37.48  ? 781  HOH A O     1 
HETATM 7969 O O     . HOH J 6 .   ? 40.620  10.672  46.765 1.00 28.23  ? 782  HOH A O     1 
HETATM 7970 O O     . HOH J 6 .   ? 3.635   27.451  57.725 1.00 31.31  ? 783  HOH A O     1 
HETATM 7971 O O     . HOH J 6 .   ? 1.185   14.633  54.458 1.00 22.99  ? 784  HOH A O     1 
HETATM 7972 O O     . HOH J 6 .   ? -0.458  12.950  56.118 1.00 33.70  ? 785  HOH A O     1 
HETATM 7973 O O     . HOH J 6 .   ? -7.519  19.372  47.622 1.00 25.71  ? 786  HOH A O     1 
HETATM 7974 O O     . HOH J 6 .   ? 20.278  12.685  60.022 1.00 12.50  ? 787  HOH A O     1 
HETATM 7975 O O     . HOH J 6 .   ? -3.376  9.550   50.392 1.00 27.20  ? 788  HOH A O     1 
HETATM 7976 O O     . HOH J 6 .   ? 13.009  1.290   31.094 1.00 21.96  ? 789  HOH A O     1 
HETATM 7977 O O     . HOH J 6 .   ? 17.651  14.205  29.901 1.00 20.62  ? 790  HOH A O     1 
HETATM 7978 O O     . HOH J 6 .   ? 8.137   -2.615  49.544 1.00 17.79  ? 791  HOH A O     1 
HETATM 7979 O O     . HOH J 6 .   ? 25.472  31.855  54.270 1.00 33.61  ? 792  HOH A O     1 
HETATM 7980 O O     . HOH J 6 .   ? 20.514  36.868  50.598 1.00 33.15  ? 793  HOH A O     1 
HETATM 7981 O O     . HOH J 6 .   ? -6.282  19.121  13.548 1.00 41.23  ? 794  HOH A O     1 
HETATM 7982 O O     . HOH J 6 .   ? -10.953 2.380   46.119 1.00 20.51  ? 795  HOH A O     1 
HETATM 7983 O O     . HOH J 6 .   ? -21.011 18.883  24.855 1.00 33.74  ? 796  HOH A O     1 
HETATM 7984 O O     . HOH J 6 .   ? 6.783   -9.724  23.020 1.00 22.36  ? 797  HOH A O     1 
HETATM 7985 O O     . HOH J 6 .   ? 15.053  5.570   3.792  1.00 29.97  ? 798  HOH A O     1 
HETATM 7986 O O     . HOH J 6 .   ? 35.851  15.577  41.196 1.00 19.67  ? 799  HOH A O     1 
HETATM 7987 O O     . HOH J 6 .   ? 18.495  34.678  61.617 1.00 30.11  ? 800  HOH A O     1 
HETATM 7988 O O     . HOH J 6 .   ? 4.496   -7.762  34.160 1.00 25.56  ? 801  HOH A O     1 
HETATM 7989 O O     . HOH J 6 .   ? 33.901  -0.857  38.183 1.00 12.48  ? 802  HOH A O     1 
HETATM 7990 O O     . HOH J 6 .   ? 1.962   5.184   39.789 1.00 11.61  ? 803  HOH A O     1 
HETATM 7991 O O     . HOH J 6 .   ? -7.408  17.572  34.252 1.00 19.70  ? 804  HOH A O     1 
HETATM 7992 O O     . HOH J 6 .   ? 33.259  22.131  37.426 1.00 34.42  ? 805  HOH A O     1 
HETATM 7993 O O     . HOH J 6 .   ? 4.642   8.156   51.852 1.00 16.32  ? 806  HOH A O     1 
HETATM 7994 O O     . HOH J 6 .   ? 30.178  17.712  20.141 1.00 26.95  ? 807  HOH A O     1 
HETATM 7995 O O     . HOH J 6 .   ? 10.891  36.882  50.251 1.00 27.72  ? 808  HOH A O     1 
HETATM 7996 O O     . HOH J 6 .   ? -16.822 12.483  17.365 1.00 25.71  ? 809  HOH A O     1 
HETATM 7997 O O     . HOH J 6 .   ? 0.574   10.094  40.804 1.00 12.92  ? 810  HOH A O     1 
HETATM 7998 O O     . HOH J 6 .   ? 2.431   23.997  42.356 1.00 22.62  ? 811  HOH A O     1 
HETATM 7999 O O     . HOH J 6 .   ? -16.239 -0.636  34.486 1.00 26.12  ? 812  HOH A O     1 
HETATM 8000 O O     . HOH J 6 .   ? 19.816  5.360   11.104 1.00 31.02  ? 813  HOH A O     1 
HETATM 8001 O O     . HOH J 6 .   ? 21.541  21.482  20.710 1.00 18.76  ? 814  HOH A O     1 
HETATM 8002 O O     . HOH J 6 .   ? 6.604   16.591  45.731 1.00 11.39  ? 815  HOH A O     1 
HETATM 8003 O O     . HOH J 6 .   ? -0.577  9.338   43.105 1.00 16.09  ? 816  HOH A O     1 
HETATM 8004 O O     . HOH J 6 .   ? 18.302  2.595   13.533 1.00 21.52  ? 817  HOH A O     1 
HETATM 8005 O O     . HOH J 6 .   ? 19.983  5.318   63.237 1.00 37.26  ? 818  HOH A O     1 
HETATM 8006 O O     . HOH J 6 .   ? -11.365 11.373  33.068 1.00 15.36  ? 819  HOH A O     1 
HETATM 8007 O O     . HOH J 6 .   ? 12.210  4.695   34.035 1.00 9.88   ? 820  HOH A O     1 
HETATM 8008 O O     . HOH J 6 .   ? 10.124  2.463   28.502 1.00 16.56  ? 821  HOH A O     1 
HETATM 8009 O O     . HOH J 6 .   ? 2.710   17.049  53.280 1.00 23.62  ? 822  HOH A O     1 
HETATM 8010 O O     . HOH J 6 .   ? 28.594  18.561  58.394 1.00 27.35  ? 823  HOH A O     1 
HETATM 8011 O O     . HOH J 6 .   ? 4.982   18.719  54.782 1.00 12.06  ? 824  HOH A O     1 
HETATM 8012 O O     . HOH J 6 .   ? -7.613  -4.525  26.061 1.00 28.26  ? 825  HOH A O     1 
HETATM 8013 O O     . HOH J 6 .   ? -7.552  4.146   21.820 1.00 21.28  ? 826  HOH A O     1 
HETATM 8014 O O     . HOH J 6 .   ? 9.763   1.616   50.621 1.00 21.13  ? 827  HOH A O     1 
HETATM 8015 O O     . HOH J 6 .   ? 31.564  20.981  45.587 1.00 25.82  ? 828  HOH A O     1 
HETATM 8016 O O     . HOH J 6 .   ? 5.730   33.777  48.874 1.00 26.92  ? 829  HOH A O     1 
HETATM 8017 O O     . HOH J 6 .   ? 12.941  13.877  24.153 1.00 12.34  ? 830  HOH A O     1 
HETATM 8018 O O     . HOH J 6 .   ? 7.941   16.296  59.102 1.00 34.59  ? 831  HOH A O     1 
HETATM 8019 O O     . HOH J 6 .   ? 19.281  -3.795  5.584  1.00 33.14  ? 832  HOH A O     1 
HETATM 8020 O O     . HOH J 6 .   ? -16.927 6.438   14.481 1.00 28.74  ? 833  HOH A O     1 
HETATM 8021 O O     . HOH J 6 .   ? -1.996  18.502  47.891 1.00 19.90  ? 834  HOH A O     1 
HETATM 8022 O O     . HOH J 6 .   ? 14.535  13.495  7.537  1.00 40.71  ? 835  HOH A O     1 
HETATM 8023 O O     . HOH J 6 .   ? 27.904  7.287   38.002 1.00 14.32  ? 836  HOH A O     1 
HETATM 8024 O O     . HOH J 6 .   ? 10.371  35.845  52.685 1.00 29.14  ? 837  HOH A O     1 
HETATM 8025 O O     . HOH J 6 .   ? 11.972  -9.433  47.868 1.00 13.41  ? 838  HOH A O     1 
HETATM 8026 O O     . HOH J 6 .   ? -1.664  -11.450 35.997 1.00 32.67  ? 839  HOH A O     1 
HETATM 8027 O O     . HOH J 6 .   ? 11.898  35.308  56.077 1.00 21.10  ? 840  HOH A O     1 
HETATM 8028 O O     . HOH J 6 .   ? 6.557   14.392  43.833 1.00 12.73  ? 841  HOH A O     1 
HETATM 8029 O O     . HOH J 6 .   ? 1.745   -10.476 36.092 1.00 33.51  ? 842  HOH A O     1 
HETATM 8030 O O     . HOH J 6 .   ? 32.284  8.700   37.524 1.00 14.46  ? 843  HOH A O     1 
HETATM 8031 O O     . HOH J 6 .   ? -14.382 14.927  37.374 1.00 16.26  ? 844  HOH A O     1 
HETATM 8032 O O     . HOH J 6 .   ? 1.957   26.272  43.953 1.00 27.55  ? 845  HOH A O     1 
HETATM 8033 O O     . HOH J 6 .   ? 4.683   -4.073  36.846 1.00 24.63  ? 846  HOH A O     1 
HETATM 8034 O O     . HOH J 6 .   ? 8.777   8.004   45.183 1.00 10.33  ? 847  HOH A O     1 
HETATM 8035 O O     . HOH J 6 .   ? 1.584   15.398  26.845 1.00 27.15  ? 848  HOH A O     1 
HETATM 8036 O O     . HOH J 6 .   ? -5.834  22.072  40.532 1.00 27.21  ? 849  HOH A O     1 
HETATM 8037 O O     . HOH J 6 .   ? 11.562  15.519  63.259 1.00 30.41  ? 850  HOH A O     1 
HETATM 8038 O O     . HOH J 6 .   ? 8.069   9.882   42.413 1.00 14.67  ? 851  HOH A O     1 
HETATM 8039 O O     . HOH J 6 .   ? 12.690  3.395   28.088 1.00 20.48  ? 852  HOH A O     1 
HETATM 8040 O O     . HOH J 6 .   ? 31.619  2.639   46.655 1.00 16.83  ? 853  HOH A O     1 
HETATM 8041 O O     . HOH J 6 .   ? 5.056   1.974   4.850  1.00 26.33  ? 854  HOH A O     1 
HETATM 8042 O O     . HOH J 6 .   ? 0.043   -1.649  41.387 1.00 13.00  ? 855  HOH A O     1 
HETATM 8043 O O     . HOH J 6 .   ? 22.588  4.145   35.876 1.00 19.30  ? 856  HOH A O     1 
HETATM 8044 O O     . HOH J 6 .   ? -12.921 5.415   25.905 1.00 21.54  ? 857  HOH A O     1 
HETATM 8045 O O     . HOH J 6 .   ? 31.053  17.015  31.841 1.00 23.20  ? 858  HOH A O     1 
HETATM 8046 O O     . HOH J 6 .   ? -7.095  7.247   32.291 1.00 12.91  ? 859  HOH A O     1 
HETATM 8047 O O     . HOH J 6 .   ? 13.554  11.219  43.144 1.00 17.26  ? 860  HOH A O     1 
HETATM 8048 O O     . HOH J 6 .   ? -4.103  2.089   10.217 1.00 32.68  ? 861  HOH A O     1 
HETATM 8049 O O     . HOH J 6 .   ? 23.349  23.675  64.382 1.00 33.87  ? 862  HOH A O     1 
HETATM 8050 O O     . HOH J 6 .   ? -6.838  -7.629  40.213 1.00 20.80  ? 863  HOH A O     1 
HETATM 8051 O O     . HOH J 6 .   ? -12.747 5.699   28.676 1.00 19.84  ? 864  HOH A O     1 
HETATM 8052 O O     . HOH J 6 .   ? 0.154   2.935   16.565 1.00 15.52  ? 865  HOH A O     1 
HETATM 8053 O O     . HOH J 6 .   ? -7.339  -7.444  32.403 1.00 25.74  ? 866  HOH A O     1 
HETATM 8054 O O     . HOH J 6 .   ? 16.645  19.582  18.496 1.00 25.61  ? 867  HOH A O     1 
HETATM 8055 O O     . HOH J 6 .   ? -0.096  18.171  56.280 1.00 21.55  ? 868  HOH A O     1 
HETATM 8056 O O     . HOH J 6 .   ? -16.612 10.558  38.568 1.00 28.09  ? 869  HOH A O     1 
HETATM 8057 O O     . HOH J 6 .   ? -8.842  10.379  32.395 1.00 13.07  ? 870  HOH A O     1 
HETATM 8058 O O     . HOH J 6 .   ? -2.679  -5.432  45.776 1.00 22.34  ? 871  HOH A O     1 
HETATM 8059 O O     . HOH J 6 .   ? 20.143  4.136   22.806 1.00 29.36  ? 872  HOH A O     1 
HETATM 8060 O O     . HOH J 6 .   ? 41.782  11.741  35.968 1.00 31.32  ? 873  HOH A O     1 
HETATM 8061 O O     . HOH J 6 .   ? 7.232   12.131  58.684 1.00 26.46  ? 874  HOH A O     1 
HETATM 8062 O O     . HOH J 6 .   ? -9.427  4.807   13.242 1.00 27.54  ? 875  HOH A O     1 
HETATM 8063 O O     . HOH J 6 .   ? 21.092  13.725  24.731 1.00 12.15  ? 876  HOH A O     1 
HETATM 8064 O O     . HOH J 6 .   ? 26.615  22.421  43.404 1.00 12.48  ? 877  HOH A O     1 
HETATM 8065 O O     . HOH J 6 .   ? 19.305  11.393  28.761 1.00 14.02  ? 878  HOH A O     1 
HETATM 8066 O O     . HOH J 6 .   ? -12.643 16.171  48.197 1.00 20.96  ? 879  HOH A O     1 
HETATM 8067 O O     . HOH J 6 .   ? 11.317  31.692  62.998 1.00 24.96  ? 880  HOH A O     1 
HETATM 8068 O O     . HOH J 6 .   ? -15.215 19.314  29.364 1.00 12.66  ? 881  HOH A O     1 
HETATM 8069 O O     . HOH J 6 .   ? 21.854  35.251  47.757 1.00 28.17  ? 882  HOH A O     1 
HETATM 8070 O O     . HOH J 6 .   ? 7.939   21.080  61.424 1.00 22.99  ? 883  HOH A O     1 
HETATM 8071 O O     . HOH J 6 .   ? 19.423  20.254  36.065 1.00 11.22  ? 884  HOH A O     1 
HETATM 8072 O O     . HOH J 6 .   ? 20.989  13.175  27.422 1.00 10.94  ? 885  HOH A O     1 
HETATM 8073 O O     . HOH J 6 .   ? -18.015 15.683  28.431 1.00 13.18  ? 886  HOH A O     1 
HETATM 8074 O O     . HOH J 6 .   ? -5.195  -0.760  12.253 1.00 26.38  ? 887  HOH A O     1 
HETATM 8075 O O     . HOH J 6 .   ? 33.638  16.084  51.414 1.00 38.21  ? 888  HOH A O     1 
HETATM 8076 O O     . HOH J 6 .   ? 28.669  25.243  54.808 1.00 21.08  ? 889  HOH A O     1 
HETATM 8077 O O     . HOH J 6 .   ? 32.856  12.579  19.707 1.00 27.60  ? 890  HOH A O     1 
HETATM 8078 O O     . HOH J 6 .   ? 19.237  13.327  22.726 1.00 13.42  ? 891  HOH A O     1 
HETATM 8079 O O     . HOH J 6 .   ? 1.845   -7.708  15.516 1.00 20.34  ? 892  HOH A O     1 
HETATM 8080 O O     . HOH J 6 .   ? 38.794  15.091  23.999 1.00 26.53  ? 893  HOH A O     1 
HETATM 8081 O O     . HOH J 6 .   ? 21.639  0.926   9.059  1.00 35.50  ? 894  HOH A O     1 
HETATM 8082 O O     . HOH J 6 .   ? 18.210  10.743  47.612 1.00 15.78  ? 895  HOH A O     1 
HETATM 8083 O O     . HOH J 6 .   ? 16.206  -0.548  21.626 1.00 21.96  ? 896  HOH A O     1 
HETATM 8084 O O     . HOH J 6 .   ? 2.072   19.870  56.561 1.00 18.60  ? 897  HOH A O     1 
HETATM 8085 O O     . HOH J 6 .   ? 18.342  38.493  56.054 1.00 30.02  ? 898  HOH A O     1 
HETATM 8086 O O     . HOH J 6 .   ? -10.090 23.237  39.070 1.00 32.09  ? 899  HOH A O     1 
HETATM 8087 O O     . HOH J 6 .   ? -10.047 5.739   25.543 1.00 17.61  ? 900  HOH A O     1 
HETATM 8088 O O     . HOH J 6 .   ? 19.847  0.805   60.296 1.00 19.17  ? 901  HOH A O     1 
HETATM 8089 O O     . HOH J 6 .   ? 16.060  5.042   16.476 1.00 16.32  ? 902  HOH A O     1 
HETATM 8090 O O     . HOH J 6 .   ? 29.923  27.386  35.489 1.00 16.77  ? 903  HOH A O     1 
HETATM 8091 O O     . HOH J 6 .   ? 1.998   8.228   50.503 1.00 22.64  ? 904  HOH A O     1 
HETATM 8092 O O     . HOH J 6 .   ? 18.056  34.010  42.676 1.00 35.92  ? 905  HOH A O     1 
HETATM 8093 O O     . HOH J 6 .   ? 25.389  17.209  60.849 1.00 20.14  ? 906  HOH A O     1 
HETATM 8094 O O     . HOH J 6 .   ? 13.879  -2.395  29.198 1.00 15.81  ? 907  HOH A O     1 
HETATM 8095 O O     . HOH J 6 .   ? 26.302  32.241  51.358 1.00 31.51  ? 908  HOH A O     1 
HETATM 8096 O O     . HOH J 6 .   ? 3.110   21.741  45.367 1.00 14.00  ? 909  HOH A O     1 
HETATM 8097 O O     . HOH J 6 .   ? 15.621  -2.824  5.988  1.00 35.42  ? 910  HOH A O     1 
HETATM 8098 O O     . HOH J 6 .   ? 31.761  5.050   29.208 1.00 16.51  ? 911  HOH A O     1 
HETATM 8099 O O     . HOH J 6 .   ? -4.692  19.992  47.032 1.00 20.11  ? 912  HOH A O     1 
HETATM 8100 O O     . HOH J 6 .   ? 15.389  7.032   33.719 1.00 9.51   ? 913  HOH A O     1 
HETATM 8101 O O     . HOH J 6 .   ? -9.160  -7.708  38.688 1.00 34.51  ? 914  HOH A O     1 
HETATM 8102 O O     . HOH J 6 .   ? -10.082 17.583  33.993 1.00 18.41  ? 915  HOH A O     1 
HETATM 8103 O O     . HOH J 6 .   ? -19.896 15.650  41.271 1.00 28.91  ? 916  HOH A O     1 
HETATM 8104 O O     . HOH J 6 .   ? 30.469  24.024  44.091 1.00 31.28  ? 917  HOH A O     1 
HETATM 8105 O O     . HOH J 6 .   ? 32.475  20.347  53.020 1.00 36.28  ? 918  HOH A O     1 
HETATM 8106 O O     . HOH J 6 .   ? 16.304  -4.941  57.002 1.00 26.50  ? 919  HOH A O     1 
HETATM 8107 O O     . HOH J 6 .   ? 43.792  12.907  33.485 1.00 24.22  ? 920  HOH A O     1 
HETATM 8108 O O     . HOH J 6 .   ? 1.808   0.520   41.889 1.00 10.55  ? 921  HOH A O     1 
HETATM 8109 O O     . HOH J 6 .   ? 34.785  19.882  40.452 1.00 45.47  ? 922  HOH A O     1 
HETATM 8110 O O     . HOH J 6 .   ? 8.470   8.631   20.812 1.00 12.02  ? 923  HOH A O     1 
HETATM 8111 O O     . HOH J 6 .   ? 10.385  -3.501  23.356 1.00 23.96  ? 924  HOH A O     1 
HETATM 8112 O O     . HOH J 6 .   ? 13.816  35.040  62.246 1.00 29.34  ? 925  HOH A O     1 
HETATM 8113 O O     . HOH J 6 .   ? 18.135  18.632  21.572 1.00 14.96  ? 926  HOH A O     1 
HETATM 8114 O O     . HOH J 6 .   ? -9.432  7.150   14.058 1.00 23.43  ? 927  HOH A O     1 
HETATM 8115 O O     . HOH J 6 .   ? 21.171  33.119  49.453 1.00 18.70  ? 928  HOH A O     1 
HETATM 8116 O O     . HOH J 6 .   ? 2.119   21.069  18.059 1.00 28.82  ? 929  HOH A O     1 
HETATM 8117 O O     . HOH J 6 .   ? 2.378   1.934   6.002  1.00 29.20  ? 930  HOH A O     1 
HETATM 8118 O O     . HOH J 6 .   ? -14.856 22.007  30.554 1.00 20.67  ? 931  HOH A O     1 
HETATM 8119 O O     . HOH J 6 .   ? 27.861  31.269  45.089 1.00 26.18  ? 932  HOH A O     1 
HETATM 8120 O O     . HOH J 6 .   ? 8.826   13.088  44.850 1.00 11.28  ? 933  HOH A O     1 
HETATM 8121 O O     . HOH J 6 .   ? 6.362   -9.459  50.804 1.00 27.32  ? 934  HOH A O     1 
HETATM 8122 O O     . HOH J 6 .   ? -22.369 18.508  28.279 1.00 28.42  ? 935  HOH A O     1 
HETATM 8123 O O     . HOH J 6 .   ? 30.466  23.794  53.952 1.00 40.04  ? 936  HOH A O     1 
HETATM 8124 O O     . HOH J 6 .   ? 17.449  5.097   26.117 1.00 14.20  ? 937  HOH A O     1 
HETATM 8125 O O     . HOH J 6 .   ? 4.602   17.610  9.083  1.00 41.49  ? 938  HOH A O     1 
HETATM 8126 O O     . HOH J 6 .   ? 13.514  3.350   25.300 1.00 19.97  ? 939  HOH A O     1 
HETATM 8127 O O     . HOH J 6 .   ? 34.095  4.733   43.248 1.00 15.60  ? 940  HOH A O     1 
HETATM 8128 O O     . HOH J 6 .   ? 19.434  15.570  28.107 1.00 12.03  ? 941  HOH A O     1 
HETATM 8129 O O     . HOH J 6 .   ? 33.085  22.921  30.078 1.00 24.51  ? 942  HOH A O     1 
HETATM 8130 O O     . HOH J 6 .   ? -11.564 26.271  35.829 1.00 35.29  ? 943  HOH A O     1 
HETATM 8131 O O     . HOH J 6 .   ? 29.062  24.646  41.917 1.00 27.41  ? 944  HOH A O     1 
HETATM 8132 O O     . HOH J 6 .   ? 32.955  17.614  47.032 1.00 27.72  ? 945  HOH A O     1 
HETATM 8133 O O     . HOH J 6 .   ? -7.073  -12.580 39.843 1.00 43.70  ? 946  HOH A O     1 
HETATM 8134 O O     . HOH J 6 .   ? 29.505  4.290   43.217 1.00 19.05  ? 947  HOH A O     1 
HETATM 8135 O O     . HOH J 6 .   ? 33.684  14.891  30.582 1.00 17.72  ? 948  HOH A O     1 
HETATM 8136 O O     . HOH J 6 .   ? 26.991  25.954  44.456 1.00 18.10  ? 949  HOH A O     1 
HETATM 8137 O O     . HOH J 6 .   ? 34.725  13.148  32.533 1.00 13.23  ? 950  HOH A O     1 
HETATM 8138 O O     . HOH J 6 .   ? 5.452   -4.403  51.421 1.00 27.27  ? 951  HOH A O     1 
HETATM 8139 O O     . HOH J 6 .   ? 28.840  15.844  18.488 1.00 25.19  ? 952  HOH A O     1 
HETATM 8140 O O     . HOH J 6 .   ? 9.041   19.009  26.039 1.00 30.17  ? 953  HOH A O     1 
HETATM 8141 O O     . HOH J 6 .   ? 22.172  28.837  29.254 1.00 23.26  ? 954  HOH A O     1 
HETATM 8142 O O     . HOH J 6 .   ? 17.399  28.531  35.848 1.00 24.64  ? 955  HOH A O     1 
HETATM 8143 O O     . HOH J 6 .   ? 9.584   33.575  56.507 1.00 28.68  ? 956  HOH A O     1 
HETATM 8144 O O     . HOH J 6 .   ? 4.951   23.933  43.277 1.00 20.79  ? 957  HOH A O     1 
HETATM 8145 O O     . HOH J 6 .   ? 7.532   34.089  55.581 1.00 32.63  ? 958  HOH A O     1 
HETATM 8146 O O     . HOH J 6 .   ? 36.015  14.706  35.466 1.00 17.95  ? 959  HOH A O     1 
HETATM 8147 O O     . HOH J 6 .   ? 15.233  -3.739  44.568 1.00 23.40  ? 960  HOH A O     1 
HETATM 8148 O O     . HOH J 6 .   ? 10.757  1.487   53.604 1.00 17.17  ? 961  HOH A O     1 
HETATM 8149 O O     . HOH J 6 .   ? 3.315   18.383  11.471 1.00 34.87  ? 962  HOH A O     1 
HETATM 8150 O O     . HOH J 6 .   ? -17.310 19.737  31.029 1.00 32.62  ? 963  HOH A O     1 
HETATM 8151 O O     . HOH J 6 .   ? 25.185  8.247   59.116 1.00 34.11  ? 964  HOH A O     1 
HETATM 8152 O O     . HOH J 6 .   ? -12.937 1.068   45.140 1.00 36.13  ? 965  HOH A O     1 
HETATM 8153 O O     . HOH J 6 .   ? 34.396  20.956  25.243 1.00 24.94  ? 966  HOH A O     1 
HETATM 8154 O O     . HOH J 6 .   ? 0.502   12.628  14.076 1.00 32.27  ? 967  HOH A O     1 
HETATM 8155 O O     . HOH J 6 .   ? 15.865  10.799  44.765 1.00 15.31  ? 968  HOH A O     1 
HETATM 8156 O O     . HOH J 6 .   ? 17.825  15.685  9.212  1.00 29.70  ? 969  HOH A O     1 
HETATM 8157 O O     . HOH J 6 .   ? -11.224 -7.831  35.452 1.00 36.41  ? 970  HOH A O     1 
HETATM 8158 O O     . HOH J 6 .   ? 16.484  13.447  49.621 1.00 14.01  ? 971  HOH A O     1 
HETATM 8159 O O     . HOH J 6 .   ? -17.395 16.096  32.302 1.00 40.62  ? 972  HOH A O     1 
HETATM 8160 O O     . HOH J 6 .   ? 12.805  36.558  47.166 1.00 32.65  ? 973  HOH A O     1 
HETATM 8161 O O     . HOH J 6 .   ? 13.964  -2.284  58.961 1.00 30.58  ? 974  HOH A O     1 
HETATM 8162 O O     . HOH J 6 .   ? 9.588   2.732   55.802 1.00 19.81  ? 975  HOH A O     1 
HETATM 8163 O O     . HOH J 6 .   ? 1.847   -11.262 23.674 1.00 24.98  ? 976  HOH A O     1 
HETATM 8164 O O     . HOH J 6 .   ? 25.402  28.441  33.755 1.00 16.50  ? 977  HOH A O     1 
HETATM 8165 O O     . HOH J 6 .   ? -8.763  24.135  27.105 1.00 36.90  ? 978  HOH A O     1 
HETATM 8166 O O     . HOH J 6 .   ? 23.137  29.186  31.810 1.00 21.89  ? 979  HOH A O     1 
HETATM 8167 O O     . HOH J 6 .   ? 8.140   26.207  66.337 1.00 32.49  ? 980  HOH A O     1 
HETATM 8168 O O     . HOH J 6 .   ? 32.216  17.754  52.940 1.00 22.66  ? 981  HOH A O     1 
HETATM 8169 O O     . HOH J 6 .   ? 0.300   13.262  21.105 1.00 22.21  ? 982  HOH A O     1 
HETATM 8170 O O     . HOH J 6 .   ? -2.426  -3.527  48.602 1.00 30.21  ? 983  HOH A O     1 
HETATM 8171 O O     . HOH J 6 .   ? 36.183  15.717  38.889 1.00 32.63  ? 984  HOH A O     1 
HETATM 8172 O O     . HOH J 6 .   ? -19.062 3.462   20.415 1.00 32.39  ? 985  HOH A O     1 
HETATM 8173 O O     . HOH J 6 .   ? -8.457  6.311   23.254 1.00 18.27  ? 986  HOH A O     1 
HETATM 8174 O O     . HOH J 6 .   ? 5.237   -2.864  53.110 1.00 23.83  ? 987  HOH A O     1 
HETATM 8175 O O     . HOH J 6 .   ? -19.089 14.018  32.722 1.00 33.47  ? 988  HOH A O     1 
HETATM 8176 O O     . HOH J 6 .   ? -0.261  5.884   49.929 1.00 17.08  ? 989  HOH A O     1 
HETATM 8177 O O     . HOH J 6 .   ? 9.212   -13.270 32.486 1.00 24.21  ? 990  HOH A O     1 
HETATM 8178 O O     . HOH J 6 .   ? -3.772  21.993  45.577 1.00 16.99  ? 991  HOH A O     1 
HETATM 8179 O O     . HOH J 6 .   ? 30.687  3.705   32.017 1.00 25.76  ? 992  HOH A O     1 
HETATM 8180 O O     . HOH J 6 .   ? -3.568  15.383  9.520  1.00 31.65  ? 993  HOH A O     1 
HETATM 8181 O O     . HOH J 6 .   ? 14.340  23.317  20.916 1.00 31.47  ? 994  HOH A O     1 
HETATM 8182 O O     . HOH J 6 .   ? -17.372 2.417   23.369 1.00 33.22  ? 995  HOH A O     1 
HETATM 8183 O O     . HOH J 6 .   ? 10.795  32.405  45.187 1.00 37.67  ? 996  HOH A O     1 
HETATM 8184 O O     . HOH J 6 .   ? -5.754  24.176  38.703 1.00 36.09  ? 997  HOH A O     1 
HETATM 8185 O O     . HOH J 6 .   ? 14.545  1.159   27.618 1.00 19.45  ? 998  HOH A O     1 
HETATM 8186 O O     . HOH J 6 .   ? 38.288  17.244  42.238 1.00 37.12  ? 999  HOH A O     1 
HETATM 8187 O O     . HOH J 6 .   ? -5.368  22.673  43.072 1.00 29.45  ? 1000 HOH A O     1 
HETATM 8188 O O     . HOH J 6 .   ? 11.390  26.328  39.687 1.00 29.52  ? 1001 HOH A O     1 
HETATM 8189 O O     . HOH J 6 .   ? 31.960  25.675  21.792 1.00 35.38  ? 1002 HOH A O     1 
HETATM 8190 O O     . HOH J 6 .   ? 31.528  24.082  26.869 1.00 27.87  ? 1003 HOH A O     1 
HETATM 8191 O O     . HOH J 6 .   ? 9.647   -9.692  50.534 1.00 25.08  ? 1004 HOH A O     1 
HETATM 8192 O O     . HOH J 6 .   ? 18.231  5.235   14.603 1.00 21.52  ? 1005 HOH A O     1 
HETATM 8193 O O     . HOH J 6 .   ? 35.657  18.978  24.366 1.00 34.00  ? 1006 HOH A O     1 
HETATM 8194 O O     . HOH J 6 .   ? 8.209   7.146   42.610 1.00 12.36  ? 1007 HOH A O     1 
HETATM 8195 O O     . HOH J 6 .   ? -20.473 16.084  21.678 1.00 57.12  ? 1008 HOH A O     1 
HETATM 8196 O O     . HOH J 6 .   ? -15.548 6.593   43.204 1.00 30.51  ? 1009 HOH A O     1 
HETATM 8197 O O     . HOH J 6 .   ? 30.765  6.149   44.416 1.00 22.18  ? 1010 HOH A O     1 
HETATM 8198 O O     . HOH J 6 .   ? 0.569   17.197  41.225 1.00 0.50   ? 1011 HOH A O     1 
HETATM 8199 O O     . HOH J 6 .   ? 20.627  14.965  68.638 1.00 29.43  ? 1012 HOH A O     1 
HETATM 8200 O O     . HOH J 6 .   ? 15.514  5.181   24.451 1.00 23.09  ? 1013 HOH A O     1 
HETATM 8201 O O     . HOH J 6 .   ? -6.593  -8.700  34.686 1.00 33.19  ? 1014 HOH A O     1 
HETATM 8202 O O     . HOH J 6 .   ? 9.384   28.073  39.171 1.00 36.46  ? 1015 HOH A O     1 
HETATM 8203 O O     . HOH J 6 .   ? 28.340  31.859  47.894 1.00 38.51  ? 1016 HOH A O     1 
HETATM 8204 O O     . HOH J 6 .   ? 20.890  -6.036  18.731 1.00 37.35  ? 1017 HOH A O     1 
HETATM 8205 O O     . HOH J 6 .   ? -9.449  6.472   48.888 1.00 44.13  ? 1018 HOH A O     1 
HETATM 8206 O O     . HOH J 6 .   ? 25.367  11.024  56.625 1.00 27.68  ? 1019 HOH A O     1 
HETATM 8207 O O     . HOH J 6 .   ? 15.025  7.662   61.965 1.00 32.27  ? 1020 HOH A O     1 
HETATM 8208 O O     . HOH J 6 .   ? -3.758  6.243   47.971 1.00 35.90  ? 1021 HOH A O     1 
HETATM 8209 O O     . HOH J 6 .   ? -0.048  40.687  51.223 1.00 35.72  ? 1022 HOH A O     1 
HETATM 8210 O O     . HOH J 6 .   ? 33.354  17.069  32.552 1.00 33.95  ? 1023 HOH A O     1 
HETATM 8211 O O     . HOH J 6 .   ? 23.157  12.896  60.270 1.00 23.31  ? 1024 HOH A O     1 
HETATM 8212 O O     . HOH J 6 .   ? -6.123  23.693  35.795 1.00 36.83  ? 1025 HOH A O     1 
HETATM 8213 O O     . HOH J 6 .   ? -20.119 9.088   16.918 1.00 36.97  ? 1026 HOH A O     1 
HETATM 8214 O O     . HOH J 6 .   ? 7.136   2.074   56.657 1.00 33.29  ? 1027 HOH A O     1 
HETATM 8215 O O     . HOH J 6 .   ? -8.762  22.667  40.936 1.00 29.22  ? 1028 HOH A O     1 
HETATM 8216 O O     . HOH J 6 .   ? 11.521  2.356   3.148  1.00 37.63  ? 1029 HOH A O     1 
HETATM 8217 O O     . HOH J 6 .   ? 20.407  5.284   16.100 1.00 36.50  ? 1030 HOH A O     1 
HETATM 8218 O O     . HOH J 6 .   ? 28.570  28.465  44.211 1.00 22.48  ? 1031 HOH A O     1 
HETATM 8219 O O     . HOH J 6 .   ? -0.252  -10.534 21.744 1.00 34.89  ? 1032 HOH A O     1 
HETATM 8220 O O     . HOH J 6 .   ? -0.734  -9.776  18.920 1.00 34.62  ? 1033 HOH A O     1 
HETATM 8221 O O     . HOH J 6 .   ? -7.201  -6.462  44.838 1.00 32.36  ? 1034 HOH A O     1 
HETATM 8222 O O     . HOH J 6 .   ? 4.318   -8.581  14.697 1.00 38.40  ? 1035 HOH A O     1 
HETATM 8223 O O     . HOH J 6 .   ? 22.946  8.846   15.284 1.00 32.15  ? 1036 HOH A O     1 
HETATM 8224 O O     . HOH J 6 .   ? -9.548  -3.097  26.520 1.00 29.24  ? 1037 HOH A O     1 
HETATM 8225 O O     . HOH J 6 .   ? -16.481 2.364   16.648 1.00 38.24  ? 1038 HOH A O     1 
HETATM 8226 O O     . HOH J 6 .   ? -8.114  21.997  26.284 1.00 37.15  ? 1039 HOH A O     1 
HETATM 8227 O O     . HOH J 6 .   ? -9.647  -0.161  46.422 1.00 29.89  ? 1040 HOH A O     1 
HETATM 8228 O O     . HOH J 6 .   ? 12.782  39.902  53.549 1.00 39.32  ? 1041 HOH A O     1 
HETATM 8229 O O     . HOH J 6 .   ? -8.437  -8.748  36.378 1.00 35.63  ? 1042 HOH A O     1 
HETATM 8230 O O     . HOH J 6 .   ? 7.434   9.472   58.496 1.00 22.89  ? 1043 HOH A O     1 
HETATM 8231 O O     . HOH J 6 .   ? 21.526  2.163   61.835 1.00 30.46  ? 1044 HOH A O     1 
HETATM 8232 O O     . HOH J 6 .   ? 7.596   11.287  21.228 1.00 15.51  ? 1045 HOH A O     1 
HETATM 8233 O O     . HOH J 6 .   ? -15.335 7.023   12.188 1.00 42.47  ? 1046 HOH A O     1 
HETATM 8234 O O     . HOH J 6 .   ? -6.664  -3.973  23.786 1.00 31.11  ? 1047 HOH A O     1 
HETATM 8235 O O     . HOH J 6 .   ? 0.413   28.210  43.163 1.00 35.78  ? 1048 HOH A O     1 
HETATM 8236 O O     . HOH J 6 .   ? -17.989 21.954  32.197 1.00 26.50  ? 1049 HOH A O     1 
HETATM 8237 O O     . HOH J 6 .   ? 20.348  2.751   12.100 1.00 36.46  ? 1050 HOH A O     1 
HETATM 8238 O O     . HOH J 6 .   ? 15.786  -0.183  29.642 1.00 28.65  ? 1051 HOH A O     1 
HETATM 8239 O O     . HOH J 6 .   ? -8.733  21.259  46.680 1.00 42.54  ? 1052 HOH A O     1 
HETATM 8240 O O     . HOH J 6 .   ? -11.291 25.640  39.114 1.00 34.48  ? 1053 HOH A O     1 
HETATM 8241 O O     . HOH J 6 .   ? 5.365   0.040   3.053  1.00 35.55  ? 1054 HOH A O     1 
HETATM 8242 O O     . HOH J 6 .   ? 15.190  21.755  18.522 1.00 33.00  ? 1055 HOH A O     1 
HETATM 8243 O O     . HOH J 6 .   ? 32.056  18.844  18.700 1.00 30.92  ? 1056 HOH A O     1 
HETATM 8244 O O     . HOH J 6 .   ? 24.060  3.132   61.640 1.00 34.17  ? 1057 HOH A O     1 
HETATM 8245 O O     . HOH J 6 .   ? 22.808  25.561  66.386 1.00 37.53  ? 1058 HOH A O     1 
HETATM 8246 O O     . HOH J 6 .   ? -11.371 3.858   48.620 1.00 34.61  ? 1059 HOH A O     1 
HETATM 8247 O O     . HOH J 6 .   ? 16.747  2.394   25.987 1.00 28.57  ? 1060 HOH A O     1 
HETATM 8248 O O     . HOH J 6 .   ? 17.632  -0.186  61.476 1.00 32.31  ? 1061 HOH A O     1 
HETATM 8249 O O     . HOH J 6 .   ? -22.682 10.789  23.287 1.00 34.60  ? 1062 HOH A O     1 
HETATM 8250 O O     . HOH J 6 .   ? 16.100  30.036  67.744 1.00 39.09  ? 1063 HOH A O     1 
HETATM 8251 O O     . HOH J 6 .   ? 6.177   35.735  50.801 1.00 34.92  ? 1064 HOH A O     1 
HETATM 8252 O O     . HOH J 6 .   ? 22.829  1.299   34.849 1.00 25.04  ? 1065 HOH A O     1 
HETATM 8253 O O     . HOH J 6 .   ? 0.580   1.643   4.396  1.00 38.38  ? 1066 HOH A O     1 
HETATM 8254 O O     . HOH J 6 .   ? 11.761  13.932  7.585  1.00 33.58  ? 1067 HOH A O     1 
HETATM 8255 O O     . HOH J 6 .   ? 8.877   13.763  60.104 1.00 24.93  ? 1068 HOH A O     1 
HETATM 8256 O O     . HOH J 6 .   ? 10.158  0.379   2.101  1.00 30.83  ? 1069 HOH A O     1 
HETATM 8257 O O     . HOH J 6 .   ? -17.209 3.959   14.518 1.00 34.99  ? 1070 HOH A O     1 
HETATM 8258 O O     . HOH J 6 .   ? 5.336   -4.777  3.367  1.00 36.69  ? 1071 HOH A O     1 
HETATM 8259 O O     . HOH J 6 .   ? -11.872 -4.170  27.670 1.00 32.98  ? 1072 HOH A O     1 
HETATM 8260 O O     . HOH J 6 .   ? -16.118 6.741   45.552 1.00 33.38  ? 1073 HOH A O     1 
HETATM 8261 O O     . HOH J 6 .   ? -1.798  17.208  58.252 1.00 34.86  ? 1074 HOH A O     1 
HETATM 8262 O O     . HOH J 6 .   ? 32.731  24.476  24.565 1.00 48.60  ? 1075 HOH A O     1 
HETATM 8263 O O     . HOH J 6 .   ? 0.671   -9.974  17.050 1.00 28.09  ? 1076 HOH A O     1 
HETATM 8264 O O     . HOH J 6 .   ? -7.980  -8.148  42.886 1.00 29.75  ? 1077 HOH A O     1 
HETATM 8265 O O     . HOH J 6 .   ? 34.642  18.157  37.180 1.00 38.97  ? 1078 HOH A O     1 
HETATM 8266 O O     . HOH J 6 .   ? 7.247   33.676  46.754 1.00 40.48  ? 1079 HOH A O     1 
HETATM 8267 O O     . HOH J 6 .   ? 13.435  27.613  37.715 1.00 25.16  ? 1080 HOH A O     1 
HETATM 8268 O O     . HOH J 6 .   ? 12.114  0.000   0.000  0.50 36.76  ? 1081 HOH A O     1 
HETATM 8269 O O     . HOH K 6 .   ? 56.325  -16.958 48.165 1.00 41.27  ? 701  HOH B O     1 
HETATM 8270 O O     . HOH K 6 .   ? 21.070  -3.067  60.914 1.00 33.39  ? 702  HOH B O     1 
HETATM 8271 O O     . HOH K 6 .   ? 13.069  -14.283 33.329 1.00 43.04  ? 703  HOH B O     1 
HETATM 8272 O O     . HOH K 6 .   ? 49.349  -7.309  43.232 1.00 24.45  ? 704  HOH B O     1 
HETATM 8273 O O     . HOH K 6 .   ? 60.642  6.400   38.224 1.00 36.33  ? 705  HOH B O     1 
HETATM 8274 O O     . HOH K 6 .   ? 37.131  -5.397  60.599 1.00 30.90  ? 706  HOH B O     1 
HETATM 8275 O O     . HOH K 6 .   ? 53.635  -16.958 27.469 1.00 25.01  ? 707  HOH B O     1 
HETATM 8276 O O     . HOH K 6 .   ? 39.238  12.376  16.482 1.00 35.32  ? 708  HOH B O     1 
HETATM 8277 O O     . HOH K 6 .   ? 55.083  -1.983  13.342 1.00 29.63  ? 709  HOH B O     1 
HETATM 8278 O O     . HOH K 6 .   ? 65.490  0.346   38.785 1.00 38.39  ? 710  HOH B O     1 
HETATM 8279 O O     . HOH K 6 .   ? 42.509  -33.176 54.869 1.00 41.95  ? 711  HOH B O     1 
HETATM 8280 O O     . HOH K 6 .   ? 68.195  -17.076 32.507 1.00 26.88  ? 712  HOH B O     1 
HETATM 8281 O O     . HOH K 6 .   ? 5.098   -8.204  46.806 1.00 26.08  ? 713  HOH B O     1 
HETATM 8282 O O     . HOH K 6 .   ? 20.103  -3.607  37.081 1.00 16.57  ? 714  HOH B O     1 
HETATM 8283 O O     . HOH K 6 .   ? 57.588  -20.300 32.184 1.00 22.17  ? 715  HOH B O     1 
HETATM 8284 O O     . HOH K 6 .   ? 30.614  -2.923  3.930  1.00 31.81  ? 716  HOH B O     1 
HETATM 8285 O O     . HOH K 6 .   ? 61.128  -4.442  29.586 1.00 23.52  ? 717  HOH B O     1 
HETATM 8286 O O     . HOH K 6 .   ? 62.476  -9.212  36.733 1.00 42.64  ? 718  HOH B O     1 
HETATM 8287 O O     . HOH K 6 .   ? 23.595  -28.096 60.765 1.00 23.98  ? 719  HOH B O     1 
HETATM 8288 O O     . HOH K 6 .   ? 16.172  -2.907  40.778 1.00 15.44  ? 720  HOH B O     1 
HETATM 8289 O O     . HOH K 6 .   ? 53.133  -14.884 34.327 1.00 18.22  ? 721  HOH B O     1 
HETATM 8290 O O     . HOH K 6 .   ? 51.426  -10.628 50.986 1.00 22.33  ? 722  HOH B O     1 
HETATM 8291 O O     . HOH K 6 .   ? 60.102  -9.251  11.301 1.00 26.86  ? 723  HOH B O     1 
HETATM 8292 O O     . HOH K 6 .   ? 14.094  -0.098  43.003 1.00 23.12  ? 724  HOH B O     1 
HETATM 8293 O O     . HOH K 6 .   ? 36.570  4.873   3.425  1.00 27.02  ? 725  HOH B O     1 
HETATM 8294 O O     . HOH K 6 .   ? 38.848  12.311  22.960 1.00 23.26  ? 726  HOH B O     1 
HETATM 8295 O O     . HOH K 6 .   ? 66.779  -6.028  24.460 1.00 20.30  ? 727  HOH B O     1 
HETATM 8296 O O     . HOH K 6 .   ? 11.406  -6.121  43.785 1.00 14.28  ? 728  HOH B O     1 
HETATM 8297 O O     . HOH K 6 .   ? 41.160  14.557  18.269 1.00 33.77  ? 729  HOH B O     1 
HETATM 8298 O O     . HOH K 6 .   ? 40.990  6.758   36.701 1.00 25.63  ? 730  HOH B O     1 
HETATM 8299 O O     . HOH K 6 .   ? 35.995  -9.565  8.373  1.00 24.12  ? 731  HOH B O     1 
HETATM 8300 O O     . HOH K 6 .   ? 59.050  -0.138  25.693 1.00 40.47  ? 732  HOH B O     1 
HETATM 8301 O O     . HOH K 6 .   ? 57.803  -17.408 45.761 1.00 36.28  ? 733  HOH B O     1 
HETATM 8302 O O     . HOH K 6 .   ? 24.678  -29.051 40.661 1.00 32.89  ? 734  HOH B O     1 
HETATM 8303 O O     . HOH K 6 .   ? 38.703  -21.444 41.435 1.00 22.45  ? 735  HOH B O     1 
HETATM 8304 O O     . HOH K 6 .   ? 52.630  8.830   22.077 1.00 30.96  ? 736  HOH B O     1 
HETATM 8305 O O     . HOH K 6 .   ? 59.496  -20.666 45.548 1.00 31.71  ? 737  HOH B O     1 
HETATM 8306 O O     . HOH K 6 .   ? 46.233  -19.230 49.577 1.00 23.65  ? 738  HOH B O     1 
HETATM 8307 O O     . HOH K 6 .   ? 40.353  -4.766  4.498  1.00 27.95  ? 739  HOH B O     1 
HETATM 8308 O O     . HOH K 6 .   ? 41.903  -24.864 57.843 1.00 30.06  ? 740  HOH B O     1 
HETATM 8309 O O     . HOH K 6 .   ? 44.373  -22.787 54.662 1.00 38.32  ? 741  HOH B O     1 
HETATM 8310 O O     . HOH K 6 .   ? 25.464  -1.701  22.793 1.00 31.69  ? 742  HOH B O     1 
HETATM 8311 O O     . HOH K 6 .   ? 29.578  -24.471 37.944 1.00 12.61  ? 743  HOH B O     1 
HETATM 8312 O O     . HOH K 6 .   ? 28.092  -25.736 35.635 1.00 24.36  ? 744  HOH B O     1 
HETATM 8313 O O     . HOH K 6 .   ? 11.856  -14.026 35.412 1.00 28.96  ? 745  HOH B O     1 
HETATM 8314 O O     . HOH K 6 .   ? 34.044  -10.318 60.567 1.00 27.21  ? 746  HOH B O     1 
HETATM 8315 O O     . HOH K 6 .   ? 36.500  -15.128 43.093 1.00 14.08  ? 747  HOH B O     1 
HETATM 8316 O O     . HOH K 6 .   ? 41.169  8.683   5.505  1.00 33.12  ? 748  HOH B O     1 
HETATM 8317 O O     . HOH K 6 .   ? 57.875  5.881   30.217 1.00 27.65  ? 749  HOH B O     1 
HETATM 8318 O O     . HOH K 6 .   ? 30.830  -25.535 31.825 1.00 27.10  ? 750  HOH B O     1 
HETATM 8319 O O     . HOH K 6 .   ? 40.684  -11.648 59.545 1.00 35.43  ? 751  HOH B O     1 
HETATM 8320 O O     . HOH K 6 .   ? 17.025  -15.820 58.290 1.00 24.96  ? 752  HOH B O     1 
HETATM 8321 O O     . HOH K 6 .   ? 53.196  -1.458  21.653 1.00 20.59  ? 753  HOH B O     1 
HETATM 8322 O O     . HOH K 6 .   ? 53.208  -16.726 47.649 1.00 29.16  ? 754  HOH B O     1 
HETATM 8323 O O     . HOH K 6 .   ? 44.484  -12.074 54.456 1.00 24.79  ? 755  HOH B O     1 
HETATM 8324 O O     . HOH K 6 .   ? 50.968  -5.942  45.498 1.00 27.32  ? 756  HOH B O     1 
HETATM 8325 O O     . HOH K 6 .   ? 25.626  8.099   21.215 1.00 23.61  ? 757  HOH B O     1 
HETATM 8326 O O     . HOH K 6 .   ? 32.764  -21.100 30.566 1.00 17.38  ? 758  HOH B O     1 
HETATM 8327 O O     . HOH K 6 .   ? 28.419  -25.211 45.334 1.00 11.27  ? 759  HOH B O     1 
HETATM 8328 O O     . HOH K 6 .   ? 32.847  -12.316 47.923 1.00 16.07  ? 760  HOH B O     1 
HETATM 8329 O O     . HOH K 6 .   ? 40.011  -31.142 48.914 1.00 25.27  ? 761  HOH B O     1 
HETATM 8330 O O     . HOH K 6 .   ? 28.384  -4.655  3.758  1.00 33.77  ? 762  HOH B O     1 
HETATM 8331 O O     . HOH K 6 .   ? 50.808  3.314   12.117 1.00 25.00  ? 763  HOH B O     1 
HETATM 8332 O O     . HOH K 6 .   ? 23.973  -32.581 47.591 1.00 30.32  ? 764  HOH B O     1 
HETATM 8333 O O     . HOH K 6 .   ? 61.862  3.156   34.388 1.00 26.03  ? 765  HOH B O     1 
HETATM 8334 O O     . HOH K 6 .   ? 45.163  -6.516  52.354 1.00 33.75  ? 766  HOH B O     1 
HETATM 8335 O O     . HOH K 6 .   ? 17.984  -27.801 49.797 1.00 22.66  ? 767  HOH B O     1 
HETATM 8336 O O     . HOH K 6 .   ? 42.283  14.918  30.221 1.00 29.13  ? 768  HOH B O     1 
HETATM 8337 O O     . HOH K 6 .   ? 44.346  -22.030 39.791 1.00 27.24  ? 769  HOH B O     1 
HETATM 8338 O O     . HOH K 6 .   ? 15.424  -14.991 20.057 1.00 26.38  ? 770  HOH B O     1 
HETATM 8339 O O     . HOH K 6 .   ? 25.165  -34.248 50.532 1.00 34.09  ? 771  HOH B O     1 
HETATM 8340 O O     . HOH K 6 .   ? 27.369  0.098   13.622 1.00 24.12  ? 772  HOH B O     1 
HETATM 8341 O O     . HOH K 6 .   ? 11.100  -10.799 56.851 1.00 37.23  ? 773  HOH B O     1 
HETATM 8342 O O     . HOH K 6 .   ? 65.266  -16.004 44.677 1.00 35.26  ? 774  HOH B O     1 
HETATM 8343 O O     . HOH K 6 .   ? 43.694  -23.637 43.961 1.00 26.43  ? 775  HOH B O     1 
HETATM 8344 O O     . HOH K 6 .   ? 24.118  -18.825 20.741 1.00 20.26  ? 776  HOH B O     1 
HETATM 8345 O O     . HOH K 6 .   ? 24.498  -24.608 67.097 1.00 28.73  ? 777  HOH B O     1 
HETATM 8346 O O     . HOH K 6 .   ? 29.009  -16.875 18.480 1.00 25.19  ? 778  HOH B O     1 
HETATM 8347 O O     . HOH K 6 .   ? 52.479  10.203  40.308 1.00 19.33  ? 779  HOH B O     1 
HETATM 8348 O O     . HOH K 6 .   ? 27.990  -11.562 29.838 1.00 20.96  ? 780  HOH B O     1 
HETATM 8349 O O     . HOH K 6 .   ? 66.642  -16.421 24.929 1.00 31.95  ? 781  HOH B O     1 
HETATM 8350 O O     . HOH K 6 .   ? 9.814   -12.890 41.094 1.00 20.13  ? 782  HOH B O     1 
HETATM 8351 O O     . HOH K 6 .   ? 43.263  -21.383 42.350 1.00 22.60  ? 783  HOH B O     1 
HETATM 8352 O O     . HOH K 6 .   ? 14.066  -22.952 45.799 1.00 34.20  ? 784  HOH B O     1 
HETATM 8353 O O     . HOH K 6 .   ? 33.483  -2.053  34.002 1.00 10.36  ? 785  HOH B O     1 
HETATM 8354 O O     . HOH K 6 .   ? 62.627  -3.783  14.524 1.00 30.45  ? 786  HOH B O     1 
HETATM 8355 O O     . HOH K 6 .   ? 19.521  -29.543 51.327 1.00 26.62  ? 787  HOH B O     1 
HETATM 8356 O O     . HOH K 6 .   ? 51.301  -19.383 40.499 1.00 25.35  ? 788  HOH B O     1 
HETATM 8357 O O     . HOH K 6 .   ? 13.807  -20.006 50.566 1.00 25.73  ? 789  HOH B O     1 
HETATM 8358 O O     . HOH K 6 .   ? 61.396  -20.978 26.633 1.00 16.35  ? 790  HOH B O     1 
HETATM 8359 O O     . HOH K 6 .   ? 29.651  -2.431  16.301 1.00 17.58  ? 791  HOH B O     1 
HETATM 8360 O O     . HOH K 6 .   ? 37.781  -13.832 59.072 1.00 33.20  ? 792  HOH B O     1 
HETATM 8361 O O     . HOH K 6 .   ? 47.726  -15.887 47.886 1.00 20.61  ? 793  HOH B O     1 
HETATM 8362 O O     . HOH K 6 .   ? 41.073  10.137  12.024 1.00 32.35  ? 794  HOH B O     1 
HETATM 8363 O O     . HOH K 6 .   ? 58.824  -4.211  11.387 1.00 38.17  ? 795  HOH B O     1 
HETATM 8364 O O     . HOH K 6 .   ? 28.082  -27.052 65.427 1.00 21.86  ? 796  HOH B O     1 
HETATM 8365 O O     . HOH K 6 .   ? 38.488  -9.564  58.655 1.00 28.71  ? 797  HOH B O     1 
HETATM 8366 O O     . HOH K 6 .   ? 43.467  -18.335 17.923 1.00 27.76  ? 798  HOH B O     1 
HETATM 8367 O O     . HOH K 6 .   ? 34.020  -12.870 63.240 1.00 25.96  ? 799  HOH B O     1 
HETATM 8368 O O     . HOH K 6 .   ? 25.886  1.711   60.330 1.00 20.38  ? 800  HOH B O     1 
HETATM 8369 O O     . HOH K 6 .   ? 32.652  1.468   31.105 1.00 18.68  ? 801  HOH B O     1 
HETATM 8370 O O     . HOH K 6 .   ? 44.042  -12.752 26.873 1.00 26.94  ? 802  HOH B O     1 
HETATM 8371 O O     . HOH K 6 .   ? 34.098  -22.586 42.118 1.00 27.95  ? 803  HOH B O     1 
HETATM 8372 O O     . HOH K 6 .   ? 7.756   -10.687 47.721 1.00 30.49  ? 804  HOH B O     1 
HETATM 8373 O O     . HOH K 6 .   ? 21.348  -8.121  16.803 1.00 25.90  ? 805  HOH B O     1 
HETATM 8374 O O     . HOH K 6 .   ? 29.059  -9.481  66.115 1.00 37.91  ? 806  HOH B O     1 
HETATM 8375 O O     . HOH K 6 .   ? 66.014  -18.276 29.606 1.00 30.51  ? 807  HOH B O     1 
HETATM 8376 O O     . HOH K 6 .   ? 43.698  -2.562  39.723 1.00 12.05  ? 808  HOH B O     1 
HETATM 8377 O O     . HOH K 6 .   ? 31.640  -13.380 9.954  1.00 36.45  ? 809  HOH B O     1 
HETATM 8378 O O     . HOH K 6 .   ? 66.829  -4.930  19.166 1.00 36.99  ? 810  HOH B O     1 
HETATM 8379 O O     . HOH K 6 .   ? 37.527  5.210   49.485 1.00 19.56  ? 811  HOH B O     1 
HETATM 8380 O O     . HOH K 6 .   ? 25.616  -2.621  10.964 1.00 34.81  ? 812  HOH B O     1 
HETATM 8381 O O     . HOH K 6 .   ? 12.738  -9.958  19.745 1.00 23.58  ? 813  HOH B O     1 
HETATM 8382 O O     . HOH K 6 .   ? 46.219  -6.759  43.087 1.00 15.89  ? 814  HOH B O     1 
HETATM 8383 O O     . HOH K 6 .   ? 3.818   -9.325  36.155 1.00 35.45  ? 815  HOH B O     1 
HETATM 8384 O O     . HOH K 6 .   ? 32.678  -11.230 24.129 1.00 12.18  ? 816  HOH B O     1 
HETATM 8385 O O     . HOH K 6 .   ? 21.918  -17.021 63.497 1.00 31.08  ? 817  HOH B O     1 
HETATM 8386 O O     . HOH K 6 .   ? 13.356  -6.101  37.508 1.00 13.76  ? 818  HOH B O     1 
HETATM 8387 O O     . HOH K 6 .   ? 29.365  -16.747 13.090 1.00 39.94  ? 819  HOH B O     1 
HETATM 8388 O O     . HOH K 6 .   ? 11.791  3.467   38.246 1.00 8.71   ? 820  HOH B O     1 
HETATM 8389 O O     . HOH K 6 .   ? 50.171  -21.378 31.175 1.00 37.18  ? 821  HOH B O     1 
HETATM 8390 O O     . HOH K 6 .   ? 45.463  -0.295  16.512 1.00 16.30  ? 822  HOH B O     1 
HETATM 8391 O O     . HOH K 6 .   ? 57.077  -8.752  33.033 1.00 13.68  ? 823  HOH B O     1 
HETATM 8392 O O     . HOH K 6 .   ? 30.604  -20.782 69.680 1.00 36.33  ? 824  HOH B O     1 
HETATM 8393 O O     . HOH K 6 .   ? 50.602  -8.977  48.233 1.00 22.07  ? 825  HOH B O     1 
HETATM 8394 O O     . HOH K 6 .   ? 33.756  -32.735 56.061 1.00 20.60  ? 826  HOH B O     1 
HETATM 8395 O O     . HOH K 6 .   ? 60.043  -12.273 37.285 1.00 16.15  ? 827  HOH B O     1 
HETATM 8396 O O     . HOH K 6 .   ? 26.486  -10.665 22.746 1.00 13.78  ? 828  HOH B O     1 
HETATM 8397 O O     . HOH K 6 .   ? 65.518  -13.056 41.198 1.00 30.64  ? 829  HOH B O     1 
HETATM 8398 O O     . HOH K 6 .   ? 25.410  -10.109 60.039 1.00 12.08  ? 830  HOH B O     1 
HETATM 8399 O O     . HOH K 6 .   ? 18.781  -23.272 44.354 1.00 18.95  ? 831  HOH B O     1 
HETATM 8400 O O     . HOH K 6 .   ? 56.618  0.268   46.185 1.00 20.59  ? 832  HOH B O     1 
HETATM 8401 O O     . HOH K 6 .   ? 30.678  -10.539 47.360 1.00 10.61  ? 833  HOH B O     1 
HETATM 8402 O O     . HOH K 6 .   ? 3.526   -9.995  45.808 1.00 34.10  ? 834  HOH B O     1 
HETATM 8403 O O     . HOH K 6 .   ? 32.181  -8.577  43.169 1.00 17.53  ? 835  HOH B O     1 
HETATM 8404 O O     . HOH K 6 .   ? 55.841  -20.767 23.772 1.00 36.93  ? 836  HOH B O     1 
HETATM 8405 O O     . HOH K 6 .   ? 37.669  -20.638 66.092 1.00 42.41  ? 837  HOH B O     1 
HETATM 8406 O O     . HOH K 6 .   ? 27.433  -8.115  47.564 1.00 17.08  ? 838  HOH B O     1 
HETATM 8407 O O     . HOH K 6 .   ? 35.550  0.217   28.482 1.00 15.16  ? 839  HOH B O     1 
HETATM 8408 O O     . HOH K 6 .   ? 53.255  7.166   26.012 1.00 29.90  ? 840  HOH B O     1 
HETATM 8409 O O     . HOH K 6 .   ? 20.126  -29.231 54.253 1.00 36.44  ? 841  HOH B O     1 
HETATM 8410 O O     . HOH K 6 .   ? 43.558  -5.594  50.388 1.00 20.86  ? 842  HOH B O     1 
HETATM 8411 O O     . HOH K 6 .   ? 58.335  -13.557 48.148 1.00 21.80  ? 843  HOH B O     1 
HETATM 8412 O O     . HOH K 6 .   ? 63.065  -15.699 37.081 1.00 34.33  ? 844  HOH B O     1 
HETATM 8413 O O     . HOH K 6 .   ? 45.605  4.311   41.413 1.00 12.80  ? 845  HOH B O     1 
HETATM 8414 O O     . HOH K 6 .   ? 43.056  -18.290 20.847 1.00 35.91  ? 846  HOH B O     1 
HETATM 8415 O O     . HOH K 6 .   ? 63.052  0.192   23.082 1.00 33.60  ? 847  HOH B O     1 
HETATM 8416 O O     . HOH K 6 .   ? 54.512  -7.749  32.351 1.00 12.94  ? 848  HOH B O     1 
HETATM 8417 O O     . HOH K 6 .   ? 26.291  -17.595 36.101 1.00 11.51  ? 849  HOH B O     1 
HETATM 8418 O O     . HOH K 6 .   ? 52.776  -4.631  32.309 1.00 12.53  ? 850  HOH B O     1 
HETATM 8419 O O     . HOH K 6 .   ? 33.686  12.020  47.807 1.00 12.20  ? 851  HOH B O     1 
HETATM 8420 O O     . HOH K 6 .   ? 27.592  -15.979 21.528 1.00 15.68  ? 852  HOH B O     1 
HETATM 8421 O O     . HOH K 6 .   ? 48.339  8.032   45.750 1.00 22.35  ? 853  HOH B O     1 
HETATM 8422 O O     . HOH K 6 .   ? 43.835  13.013  36.101 1.00 32.18  ? 854  HOH B O     1 
HETATM 8423 O O     . HOH K 6 .   ? 49.141  -6.903  50.317 1.00 26.45  ? 855  HOH B O     1 
HETATM 8424 O O     . HOH K 6 .   ? 62.523  -9.886  17.419 1.00 21.82  ? 856  HOH B O     1 
HETATM 8425 O O     . HOH K 6 .   ? 12.444  -19.599 37.530 1.00 35.53  ? 857  HOH B O     1 
HETATM 8426 O O     . HOH K 6 .   ? 60.848  -16.741 29.341 1.00 12.67  ? 858  HOH B O     1 
HETATM 8427 O O     . HOH K 6 .   ? 16.422  -24.655 32.017 1.00 21.26  ? 859  HOH B O     1 
HETATM 8428 O O     . HOH K 6 .   ? 34.538  -19.146 29.802 1.00 34.02  ? 860  HOH B O     1 
HETATM 8429 O O     . HOH K 6 .   ? 32.912  -0.778  28.085 1.00 22.13  ? 861  HOH B O     1 
HETATM 8430 O O     . HOH K 6 .   ? 53.038  10.086  32.315 1.00 26.89  ? 862  HOH B O     1 
HETATM 8431 O O     . HOH K 6 .   ? 45.830  -15.591 56.240 1.00 20.03  ? 863  HOH B O     1 
HETATM 8432 O O     . HOH K 6 .   ? 45.086  -7.492  40.743 1.00 12.03  ? 864  HOH B O     1 
HETATM 8433 O O     . HOH K 6 .   ? 22.574  0.396   43.059 1.00 35.03  ? 865  HOH B O     1 
HETATM 8434 O O     . HOH K 6 .   ? 36.904  -5.373  45.212 1.00 13.43  ? 866  HOH B O     1 
HETATM 8435 O O     . HOH K 6 .   ? 34.862  -34.312 50.247 1.00 28.84  ? 867  HOH B O     1 
HETATM 8436 O O     . HOH K 6 .   ? 14.100  -0.011  46.676 1.00 18.56  ? 868  HOH B O     1 
HETATM 8437 O O     . HOH K 6 .   ? 40.984  -5.608  51.888 1.00 17.43  ? 869  HOH B O     1 
HETATM 8438 O O     . HOH K 6 .   ? 35.406  -33.312 52.791 1.00 27.17  ? 870  HOH B O     1 
HETATM 8439 O O     . HOH K 6 .   ? 43.763  10.361  15.564 1.00 20.32  ? 871  HOH B O     1 
HETATM 8440 O O     . HOH K 6 .   ? 24.676  -10.554 27.417 1.00 11.50  ? 872  HOH B O     1 
HETATM 8441 O O     . HOH K 6 .   ? 27.548  5.642   60.619 1.00 36.95  ? 873  HOH B O     1 
HETATM 8442 O O     . HOH K 6 .   ? 20.572  -5.578  59.247 1.00 33.81  ? 874  HOH B O     1 
HETATM 8443 O O     . HOH K 6 .   ? 58.361  -3.052  28.590 1.00 19.08  ? 875  HOH B O     1 
HETATM 8444 O O     . HOH K 6 .   ? 30.051  -5.282  59.596 1.00 20.41  ? 876  HOH B O     1 
HETATM 8445 O O     . HOH K 6 .   ? 19.085  -19.782 43.389 1.00 11.69  ? 877  HOH B O     1 
HETATM 8446 O O     . HOH K 6 .   ? 62.179  -7.874  38.528 1.00 26.63  ? 878  HOH B O     1 
HETATM 8447 O O     . HOH K 6 .   ? 17.732  -4.691  37.965 1.00 13.46  ? 879  HOH B O     1 
HETATM 8448 O O     . HOH K 6 .   ? 49.863  0.460   10.221 1.00 32.75  ? 880  HOH B O     1 
HETATM 8449 O O     . HOH K 6 .   ? 55.124  -4.635  14.202 1.00 23.59  ? 881  HOH B O     1 
HETATM 8450 O O     . HOH K 6 .   ? 51.616  -21.686 38.832 1.00 32.02  ? 882  HOH B O     1 
HETATM 8451 O O     . HOH K 6 .   ? 36.810  -10.503 44.885 1.00 9.26   ? 883  HOH B O     1 
HETATM 8452 O O     . HOH K 6 .   ? 24.540  -11.078 24.703 1.00 12.29  ? 884  HOH B O     1 
HETATM 8453 O O     . HOH K 6 .   ? 39.038  -13.898 45.743 1.00 11.00  ? 885  HOH B O     1 
HETATM 8454 O O     . HOH K 6 .   ? 39.185  12.040  50.794 1.00 27.48  ? 886  HOH B O     1 
HETATM 8455 O O     . HOH K 6 .   ? 39.042  -11.782 43.836 1.00 12.01  ? 887  HOH B O     1 
HETATM 8456 O O     . HOH K 6 .   ? 47.399  14.322  36.289 1.00 34.47  ? 888  HOH B O     1 
HETATM 8457 O O     . HOH K 6 .   ? 27.300  -32.248 61.667 1.00 25.28  ? 889  HOH B O     1 
HETATM 8458 O O     . HOH K 6 .   ? 15.835  -24.846 35.528 1.00 19.35  ? 890  HOH B O     1 
HETATM 8459 O O     . HOH K 6 .   ? 42.603  -19.109 45.314 1.00 16.45  ? 891  HOH B O     1 
HETATM 8460 O O     . HOH K 6 .   ? 51.820  -16.535 13.492 1.00 41.12  ? 892  HOH B O     1 
HETATM 8461 O O     . HOH K 6 .   ? 67.735  -15.836 28.169 1.00 29.29  ? 893  HOH B O     1 
HETATM 8462 O O     . HOH K 6 .   ? 12.010  -12.231 30.604 1.00 17.95  ? 894  HOH B O     1 
HETATM 8463 O O     . HOH K 6 .   ? 50.425  -17.381 46.998 1.00 20.19  ? 895  HOH B O     1 
HETATM 8464 O O     . HOH K 6 .   ? 37.606  -7.223  42.402 1.00 15.01  ? 896  HOH B O     1 
HETATM 8465 O O     . HOH K 6 .   ? 8.316   -13.353 26.128 1.00 24.63  ? 897  HOH B O     1 
HETATM 8466 O O     . HOH K 6 .   ? 30.137  -13.111 50.943 1.00 11.11  ? 898  HOH B O     1 
HETATM 8467 O O     . HOH K 6 .   ? 40.721  -16.203 54.697 1.00 11.93  ? 899  HOH B O     1 
HETATM 8468 O O     . HOH K 6 .   ? 16.843  -13.284 18.467 1.00 26.59  ? 900  HOH B O     1 
HETATM 8469 O O     . HOH K 6 .   ? 35.366  -2.510  2.272  1.00 36.75  ? 901  HOH B O     1 
HETATM 8470 O O     . HOH K 6 .   ? 14.117  -18.387 45.668 1.00 26.38  ? 902  HOH B O     1 
HETATM 8471 O O     . HOH K 6 .   ? 42.951  -14.557 53.271 1.00 18.23  ? 903  HOH B O     1 
HETATM 8472 O O     . HOH K 6 .   ? 30.255  -4.352  33.692 1.00 10.48  ? 904  HOH B O     1 
HETATM 8473 O O     . HOH K 6 .   ? 37.377  15.935  26.138 1.00 22.19  ? 905  HOH B O     1 
HETATM 8474 O O     . HOH K 6 .   ? 43.603  -17.224 56.550 1.00 17.15  ? 906  HOH B O     1 
HETATM 8475 O O     . HOH K 6 .   ? 34.368  -29.103 62.923 1.00 19.90  ? 907  HOH B O     1 
HETATM 8476 O O     . HOH K 6 .   ? 15.185  -21.371 44.083 1.00 33.30  ? 908  HOH B O     1 
HETATM 8477 O O     . HOH K 6 .   ? 26.216  -36.685 53.374 1.00 40.79  ? 909  HOH B O     1 
HETATM 8478 O O     . HOH K 6 .   ? 13.177  -17.740 53.203 1.00 36.83  ? 910  HOH B O     1 
HETATM 8479 O O     . HOH K 6 .   ? 60.620  -19.209 30.538 1.00 22.72  ? 911  HOH B O     1 
HETATM 8480 O O     . HOH K 6 .   ? 26.370  -8.809  28.746 1.00 14.58  ? 912  HOH B O     1 
HETATM 8481 O O     . HOH K 6 .   ? 34.788  1.144   53.642 1.00 18.53  ? 913  HOH B O     1 
HETATM 8482 O O     . HOH K 6 .   ? 57.547  -15.418 15.933 1.00 35.98  ? 914  HOH B O     1 
HETATM 8483 O O     . HOH K 6 .   ? 43.107  0.887   54.149 1.00 36.97  ? 915  HOH B O     1 
HETATM 8484 O O     . HOH K 6 .   ? 40.671  0.713   4.907  1.00 31.54  ? 916  HOH B O     1 
HETATM 8485 O O     . HOH K 6 .   ? 63.667  -13.019 28.435 1.00 14.00  ? 917  HOH B O     1 
HETATM 8486 O O     . HOH K 6 .   ? 36.265  -25.499 39.146 1.00 35.21  ? 918  HOH B O     1 
HETATM 8487 O O     . HOH K 6 .   ? 37.079  -28.524 60.207 1.00 39.25  ? 919  HOH B O     1 
HETATM 8488 O O     . HOH K 6 .   ? 58.489  -2.778  25.908 1.00 21.31  ? 920  HOH B O     1 
HETATM 8489 O O     . HOH K 6 .   ? 43.308  0.665   5.916  1.00 28.42  ? 921  HOH B O     1 
HETATM 8490 O O     . HOH K 6 .   ? 17.829  -28.606 44.989 1.00 26.05  ? 922  HOH B O     1 
HETATM 8491 O O     . HOH K 6 .   ? 40.221  6.989   51.353 1.00 25.93  ? 923  HOH B O     1 
HETATM 8492 O O     . HOH K 6 .   ? 37.780  -18.345 61.382 1.00 26.58  ? 924  HOH B O     1 
HETATM 8493 O O     . HOH K 6 .   ? 55.743  -3.055  25.522 1.00 17.27  ? 925  HOH B O     1 
HETATM 8494 O O     . HOH K 6 .   ? 24.618  -30.477 49.344 1.00 18.68  ? 926  HOH B O     1 
HETATM 8495 O O     . HOH K 6 .   ? 16.592  -22.131 41.902 1.00 23.97  ? 927  HOH B O     1 
HETATM 8496 O O     . HOH K 6 .   ? 26.213  -12.900 28.073 1.00 13.06  ? 928  HOH B O     1 
HETATM 8497 O O     . HOH K 6 .   ? 10.956  -10.478 32.541 1.00 13.23  ? 929  HOH B O     1 
HETATM 8498 O O     . HOH K 6 .   ? 35.297  6.132   23.290 1.00 23.71  ? 930  HOH B O     1 
HETATM 8499 O O     . HOH K 6 .   ? 58.149  -5.964  48.412 1.00 36.17  ? 931  HOH B O     1 
HETATM 8500 O O     . HOH K 6 .   ? 23.058  -1.450  35.985 1.00 21.71  ? 932  HOH B O     1 
HETATM 8501 O O     . HOH K 6 .   ? 10.755  -18.811 28.034 1.00 33.92  ? 933  HOH B O     1 
HETATM 8502 O O     . HOH K 6 .   ? 27.485  -31.370 42.516 1.00 30.77  ? 934  HOH B O     1 
HETATM 8503 O O     . HOH K 6 .   ? 16.921  -22.533 54.739 1.00 30.36  ? 935  HOH B O     1 
HETATM 8504 O O     . HOH K 6 .   ? 57.412  1.526   17.836 1.00 28.74  ? 936  HOH B O     1 
HETATM 8505 O O     . HOH K 6 .   ? 27.338  -35.937 55.991 1.00 30.81  ? 937  HOH B O     1 
HETATM 8506 O O     . HOH K 6 .   ? 64.879  -3.691  39.472 1.00 38.11  ? 938  HOH B O     1 
HETATM 8507 O O     . HOH K 6 .   ? 37.227  -6.019  20.753 1.00 13.11  ? 939  HOH B O     1 
HETATM 8508 O O     . HOH K 6 .   ? 12.538  -20.324 30.074 1.00 26.53  ? 940  HOH B O     1 
HETATM 8509 O O     . HOH K 6 .   ? 16.230  -1.648  43.255 1.00 17.28  ? 941  HOH B O     1 
HETATM 8510 O O     . HOH K 6 .   ? 35.974  -30.972 56.444 1.00 23.72  ? 942  HOH B O     1 
HETATM 8511 O O     . HOH K 6 .   ? 23.532  -26.243 29.110 1.00 23.47  ? 943  HOH B O     1 
HETATM 8512 O O     . HOH K 6 .   ? 29.465  3.062   21.602 1.00 25.39  ? 944  HOH B O     1 
HETATM 8513 O O     . HOH K 6 .   ? 23.521  -11.806 65.763 1.00 33.20  ? 945  HOH B O     1 
HETATM 8514 O O     . HOH K 6 .   ? 6.858   -12.476 24.183 1.00 23.42  ? 946  HOH B O     1 
HETATM 8515 O O     . HOH K 6 .   ? 36.019  -0.117  55.751 1.00 19.71  ? 947  HOH B O     1 
HETATM 8516 O O     . HOH K 6 .   ? 27.892  -12.943 9.142  1.00 31.32  ? 948  HOH B O     1 
HETATM 8517 O O     . HOH K 6 .   ? 43.847  2.226   41.846 1.00 10.55  ? 949  HOH B O     1 
HETATM 8518 O O     . HOH K 6 .   ? 22.246  -20.375 19.141 1.00 35.56  ? 950  HOH B O     1 
HETATM 8519 O O     . HOH K 6 .   ? 20.209  -25.803 33.812 1.00 17.41  ? 951  HOH B O     1 
HETATM 8520 O O     . HOH K 6 .   ? 45.322  -10.024 14.176 1.00 32.51  ? 952  HOH B O     1 
HETATM 8521 O O     . HOH K 6 .   ? 48.285  13.499  22.899 1.00 40.63  ? 953  HOH B O     1 
HETATM 8522 O O     . HOH K 6 .   ? 1.816   -10.201 33.459 1.00 27.08  ? 954  HOH B O     1 
HETATM 8523 O O     . HOH K 6 .   ? 9.451   -13.136 38.704 1.00 36.03  ? 955  HOH B O     1 
HETATM 8524 O O     . HOH K 6 .   ? 29.251  7.595   57.025 1.00 31.10  ? 956  HOH B O     1 
HETATM 8525 O O     . HOH K 6 .   ? 62.795  -16.871 31.092 1.00 34.23  ? 957  HOH B O     1 
HETATM 8526 O O     . HOH K 6 .   ? 43.723  13.877  23.712 1.00 23.81  ? 958  HOH B O     1 
HETATM 8527 O O     . HOH K 6 .   ? 28.241  -2.478  26.145 1.00 12.13  ? 959  HOH B O     1 
HETATM 8528 O O     . HOH K 6 .   ? 54.108  -3.746  23.273 1.00 15.11  ? 960  HOH B O     1 
HETATM 8529 O O     . HOH K 6 .   ? 40.306  5.462   53.095 1.00 28.77  ? 961  HOH B O     1 
HETATM 8530 O O     . HOH K 6 .   ? 11.398  -18.351 25.157 1.00 26.01  ? 962  HOH B O     1 
HETATM 8531 O O     . HOH K 6 .   ? 55.645  -20.709 39.027 1.00 30.77  ? 963  HOH B O     1 
HETATM 8532 O O     . HOH K 6 .   ? 12.721  -14.958 47.031 1.00 28.06  ? 964  HOH B O     1 
HETATM 8533 O O     . HOH K 6 .   ? 29.169  -10.897 49.609 1.00 13.58  ? 965  HOH B O     1 
HETATM 8534 O O     . HOH K 6 .   ? 41.011  -15.162 9.003  1.00 40.39  ? 966  HOH B O     1 
HETATM 8535 O O     . HOH K 6 .   ? 32.050  -0.737  25.333 1.00 17.76  ? 967  HOH B O     1 
HETATM 8536 O O     . HOH K 6 .   ? 41.139  10.321  34.315 1.00 24.27  ? 968  HOH B O     1 
HETATM 8537 O O     . HOH K 6 .   ? 36.667  -16.423 26.010 1.00 31.75  ? 969  HOH B O     1 
HETATM 8538 O O     . HOH K 6 .   ? 40.688  -21.306 43.183 1.00 21.29  ? 970  HOH B O     1 
HETATM 8539 O O     . HOH K 6 .   ? 32.358  5.245   46.417 1.00 16.52  ? 971  HOH B O     1 
HETATM 8540 O O     . HOH K 6 .   ? 64.849  -11.333 32.802 1.00 34.75  ? 972  HOH B O     1 
HETATM 8541 O O     . HOH K 6 .   ? 34.688  -29.504 45.164 1.00 36.73  ? 973  HOH B O     1 
HETATM 8542 O O     . HOH K 6 .   ? 45.857  -3.286  49.887 1.00 17.79  ? 974  HOH B O     1 
HETATM 8543 O O     . HOH K 6 .   ? 22.465  -26.475 31.851 1.00 20.01  ? 975  HOH B O     1 
HETATM 8544 O O     . HOH K 6 .   ? 38.079  -31.546 55.553 1.00 35.25  ? 976  HOH B O     1 
HETATM 8545 O O     . HOH K 6 .   ? 55.672  -14.944 33.993 1.00 19.86  ? 977  HOH B O     1 
HETATM 8546 O O     . HOH K 6 .   ? 57.257  -23.703 35.628 1.00 28.99  ? 978  HOH B O     1 
HETATM 8547 O O     . HOH K 6 .   ? 31.823  4.862   59.006 1.00 31.37  ? 979  HOH B O     1 
HETATM 8548 O O     . HOH K 6 .   ? 49.437  -19.421 45.523 1.00 17.37  ? 980  HOH B O     1 
HETATM 8549 O O     . HOH K 6 .   ? 48.072  6.039   48.718 1.00 27.97  ? 981  HOH B O     1 
HETATM 8550 O O     . HOH K 6 .   ? 24.163  -14.944 67.780 1.00 21.16  ? 982  HOH B O     1 
HETATM 8551 O O     . HOH K 6 .   ? 70.985  -10.052 29.065 1.00 40.12  ? 983  HOH B O     1 
HETATM 8552 O O     . HOH K 6 .   ? 27.801  -24.419 21.798 1.00 39.12  ? 984  HOH B O     1 
HETATM 8553 O O     . HOH K 6 .   ? 54.840  10.518  38.681 1.00 34.01  ? 985  HOH B O     1 
HETATM 8554 O O     . HOH K 6 .   ? 32.851  -33.927 47.061 1.00 35.79  ? 986  HOH B O     1 
HETATM 8555 O O     . HOH K 6 .   ? 31.680  -32.611 62.158 1.00 24.80  ? 987  HOH B O     1 
HETATM 8556 O O     . HOH K 6 .   ? 26.360  -35.171 46.758 1.00 37.36  ? 988  HOH B O     1 
HETATM 8557 O O     . HOH K 6 .   ? 36.482  15.920  32.461 1.00 23.97  ? 989  HOH B O     1 
HETATM 8558 O O     . HOH K 6 .   ? 37.389  -23.453 66.379 1.00 32.75  ? 990  HOH B O     1 
HETATM 8559 O O     . HOH K 6 .   ? 42.307  -15.769 11.460 1.00 33.55  ? 991  HOH B O     1 
HETATM 8560 O O     . HOH K 6 .   ? 28.777  1.080   23.360 1.00 30.11  ? 992  HOH B O     1 
HETATM 8561 O O     . HOH K 6 .   ? 14.865  -1.007  32.050 1.00 22.06  ? 993  HOH B O     1 
HETATM 8562 O O     . HOH K 6 .   ? 49.235  -12.651 9.536  1.00 27.07  ? 994  HOH B O     1 
HETATM 8563 O O     . HOH K 6 .   ? 35.874  12.229  50.514 1.00 24.24  ? 995  HOH B O     1 
HETATM 8564 O O     . HOH K 6 .   ? 37.467  -4.524  42.628 1.00 12.95  ? 996  HOH B O     1 
HETATM 8565 O O     . HOH K 6 .   ? 27.427  -2.589  14.510 1.00 20.93  ? 997  HOH B O     1 
HETATM 8566 O O     . HOH K 6 .   ? 14.076  -21.466 26.927 1.00 28.40  ? 998  HOH B O     1 
HETATM 8567 O O     . HOH K 6 .   ? 36.020  1.057   50.847 1.00 25.42  ? 999  HOH B O     1 
HETATM 8568 O O     . HOH K 6 .   ? 13.386  -15.180 52.889 1.00 24.66  ? 1000 HOH B O     1 
HETATM 8569 O O     . HOH K 6 .   ? 9.909   -16.253 24.348 1.00 32.45  ? 1001 HOH B O     1 
HETATM 8570 O O     . HOH K 6 .   ? 31.114  1.481   27.625 1.00 20.50  ? 1002 HOH B O     1 
HETATM 8571 O O     . HOH K 6 .   ? 54.265  -21.767 27.338 1.00 37.10  ? 1003 HOH B O     1 
HETATM 8572 O O     . HOH K 6 .   ? 9.752   -12.177 35.358 1.00 19.57  ? 1004 HOH B O     1 
HETATM 8573 O O     . HOH K 6 .   ? 29.827  -8.336  44.746 1.00 14.73  ? 1005 HOH B O     1 
HETATM 8574 O O     . HOH K 6 .   ? 64.735  -0.600  20.465 1.00 32.71  ? 1006 HOH B O     1 
HETATM 8575 O O     . HOH K 6 .   ? 51.047  -20.076 43.031 1.00 29.74  ? 1007 HOH B O     1 
HETATM 8576 O O     . HOH K 6 .   ? 51.466  -21.319 22.506 1.00 44.88  ? 1008 HOH B O     1 
HETATM 8577 O O     . HOH K 6 .   ? 61.269  -3.958  43.133 1.00 27.59  ? 1009 HOH B O     1 
HETATM 8578 O O     . HOH K 6 .   ? 45.371  -10.604 21.150 1.00 23.69  ? 1010 HOH B O     1 
HETATM 8579 O O     . HOH K 6 .   ? 31.396  -20.723 20.941 1.00 30.35  ? 1011 HOH B O     1 
HETATM 8580 O O     . HOH K 6 .   ? 34.300  -23.754 39.734 1.00 32.04  ? 1012 HOH B O     1 
HETATM 8581 O O     . HOH K 6 .   ? 45.114  -14.559 41.196 1.00 0.50   ? 1013 HOH B O     1 
HETATM 8582 O O     . HOH K 6 .   ? 56.149  10.178  42.088 1.00 34.93  ? 1014 HOH B O     1 
HETATM 8583 O O     . HOH K 6 .   ? 30.208  -2.420  24.361 1.00 22.58  ? 1015 HOH B O     1 
HETATM 8584 O O     . HOH K 6 .   ? 20.420  -8.287  56.716 1.00 31.07  ? 1016 HOH B O     1 
HETATM 8585 O O     . HOH K 6 .   ? 24.355  -34.247 56.545 1.00 38.40  ? 1017 HOH B O     1 
HETATM 8586 O O     . HOH K 6 .   ? 46.903  -16.064 27.510 1.00 40.51  ? 1018 HOH B O     1 
HETATM 8587 O O     . HOH K 6 .   ? 26.015  -14.041 11.758 1.00 41.00  ? 1019 HOH B O     1 
HETATM 8588 O O     . HOH K 6 .   ? 52.193  11.174  34.770 1.00 32.75  ? 1020 HOH B O     1 
HETATM 8589 O O     . HOH K 6 .   ? 45.908  -38.104 51.379 1.00 37.29  ? 1021 HOH B O     1 
HETATM 8590 O O     . HOH K 6 .   ? 26.906  -9.786  31.114 1.00 28.81  ? 1022 HOH B O     1 
HETATM 8591 O O     . HOH K 6 .   ? 37.618  -15.536 61.480 1.00 40.25  ? 1023 HOH B O     1 
HETATM 8592 O O     . HOH K 6 .   ? 25.151  -30.303 37.996 1.00 37.12  ? 1024 HOH B O     1 
HETATM 8593 O O     . HOH K 6 .   ? 39.207  4.964   3.808  1.00 38.05  ? 1025 HOH B O     1 
HETATM 8594 O O     . HOH K 6 .   ? 17.237  -29.223 47.898 1.00 38.03  ? 1026 HOH B O     1 
HETATM 8595 O O     . HOH K 6 .   ? 36.248  -0.426  60.069 1.00 44.50  ? 1027 HOH B O     1 
HETATM 8596 O O     . HOH K 6 .   ? 61.949  -12.574 35.443 1.00 34.56  ? 1028 HOH B O     1 
HETATM 8597 O O     . HOH K 6 .   ? 41.394  -17.434 25.865 1.00 37.91  ? 1029 HOH B O     1 
HETATM 8598 O O     . HOH K 6 .   ? 29.868  -18.360 68.969 1.00 38.46  ? 1030 HOH B O     1 
HETATM 8599 O O     . HOH K 6 .   ? 55.648  9.271   32.857 1.00 41.29  ? 1031 HOH B O     1 
HETATM 8600 O O     . HOH K 6 .   ? 45.234  -25.436 43.551 1.00 35.56  ? 1032 HOH B O     1 
HETATM 8601 O O     . HOH K 6 .   ? 38.332  0.911   56.695 1.00 38.31  ? 1033 HOH B O     1 
HETATM 8602 O O     . HOH K 6 .   ? 21.641  -12.429 61.695 1.00 25.26  ? 1034 HOH B O     1 
HETATM 8603 O O     . HOH K 6 .   ? 63.920  1.502   34.013 1.00 36.00  ? 1035 HOH B O     1 
HETATM 8604 O O     . HOH K 6 .   ? 22.567  -10.253 60.312 1.00 23.93  ? 1036 HOH B O     1 
HETATM 8605 O O     . HOH K 6 .   ? 26.105  -27.778 29.004 1.00 38.52  ? 1037 HOH B O     1 
HETATM 8606 O O     . HOH K 6 .   ? 45.943  13.050  21.764 1.00 37.99  ? 1038 HOH B O     1 
HETATM 8607 O O     . HOH K 6 .   ? 17.242  -25.822 44.109 1.00 27.35  ? 1039 HOH B O     1 
HETATM 8608 O O     . HOH K 6 .   ? 54.483  -20.023 40.872 1.00 32.87  ? 1040 HOH B O     1 
HETATM 8609 O O     . HOH K 6 .   ? 46.389  12.300  18.934 1.00 32.76  ? 1041 HOH B O     1 
HETATM 8610 O O     . HOH K 6 .   ? 51.862  -21.000 35.935 1.00 36.51  ? 1042 HOH B O     1 
HETATM 8611 O O     . HOH K 6 .   ? 52.927  8.913   44.738 1.00 35.03  ? 1043 HOH B O     1 
HETATM 8612 O O     . HOH K 6 .   ? 32.487  -28.059 67.515 1.00 36.78  ? 1044 HOH B O     1 
HETATM 8613 O O     . HOH K 6 .   ? 65.834  -6.362  16.909 1.00 36.12  ? 1045 HOH B O     1 
HETATM 8614 O O     . HOH K 6 .   ? 55.358  2.719   46.338 1.00 29.56  ? 1046 HOH B O     1 
HETATM 8615 O O     . HOH K 6 .   ? 25.302  -2.769  16.131 1.00 37.42  ? 1047 HOH B O     1 
HETATM 8616 O O     . HOH K 6 .   ? 41.306  11.206  14.613 1.00 36.06  ? 1048 HOH B O     1 
HETATM 8617 O O     . HOH K 6 .   ? 55.250  5.700   26.469 1.00 27.19  ? 1049 HOH B O     1 
HETATM 8618 O O     . HOH K 6 .   ? 32.710  -37.444 53.451 1.00 38.33  ? 1050 HOH B O     1 
HETATM 8619 O O     . HOH K 6 .   ? 26.078  -28.741 64.705 1.00 34.49  ? 1051 HOH B O     1 
HETATM 8620 O O     . HOH K 6 .   ? 38.042  -8.594  21.225 1.00 14.78  ? 1052 HOH B O     1 
HETATM 8621 O O     . HOH K 6 .   ? 63.677  -19.207 32.129 1.00 22.28  ? 1053 HOH B O     1 
HETATM 8622 O O     . HOH K 6 .   ? 38.215  -6.872  58.444 1.00 24.33  ? 1054 HOH B O     1 
HETATM 8623 O O     . HOH K 6 .   ? 20.880  -8.192  59.699 1.00 36.31  ? 1055 HOH B O     1 
HETATM 8624 O O     . HOH K 6 .   ? 52.199  6.484   23.732 1.00 31.46  ? 1056 HOH B O     1 
HETATM 8625 O O     . HOH K 6 .   ? 19.366  -28.617 28.286 1.00 35.68  ? 1057 HOH B O     1 
HETATM 8626 O O     . HOH K 6 .   ? 54.207  11.325  36.404 1.00 32.17  ? 1058 HOH B O     1 
HETATM 8627 O O     . HOH K 6 .   ? 13.581  -16.183 18.830 1.00 32.35  ? 1059 HOH B O     1 
HETATM 8628 O O     . HOH K 6 .   ? 29.189  0.300   25.995 1.00 39.72  ? 1060 HOH B O     1 
HETATM 8629 O O     . HOH K 6 .   ? 40.284  2.534   3.150  1.00 31.01  ? 1061 HOH B O     1 
HETATM 8630 O O     . HOH K 6 .   ? 30.586  -18.894 18.387 1.00 37.57  ? 1062 HOH B O     1 
HETATM 8631 O O     . HOH K 6 .   ? 54.578  -18.678 46.624 1.00 38.37  ? 1063 HOH B O     1 
HETATM 8632 O O     . HOH K 6 .   ? 29.817  2.758   29.705 1.00 33.80  ? 1064 HOH B O     1 
HETATM 8633 O O     . HOH K 6 .   ? 28.167  2.739   61.521 1.00 30.56  ? 1065 HOH B O     1 
HETATM 8634 O O     . HOH K 6 .   ? 68.490  -4.016  24.604 1.00 38.09  ? 1066 HOH B O     1 
HETATM 8635 O O     . HOH K 6 .   ? 44.992  1.048   4.234  1.00 39.57  ? 1067 HOH B O     1 
HETATM 8636 O O     . HOH K 6 .   ? 42.682  -32.117 47.458 1.00 45.50  ? 1068 HOH B O     1 
HETATM 8637 O O     . HOH K 6 .   ? 68.308  -8.114  23.323 1.00 35.23  ? 1069 HOH B O     1 
HETATM 8638 O O     . HOH K 6 .   ? 57.063  -22.315 43.718 1.00 33.16  ? 1070 HOH B O     1 
HETATM 8639 O O     . HOH K 6 .   ? 36.965  -28.057 62.702 1.00 42.55  ? 1071 HOH B O     1 
HETATM 8640 O O     . HOH K 6 .   ? 57.031  -1.030  48.511 1.00 34.84  ? 1072 HOH B O     1 
HETATM 8641 O O     . HOH K 6 .   ? 44.560  -22.859 35.056 1.00 38.69  ? 1073 HOH B O     1 
HETATM 8642 O O     . HOH K 6 .   ? 23.122  6.323   20.301 1.00 40.27  ? 1074 HOH B O     1 
HETATM 8643 O O     . HOH K 6 .   ? 33.855  -11.317 7.467  1.00 34.42  ? 1075 HOH B O     1 
HETATM 8644 O O     . HOH K 6 .   ? 29.704  -33.736 62.066 1.00 40.09  ? 1076 HOH B O     1 
HETATM 8645 O O     . HOH K 6 .   ? 12.997  -21.843 24.630 1.00 35.23  ? 1077 HOH B O     1 
HETATM 8646 O O     . HOH K 6 .   ? 61.828  -4.132  45.462 1.00 31.51  ? 1078 HOH B O     1 
HETATM 8647 O O     . HOH K 6 .   ? 35.651  2.162   2.139  1.00 37.59  ? 1079 HOH B O     1 
HETATM 8648 O O     . HOH K 6 .   ? 47.491  -14.608 58.188 1.00 33.19  ? 1080 HOH B O     1 
HETATM 8649 O O     . HOH K 6 .   ? 62.938  -1.261  14.479 1.00 32.69  ? 1081 HOH B O     1 
HETATM 8650 O O     . HOH K 6 .   ? 45.070  12.536  17.072 1.00 27.54  ? 1082 HOH B O     1 
HETATM 8651 O O     . HOH K 6 .   ? 11.189  -15.557 37.118 1.00 32.14  ? 1083 HOH B O     1 
HETATM 8652 O O     . HOH K 6 .   ? 36.775  -11.120 60.241 1.00 23.96  ? 1084 HOH B O     1 
HETATM 8653 O O     . HOH K 6 .   ? 57.457  6.648   27.551 1.00 36.81  ? 1085 HOH B O     1 
HETATM 8654 O O     . HOH K 6 .   ? 53.649  10.783  42.800 1.00 28.59  ? 1086 HOH B O     1 
HETATM 8655 O O     . HOH K 6 .   ? 29.936  -23.032 20.920 1.00 39.96  ? 1087 HOH B O     1 
HETATM 8656 O O     . HOH K 6 .   ? 38.280  -31.009 46.575 1.00 42.94  ? 1088 HOH B O     1 
HETATM 8657 O O     . HOH K 6 .   ? 32.284  -24.947 37.712 1.00 21.28  ? 1089 HOH B O     1 
HETATM 8658 O O     . HOH K 6 .   ? 32.045  10.325  12.530 1.00 49.32  ? 1090 HOH B O     1 
HETATM 8659 O O     . HOH K 6 .   ? 27.183  -0.000  64.803 0.50 37.95  ? 1091 HOH B O     1 
# 
