data_9U5L
# 
_entry.id   9U5L 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9U5L         pdb_00009u5l 10.2210/pdb9u5l/pdb 
WWPDB D_1300057740 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9U5L 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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              zfli@jiangnan.edu.cn 
_pdbx_contact_author.name_first         Zhaofeng 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7571-1083 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, Z.F.'   1 0000-0001-7571-1083 
'Tian, Y.X.' 2 0009-0000-0009-405X 
'Xiao, Y.'   3 0000-0002-2484-1424 
'Ban, X.F.'  4 0000-0001-9037-7335 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'The X-ray Crystallographic Structure of 4-alpha-glycosyltransferase from Thermus thermophilus STB20' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, Z.F.'   1 0000-0001-7571-1083 
primary 'Tian, Y.X.' 2 0009-0000-0009-405X 
primary 'Xiao, Y.'   3 0000-0002-2484-1424 
primary 'Ban, X.F.'  4 0000-0001-9037-7335 
# 
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 4-alpha-glucanotransferase 57399.047 1   2.4.1.25 ? ? ? 
2 water   nat water                      18.015    147 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Amylomaltase,Disproportionating enzyme,D-enzyme' 
# 
_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       
;MELPRAFGLLLHPTSLPGPYGVGVLGQEARDFLRFLKEAGGQYWQVLPLGPTGYGDSPYQSFSAFAGNPYLVDLRPLAKR
GYVRLEDPGFPQGRVDYGLLYAWKWPALKEAFRGFQEKAPPEEREDFAAFREKEAWWLEDYALFMALKGAHGGLPWNRWP
LPLRKREEQALREAKSALAEEVAFHAFTQWLFFRQWGALKAEAEALGIRILGDMPIFVAEDSAEVWAHPEWFHLDEEGRP
TVVAGVPPDYFSETGQRWGNPLYRWDVLEREGFSFWIRRLEKALELFHLVRIDHFRGFEAYWEIPASCPTAVEGRWVKAP
GEKLFQKIQETFGQVPILAEDLGVITPEVEALRDRFGLPGMKVLQFAFDDGMENPFLPHNYPSHGRVVVYTGTHDNDTTL
GWYRTATPHEKAFMARYLADWGIFFREEEEVPWALMRLGMKSVARLAVYPVQDVLALGSEARMNYPGRPSGNWAWRLLPG
ELSPEHGERLRAMAEATERL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MELPRAFGLLLHPTSLPGPYGVGVLGQEARDFLRFLKEAGGQYWQVLPLGPTGYGDSPYQSFSAFAGNPYLVDLRPLAKR
GYVRLEDPGFPQGRVDYGLLYAWKWPALKEAFRGFQEKAPPEEREDFAAFREKEAWWLEDYALFMALKGAHGGLPWNRWP
LPLRKREEQALREAKSALAEEVAFHAFTQWLFFRQWGALKAEAEALGIRILGDMPIFVAEDSAEVWAHPEWFHLDEEGRP
TVVAGVPPDYFSETGQRWGNPLYRWDVLEREGFSFWIRRLEKALELFHLVRIDHFRGFEAYWEIPASCPTAVEGRWVKAP
GEKLFQKIQETFGQVPILAEDLGVITPEVEALRDRFGLPGMKVLQFAFDDGMENPFLPHNYPSHGRVVVYTGTHDNDTTL
GWYRTATPHEKAFMARYLADWGIFFREEEEVPWALMRLGMKSVARLAVYPVQDVLALGSEARMNYPGRPSGNWAWRLLPG
ELSPEHGERLRAMAEATERL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   LEU n 
1 4   PRO n 
1 5   ARG n 
1 6   ALA n 
1 7   PHE n 
1 8   GLY n 
1 9   LEU n 
1 10  LEU n 
1 11  LEU n 
1 12  HIS n 
1 13  PRO n 
1 14  THR n 
1 15  SER n 
1 16  LEU n 
1 17  PRO n 
1 18  GLY n 
1 19  PRO n 
1 20  TYR n 
1 21  GLY n 
1 22  VAL n 
1 23  GLY n 
1 24  VAL n 
1 25  LEU n 
1 26  GLY n 
1 27  GLN n 
1 28  GLU n 
1 29  ALA n 
1 30  ARG n 
1 31  ASP n 
1 32  PHE n 
1 33  LEU n 
1 34  ARG n 
1 35  PHE n 
1 36  LEU n 
1 37  LYS n 
1 38  GLU n 
1 39  ALA n 
1 40  GLY n 
1 41  GLY n 
1 42  GLN n 
1 43  TYR n 
1 44  TRP n 
1 45  GLN n 
1 46  VAL n 
1 47  LEU n 
1 48  PRO n 
1 49  LEU n 
1 50  GLY n 
1 51  PRO n 
1 52  THR n 
1 53  GLY n 
1 54  TYR n 
1 55  GLY n 
1 56  ASP n 
1 57  SER n 
1 58  PRO n 
1 59  TYR n 
1 60  GLN n 
1 61  SER n 
1 62  PHE n 
1 63  SER n 
1 64  ALA n 
1 65  PHE n 
1 66  ALA n 
1 67  GLY n 
1 68  ASN n 
1 69  PRO n 
1 70  TYR n 
1 71  LEU n 
1 72  VAL n 
1 73  ASP n 
1 74  LEU n 
1 75  ARG n 
1 76  PRO n 
1 77  LEU n 
1 78  ALA n 
1 79  LYS n 
1 80  ARG n 
1 81  GLY n 
1 82  TYR n 
1 83  VAL n 
1 84  ARG n 
1 85  LEU n 
1 86  GLU n 
1 87  ASP n 
1 88  PRO n 
1 89  GLY n 
1 90  PHE n 
1 91  PRO n 
1 92  GLN n 
1 93  GLY n 
1 94  ARG n 
1 95  VAL n 
1 96  ASP n 
1 97  TYR n 
1 98  GLY n 
1 99  LEU n 
1 100 LEU n 
1 101 TYR n 
1 102 ALA n 
1 103 TRP n 
1 104 LYS n 
1 105 TRP n 
1 106 PRO n 
1 107 ALA n 
1 108 LEU n 
1 109 LYS n 
1 110 GLU n 
1 111 ALA n 
1 112 PHE n 
1 113 ARG n 
1 114 GLY n 
1 115 PHE n 
1 116 GLN n 
1 117 GLU n 
1 118 LYS n 
1 119 ALA n 
1 120 PRO n 
1 121 PRO n 
1 122 GLU n 
1 123 GLU n 
1 124 ARG n 
1 125 GLU n 
1 126 ASP n 
1 127 PHE n 
1 128 ALA n 
1 129 ALA n 
1 130 PHE n 
1 131 ARG n 
1 132 GLU n 
1 133 LYS n 
1 134 GLU n 
1 135 ALA n 
1 136 TRP n 
1 137 TRP n 
1 138 LEU n 
1 139 GLU n 
1 140 ASP n 
1 141 TYR n 
1 142 ALA n 
1 143 LEU n 
1 144 PHE n 
1 145 MET n 
1 146 ALA n 
1 147 LEU n 
1 148 LYS n 
1 149 GLY n 
1 150 ALA n 
1 151 HIS n 
1 152 GLY n 
1 153 GLY n 
1 154 LEU n 
1 155 PRO n 
1 156 TRP n 
1 157 ASN n 
1 158 ARG n 
1 159 TRP n 
1 160 PRO n 
1 161 LEU n 
1 162 PRO n 
1 163 LEU n 
1 164 ARG n 
1 165 LYS n 
1 166 ARG n 
1 167 GLU n 
1 168 GLU n 
1 169 GLN n 
1 170 ALA n 
1 171 LEU n 
1 172 ARG n 
1 173 GLU n 
1 174 ALA n 
1 175 LYS n 
1 176 SER n 
1 177 ALA n 
1 178 LEU n 
1 179 ALA n 
1 180 GLU n 
1 181 GLU n 
1 182 VAL n 
1 183 ALA n 
1 184 PHE n 
1 185 HIS n 
1 186 ALA n 
1 187 PHE n 
1 188 THR n 
1 189 GLN n 
1 190 TRP n 
1 191 LEU n 
1 192 PHE n 
1 193 PHE n 
1 194 ARG n 
1 195 GLN n 
1 196 TRP n 
1 197 GLY n 
1 198 ALA n 
1 199 LEU n 
1 200 LYS n 
1 201 ALA n 
1 202 GLU n 
1 203 ALA n 
1 204 GLU n 
1 205 ALA n 
1 206 LEU n 
1 207 GLY n 
1 208 ILE n 
1 209 ARG n 
1 210 ILE n 
1 211 LEU n 
1 212 GLY n 
1 213 ASP n 
1 214 MET n 
1 215 PRO n 
1 216 ILE n 
1 217 PHE n 
1 218 VAL n 
1 219 ALA n 
1 220 GLU n 
1 221 ASP n 
1 222 SER n 
1 223 ALA n 
1 224 GLU n 
1 225 VAL n 
1 226 TRP n 
1 227 ALA n 
1 228 HIS n 
1 229 PRO n 
1 230 GLU n 
1 231 TRP n 
1 232 PHE n 
1 233 HIS n 
1 234 LEU n 
1 235 ASP n 
1 236 GLU n 
1 237 GLU n 
1 238 GLY n 
1 239 ARG n 
1 240 PRO n 
1 241 THR n 
1 242 VAL n 
1 243 VAL n 
1 244 ALA n 
1 245 GLY n 
1 246 VAL n 
1 247 PRO n 
1 248 PRO n 
1 249 ASP n 
1 250 TYR n 
1 251 PHE n 
1 252 SER n 
1 253 GLU n 
1 254 THR n 
1 255 GLY n 
1 256 GLN n 
1 257 ARG n 
1 258 TRP n 
1 259 GLY n 
1 260 ASN n 
1 261 PRO n 
1 262 LEU n 
1 263 TYR n 
1 264 ARG n 
1 265 TRP n 
1 266 ASP n 
1 267 VAL n 
1 268 LEU n 
1 269 GLU n 
1 270 ARG n 
1 271 GLU n 
1 272 GLY n 
1 273 PHE n 
1 274 SER n 
1 275 PHE n 
1 276 TRP n 
1 277 ILE n 
1 278 ARG n 
1 279 ARG n 
1 280 LEU n 
1 281 GLU n 
1 282 LYS n 
1 283 ALA n 
1 284 LEU n 
1 285 GLU n 
1 286 LEU n 
1 287 PHE n 
1 288 HIS n 
1 289 LEU n 
1 290 VAL n 
1 291 ARG n 
1 292 ILE n 
1 293 ASP n 
1 294 HIS n 
1 295 PHE n 
1 296 ARG n 
1 297 GLY n 
1 298 PHE n 
1 299 GLU n 
1 300 ALA n 
1 301 TYR n 
1 302 TRP n 
1 303 GLU n 
1 304 ILE n 
1 305 PRO n 
1 306 ALA n 
1 307 SER n 
1 308 CYS n 
1 309 PRO n 
1 310 THR n 
1 311 ALA n 
1 312 VAL n 
1 313 GLU n 
1 314 GLY n 
1 315 ARG n 
1 316 TRP n 
1 317 VAL n 
1 318 LYS n 
1 319 ALA n 
1 320 PRO n 
1 321 GLY n 
1 322 GLU n 
1 323 LYS n 
1 324 LEU n 
1 325 PHE n 
1 326 GLN n 
1 327 LYS n 
1 328 ILE n 
1 329 GLN n 
1 330 GLU n 
1 331 THR n 
1 332 PHE n 
1 333 GLY n 
1 334 GLN n 
1 335 VAL n 
1 336 PRO n 
1 337 ILE n 
1 338 LEU n 
1 339 ALA n 
1 340 GLU n 
1 341 ASP n 
1 342 LEU n 
1 343 GLY n 
1 344 VAL n 
1 345 ILE n 
1 346 THR n 
1 347 PRO n 
1 348 GLU n 
1 349 VAL n 
1 350 GLU n 
1 351 ALA n 
1 352 LEU n 
1 353 ARG n 
1 354 ASP n 
1 355 ARG n 
1 356 PHE n 
1 357 GLY n 
1 358 LEU n 
1 359 PRO n 
1 360 GLY n 
1 361 MET n 
1 362 LYS n 
1 363 VAL n 
1 364 LEU n 
1 365 GLN n 
1 366 PHE n 
1 367 ALA n 
1 368 PHE n 
1 369 ASP n 
1 370 ASP n 
1 371 GLY n 
1 372 MET n 
1 373 GLU n 
1 374 ASN n 
1 375 PRO n 
1 376 PHE n 
1 377 LEU n 
1 378 PRO n 
1 379 HIS n 
1 380 ASN n 
1 381 TYR n 
1 382 PRO n 
1 383 SER n 
1 384 HIS n 
1 385 GLY n 
1 386 ARG n 
1 387 VAL n 
1 388 VAL n 
1 389 VAL n 
1 390 TYR n 
1 391 THR n 
1 392 GLY n 
1 393 THR n 
1 394 HIS n 
1 395 ASP n 
1 396 ASN n 
1 397 ASP n 
1 398 THR n 
1 399 THR n 
1 400 LEU n 
1 401 GLY n 
1 402 TRP n 
1 403 TYR n 
1 404 ARG n 
1 405 THR n 
1 406 ALA n 
1 407 THR n 
1 408 PRO n 
1 409 HIS n 
1 410 GLU n 
1 411 LYS n 
1 412 ALA n 
1 413 PHE n 
1 414 MET n 
1 415 ALA n 
1 416 ARG n 
1 417 TYR n 
1 418 LEU n 
1 419 ALA n 
1 420 ASP n 
1 421 TRP n 
1 422 GLY n 
1 423 ILE n 
1 424 PHE n 
1 425 PHE n 
1 426 ARG n 
1 427 GLU n 
1 428 GLU n 
1 429 GLU n 
1 430 GLU n 
1 431 VAL n 
1 432 PRO n 
1 433 TRP n 
1 434 ALA n 
1 435 LEU n 
1 436 MET n 
1 437 ARG n 
1 438 LEU n 
1 439 GLY n 
1 440 MET n 
1 441 LYS n 
1 442 SER n 
1 443 VAL n 
1 444 ALA n 
1 445 ARG n 
1 446 LEU n 
1 447 ALA n 
1 448 VAL n 
1 449 TYR n 
1 450 PRO n 
1 451 VAL n 
1 452 GLN n 
1 453 ASP n 
1 454 VAL n 
1 455 LEU n 
1 456 ALA n 
1 457 LEU n 
1 458 GLY n 
1 459 SER n 
1 460 GLU n 
1 461 ALA n 
1 462 ARG n 
1 463 MET n 
1 464 ASN n 
1 465 TYR n 
1 466 PRO n 
1 467 GLY n 
1 468 ARG n 
1 469 PRO n 
1 470 SER n 
1 471 GLY n 
1 472 ASN n 
1 473 TRP n 
1 474 ALA n 
1 475 TRP n 
1 476 ARG n 
1 477 LEU n 
1 478 LEU n 
1 479 PRO n 
1 480 GLY n 
1 481 GLU n 
1 482 LEU n 
1 483 SER n 
1 484 PRO n 
1 485 GLU n 
1 486 HIS n 
1 487 GLY n 
1 488 GLU n 
1 489 ARG n 
1 490 LEU n 
1 491 ARG n 
1 492 ALA n 
1 493 MET n 
1 494 ALA n 
1 495 GLU n 
1 496 ALA n 
1 497 THR n 
1 498 GLU n 
1 499 ARG n 
1 500 LEU 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                   500 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 malQ 
_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      'Thermus thermophilus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     274 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   2   GLU GLU A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   PRO 4   4   4   PRO PRO A . n 
A 1 5   ARG 5   5   5   ARG ARG A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  THR 14  14  14  THR THR A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  PRO 17  17  17  PRO PRO A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  PRO 19  19  19  PRO PRO A . n 
A 1 20  TYR 20  20  20  TYR TYR A . n 
A 1 21  GLY 21  21  21  GLY GLY A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  GLU 38  38  38  GLU GLU A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  GLY 40  40  40  GLY GLY A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  GLN 42  42  42  GLN GLN A . n 
A 1 43  TYR 43  43  43  TYR TYR A . n 
A 1 44  TRP 44  44  44  TRP TRP A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  PRO 51  51  51  PRO PRO A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  PHE 62  62  62  PHE PHE A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  PHE 65  65  65  PHE PHE A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  TYR 70  70  70  TYR TYR A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  LYS 79  79  79  LYS LYS A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  PRO 88  88  88  PRO PRO A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  ARG 94  94  94  ARG ARG A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 TRP 103 103 103 TRP TRP A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 TRP 105 105 105 TRP TRP A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 PHE 115 115 115 PHE PHE A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 ASP 126 126 126 ASP ASP A . n 
A 1 127 PHE 127 127 127 PHE PHE A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 TRP 136 136 136 TRP TRP A . n 
A 1 137 TRP 137 137 137 TRP TRP A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 TYR 141 141 141 TYR TYR A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 MET 145 145 145 MET MET A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 HIS 151 151 151 HIS HIS A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 TRP 156 156 156 TRP TRP A . n 
A 1 157 ASN 157 157 157 ASN ASN A . n 
A 1 158 ARG 158 158 158 ARG ARG A . n 
A 1 159 TRP 159 159 159 TRP TRP A . n 
A 1 160 PRO 160 160 160 PRO PRO A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 PRO 162 162 162 PRO PRO A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 ARG 166 166 166 ARG ARG A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 GLU 173 173 173 GLU GLU A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 PHE 184 184 184 PHE PHE A . n 
A 1 185 HIS 185 185 185 HIS HIS A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 PHE 187 187 187 PHE PHE A . n 
A 1 188 THR 188 188 188 THR THR A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 TRP 190 190 190 TRP TRP A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 PHE 192 192 192 PHE PHE A . n 
A 1 193 PHE 193 193 193 PHE PHE A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 GLN 195 195 195 GLN GLN A . n 
A 1 196 TRP 196 196 196 TRP TRP A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 LYS 200 200 200 LYS LYS A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 GLY 207 207 207 GLY GLY A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 ARG 209 209 209 ARG ARG A . n 
A 1 210 ILE 210 210 210 ILE ILE A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 GLY 212 212 212 GLY GLY A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 MET 214 214 214 MET MET A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 VAL 218 218 218 VAL VAL A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 TRP 226 226 226 TRP TRP A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 HIS 228 228 228 HIS HIS A . n 
A 1 229 PRO 229 229 229 PRO PRO A . n 
A 1 230 GLU 230 230 230 GLU GLU A . n 
A 1 231 TRP 231 231 231 TRP TRP A . n 
A 1 232 PHE 232 232 232 PHE PHE A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 GLU 236 236 236 GLU GLU A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 ARG 239 239 239 ARG ARG A . n 
A 1 240 PRO 240 240 240 PRO PRO A . n 
A 1 241 THR 241 241 241 THR THR A . n 
A 1 242 VAL 242 242 242 VAL VAL A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 VAL 246 246 246 VAL VAL A . n 
A 1 247 PRO 247 247 247 PRO PRO A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 ASP 249 249 ?   ?   ?   A . n 
A 1 250 TYR 250 250 ?   ?   ?   A . n 
A 1 251 PHE 251 251 ?   ?   ?   A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 GLU 253 253 253 GLU GLU A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 ARG 257 257 257 ARG ARG A . n 
A 1 258 TRP 258 258 258 TRP TRP A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 ASN 260 260 260 ASN ASN A . n 
A 1 261 PRO 261 261 261 PRO PRO A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 TYR 263 263 263 TYR TYR A . n 
A 1 264 ARG 264 264 264 ARG ARG A . n 
A 1 265 TRP 265 265 265 TRP TRP A . n 
A 1 266 ASP 266 266 266 ASP ASP A . n 
A 1 267 VAL 267 267 267 VAL VAL A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 ARG 270 270 270 ARG ARG A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 PHE 273 273 273 PHE PHE A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 TRP 276 276 276 TRP TRP A . n 
A 1 277 ILE 277 277 277 ILE ILE A . n 
A 1 278 ARG 278 278 278 ARG ARG A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 GLU 281 281 281 GLU GLU A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 LEU 284 284 284 LEU LEU A . n 
A 1 285 GLU 285 285 285 GLU GLU A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 PHE 287 287 287 PHE PHE A . n 
A 1 288 HIS 288 288 288 HIS HIS A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 VAL 290 290 290 VAL VAL A . n 
A 1 291 ARG 291 291 291 ARG ARG A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 ASP 293 293 293 ASP ASP A . n 
A 1 294 HIS 294 294 294 HIS HIS A . n 
A 1 295 PHE 295 295 295 PHE PHE A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 GLY 297 297 297 GLY GLY A . n 
A 1 298 PHE 298 298 298 PHE PHE A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 ALA 300 300 300 ALA ALA A . n 
A 1 301 TYR 301 301 301 TYR TYR A . n 
A 1 302 TRP 302 302 302 TRP TRP A . n 
A 1 303 GLU 303 303 303 GLU GLU A . n 
A 1 304 ILE 304 304 304 ILE ILE A . n 
A 1 305 PRO 305 305 305 PRO PRO A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 CYS 308 308 308 CYS CYS A . n 
A 1 309 PRO 309 309 309 PRO PRO A . n 
A 1 310 THR 310 310 310 THR THR A . n 
A 1 311 ALA 311 311 311 ALA ALA A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 GLU 313 313 313 GLU GLU A . n 
A 1 314 GLY 314 314 314 GLY GLY A . n 
A 1 315 ARG 315 315 315 ARG ARG A . n 
A 1 316 TRP 316 316 316 TRP TRP A . n 
A 1 317 VAL 317 317 317 VAL VAL A . n 
A 1 318 LYS 318 318 318 LYS LYS A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 PRO 320 320 320 PRO PRO A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 GLU 322 322 322 GLU GLU A . n 
A 1 323 LYS 323 323 323 LYS LYS A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 PHE 325 325 325 PHE PHE A . n 
A 1 326 GLN 326 326 326 GLN GLN A . n 
A 1 327 LYS 327 327 327 LYS LYS A . n 
A 1 328 ILE 328 328 328 ILE ILE A . n 
A 1 329 GLN 329 329 329 GLN GLN A . n 
A 1 330 GLU 330 330 330 GLU GLU A . n 
A 1 331 THR 331 331 331 THR THR A . n 
A 1 332 PHE 332 332 332 PHE PHE A . n 
A 1 333 GLY 333 333 333 GLY GLY A . n 
A 1 334 GLN 334 334 334 GLN GLN A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 PRO 336 336 336 PRO PRO A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 LEU 338 338 338 LEU LEU A . n 
A 1 339 ALA 339 339 339 ALA ALA A . n 
A 1 340 GLU 340 340 340 GLU GLU A . n 
A 1 341 ASP 341 341 341 ASP ASP A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 VAL 344 344 344 VAL VAL A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 THR 346 346 346 THR THR A . n 
A 1 347 PRO 347 347 347 PRO PRO A . n 
A 1 348 GLU 348 348 348 GLU GLU A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 GLU 350 350 350 GLU GLU A . n 
A 1 351 ALA 351 351 351 ALA ALA A . n 
A 1 352 LEU 352 352 352 LEU LEU A . n 
A 1 353 ARG 353 353 353 ARG ARG A . n 
A 1 354 ASP 354 354 354 ASP ASP A . n 
A 1 355 ARG 355 355 355 ARG ARG A . n 
A 1 356 PHE 356 356 356 PHE PHE A . n 
A 1 357 GLY 357 357 357 GLY GLY A . n 
A 1 358 LEU 358 358 358 LEU LEU A . n 
A 1 359 PRO 359 359 359 PRO PRO A . n 
A 1 360 GLY 360 360 360 GLY GLY A . n 
A 1 361 MET 361 361 361 MET MET A . n 
A 1 362 LYS 362 362 362 LYS LYS A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 LEU 364 364 364 LEU LEU A . n 
A 1 365 GLN 365 365 365 GLN GLN A . n 
A 1 366 PHE 366 366 366 PHE PHE A . n 
A 1 367 ALA 367 367 367 ALA ALA A . n 
A 1 368 PHE 368 368 368 PHE PHE A . n 
A 1 369 ASP 369 369 369 ASP ASP A . n 
A 1 370 ASP 370 370 370 ASP ASP A . n 
A 1 371 GLY 371 371 371 GLY GLY A . n 
A 1 372 MET 372 372 372 MET MET A . n 
A 1 373 GLU 373 373 373 GLU GLU A . n 
A 1 374 ASN 374 374 374 ASN ASN A . n 
A 1 375 PRO 375 375 375 PRO PRO A . n 
A 1 376 PHE 376 376 376 PHE PHE A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 PRO 378 378 378 PRO PRO A . n 
A 1 379 HIS 379 379 379 HIS HIS A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 TYR 381 381 381 TYR TYR A . n 
A 1 382 PRO 382 382 382 PRO PRO A . n 
A 1 383 SER 383 383 383 SER SER A . n 
A 1 384 HIS 384 384 384 HIS HIS A . n 
A 1 385 GLY 385 385 385 GLY GLY A . n 
A 1 386 ARG 386 386 386 ARG ARG A . n 
A 1 387 VAL 387 387 387 VAL VAL A . n 
A 1 388 VAL 388 388 388 VAL VAL A . n 
A 1 389 VAL 389 389 389 VAL VAL A . n 
A 1 390 TYR 390 390 390 TYR TYR A . n 
A 1 391 THR 391 391 391 THR THR A . n 
A 1 392 GLY 392 392 392 GLY GLY A . n 
A 1 393 THR 393 393 393 THR THR A . n 
A 1 394 HIS 394 394 394 HIS HIS A . n 
A 1 395 ASP 395 395 395 ASP ASP A . n 
A 1 396 ASN 396 396 396 ASN ASN A . n 
A 1 397 ASP 397 397 397 ASP ASP A . n 
A 1 398 THR 398 398 398 THR THR A . n 
A 1 399 THR 399 399 399 THR THR A . n 
A 1 400 LEU 400 400 400 LEU LEU A . n 
A 1 401 GLY 401 401 401 GLY GLY A . n 
A 1 402 TRP 402 402 402 TRP TRP A . n 
A 1 403 TYR 403 403 403 TYR TYR A . n 
A 1 404 ARG 404 404 404 ARG ARG A . n 
A 1 405 THR 405 405 405 THR THR A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 THR 407 407 407 THR THR A . n 
A 1 408 PRO 408 408 408 PRO PRO A . n 
A 1 409 HIS 409 409 409 HIS HIS A . n 
A 1 410 GLU 410 410 410 GLU GLU A . n 
A 1 411 LYS 411 411 411 LYS LYS A . n 
A 1 412 ALA 412 412 412 ALA ALA A . n 
A 1 413 PHE 413 413 413 PHE PHE A . n 
A 1 414 MET 414 414 414 MET MET A . n 
A 1 415 ALA 415 415 415 ALA ALA A . n 
A 1 416 ARG 416 416 416 ARG ARG A . n 
A 1 417 TYR 417 417 417 TYR TYR A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 ALA 419 419 419 ALA ALA A . n 
A 1 420 ASP 420 420 420 ASP ASP A . n 
A 1 421 TRP 421 421 421 TRP TRP A . n 
A 1 422 GLY 422 422 422 GLY GLY A . n 
A 1 423 ILE 423 423 423 ILE ILE A . n 
A 1 424 PHE 424 424 424 PHE PHE A . n 
A 1 425 PHE 425 425 425 PHE PHE A . n 
A 1 426 ARG 426 426 426 ARG ARG A . n 
A 1 427 GLU 427 427 427 GLU GLU A . n 
A 1 428 GLU 428 428 428 GLU GLU A . n 
A 1 429 GLU 429 429 429 GLU GLU A . n 
A 1 430 GLU 430 430 430 GLU GLU A . n 
A 1 431 VAL 431 431 431 VAL VAL A . n 
A 1 432 PRO 432 432 432 PRO PRO A . n 
A 1 433 TRP 433 433 433 TRP TRP A . n 
A 1 434 ALA 434 434 434 ALA ALA A . n 
A 1 435 LEU 435 435 435 LEU LEU A . n 
A 1 436 MET 436 436 436 MET MET A . n 
A 1 437 ARG 437 437 437 ARG ARG A . n 
A 1 438 LEU 438 438 438 LEU LEU A . n 
A 1 439 GLY 439 439 439 GLY GLY A . n 
A 1 440 MET 440 440 440 MET MET A . n 
A 1 441 LYS 441 441 441 LYS LYS A . n 
A 1 442 SER 442 442 442 SER SER A . n 
A 1 443 VAL 443 443 443 VAL VAL A . n 
A 1 444 ALA 444 444 444 ALA ALA A . n 
A 1 445 ARG 445 445 445 ARG ARG A . n 
A 1 446 LEU 446 446 446 LEU LEU A . n 
A 1 447 ALA 447 447 447 ALA ALA A . n 
A 1 448 VAL 448 448 448 VAL VAL A . n 
A 1 449 TYR 449 449 449 TYR TYR A . n 
A 1 450 PRO 450 450 450 PRO PRO A . n 
A 1 451 VAL 451 451 451 VAL VAL A . n 
A 1 452 GLN 452 452 452 GLN GLN A . n 
A 1 453 ASP 453 453 453 ASP ASP A . n 
A 1 454 VAL 454 454 454 VAL VAL A . n 
A 1 455 LEU 455 455 455 LEU LEU A . n 
A 1 456 ALA 456 456 456 ALA ALA A . n 
A 1 457 LEU 457 457 457 LEU LEU A . n 
A 1 458 GLY 458 458 458 GLY GLY A . n 
A 1 459 SER 459 459 459 SER SER A . n 
A 1 460 GLU 460 460 460 GLU GLU A . n 
A 1 461 ALA 461 461 461 ALA ALA A . n 
A 1 462 ARG 462 462 462 ARG ARG A . n 
A 1 463 MET 463 463 463 MET MET A . n 
A 1 464 ASN 464 464 464 ASN ASN A . n 
A 1 465 TYR 465 465 465 TYR TYR A . n 
A 1 466 PRO 466 466 466 PRO PRO A . n 
A 1 467 GLY 467 467 467 GLY GLY A . n 
A 1 468 ARG 468 468 468 ARG ARG A . n 
A 1 469 PRO 469 469 469 PRO PRO A . n 
A 1 470 SER 470 470 470 SER SER A . n 
A 1 471 GLY 471 471 471 GLY GLY A . n 
A 1 472 ASN 472 472 472 ASN ASN A . n 
A 1 473 TRP 473 473 473 TRP TRP A . n 
A 1 474 ALA 474 474 474 ALA ALA A . n 
A 1 475 TRP 475 475 475 TRP TRP A . n 
A 1 476 ARG 476 476 476 ARG ARG A . n 
A 1 477 LEU 477 477 477 LEU LEU A . n 
A 1 478 LEU 478 478 478 LEU LEU A . n 
A 1 479 PRO 479 479 479 PRO PRO A . n 
A 1 480 GLY 480 480 480 GLY GLY A . n 
A 1 481 GLU 481 481 481 GLU GLU A . n 
A 1 482 LEU 482 482 482 LEU LEU A . n 
A 1 483 SER 483 483 483 SER SER A . n 
A 1 484 PRO 484 484 484 PRO PRO A . n 
A 1 485 GLU 485 485 485 GLU GLU A . n 
A 1 486 HIS 486 486 486 HIS HIS A . n 
A 1 487 GLY 487 487 487 GLY GLY A . n 
A 1 488 GLU 488 488 488 GLU GLU A . n 
A 1 489 ARG 489 489 489 ARG ARG A . n 
A 1 490 LEU 490 490 490 LEU LEU A . n 
A 1 491 ARG 491 491 491 ARG ARG A . n 
A 1 492 ALA 492 492 492 ALA ALA A . n 
A 1 493 MET 493 493 493 MET MET A . n 
A 1 494 ALA 494 494 494 ALA ALA A . n 
A 1 495 GLU 495 495 495 GLU GLU A . n 
A 1 496 ALA 496 496 496 ALA ALA A . n 
A 1 497 THR 497 497 497 THR THR A . n 
A 1 498 GLU 498 498 498 GLU GLU A . n 
A 1 499 ARG 499 499 499 ARG ARG A . n 
A 1 500 LEU 500 500 500 LEU LEU A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HOH 1   601 21  HOH HOH A . 
B 2 HOH 2   602 30  HOH HOH A . 
B 2 HOH 3   603 115 HOH HOH A . 
B 2 HOH 4   604 111 HOH HOH A . 
B 2 HOH 5   605 27  HOH HOH A . 
B 2 HOH 6   606 137 HOH HOH A . 
B 2 HOH 7   607 71  HOH HOH A . 
B 2 HOH 8   608 101 HOH HOH A . 
B 2 HOH 9   609 50  HOH HOH A . 
B 2 HOH 10  610 34  HOH HOH A . 
B 2 HOH 11  611 20  HOH HOH A . 
B 2 HOH 12  612 141 HOH HOH A . 
B 2 HOH 13  613 61  HOH HOH A . 
B 2 HOH 14  614 49  HOH HOH A . 
B 2 HOH 15  615 108 HOH HOH A . 
B 2 HOH 16  616 68  HOH HOH A . 
B 2 HOH 17  617 97  HOH HOH A . 
B 2 HOH 18  618 10  HOH HOH A . 
B 2 HOH 19  619 31  HOH HOH A . 
B 2 HOH 20  620 36  HOH HOH A . 
B 2 HOH 21  621 121 HOH HOH A . 
B 2 HOH 22  622 51  HOH HOH A . 
B 2 HOH 23  623 37  HOH HOH A . 
B 2 HOH 24  624 4   HOH HOH A . 
B 2 HOH 25  625 62  HOH HOH A . 
B 2 HOH 26  626 125 HOH HOH A . 
B 2 HOH 27  627 128 HOH HOH A . 
B 2 HOH 28  628 104 HOH HOH A . 
B 2 HOH 29  629 16  HOH HOH A . 
B 2 HOH 30  630 3   HOH HOH A . 
B 2 HOH 31  631 75  HOH HOH A . 
B 2 HOH 32  632 107 HOH HOH A . 
B 2 HOH 33  633 22  HOH HOH A . 
B 2 HOH 34  634 73  HOH HOH A . 
B 2 HOH 35  635 15  HOH HOH A . 
B 2 HOH 36  636 133 HOH HOH A . 
B 2 HOH 37  637 147 HOH HOH A . 
B 2 HOH 38  638 2   HOH HOH A . 
B 2 HOH 39  639 63  HOH HOH A . 
B 2 HOH 40  640 13  HOH HOH A . 
B 2 HOH 41  641 7   HOH HOH A . 
B 2 HOH 42  642 144 HOH HOH A . 
B 2 HOH 43  643 146 HOH HOH A . 
B 2 HOH 44  644 28  HOH HOH A . 
B 2 HOH 45  645 26  HOH HOH A . 
B 2 HOH 46  646 69  HOH HOH A . 
B 2 HOH 47  647 56  HOH HOH A . 
B 2 HOH 48  648 100 HOH HOH A . 
B 2 HOH 49  649 24  HOH HOH A . 
B 2 HOH 50  650 114 HOH HOH A . 
B 2 HOH 51  651 53  HOH HOH A . 
B 2 HOH 52  652 44  HOH HOH A . 
B 2 HOH 53  653 45  HOH HOH A . 
B 2 HOH 54  654 83  HOH HOH A . 
B 2 HOH 55  655 5   HOH HOH A . 
B 2 HOH 56  656 39  HOH HOH A . 
B 2 HOH 57  657 35  HOH HOH A . 
B 2 HOH 58  658 29  HOH HOH A . 
B 2 HOH 59  659 38  HOH HOH A . 
B 2 HOH 60  660 84  HOH HOH A . 
B 2 HOH 61  661 19  HOH HOH A . 
B 2 HOH 62  662 136 HOH HOH A . 
B 2 HOH 63  663 70  HOH HOH A . 
B 2 HOH 64  664 126 HOH HOH A . 
B 2 HOH 65  665 41  HOH HOH A . 
B 2 HOH 66  666 148 HOH HOH A . 
B 2 HOH 67  667 23  HOH HOH A . 
B 2 HOH 68  668 32  HOH HOH A . 
B 2 HOH 69  669 99  HOH HOH A . 
B 2 HOH 70  670 9   HOH HOH A . 
B 2 HOH 71  671 1   HOH HOH A . 
B 2 HOH 72  672 42  HOH HOH A . 
B 2 HOH 73  673 77  HOH HOH A . 
B 2 HOH 74  674 64  HOH HOH A . 
B 2 HOH 75  675 116 HOH HOH A . 
B 2 HOH 76  676 74  HOH HOH A . 
B 2 HOH 77  677 112 HOH HOH A . 
B 2 HOH 78  678 14  HOH HOH A . 
B 2 HOH 79  679 17  HOH HOH A . 
B 2 HOH 80  680 11  HOH HOH A . 
B 2 HOH 81  681 6   HOH HOH A . 
B 2 HOH 82  682 33  HOH HOH A . 
B 2 HOH 83  683 46  HOH HOH A . 
B 2 HOH 84  684 95  HOH HOH A . 
B 2 HOH 85  685 40  HOH HOH A . 
B 2 HOH 86  686 142 HOH HOH A . 
B 2 HOH 87  687 8   HOH HOH A . 
B 2 HOH 88  688 92  HOH HOH A . 
B 2 HOH 89  689 139 HOH HOH A . 
B 2 HOH 90  690 18  HOH HOH A . 
B 2 HOH 91  691 72  HOH HOH A . 
B 2 HOH 92  692 81  HOH HOH A . 
B 2 HOH 93  693 25  HOH HOH A . 
B 2 HOH 94  694 12  HOH HOH A . 
B 2 HOH 95  695 58  HOH HOH A . 
B 2 HOH 96  696 118 HOH HOH A . 
B 2 HOH 97  697 117 HOH HOH A . 
B 2 HOH 98  698 57  HOH HOH A . 
B 2 HOH 99  699 85  HOH HOH A . 
B 2 HOH 100 700 102 HOH HOH A . 
B 2 HOH 101 701 54  HOH HOH A . 
B 2 HOH 102 702 91  HOH HOH A . 
B 2 HOH 103 703 65  HOH HOH A . 
B 2 HOH 104 704 93  HOH HOH A . 
B 2 HOH 105 705 106 HOH HOH A . 
B 2 HOH 106 706 48  HOH HOH A . 
B 2 HOH 107 707 113 HOH HOH A . 
B 2 HOH 108 708 60  HOH HOH A . 
B 2 HOH 109 709 145 HOH HOH A . 
B 2 HOH 110 710 52  HOH HOH A . 
B 2 HOH 111 711 80  HOH HOH A . 
B 2 HOH 112 712 59  HOH HOH A . 
B 2 HOH 113 713 123 HOH HOH A . 
B 2 HOH 114 714 88  HOH HOH A . 
B 2 HOH 115 715 131 HOH HOH A . 
B 2 HOH 116 716 149 HOH HOH A . 
B 2 HOH 117 717 90  HOH HOH A . 
B 2 HOH 118 718 132 HOH HOH A . 
B 2 HOH 119 719 140 HOH HOH A . 
B 2 HOH 120 720 96  HOH HOH A . 
B 2 HOH 121 721 127 HOH HOH A . 
B 2 HOH 122 722 122 HOH HOH A . 
B 2 HOH 123 723 94  HOH HOH A . 
B 2 HOH 124 724 98  HOH HOH A . 
B 2 HOH 125 725 138 HOH HOH A . 
B 2 HOH 126 726 55  HOH HOH A . 
B 2 HOH 127 727 103 HOH HOH A . 
B 2 HOH 128 728 47  HOH HOH A . 
B 2 HOH 129 729 89  HOH HOH A . 
B 2 HOH 130 730 130 HOH HOH A . 
B 2 HOH 131 731 67  HOH HOH A . 
B 2 HOH 132 732 76  HOH HOH A . 
B 2 HOH 133 733 43  HOH HOH A . 
B 2 HOH 134 734 134 HOH HOH A . 
B 2 HOH 135 735 119 HOH HOH A . 
B 2 HOH 136 736 79  HOH HOH A . 
B 2 HOH 137 737 82  HOH HOH A . 
B 2 HOH 138 738 143 HOH HOH A . 
B 2 HOH 139 739 78  HOH HOH A . 
B 2 HOH 140 740 109 HOH HOH A . 
B 2 HOH 141 741 86  HOH HOH A . 
B 2 HOH 142 742 110 HOH HOH A . 
B 2 HOH 143 743 135 HOH HOH A . 
B 2 HOH 144 744 66  HOH HOH A . 
B 2 HOH 145 745 87  HOH HOH A . 
B 2 HOH 146 746 120 HOH HOH A . 
B 2 HOH 147 747 124 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0430 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   98.26 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9U5L 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     197.783 
_cell.length_a_esd                 ? 
_cell.length_b                     41.391 
_cell.length_b_esd                 ? 
_cell.length_c                     58.458 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9U5L 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9U5L 
_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             2.06 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.37 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Bis-Tris pH 5.5, 35% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   5.5-6.5 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-12-13 
_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   0.979183 
_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                        'ALS BEAMLINE 5.0.3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979183 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.0.3 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9U5L 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.1 
_reflns.d_resolution_low                               40.50 
_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                                     27285 
_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                           98.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.120 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.10 
_reflns_shell.d_res_low                                     8.91 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             27285 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.136 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_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                                  ? 
_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]                            29.91 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.60 
_refine.aniso_B[2][2]                            -7.07 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -22.84 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.865 
_refine.correlation_coeff_Fo_to_Fc_free          0.822 
_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                                 9U5L 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             40.50 
_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                     25946 
_refine.ls_number_reflns_R_free                  1333 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.28 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.26675 
_refine.ls_R_factor_R_free                       0.31558 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.26431 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                       0.082 
_refine.pdbx_overall_ESU_R_Free                  0.058 
_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                             7.612 
_refine.overall_SU_ML                            0.210 
_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                       2.10 
_refine_hist.d_res_low                        40.50 
_refine_hist.number_atoms_solvent             149 
_refine_hist.number_atoms_total               4182 
_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        4033 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.002  0.012  4200 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3860 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 0.960  1.838  5718 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.363  1.752  8872 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.972  5.000  500  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 3.874  5.000  39   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.054 10.000 643  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.048  0.200  564  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  5151 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1075 ? 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' ? 0.817  2.503  1997 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.817  2.503  1997 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.394  4.500  2498 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.393  4.500  2499 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 0.677  2.588  2203 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.677  2.588  2204 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.187  4.716  3221 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.709  24.94  4836 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 2.696  24.80  4830 ? 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                          2.100 
_refine_ls_shell.d_res_low                           2.155 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                93 
_refine_ls_shell.number_reflns_R_work                1824 
_refine_ls_shell.percent_reflns_obs                  94.90 
_refine_ls_shell.percent_reflns_R_free               ? 
_refine_ls_shell.R_factor_all                        ? 
_refine_ls_shell.R_factor_obs                        ? 
_refine_ls_shell.R_factor_R_free_error               ? 
_refine_ls_shell.R_factor_R_work                     0.267 
_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.correlation_coeff_Fo_to_Fc          ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free     ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free   ? 
_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                     0.319 
# 
_struct.entry_id                     9U5L 
_struct.title                        '4-alpha-glucanotransferase from Thermus thermophilus STB20' 
_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        9U5L 
_struct_keywords.text            'Alpha amylase, Thermoduric, Disproportionation, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MALQ_THETH 
_struct_ref.pdbx_db_accession          O87172 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MELPRAFGLLLHPTSLPGPYGVGVLGREARDFLRFLKEAGGRYWQVLPLGPTGYGDSPYQSFSAFAGNPYLIDLRPLAER
GYVRLEDPGFPQGRVDYGLLYAWKWPALKEAFRGFKEKASPEEREAFAAFREREAWWLEDYALFMALKGAHGGLPWNRWP
LPLRKREEKALREAKSALAEEVAFHAFTQWLFFRQWGALKAEAEALGIRIIGDMPIFVAEDSAEVWAHPEWFHLDEEGRP
TVVAGVPPDYFSETGQRWGNPLYRWDVLEREGFSFWIRRLEKALELFHLVRIDHFRGFEAYWEIPASCPTAVEGRWVKAP
GEKLFQKIQEVFGEVPVLAEDLGVITPEVEALRDRFGLPGMKVLQFAFDDGMENPFLPHNYPAHGRVVVYTGTHDNDTTL
GWYRTATPHEKAFMARYLADWGITFREEEEVPWALMHLGMKSVARLAVYPVQDVLALGSEARMNYPGRPSGNWAWRLLPG
ELSPEHGARLRAMAEATERL
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9U5L 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 500 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O87172 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  500 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       500 
# 
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 9U5L GLN A 27  ? UNP O87172 ARG 27  conflict 27  1  
1 9U5L GLN A 42  ? UNP O87172 ARG 42  conflict 42  2  
1 9U5L VAL A 72  ? UNP O87172 ILE 72  conflict 72  3  
1 9U5L LYS A 79  ? UNP O87172 GLU 79  conflict 79  4  
1 9U5L GLN A 116 ? UNP O87172 LYS 116 conflict 116 5  
1 9U5L PRO A 120 ? UNP O87172 SER 120 conflict 120 6  
1 9U5L ASP A 126 ? UNP O87172 ALA 126 conflict 126 7  
1 9U5L LYS A 133 ? UNP O87172 ARG 133 conflict 133 8  
1 9U5L GLN A 169 ? UNP O87172 LYS 169 conflict 169 9  
1 9U5L LEU A 211 ? UNP O87172 ILE 211 conflict 211 10 
1 9U5L THR A 331 ? UNP O87172 VAL 331 conflict 331 11 
1 9U5L GLN A 334 ? UNP O87172 GLU 334 conflict 334 12 
1 9U5L ILE A 337 ? UNP O87172 VAL 337 conflict 337 13 
1 9U5L SER A 383 ? UNP O87172 ALA 383 conflict 383 14 
1 9U5L PHE A 424 ? UNP O87172 THR 424 conflict 424 15 
1 9U5L ARG A 437 ? UNP O87172 HIS 437 conflict 437 16 
1 9U5L GLU A 488 ? UNP O87172 ALA 488 conflict 488 17 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'native gel electrophoresis' 
_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 HIS A 12  ? LEU A 16  ? HIS A 12  LEU A 16  5 ? 5  
HELX_P HELX_P2  AA2 GLY A 26  ? ALA A 39  ? GLY A 26  ALA A 39  1 ? 14 
HELX_P HELX_P3  AA3 ASN A 68  ? VAL A 72  ? ASN A 68  VAL A 72  5 ? 5  
HELX_P HELX_P4  AA4 LEU A 74  ? GLY A 81  ? LEU A 74  GLY A 81  1 ? 8  
HELX_P HELX_P5  AA5 ASP A 96  ? ALA A 119 ? ASP A 96  ALA A 119 1 ? 24 
HELX_P HELX_P6  AA6 PRO A 120 ? HIS A 151 ? PRO A 120 HIS A 151 1 ? 32 
HELX_P HELX_P7  AA7 PRO A 155 ? TRP A 159 ? PRO A 155 TRP A 159 5 ? 5  
HELX_P HELX_P8  AA8 PRO A 160 ? ARG A 166 ? PRO A 160 ARG A 166 1 ? 7  
HELX_P HELX_P9  AA9 GLU A 167 ? LEU A 178 ? GLU A 167 LEU A 178 1 ? 12 
HELX_P HELX_P10 AB1 LEU A 178 ? LEU A 206 ? LEU A 178 LEU A 206 1 ? 29 
HELX_P HELX_P11 AB2 SER A 222 ? HIS A 228 ? SER A 222 HIS A 228 1 ? 7  
HELX_P HELX_P12 AB3 PRO A 229 ? PHE A 232 ? PRO A 229 PHE A 232 5 ? 4  
HELX_P HELX_P13 AB4 ARG A 264 ? GLU A 271 ? ARG A 264 GLU A 271 1 ? 8  
HELX_P HELX_P14 AB5 PHE A 273 ? PHE A 287 ? PHE A 273 PHE A 287 1 ? 15 
HELX_P HELX_P15 AB6 HIS A 294 ? PHE A 298 ? HIS A 294 PHE A 298 5 ? 5  
HELX_P HELX_P16 AB7 PRO A 320 ? GLY A 333 ? PRO A 320 GLY A 333 1 ? 14 
HELX_P HELX_P17 AB8 THR A 346 ? PHE A 356 ? THR A 346 PHE A 356 1 ? 11 
HELX_P HELX_P18 AB9 GLN A 365 ? ALA A 367 ? GLN A 365 ALA A 367 5 ? 3  
HELX_P HELX_P19 AC1 LEU A 377 ? TYR A 381 ? LEU A 377 TYR A 381 5 ? 5  
HELX_P HELX_P20 AC2 THR A 398 ? ALA A 406 ? THR A 398 ALA A 406 1 ? 9  
HELX_P HELX_P21 AC3 THR A 407 ? TRP A 421 ? THR A 407 TRP A 421 1 ? 15 
HELX_P HELX_P22 AC4 GLU A 430 ? SER A 442 ? GLU A 430 SER A 442 1 ? 13 
HELX_P HELX_P23 AC5 VAL A 451 ? LEU A 455 ? VAL A 451 LEU A 455 1 ? 5  
HELX_P HELX_P24 AC6 GLY A 458 ? ARG A 462 ? GLY A 458 ARG A 462 5 ? 5  
HELX_P HELX_P25 AC7 SER A 483 ? THR A 497 ? SER A 483 THR A 497 1 ? 15 
# 
_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 ? 9 ? 
AA2 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 6   ? LEU A 10  ? ALA A 6   LEU A 10  
AA1 2 TYR A 43  ? GLN A 45  ? TYR A 43  GLN A 45  
AA1 3 ARG A 209 ? PRO A 215 ? ARG A 209 PRO A 215 
AA1 4 LEU A 289 ? ASP A 293 ? LEU A 289 ASP A 293 
AA1 5 ILE A 337 ? ALA A 339 ? ILE A 337 ALA A 339 
AA1 6 GLY A 360 ? VAL A 363 ? GLY A 360 VAL A 363 
AA1 7 VAL A 387 ? TYR A 390 ? VAL A 387 TYR A 390 
AA1 8 LEU A 446 ? PRO A 450 ? LEU A 446 PRO A 450 
AA1 9 ALA A 6   ? LEU A 10  ? ALA A 6   LEU A 10  
AA2 1 GLN A 256 ? PRO A 261 ? GLN A 256 PRO A 261 
AA2 2 VAL A 242 ? VAL A 246 ? VAL A 242 VAL A 246 
AA2 3 ALA A 300 ? PRO A 305 ? ALA A 300 PRO A 305 
AA2 4 ARG A 315 ? LYS A 318 ? ARG A 315 LYS A 318 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 9   ? N LEU A 9   O GLN A 45  ? O GLN A 45  
AA1 2 3 N TRP A 44  ? N TRP A 44  O LEU A 211 ? O LEU A 211 
AA1 3 4 N GLY A 212 ? N GLY A 212 O LEU A 289 ? O LEU A 289 
AA1 4 5 N ILE A 292 ? N ILE A 292 O LEU A 338 ? O LEU A 338 
AA1 5 6 O ALA A 339 ? O ALA A 339 N MET A 361 ? N MET A 361 
AA1 6 7 N LYS A 362 ? N LYS A 362 O TYR A 390 ? O TYR A 390 
AA1 7 8 N VAL A 389 ? N VAL A 389 O VAL A 448 ? O VAL A 448 
AA1 8 9 O ALA A 447 ? O ALA A 447 N GLY A 8   ? N GLY A 8   
AA2 1 2 O ASN A 260 ? O ASN A 260 N ALA A 244 ? N ALA A 244 
AA2 2 3 N VAL A 243 ? N VAL A 243 O ILE A 304 ? O ILE A 304 
AA2 3 4 N GLU A 303 ? N GLU A 303 O ARG A 315 ? O ARG A 315 
# 
_pdbx_entry_details.entry_id                   9U5L 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASP 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     370 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -102.22 
_pdbx_validate_torsion.psi             -145.69 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A ASP 249 ? A ASP 249 
3 1 Y 1 A TYR 250 ? A TYR 250 
4 1 Y 1 A PHE 251 ? A PHE 251 
# 
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  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           32472281 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1FP8 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9U5L 
_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]   0.005056 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000734 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024160 
_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]   0.017286 
_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 
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   . GLU A 1 2   ? 12.774 -16.680 34.312  1.00 40.68 ? 2   GLU A N   1 
ATOM   2    C CA  . GLU A 1 2   ? 13.106 -15.701 35.382  1.00 40.07 ? 2   GLU A CA  1 
ATOM   3    C C   . GLU A 1 2   ? 14.618 -15.482 35.414  1.00 40.19 ? 2   GLU A C   1 
ATOM   4    O O   . GLU A 1 2   ? 15.380 -16.433 35.578  1.00 42.12 ? 2   GLU A O   1 
ATOM   5    C CB  . GLU A 1 2   ? 12.575 -16.187 36.731  1.00 40.20 ? 2   GLU A CB  1 
ATOM   6    C CG  . GLU A 1 2   ? 11.051 -16.256 36.790  1.00 40.47 ? 2   GLU A CG  1 
ATOM   7    C CD  . GLU A 1 2   ? 10.483 -16.686 38.130  1.00 40.13 ? 2   GLU A CD  1 
ATOM   8    O OE1 . GLU A 1 2   ? 11.272 -16.980 39.053  1.00 40.45 ? 2   GLU A OE1 1 
ATOM   9    O OE2 . GLU A 1 2   ? 9.241  -16.718 38.246  1.00 39.35 ? 2   GLU A OE2 1 
ATOM   10   N N   . LEU A 1 3   ? 15.039 -14.220 35.258  1.00 37.71 ? 3   LEU A N   1 
ATOM   11   C CA  . LEU A 1 3   ? 16.445 -13.886 35.095  1.00 35.34 ? 3   LEU A CA  1 
ATOM   12   C C   . LEU A 1 3   ? 17.219 -14.234 36.363  1.00 33.83 ? 3   LEU A C   1 
ATOM   13   O O   . LEU A 1 3   ? 16.778 -13.923 37.468  1.00 32.05 ? 3   LEU A O   1 
ATOM   14   C CB  . LEU A 1 3   ? 16.622 -12.405 34.756  1.00 35.00 ? 3   LEU A CB  1 
ATOM   15   C CG  . LEU A 1 3   ? 16.324 -11.986 33.314  1.00 34.94 ? 3   LEU A CG  1 
ATOM   16   C CD1 . LEU A 1 3   ? 16.480 -10.480 33.183  1.00 34.91 ? 3   LEU A CD1 1 
ATOM   17   C CD2 . LEU A 1 3   ? 17.223 -12.705 32.324  1.00 34.97 ? 3   LEU A CD2 1 
ATOM   18   N N   . PRO A 1 4   ? 18.412 -14.861 36.240  1.00 31.58 ? 4   PRO A N   1 
ATOM   19   C CA  . PRO A 1 4   ? 19.271 -15.088 37.390  1.00 30.69 ? 4   PRO A CA  1 
ATOM   20   C C   . PRO A 1 4   ? 19.942 -13.794 37.836  1.00 28.51 ? 4   PRO A C   1 
ATOM   21   O O   . PRO A 1 4   ? 20.200 -12.921 37.010  1.00 27.35 ? 4   PRO A O   1 
ATOM   22   C CB  . PRO A 1 4   ? 20.268 -16.119 36.872  1.00 31.45 ? 4   PRO A CB  1 
ATOM   23   C CG  . PRO A 1 4   ? 20.402 -15.722 35.412  1.00 31.51 ? 4   PRO A CG  1 
ATOM   24   C CD  . PRO A 1 4   ? 19.022 -15.323 34.982  1.00 32.26 ? 4   PRO A CD  1 
ATOM   25   N N   . ARG A 1 5   ? 20.189 -13.663 39.142  1.00 26.24 ? 5   ARG A N   1 
ATOM   26   C CA  . ARG A 1 5   ? 21.027 -12.584 39.636  1.00 24.73 ? 5   ARG A CA  1 
ATOM   27   C C   . ARG A 1 5   ? 22.455 -12.871 39.177  1.00 23.11 ? 5   ARG A C   1 
ATOM   28   O O   . ARG A 1 5   ? 23.048 -13.868 39.590  1.00 23.71 ? 5   ARG A O   1 
ATOM   29   C CB  . ARG A 1 5   ? 20.881 -12.435 41.154  1.00 24.57 ? 5   ARG A CB  1 
ATOM   30   C CG  . ARG A 1 5   ? 21.580 -11.207 41.716  1.00 24.39 ? 5   ARG A CG  1 
ATOM   31   C CD  . ARG A 1 5   ? 21.507 -11.150 43.233  1.00 24.24 ? 5   ARG A CD  1 
ATOM   32   N NE  . ARG A 1 5   ? 22.302 -10.035 43.762  1.00 23.69 ? 5   ARG A NE  1 
ATOM   33   C CZ  . ARG A 1 5   ? 22.025 -8.746  43.593  1.00 24.28 ? 5   ARG A CZ  1 
ATOM   34   N NH1 . ARG A 1 5   ? 20.916 -8.366  42.973  1.00 25.06 ? 5   ARG A NH1 1 
ATOM   35   N NH2 . ARG A 1 5   ? 22.851 -7.832  44.068  1.00 23.86 ? 5   ARG A NH2 1 
ATOM   36   N N   . ALA A 1 6   ? 22.974 -12.022 38.280  1.00 21.69 ? 6   ALA A N   1 
ATOM   37   C CA  . ALA A 1 6   ? 24.216 -12.302 37.574  1.00 21.22 ? 6   ALA A CA  1 
ATOM   38   C C   . ALA A 1 6   ? 24.836 -11.011 37.044  1.00 20.15 ? 6   ALA A C   1 
ATOM   39   O O   . ALA A 1 6   ? 24.241 -9.942  37.161  1.00 19.62 ? 6   ALA A O   1 
ATOM   40   C CB  . ALA A 1 6   ? 23.945 -13.281 36.450  1.00 21.17 ? 6   ALA A CB  1 
ATOM   41   N N   . PHE A 1 7   ? 26.040 -11.129 36.467  1.00 19.07 ? 7   PHE A N   1 
ATOM   42   C CA  . PHE A 1 7   ? 26.682 -10.011 35.793  1.00 18.87 ? 7   PHE A CA  1 
ATOM   43   C C   . PHE A 1 7   ? 27.126 -10.456 34.402  1.00 18.56 ? 7   PHE A C   1 
ATOM   44   O O   . PHE A 1 7   ? 27.422 -11.628 34.173  1.00 18.25 ? 7   PHE A O   1 
ATOM   45   C CB  . PHE A 1 7   ? 27.854 -9.405  36.577  1.00 19.05 ? 7   PHE A CB  1 
ATOM   46   C CG  . PHE A 1 7   ? 29.258 -9.945  36.323  1.00 19.43 ? 7   PHE A CG  1 
ATOM   47   C CD1 . PHE A 1 7   ? 29.794 -10.955 37.118  1.00 19.68 ? 7   PHE A CD1 1 
ATOM   48   C CD2 . PHE A 1 7   ? 30.067 -9.394  35.331  1.00 19.38 ? 7   PHE A CD2 1 
ATOM   49   C CE1 . PHE A 1 7   ? 31.084 -11.423 36.902  1.00 19.42 ? 7   PHE A CE1 1 
ATOM   50   C CE2 . PHE A 1 7   ? 31.355 -9.866  35.118  1.00 19.47 ? 7   PHE A CE2 1 
ATOM   51   C CZ  . PHE A 1 7   ? 31.858 -10.883 35.901  1.00 19.68 ? 7   PHE A CZ  1 
ATOM   52   N N   . GLY A 1 8   ? 27.157 -9.485  33.484  1.00 18.12 ? 8   GLY A N   1 
ATOM   53   C CA  . GLY A 1 8   ? 27.659 -9.689  32.139  1.00 17.62 ? 8   GLY A CA  1 
ATOM   54   C C   . GLY A 1 8   ? 28.610 -8.565  31.742  1.00 17.12 ? 8   GLY A C   1 
ATOM   55   O O   . GLY A 1 8   ? 28.799 -7.608  32.494  1.00 16.60 ? 8   GLY A O   1 
ATOM   56   N N   . LEU A 1 9   ? 29.210 -8.713  30.558  1.00 16.93 ? 9   LEU A N   1 
ATOM   57   C CA  . LEU A 1 9   ? 30.043 -7.681  29.967  1.00 16.82 ? 9   LEU A CA  1 
ATOM   58   C C   . LEU A 1 9   ? 29.527 -7.400  28.558  1.00 17.13 ? 9   LEU A C   1 
ATOM   59   O O   . LEU A 1 9   ? 29.107 -8.308  27.843  1.00 17.04 ? 9   LEU A O   1 
ATOM   60   C CB  . LEU A 1 9   ? 31.519 -8.083  29.943  1.00 16.43 ? 9   LEU A CB  1 
ATOM   61   C CG  . LEU A 1 9   ? 32.208 -8.302  31.296  1.00 16.26 ? 9   LEU A CG  1 
ATOM   62   C CD1 . LEU A 1 9   ? 33.679 -8.604  31.072  1.00 15.95 ? 9   LEU A CD1 1 
ATOM   63   C CD2 . LEU A 1 9   ? 32.073 -7.130  32.257  1.00 16.36 ? 9   LEU A CD2 1 
ATOM   64   N N   . LEU A 1 10  ? 29.564 -6.123  28.172  1.00 17.37 ? 10  LEU A N   1 
ATOM   65   C CA  . LEU A 1 10  ? 29.151 -5.711  26.844  1.00 17.97 ? 10  LEU A CA  1 
ATOM   66   C C   . LEU A 1 10  ? 30.396 -5.562  25.979  1.00 17.69 ? 10  LEU A C   1 
ATOM   67   O O   . LEU A 1 10  ? 31.295 -4.798  26.322  1.00 17.91 ? 10  LEU A O   1 
ATOM   68   C CB  . LEU A 1 10  ? 28.354 -4.411  26.934  1.00 18.53 ? 10  LEU A CB  1 
ATOM   69   C CG  . LEU A 1 10  ? 28.221 -3.599  25.640  1.00 19.40 ? 10  LEU A CG  1 
ATOM   70   C CD1 . LEU A 1 10  ? 27.458 -4.339  24.558  1.00 20.04 ? 10  LEU A CD1 1 
ATOM   71   C CD2 . LEU A 1 10  ? 27.553 -2.272  25.940  1.00 20.02 ? 10  LEU A CD2 1 
ATOM   72   N N   . LEU A 1 11  ? 30.442 -6.320  24.875  1.00 17.51 ? 11  LEU A N   1 
ATOM   73   C CA  . LEU A 1 11  ? 31.496 -6.180  23.886  1.00 17.77 ? 11  LEU A CA  1 
ATOM   74   C C   . LEU A 1 11  ? 30.950 -6.578  22.515  1.00 17.24 ? 11  LEU A C   1 
ATOM   75   O O   . LEU A 1 11  ? 30.492 -7.702  22.328  1.00 17.35 ? 11  LEU A O   1 
ATOM   76   C CB  . LEU A 1 11  ? 32.701 -7.033  24.287  1.00 17.88 ? 11  LEU A CB  1 
ATOM   77   C CG  . LEU A 1 11  ? 33.964 -6.856  23.438  1.00 18.19 ? 11  LEU A CG  1 
ATOM   78   C CD1 . LEU A 1 11  ? 34.602 -5.501  23.695  1.00 18.38 ? 11  LEU A CD1 1 
ATOM   79   C CD2 . LEU A 1 11  ? 34.962 -7.971  23.688  1.00 18.20 ? 11  LEU A CD2 1 
ATOM   80   N N   . HIS A 1 12  ? 30.998 -5.635  21.568  1.00 16.64 ? 12  HIS A N   1 
ATOM   81   C CA  . HIS A 1 12  ? 30.637 -5.895  20.184  1.00 15.85 ? 12  HIS A CA  1 
ATOM   82   C C   . HIS A 1 12  ? 31.811 -6.604  19.506  1.00 15.17 ? 12  HIS A C   1 
ATOM   83   O O   . HIS A 1 12  ? 32.964 -6.242  19.738  1.00 14.78 ? 12  HIS A O   1 
ATOM   84   C CB  . HIS A 1 12  ? 30.215 -4.584  19.509  1.00 15.85 ? 12  HIS A CB  1 
ATOM   85   C CG  . HIS A 1 12  ? 29.564 -4.755  18.180  1.00 16.16 ? 12  HIS A CG  1 
ATOM   86   N ND1 . HIS A 1 12  ? 30.052 -4.186  17.024  1.00 16.18 ? 12  HIS A ND1 1 
ATOM   87   C CD2 . HIS A 1 12  ? 28.432 -5.384  17.832  1.00 16.51 ? 12  HIS A CD2 1 
ATOM   88   C CE1 . HIS A 1 12  ? 29.247 -4.489  16.015  1.00 16.74 ? 12  HIS A CE1 1 
ATOM   89   N NE2 . HIS A 1 12  ? 28.259 -5.220  16.481  1.00 16.50 ? 12  HIS A NE2 1 
ATOM   90   N N   . PRO A 1 13  ? 31.562 -7.628  18.654  1.00 14.78 ? 13  PRO A N   1 
ATOM   91   C CA  . PRO A 1 13  ? 32.625 -8.462  18.100  1.00 14.76 ? 13  PRO A CA  1 
ATOM   92   C C   . PRO A 1 13  ? 33.703 -7.731  17.301  1.00 14.69 ? 13  PRO A C   1 
ATOM   93   O O   . PRO A 1 13  ? 34.796 -8.267  17.137  1.00 14.48 ? 13  PRO A O   1 
ATOM   94   C CB  . PRO A 1 13  ? 31.878 -9.437  17.190  1.00 14.76 ? 13  PRO A CB  1 
ATOM   95   C CG  . PRO A 1 13  ? 30.493 -9.480  17.802  1.00 14.69 ? 13  PRO A CG  1 
ATOM   96   C CD  . PRO A 1 13  ? 30.230 -8.077  18.216  1.00 14.69 ? 13  PRO A CD  1 
ATOM   97   N N   . THR A 1 14  ? 33.377 -6.538  16.783  1.00 14.77 ? 14  THR A N   1 
ATOM   98   C CA  . THR A 1 14  ? 34.313 -5.743  16.004  1.00 15.01 ? 14  THR A CA  1 
ATOM   99   C C   . THR A 1 14  ? 35.422 -5.227  16.915  1.00 15.62 ? 14  THR A C   1 
ATOM   100  O O   . THR A 1 14  ? 36.543 -5.035  16.457  1.00 16.37 ? 14  THR A O   1 
ATOM   101  C CB  . THR A 1 14  ? 33.602 -4.579  15.312  1.00 14.83 ? 14  THR A CB  1 
ATOM   102  O OG1 . THR A 1 14  ? 33.120 -3.725  16.346  1.00 14.33 ? 14  THR A OG1 1 
ATOM   103  C CG2 . THR A 1 14  ? 32.471 -5.026  14.404  1.00 14.89 ? 14  THR A CG2 1 
ATOM   104  N N   . SER A 1 15  ? 35.082 -5.004  18.195  1.00 16.00 ? 15  SER A N   1 
ATOM   105  C CA  . SER A 1 15  ? 36.009 -4.494  19.193  1.00 16.59 ? 15  SER A CA  1 
ATOM   106  C C   . SER A 1 15  ? 36.988 -5.575  19.661  1.00 17.62 ? 15  SER A C   1 
ATOM   107  O O   . SER A 1 15  ? 37.980 -5.264  20.320  1.00 18.57 ? 15  SER A O   1 
ATOM   108  C CB  . SER A 1 15  ? 35.265 -3.910  20.375  1.00 16.69 ? 15  SER A CB  1 
ATOM   109  O OG  . SER A 1 15  ? 34.435 -2.819  19.999  1.00 16.51 ? 15  SER A OG  1 
ATOM   110  N N   . LEU A 1 16  ? 36.707 -6.849  19.359  1.00 17.95 ? 16  LEU A N   1 
ATOM   111  C CA  . LEU A 1 16  ? 37.614 -7.925  19.736  1.00 18.24 ? 16  LEU A CA  1 
ATOM   112  C C   . LEU A 1 16  ? 39.002 -7.653  19.157  1.00 18.47 ? 16  LEU A C   1 
ATOM   113  O O   . LEU A 1 16  ? 39.127 -7.079  18.073  1.00 18.82 ? 16  LEU A O   1 
ATOM   114  C CB  . LEU A 1 16  ? 37.093 -9.288  19.280  1.00 18.17 ? 16  LEU A CB  1 
ATOM   115  C CG  . LEU A 1 16  ? 36.094 -9.983  20.211  1.00 17.80 ? 16  LEU A CG  1 
ATOM   116  C CD1 . LEU A 1 16  ? 35.257 -10.997 19.446  1.00 17.68 ? 16  LEU A CD1 1 
ATOM   117  C CD2 . LEU A 1 16  ? 36.816 -10.665 21.358  1.00 17.77 ? 16  LEU A CD2 1 
ATOM   118  N N   . PRO A 1 17  ? 40.086 -8.055  19.861  1.00 18.21 ? 17  PRO A N   1 
ATOM   119  C CA  . PRO A 1 17  ? 41.431 -7.948  19.313  1.00 18.19 ? 17  PRO A CA  1 
ATOM   120  C C   . PRO A 1 17  ? 41.684 -8.987  18.227  1.00 18.24 ? 17  PRO A C   1 
ATOM   121  O O   . PRO A 1 17  ? 40.961 -9.975  18.137  1.00 17.48 ? 17  PRO A O   1 
ATOM   122  C CB  . PRO A 1 17  ? 42.331 -8.156  20.526  1.00 18.14 ? 17  PRO A CB  1 
ATOM   123  C CG  . PRO A 1 17  ? 41.496 -9.058  21.415  1.00 18.07 ? 17  PRO A CG  1 
ATOM   124  C CD  . PRO A 1 17  ? 40.067 -8.640  21.211  1.00 18.14 ? 17  PRO A CD  1 
ATOM   125  N N   . GLY A 1 18  ? 42.698 -8.739  17.394  1.00 18.36 ? 18  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18  ? 43.139 -9.727  16.423  1.00 18.76 ? 18  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18  ? 43.592 -9.090  15.114  1.00 18.68 ? 18  GLY A C   1 
ATOM   128  O O   . GLY A 1 18  ? 43.392 -7.899  14.896  1.00 18.45 ? 18  GLY A O   1 
ATOM   129  N N   . PRO A 1 19  ? 44.175 -9.887  14.190  1.00 19.73 ? 19  PRO A N   1 
ATOM   130  C CA  . PRO A 1 19  ? 44.714 -9.363  12.941  1.00 20.46 ? 19  PRO A CA  1 
ATOM   131  C C   . PRO A 1 19  ? 43.641 -9.066  11.897  1.00 21.20 ? 19  PRO A C   1 
ATOM   132  O O   . PRO A 1 19  ? 42.483 -9.449  12.062  1.00 21.09 ? 19  PRO A O   1 
ATOM   133  C CB  . PRO A 1 19  ? 45.648 -10.480 12.487  1.00 19.93 ? 19  PRO A CB  1 
ATOM   134  C CG  . PRO A 1 19  ? 44.923 -11.726 12.977  1.00 19.96 ? 19  PRO A CG  1 
ATOM   135  C CD  . PRO A 1 19  ? 44.277 -11.353 14.279  1.00 19.87 ? 19  PRO A CD  1 
ATOM   136  N N   . TYR A 1 20  ? 44.054 -8.349  10.843  1.00 22.56 ? 20  TYR A N   1 
ATOM   137  C CA  . TYR A 1 20  ? 43.269 -8.128  9.636   1.00 23.91 ? 20  TYR A CA  1 
ATOM   138  C C   . TYR A 1 20  ? 42.218 -7.039  9.845   1.00 23.39 ? 20  TYR A C   1 
ATOM   139  O O   . TYR A 1 20  ? 41.302 -6.913  9.035   1.00 24.37 ? 20  TYR A O   1 
ATOM   140  C CB  . TYR A 1 20  ? 42.714 -9.462  9.123   1.00 24.91 ? 20  TYR A CB  1 
ATOM   141  C CG  . TYR A 1 20  ? 43.822 -10.420 8.708   1.00 26.08 ? 20  TYR A CG  1 
ATOM   142  C CD1 . TYR A 1 20  ? 44.952 -9.951  8.047   1.00 27.46 ? 20  TYR A CD1 1 
ATOM   143  C CD2 . TYR A 1 20  ? 43.755 -11.781 8.987   1.00 27.59 ? 20  TYR A CD2 1 
ATOM   144  C CE1 . TYR A 1 20  ? 45.975 -10.801 7.666   1.00 27.28 ? 20  TYR A CE1 1 
ATOM   145  C CE2 . TYR A 1 20  ? 44.772 -12.644 8.609   1.00 28.03 ? 20  TYR A CE2 1 
ATOM   146  C CZ  . TYR A 1 20  ? 45.886 -12.149 7.951   1.00 28.42 ? 20  TYR A CZ  1 
ATOM   147  O OH  . TYR A 1 20  ? 46.912 -12.956 7.554   1.00 29.40 ? 20  TYR A OH  1 
ATOM   148  N N   . GLY A 1 21  ? 42.377 -6.240  10.908  1.00 22.49 ? 21  GLY A N   1 
ATOM   149  C CA  . GLY A 1 21  ? 41.775 -4.917  10.974  1.00 21.41 ? 21  GLY A CA  1 
ATOM   150  C C   . GLY A 1 21  ? 40.405 -4.896  11.648  1.00 20.21 ? 21  GLY A C   1 
ATOM   151  O O   . GLY A 1 21  ? 39.810 -3.828  11.778  1.00 20.62 ? 21  GLY A O   1 
ATOM   152  N N   . VAL A 1 22  ? 39.912 -6.058  12.090  1.00 19.01 ? 22  VAL A N   1 
ATOM   153  C CA  . VAL A 1 22  ? 38.624 -6.126  12.759  1.00 18.21 ? 22  VAL A CA  1 
ATOM   154  C C   . VAL A 1 22  ? 38.583 -7.386  13.620  1.00 17.83 ? 22  VAL A C   1 
ATOM   155  O O   . VAL A 1 22  ? 39.255 -8.370  13.319  1.00 17.50 ? 22  VAL A O   1 
ATOM   156  C CB  . VAL A 1 22  ? 37.472 -6.097  11.734  1.00 17.76 ? 22  VAL A CB  1 
ATOM   157  C CG1 . VAL A 1 22  ? 37.416 -7.370  10.898  1.00 17.65 ? 22  VAL A CG1 1 
ATOM   158  C CG2 . VAL A 1 22  ? 36.122 -5.828  12.390  1.00 17.86 ? 22  VAL A CG2 1 
ATOM   159  N N   . GLY A 1 23  ? 37.790 -7.336  14.696  1.00 16.95 ? 23  GLY A N   1 
ATOM   160  C CA  . GLY A 1 23  ? 37.498 -8.521  15.482  1.00 16.71 ? 23  GLY A CA  1 
ATOM   161  C C   . GLY A 1 23  ? 36.540 -9.434  14.722  1.00 16.35 ? 23  GLY A C   1 
ATOM   162  O O   . GLY A 1 23  ? 35.579 -8.956  14.117  1.00 16.83 ? 23  GLY A O   1 
ATOM   163  N N   . VAL A 1 24  ? 36.829 -10.739 14.757  1.00 15.61 ? 24  VAL A N   1 
ATOM   164  C CA  . VAL A 1 24  ? 36.117 -11.729 13.966  1.00 15.46 ? 24  VAL A CA  1 
ATOM   165  C C   . VAL A 1 24  ? 35.640 -12.843 14.896  1.00 15.20 ? 24  VAL A C   1 
ATOM   166  O O   . VAL A 1 24  ? 35.940 -12.825 16.089  1.00 15.08 ? 24  VAL A O   1 
ATOM   167  C CB  . VAL A 1 24  ? 36.998 -12.273 12.821  1.00 15.36 ? 24  VAL A CB  1 
ATOM   168  C CG1 . VAL A 1 24  ? 37.337 -11.194 11.801  1.00 15.38 ? 24  VAL A CG1 1 
ATOM   169  C CG2 . VAL A 1 24  ? 38.277 -12.932 13.328  1.00 15.38 ? 24  VAL A CG2 1 
ATOM   170  N N   . LEU A 1 25  ? 34.898 -13.804 14.332  1.00 15.15 ? 25  LEU A N   1 
ATOM   171  C CA  . LEU A 1 25  ? 34.319 -14.902 15.090  1.00 15.19 ? 25  LEU A CA  1 
ATOM   172  C C   . LEU A 1 25  ? 35.320 -16.054 15.170  1.00 15.52 ? 25  LEU A C   1 
ATOM   173  O O   . LEU A 1 25  ? 35.050 -17.151 14.681  1.00 15.98 ? 25  LEU A O   1 
ATOM   174  C CB  . LEU A 1 25  ? 33.015 -15.337 14.421  1.00 15.07 ? 25  LEU A CB  1 
ATOM   175  C CG  . LEU A 1 25  ? 32.000 -14.228 14.118  1.00 15.17 ? 25  LEU A CG  1 
ATOM   176  C CD1 . LEU A 1 25  ? 30.751 -14.837 13.508  1.00 15.24 ? 25  LEU A CD1 1 
ATOM   177  C CD2 . LEU A 1 25  ? 31.649 -13.410 15.353  1.00 14.95 ? 25  LEU A CD2 1 
ATOM   178  N N   . GLY A 1 26  ? 36.463 -15.801 15.817  1.00 15.63 ? 26  GLY A N   1 
ATOM   179  C CA  . GLY A 1 26  ? 37.571 -16.743 15.826  1.00 15.98 ? 26  GLY A CA  1 
ATOM   180  C C   . GLY A 1 26  ? 38.080 -17.030 17.235  1.00 16.14 ? 26  GLY A C   1 
ATOM   181  O O   . GLY A 1 26  ? 37.311 -17.079 18.195  1.00 15.75 ? 26  GLY A O   1 
ATOM   182  N N   . GLN A 1 27  ? 39.396 -17.238 17.334  1.00 16.73 ? 27  GLN A N   1 
ATOM   183  C CA  . GLN A 1 27  ? 40.019 -17.701 18.563  1.00 17.89 ? 27  GLN A CA  1 
ATOM   184  C C   . GLN A 1 27  ? 39.916 -16.628 19.648  1.00 17.00 ? 27  GLN A C   1 
ATOM   185  O O   . GLN A 1 27  ? 39.723 -16.953 20.817  1.00 16.43 ? 27  GLN A O   1 
ATOM   186  C CB  . GLN A 1 27  ? 41.457 -18.134 18.271  1.00 19.15 ? 27  GLN A CB  1 
ATOM   187  C CG  . GLN A 1 27  ? 42.340 -17.011 17.739  1.00 20.86 ? 27  GLN A CG  1 
ATOM   188  C CD  . GLN A 1 27  ? 43.409 -17.497 16.786  1.00 22.71 ? 27  GLN A CD  1 
ATOM   189  O OE1 . GLN A 1 27  ? 43.113 -18.006 15.698  1.00 24.37 ? 27  GLN A OE1 1 
ATOM   190  N NE2 . GLN A 1 27  ? 44.665 -17.339 17.184  1.00 23.08 ? 27  GLN A NE2 1 
ATOM   191  N N   . GLU A 1 28  ? 40.001 -15.352 19.257  1.00 17.43 ? 28  GLU A N   1 
ATOM   192  C CA  . GLU A 1 28  ? 40.001 -14.265 20.227  1.00 17.85 ? 28  GLU A CA  1 
ATOM   193  C C   . GLU A 1 28  ? 38.634 -14.171 20.909  1.00 18.08 ? 28  GLU A C   1 
ATOM   194  O O   . GLU A 1 28  ? 38.547 -13.789 22.074  1.00 18.22 ? 28  GLU A O   1 
ATOM   195  C CB  . GLU A 1 28  ? 40.401 -12.931 19.597  1.00 17.69 ? 28  GLU A CB  1 
ATOM   196  C CG  . GLU A 1 28  ? 41.809 -12.932 19.007  1.00 17.90 ? 28  GLU A CG  1 
ATOM   197  C CD  . GLU A 1 28  ? 41.910 -13.396 17.564  1.00 18.03 ? 28  GLU A CD  1 
ATOM   198  O OE1 . GLU A 1 28  ? 40.854 -13.697 16.962  1.00 18.51 ? 28  GLU A OE1 1 
ATOM   199  O OE2 . GLU A 1 28  ? 43.042 -13.463 17.043  1.00 17.40 ? 28  GLU A OE2 1 
ATOM   200  N N   . ALA A 1 29  ? 37.575 -14.541 20.181  1.00 18.35 ? 29  ALA A N   1 
ATOM   201  C CA  . ALA A 1 29  ? 36.222 -14.505 20.712  1.00 18.35 ? 29  ALA A CA  1 
ATOM   202  C C   . ALA A 1 29  ? 36.044 -15.594 21.767  1.00 18.72 ? 29  ALA A C   1 
ATOM   203  O O   . ALA A 1 29  ? 35.431 -15.356 22.805  1.00 17.75 ? 29  ALA A O   1 
ATOM   204  C CB  . ALA A 1 29  ? 35.224 -14.647 19.586  1.00 18.65 ? 29  ALA A CB  1 
ATOM   205  N N   . ARG A 1 30  ? 36.607 -16.778 21.497  1.00 19.51 ? 30  ARG A N   1 
ATOM   206  C CA  . ARG A 1 30  ? 36.621 -17.868 22.461  1.00 20.31 ? 30  ARG A CA  1 
ATOM   207  C C   . ARG A 1 30  ? 37.411 -17.451 23.704  1.00 20.25 ? 30  ARG A C   1 
ATOM   208  O O   . ARG A 1 30  ? 37.013 -17.755 24.827  1.00 20.01 ? 30  ARG A O   1 
ATOM   209  C CB  . ARG A 1 30  ? 37.198 -19.142 21.831  1.00 21.24 ? 30  ARG A CB  1 
ATOM   210  C CG  . ARG A 1 30  ? 36.508 -19.623 20.560  1.00 22.05 ? 30  ARG A CG  1 
ATOM   211  C CD  . ARG A 1 30  ? 37.152 -20.881 19.975  1.00 23.48 ? 30  ARG A CD  1 
ATOM   212  N NE  . ARG A 1 30  ? 37.059 -20.920 18.509  1.00 24.74 ? 30  ARG A NE  1 
ATOM   213  C CZ  . ARG A 1 30  ? 38.085 -21.044 17.664  1.00 26.07 ? 30  ARG A CZ  1 
ATOM   214  N NH1 . ARG A 1 30  ? 39.303 -21.303 18.114  1.00 26.26 ? 30  ARG A NH1 1 
ATOM   215  N NH2 . ARG A 1 30  ? 37.888 -20.925 16.361  1.00 26.06 ? 30  ARG A NH2 1 
ATOM   216  N N   . ASP A 1 31  ? 38.538 -16.760 23.488  1.00 20.68 ? 31  ASP A N   1 
ATOM   217  C CA  . ASP A 1 31  ? 39.366 -16.242 24.566  1.00 20.33 ? 31  ASP A CA  1 
ATOM   218  C C   . ASP A 1 31  ? 38.555 -15.292 25.445  1.00 19.80 ? 31  ASP A C   1 
ATOM   219  O O   . ASP A 1 31  ? 38.611 -15.379 26.670  1.00 19.48 ? 31  ASP A O   1 
ATOM   220  C CB  . ASP A 1 31  ? 40.612 -15.558 24.022  1.00 20.75 ? 31  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 31  ? 41.656 -16.483 23.410  1.00 21.22 ? 31  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 31  ? 41.543 -17.713 23.599  1.00 21.21 ? 31  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 31  ? 42.570 -15.967 22.741  1.00 21.68 ? 31  ASP A OD2 1 
ATOM   224  N N   . PHE A 1 32  ? 37.800 -14.385 24.815  1.00 19.13 ? 32  PHE A N   1 
ATOM   225  C CA  . PHE A 1 32  ? 36.969 -13.452 25.558  1.00 18.44 ? 32  PHE A CA  1 
ATOM   226  C C   . PHE A 1 32  ? 35.969 -14.239 26.402  1.00 18.49 ? 32  PHE A C   1 
ATOM   227  O O   . PHE A 1 32  ? 35.807 -13.940 27.586  1.00 17.55 ? 32  PHE A O   1 
ATOM   228  C CB  . PHE A 1 32  ? 36.265 -12.434 24.655  1.00 18.39 ? 32  PHE A CB  1 
ATOM   229  C CG  . PHE A 1 32  ? 35.290 -11.537 25.407  1.00 18.64 ? 32  PHE A CG  1 
ATOM   230  C CD1 . PHE A 1 32  ? 35.750 -10.483 26.191  1.00 18.57 ? 32  PHE A CD1 1 
ATOM   231  C CD2 . PHE A 1 32  ? 33.919 -11.760 25.345  1.00 19.52 ? 32  PHE A CD2 1 
ATOM   232  C CE1 . PHE A 1 32  ? 34.865 -9.679  26.891  1.00 19.11 ? 32  PHE A CE1 1 
ATOM   233  C CE2 . PHE A 1 32  ? 33.036 -10.946 26.042  1.00 19.51 ? 32  PHE A CE2 1 
ATOM   234  C CZ  . PHE A 1 32  ? 33.510 -9.906  26.810  1.00 19.42 ? 32  PHE A CZ  1 
ATOM   235  N N   . LEU A 1 33  ? 35.321 -15.249 25.796  1.00 18.64 ? 33  LEU A N   1 
ATOM   236  C CA  . LEU A 1 33  ? 34.323 -16.054 26.488  1.00 19.95 ? 33  LEU A CA  1 
ATOM   237  C C   . LEU A 1 33  ? 34.948 -16.735 27.704  1.00 20.62 ? 33  LEU A C   1 
ATOM   238  O O   . LEU A 1 33  ? 34.301 -16.860 28.745  1.00 19.91 ? 33  LEU A O   1 
ATOM   239  C CB  . LEU A 1 33  ? 33.679 -17.097 25.573  1.00 20.42 ? 33  LEU A CB  1 
ATOM   240  C CG  . LEU A 1 33  ? 32.826 -16.578 24.412  1.00 20.23 ? 33  LEU A CG  1 
ATOM   241  C CD1 . LEU A 1 33  ? 32.274 -17.760 23.635  1.00 20.29 ? 33  LEU A CD1 1 
ATOM   242  C CD2 . LEU A 1 33  ? 31.697 -15.671 24.861  1.00 20.52 ? 33  LEU A CD2 1 
ATOM   243  N N   . ARG A 1 34  ? 36.197 -17.196 27.553  1.00 22.01 ? 34  ARG A N   1 
ATOM   244  C CA  . ARG A 1 34  ? 36.909 -17.843 28.644  1.00 22.82 ? 34  ARG A CA  1 
ATOM   245  C C   . ARG A 1 34  ? 37.113 -16.839 29.774  1.00 21.65 ? 34  ARG A C   1 
ATOM   246  O O   . ARG A 1 34  ? 36.830 -17.150 30.925  1.00 21.53 ? 34  ARG A O   1 
ATOM   247  C CB  . ARG A 1 34  ? 38.223 -18.468 28.159  1.00 24.77 ? 34  ARG A CB  1 
ATOM   248  C CG  . ARG A 1 34  ? 38.019 -19.795 27.440  1.00 26.92 ? 34  ARG A CG  1 
ATOM   249  C CD  . ARG A 1 34  ? 39.285 -20.361 26.807  1.00 28.73 ? 34  ARG A CD  1 
ATOM   250  N NE  . ARG A 1 34  ? 40.416 -20.449 27.741  1.00 30.04 ? 34  ARG A NE  1 
ATOM   251  C CZ  . ARG A 1 34  ? 40.977 -21.565 28.198  1.00 30.78 ? 34  ARG A CZ  1 
ATOM   252  N NH1 . ARG A 1 34  ? 42.057 -21.496 28.959  1.00 32.51 ? 34  ARG A NH1 1 
ATOM   253  N NH2 . ARG A 1 34  ? 40.475 -22.747 27.888  1.00 30.61 ? 34  ARG A NH2 1 
ATOM   254  N N   . PHE A 1 35  ? 37.584 -15.635 29.427  1.00 21.82 ? 35  PHE A N   1 
ATOM   255  C CA  . PHE A 1 35  ? 37.798 -14.568 30.395  1.00 21.35 ? 35  PHE A CA  1 
ATOM   256  C C   . PHE A 1 35  ? 36.493 -14.264 31.127  1.00 21.04 ? 35  PHE A C   1 
ATOM   257  O O   . PHE A 1 35  ? 36.470 -14.164 32.356  1.00 19.41 ? 35  PHE A O   1 
ATOM   258  C CB  . PHE A 1 35  ? 38.344 -13.308 29.712  1.00 21.66 ? 35  PHE A CB  1 
ATOM   259  C CG  . PHE A 1 35  ? 38.319 -12.072 30.601  1.00 22.09 ? 35  PHE A CG  1 
ATOM   260  C CD1 . PHE A 1 35  ? 37.208 -11.232 30.625  1.00 21.90 ? 35  PHE A CD1 1 
ATOM   261  C CD2 . PHE A 1 35  ? 39.394 -11.767 31.431  1.00 22.16 ? 35  PHE A CD2 1 
ATOM   262  C CE1 . PHE A 1 35  ? 37.179 -10.120 31.453  1.00 21.91 ? 35  PHE A CE1 1 
ATOM   263  C CE2 . PHE A 1 35  ? 39.362 -10.647 32.250  1.00 22.09 ? 35  PHE A CE2 1 
ATOM   264  C CZ  . PHE A 1 35  ? 38.257 -9.826  32.257  1.00 22.04 ? 35  PHE A CZ  1 
ATOM   265  N N   . LEU A 1 36  ? 35.410 -14.119 30.352  1.00 20.50 ? 36  LEU A N   1 
ATOM   266  C CA  . LEU A 1 36  ? 34.092 -13.850 30.906  1.00 20.53 ? 36  LEU A CA  1 
ATOM   267  C C   . LEU A 1 36  ? 33.685 -14.967 31.864  1.00 20.93 ? 36  LEU A C   1 
ATOM   268  O O   . LEU A 1 36  ? 33.116 -14.690 32.917  1.00 20.96 ? 36  LEU A O   1 
ATOM   269  C CB  . LEU A 1 36  ? 33.083 -13.689 29.770  1.00 20.47 ? 36  LEU A CB  1 
ATOM   270  C CG  . LEU A 1 36  ? 31.672 -13.253 30.176  1.00 20.50 ? 36  LEU A CG  1 
ATOM   271  C CD1 . LEU A 1 36  ? 31.670 -11.952 30.957  1.00 20.22 ? 36  LEU A CD1 1 
ATOM   272  C CD2 . LEU A 1 36  ? 30.805 -13.134 28.936  1.00 20.95 ? 36  LEU A CD2 1 
ATOM   273  N N   . LYS A 1 37  ? 33.970 -16.217 31.470  1.00 21.87 ? 37  LYS A N   1 
ATOM   274  C CA  . LYS A 1 37  ? 33.678 -17.397 32.270  1.00 23.06 ? 37  LYS A CA  1 
ATOM   275  C C   . LYS A 1 37  ? 34.511 -17.391 33.550  1.00 23.79 ? 37  LYS A C   1 
ATOM   276  O O   . LYS A 1 37  ? 33.972 -17.601 34.634  1.00 23.99 ? 37  LYS A O   1 
ATOM   277  C CB  . LYS A 1 37  ? 33.937 -18.663 31.443  1.00 23.34 ? 37  LYS A CB  1 
ATOM   278  C CG  . LYS A 1 37  ? 34.312 -19.929 32.203  1.00 24.28 ? 37  LYS A CG  1 
ATOM   279  C CD  . LYS A 1 37  ? 33.193 -20.582 33.004  1.00 24.61 ? 37  LYS A CD  1 
ATOM   280  C CE  . LYS A 1 37  ? 33.531 -21.998 33.354  1.00 25.52 ? 37  LYS A CE  1 
ATOM   281  N NZ  . LYS A 1 37  ? 34.846 -22.148 33.987  1.00 25.43 ? 37  LYS A NZ  1 
ATOM   282  N N   . GLU A 1 38  ? 35.822 -17.151 33.405  1.00 24.61 ? 38  GLU A N   1 
ATOM   283  C CA  . GLU A 1 38  ? 36.759 -17.164 34.520  1.00 24.97 ? 38  GLU A CA  1 
ATOM   284  C C   . GLU A 1 38  ? 36.458 -16.033 35.502  1.00 24.37 ? 38  GLU A C   1 
ATOM   285  O O   . GLU A 1 38  ? 36.680 -16.192 36.700  1.00 24.45 ? 38  GLU A O   1 
ATOM   286  C CB  . GLU A 1 38  ? 38.197 -17.085 34.008  1.00 26.47 ? 38  GLU A CB  1 
ATOM   287  C CG  . GLU A 1 38  ? 38.629 -18.360 33.287  1.00 28.51 ? 38  GLU A CG  1 
ATOM   288  C CD  . GLU A 1 38  ? 39.964 -18.306 32.569  1.00 30.26 ? 38  GLU A CD  1 
ATOM   289  O OE1 . GLU A 1 38  ? 40.757 -17.368 32.800  1.00 31.61 ? 38  GLU A OE1 1 
ATOM   290  O OE2 . GLU A 1 38  ? 40.200 -19.220 31.752  1.00 33.09 ? 38  GLU A OE2 1 
ATOM   291  N N   . ALA A 1 39  ? 35.959 -14.902 34.984  1.00 23.83 ? 39  ALA A N   1 
ATOM   292  C CA  . ALA A 1 39  ? 35.604 -13.749 35.797  1.00 23.54 ? 39  ALA A CA  1 
ATOM   293  C C   . ALA A 1 39  ? 34.273 -13.974 36.514  1.00 23.05 ? 39  ALA A C   1 
ATOM   294  O O   . ALA A 1 39  ? 33.878 -13.162 37.350  1.00 22.45 ? 39  ALA A O   1 
ATOM   295  C CB  . ALA A 1 39  ? 35.547 -12.514 34.929  1.00 23.54 ? 39  ALA A CB  1 
ATOM   296  N N   . GLY A 1 40  ? 33.576 -15.058 36.150  1.00 23.52 ? 40  GLY A N   1 
ATOM   297  C CA  . GLY A 1 40  ? 32.336 -15.451 36.798  1.00 23.43 ? 40  GLY A CA  1 
ATOM   298  C C   . GLY A 1 40  ? 31.115 -14.799 36.153  1.00 23.21 ? 40  GLY A C   1 
ATOM   299  O O   . GLY A 1 40  ? 30.013 -14.912 36.684  1.00 22.48 ? 40  GLY A O   1 
ATOM   300  N N   . GLY A 1 41  ? 31.313 -14.122 35.013  1.00 22.90 ? 41  GLY A N   1 
ATOM   301  C CA  . GLY A 1 41  ? 30.209 -13.530 34.276  1.00 23.32 ? 41  GLY A CA  1 
ATOM   302  C C   . GLY A 1 41  ? 29.408 -14.609 33.552  1.00 23.38 ? 41  GLY A C   1 
ATOM   303  O O   . GLY A 1 41  ? 29.960 -15.647 33.194  1.00 23.38 ? 41  GLY A O   1 
ATOM   304  N N   . GLN A 1 42  ? 28.107 -14.363 33.355  1.00 23.66 ? 42  GLN A N   1 
ATOM   305  C CA  . GLN A 1 42  ? 27.227 -15.337 32.723  1.00 24.29 ? 42  GLN A CA  1 
ATOM   306  C C   . GLN A 1 42  ? 26.520 -14.746 31.503  1.00 24.09 ? 42  GLN A C   1 
ATOM   307  O O   . GLN A 1 42  ? 25.708 -15.437 30.886  1.00 24.70 ? 42  GLN A O   1 
ATOM   308  C CB  . GLN A 1 42  ? 26.207 -15.867 33.734  1.00 24.86 ? 42  GLN A CB  1 
ATOM   309  C CG  . GLN A 1 42  ? 26.799 -16.821 34.767  1.00 25.95 ? 42  GLN A CG  1 
ATOM   310  C CD  . GLN A 1 42  ? 25.857 -17.130 35.912  1.00 26.45 ? 42  GLN A CD  1 
ATOM   311  O OE1 . GLN A 1 42  ? 25.558 -16.268 36.746  1.00 27.26 ? 42  GLN A OE1 1 
ATOM   312  N NE2 . GLN A 1 42  ? 25.400 -18.372 35.986  1.00 26.85 ? 42  GLN A NE2 1 
ATOM   313  N N   . TYR A 1 43  ? 26.827 -13.488 31.145  1.00 22.95 ? 43  TYR A N   1 
ATOM   314  C CA  . TYR A 1 43  ? 26.137 -12.831 30.046  1.00 22.49 ? 43  TYR A CA  1 
ATOM   315  C C   . TYR A 1 43  ? 27.108 -12.034 29.178  1.00 20.99 ? 43  TYR A C   1 
ATOM   316  O O   . TYR A 1 43  ? 27.929 -11.273 29.682  1.00 20.62 ? 43  TYR A O   1 
ATOM   317  C CB  . TYR A 1 43  ? 25.012 -11.944 30.590  1.00 23.33 ? 43  TYR A CB  1 
ATOM   318  C CG  . TYR A 1 43  ? 23.747 -12.717 30.937  1.00 24.44 ? 43  TYR A CG  1 
ATOM   319  C CD1 . TYR A 1 43  ? 23.564 -13.261 32.202  1.00 25.77 ? 43  TYR A CD1 1 
ATOM   320  C CD2 . TYR A 1 43  ? 22.746 -12.917 29.995  1.00 25.25 ? 43  TYR A CD2 1 
ATOM   321  C CE1 . TYR A 1 43  ? 22.421 -13.975 32.525  1.00 26.45 ? 43  TYR A CE1 1 
ATOM   322  C CE2 . TYR A 1 43  ? 21.595 -13.625 30.306  1.00 25.54 ? 43  TYR A CE2 1 
ATOM   323  C CZ  . TYR A 1 43  ? 21.433 -14.156 31.574  1.00 26.17 ? 43  TYR A CZ  1 
ATOM   324  O OH  . TYR A 1 43  ? 20.313 -14.859 31.903  1.00 27.58 ? 43  TYR A OH  1 
ATOM   325  N N   . TRP A 1 44  ? 26.973 -12.206 27.858  1.00 20.47 ? 44  TRP A N   1 
ATOM   326  C CA  . TRP A 1 44  ? 27.691 -11.405 26.878  1.00 19.75 ? 44  TRP A CA  1 
ATOM   327  C C   . TRP A 1 44  ? 26.688 -10.619 26.038  1.00 19.13 ? 44  TRP A C   1 
ATOM   328  O O   . TRP A 1 44  ? 25.777 -11.199 25.450  1.00 17.80 ? 44  TRP A O   1 
ATOM   329  C CB  . TRP A 1 44  ? 28.568 -12.298 25.991  1.00 20.18 ? 44  TRP A CB  1 
ATOM   330  C CG  . TRP A 1 44  ? 29.347 -11.545 24.942  1.00 21.05 ? 44  TRP A CG  1 
ATOM   331  C CD1 . TRP A 1 44  ? 29.847 -10.280 25.041  1.00 21.36 ? 44  TRP A CD1 1 
ATOM   332  C CD2 . TRP A 1 44  ? 29.719 -12.020 23.628  1.00 21.78 ? 44  TRP A CD2 1 
ATOM   333  N NE1 . TRP A 1 44  ? 30.504 -9.934  23.890  1.00 21.51 ? 44  TRP A NE1 1 
ATOM   334  C CE2 . TRP A 1 44  ? 30.442 -10.978 23.005  1.00 21.94 ? 44  TRP A CE2 1 
ATOM   335  C CE3 . TRP A 1 44  ? 29.513 -13.211 22.921  1.00 22.35 ? 44  TRP A CE3 1 
ATOM   336  C CZ2 . TRP A 1 44  ? 30.955 -11.098 21.715  1.00 22.77 ? 44  TRP A CZ2 1 
ATOM   337  C CZ3 . TRP A 1 44  ? 30.012 -13.325 21.641  1.00 22.18 ? 44  TRP A CZ3 1 
ATOM   338  C CH2 . TRP A 1 44  ? 30.726 -12.282 21.049  1.00 22.94 ? 44  TRP A CH2 1 
ATOM   339  N N   . GLN A 1 45  ? 26.859 -9.295  25.993  1.00 19.04 ? 45  GLN A N   1 
ATOM   340  C CA  . GLN A 1 45  ? 25.960 -8.442  25.235  1.00 19.05 ? 45  GLN A CA  1 
ATOM   341  C C   . GLN A 1 45  ? 26.678 -7.924  23.993  1.00 18.25 ? 45  GLN A C   1 
ATOM   342  O O   . GLN A 1 45  ? 27.843 -7.527  24.064  1.00 17.53 ? 45  GLN A O   1 
ATOM   343  C CB  . GLN A 1 45  ? 25.405 -7.303  26.087  1.00 19.97 ? 45  GLN A CB  1 
ATOM   344  C CG  . GLN A 1 45  ? 24.382 -6.439  25.355  1.00 20.91 ? 45  GLN A CG  1 
ATOM   345  C CD  . GLN A 1 45  ? 23.398 -5.745  26.274  1.00 21.99 ? 45  GLN A CD  1 
ATOM   346  O OE1 . GLN A 1 45  ? 23.295 -6.039  27.470  1.00 23.48 ? 45  GLN A OE1 1 
ATOM   347  N NE2 . GLN A 1 45  ? 22.637 -4.824  25.710  1.00 23.19 ? 45  GLN A NE2 1 
ATOM   348  N N   . VAL A 1 46  ? 25.948 -7.928  22.870  1.00 17.09 ? 46  VAL A N   1 
ATOM   349  C CA  . VAL A 1 46  ? 26.453 -7.452  21.594  1.00 17.15 ? 46  VAL A CA  1 
ATOM   350  C C   . VAL A 1 46  ? 25.463 -6.436  21.026  1.00 17.02 ? 46  VAL A C   1 
ATOM   351  O O   . VAL A 1 46  ? 24.282 -6.454  21.361  1.00 17.95 ? 46  VAL A O   1 
ATOM   352  C CB  . VAL A 1 46  ? 26.698 -8.618  20.613  1.00 16.79 ? 46  VAL A CB  1 
ATOM   353  C CG1 . VAL A 1 46  ? 27.928 -9.436  20.993  1.00 17.10 ? 46  VAL A CG1 1 
ATOM   354  C CG2 . VAL A 1 46  ? 25.482 -9.530  20.478  1.00 16.20 ? 46  VAL A CG2 1 
ATOM   355  N N   . LEU A 1 47  ? 25.970 -5.540  20.175  1.00 16.74 ? 47  LEU A N   1 
ATOM   356  C CA  . LEU A 1 47  ? 25.141 -4.632  19.397  1.00 17.11 ? 47  LEU A CA  1 
ATOM   357  C C   . LEU A 1 47  ? 24.714 -5.357  18.118  1.00 17.35 ? 47  LEU A C   1 
ATOM   358  O O   . LEU A 1 47  ? 25.181 -6.468  17.857  1.00 17.25 ? 47  LEU A O   1 
ATOM   359  C CB  . LEU A 1 47  ? 25.920 -3.348  19.111  1.00 17.09 ? 47  LEU A CB  1 
ATOM   360  C CG  . LEU A 1 47  ? 26.657 -2.703  20.291  1.00 17.14 ? 47  LEU A CG  1 
ATOM   361  C CD1 . LEU A 1 47  ? 27.281 -1.392  19.833  1.00 17.30 ? 47  LEU A CD1 1 
ATOM   362  C CD2 . LEU A 1 47  ? 25.761 -2.467  21.498  1.00 17.40 ? 47  LEU A CD2 1 
ATOM   363  N N   . PRO A 1 48  ? 23.810 -4.786  17.285  1.00 17.49 ? 48  PRO A N   1 
ATOM   364  C CA  . PRO A 1 48  ? 23.305 -5.499  16.115  1.00 17.81 ? 48  PRO A CA  1 
ATOM   365  C C   . PRO A 1 48  ? 24.417 -6.040  15.220  1.00 17.63 ? 48  PRO A C   1 
ATOM   366  O O   . PRO A 1 48  ? 25.486 -5.442  15.123  1.00 16.69 ? 48  PRO A O   1 
ATOM   367  C CB  . PRO A 1 48  ? 22.420 -4.469  15.410  1.00 17.86 ? 48  PRO A CB  1 
ATOM   368  C CG  . PRO A 1 48  ? 22.039 -3.506  16.527  1.00 17.71 ? 48  PRO A CG  1 
ATOM   369  C CD  . PRO A 1 48  ? 23.238 -3.435  17.415  1.00 17.66 ? 48  PRO A CD  1 
ATOM   370  N N   . LEU A 1 49  ? 24.149 -7.182  14.574  1.00 17.97 ? 49  LEU A N   1 
ATOM   371  C CA  . LEU A 1 49  ? 25.181 -7.933  13.878  1.00 18.79 ? 49  LEU A CA  1 
ATOM   372  C C   . LEU A 1 49  ? 24.934 -7.943  12.373  1.00 19.10 ? 49  LEU A C   1 
ATOM   373  O O   . LEU A 1 49  ? 25.483 -8.794  11.676  1.00 18.69 ? 49  LEU A O   1 
ATOM   374  C CB  . LEU A 1 49  ? 25.216 -9.360  14.418  1.00 19.18 ? 49  LEU A CB  1 
ATOM   375  C CG  . LEU A 1 49  ? 25.614 -9.528  15.885  1.00 19.32 ? 49  LEU A CG  1 
ATOM   376  C CD1 . LEU A 1 49  ? 25.644 -11.016 16.198  1.00 19.50 ? 49  LEU A CD1 1 
ATOM   377  C CD2 . LEU A 1 49  ? 26.954 -8.879  16.204  1.00 19.54 ? 49  LEU A CD2 1 
ATOM   378  N N   . GLY A 1 50  ? 24.135 -6.988  11.879  1.00 19.06 ? 50  GLY A N   1 
ATOM   379  C CA  . GLY A 1 50  ? 23.792 -6.929  10.468  1.00 19.34 ? 50  GLY A CA  1 
ATOM   380  C C   . GLY A 1 50  ? 24.852 -6.201  9.644   1.00 19.80 ? 50  GLY A C   1 
ATOM   381  O O   . GLY A 1 50  ? 25.741 -5.555  10.198  1.00 19.97 ? 50  GLY A O   1 
ATOM   382  N N   . PRO A 1 51  ? 24.798 -6.311  8.294   1.00 20.25 ? 51  PRO A N   1 
ATOM   383  C CA  . PRO A 1 51  ? 25.727 -5.608  7.412   1.00 20.50 ? 51  PRO A CA  1 
ATOM   384  C C   . PRO A 1 51  ? 25.573 -4.088  7.419   1.00 20.55 ? 51  PRO A C   1 
ATOM   385  O O   . PRO A 1 51  ? 24.458 -3.581  7.304   1.00 19.50 ? 51  PRO A O   1 
ATOM   386  C CB  . PRO A 1 51  ? 25.422 -6.183  6.031   1.00 20.56 ? 51  PRO A CB  1 
ATOM   387  C CG  . PRO A 1 51  ? 24.001 -6.700  6.151   1.00 20.64 ? 51  PRO A CG  1 
ATOM   388  C CD  . PRO A 1 51  ? 23.857 -7.174  7.562   1.00 20.57 ? 51  PRO A CD  1 
ATOM   389  N N   . THR A 1 52  ? 26.715 -3.385  7.497   1.00 20.78 ? 52  THR A N   1 
ATOM   390  C CA  . THR A 1 52  ? 26.762 -1.948  7.735   1.00 22.17 ? 52  THR A CA  1 
ATOM   391  C C   . THR A 1 52  ? 26.965 -1.185  6.426   1.00 22.76 ? 52  THR A C   1 
ATOM   392  O O   . THR A 1 52  ? 27.616 -1.679  5.507   1.00 24.04 ? 52  THR A O   1 
ATOM   393  C CB  . THR A 1 52  ? 27.898 -1.629  8.709   1.00 22.00 ? 52  THR A CB  1 
ATOM   394  O OG1 . THR A 1 52  ? 29.082 -2.083  8.064   1.00 22.61 ? 52  THR A OG1 1 
ATOM   395  C CG2 . THR A 1 52  ? 27.730 -2.301  10.060  1.00 22.01 ? 52  THR A CG2 1 
ATOM   396  N N   . GLY A 1 53  ? 26.435 0.045   6.380   1.00 23.02 ? 53  GLY A N   1 
ATOM   397  C CA  . GLY A 1 53  ? 26.602 0.937   5.243   1.00 23.56 ? 53  GLY A CA  1 
ATOM   398  C C   . GLY A 1 53  ? 27.575 2.074   5.561   1.00 24.39 ? 53  GLY A C   1 
ATOM   399  O O   . GLY A 1 53  ? 28.496 1.903   6.357   1.00 22.77 ? 53  GLY A O   1 
ATOM   400  N N   . TYR A 1 54  ? 27.371 3.227   4.908   1.00 25.62 ? 54  TYR A N   1 
ATOM   401  C CA  . TYR A 1 54  ? 28.143 4.428   5.188   1.00 26.71 ? 54  TYR A CA  1 
ATOM   402  C C   . TYR A 1 54  ? 27.848 4.890   6.612   1.00 26.12 ? 54  TYR A C   1 
ATOM   403  O O   . TYR A 1 54  ? 26.688 5.000   7.000   1.00 26.62 ? 54  TYR A O   1 
ATOM   404  C CB  . TYR A 1 54  ? 27.810 5.607   4.267   1.00 27.60 ? 54  TYR A CB  1 
ATOM   405  C CG  . TYR A 1 54  ? 28.287 5.524   2.822   1.00 29.30 ? 54  TYR A CG  1 
ATOM   406  C CD1 . TYR A 1 54  ? 29.473 4.884   2.472   1.00 29.59 ? 54  TYR A CD1 1 
ATOM   407  C CD2 . TYR A 1 54  ? 27.553 6.128   1.806   1.00 29.83 ? 54  TYR A CD2 1 
ATOM   408  C CE1 . TYR A 1 54  ? 29.899 4.827   1.154   1.00 30.23 ? 54  TYR A CE1 1 
ATOM   409  C CE2 . TYR A 1 54  ? 27.970 6.077   0.486   1.00 30.27 ? 54  TYR A CE2 1 
ATOM   410  C CZ  . TYR A 1 54  ? 29.149 5.431   0.160   1.00 30.30 ? 54  TYR A CZ  1 
ATOM   411  O OH  . TYR A 1 54  ? 29.563 5.382   -1.141  1.00 31.85 ? 54  TYR A OH  1 
ATOM   412  N N   . GLY A 1 55  ? 28.908 5.176   7.375   1.00 25.36 ? 55  GLY A N   1 
ATOM   413  C CA  . GLY A 1 55  ? 28.770 5.553   8.773   1.00 25.05 ? 55  GLY A CA  1 
ATOM   414  C C   . GLY A 1 55  ? 28.947 4.349   9.696   1.00 24.53 ? 55  GLY A C   1 
ATOM   415  O O   . GLY A 1 55  ? 29.064 4.514   10.908  1.00 24.18 ? 55  GLY A O   1 
ATOM   416  N N   . ASP A 1 56  ? 28.920 3.145   9.108   1.00 23.87 ? 56  ASP A N   1 
ATOM   417  C CA  . ASP A 1 56  ? 29.387 1.926   9.753   1.00 23.72 ? 56  ASP A CA  1 
ATOM   418  C C   . ASP A 1 56  ? 28.537 1.574   10.974  1.00 22.91 ? 56  ASP A C   1 
ATOM   419  O O   . ASP A 1 56  ? 28.979 0.808   11.828  1.00 23.05 ? 56  ASP A O   1 
ATOM   420  C CB  . ASP A 1 56  ? 30.854 2.031   10.142  1.00 23.74 ? 56  ASP A CB  1 
ATOM   421  C CG  . ASP A 1 56  ? 31.799 2.544   9.064   1.00 24.52 ? 56  ASP A CG  1 
ATOM   422  O OD1 . ASP A 1 56  ? 31.786 1.979   7.948   1.00 24.09 ? 56  ASP A OD1 1 
ATOM   423  O OD2 . ASP A 1 56  ? 32.570 3.484   9.363   1.00 24.79 ? 56  ASP A OD2 1 
ATOM   424  N N   . SER A 1 57  ? 27.309 2.103   11.040  1.00 21.45 ? 57  SER A N   1 
ATOM   425  C CA  . SER A 1 57  ? 26.464 1.936   12.210  1.00 21.33 ? 57  SER A CA  1 
ATOM   426  C C   . SER A 1 57  ? 25.791 0.565   12.179  1.00 21.60 ? 57  SER A C   1 
ATOM   427  O O   . SER A 1 57  ? 25.171 0.201   11.179  1.00 20.95 ? 57  SER A O   1 
ATOM   428  C CB  . SER A 1 57  ? 25.438 3.040   12.301  1.00 21.00 ? 57  SER A CB  1 
ATOM   429  O OG  . SER A 1 57  ? 24.544 2.828   13.384  1.00 20.39 ? 57  SER A OG  1 
ATOM   430  N N   . PRO A 1 58  ? 25.867 -0.229  13.275  1.00 21.25 ? 58  PRO A N   1 
ATOM   431  C CA  . PRO A 1 58  ? 25.090 -1.459  13.373  1.00 20.88 ? 58  PRO A CA  1 
ATOM   432  C C   . PRO A 1 58  ? 23.583 -1.210  13.381  1.00 20.57 ? 58  PRO A C   1 
ATOM   433  O O   . PRO A 1 58  ? 22.806 -2.098  13.039  1.00 20.18 ? 58  PRO A O   1 
ATOM   434  C CB  . PRO A 1 58  ? 25.554 -2.086  14.688  1.00 21.18 ? 58  PRO A CB  1 
ATOM   435  C CG  . PRO A 1 58  ? 26.825 -1.345  15.061  1.00 21.31 ? 58  PRO A CG  1 
ATOM   436  C CD  . PRO A 1 58  ? 26.700 0.017   14.463  1.00 21.27 ? 58  PRO A CD  1 
ATOM   437  N N   . TYR A 1 59  ? 23.193 0.011   13.773  1.00 20.19 ? 59  TYR A N   1 
ATOM   438  C CA  . TYR A 1 59  ? 21.798 0.384   13.946  1.00 20.48 ? 59  TYR A CA  1 
ATOM   439  C C   . TYR A 1 59  ? 21.169 0.822   12.624  1.00 21.50 ? 59  TYR A C   1 
ATOM   440  O O   . TYR A 1 59  ? 19.953 1.022   12.572  1.00 21.96 ? 59  TYR A O   1 
ATOM   441  C CB  . TYR A 1 59  ? 21.718 1.454   15.041  1.00 19.75 ? 59  TYR A CB  1 
ATOM   442  C CG  . TYR A 1 59  ? 22.111 0.882   16.395  1.00 19.32 ? 59  TYR A CG  1 
ATOM   443  C CD1 . TYR A 1 59  ? 21.191 0.186   17.168  1.00 19.07 ? 59  TYR A CD1 1 
ATOM   444  C CD2 . TYR A 1 59  ? 23.416 0.976   16.867  1.00 19.28 ? 59  TYR A CD2 1 
ATOM   445  C CE1 . TYR A 1 59  ? 21.547 -0.365  18.388  1.00 19.25 ? 59  TYR A CE1 1 
ATOM   446  C CE2 . TYR A 1 59  ? 23.786 0.422   18.082  1.00 19.12 ? 59  TYR A CE2 1 
ATOM   447  C CZ  . TYR A 1 59  ? 22.848 -0.249  18.845  1.00 19.27 ? 59  TYR A CZ  1 
ATOM   448  O OH  . TYR A 1 59  ? 23.186 -0.804  20.045  1.00 19.37 ? 59  TYR A OH  1 
ATOM   449  N N   . GLN A 1 60  ? 21.982 0.970   11.569  1.00 21.92 ? 60  GLN A N   1 
ATOM   450  C CA  . GLN A 1 60  ? 21.454 1.122   10.219  1.00 23.06 ? 60  GLN A CA  1 
ATOM   451  C C   . GLN A 1 60  ? 22.038 0.028   9.327   1.00 22.99 ? 60  GLN A C   1 
ATOM   452  O O   . GLN A 1 60  ? 23.159 0.147   8.838   1.00 23.44 ? 60  GLN A O   1 
ATOM   453  C CB  . GLN A 1 60  ? 21.699 2.506   9.616   1.00 23.89 ? 60  GLN A CB  1 
ATOM   454  C CG  . GLN A 1 60  ? 21.398 2.571   8.121   1.00 24.63 ? 60  GLN A CG  1 
ATOM   455  C CD  . GLN A 1 60  ? 20.881 3.913   7.655   1.00 25.36 ? 60  GLN A CD  1 
ATOM   456  O OE1 . GLN A 1 60  ? 19.723 4.273   7.901   1.00 25.75 ? 60  GLN A OE1 1 
ATOM   457  N NE2 . GLN A 1 60  ? 21.725 4.653   6.947   1.00 25.74 ? 60  GLN A NE2 1 
ATOM   458  N N   . SER A 1 61  ? 21.242 -1.020  9.087   1.00 22.46 ? 61  SER A N   1 
ATOM   459  C CA  . SER A 1 61  ? 21.742 -2.238  8.472   1.00 22.24 ? 61  SER A CA  1 
ATOM   460  C C   . SER A 1 61  ? 21.070 -2.472  7.119   1.00 22.53 ? 61  SER A C   1 
ATOM   461  O O   . SER A 1 61  ? 19.963 -1.994  6.880   1.00 23.78 ? 61  SER A O   1 
ATOM   462  C CB  . SER A 1 61  ? 21.546 -3.408  9.400   1.00 21.50 ? 61  SER A CB  1 
ATOM   463  O OG  . SER A 1 61  ? 22.112 -4.594  8.861   1.00 21.58 ? 61  SER A OG  1 
ATOM   464  N N   . PHE A 1 62  ? 21.765 -3.210  6.241   1.00 22.09 ? 62  PHE A N   1 
ATOM   465  C CA  . PHE A 1 62  ? 21.243 -3.584  4.935   1.00 22.09 ? 62  PHE A CA  1 
ATOM   466  C C   . PHE A 1 62  ? 20.267 -4.752  5.055   1.00 22.11 ? 62  PHE A C   1 
ATOM   467  O O   . PHE A 1 62  ? 19.471 -4.982  4.147   1.00 22.36 ? 62  PHE A O   1 
ATOM   468  C CB  . PHE A 1 62  ? 22.373 -3.956  3.969   1.00 22.00 ? 62  PHE A CB  1 
ATOM   469  C CG  . PHE A 1 62  ? 23.257 -2.789  3.553   1.00 21.51 ? 62  PHE A CG  1 
ATOM   470  C CD1 . PHE A 1 62  ? 22.698 -1.577  3.161   1.00 21.28 ? 62  PHE A CD1 1 
ATOM   471  C CD2 . PHE A 1 62  ? 24.643 -2.900  3.580   1.00 21.42 ? 62  PHE A CD2 1 
ATOM   472  C CE1 . PHE A 1 62  ? 23.502 -0.514  2.791   1.00 21.39 ? 62  PHE A CE1 1 
ATOM   473  C CE2 . PHE A 1 62  ? 25.443 -1.829  3.211   1.00 21.49 ? 62  PHE A CE2 1 
ATOM   474  C CZ  . PHE A 1 62  ? 24.873 -0.643  2.815   1.00 21.64 ? 62  PHE A CZ  1 
ATOM   475  N N   . SER A 1 63  ? 20.344 -5.508  6.156   1.00 22.11 ? 63  SER A N   1 
ATOM   476  C CA  . SER A 1 63  ? 19.415 -6.604  6.373   1.00 22.26 ? 63  SER A CA  1 
ATOM   477  C C   . SER A 1 63  ? 19.144 -6.790  7.862   1.00 22.92 ? 63  SER A C   1 
ATOM   478  O O   . SER A 1 63  ? 20.059 -6.725  8.681   1.00 22.77 ? 63  SER A O   1 
ATOM   479  C CB  . SER A 1 63  ? 19.920 -7.876  5.739   1.00 21.93 ? 63  SER A CB  1 
ATOM   480  O OG  . SER A 1 63  ? 19.164 -9.007  6.151   1.00 21.46 ? 63  SER A OG  1 
ATOM   481  N N   . ALA A 1 64  ? 17.867 -7.035  8.183   1.00 23.26 ? 64  ALA A N   1 
ATOM   482  C CA  . ALA A 1 64  ? 17.452 -7.438  9.516   1.00 23.48 ? 64  ALA A CA  1 
ATOM   483  C C   . ALA A 1 64  ? 17.918 -8.863  9.804   1.00 23.02 ? 64  ALA A C   1 
ATOM   484  O O   . ALA A 1 64  ? 18.119 -9.228  10.961  1.00 24.28 ? 64  ALA A O   1 
ATOM   485  C CB  . ALA A 1 64  ? 15.950 -7.325  9.636   1.00 23.58 ? 64  ALA A CB  1 
ATOM   486  N N   . PHE A 1 65  ? 18.096 -9.659  8.742   1.00 21.77 ? 65  PHE A N   1 
ATOM   487  C CA  . PHE A 1 65  ? 18.351 -11.083 8.877   1.00 21.12 ? 65  PHE A CA  1 
ATOM   488  C C   . PHE A 1 65  ? 19.836 -11.402 8.713   1.00 19.74 ? 65  PHE A C   1 
ATOM   489  O O   . PHE A 1 65  ? 20.337 -12.309 9.371   1.00 19.39 ? 65  PHE A O   1 
ATOM   490  C CB  . PHE A 1 65  ? 17.465 -11.807 7.861   1.00 21.34 ? 65  PHE A CB  1 
ATOM   491  C CG  . PHE A 1 65  ? 15.988 -11.790 8.228   1.00 21.99 ? 65  PHE A CG  1 
ATOM   492  C CD1 . PHE A 1 65  ? 15.477 -12.697 9.151   1.00 21.96 ? 65  PHE A CD1 1 
ATOM   493  C CD2 . PHE A 1 65  ? 15.114 -10.874 7.653   1.00 21.98 ? 65  PHE A CD2 1 
ATOM   494  C CE1 . PHE A 1 65  ? 14.134 -12.686 9.486   1.00 22.37 ? 65  PHE A CE1 1 
ATOM   495  C CE2 . PHE A 1 65  ? 13.768 -10.871 7.990   1.00 22.29 ? 65  PHE A CE2 1 
ATOM   496  C CZ  . PHE A 1 65  ? 13.282 -11.775 8.908   1.00 22.11 ? 65  PHE A CZ  1 
ATOM   497  N N   . ALA A 1 66  ? 20.530 -10.669 7.833   1.00 18.89 ? 66  ALA A N   1 
ATOM   498  C CA  . ALA A 1 66  ? 21.885 -11.025 7.437   1.00 18.03 ? 66  ALA A CA  1 
ATOM   499  C C   . ALA A 1 66  ? 22.869 -10.752 8.569   1.00 17.69 ? 66  ALA A C   1 
ATOM   500  O O   . ALA A 1 66  ? 22.638 -9.881  9.402   1.00 16.75 ? 66  ALA A O   1 
ATOM   501  C CB  . ALA A 1 66  ? 22.287 -10.272 6.189   1.00 17.84 ? 66  ALA A CB  1 
ATOM   502  N N   . GLY A 1 67  ? 23.970 -11.514 8.563   1.00 17.82 ? 67  GLY A N   1 
ATOM   503  C CA  . GLY A 1 67  ? 25.110 -11.257 9.427   1.00 17.71 ? 67  GLY A CA  1 
ATOM   504  C C   . GLY A 1 67  ? 26.089 -10.283 8.778   1.00 17.54 ? 67  GLY A C   1 
ATOM   505  O O   . GLY A 1 67  ? 26.088 -10.105 7.561   1.00 17.82 ? 67  GLY A O   1 
ATOM   506  N N   . ASN A 1 68  ? 26.925 -9.658  9.615   1.00 16.60 ? 68  ASN A N   1 
ATOM   507  C CA  . ASN A 1 68  ? 27.949 -8.734  9.162   1.00 15.95 ? 68  ASN A CA  1 
ATOM   508  C C   . ASN A 1 68  ? 29.055 -9.530  8.471   1.00 16.04 ? 68  ASN A C   1 
ATOM   509  O O   . ASN A 1 68  ? 29.654 -10.419 9.073   1.00 15.56 ? 68  ASN A O   1 
ATOM   510  C CB  . ASN A 1 68  ? 28.460 -7.892  10.326  1.00 15.41 ? 68  ASN A CB  1 
ATOM   511  C CG  . ASN A 1 68  ? 29.204 -6.648  9.902   1.00 14.91 ? 68  ASN A CG  1 
ATOM   512  O OD1 . ASN A 1 68  ? 29.678 -6.543  8.765   1.00 14.91 ? 68  ASN A OD1 1 
ATOM   513  N ND2 . ASN A 1 68  ? 29.348 -5.701  10.818  1.00 14.73 ? 68  ASN A ND2 1 
ATOM   514  N N   . PRO A 1 69  ? 29.348 -9.258  7.180   1.00 16.38 ? 69  PRO A N   1 
ATOM   515  C CA  . PRO A 1 69  ? 30.451 -9.915  6.488   1.00 16.37 ? 69  PRO A CA  1 
ATOM   516  C C   . PRO A 1 69  ? 31.825 -9.633  7.094   1.00 16.20 ? 69  PRO A C   1 
ATOM   517  O O   . PRO A 1 69  ? 32.734 -10.440 6.932   1.00 16.05 ? 69  PRO A O   1 
ATOM   518  C CB  . PRO A 1 69  ? 30.342 -9.390  5.055   1.00 16.16 ? 69  PRO A CB  1 
ATOM   519  C CG  . PRO A 1 69  ? 28.903 -8.932  4.958   1.00 16.54 ? 69  PRO A CG  1 
ATOM   520  C CD  . PRO A 1 69  ? 28.606 -8.347  6.299   1.00 16.43 ? 69  PRO A CD  1 
ATOM   521  N N   . TYR A 1 70  ? 31.965 -8.506  7.806   1.00 16.51 ? 70  TYR A N   1 
ATOM   522  C CA  . TYR A 1 70  ? 33.249 -8.106  8.367   1.00 17.32 ? 70  TYR A CA  1 
ATOM   523  C C   . TYR A 1 70  ? 33.614 -8.943  9.591   1.00 16.65 ? 70  TYR A C   1 
ATOM   524  O O   . TYR A 1 70  ? 34.770 -8.932  10.001  1.00 17.21 ? 70  TYR A O   1 
ATOM   525  C CB  . TYR A 1 70  ? 33.273 -6.623  8.756   1.00 17.98 ? 70  TYR A CB  1 
ATOM   526  C CG  . TYR A 1 70  ? 33.192 -5.644  7.591   1.00 18.53 ? 70  TYR A CG  1 
ATOM   527  C CD1 . TYR A 1 70  ? 33.745 -5.949  6.351   1.00 19.52 ? 70  TYR A CD1 1 
ATOM   528  C CD2 . TYR A 1 70  ? 32.578 -4.406  7.736   1.00 18.53 ? 70  TYR A CD2 1 
ATOM   529  C CE1 . TYR A 1 70  ? 33.679 -5.060  5.291   1.00 19.85 ? 70  TYR A CE1 1 
ATOM   530  C CE2 . TYR A 1 70  ? 32.505 -3.507  6.682   1.00 19.17 ? 70  TYR A CE2 1 
ATOM   531  C CZ  . TYR A 1 70  ? 33.056 -3.836  5.457   1.00 19.63 ? 70  TYR A CZ  1 
ATOM   532  O OH  . TYR A 1 70  ? 33.006 -2.978  4.399   1.00 20.26 ? 70  TYR A OH  1 
ATOM   533  N N   . LEU A 1 71  ? 32.640 -9.650  10.177  1.00 16.11 ? 71  LEU A N   1 
ATOM   534  C CA  . LEU A 1 71  ? 32.877 -10.408 11.394  1.00 16.08 ? 71  LEU A CA  1 
ATOM   535  C C   . LEU A 1 71  ? 33.347 -11.823 11.073  1.00 15.69 ? 71  LEU A C   1 
ATOM   536  O O   . LEU A 1 71  ? 33.736 -12.546 11.984  1.00 15.62 ? 71  LEU A O   1 
ATOM   537  C CB  . LEU A 1 71  ? 31.621 -10.435 12.261  1.00 16.01 ? 71  LEU A CB  1 
ATOM   538  C CG  . LEU A 1 71  ? 31.186 -9.088  12.840  1.00 15.98 ? 71  LEU A CG  1 
ATOM   539  C CD1 . LEU A 1 71  ? 29.996 -9.266  13.762  1.00 15.89 ? 71  LEU A CD1 1 
ATOM   540  C CD2 . LEU A 1 71  ? 32.344 -8.415  13.560  1.00 16.16 ? 71  LEU A CD2 1 
ATOM   541  N N   . VAL A 1 72  ? 33.305 -12.202 9.790   1.00 15.40 ? 72  VAL A N   1 
ATOM   542  C CA  . VAL A 1 72  ? 33.725 -13.520 9.342   1.00 15.61 ? 72  VAL A CA  1 
ATOM   543  C C   . VAL A 1 72  ? 35.242 -13.640 9.493   1.00 15.44 ? 72  VAL A C   1 
ATOM   544  O O   . VAL A 1 72  ? 35.988 -12.789 9.016   1.00 15.76 ? 72  VAL A O   1 
ATOM   545  C CB  . VAL A 1 72  ? 33.285 -13.770 7.883   1.00 15.71 ? 72  VAL A CB  1 
ATOM   546  C CG1 . VAL A 1 72  ? 33.949 -15.004 7.276   1.00 15.76 ? 72  VAL A CG1 1 
ATOM   547  C CG2 . VAL A 1 72  ? 31.767 -13.862 7.749   1.00 15.76 ? 72  VAL A CG2 1 
ATOM   548  N N   . ASP A 1 73  ? 35.686 -14.713 10.153  1.00 15.80 ? 73  ASP A N   1 
ATOM   549  C CA  . ASP A 1 73  ? 37.103 -15.025 10.267  1.00 16.43 ? 73  ASP A CA  1 
ATOM   550  C C   . ASP A 1 73  ? 37.569 -15.691 8.973   1.00 17.44 ? 73  ASP A C   1 
ATOM   551  O O   . ASP A 1 73  ? 36.943 -16.648 8.523   1.00 16.86 ? 73  ASP A O   1 
ATOM   552  C CB  . ASP A 1 73  ? 37.364 -15.892 11.489  1.00 15.95 ? 73  ASP A CB  1 
ATOM   553  C CG  . ASP A 1 73  ? 38.826 -16.148 11.842  1.00 15.77 ? 73  ASP A CG  1 
ATOM   554  O OD1 . ASP A 1 73  ? 39.713 -15.549 11.200  1.00 15.44 ? 73  ASP A OD1 1 
ATOM   555  O OD2 . ASP A 1 73  ? 39.068 -16.945 12.771  1.00 16.20 ? 73  ASP A OD2 1 
ATOM   556  N N   . LEU A 1 74  ? 38.665 -15.174 8.393   1.00 19.47 ? 74  LEU A N   1 
ATOM   557  C CA  . LEU A 1 74  ? 39.205 -15.655 7.124   1.00 21.66 ? 74  LEU A CA  1 
ATOM   558  C C   . LEU A 1 74  ? 40.330 -16.666 7.344   1.00 22.38 ? 74  LEU A C   1 
ATOM   559  O O   . LEU A 1 74  ? 40.754 -17.316 6.392   1.00 22.88 ? 74  LEU A O   1 
ATOM   560  C CB  . LEU A 1 74  ? 39.731 -14.489 6.284   1.00 22.48 ? 74  LEU A CB  1 
ATOM   561  C CG  . LEU A 1 74  ? 38.714 -13.721 5.437   1.00 23.14 ? 74  LEU A CG  1 
ATOM   562  C CD1 . LEU A 1 74  ? 39.132 -12.270 5.342   1.00 23.75 ? 74  LEU A CD1 1 
ATOM   563  C CD2 . LEU A 1 74  ? 38.598 -14.324 4.042   1.00 23.72 ? 74  LEU A CD2 1 
ATOM   564  N N   . ARG A 1 75  ? 40.852 -16.756 8.572   1.00 23.14 ? 75  ARG A N   1 
ATOM   565  C CA  . ARG A 1 75  ? 42.028 -17.571 8.846   1.00 23.82 ? 75  ARG A CA  1 
ATOM   566  C C   . ARG A 1 75  ? 41.745 -19.056 8.613   1.00 24.77 ? 75  ARG A C   1 
ATOM   567  O O   . ARG A 1 75  ? 42.595 -19.747 8.058   1.00 25.52 ? 75  ARG A O   1 
ATOM   568  C CB  . ARG A 1 75  ? 42.572 -17.263 10.246  1.00 23.80 ? 75  ARG A CB  1 
ATOM   569  C CG  . ARG A 1 75  ? 43.176 -15.869 10.337  1.00 23.61 ? 75  ARG A CG  1 
ATOM   570  C CD  . ARG A 1 75  ? 43.397 -15.428 11.774  1.00 23.74 ? 75  ARG A CD  1 
ATOM   571  N NE  . ARG A 1 75  ? 42.138 -15.245 12.506  1.00 23.54 ? 75  ARG A NE  1 
ATOM   572  C CZ  . ARG A 1 75  ? 42.048 -14.904 13.789  1.00 23.59 ? 75  ARG A CZ  1 
ATOM   573  N NH1 . ARG A 1 75  ? 43.144 -14.675 14.495  1.00 22.91 ? 75  ARG A NH1 1 
ATOM   574  N NH2 . ARG A 1 75  ? 40.861 -14.782 14.363  1.00 23.40 ? 75  ARG A NH2 1 
ATOM   575  N N   . PRO A 1 76  ? 40.583 -19.621 9.029   1.00 25.58 ? 76  PRO A N   1 
ATOM   576  C CA  . PRO A 1 76  ? 40.233 -20.991 8.664   1.00 26.27 ? 76  PRO A CA  1 
ATOM   577  C C   . PRO A 1 76  ? 40.283 -21.275 7.163   1.00 26.54 ? 76  PRO A C   1 
ATOM   578  O O   . PRO A 1 76  ? 40.688 -22.363 6.757   1.00 28.26 ? 76  PRO A O   1 
ATOM   579  C CB  . PRO A 1 76  ? 38.826 -21.188 9.230   1.00 26.04 ? 76  PRO A CB  1 
ATOM   580  C CG  . PRO A 1 76  ? 38.351 -19.799 9.600   1.00 25.87 ? 76  PRO A CG  1 
ATOM   581  C CD  . PRO A 1 76  ? 39.580 -19.010 9.915   1.00 25.69 ? 76  PRO A CD  1 
ATOM   582  N N   . LEU A 1 77  ? 39.872 -20.294 6.351   1.00 26.65 ? 77  LEU A N   1 
ATOM   583  C CA  . LEU A 1 77  ? 39.948 -20.403 4.901   1.00 26.98 ? 77  LEU A CA  1 
ATOM   584  C C   . LEU A 1 77  ? 41.410 -20.405 4.455   1.00 27.76 ? 77  LEU A C   1 
ATOM   585  O O   . LEU A 1 77  ? 41.786 -21.174 3.572   1.00 27.84 ? 77  LEU A O   1 
ATOM   586  C CB  . LEU A 1 77  ? 39.172 -19.252 4.263   1.00 26.85 ? 77  LEU A CB  1 
ATOM   587  C CG  . LEU A 1 77  ? 37.676 -19.185 4.596   1.00 27.42 ? 77  LEU A CG  1 
ATOM   588  C CD1 . LEU A 1 77  ? 37.124 -17.784 4.405   1.00 27.49 ? 77  LEU A CD1 1 
ATOM   589  C CD2 . LEU A 1 77  ? 36.886 -20.171 3.764   1.00 27.37 ? 77  LEU A CD2 1 
ATOM   590  N N   . ALA A 1 78  ? 42.225 -19.534 5.067   1.00 27.93 ? 78  ALA A N   1 
ATOM   591  C CA  . ALA A 1 78  ? 43.615 -19.361 4.671   1.00 30.03 ? 78  ALA A CA  1 
ATOM   592  C C   . ALA A 1 78  ? 44.445 -20.601 5.006   1.00 31.20 ? 78  ALA A C   1 
ATOM   593  O O   . ALA A 1 78  ? 45.403 -20.909 4.299   1.00 32.72 ? 78  ALA A O   1 
ATOM   594  C CB  . ALA A 1 78  ? 44.189 -18.125 5.328   1.00 29.63 ? 78  ALA A CB  1 
ATOM   595  N N   . LYS A 1 79  ? 44.076 -21.294 6.091   1.00 31.81 ? 79  LYS A N   1 
ATOM   596  C CA  . LYS A 1 79  ? 44.714 -22.543 6.480   1.00 32.63 ? 79  LYS A CA  1 
ATOM   597  C C   . LYS A 1 79  ? 44.392 -23.632 5.456   1.00 33.46 ? 79  LYS A C   1 
ATOM   598  O O   . LYS A 1 79  ? 45.232 -24.482 5.166   1.00 33.17 ? 79  LYS A O   1 
ATOM   599  C CB  . LYS A 1 79  ? 44.244 -22.966 7.877   1.00 32.22 ? 79  LYS A CB  1 
ATOM   600  C CG  . LYS A 1 79  ? 44.598 -22.000 9.003   1.00 32.39 ? 79  LYS A CG  1 
ATOM   601  C CD  . LYS A 1 79  ? 43.646 -22.052 10.194  1.00 32.10 ? 79  LYS A CD  1 
ATOM   602  C CE  . LYS A 1 79  ? 43.819 -20.893 11.127  1.00 32.26 ? 79  LYS A CE  1 
ATOM   603  N NZ  . LYS A 1 79  ? 42.695 -20.739 12.055  1.00 31.97 ? 79  LYS A NZ  1 
ATOM   604  N N   . ARG A 1 80  ? 43.169 -23.586 4.915   1.00 33.90 ? 80  ARG A N   1 
ATOM   605  C CA  . ARG A 1 80  ? 42.721 -24.520 3.893   1.00 34.08 ? 80  ARG A CA  1 
ATOM   606  C C   . ARG A 1 80  ? 43.331 -24.176 2.534   1.00 34.01 ? 80  ARG A C   1 
ATOM   607  O O   . ARG A 1 80  ? 43.248 -24.978 1.606   1.00 32.84 ? 80  ARG A O   1 
ATOM   608  C CB  . ARG A 1 80  ? 41.189 -24.513 3.825   1.00 34.75 ? 80  ARG A CB  1 
ATOM   609  C CG  . ARG A 1 80  ? 40.541 -25.254 4.985   1.00 35.13 ? 80  ARG A CG  1 
ATOM   610  C CD  . ARG A 1 80  ? 39.048 -24.989 5.078   1.00 35.53 ? 80  ARG A CD  1 
ATOM   611  N NE  . ARG A 1 80  ? 38.418 -25.723 6.181   1.00 35.82 ? 80  ARG A NE  1 
ATOM   612  C CZ  . ARG A 1 80  ? 38.631 -25.528 7.480   1.00 35.81 ? 80  ARG A CZ  1 
ATOM   613  N NH1 . ARG A 1 80  ? 39.440 -24.571 7.899   1.00 35.61 ? 80  ARG A NH1 1 
ATOM   614  N NH2 . ARG A 1 80  ? 38.017 -26.292 8.367   1.00 36.40 ? 80  ARG A NH2 1 
ATOM   615  N N   . GLY A 1 81  ? 43.914 -22.975 2.417   1.00 34.57 ? 81  GLY A N   1 
ATOM   616  C CA  . GLY A 1 81  ? 44.618 -22.564 1.214   1.00 34.47 ? 81  GLY A CA  1 
ATOM   617  C C   . GLY A 1 81  ? 43.684 -21.901 0.202   1.00 34.58 ? 81  GLY A C   1 
ATOM   618  O O   . GLY A 1 81  ? 44.076 -21.672 -0.941  1.00 34.83 ? 81  GLY A O   1 
ATOM   619  N N   . TYR A 1 82  ? 42.459 -21.582 0.638   1.00 34.56 ? 82  TYR A N   1 
ATOM   620  C CA  . TYR A 1 82  ? 41.453 -20.984 -0.225  1.00 34.22 ? 82  TYR A CA  1 
ATOM   621  C C   . TYR A 1 82  ? 41.814 -19.531 -0.535  1.00 33.66 ? 82  TYR A C   1 
ATOM   622  O O   . TYR A 1 82  ? 41.416 -19.009 -1.574  1.00 34.34 ? 82  TYR A O   1 
ATOM   623  C CB  . TYR A 1 82  ? 40.070 -21.049 0.432   1.00 34.55 ? 82  TYR A CB  1 
ATOM   624  C CG  . TYR A 1 82  ? 39.508 -22.438 0.714   1.00 35.28 ? 82  TYR A CG  1 
ATOM   625  C CD1 . TYR A 1 82  ? 39.903 -23.557 -0.016  1.00 36.07 ? 82  TYR A CD1 1 
ATOM   626  C CD2 . TYR A 1 82  ? 38.553 -22.623 1.707   1.00 35.23 ? 82  TYR A CD2 1 
ATOM   627  C CE1 . TYR A 1 82  ? 39.378 -24.813 0.246   1.00 36.11 ? 82  TYR A CE1 1 
ATOM   628  C CE2 . TYR A 1 82  ? 38.018 -23.872 1.977   1.00 35.48 ? 82  TYR A CE2 1 
ATOM   629  C CZ  . TYR A 1 82  ? 38.432 -24.971 1.245   1.00 36.30 ? 82  TYR A CZ  1 
ATOM   630  O OH  . TYR A 1 82  ? 37.914 -26.206 1.506   1.00 35.52 ? 82  TYR A OH  1 
ATOM   631  N N   . VAL A 1 83  ? 42.547 -18.877 0.377   1.00 32.30 ? 83  VAL A N   1 
ATOM   632  C CA  . VAL A 1 83  ? 42.897 -17.474 0.221   1.00 32.58 ? 83  VAL A CA  1 
ATOM   633  C C   . VAL A 1 83  ? 44.256 -17.209 0.870   1.00 32.64 ? 83  VAL A C   1 
ATOM   634  O O   . VAL A 1 83  ? 44.684 -17.951 1.752   1.00 30.36 ? 83  VAL A O   1 
ATOM   635  C CB  . VAL A 1 83  ? 41.797 -16.576 0.825   1.00 31.97 ? 83  VAL A CB  1 
ATOM   636  C CG1 . VAL A 1 83  ? 41.750 -16.658 2.349   1.00 31.40 ? 83  VAL A CG1 1 
ATOM   637  C CG2 . VAL A 1 83  ? 41.929 -15.127 0.370   1.00 32.00 ? 83  VAL A CG2 1 
ATOM   638  N N   . ARG A 1 84  ? 44.918 -16.140 0.408   1.00 34.22 ? 84  ARG A N   1 
ATOM   639  C CA  . ARG A 1 84  ? 46.145 -15.639 1.006   1.00 35.39 ? 84  ARG A CA  1 
ATOM   640  C C   . ARG A 1 84  ? 45.886 -14.244 1.566   1.00 35.67 ? 84  ARG A C   1 
ATOM   641  O O   . ARG A 1 84  ? 45.457 -13.357 0.833   1.00 36.13 ? 84  ARG A O   1 
ATOM   642  C CB  . ARG A 1 84  ? 47.274 -15.574 -0.029  1.00 36.27 ? 84  ARG A CB  1 
ATOM   643  C CG  . ARG A 1 84  ? 48.539 -14.897 0.479   1.00 37.48 ? 84  ARG A CG  1 
ATOM   644  C CD  . ARG A 1 84  ? 49.704 -14.970 -0.496  1.00 38.53 ? 84  ARG A CD  1 
ATOM   645  N NE  . ARG A 1 84  ? 50.878 -14.268 0.038   1.00 40.19 ? 84  ARG A NE  1 
ATOM   646  C CZ  . ARG A 1 84  ? 52.093 -14.231 -0.505  1.00 41.34 ? 84  ARG A CZ  1 
ATOM   647  N NH1 . ARG A 1 84  ? 53.049 -13.532 0.083   1.00 42.16 ? 84  ARG A NH1 1 
ATOM   648  N NH2 . ARG A 1 84  ? 52.359 -14.882 -1.627  1.00 41.83 ? 84  ARG A NH2 1 
ATOM   649  N N   . LEU A 1 85  ? 46.189 -14.057 2.857   1.00 36.31 ? 85  LEU A N   1 
ATOM   650  C CA  . LEU A 1 85  ? 45.875 -12.823 3.560   1.00 36.97 ? 85  LEU A CA  1 
ATOM   651  C C   . LEU A 1 85  ? 47.161 -12.063 3.881   1.00 38.83 ? 85  LEU A C   1 
ATOM   652  O O   . LEU A 1 85  ? 48.136 -12.653 4.344   1.00 38.31 ? 85  LEU A O   1 
ATOM   653  C CB  . LEU A 1 85  ? 45.098 -13.173 4.828   1.00 36.94 ? 85  LEU A CB  1 
ATOM   654  C CG  . LEU A 1 85  ? 43.812 -13.980 4.628   1.00 36.88 ? 85  LEU A CG  1 
ATOM   655  C CD1 . LEU A 1 85  ? 43.272 -14.466 5.961   1.00 37.06 ? 85  LEU A CD1 1 
ATOM   656  C CD2 . LEU A 1 85  ? 42.760 -13.170 3.888   1.00 36.68 ? 85  LEU A CD2 1 
ATOM   657  N N   . GLU A 1 86  ? 47.145 -10.749 3.624   1.00 41.28 ? 86  GLU A N   1 
ATOM   658  C CA  . GLU A 1 86  ? 48.226 -9.857  4.015   1.00 42.34 ? 86  GLU A CA  1 
ATOM   659  C C   . GLU A 1 86  ? 47.628 -8.594  4.633   1.00 42.61 ? 86  GLU A C   1 
ATOM   660  O O   . GLU A 1 86  ? 46.463 -8.277  4.396   1.00 44.00 ? 86  GLU A O   1 
ATOM   661  C CB  . GLU A 1 86  ? 49.134 -9.517  2.831   1.00 43.10 ? 86  GLU A CB  1 
ATOM   662  C CG  . GLU A 1 86  ? 49.831 -10.734 2.230   1.00 43.85 ? 86  GLU A CG  1 
ATOM   663  C CD  . GLU A 1 86  ? 51.241 -10.470 1.727   1.00 43.95 ? 86  GLU A CD  1 
ATOM   664  O OE1 . GLU A 1 86  ? 52.101 -10.131 2.568   1.00 41.64 ? 86  GLU A OE1 1 
ATOM   665  O OE2 . GLU A 1 86  ? 51.482 -10.609 0.507   1.00 44.69 ? 86  GLU A OE2 1 
ATOM   666  N N   . ASP A 1 87  ? 48.444 -7.886  5.426   1.00 41.98 ? 87  ASP A N   1 
ATOM   667  C CA  . ASP A 1 87  ? 48.007 -6.707  6.159   1.00 41.40 ? 87  ASP A CA  1 
ATOM   668  C C   . ASP A 1 87  ? 48.349 -5.444  5.371   1.00 41.52 ? 87  ASP A C   1 
ATOM   669  O O   . ASP A 1 87  ? 49.522 -5.158  5.140   1.00 42.32 ? 87  ASP A O   1 
ATOM   670  C CB  . ASP A 1 87  ? 48.627 -6.661  7.547   1.00 41.78 ? 87  ASP A CB  1 
ATOM   671  C CG  . ASP A 1 87  ? 48.469 -5.342  8.290   1.00 41.49 ? 87  ASP A CG  1 
ATOM   672  O OD1 . ASP A 1 87  ? 47.335 -4.820  8.324   1.00 41.13 ? 87  ASP A OD1 1 
ATOM   673  O OD2 . ASP A 1 87  ? 49.481 -4.845  8.830   1.00 42.55 ? 87  ASP A OD2 1 
ATOM   674  N N   . PRO A 1 88  ? 47.346 -4.626  4.972   1.00 40.30 ? 88  PRO A N   1 
ATOM   675  C CA  . PRO A 1 88  ? 47.602 -3.413  4.203   1.00 40.05 ? 88  PRO A CA  1 
ATOM   676  C C   . PRO A 1 88  ? 48.099 -2.230  5.035   1.00 40.00 ? 88  PRO A C   1 
ATOM   677  O O   . PRO A 1 88  ? 48.395 -1.173  4.484   1.00 39.41 ? 88  PRO A O   1 
ATOM   678  C CB  . PRO A 1 88  ? 46.244 -3.124  3.570   1.00 40.18 ? 88  PRO A CB  1 
ATOM   679  C CG  . PRO A 1 88  ? 45.272 -3.632  4.621   1.00 39.99 ? 88  PRO A CG  1 
ATOM   680  C CD  . PRO A 1 88  ? 45.914 -4.839  5.235   1.00 39.88 ? 88  PRO A CD  1 
ATOM   681  N N   . GLY A 1 89  ? 48.185 -2.419  6.358   1.00 40.24 ? 89  GLY A N   1 
ATOM   682  C CA  . GLY A 1 89  ? 48.574 -1.363  7.280   1.00 40.15 ? 89  GLY A CA  1 
ATOM   683  C C   . GLY A 1 89  ? 47.418 -0.985  8.203   1.00 38.63 ? 89  GLY A C   1 
ATOM   684  O O   . GLY A 1 89  ? 47.176 0.195   8.448   1.00 39.86 ? 89  GLY A O   1 
ATOM   685  N N   . PHE A 1 90  ? 46.712 -2.002  8.712   1.00 37.76 ? 90  PHE A N   1 
ATOM   686  C CA  . PHE A 1 90  ? 45.548 -1.794  9.557   1.00 36.02 ? 90  PHE A CA  1 
ATOM   687  C C   . PHE A 1 90  ? 45.994 -1.182  10.881  1.00 35.86 ? 90  PHE A C   1 
ATOM   688  O O   . PHE A 1 90  ? 47.024 -1.573  11.428  1.00 36.01 ? 90  PHE A O   1 
ATOM   689  C CB  . PHE A 1 90  ? 44.803 -3.111  9.795   1.00 35.45 ? 90  PHE A CB  1 
ATOM   690  C CG  . PHE A 1 90  ? 43.856 -3.539  8.681   1.00 34.52 ? 90  PHE A CG  1 
ATOM   691  C CD1 . PHE A 1 90  ? 42.847 -2.689  8.236   1.00 33.97 ? 90  PHE A CD1 1 
ATOM   692  C CD2 . PHE A 1 90  ? 43.976 -4.789  8.083   1.00 33.38 ? 90  PHE A CD2 1 
ATOM   693  C CE1 . PHE A 1 90  ? 41.984 -3.083  7.225   1.00 33.88 ? 90  PHE A CE1 1 
ATOM   694  C CE2 . PHE A 1 90  ? 43.109 -5.176  7.071   1.00 33.69 ? 90  PHE A CE2 1 
ATOM   695  C CZ  . PHE A 1 90  ? 42.117 -4.323  6.644   1.00 33.69 ? 90  PHE A CZ  1 
ATOM   696  N N   . PRO A 1 91  ? 45.237 -0.208  11.437  1.00 35.00 ? 91  PRO A N   1 
ATOM   697  C CA  . PRO A 1 91  ? 45.535 0.321   12.761  1.00 34.63 ? 91  PRO A CA  1 
ATOM   698  C C   . PRO A 1 91  ? 45.222 -0.689  13.860  1.00 34.65 ? 91  PRO A C   1 
ATOM   699  O O   . PRO A 1 91  ? 44.377 -1.563  13.677  1.00 34.79 ? 91  PRO A O   1 
ATOM   700  C CB  . PRO A 1 91  ? 44.648 1.556   12.850  1.00 34.51 ? 91  PRO A CB  1 
ATOM   701  C CG  . PRO A 1 91  ? 43.457 1.159   11.996  1.00 34.71 ? 91  PRO A CG  1 
ATOM   702  C CD  . PRO A 1 91  ? 44.036 0.401   10.843  1.00 34.85 ? 91  PRO A CD  1 
ATOM   703  N N   . GLN A 1 92  ? 45.911 -0.568  14.997  1.00 33.90 ? 92  GLN A N   1 
ATOM   704  C CA  . GLN A 1 92  ? 45.648 -1.440  16.129  1.00 33.56 ? 92  GLN A CA  1 
ATOM   705  C C   . GLN A 1 92  ? 44.949 -0.618  17.210  1.00 30.54 ? 92  GLN A C   1 
ATOM   706  O O   . GLN A 1 92  ? 45.292 0.539   17.432  1.00 28.95 ? 92  GLN A O   1 
ATOM   707  C CB  . GLN A 1 92  ? 46.950 -2.122  16.554  1.00 35.06 ? 92  GLN A CB  1 
ATOM   708  C CG  . GLN A 1 92  ? 46.767 -3.267  17.546  1.00 36.34 ? 92  GLN A CG  1 
ATOM   709  C CD  . GLN A 1 92  ? 45.715 -4.272  17.126  1.00 37.14 ? 92  GLN A CD  1 
ATOM   710  O OE1 . GLN A 1 92  ? 44.792 -4.592  17.884  1.00 37.94 ? 92  GLN A OE1 1 
ATOM   711  N NE2 . GLN A 1 92  ? 45.847 -4.788  15.912  1.00 37.51 ? 92  GLN A NE2 1 
ATOM   712  N N   . GLY A 1 93  ? 43.927 -1.215  17.834  1.00 28.94 ? 93  GLY A N   1 
ATOM   713  C CA  . GLY A 1 93  ? 43.113 -0.528  18.825  1.00 28.40 ? 93  GLY A CA  1 
ATOM   714  C C   . GLY A 1 93  ? 41.981 0.286   18.195  1.00 27.42 ? 93  GLY A C   1 
ATOM   715  O O   . GLY A 1 93  ? 41.194 0.903   18.911  1.00 26.32 ? 93  GLY A O   1 
ATOM   716  N N   . ARG A 1 94  ? 41.895 0.276   16.858  1.00 26.68 ? 94  ARG A N   1 
ATOM   717  C CA  . ARG A 1 94  ? 40.878 1.030   16.145  1.00 26.43 ? 94  ARG A CA  1 
ATOM   718  C C   . ARG A 1 94  ? 40.522 0.288   14.859  1.00 24.71 ? 94  ARG A C   1 
ATOM   719  O O   . ARG A 1 94  ? 41.385 -0.333  14.245  1.00 23.14 ? 94  ARG A O   1 
ATOM   720  C CB  . ARG A 1 94  ? 41.385 2.447   15.844  1.00 28.11 ? 94  ARG A CB  1 
ATOM   721  C CG  . ARG A 1 94  ? 40.289 3.450   15.515  1.00 30.01 ? 94  ARG A CG  1 
ATOM   722  C CD  . ARG A 1 94  ? 40.843 4.792   15.056  1.00 32.20 ? 94  ARG A CD  1 
ATOM   723  N NE  . ARG A 1 94  ? 41.426 4.724   13.711  1.00 33.87 ? 94  ARG A NE  1 
ATOM   724  C CZ  . ARG A 1 94  ? 42.725 4.754   13.419  1.00 36.01 ? 94  ARG A CZ  1 
ATOM   725  N NH1 . ARG A 1 94  ? 43.630 4.797   14.381  1.00 36.56 ? 94  ARG A NH1 1 
ATOM   726  N NH2 . ARG A 1 94  ? 43.119 4.721   12.157  1.00 37.52 ? 94  ARG A NH2 1 
ATOM   727  N N   . VAL A 1 95  ? 39.240 0.334   14.479  1.00 23.94 ? 95  VAL A N   1 
ATOM   728  C CA  . VAL A 1 95  ? 38.804 -0.168  13.188  1.00 23.77 ? 95  VAL A CA  1 
ATOM   729  C C   . VAL A 1 95  ? 38.908 0.989   12.199  1.00 23.65 ? 95  VAL A C   1 
ATOM   730  O O   . VAL A 1 95  ? 38.334 2.052   12.430  1.00 24.94 ? 95  VAL A O   1 
ATOM   731  C CB  . VAL A 1 95  ? 37.375 -0.752  13.194  1.00 23.47 ? 95  VAL A CB  1 
ATOM   732  C CG1 . VAL A 1 95  ? 36.942 -1.205  11.805  1.00 23.37 ? 95  VAL A CG1 1 
ATOM   733  C CG2 . VAL A 1 95  ? 37.219 -1.904  14.182  1.00 23.26 ? 95  VAL A CG2 1 
ATOM   734  N N   . ASP A 1 96  ? 39.663 0.786   11.116  1.00 22.84 ? 96  ASP A N   1 
ATOM   735  C CA  . ASP A 1 96  ? 39.625 1.694   9.980   1.00 22.26 ? 96  ASP A CA  1 
ATOM   736  C C   . ASP A 1 96  ? 38.735 1.071   8.910   1.00 21.17 ? 96  ASP A C   1 
ATOM   737  O O   . ASP A 1 96  ? 39.193 0.232   8.137   1.00 21.16 ? 96  ASP A O   1 
ATOM   738  C CB  . ASP A 1 96  ? 41.019 2.019   9.469   1.00 22.51 ? 96  ASP A CB  1 
ATOM   739  C CG  . ASP A 1 96  ? 41.085 2.963   8.276   1.00 22.55 ? 96  ASP A CG  1 
ATOM   740  O OD1 . ASP A 1 96  ? 40.026 3.233   7.667   1.00 22.96 ? 96  ASP A OD1 1 
ATOM   741  O OD2 . ASP A 1 96  ? 42.196 3.433   7.970   1.00 21.47 ? 96  ASP A OD2 1 
ATOM   742  N N   . TYR A 1 97  ? 37.470 1.510   8.868   1.00 19.84 ? 97  TYR A N   1 
ATOM   743  C CA  . TYR A 1 97  ? 36.450 0.887   8.039   1.00 19.39 ? 97  TYR A CA  1 
ATOM   744  C C   . TYR A 1 97  ? 36.768 1.051   6.554   1.00 19.29 ? 97  TYR A C   1 
ATOM   745  O O   . TYR A 1 97  ? 36.417 0.182   5.760   1.00 19.12 ? 97  TYR A O   1 
ATOM   746  C CB  . TYR A 1 97  ? 35.069 1.450   8.394   1.00 18.71 ? 97  TYR A CB  1 
ATOM   747  C CG  . TYR A 1 97  ? 34.499 0.860   9.675   1.00 18.26 ? 97  TYR A CG  1 
ATOM   748  C CD1 . TYR A 1 97  ? 33.809 -0.346  9.652   1.00 17.79 ? 97  TYR A CD1 1 
ATOM   749  C CD2 . TYR A 1 97  ? 34.664 1.491   10.906  1.00 17.83 ? 97  TYR A CD2 1 
ATOM   750  C CE1 . TYR A 1 97  ? 33.288 -0.900  10.808  1.00 17.72 ? 97  TYR A CE1 1 
ATOM   751  C CE2 . TYR A 1 97  ? 34.147 0.944   12.072  1.00 17.43 ? 97  TYR A CE2 1 
ATOM   752  C CZ  . TYR A 1 97  ? 33.458 -0.257  12.020  1.00 17.32 ? 97  TYR A CZ  1 
ATOM   753  O OH  . TYR A 1 97  ? 32.933 -0.826  13.142  1.00 16.82 ? 97  TYR A OH  1 
ATOM   754  N N   . GLY A 1 98  ? 37.408 2.165   6.184   1.00 19.56 ? 98  GLY A N   1 
ATOM   755  C CA  . GLY A 1 98  ? 37.727 2.446   4.791   1.00 20.11 ? 98  GLY A CA  1 
ATOM   756  C C   . GLY A 1 98  ? 38.774 1.474   4.252   1.00 20.27 ? 98  GLY A C   1 
ATOM   757  O O   . GLY A 1 98  ? 38.636 0.940   3.152   1.00 20.21 ? 98  GLY A O   1 
ATOM   758  N N   . LEU A 1 99  ? 39.829 1.257   5.039   1.00 20.89 ? 99  LEU A N   1 
ATOM   759  C CA  . LEU A 1 99  ? 40.831 0.263   4.697   1.00 21.71 ? 99  LEU A CA  1 
ATOM   760  C C   . LEU A 1 99  ? 40.176 -1.117  4.683   1.00 21.74 ? 99  LEU A C   1 
ATOM   761  O O   . LEU A 1 99  ? 40.451 -1.919  3.796   1.00 21.12 ? 99  LEU A O   1 
ATOM   762  C CB  . LEU A 1 99  ? 42.001 0.338   5.677   1.00 22.13 ? 99  LEU A CB  1 
ATOM   763  C CG  . LEU A 1 99  ? 43.291 -0.367  5.245   1.00 22.47 ? 99  LEU A CG  1 
ATOM   764  C CD1 . LEU A 1 99  ? 43.710 0.009   3.828   1.00 22.58 ? 99  LEU A CD1 1 
ATOM   765  C CD2 . LEU A 1 99  ? 44.401 -0.035  6.225   1.00 22.60 ? 99  LEU A CD2 1 
ATOM   766  N N   . LEU A 1 100 ? 39.278 -1.356  5.649   1.00 22.04 ? 100 LEU A N   1 
ATOM   767  C CA  . LEU A 1 100 ? 38.628 -2.647  5.816   1.00 22.46 ? 100 LEU A CA  1 
ATOM   768  C C   . LEU A 1 100 ? 37.732 -2.947  4.616   1.00 22.70 ? 100 LEU A C   1 
ATOM   769  O O   . LEU A 1 100 ? 37.712 -4.075  4.130   1.00 22.31 ? 100 LEU A O   1 
ATOM   770  C CB  . LEU A 1 100 ? 37.842 -2.662  7.128   1.00 22.13 ? 100 LEU A CB  1 
ATOM   771  C CG  . LEU A 1 100 ? 37.331 -4.028  7.600   1.00 21.96 ? 100 LEU A CG  1 
ATOM   772  C CD1 . LEU A 1 100 ? 38.480 -4.977  7.912   1.00 22.28 ? 100 LEU A CD1 1 
ATOM   773  C CD2 . LEU A 1 100 ? 36.428 -3.862  8.810   1.00 21.71 ? 100 LEU A CD2 1 
ATOM   774  N N   . TYR A 1 101 ? 36.995 -1.932  4.148   1.00 23.50 ? 101 TYR A N   1 
ATOM   775  C CA  . TYR A 1 101 ? 36.133 -2.064  2.983   1.00 24.46 ? 101 TYR A CA  1 
ATOM   776  C C   . TYR A 1 101 ? 36.957 -2.497  1.772   1.00 23.62 ? 101 TYR A C   1 
ATOM   777  O O   . TYR A 1 101 ? 36.558 -3.398  1.036   1.00 23.45 ? 101 TYR A O   1 
ATOM   778  C CB  . TYR A 1 101 ? 35.413 -0.734  2.732   1.00 25.98 ? 101 TYR A CB  1 
ATOM   779  C CG  . TYR A 1 101 ? 34.486 -0.700  1.521   1.00 27.30 ? 101 TYR A CG  1 
ATOM   780  C CD1 . TYR A 1 101 ? 33.164 -1.126  1.612   1.00 27.74 ? 101 TYR A CD1 1 
ATOM   781  C CD2 . TYR A 1 101 ? 34.924 -0.217  0.293   1.00 27.84 ? 101 TYR A CD2 1 
ATOM   782  C CE1 . TYR A 1 101 ? 32.316 -1.089  0.517   1.00 28.16 ? 101 TYR A CE1 1 
ATOM   783  C CE2 . TYR A 1 101 ? 34.085 -0.174  -0.810  1.00 28.61 ? 101 TYR A CE2 1 
ATOM   784  C CZ  . TYR A 1 101 ? 32.775 -0.606  -0.697  1.00 28.50 ? 101 TYR A CZ  1 
ATOM   785  O OH  . TYR A 1 101 ? 31.939 -0.566  -1.777  1.00 28.59 ? 101 TYR A OH  1 
ATOM   786  N N   . ALA A 1 102 ? 38.113 -1.850  1.588   1.00 23.02 ? 102 ALA A N   1 
ATOM   787  C CA  . ALA A 1 102 ? 38.943 -2.048  0.410   1.00 23.33 ? 102 ALA A CA  1 
ATOM   788  C C   . ALA A 1 102 ? 39.625 -3.416  0.417   1.00 23.61 ? 102 ALA A C   1 
ATOM   789  O O   . ALA A 1 102 ? 39.898 -3.953  -0.652  1.00 24.22 ? 102 ALA A O   1 
ATOM   790  C CB  . ALA A 1 102 ? 39.972 -0.945  0.322   1.00 23.28 ? 102 ALA A CB  1 
ATOM   791  N N   . TRP A 1 103 ? 39.932 -3.961  1.603   1.00 23.13 ? 103 TRP A N   1 
ATOM   792  C CA  . TRP A 1 103 ? 40.744 -5.168  1.688   1.00 23.54 ? 103 TRP A CA  1 
ATOM   793  C C   . TRP A 1 103 ? 39.893 -6.414  1.920   1.00 22.03 ? 103 TRP A C   1 
ATOM   794  O O   . TRP A 1 103 ? 40.136 -7.437  1.284   1.00 21.68 ? 103 TRP A O   1 
ATOM   795  C CB  . TRP A 1 103 ? 41.816 -5.048  2.781   1.00 25.10 ? 103 TRP A CB  1 
ATOM   796  C CG  . TRP A 1 103 ? 42.608 -6.315  2.994   1.00 26.89 ? 103 TRP A CG  1 
ATOM   797  C CD1 . TRP A 1 103 ? 43.730 -6.708  2.324   1.00 28.09 ? 103 TRP A CD1 1 
ATOM   798  C CD2 . TRP A 1 103 ? 42.330 -7.365  3.949   1.00 28.30 ? 103 TRP A CD2 1 
ATOM   799  N NE1 . TRP A 1 103 ? 44.172 -7.916  2.795   1.00 28.36 ? 103 TRP A NE1 1 
ATOM   800  C CE2 . TRP A 1 103 ? 43.334 -8.346  3.789   1.00 28.27 ? 103 TRP A CE2 1 
ATOM   801  C CE3 . TRP A 1 103 ? 41.337 -7.570  4.915   1.00 28.43 ? 103 TRP A CE3 1 
ATOM   802  C CZ2 . TRP A 1 103 ? 43.371 -9.505  4.561   1.00 28.92 ? 103 TRP A CZ2 1 
ATOM   803  C CZ3 . TRP A 1 103 ? 41.378 -8.716  5.679   1.00 28.88 ? 103 TRP A CZ3 1 
ATOM   804  C CH2 . TRP A 1 103 ? 42.382 -9.669  5.504   1.00 28.91 ? 103 TRP A CH2 1 
ATOM   805  N N   . LYS A 1 104 ? 38.924 -6.340  2.842   1.00 20.83 ? 104 LYS A N   1 
ATOM   806  C CA  . LYS A 1 104 ? 38.239 -7.537  3.304   1.00 20.63 ? 104 LYS A CA  1 
ATOM   807  C C   . LYS A 1 104 ? 37.310 -8.079  2.218   1.00 20.28 ? 104 LYS A C   1 
ATOM   808  O O   . LYS A 1 104 ? 37.308 -9.281  1.971   1.00 19.92 ? 104 LYS A O   1 
ATOM   809  C CB  . LYS A 1 104 ? 37.486 -7.326  4.622   1.00 20.32 ? 104 LYS A CB  1 
ATOM   810  C CG  . LYS A 1 104 ? 36.831 -8.593  5.151   1.00 20.41 ? 104 LYS A CG  1 
ATOM   811  C CD  . LYS A 1 104 ? 36.746 -8.680  6.670   1.00 20.22 ? 104 LYS A CD  1 
ATOM   812  C CE  . LYS A 1 104 ? 36.430 -10.059 7.143   1.00 20.06 ? 104 LYS A CE  1 
ATOM   813  N NZ  . LYS A 1 104 ? 36.645 -10.190 8.586   1.00 19.93 ? 104 LYS A NZ  1 
ATOM   814  N N   . TRP A 1 105 ? 36.518 -7.202  1.587   1.00 20.39 ? 105 TRP A N   1 
ATOM   815  C CA  . TRP A 1 105 ? 35.581 -7.634  0.559   1.00 21.09 ? 105 TRP A CA  1 
ATOM   816  C C   . TRP A 1 105 ? 36.315 -8.390  -0.550  1.00 20.19 ? 105 TRP A C   1 
ATOM   817  O O   . TRP A 1 105 ? 35.862 -9.455  -0.963  1.00 19.27 ? 105 TRP A O   1 
ATOM   818  C CB  . TRP A 1 105 ? 34.772 -6.456  -0.007  1.00 21.72 ? 105 TRP A CB  1 
ATOM   819  C CG  . TRP A 1 105 ? 33.621 -6.024  0.863   1.00 22.80 ? 105 TRP A CG  1 
ATOM   820  C CD1 . TRP A 1 105 ? 33.558 -4.914  1.652   1.00 23.21 ? 105 TRP A CD1 1 
ATOM   821  C CD2 . TRP A 1 105 ? 32.362 -6.711  1.039   1.00 22.99 ? 105 TRP A CD2 1 
ATOM   822  N NE1 . TRP A 1 105 ? 32.354 -4.855  2.300   1.00 22.86 ? 105 TRP A NE1 1 
ATOM   823  C CE2 . TRP A 1 105 ? 31.602 -5.945  1.950   1.00 22.76 ? 105 TRP A CE2 1 
ATOM   824  C CE3 . TRP A 1 105 ? 31.810 -7.889  0.524   1.00 22.85 ? 105 TRP A CE3 1 
ATOM   825  C CZ2 . TRP A 1 105 ? 30.322 -6.320  2.348   1.00 23.08 ? 105 TRP A CZ2 1 
ATOM   826  C CZ3 . TRP A 1 105 ? 30.546 -8.261  0.924   1.00 22.84 ? 105 TRP A CZ3 1 
ATOM   827  C CH2 . TRP A 1 105 ? 29.815 -7.487  1.826   1.00 23.14 ? 105 TRP A CH2 1 
ATOM   828  N N   . PRO A 1 106 ? 37.446 -7.873  -1.086  1.00 20.03 ? 106 PRO A N   1 
ATOM   829  C CA  . PRO A 1 106 ? 38.265 -8.641  -2.019  1.00 20.22 ? 106 PRO A CA  1 
ATOM   830  C C   . PRO A 1 106 ? 38.815 -9.939  -1.432  1.00 19.76 ? 106 PRO A C   1 
ATOM   831  O O   . PRO A 1 106 ? 38.908 -10.946 -2.130  1.00 19.59 ? 106 PRO A O   1 
ATOM   832  C CB  . PRO A 1 106 ? 39.375 -7.663  -2.407  1.00 20.44 ? 106 PRO A CB  1 
ATOM   833  C CG  . PRO A 1 106 ? 38.729 -6.312  -2.176  1.00 20.35 ? 106 PRO A CG  1 
ATOM   834  C CD  . PRO A 1 106 ? 37.945 -6.500  -0.919  1.00 20.33 ? 106 PRO A CD  1 
ATOM   835  N N   . ALA A 1 107 ? 39.183 -9.907  -0.146  1.00 19.73 ? 107 ALA A N   1 
ATOM   836  C CA  . ALA A 1 107 ? 39.671 -11.094 0.536   1.00 19.72 ? 107 ALA A CA  1 
ATOM   837  C C   . ALA A 1 107 ? 38.590 -12.173 0.535   1.00 19.77 ? 107 ALA A C   1 
ATOM   838  O O   . ALA A 1 107 ? 38.875 -13.341 0.281   1.00 20.10 ? 107 ALA A O   1 
ATOM   839  C CB  . ALA A 1 107 ? 40.108 -10.747 1.939   1.00 19.58 ? 107 ALA A CB  1 
ATOM   840  N N   . LEU A 1 108 ? 37.346 -11.756 0.794   1.00 19.98 ? 108 LEU A N   1 
ATOM   841  C CA  . LEU A 1 108 ? 36.215 -12.666 0.872   1.00 20.13 ? 108 LEU A CA  1 
ATOM   842  C C   . LEU A 1 108 ? 35.918 -13.272 -0.500  1.00 20.81 ? 108 LEU A C   1 
ATOM   843  O O   . LEU A 1 108 ? 35.588 -14.452 -0.584  1.00 21.92 ? 108 LEU A O   1 
ATOM   844  C CB  . LEU A 1 108 ? 35.011 -11.917 1.444   1.00 19.61 ? 108 LEU A CB  1 
ATOM   845  C CG  . LEU A 1 108 ? 35.143 -11.463 2.903   1.00 19.44 ? 108 LEU A CG  1 
ATOM   846  C CD1 . LEU A 1 108 ? 34.041 -10.492 3.292   1.00 19.24 ? 108 LEU A CD1 1 
ATOM   847  C CD2 . LEU A 1 108 ? 35.158 -12.651 3.851   1.00 19.52 ? 108 LEU A CD2 1 
ATOM   848  N N   . LYS A 1 109 ? 36.019 -12.464 -1.565  1.00 21.30 ? 109 LYS A N   1 
ATOM   849  C CA  . LYS A 1 109 ? 35.776 -12.937 -2.923  1.00 21.85 ? 109 LYS A CA  1 
ATOM   850  C C   . LYS A 1 109 ? 36.806 -13.995 -3.318  1.00 21.54 ? 109 LYS A C   1 
ATOM   851  O O   . LYS A 1 109 ? 36.461 -15.014 -3.911  1.00 21.21 ? 109 LYS A O   1 
ATOM   852  C CB  . LYS A 1 109 ? 35.833 -11.784 -3.931  1.00 22.18 ? 109 LYS A CB  1 
ATOM   853  C CG  . LYS A 1 109 ? 34.681 -10.794 -3.876  1.00 22.97 ? 109 LYS A CG  1 
ATOM   854  C CD  . LYS A 1 109 ? 34.933 -9.544  -4.709  1.00 24.12 ? 109 LYS A CD  1 
ATOM   855  C CE  . LYS A 1 109 ? 33.684 -8.823  -5.104  1.00 24.28 ? 109 LYS A CE  1 
ATOM   856  N NZ  . LYS A 1 109 ? 32.883 -8.439  -3.943  1.00 24.74 ? 109 LYS A NZ  1 
ATOM   857  N N   . GLU A 1 110 ? 38.075 -13.734 -2.994  1.00 21.34 ? 110 GLU A N   1 
ATOM   858  C CA  . GLU A 1 110 ? 39.166 -14.634 -3.331  1.00 21.55 ? 110 GLU A CA  1 
ATOM   859  C C   . GLU A 1 110 ? 38.965 -15.969 -2.616  1.00 21.26 ? 110 GLU A C   1 
ATOM   860  O O   . GLU A 1 110 ? 39.106 -17.028 -3.227  1.00 20.74 ? 110 GLU A O   1 
ATOM   861  C CB  . GLU A 1 110 ? 40.491 -13.934 -3.026  1.00 22.22 ? 110 GLU A CB  1 
ATOM   862  C CG  . GLU A 1 110 ? 40.769 -12.789 -3.997  1.00 23.16 ? 110 GLU A CG  1 
ATOM   863  C CD  . GLU A 1 110 ? 41.849 -11.784 -3.635  1.00 23.94 ? 110 GLU A CD  1 
ATOM   864  O OE1 . GLU A 1 110 ? 42.478 -11.877 -2.560  1.00 25.67 ? 110 GLU A OE1 1 
ATOM   865  O OE2 . GLU A 1 110 ? 42.055 -10.884 -4.475  1.00 24.43 ? 110 GLU A OE2 1 
ATOM   866  N N   . ALA A 1 111 ? 38.605 -15.901 -1.329  1.00 20.81 ? 111 ALA A N   1 
ATOM   867  C CA  . ALA A 1 111 ? 38.273 -17.081 -0.548  1.00 20.64 ? 111 ALA A CA  1 
ATOM   868  C C   . ALA A 1 111 ? 37.173 -17.897 -1.230  1.00 20.49 ? 111 ALA A C   1 
ATOM   869  O O   . ALA A 1 111 ? 37.278 -19.118 -1.312  1.00 18.90 ? 111 ALA A O   1 
ATOM   870  C CB  . ALA A 1 111 ? 37.862 -16.672 0.846   1.00 20.81 ? 111 ALA A CB  1 
ATOM   871  N N   . PHE A 1 112 ? 36.128 -17.211 -1.716  1.00 20.91 ? 112 PHE A N   1 
ATOM   872  C CA  . PHE A 1 112 ? 34.982 -17.866 -2.332  1.00 21.86 ? 112 PHE A CA  1 
ATOM   873  C C   . PHE A 1 112 ? 35.436 -18.669 -3.551  1.00 22.87 ? 112 PHE A C   1 
ATOM   874  O O   . PHE A 1 112 ? 35.061 -19.829 -3.713  1.00 23.08 ? 112 PHE A O   1 
ATOM   875  C CB  . PHE A 1 112 ? 33.924 -16.821 -2.710  1.00 21.77 ? 112 PHE A CB  1 
ATOM   876  C CG  . PHE A 1 112 ? 32.668 -17.379 -3.369  1.00 21.65 ? 112 PHE A CG  1 
ATOM   877  C CD1 . PHE A 1 112 ? 32.014 -18.487 -2.839  1.00 21.40 ? 112 PHE A CD1 1 
ATOM   878  C CD2 . PHE A 1 112 ? 32.160 -16.812 -4.536  1.00 21.65 ? 112 PHE A CD2 1 
ATOM   879  C CE1 . PHE A 1 112 ? 30.875 -18.995 -3.443  1.00 21.57 ? 112 PHE A CE1 1 
ATOM   880  C CE2 . PHE A 1 112 ? 31.019 -17.325 -5.136  1.00 21.62 ? 112 PHE A CE2 1 
ATOM   881  C CZ  . PHE A 1 112 ? 30.382 -18.416 -4.592  1.00 21.47 ? 112 PHE A CZ  1 
ATOM   882  N N   . ARG A 1 113 ? 36.255 -18.039 -4.398  1.00 24.35 ? 113 ARG A N   1 
ATOM   883  C CA  . ARG A 1 113 ? 36.764 -18.669 -5.607  1.00 25.39 ? 113 ARG A CA  1 
ATOM   884  C C   . ARG A 1 113 ? 37.613 -19.885 -5.239  1.00 26.00 ? 113 ARG A C   1 
ATOM   885  O O   . ARG A 1 113 ? 37.535 -20.921 -5.897  1.00 26.73 ? 113 ARG A O   1 
ATOM   886  C CB  . ARG A 1 113 ? 37.550 -17.647 -6.438  1.00 25.53 ? 113 ARG A CB  1 
ATOM   887  C CG  . ARG A 1 113 ? 36.740 -16.425 -6.852  1.00 26.14 ? 113 ARG A CG  1 
ATOM   888  C CD  . ARG A 1 113 ? 37.494 -15.517 -7.806  1.00 26.50 ? 113 ARG A CD  1 
ATOM   889  N NE  . ARG A 1 113 ? 37.231 -14.097 -7.545  1.00 27.47 ? 113 ARG A NE  1 
ATOM   890  C CZ  . ARG A 1 113 ? 38.144 -13.200 -7.171  1.00 27.39 ? 113 ARG A CZ  1 
ATOM   891  N NH1 . ARG A 1 113 ? 39.404 -13.556 -6.992  1.00 27.09 ? 113 ARG A NH1 1 
ATOM   892  N NH2 . ARG A 1 113 ? 37.794 -11.944 -6.963  1.00 27.67 ? 113 ARG A NH2 1 
ATOM   893  N N   . GLY A 1 114 ? 38.410 -19.754 -4.172  1.00 26.62 ? 114 GLY A N   1 
ATOM   894  C CA  . GLY A 1 114 ? 39.247 -20.842 -3.688  1.00 27.16 ? 114 GLY A CA  1 
ATOM   895  C C   . GLY A 1 114 ? 38.419 -22.006 -3.143  1.00 27.27 ? 114 GLY A C   1 
ATOM   896  O O   . GLY A 1 114 ? 38.800 -23.166 -3.297  1.00 26.99 ? 114 GLY A O   1 
ATOM   897  N N   . PHE A 1 115 ? 37.289 -21.682 -2.504  1.00 27.16 ? 115 PHE A N   1 
ATOM   898  C CA  . PHE A 1 115 ? 36.396 -22.688 -1.948  1.00 27.67 ? 115 PHE A CA  1 
ATOM   899  C C   . PHE A 1 115 ? 35.738 -23.465 -3.085  1.00 28.58 ? 115 PHE A C   1 
ATOM   900  O O   . PHE A 1 115 ? 35.726 -24.691 -3.074  1.00 28.86 ? 115 PHE A O   1 
ATOM   901  C CB  . PHE A 1 115 ? 35.372 -22.009 -1.032  1.00 27.02 ? 115 PHE A CB  1 
ATOM   902  C CG  . PHE A 1 115 ? 34.301 -22.928 -0.460  1.00 27.05 ? 115 PHE A CG  1 
ATOM   903  C CD1 . PHE A 1 115 ? 34.496 -23.595 0.745   1.00 26.74 ? 115 PHE A CD1 1 
ATOM   904  C CD2 . PHE A 1 115 ? 33.086 -23.100 -1.118  1.00 27.27 ? 115 PHE A CD2 1 
ATOM   905  C CE1 . PHE A 1 115 ? 33.509 -24.424 1.262   1.00 27.01 ? 115 PHE A CE1 1 
ATOM   906  C CE2 . PHE A 1 115 ? 32.104 -23.927 -0.594  1.00 27.37 ? 115 PHE A CE2 1 
ATOM   907  C CZ  . PHE A 1 115 ? 32.319 -24.589 0.594   1.00 27.13 ? 115 PHE A CZ  1 
ATOM   908  N N   . GLN A 1 116 ? 35.210 -22.739 -4.074  1.00 30.84 ? 116 GLN A N   1 
ATOM   909  C CA  . GLN A 1 116 ? 34.471 -23.347 -5.170  1.00 32.54 ? 116 GLN A CA  1 
ATOM   910  C C   . GLN A 1 116 ? 35.367 -24.314 -5.942  1.00 33.36 ? 116 GLN A C   1 
ATOM   911  O O   . GLN A 1 116 ? 34.891 -25.331 -6.439  1.00 34.14 ? 116 GLN A O   1 
ATOM   912  C CB  . GLN A 1 116 ? 33.899 -22.266 -6.087  1.00 33.00 ? 116 GLN A CB  1 
ATOM   913  C CG  . GLN A 1 116 ? 32.865 -21.363 -5.421  1.00 33.52 ? 116 GLN A CG  1 
ATOM   914  C CD  . GLN A 1 116 ? 31.621 -22.096 -4.969  1.00 35.33 ? 116 GLN A CD  1 
ATOM   915  O OE1 . GLN A 1 116 ? 31.271 -22.098 -3.784  1.00 37.27 ? 116 GLN A OE1 1 
ATOM   916  N NE2 . GLN A 1 116 ? 30.935 -22.724 -5.914  1.00 35.82 ? 116 GLN A NE2 1 
ATOM   917  N N   . GLU A 1 117 ? 36.662 -23.987 -6.036  1.00 34.44 ? 117 GLU A N   1 
ATOM   918  C CA  . GLU A 1 117 ? 37.632 -24.832 -6.716  1.00 36.66 ? 117 GLU A CA  1 
ATOM   919  C C   . GLU A 1 117 ? 37.988 -26.038 -5.848  1.00 36.63 ? 117 GLU A C   1 
ATOM   920  O O   . GLU A 1 117 ? 37.938 -27.170 -6.323  1.00 39.13 ? 117 GLU A O   1 
ATOM   921  C CB  . GLU A 1 117 ? 38.887 -24.029 -7.069  1.00 37.63 ? 117 GLU A CB  1 
ATOM   922  C CG  . GLU A 1 117 ? 40.029 -24.866 -7.643  1.00 38.97 ? 117 GLU A CG  1 
ATOM   923  C CD  . GLU A 1 117 ? 41.242 -24.062 -8.081  1.00 40.15 ? 117 GLU A CD  1 
ATOM   924  O OE1 . GLU A 1 117 ? 41.887 -23.450 -7.203  1.00 40.24 ? 117 GLU A OE1 1 
ATOM   925  O OE2 . GLU A 1 117 ? 41.544 -24.044 -9.296  1.00 41.66 ? 117 GLU A OE2 1 
ATOM   926  N N   . LYS A 1 118 ? 38.338 -25.788 -4.580  1.00 36.03 ? 118 LYS A N   1 
ATOM   927  C CA  . LYS A 1 118 ? 39.130 -26.730 -3.802  1.00 36.38 ? 118 LYS A CA  1 
ATOM   928  C C   . LYS A 1 118 ? 38.333 -27.435 -2.705  1.00 35.76 ? 118 LYS A C   1 
ATOM   929  O O   . LYS A 1 118 ? 38.793 -28.457 -2.198  1.00 36.36 ? 118 LYS A O   1 
ATOM   930  C CB  . LYS A 1 118 ? 40.303 -26.010 -3.128  1.00 37.21 ? 118 LYS A CB  1 
ATOM   931  C CG  . LYS A 1 118 ? 41.225 -25.240 -4.062  1.00 37.71 ? 118 LYS A CG  1 
ATOM   932  C CD  . LYS A 1 118 ? 42.422 -24.624 -3.349  1.00 38.34 ? 118 LYS A CD  1 
ATOM   933  C CE  . LYS A 1 118 ? 43.232 -23.744 -4.244  1.00 38.91 ? 118 LYS A CE  1 
ATOM   934  N NZ  . LYS A 1 118 ? 44.476 -23.320 -3.599  1.00 39.74 ? 118 LYS A NZ  1 
ATOM   935  N N   . ALA A 1 119 ? 37.164 -26.903 -2.325  1.00 34.79 ? 119 ALA A N   1 
ATOM   936  C CA  . ALA A 1 119 ? 36.485 -27.362 -1.121  1.00 34.38 ? 119 ALA A CA  1 
ATOM   937  C C   . ALA A 1 119 ? 36.096 -28.832 -1.246  1.00 33.81 ? 119 ALA A C   1 
ATOM   938  O O   . ALA A 1 119 ? 35.801 -29.299 -2.345  1.00 33.49 ? 119 ALA A O   1 
ATOM   939  C CB  . ALA A 1 119 ? 35.268 -26.507 -0.839  1.00 35.08 ? 119 ALA A CB  1 
ATOM   940  N N   . PRO A 1 120 ? 36.071 -29.605 -0.132  1.00 34.02 ? 120 PRO A N   1 
ATOM   941  C CA  . PRO A 1 120 ? 35.519 -30.953 -0.161  1.00 33.99 ? 120 PRO A CA  1 
ATOM   942  C C   . PRO A 1 120 ? 34.025 -30.941 -0.475  1.00 33.77 ? 120 PRO A C   1 
ATOM   943  O O   . PRO A 1 120 ? 33.338 -29.986 -0.116  1.00 34.87 ? 120 PRO A O   1 
ATOM   944  C CB  . PRO A 1 120 ? 35.827 -31.501 1.230   1.00 33.92 ? 120 PRO A CB  1 
ATOM   945  C CG  . PRO A 1 120 ? 35.941 -30.253 2.091   1.00 33.68 ? 120 PRO A CG  1 
ATOM   946  C CD  . PRO A 1 120 ? 36.547 -29.212 1.204   1.00 33.36 ? 120 PRO A CD  1 
ATOM   947  N N   . PRO A 1 121 ? 33.477 -31.979 -1.151  1.00 32.53 ? 121 PRO A N   1 
ATOM   948  C CA  . PRO A 1 121 ? 32.057 -32.007 -1.487  1.00 32.15 ? 121 PRO A CA  1 
ATOM   949  C C   . PRO A 1 121 ? 31.144 -31.924 -0.266  1.00 32.92 ? 121 PRO A C   1 
ATOM   950  O O   . PRO A 1 121 ? 30.031 -31.410 -0.355  1.00 34.49 ? 121 PRO A O   1 
ATOM   951  C CB  . PRO A 1 121 ? 31.886 -33.317 -2.252  1.00 31.62 ? 121 PRO A CB  1 
ATOM   952  C CG  . PRO A 1 121 ? 33.090 -34.150 -1.861  1.00 31.53 ? 121 PRO A CG  1 
ATOM   953  C CD  . PRO A 1 121 ? 34.197 -33.178 -1.611  1.00 31.86 ? 121 PRO A CD  1 
ATOM   954  N N   . GLU A 1 122 ? 31.630 -32.430 0.873   1.00 32.80 ? 122 GLU A N   1 
ATOM   955  C CA  . GLU A 1 122 ? 30.884 -32.388 2.120   1.00 33.11 ? 122 GLU A CA  1 
ATOM   956  C C   . GLU A 1 122 ? 30.608 -30.937 2.509   1.00 32.02 ? 122 GLU A C   1 
ATOM   957  O O   . GLU A 1 122 ? 29.491 -30.609 2.900   1.00 32.43 ? 122 GLU A O   1 
ATOM   958  C CB  . GLU A 1 122 ? 31.607 -33.100 3.264   1.00 34.17 ? 122 GLU A CB  1 
ATOM   959  C CG  . GLU A 1 122 ? 32.159 -34.474 2.895   1.00 35.98 ? 122 GLU A CG  1 
ATOM   960  C CD  . GLU A 1 122 ? 33.607 -34.473 2.442   1.00 37.02 ? 122 GLU A CD  1 
ATOM   961  O OE1 . GLU A 1 122 ? 34.483 -34.100 3.252   1.00 38.60 ? 122 GLU A OE1 1 
ATOM   962  O OE2 . GLU A 1 122 ? 33.853 -34.844 1.276   1.00 38.09 ? 122 GLU A OE2 1 
ATOM   963  N N   . GLU A 1 123 ? 31.633 -30.082 2.403   1.00 31.15 ? 123 GLU A N   1 
ATOM   964  C CA  . GLU A 1 123 ? 31.489 -28.657 2.671   1.00 30.70 ? 123 GLU A CA  1 
ATOM   965  C C   . GLU A 1 123 ? 30.534 -28.018 1.664   1.00 29.14 ? 123 GLU A C   1 
ATOM   966  O O   . GLU A 1 123 ? 29.675 -27.225 2.038   1.00 28.01 ? 123 GLU A O   1 
ATOM   967  C CB  . GLU A 1 123 ? 32.819 -27.901 2.629   1.00 31.29 ? 123 GLU A CB  1 
ATOM   968  C CG  . GLU A 1 123 ? 33.409 -27.602 4.005   1.00 32.67 ? 123 GLU A CG  1 
ATOM   969  C CD  . GLU A 1 123 ? 34.560 -26.609 3.969   1.00 33.27 ? 123 GLU A CD  1 
ATOM   970  O OE1 . GLU A 1 123 ? 34.399 -25.494 4.510   1.00 35.25 ? 123 GLU A OE1 1 
ATOM   971  O OE2 . GLU A 1 123 ? 35.617 -26.939 3.392   1.00 32.84 ? 123 GLU A OE2 1 
ATOM   972  N N   . ARG A 1 124 ? 30.700 -28.355 0.383   1.00 28.56 ? 124 ARG A N   1 
ATOM   973  C CA  . ARG A 1 124 ? 29.927 -27.717 -0.670  1.00 29.33 ? 124 ARG A CA  1 
ATOM   974  C C   . ARG A 1 124 ? 28.458 -28.128 -0.575  1.00 29.45 ? 124 ARG A C   1 
ATOM   975  O O   . ARG A 1 124 ? 27.590 -27.403 -1.056  1.00 29.09 ? 124 ARG A O   1 
ATOM   976  C CB  . ARG A 1 124 ? 30.570 -27.981 -2.038  1.00 29.87 ? 124 ARG A CB  1 
ATOM   977  C CG  . ARG A 1 124 ? 31.829 -27.151 -2.244  1.00 30.35 ? 124 ARG A CG  1 
ATOM   978  C CD  . ARG A 1 124 ? 32.568 -27.447 -3.538  1.00 30.79 ? 124 ARG A CD  1 
ATOM   979  N NE  . ARG A 1 124 ? 33.414 -28.641 -3.426  1.00 31.40 ? 124 ARG A NE  1 
ATOM   980  C CZ  . ARG A 1 124 ? 33.295 -29.772 -4.117  1.00 30.72 ? 124 ARG A CZ  1 
ATOM   981  N NH1 . ARG A 1 124 ? 34.181 -30.739 -3.944  1.00 30.33 ? 124 ARG A NH1 1 
ATOM   982  N NH2 . ARG A 1 124 ? 32.309 -29.935 -4.982  1.00 30.33 ? 124 ARG A NH2 1 
ATOM   983  N N   . GLU A 1 125 ? 28.177 -29.271 0.067   1.00 29.42 ? 125 GLU A N   1 
ATOM   984  C CA  . GLU A 1 125 ? 26.802 -29.709 0.262   1.00 29.96 ? 125 GLU A CA  1 
ATOM   985  C C   . GLU A 1 125 ? 26.140 -28.903 1.380   1.00 29.08 ? 125 GLU A C   1 
ATOM   986  O O   . GLU A 1 125 ? 24.979 -28.525 1.240   1.00 29.81 ? 125 GLU A O   1 
ATOM   987  C CB  . GLU A 1 125 ? 26.715 -31.217 0.514   1.00 30.39 ? 125 GLU A CB  1 
ATOM   988  C CG  . GLU A 1 125 ? 25.295 -31.732 0.748   1.00 30.88 ? 125 GLU A CG  1 
ATOM   989  C CD  . GLU A 1 125 ? 24.308 -31.595 -0.400  1.00 31.40 ? 125 GLU A CD  1 
ATOM   990  O OE1 . GLU A 1 125 ? 24.676 -31.150 -1.507  1.00 30.74 ? 125 GLU A OE1 1 
ATOM   991  O OE2 . GLU A 1 125 ? 23.133 -31.950 -0.166  1.00 32.76 ? 125 GLU A OE2 1 
ATOM   992  N N   . ASP A 1 126 ? 26.862 -28.642 2.481   1.00 27.79 ? 126 ASP A N   1 
ATOM   993  C CA  . ASP A 1 126 ? 26.269 -27.934 3.610   1.00 26.90 ? 126 ASP A CA  1 
ATOM   994  C C   . ASP A 1 126 ? 26.044 -26.462 3.259   1.00 24.87 ? 126 ASP A C   1 
ATOM   995  O O   . ASP A 1 126 ? 25.099 -25.857 3.754   1.00 25.66 ? 126 ASP A O   1 
ATOM   996  C CB  . ASP A 1 126 ? 26.991 -28.203 4.926   1.00 27.61 ? 126 ASP A CB  1 
ATOM   997  C CG  . ASP A 1 126 ? 28.495 -27.977 4.956   1.00 28.66 ? 126 ASP A CG  1 
ATOM   998  O OD1 . ASP A 1 126 ? 28.923 -26.858 4.615   1.00 28.34 ? 126 ASP A OD1 1 
ATOM   999  O OD2 . ASP A 1 126 ? 29.221 -28.918 5.352   1.00 30.62 ? 126 ASP A OD2 1 
ATOM   1000 N N   . PHE A 1 127 ? 26.895 -25.897 2.393   1.00 23.11 ? 127 PHE A N   1 
ATOM   1001 C CA  . PHE A 1 127 ? 26.667 -24.573 1.832   1.00 21.97 ? 127 PHE A CA  1 
ATOM   1002 C C   . PHE A 1 127 ? 25.415 -24.593 0.955   1.00 22.28 ? 127 PHE A C   1 
ATOM   1003 O O   . PHE A 1 127 ? 24.619 -23.658 0.990   1.00 21.56 ? 127 PHE A O   1 
ATOM   1004 C CB  . PHE A 1 127 ? 27.876 -24.104 1.016   1.00 21.20 ? 127 PHE A CB  1 
ATOM   1005 C CG  . PHE A 1 127 ? 27.705 -22.778 0.283   1.00 20.23 ? 127 PHE A CG  1 
ATOM   1006 C CD1 . PHE A 1 127 ? 27.025 -21.712 0.868   1.00 19.70 ? 127 PHE A CD1 1 
ATOM   1007 C CD2 . PHE A 1 127 ? 28.220 -22.603 -0.999  1.00 20.01 ? 127 PHE A CD2 1 
ATOM   1008 C CE1 . PHE A 1 127 ? 26.874 -20.511 0.193   1.00 19.57 ? 127 PHE A CE1 1 
ATOM   1009 C CE2 . PHE A 1 127 ? 28.069 -21.396 -1.668  1.00 19.74 ? 127 PHE A CE2 1 
ATOM   1010 C CZ  . PHE A 1 127 ? 27.399 -20.353 -1.071  1.00 19.50 ? 127 PHE A CZ  1 
ATOM   1011 N N   . ALA A 1 128 ? 25.265 -25.658 0.158   1.00 22.50 ? 128 ALA A N   1 
ATOM   1012 C CA  . ALA A 1 128 ? 24.122 -25.805 -0.728  1.00 23.07 ? 128 ALA A CA  1 
ATOM   1013 C C   . ALA A 1 128 ? 22.838 -25.977 0.083   1.00 22.96 ? 128 ALA A C   1 
ATOM   1014 O O   . ALA A 1 128 ? 21.826 -25.347 -0.213  1.00 23.55 ? 128 ALA A O   1 
ATOM   1015 C CB  . ALA A 1 128 ? 24.348 -26.963 -1.673  1.00 23.25 ? 128 ALA A CB  1 
ATOM   1016 N N   . ALA A 1 129 ? 22.900 -26.819 1.119   1.00 23.57 ? 129 ALA A N   1 
ATOM   1017 C CA  . ALA A 1 129 ? 21.768 -27.047 2.005   1.00 23.28 ? 129 ALA A CA  1 
ATOM   1018 C C   . ALA A 1 129 ? 21.380 -25.767 2.750   1.00 22.50 ? 129 ALA A C   1 
ATOM   1019 O O   . ALA A 1 129 ? 20.198 -25.547 3.006   1.00 21.62 ? 129 ALA A O   1 
ATOM   1020 C CB  . ALA A 1 129 ? 22.089 -28.175 2.959   1.00 23.05 ? 129 ALA A CB  1 
ATOM   1021 N N   . PHE A 1 130 ? 22.376 -24.929 3.081   1.00 22.42 ? 130 PHE A N   1 
ATOM   1022 C CA  . PHE A 1 130 ? 22.161 -23.689 3.817   1.00 22.87 ? 130 PHE A CA  1 
ATOM   1023 C C   . PHE A 1 130 ? 21.379 -22.683 2.974   1.00 23.19 ? 130 PHE A C   1 
ATOM   1024 O O   . PHE A 1 130 ? 20.530 -21.961 3.495   1.00 22.55 ? 130 PHE A O   1 
ATOM   1025 C CB  . PHE A 1 130 ? 23.507 -23.086 4.238   1.00 23.80 ? 130 PHE A CB  1 
ATOM   1026 C CG  . PHE A 1 130 ? 23.458 -21.644 4.732   1.00 23.79 ? 130 PHE A CG  1 
ATOM   1027 C CD1 . PHE A 1 130 ? 23.506 -20.581 3.834   1.00 24.01 ? 130 PHE A CD1 1 
ATOM   1028 C CD2 . PHE A 1 130 ? 23.398 -21.354 6.092   1.00 24.15 ? 130 PHE A CD2 1 
ATOM   1029 C CE1 . PHE A 1 130 ? 23.478 -19.269 4.284   1.00 23.97 ? 130 PHE A CE1 1 
ATOM   1030 C CE2 . PHE A 1 130 ? 23.364 -20.039 6.536   1.00 23.75 ? 130 PHE A CE2 1 
ATOM   1031 C CZ  . PHE A 1 130 ? 23.402 -19.001 5.631   1.00 24.04 ? 130 PHE A CZ  1 
ATOM   1032 N N   . ARG A 1 131 ? 21.703 -22.613 1.680   1.00 23.88 ? 131 ARG A N   1 
ATOM   1033 C CA  . ARG A 1 131 ? 21.099 -21.636 0.789   1.00 25.04 ? 131 ARG A CA  1 
ATOM   1034 C C   . ARG A 1 131 ? 19.612 -21.932 0.604   1.00 26.34 ? 131 ARG A C   1 
ATOM   1035 O O   . ARG A 1 131 ? 18.811 -21.013 0.469   1.00 25.93 ? 131 ARG A O   1 
ATOM   1036 C CB  . ARG A 1 131 ? 21.835 -21.630 -0.553  1.00 24.66 ? 131 ARG A CB  1 
ATOM   1037 C CG  . ARG A 1 131 ? 23.274 -21.145 -0.451  1.00 24.73 ? 131 ARG A CG  1 
ATOM   1038 C CD  . ARG A 1 131 ? 23.958 -21.212 -1.800  1.00 24.58 ? 131 ARG A CD  1 
ATOM   1039 N NE  . ARG A 1 131 ? 23.416 -20.218 -2.730  1.00 24.72 ? 131 ARG A NE  1 
ATOM   1040 C CZ  . ARG A 1 131 ? 23.756 -20.105 -4.008  1.00 24.77 ? 131 ARG A CZ  1 
ATOM   1041 N NH1 . ARG A 1 131 ? 24.612 -20.956 -4.549  1.00 25.05 ? 131 ARG A NH1 1 
ATOM   1042 N NH2 . ARG A 1 131 ? 23.230 -19.141 -4.743  1.00 24.90 ? 131 ARG A NH2 1 
ATOM   1043 N N   . GLU A 1 132 ? 19.256 -23.219 0.600   1.00 28.75 ? 132 GLU A N   1 
ATOM   1044 C CA  . GLU A 1 132 ? 17.878 -23.640 0.401   1.00 30.68 ? 132 GLU A CA  1 
ATOM   1045 C C   . GLU A 1 132 ? 17.059 -23.356 1.661   1.00 31.33 ? 132 GLU A C   1 
ATOM   1046 O O   . GLU A 1 132 ? 15.904 -22.945 1.573   1.00 32.33 ? 132 GLU A O   1 
ATOM   1047 C CB  . GLU A 1 132 ? 17.883 -25.123 0.031   1.00 31.80 ? 132 GLU A CB  1 
ATOM   1048 C CG  . GLU A 1 132 ? 16.555 -25.625 -0.526  1.00 33.00 ? 132 GLU A CG  1 
ATOM   1049 C CD  . GLU A 1 132 ? 16.604 -27.095 -0.899  1.00 34.06 ? 132 GLU A CD  1 
ATOM   1050 O OE1 . GLU A 1 132 ? 16.366 -27.431 -2.081  1.00 34.95 ? 132 GLU A OE1 1 
ATOM   1051 O OE2 . GLU A 1 132 ? 16.892 -27.904 0.006   1.00 33.74 ? 132 GLU A OE2 1 
ATOM   1052 N N   . LYS A 1 133 ? 17.679 -23.568 2.827   1.00 31.76 ? 133 LYS A N   1 
ATOM   1053 C CA  . LYS A 1 133 ? 17.028 -23.394 4.118   1.00 33.36 ? 133 LYS A CA  1 
ATOM   1054 C C   . LYS A 1 133 ? 16.791 -21.914 4.420   1.00 33.02 ? 133 LYS A C   1 
ATOM   1055 O O   . LYS A 1 133 ? 15.763 -21.566 4.995   1.00 33.22 ? 133 LYS A O   1 
ATOM   1056 C CB  . LYS A 1 133 ? 17.896 -24.058 5.196   1.00 34.31 ? 133 LYS A CB  1 
ATOM   1057 C CG  . LYS A 1 133 ? 17.716 -23.586 6.635   1.00 34.92 ? 133 LYS A CG  1 
ATOM   1058 C CD  . LYS A 1 133 ? 18.939 -23.908 7.484   1.00 35.95 ? 133 LYS A CD  1 
ATOM   1059 C CE  . LYS A 1 133 ? 18.821 -23.493 8.912   1.00 35.96 ? 133 LYS A CE  1 
ATOM   1060 N NZ  . LYS A 1 133 ? 20.125 -23.581 9.574   1.00 36.77 ? 133 LYS A NZ  1 
ATOM   1061 N N   . GLU A 1 134 ? 17.754 -21.057 4.051   1.00 32.53 ? 134 GLU A N   1 
ATOM   1062 C CA  . GLU A 1 134 ? 17.718 -19.648 4.412   1.00 32.00 ? 134 GLU A CA  1 
ATOM   1063 C C   . GLU A 1 134 ? 17.196 -18.799 3.253   1.00 31.32 ? 134 GLU A C   1 
ATOM   1064 O O   . GLU A 1 134 ? 17.097 -17.582 3.386   1.00 30.94 ? 134 GLU A O   1 
ATOM   1065 C CB  . GLU A 1 134 ? 19.116 -19.182 4.825   1.00 31.79 ? 134 GLU A CB  1 
ATOM   1066 C CG  . GLU A 1 134 ? 19.709 -19.956 6.000   1.00 32.31 ? 134 GLU A CG  1 
ATOM   1067 C CD  . GLU A 1 134 ? 19.004 -19.795 7.337   1.00 32.57 ? 134 GLU A CD  1 
ATOM   1068 O OE1 . GLU A 1 134 ? 17.945 -19.134 7.399   1.00 32.15 ? 134 GLU A OE1 1 
ATOM   1069 O OE2 . GLU A 1 134 ? 19.530 -20.329 8.336   1.00 33.93 ? 134 GLU A OE2 1 
ATOM   1070 N N   . ALA A 1 135 ? 16.842 -19.453 2.138   1.00 30.94 ? 135 ALA A N   1 
ATOM   1071 C CA  . ALA A 1 135 ? 16.428 -18.787 0.911   1.00 30.80 ? 135 ALA A CA  1 
ATOM   1072 C C   . ALA A 1 135 ? 15.383 -17.702 1.170   1.00 29.81 ? 135 ALA A C   1 
ATOM   1073 O O   . ALA A 1 135 ? 15.434 -16.645 0.546   1.00 30.08 ? 135 ALA A O   1 
ATOM   1074 C CB  . ALA A 1 135 ? 15.897 -19.811 -0.071  1.00 31.62 ? 135 ALA A CB  1 
ATOM   1075 N N   . TRP A 1 136 ? 14.433 -17.976 2.075   1.00 28.64 ? 136 TRP A N   1 
ATOM   1076 C CA  . TRP A 1 136 ? 13.307 -17.083 2.324   1.00 27.72 ? 136 TRP A CA  1 
ATOM   1077 C C   . TRP A 1 136 ? 13.770 -15.664 2.659   1.00 26.85 ? 136 TRP A C   1 
ATOM   1078 O O   . TRP A 1 136 ? 13.048 -14.707 2.383   1.00 27.14 ? 136 TRP A O   1 
ATOM   1079 C CB  . TRP A 1 136 ? 12.389 -17.639 3.424   1.00 27.56 ? 136 TRP A CB  1 
ATOM   1080 C CG  . TRP A 1 136 ? 13.077 -17.984 4.719   1.00 27.84 ? 136 TRP A CG  1 
ATOM   1081 C CD1 . TRP A 1 136 ? 13.695 -19.161 5.025   1.00 27.99 ? 136 TRP A CD1 1 
ATOM   1082 C CD2 . TRP A 1 136 ? 13.195 -17.154 5.897   1.00 27.72 ? 136 TRP A CD2 1 
ATOM   1083 N NE1 . TRP A 1 136 ? 14.197 -19.121 6.298   1.00 27.88 ? 136 TRP A NE1 1 
ATOM   1084 C CE2 . TRP A 1 136 ? 13.904 -17.907 6.859   1.00 27.70 ? 136 TRP A CE2 1 
ATOM   1085 C CE3 . TRP A 1 136 ? 12.778 -15.860 6.231   1.00 27.60 ? 136 TRP A CE3 1 
ATOM   1086 C CZ2 . TRP A 1 136 ? 14.203 -17.406 8.125   1.00 27.85 ? 136 TRP A CZ2 1 
ATOM   1087 C CZ3 . TRP A 1 136 ? 13.072 -15.366 7.483   1.00 27.41 ? 136 TRP A CZ3 1 
ATOM   1088 C CH2 . TRP A 1 136 ? 13.772 -16.131 8.417   1.00 27.67 ? 136 TRP A CH2 1 
ATOM   1089 N N   . TRP A 1 137 ? 14.960 -15.528 3.260   1.00 24.58 ? 137 TRP A N   1 
ATOM   1090 C CA  . TRP A 1 137 ? 15.563 -14.218 3.454   1.00 23.26 ? 137 TRP A CA  1 
ATOM   1091 C C   . TRP A 1 137 ? 16.819 -14.057 2.596   1.00 22.81 ? 137 TRP A C   1 
ATOM   1092 O O   . TRP A 1 137 ? 17.120 -12.952 2.157   1.00 22.95 ? 137 TRP A O   1 
ATOM   1093 C CB  . TRP A 1 137 ? 15.856 -13.964 4.941   1.00 22.14 ? 137 TRP A CB  1 
ATOM   1094 C CG  . TRP A 1 137 ? 16.938 -14.829 5.533   1.00 21.43 ? 137 TRP A CG  1 
ATOM   1095 C CD1 . TRP A 1 137 ? 16.779 -16.025 6.166   1.00 21.28 ? 137 TRP A CD1 1 
ATOM   1096 C CD2 . TRP A 1 137 ? 18.352 -14.551 5.558   1.00 20.79 ? 137 TRP A CD2 1 
ATOM   1097 N NE1 . TRP A 1 137 ? 17.987 -16.516 6.576   1.00 21.16 ? 137 TRP A NE1 1 
ATOM   1098 C CE2 . TRP A 1 137 ? 18.972 -15.635 6.218   1.00 21.36 ? 137 TRP A CE2 1 
ATOM   1099 C CE3 . TRP A 1 137 ? 19.147 -13.502 5.087   1.00 20.65 ? 137 TRP A CE3 1 
ATOM   1100 C CZ2 . TRP A 1 137 ? 20.350 -15.690 6.420   1.00 21.10 ? 137 TRP A CZ2 1 
ATOM   1101 C CZ3 . TRP A 1 137 ? 20.508 -13.563 5.276   1.00 20.91 ? 137 TRP A CZ3 1 
ATOM   1102 C CH2 . TRP A 1 137 ? 21.098 -14.638 5.939   1.00 21.02 ? 137 TRP A CH2 1 
ATOM   1103 N N   . LEU A 1 138 ? 17.541 -15.159 2.356   1.00 22.82 ? 138 LEU A N   1 
ATOM   1104 C CA  . LEU A 1 138 ? 18.872 -15.101 1.772   1.00 22.59 ? 138 LEU A CA  1 
ATOM   1105 C C   . LEU A 1 138 ? 18.827 -14.698 0.298   1.00 22.25 ? 138 LEU A C   1 
ATOM   1106 O O   . LEU A 1 138 ? 19.718 -13.992 -0.168  1.00 20.98 ? 138 LEU A O   1 
ATOM   1107 C CB  . LEU A 1 138 ? 19.572 -16.447 1.937   1.00 22.93 ? 138 LEU A CB  1 
ATOM   1108 C CG  . LEU A 1 138 ? 21.042 -16.481 1.507   1.00 23.35 ? 138 LEU A CG  1 
ATOM   1109 C CD1 . LEU A 1 138 ? 21.855 -15.496 2.328   1.00 23.51 ? 138 LEU A CD1 1 
ATOM   1110 C CD2 . LEU A 1 138 ? 21.622 -17.877 1.628   1.00 23.64 ? 138 LEU A CD2 1 
ATOM   1111 N N   . GLU A 1 139 ? 17.819 -15.181 -0.438  1.00 23.14 ? 139 GLU A N   1 
ATOM   1112 C CA  . GLU A 1 139 ? 17.716 -14.913 -1.864  1.00 24.14 ? 139 GLU A CA  1 
ATOM   1113 C C   . GLU A 1 139 ? 17.682 -13.409 -2.123  1.00 22.67 ? 139 GLU A C   1 
ATOM   1114 O O   . GLU A 1 139 ? 18.344 -12.929 -3.040  1.00 22.81 ? 139 GLU A O   1 
ATOM   1115 C CB  . GLU A 1 139 ? 16.477 -15.559 -2.485  1.00 26.12 ? 139 GLU A CB  1 
ATOM   1116 C CG  . GLU A 1 139 ? 16.691 -17.013 -2.894  1.00 28.13 ? 139 GLU A CG  1 
ATOM   1117 C CD  . GLU A 1 139 ? 17.233 -17.183 -4.303  1.00 29.91 ? 139 GLU A CD  1 
ATOM   1118 O OE1 . GLU A 1 139 ? 18.194 -16.467 -4.658  1.00 32.58 ? 139 GLU A OE1 1 
ATOM   1119 O OE2 . GLU A 1 139 ? 16.703 -18.041 -5.041  1.00 30.34 ? 139 GLU A OE2 1 
ATOM   1120 N N   . ASP A 1 140 ? 16.878 -12.691 -1.331  1.00 21.86 ? 140 ASP A N   1 
ATOM   1121 C CA  . ASP A 1 140 ? 16.686 -11.261 -1.511  1.00 21.00 ? 140 ASP A CA  1 
ATOM   1122 C C   . ASP A 1 140 ? 17.928 -10.515 -1.031  1.00 19.70 ? 140 ASP A C   1 
ATOM   1123 O O   . ASP A 1 140 ? 18.357 -9.562  -1.673  1.00 18.96 ? 140 ASP A O   1 
ATOM   1124 C CB  . ASP A 1 140 ? 15.429 -10.767 -0.810  1.00 21.25 ? 140 ASP A CB  1 
ATOM   1125 C CG  . ASP A 1 140 ? 14.109 -11.308 -1.345  1.00 21.42 ? 140 ASP A CG  1 
ATOM   1126 O OD1 . ASP A 1 140 ? 13.912 -11.269 -2.577  1.00 22.15 ? 140 ASP A OD1 1 
ATOM   1127 O OD2 . ASP A 1 140 ? 13.277 -11.744 -0.523  1.00 21.11 ? 140 ASP A OD2 1 
ATOM   1128 N N   . TYR A 1 141 ? 18.494 -10.955 0.101   1.00 19.35 ? 141 TYR A N   1 
ATOM   1129 C CA  . TYR A 1 141 ? 19.646 -10.280 0.676   1.00 19.02 ? 141 TYR A CA  1 
ATOM   1130 C C   . TYR A 1 141 ? 20.787 -10.294 -0.337  1.00 19.87 ? 141 TYR A C   1 
ATOM   1131 O O   . TYR A 1 141 ? 21.305 -9.239  -0.689  1.00 19.98 ? 141 TYR A O   1 
ATOM   1132 C CB  . TYR A 1 141 ? 20.135 -10.877 1.998   1.00 18.09 ? 141 TYR A CB  1 
ATOM   1133 C CG  . TYR A 1 141 ? 21.519 -10.369 2.377   1.00 16.79 ? 141 TYR A CG  1 
ATOM   1134 C CD1 . TYR A 1 141 ? 21.708 -9.056  2.793   1.00 16.41 ? 141 TYR A CD1 1 
ATOM   1135 C CD2 . TYR A 1 141 ? 22.641 -11.185 2.276   1.00 16.23 ? 141 TYR A CD2 1 
ATOM   1136 C CE1 . TYR A 1 141 ? 22.966 -8.575  3.115   1.00 16.21 ? 141 TYR A CE1 1 
ATOM   1137 C CE2 . TYR A 1 141 ? 23.904 -10.717 2.601   1.00 15.81 ? 141 TYR A CE2 1 
ATOM   1138 C CZ  . TYR A 1 141 ? 24.066 -9.410  3.029   1.00 15.98 ? 141 TYR A CZ  1 
ATOM   1139 O OH  . TYR A 1 141 ? 25.304 -8.932  3.352   1.00 15.68 ? 141 TYR A OH  1 
ATOM   1140 N N   . ALA A 1 142 ? 21.139 -11.500 -0.801  1.00 21.33 ? 142 ALA A N   1 
ATOM   1141 C CA  . ALA A 1 142 ? 22.241 -11.723 -1.726  1.00 21.76 ? 142 ALA A CA  1 
ATOM   1142 C C   . ALA A 1 142 ? 22.085 -10.893 -3.000  1.00 21.88 ? 142 ALA A C   1 
ATOM   1143 O O   . ALA A 1 142 ? 23.072 -10.381 -3.525  1.00 21.40 ? 142 ALA A O   1 
ATOM   1144 C CB  . ALA A 1 142 ? 22.323 -13.195 -2.055  1.00 22.11 ? 142 ALA A CB  1 
ATOM   1145 N N   . LEU A 1 143 ? 20.844 -10.786 -3.492  1.00 22.16 ? 143 LEU A N   1 
ATOM   1146 C CA  . LEU A 1 143 ? 20.546 -10.048 -4.709  1.00 21.93 ? 143 LEU A CA  1 
ATOM   1147 C C   . LEU A 1 143 ? 20.588 -8.547  -4.422  1.00 21.91 ? 143 LEU A C   1 
ATOM   1148 O O   . LEU A 1 143 ? 21.081 -7.772  -5.236  1.00 23.09 ? 143 LEU A O   1 
ATOM   1149 C CB  . LEU A 1 143 ? 19.195 -10.504 -5.266  1.00 21.77 ? 143 LEU A CB  1 
ATOM   1150 C CG  . LEU A 1 143 ? 18.794 -9.952  -6.640  1.00 22.05 ? 143 LEU A CG  1 
ATOM   1151 C CD1 . LEU A 1 143 ? 19.864 -10.194 -7.698  1.00 22.11 ? 143 LEU A CD1 1 
ATOM   1152 C CD2 . LEU A 1 143 ? 17.471 -10.551 -7.095  1.00 22.02 ? 143 LEU A CD2 1 
ATOM   1153 N N   . PHE A 1 144 ? 20.094 -8.137  -3.248  1.00 22.03 ? 144 PHE A N   1 
ATOM   1154 C CA  . PHE A 1 144 ? 20.109 -6.735  -2.862  1.00 21.18 ? 144 PHE A CA  1 
ATOM   1155 C C   . PHE A 1 144 ? 21.551 -6.229  -2.829  1.00 20.97 ? 144 PHE A C   1 
ATOM   1156 O O   . PHE A 1 144 ? 21.830 -5.121  -3.282  1.00 20.41 ? 144 PHE A O   1 
ATOM   1157 C CB  . PHE A 1 144 ? 19.404 -6.556  -1.514  1.00 21.28 ? 144 PHE A CB  1 
ATOM   1158 C CG  . PHE A 1 144 ? 19.386 -5.130  -0.980  1.00 21.27 ? 144 PHE A CG  1 
ATOM   1159 C CD1 . PHE A 1 144 ? 18.403 -4.230  -1.384  1.00 21.41 ? 144 PHE A CD1 1 
ATOM   1160 C CD2 . PHE A 1 144 ? 20.346 -4.694  -0.072  1.00 21.58 ? 144 PHE A CD2 1 
ATOM   1161 C CE1 . PHE A 1 144 ? 18.385 -2.934  -0.892  1.00 21.25 ? 144 PHE A CE1 1 
ATOM   1162 C CE2 . PHE A 1 144 ? 20.323 -3.393  0.414   1.00 21.36 ? 144 PHE A CE2 1 
ATOM   1163 C CZ  . PHE A 1 144 ? 19.341 -2.519  0.007   1.00 20.81 ? 144 PHE A CZ  1 
ATOM   1164 N N   . MET A 1 145 ? 22.461 -7.046  -2.290  1.00 20.52 ? 145 MET A N   1 
ATOM   1165 C CA  . MET A 1 145 ? 23.860 -6.663  -2.189  1.00 20.90 ? 145 MET A CA  1 
ATOM   1166 C C   . MET A 1 145 ? 24.495 -6.620  -3.579  1.00 21.28 ? 145 MET A C   1 
ATOM   1167 O O   . MET A 1 145 ? 25.249 -5.697  -3.881  1.00 21.93 ? 145 MET A O   1 
ATOM   1168 C CB  . MET A 1 145 ? 24.632 -7.630  -1.282  1.00 20.73 ? 145 MET A CB  1 
ATOM   1169 C CG  . MET A 1 145 ? 24.181 -7.612  0.173   1.00 20.28 ? 145 MET A CG  1 
ATOM   1170 S SD  . MET A 1 145 ? 24.514 -6.067  1.047   1.00 19.87 ? 145 MET A SD  1 
ATOM   1171 C CE  . MET A 1 145 ? 26.306 -6.152  1.176   1.00 19.72 ? 145 MET A CE  1 
ATOM   1172 N N   . ALA A 1 146 ? 24.180 -7.621  -4.413  1.00 21.55 ? 146 ALA A N   1 
ATOM   1173 C CA  . ALA A 1 146 ? 24.737 -7.732  -5.753  1.00 22.07 ? 146 ALA A CA  1 
ATOM   1174 C C   . ALA A 1 146 ? 24.274 -6.560  -6.616  1.00 22.44 ? 146 ALA A C   1 
ATOM   1175 O O   . ALA A 1 146 ? 25.068 -5.965  -7.342  1.00 22.25 ? 146 ALA A O   1 
ATOM   1176 C CB  . ALA A 1 146 ? 24.339 -9.060  -6.362  1.00 22.44 ? 146 ALA A CB  1 
ATOM   1177 N N   . LEU A 1 147 ? 22.980 -6.239  -6.522  1.00 23.17 ? 147 LEU A N   1 
ATOM   1178 C CA  . LEU A 1 147 ? 22.408 -5.108  -7.231  1.00 23.94 ? 147 LEU A CA  1 
ATOM   1179 C C   . LEU A 1 147 ? 23.031 -3.806  -6.734  1.00 24.22 ? 147 LEU A C   1 
ATOM   1180 O O   . LEU A 1 147 ? 23.268 -2.899  -7.528  1.00 23.82 ? 147 LEU A O   1 
ATOM   1181 C CB  . LEU A 1 147 ? 20.891 -5.116  -7.050  1.00 24.46 ? 147 LEU A CB  1 
ATOM   1182 C CG  . LEU A 1 147 ? 20.147 -6.237  -7.781  1.00 25.46 ? 147 LEU A CG  1 
ATOM   1183 C CD1 . LEU A 1 147 ? 18.707 -6.317  -7.316  1.00 25.87 ? 147 LEU A CD1 1 
ATOM   1184 C CD2 . LEU A 1 147 ? 20.219 -6.046  -9.287  1.00 25.91 ? 147 LEU A CD2 1 
ATOM   1185 N N   . LYS A 1 148 ? 23.308 -3.732  -5.426  1.00 24.92 ? 148 LYS A N   1 
ATOM   1186 C CA  . LYS A 1 148 ? 23.832 -2.517  -4.821  1.00 25.57 ? 148 LYS A CA  1 
ATOM   1187 C C   . LYS A 1 148 ? 25.206 -2.185  -5.401  1.00 25.36 ? 148 LYS A C   1 
ATOM   1188 O O   . LYS A 1 148 ? 25.463 -1.038  -5.757  1.00 25.74 ? 148 LYS A O   1 
ATOM   1189 C CB  . LYS A 1 148 ? 23.898 -2.620  -3.291  1.00 26.00 ? 148 LYS A CB  1 
ATOM   1190 C CG  . LYS A 1 148 ? 24.225 -1.298  -2.611  1.00 26.42 ? 148 LYS A CG  1 
ATOM   1191 C CD  . LYS A 1 148 ? 23.922 -1.242  -1.118  1.00 26.86 ? 148 LYS A CD  1 
ATOM   1192 C CE  . LYS A 1 148 ? 23.982 0.159   -0.601  1.00 26.84 ? 148 LYS A CE  1 
ATOM   1193 N NZ  . LYS A 1 148 ? 22.894 0.998   -1.108  1.00 26.65 ? 148 LYS A NZ  1 
ATOM   1194 N N   . GLY A 1 149 ? 26.084 -3.190  -5.477  1.00 25.99 ? 149 GLY A N   1 
ATOM   1195 C CA  . GLY A 1 149 ? 27.408 -3.018  -6.055  1.00 26.22 ? 149 GLY A CA  1 
ATOM   1196 C C   . GLY A 1 149 ? 27.333 -2.678  -7.542  1.00 26.01 ? 149 GLY A C   1 
ATOM   1197 O O   . GLY A 1 149 ? 28.069 -1.819  -8.026  1.00 26.07 ? 149 GLY A O   1 
ATOM   1198 N N   . ALA A 1 150 ? 26.432 -3.366  -8.252  1.00 25.88 ? 150 ALA A N   1 
ATOM   1199 C CA  . ALA A 1 150 ? 26.210 -3.138  -9.670  1.00 26.24 ? 150 ALA A CA  1 
ATOM   1200 C C   . ALA A 1 150 ? 25.634 -1.742  -9.909  1.00 26.87 ? 150 ALA A C   1 
ATOM   1201 O O   . ALA A 1 150 ? 25.930 -1.122  -10.930 1.00 25.73 ? 150 ALA A O   1 
ATOM   1202 C CB  . ALA A 1 150 ? 25.302 -4.220  -10.216 1.00 26.35 ? 150 ALA A CB  1 
ATOM   1203 N N   . HIS A 1 151 ? 24.814 -1.255  -8.964  1.00 28.14 ? 151 HIS A N   1 
ATOM   1204 C CA  . HIS A 1 151 ? 24.210 0.067   -9.067  1.00 29.22 ? 151 HIS A CA  1 
ATOM   1205 C C   . HIS A 1 151 ? 24.999 1.084   -8.242  1.00 29.36 ? 151 HIS A C   1 
ATOM   1206 O O   . HIS A 1 151 ? 24.479 2.147   -7.906  1.00 28.32 ? 151 HIS A O   1 
ATOM   1207 C CB  . HIS A 1 151 ? 22.729 0.022   -8.672  1.00 30.78 ? 151 HIS A CB  1 
ATOM   1208 C CG  . HIS A 1 151 ? 21.891 -0.759  -9.624  1.00 32.07 ? 151 HIS A CG  1 
ATOM   1209 N ND1 . HIS A 1 151 ? 21.775 -2.126  -9.522  1.00 33.12 ? 151 HIS A ND1 1 
ATOM   1210 C CD2 . HIS A 1 151 ? 21.157 -0.401  -10.689 1.00 33.31 ? 151 HIS A CD2 1 
ATOM   1211 C CE1 . HIS A 1 151 ? 20.988 -2.568  -10.489 1.00 33.14 ? 151 HIS A CE1 1 
ATOM   1212 N NE2 . HIS A 1 151 ? 20.599 -1.540  -11.212 1.00 32.89 ? 151 HIS A NE2 1 
ATOM   1213 N N   . GLY A 1 152 ? 26.249 0.739   -7.908  1.00 30.10 ? 152 GLY A N   1 
ATOM   1214 C CA  . GLY A 1 152 ? 27.233 1.702   -7.439  1.00 31.01 ? 152 GLY A CA  1 
ATOM   1215 C C   . GLY A 1 152 ? 26.932 2.241   -6.043  1.00 31.79 ? 152 GLY A C   1 
ATOM   1216 O O   . GLY A 1 152 ? 27.294 3.375   -5.736  1.00 33.73 ? 152 GLY A O   1 
ATOM   1217 N N   . GLY A 1 153 ? 26.273 1.429   -5.209  1.00 31.93 ? 153 GLY A N   1 
ATOM   1218 C CA  . GLY A 1 153 ? 25.977 1.806   -3.836  1.00 32.85 ? 153 GLY A CA  1 
ATOM   1219 C C   . GLY A 1 153 ? 24.709 2.653   -3.718  1.00 33.81 ? 153 GLY A C   1 
ATOM   1220 O O   . GLY A 1 153 ? 24.342 3.058   -2.617  1.00 33.11 ? 153 GLY A O   1 
ATOM   1221 N N   . LEU A 1 154 ? 24.033 2.910   -4.846  1.00 35.01 ? 154 LEU A N   1 
ATOM   1222 C CA  . LEU A 1 154 ? 22.793 3.667   -4.825  1.00 35.97 ? 154 LEU A CA  1 
ATOM   1223 C C   . LEU A 1 154 ? 21.768 2.901   -3.992  1.00 36.34 ? 154 LEU A C   1 
ATOM   1224 O O   . LEU A 1 154 ? 21.746 1.671   -4.003  1.00 37.13 ? 154 LEU A O   1 
ATOM   1225 C CB  . LEU A 1 154 ? 22.259 3.941   -6.232  1.00 36.93 ? 154 LEU A CB  1 
ATOM   1226 C CG  . LEU A 1 154 ? 23.052 4.927   -7.098  1.00 38.04 ? 154 LEU A CG  1 
ATOM   1227 C CD1 . LEU A 1 154 ? 22.232 5.268   -8.330  1.00 38.46 ? 154 LEU A CD1 1 
ATOM   1228 C CD2 . LEU A 1 154 ? 23.456 6.197   -6.367  1.00 38.59 ? 154 LEU A CD2 1 
ATOM   1229 N N   . PRO A 1 155 ? 20.902 3.600   -3.223  1.00 36.50 ? 155 PRO A N   1 
ATOM   1230 C CA  . PRO A 1 155 ? 19.776 2.945   -2.568  1.00 36.52 ? 155 PRO A CA  1 
ATOM   1231 C C   . PRO A 1 155 ? 18.829 2.287   -3.567  1.00 35.73 ? 155 PRO A C   1 
ATOM   1232 O O   . PRO A 1 155 ? 18.786 2.678   -4.731  1.00 36.40 ? 155 PRO A O   1 
ATOM   1233 C CB  . PRO A 1 155 ? 19.102 4.070   -1.781  1.00 36.66 ? 155 PRO A CB  1 
ATOM   1234 C CG  . PRO A 1 155 ? 20.152 5.163   -1.692  1.00 36.65 ? 155 PRO A CG  1 
ATOM   1235 C CD  . PRO A 1 155 ? 20.988 5.038   -2.924  1.00 36.39 ? 155 PRO A CD  1 
ATOM   1236 N N   . TRP A 1 156 ? 18.072 1.289   -3.099  1.00 34.40 ? 156 TRP A N   1 
ATOM   1237 C CA  . TRP A 1 156 ? 17.125 0.579   -3.945  1.00 33.20 ? 156 TRP A CA  1 
ATOM   1238 C C   . TRP A 1 156 ? 16.041 1.530   -4.450  1.00 34.12 ? 156 TRP A C   1 
ATOM   1239 O O   . TRP A 1 156 ? 15.464 1.307   -5.511  1.00 33.75 ? 156 TRP A O   1 
ATOM   1240 C CB  . TRP A 1 156 ? 16.508 -0.604  -3.189  1.00 31.03 ? 156 TRP A CB  1 
ATOM   1241 C CG  . TRP A 1 156 ? 15.544 -0.185  -2.112  1.00 29.46 ? 156 TRP A CG  1 
ATOM   1242 C CD1 . TRP A 1 156 ? 15.839 0.100   -0.812  1.00 28.86 ? 156 TRP A CD1 1 
ATOM   1243 C CD2 . TRP A 1 156 ? 14.122 0.019   -2.258  1.00 28.50 ? 156 TRP A CD2 1 
ATOM   1244 N NE1 . TRP A 1 156 ? 14.704 0.458   -0.136  1.00 28.73 ? 156 TRP A NE1 1 
ATOM   1245 C CE2 . TRP A 1 156 ? 13.636 0.421   -0.994  1.00 27.94 ? 156 TRP A CE2 1 
ATOM   1246 C CE3 . TRP A 1 156 ? 13.219 -0.100  -3.322  1.00 27.41 ? 156 TRP A CE3 1 
ATOM   1247 C CZ2 . TRP A 1 156 ? 12.289 0.701   -0.773  1.00 26.97 ? 156 TRP A CZ2 1 
ATOM   1248 C CZ3 . TRP A 1 156 ? 11.887 0.175   -3.098  1.00 27.37 ? 156 TRP A CZ3 1 
ATOM   1249 C CH2 . TRP A 1 156 ? 11.431 0.570   -1.840  1.00 27.00 ? 156 TRP A CH2 1 
ATOM   1250 N N   . ASN A 1 157 ? 15.770 2.584   -3.671  1.00 35.45 ? 157 ASN A N   1 
ATOM   1251 C CA  . ASN A 1 157 ? 14.798 3.602   -4.037  1.00 36.87 ? 157 ASN A CA  1 
ATOM   1252 C C   . ASN A 1 157 ? 15.285 4.380   -5.256  1.00 35.75 ? 157 ASN A C   1 
ATOM   1253 O O   . ASN A 1 157 ? 14.485 5.000   -5.950  1.00 36.10 ? 157 ASN A O   1 
ATOM   1254 C CB  . ASN A 1 157 ? 14.544 4.589   -2.903  1.00 38.65 ? 157 ASN A CB  1 
ATOM   1255 C CG  . ASN A 1 157 ? 14.387 3.914   -1.561  1.00 39.63 ? 157 ASN A CG  1 
ATOM   1256 O OD1 . ASN A 1 157 ? 15.319 3.254   -1.087  1.00 42.90 ? 157 ASN A OD1 1 
ATOM   1257 N ND2 . ASN A 1 157 ? 13.235 4.073   -0.925  1.00 39.36 ? 157 ASN A ND2 1 
ATOM   1258 N N   . ARG A 1 158 ? 16.605 4.369   -5.479  1.00 36.09 ? 158 ARG A N   1 
ATOM   1259 C CA  . ARG A 1 158 ? 17.228 5.109   -6.563  1.00 36.74 ? 158 ARG A CA  1 
ATOM   1260 C C   . ARG A 1 158 ? 17.519 4.189   -7.751  1.00 35.21 ? 158 ARG A C   1 
ATOM   1261 O O   . ARG A 1 158 ? 18.101 4.639   -8.733  1.00 35.22 ? 158 ARG A O   1 
ATOM   1262 C CB  . ARG A 1 158 ? 18.496 5.769   -6.004  1.00 37.82 ? 158 ARG A CB  1 
ATOM   1263 C CG  . ARG A 1 158 ? 18.241 6.673   -4.804  1.00 39.29 ? 158 ARG A CG  1 
ATOM   1264 C CD  . ARG A 1 158 ? 18.495 8.151   -5.057  1.00 40.47 ? 158 ARG A CD  1 
ATOM   1265 N NE  . ARG A 1 158 ? 19.920 8.479   -4.922  1.00 41.48 ? 158 ARG A NE  1 
ATOM   1266 C CZ  . ARG A 1 158 ? 20.654 9.200   -5.769  1.00 42.37 ? 158 ARG A CZ  1 
ATOM   1267 N NH1 . ARG A 1 158 ? 20.102 9.755   -6.833  1.00 43.88 ? 158 ARG A NH1 1 
ATOM   1268 N NH2 . ARG A 1 158 ? 21.944 9.376   -5.543  1.00 41.60 ? 158 ARG A NH2 1 
ATOM   1269 N N   . TRP A 1 159 ? 17.106 2.914   -7.668  1.00 35.61 ? 159 TRP A N   1 
ATOM   1270 C CA  . TRP A 1 159 ? 17.376 1.936   -8.716  1.00 34.92 ? 159 TRP A CA  1 
ATOM   1271 C C   . TRP A 1 159 ? 16.389 2.091   -9.872  1.00 36.40 ? 159 TRP A C   1 
ATOM   1272 O O   . TRP A 1 159 ? 15.367 2.756   -9.730  1.00 37.33 ? 159 TRP A O   1 
ATOM   1273 C CB  . TRP A 1 159 ? 17.315 0.503   -8.167  1.00 33.70 ? 159 TRP A CB  1 
ATOM   1274 C CG  . TRP A 1 159 ? 18.479 0.095   -7.300  1.00 32.98 ? 159 TRP A CG  1 
ATOM   1275 C CD1 . TRP A 1 159 ? 19.672 0.736   -7.145  1.00 32.72 ? 159 TRP A CD1 1 
ATOM   1276 C CD2 . TRP A 1 159 ? 18.553 -1.089  -6.474  1.00 31.90 ? 159 TRP A CD2 1 
ATOM   1277 N NE1 . TRP A 1 159 ? 20.475 0.049   -6.274  1.00 32.42 ? 159 TRP A NE1 1 
ATOM   1278 C CE2 . TRP A 1 159 ? 19.819 -1.075  -5.847  1.00 32.23 ? 159 TRP A CE2 1 
ATOM   1279 C CE3 . TRP A 1 159 ? 17.678 -2.146  -6.199  1.00 31.50 ? 159 TRP A CE3 1 
ATOM   1280 C CZ2 . TRP A 1 159 ? 20.223 -2.077  -4.965  1.00 31.72 ? 159 TRP A CZ2 1 
ATOM   1281 C CZ3 . TRP A 1 159 ? 18.080 -3.136  -5.328  1.00 31.17 ? 159 TRP A CZ3 1 
ATOM   1282 C CH2 . TRP A 1 159 ? 19.335 -3.099  -4.719  1.00 31.27 ? 159 TRP A CH2 1 
ATOM   1283 N N   . PRO A 1 160 ? 16.661 1.478   -11.050 1.00 38.75 ? 160 PRO A N   1 
ATOM   1284 C CA  . PRO A 1 160 ? 15.703 1.454   -12.154 1.00 39.48 ? 160 PRO A CA  1 
ATOM   1285 C C   . PRO A 1 160 ? 14.389 0.755   -11.807 1.00 40.67 ? 160 PRO A C   1 
ATOM   1286 O O   . PRO A 1 160 ? 14.385 -0.243  -11.091 1.00 42.97 ? 160 PRO A O   1 
ATOM   1287 C CB  . PRO A 1 160 ? 16.456 0.738   -13.275 1.00 39.67 ? 160 PRO A CB  1 
ATOM   1288 C CG  . PRO A 1 160 ? 17.919 0.863   -12.887 1.00 39.67 ? 160 PRO A CG  1 
ATOM   1289 C CD  . PRO A 1 160 ? 17.933 0.822   -11.395 1.00 39.19 ? 160 PRO A CD  1 
ATOM   1290 N N   . LEU A 1 161 ? 13.286 1.266   -12.368 1.00 39.93 ? 161 LEU A N   1 
ATOM   1291 C CA  . LEU A 1 161 ? 11.952 1.047   -11.825 1.00 40.37 ? 161 LEU A CA  1 
ATOM   1292 C C   . LEU A 1 161 ? 11.573 -0.434  -11.794 1.00 40.63 ? 161 LEU A C   1 
ATOM   1293 O O   . LEU A 1 161 ? 11.125 -0.913  -10.754 1.00 43.33 ? 161 LEU A O   1 
ATOM   1294 C CB  . LEU A 1 161 ? 10.916 1.882   -12.581 1.00 41.11 ? 161 LEU A CB  1 
ATOM   1295 C CG  . LEU A 1 161 ? 10.922 3.387   -12.292 1.00 40.91 ? 161 LEU A CG  1 
ATOM   1296 C CD1 . LEU A 1 161 ? 9.974  4.109   -13.235 1.00 40.93 ? 161 LEU A CD1 1 
ATOM   1297 C CD2 . LEU A 1 161 ? 10.560 3.696   -10.846 1.00 41.78 ? 161 LEU A CD2 1 
ATOM   1298 N N   . PRO A 1 162 ? 11.700 -1.213  -12.895 1.00 40.15 ? 162 PRO A N   1 
ATOM   1299 C CA  . PRO A 1 162 ? 11.281 -2.613  -12.875 1.00 38.88 ? 162 PRO A CA  1 
ATOM   1300 C C   . PRO A 1 162 ? 11.970 -3.436  -11.786 1.00 38.49 ? 162 PRO A C   1 
ATOM   1301 O O   . PRO A 1 162 ? 11.352 -4.305  -11.172 1.00 37.74 ? 162 PRO A O   1 
ATOM   1302 C CB  . PRO A 1 162 ? 11.612 -3.114  -14.280 1.00 38.74 ? 162 PRO A CB  1 
ATOM   1303 C CG  . PRO A 1 162 ? 11.697 -1.848  -15.115 1.00 38.98 ? 162 PRO A CG  1 
ATOM   1304 C CD  . PRO A 1 162 ? 12.249 -0.804  -14.198 1.00 39.56 ? 162 PRO A CD  1 
ATOM   1305 N N   . LEU A 1 163 ? 13.255 -3.144  -11.556 1.00 36.69 ? 163 LEU A N   1 
ATOM   1306 C CA  . LEU A 1 163 ? 14.028 -3.778  -10.502 1.00 36.53 ? 163 LEU A CA  1 
ATOM   1307 C C   . LEU A 1 163 ? 13.526 -3.319  -9.134  1.00 36.42 ? 163 LEU A C   1 
ATOM   1308 O O   . LEU A 1 163 ? 13.434 -4.117  -8.204  1.00 35.22 ? 163 LEU A O   1 
ATOM   1309 C CB  . LEU A 1 163 ? 15.500 -3.416  -10.687 1.00 36.11 ? 163 LEU A CB  1 
ATOM   1310 C CG  . LEU A 1 163 ? 16.480 -4.096  -9.726  1.00 36.40 ? 163 LEU A CG  1 
ATOM   1311 C CD1 . LEU A 1 163 ? 16.772 -5.512  -10.191 1.00 36.89 ? 163 LEU A CD1 1 
ATOM   1312 C CD2 . LEU A 1 163 ? 17.747 -3.275  -9.582  1.00 37.04 ? 163 LEU A CD2 1 
ATOM   1313 N N   . ARG A 1 164 ? 13.233 -2.019  -9.024  1.00 37.27 ? 164 ARG A N   1 
ATOM   1314 C CA  . ARG A 1 164 ? 12.793 -1.420  -7.773  1.00 38.18 ? 164 ARG A CA  1 
ATOM   1315 C C   . ARG A 1 164 ? 11.449 -2.017  -7.358  1.00 38.83 ? 164 ARG A C   1 
ATOM   1316 O O   . ARG A 1 164 ? 11.224 -2.279  -6.178  1.00 38.27 ? 164 ARG A O   1 
ATOM   1317 C CB  . ARG A 1 164 ? 12.718 0.100   -7.948  1.00 38.45 ? 164 ARG A CB  1 
ATOM   1318 C CG  . ARG A 1 164 ? 12.522 0.886   -6.658  1.00 39.17 ? 164 ARG A CG  1 
ATOM   1319 C CD  . ARG A 1 164 ? 12.206 2.352   -6.912  1.00 39.62 ? 164 ARG A CD  1 
ATOM   1320 N NE  . ARG A 1 164 ? 13.159 3.028   -7.799  1.00 40.20 ? 164 ARG A NE  1 
ATOM   1321 C CZ  . ARG A 1 164 ? 13.009 4.261   -8.281  1.00 40.58 ? 164 ARG A CZ  1 
ATOM   1322 N NH1 . ARG A 1 164 ? 11.977 5.005   -7.917  1.00 40.39 ? 164 ARG A NH1 1 
ATOM   1323 N NH2 . ARG A 1 164 ? 13.907 4.757   -9.115  1.00 41.07 ? 164 ARG A NH2 1 
ATOM   1324 N N   . LYS A 1 165 ? 10.576 -2.240  -8.349  1.00 38.92 ? 165 LYS A N   1 
ATOM   1325 C CA  . LYS A 1 165 ? 9.226  -2.733  -8.123  1.00 39.98 ? 165 LYS A CA  1 
ATOM   1326 C C   . LYS A 1 165 ? 9.207  -4.261  -8.074  1.00 38.68 ? 165 LYS A C   1 
ATOM   1327 O O   . LYS A 1 165 ? 8.188  -4.846  -7.715  1.00 39.51 ? 165 LYS A O   1 
ATOM   1328 C CB  . LYS A 1 165 ? 8.315  -2.202  -9.236  1.00 41.29 ? 165 LYS A CB  1 
ATOM   1329 C CG  . LYS A 1 165 ? 8.208  -0.683  -9.295  1.00 43.00 ? 165 LYS A CG  1 
ATOM   1330 C CD  . LYS A 1 165 ? 7.625  -0.140  -10.594 1.00 44.48 ? 165 LYS A CD  1 
ATOM   1331 C CE  . LYS A 1 165 ? 7.423  1.343   -10.540 1.00 45.92 ? 165 LYS A CE  1 
ATOM   1332 N NZ  . LYS A 1 165 ? 6.939  1.898   -11.808 1.00 45.47 ? 165 LYS A NZ  1 
ATOM   1333 N N   . ARG A 1 166 ? 10.329 -4.890  -8.456  1.00 37.97 ? 166 ARG A N   1 
ATOM   1334 C CA  . ARG A 1 166 ? 10.534 -6.327  -8.335  1.00 37.45 ? 166 ARG A CA  1 
ATOM   1335 C C   . ARG A 1 166 ? 9.627  -7.086  -9.305  1.00 37.73 ? 166 ARG A C   1 
ATOM   1336 O O   . ARG A 1 166 ? 8.985  -8.063  -8.927  1.00 38.66 ? 166 ARG A O   1 
ATOM   1337 C CB  . ARG A 1 166 ? 10.359 -6.795  -6.883  1.00 36.44 ? 166 ARG A CB  1 
ATOM   1338 C CG  . ARG A 1 166 ? 11.449 -6.304  -5.941  1.00 35.77 ? 166 ARG A CG  1 
ATOM   1339 C CD  . ARG A 1 166 ? 11.129 -6.648  -4.499  1.00 34.53 ? 166 ARG A CD  1 
ATOM   1340 N NE  . ARG A 1 166 ? 10.972 -8.088  -4.269  1.00 33.17 ? 166 ARG A NE  1 
ATOM   1341 C CZ  . ARG A 1 166 ? 11.960 -8.978  -4.215  1.00 32.73 ? 166 ARG A CZ  1 
ATOM   1342 N NH1 . ARG A 1 166 ? 13.217 -8.600  -4.376  1.00 32.78 ? 166 ARG A NH1 1 
ATOM   1343 N NH2 . ARG A 1 166 ? 11.690 -10.251 -3.986  1.00 31.90 ? 166 ARG A NH2 1 
ATOM   1344 N N   . GLU A 1 167 ? 9.607  -6.641  -10.567 1.00 38.75 ? 167 GLU A N   1 
ATOM   1345 C CA  . GLU A 1 167 ? 8.929  -7.360  -11.635 1.00 38.89 ? 167 GLU A CA  1 
ATOM   1346 C C   . GLU A 1 167 ? 9.690  -8.657  -11.903 1.00 39.23 ? 167 GLU A C   1 
ATOM   1347 O O   . GLU A 1 167 ? 10.919 -8.652  -11.936 1.00 38.58 ? 167 GLU A O   1 
ATOM   1348 C CB  . GLU A 1 167 ? 8.847  -6.496  -12.894 1.00 40.19 ? 167 GLU A CB  1 
ATOM   1349 C CG  . GLU A 1 167 ? 8.048  -5.208  -12.703 1.00 41.48 ? 167 GLU A CG  1 
ATOM   1350 C CD  . GLU A 1 167 ? 8.011  -4.302  -13.922 1.00 42.48 ? 167 GLU A CD  1 
ATOM   1351 O OE1 . GLU A 1 167 ? 8.623  -4.662  -14.950 1.00 43.91 ? 167 GLU A OE1 1 
ATOM   1352 O OE2 . GLU A 1 167 ? 7.373  -3.230  -13.842 1.00 43.09 ? 167 GLU A OE2 1 
ATOM   1353 N N   . GLU A 1 168 ? 8.945  -9.752  -12.113 1.00 38.34 ? 168 GLU A N   1 
ATOM   1354 C CA  . GLU A 1 168 ? 9.495  -11.099 -12.055 1.00 37.88 ? 168 GLU A CA  1 
ATOM   1355 C C   . GLU A 1 168 ? 10.579 -11.305 -13.114 1.00 37.66 ? 168 GLU A C   1 
ATOM   1356 O O   . GLU A 1 168 ? 11.582 -11.962 -12.847 1.00 37.18 ? 168 GLU A O   1 
ATOM   1357 C CB  . GLU A 1 168 ? 8.407  -12.165 -12.201 1.00 37.77 ? 168 GLU A CB  1 
ATOM   1358 C CG  . GLU A 1 168 ? 7.723  -12.190 -13.566 1.00 37.33 ? 168 GLU A CG  1 
ATOM   1359 C CD  . GLU A 1 168 ? 7.028  -13.499 -13.891 1.00 37.25 ? 168 GLU A CD  1 
ATOM   1360 O OE1 . GLU A 1 168 ? 5.850  -13.460 -14.307 1.00 37.33 ? 168 GLU A OE1 1 
ATOM   1361 O OE2 . GLU A 1 168 ? 7.669  -14.558 -13.733 1.00 37.17 ? 168 GLU A OE2 1 
ATOM   1362 N N   . GLN A 1 169 ? 10.358 -10.756 -14.314 1.00 37.63 ? 169 GLN A N   1 
ATOM   1363 C CA  . GLN A 1 169 ? 11.277 -10.924 -15.427 1.00 37.89 ? 169 GLN A CA  1 
ATOM   1364 C C   . GLN A 1 169 ? 12.601 -10.250 -15.070 1.00 38.04 ? 169 GLN A C   1 
ATOM   1365 O O   . GLN A 1 169 ? 13.666 -10.834 -15.258 1.00 37.80 ? 169 GLN A O   1 
ATOM   1366 C CB  . GLN A 1 169 ? 10.623 -10.351 -16.687 1.00 38.78 ? 169 GLN A CB  1 
ATOM   1367 C CG  . GLN A 1 169 ? 11.478 -10.424 -17.950 1.00 39.76 ? 169 GLN A CG  1 
ATOM   1368 C CD  . GLN A 1 169 ? 11.350 -11.723 -18.719 1.00 40.06 ? 169 GLN A CD  1 
ATOM   1369 O OE1 . GLN A 1 169 ? 10.697 -12.679 -18.286 1.00 39.58 ? 169 GLN A OE1 1 
ATOM   1370 N NE2 . GLN A 1 169 ? 11.982 -11.765 -19.884 1.00 40.85 ? 169 GLN A NE2 1 
ATOM   1371 N N   . ALA A 1 170 ? 12.511 -9.026  -14.532 1.00 36.82 ? 170 ALA A N   1 
ATOM   1372 C CA  . ALA A 1 170 ? 13.677 -8.249  -14.141 1.00 36.62 ? 170 ALA A CA  1 
ATOM   1373 C C   . ALA A 1 170 ? 14.451 -8.950  -13.026 1.00 35.61 ? 170 ALA A C   1 
ATOM   1374 O O   . ALA A 1 170 ? 15.679 -8.908  -13.015 1.00 35.15 ? 170 ALA A O   1 
ATOM   1375 C CB  . ALA A 1 170 ? 13.253 -6.859  -13.720 1.00 36.02 ? 170 ALA A CB  1 
ATOM   1376 N N   . LEU A 1 171 ? 13.722 -9.572  -12.087 1.00 36.49 ? 171 LEU A N   1 
ATOM   1377 C CA  . LEU A 1 171 ? 14.324 -10.278 -10.965 1.00 36.43 ? 171 LEU A CA  1 
ATOM   1378 C C   . LEU A 1 171 ? 15.108 -11.485 -11.470 1.00 35.63 ? 171 LEU A C   1 
ATOM   1379 O O   . LEU A 1 171 ? 16.216 -11.751 -11.006 1.00 36.13 ? 171 LEU A O   1 
ATOM   1380 C CB  . LEU A 1 171 ? 13.255 -10.716 -9.963  1.00 37.10 ? 171 LEU A CB  1 
ATOM   1381 C CG  . LEU A 1 171 ? 12.611 -9.616  -9.111  1.00 38.03 ? 171 LEU A CG  1 
ATOM   1382 C CD1 . LEU A 1 171 ? 11.702 -10.257 -8.078  1.00 37.33 ? 171 LEU A CD1 1 
ATOM   1383 C CD2 . LEU A 1 171 ? 13.635 -8.713  -8.436  1.00 38.29 ? 171 LEU A CD2 1 
ATOM   1384 N N   . ARG A 1 172 ? 14.491 -12.223 -12.396 1.00 35.56 ? 172 ARG A N   1 
ATOM   1385 C CA  . ARG A 1 172 ? 15.070 -13.421 -12.982 1.00 35.67 ? 172 ARG A CA  1 
ATOM   1386 C C   . ARG A 1 172 ? 16.359 -13.064 -13.719 1.00 33.99 ? 172 ARG A C   1 
ATOM   1387 O O   . ARG A 1 172 ? 17.385 -13.711 -13.523 1.00 33.58 ? 172 ARG A O   1 
ATOM   1388 C CB  . ARG A 1 172 ? 13.991 -14.014 -13.896 1.00 36.59 ? 172 ARG A CB  1 
ATOM   1389 C CG  . ARG A 1 172 ? 14.211 -15.404 -14.471 1.00 37.41 ? 172 ARG A CG  1 
ATOM   1390 C CD  . ARG A 1 172 ? 12.984 -15.770 -15.294 1.00 37.87 ? 172 ARG A CD  1 
ATOM   1391 N NE  . ARG A 1 172 ? 12.982 -17.139 -15.822 1.00 38.31 ? 172 ARG A NE  1 
ATOM   1392 C CZ  . ARG A 1 172 ? 12.002 -17.670 -16.551 1.00 38.21 ? 172 ARG A CZ  1 
ATOM   1393 N NH1 . ARG A 1 172 ? 10.926 -16.959 -16.854 1.00 38.01 ? 172 ARG A NH1 1 
ATOM   1394 N NH2 . ARG A 1 172 ? 12.098 -18.919 -16.975 1.00 38.04 ? 172 ARG A NH2 1 
ATOM   1395 N N   . GLU A 1 173 ? 16.287 -12.018 -14.553 1.00 32.62 ? 173 GLU A N   1 
ATOM   1396 C CA  . GLU A 1 173 ? 17.390 -11.611 -15.411 1.00 33.09 ? 173 GLU A CA  1 
ATOM   1397 C C   . GLU A 1 173 ? 18.538 -11.035 -14.582 1.00 31.41 ? 173 GLU A C   1 
ATOM   1398 O O   . GLU A 1 173 ? 19.700 -11.177 -14.953 1.00 30.46 ? 173 GLU A O   1 
ATOM   1399 C CB  . GLU A 1 173 ? 16.904 -10.585 -16.436 1.00 34.12 ? 173 GLU A CB  1 
ATOM   1400 C CG  . GLU A 1 173 ? 15.976 -11.184 -17.490 1.00 35.42 ? 173 GLU A CG  1 
ATOM   1401 C CD  . GLU A 1 173 ? 15.179 -10.189 -18.318 1.00 36.76 ? 173 GLU A CD  1 
ATOM   1402 O OE1 . GLU A 1 173 ? 15.334 -8.963  -18.137 1.00 36.66 ? 173 GLU A OE1 1 
ATOM   1403 O OE2 . GLU A 1 173 ? 14.390 -10.652 -19.167 1.00 38.59 ? 173 GLU A OE2 1 
ATOM   1404 N N   . ALA A 1 174 ? 18.199 -10.362 -13.478 1.00 31.35 ? 174 ALA A N   1 
ATOM   1405 C CA  . ALA A 1 174 ? 19.196 -9.790  -12.590 1.00 31.19 ? 174 ALA A CA  1 
ATOM   1406 C C   . ALA A 1 174 ? 19.968 -10.905 -11.889 1.00 31.34 ? 174 ALA A C   1 
ATOM   1407 O O   . ALA A 1 174 ? 21.187 -10.826 -11.759 1.00 31.67 ? 174 ALA A O   1 
ATOM   1408 C CB  . ALA A 1 174 ? 18.533 -8.859  -11.599 1.00 31.11 ? 174 ALA A CB  1 
ATOM   1409 N N   . LYS A 1 175 ? 19.248 -11.949 -11.458 1.00 32.12 ? 175 LYS A N   1 
ATOM   1410 C CA  . LYS A 1 175 ? 19.855 -13.069 -10.755 1.00 32.09 ? 175 LYS A CA  1 
ATOM   1411 C C   . LYS A 1 175 ? 20.837 -13.799 -11.673 1.00 30.36 ? 175 LYS A C   1 
ATOM   1412 O O   . LYS A 1 175 ? 21.927 -14.169 -11.241 1.00 28.76 ? 175 LYS A O   1 
ATOM   1413 C CB  . LYS A 1 175 ? 18.806 -14.050 -10.220 1.00 34.22 ? 175 LYS A CB  1 
ATOM   1414 C CG  . LYS A 1 175 ? 19.365 -15.036 -9.196  1.00 36.08 ? 175 LYS A CG  1 
ATOM   1415 C CD  . LYS A 1 175 ? 18.414 -16.131 -8.728  1.00 37.00 ? 175 LYS A CD  1 
ATOM   1416 C CE  . LYS A 1 175 ? 19.129 -17.121 -7.857  1.00 38.44 ? 175 LYS A CE  1 
ATOM   1417 N NZ  . LYS A 1 175 ? 18.279 -18.241 -7.443  1.00 39.98 ? 175 LYS A NZ  1 
ATOM   1418 N N   . SER A 1 176 ? 20.440 -14.006 -12.935 1.00 28.44 ? 176 SER A N   1 
ATOM   1419 C CA  . SER A 1 176 ? 21.293 -14.661 -13.913 1.00 27.19 ? 176 SER A CA  1 
ATOM   1420 C C   . SER A 1 176 ? 22.537 -13.812 -14.176 1.00 25.15 ? 176 SER A C   1 
ATOM   1421 O O   . SER A 1 176 ? 23.630 -14.346 -14.319 1.00 25.17 ? 176 SER A O   1 
ATOM   1422 C CB  . SER A 1 176 ? 20.543 -14.938 -15.194 1.00 28.05 ? 176 SER A CB  1 
ATOM   1423 O OG  . SER A 1 176 ? 19.237 -15.436 -14.937 1.00 29.16 ? 176 SER A OG  1 
ATOM   1424 N N   . ALA A 1 177 ? 22.356 -12.487 -14.227 1.00 23.95 ? 177 ALA A N   1 
ATOM   1425 C CA  . ALA A 1 177 ? 23.433 -11.562 -14.547 1.00 23.50 ? 177 ALA A CA  1 
ATOM   1426 C C   . ALA A 1 177 ? 24.420 -11.438 -13.388 1.00 22.79 ? 177 ALA A C   1 
ATOM   1427 O O   . ALA A 1 177 ? 25.605 -11.208 -13.612 1.00 23.20 ? 177 ALA A O   1 
ATOM   1428 C CB  . ALA A 1 177 ? 22.855 -10.213 -14.917 1.00 22.94 ? 177 ALA A CB  1 
ATOM   1429 N N   . LEU A 1 178 ? 23.923 -11.577 -12.154 1.00 23.11 ? 178 LEU A N   1 
ATOM   1430 C CA  . LEU A 1 178 ? 24.743 -11.406 -10.964 1.00 23.00 ? 178 LEU A CA  1 
ATOM   1431 C C   . LEU A 1 178 ? 24.831 -12.714 -10.178 1.00 23.22 ? 178 LEU A C   1 
ATOM   1432 O O   . LEU A 1 178 ? 24.953 -12.687 -8.958  1.00 21.85 ? 178 LEU A O   1 
ATOM   1433 C CB  . LEU A 1 178 ? 24.105 -10.292 -10.134 1.00 23.03 ? 178 LEU A CB  1 
ATOM   1434 C CG  . LEU A 1 178 ? 24.018 -8.916  -10.803 1.00 22.62 ? 178 LEU A CG  1 
ATOM   1435 C CD1 . LEU A 1 178 ? 23.162 -7.970  -9.982  1.00 23.09 ? 178 LEU A CD1 1 
ATOM   1436 C CD2 . LEU A 1 178 ? 25.398 -8.324  -11.013 1.00 22.50 ? 178 LEU A CD2 1 
ATOM   1437 N N   . ALA A 1 179 ? 24.788 -13.856 -10.879 1.00 24.06 ? 179 ALA A N   1 
ATOM   1438 C CA  . ALA A 1 179 ? 24.653 -15.152 -10.227 1.00 25.47 ? 179 ALA A CA  1 
ATOM   1439 C C   . ALA A 1 179 ? 25.901 -15.478 -9.406  1.00 26.13 ? 179 ALA A C   1 
ATOM   1440 O O   . ALA A 1 179 ? 25.798 -16.042 -8.319  1.00 25.66 ? 179 ALA A O   1 
ATOM   1441 C CB  . ALA A 1 179 ? 24.375 -16.231 -11.251 1.00 25.91 ? 179 ALA A CB  1 
ATOM   1442 N N   . GLU A 1 180 ? 27.078 -15.134 -9.937  1.00 27.72 ? 180 GLU A N   1 
ATOM   1443 C CA  . GLU A 1 180 ? 28.320 -15.303 -9.200  1.00 29.28 ? 180 GLU A CA  1 
ATOM   1444 C C   . GLU A 1 180 ? 28.315 -14.396 -7.970  1.00 28.22 ? 180 GLU A C   1 
ATOM   1445 O O   . GLU A 1 180 ? 28.780 -14.795 -6.902  1.00 26.92 ? 180 GLU A O   1 
ATOM   1446 C CB  . GLU A 1 180 ? 29.521 -15.061 -10.115 1.00 31.36 ? 180 GLU A CB  1 
ATOM   1447 C CG  . GLU A 1 180 ? 29.694 -16.164 -11.156 1.00 33.64 ? 180 GLU A CG  1 
ATOM   1448 C CD  . GLU A 1 180 ? 30.862 -15.978 -12.108 1.00 35.40 ? 180 GLU A CD  1 
ATOM   1449 O OE1 . GLU A 1 180 ? 30.755 -15.128 -13.019 1.00 36.65 ? 180 GLU A OE1 1 
ATOM   1450 O OE2 . GLU A 1 180 ? 31.884 -16.679 -11.930 1.00 37.45 ? 180 GLU A OE2 1 
ATOM   1451 N N   . GLU A 1 181 ? 27.781 -13.179 -8.131  1.00 27.90 ? 181 GLU A N   1 
ATOM   1452 C CA  . GLU A 1 181 ? 27.716 -12.217 -7.043  1.00 28.22 ? 181 GLU A CA  1 
ATOM   1453 C C   . GLU A 1 181 ? 26.712 -12.690 -5.995  1.00 26.55 ? 181 GLU A C   1 
ATOM   1454 O O   . GLU A 1 181 ? 26.972 -12.579 -4.799  1.00 27.25 ? 181 GLU A O   1 
ATOM   1455 C CB  . GLU A 1 181 ? 27.371 -10.816 -7.549  1.00 30.35 ? 181 GLU A CB  1 
ATOM   1456 C CG  . GLU A 1 181 ? 28.452 -10.223 -8.449  1.00 31.78 ? 181 GLU A CG  1 
ATOM   1457 C CD  . GLU A 1 181 ? 28.340 -8.730  -8.705  1.00 33.19 ? 181 GLU A CD  1 
ATOM   1458 O OE1 . GLU A 1 181 ? 27.409 -8.085  -8.173  1.00 33.66 ? 181 GLU A OE1 1 
ATOM   1459 O OE2 . GLU A 1 181 ? 29.206 -8.209  -9.441  1.00 34.31 ? 181 GLU A OE2 1 
ATOM   1460 N N   . VAL A 1 182 ? 25.576 -13.227 -6.457  1.00 24.79 ? 182 VAL A N   1 
ATOM   1461 C CA  . VAL A 1 182 ? 24.534 -13.710 -5.567  1.00 23.97 ? 182 VAL A CA  1 
ATOM   1462 C C   . VAL A 1 182 ? 25.080 -14.881 -4.754  1.00 22.80 ? 182 VAL A C   1 
ATOM   1463 O O   . VAL A 1 182 ? 24.834 -14.968 -3.555  1.00 23.59 ? 182 VAL A O   1 
ATOM   1464 C CB  . VAL A 1 182 ? 23.257 -14.102 -6.335  1.00 23.25 ? 182 VAL A CB  1 
ATOM   1465 C CG1 . VAL A 1 182 ? 22.292 -14.899 -5.464  1.00 22.88 ? 182 VAL A CG1 1 
ATOM   1466 C CG2 . VAL A 1 182 ? 22.559 -12.884 -6.930  1.00 23.05 ? 182 VAL A CG2 1 
ATOM   1467 N N   . ALA A 1 183 ? 25.813 -15.776 -5.422  1.00 22.63 ? 183 ALA A N   1 
ATOM   1468 C CA  . ALA A 1 183 ? 26.438 -16.913 -4.764  1.00 21.69 ? 183 ALA A CA  1 
ATOM   1469 C C   . ALA A 1 183 ? 27.433 -16.448 -3.702  1.00 20.71 ? 183 ALA A C   1 
ATOM   1470 O O   . ALA A 1 183 ? 27.521 -17.052 -2.633  1.00 20.97 ? 183 ALA A O   1 
ATOM   1471 C CB  . ALA A 1 183 ? 27.101 -17.799 -5.790  1.00 21.47 ? 183 ALA A CB  1 
ATOM   1472 N N   . PHE A 1 184 ? 28.174 -15.373 -4.000  1.00 20.43 ? 184 PHE A N   1 
ATOM   1473 C CA  . PHE A 1 184 ? 29.227 -14.891 -3.120  1.00 19.64 ? 184 PHE A CA  1 
ATOM   1474 C C   . PHE A 1 184 ? 28.631 -14.381 -1.807  1.00 19.75 ? 184 PHE A C   1 
ATOM   1475 O O   . PHE A 1 184 ? 29.101 -14.751 -0.734  1.00 20.27 ? 184 PHE A O   1 
ATOM   1476 C CB  . PHE A 1 184 ? 30.072 -13.822 -3.820  1.00 19.68 ? 184 PHE A CB  1 
ATOM   1477 C CG  . PHE A 1 184 ? 30.896 -12.976 -2.859  1.00 19.44 ? 184 PHE A CG  1 
ATOM   1478 C CD1 . PHE A 1 184 ? 31.972 -13.524 -2.168  1.00 19.79 ? 184 PHE A CD1 1 
ATOM   1479 C CD2 . PHE A 1 184 ? 30.584 -11.638 -2.640  1.00 19.43 ? 184 PHE A CD2 1 
ATOM   1480 C CE1 . PHE A 1 184 ? 32.715 -12.750 -1.290  1.00 19.64 ? 184 PHE A CE1 1 
ATOM   1481 C CE2 . PHE A 1 184 ? 31.330 -10.870 -1.759  1.00 19.48 ? 184 PHE A CE2 1 
ATOM   1482 C CZ  . PHE A 1 184 ? 32.392 -11.426 -1.089  1.00 20.00 ? 184 PHE A CZ  1 
ATOM   1483 N N   . HIS A 1 185 ? 27.603 -13.528 -1.898  1.00 19.29 ? 185 HIS A N   1 
ATOM   1484 C CA  . HIS A 1 185 ? 26.968 -12.958 -0.720  1.00 19.03 ? 185 HIS A CA  1 
ATOM   1485 C C   . HIS A 1 185 ? 26.341 -14.059 0.130   1.00 18.33 ? 185 HIS A C   1 
ATOM   1486 O O   . HIS A 1 185 ? 26.301 -13.945 1.353   1.00 19.31 ? 185 HIS A O   1 
ATOM   1487 C CB  . HIS A 1 185 ? 25.955 -11.875 -1.108  1.00 19.30 ? 185 HIS A CB  1 
ATOM   1488 C CG  . HIS A 1 185 ? 26.615 -10.616 -1.548  1.00 19.70 ? 185 HIS A CG  1 
ATOM   1489 N ND1 . HIS A 1 185 ? 27.225 -9.773  -0.644  1.00 20.00 ? 185 HIS A ND1 1 
ATOM   1490 C CD2 . HIS A 1 185 ? 26.810 -10.076 -2.757  1.00 19.77 ? 185 HIS A CD2 1 
ATOM   1491 C CE1 . HIS A 1 185 ? 27.754 -8.748  -1.294  1.00 20.01 ? 185 HIS A CE1 1 
ATOM   1492 N NE2 . HIS A 1 185 ? 27.512 -8.910  -2.578  1.00 20.59 ? 185 HIS A NE2 1 
ATOM   1493 N N   . ALA A 1 186 ? 25.864 -15.118 -0.533  1.00 17.52 ? 186 ALA A N   1 
ATOM   1494 C CA  . ALA A 1 186 ? 25.313 -16.284 0.138   1.00 16.71 ? 186 ALA A CA  1 
ATOM   1495 C C   . ALA A 1 186 ? 26.400 -17.023 0.919   1.00 16.48 ? 186 ALA A C   1 
ATOM   1496 O O   . ALA A 1 186 ? 26.148 -17.526 2.014   1.00 16.77 ? 186 ALA A O   1 
ATOM   1497 C CB  . ALA A 1 186 ? 24.655 -17.186 -0.880  1.00 16.08 ? 186 ALA A CB  1 
ATOM   1498 N N   . PHE A 1 187 ? 27.602 -17.092 0.336   1.00 16.35 ? 187 PHE A N   1 
ATOM   1499 C CA  . PHE A 1 187 ? 28.746 -17.738 0.963   1.00 16.30 ? 187 PHE A CA  1 
ATOM   1500 C C   . PHE A 1 187 ? 29.159 -16.975 2.220   1.00 16.56 ? 187 PHE A C   1 
ATOM   1501 O O   . PHE A 1 187 ? 29.509 -17.596 3.222   1.00 17.48 ? 187 PHE A O   1 
ATOM   1502 C CB  . PHE A 1 187 ? 29.851 -17.855 -0.094  1.00 16.34 ? 187 PHE A CB  1 
ATOM   1503 C CG  . PHE A 1 187 ? 31.218 -18.336 0.381   1.00 15.97 ? 187 PHE A CG  1 
ATOM   1504 C CD1 . PHE A 1 187 ? 31.478 -19.691 0.559   1.00 16.12 ? 187 PHE A CD1 1 
ATOM   1505 C CD2 . PHE A 1 187 ? 32.256 -17.433 0.592   1.00 16.00 ? 187 PHE A CD2 1 
ATOM   1506 C CE1 . PHE A 1 187 ? 32.730 -20.126 0.972   1.00 16.12 ? 187 PHE A CE1 1 
ATOM   1507 C CE2 . PHE A 1 187 ? 33.507 -17.874 1.006   1.00 15.86 ? 187 PHE A CE2 1 
ATOM   1508 C CZ  . PHE A 1 187 ? 33.741 -19.217 1.193   1.00 15.85 ? 187 PHE A CZ  1 
ATOM   1509 N N   . THR A 1 188 ? 29.122 -15.636 2.175   1.00 16.83 ? 188 THR A N   1 
ATOM   1510 C CA  . THR A 1 188 ? 29.548 -14.840 3.320   1.00 17.06 ? 188 THR A CA  1 
ATOM   1511 C C   . THR A 1 188 ? 28.657 -15.164 4.516   1.00 17.06 ? 188 THR A C   1 
ATOM   1512 O O   . THR A 1 188 ? 29.148 -15.258 5.641   1.00 17.87 ? 188 THR A O   1 
ATOM   1513 C CB  . THR A 1 188 ? 29.551 -13.338 3.021   1.00 16.69 ? 188 THR A CB  1 
ATOM   1514 O OG1 . THR A 1 188 ? 28.218 -12.942 2.718   1.00 16.64 ? 188 THR A OG1 1 
ATOM   1515 C CG2 . THR A 1 188 ? 30.491 -12.970 1.887   1.00 16.60 ? 188 THR A CG2 1 
ATOM   1516 N N   . GLN A 1 189 ? 27.357 -15.351 4.248   1.00 17.30 ? 189 GLN A N   1 
ATOM   1517 C CA  . GLN A 1 189 ? 26.370 -15.628 5.277   1.00 16.60 ? 189 GLN A CA  1 
ATOM   1518 C C   . GLN A 1 189 ? 26.614 -17.019 5.856   1.00 17.63 ? 189 GLN A C   1 
ATOM   1519 O O   . GLN A 1 189 ? 26.688 -17.166 7.072   1.00 18.11 ? 189 GLN A O   1 
ATOM   1520 C CB  . GLN A 1 189 ? 24.959 -15.468 4.710   1.00 16.17 ? 189 GLN A CB  1 
ATOM   1521 C CG  . GLN A 1 189 ? 24.638 -14.057 4.228   1.00 15.76 ? 189 GLN A CG  1 
ATOM   1522 C CD  . GLN A 1 189 ? 24.868 -13.003 5.288   1.00 15.17 ? 189 GLN A CD  1 
ATOM   1523 O OE1 . GLN A 1 189 ? 24.309 -13.074 6.385   1.00 14.95 ? 189 GLN A OE1 1 
ATOM   1524 N NE2 . GLN A 1 189 ? 25.721 -12.034 4.991   1.00 14.98 ? 189 GLN A NE2 1 
ATOM   1525 N N   . TRP A 1 190 ? 26.756 -18.024 4.981   1.00 18.23 ? 190 TRP A N   1 
ATOM   1526 C CA  . TRP A 1 190 ? 27.043 -19.388 5.404   1.00 18.81 ? 190 TRP A CA  1 
ATOM   1527 C C   . TRP A 1 190 ? 28.224 -19.415 6.372   1.00 18.51 ? 190 TRP A C   1 
ATOM   1528 O O   . TRP A 1 190 ? 28.158 -20.065 7.411   1.00 18.27 ? 190 TRP A O   1 
ATOM   1529 C CB  . TRP A 1 190 ? 27.303 -20.288 4.188   1.00 19.54 ? 190 TRP A CB  1 
ATOM   1530 C CG  . TRP A 1 190 ? 27.862 -21.645 4.524   1.00 19.96 ? 190 TRP A CG  1 
ATOM   1531 C CD1 . TRP A 1 190 ? 27.216 -22.684 5.127   1.00 20.38 ? 190 TRP A CD1 1 
ATOM   1532 C CD2 . TRP A 1 190 ? 29.196 -22.115 4.237   1.00 20.25 ? 190 TRP A CD2 1 
ATOM   1533 N NE1 . TRP A 1 190 ? 28.056 -23.757 5.254   1.00 20.31 ? 190 TRP A NE1 1 
ATOM   1534 C CE2 . TRP A 1 190 ? 29.275 -23.442 4.712   1.00 20.23 ? 190 TRP A CE2 1 
ATOM   1535 C CE3 . TRP A 1 190 ? 30.324 -21.545 3.633   1.00 19.71 ? 190 TRP A CE3 1 
ATOM   1536 C CZ2 . TRP A 1 190 ? 30.439 -24.201 4.600   1.00 19.80 ? 190 TRP A CZ2 1 
ATOM   1537 C CZ3 . TRP A 1 190 ? 31.468 -22.302 3.515   1.00 19.29 ? 190 TRP A CZ3 1 
ATOM   1538 C CH2 . TRP A 1 190 ? 31.522 -23.610 3.991   1.00 19.52 ? 190 TRP A CH2 1 
ATOM   1539 N N   . LEU A 1 191 ? 29.301 -18.705 6.023   1.00 18.55 ? 191 LEU A N   1 
ATOM   1540 C CA  . LEU A 1 191 ? 30.462 -18.608 6.896   1.00 18.71 ? 191 LEU A CA  1 
ATOM   1541 C C   . LEU A 1 191 ? 30.071 -17.961 8.224   1.00 18.81 ? 191 LEU A C   1 
ATOM   1542 O O   . LEU A 1 191 ? 30.455 -18.450 9.283   1.00 18.38 ? 191 LEU A O   1 
ATOM   1543 C CB  . LEU A 1 191 ? 31.582 -17.823 6.217   1.00 18.38 ? 191 LEU A CB  1 
ATOM   1544 C CG  . LEU A 1 191 ? 32.361 -18.556 5.122   1.00 18.49 ? 191 LEU A CG  1 
ATOM   1545 C CD1 . LEU A 1 191 ? 33.381 -17.603 4.515   1.00 18.24 ? 191 LEU A CD1 1 
ATOM   1546 C CD2 . LEU A 1 191 ? 33.039 -19.815 5.650   1.00 18.31 ? 191 LEU A CD2 1 
ATOM   1547 N N   . PHE A 1 192 ? 29.309 -16.860 8.157   1.00 19.21 ? 192 PHE A N   1 
ATOM   1548 C CA  . PHE A 1 192 ? 28.932 -16.106 9.343   1.00 19.03 ? 192 PHE A CA  1 
ATOM   1549 C C   . PHE A 1 192 ? 28.163 -17.006 10.307  1.00 18.70 ? 192 PHE A C   1 
ATOM   1550 O O   . PHE A 1 192 ? 28.485 -17.060 11.492  1.00 18.68 ? 192 PHE A O   1 
ATOM   1551 C CB  . PHE A 1 192 ? 28.088 -14.871 9.009   1.00 19.29 ? 192 PHE A CB  1 
ATOM   1552 C CG  . PHE A 1 192 ? 27.644 -14.076 10.232  1.00 19.55 ? 192 PHE A CG  1 
ATOM   1553 C CD1 . PHE A 1 192 ? 28.442 -13.064 10.755  1.00 19.85 ? 192 PHE A CD1 1 
ATOM   1554 C CD2 . PHE A 1 192 ? 26.440 -14.359 10.870  1.00 19.64 ? 192 PHE A CD2 1 
ATOM   1555 C CE1 . PHE A 1 192 ? 28.038 -12.349 11.874  1.00 20.25 ? 192 PHE A CE1 1 
ATOM   1556 C CE2 . PHE A 1 192 ? 26.040 -13.641 11.987  1.00 19.55 ? 192 PHE A CE2 1 
ATOM   1557 C CZ  . PHE A 1 192 ? 26.839 -12.638 12.488  1.00 19.80 ? 192 PHE A CZ  1 
ATOM   1558 N N   . PHE A 1 193 ? 27.134 -17.688 9.794   1.00 18.70 ? 193 PHE A N   1 
ATOM   1559 C CA  . PHE A 1 193 ? 26.203 -18.415 10.642  1.00 18.77 ? 193 PHE A CA  1 
ATOM   1560 C C   . PHE A 1 193 ? 26.904 -19.651 11.204  1.00 19.07 ? 193 PHE A C   1 
ATOM   1561 O O   . PHE A 1 193 ? 26.691 -20.016 12.356  1.00 18.06 ? 193 PHE A O   1 
ATOM   1562 C CB  . PHE A 1 193 ? 24.909 -18.670 9.857   1.00 18.47 ? 193 PHE A CB  1 
ATOM   1563 C CG  . PHE A 1 193 ? 24.069 -17.410 9.692   1.00 17.63 ? 193 PHE A CG  1 
ATOM   1564 C CD1 . PHE A 1 193 ? 23.407 -16.850 10.781  1.00 17.56 ? 193 PHE A CD1 1 
ATOM   1565 C CD2 . PHE A 1 193 ? 23.953 -16.777 8.460   1.00 17.30 ? 193 PHE A CD2 1 
ATOM   1566 C CE1 . PHE A 1 193 ? 22.660 -15.686 10.640  1.00 17.09 ? 193 PHE A CE1 1 
ATOM   1567 C CE2 . PHE A 1 193 ? 23.205 -15.618 8.324   1.00 16.70 ? 193 PHE A CE2 1 
ATOM   1568 C CZ  . PHE A 1 193 ? 22.561 -15.073 9.412   1.00 16.89 ? 193 PHE A CZ  1 
ATOM   1569 N N   . ARG A 1 194 ? 27.777 -20.253 10.391  1.00 20.13 ? 194 ARG A N   1 
ATOM   1570 C CA  . ARG A 1 194 ? 28.596 -21.377 10.813  1.00 21.07 ? 194 ARG A CA  1 
ATOM   1571 C C   . ARG A 1 194 ? 29.485 -20.962 11.985  1.00 19.96 ? 194 ARG A C   1 
ATOM   1572 O O   . ARG A 1 194 ? 29.520 -21.647 13.008  1.00 20.92 ? 194 ARG A O   1 
ATOM   1573 C CB  . ARG A 1 194 ? 29.359 -21.840 9.566   1.00 22.25 ? 194 ARG A CB  1 
ATOM   1574 C CG  . ARG A 1 194 ? 30.309 -23.020 9.703   1.00 23.65 ? 194 ARG A CG  1 
ATOM   1575 C CD  . ARG A 1 194 ? 30.776 -23.430 8.313   1.00 24.74 ? 194 ARG A CD  1 
ATOM   1576 N NE  . ARG A 1 194 ? 31.572 -24.663 8.303   1.00 25.46 ? 194 ARG A NE  1 
ATOM   1577 C CZ  . ARG A 1 194 ? 31.147 -25.860 7.901   1.00 26.00 ? 194 ARG A CZ  1 
ATOM   1578 N NH1 . ARG A 1 194 ? 29.901 -26.041 7.497   1.00 25.93 ? 194 ARG A NH1 1 
ATOM   1579 N NH2 . ARG A 1 194 ? 31.976 -26.888 7.926   1.00 26.40 ? 194 ARG A NH2 1 
ATOM   1580 N N   . GLN A 1 195 ? 30.178 -19.826 11.836  1.00 18.66 ? 195 GLN A N   1 
ATOM   1581 C CA  . GLN A 1 195 ? 31.145 -19.368 12.826  1.00 18.14 ? 195 GLN A CA  1 
ATOM   1582 C C   . GLN A 1 195 ? 30.442 -18.901 14.099  1.00 17.48 ? 195 GLN A C   1 
ATOM   1583 O O   . GLN A 1 195 ? 30.978 -19.071 15.192  1.00 17.18 ? 195 GLN A O   1 
ATOM   1584 C CB  . GLN A 1 195 ? 32.041 -18.258 12.275  1.00 17.84 ? 195 GLN A CB  1 
ATOM   1585 C CG  . GLN A 1 195 ? 32.992 -18.724 11.178  1.00 17.65 ? 195 GLN A CG  1 
ATOM   1586 C CD  . GLN A 1 195 ? 33.964 -17.659 10.720  1.00 17.87 ? 195 GLN A CD  1 
ATOM   1587 O OE1 . GLN A 1 195 ? 34.051 -16.564 11.287  1.00 17.84 ? 195 GLN A OE1 1 
ATOM   1588 N NE2 . GLN A 1 195 ? 34.733 -17.982 9.692   1.00 18.22 ? 195 GLN A NE2 1 
ATOM   1589 N N   . TRP A 1 196 ? 29.248 -18.310 13.968  1.00 17.43 ? 196 TRP A N   1 
ATOM   1590 C CA  . TRP A 1 196 ? 28.518 -17.880 15.150  1.00 17.72 ? 196 TRP A CA  1 
ATOM   1591 C C   . TRP A 1 196 ? 27.911 -19.086 15.866  1.00 17.71 ? 196 TRP A C   1 
ATOM   1592 O O   . TRP A 1 196 ? 27.800 -19.084 17.089  1.00 17.93 ? 196 TRP A O   1 
ATOM   1593 C CB  . TRP A 1 196 ? 27.435 -16.847 14.817  1.00 17.69 ? 196 TRP A CB  1 
ATOM   1594 C CG  . TRP A 1 196 ? 26.817 -16.281 16.066  1.00 17.23 ? 196 TRP A CG  1 
ATOM   1595 C CD1 . TRP A 1 196 ? 25.766 -16.789 16.772  1.00 16.93 ? 196 TRP A CD1 1 
ATOM   1596 C CD2 . TRP A 1 196 ? 27.267 -15.119 16.794  1.00 16.94 ? 196 TRP A CD2 1 
ATOM   1597 N NE1 . TRP A 1 196 ? 25.516 -16.015 17.874  1.00 17.00 ? 196 TRP A NE1 1 
ATOM   1598 C CE2 . TRP A 1 196 ? 26.422 -14.988 17.916  1.00 17.00 ? 196 TRP A CE2 1 
ATOM   1599 C CE3 . TRP A 1 196 ? 28.288 -14.183 16.605  1.00 17.31 ? 196 TRP A CE3 1 
ATOM   1600 C CZ2 . TRP A 1 196 ? 26.572 -13.956 18.838  1.00 17.08 ? 196 TRP A CZ2 1 
ATOM   1601 C CZ3 . TRP A 1 196 ? 28.430 -13.159 17.517  1.00 17.38 ? 196 TRP A CZ3 1 
ATOM   1602 C CH2 . TRP A 1 196 ? 27.585 -13.052 18.621  1.00 17.11 ? 196 TRP A CH2 1 
ATOM   1603 N N   . GLY A 1 197 ? 27.508 -20.100 15.090  1.00 17.93 ? 197 GLY A N   1 
ATOM   1604 C CA  . GLY A 1 197 ? 26.920 -21.314 15.634  1.00 18.46 ? 197 GLY A CA  1 
ATOM   1605 C C   . GLY A 1 197 ? 27.900 -22.053 16.544  1.00 18.58 ? 197 GLY A C   1 
ATOM   1606 O O   . GLY A 1 197 ? 27.517 -22.556 17.598  1.00 18.00 ? 197 GLY A O   1 
ATOM   1607 N N   . ALA A 1 198 ? 29.170 -22.092 16.128  1.00 19.68 ? 198 ALA A N   1 
ATOM   1608 C CA  . ALA A 1 198 ? 30.237 -22.657 16.941  1.00 20.25 ? 198 ALA A CA  1 
ATOM   1609 C C   . ALA A 1 198 ? 30.472 -21.800 18.183  1.00 20.76 ? 198 ALA A C   1 
ATOM   1610 O O   . ALA A 1 198 ? 30.696 -22.331 19.267  1.00 21.44 ? 198 ALA A O   1 
ATOM   1611 C CB  . ALA A 1 198 ? 31.502 -22.777 16.122  1.00 20.50 ? 198 ALA A CB  1 
ATOM   1612 N N   . LEU A 1 199 ? 30.431 -20.475 18.002  1.00 21.04 ? 199 LEU A N   1 
ATOM   1613 C CA  . LEU A 1 199 ? 30.751 -19.536 19.063  1.00 21.44 ? 199 LEU A CA  1 
ATOM   1614 C C   . LEU A 1 199 ? 29.686 -19.623 20.154  1.00 21.71 ? 199 LEU A C   1 
ATOM   1615 O O   . LEU A 1 199 ? 30.015 -19.676 21.334  1.00 21.50 ? 199 LEU A O   1 
ATOM   1616 C CB  . LEU A 1 199 ? 30.870 -18.127 18.484  1.00 21.31 ? 199 LEU A CB  1 
ATOM   1617 C CG  . LEU A 1 199 ? 31.802 -17.160 19.219  1.00 21.94 ? 199 LEU A CG  1 
ATOM   1618 C CD1 . LEU A 1 199 ? 33.219 -17.705 19.338  1.00 21.71 ? 199 LEU A CD1 1 
ATOM   1619 C CD2 . LEU A 1 199 ? 31.817 -15.817 18.506  1.00 22.01 ? 199 LEU A CD2 1 
ATOM   1620 N N   . LYS A 1 200 ? 28.412 -19.664 19.741  1.00 21.78 ? 200 LYS A N   1 
ATOM   1621 C CA  . LYS A 1 200 ? 27.295 -19.786 20.664  1.00 21.46 ? 200 LYS A CA  1 
ATOM   1622 C C   . LYS A 1 200 ? 27.393 -21.103 21.435  1.00 21.70 ? 200 LYS A C   1 
ATOM   1623 O O   . LYS A 1 200 ? 27.085 -21.152 22.627  1.00 20.31 ? 200 LYS A O   1 
ATOM   1624 C CB  . LYS A 1 200 ? 25.985 -19.650 19.879  1.00 21.55 ? 200 LYS A CB  1 
ATOM   1625 C CG  . LYS A 1 200 ? 24.714 -19.569 20.711  1.00 21.99 ? 200 LYS A CG  1 
ATOM   1626 C CD  . LYS A 1 200 ? 23.502 -19.145 19.887  1.00 22.32 ? 200 LYS A CD  1 
ATOM   1627 C CE  . LYS A 1 200 ? 22.247 -18.990 20.689  1.00 22.48 ? 200 LYS A CE  1 
ATOM   1628 N NZ  . LYS A 1 200 ? 21.594 -20.277 20.944  1.00 22.88 ? 200 LYS A NZ  1 
ATOM   1629 N N   . ALA A 1 201 ? 27.837 -22.163 20.748  1.00 22.26 ? 201 ALA A N   1 
ATOM   1630 C CA  . ALA A 1 201 ? 27.999 -23.470 21.362  1.00 22.61 ? 201 ALA A CA  1 
ATOM   1631 C C   . ALA A 1 201 ? 28.991 -23.384 22.518  1.00 23.51 ? 201 ALA A C   1 
ATOM   1632 O O   . ALA A 1 201 ? 28.729 -23.907 23.600  1.00 23.24 ? 201 ALA A O   1 
ATOM   1633 C CB  . ALA A 1 201 ? 28.448 -24.482 20.330  1.00 22.63 ? 201 ALA A CB  1 
ATOM   1634 N N   . GLU A 1 202 ? 30.122 -22.713 22.261  1.00 24.28 ? 202 GLU A N   1 
ATOM   1635 C CA  . GLU A 1 202 ? 31.176 -22.540 23.246  1.00 25.82 ? 202 GLU A CA  1 
ATOM   1636 C C   . GLU A 1 202 ? 30.622 -21.779 24.450  1.00 24.17 ? 202 GLU A C   1 
ATOM   1637 O O   . GLU A 1 202 ? 30.873 -22.162 25.588  1.00 23.84 ? 202 GLU A O   1 
ATOM   1638 C CB  . GLU A 1 202 ? 32.365 -21.809 22.616  1.00 27.20 ? 202 GLU A CB  1 
ATOM   1639 C CG  . GLU A 1 202 ? 33.683 -22.001 23.363  1.00 29.03 ? 202 GLU A CG  1 
ATOM   1640 C CD  . GLU A 1 202 ? 34.421 -23.287 23.022  1.00 30.94 ? 202 GLU A CD  1 
ATOM   1641 O OE1 . GLU A 1 202 ? 33.912 -24.380 23.354  1.00 32.32 ? 202 GLU A OE1 1 
ATOM   1642 O OE2 . GLU A 1 202 ? 35.507 -23.200 22.407  1.00 31.38 ? 202 GLU A OE2 1 
ATOM   1643 N N   . ALA A 1 203 ? 29.858 -20.711 24.182  1.00 23.15 ? 203 ALA A N   1 
ATOM   1644 C CA  . ALA A 1 203 ? 29.278 -19.882 25.230  1.00 22.48 ? 203 ALA A CA  1 
ATOM   1645 C C   . ALA A 1 203 ? 28.402 -20.732 26.146  1.00 22.54 ? 203 ALA A C   1 
ATOM   1646 O O   . ALA A 1 203 ? 28.586 -20.727 27.363  1.00 21.86 ? 203 ALA A O   1 
ATOM   1647 C CB  . ALA A 1 203 ? 28.489 -18.741 24.615  1.00 22.23 ? 203 ALA A CB  1 
ATOM   1648 N N   . GLU A 1 204 ? 27.465 -21.474 25.540  1.00 22.47 ? 204 GLU A N   1 
ATOM   1649 C CA  . GLU A 1 204 ? 26.524 -22.307 26.273  1.00 22.80 ? 204 GLU A CA  1 
ATOM   1650 C C   . GLU A 1 204 ? 27.263 -23.321 27.145  1.00 22.25 ? 204 GLU A C   1 
ATOM   1651 O O   . GLU A 1 204 ? 26.871 -23.564 28.287  1.00 22.22 ? 204 GLU A O   1 
ATOM   1652 C CB  . GLU A 1 204 ? 25.585 -23.003 25.290  1.00 23.32 ? 204 GLU A CB  1 
ATOM   1653 C CG  . GLU A 1 204 ? 24.588 -22.046 24.642  1.00 23.89 ? 204 GLU A CG  1 
ATOM   1654 C CD  . GLU A 1 204 ? 23.879 -22.615 23.427  1.00 24.89 ? 204 GLU A CD  1 
ATOM   1655 O OE1 . GLU A 1 204 ? 23.049 -21.889 22.840  1.00 24.98 ? 204 GLU A OE1 1 
ATOM   1656 O OE2 . GLU A 1 204 ? 24.163 -23.776 23.062  1.00 26.22 ? 204 GLU A OE2 1 
ATOM   1657 N N   . ALA A 1 205 ? 28.336 -23.907 26.606  1.00 21.66 ? 205 ALA A N   1 
ATOM   1658 C CA  . ALA A 1 205 ? 29.152 -24.834 27.369  1.00 21.74 ? 205 ALA A CA  1 
ATOM   1659 C C   . ALA A 1 205 ? 29.675 -24.150 28.633  1.00 21.93 ? 205 ALA A C   1 
ATOM   1660 O O   . ALA A 1 205 ? 29.682 -24.757 29.703  1.00 21.12 ? 205 ALA A O   1 
ATOM   1661 C CB  . ALA A 1 205 ? 30.281 -25.356 26.512  1.00 22.22 ? 205 ALA A CB  1 
ATOM   1662 N N   . LEU A 1 206 ? 30.090 -22.883 28.489  1.00 22.06 ? 206 LEU A N   1 
ATOM   1663 C CA  . LEU A 1 206 ? 30.648 -22.092 29.578  1.00 22.14 ? 206 LEU A CA  1 
ATOM   1664 C C   . LEU A 1 206 ? 29.549 -21.408 30.390  1.00 22.28 ? 206 LEU A C   1 
ATOM   1665 O O   . LEU A 1 206 ? 29.846 -20.629 31.294  1.00 22.49 ? 206 LEU A O   1 
ATOM   1666 C CB  . LEU A 1 206 ? 31.607 -21.059 28.987  1.00 21.99 ? 206 LEU A CB  1 
ATOM   1667 C CG  . LEU A 1 206 ? 32.884 -21.599 28.335  1.00 22.33 ? 206 LEU A CG  1 
ATOM   1668 C CD1 . LEU A 1 206 ? 33.666 -20.468 27.685  1.00 21.95 ? 206 LEU A CD1 1 
ATOM   1669 C CD2 . LEU A 1 206 ? 33.757 -22.339 29.333  1.00 22.37 ? 206 LEU A CD2 1 
ATOM   1670 N N   . GLY A 1 207 ? 28.282 -21.681 30.061  1.00 22.42 ? 207 GLY A N   1 
ATOM   1671 C CA  . GLY A 1 207 ? 27.157 -21.124 30.794  1.00 23.02 ? 207 GLY A CA  1 
ATOM   1672 C C   . GLY A 1 207 ? 27.007 -19.623 30.557  1.00 22.49 ? 207 GLY A C   1 
ATOM   1673 O O   . GLY A 1 207 ? 26.706 -18.874 31.485  1.00 21.73 ? 207 GLY A O   1 
ATOM   1674 N N   . ILE A 1 208 ? 27.219 -19.196 29.307  1.00 22.17 ? 208 ILE A N   1 
ATOM   1675 C CA  . ILE A 1 208 ? 27.111 -17.792 28.945  1.00 22.91 ? 208 ILE A CA  1 
ATOM   1676 C C   . ILE A 1 208 ? 25.937 -17.632 27.985  1.00 23.08 ? 208 ILE A C   1 
ATOM   1677 O O   . ILE A 1 208 ? 25.840 -18.352 26.992  1.00 23.98 ? 208 ILE A O   1 
ATOM   1678 C CB  . ILE A 1 208 ? 28.423 -17.258 28.336  1.00 22.93 ? 208 ILE A CB  1 
ATOM   1679 C CG1 . ILE A 1 208 ? 29.599 -17.405 29.310  1.00 22.53 ? 208 ILE A CG1 1 
ATOM   1680 C CG2 . ILE A 1 208 ? 28.249 -15.809 27.870  1.00 22.98 ? 208 ILE A CG2 1 
ATOM   1681 C CD1 . ILE A 1 208 ? 30.968 -17.220 28.676  1.00 23.17 ? 208 ILE A CD1 1 
ATOM   1682 N N   . ARG A 1 209 ? 25.053 -16.681 28.303  1.00 22.88 ? 209 ARG A N   1 
ATOM   1683 C CA  . ARG A 1 209 ? 23.949 -16.325 27.428  1.00 22.50 ? 209 ARG A CA  1 
ATOM   1684 C C   . ARG A 1 209 ? 24.316 -15.042 26.688  1.00 20.71 ? 209 ARG A C   1 
ATOM   1685 O O   . ARG A 1 209 ? 24.801 -14.089 27.295  1.00 20.73 ? 209 ARG A O   1 
ATOM   1686 C CB  . ARG A 1 209 ? 22.654 -16.190 28.235  1.00 24.05 ? 209 ARG A CB  1 
ATOM   1687 C CG  . ARG A 1 209 ? 22.150 -17.503 28.816  1.00 25.87 ? 209 ARG A CG  1 
ATOM   1688 C CD  . ARG A 1 209 ? 20.906 -17.319 29.671  1.00 27.13 ? 209 ARG A CD  1 
ATOM   1689 N NE  . ARG A 1 209 ? 20.682 -18.442 30.592  1.00 29.27 ? 209 ARG A NE  1 
ATOM   1690 C CZ  . ARG A 1 209 ? 19.814 -18.456 31.605  1.00 31.40 ? 209 ARG A CZ  1 
ATOM   1691 N NH1 . ARG A 1 209 ? 19.063 -17.401 31.871  1.00 32.60 ? 209 ARG A NH1 1 
ATOM   1692 N NH2 . ARG A 1 209 ? 19.700 -19.534 32.363  1.00 33.18 ? 209 ARG A NH2 1 
ATOM   1693 N N   . ILE A 1 210 ? 24.100 -15.049 25.370  1.00 18.46 ? 210 ILE A N   1 
ATOM   1694 C CA  . ILE A 1 210 ? 24.380 -13.903 24.526  1.00 17.75 ? 210 ILE A CA  1 
ATOM   1695 C C   . ILE A 1 210 ? 23.140 -13.014 24.483  1.00 17.74 ? 210 ILE A C   1 
ATOM   1696 O O   . ILE A 1 210 ? 22.053 -13.483 24.133  1.00 17.04 ? 210 ILE A O   1 
ATOM   1697 C CB  . ILE A 1 210 ? 24.790 -14.362 23.117  1.00 17.29 ? 210 ILE A CB  1 
ATOM   1698 C CG1 . ILE A 1 210 ? 25.987 -15.314 23.167  1.00 17.61 ? 210 ILE A CG1 1 
ATOM   1699 C CG2 . ILE A 1 210 ? 25.052 -13.159 22.209  1.00 16.85 ? 210 ILE A CG2 1 
ATOM   1700 C CD1 . ILE A 1 210 ? 26.214 -16.095 21.884  1.00 17.74 ? 210 ILE A CD1 1 
ATOM   1701 N N   A LEU A 1 211 ? 23.314 -11.739 24.855  0.50 17.38 ? 211 LEU A N   1 
ATOM   1702 N N   B LEU A 1 211 ? 23.320 -11.735 24.831  0.50 17.48 ? 211 LEU A N   1 
ATOM   1703 C CA  A LEU A 1 211 ? 22.268 -10.738 24.724  0.50 17.49 ? 211 LEU A CA  1 
ATOM   1704 C CA  B LEU A 1 211 ? 22.257 -10.752 24.720  0.50 17.66 ? 211 LEU A CA  1 
ATOM   1705 C C   A LEU A 1 211 ? 22.451 -10.029 23.386  0.50 17.78 ? 211 LEU A C   1 
ATOM   1706 C C   B LEU A 1 211 ? 22.434 -10.004 23.401  0.50 17.87 ? 211 LEU A C   1 
ATOM   1707 O O   A LEU A 1 211 ? 23.483 -9.402  23.153  0.50 17.95 ? 211 LEU A O   1 
ATOM   1708 O O   B LEU A 1 211 ? 23.447 -9.338  23.193  0.50 18.07 ? 211 LEU A O   1 
ATOM   1709 C CB  A LEU A 1 211 ? 22.336 -9.751  25.888  0.50 17.33 ? 211 LEU A CB  1 
ATOM   1710 C CB  B LEU A 1 211 ? 22.291 -9.816  25.927  0.50 17.61 ? 211 LEU A CB  1 
ATOM   1711 C CG  A LEU A 1 211 ? 22.394 -10.361 27.292  0.50 17.25 ? 211 LEU A CG  1 
ATOM   1712 C CG  B LEU A 1 211 ? 20.948 -9.204  26.340  0.50 17.67 ? 211 LEU A CG  1 
ATOM   1713 C CD1 A LEU A 1 211 ? 23.381 -9.593  28.147  0.50 17.11 ? 211 LEU A CD1 1 
ATOM   1714 C CD1 B LEU A 1 211 ? 20.972 -8.794  27.801  0.50 17.77 ? 211 LEU A CD1 1 
ATOM   1715 C CD2 A LEU A 1 211 ? 21.035 -10.376 27.968  0.50 17.30 ? 211 LEU A CD2 1 
ATOM   1716 C CD2 B LEU A 1 211 ? 20.573 -8.024  25.467  0.50 17.70 ? 211 LEU A CD2 1 
ATOM   1717 N N   . GLY A 1 212 ? 21.451 -10.152 22.507  1.00 17.91 ? 212 GLY A N   1 
ATOM   1718 C CA  . GLY A 1 212 ? 21.475 -9.500  21.210  1.00 18.35 ? 212 GLY A CA  1 
ATOM   1719 C C   . GLY A 1 212 ? 20.819 -8.127  21.284  1.00 19.09 ? 212 GLY A C   1 
ATOM   1720 O O   . GLY A 1 212 ? 20.250 -7.764  22.309  1.00 18.59 ? 212 GLY A O   1 
ATOM   1721 N N   . ASP A 1 213 ? 20.899 -7.392  20.172  1.00 20.29 ? 213 ASP A N   1 
ATOM   1722 C CA  . ASP A 1 213 ? 20.382 -6.040  20.079  1.00 21.60 ? 213 ASP A CA  1 
ATOM   1723 C C   . ASP A 1 213 ? 19.735 -5.881  18.708  1.00 22.00 ? 213 ASP A C   1 
ATOM   1724 O O   . ASP A 1 213 ? 20.322 -6.280  17.705  1.00 22.39 ? 213 ASP A O   1 
ATOM   1725 C CB  . ASP A 1 213 ? 21.504 -5.040  20.314  1.00 22.52 ? 213 ASP A CB  1 
ATOM   1726 C CG  . ASP A 1 213 ? 21.084 -3.673  20.828  1.00 23.16 ? 213 ASP A CG  1 
ATOM   1727 O OD1 . ASP A 1 213 ? 19.865 -3.465  21.020  1.00 23.12 ? 213 ASP A OD1 1 
ATOM   1728 O OD2 . ASP A 1 213 ? 21.986 -2.837  21.050  1.00 23.64 ? 213 ASP A OD2 1 
ATOM   1729 N N   . MET A 1 214 ? 18.511 -5.341  18.671  1.00 22.40 ? 214 MET A N   1 
ATOM   1730 C CA  . MET A 1 214 ? 17.864 -5.052  17.401  1.00 22.54 ? 214 MET A CA  1 
ATOM   1731 C C   . MET A 1 214 ? 17.111 -3.728  17.509  1.00 22.33 ? 214 MET A C   1 
ATOM   1732 O O   . MET A 1 214 ? 16.387 -3.493  18.473  1.00 22.34 ? 214 MET A O   1 
ATOM   1733 C CB  . MET A 1 214 ? 16.940 -6.195  16.943  1.00 23.03 ? 214 MET A CB  1 
ATOM   1734 C CG  . MET A 1 214 ? 15.575 -6.272  17.617  1.00 23.78 ? 214 MET A CG  1 
ATOM   1735 S SD  . MET A 1 214 ? 14.395 -7.344  16.764  1.00 24.87 ? 214 MET A SD  1 
ATOM   1736 C CE  . MET A 1 214 ? 15.311 -8.883  16.604  1.00 24.58 ? 214 MET A CE  1 
ATOM   1737 N N   . PRO A 1 215 ? 17.257 -2.812  16.524  1.00 21.42 ? 215 PRO A N   1 
ATOM   1738 C CA  . PRO A 1 215 ? 16.419 -1.622  16.480  1.00 20.90 ? 215 PRO A CA  1 
ATOM   1739 C C   . PRO A 1 215 ? 14.983 -1.996  16.128  1.00 20.66 ? 215 PRO A C   1 
ATOM   1740 O O   . PRO A 1 215 ? 14.762 -2.954  15.394  1.00 20.17 ? 215 PRO A O   1 
ATOM   1741 C CB  . PRO A 1 215 ? 17.104 -0.748  15.437  1.00 20.82 ? 215 PRO A CB  1 
ATOM   1742 C CG  . PRO A 1 215 ? 17.760 -1.761  14.516  1.00 21.25 ? 215 PRO A CG  1 
ATOM   1743 C CD  . PRO A 1 215 ? 18.181 -2.908  15.384  1.00 21.16 ? 215 PRO A CD  1 
ATOM   1744 N N   . ILE A 1 216 ? 14.010 -1.281  16.697  1.00 21.13 ? 216 ILE A N   1 
ATOM   1745 C CA  . ILE A 1 216 ? 12.614 -1.566  16.403  1.00 21.93 ? 216 ILE A CA  1 
ATOM   1746 C C   . ILE A 1 216 ? 12.348 -1.283  14.924  1.00 22.02 ? 216 ILE A C   1 
ATOM   1747 O O   . ILE A 1 216 ? 11.639 -2.047  14.272  1.00 22.40 ? 216 ILE A O   1 
ATOM   1748 C CB  . ILE A 1 216 ? 11.662 -0.787  17.327  1.00 22.14 ? 216 ILE A CB  1 
ATOM   1749 C CG1 . ILE A 1 216 ? 10.208 -1.244  17.132  1.00 22.47 ? 216 ILE A CG1 1 
ATOM   1750 C CG2 . ILE A 1 216 ? 11.817 0.725   17.144  1.00 22.13 ? 216 ILE A CG2 1 
ATOM   1751 C CD1 . ILE A 1 216 ? 9.223  -0.647  18.123  1.00 22.10 ? 216 ILE A CD1 1 
ATOM   1752 N N   . PHE A 1 217 ? 12.941 -0.198  14.405  1.00 21.96 ? 217 PHE A N   1 
ATOM   1753 C CA  . PHE A 1 217 ? 12.773 0.193   13.015  1.00 22.31 ? 217 PHE A CA  1 
ATOM   1754 C C   . PHE A 1 217 ? 14.007 -0.213  12.212  1.00 22.62 ? 217 PHE A C   1 
ATOM   1755 O O   . PHE A 1 217 ? 15.134 0.007   12.646  1.00 22.13 ? 217 PHE A O   1 
ATOM   1756 C CB  . PHE A 1 217 ? 12.508 1.701   12.969  1.00 22.21 ? 217 PHE A CB  1 
ATOM   1757 C CG  . PHE A 1 217 ? 11.225 2.118   13.673  1.00 21.76 ? 217 PHE A CG  1 
ATOM   1758 C CD1 . PHE A 1 217 ? 10.037 1.431   13.448  1.00 21.74 ? 217 PHE A CD1 1 
ATOM   1759 C CD2 . PHE A 1 217 ? 11.218 3.169   14.585  1.00 22.07 ? 217 PHE A CD2 1 
ATOM   1760 C CE1 . PHE A 1 217 ? 8.870  1.807   14.093  1.00 22.15 ? 217 PHE A CE1 1 
ATOM   1761 C CE2 . PHE A 1 217 ? 10.048 3.535   15.234  1.00 22.20 ? 217 PHE A CE2 1 
ATOM   1762 C CZ  . PHE A 1 217 ? 8.878  2.855   14.986  1.00 22.20 ? 217 PHE A CZ  1 
ATOM   1763 N N   . VAL A 1 218 ? 13.767 -0.826  11.046  1.00 22.78 ? 218 VAL A N   1 
ATOM   1764 C CA  . VAL A 1 218 ? 14.814 -1.140  10.086  1.00 22.65 ? 218 VAL A CA  1 
ATOM   1765 C C   . VAL A 1 218 ? 15.155 0.134   9.317   1.00 23.06 ? 218 VAL A C   1 
ATOM   1766 O O   . VAL A 1 218 ? 14.477 1.150   9.464   1.00 24.21 ? 218 VAL A O   1 
ATOM   1767 C CB  . VAL A 1 218 ? 14.407 -2.277  9.123   1.00 22.31 ? 218 VAL A CB  1 
ATOM   1768 C CG1 . VAL A 1 218 ? 14.035 -3.550  9.873   1.00 22.10 ? 218 VAL A CG1 1 
ATOM   1769 C CG2 . VAL A 1 218 ? 13.274 -1.869  8.186   1.00 22.55 ? 218 VAL A CG2 1 
ATOM   1770 N N   . ALA A 1 219 ? 16.213 0.055   8.501   1.00 22.85 ? 219 ALA A N   1 
ATOM   1771 C CA  . ALA A 1 219 ? 16.649 1.152   7.653   1.00 22.41 ? 219 ALA A CA  1 
ATOM   1772 C C   . ALA A 1 219 ? 15.847 1.168   6.353   1.00 22.06 ? 219 ALA A C   1 
ATOM   1773 O O   . ALA A 1 219 ? 15.310 0.145   5.936   1.00 22.00 ? 219 ALA A O   1 
ATOM   1774 C CB  . ALA A 1 219 ? 18.130 1.017   7.373   1.00 22.42 ? 219 ALA A CB  1 
ATOM   1775 N N   . GLU A 1 220 ? 15.797 2.343   5.716   1.00 22.28 ? 220 GLU A N   1 
ATOM   1776 C CA  . GLU A 1 220 ? 15.106 2.523   4.448   1.00 22.54 ? 220 GLU A CA  1 
ATOM   1777 C C   . GLU A 1 220 ? 15.822 1.732   3.355   1.00 21.68 ? 220 GLU A C   1 
ATOM   1778 O O   . GLU A 1 220 ? 15.171 1.073   2.546   1.00 20.80 ? 220 GLU A O   1 
ATOM   1779 C CB  . GLU A 1 220 ? 15.052 4.017   4.120   1.00 23.49 ? 220 GLU A CB  1 
ATOM   1780 C CG  . GLU A 1 220 ? 14.407 4.354   2.776   1.00 23.94 ? 220 GLU A CG  1 
ATOM   1781 C CD  . GLU A 1 220 ? 14.653 5.788   2.327   1.00 24.36 ? 220 GLU A CD  1 
ATOM   1782 O OE1 . GLU A 1 220 ? 15.385 6.512   3.035   1.00 24.64 ? 220 GLU A OE1 1 
ATOM   1783 O OE2 . GLU A 1 220 ? 14.118 6.188   1.272   1.00 24.44 ? 220 GLU A OE2 1 
ATOM   1784 N N   . ASP A 1 221 ? 17.162 1.814   3.342   1.00 20.89 ? 221 ASP A N   1 
ATOM   1785 C CA  . ASP A 1 221 ? 17.974 1.106   2.365   1.00 20.58 ? 221 ASP A CA  1 
ATOM   1786 C C   . ASP A 1 221 ? 18.318 -0.276  2.911   1.00 20.78 ? 221 ASP A C   1 
ATOM   1787 O O   . ASP A 1 221 ? 19.414 -0.490  3.428   1.00 20.13 ? 221 ASP A O   1 
ATOM   1788 C CB  . ASP A 1 221 ? 19.212 1.895   1.967   1.00 20.36 ? 221 ASP A CB  1 
ATOM   1789 C CG  . ASP A 1 221 ? 20.039 1.262   0.856   1.00 20.23 ? 221 ASP A CG  1 
ATOM   1790 O OD1 . ASP A 1 221 ? 19.430 0.801   -0.132  1.00 19.79 ? 221 ASP A OD1 1 
ATOM   1791 O OD2 . ASP A 1 221 ? 21.281 1.230   0.985   1.00 19.89 ? 221 ASP A OD2 1 
ATOM   1792 N N   . SER A 1 222 ? 17.365 -1.206  2.777   1.00 21.08 ? 222 SER A N   1 
ATOM   1793 C CA  . SER A 1 222 ? 17.512 -2.551  3.308   1.00 21.16 ? 222 SER A CA  1 
ATOM   1794 C C   . SER A 1 222 ? 16.779 -3.543  2.409   1.00 21.26 ? 222 SER A C   1 
ATOM   1795 O O   . SER A 1 222 ? 15.860 -3.168  1.683   1.00 21.01 ? 222 SER A O   1 
ATOM   1796 C CB  . SER A 1 222 ? 17.008 -2.628  4.732   1.00 21.07 ? 222 SER A CB  1 
ATOM   1797 O OG  . SER A 1 222 ? 15.589 -2.714  4.775   1.00 21.53 ? 222 SER A OG  1 
ATOM   1798 N N   . ALA A 1 223 ? 17.186 -4.815  2.496   1.00 21.50 ? 223 ALA A N   1 
ATOM   1799 C CA  . ALA A 1 223 ? 16.679 -5.864  1.626   1.00 21.92 ? 223 ALA A CA  1 
ATOM   1800 C C   . ALA A 1 223 ? 15.204 -6.150  1.907   1.00 22.20 ? 223 ALA A C   1 
ATOM   1801 O O   . ALA A 1 223 ? 14.434 -6.380  0.976   1.00 20.78 ? 223 ALA A O   1 
ATOM   1802 C CB  . ALA A 1 223 ? 17.517 -7.112  1.791   1.00 21.81 ? 223 ALA A CB  1 
ATOM   1803 N N   . GLU A 1 224 ? 14.823 -6.132  3.191   1.00 22.53 ? 224 GLU A N   1 
ATOM   1804 C CA  . GLU A 1 224 ? 13.477 -6.505  3.601   1.00 23.67 ? 224 GLU A CA  1 
ATOM   1805 C C   . GLU A 1 224 ? 12.476 -5.459  3.119   1.00 23.34 ? 224 GLU A C   1 
ATOM   1806 O O   . GLU A 1 224 ? 11.387 -5.810  2.672   1.00 23.74 ? 224 GLU A O   1 
ATOM   1807 C CB  . GLU A 1 224 ? 13.362 -6.676  5.117   1.00 24.44 ? 224 GLU A CB  1 
ATOM   1808 C CG  . GLU A 1 224 ? 14.055 -7.929  5.646   1.00 24.59 ? 224 GLU A CG  1 
ATOM   1809 C CD  . GLU A 1 224 ? 15.547 -7.977  5.370   1.00 25.04 ? 224 GLU A CD  1 
ATOM   1810 O OE1 . GLU A 1 224 ? 16.219 -6.964  5.652   1.00 25.26 ? 224 GLU A OE1 1 
ATOM   1811 O OE2 . GLU A 1 224 ? 16.039 -9.018  4.883   1.00 26.56 ? 224 GLU A OE2 1 
ATOM   1812 N N   . VAL A 1 225 ? 12.855 -4.179  3.219   1.00 23.28 ? 225 VAL A N   1 
ATOM   1813 C CA  . VAL A 1 225 ? 12.010 -3.085  2.768   1.00 23.02 ? 225 VAL A CA  1 
ATOM   1814 C C   . VAL A 1 225 ? 11.827 -3.199  1.256   1.00 23.26 ? 225 VAL A C   1 
ATOM   1815 O O   . VAL A 1 225 ? 10.710 -3.079  0.756   1.00 23.85 ? 225 VAL A O   1 
ATOM   1816 C CB  . VAL A 1 225 ? 12.586 -1.713  3.170   1.00 22.81 ? 225 VAL A CB  1 
ATOM   1817 C CG1 . VAL A 1 225 ? 11.838 -0.559  2.512   1.00 23.02 ? 225 VAL A CG1 1 
ATOM   1818 C CG2 . VAL A 1 225 ? 12.600 -1.525  4.682   1.00 22.67 ? 225 VAL A CG2 1 
ATOM   1819 N N   . TRP A 1 226 ? 12.935 -3.431  0.543   1.00 23.11 ? 226 TRP A N   1 
ATOM   1820 C CA  . TRP A 1 226 ? 12.904 -3.645  -0.894  1.00 24.08 ? 226 TRP A CA  1 
ATOM   1821 C C   . TRP A 1 226 ? 12.012 -4.838  -1.236  1.00 24.90 ? 226 TRP A C   1 
ATOM   1822 O O   . TRP A 1 226 ? 11.242 -4.777  -2.189  1.00 24.98 ? 226 TRP A O   1 
ATOM   1823 C CB  . TRP A 1 226 ? 14.328 -3.850  -1.426  1.00 23.40 ? 226 TRP A CB  1 
ATOM   1824 C CG  . TRP A 1 226 ? 14.402 -4.140  -2.902  1.00 23.24 ? 226 TRP A CG  1 
ATOM   1825 C CD1 . TRP A 1 226 ? 13.840 -3.425  -3.920  1.00 22.70 ? 226 TRP A CD1 1 
ATOM   1826 C CD2 . TRP A 1 226 ? 15.072 -5.258  -3.523  1.00 23.10 ? 226 TRP A CD2 1 
ATOM   1827 N NE1 . TRP A 1 226 ? 14.127 -4.006  -5.127  1.00 22.50 ? 226 TRP A NE1 1 
ATOM   1828 C CE2 . TRP A 1 226 ? 14.877 -5.132  -4.916  1.00 22.76 ? 226 TRP A CE2 1 
ATOM   1829 C CE3 . TRP A 1 226 ? 15.814 -6.342  -3.041  1.00 23.64 ? 226 TRP A CE3 1 
ATOM   1830 C CZ2 . TRP A 1 226 ? 15.399 -6.051  -5.823  1.00 22.82 ? 226 TRP A CZ2 1 
ATOM   1831 C CZ3 . TRP A 1 226 ? 16.330 -7.249  -3.941  1.00 23.49 ? 226 TRP A CZ3 1 
ATOM   1832 C CH2 . TRP A 1 226 ? 16.124 -7.103  -5.313  1.00 23.29 ? 226 TRP A CH2 1 
ATOM   1833 N N   . ALA A 1 227 ? 12.120 -5.903  -0.431  1.00 26.20 ? 227 ALA A N   1 
ATOM   1834 C CA  . ALA A 1 227 ? 11.465 -7.175  -0.694  1.00 27.62 ? 227 ALA A CA  1 
ATOM   1835 C C   . ALA A 1 227 ? 9.965  -7.123  -0.403  1.00 28.66 ? 227 ALA A C   1 
ATOM   1836 O O   . ALA A 1 227 ? 9.194  -7.772  -1.103  1.00 29.45 ? 227 ALA A O   1 
ATOM   1837 C CB  . ALA A 1 227 ? 12.130 -8.262  0.125   1.00 27.86 ? 227 ALA A CB  1 
ATOM   1838 N N   . HIS A 1 228 ? 9.561  -6.392  0.645   1.00 29.49 ? 228 HIS A N   1 
ATOM   1839 C CA  . HIS A 1 228 ? 8.183  -6.423  1.118   1.00 30.09 ? 228 HIS A CA  1 
ATOM   1840 C C   . HIS A 1 228 ? 7.645  -5.008  1.317   1.00 29.83 ? 228 HIS A C   1 
ATOM   1841 O O   . HIS A 1 228 ? 7.304  -4.630  2.438   1.00 30.24 ? 228 HIS A O   1 
ATOM   1842 C CB  . HIS A 1 228 ? 8.087  -7.235  2.413   1.00 30.49 ? 228 HIS A CB  1 
ATOM   1843 C CG  . HIS A 1 228 ? 8.571  -8.636  2.266   1.00 30.77 ? 228 HIS A CG  1 
ATOM   1844 N ND1 . HIS A 1 228 ? 7.754  -9.674  1.877   1.00 31.12 ? 228 HIS A ND1 1 
ATOM   1845 C CD2 . HIS A 1 228 ? 9.787  -9.164  2.441   1.00 31.57 ? 228 HIS A CD2 1 
ATOM   1846 C CE1 . HIS A 1 228 ? 8.465  -10.791 1.829   1.00 31.31 ? 228 HIS A CE1 1 
ATOM   1847 N NE2 . HIS A 1 228 ? 9.703  -10.504 2.166   1.00 31.29 ? 228 HIS A NE2 1 
ATOM   1848 N N   . PRO A 1 229 ? 7.510  -4.205  0.234   1.00 28.97 ? 229 PRO A N   1 
ATOM   1849 C CA  . PRO A 1 229 ? 7.152  -2.795  0.359   1.00 29.54 ? 229 PRO A CA  1 
ATOM   1850 C C   . PRO A 1 229 ? 5.800  -2.549  1.029   1.00 30.78 ? 229 PRO A C   1 
ATOM   1851 O O   . PRO A 1 229 ? 5.613  -1.520  1.674   1.00 29.99 ? 229 PRO A O   1 
ATOM   1852 C CB  . PRO A 1 229 ? 7.178  -2.279  -1.080  1.00 29.10 ? 229 PRO A CB  1 
ATOM   1853 C CG  . PRO A 1 229 ? 7.026  -3.528  -1.931  1.00 29.06 ? 229 PRO A CG  1 
ATOM   1854 C CD  . PRO A 1 229 ? 7.688  -4.627  -1.166  1.00 29.04 ? 229 PRO A CD  1 
ATOM   1855 N N   . GLU A 1 230 ? 4.867  -3.497  0.871   1.00 32.63 ? 230 GLU A N   1 
ATOM   1856 C CA  . GLU A 1 230 ? 3.539  -3.385  1.458   1.00 34.24 ? 230 GLU A CA  1 
ATOM   1857 C C   . GLU A 1 230 ? 3.633  -3.262  2.982   1.00 33.98 ? 230 GLU A C   1 
ATOM   1858 O O   . GLU A 1 230 ? 2.848  -2.538  3.590   1.00 34.11 ? 230 GLU A O   1 
ATOM   1859 C CB  . GLU A 1 230 ? 2.628  -4.537  1.019   1.00 35.06 ? 230 GLU A CB  1 
ATOM   1860 C CG  . GLU A 1 230 ? 3.023  -5.911  1.556   1.00 36.47 ? 230 GLU A CG  1 
ATOM   1861 C CD  . GLU A 1 230 ? 4.288  -6.520  0.979   1.00 37.18 ? 230 GLU A CD  1 
ATOM   1862 O OE1 . GLU A 1 230 ? 4.819  -5.963  -0.004  1.00 39.38 ? 230 GLU A OE1 1 
ATOM   1863 O OE2 . GLU A 1 230 ? 4.745  -7.551  1.516   1.00 38.60 ? 230 GLU A OE2 1 
ATOM   1864 N N   . TRP A 1 231 ? 4.597  -3.959  3.597   1.00 33.71 ? 231 TRP A N   1 
ATOM   1865 C CA  . TRP A 1 231 ? 4.791  -3.893  5.039   1.00 34.31 ? 231 TRP A CA  1 
ATOM   1866 C C   . TRP A 1 231 ? 5.130  -2.472  5.483   1.00 34.34 ? 231 TRP A C   1 
ATOM   1867 O O   . TRP A 1 231 ? 4.875  -2.108  6.627   1.00 35.21 ? 231 TRP A O   1 
ATOM   1868 C CB  . TRP A 1 231 ? 5.906  -4.845  5.494   1.00 34.12 ? 231 TRP A CB  1 
ATOM   1869 C CG  . TRP A 1 231 ? 5.622  -6.308  5.287   1.00 34.35 ? 231 TRP A CG  1 
ATOM   1870 C CD1 . TRP A 1 231 ? 4.434  -6.897  4.967   1.00 34.57 ? 231 TRP A CD1 1 
ATOM   1871 C CD2 . TRP A 1 231 ? 6.577  -7.381  5.427   1.00 34.43 ? 231 TRP A CD2 1 
ATOM   1872 N NE1 . TRP A 1 231 ? 4.585  -8.256  4.883   1.00 34.04 ? 231 TRP A NE1 1 
ATOM   1873 C CE2 . TRP A 1 231 ? 5.886  -8.583  5.161   1.00 34.65 ? 231 TRP A CE2 1 
ATOM   1874 C CE3 . TRP A 1 231 ? 7.939  -7.439  5.743   1.00 34.93 ? 231 TRP A CE3 1 
ATOM   1875 C CZ2 . TRP A 1 231 ? 6.516  -9.825  5.205   1.00 34.76 ? 231 TRP A CZ2 1 
ATOM   1876 C CZ3 . TRP A 1 231 ? 8.560  -8.668  5.784   1.00 34.82 ? 231 TRP A CZ3 1 
ATOM   1877 C CH2 . TRP A 1 231 ? 7.855  -9.844  5.523   1.00 34.60 ? 231 TRP A CH2 1 
ATOM   1878 N N   . PHE A 1 232 ? 5.751  -1.696  4.590   1.00 34.49 ? 232 PHE A N   1 
ATOM   1879 C CA  . PHE A 1 232 ? 6.189  -0.347  4.907   1.00 34.90 ? 232 PHE A CA  1 
ATOM   1880 C C   . PHE A 1 232 ? 5.238  0.663   4.269   1.00 35.67 ? 232 PHE A C   1 
ATOM   1881 O O   . PHE A 1 232 ? 4.552  0.348   3.299   1.00 35.91 ? 232 PHE A O   1 
ATOM   1882 C CB  . PHE A 1 232 ? 7.652  -0.265  4.459   1.00 33.45 ? 232 PHE A CB  1 
ATOM   1883 C CG  . PHE A 1 232 ? 8.554  -1.211  5.240   1.00 33.10 ? 232 PHE A CG  1 
ATOM   1884 C CD1 . PHE A 1 232 ? 9.089  -0.831  6.468   1.00 32.56 ? 232 PHE A CD1 1 
ATOM   1885 C CD2 . PHE A 1 232 ? 8.842  -2.487  4.762   1.00 32.90 ? 232 PHE A CD2 1 
ATOM   1886 C CE1 . PHE A 1 232 ? 9.908  -1.694  7.183   1.00 32.18 ? 232 PHE A CE1 1 
ATOM   1887 C CE2 . PHE A 1 232 ? 9.654  -3.349  5.486   1.00 31.94 ? 232 PHE A CE2 1 
ATOM   1888 C CZ  . PHE A 1 232 ? 10.185 -2.950  6.692   1.00 32.05 ? 232 PHE A CZ  1 
ATOM   1889 N N   . HIS A 1 233 ? 5.179  1.866   4.855   1.00 36.68 ? 233 HIS A N   1 
ATOM   1890 C CA  . HIS A 1 233 ? 4.419  2.972   4.293   1.00 37.90 ? 233 HIS A CA  1 
ATOM   1891 C C   . HIS A 1 233 ? 5.264  3.656   3.221   1.00 39.22 ? 233 HIS A C   1 
ATOM   1892 O O   . HIS A 1 233 ? 6.066  4.534   3.534   1.00 41.00 ? 233 HIS A O   1 
ATOM   1893 C CB  . HIS A 1 233 ? 4.062  4.006   5.368   1.00 37.22 ? 233 HIS A CB  1 
ATOM   1894 C CG  . HIS A 1 233 ? 3.132  3.546   6.443   1.00 36.69 ? 233 HIS A CG  1 
ATOM   1895 N ND1 . HIS A 1 233 ? 1.770  3.743   6.382   1.00 36.83 ? 233 HIS A ND1 1 
ATOM   1896 C CD2 . HIS A 1 233 ? 3.366  2.954   7.620   1.00 36.97 ? 233 HIS A CD2 1 
ATOM   1897 C CE1 . HIS A 1 233 ? 1.208  3.263   7.484   1.00 37.48 ? 233 HIS A CE1 1 
ATOM   1898 N NE2 . HIS A 1 233 ? 2.160  2.775   8.248   1.00 37.01 ? 233 HIS A NE2 1 
ATOM   1899 N N   . LEU A 1 234 ? 5.079  3.257   1.958   1.00 38.85 ? 234 LEU A N   1 
ATOM   1900 C CA  . LEU A 1 234 ? 5.951  3.707   0.885   1.00 40.17 ? 234 LEU A CA  1 
ATOM   1901 C C   . LEU A 1 234 ? 5.122  4.218   -0.287  1.00 41.30 ? 234 LEU A C   1 
ATOM   1902 O O   . LEU A 1 234 ? 4.080  3.653   -0.609  1.00 42.04 ? 234 LEU A O   1 
ATOM   1903 C CB  . LEU A 1 234 ? 6.861  2.563   0.446   1.00 40.03 ? 234 LEU A CB  1 
ATOM   1904 C CG  . LEU A 1 234 ? 7.855  2.047   1.489   1.00 40.26 ? 234 LEU A CG  1 
ATOM   1905 C CD1 . LEU A 1 234 ? 8.583  0.835   0.940   1.00 40.63 ? 234 LEU A CD1 1 
ATOM   1906 C CD2 . LEU A 1 234 ? 8.850  3.113   1.916   1.00 40.36 ? 234 LEU A CD2 1 
ATOM   1907 N N   . ASP A 1 235 ? 5.625  5.272   -0.939  1.00 42.68 ? 235 ASP A N   1 
ATOM   1908 C CA  . ASP A 1 235 ? 4.977  5.829   -2.113  1.00 44.35 ? 235 ASP A CA  1 
ATOM   1909 C C   . ASP A 1 235 ? 5.311  4.953   -3.321  1.00 45.44 ? 235 ASP A C   1 
ATOM   1910 O O   . ASP A 1 235 ? 6.009  3.947   -3.198  1.00 45.83 ? 235 ASP A O   1 
ATOM   1911 C CB  . ASP A 1 235 ? 5.317  7.304   -2.284  1.00 44.28 ? 235 ASP A CB  1 
ATOM   1912 C CG  . ASP A 1 235 ? 6.736  7.632   -2.725  1.00 45.06 ? 235 ASP A CG  1 
ATOM   1913 O OD1 . ASP A 1 235 ? 7.519  6.686   -2.952  1.00 45.24 ? 235 ASP A OD1 1 
ATOM   1914 O OD2 . ASP A 1 235 ? 7.044  8.839   -2.841  1.00 46.85 ? 235 ASP A OD2 1 
ATOM   1915 N N   . GLU A 1 236 ? 4.809  5.370   -4.487  1.00 46.48 ? 236 GLU A N   1 
ATOM   1916 C CA  . GLU A 1 236 ? 4.991  4.663   -5.747  1.00 47.16 ? 236 GLU A CA  1 
ATOM   1917 C C   . GLU A 1 236 ? 6.478  4.576   -6.090  1.00 47.03 ? 236 GLU A C   1 
ATOM   1918 O O   . GLU A 1 236 ? 6.918  3.615   -6.719  1.00 48.45 ? 236 GLU A O   1 
ATOM   1919 C CB  . GLU A 1 236 ? 4.274  5.378   -6.896  1.00 46.25 ? 236 GLU A CB  1 
ATOM   1920 C CG  . GLU A 1 236 ? 3.049  6.195   -6.483  1.00 46.14 ? 236 GLU A CG  1 
ATOM   1921 C CD  . GLU A 1 236 ? 3.347  7.551   -5.857  1.00 46.92 ? 236 GLU A CD  1 
ATOM   1922 O OE1 . GLU A 1 236 ? 2.392  8.308   -5.579  1.00 46.42 ? 236 GLU A OE1 1 
ATOM   1923 O OE2 . GLU A 1 236 ? 4.537  7.851   -5.626  1.00 48.91 ? 236 GLU A OE2 1 
ATOM   1924 N N   . GLU A 1 237 ? 7.230  5.603   -5.674  1.00 46.81 ? 237 GLU A N   1 
ATOM   1925 C CA  . GLU A 1 237 ? 8.658  5.715   -5.928  1.00 46.71 ? 237 GLU A CA  1 
ATOM   1926 C C   . GLU A 1 237 ? 9.433  4.807   -4.973  1.00 45.14 ? 237 GLU A C   1 
ATOM   1927 O O   . GLU A 1 237 ? 10.599 4.503   -5.215  1.00 43.05 ? 237 GLU A O   1 
ATOM   1928 C CB  . GLU A 1 237 ? 9.144  7.150   -5.703  1.00 47.85 ? 237 GLU A CB  1 
ATOM   1929 C CG  . GLU A 1 237 ? 8.223  8.235   -6.262  1.00 49.86 ? 237 GLU A CG  1 
ATOM   1930 C CD  . GLU A 1 237 ? 8.420  9.620   -5.664  1.00 50.89 ? 237 GLU A CD  1 
ATOM   1931 O OE1 . GLU A 1 237 ? 9.255  9.781   -4.746  1.00 51.77 ? 237 GLU A OE1 1 
ATOM   1932 O OE2 . GLU A 1 237 ? 7.719  10.549  -6.120  1.00 52.23 ? 237 GLU A OE2 1 
ATOM   1933 N N   . GLY A 1 238 ? 8.783  4.413   -3.870  1.00 43.90 ? 238 GLY A N   1 
ATOM   1934 C CA  . GLY A 1 238 ? 9.428  3.670   -2.802  1.00 41.98 ? 238 GLY A CA  1 
ATOM   1935 C C   . GLY A 1 238 ? 10.013 4.606   -1.746  1.00 41.62 ? 238 GLY A C   1 
ATOM   1936 O O   . GLY A 1 238 ? 10.692 4.148   -0.830  1.00 40.27 ? 238 GLY A O   1 
ATOM   1937 N N   . ARG A 1 239 ? 9.754  5.915   -1.892  1.00 41.21 ? 239 ARG A N   1 
ATOM   1938 C CA  . ARG A 1 239 ? 10.135 6.903   -0.894  1.00 41.68 ? 239 ARG A CA  1 
ATOM   1939 C C   . ARG A 1 239 ? 9.143  6.831   0.264   1.00 40.01 ? 239 ARG A C   1 
ATOM   1940 O O   . ARG A 1 239 ? 7.938  6.742   0.033   1.00 40.25 ? 239 ARG A O   1 
ATOM   1941 C CB  . ARG A 1 239 ? 10.175 8.310   -1.507  1.00 43.02 ? 239 ARG A CB  1 
ATOM   1942 C CG  . ARG A 1 239 ? 10.102 9.460   -0.511  1.00 44.10 ? 239 ARG A CG  1 
ATOM   1943 C CD  . ARG A 1 239 ? 10.305 10.819  -1.167  1.00 45.43 ? 239 ARG A CD  1 
ATOM   1944 N NE  . ARG A 1 239 ? 10.406 11.905  -0.185  1.00 46.61 ? 239 ARG A NE  1 
ATOM   1945 C CZ  . ARG A 1 239 ? 10.646 13.183  -0.471  1.00 48.06 ? 239 ARG A CZ  1 
ATOM   1946 N NH1 . ARG A 1 239 ? 10.797 13.574  -1.725  1.00 48.09 ? 239 ARG A NH1 1 
ATOM   1947 N NH2 . ARG A 1 239 ? 10.735 14.072  0.505   1.00 48.96 ? 239 ARG A NH2 1 
ATOM   1948 N N   . PRO A 1 240 ? 9.596  6.874   1.540   1.00 38.14 ? 240 PRO A N   1 
ATOM   1949 C CA  . PRO A 1 240 ? 8.669  6.798   2.664   1.00 36.87 ? 240 PRO A CA  1 
ATOM   1950 C C   . PRO A 1 240 ? 7.704  7.981   2.702   1.00 34.78 ? 240 PRO A C   1 
ATOM   1951 O O   . PRO A 1 240 ? 8.120  9.126   2.533   1.00 34.56 ? 240 PRO A O   1 
ATOM   1952 C CB  . PRO A 1 240 ? 9.576  6.726   3.894   1.00 37.26 ? 240 PRO A CB  1 
ATOM   1953 C CG  . PRO A 1 240 ? 10.976 6.471   3.359   1.00 37.44 ? 240 PRO A CG  1 
ATOM   1954 C CD  . PRO A 1 240 ? 11.000 7.006   1.963   1.00 38.21 ? 240 PRO A CD  1 
ATOM   1955 N N   . THR A 1 241 ? 6.412  7.686   2.898   1.00 32.75 ? 241 THR A N   1 
ATOM   1956 C CA  . THR A 1 241 ? 5.383  8.711   3.002   1.00 30.68 ? 241 THR A CA  1 
ATOM   1957 C C   . THR A 1 241 ? 5.479  9.372   4.375   1.00 29.24 ? 241 THR A C   1 
ATOM   1958 O O   . THR A 1 241 ? 5.128  10.540  4.534   1.00 28.40 ? 241 THR A O   1 
ATOM   1959 C CB  . THR A 1 241 ? 3.999  8.098   2.787   1.00 30.85 ? 241 THR A CB  1 
ATOM   1960 O OG1 . THR A 1 241 ? 3.828  7.132   3.819   1.00 31.32 ? 241 THR A OG1 1 
ATOM   1961 C CG2 . THR A 1 241 ? 3.850  7.432   1.433   1.00 31.43 ? 241 THR A CG2 1 
ATOM   1962 N N   . VAL A 1 242 ? 5.931  8.585   5.359   1.00 28.03 ? 242 VAL A N   1 
ATOM   1963 C CA  . VAL A 1 242 ? 6.150  9.040   6.721   1.00 27.53 ? 242 VAL A CA  1 
ATOM   1964 C C   . VAL A 1 242 ? 7.449  8.413   7.223   1.00 27.03 ? 242 VAL A C   1 
ATOM   1965 O O   . VAL A 1 242 ? 7.867  7.374   6.715   1.00 27.11 ? 242 VAL A O   1 
ATOM   1966 C CB  . VAL A 1 242 ? 4.961  8.678   7.633   1.00 27.79 ? 242 VAL A CB  1 
ATOM   1967 C CG1 . VAL A 1 242 ? 3.717  9.495   7.302   1.00 27.78 ? 242 VAL A CG1 1 
ATOM   1968 C CG2 . VAL A 1 242 ? 4.643  7.187   7.597   1.00 28.01 ? 242 VAL A CG2 1 
ATOM   1969 N N   . VAL A 1 243 ? 8.074  9.050   8.221   1.00 26.15 ? 243 VAL A N   1 
ATOM   1970 C CA  . VAL A 1 243 ? 9.366  8.609   8.725   1.00 25.74 ? 243 VAL A CA  1 
ATOM   1971 C C   . VAL A 1 243 ? 9.319  8.501   10.249  1.00 24.93 ? 243 VAL A C   1 
ATOM   1972 O O   . VAL A 1 243 ? 8.611  9.252   10.917  1.00 24.38 ? 243 VAL A O   1 
ATOM   1973 C CB  . VAL A 1 243 ? 10.507 9.541   8.277   1.00 26.09 ? 243 VAL A CB  1 
ATOM   1974 C CG1 . VAL A 1 243 ? 10.747 9.459   6.774   1.00 26.65 ? 243 VAL A CG1 1 
ATOM   1975 C CG2 . VAL A 1 243 ? 10.282 10.986  8.704   1.00 26.35 ? 243 VAL A CG2 1 
ATOM   1976 N N   . ALA A 1 244 ? 10.108 7.562   10.782  1.00 24.14 ? 244 ALA A N   1 
ATOM   1977 C CA  . ALA A 1 244 ? 10.224 7.366   12.216  1.00 24.14 ? 244 ALA A CA  1 
ATOM   1978 C C   . ALA A 1 244 ? 10.946 8.558   12.837  1.00 24.35 ? 244 ALA A C   1 
ATOM   1979 O O   . ALA A 1 244 ? 11.793 9.184   12.199  1.00 24.51 ? 244 ALA A O   1 
ATOM   1980 C CB  . ALA A 1 244 ? 10.946 6.069   12.503  1.00 24.67 ? 244 ALA A CB  1 
ATOM   1981 N N   . GLY A 1 245 ? 10.588 8.866   14.086  1.00 24.10 ? 245 GLY A N   1 
ATOM   1982 C CA  . GLY A 1 245 ? 11.219 9.953   14.814  1.00 24.16 ? 245 GLY A CA  1 
ATOM   1983 C C   . GLY A 1 245 ? 10.813 9.941   16.283  1.00 24.25 ? 245 GLY A C   1 
ATOM   1984 O O   . GLY A 1 245 ? 10.112 9.039   16.733  1.00 24.31 ? 245 GLY A O   1 
ATOM   1985 N N   . VAL A 1 246 ? 11.285 10.949  17.021  1.00 25.24 ? 246 VAL A N   1 
ATOM   1986 C CA  . VAL A 1 246 ? 10.924 11.130  18.415  1.00 25.79 ? 246 VAL A CA  1 
ATOM   1987 C C   . VAL A 1 246 ? 10.502 12.586  18.586  1.00 26.72 ? 246 VAL A C   1 
ATOM   1988 O O   . VAL A 1 246 ? 11.179 13.484  18.089  1.00 27.72 ? 246 VAL A O   1 
ATOM   1989 C CB  . VAL A 1 246 ? 12.079 10.754  19.365  1.00 26.11 ? 246 VAL A CB  1 
ATOM   1990 C CG1 . VAL A 1 246 ? 13.249 11.724  19.268  1.00 25.82 ? 246 VAL A CG1 1 
ATOM   1991 C CG2 . VAL A 1 246 ? 11.620 10.633  20.813  1.00 26.85 ? 246 VAL A CG2 1 
ATOM   1992 N N   . PRO A 1 247 ? 9.382  12.876  19.286  1.00 27.83 ? 247 PRO A N   1 
ATOM   1993 C CA  . PRO A 1 247 ? 8.916  14.249  19.416  1.00 28.20 ? 247 PRO A CA  1 
ATOM   1994 C C   . PRO A 1 247 ? 9.879  15.124  20.212  1.00 27.70 ? 247 PRO A C   1 
ATOM   1995 O O   . PRO A 1 247 ? 10.744 14.616  20.923  1.00 25.91 ? 247 PRO A O   1 
ATOM   1996 C CB  . PRO A 1 247 ? 7.571  14.105  20.119  1.00 28.29 ? 247 PRO A CB  1 
ATOM   1997 C CG  . PRO A 1 247 ? 7.758  12.833  20.920  1.00 28.25 ? 247 PRO A CG  1 
ATOM   1998 C CD  . PRO A 1 247 ? 8.534  11.924  20.022  1.00 28.18 ? 247 PRO A CD  1 
ATOM   1999 N N   . PRO A 1 248 ? 9.765  16.466  20.107  1.00 28.82 ? 248 PRO A N   1 
ATOM   2000 C CA  . PRO A 1 248 ? 10.547 17.371  20.942  1.00 29.36 ? 248 PRO A CA  1 
ATOM   2001 C C   . PRO A 1 248 ? 10.421 17.083  22.434  1.00 30.06 ? 248 PRO A C   1 
ATOM   2002 O O   . PRO A 1 248 ? 9.329  16.628  22.844  1.00 31.93 ? 248 PRO A O   1 
ATOM   2003 C CB  . PRO A 1 248 ? 10.002 18.750  20.587  1.00 29.52 ? 248 PRO A CB  1 
ATOM   2004 C CG  . PRO A 1 248 ? 9.454  18.560  19.187  1.00 29.75 ? 248 PRO A CG  1 
ATOM   2005 C CD  . PRO A 1 248 ? 8.900  17.174  19.151  1.00 29.39 ? 248 PRO A CD  1 
ATOM   2006 N N   . SER A 1 252 ? 14.856 16.580  24.509  1.00 39.90 ? 252 SER A N   1 
ATOM   2007 C CA  . SER A 1 252 ? 15.249 16.978  23.130  1.00 39.56 ? 252 SER A CA  1 
ATOM   2008 C C   . SER A 1 252 ? 14.300 18.069  22.637  1.00 38.45 ? 252 SER A C   1 
ATOM   2009 O O   . SER A 1 252 ? 13.139 17.790  22.364  1.00 39.31 ? 252 SER A O   1 
ATOM   2010 C CB  . SER A 1 252 ? 15.263 15.775  22.207  1.00 39.60 ? 252 SER A CB  1 
ATOM   2011 O OG  . SER A 1 252 ? 15.711 16.118  20.903  1.00 40.12 ? 252 SER A OG  1 
ATOM   2012 N N   . GLU A 1 253 ? 14.801 19.309  22.551  1.00 37.29 ? 253 GLU A N   1 
ATOM   2013 C CA  . GLU A 1 253 ? 13.974 20.471  22.258  1.00 36.16 ? 253 GLU A CA  1 
ATOM   2014 C C   . GLU A 1 253 ? 13.617 20.518  20.773  1.00 35.25 ? 253 GLU A C   1 
ATOM   2015 O O   . GLU A 1 253 ? 12.602 21.098  20.403  1.00 36.52 ? 253 GLU A O   1 
ATOM   2016 C CB  . GLU A 1 253 ? 14.688 21.755  22.680  1.00 36.28 ? 253 GLU A CB  1 
ATOM   2017 C CG  . GLU A 1 253 ? 15.031 21.801  24.167  1.00 36.78 ? 253 GLU A CG  1 
ATOM   2018 C CD  . GLU A 1 253 ? 15.907 22.973  24.571  1.00 36.89 ? 253 GLU A CD  1 
ATOM   2019 O OE1 . GLU A 1 253 ? 15.450 24.121  24.413  1.00 37.56 ? 253 GLU A OE1 1 
ATOM   2020 O OE2 . GLU A 1 253 ? 17.043 22.740  25.040  1.00 37.48 ? 253 GLU A OE2 1 
ATOM   2021 N N   . THR A 1 254 ? 14.464 19.922  19.926  1.00 34.49 ? 254 THR A N   1 
ATOM   2022 C CA  . THR A 1 254 ? 14.206 19.848  18.495  1.00 34.11 ? 254 THR A CA  1 
ATOM   2023 C C   . THR A 1 254 ? 13.319 18.645  18.185  1.00 32.49 ? 254 THR A C   1 
ATOM   2024 O O   . THR A 1 254 ? 12.584 18.656  17.203  1.00 32.63 ? 254 THR A O   1 
ATOM   2025 C CB  . THR A 1 254 ? 15.527 19.739  17.732  1.00 34.57 ? 254 THR A CB  1 
ATOM   2026 O OG1 . THR A 1 254 ? 16.117 18.520  18.171  1.00 35.31 ? 254 THR A OG1 1 
ATOM   2027 C CG2 . THR A 1 254 ? 16.469 20.899  17.998  1.00 34.61 ? 254 THR A CG2 1 
ATOM   2028 N N   . GLY A 1 255 ? 13.408 17.605  19.024  1.00 31.23 ? 255 GLY A N   1 
ATOM   2029 C CA  . GLY A 1 255 ? 12.979 16.269  18.645  1.00 29.76 ? 255 GLY A CA  1 
ATOM   2030 C C   . GLY A 1 255 ? 14.060 15.611  17.792  1.00 28.50 ? 255 GLY A C   1 
ATOM   2031 O O   . GLY A 1 255 ? 15.163 16.141  17.684  1.00 28.70 ? 255 GLY A O   1 
ATOM   2032 N N   . GLN A 1 256 ? 13.749 14.457  17.193  1.00 26.92 ? 256 GLN A N   1 
ATOM   2033 C CA  . GLN A 1 256 ? 14.685 13.819  16.279  1.00 27.36 ? 256 GLN A CA  1 
ATOM   2034 C C   . GLN A 1 256 ? 13.921 13.181  15.124  1.00 26.51 ? 256 GLN A C   1 
ATOM   2035 O O   . GLN A 1 256 ? 12.939 12.477  15.338  1.00 26.49 ? 256 GLN A O   1 
ATOM   2036 C CB  . GLN A 1 256 ? 15.561 12.768  16.963  1.00 27.32 ? 256 GLN A CB  1 
ATOM   2037 C CG  . GLN A 1 256 ? 16.265 13.257  18.225  1.00 27.74 ? 256 GLN A CG  1 
ATOM   2038 C CD  . GLN A 1 256 ? 16.957 12.153  18.995  1.00 28.19 ? 256 GLN A CD  1 
ATOM   2039 O OE1 . GLN A 1 256 ? 16.958 10.984  18.593  1.00 27.42 ? 256 GLN A OE1 1 
ATOM   2040 N NE2 . GLN A 1 256 ? 17.547 12.515  20.126  1.00 28.38 ? 256 GLN A NE2 1 
ATOM   2041 N N   . ARG A 1 257 ? 14.405 13.432  13.903  1.00 26.41 ? 257 ARG A N   1 
ATOM   2042 C CA  . ARG A 1 257 ? 13.861 12.825  12.699  1.00 27.15 ? 257 ARG A CA  1 
ATOM   2043 C C   . ARG A 1 257 ? 14.854 11.782  12.192  1.00 26.65 ? 257 ARG A C   1 
ATOM   2044 O O   . ARG A 1 257 ? 15.886 12.134  11.620  1.00 26.55 ? 257 ARG A O   1 
ATOM   2045 C CB  . ARG A 1 257 ? 13.590 13.936  11.679  1.00 27.56 ? 257 ARG A CB  1 
ATOM   2046 C CG  . ARG A 1 257 ? 12.809 13.527  10.438  1.00 28.28 ? 257 ARG A CG  1 
ATOM   2047 C CD  . ARG A 1 257 ? 12.534 14.763  9.588   1.00 28.77 ? 257 ARG A CD  1 
ATOM   2048 N NE  . ARG A 1 257 ? 11.915 14.484  8.288   1.00 29.54 ? 257 ARG A NE  1 
ATOM   2049 C CZ  . ARG A 1 257 ? 12.490 13.861  7.265   1.00 30.69 ? 257 ARG A CZ  1 
ATOM   2050 N NH1 . ARG A 1 257 ? 13.719 13.381  7.362   1.00 31.62 ? 257 ARG A NH1 1 
ATOM   2051 N NH2 . ARG A 1 257 ? 11.830 13.726  6.130   1.00 31.35 ? 257 ARG A NH2 1 
ATOM   2052 N N   . TRP A 1 258 ? 14.530 10.502  12.419  1.00 26.01 ? 258 TRP A N   1 
ATOM   2053 C CA  . TRP A 1 258 ? 15.442 9.400   12.147  1.00 25.44 ? 258 TRP A CA  1 
ATOM   2054 C C   . TRP A 1 258 ? 15.398 9.023   10.669  1.00 24.73 ? 258 TRP A C   1 
ATOM   2055 O O   . TRP A 1 258 ? 16.430 8.714   10.077  1.00 23.32 ? 258 TRP A O   1 
ATOM   2056 C CB  . TRP A 1 258 ? 15.108 8.201   13.048  1.00 25.49 ? 258 TRP A CB  1 
ATOM   2057 C CG  . TRP A 1 258 ? 15.305 8.482   14.515  1.00 25.42 ? 258 TRP A CG  1 
ATOM   2058 C CD1 . TRP A 1 258 ? 16.156 9.396   15.067  1.00 25.58 ? 258 TRP A CD1 1 
ATOM   2059 C CD2 . TRP A 1 258 ? 14.634 7.844   15.624  1.00 25.96 ? 258 TRP A CD2 1 
ATOM   2060 N NE1 . TRP A 1 258 ? 16.064 9.372   16.433  1.00 25.44 ? 258 TRP A NE1 1 
ATOM   2061 C CE2 . TRP A 1 258 ? 15.141 8.433   16.804  1.00 25.72 ? 258 TRP A CE2 1 
ATOM   2062 C CE3 . TRP A 1 258 ? 13.662 6.844   15.735  1.00 26.64 ? 258 TRP A CE3 1 
ATOM   2063 C CZ2 . TRP A 1 258 ? 14.707 8.051   18.072  1.00 26.70 ? 258 TRP A CZ2 1 
ATOM   2064 C CZ3 . TRP A 1 258 ? 13.232 6.469   16.990  1.00 26.98 ? 258 TRP A CZ3 1 
ATOM   2065 C CH2 . TRP A 1 258 ? 13.749 7.064   18.141  1.00 26.90 ? 258 TRP A CH2 1 
ATOM   2066 N N   . GLY A 1 259 ? 14.197 9.048   10.085  1.00 24.63 ? 259 GLY A N   1 
ATOM   2067 C CA  . GLY A 1 259 ? 14.029 8.810   8.661   1.00 24.75 ? 259 GLY A CA  1 
ATOM   2068 C C   . GLY A 1 259 ? 13.626 7.368   8.367   1.00 24.18 ? 259 GLY A C   1 
ATOM   2069 O O   . GLY A 1 259 ? 13.309 7.038   7.228   1.00 24.03 ? 259 GLY A O   1 
ATOM   2070 N N   . ASN A 1 260 ? 13.649 6.513   9.397   1.00 24.68 ? 260 ASN A N   1 
ATOM   2071 C CA  . ASN A 1 260 ? 13.416 5.090   9.209   1.00 24.97 ? 260 ASN A CA  1 
ATOM   2072 C C   . ASN A 1 260 ? 11.987 4.871   8.719   1.00 24.57 ? 260 ASN A C   1 
ATOM   2073 O O   . ASN A 1 260 ? 11.071 5.584   9.131   1.00 22.61 ? 260 ASN A O   1 
ATOM   2074 C CB  . ASN A 1 260 ? 13.677 4.288   10.478  1.00 25.39 ? 260 ASN A CB  1 
ATOM   2075 C CG  . ASN A 1 260 ? 15.138 4.266   10.857  1.00 26.74 ? 260 ASN A CG  1 
ATOM   2076 O OD1 . ASN A 1 260 ? 15.704 5.305   11.216  1.00 28.12 ? 260 ASN A OD1 1 
ATOM   2077 N ND2 . ASN A 1 260 ? 15.759 3.096   10.801  1.00 26.99 ? 260 ASN A ND2 1 
ATOM   2078 N N   . PRO A 1 261 ? 11.754 3.874   7.832   1.00 24.88 ? 261 PRO A N   1 
ATOM   2079 C CA  . PRO A 1 261 ? 10.404 3.547   7.392   1.00 25.16 ? 261 PRO A CA  1 
ATOM   2080 C C   . PRO A 1 261 ? 9.562  2.964   8.519   1.00 25.98 ? 261 PRO A C   1 
ATOM   2081 O O   . PRO A 1 261 ? 10.058 2.184   9.330   1.00 26.92 ? 261 PRO A O   1 
ATOM   2082 C CB  . PRO A 1 261 ? 10.626 2.540   6.269   1.00 25.30 ? 261 PRO A CB  1 
ATOM   2083 C CG  . PRO A 1 261 ? 11.932 1.879   6.680   1.00 25.40 ? 261 PRO A CG  1 
ATOM   2084 C CD  . PRO A 1 261 ? 12.767 2.991   7.237   1.00 25.05 ? 261 PRO A CD  1 
ATOM   2085 N N   . LEU A 1 262 ? 8.289  3.364   8.564   1.00 25.60 ? 262 LEU A N   1 
ATOM   2086 C CA  . LEU A 1 262 ? 7.375  2.897   9.589   1.00 24.91 ? 262 LEU A CA  1 
ATOM   2087 C C   . LEU A 1 262 ? 6.574  1.720   9.039   1.00 24.15 ? 262 LEU A C   1 
ATOM   2088 O O   . LEU A 1 262 ? 6.391  1.592   7.829   1.00 21.78 ? 262 LEU A O   1 
ATOM   2089 C CB  . LEU A 1 262 ? 6.515  4.081   10.030  1.00 25.24 ? 262 LEU A CB  1 
ATOM   2090 C CG  . LEU A 1 262 ? 7.283  5.202   10.740  1.00 25.66 ? 262 LEU A CG  1 
ATOM   2091 C CD1 . LEU A 1 262 ? 6.487  6.493   10.864  1.00 25.14 ? 262 LEU A CD1 1 
ATOM   2092 C CD2 . LEU A 1 262 ? 7.735  4.719   12.111  1.00 26.00 ? 262 LEU A CD2 1 
ATOM   2093 N N   . TYR A 1 263 ? 6.144  0.837   9.947   1.00 24.01 ? 263 TYR A N   1 
ATOM   2094 C CA  . TYR A 1 263 ? 5.479  -0.394  9.560   1.00 23.72 ? 263 TYR A CA  1 
ATOM   2095 C C   . TYR A 1 263 ? 3.996  -0.114  9.347   1.00 24.62 ? 263 TYR A C   1 
ATOM   2096 O O   . TYR A 1 263 ? 3.374  0.595   10.136  1.00 22.54 ? 263 TYR A O   1 
ATOM   2097 C CB  . TYR A 1 263 ? 5.611  -1.496  10.615  1.00 23.24 ? 263 TYR A CB  1 
ATOM   2098 C CG  . TYR A 1 263 ? 7.033  -1.919  10.964  1.00 22.47 ? 263 TYR A CG  1 
ATOM   2099 C CD1 . TYR A 1 263 ? 7.756  -2.790  10.154  1.00 22.09 ? 263 TYR A CD1 1 
ATOM   2100 C CD2 . TYR A 1 263 ? 7.642  -1.465  12.127  1.00 22.10 ? 263 TYR A CD2 1 
ATOM   2101 C CE1 . TYR A 1 263 ? 9.046  -3.180  10.484  1.00 21.75 ? 263 TYR A CE1 1 
ATOM   2102 C CE2 . TYR A 1 263 ? 8.928  -1.844  12.465  1.00 21.95 ? 263 TYR A CE2 1 
ATOM   2103 C CZ  . TYR A 1 263 ? 9.634  -2.705  11.644  1.00 21.85 ? 263 TYR A CZ  1 
ATOM   2104 O OH  . TYR A 1 263 ? 10.902 -3.067  12.010  1.00 21.52 ? 263 TYR A OH  1 
ATOM   2105 N N   . ARG A 1 264 ? 3.446  -0.685  8.272   1.00 25.60 ? 264 ARG A N   1 
ATOM   2106 C CA  . ARG A 1 264 ? 2.010  -0.842  8.145   1.00 27.58 ? 264 ARG A CA  1 
ATOM   2107 C C   . ARG A 1 264 ? 1.592  -1.970  9.082   1.00 27.29 ? 264 ARG A C   1 
ATOM   2108 O O   . ARG A 1 264 ? 1.566  -3.130  8.683   1.00 27.24 ? 264 ARG A O   1 
ATOM   2109 C CB  . ARG A 1 264 ? 1.613  -1.093  6.686   1.00 28.96 ? 264 ARG A CB  1 
ATOM   2110 C CG  . ARG A 1 264 ? 1.896  0.097   5.780   1.00 30.18 ? 264 ARG A CG  1 
ATOM   2111 C CD  . ARG A 1 264 ? 0.805  0.356   4.750   1.00 32.26 ? 264 ARG A CD  1 
ATOM   2112 N NE  . ARG A 1 264 ? -0.514 0.438   5.390   1.00 33.88 ? 264 ARG A NE  1 
ATOM   2113 C CZ  . ARG A 1 264 ? -1.340 1.480   5.418   1.00 36.18 ? 264 ARG A CZ  1 
ATOM   2114 N NH1 . ARG A 1 264 ? -2.412 1.438   6.192   1.00 37.92 ? 264 ARG A NH1 1 
ATOM   2115 N NH2 . ARG A 1 264 ? -1.091 2.569   4.711   1.00 36.40 ? 264 ARG A NH2 1 
ATOM   2116 N N   . TRP A 1 265 ? 1.301  -1.607  10.338  1.00 27.97 ? 265 TRP A N   1 
ATOM   2117 C CA  . TRP A 1 265 ? 1.037  -2.572  11.393  1.00 28.80 ? 265 TRP A CA  1 
ATOM   2118 C C   . TRP A 1 265 ? -0.207 -3.400  11.080  1.00 31.23 ? 265 TRP A C   1 
ATOM   2119 O O   . TRP A 1 265 ? -0.230 -4.598  11.350  1.00 31.91 ? 265 TRP A O   1 
ATOM   2120 C CB  . TRP A 1 265 ? 0.919  -1.863  12.750  1.00 28.29 ? 265 TRP A CB  1 
ATOM   2121 C CG  . TRP A 1 265 ? 2.262  -1.575  13.364  1.00 27.26 ? 265 TRP A CG  1 
ATOM   2122 C CD1 . TRP A 1 265 ? 2.962  -0.405  13.333  1.00 26.64 ? 265 TRP A CD1 1 
ATOM   2123 C CD2 . TRP A 1 265 ? 3.095  -2.524  14.065  1.00 27.01 ? 265 TRP A CD2 1 
ATOM   2124 N NE1 . TRP A 1 265 ? 4.158  -0.552  13.985  1.00 27.19 ? 265 TRP A NE1 1 
ATOM   2125 C CE2 . TRP A 1 265 ? 4.271  -1.840  14.440  1.00 26.50 ? 265 TRP A CE2 1 
ATOM   2126 C CE3 . TRP A 1 265 ? 2.958  -3.874  14.412  1.00 26.77 ? 265 TRP A CE3 1 
ATOM   2127 C CZ2 . TRP A 1 265 ? 5.299  -2.464  15.144  1.00 26.97 ? 265 TRP A CZ2 1 
ATOM   2128 C CZ3 . TRP A 1 265 ? 3.976  -4.490  15.106  1.00 26.66 ? 265 TRP A CZ3 1 
ATOM   2129 C CH2 . TRP A 1 265 ? 5.133  -3.794  15.462  1.00 26.86 ? 265 TRP A CH2 1 
ATOM   2130 N N   . ASP A 1 266 ? -1.228 -2.749  10.513  1.00 33.75 ? 266 ASP A N   1 
ATOM   2131 C CA  . ASP A 1 266 ? -2.446 -3.427  10.096  1.00 36.46 ? 266 ASP A CA  1 
ATOM   2132 C C   . ASP A 1 266 ? -2.098 -4.596  9.176   1.00 37.96 ? 266 ASP A C   1 
ATOM   2133 O O   . ASP A 1 266 ? -2.579 -5.707  9.386   1.00 39.19 ? 266 ASP A O   1 
ATOM   2134 C CB  . ASP A 1 266 ? -3.439 -2.454  9.473   1.00 37.08 ? 266 ASP A CB  1 
ATOM   2135 C CG  . ASP A 1 266 ? -2.891 -1.541  8.383   1.00 38.41 ? 266 ASP A CG  1 
ATOM   2136 O OD1 . ASP A 1 266 ? -1.671 -1.608  8.115   1.00 40.70 ? 266 ASP A OD1 1 
ATOM   2137 O OD2 . ASP A 1 266 ? -3.686 -0.764  7.815   1.00 38.94 ? 266 ASP A OD2 1 
ATOM   2138 N N   . VAL A 1 267 ? -1.240 -4.339  8.178   1.00 38.25 ? 267 VAL A N   1 
ATOM   2139 C CA  . VAL A 1 267 ? -0.844 -5.354  7.212   1.00 38.54 ? 267 VAL A CA  1 
ATOM   2140 C C   . VAL A 1 267 ? -0.170 -6.510  7.950   1.00 38.58 ? 267 VAL A C   1 
ATOM   2141 O O   . VAL A 1 267 ? -0.490 -7.672  7.710   1.00 37.88 ? 267 VAL A O   1 
ATOM   2142 C CB  . VAL A 1 267 ? 0.070  -4.772  6.113   1.00 39.11 ? 267 VAL A CB  1 
ATOM   2143 C CG1 . VAL A 1 267 ? 0.640  -5.855  5.204   1.00 39.25 ? 267 VAL A CG1 1 
ATOM   2144 C CG2 . VAL A 1 267 ? -0.645 -3.712  5.282   1.00 38.82 ? 267 VAL A CG2 1 
ATOM   2145 N N   . LEU A 1 268 ? 0.753  -6.174  8.859   1.00 39.09 ? 268 LEU A N   1 
ATOM   2146 C CA  . LEU A 1 268 ? 1.481  -7.164  9.639   1.00 38.78 ? 268 LEU A CA  1 
ATOM   2147 C C   . LEU A 1 268 ? 0.524  -7.936  10.548  1.00 39.37 ? 268 LEU A C   1 
ATOM   2148 O O   . LEU A 1 268 ? 0.676  -9.144  10.716  1.00 38.88 ? 268 LEU A O   1 
ATOM   2149 C CB  . LEU A 1 268 ? 2.582  -6.473  10.445  1.00 38.47 ? 268 LEU A CB  1 
ATOM   2150 C CG  . LEU A 1 268 ? 3.678  -5.767  9.637   1.00 38.07 ? 268 LEU A CG  1 
ATOM   2151 C CD1 . LEU A 1 268 ? 4.650  -5.059  10.568  1.00 37.97 ? 268 LEU A CD1 1 
ATOM   2152 C CD2 . LEU A 1 268 ? 4.426  -6.725  8.726   1.00 37.16 ? 268 LEU A CD2 1 
ATOM   2153 N N   . GLU A 1 269 ? -0.457 -7.234  11.129  1.00 41.12 ? 269 GLU A N   1 
ATOM   2154 C CA  . GLU A 1 269 ? -1.428 -7.850  12.020  1.00 42.85 ? 269 GLU A CA  1 
ATOM   2155 C C   . GLU A 1 269 ? -2.267 -8.859  11.237  1.00 43.22 ? 269 GLU A C   1 
ATOM   2156 O O   . GLU A 1 269 ? -2.486 -9.976  11.703  1.00 43.53 ? 269 GLU A O   1 
ATOM   2157 C CB  . GLU A 1 269 ? -2.296 -6.792  12.705  1.00 43.94 ? 269 GLU A CB  1 
ATOM   2158 C CG  . GLU A 1 269 ? -3.350 -7.382  13.640  1.00 44.99 ? 269 GLU A CG  1 
ATOM   2159 C CD  . GLU A 1 269 ? -4.134 -6.372  14.461  1.00 46.66 ? 269 GLU A CD  1 
ATOM   2160 O OE1 . GLU A 1 269 ? -3.836 -5.161  14.384  1.00 48.44 ? 269 GLU A OE1 1 
ATOM   2161 O OE2 . GLU A 1 269 ? -5.057 -6.805  15.185  1.00 48.30 ? 269 GLU A OE2 1 
ATOM   2162 N N   . ARG A 1 270 ? -2.724 -8.457  10.045  1.00 42.26 ? 270 ARG A N   1 
ATOM   2163 C CA  . ARG A 1 270 ? -3.386 -9.373  9.129   1.00 43.09 ? 270 ARG A CA  1 
ATOM   2164 C C   . ARG A 1 270 ? -2.528 -10.623 8.945   1.00 42.73 ? 270 ARG A C   1 
ATOM   2165 O O   . ARG A 1 270 ? -3.046 -11.736 8.969   1.00 41.82 ? 270 ARG A O   1 
ATOM   2166 C CB  . ARG A 1 270 ? -3.632 -8.759  7.744   1.00 43.72 ? 270 ARG A CB  1 
ATOM   2167 C CG  . ARG A 1 270 ? -4.632 -7.614  7.667   1.00 44.80 ? 270 ARG A CG  1 
ATOM   2168 C CD  . ARG A 1 270 ? -4.952 -7.289  6.213   1.00 45.52 ? 270 ARG A CD  1 
ATOM   2169 N NE  . ARG A 1 270 ? -5.744 -6.065  6.042   1.00 46.02 ? 270 ARG A NE  1 
ATOM   2170 C CZ  . ARG A 1 270 ? -5.443 -5.049  5.233   1.00 46.59 ? 270 ARG A CZ  1 
ATOM   2171 N NH1 . ARG A 1 270 ? -6.226 -3.984  5.190   1.00 46.41 ? 270 ARG A NH1 1 
ATOM   2172 N NH2 . ARG A 1 270 ? -4.362 -5.089  4.472   1.00 46.40 ? 270 ARG A NH2 1 
ATOM   2173 N N   . GLU A 1 271 ? -1.213 -10.420 8.778   1.00 44.06 ? 271 GLU A N   1 
ATOM   2174 C CA  . GLU A 1 271 ? -0.289 -11.486 8.421   1.00 44.26 ? 271 GLU A CA  1 
ATOM   2175 C C   . GLU A 1 271 ? 0.148  -12.296 9.643   1.00 43.33 ? 271 GLU A C   1 
ATOM   2176 O O   . GLU A 1 271 ? 0.965  -13.208 9.514   1.00 44.34 ? 271 GLU A O   1 
ATOM   2177 C CB  . GLU A 1 271 ? 0.944  -10.911 7.722   1.00 46.27 ? 271 GLU A CB  1 
ATOM   2178 C CG  . GLU A 1 271 ? 0.656  -10.381 6.320   1.00 47.81 ? 271 GLU A CG  1 
ATOM   2179 C CD  . GLU A 1 271 ? 1.882  -10.140 5.456   1.00 50.21 ? 271 GLU A CD  1 
ATOM   2180 O OE1 . GLU A 1 271 ? 1.699  -9.666  4.314   1.00 51.21 ? 271 GLU A OE1 1 
ATOM   2181 O OE2 . GLU A 1 271 ? 3.014  -10.426 5.906   1.00 52.17 ? 271 GLU A OE2 1 
ATOM   2182 N N   . GLY A 1 272 ? -0.394 -11.975 10.823  1.00 41.26 ? 272 GLY A N   1 
ATOM   2183 C CA  . GLY A 1 272 ? 0.021  -12.623 12.056  1.00 39.26 ? 272 GLY A CA  1 
ATOM   2184 C C   . GLY A 1 272 ? 1.426  -12.189 12.468  1.00 37.21 ? 272 GLY A C   1 
ATOM   2185 O O   . GLY A 1 272 ? 2.148  -12.954 13.104  1.00 37.00 ? 272 GLY A O   1 
ATOM   2186 N N   . PHE A 1 273 ? 1.795  -10.957 12.087  1.00 35.51 ? 273 PHE A N   1 
ATOM   2187 C CA  . PHE A 1 273 ? 3.054  -10.335 12.472  1.00 33.54 ? 273 PHE A CA  1 
ATOM   2188 C C   . PHE A 1 273 ? 4.241  -11.175 12.005  1.00 33.49 ? 273 PHE A C   1 
ATOM   2189 O O   . PHE A 1 273 ? 5.221  -11.304 12.734  1.00 34.76 ? 273 PHE A O   1 
ATOM   2190 C CB  . PHE A 1 273 ? 3.123  -10.142 13.992  1.00 32.76 ? 273 PHE A CB  1 
ATOM   2191 C CG  . PHE A 1 273 ? 1.998  -9.323  14.610  1.00 31.77 ? 273 PHE A CG  1 
ATOM   2192 C CD1 . PHE A 1 273 ? 2.011  -7.933  14.541  1.00 31.66 ? 273 PHE A CD1 1 
ATOM   2193 C CD2 . PHE A 1 273 ? 0.952  -9.940  15.289  1.00 31.71 ? 273 PHE A CD2 1 
ATOM   2194 C CE1 . PHE A 1 273 ? 0.994  -7.185  15.116  1.00 31.65 ? 273 PHE A CE1 1 
ATOM   2195 C CE2 . PHE A 1 273 ? -0.060 -9.187  15.866  1.00 31.46 ? 273 PHE A CE2 1 
ATOM   2196 C CZ  . PHE A 1 273 ? -0.038 -7.813  15.776  1.00 31.77 ? 273 PHE A CZ  1 
ATOM   2197 N N   . SER A 1 274 ? 4.171  -11.703 10.776  1.00 32.59 ? 274 SER A N   1 
ATOM   2198 C CA  . SER A 1 274 ? 5.102  -12.724 10.318  1.00 32.44 ? 274 SER A CA  1 
ATOM   2199 C C   . SER A 1 274 ? 6.539  -12.200 10.293  1.00 31.17 ? 274 SER A C   1 
ATOM   2200 O O   . SER A 1 274 ? 7.452  -12.892 10.737  1.00 32.57 ? 274 SER A O   1 
ATOM   2201 C CB  . SER A 1 274 ? 4.696  -13.266 8.970   1.00 32.79 ? 274 SER A CB  1 
ATOM   2202 O OG  . SER A 1 274 ? 5.477  -14.400 8.616   1.00 33.84 ? 274 SER A OG  1 
ATOM   2203 N N   . PHE A 1 275 ? 6.733  -10.983 9.769   1.00 29.14 ? 275 PHE A N   1 
ATOM   2204 C CA  . PHE A 1 275 ? 8.050  -10.365 9.711   1.00 28.28 ? 275 PHE A CA  1 
ATOM   2205 C C   . PHE A 1 275 ? 8.714  -10.384 11.089  1.00 27.60 ? 275 PHE A C   1 
ATOM   2206 O O   . PHE A 1 275 ? 9.889  -10.726 11.206  1.00 26.35 ? 275 PHE A O   1 
ATOM   2207 C CB  . PHE A 1 275 ? 7.979  -8.924  9.195   1.00 27.34 ? 275 PHE A CB  1 
ATOM   2208 C CG  . PHE A 1 275 ? 9.210  -8.086  9.520   1.00 26.73 ? 275 PHE A CG  1 
ATOM   2209 C CD1 . PHE A 1 275 ? 10.403 -8.259  8.826   1.00 26.13 ? 275 PHE A CD1 1 
ATOM   2210 C CD2 . PHE A 1 275 ? 9.168  -7.124  10.525  1.00 26.26 ? 275 PHE A CD2 1 
ATOM   2211 C CE1 . PHE A 1 275 ? 11.520 -7.496  9.134   1.00 25.58 ? 275 PHE A CE1 1 
ATOM   2212 C CE2 . PHE A 1 275 ? 10.288 -6.366  10.829  1.00 25.67 ? 275 PHE A CE2 1 
ATOM   2213 C CZ  . PHE A 1 275 ? 11.459 -6.550  10.132  1.00 25.68 ? 275 PHE A CZ  1 
ATOM   2214 N N   . TRP A 1 276 ? 7.956  -9.998  12.122  1.00 27.36 ? 276 TRP A N   1 
ATOM   2215 C CA  . TRP A 1 276 ? 8.497  -9.891  13.468  1.00 27.89 ? 276 TRP A CA  1 
ATOM   2216 C C   . TRP A 1 276 ? 8.833  -11.271 14.025  1.00 28.18 ? 276 TRP A C   1 
ATOM   2217 O O   . TRP A 1 276 ? 9.912  -11.458 14.582  1.00 27.87 ? 276 TRP A O   1 
ATOM   2218 C CB  . TRP A 1 276 ? 7.534  -9.122  14.384  1.00 27.70 ? 276 TRP A CB  1 
ATOM   2219 C CG  . TRP A 1 276 ? 7.635  -7.630  14.214  1.00 27.74 ? 276 TRP A CG  1 
ATOM   2220 C CD1 . TRP A 1 276 ? 6.809  -6.815  13.497  1.00 28.10 ? 276 TRP A CD1 1 
ATOM   2221 C CD2 . TRP A 1 276 ? 8.667  -6.780  14.759  1.00 27.49 ? 276 TRP A CD2 1 
ATOM   2222 N NE1 . TRP A 1 276 ? 7.241  -5.518  13.573  1.00 28.52 ? 276 TRP A NE1 1 
ATOM   2223 C CE2 . TRP A 1 276 ? 8.379  -5.465  14.336  1.00 27.56 ? 276 TRP A CE2 1 
ATOM   2224 C CE3 . TRP A 1 276 ? 9.793  -7.003  15.562  1.00 26.91 ? 276 TRP A CE3 1 
ATOM   2225 C CZ2 . TRP A 1 276 ? 9.180  -4.382  14.692  1.00 27.06 ? 276 TRP A CZ2 1 
ATOM   2226 C CZ3 . TRP A 1 276 ? 10.584 -5.931  15.908  1.00 26.70 ? 276 TRP A CZ3 1 
ATOM   2227 C CH2 . TRP A 1 276 ? 10.278 -4.640  15.482  1.00 26.66 ? 276 TRP A CH2 1 
ATOM   2228 N N   . ILE A 1 277 ? 7.916  -12.232 13.849  1.00 28.27 ? 277 ILE A N   1 
ATOM   2229 C CA  . ILE A 1 277 ? 8.135  -13.595 14.307  1.00 28.89 ? 277 ILE A CA  1 
ATOM   2230 C C   . ILE A 1 277 ? 9.437  -14.114 13.701  1.00 29.87 ? 277 ILE A C   1 
ATOM   2231 O O   . ILE A 1 277 ? 10.280 -14.650 14.419  1.00 30.37 ? 277 ILE A O   1 
ATOM   2232 C CB  . ILE A 1 277 ? 6.941  -14.513 13.970  1.00 28.91 ? 277 ILE A CB  1 
ATOM   2233 C CG1 . ILE A 1 277 ? 5.622  -13.998 14.575  1.00 28.87 ? 277 ILE A CG1 1 
ATOM   2234 C CG2 . ILE A 1 277 ? 7.218  -15.959 14.388  1.00 28.22 ? 277 ILE A CG2 1 
ATOM   2235 C CD1 . ILE A 1 277 ? 5.660  -13.766 16.076  1.00 28.52 ? 277 ILE A CD1 1 
ATOM   2236 N N   . ARG A 1 278 ? 9.586  -13.944 12.381  1.00 30.18 ? 278 ARG A N   1 
ATOM   2237 C CA  . ARG A 1 278 ? 10.772 -14.397 11.672  1.00 30.75 ? 278 ARG A CA  1 
ATOM   2238 C C   . ARG A 1 278 ? 12.002 -13.655 12.192  1.00 29.08 ? 278 ARG A C   1 
ATOM   2239 O O   . ARG A 1 278 ? 13.048 -14.261 12.412  1.00 28.77 ? 278 ARG A O   1 
ATOM   2240 C CB  . ARG A 1 278 ? 10.610 -14.212 10.159  1.00 32.41 ? 278 ARG A CB  1 
ATOM   2241 C CG  . ARG A 1 278 ? 9.535  -15.107 9.559   1.00 33.34 ? 278 ARG A CG  1 
ATOM   2242 C CD  . ARG A 1 278 ? 9.266  -14.830 8.091   1.00 34.72 ? 278 ARG A CD  1 
ATOM   2243 N NE  . ARG A 1 278 ? 8.212  -15.726 7.598   1.00 35.69 ? 278 ARG A NE  1 
ATOM   2244 C CZ  . ARG A 1 278 ? 8.343  -16.653 6.652   1.00 37.06 ? 278 ARG A CZ  1 
ATOM   2245 N NH1 . ARG A 1 278 ? 9.464  -16.759 5.958   1.00 37.47 ? 278 ARG A NH1 1 
ATOM   2246 N NH2 . ARG A 1 278 ? 7.336  -17.468 6.384   1.00 36.82 ? 278 ARG A NH2 1 
ATOM   2247 N N   . ARG A 1 279 ? 11.869 -12.339 12.383  1.00 28.06 ? 279 ARG A N   1 
ATOM   2248 C CA  . ARG A 1 279 ? 12.977 -11.515 12.839  1.00 27.38 ? 279 ARG A CA  1 
ATOM   2249 C C   . ARG A 1 279 ? 13.488 -12.016 14.190  1.00 27.17 ? 279 ARG A C   1 
ATOM   2250 O O   . ARG A 1 279 ? 14.696 -12.138 14.388  1.00 26.72 ? 279 ARG A O   1 
ATOM   2251 C CB  . ARG A 1 279 ? 12.546 -10.047 12.914  1.00 27.20 ? 279 ARG A CB  1 
ATOM   2252 C CG  . ARG A 1 279 ? 13.688 -9.097  13.236  1.00 27.54 ? 279 ARG A CG  1 
ATOM   2253 C CD  . ARG A 1 279 ? 13.235 -7.655  13.238  1.00 27.55 ? 279 ARG A CD  1 
ATOM   2254 N NE  . ARG A 1 279 ? 14.363 -6.731  13.401  1.00 27.77 ? 279 ARG A NE  1 
ATOM   2255 C CZ  . ARG A 1 279 ? 14.253 -5.418  13.567  1.00 27.90 ? 279 ARG A CZ  1 
ATOM   2256 N NH1 . ARG A 1 279 ? 13.060 -4.846  13.619  1.00 28.26 ? 279 ARG A NH1 1 
ATOM   2257 N NH2 . ARG A 1 279 ? 15.341 -4.677  13.686  1.00 27.36 ? 279 ARG A NH2 1 
ATOM   2258 N N   . LEU A 1 280 ? 12.559 -12.305 15.111  1.00 26.35 ? 280 LEU A N   1 
ATOM   2259 C CA  . LEU A 1 280 ? 12.913 -12.770 16.444  1.00 26.21 ? 280 LEU A CA  1 
ATOM   2260 C C   . LEU A 1 280 ? 13.488 -14.182 16.373  1.00 25.96 ? 280 LEU A C   1 
ATOM   2261 O O   . LEU A 1 280 ? 14.475 -14.478 17.042  1.00 24.24 ? 280 LEU A O   1 
ATOM   2262 C CB  . LEU A 1 280 ? 11.695 -12.710 17.363  1.00 26.22 ? 280 LEU A CB  1 
ATOM   2263 C CG  . LEU A 1 280 ? 11.135 -11.311 17.636  1.00 26.84 ? 280 LEU A CG  1 
ATOM   2264 C CD1 . LEU A 1 280 ? 9.747  -11.396 18.255  1.00 26.28 ? 280 LEU A CD1 1 
ATOM   2265 C CD2 . LEU A 1 280 ? 12.086 -10.518 18.524  1.00 27.19 ? 280 LEU A CD2 1 
ATOM   2266 N N   . GLU A 1 281 ? 12.874 -15.048 15.556  1.00 26.82 ? 281 GLU A N   1 
ATOM   2267 C CA  . GLU A 1 281 ? 13.305 -16.434 15.470  1.00 26.55 ? 281 GLU A CA  1 
ATOM   2268 C C   . GLU A 1 281 ? 14.761 -16.467 15.004  1.00 26.09 ? 281 GLU A C   1 
ATOM   2269 O O   . GLU A 1 281 ? 15.564 -17.219 15.551  1.00 25.30 ? 281 GLU A O   1 
ATOM   2270 C CB  . GLU A 1 281 ? 12.335 -17.285 14.642  1.00 27.48 ? 281 GLU A CB  1 
ATOM   2271 C CG  . GLU A 1 281 ? 12.541 -17.251 13.130  1.00 28.21 ? 281 GLU A CG  1 
ATOM   2272 C CD  . GLU A 1 281 ? 13.835 -17.871 12.631  1.00 28.68 ? 281 GLU A CD  1 
ATOM   2273 O OE1 . GLU A 1 281 ? 14.432 -17.316 11.684  1.00 28.39 ? 281 GLU A OE1 1 
ATOM   2274 O OE2 . GLU A 1 281 ? 14.257 -18.893 13.210  1.00 29.49 ? 281 GLU A OE2 1 
ATOM   2275 N N   . LYS A 1 282 ? 15.092 -15.626 14.013  1.00 25.97 ? 282 LYS A N   1 
ATOM   2276 C CA  . LYS A 1 282 ? 16.446 -15.525 13.492  1.00 25.91 ? 282 LYS A CA  1 
ATOM   2277 C C   . LYS A 1 282 ? 17.381 -15.002 14.579  1.00 25.37 ? 282 LYS A C   1 
ATOM   2278 O O   . LYS A 1 282 ? 18.498 -15.494 14.726  1.00 25.35 ? 282 LYS A O   1 
ATOM   2279 C CB  . LYS A 1 282 ? 16.492 -14.598 12.271  1.00 26.92 ? 282 LYS A CB  1 
ATOM   2280 C CG  . LYS A 1 282 ? 17.843 -14.492 11.563  1.00 27.44 ? 282 LYS A CG  1 
ATOM   2281 C CD  . LYS A 1 282 ? 18.428 -15.817 11.085  1.00 27.97 ? 282 LYS A CD  1 
ATOM   2282 C CE  . LYS A 1 282 ? 17.524 -16.555 10.151  1.00 28.79 ? 282 LYS A CE  1 
ATOM   2283 N NZ  . LYS A 1 282 ? 18.052 -17.884 9.843   1.00 29.34 ? 282 LYS A NZ  1 
ATOM   2284 N N   . ALA A 1 283 ? 16.916 -13.997 15.328  1.00 24.36 ? 283 ALA A N   1 
ATOM   2285 C CA  . ALA A 1 283 ? 17.692 -13.426 16.417  1.00 24.09 ? 283 ALA A CA  1 
ATOM   2286 C C   . ALA A 1 283 ? 17.963 -14.481 17.490  1.00 23.48 ? 283 ALA A C   1 
ATOM   2287 O O   . ALA A 1 283 ? 19.065 -14.541 18.036  1.00 23.00 ? 283 ALA A O   1 
ATOM   2288 C CB  . ALA A 1 283 ? 16.972 -12.221 16.984  1.00 24.00 ? 283 ALA A CB  1 
ATOM   2289 N N   . LEU A 1 284 ? 16.959 -15.326 17.761  1.00 22.49 ? 284 LEU A N   1 
ATOM   2290 C CA  . LEU A 1 284 ? 17.042 -16.327 18.816  1.00 22.21 ? 284 LEU A CA  1 
ATOM   2291 C C   . LEU A 1 284 ? 18.024 -17.439 18.450  1.00 21.76 ? 284 LEU A C   1 
ATOM   2292 O O   . LEU A 1 284 ? 18.512 -18.138 19.333  1.00 21.38 ? 284 LEU A O   1 
ATOM   2293 C CB  . LEU A 1 284 ? 15.659 -16.904 19.112  1.00 22.65 ? 284 LEU A CB  1 
ATOM   2294 C CG  . LEU A 1 284 ? 14.669 -15.976 19.824  1.00 22.88 ? 284 LEU A CG  1 
ATOM   2295 C CD1 . LEU A 1 284 ? 13.421 -16.752 20.186  1.00 23.26 ? 284 LEU A CD1 1 
ATOM   2296 C CD2 . LEU A 1 284 ? 15.271 -15.317 21.057  1.00 23.10 ? 284 LEU A CD2 1 
ATOM   2297 N N   . GLU A 1 285 ? 18.282 -17.628 17.152  1.00 21.43 ? 285 GLU A N   1 
ATOM   2298 C CA  . GLU A 1 285 ? 19.314 -18.553 16.718  1.00 21.76 ? 285 GLU A CA  1 
ATOM   2299 C C   . GLU A 1 285 ? 20.674 -18.040 17.181  1.00 20.65 ? 285 GLU A C   1 
ATOM   2300 O O   . GLU A 1 285 ? 21.505 -18.823 17.624  1.00 19.99 ? 285 GLU A O   1 
ATOM   2301 C CB  . GLU A 1 285 ? 19.333 -18.718 15.201  1.00 23.13 ? 285 GLU A CB  1 
ATOM   2302 C CG  . GLU A 1 285 ? 18.032 -19.265 14.621  1.00 24.32 ? 285 GLU A CG  1 
ATOM   2303 C CD  . GLU A 1 285 ? 18.025 -19.199 13.107  1.00 25.51 ? 285 GLU A CD  1 
ATOM   2304 O OE1 . GLU A 1 285 ? 17.016 -19.592 12.488  1.00 27.03 ? 285 GLU A OE1 1 
ATOM   2305 O OE2 . GLU A 1 285 ? 19.042 -18.742 12.543  1.00 26.01 ? 285 GLU A OE2 1 
ATOM   2306 N N   . LEU A 1 286 ? 20.881 -16.721 17.081  1.00 20.24 ? 286 LEU A N   1 
ATOM   2307 C CA  . LEU A 1 286 ? 22.142 -16.104 17.467  1.00 20.35 ? 286 LEU A CA  1 
ATOM   2308 C C   . LEU A 1 286 ? 22.171 -15.811 18.969  1.00 20.00 ? 286 LEU A C   1 
ATOM   2309 O O   . LEU A 1 286 ? 23.223 -15.939 19.592  1.00 20.72 ? 286 LEU A O   1 
ATOM   2310 C CB  . LEU A 1 286 ? 22.376 -14.832 16.651  1.00 20.28 ? 286 LEU A CB  1 
ATOM   2311 C CG  . LEU A 1 286 ? 22.349 -14.981 15.126  1.00 20.46 ? 286 LEU A CG  1 
ATOM   2312 C CD1 . LEU A 1 286 ? 22.868 -13.716 14.466  1.00 20.73 ? 286 LEU A CD1 1 
ATOM   2313 C CD2 . LEU A 1 286 ? 23.142 -16.185 14.640  1.00 20.72 ? 286 LEU A CD2 1 
ATOM   2314 N N   . PHE A 1 287 ? 21.026 -15.427 19.548  1.00 19.74 ? 287 PHE A N   1 
ATOM   2315 C CA  . PHE A 1 287 ? 21.000 -14.828 20.876  1.00 19.42 ? 287 PHE A CA  1 
ATOM   2316 C C   . PHE A 1 287 ? 20.088 -15.612 21.812  1.00 19.03 ? 287 PHE A C   1 
ATOM   2317 O O   . PHE A 1 287 ? 19.240 -16.381 21.369  1.00 18.36 ? 287 PHE A O   1 
ATOM   2318 C CB  . PHE A 1 287 ? 20.509 -13.383 20.769  1.00 19.02 ? 287 PHE A CB  1 
ATOM   2319 C CG  . PHE A 1 287 ? 21.244 -12.586 19.703  1.00 19.47 ? 287 PHE A CG  1 
ATOM   2320 C CD1 . PHE A 1 287 ? 22.637 -12.595 19.639  1.00 19.79 ? 287 PHE A CD1 1 
ATOM   2321 C CD2 . PHE A 1 287 ? 20.543 -11.860 18.747  1.00 19.13 ? 287 PHE A CD2 1 
ATOM   2322 C CE1 . PHE A 1 287 ? 23.304 -11.875 18.661  1.00 19.30 ? 287 PHE A CE1 1 
ATOM   2323 C CE2 . PHE A 1 287 ? 21.216 -11.143 17.772  1.00 19.13 ? 287 PHE A CE2 1 
ATOM   2324 C CZ  . PHE A 1 287 ? 22.592 -11.154 17.730  1.00 19.36 ? 287 PHE A CZ  1 
ATOM   2325 N N   . HIS A 1 288 ? 20.286 -15.390 23.115  1.00 19.11 ? 288 HIS A N   1 
ATOM   2326 C CA  . HIS A 1 288 ? 19.434 -15.970 24.137  1.00 19.88 ? 288 HIS A CA  1 
ATOM   2327 C C   . HIS A 1 288 ? 18.364 -14.951 24.520  1.00 20.75 ? 288 HIS A C   1 
ATOM   2328 O O   . HIS A 1 288 ? 17.210 -15.322 24.717  1.00 20.96 ? 288 HIS A O   1 
ATOM   2329 C CB  . HIS A 1 288 ? 20.276 -16.506 25.301  1.00 19.79 ? 288 HIS A CB  1 
ATOM   2330 C CG  . HIS A 1 288 ? 21.179 -17.627 24.902  1.00 19.26 ? 288 HIS A CG  1 
ATOM   2331 N ND1 . HIS A 1 288 ? 22.528 -17.450 24.689  1.00 18.85 ? 288 HIS A ND1 1 
ATOM   2332 C CD2 . HIS A 1 288 ? 20.939 -18.929 24.681  1.00 18.86 ? 288 HIS A CD2 1 
ATOM   2333 C CE1 . HIS A 1 288 ? 23.075 -18.606 24.347  1.00 18.56 ? 288 HIS A CE1 1 
ATOM   2334 N NE2 . HIS A 1 288 ? 22.127 -19.518 24.334  1.00 18.69 ? 288 HIS A NE2 1 
ATOM   2335 N N   . LEU A 1 289 ? 18.758 -13.673 24.615  1.00 20.74 ? 289 LEU A N   1 
ATOM   2336 C CA  . LEU A 1 289 ? 17.827 -12.580 24.857  1.00 20.70 ? 289 LEU A CA  1 
ATOM   2337 C C   . LEU A 1 289 ? 18.063 -11.479 23.826  1.00 20.15 ? 289 LEU A C   1 
ATOM   2338 O O   . LEU A 1 289 ? 19.188 -11.296 23.367  1.00 19.51 ? 289 LEU A O   1 
ATOM   2339 C CB  . LEU A 1 289 ? 17.989 -12.039 26.274  1.00 21.03 ? 289 LEU A CB  1 
ATOM   2340 C CG  . LEU A 1 289 ? 17.830 -13.057 27.407  1.00 21.80 ? 289 LEU A CG  1 
ATOM   2341 C CD1 . LEU A 1 289 ? 19.132 -13.790 27.701  1.00 22.45 ? 289 LEU A CD1 1 
ATOM   2342 C CD2 . LEU A 1 289 ? 17.307 -12.386 28.658  1.00 22.17 ? 289 LEU A CD2 1 
ATOM   2343 N N   . VAL A 1 290 ? 16.996 -10.739 23.494  1.00 19.69 ? 290 VAL A N   1 
ATOM   2344 C CA  . VAL A 1 290 ? 17.050 -9.724  22.453  1.00 19.89 ? 290 VAL A CA  1 
ATOM   2345 C C   . VAL A 1 290 ? 16.577 -8.391  23.021  1.00 20.13 ? 290 VAL A C   1 
ATOM   2346 O O   . VAL A 1 290 ? 15.394 -8.231  23.300  1.00 18.93 ? 290 VAL A O   1 
ATOM   2347 C CB  . VAL A 1 290 ? 16.184 -10.099 21.235  1.00 20.09 ? 290 VAL A CB  1 
ATOM   2348 C CG1 . VAL A 1 290 ? 16.259 -9.033  20.147  1.00 19.71 ? 290 VAL A CG1 1 
ATOM   2349 C CG2 . VAL A 1 290 ? 16.541 -11.472 20.673  1.00 20.13 ? 290 VAL A CG2 1 
ATOM   2350 N N   . ARG A 1 291 ? 17.490 -7.419  23.131  1.00 20.76 ? 291 ARG A N   1 
ATOM   2351 C CA  . ARG A 1 291 ? 17.089 -6.065  23.473  1.00 21.33 ? 291 ARG A CA  1 
ATOM   2352 C C   . ARG A 1 291 ? 16.535 -5.393  22.223  1.00 21.01 ? 291 ARG A C   1 
ATOM   2353 O O   . ARG A 1 291 ? 17.105 -5.517  21.143  1.00 21.83 ? 291 ARG A O   1 
ATOM   2354 C CB  . ARG A 1 291 ? 18.236 -5.223  24.040  1.00 22.26 ? 291 ARG A CB  1 
ATOM   2355 C CG  . ARG A 1 291 ? 17.873 -3.752  24.191  1.00 22.69 ? 291 ARG A CG  1 
ATOM   2356 C CD  . ARG A 1 291 ? 19.006 -2.935  24.763  1.00 22.83 ? 291 ARG A CD  1 
ATOM   2357 N NE  . ARG A 1 291 ? 20.220 -2.958  23.938  1.00 22.91 ? 291 ARG A NE  1 
ATOM   2358 C CZ  . ARG A 1 291 ? 21.333 -2.299  24.242  1.00 23.45 ? 291 ARG A CZ  1 
ATOM   2359 N NH1 . ARG A 1 291 ? 21.372 -1.532  25.318  1.00 23.97 ? 291 ARG A NH1 1 
ATOM   2360 N NH2 . ARG A 1 291 ? 22.410 -2.400  23.481  1.00 23.08 ? 291 ARG A NH2 1 
ATOM   2361 N N   . ILE A 1 292 ? 15.418 -4.682  22.379  1.00 20.83 ? 292 ILE A N   1 
ATOM   2362 C CA  . ILE A 1 292 ? 14.870 -3.900  21.286  1.00 20.93 ? 292 ILE A CA  1 
ATOM   2363 C C   . ILE A 1 292 ? 14.977 -2.425  21.664  1.00 21.17 ? 292 ILE A C   1 
ATOM   2364 O O   . ILE A 1 292 ? 14.509 -2.012  22.725  1.00 20.85 ? 292 ILE A O   1 
ATOM   2365 C CB  . ILE A 1 292 ? 13.437 -4.351  20.946  1.00 20.25 ? 292 ILE A CB  1 
ATOM   2366 C CG1 . ILE A 1 292 ? 13.402 -5.858  20.646  1.00 20.10 ? 292 ILE A CG1 1 
ATOM   2367 C CG2 . ILE A 1 292 ? 12.867 -3.523  19.792  1.00 20.26 ? 292 ILE A CG2 1 
ATOM   2368 C CD1 . ILE A 1 292 ? 12.019 -6.428  20.380  1.00 20.03 ? 292 ILE A CD1 1 
ATOM   2369 N N   . ASP A 1 293 ? 15.648 -1.658  20.798  1.00 22.51 ? 293 ASP A N   1 
ATOM   2370 C CA  . ASP A 1 293 ? 15.810 -0.226  20.981  1.00 23.40 ? 293 ASP A CA  1 
ATOM   2371 C C   . ASP A 1 293 ? 14.487 0.441   20.612  1.00 23.41 ? 293 ASP A C   1 
ATOM   2372 O O   . ASP A 1 293 ? 13.728 -0.105  19.816  1.00 23.28 ? 293 ASP A O   1 
ATOM   2373 C CB  . ASP A 1 293 ? 17.000 0.292   20.190  1.00 24.06 ? 293 ASP A CB  1 
ATOM   2374 C CG  . ASP A 1 293 ? 18.266 -0.551  20.304  1.00 25.21 ? 293 ASP A CG  1 
ATOM   2375 O OD1 . ASP A 1 293 ? 18.837 -0.623  21.417  1.00 24.75 ? 293 ASP A OD1 1 
ATOM   2376 O OD2 . ASP A 1 293 ? 18.647 -1.163  19.285  1.00 25.91 ? 293 ASP A OD2 1 
ATOM   2377 N N   . HIS A 1 294 ? 14.220 1.604   21.220  1.00 23.61 ? 294 HIS A N   1 
ATOM   2378 C CA  . HIS A 1 294 ? 12.960 2.318   21.063  1.00 23.44 ? 294 HIS A CA  1 
ATOM   2379 C C   . HIS A 1 294 ? 11.782 1.350   21.210  1.00 23.50 ? 294 HIS A C   1 
ATOM   2380 O O   . HIS A 1 294 ? 10.843 1.370   20.415  1.00 23.15 ? 294 HIS A O   1 
ATOM   2381 C CB  . HIS A 1 294 ? 12.949 3.101   19.746  1.00 23.44 ? 294 HIS A CB  1 
ATOM   2382 C CG  . HIS A 1 294 ? 11.985 4.240   19.743  1.00 23.80 ? 294 HIS A CG  1 
ATOM   2383 N ND1 . HIS A 1 294 ? 11.971 5.191   20.740  1.00 24.16 ? 294 HIS A ND1 1 
ATOM   2384 C CD2 . HIS A 1 294 ? 11.030 4.596   18.875  1.00 23.96 ? 294 HIS A CD2 1 
ATOM   2385 C CE1 . HIS A 1 294 ? 11.026 6.082   20.480  1.00 24.65 ? 294 HIS A CE1 1 
ATOM   2386 N NE2 . HIS A 1 294 ? 10.441 5.739   19.351  1.00 24.49 ? 294 HIS A NE2 1 
ATOM   2387 N N   . PHE A 1 295 ? 11.833 0.535   22.271  1.00 23.57 ? 295 PHE A N   1 
ATOM   2388 C CA  . PHE A 1 295 ? 10.805 -0.442  22.591  1.00 24.31 ? 295 PHE A CA  1 
ATOM   2389 C C   . PHE A 1 295 ? 9.438  0.231   22.723  1.00 24.79 ? 295 PHE A C   1 
ATOM   2390 O O   . PHE A 1 295 ? 8.414  -0.426  22.553  1.00 25.88 ? 295 PHE A O   1 
ATOM   2391 C CB  . PHE A 1 295 ? 11.209 -1.170  23.879  1.00 25.12 ? 295 PHE A CB  1 
ATOM   2392 C CG  . PHE A 1 295 ? 10.092 -1.961  24.546  1.00 25.75 ? 295 PHE A CG  1 
ATOM   2393 C CD1 . PHE A 1 295 ? 9.898  -3.309  24.262  1.00 25.66 ? 295 PHE A CD1 1 
ATOM   2394 C CD2 . PHE A 1 295 ? 9.228  -1.347  25.451  1.00 26.24 ? 295 PHE A CD2 1 
ATOM   2395 C CE1 . PHE A 1 295 ? 8.869  -4.019  24.868  1.00 26.16 ? 295 PHE A CE1 1 
ATOM   2396 C CE2 . PHE A 1 295 ? 8.201  -2.061  26.051  1.00 25.87 ? 295 PHE A CE2 1 
ATOM   2397 C CZ  . PHE A 1 295 ? 8.024  -3.396  25.761  1.00 26.02 ? 295 PHE A CZ  1 
ATOM   2398 N N   . ARG A 1 296 ? 9.423  1.532   23.036  1.00 24.59 ? 296 ARG A N   1 
ATOM   2399 C CA  . ARG A 1 296 ? 8.179  2.258   23.246  1.00 25.12 ? 296 ARG A CA  1 
ATOM   2400 C C   . ARG A 1 296 ? 7.335  2.257   21.970  1.00 25.06 ? 296 ARG A C   1 
ATOM   2401 O O   . ARG A 1 296 ? 6.111  2.306   22.051  1.00 25.59 ? 296 ARG A O   1 
ATOM   2402 C CB  . ARG A 1 296 ? 8.468  3.667   23.779  1.00 25.10 ? 296 ARG A CB  1 
ATOM   2403 C CG  . ARG A 1 296 ? 8.967  4.693   22.769  1.00 25.28 ? 296 ARG A CG  1 
ATOM   2404 C CD  . ARG A 1 296 ? 7.839  5.483   22.108  1.00 24.74 ? 296 ARG A CD  1 
ATOM   2405 N NE  . ARG A 1 296 ? 7.059  6.244   23.092  1.00 24.58 ? 296 ARG A NE  1 
ATOM   2406 C CZ  . ARG A 1 296 ? 5.807  6.008   23.495  1.00 24.90 ? 296 ARG A CZ  1 
ATOM   2407 N NH1 . ARG A 1 296 ? 5.104  4.996   23.011  1.00 25.07 ? 296 ARG A NH1 1 
ATOM   2408 N NH2 . ARG A 1 296 ? 5.256  6.798   24.401  1.00 24.33 ? 296 ARG A NH2 1 
ATOM   2409 N N   . GLY A 1 297 ? 7.993  2.187   20.803  1.00 24.99 ? 297 GLY A N   1 
ATOM   2410 C CA  . GLY A 1 297 ? 7.321  2.145   19.512  1.00 25.45 ? 297 GLY A CA  1 
ATOM   2411 C C   . GLY A 1 297 ? 6.192  1.112   19.445  1.00 26.09 ? 297 GLY A C   1 
ATOM   2412 O O   . GLY A 1 297 ? 5.202  1.330   18.746  1.00 25.42 ? 297 GLY A O   1 
ATOM   2413 N N   . PHE A 1 298 ? 6.353  -0.015  20.155  1.00 25.88 ? 298 PHE A N   1 
ATOM   2414 C CA  . PHE A 1 298 ? 5.358  -1.081  20.166  1.00 25.18 ? 298 PHE A CA  1 
ATOM   2415 C C   . PHE A 1 298 ? 4.039  -0.586  20.760  1.00 25.30 ? 298 PHE A C   1 
ATOM   2416 O O   . PHE A 1 298 ? 2.969  -1.018  20.332  1.00 24.08 ? 298 PHE A O   1 
ATOM   2417 C CB  . PHE A 1 298 ? 5.818  -2.311  20.957  1.00 24.76 ? 298 PHE A CB  1 
ATOM   2418 C CG  . PHE A 1 298 ? 6.996  -3.073  20.363  1.00 24.87 ? 298 PHE A CG  1 
ATOM   2419 C CD1 . PHE A 1 298 ? 6.862  -3.783  19.172  1.00 24.75 ? 298 PHE A CD1 1 
ATOM   2420 C CD2 . PHE A 1 298 ? 8.223  -3.110  21.017  1.00 23.99 ? 298 PHE A CD2 1 
ATOM   2421 C CE1 . PHE A 1 298 ? 7.933  -4.483  18.640  1.00 24.04 ? 298 PHE A CE1 1 
ATOM   2422 C CE2 . PHE A 1 298 ? 9.289  -3.818  20.484  1.00 24.49 ? 298 PHE A CE2 1 
ATOM   2423 C CZ  . PHE A 1 298 ? 9.142  -4.504  19.298  1.00 24.65 ? 298 PHE A CZ  1 
ATOM   2424 N N   . GLU A 1 299 ? 4.124  0.293   21.768  1.00 25.88 ? 299 GLU A N   1 
ATOM   2425 C CA  . GLU A 1 299 ? 2.944  0.929   22.333  1.00 26.17 ? 299 GLU A CA  1 
ATOM   2426 C C   . GLU A 1 299 ? 2.436  1.988   21.359  1.00 26.03 ? 299 GLU A C   1 
ATOM   2427 O O   . GLU A 1 299 ? 1.256  2.003   21.012  1.00 25.47 ? 299 GLU A O   1 
ATOM   2428 C CB  . GLU A 1 299 ? 3.253  1.528   23.707  1.00 26.77 ? 299 GLU A CB  1 
ATOM   2429 C CG  . GLU A 1 299 ? 2.049  2.164   24.399  1.00 27.50 ? 299 GLU A CG  1 
ATOM   2430 C CD  . GLU A 1 299 ? 1.749  3.607   24.020  1.00 28.17 ? 299 GLU A CD  1 
ATOM   2431 O OE1 . GLU A 1 299 ? 2.662  4.456   24.117  1.00 29.55 ? 299 GLU A OE1 1 
ATOM   2432 O OE2 . GLU A 1 299 ? 0.597  3.889   23.634  1.00 27.48 ? 299 GLU A OE2 1 
ATOM   2433 N N   . ALA A 1 300 ? 3.340  2.879   20.935  1.00 25.98 ? 300 ALA A N   1 
ATOM   2434 C CA  . ALA A 1 300 ? 2.985  3.974   20.048  1.00 26.37 ? 300 ALA A CA  1 
ATOM   2435 C C   . ALA A 1 300 ? 4.244  4.585   19.439  1.00 27.00 ? 300 ALA A C   1 
ATOM   2436 O O   . ALA A 1 300 ? 5.317  4.536   20.042  1.00 27.13 ? 300 ALA A O   1 
ATOM   2437 C CB  . ALA A 1 300 ? 2.187  5.015   20.804  1.00 26.03 ? 300 ALA A CB  1 
ATOM   2438 N N   . TYR A 1 301 ? 4.087  5.172   18.247  1.00 27.69 ? 301 TYR A N   1 
ATOM   2439 C CA  . TYR A 1 301 ? 5.207  5.738   17.516  1.00 28.46 ? 301 TYR A CA  1 
ATOM   2440 C C   . TYR A 1 301 ? 4.816  7.106   16.961  1.00 28.81 ? 301 TYR A C   1 
ATOM   2441 O O   . TYR A 1 301 ? 3.658  7.351   16.620  1.00 28.15 ? 301 TYR A O   1 
ATOM   2442 C CB  . TYR A 1 301 ? 5.704  4.784   16.424  1.00 28.64 ? 301 TYR A CB  1 
ATOM   2443 C CG  . TYR A 1 301 ? 4.739  4.486   15.283  1.00 29.15 ? 301 TYR A CG  1 
ATOM   2444 C CD1 . TYR A 1 301 ? 3.885  3.389   15.329  1.00 29.25 ? 301 TYR A CD1 1 
ATOM   2445 C CD2 . TYR A 1 301 ? 4.714  5.277   14.139  1.00 29.36 ? 301 TYR A CD2 1 
ATOM   2446 C CE1 . TYR A 1 301 ? 3.019  3.103   14.284  1.00 29.97 ? 301 TYR A CE1 1 
ATOM   2447 C CE2 . TYR A 1 301 ? 3.851  5.003   13.090  1.00 29.43 ? 301 TYR A CE2 1 
ATOM   2448 C CZ  . TYR A 1 301 ? 3.002  3.914   13.162  1.00 29.90 ? 301 TYR A CZ  1 
ATOM   2449 O OH  . TYR A 1 301 ? 2.149  3.651   12.129  1.00 31.33 ? 301 TYR A OH  1 
ATOM   2450 N N   . TRP A 1 302 ? 5.822  7.986   16.907  1.00 29.54 ? 302 TRP A N   1 
ATOM   2451 C CA  . TRP A 1 302 ? 5.690  9.350   16.426  1.00 30.09 ? 302 TRP A CA  1 
ATOM   2452 C C   . TRP A 1 302 ? 5.865  9.356   14.910  1.00 30.26 ? 302 TRP A C   1 
ATOM   2453 O O   . TRP A 1 302 ? 6.921  8.983   14.403  1.00 29.22 ? 302 TRP A O   1 
ATOM   2454 C CB  . TRP A 1 302 ? 6.735  10.222  17.138  1.00 30.58 ? 302 TRP A CB  1 
ATOM   2455 C CG  . TRP A 1 302 ? 6.777  11.673  16.734  1.00 31.93 ? 302 TRP A CG  1 
ATOM   2456 C CD1 . TRP A 1 302 ? 7.690  12.263  15.911  1.00 32.53 ? 302 TRP A CD1 1 
ATOM   2457 C CD2 . TRP A 1 302 ? 5.892  12.729  17.171  1.00 32.69 ? 302 TRP A CD2 1 
ATOM   2458 N NE1 . TRP A 1 302 ? 7.433  13.603  15.794  1.00 32.21 ? 302 TRP A NE1 1 
ATOM   2459 C CE2 . TRP A 1 302 ? 6.337  13.919  16.554  1.00 32.83 ? 302 TRP A CE2 1 
ATOM   2460 C CE3 . TRP A 1 302 ? 4.776  12.785  18.013  1.00 32.95 ? 302 TRP A CE3 1 
ATOM   2461 C CZ2 . TRP A 1 302 ? 5.701  15.144  16.754  1.00 32.96 ? 302 TRP A CZ2 1 
ATOM   2462 C CZ3 . TRP A 1 302 ? 4.149  13.996  18.213  1.00 33.21 ? 302 TRP A CZ3 1 
ATOM   2463 C CH2 . TRP A 1 302 ? 4.610  15.160  17.594  1.00 33.49 ? 302 TRP A CH2 1 
ATOM   2464 N N   . GLU A 1 303 ? 4.808  9.766   14.200  1.00 30.58 ? 303 GLU A N   1 
ATOM   2465 C CA  . GLU A 1 303 ? 4.762  9.695   12.749  1.00 30.97 ? 303 GLU A CA  1 
ATOM   2466 C C   . GLU A 1 303 ? 4.999  11.086  12.173  1.00 31.31 ? 303 GLU A C   1 
ATOM   2467 O O   . GLU A 1 303 ? 4.194  11.986  12.393  1.00 32.16 ? 303 GLU A O   1 
ATOM   2468 C CB  . GLU A 1 303 ? 3.401  9.150   12.316  1.00 31.60 ? 303 GLU A CB  1 
ATOM   2469 C CG  . GLU A 1 303 ? 3.247  8.967   10.808  1.00 31.68 ? 303 GLU A CG  1 
ATOM   2470 C CD  . GLU A 1 303 ? 1.857  8.514   10.395  1.00 32.89 ? 303 GLU A CD  1 
ATOM   2471 O OE1 . GLU A 1 303 ? 1.723  7.401   9.840   1.00 32.72 ? 303 GLU A OE1 1 
ATOM   2472 O OE2 . GLU A 1 303 ? 0.903  9.285   10.626  1.00 33.43 ? 303 GLU A OE2 1 
ATOM   2473 N N   . ILE A 1 304 ? 6.101  11.237  11.428  1.00 31.07 ? 304 ILE A N   1 
ATOM   2474 C CA  . ILE A 1 304 ? 6.457  12.496  10.794  1.00 31.28 ? 304 ILE A CA  1 
ATOM   2475 C C   . ILE A 1 304 ? 6.266  12.337  9.288   1.00 30.49 ? 304 ILE A C   1 
ATOM   2476 O O   . ILE A 1 304 ? 6.803  11.397  8.709   1.00 30.39 ? 304 ILE A O   1 
ATOM   2477 C CB  . ILE A 1 304 ? 7.910  12.891  11.128  1.00 30.96 ? 304 ILE A CB  1 
ATOM   2478 C CG1 . ILE A 1 304 ? 8.224  12.731  12.618  1.00 30.84 ? 304 ILE A CG1 1 
ATOM   2479 C CG2 . ILE A 1 304 ? 8.218  14.303  10.632  1.00 31.34 ? 304 ILE A CG2 1 
ATOM   2480 C CD1 . ILE A 1 304 ? 9.676  12.992  12.980  1.00 30.57 ? 304 ILE A CD1 1 
ATOM   2481 N N   . PRO A 1 305 ? 5.520  13.236  8.601   1.00 30.67 ? 305 PRO A N   1 
ATOM   2482 C CA  . PRO A 1 305 ? 5.492  13.228  7.143   1.00 31.39 ? 305 PRO A CA  1 
ATOM   2483 C C   . PRO A 1 305 ? 6.881  13.467  6.560   1.00 32.18 ? 305 PRO A C   1 
ATOM   2484 O O   . PRO A 1 305 ? 7.607  14.330  7.046   1.00 31.16 ? 305 PRO A O   1 
ATOM   2485 C CB  . PRO A 1 305 ? 4.516  14.346  6.776   1.00 31.25 ? 305 PRO A CB  1 
ATOM   2486 C CG  . PRO A 1 305 ? 3.769  14.657  8.063   1.00 30.71 ? 305 PRO A CG  1 
ATOM   2487 C CD  . PRO A 1 305 ? 4.689  14.300  9.186   1.00 30.76 ? 305 PRO A CD  1 
ATOM   2488 N N   . ALA A 1 306 ? 7.248  12.688  5.537   1.00 33.99 ? 306 ALA A N   1 
ATOM   2489 C CA  . ALA A 1 306 ? 8.596  12.733  4.990   1.00 36.46 ? 306 ALA A CA  1 
ATOM   2490 C C   . ALA A 1 306 ? 8.894  14.112  4.403   1.00 38.15 ? 306 ALA A C   1 
ATOM   2491 O O   . ALA A 1 306 ? 10.029 14.578  4.461   1.00 39.74 ? 306 ALA A O   1 
ATOM   2492 C CB  . ALA A 1 306 ? 8.770  11.646  3.955   1.00 37.00 ? 306 ALA A CB  1 
ATOM   2493 N N   . SER A 1 307 ? 7.867  14.750  3.833   1.00 39.48 ? 307 SER A N   1 
ATOM   2494 C CA  . SER A 1 307 ? 7.992  16.085  3.270   1.00 40.73 ? 307 SER A CA  1 
ATOM   2495 C C   . SER A 1 307 ? 8.332  17.110  4.353   1.00 42.68 ? 307 SER A C   1 
ATOM   2496 O O   . SER A 1 307 ? 9.075  18.054  4.089   1.00 44.82 ? 307 SER A O   1 
ATOM   2497 C CB  . SER A 1 307 ? 6.742  16.462  2.515   1.00 39.68 ? 307 SER A CB  1 
ATOM   2498 O OG  . SER A 1 307 ? 5.577  16.043  3.214   1.00 38.26 ? 307 SER A OG  1 
ATOM   2499 N N   . CYS A 1 308 ? 7.789  16.924  5.565   1.00 43.24 ? 308 CYS A N   1 
ATOM   2500 C CA  . CYS A 1 308 ? 8.128  17.765  6.704   1.00 43.04 ? 308 CYS A CA  1 
ATOM   2501 C C   . CYS A 1 308 ? 9.585  17.529  7.104   1.00 43.44 ? 308 CYS A C   1 
ATOM   2502 O O   . CYS A 1 308 ? 9.998  16.385  7.284   1.00 43.37 ? 308 CYS A O   1 
ATOM   2503 C CB  . CYS A 1 308 ? 7.215  17.491  7.891   1.00 42.61 ? 308 CYS A CB  1 
ATOM   2504 S SG  . CYS A 1 308 ? 5.459  17.760  7.537   1.00 42.40 ? 308 CYS A SG  1 
ATOM   2505 N N   . PRO A 1 309 ? 10.411 18.591  7.257   1.00 43.82 ? 309 PRO A N   1 
ATOM   2506 C CA  . PRO A 1 309 ? 11.846 18.420  7.454   1.00 43.86 ? 309 PRO A CA  1 
ATOM   2507 C C   . PRO A 1 309 ? 12.292 18.198  8.899   1.00 42.36 ? 309 PRO A C   1 
ATOM   2508 O O   . PRO A 1 309 ? 13.431 17.797  9.125   1.00 40.76 ? 309 PRO A O   1 
ATOM   2509 C CB  . PRO A 1 309 ? 12.411 19.723  6.906   1.00 43.93 ? 309 PRO A CB  1 
ATOM   2510 C CG  . PRO A 1 309 ? 11.333 20.732  7.269   1.00 44.60 ? 309 PRO A CG  1 
ATOM   2511 C CD  . PRO A 1 309 ? 10.017 20.009  7.202   1.00 44.34 ? 309 PRO A CD  1 
ATOM   2512 N N   . THR A 1 310 ? 11.406 18.460  9.869   1.00 42.99 ? 310 THR A N   1 
ATOM   2513 C CA  . THR A 1 310 ? 11.794 18.472  11.273  1.00 43.14 ? 310 THR A CA  1 
ATOM   2514 C C   . THR A 1 310 ? 10.976 17.446  12.055  1.00 43.02 ? 310 THR A C   1 
ATOM   2515 O O   . THR A 1 310 ? 10.099 16.789  11.497  1.00 42.45 ? 310 THR A O   1 
ATOM   2516 C CB  . THR A 1 310 ? 11.622 19.886  11.826  1.00 43.71 ? 310 THR A CB  1 
ATOM   2517 O OG1 . THR A 1 310 ? 10.247 20.203  11.632  1.00 44.47 ? 310 THR A OG1 1 
ATOM   2518 C CG2 . THR A 1 310 ? 12.511 20.893  11.120  1.00 43.79 ? 310 THR A CG2 1 
ATOM   2519 N N   . ALA A 1 311 ? 11.291 17.328  13.353  1.00 42.63 ? 311 ALA A N   1 
ATOM   2520 C CA  . ALA A 1 311 ? 10.678 16.351  14.240  1.00 42.50 ? 311 ALA A CA  1 
ATOM   2521 C C   . ALA A 1 311 ? 9.376  16.871  14.851  1.00 42.95 ? 311 ALA A C   1 
ATOM   2522 O O   . ALA A 1 311 ? 8.581  16.081  15.354  1.00 44.28 ? 311 ALA A O   1 
ATOM   2523 C CB  . ALA A 1 311 ? 11.661 15.970  15.325  1.00 41.69 ? 311 ALA A CB  1 
ATOM   2524 N N   . VAL A 1 312 ? 9.163  18.193  14.808  1.00 43.35 ? 312 VAL A N   1 
ATOM   2525 C CA  . VAL A 1 312 ? 8.094  18.833  15.564  1.00 43.90 ? 312 VAL A CA  1 
ATOM   2526 C C   . VAL A 1 312 ? 6.730  18.596  14.913  1.00 42.85 ? 312 VAL A C   1 
ATOM   2527 O O   . VAL A 1 312 ? 5.705  18.777  15.568  1.00 41.66 ? 312 VAL A O   1 
ATOM   2528 C CB  . VAL A 1 312 ? 8.333  20.348  15.742  1.00 44.45 ? 312 VAL A CB  1 
ATOM   2529 C CG1 . VAL A 1 312 ? 9.642  20.655  16.462  1.00 45.12 ? 312 VAL A CG1 1 
ATOM   2530 C CG2 . VAL A 1 312 ? 8.265  21.106  14.419  1.00 44.02 ? 312 VAL A CG2 1 
ATOM   2531 N N   . GLU A 1 313 ? 6.716  18.192  13.636  1.00 42.90 ? 313 GLU A N   1 
ATOM   2532 C CA  . GLU A 1 313 ? 5.547  18.363  12.785  1.00 44.46 ? 313 GLU A CA  1 
ATOM   2533 C C   . GLU A 1 313 ? 4.566  17.197  12.925  1.00 45.22 ? 313 GLU A C   1 
ATOM   2534 O O   . GLU A 1 313 ? 3.383  17.357  12.630  1.00 48.01 ? 313 GLU A O   1 
ATOM   2535 C CB  . GLU A 1 313 ? 5.959  18.472  11.315  1.00 45.60 ? 313 GLU A CB  1 
ATOM   2536 C CG  . GLU A 1 313 ? 7.178  19.358  11.063  1.00 46.21 ? 313 GLU A CG  1 
ATOM   2537 C CD  . GLU A 1 313 ? 6.945  20.857  11.009  1.00 46.25 ? 313 GLU A CD  1 
ATOM   2538 O OE1 . GLU A 1 313 ? 5.789  21.310  11.141  1.00 45.82 ? 313 GLU A OE1 1 
ATOM   2539 O OE2 . GLU A 1 313 ? 7.946  21.578  10.822  1.00 48.02 ? 313 GLU A OE2 1 
ATOM   2540 N N   . GLY A 1 314 ? 5.055  16.029  13.364  1.00 44.42 ? 314 GLY A N   1 
ATOM   2541 C CA  . GLY A 1 314 ? 4.329  14.774  13.218  1.00 42.08 ? 314 GLY A CA  1 
ATOM   2542 C C   . GLY A 1 314 ? 3.265  14.556  14.293  1.00 40.88 ? 314 GLY A C   1 
ATOM   2543 O O   . GLY A 1 314 ? 2.996  15.445  15.096  1.00 42.26 ? 314 GLY A O   1 
ATOM   2544 N N   . ARG A 1 315 ? 2.666  13.354  14.279  1.00 38.55 ? 315 ARG A N   1 
ATOM   2545 C CA  . ARG A 1 315 ? 1.640  12.946  15.230  1.00 37.04 ? 315 ARG A CA  1 
ATOM   2546 C C   . ARG A 1 315 ? 2.007  11.598  15.855  1.00 34.61 ? 315 ARG A C   1 
ATOM   2547 O O   . ARG A 1 315 ? 2.757  10.824  15.265  1.00 34.79 ? 315 ARG A O   1 
ATOM   2548 C CB  . ARG A 1 315 ? 0.279  12.805  14.535  1.00 37.77 ? 315 ARG A CB  1 
ATOM   2549 C CG  . ARG A 1 315 ? 0.260  11.791  13.399  1.00 38.00 ? 315 ARG A CG  1 
ATOM   2550 C CD  . ARG A 1 315 ? -1.141 11.402  12.948  1.00 38.45 ? 315 ARG A CD  1 
ATOM   2551 N NE  . ARG A 1 315 ? -1.100 10.228  12.068  1.00 38.30 ? 315 ARG A NE  1 
ATOM   2552 C CZ  . ARG A 1 315 ? -2.139 9.662   11.457  1.00 38.85 ? 315 ARG A CZ  1 
ATOM   2553 N NH1 . ARG A 1 315 ? -3.349 10.188  11.553  1.00 39.31 ? 315 ARG A NH1 1 
ATOM   2554 N NH2 . ARG A 1 315 ? -1.958 8.568   10.735  1.00 38.19 ? 315 ARG A NH2 1 
ATOM   2555 N N   . TRP A 1 316 ? 1.456  11.319  17.045  1.00 31.16 ? 316 TRP A N   1 
ATOM   2556 C CA  . TRP A 1 316 ? 1.583  10.010  17.670  1.00 29.15 ? 316 TRP A CA  1 
ATOM   2557 C C   . TRP A 1 316 ? 0.553  9.051   17.077  1.00 29.03 ? 316 TRP A C   1 
ATOM   2558 O O   . TRP A 1 316 ? -0.579 9.440   16.797  1.00 28.43 ? 316 TRP A O   1 
ATOM   2559 C CB  . TRP A 1 316 ? 1.411  10.095  19.195  1.00 27.70 ? 316 TRP A CB  1 
ATOM   2560 C CG  . TRP A 1 316 ? 2.639  10.524  19.953  1.00 26.73 ? 316 TRP A CG  1 
ATOM   2561 C CD1 . TRP A 1 316 ? 2.874  11.743  20.519  1.00 26.70 ? 316 TRP A CD1 1 
ATOM   2562 C CD2 . TRP A 1 316 ? 3.806  9.719   20.237  1.00 25.86 ? 316 TRP A CD2 1 
ATOM   2563 N NE1 . TRP A 1 316 ? 4.102  11.756  21.127  1.00 26.46 ? 316 TRP A NE1 1 
ATOM   2564 C CE2 . TRP A 1 316 ? 4.696  10.531  20.974  1.00 25.93 ? 316 TRP A CE2 1 
ATOM   2565 C CE3 . TRP A 1 316 ? 4.182  8.403   19.945  1.00 25.64 ? 316 TRP A CE3 1 
ATOM   2566 C CZ2 . TRP A 1 316 ? 5.932  10.063  21.418  1.00 25.38 ? 316 TRP A CZ2 1 
ATOM   2567 C CZ3 . TRP A 1 316 ? 5.405  7.945   20.384  1.00 25.63 ? 316 TRP A CZ3 1 
ATOM   2568 C CH2 . TRP A 1 316 ? 6.267  8.765   21.110  1.00 25.38 ? 316 TRP A CH2 1 
ATOM   2569 N N   . VAL A 1 317 ? 0.956  7.788   16.907  1.00 28.37 ? 317 VAL A N   1 
ATOM   2570 C CA  . VAL A 1 317 ? 0.065  6.753   16.415  1.00 28.68 ? 317 VAL A CA  1 
ATOM   2571 C C   . VAL A 1 317 ? 0.170  5.556   17.355  1.00 28.83 ? 317 VAL A C   1 
ATOM   2572 O O   . VAL A 1 317 ? 1.267  5.188   17.767  1.00 28.17 ? 317 VAL A O   1 
ATOM   2573 C CB  . VAL A 1 317 ? 0.396  6.362   14.962  1.00 29.00 ? 317 VAL A CB  1 
ATOM   2574 C CG1 . VAL A 1 317 ? -0.554 5.296   14.428  1.00 29.27 ? 317 VAL A CG1 1 
ATOM   2575 C CG2 . VAL A 1 317 ? 0.415  7.575   14.036  1.00 29.17 ? 317 VAL A CG2 1 
ATOM   2576 N N   . LYS A 1 318 ? -0.984 4.964   17.688  1.00 28.98 ? 318 LYS A N   1 
ATOM   2577 C CA  . LYS A 1 318 ? -1.037 3.773   18.520  1.00 29.07 ? 318 LYS A CA  1 
ATOM   2578 C C   . LYS A 1 318 ? -0.577 2.568   17.702  1.00 28.69 ? 318 LYS A C   1 
ATOM   2579 O O   . LYS A 1 318 ? -0.828 2.498   16.500  1.00 27.48 ? 318 LYS A O   1 
ATOM   2580 C CB  . LYS A 1 318 ? -2.456 3.538   19.054  1.00 30.10 ? 318 LYS A CB  1 
ATOM   2581 C CG  . LYS A 1 318 ? -3.016 4.647   19.942  1.00 30.98 ? 318 LYS A CG  1 
ATOM   2582 C CD  . LYS A 1 318 ? -4.505 4.509   20.250  1.00 31.03 ? 318 LYS A CD  1 
ATOM   2583 C CE  . LYS A 1 318 ? -5.178 5.823   20.495  1.00 31.27 ? 318 LYS A CE  1 
ATOM   2584 N NZ  . LYS A 1 318 ? -6.639 5.706   20.516  1.00 31.40 ? 318 LYS A NZ  1 
ATOM   2585 N N   . ALA A 1 319 ? 0.085  1.620   18.381  1.00 28.13 ? 319 ALA A N   1 
ATOM   2586 C CA  . ALA A 1 319 ? 0.604  0.418   17.749  1.00 27.74 ? 319 ALA A CA  1 
ATOM   2587 C C   . ALA A 1 319 ? 0.181  -0.805  18.560  1.00 27.18 ? 319 ALA A C   1 
ATOM   2588 O O   . ALA A 1 319 ? 0.065  -0.720  19.780  1.00 26.89 ? 319 ALA A O   1 
ATOM   2589 C CB  . ALA A 1 319 ? 2.110  0.516   17.626  1.00 27.53 ? 319 ALA A CB  1 
ATOM   2590 N N   . PRO A 1 320 ? -0.051 -1.974  17.915  1.00 26.69 ? 320 PRO A N   1 
ATOM   2591 C CA  . PRO A 1 320 ? -0.518 -3.166  18.613  1.00 27.34 ? 320 PRO A CA  1 
ATOM   2592 C C   . PRO A 1 320 ? 0.599  -3.992  19.253  1.00 27.58 ? 320 PRO A C   1 
ATOM   2593 O O   . PRO A 1 320 ? 0.829  -5.136  18.873  1.00 26.24 ? 320 PRO A O   1 
ATOM   2594 C CB  . PRO A 1 320 ? -1.231 -3.928  17.502  1.00 27.21 ? 320 PRO A CB  1 
ATOM   2595 C CG  . PRO A 1 320 ? -0.339 -3.631  16.308  1.00 27.06 ? 320 PRO A CG  1 
ATOM   2596 C CD  . PRO A 1 320 ? 0.113  -2.206  16.472  1.00 26.88 ? 320 PRO A CD  1 
ATOM   2597 N N   . GLY A 1 321 ? 1.272  -3.410  20.249  1.00 28.81 ? 321 GLY A N   1 
ATOM   2598 C CA  . GLY A 1 321 ? 2.296  -4.116  21.004  1.00 29.44 ? 321 GLY A CA  1 
ATOM   2599 C C   . GLY A 1 321 ? 1.730  -5.363  21.680  1.00 29.95 ? 321 GLY A C   1 
ATOM   2600 O O   . GLY A 1 321 ? 2.292  -6.449  21.544  1.00 29.55 ? 321 GLY A O   1 
ATOM   2601 N N   A GLU A 1 322 ? 0.613  -5.174  22.398  0.50 30.05 ? 322 GLU A N   1 
ATOM   2602 N N   B GLU A 1 322 ? 0.594  -5.203  22.370  0.50 30.18 ? 322 GLU A N   1 
ATOM   2603 C CA  A GLU A 1 322 ? -0.078 -6.227  23.128  0.50 30.21 ? 322 GLU A CA  1 
ATOM   2604 C CA  B GLU A 1 322 ? -0.000 -6.277  23.151  0.50 30.44 ? 322 GLU A CA  1 
ATOM   2605 C C   A GLU A 1 322 ? -0.235 -7.478  22.268  0.50 30.12 ? 322 GLU A C   1 
ATOM   2606 C C   B GLU A 1 322 ? -0.251 -7.503  22.274  0.50 30.25 ? 322 GLU A C   1 
ATOM   2607 O O   A GLU A 1 322 ? 0.108  -8.580  22.695  0.50 30.01 ? 322 GLU A O   1 
ATOM   2608 O O   B GLU A 1 322 ? 0.018  -8.626  22.696  0.50 30.19 ? 322 GLU A O   1 
ATOM   2609 C CB  A GLU A 1 322 ? -1.476 -5.743  23.514  0.50 30.57 ? 322 GLU A CB  1 
ATOM   2610 C CB  B GLU A 1 322 ? -1.312 -5.839  23.799  0.50 30.93 ? 322 GLU A CB  1 
ATOM   2611 C CG  A GLU A 1 322 ? -2.327 -6.805  24.204  0.50 30.67 ? 322 GLU A CG  1 
ATOM   2612 C CG  B GLU A 1 322 ? -1.776 -6.787  24.902  0.50 31.01 ? 322 GLU A CG  1 
ATOM   2613 C CD  A GLU A 1 322 ? -2.021 -6.975  25.679  0.50 30.74 ? 322 GLU A CD  1 
ATOM   2614 C CD  B GLU A 1 322 ? -3.189 -6.533  25.391  0.50 31.51 ? 322 GLU A CD  1 
ATOM   2615 O OE1 A GLU A 1 322 ? -2.117 -5.964  26.406  0.50 30.74 ? 322 GLU A OE1 1 
ATOM   2616 O OE1 B GLU A 1 322 ? -3.861 -5.643  24.828  0.50 31.66 ? 322 GLU A OE1 1 
ATOM   2617 O OE2 A GLU A 1 322 ? -1.702 -8.104  26.106  0.50 31.43 ? 322 GLU A OE2 1 
ATOM   2618 O OE2 B GLU A 1 322 ? -3.615 -7.227  26.338  0.50 31.87 ? 322 GLU A OE2 1 
ATOM   2619 N N   . LYS A 1 323 ? -0.762 -7.277  21.056  1.00 29.85 ? 323 LYS A N   1 
ATOM   2620 C CA  . LYS A 1 323 ? -1.096 -8.361  20.145  1.00 30.10 ? 323 LYS A CA  1 
ATOM   2621 C C   . LYS A 1 323 ? 0.177  -9.078  19.701  1.00 29.32 ? 323 LYS A C   1 
ATOM   2622 O O   . LYS A 1 323 ? 0.225  -10.307 19.668  1.00 29.00 ? 323 LYS A O   1 
ATOM   2623 C CB  . LYS A 1 323 ? -1.852 -7.812  18.928  1.00 30.07 ? 323 LYS A CB  1 
ATOM   2624 C CG  . LYS A 1 323 ? -2.959 -6.812  19.248  1.00 30.70 ? 323 LYS A CG  1 
ATOM   2625 C CD  . LYS A 1 323 ? -3.844 -6.433  18.069  1.00 31.40 ? 323 LYS A CD  1 
ATOM   2626 C CE  . LYS A 1 323 ? -4.748 -5.290  18.408  1.00 32.27 ? 323 LYS A CE  1 
ATOM   2627 N NZ  . LYS A 1 323 ? -5.795 -5.097  17.399  1.00 32.63 ? 323 LYS A NZ  1 
ATOM   2628 N N   . LEU A 1 324 ? 1.201  -8.289  19.360  1.00 29.23 ? 324 LEU A N   1 
ATOM   2629 C CA  . LEU A 1 324 ? 2.461  -8.818  18.868  1.00 29.50 ? 324 LEU A CA  1 
ATOM   2630 C C   . LEU A 1 324 ? 3.094  -9.707  19.936  1.00 29.90 ? 324 LEU A C   1 
ATOM   2631 O O   . LEU A 1 324 ? 3.604  -10.778 19.621  1.00 30.03 ? 324 LEU A O   1 
ATOM   2632 C CB  . LEU A 1 324 ? 3.386  -7.671  18.461  1.00 29.58 ? 324 LEU A CB  1 
ATOM   2633 C CG  . LEU A 1 324 ? 4.811  -8.056  18.052  1.00 30.15 ? 324 LEU A CG  1 
ATOM   2634 C CD1 . LEU A 1 324 ? 4.813  -8.992  16.853  1.00 30.31 ? 324 LEU A CD1 1 
ATOM   2635 C CD2 . LEU A 1 324 ? 5.639  -6.813  17.766  1.00 30.61 ? 324 LEU A CD2 1 
ATOM   2636 N N   . PHE A 1 325 ? 3.048  -9.255  21.194  1.00 30.04 ? 325 PHE A N   1 
ATOM   2637 C CA  . PHE A 1 325 ? 3.634  -9.996  22.299  1.00 30.91 ? 325 PHE A CA  1 
ATOM   2638 C C   . PHE A 1 325 ? 2.808  -11.250 22.588  1.00 31.40 ? 325 PHE A C   1 
ATOM   2639 O O   . PHE A 1 325 ? 3.366  -12.275 22.974  1.00 30.95 ? 325 PHE A O   1 
ATOM   2640 C CB  . PHE A 1 325 ? 3.807  -9.049  23.492  1.00 30.55 ? 325 PHE A CB  1 
ATOM   2641 C CG  . PHE A 1 325 ? 4.929  -8.039  23.279  1.00 31.18 ? 325 PHE A CG  1 
ATOM   2642 C CD1 . PHE A 1 325 ? 6.257  -8.450  23.266  1.00 31.27 ? 325 PHE A CD1 1 
ATOM   2643 C CD2 . PHE A 1 325 ? 4.661  -6.688  23.087  1.00 31.57 ? 325 PHE A CD2 1 
ATOM   2644 C CE1 . PHE A 1 325 ? 7.284  -7.539  23.061  1.00 31.45 ? 325 PHE A CE1 1 
ATOM   2645 C CE2 . PHE A 1 325 ? 5.690  -5.780  22.888  1.00 31.78 ? 325 PHE A CE2 1 
ATOM   2646 C CZ  . PHE A 1 325 ? 6.998  -6.206  22.875  1.00 31.32 ? 325 PHE A CZ  1 
ATOM   2647 N N   . GLN A 1 326 ? 1.487  -11.168 22.394  1.00 32.49 ? 326 GLN A N   1 
ATOM   2648 C CA  . GLN A 1 326 ? 0.610  -12.319 22.557  1.00 33.33 ? 326 GLN A CA  1 
ATOM   2649 C C   . GLN A 1 326 ? 0.984  -13.409 21.555  1.00 32.45 ? 326 GLN A C   1 
ATOM   2650 O O   . GLN A 1 326 ? 1.023  -14.587 21.904  1.00 31.90 ? 326 GLN A O   1 
ATOM   2651 C CB  . GLN A 1 326 ? -0.859 -11.923 22.398  1.00 35.17 ? 326 GLN A CB  1 
ATOM   2652 C CG  . GLN A 1 326 ? -1.468 -11.287 23.643  1.00 37.22 ? 326 GLN A CG  1 
ATOM   2653 C CD  . GLN A 1 326 ? -2.804 -10.620 23.386  1.00 39.45 ? 326 GLN A CD  1 
ATOM   2654 O OE1 . GLN A 1 326 ? -3.315 -10.603 22.260  1.00 39.44 ? 326 GLN A OE1 1 
ATOM   2655 N NE2 . GLN A 1 326 ? -3.385 -10.055 24.436  1.00 39.89 ? 326 GLN A NE2 1 
ATOM   2656 N N   . LYS A 1 327 ? 1.261  -13.000 20.312  1.00 32.11 ? 327 LYS A N   1 
ATOM   2657 C CA  . LYS A 1 327 ? 1.663  -13.922 19.263  1.00 31.19 ? 327 LYS A CA  1 
ATOM   2658 C C   . LYS A 1 327 ? 3.024  -14.532 19.600  1.00 31.61 ? 327 LYS A C   1 
ATOM   2659 O O   . LYS A 1 327 ? 3.207  -15.741 19.466  1.00 31.19 ? 327 LYS A O   1 
ATOM   2660 C CB  . LYS A 1 327 ? 1.679  -13.184 17.919  1.00 30.64 ? 327 LYS A CB  1 
ATOM   2661 C CG  . LYS A 1 327 ? 1.901  -14.058 16.693  1.00 30.99 ? 327 LYS A CG  1 
ATOM   2662 C CD  . LYS A 1 327 ? 0.845  -15.137 16.483  1.00 31.32 ? 327 LYS A CD  1 
ATOM   2663 C CE  . LYS A 1 327 ? 1.101  -15.951 15.255  1.00 31.50 ? 327 LYS A CE  1 
ATOM   2664 N NZ  . LYS A 1 327 ? 0.269  -17.157 15.225  1.00 32.40 ? 327 LYS A NZ  1 
ATOM   2665 N N   . ILE A 1 328 ? 3.966  -13.685 20.042  1.00 31.28 ? 328 ILE A N   1 
ATOM   2666 C CA  . ILE A 1 328 ? 5.311  -14.119 20.392  1.00 31.48 ? 328 ILE A CA  1 
ATOM   2667 C C   . ILE A 1 328 ? 5.225  -15.137 21.528  1.00 31.57 ? 328 ILE A C   1 
ATOM   2668 O O   . ILE A 1 328 ? 5.767  -16.236 21.423  1.00 32.78 ? 328 ILE A O   1 
ATOM   2669 C CB  . ILE A 1 328 ? 6.202  -12.923 20.783  1.00 31.29 ? 328 ILE A CB  1 
ATOM   2670 C CG1 . ILE A 1 328 ? 6.390  -11.935 19.628  1.00 30.96 ? 328 ILE A CG1 1 
ATOM   2671 C CG2 . ILE A 1 328 ? 7.553  -13.399 21.324  1.00 31.02 ? 328 ILE A CG2 1 
ATOM   2672 C CD1 . ILE A 1 328 ? 6.908  -10.573 20.057  1.00 30.86 ? 328 ILE A CD1 1 
ATOM   2673 N N   . GLN A 1 329 ? 4.531  -14.751 22.605  1.00 31.52 ? 329 GLN A N   1 
ATOM   2674 C CA  . GLN A 1 329 ? 4.387  -15.573 23.798  1.00 31.52 ? 329 GLN A CA  1 
ATOM   2675 C C   . GLN A 1 329 ? 3.830  -16.949 23.432  1.00 31.38 ? 329 GLN A C   1 
ATOM   2676 O O   . GLN A 1 329 ? 4.234  -17.952 24.016  1.00 32.19 ? 329 GLN A O   1 
ATOM   2677 C CB  . GLN A 1 329 ? 3.497  -14.827 24.796  1.00 31.53 ? 329 GLN A CB  1 
ATOM   2678 C CG  . GLN A 1 329 ? 3.202  -15.578 26.092  1.00 31.71 ? 329 GLN A CG  1 
ATOM   2679 C CD  . GLN A 1 329 ? 4.442  -15.881 26.906  1.00 32.14 ? 329 GLN A CD  1 
ATOM   2680 O OE1 . GLN A 1 329 ? 5.226  -14.988 27.241  1.00 32.20 ? 329 GLN A OE1 1 
ATOM   2681 N NE2 . GLN A 1 329 ? 4.636  -17.149 27.237  1.00 32.83 ? 329 GLN A NE2 1 
ATOM   2682 N N   . GLU A 1 330 ? 2.914  -16.988 22.457  1.00 31.50 ? 330 GLU A N   1 
ATOM   2683 C CA  . GLU A 1 330 ? 2.232  -18.218 22.083  1.00 32.04 ? 330 GLU A CA  1 
ATOM   2684 C C   . GLU A 1 330 ? 3.108  -19.049 21.144  1.00 30.66 ? 330 GLU A C   1 
ATOM   2685 O O   . GLU A 1 330 ? 2.968  -20.270 21.094  1.00 29.72 ? 330 GLU A O   1 
ATOM   2686 C CB  . GLU A 1 330 ? 0.882  -17.870 21.454  1.00 33.37 ? 330 GLU A CB  1 
ATOM   2687 C CG  . GLU A 1 330 ? -0.214 -18.887 21.757  1.00 34.82 ? 330 GLU A CG  1 
ATOM   2688 C CD  . GLU A 1 330 ? -1.624 -18.333 21.620  1.00 36.62 ? 330 GLU A CD  1 
ATOM   2689 O OE1 . GLU A 1 330 ? -1.784 -17.221 21.071  1.00 38.42 ? 330 GLU A OE1 1 
ATOM   2690 O OE2 . GLU A 1 330 ? -2.563 -19.007 22.092  1.00 36.97 ? 330 GLU A OE2 1 
ATOM   2691 N N   . THR A 1 331 ? 4.003  -18.381 20.402  1.00 30.05 ? 331 THR A N   1 
ATOM   2692 C CA  . THR A 1 331 ? 4.876  -19.045 19.446  1.00 29.28 ? 331 THR A CA  1 
ATOM   2693 C C   . THR A 1 331 ? 6.061  -19.679 20.176  1.00 28.48 ? 331 THR A C   1 
ATOM   2694 O O   . THR A 1 331 ? 6.353  -20.857 19.983  1.00 27.82 ? 331 THR A O   1 
ATOM   2695 C CB  . THR A 1 331 ? 5.325  -18.027 18.396  1.00 29.93 ? 331 THR A CB  1 
ATOM   2696 O OG1 . THR A 1 331 ? 4.123  -17.580 17.774  1.00 31.02 ? 331 THR A OG1 1 
ATOM   2697 C CG2 . THR A 1 331 ? 6.242  -18.617 17.340  1.00 30.03 ? 331 THR A CG2 1 
ATOM   2698 N N   . PHE A 1 332 ? 6.738  -18.884 21.013  1.00 27.91 ? 332 PHE A N   1 
ATOM   2699 C CA  . PHE A 1 332 ? 7.994  -19.288 21.625  1.00 27.29 ? 332 PHE A CA  1 
ATOM   2700 C C   . PHE A 1 332 ? 7.777  -19.791 23.050  1.00 28.17 ? 332 PHE A C   1 
ATOM   2701 O O   . PHE A 1 332 ? 8.696  -20.350 23.645  1.00 28.83 ? 332 PHE A O   1 
ATOM   2702 C CB  . PHE A 1 332 ? 8.955  -18.097 21.601  1.00 26.48 ? 332 PHE A CB  1 
ATOM   2703 C CG  . PHE A 1 332 ? 9.241  -17.568 20.204  1.00 24.94 ? 332 PHE A CG  1 
ATOM   2704 C CD1 . PHE A 1 332 ? 10.254 -18.119 19.426  1.00 24.12 ? 332 PHE A CD1 1 
ATOM   2705 C CD2 . PHE A 1 332 ? 8.492  -16.524 19.669  1.00 24.58 ? 332 PHE A CD2 1 
ATOM   2706 C CE1 . PHE A 1 332 ? 10.509 -17.636 18.151  1.00 24.25 ? 332 PHE A CE1 1 
ATOM   2707 C CE2 . PHE A 1 332 ? 8.753  -16.042 18.396  1.00 23.89 ? 332 PHE A CE2 1 
ATOM   2708 C CZ  . PHE A 1 332 ? 9.759  -16.598 17.641  1.00 24.20 ? 332 PHE A CZ  1 
ATOM   2709 N N   . GLY A 1 333 ? 6.569  -19.589 23.593  1.00 28.50 ? 333 GLY A N   1 
ATOM   2710 C CA  . GLY A 1 333 ? 6.286  -19.918 24.981  1.00 29.23 ? 333 GLY A CA  1 
ATOM   2711 C C   . GLY A 1 333 ? 6.855  -18.865 25.930  1.00 30.21 ? 333 GLY A C   1 
ATOM   2712 O O   . GLY A 1 333 ? 6.807  -19.037 27.146  1.00 30.45 ? 333 GLY A O   1 
ATOM   2713 N N   . GLN A 1 334 ? 7.366  -17.765 25.362  1.00 30.50 ? 334 GLN A N   1 
ATOM   2714 C CA  . GLN A 1 334 ? 8.085  -16.756 26.121  1.00 31.12 ? 334 GLN A CA  1 
ATOM   2715 C C   . GLN A 1 334 ? 8.228  -15.501 25.265  1.00 30.62 ? 334 GLN A C   1 
ATOM   2716 O O   . GLN A 1 334 ? 8.013  -15.545 24.055  1.00 29.31 ? 334 GLN A O   1 
ATOM   2717 C CB  . GLN A 1 334 ? 9.450  -17.306 26.543  1.00 32.20 ? 334 GLN A CB  1 
ATOM   2718 C CG  . GLN A 1 334 ? 10.367 -17.654 25.374  1.00 32.52 ? 334 GLN A CG  1 
ATOM   2719 C CD  . GLN A 1 334 ? 11.306 -18.806 25.668  1.00 33.81 ? 334 GLN A CD  1 
ATOM   2720 O OE1 . GLN A 1 334 ? 11.992 -18.833 26.696  1.00 34.49 ? 334 GLN A OE1 1 
ATOM   2721 N NE2 . GLN A 1 334 ? 11.342 -19.782 24.769  1.00 33.60 ? 334 GLN A NE2 1 
ATOM   2722 N N   . VAL A 1 335 ? 8.573  -14.385 25.919  1.00 30.37 ? 335 VAL A N   1 
ATOM   2723 C CA  . VAL A 1 335 ? 8.872  -13.137 25.237  1.00 29.58 ? 335 VAL A CA  1 
ATOM   2724 C C   . VAL A 1 335 ? 10.289 -12.728 25.633  1.00 29.01 ? 335 VAL A C   1 
ATOM   2725 O O   . VAL A 1 335 ? 10.481 -11.998 26.602  1.00 27.50 ? 335 VAL A O   1 
ATOM   2726 C CB  . VAL A 1 335 ? 7.837  -12.040 25.553  1.00 30.23 ? 335 VAL A CB  1 
ATOM   2727 C CG1 . VAL A 1 335 ? 8.158  -10.731 24.842  1.00 30.64 ? 335 VAL A CG1 1 
ATOM   2728 C CG2 . VAL A 1 335 ? 6.423  -12.488 25.200  1.00 30.38 ? 335 VAL A CG2 1 
ATOM   2729 N N   . PRO A 1 336 ? 11.326 -13.192 24.896  1.00 28.73 ? 336 PRO A N   1 
ATOM   2730 C CA  . PRO A 1 336 ? 12.711 -13.003 25.306  1.00 28.40 ? 336 PRO A CA  1 
ATOM   2731 C C   . PRO A 1 336 ? 13.268 -11.647 24.879  1.00 27.80 ? 336 PRO A C   1 
ATOM   2732 O O   . PRO A 1 336 ? 14.172 -11.578 24.047  1.00 27.26 ? 336 PRO A O   1 
ATOM   2733 C CB  . PRO A 1 336 ? 13.419 -14.193 24.659  1.00 28.90 ? 336 PRO A CB  1 
ATOM   2734 C CG  . PRO A 1 336 ? 12.474 -14.717 23.584  1.00 28.87 ? 336 PRO A CG  1 
ATOM   2735 C CD  . PRO A 1 336 ? 11.218 -13.908 23.617  1.00 28.78 ? 336 PRO A CD  1 
ATOM   2736 N N   . ILE A 1 337 ? 12.702 -10.579 25.459  1.00 26.48 ? 337 ILE A N   1 
ATOM   2737 C CA  . ILE A 1 337 ? 13.008 -9.214  25.062  1.00 25.70 ? 337 ILE A CA  1 
ATOM   2738 C C   . ILE A 1 337 ? 13.476 -8.425  26.282  1.00 24.93 ? 337 ILE A C   1 
ATOM   2739 O O   . ILE A 1 337 ? 12.817 -8.433  27.319  1.00 25.50 ? 337 ILE A O   1 
ATOM   2740 C CB  . ILE A 1 337 ? 11.789 -8.543  24.395  1.00 25.49 ? 337 ILE A CB  1 
ATOM   2741 C CG1 . ILE A 1 337 ? 11.653 -8.927  22.915  1.00 25.84 ? 337 ILE A CG1 1 
ATOM   2742 C CG2 . ILE A 1 337 ? 11.833 -7.022  24.558  1.00 25.59 ? 337 ILE A CG2 1 
ATOM   2743 C CD1 . ILE A 1 337 ? 10.987 -10.269 22.664  1.00 25.54 ? 337 ILE A CD1 1 
ATOM   2744 N N   . LEU A 1 338 ? 14.620 -7.746  26.133  1.00 24.15 ? 338 LEU A N   1 
ATOM   2745 C CA  . LEU A 1 338 ? 14.979 -6.624  26.985  1.00 23.73 ? 338 LEU A CA  1 
ATOM   2746 C C   . LEU A 1 338 ? 14.431 -5.353  26.336  1.00 23.53 ? 338 LEU A C   1 
ATOM   2747 O O   . LEU A 1 338 ? 14.583 -5.154  25.136  1.00 23.00 ? 338 LEU A O   1 
ATOM   2748 C CB  . LEU A 1 338 ? 16.496 -6.570  27.179  1.00 23.70 ? 338 LEU A CB  1 
ATOM   2749 C CG  . LEU A 1 338 ? 17.057 -5.339  27.901  1.00 23.46 ? 338 LEU A CG  1 
ATOM   2750 C CD1 . LEU A 1 338 ? 16.475 -5.180  29.293  1.00 23.27 ? 338 LEU A CD1 1 
ATOM   2751 C CD2 . LEU A 1 338 ? 18.577 -5.400  27.979  1.00 23.63 ? 338 LEU A CD2 1 
ATOM   2752 N N   . ALA A 1 339 ? 13.752 -4.518  27.129  1.00 23.77 ? 339 ALA A N   1 
ATOM   2753 C CA  . ALA A 1 339 ? 13.169 -3.287  26.625  1.00 24.69 ? 339 ALA A CA  1 
ATOM   2754 C C   . ALA A 1 339 ? 14.117 -2.128  26.899  1.00 25.00 ? 339 ALA A C   1 
ATOM   2755 O O   . ALA A 1 339 ? 14.383 -1.816  28.058  1.00 26.17 ? 339 ALA A O   1 
ATOM   2756 C CB  . ALA A 1 339 ? 11.827 -3.043  27.277  1.00 25.05 ? 339 ALA A CB  1 
ATOM   2757 N N   . GLU A 1 340 ? 14.622 -1.505  25.830  1.00 24.84 ? 340 GLU A N   1 
ATOM   2758 C CA  . GLU A 1 340 ? 15.272 -0.213  25.950  1.00 25.57 ? 340 GLU A CA  1 
ATOM   2759 C C   . GLU A 1 340 ? 14.177 0.813   26.222  1.00 24.98 ? 340 GLU A C   1 
ATOM   2760 O O   . GLU A 1 340 ? 13.470 1.213   25.301  1.00 24.57 ? 340 GLU A O   1 
ATOM   2761 C CB  . GLU A 1 340 ? 16.099 0.074   24.696  1.00 26.56 ? 340 GLU A CB  1 
ATOM   2762 C CG  . GLU A 1 340 ? 16.851 1.401   24.737  1.00 28.42 ? 340 GLU A CG  1 
ATOM   2763 C CD  . GLU A 1 340 ? 15.991 2.625   24.474  1.00 30.15 ? 340 GLU A CD  1 
ATOM   2764 O OE1 . GLU A 1 340 ? 15.499 2.780   23.335  1.00 31.77 ? 340 GLU A OE1 1 
ATOM   2765 O OE2 . GLU A 1 340 ? 15.803 3.419   25.423  1.00 31.90 ? 340 GLU A OE2 1 
ATOM   2766 N N   . ASP A 1 341 ? 14.033 1.193   27.500  1.00 25.44 ? 341 ASP A N   1 
ATOM   2767 C CA  . ASP A 1 341 ? 12.961 2.065   27.955  1.00 25.91 ? 341 ASP A CA  1 
ATOM   2768 C C   . ASP A 1 341 ? 13.541 3.366   28.509  1.00 27.26 ? 341 ASP A C   1 
ATOM   2769 O O   . ASP A 1 341 ? 12.960 3.969   29.410  1.00 27.18 ? 341 ASP A O   1 
ATOM   2770 C CB  . ASP A 1 341 ? 12.075 1.358   28.973  1.00 25.47 ? 341 ASP A CB  1 
ATOM   2771 C CG  . ASP A 1 341 ? 12.784 0.722   30.162  1.00 25.45 ? 341 ASP A CG  1 
ATOM   2772 O OD1 . ASP A 1 341 ? 14.037 0.689   30.168  1.00 24.49 ? 341 ASP A OD1 1 
ATOM   2773 O OD2 . ASP A 1 341 ? 12.074 0.254   31.074  1.00 24.63 ? 341 ASP A OD2 1 
ATOM   2774 N N   . LEU A 1 342 ? 14.680 3.797   27.945  1.00 27.44 ? 342 LEU A N   1 
ATOM   2775 C CA  . LEU A 1 342 ? 15.361 5.003   28.391  1.00 28.53 ? 342 LEU A CA  1 
ATOM   2776 C C   . LEU A 1 342 ? 14.657 6.222   27.797  1.00 29.06 ? 342 LEU A C   1 
ATOM   2777 O O   . LEU A 1 342 ? 13.929 6.108   26.814  1.00 28.98 ? 342 LEU A O   1 
ATOM   2778 C CB  . LEU A 1 342 ? 16.838 4.951   27.994  1.00 28.31 ? 342 LEU A CB  1 
ATOM   2779 C CG  . LEU A 1 342 ? 17.605 3.688   28.406  1.00 28.81 ? 342 LEU A CG  1 
ATOM   2780 C CD1 . LEU A 1 342 ? 19.025 3.700   27.873  1.00 28.93 ? 342 LEU A CD1 1 
ATOM   2781 C CD2 . LEU A 1 342 ? 17.617 3.521   29.918  1.00 29.26 ? 342 LEU A CD2 1 
ATOM   2782 N N   . GLY A 1 343 ? 14.868 7.387   28.420  1.00 31.24 ? 343 GLY A N   1 
ATOM   2783 C CA  . GLY A 1 343 ? 14.287 8.634   27.948  1.00 33.46 ? 343 GLY A CA  1 
ATOM   2784 C C   . GLY A 1 343 ? 12.839 8.792   28.408  1.00 35.13 ? 343 GLY A C   1 
ATOM   2785 O O   . GLY A 1 343 ? 12.396 8.110   29.329  1.00 36.55 ? 343 GLY A O   1 
ATOM   2786 N N   . VAL A 1 344 ? 12.108 9.702   27.751  1.00 36.52 ? 344 VAL A N   1 
ATOM   2787 C CA  . VAL A 1 344 ? 10.729 9.988   28.115  1.00 38.16 ? 344 VAL A CA  1 
ATOM   2788 C C   . VAL A 1 344 ? 9.901  8.721   27.909  1.00 38.18 ? 344 VAL A C   1 
ATOM   2789 O O   . VAL A 1 344 ? 9.879  8.170   26.811  1.00 38.32 ? 344 VAL A O   1 
ATOM   2790 C CB  . VAL A 1 344 ? 10.132 11.173  27.329  1.00 38.69 ? 344 VAL A CB  1 
ATOM   2791 C CG1 . VAL A 1 344 ? 8.661  11.394  27.669  1.00 39.27 ? 344 VAL A CG1 1 
ATOM   2792 C CG2 . VAL A 1 344 ? 10.921 12.460  27.551  1.00 38.97 ? 344 VAL A CG2 1 
ATOM   2793 N N   . ILE A 1 345 ? 9.217  8.291   28.978  1.00 38.86 ? 345 ILE A N   1 
ATOM   2794 C CA  . ILE A 1 345 ? 8.407  7.081   28.981  1.00 39.66 ? 345 ILE A CA  1 
ATOM   2795 C C   . ILE A 1 345 ? 7.026  7.415   29.537  1.00 40.78 ? 345 ILE A C   1 
ATOM   2796 O O   . ILE A 1 345 ? 6.865  8.398   30.259  1.00 41.57 ? 345 ILE A O   1 
ATOM   2797 C CB  . ILE A 1 345 ? 9.082  5.952   29.785  1.00 40.18 ? 345 ILE A CB  1 
ATOM   2798 C CG1 . ILE A 1 345 ? 9.831  6.495   31.014  1.00 40.37 ? 345 ILE A CG1 1 
ATOM   2799 C CG2 . ILE A 1 345 ? 9.995  5.117   28.885  1.00 40.82 ? 345 ILE A CG2 1 
ATOM   2800 C CD1 . ILE A 1 345 ? 10.513 5.436   31.861  1.00 40.73 ? 345 ILE A CD1 1 
ATOM   2801 N N   . THR A 1 346 ? 6.041  6.575   29.197  1.00 41.25 ? 346 THR A N   1 
ATOM   2802 C CA  . THR A 1 346 ? 4.662  6.789   29.602  1.00 42.10 ? 346 THR A CA  1 
ATOM   2803 C C   . THR A 1 346 ? 4.201  5.603   30.445  1.00 43.32 ? 346 THR A C   1 
ATOM   2804 O O   . THR A 1 346 ? 4.773  4.519   30.356  1.00 44.89 ? 346 THR A O   1 
ATOM   2805 C CB  . THR A 1 346 ? 3.781  6.973   28.366  1.00 42.82 ? 346 THR A CB  1 
ATOM   2806 O OG1 . THR A 1 346 ? 3.525  5.669   27.850  1.00 43.45 ? 346 THR A OG1 1 
ATOM   2807 C CG2 . THR A 1 346 ? 4.424  7.860   27.316  1.00 42.18 ? 346 THR A CG2 1 
ATOM   2808 N N   . PRO A 1 347 ? 3.153  5.767   31.287  1.00 43.51 ? 347 PRO A N   1 
ATOM   2809 C CA  . PRO A 1 347 ? 2.566  4.643   32.008  1.00 42.00 ? 347 PRO A CA  1 
ATOM   2810 C C   . PRO A 1 347 ? 2.104  3.507   31.096  1.00 40.04 ? 347 PRO A C   1 
ATOM   2811 O O   . PRO A 1 347 ? 2.150  2.342   31.486  1.00 38.65 ? 347 PRO A O   1 
ATOM   2812 C CB  . PRO A 1 347 ? 1.403  5.276   32.771  1.00 42.52 ? 347 PRO A CB  1 
ATOM   2813 C CG  . PRO A 1 347 ? 1.804  6.737   32.886  1.00 43.29 ? 347 PRO A CG  1 
ATOM   2814 C CD  . PRO A 1 347 ? 2.497  7.047   31.601  1.00 43.07 ? 347 PRO A CD  1 
ATOM   2815 N N   . GLU A 1 348 ? 1.667  3.862   29.880  1.00 37.63 ? 348 GLU A N   1 
ATOM   2816 C CA  . GLU A 1 348 ? 1.233  2.887   28.891  1.00 36.99 ? 348 GLU A CA  1 
ATOM   2817 C C   . GLU A 1 348 ? 2.400  1.976   28.516  1.00 34.91 ? 348 GLU A C   1 
ATOM   2818 O O   . GLU A 1 348 ? 2.254  0.756   28.513  1.00 35.34 ? 348 GLU A O   1 
ATOM   2819 C CB  . GLU A 1 348 ? 0.694  3.532   27.612  1.00 37.39 ? 348 GLU A CB  1 
ATOM   2820 C CG  . GLU A 1 348 ? -0.542 4.408   27.811  1.00 38.23 ? 348 GLU A CG  1 
ATOM   2821 C CD  . GLU A 1 348 ? -0.270 5.825   28.286  1.00 38.27 ? 348 GLU A CD  1 
ATOM   2822 O OE1 . GLU A 1 348 ? 0.831  6.072   28.811  1.00 40.13 ? 348 GLU A OE1 1 
ATOM   2823 O OE2 . GLU A 1 348 ? -1.148 6.693   28.108  1.00 39.46 ? 348 GLU A OE2 1 
ATOM   2824 N N   . VAL A 1 349 ? 3.554  2.578   28.199  1.00 33.02 ? 349 VAL A N   1 
ATOM   2825 C CA  . VAL A 1 349 ? 4.732  1.826   27.792  1.00 32.01 ? 349 VAL A CA  1 
ATOM   2826 C C   . VAL A 1 349 ? 5.166  0.925   28.948  1.00 31.29 ? 349 VAL A C   1 
ATOM   2827 O O   . VAL A 1 349 ? 5.533  -0.227  28.730  1.00 30.49 ? 349 VAL A O   1 
ATOM   2828 C CB  . VAL A 1 349 ? 5.904  2.720   27.336  1.00 32.22 ? 349 VAL A CB  1 
ATOM   2829 C CG1 . VAL A 1 349 ? 7.145  1.900   26.996  1.00 32.64 ? 349 VAL A CG1 1 
ATOM   2830 C CG2 . VAL A 1 349 ? 5.531  3.608   26.154  1.00 31.95 ? 349 VAL A CG2 1 
ATOM   2831 N N   . GLU A 1 350 ? 5.135  1.470   30.171  1.00 30.69 ? 350 GLU A N   1 
ATOM   2832 C CA  . GLU A 1 350 ? 5.465  0.712   31.368  1.00 30.56 ? 350 GLU A CA  1 
ATOM   2833 C C   . GLU A 1 350 ? 4.482  -0.444  31.539  1.00 29.73 ? 350 GLU A C   1 
ATOM   2834 O O   . GLU A 1 350 ? 4.876  -1.544  31.917  1.00 30.59 ? 350 GLU A O   1 
ATOM   2835 C CB  . GLU A 1 350 ? 5.464  1.626   32.596  1.00 30.56 ? 350 GLU A CB  1 
ATOM   2836 C CG  . GLU A 1 350 ? 6.612  2.633   32.595  1.00 30.64 ? 350 GLU A CG  1 
ATOM   2837 C CD  . GLU A 1 350 ? 6.654  3.592   33.773  1.00 30.56 ? 350 GLU A CD  1 
ATOM   2838 O OE1 . GLU A 1 350 ? 5.769  3.519   34.651  1.00 31.67 ? 350 GLU A OE1 1 
ATOM   2839 O OE2 . GLU A 1 350 ? 7.587  4.420   33.815  1.00 30.81 ? 350 GLU A OE2 1 
ATOM   2840 N N   . ALA A 1 351 ? 3.200  -0.182  31.258  1.00 28.94 ? 351 ALA A N   1 
ATOM   2841 C CA  . ALA A 1 351 ? 2.156  -1.184  31.404  1.00 28.45 ? 351 ALA A CA  1 
ATOM   2842 C C   . ALA A 1 351 ? 2.458  -2.403  30.533  1.00 27.75 ? 351 ALA A C   1 
ATOM   2843 O O   . ALA A 1 351 ? 2.413  -3.534  31.015  1.00 27.00 ? 351 ALA A O   1 
ATOM   2844 C CB  . ALA A 1 351 ? 0.810  -0.580  31.066  1.00 28.37 ? 351 ALA A CB  1 
ATOM   2845 N N   . LEU A 1 352 ? 2.762  -2.152  29.252  1.00 28.28 ? 352 LEU A N   1 
ATOM   2846 C CA  . LEU A 1 352 ? 3.086  -3.200  28.294  1.00 28.50 ? 352 LEU A CA  1 
ATOM   2847 C C   . LEU A 1 352 ? 4.284  -4.019  28.776  1.00 28.80 ? 352 LEU A C   1 
ATOM   2848 O O   . LEU A 1 352 ? 4.226  -5.244  28.805  1.00 28.81 ? 352 LEU A O   1 
ATOM   2849 C CB  . LEU A 1 352 ? 3.351  -2.553  26.934  1.00 29.06 ? 352 LEU A CB  1 
ATOM   2850 C CG  . LEU A 1 352 ? 3.777  -3.488  25.796  1.00 29.42 ? 352 LEU A CG  1 
ATOM   2851 C CD1 . LEU A 1 352 ? 2.653  -4.422  25.379  1.00 29.06 ? 352 LEU A CD1 1 
ATOM   2852 C CD2 . LEU A 1 352 ? 4.272  -2.680  24.608  1.00 29.18 ? 352 LEU A CD2 1 
ATOM   2853 N N   . ARG A 1 353 ? 5.370  -3.338  29.157  1.00 28.65 ? 353 ARG A N   1 
ATOM   2854 C CA  . ARG A 1 353 ? 6.607  -4.007  29.534  1.00 28.88 ? 353 ARG A CA  1 
ATOM   2855 C C   . ARG A 1 353 ? 6.388  -4.909  30.752  1.00 29.29 ? 353 ARG A C   1 
ATOM   2856 O O   . ARG A 1 353 ? 6.892  -6.030  30.787  1.00 28.35 ? 353 ARG A O   1 
ATOM   2857 C CB  . ARG A 1 353 ? 7.686  -2.946  29.783  1.00 29.54 ? 353 ARG A CB  1 
ATOM   2858 C CG  . ARG A 1 353 ? 9.019  -3.470  30.302  1.00 29.95 ? 353 ARG A CG  1 
ATOM   2859 C CD  . ARG A 1 353 ? 9.782  -2.404  31.079  1.00 30.83 ? 353 ARG A CD  1 
ATOM   2860 N NE  . ARG A 1 353 ? 8.981  -1.908  32.205  1.00 31.98 ? 353 ARG A NE  1 
ATOM   2861 C CZ  . ARG A 1 353 ? 9.297  -0.911  33.026  1.00 32.33 ? 353 ARG A CZ  1 
ATOM   2862 N NH1 . ARG A 1 353 ? 10.507 -0.380  33.007  1.00 32.63 ? 353 ARG A NH1 1 
ATOM   2863 N NH2 . ARG A 1 353 ? 8.402  -0.470  33.895  1.00 32.21 ? 353 ARG A NH2 1 
ATOM   2864 N N   . ASP A 1 354 ? 5.644  -4.412  31.749  1.00 29.07 ? 354 ASP A N   1 
ATOM   2865 C CA  . ASP A 1 354 ? 5.406  -5.149  32.982  1.00 30.36 ? 354 ASP A CA  1 
ATOM   2866 C C   . ASP A 1 354 ? 4.432  -6.306  32.750  1.00 30.67 ? 354 ASP A C   1 
ATOM   2867 O O   . ASP A 1 354 ? 4.494  -7.311  33.457  1.00 32.20 ? 354 ASP A O   1 
ATOM   2868 C CB  . ASP A 1 354 ? 4.939  -4.225  34.098  1.00 30.63 ? 354 ASP A CB  1 
ATOM   2869 C CG  . ASP A 1 354 ? 5.989  -3.269  34.648  1.00 31.47 ? 354 ASP A CG  1 
ATOM   2870 O OD1 . ASP A 1 354 ? 7.145  -3.316  34.173  1.00 32.85 ? 354 ASP A OD1 1 
ATOM   2871 O OD2 . ASP A 1 354 ? 5.643  -2.479  35.550  1.00 32.92 ? 354 ASP A OD2 1 
ATOM   2872 N N   . ARG A 1 355 ? 3.541  -6.168  31.759  1.00 30.95 ? 355 ARG A N   1 
ATOM   2873 C CA  . ARG A 1 355 ? 2.542  -7.187  31.465  1.00 30.79 ? 355 ARG A CA  1 
ATOM   2874 C C   . ARG A 1 355 ? 3.206  -8.481  30.997  1.00 30.11 ? 355 ARG A C   1 
ATOM   2875 O O   . ARG A 1 355 ? 2.734  -9.568  31.323  1.00 29.29 ? 355 ARG A O   1 
ATOM   2876 C CB  . ARG A 1 355 ? 1.557  -6.689  30.399  1.00 30.96 ? 355 ARG A CB  1 
ATOM   2877 C CG  . ARG A 1 355 ? 0.510  -7.704  29.959  1.00 32.04 ? 355 ARG A CG  1 
ATOM   2878 C CD  . ARG A 1 355 ? -0.544 -7.079  29.052  1.00 32.45 ? 355 ARG A CD  1 
ATOM   2879 N NE  . ARG A 1 355 ? -1.063 -5.848  29.661  1.00 33.04 ? 355 ARG A NE  1 
ATOM   2880 C CZ  . ARG A 1 355 ? -0.948 -4.616  29.169  1.00 32.83 ? 355 ARG A CZ  1 
ATOM   2881 N NH1 . ARG A 1 355 ? -0.510 -4.414  27.938  1.00 32.82 ? 355 ARG A NH1 1 
ATOM   2882 N NH2 . ARG A 1 355 ? -1.304 -3.580  29.909  1.00 33.01 ? 355 ARG A NH2 1 
ATOM   2883 N N   . PHE A 1 356 ? 4.289  -8.356  30.219  1.00 29.38 ? 356 PHE A N   1 
ATOM   2884 C CA  . PHE A 1 356 ? 4.980  -9.511  29.669  1.00 28.67 ? 356 PHE A CA  1 
ATOM   2885 C C   . PHE A 1 356 ? 6.214  -9.825  30.513  1.00 28.96 ? 356 PHE A C   1 
ATOM   2886 O O   . PHE A 1 356 ? 7.041  -10.648 30.122  1.00 30.33 ? 356 PHE A O   1 
ATOM   2887 C CB  . PHE A 1 356 ? 5.234  -9.221  28.185  1.00 28.41 ? 356 PHE A CB  1 
ATOM   2888 C CG  . PHE A 1 356 ? 3.929  -9.131  27.403  1.00 27.46 ? 356 PHE A CG  1 
ATOM   2889 C CD1 . PHE A 1 356 ? 3.198  -10.279 27.119  1.00 27.38 ? 356 PHE A CD1 1 
ATOM   2890 C CD2 . PHE A 1 356 ? 3.421  -7.905  26.985  1.00 26.71 ? 356 PHE A CD2 1 
ATOM   2891 C CE1 . PHE A 1 356 ? 1.994  -10.203 26.434  1.00 27.42 ? 356 PHE A CE1 1 
ATOM   2892 C CE2 . PHE A 1 356 ? 2.220  -7.838  26.294  1.00 27.16 ? 356 PHE A CE2 1 
ATOM   2893 C CZ  . PHE A 1 356 ? 1.508  -8.983  26.024  1.00 26.94 ? 356 PHE A CZ  1 
ATOM   2894 N N   . GLY A 1 357 ? 6.311  -9.171  31.679  1.00 28.07 ? 357 GLY A N   1 
ATOM   2895 C CA  . GLY A 1 357 ? 7.391  -9.395  32.624  1.00 27.46 ? 357 GLY A CA  1 
ATOM   2896 C C   . GLY A 1 357 ? 8.750  -9.049  32.022  1.00 26.38 ? 357 GLY A C   1 
ATOM   2897 O O   . GLY A 1 357 ? 9.758  -9.626  32.412  1.00 26.74 ? 357 GLY A O   1 
ATOM   2898 N N   . LEU A 1 358 ? 8.764  -8.104  31.075  1.00 25.80 ? 358 LEU A N   1 
ATOM   2899 C CA  . LEU A 1 358 ? 9.975  -7.785  30.341  1.00 24.74 ? 358 LEU A CA  1 
ATOM   2900 C C   . LEU A 1 358 ? 10.893 -6.958  31.235  1.00 24.30 ? 358 LEU A C   1 
ATOM   2901 O O   . LEU A 1 358 ? 10.432 -6.048  31.922  1.00 23.42 ? 358 LEU A O   1 
ATOM   2902 C CB  . LEU A 1 358 ? 9.647  -7.046  29.045  1.00 24.75 ? 358 LEU A CB  1 
ATOM   2903 C CG  . LEU A 1 358 ? 8.709  -7.771  28.073  1.00 24.98 ? 358 LEU A CG  1 
ATOM   2904 C CD1 . LEU A 1 358 ? 8.649  -7.027  26.751  1.00 25.07 ? 358 LEU A CD1 1 
ATOM   2905 C CD2 . LEU A 1 358 ? 9.116  -9.215  27.846  1.00 25.30 ? 358 LEU A CD2 1 
ATOM   2906 N N   . PRO A 1 359 ? 12.217 -7.243  31.250  1.00 23.61 ? 359 PRO A N   1 
ATOM   2907 C CA  . PRO A 1 359 ? 13.163 -6.420  31.991  1.00 23.45 ? 359 PRO A CA  1 
ATOM   2908 C C   . PRO A 1 359 ? 13.436 -5.083  31.305  1.00 22.89 ? 359 PRO A C   1 
ATOM   2909 O O   . PRO A 1 359 ? 13.327 -4.979  30.087  1.00 23.24 ? 359 PRO A O   1 
ATOM   2910 C CB  . PRO A 1 359 ? 14.419 -7.285  32.089  1.00 23.08 ? 359 PRO A CB  1 
ATOM   2911 C CG  . PRO A 1 359 ? 14.140 -8.551  31.296  1.00 23.32 ? 359 PRO A CG  1 
ATOM   2912 C CD  . PRO A 1 359 ? 12.861 -8.361  30.544  1.00 23.49 ? 359 PRO A CD  1 
ATOM   2913 N N   . GLY A 1 360 ? 13.791 -4.074  32.108  1.00 22.81 ? 360 GLY A N   1 
ATOM   2914 C CA  . GLY A 1 360 ? 14.039 -2.726  31.626  1.00 22.70 ? 360 GLY A CA  1 
ATOM   2915 C C   . GLY A 1 360 ? 15.489 -2.311  31.851  1.00 22.30 ? 360 GLY A C   1 
ATOM   2916 O O   . GLY A 1 360 ? 16.238 -2.990  32.549  1.00 23.32 ? 360 GLY A O   1 
ATOM   2917 N N   . MET A 1 361 ? 15.875 -1.181  31.255  1.00 22.21 ? 361 MET A N   1 
ATOM   2918 C CA  . MET A 1 361 ? 17.252 -0.720  31.316  1.00 21.41 ? 361 MET A CA  1 
ATOM   2919 C C   . MET A 1 361 ? 17.414 0.321   32.420  1.00 21.52 ? 361 MET A C   1 
ATOM   2920 O O   . MET A 1 361 ? 16.513 1.115   32.683  1.00 22.12 ? 361 MET A O   1 
ATOM   2921 C CB  . MET A 1 361 ? 17.688 -0.116  29.978  1.00 21.37 ? 361 MET A CB  1 
ATOM   2922 C CG  . MET A 1 361 ? 17.854 -1.137  28.876  1.00 21.86 ? 361 MET A CG  1 
ATOM   2923 S SD  . MET A 1 361 ? 18.684 -0.471  27.420  1.00 22.17 ? 361 MET A SD  1 
ATOM   2924 C CE  . MET A 1 361 ? 20.301 0.005   28.051  1.00 22.05 ? 361 MET A CE  1 
ATOM   2925 N N   . LYS A 1 362 ? 18.585 0.295   33.061  1.00 20.71 ? 362 LYS A N   1 
ATOM   2926 C CA  . LYS A 1 362 ? 18.998 1.334   33.990  1.00 20.21 ? 362 LYS A CA  1 
ATOM   2927 C C   . LYS A 1 362 ? 20.436 1.718   33.650  1.00 19.48 ? 362 LYS A C   1 
ATOM   2928 O O   . LYS A 1 362 ? 21.238 0.845   33.329  1.00 20.19 ? 362 LYS A O   1 
ATOM   2929 C CB  . LYS A 1 362 ? 18.849 0.822   35.429  1.00 20.21 ? 362 LYS A CB  1 
ATOM   2930 C CG  . LYS A 1 362 ? 17.427 0.504   35.880  1.00 20.02 ? 362 LYS A CG  1 
ATOM   2931 C CD  . LYS A 1 362 ? 16.527 1.716   36.091  1.00 20.21 ? 362 LYS A CD  1 
ATOM   2932 C CE  . LYS A 1 362 ? 15.156 1.326   36.569  1.00 20.47 ? 362 LYS A CE  1 
ATOM   2933 N NZ  . LYS A 1 362 ? 14.312 2.493   36.835  1.00 20.58 ? 362 LYS A NZ  1 
ATOM   2934 N N   . VAL A 1 363 ? 20.746 3.023   33.694  1.00 19.00 ? 363 VAL A N   1 
ATOM   2935 C CA  . VAL A 1 363 ? 22.078 3.520   33.376  1.00 18.57 ? 363 VAL A CA  1 
ATOM   2936 C C   . VAL A 1 363 ? 22.551 4.438   34.500  1.00 18.61 ? 363 VAL A C   1 
ATOM   2937 O O   . VAL A 1 363 ? 21.915 5.449   34.790  1.00 18.34 ? 363 VAL A O   1 
ATOM   2938 C CB  . VAL A 1 363 ? 22.136 4.263   32.029  1.00 18.50 ? 363 VAL A CB  1 
ATOM   2939 C CG1 . VAL A 1 363 ? 23.523 4.842   31.755  1.00 18.07 ? 363 VAL A CG1 1 
ATOM   2940 C CG2 . VAL A 1 363 ? 21.684 3.382   30.873  1.00 18.70 ? 363 VAL A CG2 1 
ATOM   2941 N N   . LEU A 1 364 ? 23.717 4.109   35.067  1.00 18.48 ? 364 LEU A N   1 
ATOM   2942 C CA  . LEU A 1 364 ? 24.222 4.755   36.269  1.00 18.52 ? 364 LEU A CA  1 
ATOM   2943 C C   . LEU A 1 364 ? 24.728 6.165   35.972  1.00 18.47 ? 364 LEU A C   1 
ATOM   2944 O O   . LEU A 1 364 ? 24.655 7.028   36.843  1.00 18.28 ? 364 LEU A O   1 
ATOM   2945 C CB  . LEU A 1 364 ? 25.305 3.875   36.895  1.00 18.62 ? 364 LEU A CB  1 
ATOM   2946 C CG  . LEU A 1 364 ? 24.813 2.581   37.553  1.00 18.58 ? 364 LEU A CG  1 
ATOM   2947 C CD1 . LEU A 1 364 ? 25.960 1.666   37.964  1.00 18.57 ? 364 LEU A CD1 1 
ATOM   2948 C CD2 . LEU A 1 364 ? 23.947 2.896   38.759  1.00 18.47 ? 364 LEU A CD2 1 
ATOM   2949 N N   . GLN A 1 365 ? 25.231 6.402   34.751  1.00 18.77 ? 365 GLN A N   1 
ATOM   2950 C CA  . GLN A 1 365 ? 25.737 7.715   34.371  1.00 18.51 ? 365 GLN A CA  1 
ATOM   2951 C C   . GLN A 1 365 ? 24.625 8.765   34.406  1.00 18.85 ? 365 GLN A C   1 
ATOM   2952 O O   . GLN A 1 365 ? 24.905 9.938   34.630  1.00 19.37 ? 365 GLN A O   1 
ATOM   2953 C CB  . GLN A 1 365 ? 26.393 7.704   32.990  1.00 18.54 ? 365 GLN A CB  1 
ATOM   2954 C CG  . GLN A 1 365 ? 27.801 7.118   32.975  1.00 18.41 ? 365 GLN A CG  1 
ATOM   2955 C CD  . GLN A 1 365 ? 28.386 7.009   31.584  1.00 18.30 ? 365 GLN A CD  1 
ATOM   2956 O OE1 . GLN A 1 365 ? 27.899 7.625   30.633  1.00 18.01 ? 365 GLN A OE1 1 
ATOM   2957 N NE2 . GLN A 1 365 ? 29.455 6.238   31.453  1.00 19.28 ? 365 GLN A NE2 1 
ATOM   2958 N N   . PHE A 1 366 ? 23.372 8.347   34.187  1.00 19.07 ? 366 PHE A N   1 
ATOM   2959 C CA  . PHE A 1 366 ? 22.236 9.258   34.179  1.00 20.07 ? 366 PHE A CA  1 
ATOM   2960 C C   . PHE A 1 366 ? 21.816 9.670   35.593  1.00 20.86 ? 366 PHE A C   1 
ATOM   2961 O O   . PHE A 1 366 ? 21.074 10.637  35.749  1.00 22.04 ? 366 PHE A O   1 
ATOM   2962 C CB  . PHE A 1 366 ? 21.024 8.600   33.509  1.00 20.63 ? 366 PHE A CB  1 
ATOM   2963 C CG  . PHE A 1 366 ? 21.177 8.199   32.047  1.00 21.09 ? 366 PHE A CG  1 
ATOM   2964 C CD1 . PHE A 1 366 ? 22.092 8.831   31.208  1.00 21.53 ? 366 PHE A CD1 1 
ATOM   2965 C CD2 . PHE A 1 366 ? 20.379 7.194   31.506  1.00 21.12 ? 366 PHE A CD2 1 
ATOM   2966 C CE1 . PHE A 1 366 ? 22.213 8.452   29.879  1.00 21.82 ? 366 PHE A CE1 1 
ATOM   2967 C CE2 . PHE A 1 366 ? 20.505 6.822   30.176  1.00 21.07 ? 366 PHE A CE2 1 
ATOM   2968 C CZ  . PHE A 1 366 ? 21.419 7.451   29.367  1.00 21.10 ? 366 PHE A CZ  1 
ATOM   2969 N N   . ALA A 1 367 ? 22.297 8.950   36.616  1.00 21.41 ? 367 ALA A N   1 
ATOM   2970 C CA  . ALA A 1 367 ? 21.608 8.860   37.895  1.00 22.17 ? 367 ALA A CA  1 
ATOM   2971 C C   . ALA A 1 367 ? 21.833 10.067  38.809  1.00 23.23 ? 367 ALA A C   1 
ATOM   2972 O O   . ALA A 1 367 ? 21.039 10.277  39.724  1.00 23.49 ? 367 ALA A O   1 
ATOM   2973 C CB  . ALA A 1 367 ? 22.026 7.582   38.590  1.00 22.20 ? 367 ALA A CB  1 
ATOM   2974 N N   . PHE A 1 368 ? 22.899 10.849  38.587  1.00 23.89 ? 368 PHE A N   1 
ATOM   2975 C CA  . PHE A 1 368 ? 23.352 11.801  39.592  1.00 24.90 ? 368 PHE A CA  1 
ATOM   2976 C C   . PHE A 1 368 ? 23.167 13.255  39.157  1.00 26.90 ? 368 PHE A C   1 
ATOM   2977 O O   . PHE A 1 368 ? 23.735 14.149  39.780  1.00 27.94 ? 368 PHE A O   1 
ATOM   2978 C CB  . PHE A 1 368 ? 24.824 11.510  39.891  1.00 24.13 ? 368 PHE A CB  1 
ATOM   2979 C CG  . PHE A 1 368 ? 25.090 10.061  40.268  1.00 23.65 ? 368 PHE A CG  1 
ATOM   2980 C CD1 . PHE A 1 368 ? 24.835 9.602   41.556  1.00 23.72 ? 368 PHE A CD1 1 
ATOM   2981 C CD2 . PHE A 1 368 ? 25.591 9.164   39.331  1.00 23.30 ? 368 PHE A CD2 1 
ATOM   2982 C CE1 . PHE A 1 368 ? 25.080 8.281   41.897  1.00 23.46 ? 368 PHE A CE1 1 
ATOM   2983 C CE2 . PHE A 1 368 ? 25.836 7.846   39.679  1.00 23.10 ? 368 PHE A CE2 1 
ATOM   2984 C CZ  . PHE A 1 368 ? 25.576 7.407   40.957  1.00 23.28 ? 368 PHE A CZ  1 
ATOM   2985 N N   . ASP A 1 369 ? 22.374 13.498  38.108  1.00 28.53 ? 369 ASP A N   1 
ATOM   2986 C CA  . ASP A 1 369 ? 22.137 14.855  37.636  1.00 31.20 ? 369 ASP A CA  1 
ATOM   2987 C C   . ASP A 1 369 ? 20.954 15.481  38.381  1.00 33.35 ? 369 ASP A C   1 
ATOM   2988 O O   . ASP A 1 369 ? 20.848 16.704  38.445  1.00 34.14 ? 369 ASP A O   1 
ATOM   2989 C CB  . ASP A 1 369 ? 21.978 14.894  36.122  1.00 31.39 ? 369 ASP A CB  1 
ATOM   2990 C CG  . ASP A 1 369 ? 20.796 14.124  35.554  1.00 32.21 ? 369 ASP A CG  1 
ATOM   2991 O OD1 . ASP A 1 369 ? 19.960 13.650  36.354  1.00 33.40 ? 369 ASP A OD1 1 
ATOM   2992 O OD2 . ASP A 1 369 ? 20.725 13.999  34.314  1.00 33.84 ? 369 ASP A OD2 1 
ATOM   2993 N N   . ASP A 1 370 ? 20.075 14.637  38.942  1.00 34.65 ? 370 ASP A N   1 
ATOM   2994 C CA  . ASP A 1 370 ? 18.838 15.079  39.570  1.00 35.66 ? 370 ASP A CA  1 
ATOM   2995 C C   . ASP A 1 370 ? 19.018 15.062  41.091  1.00 35.30 ? 370 ASP A C   1 
ATOM   2996 O O   . ASP A 1 370 ? 20.100 15.368  41.592  1.00 33.82 ? 370 ASP A O   1 
ATOM   2997 C CB  . ASP A 1 370 ? 17.682 14.225  39.067  1.00 37.57 ? 370 ASP A CB  1 
ATOM   2998 C CG  . ASP A 1 370 ? 16.275 14.742  39.336  1.00 40.24 ? 370 ASP A CG  1 
ATOM   2999 O OD1 . ASP A 1 370 ? 16.148 15.829  39.944  1.00 42.52 ? 370 ASP A OD1 1 
ATOM   3000 O OD2 . ASP A 1 370 ? 15.316 14.044  38.945  1.00 40.73 ? 370 ASP A OD2 1 
ATOM   3001 N N   . GLY A 1 371 ? 17.940 14.738  41.819  1.00 34.83 ? 371 GLY A N   1 
ATOM   3002 C CA  . GLY A 1 371 ? 18.003 14.461  43.246  1.00 33.68 ? 371 GLY A CA  1 
ATOM   3003 C C   . GLY A 1 371 ? 17.881 12.962  43.510  1.00 32.01 ? 371 GLY A C   1 
ATOM   3004 O O   . GLY A 1 371 ? 18.235 12.155  42.653  1.00 30.26 ? 371 GLY A O   1 
ATOM   3005 N N   . MET A 1 372 ? 17.355 12.604  44.691  1.00 31.30 ? 372 MET A N   1 
ATOM   3006 C CA  . MET A 1 372 ? 17.249 11.211  45.106  1.00 31.44 ? 372 MET A CA  1 
ATOM   3007 C C   . MET A 1 372 ? 16.075 10.523  44.406  1.00 30.48 ? 372 MET A C   1 
ATOM   3008 O O   . MET A 1 372 ? 15.974 9.299   44.430  1.00 30.02 ? 372 MET A O   1 
ATOM   3009 C CB  . MET A 1 372 ? 17.074 11.094  46.625  1.00 32.50 ? 372 MET A CB  1 
ATOM   3010 C CG  . MET A 1 372 ? 18.313 11.459  47.424  1.00 33.64 ? 372 MET A CG  1 
ATOM   3011 S SD  . MET A 1 372 ? 19.641 10.239  47.317  1.00 35.42 ? 372 MET A SD  1 
ATOM   3012 C CE  . MET A 1 372 ? 19.026 8.941   48.399  1.00 34.47 ? 372 MET A CE  1 
ATOM   3013 N N   . GLU A 1 373 ? 15.191 11.316  43.789  1.00 29.81 ? 373 GLU A N   1 
ATOM   3014 C CA  . GLU A 1 373 ? 14.047 10.799  43.053  1.00 29.69 ? 373 GLU A CA  1 
ATOM   3015 C C   . GLU A 1 373 ? 14.489 10.134  41.746  1.00 28.43 ? 373 GLU A C   1 
ATOM   3016 O O   . GLU A 1 373 ? 13.726 9.367   41.159  1.00 27.08 ? 373 GLU A O   1 
ATOM   3017 C CB  . GLU A 1 373 ? 13.015 11.897  42.773  1.00 31.09 ? 373 GLU A CB  1 
ATOM   3018 C CG  . GLU A 1 373 ? 13.592 13.193  42.200  1.00 32.11 ? 373 GLU A CG  1 
ATOM   3019 C CD  . GLU A 1 373 ? 14.027 14.228  43.227  1.00 32.93 ? 373 GLU A CD  1 
ATOM   3020 O OE1 . GLU A 1 373 ? 13.495 15.357  43.198  1.00 34.54 ? 373 GLU A OE1 1 
ATOM   3021 O OE2 . GLU A 1 373 ? 14.902 13.910  44.059  1.00 33.57 ? 373 GLU A OE2 1 
ATOM   3022 N N   . ASN A 1 374 ? 15.720 10.429  41.304  1.00 26.37 ? 374 ASN A N   1 
ATOM   3023 C CA  . ASN A 1 374 ? 16.237 9.956   40.029  1.00 25.86 ? 374 ASN A CA  1 
ATOM   3024 C C   . ASN A 1 374 ? 16.003 8.450   39.883  1.00 24.75 ? 374 ASN A C   1 
ATOM   3025 O O   . ASN A 1 374 ? 16.455 7.674   40.723  1.00 23.52 ? 374 ASN A O   1 
ATOM   3026 C CB  . ASN A 1 374 ? 17.718 10.295  39.889  1.00 25.59 ? 374 ASN A CB  1 
ATOM   3027 C CG  . ASN A 1 374 ? 18.225 10.100  38.481  1.00 25.42 ? 374 ASN A CG  1 
ATOM   3028 O OD1 . ASN A 1 374 ? 18.006 9.042   37.882  1.00 25.97 ? 374 ASN A OD1 1 
ATOM   3029 N ND2 . ASN A 1 374 ? 18.906 11.096  37.935  1.00 26.15 ? 374 ASN A ND2 1 
ATOM   3030 N N   . PRO A 1 375 ? 15.323 7.982   38.804  1.00 24.34 ? 375 PRO A N   1 
ATOM   3031 C CA  . PRO A 1 375 ? 14.996 6.565   38.654  1.00 23.58 ? 375 PRO A CA  1 
ATOM   3032 C C   . PRO A 1 375 ? 16.206 5.640   38.549  1.00 22.61 ? 375 PRO A C   1 
ATOM   3033 O O   . PRO A 1 375 ? 16.112 4.459   38.877  1.00 21.70 ? 375 PRO A O   1 
ATOM   3034 C CB  . PRO A 1 375 ? 14.187 6.500   37.361  1.00 24.15 ? 375 PRO A CB  1 
ATOM   3035 C CG  . PRO A 1 375 ? 13.762 7.933   37.095  1.00 24.64 ? 375 PRO A CG  1 
ATOM   3036 C CD  . PRO A 1 375 ? 14.841 8.792   37.672  1.00 24.58 ? 375 PRO A CD  1 
ATOM   3037 N N   . PHE A 1 376 ? 17.336 6.190   38.087  1.00 22.34 ? 376 PHE A N   1 
ATOM   3038 C CA  . PHE A 1 376 ? 18.528 5.401   37.815  1.00 21.70 ? 376 PHE A CA  1 
ATOM   3039 C C   . PHE A 1 376 ? 19.322 5.162   39.099  1.00 21.23 ? 376 PHE A C   1 
ATOM   3040 O O   . PHE A 1 376 ? 20.265 4.372   39.093  1.00 21.05 ? 376 PHE A O   1 
ATOM   3041 C CB  . PHE A 1 376 ? 19.312 6.114   36.710  1.00 21.74 ? 376 PHE A CB  1 
ATOM   3042 C CG  . PHE A 1 376 ? 18.530 6.223   35.407  1.00 21.66 ? 376 PHE A CG  1 
ATOM   3043 C CD1 . PHE A 1 376 ? 18.249 5.086   34.659  1.00 22.20 ? 376 PHE A CD1 1 
ATOM   3044 C CD2 . PHE A 1 376 ? 18.073 7.450   34.934  1.00 21.93 ? 376 PHE A CD2 1 
ATOM   3045 C CE1 . PHE A 1 376 ? 17.542 5.171   33.468  1.00 22.12 ? 376 PHE A CE1 1 
ATOM   3046 C CE2 . PHE A 1 376 ? 17.363 7.530   33.744  1.00 21.97 ? 376 PHE A CE2 1 
ATOM   3047 C CZ  . PHE A 1 376 ? 17.102 6.391   33.014  1.00 21.73 ? 376 PHE A CZ  1 
ATOM   3048 N N   . LEU A 1 377 ? 18.947 5.838   40.194  1.00 21.01 ? 377 LEU A N   1 
ATOM   3049 C CA  . LEU A 1 377 ? 19.532 5.561   41.497  1.00 20.83 ? 377 LEU A CA  1 
ATOM   3050 C C   . LEU A 1 377 ? 19.021 4.207   41.986  1.00 20.57 ? 377 LEU A C   1 
ATOM   3051 O O   . LEU A 1 377 ? 17.815 3.958   41.954  1.00 19.89 ? 377 LEU A O   1 
ATOM   3052 C CB  . LEU A 1 377 ? 19.206 6.672   42.494  1.00 21.05 ? 377 LEU A CB  1 
ATOM   3053 C CG  . LEU A 1 377 ? 19.859 8.034   42.234  1.00 21.00 ? 377 LEU A CG  1 
ATOM   3054 C CD1 . LEU A 1 377 ? 19.312 9.072   43.196  1.00 21.07 ? 377 LEU A CD1 1 
ATOM   3055 C CD2 . LEU A 1 377 ? 21.372 7.975   42.334  1.00 21.22 ? 377 LEU A CD2 1 
ATOM   3056 N N   . PRO A 1 378 ? 19.922 3.296   42.433  1.00 19.80 ? 378 PRO A N   1 
ATOM   3057 C CA  . PRO A 1 378 ? 19.551 1.925   42.759  1.00 19.50 ? 378 PRO A CA  1 
ATOM   3058 C C   . PRO A 1 378 ? 18.369 1.771   43.712  1.00 18.95 ? 378 PRO A C   1 
ATOM   3059 O O   . PRO A 1 378 ? 17.571 0.853   43.534  1.00 17.38 ? 378 PRO A O   1 
ATOM   3060 C CB  . PRO A 1 378 ? 20.811 1.319   43.376  1.00 19.79 ? 378 PRO A CB  1 
ATOM   3061 C CG  . PRO A 1 378 ? 21.770 2.474   43.568  1.00 19.77 ? 378 PRO A CG  1 
ATOM   3062 C CD  . PRO A 1 378 ? 21.366 3.532   42.588  1.00 20.03 ? 378 PRO A CD  1 
ATOM   3063 N N   . HIS A 1 379 ? 18.268 2.654   44.716  1.00 19.08 ? 379 HIS A N   1 
ATOM   3064 C CA  . HIS A 1 379 ? 17.239 2.525   45.739  1.00 19.63 ? 379 HIS A CA  1 
ATOM   3065 C C   . HIS A 1 379 ? 15.853 2.625   45.098  1.00 19.73 ? 379 HIS A C   1 
ATOM   3066 O O   . HIS A 1 379 ? 14.887 2.075   45.624  1.00 20.41 ? 379 HIS A O   1 
ATOM   3067 C CB  . HIS A 1 379 ? 17.476 3.505   46.897  1.00 20.00 ? 379 HIS A CB  1 
ATOM   3068 C CG  . HIS A 1 379 ? 17.218 4.943   46.589  1.00 20.32 ? 379 HIS A CG  1 
ATOM   3069 N ND1 . HIS A 1 379 ? 18.208 5.820   46.203  1.00 20.93 ? 379 HIS A ND1 1 
ATOM   3070 C CD2 . HIS A 1 379 ? 16.089 5.662   46.642  1.00 20.46 ? 379 HIS A CD2 1 
ATOM   3071 C CE1 . HIS A 1 379 ? 17.678 7.021   46.012  1.00 21.25 ? 379 HIS A CE1 1 
ATOM   3072 N NE2 . HIS A 1 379 ? 16.392 6.947   46.273  1.00 20.82 ? 379 HIS A NE2 1 
ATOM   3073 N N   . ASN A 1 380 ? 15.778 3.281   43.933  1.00 19.39 ? 380 ASN A N   1 
ATOM   3074 C CA  . ASN A 1 380 ? 14.526 3.436   43.208  1.00 19.88 ? 380 ASN A CA  1 
ATOM   3075 C C   . ASN A 1 380 ? 14.297 2.284   42.227  1.00 20.10 ? 380 ASN A C   1 
ATOM   3076 O O   . ASN A 1 380 ? 13.312 2.304   41.493  1.00 20.07 ? 380 ASN A O   1 
ATOM   3077 C CB  . ASN A 1 380 ? 14.481 4.774   42.476  1.00 19.39 ? 380 ASN A CB  1 
ATOM   3078 C CG  . ASN A 1 380 ? 14.623 5.943   43.420  1.00 19.44 ? 380 ASN A CG  1 
ATOM   3079 O OD1 . ASN A 1 380 ? 14.007 5.948   44.492  1.00 19.98 ? 380 ASN A OD1 1 
ATOM   3080 N ND2 . ASN A 1 380 ? 15.434 6.929   43.063  1.00 19.70 ? 380 ASN A ND2 1 
ATOM   3081 N N   . TYR A 1 381 ? 15.193 1.287   42.194  1.00 20.39 ? 381 TYR A N   1 
ATOM   3082 C CA  . TYR A 1 381 ? 15.026 0.162   41.284  1.00 20.96 ? 381 TYR A CA  1 
ATOM   3083 C C   . TYR A 1 381 ? 13.877 -0.713  41.783  1.00 21.54 ? 381 TYR A C   1 
ATOM   3084 O O   . TYR A 1 381 ? 13.674 -0.839  42.991  1.00 23.02 ? 381 TYR A O   1 
ATOM   3085 C CB  . TYR A 1 381 ? 16.276 -0.712  41.109  1.00 20.93 ? 381 TYR A CB  1 
ATOM   3086 C CG  . TYR A 1 381 ? 17.465 -0.072  40.401  1.00 20.58 ? 381 TYR A CG  1 
ATOM   3087 C CD1 . TYR A 1 381 ? 17.347 1.129   39.703  1.00 20.50 ? 381 TYR A CD1 1 
ATOM   3088 C CD2 . TYR A 1 381 ? 18.708 -0.696  40.403  1.00 20.44 ? 381 TYR A CD2 1 
ATOM   3089 C CE1 . TYR A 1 381 ? 18.435 1.701   39.062  1.00 20.67 ? 381 TYR A CE1 1 
ATOM   3090 C CE2 . TYR A 1 381 ? 19.802 -0.135  39.765  1.00 20.54 ? 381 TYR A CE2 1 
ATOM   3091 C CZ  . TYR A 1 381 ? 19.665 1.066   39.089  1.00 20.49 ? 381 TYR A CZ  1 
ATOM   3092 O OH  . TYR A 1 381 ? 20.744 1.621   38.464  1.00 20.52 ? 381 TYR A OH  1 
ATOM   3093 N N   . PRO A 1 382 ? 13.088 -1.331  40.870  1.00 21.67 ? 382 PRO A N   1 
ATOM   3094 C CA  . PRO A 1 382 ? 11.970 -2.183  41.265  1.00 21.53 ? 382 PRO A CA  1 
ATOM   3095 C C   . PRO A 1 382 ? 12.410 -3.448  41.995  1.00 21.73 ? 382 PRO A C   1 
ATOM   3096 O O   . PRO A 1 382 ? 13.457 -4.008  41.682  1.00 21.71 ? 382 PRO A O   1 
ATOM   3097 C CB  . PRO A 1 382 ? 11.283 -2.511  39.944  1.00 21.78 ? 382 PRO A CB  1 
ATOM   3098 C CG  . PRO A 1 382 ? 12.396 -2.370  38.924  1.00 21.71 ? 382 PRO A CG  1 
ATOM   3099 C CD  . PRO A 1 382 ? 13.231 -1.230  39.409  1.00 21.50 ? 382 PRO A CD  1 
ATOM   3100 N N   . SER A 1 383 ? 11.596 -3.884  42.963  1.00 22.28 ? 383 SER A N   1 
ATOM   3101 C CA  . SER A 1 383 ? 11.924 -5.020  43.811  1.00 23.36 ? 383 SER A CA  1 
ATOM   3102 C C   . SER A 1 383 ? 11.887 -6.327  43.027  1.00 23.51 ? 383 SER A C   1 
ATOM   3103 O O   . SER A 1 383 ? 12.530 -7.297  43.425  1.00 24.38 ? 383 SER A O   1 
ATOM   3104 C CB  . SER A 1 383 ? 11.005 -5.104  44.994  1.00 23.85 ? 383 SER A CB  1 
ATOM   3105 O OG  . SER A 1 383 ? 11.124 -3.935  45.785  1.00 24.76 ? 383 SER A OG  1 
ATOM   3106 N N   . HIS A 1 384 ? 11.110 -6.354  41.938  1.00 23.46 ? 384 HIS A N   1 
ATOM   3107 C CA  . HIS A 1 384 ? 11.015 -7.543  41.106  1.00 23.28 ? 384 HIS A CA  1 
ATOM   3108 C C   . HIS A 1 384 ? 12.374 -7.813  40.457  1.00 22.87 ? 384 HIS A C   1 
ATOM   3109 O O   . HIS A 1 384 ? 12.677 -8.953  40.117  1.00 22.82 ? 384 HIS A O   1 
ATOM   3110 C CB  . HIS A 1 384 ? 9.814  -7.452  40.154  1.00 22.50 ? 384 HIS A CB  1 
ATOM   3111 C CG  . HIS A 1 384 ? 9.855  -6.337  39.159  1.00 21.96 ? 384 HIS A CG  1 
ATOM   3112 N ND1 . HIS A 1 384 ? 10.931 -6.093  38.334  1.00 21.84 ? 384 HIS A ND1 1 
ATOM   3113 C CD2 . HIS A 1 384 ? 8.930  -5.424  38.833  1.00 21.45 ? 384 HIS A CD2 1 
ATOM   3114 C CE1 . HIS A 1 384 ? 10.661 -5.058  37.551  1.00 21.29 ? 384 HIS A CE1 1 
ATOM   3115 N NE2 . HIS A 1 384 ? 9.452  -4.633  37.841  1.00 21.29 ? 384 HIS A NE2 1 
ATOM   3116 N N   . GLY A 1 385 ? 13.188 -6.758  40.304  1.00 22.71 ? 385 GLY A N   1 
ATOM   3117 C CA  . GLY A 1 385 ? 14.589 -6.893  39.936  1.00 22.35 ? 385 GLY A CA  1 
ATOM   3118 C C   . GLY A 1 385 ? 14.803 -7.076  38.433  1.00 22.44 ? 385 GLY A C   1 
ATOM   3119 O O   . GLY A 1 385 ? 15.940 -7.229  37.988  1.00 21.84 ? 385 GLY A O   1 
ATOM   3120 N N   . ARG A 1 386 ? 13.715 -7.039  37.653  1.00 22.48 ? 386 ARG A N   1 
ATOM   3121 C CA  . ARG A 1 386 ? 13.782 -7.277  36.220  1.00 23.17 ? 386 ARG A CA  1 
ATOM   3122 C C   . ARG A 1 386 ? 14.296 -6.007  35.546  1.00 22.76 ? 386 ARG A C   1 
ATOM   3123 O O   . ARG A 1 386 ? 13.550 -5.288  34.881  1.00 21.39 ? 386 ARG A O   1 
ATOM   3124 C CB  . ARG A 1 386 ? 12.419 -7.736  35.686  1.00 24.69 ? 386 ARG A CB  1 
ATOM   3125 C CG  . ARG A 1 386 ? 11.785 -8.876  36.475  1.00 25.63 ? 386 ARG A CG  1 
ATOM   3126 C CD  . ARG A 1 386 ? 10.522 -9.443  35.829  1.00 27.17 ? 386 ARG A CD  1 
ATOM   3127 N NE  . ARG A 1 386 ? 9.557  -8.410  35.424  1.00 28.94 ? 386 ARG A NE  1 
ATOM   3128 C CZ  . ARG A 1 386 ? 8.395  -8.135  36.014  1.00 29.46 ? 386 ARG A CZ  1 
ATOM   3129 N NH1 . ARG A 1 386 ? 8.047  -8.740  37.135  1.00 29.98 ? 386 ARG A NH1 1 
ATOM   3130 N NH2 . ARG A 1 386 ? 7.584  -7.233  35.490  1.00 29.69 ? 386 ARG A NH2 1 
ATOM   3131 N N   . VAL A 1 387 ? 15.586 -5.731  35.767  1.00 22.19 ? 387 VAL A N   1 
ATOM   3132 C CA  . VAL A 1 387 ? 16.263 -4.601  35.158  1.00 22.20 ? 387 VAL A CA  1 
ATOM   3133 C C   . VAL A 1 387 ? 17.704 -5.013  34.882  1.00 21.75 ? 387 VAL A C   1 
ATOM   3134 O O   . VAL A 1 387 ? 18.290 -5.793  35.631  1.00 20.58 ? 387 VAL A O   1 
ATOM   3135 C CB  . VAL A 1 387 ? 16.216 -3.308  36.000  1.00 22.44 ? 387 VAL A CB  1 
ATOM   3136 C CG1 . VAL A 1 387 ? 14.883 -2.584  35.864  1.00 22.63 ? 387 VAL A CG1 1 
ATOM   3137 C CG2 . VAL A 1 387 ? 16.545 -3.549  37.468  1.00 22.68 ? 387 VAL A CG2 1 
ATOM   3138 N N   . VAL A 1 388 ? 18.254 -4.496  33.779  1.00 21.70 ? 388 VAL A N   1 
ATOM   3139 C CA  . VAL A 1 388 ? 19.677 -4.605  33.520  1.00 21.19 ? 388 VAL A CA  1 
ATOM   3140 C C   . VAL A 1 388 ? 20.288 -3.231  33.772  1.00 20.78 ? 388 VAL A C   1 
ATOM   3141 O O   . VAL A 1 388 ? 19.895 -2.252  33.137  1.00 20.22 ? 388 VAL A O   1 
ATOM   3142 C CB  . VAL A 1 388 ? 19.970 -5.125  32.101  1.00 21.84 ? 388 VAL A CB  1 
ATOM   3143 C CG1 . VAL A 1 388 ? 21.449 -5.442  31.915  1.00 22.38 ? 388 VAL A CG1 1 
ATOM   3144 C CG2 . VAL A 1 388 ? 19.108 -6.340  31.766  1.00 21.81 ? 388 VAL A CG2 1 
ATOM   3145 N N   . VAL A 1 389 ? 21.224 -3.176  34.730  1.00 20.52 ? 389 VAL A N   1 
ATOM   3146 C CA  . VAL A 1 389 ? 21.873 -1.935  35.117  1.00 19.99 ? 389 VAL A CA  1 
ATOM   3147 C C   . VAL A 1 389 ? 23.196 -1.843  34.364  1.00 19.71 ? 389 VAL A C   1 
ATOM   3148 O O   . VAL A 1 389 ? 23.968 -2.802  34.328  1.00 20.40 ? 389 VAL A O   1 
ATOM   3149 C CB  . VAL A 1 389 ? 22.075 -1.781  36.641  1.00 19.95 ? 389 VAL A CB  1 
ATOM   3150 C CG1 . VAL A 1 389 ? 22.752 -2.992  37.276  1.00 19.99 ? 389 VAL A CG1 1 
ATOM   3151 C CG2 . VAL A 1 389 ? 22.829 -0.502  36.992  1.00 19.72 ? 389 VAL A CG2 1 
ATOM   3152 N N   . TYR A 1 390 ? 23.420 -0.680  33.747  1.00 18.98 ? 390 TYR A N   1 
ATOM   3153 C CA  . TYR A 1 390 ? 24.642 -0.388  33.021  1.00 18.81 ? 390 TYR A CA  1 
ATOM   3154 C C   . TYR A 1 390 ? 25.317 0.799   33.697  1.00 18.41 ? 390 TYR A C   1 
ATOM   3155 O O   . TYR A 1 390 ? 24.641 1.679   34.220  1.00 18.08 ? 390 TYR A O   1 
ATOM   3156 C CB  . TYR A 1 390 ? 24.335 -0.064  31.555  1.00 18.58 ? 390 TYR A CB  1 
ATOM   3157 C CG  . TYR A 1 390 ? 23.641 -1.165  30.761  1.00 18.46 ? 390 TYR A CG  1 
ATOM   3158 C CD1 . TYR A 1 390 ? 22.288 -1.426  30.938  1.00 18.00 ? 390 TYR A CD1 1 
ATOM   3159 C CD2 . TYR A 1 390 ? 24.323 -1.912  29.805  1.00 18.14 ? 390 TYR A CD2 1 
ATOM   3160 C CE1 . TYR A 1 390 ? 21.639 -2.412  30.216  1.00 17.72 ? 390 TYR A CE1 1 
ATOM   3161 C CE2 . TYR A 1 390 ? 23.685 -2.902  29.072  1.00 17.84 ? 390 TYR A CE2 1 
ATOM   3162 C CZ  . TYR A 1 390 ? 22.335 -3.146  29.274  1.00 17.91 ? 390 TYR A CZ  1 
ATOM   3163 O OH  . TYR A 1 390 ? 21.673 -4.111  28.570  1.00 17.33 ? 390 TYR A OH  1 
ATOM   3164 N N   . THR A 1 391 ? 26.653 0.806   33.693  1.00 18.57 ? 391 THR A N   1 
ATOM   3165 C CA  . THR A 1 391 ? 27.388 2.010   34.031  1.00 18.92 ? 391 THR A CA  1 
ATOM   3166 C C   . THR A 1 391 ? 27.122 3.036   32.933  1.00 19.54 ? 391 THR A C   1 
ATOM   3167 O O   . THR A 1 391 ? 26.698 4.151   33.215  1.00 19.19 ? 391 THR A O   1 
ATOM   3168 C CB  . THR A 1 391 ? 28.873 1.702   34.212  1.00 19.22 ? 391 THR A CB  1 
ATOM   3169 O OG1 . THR A 1 391 ? 29.254 0.926   33.080  1.00 19.58 ? 391 THR A OG1 1 
ATOM   3170 C CG2 . THR A 1 391 ? 29.143 0.955   35.505  1.00 18.82 ? 391 THR A CG2 1 
ATOM   3171 N N   . GLY A 1 392 ? 27.320 2.620   31.676  1.00 20.52 ? 392 GLY A N   1 
ATOM   3172 C CA  . GLY A 1 392 ? 26.979 3.447   30.531  1.00 20.44 ? 392 GLY A CA  1 
ATOM   3173 C C   . GLY A 1 392 ? 26.602 2.600   29.319  1.00 20.79 ? 392 GLY A C   1 
ATOM   3174 O O   . GLY A 1 392 ? 26.831 1.392   29.305  1.00 20.94 ? 392 GLY A O   1 
ATOM   3175 N N   . THR A 1 393 ? 26.017 3.256   28.309  1.00 20.52 ? 393 THR A N   1 
ATOM   3176 C CA  . THR A 1 393 ? 25.644 2.602   27.065  1.00 20.07 ? 393 THR A CA  1 
ATOM   3177 C C   . THR A 1 393 ? 26.724 2.872   26.023  1.00 19.19 ? 393 THR A C   1 
ATOM   3178 O O   . THR A 1 393 ? 27.676 3.610   26.276  1.00 18.80 ? 393 THR A O   1 
ATOM   3179 C CB  . THR A 1 393 ? 24.278 3.092   26.576  1.00 20.50 ? 393 THR A CB  1 
ATOM   3180 O OG1 . THR A 1 393 ? 24.474 4.384   26.008  1.00 21.01 ? 393 THR A OG1 1 
ATOM   3181 C CG2 . THR A 1 393 ? 23.236 3.123   27.679  1.00 20.71 ? 393 THR A CG2 1 
ATOM   3182 N N   . HIS A 1 394 ? 26.534 2.271   24.844  1.00 18.48 ? 394 HIS A N   1 
ATOM   3183 C CA  . HIS A 1 394 ? 27.426 2.448   23.709  1.00 18.15 ? 394 HIS A CA  1 
ATOM   3184 C C   . HIS A 1 394 ? 27.336 3.874   23.169  1.00 17.88 ? 394 HIS A C   1 
ATOM   3185 O O   . HIS A 1 394 ? 28.280 4.344   22.539  1.00 18.12 ? 394 HIS A O   1 
ATOM   3186 C CB  . HIS A 1 394 ? 27.100 1.426   22.613  1.00 18.14 ? 394 HIS A CB  1 
ATOM   3187 C CG  . HIS A 1 394 ? 25.724 1.580   22.053  1.00 17.90 ? 394 HIS A CG  1 
ATOM   3188 N ND1 . HIS A 1 394 ? 24.627 0.937   22.583  1.00 18.24 ? 394 HIS A ND1 1 
ATOM   3189 C CD2 . HIS A 1 394 ? 25.269 2.311   21.033  1.00 18.13 ? 394 HIS A CD2 1 
ATOM   3190 C CE1 . HIS A 1 394 ? 23.549 1.270   21.892  1.00 18.18 ? 394 HIS A CE1 1 
ATOM   3191 N NE2 . HIS A 1 394 ? 23.916 2.101   20.941  1.00 18.26 ? 394 HIS A NE2 1 
ATOM   3192 N N   . ASP A 1 395 ? 26.205 4.551   23.411  1.00 17.48 ? 395 ASP A N   1 
ATOM   3193 C CA  . ASP A 1 395 ? 26.022 5.928   22.980  1.00 17.98 ? 395 ASP A CA  1 
ATOM   3194 C C   . ASP A 1 395 ? 26.595 6.910   23.998  1.00 17.49 ? 395 ASP A C   1 
ATOM   3195 O O   . ASP A 1 395 ? 26.817 8.073   23.670  1.00 16.68 ? 395 ASP A O   1 
ATOM   3196 C CB  . ASP A 1 395 ? 24.560 6.246   22.713  1.00 18.66 ? 395 ASP A CB  1 
ATOM   3197 C CG  . ASP A 1 395 ? 23.969 5.536   21.506  1.00 18.99 ? 395 ASP A CG  1 
ATOM   3198 O OD1 . ASP A 1 395 ? 24.658 5.488   20.470  1.00 19.21 ? 395 ASP A OD1 1 
ATOM   3199 O OD2 . ASP A 1 395 ? 22.825 5.050   21.611  1.00 20.71 ? 395 ASP A OD2 1 
ATOM   3200 N N   . ASN A 1 396 ? 26.803 6.454   25.236  1.00 17.90 ? 396 ASN A N   1 
ATOM   3201 C CA  . ASN A 1 396 ? 27.393 7.305   26.257  1.00 18.30 ? 396 ASN A CA  1 
ATOM   3202 C C   . ASN A 1 396 ? 28.909 7.160   26.191  1.00 18.04 ? 396 ASN A C   1 
ATOM   3203 O O   . ASN A 1 396 ? 29.424 6.267   25.523  1.00 19.12 ? 396 ASN A O   1 
ATOM   3204 C CB  . ASN A 1 396 ? 26.875 6.987   27.656  1.00 18.30 ? 396 ASN A CB  1 
ATOM   3205 C CG  . ASN A 1 396 ? 25.384 6.764   27.682  1.00 18.74 ? 396 ASN A CG  1 
ATOM   3206 O OD1 . ASN A 1 396 ? 24.923 5.773   28.256  1.00 19.54 ? 396 ASN A OD1 1 
ATOM   3207 N ND2 . ASN A 1 396 ? 24.621 7.657   27.067  1.00 18.64 ? 396 ASN A ND2 1 
ATOM   3208 N N   . ASP A 1 397 ? 29.611 8.041   26.907  1.00 17.63 ? 397 ASP A N   1 
ATOM   3209 C CA  . ASP A 1 397 ? 31.062 7.984   26.995  1.00 17.03 ? 397 ASP A CA  1 
ATOM   3210 C C   . ASP A 1 397 ? 31.442 6.909   28.015  1.00 15.82 ? 397 ASP A C   1 
ATOM   3211 O O   . ASP A 1 397 ? 30.574 6.340   28.678  1.00 14.99 ? 397 ASP A O   1 
ATOM   3212 C CB  . ASP A 1 397 ? 31.615 9.367   27.313  1.00 17.46 ? 397 ASP A CB  1 
ATOM   3213 C CG  . ASP A 1 397 ? 33.125 9.540   27.218  1.00 17.92 ? 397 ASP A CG  1 
ATOM   3214 O OD1 . ASP A 1 397 ? 33.805 8.601   26.750  1.00 18.70 ? 397 ASP A OD1 1 
ATOM   3215 O OD2 . ASP A 1 397 ? 33.615 10.610  27.633  1.00 18.70 ? 397 ASP A OD2 1 
ATOM   3216 N N   . THR A 1 398 ? 32.745 6.624   28.135  1.00 15.04 ? 398 THR A N   1 
ATOM   3217 C CA  . THR A 1 398 ? 33.225 5.712   29.162  1.00 14.47 ? 398 THR A CA  1 
ATOM   3218 C C   . THR A 1 398 ? 33.015 6.389   30.511  1.00 14.38 ? 398 THR A C   1 
ATOM   3219 O O   . THR A 1 398 ? 32.961 7.614   30.583  1.00 14.45 ? 398 THR A O   1 
ATOM   3220 C CB  . THR A 1 398 ? 34.691 5.330   28.950  1.00 14.14 ? 398 THR A CB  1 
ATOM   3221 O OG1 . THR A 1 398 ? 35.455 6.487   29.269  1.00 13.79 ? 398 THR A OG1 1 
ATOM   3222 C CG2 . THR A 1 398 ? 34.984 4.848   27.540  1.00 14.08 ? 398 THR A CG2 1 
ATOM   3223 N N   . THR A 1 399 ? 32.897 5.588   31.574  1.00 14.35 ? 399 THR A N   1 
ATOM   3224 C CA  . THR A 1 399 ? 32.590 6.139   32.883  1.00 14.51 ? 399 THR A CA  1 
ATOM   3225 C C   . THR A 1 399 ? 33.689 7.120   33.287  1.00 14.59 ? 399 THR A C   1 
ATOM   3226 O O   . THR A 1 399 ? 33.386 8.165   33.854  1.00 14.64 ? 399 THR A O   1 
ATOM   3227 C CB  . THR A 1 399 ? 32.388 5.023   33.908  1.00 14.51 ? 399 THR A CB  1 
ATOM   3228 O OG1 . THR A 1 399 ? 31.279 4.244   33.470  1.00 14.76 ? 399 THR A OG1 1 
ATOM   3229 C CG2 . THR A 1 399 ? 32.036 5.548   35.287  1.00 14.75 ? 399 THR A CG2 1 
ATOM   3230 N N   . LEU A 1 400 ? 34.952 6.794   32.970  1.00 14.74 ? 400 LEU A N   1 
ATOM   3231 C CA  . LEU A 1 400 ? 36.080 7.657   33.303  1.00 15.23 ? 400 LEU A CA  1 
ATOM   3232 C C   . LEU A 1 400 ? 36.027 8.942   32.477  1.00 15.58 ? 400 LEU A C   1 
ATOM   3233 O O   . LEU A 1 400 ? 36.352 10.016  32.979  1.00 16.48 ? 400 LEU A O   1 
ATOM   3234 C CB  . LEU A 1 400 ? 37.412 6.932   33.104  1.00 15.05 ? 400 LEU A CB  1 
ATOM   3235 C CG  . LEU A 1 400 ? 38.681 7.742   33.395  1.00 15.20 ? 400 LEU A CG  1 
ATOM   3236 C CD1 . LEU A 1 400 ? 38.689 8.279   34.813  1.00 15.52 ? 400 LEU A CD1 1 
ATOM   3237 C CD2 . LEU A 1 400 ? 39.935 6.913   33.146  1.00 15.08 ? 400 LEU A CD2 1 
ATOM   3238 N N   . GLY A 1 401 ? 35.644 8.823   31.202  1.00 15.88 ? 401 GLY A N   1 
ATOM   3239 C CA  . GLY A 1 401 ? 35.473 9.985   30.346  1.00 16.13 ? 401 GLY A CA  1 
ATOM   3240 C C   . GLY A 1 401 ? 34.319 10.865  30.819  1.00 16.08 ? 401 GLY A C   1 
ATOM   3241 O O   . GLY A 1 401 ? 34.407 12.091  30.788  1.00 15.58 ? 401 GLY A O   1 
ATOM   3242 N N   . TRP A 1 402 ? 33.235 10.212  31.249  1.00 16.50 ? 402 TRP A N   1 
ATOM   3243 C CA  . TRP A 1 402 ? 32.077 10.891  31.804  1.00 17.12 ? 402 TRP A CA  1 
ATOM   3244 C C   . TRP A 1 402 ? 32.453 11.640  33.084  1.00 17.68 ? 402 TRP A C   1 
ATOM   3245 O O   . TRP A 1 402 ? 32.034 12.777  33.278  1.00 17.65 ? 402 TRP A O   1 
ATOM   3246 C CB  . TRP A 1 402 ? 30.955 9.871   32.036  1.00 17.11 ? 402 TRP A CB  1 
ATOM   3247 C CG  . TRP A 1 402 ? 29.835 10.349  32.919  1.00 17.52 ? 402 TRP A CG  1 
ATOM   3248 C CD1 . TRP A 1 402 ? 28.728 11.065  32.560  1.00 17.72 ? 402 TRP A CD1 1 
ATOM   3249 C CD2 . TRP A 1 402 ? 29.712 10.100  34.335  1.00 17.60 ? 402 TRP A CD2 1 
ATOM   3250 N NE1 . TRP A 1 402 ? 27.936 11.293  33.655  1.00 17.73 ? 402 TRP A NE1 1 
ATOM   3251 C CE2 . TRP A 1 402 ? 28.511 10.709  34.756  1.00 17.56 ? 402 TRP A CE2 1 
ATOM   3252 C CE3 . TRP A 1 402 ? 30.498 9.427   35.279  1.00 17.73 ? 402 TRP A CE3 1 
ATOM   3253 C CZ2 . TRP A 1 402 ? 28.087 10.665  36.081  1.00 17.66 ? 402 TRP A CZ2 1 
ATOM   3254 C CZ3 . TRP A 1 402 ? 30.076 9.388   36.589  1.00 17.71 ? 402 TRP A CZ3 1 
ATOM   3255 C CH2 . TRP A 1 402 ? 28.884 9.994   36.980  1.00 17.66 ? 402 TRP A CH2 1 
ATOM   3256 N N   . TYR A 1 403 ? 33.257 11.007  33.945  1.00 18.54 ? 403 TYR A N   1 
ATOM   3257 C CA  . TYR A 1 403 ? 33.625 11.595  35.224  1.00 19.72 ? 403 TYR A CA  1 
ATOM   3258 C C   . TYR A 1 403 ? 34.533 12.804  35.000  1.00 20.00 ? 403 TYR A C   1 
ATOM   3259 O O   . TYR A 1 403 ? 34.570 13.715  35.825  1.00 19.74 ? 403 TYR A O   1 
ATOM   3260 C CB  . TYR A 1 403 ? 34.287 10.570  36.153  1.00 20.37 ? 403 TYR A CB  1 
ATOM   3261 C CG  . TYR A 1 403 ? 34.578 11.131  37.539  1.00 21.05 ? 403 TYR A CG  1 
ATOM   3262 C CD1 . TYR A 1 403 ? 33.563 11.276  38.477  1.00 21.23 ? 403 TYR A CD1 1 
ATOM   3263 C CD2 . TYR A 1 403 ? 35.856 11.546  37.897  1.00 21.33 ? 403 TYR A CD2 1 
ATOM   3264 C CE1 . TYR A 1 403 ? 33.810 11.806  39.733  1.00 21.63 ? 403 TYR A CE1 1 
ATOM   3265 C CE2 . TYR A 1 403 ? 36.117 12.074  39.152  1.00 21.67 ? 403 TYR A CE2 1 
ATOM   3266 C CZ  . TYR A 1 403 ? 35.091 12.204  40.072  1.00 22.28 ? 403 TYR A CZ  1 
ATOM   3267 O OH  . TYR A 1 403 ? 35.326 12.724  41.315  1.00 23.08 ? 403 TYR A OH  1 
ATOM   3268 N N   . ARG A 1 404 ? 35.267 12.807  33.882  1.00 20.49 ? 404 ARG A N   1 
ATOM   3269 C CA  . ARG A 1 404 ? 36.169 13.901  33.560  1.00 20.33 ? 404 ARG A CA  1 
ATOM   3270 C C   . ARG A 1 404 ? 35.405 15.101  33.002  1.00 20.30 ? 404 ARG A C   1 
ATOM   3271 O O   . ARG A 1 404 ? 35.944 16.203  33.005  1.00 20.49 ? 404 ARG A O   1 
ATOM   3272 C CB  . ARG A 1 404 ? 37.242 13.444  32.568  1.00 20.60 ? 404 ARG A CB  1 
ATOM   3273 C CG  . ARG A 1 404 ? 38.294 12.559  33.218  1.00 21.01 ? 404 ARG A CG  1 
ATOM   3274 C CD  . ARG A 1 404 ? 39.166 11.844  32.209  1.00 21.42 ? 404 ARG A CD  1 
ATOM   3275 N NE  . ARG A 1 404 ? 40.249 11.122  32.888  1.00 21.93 ? 404 ARG A NE  1 
ATOM   3276 C CZ  . ARG A 1 404 ? 41.129 10.317  32.308  1.00 21.87 ? 404 ARG A CZ  1 
ATOM   3277 N NH1 . ARG A 1 404 ? 41.114 10.147  30.996  1.00 21.57 ? 404 ARG A NH1 1 
ATOM   3278 N NH2 . ARG A 1 404 ? 42.027 9.688   33.050  1.00 21.81 ? 404 ARG A NH2 1 
ATOM   3279 N N   . THR A 1 405 ? 34.175 14.880  32.512  1.00 20.01 ? 405 THR A N   1 
ATOM   3280 C CA  . THR A 1 405 ? 33.374 15.945  31.920  1.00 19.51 ? 405 THR A CA  1 
ATOM   3281 C C   . THR A 1 405 ? 32.137 16.253  32.766  1.00 19.08 ? 405 THR A C   1 
ATOM   3282 O O   . THR A 1 405 ? 31.406 17.192  32.456  1.00 18.95 ? 405 THR A O   1 
ATOM   3283 C CB  . THR A 1 405 ? 32.978 15.546  30.499  1.00 19.42 ? 405 THR A CB  1 
ATOM   3284 O OG1 . THR A 1 405 ? 32.290 14.307  30.618  1.00 19.74 ? 405 THR A OG1 1 
ATOM   3285 C CG2 . THR A 1 405 ? 34.174 15.386  29.577  1.00 19.48 ? 405 THR A CG2 1 
ATOM   3286 N N   . ALA A 1 406 ? 31.899 15.477  33.831  1.00 18.55 ? 406 ALA A N   1 
ATOM   3287 C CA  . ALA A 1 406 ? 30.670 15.595  34.601  1.00 18.44 ? 406 ALA A CA  1 
ATOM   3288 C C   . ALA A 1 406 ? 30.693 16.862  35.454  1.00 18.19 ? 406 ALA A C   1 
ATOM   3289 O O   . ALA A 1 406 ? 31.753 17.429  35.714  1.00 17.03 ? 406 ALA A O   1 
ATOM   3290 C CB  . ALA A 1 406 ? 30.466 14.364  35.458  1.00 18.52 ? 406 ALA A CB  1 
ATOM   3291 N N   . THR A 1 407 ? 29.499 17.275  35.898  1.00 18.52 ? 407 THR A N   1 
ATOM   3292 C CA  . THR A 1 407 ? 29.317 18.517  36.632  1.00 18.79 ? 407 THR A CA  1 
ATOM   3293 C C   . THR A 1 407 ? 29.834 18.324  38.055  1.00 19.28 ? 407 THR A C   1 
ATOM   3294 O O   . THR A 1 407 ? 29.886 17.200  38.545  1.00 18.77 ? 407 THR A O   1 
ATOM   3295 C CB  . THR A 1 407 ? 27.843 18.930  36.642  1.00 18.87 ? 407 THR A CB  1 
ATOM   3296 O OG1 . THR A 1 407 ? 27.171 18.002  37.487  1.00 18.90 ? 407 THR A OG1 1 
ATOM   3297 C CG2 . THR A 1 407 ? 27.199 18.922  35.266  1.00 19.03 ? 407 THR A CG2 1 
ATOM   3298 N N   . PRO A 1 408 ? 30.216 19.408  38.770  1.00 20.18 ? 408 PRO A N   1 
ATOM   3299 C CA  . PRO A 1 408 ? 30.563 19.308  40.184  1.00 20.37 ? 408 PRO A CA  1 
ATOM   3300 C C   . PRO A 1 408 ? 29.453 18.707  41.042  1.00 20.89 ? 408 PRO A C   1 
ATOM   3301 O O   . PRO A 1 408 ? 29.735 17.933  41.954  1.00 20.68 ? 408 PRO A O   1 
ATOM   3302 C CB  . PRO A 1 408 ? 30.883 20.747  40.579  1.00 20.40 ? 408 PRO A CB  1 
ATOM   3303 C CG  . PRO A 1 408 ? 31.244 21.408  39.263  1.00 20.04 ? 408 PRO A CG  1 
ATOM   3304 C CD  . PRO A 1 408 ? 30.348 20.778  38.253  1.00 19.98 ? 408 PRO A CD  1 
ATOM   3305 N N   . HIS A 1 409 ? 28.196 19.068  40.744  1.00 21.35 ? 409 HIS A N   1 
ATOM   3306 C CA  . HIS A 1 409 ? 27.052 18.469  41.415  1.00 22.01 ? 409 HIS A CA  1 
ATOM   3307 C C   . HIS A 1 409 ? 27.078 16.955  41.232  1.00 21.48 ? 409 HIS A C   1 
ATOM   3308 O O   . HIS A 1 409 ? 27.044 16.216  42.213  1.00 21.21 ? 409 HIS A O   1 
ATOM   3309 C CB  . HIS A 1 409 ? 25.721 19.025  40.892  1.00 22.67 ? 409 HIS A CB  1 
ATOM   3310 C CG  . HIS A 1 409 ? 24.533 18.227  41.335  1.00 23.26 ? 409 HIS A CG  1 
ATOM   3311 N ND1 . HIS A 1 409 ? 23.869 18.445  42.524  1.00 24.56 ? 409 HIS A ND1 1 
ATOM   3312 C CD2 . HIS A 1 409 ? 23.908 17.200  40.749  1.00 23.67 ? 409 HIS A CD2 1 
ATOM   3313 C CE1 . HIS A 1 409 ? 22.873 17.575  42.637  1.00 24.30 ? 409 HIS A CE1 1 
ATOM   3314 N NE2 . HIS A 1 409 ? 22.878 16.810  41.570  1.00 24.10 ? 409 HIS A NE2 1 
ATOM   3315 N N   . GLU A 1 410 ? 27.112 16.513  39.967  1.00 20.93 ? 410 GLU A N   1 
ATOM   3316 C CA  . GLU A 1 410 ? 27.102 15.097  39.634  1.00 20.43 ? 410 GLU A CA  1 
ATOM   3317 C C   . GLU A 1 410 ? 28.197 14.361  40.403  1.00 19.63 ? 410 GLU A C   1 
ATOM   3318 O O   . GLU A 1 410 ? 27.940 13.316  40.992  1.00 18.88 ? 410 GLU A O   1 
ATOM   3319 C CB  . GLU A 1 410 ? 27.275 14.861  38.131  1.00 20.89 ? 410 GLU A CB  1 
ATOM   3320 C CG  . GLU A 1 410 ? 25.973 14.969  37.341  1.00 21.14 ? 410 GLU A CG  1 
ATOM   3321 C CD  . GLU A 1 410 ? 26.124 14.677  35.858  1.00 21.96 ? 410 GLU A CD  1 
ATOM   3322 O OE1 . GLU A 1 410 ? 25.578 13.657  35.380  1.00 21.85 ? 410 GLU A OE1 1 
ATOM   3323 O OE2 . GLU A 1 410 ? 26.792 15.482  35.177  1.00 22.68 ? 410 GLU A OE2 1 
ATOM   3324 N N   . LYS A 1 411 ? 29.412 14.920  40.390  1.00 19.86 ? 411 LYS A N   1 
ATOM   3325 C CA  . LYS A 1 411 ? 30.571 14.273  40.987  1.00 20.13 ? 411 LYS A CA  1 
ATOM   3326 C C   . LYS A 1 411 ? 30.406 14.161  42.501  1.00 19.97 ? 411 LYS A C   1 
ATOM   3327 O O   . LYS A 1 411 ? 30.751 13.136  43.083  1.00 19.56 ? 411 LYS A O   1 
ATOM   3328 C CB  . LYS A 1 411 ? 31.849 15.044  40.636  1.00 20.63 ? 411 LYS A CB  1 
ATOM   3329 C CG  . LYS A 1 411 ? 32.212 15.022  39.155  1.00 21.04 ? 411 LYS A CG  1 
ATOM   3330 C CD  . LYS A 1 411 ? 33.485 15.780  38.804  1.00 21.53 ? 411 LYS A CD  1 
ATOM   3331 C CE  . LYS A 1 411 ? 33.340 17.258  38.991  1.00 21.55 ? 411 LYS A CE  1 
ATOM   3332 N NZ  . LYS A 1 411 ? 34.496 17.994  38.478  1.00 21.51 ? 411 LYS A NZ  1 
ATOM   3333 N N   . ALA A 1 412 ? 29.898 15.226  43.132  1.00 21.06 ? 412 ALA A N   1 
ATOM   3334 C CA  . ALA A 1 412 ? 29.751 15.266  44.580  1.00 22.02 ? 412 ALA A CA  1 
ATOM   3335 C C   . ALA A 1 412 ? 28.594 14.369  45.016  1.00 22.14 ? 412 ALA A C   1 
ATOM   3336 O O   . ALA A 1 412 ? 28.724 13.607  45.970  1.00 23.68 ? 412 ALA A O   1 
ATOM   3337 C CB  . ALA A 1 412 ? 29.561 16.694  45.044  1.00 22.17 ? 412 ALA A CB  1 
ATOM   3338 N N   . PHE A 1 413 ? 27.468 14.456  44.301  1.00 22.00 ? 413 PHE A N   1 
ATOM   3339 C CA  . PHE A 1 413 ? 26.297 13.652  44.616  1.00 22.00 ? 413 PHE A CA  1 
ATOM   3340 C C   . PHE A 1 413 ? 26.626 12.166  44.479  1.00 22.28 ? 413 PHE A C   1 
ATOM   3341 O O   . PHE A 1 413 ? 26.172 11.360  45.289  1.00 22.12 ? 413 PHE A O   1 
ATOM   3342 C CB  . PHE A 1 413 ? 25.119 14.063  43.727  1.00 21.73 ? 413 PHE A CB  1 
ATOM   3343 C CG  . PHE A 1 413 ? 23.821 13.303  43.976  1.00 21.97 ? 413 PHE A CG  1 
ATOM   3344 C CD1 . PHE A 1 413 ? 23.482 12.840  45.246  1.00 22.59 ? 413 PHE A CD1 1 
ATOM   3345 C CD2 . PHE A 1 413 ? 22.933 13.061  42.933  1.00 22.34 ? 413 PHE A CD2 1 
ATOM   3346 C CE1 . PHE A 1 413 ? 22.296 12.150  45.456  1.00 22.76 ? 413 PHE A CE1 1 
ATOM   3347 C CE2 . PHE A 1 413 ? 21.746 12.376  43.150  1.00 22.54 ? 413 PHE A CE2 1 
ATOM   3348 C CZ  . PHE A 1 413 ? 21.431 11.920  44.409  1.00 22.62 ? 413 PHE A CZ  1 
ATOM   3349 N N   . MET A 1 414 ? 27.410 11.815  43.450  1.00 22.27 ? 414 MET A N   1 
ATOM   3350 C CA  . MET A 1 414 ? 27.836 10.440  43.229  1.00 22.29 ? 414 MET A CA  1 
ATOM   3351 C C   . MET A 1 414 ? 28.644 9.939   44.424  1.00 22.26 ? 414 MET A C   1 
ATOM   3352 O O   . MET A 1 414 ? 28.282 8.940   45.041  1.00 22.94 ? 414 MET A O   1 
ATOM   3353 C CB  . MET A 1 414 ? 28.681 10.326  41.956  1.00 22.47 ? 414 MET A CB  1 
ATOM   3354 C CG  . MET A 1 414 ? 29.089 8.908   41.604  1.00 22.50 ? 414 MET A CG  1 
ATOM   3355 S SD  . MET A 1 414 ? 30.339 8.846   40.308  1.00 22.67 ? 414 MET A SD  1 
ATOM   3356 C CE  . MET A 1 414 ? 31.747 9.487   41.225  1.00 23.18 ? 414 MET A CE  1 
ATOM   3357 N N   . ALA A 1 415 ? 29.736 10.643  44.744  1.00 21.96 ? 415 ALA A N   1 
ATOM   3358 C CA  . ALA A 1 415 ? 30.655 10.229  45.795  1.00 21.43 ? 415 ALA A CA  1 
ATOM   3359 C C   . ALA A 1 415 ? 29.902 9.977   47.102  1.00 21.30 ? 415 ALA A C   1 
ATOM   3360 O O   . ALA A 1 415 ? 30.129 8.971   47.775  1.00 20.48 ? 415 ALA A O   1 
ATOM   3361 C CB  . ALA A 1 415 ? 31.729 11.284  45.971  1.00 20.72 ? 415 ALA A CB  1 
ATOM   3362 N N   . ARG A 1 416 ? 29.003 10.909  47.437  1.00 21.26 ? 416 ARG A N   1 
ATOM   3363 C CA  . ARG A 1 416 ? 28.167 10.838  48.626  1.00 21.74 ? 416 ARG A CA  1 
ATOM   3364 C C   . ARG A 1 416 ? 27.279 9.594   48.595  1.00 20.51 ? 416 ARG A C   1 
ATOM   3365 O O   . ARG A 1 416 ? 27.150 8.892   49.599  1.00 19.98 ? 416 ARG A O   1 
ATOM   3366 C CB  . ARG A 1 416 ? 27.359 12.140  48.610  1.00 23.27 ? 416 ARG A CB  1 
ATOM   3367 C CG  . ARG A 1 416 ? 26.350 12.409  49.716  1.00 24.74 ? 416 ARG A CG  1 
ATOM   3368 C CD  . ARG A 1 416 ? 25.240 13.335  49.204  1.00 26.07 ? 416 ARG A CD  1 
ATOM   3369 N NE  . ARG A 1 416 ? 25.709 14.416  48.326  1.00 27.08 ? 416 ARG A NE  1 
ATOM   3370 C CZ  . ARG A 1 416 ? 24.939 15.233  47.604  1.00 28.52 ? 416 ARG A CZ  1 
ATOM   3371 N NH1 . ARG A 1 416 ? 25.492 16.094  46.765  1.00 28.49 ? 416 ARG A NH1 1 
ATOM   3372 N NH2 . ARG A 1 416 ? 23.620 15.179  47.702  1.00 29.46 ? 416 ARG A NH2 1 
ATOM   3373 N N   . TYR A 1 417 ? 26.655 9.341   47.438  1.00 19.44 ? 417 TYR A N   1 
ATOM   3374 C CA  . TYR A 1 417 ? 25.700 8.252   47.287  1.00 18.41 ? 417 TYR A CA  1 
ATOM   3375 C C   . TYR A 1 417 ? 26.424 6.918   47.428  1.00 18.21 ? 417 TYR A C   1 
ATOM   3376 O O   . TYR A 1 417 ? 25.963 6.034   48.147  1.00 18.08 ? 417 TYR A O   1 
ATOM   3377 C CB  . TYR A 1 417 ? 24.992 8.345   45.931  1.00 18.04 ? 417 TYR A CB  1 
ATOM   3378 C CG  . TYR A 1 417 ? 23.780 7.439   45.764  1.00 18.09 ? 417 TYR A CG  1 
ATOM   3379 C CD1 . TYR A 1 417 ? 23.914 6.133   45.308  1.00 18.06 ? 417 TYR A CD1 1 
ATOM   3380 C CD2 . TYR A 1 417 ? 22.495 7.903   46.024  1.00 18.32 ? 417 TYR A CD2 1 
ATOM   3381 C CE1 . TYR A 1 417 ? 22.812 5.310   45.145  1.00 18.26 ? 417 TYR A CE1 1 
ATOM   3382 C CE2 . TYR A 1 417 ? 21.386 7.090   45.861  1.00 18.68 ? 417 TYR A CE2 1 
ATOM   3383 C CZ  . TYR A 1 417 ? 21.542 5.792   45.410  1.00 18.48 ? 417 TYR A CZ  1 
ATOM   3384 O OH  . TYR A 1 417 ? 20.451 4.986   45.238  1.00 18.92 ? 417 TYR A OH  1 
ATOM   3385 N N   . LEU A 1 418 ? 27.553 6.788   46.721  1.00 18.19 ? 418 LEU A N   1 
ATOM   3386 C CA  . LEU A 1 418 ? 28.412 5.620   46.839  1.00 18.16 ? 418 LEU A CA  1 
ATOM   3387 C C   . LEU A 1 418 ? 28.771 5.393   48.307  1.00 17.78 ? 418 LEU A C   1 
ATOM   3388 O O   . LEU A 1 418 ? 28.676 4.274   48.799  1.00 17.30 ? 418 LEU A O   1 
ATOM   3389 C CB  . LEU A 1 418 ? 29.657 5.814   45.973  1.00 18.39 ? 418 LEU A CB  1 
ATOM   3390 C CG  . LEU A 1 418 ? 29.442 5.802   44.456  1.00 18.60 ? 418 LEU A CG  1 
ATOM   3391 C CD1 . LEU A 1 418 ? 30.714 6.206   43.733  1.00 18.77 ? 418 LEU A CD1 1 
ATOM   3392 C CD2 . LEU A 1 418 ? 28.973 4.444   43.961  1.00 18.75 ? 418 LEU A CD2 1 
ATOM   3393 N N   . ALA A 1 419 ? 29.171 6.471   48.994  1.00 17.72 ? 419 ALA A N   1 
ATOM   3394 C CA  . ALA A 1 419 ? 29.611 6.410   50.379  1.00 17.85 ? 419 ALA A CA  1 
ATOM   3395 C C   . ALA A 1 419 ? 28.508 5.837   51.267  1.00 17.81 ? 419 ALA A C   1 
ATOM   3396 O O   . ALA A 1 419 ? 28.787 5.042   52.161  1.00 17.55 ? 419 ALA A O   1 
ATOM   3397 C CB  . ALA A 1 419 ? 30.032 7.787   50.843  1.00 17.77 ? 419 ALA A CB  1 
ATOM   3398 N N   . ASP A 1 420 ? 27.262 6.252   51.001  1.00 17.95 ? 420 ASP A N   1 
ATOM   3399 C CA  . ASP A 1 420 ? 26.096 5.758   51.714  1.00 17.88 ? 420 ASP A CA  1 
ATOM   3400 C C   . ASP A 1 420 ? 25.909 4.265   51.449  1.00 17.26 ? 420 ASP A C   1 
ATOM   3401 O O   . ASP A 1 420 ? 25.479 3.532   52.336  1.00 18.01 ? 420 ASP A O   1 
ATOM   3402 C CB  . ASP A 1 420 ? 24.851 6.559   51.353  1.00 18.36 ? 420 ASP A CB  1 
ATOM   3403 C CG  . ASP A 1 420 ? 24.894 8.035   51.729  1.00 19.13 ? 420 ASP A CG  1 
ATOM   3404 O OD1 . ASP A 1 420 ? 25.937 8.478   52.251  1.00 19.25 ? 420 ASP A OD1 1 
ATOM   3405 O OD2 . ASP A 1 420 ? 23.888 8.738   51.492  1.00 19.74 ? 420 ASP A OD2 1 
ATOM   3406 N N   . TRP A 1 421 ? 26.226 3.825   50.225  1.00 16.38 ? 421 TRP A N   1 
ATOM   3407 C CA  . TRP A 1 421 ? 26.112 2.424   49.850  1.00 16.23 ? 421 TRP A CA  1 
ATOM   3408 C C   . TRP A 1 421 ? 27.374 1.642   50.214  1.00 16.47 ? 421 TRP A C   1 
ATOM   3409 O O   . TRP A 1 421 ? 27.473 0.457   49.900  1.00 15.93 ? 421 TRP A O   1 
ATOM   3410 C CB  . TRP A 1 421 ? 25.785 2.299   48.354  1.00 15.73 ? 421 TRP A CB  1 
ATOM   3411 C CG  . TRP A 1 421 ? 24.313 2.444   48.066  1.00 15.10 ? 421 TRP A CG  1 
ATOM   3412 C CD1 . TRP A 1 421 ? 23.573 3.587   48.129  1.00 15.00 ? 421 TRP A CD1 1 
ATOM   3413 C CD2 . TRP A 1 421 ? 23.398 1.396   47.678  1.00 14.50 ? 421 TRP A CD2 1 
ATOM   3414 N NE1 . TRP A 1 421 ? 22.264 3.325   47.818  1.00 14.77 ? 421 TRP A NE1 1 
ATOM   3415 C CE2 . TRP A 1 421 ? 22.126 1.992   47.535  1.00 14.58 ? 421 TRP A CE2 1 
ATOM   3416 C CE3 . TRP A 1 421 ? 23.528 0.023   47.444  1.00 14.31 ? 421 TRP A CE3 1 
ATOM   3417 C CZ2 . TRP A 1 421 ? 20.998 1.260   47.164  1.00 14.57 ? 421 TRP A CZ2 1 
ATOM   3418 C CZ3 . TRP A 1 421 ? 22.414 -0.700  47.076  1.00 14.64 ? 421 TRP A CZ3 1 
ATOM   3419 C CH2 . TRP A 1 421 ? 21.165 -0.088  46.940  1.00 14.51 ? 421 TRP A CH2 1 
ATOM   3420 N N   . GLY A 1 422 ? 28.334 2.311   50.866  1.00 17.07 ? 422 GLY A N   1 
ATOM   3421 C CA  . GLY A 1 422 ? 29.527 1.660   51.385  1.00 17.73 ? 422 GLY A CA  1 
ATOM   3422 C C   . GLY A 1 422 ? 30.648 1.575   50.353  1.00 17.98 ? 422 GLY A C   1 
ATOM   3423 O O   . GLY A 1 422 ? 31.571 0.781   50.525  1.00 17.94 ? 422 GLY A O   1 
ATOM   3424 N N   . ILE A 1 423 ? 30.580 2.405   49.303  1.00 18.56 ? 423 ILE A N   1 
ATOM   3425 C CA  . ILE A 1 423 ? 31.548 2.357   48.218  1.00 19.73 ? 423 ILE A CA  1 
ATOM   3426 C C   . ILE A 1 423 ? 32.357 3.654   48.192  1.00 21.32 ? 423 ILE A C   1 
ATOM   3427 O O   . ILE A 1 423 ? 31.789 4.731   48.019  1.00 22.63 ? 423 ILE A O   1 
ATOM   3428 C CB  . ILE A 1 423 ? 30.843 2.087   46.876  1.00 19.00 ? 423 ILE A CB  1 
ATOM   3429 C CG1 . ILE A 1 423 ? 29.891 0.893   46.983  1.00 18.67 ? 423 ILE A CG1 1 
ATOM   3430 C CG2 . ILE A 1 423 ? 31.864 1.901   45.750  1.00 18.75 ? 423 ILE A CG2 1 
ATOM   3431 C CD1 . ILE A 1 423 ? 28.921 0.760   45.826  1.00 18.63 ? 423 ILE A CD1 1 
ATOM   3432 N N   . PHE A 1 424 ? 33.687 3.532   48.335  1.00 22.36 ? 424 PHE A N   1 
ATOM   3433 C CA  . PHE A 1 424 ? 34.593 4.674   48.361  1.00 23.73 ? 424 PHE A CA  1 
ATOM   3434 C C   . PHE A 1 424 ? 35.653 4.522   47.270  1.00 24.21 ? 424 PHE A C   1 
ATOM   3435 O O   . PHE A 1 424 ? 35.995 3.405   46.888  1.00 23.76 ? 424 PHE A O   1 
ATOM   3436 C CB  . PHE A 1 424 ? 35.271 4.810   49.730  1.00 24.21 ? 424 PHE A CB  1 
ATOM   3437 C CG  . PHE A 1 424 ? 34.317 4.800   50.916  1.00 24.60 ? 424 PHE A CG  1 
ATOM   3438 C CD1 . PHE A 1 424 ? 33.709 5.971   51.357  1.00 25.29 ? 424 PHE A CD1 1 
ATOM   3439 C CD2 . PHE A 1 424 ? 34.021 3.615   51.582  1.00 25.21 ? 424 PHE A CD2 1 
ATOM   3440 C CE1 . PHE A 1 424 ? 32.835 5.953   52.434  1.00 24.88 ? 424 PHE A CE1 1 
ATOM   3441 C CE2 . PHE A 1 424 ? 33.146 3.604   52.657  1.00 24.64 ? 424 PHE A CE2 1 
ATOM   3442 C CZ  . PHE A 1 424 ? 32.556 4.771   53.079  1.00 24.74 ? 424 PHE A CZ  1 
ATOM   3443 N N   . PHE A 1 425 ? 36.165 5.665   46.787  1.00 25.55 ? 425 PHE A N   1 
ATOM   3444 C CA  . PHE A 1 425 ? 37.204 5.707   45.769  1.00 25.85 ? 425 PHE A CA  1 
ATOM   3445 C C   . PHE A 1 425 ? 38.164 6.862   46.059  1.00 27.57 ? 425 PHE A C   1 
ATOM   3446 O O   . PHE A 1 425 ? 37.744 7.928   46.505  1.00 26.98 ? 425 PHE A O   1 
ATOM   3447 C CB  . PHE A 1 425 ? 36.601 5.862   44.367  1.00 25.16 ? 425 PHE A CB  1 
ATOM   3448 C CG  . PHE A 1 425 ? 35.860 7.170   44.117  1.00 24.58 ? 425 PHE A CG  1 
ATOM   3449 C CD1 . PHE A 1 425 ? 36.537 8.301   43.670  1.00 24.16 ? 425 PHE A CD1 1 
ATOM   3450 C CD2 . PHE A 1 425 ? 34.485 7.262   44.313  1.00 24.83 ? 425 PHE A CD2 1 
ATOM   3451 C CE1 . PHE A 1 425 ? 35.861 9.488   43.437  1.00 23.73 ? 425 PHE A CE1 1 
ATOM   3452 C CE2 . PHE A 1 425 ? 33.814 8.454   44.078  1.00 24.76 ? 425 PHE A CE2 1 
ATOM   3453 C CZ  . PHE A 1 425 ? 34.504 9.564   43.644  1.00 24.46 ? 425 PHE A CZ  1 
ATOM   3454 N N   . ARG A 1 426 ? 39.455 6.635   45.780  1.00 29.63 ? 426 ARG A N   1 
ATOM   3455 C CA  . ARG A 1 426 ? 40.492 7.635   45.982  1.00 32.08 ? 426 ARG A CA  1 
ATOM   3456 C C   . ARG A 1 426 ? 40.994 8.190   44.650  1.00 33.61 ? 426 ARG A C   1 
ATOM   3457 O O   . ARG A 1 426 ? 41.759 9.152   44.647  1.00 35.77 ? 426 ARG A O   1 
ATOM   3458 C CB  . ARG A 1 426 ? 41.709 7.044   46.700  1.00 33.34 ? 426 ARG A CB  1 
ATOM   3459 C CG  . ARG A 1 426 ? 41.395 6.276   47.974  1.00 35.16 ? 426 ARG A CG  1 
ATOM   3460 C CD  . ARG A 1 426 ? 42.641 5.586   48.487  1.00 35.83 ? 426 ARG A CD  1 
ATOM   3461 N NE  . ARG A 1 426 ? 42.385 4.808   49.703  1.00 36.56 ? 426 ARG A NE  1 
ATOM   3462 C CZ  . ARG A 1 426 ? 43.319 4.205   50.425  1.00 37.66 ? 426 ARG A CZ  1 
ATOM   3463 N NH1 . ARG A 1 426 ? 44.598 4.392   50.149  1.00 37.11 ? 426 ARG A NH1 1 
ATOM   3464 N NH2 . ARG A 1 426 ? 42.968 3.421   51.429  1.00 38.67 ? 426 ARG A NH2 1 
ATOM   3465 N N   . GLU A 1 427 ? 40.592 7.581   43.525  1.00 33.26 ? 427 GLU A N   1 
ATOM   3466 C CA  . GLU A 1 427 ? 41.089 8.006   42.225  1.00 33.08 ? 427 GLU A CA  1 
ATOM   3467 C C   . GLU A 1 427 ? 39.972 8.010   41.191  1.00 31.36 ? 427 GLU A C   1 
ATOM   3468 O O   . GLU A 1 427 ? 38.937 7.377   41.383  1.00 32.06 ? 427 GLU A O   1 
ATOM   3469 C CB  . GLU A 1 427 ? 42.246 7.146   41.717  1.00 33.70 ? 427 GLU A CB  1 
ATOM   3470 C CG  . GLU A 1 427 ? 43.595 7.841   41.864  1.00 34.98 ? 427 GLU A CG  1 
ATOM   3471 C CD  . GLU A 1 427 ? 43.567 9.270   41.344  1.00 36.22 ? 427 GLU A CD  1 
ATOM   3472 O OE1 . GLU A 1 427 ? 43.398 9.467   40.122  1.00 35.84 ? 427 GLU A OE1 1 
ATOM   3473 O OE2 . GLU A 1 427 ? 43.674 10.195  42.175  1.00 37.89 ? 427 GLU A OE2 1 
ATOM   3474 N N   . GLU A 1 428 ? 40.211 8.735   40.094  1.00 29.71 ? 428 GLU A N   1 
ATOM   3475 C CA  . GLU A 1 428 ? 39.223 8.846   39.035  1.00 29.00 ? 428 GLU A CA  1 
ATOM   3476 C C   . GLU A 1 428 ? 39.186 7.547   38.231  1.00 27.57 ? 428 GLU A C   1 
ATOM   3477 O O   . GLU A 1 428 ? 38.139 7.192   37.701  1.00 27.16 ? 428 GLU A O   1 
ATOM   3478 C CB  . GLU A 1 428 ? 39.384 10.097  38.172  1.00 29.26 ? 428 GLU A CB  1 
ATOM   3479 C CG  . GLU A 1 428 ? 40.709 10.250  37.434  1.00 29.53 ? 428 GLU A CG  1 
ATOM   3480 C CD  . GLU A 1 428 ? 40.622 11.488  36.557  1.00 29.37 ? 428 GLU A CD  1 
ATOM   3481 O OE1 . GLU A 1 428 ? 40.672 11.348  35.323  1.00 29.45 ? 428 GLU A OE1 1 
ATOM   3482 O OE2 . GLU A 1 428 ? 40.468 12.600  37.109  1.00 30.01 ? 428 GLU A OE2 1 
ATOM   3483 N N   . GLU A 1 429 ? 40.310 6.821   38.187  1.00 27.15 ? 429 GLU A N   1 
ATOM   3484 C CA  . GLU A 1 429 ? 40.354 5.532   37.514  1.00 26.85 ? 429 GLU A CA  1 
ATOM   3485 C C   . GLU A 1 429 ? 39.597 4.486   38.332  1.00 25.59 ? 429 GLU A C   1 
ATOM   3486 O O   . GLU A 1 429 ? 39.185 3.464   37.784  1.00 26.20 ? 429 GLU A O   1 
ATOM   3487 C CB  . GLU A 1 429 ? 41.779 5.046   37.244  1.00 27.27 ? 429 GLU A CB  1 
ATOM   3488 C CG  . GLU A 1 429 ? 42.582 5.973   36.335  1.00 27.51 ? 429 GLU A CG  1 
ATOM   3489 C CD  . GLU A 1 429 ? 43.281 7.123   37.040  1.00 27.89 ? 429 GLU A CD  1 
ATOM   3490 O OE1 . GLU A 1 429 ? 43.335 7.119   38.291  1.00 27.50 ? 429 GLU A OE1 1 
ATOM   3491 O OE2 . GLU A 1 429 ? 43.758 8.032   36.330  1.00 27.57 ? 429 GLU A OE2 1 
ATOM   3492 N N   . GLU A 1 430 ? 39.434 4.741   39.638  1.00 24.46 ? 430 GLU A N   1 
ATOM   3493 C CA  . GLU A 1 430 ? 38.667 3.874   40.520  1.00 23.89 ? 430 GLU A CA  1 
ATOM   3494 C C   . GLU A 1 430 ? 37.162 4.099   40.344  1.00 22.31 ? 430 GLU A C   1 
ATOM   3495 O O   . GLU A 1 430 ? 36.374 3.232   40.713  1.00 22.52 ? 430 GLU A O   1 
ATOM   3496 C CB  . GLU A 1 430 ? 39.049 4.111   41.984  1.00 24.79 ? 430 GLU A CB  1 
ATOM   3497 C CG  . GLU A 1 430 ? 40.484 3.715   42.322  1.00 25.95 ? 430 GLU A CG  1 
ATOM   3498 C CD  . GLU A 1 430 ? 40.922 4.039   43.743  1.00 27.13 ? 430 GLU A CD  1 
ATOM   3499 O OE1 . GLU A 1 430 ? 40.223 3.633   44.692  1.00 28.23 ? 430 GLU A OE1 1 
ATOM   3500 O OE2 . GLU A 1 430 ? 41.975 4.687   43.907  1.00 27.41 ? 430 GLU A OE2 1 
ATOM   3501 N N   . VAL A 1 431 ? 36.768 5.261   39.802  1.00 20.55 ? 431 VAL A N   1 
ATOM   3502 C CA  . VAL A 1 431 ? 35.364 5.647   39.714  1.00 19.35 ? 431 VAL A CA  1 
ATOM   3503 C C   . VAL A 1 431 ? 34.569 4.602   38.929  1.00 18.22 ? 431 VAL A C   1 
ATOM   3504 O O   . VAL A 1 431 ? 33.507 4.194   39.386  1.00 17.51 ? 431 VAL A O   1 
ATOM   3505 C CB  . VAL A 1 431 ? 35.171 7.061   39.128  1.00 19.27 ? 431 VAL A CB  1 
ATOM   3506 C CG1 . VAL A 1 431 ? 33.713 7.369   38.799  1.00 18.90 ? 431 VAL A CG1 1 
ATOM   3507 C CG2 . VAL A 1 431 ? 35.725 8.128   40.062  1.00 19.35 ? 431 VAL A CG2 1 
ATOM   3508 N N   . PRO A 1 432 ? 35.013 4.147   37.729  1.00 17.42 ? 432 PRO A N   1 
ATOM   3509 C CA  . PRO A 1 432 ? 34.287 3.099   37.016  1.00 16.80 ? 432 PRO A CA  1 
ATOM   3510 C C   . PRO A 1 432 ? 34.070 1.833   37.842  1.00 16.48 ? 432 PRO A C   1 
ATOM   3511 O O   . PRO A 1 432 ? 32.999 1.234   37.785  1.00 15.96 ? 432 PRO A O   1 
ATOM   3512 C CB  . PRO A 1 432 ? 35.122 2.832   35.764  1.00 17.16 ? 432 PRO A CB  1 
ATOM   3513 C CG  . PRO A 1 432 ? 36.440 3.563   35.978  1.00 17.29 ? 432 PRO A CG  1 
ATOM   3514 C CD  . PRO A 1 432 ? 36.182 4.648   36.986  1.00 17.34 ? 432 PRO A CD  1 
ATOM   3515 N N   . TRP A 1 433 ? 35.089 1.426   38.607  1.00 16.41 ? 433 TRP A N   1 
ATOM   3516 C CA  . TRP A 1 433 ? 34.985 0.230   39.430  1.00 16.89 ? 433 TRP A CA  1 
ATOM   3517 C C   . TRP A 1 433 ? 33.969 0.425   40.556  1.00 16.17 ? 433 TRP A C   1 
ATOM   3518 O O   . TRP A 1 433 ? 33.178 -0.475  40.824  1.00 16.18 ? 433 TRP A O   1 
ATOM   3519 C CB  . TRP A 1 433 ? 36.362 -0.201  39.954  1.00 17.37 ? 433 TRP A CB  1 
ATOM   3520 C CG  . TRP A 1 433 ? 37.169 -0.937  38.916  1.00 18.47 ? 433 TRP A CG  1 
ATOM   3521 C CD1 . TRP A 1 433 ? 38.054 -0.401  38.026  1.00 18.95 ? 433 TRP A CD1 1 
ATOM   3522 C CD2 . TRP A 1 433 ? 37.135 -2.354  38.642  1.00 18.98 ? 433 TRP A CD2 1 
ATOM   3523 N NE1 . TRP A 1 433 ? 38.583 -1.382  37.232  1.00 19.23 ? 433 TRP A NE1 1 
ATOM   3524 C CE2 . TRP A 1 433 ? 38.038 -2.589  37.582  1.00 19.51 ? 433 TRP A CE2 1 
ATOM   3525 C CE3 . TRP A 1 433 ? 36.440 -3.440  39.187  1.00 18.98 ? 433 TRP A CE3 1 
ATOM   3526 C CZ2 . TRP A 1 433 ? 38.260 -3.863  37.064  1.00 19.45 ? 433 TRP A CZ2 1 
ATOM   3527 C CZ3 . TRP A 1 433 ? 36.658 -4.698  38.670  1.00 19.34 ? 433 TRP A CZ3 1 
ATOM   3528 C CH2 . TRP A 1 433 ? 37.553 -4.904  37.622  1.00 19.42 ? 433 TRP A CH2 1 
ATOM   3529 N N   . ALA A 1 434 ? 33.982 1.600   41.196  1.00 16.06 ? 434 ALA A N   1 
ATOM   3530 C CA  . ALA A 1 434 ? 33.026 1.914   42.249  1.00 16.39 ? 434 ALA A CA  1 
ATOM   3531 C C   . ALA A 1 434 ? 31.596 1.854   41.714  1.00 16.56 ? 434 ALA A C   1 
ATOM   3532 O O   . ALA A 1 434 ? 30.705 1.357   42.399  1.00 16.25 ? 434 ALA A O   1 
ATOM   3533 C CB  . ALA A 1 434 ? 33.324 3.272   42.840  1.00 16.17 ? 434 ALA A CB  1 
ATOM   3534 N N   . LEU A 1 435 ? 31.390 2.357   40.491  1.00 16.66 ? 435 LEU A N   1 
ATOM   3535 C CA  . LEU A 1 435 ? 30.060 2.402   39.898  1.00 17.39 ? 435 LEU A CA  1 
ATOM   3536 C C   . LEU A 1 435 ? 29.614 0.997   39.505  1.00 17.06 ? 435 LEU A C   1 
ATOM   3537 O O   . LEU A 1 435 ? 28.427 0.685   39.569  1.00 16.32 ? 435 LEU A O   1 
ATOM   3538 C CB  . LEU A 1 435 ? 30.003 3.347   38.698  1.00 17.92 ? 435 LEU A CB  1 
ATOM   3539 C CG  . LEU A 1 435 ? 29.581 4.790   38.989  1.00 18.34 ? 435 LEU A CG  1 
ATOM   3540 C CD1 . LEU A 1 435 ? 29.426 5.558   37.688  1.00 18.45 ? 435 LEU A CD1 1 
ATOM   3541 C CD2 . LEU A 1 435 ? 28.292 4.860   39.797  1.00 18.81 ? 435 LEU A CD2 1 
ATOM   3542 N N   . MET A 1 436 ? 30.569 0.158   39.091  1.00 17.07 ? 436 MET A N   1 
ATOM   3543 C CA  . MET A 1 436 ? 30.258 -1.224  38.772  1.00 17.18 ? 436 MET A CA  1 
ATOM   3544 C C   . MET A 1 436 ? 29.790 -1.928  40.043  1.00 17.62 ? 436 MET A C   1 
ATOM   3545 O O   . MET A 1 436 ? 28.829 -2.694  40.011  1.00 16.89 ? 436 MET A O   1 
ATOM   3546 C CB  . MET A 1 436 ? 31.456 -1.938  38.137  1.00 16.46 ? 436 MET A CB  1 
ATOM   3547 C CG  . MET A 1 436 ? 31.677 -1.558  36.684  1.00 16.09 ? 436 MET A CG  1 
ATOM   3548 S SD  . MET A 1 436 ? 32.938 -2.538  35.845  1.00 15.11 ? 436 MET A SD  1 
ATOM   3549 C CE  . MET A 1 436 ? 34.485 -1.855  36.450  1.00 15.37 ? 436 MET A CE  1 
ATOM   3550 N N   . ARG A 1 437 ? 30.458 -1.625  41.162  1.00 18.76 ? 437 ARG A N   1 
ATOM   3551 C CA  . ARG A 1 437 ? 30.090 -2.176  42.457  1.00 19.79 ? 437 ARG A CA  1 
ATOM   3552 C C   . ARG A 1 437 ? 28.686 -1.717  42.858  1.00 18.94 ? 437 ARG A C   1 
ATOM   3553 O O   . ARG A 1 437 ? 27.911 -2.508  43.394  1.00 18.71 ? 437 ARG A O   1 
ATOM   3554 C CB  . ARG A 1 437 ? 31.152 -1.818  43.502  1.00 21.59 ? 437 ARG A CB  1 
ATOM   3555 C CG  . ARG A 1 437 ? 30.830 -2.346  44.892  1.00 23.45 ? 437 ARG A CG  1 
ATOM   3556 C CD  . ARG A 1 437 ? 32.030 -2.343  45.832  1.00 25.39 ? 437 ARG A CD  1 
ATOM   3557 N NE  . ARG A 1 437 ? 31.780 -3.206  46.994  1.00 27.91 ? 437 ARG A NE  1 
ATOM   3558 C CZ  . ARG A 1 437 ? 31.642 -4.530  46.946  1.00 28.47 ? 437 ARG A CZ  1 
ATOM   3559 N NH1 . ARG A 1 437 ? 31.859 -5.183  45.820  1.00 28.94 ? 437 ARG A NH1 1 
ATOM   3560 N NH2 . ARG A 1 437 ? 31.316 -5.204  48.034  1.00 29.70 ? 437 ARG A NH2 1 
ATOM   3561 N N   . LEU A 1 438 ? 28.356 -0.447  42.593  1.00 18.12 ? 438 LEU A N   1 
ATOM   3562 C CA  . LEU A 1 438 ? 27.052 0.084   42.966  1.00 18.01 ? 438 LEU A CA  1 
ATOM   3563 C C   . LEU A 1 438 ? 25.951 -0.716  42.267  1.00 17.12 ? 438 LEU A C   1 
ATOM   3564 O O   . LEU A 1 438 ? 24.974 -1.105  42.898  1.00 16.81 ? 438 LEU A O   1 
ATOM   3565 C CB  . LEU A 1 438 ? 26.955 1.576   42.646  1.00 18.03 ? 438 LEU A CB  1 
ATOM   3566 C CG  . LEU A 1 438 ? 25.660 2.273   43.078  1.00 18.11 ? 438 LEU A CG  1 
ATOM   3567 C CD1 . LEU A 1 438 ? 25.576 2.413   44.590  1.00 18.52 ? 438 LEU A CD1 1 
ATOM   3568 C CD2 . LEU A 1 438 ? 25.509 3.629   42.409  1.00 18.18 ? 438 LEU A CD2 1 
ATOM   3569 N N   . GLY A 1 439 ? 26.127 -0.966  40.963  1.00 16.98 ? 439 GLY A N   1 
ATOM   3570 C CA  . GLY A 1 439 ? 25.187 -1.764  40.191  1.00 16.34 ? 439 GLY A CA  1 
ATOM   3571 C C   . GLY A 1 439 ? 25.089 -3.209  40.687  1.00 16.02 ? 439 GLY A C   1 
ATOM   3572 O O   . GLY A 1 439 ? 23.997 -3.776  40.716  1.00 15.34 ? 439 GLY A O   1 
ATOM   3573 N N   . MET A 1 440 ? 26.223 -3.808  41.071  1.00 15.99 ? 440 MET A N   1 
ATOM   3574 C CA  . MET A 1 440 ? 26.220 -5.189  41.525  1.00 16.69 ? 440 MET A CA  1 
ATOM   3575 C C   . MET A 1 440 ? 25.480 -5.310  42.860  1.00 16.92 ? 440 MET A C   1 
ATOM   3576 O O   . MET A 1 440 ? 24.755 -6.281  43.062  1.00 17.37 ? 440 MET A O   1 
ATOM   3577 C CB  . MET A 1 440 ? 27.633 -5.789  41.615  1.00 17.18 ? 440 MET A CB  1 
ATOM   3578 C CG  . MET A 1 440 ? 28.253 -6.173  40.273  1.00 17.44 ? 440 MET A CG  1 
ATOM   3579 S SD  . MET A 1 440 ? 29.482 -7.498  40.372  1.00 17.98 ? 440 MET A SD  1 
ATOM   3580 C CE  . MET A 1 440 ? 30.180 -7.446  38.717  1.00 17.83 ? 440 MET A CE  1 
ATOM   3581 N N   . LYS A 1 441 ? 25.621 -4.317  43.751  1.00 16.62 ? 441 LYS A N   1 
ATOM   3582 C CA  . LYS A 1 441 ? 24.944 -4.344  45.042  1.00 16.76 ? 441 LYS A CA  1 
ATOM   3583 C C   . LYS A 1 441 ? 23.434 -4.132  44.890  1.00 16.87 ? 441 LYS A C   1 
ATOM   3584 O O   . LYS A 1 441 ? 22.679 -4.465  45.801  1.00 16.37 ? 441 LYS A O   1 
ATOM   3585 C CB  . LYS A 1 441 ? 25.489 -3.293  46.017  1.00 16.83 ? 441 LYS A CB  1 
ATOM   3586 C CG  . LYS A 1 441 ? 26.891 -3.540  46.562  1.00 17.24 ? 441 LYS A CG  1 
ATOM   3587 C CD  . LYS A 1 441 ? 27.263 -2.604  47.707  1.00 17.60 ? 441 LYS A CD  1 
ATOM   3588 C CE  . LYS A 1 441 ? 28.723 -2.627  48.064  1.00 18.43 ? 441 LYS A CE  1 
ATOM   3589 N NZ  . LYS A 1 441 ? 29.033 -1.715  49.171  1.00 18.37 ? 441 LYS A NZ  1 
ATOM   3590 N N   . SER A 1 442 ? 23.003 -3.570  43.750  1.00 16.98 ? 442 SER A N   1 
ATOM   3591 C CA  . SER A 1 442 ? 21.604 -3.237  43.518  1.00 17.25 ? 442 SER A CA  1 
ATOM   3592 C C   . SER A 1 442 ? 20.759 -4.503  43.381  1.00 16.98 ? 442 SER A C   1 
ATOM   3593 O O   . SER A 1 442 ? 21.283 -5.616  43.337  1.00 16.82 ? 442 SER A O   1 
ATOM   3594 C CB  . SER A 1 442 ? 21.452 -2.352  42.298  1.00 17.68 ? 442 SER A CB  1 
ATOM   3595 O OG  . SER A 1 442 ? 21.510 -3.109  41.095  1.00 18.48 ? 442 SER A OG  1 
ATOM   3596 N N   . VAL A 1 443 ? 19.438 -4.307  43.301  1.00 17.17 ? 443 VAL A N   1 
ATOM   3597 C CA  . VAL A 1 443 ? 18.478 -5.398  43.210  1.00 17.22 ? 443 VAL A CA  1 
ATOM   3598 C C   . VAL A 1 443 ? 18.422 -5.938  41.781  1.00 17.07 ? 443 VAL A C   1 
ATOM   3599 O O   . VAL A 1 443 ? 17.879 -7.015  41.552  1.00 18.05 ? 443 VAL A O   1 
ATOM   3600 C CB  . VAL A 1 443 ? 17.084 -4.953  43.701  1.00 17.32 ? 443 VAL A CB  1 
ATOM   3601 C CG1 . VAL A 1 443 ? 16.445 -3.911  42.789  1.00 17.29 ? 443 VAL A CG1 1 
ATOM   3602 C CG2 . VAL A 1 443 ? 16.146 -6.139  43.904  1.00 17.71 ? 443 VAL A CG2 1 
ATOM   3603 N N   . ALA A 1 444 ? 18.975 -5.195  40.817  1.00 17.31 ? 444 ALA A N   1 
ATOM   3604 C CA  . ALA A 1 444 ? 18.902 -5.577  39.415  1.00 17.58 ? 444 ALA A CA  1 
ATOM   3605 C C   . ALA A 1 444 ? 19.417 -7.003  39.223  1.00 17.83 ? 444 ALA A C   1 
ATOM   3606 O O   . ALA A 1 444 ? 20.503 -7.337  39.689  1.00 16.72 ? 444 ALA A O   1 
ATOM   3607 C CB  . ALA A 1 444 ? 19.683 -4.594  38.575  1.00 17.96 ? 444 ALA A CB  1 
ATOM   3608 N N   . ARG A 1 445 ? 18.627 -7.831  38.528  1.00 18.01 ? 445 ARG A N   1 
ATOM   3609 C CA  . ARG A 1 445 ? 18.979 -9.225  38.301  1.00 18.97 ? 445 ARG A CA  1 
ATOM   3610 C C   . ARG A 1 445 ? 20.258 -9.325  37.474  1.00 18.26 ? 445 ARG A C   1 
ATOM   3611 O O   . ARG A 1 445 ? 21.096 -10.183 37.748  1.00 17.89 ? 445 ARG A O   1 
ATOM   3612 C CB  . ARG A 1 445 ? 17.846 -10.013 37.633  1.00 19.95 ? 445 ARG A CB  1 
ATOM   3613 C CG  . ARG A 1 445 ? 16.714 -10.349 38.592  1.00 21.25 ? 445 ARG A CG  1 
ATOM   3614 C CD  . ARG A 1 445 ? 15.443 -10.740 37.864  1.00 22.56 ? 445 ARG A CD  1 
ATOM   3615 N NE  . ARG A 1 445 ? 14.357 -11.088 38.786  1.00 24.13 ? 445 ARG A NE  1 
ATOM   3616 C CZ  . ARG A 1 445 ? 14.255 -12.223 39.475  1.00 25.92 ? 445 ARG A CZ  1 
ATOM   3617 N NH1 . ARG A 1 445 ? 15.162 -13.180 39.344  1.00 26.32 ? 445 ARG A NH1 1 
ATOM   3618 N NH2 . ARG A 1 445 ? 13.236 -12.403 40.297  1.00 26.55 ? 445 ARG A NH2 1 
ATOM   3619 N N   A LEU A 1 446 ? 20.390 -8.457  36.462  0.50 17.94 ? 446 LEU A N   1 
ATOM   3620 N N   B LEU A 1 446 ? 20.402 -8.438  36.483  0.50 17.93 ? 446 LEU A N   1 
ATOM   3621 C CA  A LEU A 1 446 ? 21.567 -8.438  35.608  0.50 17.66 ? 446 LEU A CA  1 
ATOM   3622 C CA  B LEU A 1 446 ? 21.566 -8.441  35.614  0.50 17.66 ? 446 LEU A CA  1 
ATOM   3623 C C   A LEU A 1 446 ? 22.254 -7.076  35.707  0.50 17.28 ? 446 LEU A C   1 
ATOM   3624 C C   B LEU A 1 446 ? 22.257 -7.079  35.674  0.50 17.28 ? 446 LEU A C   1 
ATOM   3625 O O   A LEU A 1 446 ? 21.601 -6.035  35.680  0.50 16.86 ? 446 LEU A O   1 
ATOM   3626 O O   B LEU A 1 446 ? 21.610 -6.038  35.592  0.50 16.87 ? 446 LEU A O   1 
ATOM   3627 C CB  A LEU A 1 446 ? 21.186 -8.768  34.165  0.50 17.74 ? 446 LEU A CB  1 
ATOM   3628 C CB  B LEU A 1 446 ? 21.116 -8.800  34.199  0.50 17.73 ? 446 LEU A CB  1 
ATOM   3629 C CG  A LEU A 1 446 ? 20.703 -10.199 33.906  0.50 17.74 ? 446 LEU A CG  1 
ATOM   3630 C CG  B LEU A 1 446 ? 22.230 -9.142  33.206  0.50 17.71 ? 446 LEU A CG  1 
ATOM   3631 C CD1 A LEU A 1 446 ? 20.550 -10.461 32.418  0.50 17.74 ? 446 LEU A CD1 1 
ATOM   3632 C CD1 B LEU A 1 446 ? 23.211 -10.140 33.794  0.50 17.73 ? 446 LEU A CD1 1 
ATOM   3633 C CD2 A LEU A 1 446 ? 21.643 -11.219 34.530  0.50 17.74 ? 446 LEU A CD2 1 
ATOM   3634 C CD2 B LEU A 1 446 ? 21.633 -9.675  31.914  0.50 17.76 ? 446 LEU A CD2 1 
ATOM   3635 N N   . ALA A 1 447 ? 23.583 -7.108  35.845  1.00 16.74 ? 447 ALA A N   1 
ATOM   3636 C CA  . ALA A 1 447 ? 24.416 -5.926  35.709  1.00 16.27 ? 447 ALA A CA  1 
ATOM   3637 C C   . ALA A 1 447 ? 25.353 -6.170  34.532  1.00 15.44 ? 447 ALA A C   1 
ATOM   3638 O O   . ALA A 1 447 ? 26.127 -7.121  34.559  1.00 16.23 ? 447 ALA A O   1 
ATOM   3639 C CB  . ALA A 1 447 ? 25.178 -5.672  36.988  1.00 16.47 ? 447 ALA A CB  1 
ATOM   3640 N N   . VAL A 1 448 ? 25.250 -5.338  33.492  1.00 14.75 ? 448 VAL A N   1 
ATOM   3641 C CA  . VAL A 1 448 ? 26.060 -5.507  32.297  1.00 14.78 ? 448 VAL A CA  1 
ATOM   3642 C C   . VAL A 1 448 ? 26.990 -4.305  32.166  1.00 14.40 ? 448 VAL A C   1 
ATOM   3643 O O   . VAL A 1 448 ? 26.535 -3.168  32.118  1.00 14.60 ? 448 VAL A O   1 
ATOM   3644 C CB  . VAL A 1 448 ? 25.203 -5.709  31.032  1.00 14.61 ? 448 VAL A CB  1 
ATOM   3645 C CG1 . VAL A 1 448 ? 26.031 -5.619  29.753  1.00 14.75 ? 448 VAL A CG1 1 
ATOM   3646 C CG2 . VAL A 1 448 ? 24.453 -7.031  31.088  1.00 14.75 ? 448 VAL A CG2 1 
ATOM   3647 N N   . TYR A 1 449 ? 28.296 -4.575  32.090  1.00 13.95 ? 449 TYR A N   1 
ATOM   3648 C CA  . TYR A 1 449 ? 29.286 -3.515  32.079  1.00 13.90 ? 449 TYR A CA  1 
ATOM   3649 C C   . TYR A 1 449 ? 30.108 -3.575  30.793  1.00 13.92 ? 449 TYR A C   1 
ATOM   3650 O O   . TYR A 1 449 ? 30.599 -4.630  30.408  1.00 13.70 ? 449 TYR A O   1 
ATOM   3651 C CB  . TYR A 1 449 ? 30.122 -3.646  33.354  1.00 13.95 ? 449 TYR A CB  1 
ATOM   3652 C CG  . TYR A 1 449 ? 29.320 -3.447  34.632  1.00 13.94 ? 449 TYR A CG  1 
ATOM   3653 C CD1 . TYR A 1 449 ? 28.370 -2.434  34.739  1.00 13.95 ? 449 TYR A CD1 1 
ATOM   3654 C CD2 . TYR A 1 449 ? 29.495 -4.287  35.723  1.00 14.08 ? 449 TYR A CD2 1 
ATOM   3655 C CE1 . TYR A 1 449 ? 27.632 -2.254  35.897  1.00 14.09 ? 449 TYR A CE1 1 
ATOM   3656 C CE2 . TYR A 1 449 ? 28.762 -4.119  36.886  1.00 14.34 ? 449 TYR A CE2 1 
ATOM   3657 C CZ  . TYR A 1 449 ? 27.829 -3.101  36.973  1.00 14.41 ? 449 TYR A CZ  1 
ATOM   3658 O OH  . TYR A 1 449 ? 27.113 -2.955  38.123  1.00 14.73 ? 449 TYR A OH  1 
ATOM   3659 N N   . PRO A 1 450 ? 30.315 -2.429  30.106  1.00 14.06 ? 450 PRO A N   1 
ATOM   3660 C CA  . PRO A 1 450 ? 31.217 -2.382  28.964  1.00 13.93 ? 450 PRO A CA  1 
ATOM   3661 C C   . PRO A 1 450 ? 32.665 -2.638  29.369  1.00 13.57 ? 450 PRO A C   1 
ATOM   3662 O O   . PRO A 1 450 ? 33.078 -2.280  30.469  1.00 13.03 ? 450 PRO A O   1 
ATOM   3663 C CB  . PRO A 1 450 ? 30.998 -0.983  28.397  1.00 14.00 ? 450 PRO A CB  1 
ATOM   3664 C CG  . PRO A 1 450 ? 30.511 -0.178  29.584  1.00 13.92 ? 450 PRO A CG  1 
ATOM   3665 C CD  . PRO A 1 450 ? 29.713 -1.122  30.417  1.00 14.23 ? 450 PRO A CD  1 
ATOM   3666 N N   . VAL A 1 451 ? 33.424 -3.261  28.463  1.00 13.37 ? 451 VAL A N   1 
ATOM   3667 C CA  . VAL A 1 451 ? 34.790 -3.669  28.750  1.00 13.35 ? 451 VAL A CA  1 
ATOM   3668 C C   . VAL A 1 451 ? 35.658 -2.434  28.998  1.00 13.58 ? 451 VAL A C   1 
ATOM   3669 O O   . VAL A 1 451 ? 36.651 -2.522  29.715  1.00 13.68 ? 451 VAL A O   1 
ATOM   3670 C CB  . VAL A 1 451 ? 35.363 -4.545  27.618  1.00 13.08 ? 451 VAL A CB  1 
ATOM   3671 C CG1 . VAL A 1 451 ? 36.839 -4.861  27.826  1.00 13.15 ? 451 VAL A CG1 1 
ATOM   3672 C CG2 . VAL A 1 451 ? 34.576 -5.838  27.449  1.00 13.06 ? 451 VAL A CG2 1 
ATOM   3673 N N   . GLN A 1 452 ? 35.279 -1.291  28.402  1.00 13.78 ? 452 GLN A N   1 
ATOM   3674 C CA  . GLN A 1 452 ? 36.010 -0.041  28.561  1.00 13.85 ? 452 GLN A CA  1 
ATOM   3675 C C   . GLN A 1 452 ? 35.987 0.442   30.011  1.00 14.23 ? 452 GLN A C   1 
ATOM   3676 O O   . GLN A 1 452 ? 36.895 1.155   30.435  1.00 14.29 ? 452 GLN A O   1 
ATOM   3677 C CB  . GLN A 1 452 ? 35.458 1.082   27.682  1.00 13.92 ? 452 GLN A CB  1 
ATOM   3678 C CG  . GLN A 1 452 ? 35.553 0.813   26.184  1.00 13.59 ? 452 GLN A CG  1 
ATOM   3679 C CD  . GLN A 1 452 ? 34.262 0.281   25.603  1.00 13.44 ? 452 GLN A CD  1 
ATOM   3680 O OE1 . GLN A 1 452 ? 33.630 -0.615  26.171  1.00 13.62 ? 452 GLN A OE1 1 
ATOM   3681 N NE2 . GLN A 1 452 ? 33.841 0.854   24.484  1.00 13.44 ? 452 GLN A NE2 1 
ATOM   3682 N N   . ASP A 1 453 ? 34.943 0.074   30.761  1.00 14.33 ? 453 ASP A N   1 
ATOM   3683 C CA  . ASP A 1 453 ? 34.853 0.423   32.171  1.00 15.07 ? 453 ASP A CA  1 
ATOM   3684 C C   . ASP A 1 453 ? 35.628 -0.580  33.023  1.00 14.94 ? 453 ASP A C   1 
ATOM   3685 O O   . ASP A 1 453 ? 36.130 -0.226  34.087  1.00 15.90 ? 453 ASP A O   1 
ATOM   3686 C CB  . ASP A 1 453 ? 33.406 0.594   32.606  1.00 15.13 ? 453 ASP A CB  1 
ATOM   3687 C CG  . ASP A 1 453 ? 32.728 1.839   32.057  1.00 15.10 ? 453 ASP A CG  1 
ATOM   3688 O OD1 . ASP A 1 453 ? 33.438 2.645   31.421  1.00 15.55 ? 453 ASP A OD1 1 
ATOM   3689 O OD2 . ASP A 1 453 ? 31.501 1.993   32.267  1.00 14.76 ? 453 ASP A OD2 1 
ATOM   3690 N N   . VAL A 1 454 ? 35.735 -1.828  32.556  1.00 14.62 ? 454 VAL A N   1 
ATOM   3691 C CA  . VAL A 1 454 ? 36.571 -2.815  33.224  1.00 14.35 ? 454 VAL A CA  1 
ATOM   3692 C C   . VAL A 1 454 ? 38.022 -2.333  33.162  1.00 14.96 ? 454 VAL A C   1 
ATOM   3693 O O   . VAL A 1 454 ? 38.743 -2.390  34.158  1.00 16.09 ? 454 VAL A O   1 
ATOM   3694 C CB  . VAL A 1 454 ? 36.398 -4.224  32.613  1.00 13.71 ? 454 VAL A CB  1 
ATOM   3695 C CG1 . VAL A 1 454 ? 37.317 -5.257  33.255  1.00 13.31 ? 454 VAL A CG1 1 
ATOM   3696 C CG2 . VAL A 1 454 ? 34.950 -4.701  32.677  1.00 13.20 ? 454 VAL A CG2 1 
ATOM   3697 N N   . LEU A 1 455 ? 38.426 -1.824  31.991  1.00 14.97 ? 455 LEU A N   1 
ATOM   3698 C CA  . LEU A 1 455 ? 39.787 -1.363  31.761  1.00 15.12 ? 455 LEU A CA  1 
ATOM   3699 C C   . LEU A 1 455 ? 39.993 0.058   32.286  1.00 15.46 ? 455 LEU A C   1 
ATOM   3700 O O   . LEU A 1 455 ? 41.130 0.519   32.356  1.00 15.28 ? 455 LEU A O   1 
ATOM   3701 C CB  . LEU A 1 455 ? 40.079 -1.447  30.264  1.00 15.09 ? 455 LEU A CB  1 
ATOM   3702 C CG  . LEU A 1 455 ? 40.080 -2.852  29.656  1.00 14.84 ? 455 LEU A CG  1 
ATOM   3703 C CD1 . LEU A 1 455 ? 40.225 -2.742  28.150  1.00 14.95 ? 455 LEU A CD1 1 
ATOM   3704 C CD2 . LEU A 1 455 ? 41.169 -3.745  30.241  1.00 14.99 ? 455 LEU A CD2 1 
ATOM   3705 N N   . ALA A 1 456 ? 38.895 0.748   32.628  1.00 16.03 ? 456 ALA A N   1 
ATOM   3706 C CA  . ALA A 1 456 ? 38.938 2.126   33.092  1.00 16.82 ? 456 ALA A CA  1 
ATOM   3707 C C   . ALA A 1 456 ? 39.597 3.004   32.031  1.00 17.51 ? 456 ALA A C   1 
ATOM   3708 O O   . ALA A 1 456 ? 40.517 3.768   32.330  1.00 18.50 ? 456 ALA A O   1 
ATOM   3709 C CB  . ALA A 1 456 ? 39.652 2.215   34.427  1.00 17.02 ? 456 ALA A CB  1 
ATOM   3710 N N   . LEU A 1 457 ? 39.127 2.864   30.787  1.00 17.41 ? 457 LEU A N   1 
ATOM   3711 C CA  . LEU A 1 457 ? 39.617 3.659   29.673  1.00 18.09 ? 457 LEU A CA  1 
ATOM   3712 C C   . LEU A 1 457 ? 38.899 5.006   29.664  1.00 18.22 ? 457 LEU A C   1 
ATOM   3713 O O   . LEU A 1 457 ? 37.764 5.114   30.131  1.00 17.59 ? 457 LEU A O   1 
ATOM   3714 C CB  . LEU A 1 457 ? 39.397 2.920   28.351  1.00 17.75 ? 457 LEU A CB  1 
ATOM   3715 C CG  . LEU A 1 457 ? 40.113 1.576   28.190  1.00 18.00 ? 457 LEU A CG  1 
ATOM   3716 C CD1 . LEU A 1 457 ? 39.703 0.906   26.884  1.00 18.21 ? 457 LEU A CD1 1 
ATOM   3717 C CD2 . LEU A 1 457 ? 41.622 1.728   28.258  1.00 18.11 ? 457 LEU A CD2 1 
ATOM   3718 N N   . GLY A 1 458 ? 39.574 6.017   29.102  1.00 18.46 ? 458 GLY A N   1 
ATOM   3719 C CA  . GLY A 1 458 ? 39.009 7.348   28.931  1.00 18.76 ? 458 GLY A CA  1 
ATOM   3720 C C   . GLY A 1 458 ? 38.178 7.450   27.655  1.00 18.82 ? 458 GLY A C   1 
ATOM   3721 O O   . GLY A 1 458 ? 37.824 6.438   27.056  1.00 19.32 ? 458 GLY A O   1 
ATOM   3722 N N   . SER A 1 459 ? 37.911 8.693   27.229  1.00 19.12 ? 459 SER A N   1 
ATOM   3723 C CA  . SER A 1 459 ? 36.923 8.985   26.202  1.00 18.88 ? 459 SER A CA  1 
ATOM   3724 C C   . SER A 1 459 ? 37.397 8.563   24.814  1.00 18.94 ? 459 SER A C   1 
ATOM   3725 O O   . SER A 1 459 ? 36.599 8.506   23.883  1.00 19.15 ? 459 SER A O   1 
ATOM   3726 C CB  . SER A 1 459 ? 36.562 10.443  26.210  1.00 18.67 ? 459 SER A CB  1 
ATOM   3727 O OG  . SER A 1 459 ? 36.065 10.828  27.482  1.00 18.54 ? 459 SER A OG  1 
ATOM   3728 N N   . GLU A 1 460 ? 38.694 8.278   24.674  1.00 19.79 ? 460 GLU A N   1 
ATOM   3729 C CA  . GLU A 1 460 ? 39.230 7.773   23.421  1.00 20.69 ? 460 GLU A CA  1 
ATOM   3730 C C   . GLU A 1 460 ? 38.581 6.435   23.057  1.00 19.90 ? 460 GLU A C   1 
ATOM   3731 O O   . GLU A 1 460 ? 38.603 6.041   21.892  1.00 19.90 ? 460 GLU A O   1 
ATOM   3732 C CB  . GLU A 1 460 ? 40.758 7.668   23.485  1.00 22.15 ? 460 GLU A CB  1 
ATOM   3733 C CG  . GLU A 1 460 ? 41.289 6.610   24.452  1.00 23.05 ? 460 GLU A CG  1 
ATOM   3734 C CD  . GLU A 1 460 ? 41.418 6.996   25.917  1.00 23.97 ? 460 GLU A CD  1 
ATOM   3735 O OE1 . GLU A 1 460 ? 41.862 6.120   26.684  1.00 26.18 ? 460 GLU A OE1 1 
ATOM   3736 O OE2 . GLU A 1 460 ? 41.089 8.136   26.307  1.00 25.02 ? 460 GLU A OE2 1 
ATOM   3737 N N   . ALA A 1 461 ? 38.002 5.743   24.050  1.00 18.97 ? 461 ALA A N   1 
ATOM   3738 C CA  . ALA A 1 461 ? 37.483 4.397   23.863  1.00 18.25 ? 461 ALA A CA  1 
ATOM   3739 C C   . ALA A 1 461 ? 35.961 4.389   23.732  1.00 18.02 ? 461 ALA A C   1 
ATOM   3740 O O   . ALA A 1 461 ? 35.359 3.317   23.756  1.00 17.77 ? 461 ALA A O   1 
ATOM   3741 C CB  . ALA A 1 461 ? 37.925 3.527   25.017  1.00 18.46 ? 461 ALA A CB  1 
ATOM   3742 N N   . ARG A 1 462 ? 35.346 5.572   23.599  1.00 17.72 ? 462 ARG A N   1 
ATOM   3743 C CA  . ARG A 1 462 ? 33.908 5.674   23.415  1.00 18.03 ? 462 ARG A CA  1 
ATOM   3744 C C   . ARG A 1 462 ? 33.522 5.012   22.094  1.00 18.68 ? 462 ARG A C   1 
ATOM   3745 O O   . ARG A 1 462 ? 34.102 5.323   21.054  1.00 19.77 ? 462 ARG A O   1 
ATOM   3746 C CB  . ARG A 1 462 ? 33.470 7.143   23.426  1.00 17.75 ? 462 ARG A CB  1 
ATOM   3747 C CG  . ARG A 1 462 ? 31.974 7.363   23.259  1.00 17.53 ? 462 ARG A CG  1 
ATOM   3748 C CD  . ARG A 1 462 ? 31.611 8.821   23.465  1.00 17.29 ? 462 ARG A CD  1 
ATOM   3749 N NE  . ARG A 1 462 ? 30.162 9.041   23.556  1.00 16.98 ? 462 ARG A NE  1 
ATOM   3750 C CZ  . ARG A 1 462 ? 29.612 10.149  24.033  1.00 16.70 ? 462 ARG A CZ  1 
ATOM   3751 N NH1 . ARG A 1 462 ? 30.373 11.163  24.403  1.00 16.79 ? 462 ARG A NH1 1 
ATOM   3752 N NH2 . ARG A 1 462 ? 28.299 10.248  24.132  1.00 16.69 ? 462 ARG A NH2 1 
ATOM   3753 N N   . MET A 1 463 ? 32.544 4.099   22.147  1.00 18.61 ? 463 MET A N   1 
ATOM   3754 C CA  . MET A 1 463 ? 32.112 3.371   20.963  1.00 18.67 ? 463 MET A CA  1 
ATOM   3755 C C   . MET A 1 463 ? 31.421 4.331   19.994  1.00 17.95 ? 463 MET A C   1 
ATOM   3756 O O   . MET A 1 463 ? 31.791 4.392   18.822  1.00 17.09 ? 463 MET A O   1 
ATOM   3757 C CB  . MET A 1 463 ? 31.187 2.206   21.335  1.00 19.21 ? 463 MET A CB  1 
ATOM   3758 C CG  . MET A 1 463 ? 30.961 1.202   20.213  1.00 19.80 ? 463 MET A CG  1 
ATOM   3759 S SD  . MET A 1 463 ? 32.471 0.366   19.687  1.00 21.40 ? 463 MET A SD  1 
ATOM   3760 C CE  . MET A 1 463 ? 31.852 -0.871  18.538  1.00 20.68 ? 463 MET A CE  1 
ATOM   3761 N N   . ASN A 1 464 ? 30.432 5.086   20.497  1.00 18.06 ? 464 ASN A N   1 
ATOM   3762 C CA  . ASN A 1 464 ? 29.650 6.004   19.680  1.00 18.23 ? 464 ASN A CA  1 
ATOM   3763 C C   . ASN A 1 464 ? 29.497 7.342   20.402  1.00 18.75 ? 464 ASN A C   1 
ATOM   3764 O O   . ASN A 1 464 ? 29.203 7.376   21.593  1.00 18.78 ? 464 ASN A O   1 
ATOM   3765 C CB  . ASN A 1 464 ? 28.280 5.427   19.338  1.00 18.08 ? 464 ASN A CB  1 
ATOM   3766 C CG  . ASN A 1 464 ? 27.487 6.333   18.422  1.00 18.11 ? 464 ASN A CG  1 
ATOM   3767 O OD1 . ASN A 1 464 ? 27.990 6.756   17.375  1.00 17.48 ? 464 ASN A OD1 1 
ATOM   3768 N ND2 . ASN A 1 464 ? 26.253 6.648   18.791  1.00 18.09 ? 464 ASN A ND2 1 
ATOM   3769 N N   . TYR A 1 465 ? 29.709 8.435   19.658  1.00 19.62 ? 465 TYR A N   1 
ATOM   3770 C CA  . TYR A 1 465 ? 29.529 9.789   20.156  1.00 20.45 ? 465 TYR A CA  1 
ATOM   3771 C C   . TYR A 1 465 ? 28.432 10.439  19.316  1.00 21.19 ? 465 TYR A C   1 
ATOM   3772 O O   . TYR A 1 465 ? 28.694 10.913  18.212  1.00 20.94 ? 465 TYR A O   1 
ATOM   3773 C CB  . TYR A 1 465 ? 30.853 10.561  20.088  1.00 20.78 ? 465 TYR A CB  1 
ATOM   3774 C CG  . TYR A 1 465 ? 30.967 11.800  20.971  1.00 20.96 ? 465 TYR A CG  1 
ATOM   3775 C CD1 . TYR A 1 465 ? 29.858 12.568  21.313  1.00 20.81 ? 465 TYR A CD1 1 
ATOM   3776 C CD2 . TYR A 1 465 ? 32.201 12.195  21.479  1.00 21.20 ? 465 TYR A CD2 1 
ATOM   3777 C CE1 . TYR A 1 465 ? 29.973 13.686  22.123  1.00 20.84 ? 465 TYR A CE1 1 
ATOM   3778 C CE2 . TYR A 1 465 ? 32.327 13.309  22.294  1.00 21.61 ? 465 TYR A CE2 1 
ATOM   3779 C CZ  . TYR A 1 465 ? 31.211 14.061  22.612  1.00 21.45 ? 465 TYR A CZ  1 
ATOM   3780 O OH  . TYR A 1 465 ? 31.343 15.156  23.418  1.00 22.81 ? 465 TYR A OH  1 
ATOM   3781 N N   . PRO A 1 466 ? 27.167 10.470  19.796  1.00 22.75 ? 466 PRO A N   1 
ATOM   3782 C CA  . PRO A 1 466 ? 26.076 11.036  19.010  1.00 23.18 ? 466 PRO A CA  1 
ATOM   3783 C C   . PRO A 1 466 ? 26.292 12.513  18.688  1.00 24.34 ? 466 PRO A C   1 
ATOM   3784 O O   . PRO A 1 466 ? 26.413 13.336  19.593  1.00 24.22 ? 466 PRO A O   1 
ATOM   3785 C CB  . PRO A 1 466 ? 24.839 10.797  19.876  1.00 23.02 ? 466 PRO A CB  1 
ATOM   3786 C CG  . PRO A 1 466 ? 25.266 9.771   20.909  1.00 22.79 ? 466 PRO A CG  1 
ATOM   3787 C CD  . PRO A 1 466 ? 26.730 9.982   21.113  1.00 22.27 ? 466 PRO A CD  1 
ATOM   3788 N N   . GLY A 1 467 ? 26.346 12.831  17.389  1.00 25.70 ? 467 GLY A N   1 
ATOM   3789 C CA  . GLY A 1 467 ? 26.596 14.188  16.930  1.00 27.19 ? 467 GLY A CA  1 
ATOM   3790 C C   . GLY A 1 467 ? 28.038 14.379  16.466  1.00 28.71 ? 467 GLY A C   1 
ATOM   3791 O O   . GLY A 1 467 ? 28.426 15.495  16.124  1.00 29.91 ? 467 GLY A O   1 
ATOM   3792 N N   . ARG A 1 468 ? 28.817 13.286  16.458  1.00 30.27 ? 468 ARG A N   1 
ATOM   3793 C CA  . ARG A 1 468 ? 30.181 13.296  15.949  1.00 31.52 ? 468 ARG A CA  1 
ATOM   3794 C C   . ARG A 1 468 ? 30.218 12.533  14.625  1.00 32.58 ? 468 ARG A C   1 
ATOM   3795 O O   . ARG A 1 468 ? 29.846 11.362  14.578  1.00 34.70 ? 468 ARG A O   1 
ATOM   3796 C CB  . ARG A 1 468 ? 31.151 12.686  16.965  1.00 31.69 ? 468 ARG A CB  1 
ATOM   3797 C CG  . ARG A 1 468 ? 32.610 12.734  16.533  1.00 32.39 ? 468 ARG A CG  1 
ATOM   3798 C CD  . ARG A 1 468 ? 33.527 11.971  17.478  1.00 32.24 ? 468 ARG A CD  1 
ATOM   3799 N NE  . ARG A 1 468 ? 33.220 10.537  17.536  1.00 32.67 ? 468 ARG A NE  1 
ATOM   3800 C CZ  . ARG A 1 468 ? 33.880 9.635   18.256  1.00 32.07 ? 468 ARG A CZ  1 
ATOM   3801 N NH1 . ARG A 1 468 ? 34.945 9.987   18.958  1.00 32.26 ? 468 ARG A NH1 1 
ATOM   3802 N NH2 . ARG A 1 468 ? 33.476 8.374   18.263  1.00 31.75 ? 468 ARG A NH2 1 
ATOM   3803 N N   . PRO A 1 469 ? 30.653 13.162  13.506  1.00 32.82 ? 469 PRO A N   1 
ATOM   3804 C CA  . PRO A 1 469 ? 30.562 12.539  12.188  1.00 32.97 ? 469 PRO A CA  1 
ATOM   3805 C C   . PRO A 1 469 ? 31.449 11.312  11.971  1.00 32.80 ? 469 PRO A C   1 
ATOM   3806 O O   . PRO A 1 469 ? 31.058 10.407  11.235  1.00 34.10 ? 469 PRO A O   1 
ATOM   3807 C CB  . PRO A 1 469 ? 30.950 13.669  11.228  1.00 33.34 ? 469 PRO A CB  1 
ATOM   3808 C CG  . PRO A 1 469 ? 30.801 14.937  12.053  1.00 33.32 ? 469 PRO A CG  1 
ATOM   3809 C CD  . PRO A 1 469 ? 31.187 14.531  13.435  1.00 32.76 ? 469 PRO A CD  1 
ATOM   3810 N N   . SER A 1 470 ? 32.645 11.294  12.577  1.00 31.31 ? 470 SER A N   1 
ATOM   3811 C CA  . SER A 1 470 ? 33.611 10.232  12.334  1.00 29.86 ? 470 SER A CA  1 
ATOM   3812 C C   . SER A 1 470 ? 34.139 9.663   13.651  1.00 27.98 ? 470 SER A C   1 
ATOM   3813 O O   . SER A 1 470 ? 33.966 10.263  14.709  1.00 28.21 ? 470 SER A O   1 
ATOM   3814 C CB  . SER A 1 470 ? 34.746 10.720  11.455  1.00 30.88 ? 470 SER A CB  1 
ATOM   3815 O OG  . SER A 1 470 ? 35.645 11.563  12.166  1.00 30.96 ? 470 SER A OG  1 
ATOM   3816 N N   . GLY A 1 471 ? 34.775 8.485   13.561  1.00 26.61 ? 471 GLY A N   1 
ATOM   3817 C CA  . GLY A 1 471 ? 35.452 7.858   14.686  1.00 24.63 ? 471 GLY A CA  1 
ATOM   3818 C C   . GLY A 1 471 ? 34.530 6.944   15.493  1.00 22.84 ? 471 GLY A C   1 
ATOM   3819 O O   . GLY A 1 471 ? 34.930 6.439   16.539  1.00 22.55 ? 471 GLY A O   1 
ATOM   3820 N N   . ASN A 1 472 ? 33.306 6.723   14.994  1.00 20.84 ? 472 ASN A N   1 
ATOM   3821 C CA  . ASN A 1 472 ? 32.318 5.919   15.694  1.00 19.37 ? 472 ASN A CA  1 
ATOM   3822 C C   . ASN A 1 472 ? 32.458 4.445   15.311  1.00 17.81 ? 472 ASN A C   1 
ATOM   3823 O O   . ASN A 1 472 ? 32.824 4.114   14.184  1.00 17.30 ? 472 ASN A O   1 
ATOM   3824 C CB  . ASN A 1 472 ? 30.902 6.430   15.440  1.00 19.21 ? 472 ASN A CB  1 
ATOM   3825 C CG  . ASN A 1 472 ? 30.671 7.805   16.025  1.00 19.72 ? 472 ASN A CG  1 
ATOM   3826 O OD1 . ASN A 1 472 ? 31.032 8.059   17.181  1.00 19.37 ? 472 ASN A OD1 1 
ATOM   3827 N ND2 . ASN A 1 472 ? 30.071 8.704   15.256  1.00 19.79 ? 472 ASN A ND2 1 
ATOM   3828 N N   . TRP A 1 473 ? 32.139 3.579   16.281  1.00 16.32 ? 473 TRP A N   1 
ATOM   3829 C CA  . TRP A 1 473 ? 32.054 2.136   16.106  1.00 15.75 ? 473 TRP A CA  1 
ATOM   3830 C C   . TRP A 1 473 ? 33.428 1.518   15.851  1.00 15.00 ? 473 TRP A C   1 
ATOM   3831 O O   . TRP A 1 473 ? 33.511 0.446   15.261  1.00 14.64 ? 473 TRP A O   1 
ATOM   3832 C CB  . TRP A 1 473 ? 31.090 1.776   14.965  1.00 15.66 ? 473 TRP A CB  1 
ATOM   3833 C CG  . TRP A 1 473 ? 29.812 2.576   14.954  1.00 15.32 ? 473 TRP A CG  1 
ATOM   3834 C CD1 . TRP A 1 473 ? 29.410 3.469   14.007  1.00 15.22 ? 473 TRP A CD1 1 
ATOM   3835 C CD2 . TRP A 1 473 ? 28.777 2.562   15.958  1.00 14.92 ? 473 TRP A CD2 1 
ATOM   3836 N NE1 . TRP A 1 473 ? 28.188 3.993   14.334  1.00 15.16 ? 473 TRP A NE1 1 
ATOM   3837 C CE2 . TRP A 1 473 ? 27.775 3.461   15.526  1.00 14.95 ? 473 TRP A CE2 1 
ATOM   3838 C CE3 . TRP A 1 473 ? 28.596 1.876   17.163  1.00 14.63 ? 473 TRP A CE3 1 
ATOM   3839 C CZ2 . TRP A 1 473 ? 26.618 3.694   16.266  1.00 14.77 ? 473 TRP A CZ2 1 
ATOM   3840 C CZ3 . TRP A 1 473 ? 27.454 2.110   17.894  1.00 14.85 ? 473 TRP A CZ3 1 
ATOM   3841 C CH2 . TRP A 1 473 ? 26.476 3.001   17.446  1.00 14.73 ? 473 TRP A CH2 1 
ATOM   3842 N N   . ALA A 1 474 ? 34.501 2.173   16.306  1.00 14.78 ? 474 ALA A N   1 
ATOM   3843 C CA  . ALA A 1 474 ? 35.838 1.795   15.869  1.00 14.52 ? 474 ALA A CA  1 
ATOM   3844 C C   . ALA A 1 474 ? 36.688 1.232   17.009  1.00 14.44 ? 474 ALA A C   1 
ATOM   3845 O O   . ALA A 1 474 ? 37.664 0.528   16.746  1.00 14.18 ? 474 ALA A O   1 
ATOM   3846 C CB  . ALA A 1 474 ? 36.508 2.982   15.205  1.00 14.77 ? 474 ALA A CB  1 
ATOM   3847 N N   . TRP A 1 475 ? 36.330 1.510   18.271  1.00 14.15 ? 475 TRP A N   1 
ATOM   3848 C CA  . TRP A 1 475 ? 37.187 1.105   19.377  1.00 13.69 ? 475 TRP A CA  1 
ATOM   3849 C C   . TRP A 1 475 ? 37.457 -0.398  19.331  1.00 13.55 ? 475 TRP A C   1 
ATOM   3850 O O   . TRP A 1 475 ? 36.542 -1.182  19.087  1.00 12.52 ? 475 TRP A O   1 
ATOM   3851 C CB  . TRP A 1 475 ? 36.595 1.485   20.742  1.00 13.68 ? 475 TRP A CB  1 
ATOM   3852 C CG  . TRP A 1 475 ? 37.401 0.889   21.866  1.00 13.69 ? 475 TRP A CG  1 
ATOM   3853 C CD1 . TRP A 1 475 ? 38.638 1.297   22.272  1.00 13.65 ? 475 TRP A CD1 1 
ATOM   3854 C CD2 . TRP A 1 475 ? 37.066 -0.253  22.686  1.00 13.57 ? 475 TRP A CD2 1 
ATOM   3855 N NE1 . TRP A 1 475 ? 39.090 0.501   23.290  1.00 13.72 ? 475 TRP A NE1 1 
ATOM   3856 C CE2 . TRP A 1 475 ? 38.152 -0.457  23.567  1.00 13.68 ? 475 TRP A CE2 1 
ATOM   3857 C CE3 . TRP A 1 475 ? 35.967 -1.114  22.767  1.00 13.53 ? 475 TRP A CE3 1 
ATOM   3858 C CZ2 . TRP A 1 475 ? 38.163 -1.483  24.512  1.00 13.66 ? 475 TRP A CZ2 1 
ATOM   3859 C CZ3 . TRP A 1 475 ? 35.977 -2.126  23.703  1.00 13.49 ? 475 TRP A CZ3 1 
ATOM   3860 C CH2 . TRP A 1 475 ? 37.062 -2.307  24.563  1.00 13.67 ? 475 TRP A CH2 1 
ATOM   3861 N N   . ARG A 1 476 ? 38.718 -0.785  19.594  1.00 13.63 ? 476 ARG A N   1 
ATOM   3862 C CA  . ARG A 1 476 ? 39.102 -2.187  19.673  1.00 13.95 ? 476 ARG A CA  1 
ATOM   3863 C C   . ARG A 1 476 ? 39.981 -2.434  20.899  1.00 13.95 ? 476 ARG A C   1 
ATOM   3864 O O   . ARG A 1 476 ? 40.849 -1.629  21.227  1.00 13.22 ? 476 ARG A O   1 
ATOM   3865 C CB  . ARG A 1 476 ? 39.907 -2.672  18.459  1.00 14.10 ? 476 ARG A CB  1 
ATOM   3866 C CG  . ARG A 1 476 ? 39.214 -2.655  17.103  1.00 14.02 ? 476 ARG A CG  1 
ATOM   3867 C CD  . ARG A 1 476 ? 40.094 -3.291  16.033  1.00 13.90 ? 476 ARG A CD  1 
ATOM   3868 N NE  . ARG A 1 476 ? 40.269 -4.735  16.234  1.00 14.15 ? 476 ARG A NE  1 
ATOM   3869 C CZ  . ARG A 1 476 ? 41.052 -5.540  15.521  1.00 14.10 ? 476 ARG A CZ  1 
ATOM   3870 N NH1 . ARG A 1 476 ? 41.809 -5.066  14.547  1.00 14.52 ? 476 ARG A NH1 1 
ATOM   3871 N NH2 . ARG A 1 476 ? 41.074 -6.831  15.785  1.00 14.61 ? 476 ARG A NH2 1 
ATOM   3872 N N   . LEU A 1 477 ? 39.757 -3.580  21.548  1.00 14.84 ? 477 LEU A N   1 
ATOM   3873 C CA  . LEU A 1 477 ? 40.668 -4.112  22.547  1.00 15.97 ? 477 LEU A CA  1 
ATOM   3874 C C   . LEU A 1 477 ? 42.019 -4.407  21.896  1.00 16.65 ? 477 LEU A C   1 
ATOM   3875 O O   . LEU A 1 477 ? 42.084 -4.814  20.738  1.00 15.81 ? 477 LEU A O   1 
ATOM   3876 C CB  . LEU A 1 477 ? 40.081 -5.381  23.164  1.00 16.58 ? 477 LEU A CB  1 
ATOM   3877 C CG  . LEU A 1 477 ? 39.228 -5.216  24.423  1.00 17.09 ? 477 LEU A CG  1 
ATOM   3878 C CD1 . LEU A 1 477 ? 38.217 -6.340  24.529  1.00 17.68 ? 477 LEU A CD1 1 
ATOM   3879 C CD2 . LEU A 1 477 ? 40.093 -5.186  25.662  1.00 17.31 ? 477 LEU A CD2 1 
ATOM   3880 N N   . LEU A 1 478 ? 43.092 -4.195  22.662  1.00 17.89 ? 478 LEU A N   1 
ATOM   3881 C CA  . LEU A 1 478 ? 44.417 -4.666  22.295  1.00 18.88 ? 478 LEU A CA  1 
ATOM   3882 C C   . LEU A 1 478 ? 44.563 -6.097  22.809  1.00 19.59 ? 478 LEU A C   1 
ATOM   3883 O O   . LEU A 1 478 ? 43.975 -6.446  23.830  1.00 19.85 ? 478 LEU A O   1 
ATOM   3884 C CB  . LEU A 1 478 ? 45.476 -3.742  22.900  1.00 19.19 ? 478 LEU A CB  1 
ATOM   3885 C CG  . LEU A 1 478 ? 45.327 -2.243  22.618  1.00 19.42 ? 478 LEU A CG  1 
ATOM   3886 C CD1 . LEU A 1 478 ? 46.189 -1.437  23.573  1.00 19.96 ? 478 LEU A CD1 1 
ATOM   3887 C CD2 . LEU A 1 478 ? 45.678 -1.898  21.181  1.00 19.49 ? 478 LEU A CD2 1 
ATOM   3888 N N   . PRO A 1 479 ? 45.334 -6.985  22.141  1.00 20.95 ? 479 PRO A N   1 
ATOM   3889 C CA  . PRO A 1 479 ? 45.560 -8.322  22.683  1.00 21.39 ? 479 PRO A CA  1 
ATOM   3890 C C   . PRO A 1 479 ? 46.178 -8.290  24.080  1.00 21.90 ? 479 PRO A C   1 
ATOM   3891 O O   . PRO A 1 479 ? 47.087 -7.501  24.339  1.00 21.41 ? 479 PRO A O   1 
ATOM   3892 C CB  . PRO A 1 479 ? 46.486 -8.986  21.671  1.00 21.42 ? 479 PRO A CB  1 
ATOM   3893 C CG  . PRO A 1 479 ? 46.377 -8.135  20.416  1.00 21.46 ? 479 PRO A CG  1 
ATOM   3894 C CD  . PRO A 1 479 ? 46.019 -6.750  20.860  1.00 21.01 ? 479 PRO A CD  1 
ATOM   3895 N N   . GLY A 1 480 ? 45.640 -9.119  24.985  1.00 22.70 ? 480 GLY A N   1 
ATOM   3896 C CA  . GLY A 1 480 ? 46.166 -9.246  26.337  1.00 22.99 ? 480 GLY A CA  1 
ATOM   3897 C C   . GLY A 1 480 ? 45.672 -8.151  27.283  1.00 23.06 ? 480 GLY A C   1 
ATOM   3898 O O   . GLY A 1 480 ? 45.918 -8.225  28.483  1.00 22.86 ? 480 GLY A O   1 
ATOM   3899 N N   . GLU A 1 481 ? 44.961 -7.150  26.752  1.00 23.62 ? 481 GLU A N   1 
ATOM   3900 C CA  . GLU A 1 481 ? 44.599 -5.971  27.525  1.00 23.86 ? 481 GLU A CA  1 
ATOM   3901 C C   . GLU A 1 481 ? 43.721 -6.399  28.705  1.00 24.31 ? 481 GLU A C   1 
ATOM   3902 O O   . GLU A 1 481 ? 43.895 -5.911  29.818  1.00 24.27 ? 481 GLU A O   1 
ATOM   3903 C CB  . GLU A 1 481 ? 43.973 -4.935  26.584  1.00 23.45 ? 481 GLU A CB  1 
ATOM   3904 C CG  . GLU A 1 481 ? 43.981 -3.508  27.127  1.00 23.19 ? 481 GLU A CG  1 
ATOM   3905 C CD  . GLU A 1 481 ? 43.386 -2.448  26.208  1.00 22.72 ? 481 GLU A CD  1 
ATOM   3906 O OE1 . GLU A 1 481 ? 42.809 -2.793  25.152  1.00 21.36 ? 481 GLU A OE1 1 
ATOM   3907 O OE2 . GLU A 1 481 ? 43.517 -1.252  26.552  1.00 22.97 ? 481 GLU A OE2 1 
ATOM   3908 N N   . LEU A 1 482 ? 42.820 -7.359  28.474  1.00 25.05 ? 482 LEU A N   1 
ATOM   3909 C CA  . LEU A 1 482 ? 41.926 -7.840  29.516  1.00 25.89 ? 482 LEU A CA  1 
ATOM   3910 C C   . LEU A 1 482 ? 42.641 -8.903  30.356  1.00 26.16 ? 482 LEU A C   1 
ATOM   3911 O O   . LEU A 1 482 ? 42.519 -10.097 30.097  1.00 28.27 ? 482 LEU A O   1 
ATOM   3912 C CB  . LEU A 1 482 ? 40.663 -8.353  28.822  1.00 26.38 ? 482 LEU A CB  1 
ATOM   3913 C CG  . LEU A 1 482 ? 39.338 -8.144  29.560  1.00 27.28 ? 482 LEU A CG  1 
ATOM   3914 C CD1 . LEU A 1 482 ? 39.201 -6.761  30.184  1.00 27.03 ? 482 LEU A CD1 1 
ATOM   3915 C CD2 . LEU A 1 482 ? 38.191 -8.396  28.592  1.00 27.58 ? 482 LEU A CD2 1 
ATOM   3916 N N   . SER A 1 483 ? 43.385 -8.448  31.376  1.00 25.73 ? 483 SER A N   1 
ATOM   3917 C CA  . SER A 1 483 ? 44.306 -9.289  32.128  1.00 24.89 ? 483 SER A CA  1 
ATOM   3918 C C   . SER A 1 483 ? 43.553 -10.181 33.112  1.00 24.72 ? 483 SER A C   1 
ATOM   3919 O O   . SER A 1 483 ? 42.415 -9.886  33.470  1.00 24.54 ? 483 SER A O   1 
ATOM   3920 C CB  . SER A 1 483 ? 45.336 -8.462  32.866  1.00 24.60 ? 483 SER A CB  1 
ATOM   3921 O OG  . SER A 1 483 ? 44.891 -8.120  34.173  1.00 24.66 ? 483 SER A OG  1 
ATOM   3922 N N   . PRO A 1 484 ? 44.177 -11.282 33.598  1.00 25.02 ? 484 PRO A N   1 
ATOM   3923 C CA  . PRO A 1 484 ? 43.571 -12.124 34.626  1.00 24.61 ? 484 PRO A CA  1 
ATOM   3924 C C   . PRO A 1 484 ? 43.142 -11.355 35.875  1.00 24.34 ? 484 PRO A C   1 
ATOM   3925 O O   . PRO A 1 484 ? 42.109 -11.663 36.460  1.00 24.92 ? 484 PRO A O   1 
ATOM   3926 C CB  . PRO A 1 484 ? 44.659 -13.157 34.925  1.00 24.96 ? 484 PRO A CB  1 
ATOM   3927 C CG  . PRO A 1 484 ? 45.456 -13.204 33.633  1.00 24.91 ? 484 PRO A CG  1 
ATOM   3928 C CD  . PRO A 1 484 ? 45.490 -11.786 33.165  1.00 25.00 ? 484 PRO A CD  1 
ATOM   3929 N N   . GLU A 1 485 ? 43.937 -10.351 36.271  1.00 23.42 ? 485 GLU A N   1 
ATOM   3930 C CA  . GLU A 1 485 ? 43.642 -9.539  37.442  1.00 23.31 ? 485 GLU A CA  1 
ATOM   3931 C C   . GLU A 1 485 ? 42.297 -8.826  37.284  1.00 23.09 ? 485 GLU A C   1 
ATOM   3932 O O   . GLU A 1 485 ? 41.548 -8.718  38.253  1.00 22.40 ? 485 GLU A O   1 
ATOM   3933 C CB  . GLU A 1 485 ? 44.769 -8.538  37.705  1.00 24.25 ? 485 GLU A CB  1 
ATOM   3934 C CG  . GLU A 1 485 ? 44.468 -7.555  38.834  1.00 25.03 ? 485 GLU A CG  1 
ATOM   3935 C CD  . GLU A 1 485 ? 45.564 -6.541  39.119  1.00 26.37 ? 485 GLU A CD  1 
ATOM   3936 O OE1 . GLU A 1 485 ? 46.681 -6.673  38.563  1.00 26.86 ? 485 GLU A OE1 1 
ATOM   3937 O OE2 . GLU A 1 485 ? 45.288 -5.601  39.897  1.00 27.14 ? 485 GLU A OE2 1 
ATOM   3938 N N   . HIS A 1 486 ? 42.002 -8.318  36.078  1.00 22.23 ? 486 HIS A N   1 
ATOM   3939 C CA  . HIS A 1 486 ? 40.712 -7.698  35.823  1.00 22.33 ? 486 HIS A CA  1 
ATOM   3940 C C   . HIS A 1 486 ? 39.601 -8.704  36.118  1.00 21.89 ? 486 HIS A C   1 
ATOM   3941 O O   . HIS A 1 486 ? 38.625 -8.367  36.782  1.00 21.56 ? 486 HIS A O   1 
ATOM   3942 C CB  . HIS A 1 486 ? 40.592 -7.174  34.387  1.00 22.74 ? 486 HIS A CB  1 
ATOM   3943 C CG  . HIS A 1 486 ? 41.500 -6.037  34.046  1.00 22.31 ? 486 HIS A CG  1 
ATOM   3944 N ND1 . HIS A 1 486 ? 42.633 -6.197  33.279  1.00 22.70 ? 486 HIS A ND1 1 
ATOM   3945 C CD2 . HIS A 1 486 ? 41.430 -4.733  34.333  1.00 21.87 ? 486 HIS A CD2 1 
ATOM   3946 C CE1 . HIS A 1 486 ? 43.225 -5.021  33.125  1.00 22.82 ? 486 HIS A CE1 1 
ATOM   3947 N NE2 . HIS A 1 486 ? 42.507 -4.117  33.756  1.00 21.54 ? 486 HIS A NE2 1 
ATOM   3948 N N   . GLY A 1 487 ? 39.780 -9.940  35.632  1.00 22.41 ? 487 GLY A N   1 
ATOM   3949 C CA  . GLY A 1 487 ? 38.808 -11.006 35.812  1.00 23.01 ? 487 GLY A CA  1 
ATOM   3950 C C   . GLY A 1 487 ? 38.629 -11.384 37.282  1.00 23.75 ? 487 GLY A C   1 
ATOM   3951 O O   . GLY A 1 487 ? 37.509 -11.636 37.724  1.00 23.66 ? 487 GLY A O   1 
ATOM   3952 N N   . GLU A 1 488 ? 39.739 -11.408 38.030  1.00 24.50 ? 488 GLU A N   1 
ATOM   3953 C CA  . GLU A 1 488 ? 39.720 -11.780 39.437  1.00 25.73 ? 488 GLU A CA  1 
ATOM   3954 C C   . GLU A 1 488 ? 39.007 -10.701 40.254  1.00 24.89 ? 488 GLU A C   1 
ATOM   3955 O O   . GLU A 1 488 ? 38.328 -11.024 41.228  1.00 23.90 ? 488 GLU A O   1 
ATOM   3956 C CB  . GLU A 1 488 ? 41.140 -12.055 39.941  1.00 26.84 ? 488 GLU A CB  1 
ATOM   3957 C CG  . GLU A 1 488 ? 41.791 -13.271 39.284  1.00 28.66 ? 488 GLU A CG  1 
ATOM   3958 C CD  . GLU A 1 488 ? 43.299 -13.396 39.454  1.00 30.31 ? 488 GLU A CD  1 
ATOM   3959 O OE1 . GLU A 1 488 ? 43.873 -12.677 40.303  1.00 30.35 ? 488 GLU A OE1 1 
ATOM   3960 O OE2 . GLU A 1 488 ? 43.908 -14.205 38.713  1.00 31.10 ? 488 GLU A OE2 1 
ATOM   3961 N N   . ARG A 1 489 ? 39.164 -9.431  39.851  1.00 24.12 ? 489 ARG A N   1 
ATOM   3962 C CA  . ARG A 1 489 ? 38.500 -8.318  40.516  1.00 24.28 ? 489 ARG A CA  1 
ATOM   3963 C C   . ARG A 1 489 ? 36.987 -8.391  40.309  1.00 23.20 ? 489 ARG A C   1 
ATOM   3964 O O   . ARG A 1 489 ? 36.225 -8.108  41.228  1.00 24.63 ? 489 ARG A O   1 
ATOM   3965 C CB  . ARG A 1 489 ? 39.003 -6.951  40.037  1.00 25.11 ? 489 ARG A CB  1 
ATOM   3966 C CG  . ARG A 1 489 ? 40.371 -6.552  40.570  1.00 26.33 ? 489 ARG A CG  1 
ATOM   3967 C CD  . ARG A 1 489 ? 40.669 -5.086  40.296  1.00 27.49 ? 489 ARG A CD  1 
ATOM   3968 N NE  . ARG A 1 489 ? 39.872 -4.192  41.144  1.00 27.86 ? 489 ARG A NE  1 
ATOM   3969 C CZ  . ARG A 1 489 ? 39.966 -2.865  41.170  1.00 28.39 ? 489 ARG A CZ  1 
ATOM   3970 N NH1 . ARG A 1 489 ? 40.751 -2.228  40.315  1.00 28.03 ? 489 ARG A NH1 1 
ATOM   3971 N NH2 . ARG A 1 489 ? 39.265 -2.173  42.052  1.00 28.09 ? 489 ARG A NH2 1 
ATOM   3972 N N   . LEU A 1 490 ? 36.559 -8.754  39.097  1.00 22.69 ? 490 LEU A N   1 
ATOM   3973 C CA  . LEU A 1 490 ? 35.143 -8.906  38.792  1.00 21.74 ? 490 LEU A CA  1 
ATOM   3974 C C   . LEU A 1 490 ? 34.554 -10.056 39.604  1.00 20.96 ? 490 LEU A C   1 
ATOM   3975 O O   . LEU A 1 490 ? 33.470 -9.925  40.165  1.00 20.97 ? 490 LEU A O   1 
ATOM   3976 C CB  . LEU A 1 490 ? 34.950 -9.137  37.293  1.00 21.31 ? 490 LEU A CB  1 
ATOM   3977 C CG  . LEU A 1 490 ? 35.154 -7.918  36.390  1.00 20.63 ? 490 LEU A CG  1 
ATOM   3978 C CD1 . LEU A 1 490 ? 35.466 -8.341  34.964  1.00 20.88 ? 490 LEU A CD1 1 
ATOM   3979 C CD2 . LEU A 1 490 ? 33.934 -7.012  36.421  1.00 20.49 ? 490 LEU A CD2 1 
ATOM   3980 N N   . ARG A 1 491 ? 35.273 -11.183 39.656  1.00 20.91 ? 491 ARG A N   1 
ATOM   3981 C CA  . ARG A 1 491 ? 34.761 -12.383 40.300  1.00 21.26 ? 491 ARG A CA  1 
ATOM   3982 C C   . ARG A 1 491 ? 34.529 -12.114 41.786  1.00 20.06 ? 491 ARG A C   1 
ATOM   3983 O O   . ARG A 1 491 ? 33.508 -12.533 42.323  1.00 19.90 ? 491 ARG A O   1 
ATOM   3984 C CB  . ARG A 1 491 ? 35.674 -13.595 40.078  1.00 21.83 ? 491 ARG A CB  1 
ATOM   3985 C CG  . ARG A 1 491 ? 35.013 -14.930 40.390  1.00 22.22 ? 491 ARG A CG  1 
ATOM   3986 C CD  . ARG A 1 491 ? 35.958 -16.104 40.171  1.00 22.76 ? 491 ARG A CD  1 
ATOM   3987 N NE  . ARG A 1 491 ? 35.376 -17.394 40.559  1.00 23.15 ? 491 ARG A NE  1 
ATOM   3988 C CZ  . ARG A 1 491 ? 35.024 -18.376 39.728  1.00 24.39 ? 491 ARG A CZ  1 
ATOM   3989 N NH1 . ARG A 1 491 ? 35.054 -18.196 38.417  1.00 24.63 ? 491 ARG A NH1 1 
ATOM   3990 N NH2 . ARG A 1 491 ? 34.612 -19.536 40.213  1.00 24.27 ? 491 ARG A NH2 1 
ATOM   3991 N N   . ALA A 1 492 ? 35.467 -11.398 42.426  1.00 19.49 ? 492 ALA A N   1 
ATOM   3992 C CA  . ALA A 1 492 ? 35.366 -11.052 43.839  1.00 19.41 ? 492 ALA A CA  1 
ATOM   3993 C C   . ALA A 1 492 ? 34.140 -10.176 44.101  1.00 19.22 ? 492 ALA A C   1 
ATOM   3994 O O   . ALA A 1 492 ? 33.440 -10.363 45.092  1.00 19.06 ? 492 ALA A O   1 
ATOM   3995 C CB  . ALA A 1 492 ? 36.629 -10.356 44.294  1.00 19.32 ? 492 ALA A CB  1 
ATOM   3996 N N   . MET A 1 493 ? 33.904 -9.207  43.212  1.00 19.20 ? 493 MET A N   1 
ATOM   3997 C CA  . MET A 1 493 ? 32.749 -8.331  43.306  1.00 19.38 ? 493 MET A CA  1 
ATOM   3998 C C   . MET A 1 493 ? 31.464 -9.154  43.206  1.00 19.08 ? 493 MET A C   1 
ATOM   3999 O O   . MET A 1 493 ? 30.503 -8.879  43.921  1.00 19.45 ? 493 MET A O   1 
ATOM   4000 C CB  . MET A 1 493 ? 32.801 -7.266  42.202  1.00 20.06 ? 493 MET A CB  1 
ATOM   4001 C CG  . MET A 1 493 ? 31.861 -6.092  42.410  1.00 20.46 ? 493 MET A CG  1 
ATOM   4002 S SD  . MET A 1 493 ? 31.918 -4.911  41.046  1.00 21.36 ? 493 MET A SD  1 
ATOM   4003 C CE  . MET A 1 493 ? 33.559 -4.236  41.336  1.00 20.51 ? 493 MET A CE  1 
ATOM   4004 N N   . ALA A 1 494 ? 31.467 -10.177 42.338  1.00 18.74 ? 494 ALA A N   1 
ATOM   4005 C CA  . ALA A 1 494 ? 30.291 -10.998 42.085  1.00 18.99 ? 494 ALA A CA  1 
ATOM   4006 C C   . ALA A 1 494 ? 29.994 -11.912 43.275  1.00 18.96 ? 494 ALA A C   1 
ATOM   4007 O O   . ALA A 1 494 ? 28.831 -12.127 43.611  1.00 17.89 ? 494 ALA A O   1 
ATOM   4008 C CB  . ALA A 1 494 ? 30.481 -11.797 40.812  1.00 19.18 ? 494 ALA A CB  1 
ATOM   4009 N N   . GLU A 1 495 ? 31.050 -12.459 43.891  1.00 19.47 ? 495 GLU A N   1 
ATOM   4010 C CA  . GLU A 1 495 ? 30.939 -13.205 45.136  1.00 19.92 ? 495 GLU A CA  1 
ATOM   4011 C C   . GLU A 1 495 ? 30.338 -12.319 46.228  1.00 19.42 ? 495 GLU A C   1 
ATOM   4012 O O   . GLU A 1 495 ? 29.456 -12.752 46.963  1.00 19.54 ? 495 GLU A O   1 
ATOM   4013 C CB  . GLU A 1 495 ? 32.312 -13.733 45.562  1.00 21.20 ? 495 GLU A CB  1 
ATOM   4014 C CG  . GLU A 1 495 ? 32.314 -14.473 46.900  1.00 22.36 ? 495 GLU A CG  1 
ATOM   4015 C CD  . GLU A 1 495 ? 33.690 -14.824 47.452  1.00 23.73 ? 495 GLU A CD  1 
ATOM   4016 O OE1 . GLU A 1 495 ? 34.699 -14.647 46.738  1.00 24.59 ? 495 GLU A OE1 1 
ATOM   4017 O OE2 . GLU A 1 495 ? 33.758 -15.258 48.621  1.00 25.17 ? 495 GLU A OE2 1 
ATOM   4018 N N   . ALA A 1 496 ? 30.827 -11.079 46.337  1.00 19.21 ? 496 ALA A N   1 
ATOM   4019 C CA  . ALA A 1 496 ? 30.404 -10.178 47.399  1.00 19.01 ? 496 ALA A CA  1 
ATOM   4020 C C   . ALA A 1 496 ? 28.971 -9.688  47.183  1.00 18.69 ? 496 ALA A C   1 
ATOM   4021 O O   . ALA A 1 496 ? 28.309 -9.325  48.150  1.00 17.54 ? 496 ALA A O   1 
ATOM   4022 C CB  . ALA A 1 496 ? 31.364 -9.016  47.506  1.00 19.10 ? 496 ALA A CB  1 
ATOM   4023 N N   . THR A 1 497 ? 28.501 -9.667  45.926  1.00 18.89 ? 497 THR A N   1 
ATOM   4024 C CA  . THR A 1 497 ? 27.172 -9.156  45.617  1.00 19.49 ? 497 THR A CA  1 
ATOM   4025 C C   . THR A 1 497 ? 26.241 -10.301 45.221  1.00 19.72 ? 497 THR A C   1 
ATOM   4026 O O   . THR A 1 497 ? 25.155 -10.056 44.702  1.00 19.63 ? 497 THR A O   1 
ATOM   4027 C CB  . THR A 1 497 ? 27.256 -8.076  44.535  1.00 19.30 ? 497 THR A CB  1 
ATOM   4028 O OG1 . THR A 1 497 ? 27.832 -8.666  43.374  1.00 19.25 ? 497 THR A OG1 1 
ATOM   4029 C CG2 . THR A 1 497 ? 28.078 -6.884  44.990  1.00 19.65 ? 497 THR A CG2 1 
ATOM   4030 N N   . GLU A 1 498 ? 26.666 -11.540 45.506  1.00 20.77 ? 498 GLU A N   1 
ATOM   4031 C CA  . GLU A 1 498 ? 25.856 -12.734 45.309  1.00 21.74 ? 498 GLU A CA  1 
ATOM   4032 C C   . GLU A 1 498 ? 25.458 -12.884 43.840  1.00 21.15 ? 498 GLU A C   1 
ATOM   4033 O O   . GLU A 1 498 ? 24.325 -13.259 43.542  1.00 21.47 ? 498 GLU A O   1 
ATOM   4034 C CB  . GLU A 1 498 ? 24.619 -12.737 46.214  1.00 23.09 ? 498 GLU A CB  1 
ATOM   4035 C CG  . GLU A 1 498 ? 24.935 -12.595 47.702  1.00 24.68 ? 498 GLU A CG  1 
ATOM   4036 C CD  . GLU A 1 498 ? 24.825 -11.197 48.285  1.00 26.82 ? 498 GLU A CD  1 
ATOM   4037 O OE1 . GLU A 1 498 ? 25.280 -11.002 49.435  1.00 27.78 ? 498 GLU A OE1 1 
ATOM   4038 O OE2 . GLU A 1 498 ? 24.265 -10.306 47.610  1.00 28.93 ? 498 GLU A OE2 1 
ATOM   4039 N N   . ARG A 1 499 ? 26.398 -12.596 42.932  1.00 20.76 ? 499 ARG A N   1 
ATOM   4040 C CA  . ARG A 1 499 ? 26.170 -12.719 41.501  1.00 21.07 ? 499 ARG A CA  1 
ATOM   4041 C C   . ARG A 1 499 ? 26.979 -13.885 40.932  1.00 21.89 ? 499 ARG A C   1 
ATOM   4042 O O   . ARG A 1 499 ? 27.165 -13.970 39.719  1.00 21.78 ? 499 ARG A O   1 
ATOM   4043 C CB  . ARG A 1 499 ? 26.522 -11.399 40.805  1.00 20.48 ? 499 ARG A CB  1 
ATOM   4044 C CG  . ARG A 1 499 ? 25.646 -10.237 41.249  1.00 19.87 ? 499 ARG A CG  1 
ATOM   4045 C CD  . ARG A 1 499 ? 25.660 -9.088  40.259  1.00 19.67 ? 499 ARG A CD  1 
ATOM   4046 N NE  . ARG A 1 499 ? 24.721 -8.038  40.666  1.00 19.48 ? 499 ARG A NE  1 
ATOM   4047 C CZ  . ARG A 1 499 ? 23.539 -7.787  40.105  1.00 19.25 ? 499 ARG A CZ  1 
ATOM   4048 N NH1 . ARG A 1 499 ? 23.059 -8.585  39.166  1.00 19.11 ? 499 ARG A NH1 1 
ATOM   4049 N NH2 . ARG A 1 499 ? 22.816 -6.762  40.520  1.00 18.68 ? 499 ARG A NH2 1 
ATOM   4050 N N   . LEU A 1 500 ? 27.454 -14.780 41.811  1.00 22.74 ? 500 LEU A N   1 
ATOM   4051 C CA  . LEU A 1 500 ? 28.168 -15.979 41.398  1.00 23.30 ? 500 LEU A CA  1 
ATOM   4052 C C   . LEU A 1 500 ? 27.199 -17.174 41.374  1.00 24.73 ? 500 LEU A C   1 
ATOM   4053 O O   . LEU A 1 500 ? 26.907 -17.715 42.468  1.00 25.06 ? 500 LEU A O   1 
ATOM   4054 C CB  . LEU A 1 500 ? 29.370 -16.257 42.303  1.00 22.94 ? 500 LEU A CB  1 
ATOM   4055 C CG  . LEU A 1 500 ? 30.668 -15.519 41.960  1.00 22.43 ? 500 LEU A CG  1 
ATOM   4056 C CD1 . LEU A 1 500 ? 31.812 -16.108 42.770  1.00 22.05 ? 500 LEU A CD1 1 
ATOM   4057 C CD2 . LEU A 1 500 ? 30.990 -15.561 40.472  1.00 22.40 ? 500 LEU A CD2 1 
ATOM   4058 O OXT . LEU A 1 500 ? 26.780 -17.531 40.254  1.00 26.24 ? 500 LEU A OXT 1 
HETATM 4059 O O   . HOH B 2 .   ? 33.270 -19.380 15.567  1.00 14.36 ? 601 HOH A O   1 
HETATM 4060 O O   . HOH B 2 .   ? 20.497 -2.535  12.676  1.00 22.66 ? 602 HOH A O   1 
HETATM 4061 O O   . HOH B 2 .   ? 34.664 -1.894  16.787  1.00 9.32  ? 603 HOH A O   1 
HETATM 4062 O O   . HOH B 2 .   ? 24.224 11.626  36.252  1.00 19.42 ? 604 HOH A O   1 
HETATM 4063 O O   . HOH B 2 .   ? 10.999 1.573   41.156  1.00 29.37 ? 605 HOH A O   1 
HETATM 4064 O O   . HOH B 2 .   ? 32.618 -25.319 -7.358  1.00 23.13 ? 606 HOH A O   1 
HETATM 4065 O O   . HOH B 2 .   ? 27.133 -10.284 2.395   1.00 17.58 ? 607 HOH A O   1 
HETATM 4066 O O   . HOH B 2 .   ? 5.249  -16.024 10.477  1.00 23.98 ? 608 HOH A O   1 
HETATM 4067 O O   . HOH B 2 .   ? 25.529 0.884   8.605   1.00 15.23 ? 609 HOH A O   1 
HETATM 4068 O O   . HOH B 2 .   ? 39.949 -11.832 22.766  1.00 18.10 ? 610 HOH A O   1 
HETATM 4069 O O   . HOH B 2 .   ? 25.023 -22.855 17.665  1.00 27.84 ? 611 HOH A O   1 
HETATM 4070 O O   . HOH B 2 .   ? 24.602 -18.710 42.357  1.00 39.06 ? 612 HOH A O   1 
HETATM 4071 O O   . HOH B 2 .   ? 16.111 -10.746 2.835   1.00 36.58 ? 613 HOH A O   1 
HETATM 4072 O O   . HOH B 2 .   ? 30.494 0.002   7.068   1.00 10.68 ? 614 HOH A O   1 
HETATM 4073 O O   . HOH B 2 .   ? 19.120 -0.883  10.445  1.00 29.26 ? 615 HOH A O   1 
HETATM 4074 O O   . HOH B 2 .   ? 23.111 -7.989  46.583  1.00 28.60 ? 616 HOH A O   1 
HETATM 4075 O O   . HOH B 2 .   ? 44.134 4.765   8.925   1.00 31.33 ? 617 HOH A O   1 
HETATM 4076 O O   . HOH B 2 .   ? 25.649 2.987   3.045   1.00 22.04 ? 618 HOH A O   1 
HETATM 4077 O O   . HOH B 2 .   ? 42.447 -7.740  25.414  1.00 32.37 ? 619 HOH A O   1 
HETATM 4078 O O   . HOH B 2 .   ? 22.448 3.869   19.377  1.00 32.23 ? 620 HOH A O   1 
HETATM 4079 O O   . HOH B 2 .   ? 46.020 9.019   37.001  1.00 29.12 ? 621 HOH A O   1 
HETATM 4080 O O   . HOH B 2 .   ? 16.042 -4.746  6.919   1.00 25.28 ? 622 HOH A O   1 
HETATM 4081 O O   . HOH B 2 .   ? 39.103 -12.698 8.883   1.00 36.63 ? 623 HOH A O   1 
HETATM 4082 O O   . HOH B 2 .   ? 11.377 2.541   24.630  1.00 20.60 ? 624 HOH A O   1 
HETATM 4083 O O   . HOH B 2 .   ? 44.459 5.222   44.366  1.00 28.58 ? 625 HOH A O   1 
HETATM 4084 O O   . HOH B 2 .   ? 4.342  13.929  22.504  1.00 19.68 ? 626 HOH A O   1 
HETATM 4085 O O   . HOH B 2 .   ? 46.543 -6.171  13.839  1.00 27.14 ? 627 HOH A O   1 
HETATM 4086 O O   . HOH B 2 .   ? 34.239 16.750  35.472  1.00 17.36 ? 628 HOH A O   1 
HETATM 4087 O O   . HOH B 2 .   ? 15.015 3.184   32.202  1.00 14.76 ? 629 HOH A O   1 
HETATM 4088 O O   . HOH B 2 .   ? 38.206 -13.688 17.028  1.00 16.30 ? 630 HOH A O   1 
HETATM 4089 O O   . HOH B 2 .   ? -4.539 -11.250 12.696  1.00 47.37 ? 631 HOH A O   1 
HETATM 4090 O O   . HOH B 2 .   ? 26.599 -4.901  12.808  1.00 17.61 ? 632 HOH A O   1 
HETATM 4091 O O   . HOH B 2 .   ? 0.237  0.787   10.603  1.00 28.88 ? 633 HOH A O   1 
HETATM 4092 O O   . HOH B 2 .   ? 9.569  -2.484  43.904  1.00 29.42 ? 634 HOH A O   1 
HETATM 4093 O O   . HOH B 2 .   ? 44.199 -5.885  13.395  1.00 14.56 ? 635 HOH A O   1 
HETATM 4094 O O   . HOH B 2 .   ? 31.669 -19.191 -12.716 1.00 32.68 ? 636 HOH A O   1 
HETATM 4095 O O   . HOH B 2 .   ? 22.213 -30.807 -2.409  1.00 40.57 ? 637 HOH A O   1 
HETATM 4096 O O   . HOH B 2 .   ? 38.086 2.058   0.817   1.00 24.35 ? 638 HOH A O   1 
HETATM 4097 O O   . HOH B 2 .   ? 40.117 -18.221 14.843  1.00 25.95 ? 639 HOH A O   1 
HETATM 4098 O O   . HOH B 2 .   ? 30.026 -0.564  -6.749  1.00 34.10 ? 640 HOH A O   1 
HETATM 4099 O O   . HOH B 2 .   ? 39.533 -11.364 16.377  1.00 18.12 ? 641 HOH A O   1 
HETATM 4100 O O   . HOH B 2 .   ? 44.759 -15.912 24.251  1.00 24.11 ? 642 HOH A O   1 
HETATM 4101 O O   . HOH B 2 .   ? 34.315 -26.491 24.929  1.00 38.86 ? 643 HOH A O   1 
HETATM 4102 O O   . HOH B 2 .   ? 44.690 -9.707  0.871   1.00 19.23 ? 644 HOH A O   1 
HETATM 4103 O O   . HOH B 2 .   ? 31.596 -18.675 35.264  1.00 32.22 ? 645 HOH A O   1 
HETATM 4104 O O   . HOH B 2 .   ? 12.345 7.068   40.974  1.00 26.98 ? 646 HOH A O   1 
HETATM 4105 O O   . HOH B 2 .   ? 10.830 -11.073 -1.559  1.00 37.19 ? 647 HOH A O   1 
HETATM 4106 O O   . HOH B 2 .   ? 0.076  -14.343 7.227   1.00 23.02 ? 648 HOH A O   1 
HETATM 4107 O O   . HOH B 2 .   ? 35.746 7.608   20.013  1.00 17.18 ? 649 HOH A O   1 
HETATM 4108 O O   . HOH B 2 .   ? 29.583 15.094  48.088  1.00 46.96 ? 650 HOH A O   1 
HETATM 4109 O O   . HOH B 2 .   ? 18.616 -9.616  41.938  1.00 16.38 ? 651 HOH A O   1 
HETATM 4110 O O   . HOH B 2 .   ? 43.104 -1.293  32.930  1.00 52.78 ? 652 HOH A O   1 
HETATM 4111 O O   . HOH B 2 .   ? 35.748 3.945   32.147  1.00 14.51 ? 653 HOH A O   1 
HETATM 4112 O O   . HOH B 2 .   ? 32.462 7.519   47.925  1.00 13.25 ? 654 HOH A O   1 
HETATM 4113 O O   . HOH B 2 .   ? 34.472 0.983   49.050  1.00 33.58 ? 655 HOH A O   1 
HETATM 4114 O O   . HOH B 2 .   ? 36.878 -12.990 47.116  1.00 26.03 ? 656 HOH A O   1 
HETATM 4115 O O   . HOH B 2 .   ? 9.730  -3.338  -4.101  1.00 28.87 ? 657 HOH A O   1 
HETATM 4116 O O   . HOH B 2 .   ? 34.516 4.119   18.336  1.00 12.40 ? 658 HOH A O   1 
HETATM 4117 O O   . HOH B 2 .   ? 28.449 12.840  25.548  1.00 22.94 ? 659 HOH A O   1 
HETATM 4118 O O   . HOH B 2 .   ? 27.647 -26.444 24.162  1.00 18.49 ? 660 HOH A O   1 
HETATM 4119 O O   . HOH B 2 .   ? 33.983 -21.213 36.500  1.00 20.45 ? 661 HOH A O   1 
HETATM 4120 O O   . HOH B 2 .   ? 27.565 -24.622 8.181   1.00 16.88 ? 662 HOH A O   1 
HETATM 4121 O O   . HOH B 2 .   ? 12.832 -0.691  34.571  1.00 20.68 ? 663 HOH A O   1 
HETATM 4122 O O   . HOH B 2 .   ? 19.315 -18.559 -0.832  1.00 28.24 ? 664 HOH A O   1 
HETATM 4123 O O   . HOH B 2 .   ? 28.775 6.428   12.980  1.00 22.63 ? 665 HOH A O   1 
HETATM 4124 O O   . HOH B 2 .   ? 15.080 17.654  27.130  1.00 31.40 ? 666 HOH A O   1 
HETATM 4125 O O   . HOH B 2 .   ? 8.568  6.840   15.294  1.00 12.03 ? 667 HOH A O   1 
HETATM 4126 O O   . HOH B 2 .   ? 30.772 -3.028  10.158  1.00 16.04 ? 668 HOH A O   1 
HETATM 4127 O O   . HOH B 2 .   ? 3.256  -13.247 6.282   1.00 28.37 ? 669 HOH A O   1 
HETATM 4128 O O   . HOH B 2 .   ? 34.702 -5.436  45.576  1.00 44.17 ? 670 HOH A O   1 
HETATM 4129 O O   . HOH B 2 .   ? 34.664 -11.682 47.369  1.00 15.54 ? 671 HOH A O   1 
HETATM 4130 O O   . HOH B 2 .   ? 44.074 -15.362 -2.264  1.00 30.03 ? 672 HOH A O   1 
HETATM 4131 O O   . HOH B 2 .   ? -3.355 1.110   16.895  1.00 33.99 ? 673 HOH A O   1 
HETATM 4132 O O   . HOH B 2 .   ? 16.330 14.490  46.661  1.00 23.96 ? 674 HOH A O   1 
HETATM 4133 O O   . HOH B 2 .   ? 12.117 -10.937 28.799  1.00 25.93 ? 675 HOH A O   1 
HETATM 4134 O O   . HOH B 2 .   ? 20.917 -11.651 12.191  1.00 31.62 ? 676 HOH A O   1 
HETATM 4135 O O   . HOH B 2 .   ? 43.097 7.980   30.681  1.00 27.13 ? 677 HOH A O   1 
HETATM 4136 O O   . HOH B 2 .   ? 22.825 -8.254  18.067  1.00 14.27 ? 678 HOH A O   1 
HETATM 4137 O O   . HOH B 2 .   ? 42.810 -18.364 30.605  1.00 22.52 ? 679 HOH A O   1 
HETATM 4138 O O   . HOH B 2 .   ? 8.609  -14.330 28.917  1.00 31.77 ? 680 HOH A O   1 
HETATM 4139 O O   . HOH B 2 .   ? 32.348 -2.731  22.170  1.00 12.52 ? 681 HOH A O   1 
HETATM 4140 O O   . HOH B 2 .   ? 14.798 5.556   21.733  1.00 21.73 ? 682 HOH A O   1 
HETATM 4141 O O   . HOH B 2 .   ? 24.911 -12.830 51.815  1.00 37.60 ? 683 HOH A O   1 
HETATM 4142 O O   . HOH B 2 .   ? 21.131 1.070   5.375   1.00 27.27 ? 684 HOH A O   1 
HETATM 4143 O O   . HOH B 2 .   ? 31.118 3.548   24.773  1.00 21.75 ? 685 HOH A O   1 
HETATM 4144 O O   . HOH B 2 .   ? 34.263 -1.135  43.593  1.00 24.72 ? 686 HOH A O   1 
HETATM 4145 O O   . HOH B 2 .   ? 24.913 -0.580  25.214  1.00 8.13  ? 687 HOH A O   1 
HETATM 4146 O O   . HOH B 2 .   ? 30.265 -28.206 -6.446  1.00 23.44 ? 688 HOH A O   1 
HETATM 4147 O O   . HOH B 2 .   ? 23.274 15.053  32.941  1.00 27.63 ? 689 HOH A O   1 
HETATM 4148 O O   . HOH B 2 .   ? 28.147 10.222  28.523  1.00 19.47 ? 690 HOH A O   1 
HETATM 4149 O O   . HOH B 2 .   ? -2.602 -7.254  3.152   1.00 32.58 ? 691 HOH A O   1 
HETATM 4150 O O   . HOH B 2 .   ? 52.974 -8.206  4.832   1.00 22.47 ? 692 HOH A O   1 
HETATM 4151 O O   . HOH B 2 .   ? 35.620 1.292   44.634  1.00 22.37 ? 693 HOH A O   1 
HETATM 4152 O O   . HOH B 2 .   ? 46.974 -13.472 38.792  1.00 18.03 ? 694 HOH A O   1 
HETATM 4153 O O   . HOH B 2 .   ? 34.912 8.269   48.128  1.00 9.93  ? 695 HOH A O   1 
HETATM 4154 O O   . HOH B 2 .   ? -0.535 -11.984 3.692   1.00 40.35 ? 696 HOH A O   1 
HETATM 4155 O O   . HOH B 2 .   ? 25.789 10.602  26.216  1.00 25.97 ? 697 HOH A O   1 
HETATM 4156 O O   . HOH B 2 .   ? 36.810 -21.107 24.719  1.00 25.12 ? 698 HOH A O   1 
HETATM 4157 O O   . HOH B 2 .   ? 49.026 -6.867  28.051  1.00 40.25 ? 699 HOH A O   1 
HETATM 4158 O O   . HOH B 2 .   ? 13.645 -25.437 2.344   1.00 23.64 ? 700 HOH A O   1 
HETATM 4159 O O   . HOH B 2 .   ? 23.278 -20.463 27.995  1.00 21.59 ? 701 HOH A O   1 
HETATM 4160 O O   . HOH B 2 .   ? 17.352 11.623  34.870  1.00 34.82 ? 702 HOH A O   1 
HETATM 4161 O O   . HOH B 2 .   ? 32.891 0.150   53.714  1.00 15.29 ? 703 HOH A O   1 
HETATM 4162 O O   . HOH B 2 .   ? 46.925 0.170   1.559   1.00 29.05 ? 704 HOH A O   1 
HETATM 4163 O O   . HOH B 2 .   ? 9.334  6.097   36.400  1.00 26.40 ? 705 HOH A O   1 
HETATM 4164 O O   . HOH B 2 .   ? 31.008 -3.988  -1.601  1.00 37.69 ? 706 HOH A O   1 
HETATM 4165 O O   . HOH B 2 .   ? 47.042 -4.022  36.224  1.00 39.10 ? 707 HOH A O   1 
HETATM 4166 O O   . HOH B 2 .   ? 6.015  0.558   -2.067  1.00 19.77 ? 708 HOH A O   1 
HETATM 4167 O O   . HOH B 2 .   ? 44.423 -12.498 25.271  1.00 26.30 ? 709 HOH A O   1 
HETATM 4168 O O   . HOH B 2 .   ? 12.728 -14.700 -2.874  1.00 14.44 ? 710 HOH A O   1 
HETATM 4169 O O   . HOH B 2 .   ? 16.470 7.879   -8.274  1.00 21.17 ? 711 HOH A O   1 
HETATM 4170 O O   . HOH B 2 .   ? 40.079 2.236   48.476  1.00 40.28 ? 712 HOH A O   1 
HETATM 4171 O O   . HOH B 2 .   ? 23.804 4.959   9.980   1.00 25.59 ? 713 HOH A O   1 
HETATM 4172 O O   . HOH B 2 .   ? 3.551  10.085  24.859  1.00 30.90 ? 714 HOH A O   1 
HETATM 4173 O O   . HOH B 2 .   ? 20.318 -29.292 -0.742  1.00 23.66 ? 715 HOH A O   1 
HETATM 4174 O O   . HOH B 2 .   ? 13.375 13.108  24.654  1.00 27.13 ? 716 HOH A O   1 
HETATM 4175 O O   . HOH B 2 .   ? 18.443 8.769   28.017  1.00 28.16 ? 717 HOH A O   1 
HETATM 4176 O O   . HOH B 2 .   ? 3.659  0.129   -2.231  1.00 27.82 ? 718 HOH A O   1 
HETATM 4177 O O   . HOH B 2 .   ? 14.465 11.860  22.557  1.00 22.33 ? 719 HOH A O   1 
HETATM 4178 O O   . HOH B 2 .   ? 50.126 2.148   10.318  1.00 39.56 ? 720 HOH A O   1 
HETATM 4179 O O   . HOH B 2 .   ? 15.488 11.119  29.807  1.00 30.60 ? 721 HOH A O   1 
HETATM 4180 O O   . HOH B 2 .   ? 42.908 -1.399  -1.632  1.00 27.66 ? 722 HOH A O   1 
HETATM 4181 O O   . HOH B 2 .   ? 10.663 -19.205 30.596  1.00 31.97 ? 723 HOH A O   1 
HETATM 4182 O O   . HOH B 2 .   ? 55.107 -18.016 -1.302  1.00 31.60 ? 724 HOH A O   1 
HETATM 4183 O O   . HOH B 2 .   ? 35.381 -19.244 44.314  1.00 30.86 ? 725 HOH A O   1 
HETATM 4184 O O   . HOH B 2 .   ? 6.779  -14.666 3.311   1.00 19.94 ? 726 HOH A O   1 
HETATM 4185 O O   . HOH B 2 .   ? 36.402 16.499  42.832  1.00 32.23 ? 727 HOH A O   1 
HETATM 4186 O O   . HOH B 2 .   ? 36.243 -5.983  -4.785  1.00 22.83 ? 728 HOH A O   1 
HETATM 4187 O O   . HOH B 2 .   ? 7.851  11.328  24.757  1.00 32.03 ? 729 HOH A O   1 
HETATM 4188 O O   . HOH B 2 .   ? 20.352 8.128   4.837   1.00 25.38 ? 730 HOH A O   1 
HETATM 4189 O O   . HOH B 2 .   ? 28.178 -2.541  53.314  1.00 33.09 ? 731 HOH A O   1 
HETATM 4190 O O   . HOH B 2 .   ? -1.331 -12.171 15.673  1.00 31.33 ? 732 HOH A O   1 
HETATM 4191 O O   . HOH B 2 .   ? 21.601 6.966   17.616  1.00 17.55 ? 733 HOH A O   1 
HETATM 4192 O O   . HOH B 2 .   ? 16.095 19.062  43.215  1.00 22.97 ? 734 HOH A O   1 
HETATM 4193 O O   . HOH B 2 .   ? -0.603 -12.591 27.030  1.00 27.34 ? 735 HOH A O   1 
HETATM 4194 O O   . HOH B 2 .   ? 39.204 -26.114 21.848  1.00 30.51 ? 736 HOH A O   1 
HETATM 4195 O O   . HOH B 2 .   ? 41.864 -29.350 -7.866  1.00 31.28 ? 737 HOH A O   1 
HETATM 4196 O O   . HOH B 2 .   ? 33.555 17.004  14.099  1.00 24.88 ? 738 HOH A O   1 
HETATM 4197 O O   . HOH B 2 .   ? -5.030 7.559   15.891  1.00 24.03 ? 739 HOH A O   1 
HETATM 4198 O O   . HOH B 2 .   ? 45.859 -3.970  0.194   1.00 38.68 ? 740 HOH A O   1 
HETATM 4199 O O   . HOH B 2 .   ? 38.339 12.979  22.064  1.00 34.87 ? 741 HOH A O   1 
HETATM 4200 O O   . HOH B 2 .   ? 47.915 -7.423  -1.540  1.00 26.85 ? 742 HOH A O   1 
HETATM 4201 O O   . HOH B 2 .   ? 17.987 21.157  38.321  1.00 31.03 ? 743 HOH A O   1 
HETATM 4202 O O   . HOH B 2 .   ? -0.414 -16.788 28.847  1.00 38.52 ? 744 HOH A O   1 
HETATM 4203 O O   . HOH B 2 .   ? -5.080 10.440  22.552  1.00 31.71 ? 745 HOH A O   1 
HETATM 4204 O O   . HOH B 2 .   ? 8.670  -19.528 -11.857 1.00 31.65 ? 746 HOH A O   1 
HETATM 4205 O O   . HOH B 2 .   ? 21.022 8.449   12.920  1.00 24.93 ? 747 HOH A O   1 
# 
