data_8YP7
# 
_entry.id   8YP7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8YP7         pdb_00008yp7 10.2210/pdb8yp7/pdb 
WWPDB D_1300046083 ?            ?                   
# 
_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       2025-03-19 
_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                        8YP7 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-15 
_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              youcai@qibebt.ac.cn 
_pdbx_contact_author.name_first         You 
_pdbx_contact_author.name_last          Cai 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4817-7628 
# 
_audit_author.name               'Cai, Y.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-4817-7628 
# 
_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                     'Crystal structure of glucosyltransferase RrUGT3' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Cai, Y.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0002-4817-7628 
# 
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 Glycosyltransferase 52093.316 1   2.4.1.- ? ? ? 
2 water   nat water               18.015    160 ?       ? ? ? 
# 
_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       
;GAMAGTPHIAILPSPGMGHLIPMAEFAKRLVHHHNFSITFVIPTDGPPSSAYQQVLTSLPSSIDHIFLPQVDLTDVVSQS
PAHPRIETLISLTVARSLSSLRTTLSSLQSSKNLVSLVVDLFGTDAFDPAIELGISPYIFFPSTAMTLSLFLYMPQLDKS
VTCEFRHMTDLVRIPGCVPVRGSDLFDPVQDRTDEAYKWVIHHSNRYPMAEGVIENSFMELEHGALKYLQTVQSGKPPVY
AVGPLIKMDYDVDDSGSKIIEWLDDQPVGSVLFVSFGSGGTLSYEQMTELAHGLESSQQRFLWVVRSPNQIPNSTYFSVQ
SQKDPLAYLPEGFLNRTEGRGLVVSNWAPQAQILSHGSTGGFMSHCGWNSILESVVHGVPIIAWPLYAEQKMNSIIVVED
VKVALRPAGVGERVVERSEITAVVKALMEGEEGKKVRNRMKELKEAAARAVSDDGASTIAIADLAQKWRSSMKH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAMAGTPHIAILPSPGMGHLIPMAEFAKRLVHHHNFSITFVIPTDGPPSSAYQQVLTSLPSSIDHIFLPQVDLTDVVSQS
PAHPRIETLISLTVARSLSSLRTTLSSLQSSKNLVSLVVDLFGTDAFDPAIELGISPYIFFPSTAMTLSLFLYMPQLDKS
VTCEFRHMTDLVRIPGCVPVRGSDLFDPVQDRTDEAYKWVIHHSNRYPMAEGVIENSFMELEHGALKYLQTVQSGKPPVY
AVGPLIKMDYDVDDSGSKIIEWLDDQPVGSVLFVSFGSGGTLSYEQMTELAHGLESSQQRFLWVVRSPNQIPNSTYFSVQ
SQKDPLAYLPEGFLNRTEGRGLVVSNWAPQAQILSHGSTGGFMSHCGWNSILESVVHGVPIIAWPLYAEQKMNSIIVVED
VKVALRPAGVGERVVERSEITAVVKALMEGEEGKKVRNRMKELKEAAARAVSDDGASTIAIADLAQKWRSSMKH
;
_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   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   ALA n 
1 5   GLY n 
1 6   THR n 
1 7   PRO n 
1 8   HIS n 
1 9   ILE n 
1 10  ALA n 
1 11  ILE n 
1 12  LEU n 
1 13  PRO n 
1 14  SER n 
1 15  PRO n 
1 16  GLY n 
1 17  MET n 
1 18  GLY n 
1 19  HIS n 
1 20  LEU n 
1 21  ILE n 
1 22  PRO n 
1 23  MET n 
1 24  ALA n 
1 25  GLU n 
1 26  PHE n 
1 27  ALA n 
1 28  LYS n 
1 29  ARG n 
1 30  LEU n 
1 31  VAL n 
1 32  HIS n 
1 33  HIS n 
1 34  HIS n 
1 35  ASN n 
1 36  PHE n 
1 37  SER n 
1 38  ILE n 
1 39  THR n 
1 40  PHE n 
1 41  VAL n 
1 42  ILE n 
1 43  PRO n 
1 44  THR n 
1 45  ASP n 
1 46  GLY n 
1 47  PRO n 
1 48  PRO n 
1 49  SER n 
1 50  SER n 
1 51  ALA n 
1 52  TYR n 
1 53  GLN n 
1 54  GLN n 
1 55  VAL n 
1 56  LEU n 
1 57  THR n 
1 58  SER n 
1 59  LEU n 
1 60  PRO n 
1 61  SER n 
1 62  SER n 
1 63  ILE n 
1 64  ASP n 
1 65  HIS n 
1 66  ILE n 
1 67  PHE n 
1 68  LEU n 
1 69  PRO n 
1 70  GLN n 
1 71  VAL n 
1 72  ASP n 
1 73  LEU n 
1 74  THR n 
1 75  ASP n 
1 76  VAL n 
1 77  VAL n 
1 78  SER n 
1 79  GLN n 
1 80  SER n 
1 81  PRO n 
1 82  ALA n 
1 83  HIS n 
1 84  PRO n 
1 85  ARG n 
1 86  ILE n 
1 87  GLU n 
1 88  THR n 
1 89  LEU n 
1 90  ILE n 
1 91  SER n 
1 92  LEU n 
1 93  THR n 
1 94  VAL n 
1 95  ALA n 
1 96  ARG n 
1 97  SER n 
1 98  LEU n 
1 99  SER n 
1 100 SER n 
1 101 LEU n 
1 102 ARG n 
1 103 THR n 
1 104 THR n 
1 105 LEU n 
1 106 SER n 
1 107 SER n 
1 108 LEU n 
1 109 GLN n 
1 110 SER n 
1 111 SER n 
1 112 LYS n 
1 113 ASN n 
1 114 LEU n 
1 115 VAL n 
1 116 SER n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 ASP n 
1 121 LEU n 
1 122 PHE n 
1 123 GLY n 
1 124 THR n 
1 125 ASP n 
1 126 ALA n 
1 127 PHE n 
1 128 ASP n 
1 129 PRO n 
1 130 ALA n 
1 131 ILE n 
1 132 GLU n 
1 133 LEU n 
1 134 GLY n 
1 135 ILE n 
1 136 SER n 
1 137 PRO n 
1 138 TYR n 
1 139 ILE n 
1 140 PHE n 
1 141 PHE n 
1 142 PRO n 
1 143 SER n 
1 144 THR n 
1 145 ALA n 
1 146 MET n 
1 147 THR n 
1 148 LEU n 
1 149 SER n 
1 150 LEU n 
1 151 PHE n 
1 152 LEU n 
1 153 TYR n 
1 154 MET n 
1 155 PRO n 
1 156 GLN n 
1 157 LEU n 
1 158 ASP n 
1 159 LYS n 
1 160 SER n 
1 161 VAL n 
1 162 THR n 
1 163 CYS n 
1 164 GLU n 
1 165 PHE n 
1 166 ARG n 
1 167 HIS n 
1 168 MET n 
1 169 THR n 
1 170 ASP n 
1 171 LEU n 
1 172 VAL n 
1 173 ARG n 
1 174 ILE n 
1 175 PRO n 
1 176 GLY n 
1 177 CYS n 
1 178 VAL n 
1 179 PRO n 
1 180 VAL n 
1 181 ARG n 
1 182 GLY n 
1 183 SER n 
1 184 ASP n 
1 185 LEU n 
1 186 PHE n 
1 187 ASP n 
1 188 PRO n 
1 189 VAL n 
1 190 GLN n 
1 191 ASP n 
1 192 ARG n 
1 193 THR n 
1 194 ASP n 
1 195 GLU n 
1 196 ALA n 
1 197 TYR n 
1 198 LYS n 
1 199 TRP n 
1 200 VAL n 
1 201 ILE n 
1 202 HIS n 
1 203 HIS n 
1 204 SER n 
1 205 ASN n 
1 206 ARG n 
1 207 TYR n 
1 208 PRO n 
1 209 MET n 
1 210 ALA n 
1 211 GLU n 
1 212 GLY n 
1 213 VAL n 
1 214 ILE n 
1 215 GLU n 
1 216 ASN n 
1 217 SER n 
1 218 PHE n 
1 219 MET n 
1 220 GLU n 
1 221 LEU n 
1 222 GLU n 
1 223 HIS n 
1 224 GLY n 
1 225 ALA n 
1 226 LEU n 
1 227 LYS n 
1 228 TYR n 
1 229 LEU n 
1 230 GLN n 
1 231 THR n 
1 232 VAL n 
1 233 GLN n 
1 234 SER n 
1 235 GLY n 
1 236 LYS n 
1 237 PRO n 
1 238 PRO n 
1 239 VAL n 
1 240 TYR n 
1 241 ALA n 
1 242 VAL n 
1 243 GLY n 
1 244 PRO n 
1 245 LEU n 
1 246 ILE n 
1 247 LYS n 
1 248 MET n 
1 249 ASP n 
1 250 TYR n 
1 251 ASP n 
1 252 VAL n 
1 253 ASP n 
1 254 ASP n 
1 255 SER n 
1 256 GLY n 
1 257 SER n 
1 258 LYS n 
1 259 ILE n 
1 260 ILE n 
1 261 GLU n 
1 262 TRP n 
1 263 LEU n 
1 264 ASP n 
1 265 ASP n 
1 266 GLN n 
1 267 PRO n 
1 268 VAL n 
1 269 GLY n 
1 270 SER n 
1 271 VAL n 
1 272 LEU n 
1 273 PHE n 
1 274 VAL n 
1 275 SER n 
1 276 PHE n 
1 277 GLY n 
1 278 SER n 
1 279 GLY n 
1 280 GLY n 
1 281 THR n 
1 282 LEU n 
1 283 SER n 
1 284 TYR n 
1 285 GLU n 
1 286 GLN n 
1 287 MET n 
1 288 THR n 
1 289 GLU n 
1 290 LEU n 
1 291 ALA n 
1 292 HIS n 
1 293 GLY n 
1 294 LEU n 
1 295 GLU n 
1 296 SER n 
1 297 SER n 
1 298 GLN n 
1 299 GLN n 
1 300 ARG n 
1 301 PHE n 
1 302 LEU n 
1 303 TRP n 
1 304 VAL n 
1 305 VAL n 
1 306 ARG n 
1 307 SER n 
1 308 PRO n 
1 309 ASN n 
1 310 GLN n 
1 311 ILE n 
1 312 PRO n 
1 313 ASN n 
1 314 SER n 
1 315 THR n 
1 316 TYR n 
1 317 PHE n 
1 318 SER n 
1 319 VAL n 
1 320 GLN n 
1 321 SER n 
1 322 GLN n 
1 323 LYS n 
1 324 ASP n 
1 325 PRO n 
1 326 LEU n 
1 327 ALA n 
1 328 TYR n 
1 329 LEU n 
1 330 PRO n 
1 331 GLU n 
1 332 GLY n 
1 333 PHE n 
1 334 LEU n 
1 335 ASN n 
1 336 ARG n 
1 337 THR n 
1 338 GLU n 
1 339 GLY n 
1 340 ARG n 
1 341 GLY n 
1 342 LEU n 
1 343 VAL n 
1 344 VAL n 
1 345 SER n 
1 346 ASN n 
1 347 TRP n 
1 348 ALA n 
1 349 PRO n 
1 350 GLN n 
1 351 ALA n 
1 352 GLN n 
1 353 ILE n 
1 354 LEU n 
1 355 SER n 
1 356 HIS n 
1 357 GLY n 
1 358 SER n 
1 359 THR n 
1 360 GLY n 
1 361 GLY n 
1 362 PHE n 
1 363 MET n 
1 364 SER n 
1 365 HIS n 
1 366 CYS n 
1 367 GLY n 
1 368 TRP n 
1 369 ASN n 
1 370 SER n 
1 371 ILE n 
1 372 LEU n 
1 373 GLU n 
1 374 SER n 
1 375 VAL n 
1 376 VAL n 
1 377 HIS n 
1 378 GLY n 
1 379 VAL n 
1 380 PRO n 
1 381 ILE n 
1 382 ILE n 
1 383 ALA n 
1 384 TRP n 
1 385 PRO n 
1 386 LEU n 
1 387 TYR n 
1 388 ALA n 
1 389 GLU n 
1 390 GLN n 
1 391 LYS n 
1 392 MET n 
1 393 ASN n 
1 394 SER n 
1 395 ILE n 
1 396 ILE n 
1 397 VAL n 
1 398 VAL n 
1 399 GLU n 
1 400 ASP n 
1 401 VAL n 
1 402 LYS n 
1 403 VAL n 
1 404 ALA n 
1 405 LEU n 
1 406 ARG n 
1 407 PRO n 
1 408 ALA n 
1 409 GLY n 
1 410 VAL n 
1 411 GLY n 
1 412 GLU n 
1 413 ARG n 
1 414 VAL n 
1 415 VAL n 
1 416 GLU n 
1 417 ARG n 
1 418 SER n 
1 419 GLU n 
1 420 ILE n 
1 421 THR n 
1 422 ALA n 
1 423 VAL n 
1 424 VAL n 
1 425 LYS n 
1 426 ALA n 
1 427 LEU n 
1 428 MET n 
1 429 GLU n 
1 430 GLY n 
1 431 GLU n 
1 432 GLU n 
1 433 GLY n 
1 434 LYS n 
1 435 LYS n 
1 436 VAL n 
1 437 ARG n 
1 438 ASN n 
1 439 ARG n 
1 440 MET n 
1 441 LYS n 
1 442 GLU n 
1 443 LEU n 
1 444 LYS n 
1 445 GLU n 
1 446 ALA n 
1 447 ALA n 
1 448 ALA n 
1 449 ARG n 
1 450 ALA n 
1 451 VAL n 
1 452 SER n 
1 453 ASP n 
1 454 ASP n 
1 455 GLY n 
1 456 ALA n 
1 457 SER n 
1 458 THR n 
1 459 ILE n 
1 460 ALA n 
1 461 ILE n 
1 462 ALA n 
1 463 ASP n 
1 464 LEU n 
1 465 ALA n 
1 466 GLN n 
1 467 LYS n 
1 468 TRP n 
1 469 ARG n 
1 470 SER n 
1 471 SER n 
1 472 MET n 
1 473 LYS n 
1 474 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   474 
_entity_src_gen.gene_src_common_name               'Roseroot, Sedum rhodiola' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Rhodiola rosea' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     203015 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
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   GLY 1   -1  ?   ?   ?   A . n 
A 1 2   ALA 2   0   ?   ?   ?   A . n 
A 1 3   MET 3   1   ?   ?   ?   A . n 
A 1 4   ALA 4   2   ?   ?   ?   A . n 
A 1 5   GLY 5   3   3   GLY GLY A . n 
A 1 6   THR 6   4   4   THR THR A . n 
A 1 7   PRO 7   5   5   PRO PRO A . n 
A 1 8   HIS 8   6   6   HIS HIS A . n 
A 1 9   ILE 9   7   7   ILE ILE A . n 
A 1 10  ALA 10  8   8   ALA ALA A . n 
A 1 11  ILE 11  9   9   ILE ILE A . n 
A 1 12  LEU 12  10  10  LEU LEU A . n 
A 1 13  PRO 13  11  11  PRO PRO A . n 
A 1 14  SER 14  12  12  SER SER A . n 
A 1 15  PRO 15  13  13  PRO PRO A . n 
A 1 16  GLY 16  14  14  GLY GLY A . n 
A 1 17  MET 17  15  15  MET MET A . n 
A 1 18  GLY 18  16  16  GLY GLY A . n 
A 1 19  HIS 19  17  17  HIS HIS A . n 
A 1 20  LEU 20  18  18  LEU LEU A . n 
A 1 21  ILE 21  19  19  ILE ILE A . n 
A 1 22  PRO 22  20  20  PRO PRO A . n 
A 1 23  MET 23  21  21  MET MET A . n 
A 1 24  ALA 24  22  22  ALA ALA A . n 
A 1 25  GLU 25  23  23  GLU GLU A . n 
A 1 26  PHE 26  24  24  PHE PHE A . n 
A 1 27  ALA 27  25  25  ALA ALA A . n 
A 1 28  LYS 28  26  26  LYS LYS A . n 
A 1 29  ARG 29  27  27  ARG ARG A . n 
A 1 30  LEU 30  28  28  LEU LEU A . n 
A 1 31  VAL 31  29  29  VAL VAL A . n 
A 1 32  HIS 32  30  30  HIS HIS A . n 
A 1 33  HIS 33  31  31  HIS HIS A . n 
A 1 34  HIS 34  32  32  HIS HIS A . n 
A 1 35  ASN 35  33  33  ASN ASN A . n 
A 1 36  PHE 36  34  34  PHE PHE A . n 
A 1 37  SER 37  35  35  SER SER A . n 
A 1 38  ILE 38  36  36  ILE ILE A . n 
A 1 39  THR 39  37  37  THR THR A . n 
A 1 40  PHE 40  38  38  PHE PHE A . n 
A 1 41  VAL 41  39  39  VAL VAL A . n 
A 1 42  ILE 42  40  40  ILE ILE A . n 
A 1 43  PRO 43  41  41  PRO PRO A . n 
A 1 44  THR 44  42  42  THR THR A . n 
A 1 45  ASP 45  43  43  ASP ASP A . n 
A 1 46  GLY 46  44  44  GLY GLY A . n 
A 1 47  PRO 47  45  45  PRO PRO A . n 
A 1 48  PRO 48  46  46  PRO PRO A . n 
A 1 49  SER 49  47  47  SER SER A . n 
A 1 50  SER 50  48  48  SER SER A . n 
A 1 51  ALA 51  49  49  ALA ALA A . n 
A 1 52  TYR 52  50  50  TYR TYR A . n 
A 1 53  GLN 53  51  51  GLN GLN A . n 
A 1 54  GLN 54  52  52  GLN GLN A . n 
A 1 55  VAL 55  53  53  VAL VAL A . n 
A 1 56  LEU 56  54  54  LEU LEU A . n 
A 1 57  THR 57  55  55  THR THR A . n 
A 1 58  SER 58  56  56  SER SER A . n 
A 1 59  LEU 59  57  57  LEU LEU A . n 
A 1 60  PRO 60  58  58  PRO PRO A . n 
A 1 61  SER 61  59  59  SER SER A . n 
A 1 62  SER 62  60  60  SER SER A . n 
A 1 63  ILE 63  61  61  ILE ILE A . n 
A 1 64  ASP 64  62  62  ASP ASP A . n 
A 1 65  HIS 65  63  63  HIS HIS A . n 
A 1 66  ILE 66  64  64  ILE ILE A . n 
A 1 67  PHE 67  65  65  PHE PHE A . n 
A 1 68  LEU 68  66  66  LEU LEU A . n 
A 1 69  PRO 69  67  67  PRO PRO A . n 
A 1 70  GLN 70  68  68  GLN GLN A . n 
A 1 71  VAL 71  69  69  VAL VAL A . n 
A 1 72  ASP 72  70  70  ASP ASP A . n 
A 1 73  LEU 73  71  71  LEU LEU A . n 
A 1 74  THR 74  72  72  THR THR A . n 
A 1 75  ASP 75  73  73  ASP ASP A . n 
A 1 76  VAL 76  74  ?   ?   ?   A . n 
A 1 77  VAL 77  75  ?   ?   ?   A . n 
A 1 78  SER 78  76  ?   ?   ?   A . n 
A 1 79  GLN 79  77  ?   ?   ?   A . n 
A 1 80  SER 80  78  ?   ?   ?   A . n 
A 1 81  PRO 81  79  ?   ?   ?   A . n 
A 1 82  ALA 82  80  ?   ?   ?   A . n 
A 1 83  HIS 83  81  ?   ?   ?   A . n 
A 1 84  PRO 84  82  82  PRO PRO A . n 
A 1 85  ARG 85  83  83  ARG ARG A . n 
A 1 86  ILE 86  84  84  ILE ILE A . n 
A 1 87  GLU 87  85  85  GLU GLU A . n 
A 1 88  THR 88  86  86  THR THR A . n 
A 1 89  LEU 89  87  87  LEU LEU A . n 
A 1 90  ILE 90  88  88  ILE ILE A . n 
A 1 91  SER 91  89  89  SER SER A . n 
A 1 92  LEU 92  90  90  LEU LEU A . n 
A 1 93  THR 93  91  91  THR THR A . n 
A 1 94  VAL 94  92  92  VAL VAL A . n 
A 1 95  ALA 95  93  93  ALA ALA A . n 
A 1 96  ARG 96  94  94  ARG ARG A . n 
A 1 97  SER 97  95  95  SER SER A . n 
A 1 98  LEU 98  96  96  LEU LEU A . n 
A 1 99  SER 99  97  97  SER SER A . n 
A 1 100 SER 100 98  98  SER SER A . n 
A 1 101 LEU 101 99  99  LEU LEU A . n 
A 1 102 ARG 102 100 100 ARG ARG A . n 
A 1 103 THR 103 101 101 THR THR A . n 
A 1 104 THR 104 102 102 THR THR A . n 
A 1 105 LEU 105 103 103 LEU LEU A . n 
A 1 106 SER 106 104 104 SER SER A . n 
A 1 107 SER 107 105 105 SER SER A . n 
A 1 108 LEU 108 106 106 LEU LEU A . n 
A 1 109 GLN 109 107 107 GLN GLN A . n 
A 1 110 SER 110 108 108 SER SER A . n 
A 1 111 SER 111 109 109 SER SER A . n 
A 1 112 LYS 112 110 110 LYS LYS A . n 
A 1 113 ASN 113 111 111 ASN ASN A . n 
A 1 114 LEU 114 112 112 LEU LEU A . n 
A 1 115 VAL 115 113 113 VAL VAL A . n 
A 1 116 SER 116 114 114 SER SER A . n 
A 1 117 LEU 117 115 115 LEU LEU A . n 
A 1 118 VAL 118 116 116 VAL VAL A . n 
A 1 119 VAL 119 117 117 VAL VAL A . n 
A 1 120 ASP 120 118 118 ASP ASP A . n 
A 1 121 LEU 121 119 119 LEU LEU A . n 
A 1 122 PHE 122 120 120 PHE PHE A . n 
A 1 123 GLY 123 121 121 GLY GLY A . n 
A 1 124 THR 124 122 122 THR THR A . n 
A 1 125 ASP 125 123 123 ASP ASP A . n 
A 1 126 ALA 126 124 124 ALA ALA A . n 
A 1 127 PHE 127 125 125 PHE PHE A . n 
A 1 128 ASP 128 126 126 ASP ASP A . n 
A 1 129 PRO 129 127 127 PRO PRO A . n 
A 1 130 ALA 130 128 128 ALA ALA A . n 
A 1 131 ILE 131 129 129 ILE ILE A . n 
A 1 132 GLU 132 130 130 GLU GLU A . n 
A 1 133 LEU 133 131 131 LEU LEU A . n 
A 1 134 GLY 134 132 132 GLY GLY A . n 
A 1 135 ILE 135 133 133 ILE ILE A . n 
A 1 136 SER 136 134 134 SER SER A . n 
A 1 137 PRO 137 135 135 PRO PRO A . n 
A 1 138 TYR 138 136 136 TYR TYR A . n 
A 1 139 ILE 139 137 137 ILE ILE A . n 
A 1 140 PHE 140 138 138 PHE PHE A . n 
A 1 141 PHE 141 139 139 PHE PHE A . n 
A 1 142 PRO 142 140 140 PRO PRO A . n 
A 1 143 SER 143 141 141 SER SER A . n 
A 1 144 THR 144 142 142 THR THR A . n 
A 1 145 ALA 145 143 143 ALA ALA A . n 
A 1 146 MET 146 144 144 MET MET A . n 
A 1 147 THR 147 145 145 THR THR A . n 
A 1 148 LEU 148 146 146 LEU LEU A . n 
A 1 149 SER 149 147 147 SER SER A . n 
A 1 150 LEU 150 148 148 LEU LEU A . n 
A 1 151 PHE 151 149 149 PHE PHE A . n 
A 1 152 LEU 152 150 150 LEU LEU A . n 
A 1 153 TYR 153 151 151 TYR TYR A . n 
A 1 154 MET 154 152 152 MET MET A . n 
A 1 155 PRO 155 153 153 PRO PRO A . n 
A 1 156 GLN 156 154 154 GLN GLN A . n 
A 1 157 LEU 157 155 155 LEU LEU A . n 
A 1 158 ASP 158 156 156 ASP ASP A . n 
A 1 159 LYS 159 157 157 LYS LYS A . n 
A 1 160 SER 160 158 158 SER SER A . n 
A 1 161 VAL 161 159 159 VAL VAL A . n 
A 1 162 THR 162 160 ?   ?   ?   A . n 
A 1 163 CYS 163 161 ?   ?   ?   A . n 
A 1 164 GLU 164 162 ?   ?   ?   A . n 
A 1 165 PHE 165 163 ?   ?   ?   A . n 
A 1 166 ARG 166 164 ?   ?   ?   A . n 
A 1 167 HIS 167 165 ?   ?   ?   A . n 
A 1 168 MET 168 166 ?   ?   ?   A . n 
A 1 169 THR 169 167 ?   ?   ?   A . n 
A 1 170 ASP 170 168 168 ASP ASP A . n 
A 1 171 LEU 171 169 169 LEU LEU A . n 
A 1 172 VAL 172 170 170 VAL VAL A . n 
A 1 173 ARG 173 171 171 ARG ARG A . n 
A 1 174 ILE 174 172 172 ILE ILE A . n 
A 1 175 PRO 175 173 173 PRO PRO A . n 
A 1 176 GLY 176 174 174 GLY GLY A . n 
A 1 177 CYS 177 175 175 CYS CYS A . n 
A 1 178 VAL 178 176 176 VAL VAL A . n 
A 1 179 PRO 179 177 177 PRO PRO A . n 
A 1 180 VAL 180 178 178 VAL VAL A . n 
A 1 181 ARG 181 179 179 ARG ARG A . n 
A 1 182 GLY 182 180 180 GLY GLY A . n 
A 1 183 SER 183 181 181 SER SER A . n 
A 1 184 ASP 184 182 182 ASP ASP A . n 
A 1 185 LEU 185 183 183 LEU LEU A . n 
A 1 186 PHE 186 184 184 PHE PHE A . n 
A 1 187 ASP 187 185 185 ASP ASP A . n 
A 1 188 PRO 188 186 186 PRO PRO A . n 
A 1 189 VAL 189 187 187 VAL VAL A . n 
A 1 190 GLN 190 188 188 GLN GLN A . n 
A 1 191 ASP 191 189 189 ASP ASP A . n 
A 1 192 ARG 192 190 190 ARG ARG A . n 
A 1 193 THR 193 191 191 THR THR A . n 
A 1 194 ASP 194 192 192 ASP ASP A . n 
A 1 195 GLU 195 193 193 GLU GLU A . n 
A 1 196 ALA 196 194 194 ALA ALA A . n 
A 1 197 TYR 197 195 195 TYR TYR A . n 
A 1 198 LYS 198 196 196 LYS LYS A . n 
A 1 199 TRP 199 197 197 TRP TRP A . n 
A 1 200 VAL 200 198 198 VAL VAL A . n 
A 1 201 ILE 201 199 199 ILE ILE A . n 
A 1 202 HIS 202 200 200 HIS HIS A . n 
A 1 203 HIS 203 201 201 HIS HIS A . n 
A 1 204 SER 204 202 202 SER SER A . n 
A 1 205 ASN 205 203 203 ASN ASN A . n 
A 1 206 ARG 206 204 204 ARG ARG A . n 
A 1 207 TYR 207 205 205 TYR TYR A . n 
A 1 208 PRO 208 206 206 PRO PRO A . n 
A 1 209 MET 209 207 207 MET MET A . n 
A 1 210 ALA 210 208 208 ALA ALA A . n 
A 1 211 GLU 211 209 209 GLU GLU A . n 
A 1 212 GLY 212 210 210 GLY GLY A . n 
A 1 213 VAL 213 211 211 VAL VAL A . n 
A 1 214 ILE 214 212 212 ILE ILE A . n 
A 1 215 GLU 215 213 213 GLU GLU A . n 
A 1 216 ASN 216 214 214 ASN ASN A . n 
A 1 217 SER 217 215 215 SER SER A . n 
A 1 218 PHE 218 216 216 PHE PHE A . n 
A 1 219 MET 219 217 217 MET MET A . n 
A 1 220 GLU 220 218 218 GLU GLU A . n 
A 1 221 LEU 221 219 219 LEU LEU A . n 
A 1 222 GLU 222 220 220 GLU GLU A . n 
A 1 223 HIS 223 221 221 HIS HIS A . n 
A 1 224 GLY 224 222 222 GLY GLY A . n 
A 1 225 ALA 225 223 223 ALA ALA A . n 
A 1 226 LEU 226 224 224 LEU LEU A . n 
A 1 227 LYS 227 225 225 LYS LYS A . n 
A 1 228 TYR 228 226 226 TYR TYR A . n 
A 1 229 LEU 229 227 227 LEU LEU A . n 
A 1 230 GLN 230 228 228 GLN GLN A . n 
A 1 231 THR 231 229 229 THR THR A . n 
A 1 232 VAL 232 230 230 VAL VAL A . n 
A 1 233 GLN 233 231 231 GLN GLN A . n 
A 1 234 SER 234 232 232 SER SER A . n 
A 1 235 GLY 235 233 233 GLY GLY A . n 
A 1 236 LYS 236 234 234 LYS LYS A . n 
A 1 237 PRO 237 235 235 PRO PRO A . n 
A 1 238 PRO 238 236 236 PRO PRO A . n 
A 1 239 VAL 239 237 237 VAL VAL A . n 
A 1 240 TYR 240 238 238 TYR TYR A . n 
A 1 241 ALA 241 239 239 ALA ALA A . n 
A 1 242 VAL 242 240 240 VAL VAL A . n 
A 1 243 GLY 243 241 241 GLY GLY A . n 
A 1 244 PRO 244 242 242 PRO PRO A . n 
A 1 245 LEU 245 243 243 LEU LEU A . n 
A 1 246 ILE 246 244 244 ILE ILE A . n 
A 1 247 LYS 247 245 245 LYS LYS A . n 
A 1 248 MET 248 246 ?   ?   ?   A . n 
A 1 249 ASP 249 247 ?   ?   ?   A . n 
A 1 250 TYR 250 248 ?   ?   ?   A . n 
A 1 251 ASP 251 249 ?   ?   ?   A . n 
A 1 252 VAL 252 250 ?   ?   ?   A . n 
A 1 253 ASP 253 251 ?   ?   ?   A . n 
A 1 254 ASP 254 252 ?   ?   ?   A . n 
A 1 255 SER 255 253 253 SER SER A . n 
A 1 256 GLY 256 254 254 GLY GLY A . n 
A 1 257 SER 257 255 255 SER SER A . n 
A 1 258 LYS 258 256 256 LYS LYS A . n 
A 1 259 ILE 259 257 257 ILE ILE A . n 
A 1 260 ILE 260 258 258 ILE ILE A . n 
A 1 261 GLU 261 259 259 GLU GLU A . n 
A 1 262 TRP 262 260 260 TRP TRP A . n 
A 1 263 LEU 263 261 261 LEU LEU A . n 
A 1 264 ASP 264 262 262 ASP ASP A . n 
A 1 265 ASP 265 263 263 ASP ASP A . n 
A 1 266 GLN 266 264 264 GLN GLN A . n 
A 1 267 PRO 267 265 265 PRO PRO A . n 
A 1 268 VAL 268 266 266 VAL VAL A . n 
A 1 269 GLY 269 267 267 GLY GLY A . n 
A 1 270 SER 270 268 268 SER SER A . n 
A 1 271 VAL 271 269 269 VAL VAL A . n 
A 1 272 LEU 272 270 270 LEU LEU A . n 
A 1 273 PHE 273 271 271 PHE PHE A . n 
A 1 274 VAL 274 272 272 VAL VAL A . n 
A 1 275 SER 275 273 273 SER SER A . n 
A 1 276 PHE 276 274 274 PHE PHE A . n 
A 1 277 GLY 277 275 275 GLY GLY A . n 
A 1 278 SER 278 276 276 SER SER A . n 
A 1 279 GLY 279 277 277 GLY GLY A . n 
A 1 280 GLY 280 278 278 GLY GLY A . n 
A 1 281 THR 281 279 279 THR THR A . n 
A 1 282 LEU 282 280 280 LEU LEU A . n 
A 1 283 SER 283 281 281 SER SER A . n 
A 1 284 TYR 284 282 282 TYR TYR A . n 
A 1 285 GLU 285 283 283 GLU GLU A . n 
A 1 286 GLN 286 284 284 GLN GLN A . n 
A 1 287 MET 287 285 285 MET MET A . n 
A 1 288 THR 288 286 286 THR THR A . n 
A 1 289 GLU 289 287 287 GLU GLU A . n 
A 1 290 LEU 290 288 288 LEU LEU A . n 
A 1 291 ALA 291 289 289 ALA ALA A . n 
A 1 292 HIS 292 290 290 HIS HIS A . n 
A 1 293 GLY 293 291 291 GLY GLY A . n 
A 1 294 LEU 294 292 292 LEU LEU A . n 
A 1 295 GLU 295 293 293 GLU GLU A . n 
A 1 296 SER 296 294 294 SER SER A . n 
A 1 297 SER 297 295 295 SER SER A . n 
A 1 298 GLN 298 296 296 GLN GLN A . n 
A 1 299 GLN 299 297 297 GLN GLN A . n 
A 1 300 ARG 300 298 298 ARG ARG A . n 
A 1 301 PHE 301 299 299 PHE PHE A . n 
A 1 302 LEU 302 300 300 LEU LEU A . n 
A 1 303 TRP 303 301 301 TRP TRP A . n 
A 1 304 VAL 304 302 302 VAL VAL A . n 
A 1 305 VAL 305 303 303 VAL VAL A . n 
A 1 306 ARG 306 304 304 ARG ARG A . n 
A 1 307 SER 307 305 305 SER SER A . n 
A 1 308 PRO 308 306 306 PRO PRO A . n 
A 1 309 ASN 309 307 307 ASN ASN A . n 
A 1 310 GLN 310 308 308 GLN GLN A . n 
A 1 311 ILE 311 309 309 ILE ILE A . n 
A 1 312 PRO 312 310 310 PRO PRO A . n 
A 1 313 ASN 313 311 311 ASN ASN A . n 
A 1 314 SER 314 312 312 SER SER A . n 
A 1 315 THR 315 313 313 THR THR A . n 
A 1 316 TYR 316 314 314 TYR TYR A . n 
A 1 317 PHE 317 315 315 PHE PHE A . n 
A 1 318 SER 318 316 316 SER SER A . n 
A 1 319 VAL 319 317 317 VAL VAL A . n 
A 1 320 GLN 320 318 318 GLN GLN A . n 
A 1 321 SER 321 319 319 SER SER A . n 
A 1 322 GLN 322 320 320 GLN GLN A . n 
A 1 323 LYS 323 321 321 LYS LYS A . n 
A 1 324 ASP 324 322 322 ASP ASP A . n 
A 1 325 PRO 325 323 323 PRO PRO A . n 
A 1 326 LEU 326 324 324 LEU LEU A . n 
A 1 327 ALA 327 325 325 ALA ALA A . n 
A 1 328 TYR 328 326 326 TYR TYR A . n 
A 1 329 LEU 329 327 327 LEU LEU A . n 
A 1 330 PRO 330 328 328 PRO PRO A . n 
A 1 331 GLU 331 329 329 GLU GLU A . n 
A 1 332 GLY 332 330 330 GLY GLY A . n 
A 1 333 PHE 333 331 331 PHE PHE A . n 
A 1 334 LEU 334 332 332 LEU LEU A . n 
A 1 335 ASN 335 333 333 ASN ASN A . n 
A 1 336 ARG 336 334 334 ARG ARG A . n 
A 1 337 THR 337 335 335 THR THR A . n 
A 1 338 GLU 338 336 336 GLU GLU A . n 
A 1 339 GLY 339 337 337 GLY GLY A . n 
A 1 340 ARG 340 338 338 ARG ARG A . n 
A 1 341 GLY 341 339 339 GLY GLY A . n 
A 1 342 LEU 342 340 340 LEU LEU A . n 
A 1 343 VAL 343 341 341 VAL VAL A . n 
A 1 344 VAL 344 342 342 VAL VAL A . n 
A 1 345 SER 345 343 343 SER SER A . n 
A 1 346 ASN 346 344 344 ASN ASN A . n 
A 1 347 TRP 347 345 345 TRP TRP A . n 
A 1 348 ALA 348 346 346 ALA ALA A . n 
A 1 349 PRO 349 347 347 PRO PRO A . n 
A 1 350 GLN 350 348 348 GLN GLN A . n 
A 1 351 ALA 351 349 349 ALA ALA A . n 
A 1 352 GLN 352 350 350 GLN GLN A . n 
A 1 353 ILE 353 351 351 ILE ILE A . n 
A 1 354 LEU 354 352 352 LEU LEU A . n 
A 1 355 SER 355 353 353 SER SER A . n 
A 1 356 HIS 356 354 354 HIS HIS A . n 
A 1 357 GLY 357 355 355 GLY GLY A . n 
A 1 358 SER 358 356 356 SER SER A . n 
A 1 359 THR 359 357 357 THR THR A . n 
A 1 360 GLY 360 358 358 GLY GLY A . n 
A 1 361 GLY 361 359 359 GLY GLY A . n 
A 1 362 PHE 362 360 360 PHE PHE A . n 
A 1 363 MET 363 361 361 MET MET A . n 
A 1 364 SER 364 362 362 SER SER A . n 
A 1 365 HIS 365 363 363 HIS HIS A . n 
A 1 366 CYS 366 364 364 CYS CYS A . n 
A 1 367 GLY 367 365 365 GLY GLY A . n 
A 1 368 TRP 368 366 366 TRP TRP A . n 
A 1 369 ASN 369 367 367 ASN ASN A . n 
A 1 370 SER 370 368 368 SER SER A . n 
A 1 371 ILE 371 369 369 ILE ILE A . n 
A 1 372 LEU 372 370 370 LEU LEU A . n 
A 1 373 GLU 373 371 371 GLU GLU A . n 
A 1 374 SER 374 372 372 SER SER A . n 
A 1 375 VAL 375 373 373 VAL VAL A . n 
A 1 376 VAL 376 374 374 VAL VAL A . n 
A 1 377 HIS 377 375 375 HIS HIS A . n 
A 1 378 GLY 378 376 376 GLY GLY A . n 
A 1 379 VAL 379 377 377 VAL VAL A . n 
A 1 380 PRO 380 378 378 PRO PRO A . n 
A 1 381 ILE 381 379 379 ILE ILE A . n 
A 1 382 ILE 382 380 380 ILE ILE A . n 
A 1 383 ALA 383 381 381 ALA ALA A . n 
A 1 384 TRP 384 382 382 TRP TRP A . n 
A 1 385 PRO 385 383 383 PRO PRO A . n 
A 1 386 LEU 386 384 384 LEU LEU A . n 
A 1 387 TYR 387 385 385 TYR TYR A . n 
A 1 388 ALA 388 386 386 ALA ALA A . n 
A 1 389 GLU 389 387 387 GLU GLU A . n 
A 1 390 GLN 390 388 388 GLN GLN A . n 
A 1 391 LYS 391 389 389 LYS LYS A . n 
A 1 392 MET 392 390 390 MET MET A . n 
A 1 393 ASN 393 391 391 ASN ASN A . n 
A 1 394 SER 394 392 392 SER SER A . n 
A 1 395 ILE 395 393 393 ILE ILE A . n 
A 1 396 ILE 396 394 394 ILE ILE A . n 
A 1 397 VAL 397 395 395 VAL VAL A . n 
A 1 398 VAL 398 396 396 VAL VAL A . n 
A 1 399 GLU 399 397 397 GLU GLU A . n 
A 1 400 ASP 400 398 398 ASP ASP A . n 
A 1 401 VAL 401 399 399 VAL VAL A . n 
A 1 402 LYS 402 400 400 LYS LYS A . n 
A 1 403 VAL 403 401 401 VAL VAL A . n 
A 1 404 ALA 404 402 402 ALA ALA A . n 
A 1 405 LEU 405 403 403 LEU LEU A . n 
A 1 406 ARG 406 404 404 ARG ARG A . n 
A 1 407 PRO 407 405 405 PRO PRO A . n 
A 1 408 ALA 408 406 406 ALA ALA A . n 
A 1 409 GLY 409 407 407 GLY GLY A . n 
A 1 410 VAL 410 408 408 VAL VAL A . n 
A 1 411 GLY 411 409 409 GLY GLY A . n 
A 1 412 GLU 412 410 410 GLU GLU A . n 
A 1 413 ARG 413 411 411 ARG ARG A . n 
A 1 414 VAL 414 412 412 VAL VAL A . n 
A 1 415 VAL 415 413 413 VAL VAL A . n 
A 1 416 GLU 416 414 414 GLU GLU A . n 
A 1 417 ARG 417 415 415 ARG ARG A . n 
A 1 418 SER 418 416 416 SER SER A . n 
A 1 419 GLU 419 417 417 GLU GLU A . n 
A 1 420 ILE 420 418 418 ILE ILE A . n 
A 1 421 THR 421 419 419 THR THR A . n 
A 1 422 ALA 422 420 420 ALA ALA A . n 
A 1 423 VAL 423 421 421 VAL VAL A . n 
A 1 424 VAL 424 422 422 VAL VAL A . n 
A 1 425 LYS 425 423 423 LYS LYS A . n 
A 1 426 ALA 426 424 424 ALA ALA A . n 
A 1 427 LEU 427 425 425 LEU LEU A . n 
A 1 428 MET 428 426 426 MET MET A . n 
A 1 429 GLU 429 427 427 GLU GLU A . n 
A 1 430 GLY 430 428 428 GLY GLY A . n 
A 1 431 GLU 431 429 429 GLU GLU A . n 
A 1 432 GLU 432 430 430 GLU GLU A . n 
A 1 433 GLY 433 431 431 GLY GLY A . n 
A 1 434 LYS 434 432 432 LYS LYS A . n 
A 1 435 LYS 435 433 433 LYS LYS A . n 
A 1 436 VAL 436 434 434 VAL VAL A . n 
A 1 437 ARG 437 435 435 ARG ARG A . n 
A 1 438 ASN 438 436 436 ASN ASN A . n 
A 1 439 ARG 439 437 437 ARG ARG A . n 
A 1 440 MET 440 438 438 MET MET A . n 
A 1 441 LYS 441 439 439 LYS LYS A . n 
A 1 442 GLU 442 440 440 GLU GLU A . n 
A 1 443 LEU 443 441 441 LEU LEU A . n 
A 1 444 LYS 444 442 442 LYS LYS A . n 
A 1 445 GLU 445 443 443 GLU GLU A . n 
A 1 446 ALA 446 444 444 ALA ALA A . n 
A 1 447 ALA 447 445 445 ALA ALA A . n 
A 1 448 ALA 448 446 446 ALA ALA A . n 
A 1 449 ARG 449 447 447 ARG ARG A . n 
A 1 450 ALA 450 448 448 ALA ALA A . n 
A 1 451 VAL 451 449 449 VAL VAL A . n 
A 1 452 SER 452 450 450 SER SER A . n 
A 1 453 ASP 453 451 451 ASP ASP A . n 
A 1 454 ASP 454 452 452 ASP ASP A . n 
A 1 455 GLY 455 453 453 GLY GLY A . n 
A 1 456 ALA 456 454 454 ALA ALA A . n 
A 1 457 SER 457 455 455 SER SER A . n 
A 1 458 THR 458 456 456 THR THR A . n 
A 1 459 ILE 459 457 457 ILE ILE A . n 
A 1 460 ALA 460 458 458 ALA ALA A . n 
A 1 461 ILE 461 459 459 ILE ILE A . n 
A 1 462 ALA 462 460 460 ALA ALA A . n 
A 1 463 ASP 463 461 461 ASP ASP A . n 
A 1 464 LEU 464 462 462 LEU LEU A . n 
A 1 465 ALA 465 463 463 ALA ALA A . n 
A 1 466 GLN 466 464 464 GLN GLN A . n 
A 1 467 LYS 467 465 465 LYS LYS A . n 
A 1 468 TRP 468 466 466 TRP TRP A . n 
A 1 469 ARG 469 467 467 ARG ARG A . n 
A 1 470 SER 470 468 468 SER SER A . n 
A 1 471 SER 471 469 469 SER SER A . n 
A 1 472 MET 472 470 470 MET MET A . n 
A 1 473 LYS 473 471 ?   ?   ?   A . n 
A 1 474 HIS 474 472 ?   ?   ?   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   501 48  HOH HOH A . 
B 2 HOH 2   502 154 HOH HOH A . 
B 2 HOH 3   503 158 HOH HOH A . 
B 2 HOH 4   504 87  HOH HOH A . 
B 2 HOH 5   505 10  HOH HOH A . 
B 2 HOH 6   506 145 HOH HOH A . 
B 2 HOH 7   507 149 HOH HOH A . 
B 2 HOH 8   508 146 HOH HOH A . 
B 2 HOH 9   509 62  HOH HOH A . 
B 2 HOH 10  510 74  HOH HOH A . 
B 2 HOH 11  511 69  HOH HOH A . 
B 2 HOH 12  512 120 HOH HOH A . 
B 2 HOH 13  513 56  HOH HOH A . 
B 2 HOH 14  514 127 HOH HOH A . 
B 2 HOH 15  515 47  HOH HOH A . 
B 2 HOH 16  516 50  HOH HOH A . 
B 2 HOH 17  517 58  HOH HOH A . 
B 2 HOH 18  518 17  HOH HOH A . 
B 2 HOH 19  519 75  HOH HOH A . 
B 2 HOH 20  520 139 HOH HOH A . 
B 2 HOH 21  521 148 HOH HOH A . 
B 2 HOH 22  522 92  HOH HOH A . 
B 2 HOH 23  523 94  HOH HOH A . 
B 2 HOH 24  524 98  HOH HOH A . 
B 2 HOH 25  525 103 HOH HOH A . 
B 2 HOH 26  526 70  HOH HOH A . 
B 2 HOH 27  527 45  HOH HOH A . 
B 2 HOH 28  528 123 HOH HOH A . 
B 2 HOH 29  529 27  HOH HOH A . 
B 2 HOH 30  530 91  HOH HOH A . 
B 2 HOH 31  531 66  HOH HOH A . 
B 2 HOH 32  532 128 HOH HOH A . 
B 2 HOH 33  533 15  HOH HOH A . 
B 2 HOH 34  534 97  HOH HOH A . 
B 2 HOH 35  535 54  HOH HOH A . 
B 2 HOH 36  536 8   HOH HOH A . 
B 2 HOH 37  537 61  HOH HOH A . 
B 2 HOH 38  538 117 HOH HOH A . 
B 2 HOH 39  539 89  HOH HOH A . 
B 2 HOH 40  540 80  HOH HOH A . 
B 2 HOH 41  541 136 HOH HOH A . 
B 2 HOH 42  542 31  HOH HOH A . 
B 2 HOH 43  543 12  HOH HOH A . 
B 2 HOH 44  544 60  HOH HOH A . 
B 2 HOH 45  545 63  HOH HOH A . 
B 2 HOH 46  546 73  HOH HOH A . 
B 2 HOH 47  547 90  HOH HOH A . 
B 2 HOH 48  548 32  HOH HOH A . 
B 2 HOH 49  549 78  HOH HOH A . 
B 2 HOH 50  550 111 HOH HOH A . 
B 2 HOH 51  551 130 HOH HOH A . 
B 2 HOH 52  552 131 HOH HOH A . 
B 2 HOH 53  553 65  HOH HOH A . 
B 2 HOH 54  554 21  HOH HOH A . 
B 2 HOH 55  555 143 HOH HOH A . 
B 2 HOH 56  556 49  HOH HOH A . 
B 2 HOH 57  557 138 HOH HOH A . 
B 2 HOH 58  558 106 HOH HOH A . 
B 2 HOH 59  559 44  HOH HOH A . 
B 2 HOH 60  560 95  HOH HOH A . 
B 2 HOH 61  561 82  HOH HOH A . 
B 2 HOH 62  562 125 HOH HOH A . 
B 2 HOH 63  563 79  HOH HOH A . 
B 2 HOH 64  564 113 HOH HOH A . 
B 2 HOH 65  565 109 HOH HOH A . 
B 2 HOH 66  566 19  HOH HOH A . 
B 2 HOH 67  567 35  HOH HOH A . 
B 2 HOH 68  568 140 HOH HOH A . 
B 2 HOH 69  569 110 HOH HOH A . 
B 2 HOH 70  570 84  HOH HOH A . 
B 2 HOH 71  571 64  HOH HOH A . 
B 2 HOH 72  572 20  HOH HOH A . 
B 2 HOH 73  573 18  HOH HOH A . 
B 2 HOH 74  574 147 HOH HOH A . 
B 2 HOH 75  575 51  HOH HOH A . 
B 2 HOH 76  576 16  HOH HOH A . 
B 2 HOH 77  577 162 HOH HOH A . 
B 2 HOH 78  578 155 HOH HOH A . 
B 2 HOH 79  579 4   HOH HOH A . 
B 2 HOH 80  580 11  HOH HOH A . 
B 2 HOH 81  581 124 HOH HOH A . 
B 2 HOH 82  582 38  HOH HOH A . 
B 2 HOH 83  583 114 HOH HOH A . 
B 2 HOH 84  584 57  HOH HOH A . 
B 2 HOH 85  585 40  HOH HOH A . 
B 2 HOH 86  586 68  HOH HOH A . 
B 2 HOH 87  587 85  HOH HOH A . 
B 2 HOH 88  588 28  HOH HOH A . 
B 2 HOH 89  589 83  HOH HOH A . 
B 2 HOH 90  590 42  HOH HOH A . 
B 2 HOH 91  591 23  HOH HOH A . 
B 2 HOH 92  592 72  HOH HOH A . 
B 2 HOH 93  593 151 HOH HOH A . 
B 2 HOH 94  594 119 HOH HOH A . 
B 2 HOH 95  595 34  HOH HOH A . 
B 2 HOH 96  596 141 HOH HOH A . 
B 2 HOH 97  597 13  HOH HOH A . 
B 2 HOH 98  598 121 HOH HOH A . 
B 2 HOH 99  599 135 HOH HOH A . 
B 2 HOH 100 600 133 HOH HOH A . 
B 2 HOH 101 601 105 HOH HOH A . 
B 2 HOH 102 602 67  HOH HOH A . 
B 2 HOH 103 603 86  HOH HOH A . 
B 2 HOH 104 604 9   HOH HOH A . 
B 2 HOH 105 605 132 HOH HOH A . 
B 2 HOH 106 606 37  HOH HOH A . 
B 2 HOH 107 607 77  HOH HOH A . 
B 2 HOH 108 608 3   HOH HOH A . 
B 2 HOH 109 609 150 HOH HOH A . 
B 2 HOH 110 610 100 HOH HOH A . 
B 2 HOH 111 611 137 HOH HOH A . 
B 2 HOH 112 612 156 HOH HOH A . 
B 2 HOH 113 613 41  HOH HOH A . 
B 2 HOH 114 614 107 HOH HOH A . 
B 2 HOH 115 615 53  HOH HOH A . 
B 2 HOH 116 616 126 HOH HOH A . 
B 2 HOH 117 617 43  HOH HOH A . 
B 2 HOH 118 618 116 HOH HOH A . 
B 2 HOH 119 619 104 HOH HOH A . 
B 2 HOH 120 620 46  HOH HOH A . 
B 2 HOH 121 621 29  HOH HOH A . 
B 2 HOH 122 622 26  HOH HOH A . 
B 2 HOH 123 623 39  HOH HOH A . 
B 2 HOH 124 624 129 HOH HOH A . 
B 2 HOH 125 625 7   HOH HOH A . 
B 2 HOH 126 626 76  HOH HOH A . 
B 2 HOH 127 627 101 HOH HOH A . 
B 2 HOH 128 628 112 HOH HOH A . 
B 2 HOH 129 629 159 HOH HOH A . 
B 2 HOH 130 630 59  HOH HOH A . 
B 2 HOH 131 631 6   HOH HOH A . 
B 2 HOH 132 632 14  HOH HOH A . 
B 2 HOH 133 633 160 HOH HOH A . 
B 2 HOH 134 634 30  HOH HOH A . 
B 2 HOH 135 635 153 HOH HOH A . 
B 2 HOH 136 636 2   HOH HOH A . 
B 2 HOH 137 637 55  HOH HOH A . 
B 2 HOH 138 638 99  HOH HOH A . 
B 2 HOH 139 639 115 HOH HOH A . 
B 2 HOH 140 640 96  HOH HOH A . 
B 2 HOH 141 641 5   HOH HOH A . 
B 2 HOH 142 642 22  HOH HOH A . 
B 2 HOH 143 643 24  HOH HOH A . 
B 2 HOH 144 644 88  HOH HOH A . 
B 2 HOH 145 645 52  HOH HOH A . 
B 2 HOH 146 646 118 HOH HOH A . 
B 2 HOH 147 647 25  HOH HOH A . 
B 2 HOH 148 648 134 HOH HOH A . 
B 2 HOH 149 649 152 HOH HOH A . 
B 2 HOH 150 650 33  HOH HOH A . 
B 2 HOH 151 651 161 HOH HOH A . 
B 2 HOH 152 652 1   HOH HOH A . 
B 2 HOH 153 653 157 HOH HOH A . 
B 2 HOH 154 654 142 HOH HOH A . 
B 2 HOH 155 655 81  HOH HOH A . 
B 2 HOH 156 656 108 HOH HOH A . 
B 2 HOH 157 657 93  HOH HOH A . 
B 2 HOH 158 658 122 HOH HOH A . 
B 2 HOH 159 659 144 HOH HOH A . 
B 2 HOH 160 660 102 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LEU 119 ? CG  ? A LEU 121 CG  
2  1 Y 1 A LEU 119 ? CD1 ? A LEU 121 CD1 
3  1 Y 1 A LEU 119 ? CD2 ? A LEU 121 CD2 
4  1 Y 1 A ARG 171 ? CG  ? A ARG 173 CG  
5  1 Y 1 A ARG 171 ? CD  ? A ARG 173 CD  
6  1 Y 1 A ARG 171 ? NE  ? A ARG 173 NE  
7  1 Y 1 A ARG 171 ? CZ  ? A ARG 173 CZ  
8  1 Y 1 A ARG 171 ? NH1 ? A ARG 173 NH1 
9  1 Y 1 A ARG 171 ? NH2 ? A ARG 173 NH2 
10 1 Y 1 A LYS 245 ? CG  ? A LYS 247 CG  
11 1 Y 1 A LYS 245 ? CD  ? A LYS 247 CD  
12 1 Y 1 A LYS 245 ? CE  ? A LYS 247 CE  
13 1 Y 1 A LYS 245 ? NZ  ? A LYS 247 NZ  
14 1 Y 1 A GLU 429 ? CG  ? A GLU 431 CG  
15 1 Y 1 A GLU 429 ? CD  ? A GLU 431 CD  
16 1 Y 1 A GLU 429 ? OE1 ? A GLU 431 OE1 
17 1 Y 1 A GLU 429 ? OE2 ? A GLU 431 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0257 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YP7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     69.191 
_cell.length_a_esd                 ? 
_cell.length_b                     70.826 
_cell.length_b_esd                 ? 
_cell.length_c                     92.662 
_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                         8YP7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8YP7 
_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             2.18 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.56 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '0.05 M Citric acid, 0.05 M BIS-TRIS propane, pH 4.5, 19% PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-12-06 
_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   0.979 
_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                        'NFPSS BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       NFPSS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YP7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.87 
_reflns.d_resolution_low                               46.37 
_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                                     38051 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.093 
_reflns.pdbx_Rpim_I_all                                0.026 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.090 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.87 
_reflns_shell.d_res_low                                     1.91 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           27957 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2124 
_reflns_shell.percent_possible_obs                          87.6 
_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                               13.2 
_reflns_shell.pdbx_chi_squared                              0.98 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.4 
_reflns_shell.pdbx_Rrim_I_all                               2.099 
_reflns_shell.pdbx_Rpim_I_all                               0.572 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.585 
_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                                  2.018 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.56 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.09 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.47 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.927 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.953 
_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                                 8YP7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.87 
_refine.ls_d_res_low                             46.37 
_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                     36124 
_refine.ls_number_reflns_R_free                  1865 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.90 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18112 
_refine.ls_R_factor_R_free                       0.21208 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17948 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.139 
_refine.pdbx_overall_ESU_R_Free                  0.127 
_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                             3.118 
_refine.overall_SU_ML                            0.090 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.87 
_refine_hist.d_res_low                        46.37 
_refine_hist.number_atoms_solvent             160 
_refine_hist.number_atoms_total               3579 
_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        3419 
_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' ? 0.010  0.013  3500 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  3260 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.624  1.632  4762 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.409  1.565  7575 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.722  5.000  441  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 35.317 22.405 158  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.634 15.000 572  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.761 15.000 18   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.081  0.200  463  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  3875 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  699  ? 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' ? 2.593  2.961  1776 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.591  2.960  1775 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.534  4.420  2213 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.534  4.420  2214 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.717  3.413  1724 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.716  3.413  1725 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.580  4.942  2550 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.727  35.939 3866 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.713  35.853 3849 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.875 
_refine_ls_shell.d_res_low                        1.924 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             154 
_refine_ls_shell.number_reflns_R_work             2579 
_refine_ls_shell.percent_reflns_obs               98.95 
_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                  0.363 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.418 
# 
_struct.entry_id                     8YP7 
_struct.title                        'Crystal structure of glucosyltransferase RrUGT3' 
_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        8YP7 
_struct_keywords.text            'uridine diphosphate glucosyltransferases, glycosylation, regioselectivity, BIOSYNTHETIC PROTEIN' 
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A2I6B3N5_RHORB 
_struct_ref.pdbx_db_accession          A0A2I6B3N5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GTPHIAILPSPGMGHLIPMAEFAKRLVHHHNFSITFVIPTDGPPSSAYQQVLTSLPSSIDHIFLPQVDLTDVVSQSPAHP
RIETLISLTVARSLSSLRTTLSSLQSSKNLVSLVVDLFGTDAFDPAIELGISPYIFFPSTAMTLSLFLYMPQLDKSVTCE
FRHMTDLVRIPGCVPVRGSDLFDPVQDRTDEAYKWVIHHSNRYPMAEGVIENSFMELEHGALKYLQTVQSGKPPVYAVGP
LIKMDYDVDDSGSKIIEWLDDQPVGSVLFVSFGSGGTLSYEQMTELAHGLESSQQRFLWVVRSPNQIPNSTYFSVQSQKD
PLAYLPEGFLNRTEGRGLVVSNWAPQAQILSHGSTGGFMSHCGWNSILESVVHGVPIIAWPLYAEQKMNSIIVVEDVKVA
LRPAGVGERVVERSEITAVVKALMEGEEGKKVRNRMKELKEAAARAVSDDGASTIAIADLAQKWRSSMKH
;
_struct_ref.pdbx_align_begin           3 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YP7 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 5 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 474 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A2I6B3N5 
_struct_ref_seq.db_align_beg                  3 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  472 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       3 
_struct_ref_seq.pdbx_auth_seq_align_end       472 
# 
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 8YP7 GLY A 1 ? UNP A0A2I6B3N5 ? ? 'expression tag' -1 1 
1 8YP7 ALA A 2 ? UNP A0A2I6B3N5 ? ? 'expression tag' 0  2 
1 8YP7 MET A 3 ? UNP A0A2I6B3N5 ? ? 'expression tag' 1  3 
1 8YP7 ALA A 4 ? UNP A0A2I6B3N5 ? ? 'expression tag' 2  4 
# 
_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   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 16  ? HIS A 33  ? GLY A 14  HIS A 31  1 ? 18 
HELX_P HELX_P2  AA2 SER A 49  ? SER A 58  ? SER A 47  SER A 56  1 ? 10 
HELX_P HELX_P3  AA3 ARG A 85  ? ARG A 96  ? ARG A 83  ARG A 94  1 ? 12 
HELX_P HELX_P4  AA4 SER A 97  ? LYS A 112 ? SER A 95  LYS A 110 1 ? 16 
HELX_P HELX_P5  AA5 GLY A 123 ? ASP A 125 ? GLY A 121 ASP A 123 5 ? 3  
HELX_P HELX_P6  AA6 ALA A 126 ? GLY A 134 ? ALA A 124 GLY A 132 1 ? 9  
HELX_P HELX_P7  AA7 THR A 144 ? VAL A 161 ? THR A 142 VAL A 159 1 ? 18 
HELX_P HELX_P8  AA8 ARG A 181 ? LEU A 185 ? ARG A 179 LEU A 183 5 ? 5  
HELX_P HELX_P9  AA9 PHE A 186 ? GLN A 190 ? PHE A 184 GLN A 188 5 ? 5  
HELX_P HELX_P10 AB1 ASP A 194 ? TYR A 207 ? ASP A 192 TYR A 205 1 ? 14 
HELX_P HELX_P11 AB2 PRO A 208 ? ALA A 210 ? PRO A 206 ALA A 208 5 ? 3  
HELX_P HELX_P12 AB3 GLU A 222 ? GLN A 230 ? GLU A 220 GLN A 228 1 ? 9  
HELX_P HELX_P13 AB4 GLY A 256 ? ASP A 265 ? GLY A 254 ASP A 263 1 ? 10 
HELX_P HELX_P14 AB5 SER A 283 ? GLN A 298 ? SER A 281 GLN A 296 1 ? 16 
HELX_P HELX_P15 AB6 PRO A 312 ? PHE A 317 ? PRO A 310 PHE A 315 1 ? 6  
HELX_P HELX_P16 AB7 ASP A 324 ? LEU A 329 ? ASP A 322 LEU A 327 5 ? 6  
HELX_P HELX_P17 AB8 GLY A 332 ? THR A 337 ? GLY A 330 THR A 335 1 ? 6  
HELX_P HELX_P18 AB9 PRO A 349 ? SER A 355 ? PRO A 347 SER A 353 1 ? 7  
HELX_P HELX_P19 AC1 GLY A 367 ? HIS A 377 ? GLY A 365 HIS A 375 1 ? 11 
HELX_P HELX_P20 AC2 TYR A 387 ? ASP A 400 ? TYR A 385 ASP A 398 1 ? 14 
HELX_P HELX_P21 AC3 GLU A 416 ? GLU A 429 ? GLU A 414 GLU A 427 1 ? 14 
HELX_P HELX_P22 AC4 GLY A 430 ? VAL A 451 ? GLY A 428 VAL A 449 1 ? 22 
HELX_P HELX_P23 AC5 GLY A 455 ? SER A 471 ? GLY A 453 SER A 469 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           243 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            241 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    244 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     242 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -2.46 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 6 ? 
# 
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 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA2 5 6 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 63  ? PHE A 67  ? ILE A 61  PHE A 65  
AA1 2 SER A 37  ? ILE A 42  ? SER A 35  ILE A 40  
AA1 3 PRO A 7   ? LEU A 12  ? PRO A 5   LEU A 10  
AA1 4 ASN A 113 ? VAL A 119 ? ASN A 111 VAL A 117 
AA1 5 SER A 136 ? PHE A 141 ? SER A 134 PHE A 139 
AA1 6 GLY A 212 ? GLU A 215 ? GLY A 210 GLU A 213 
AA1 7 VAL A 239 ? ALA A 241 ? VAL A 237 ALA A 239 
AA2 1 GLY A 341 ? SER A 345 ? GLY A 339 SER A 343 
AA2 2 ARG A 300 ? VAL A 305 ? ARG A 298 VAL A 303 
AA2 3 VAL A 271 ? SER A 275 ? VAL A 269 SER A 273 
AA2 4 THR A 359 ? SER A 364 ? THR A 357 SER A 362 
AA2 5 ILE A 381 ? ALA A 383 ? ILE A 379 ALA A 381 
AA2 6 ALA A 404 ? LEU A 405 ? ALA A 402 LEU A 403 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ILE A 66  ? O ILE A 64  N ILE A 42  ? N ILE A 40  
AA1 2 3 O VAL A 41  ? O VAL A 39  N ILE A 11  ? N ILE A 9   
AA1 3 4 N LEU A 12  ? N LEU A 10  O VAL A 118 ? O VAL A 116 
AA1 4 5 N VAL A 119 ? N VAL A 117 O PHE A 140 ? O PHE A 138 
AA1 5 6 N ILE A 139 ? N ILE A 137 O ILE A 214 ? O ILE A 212 
AA1 6 7 N VAL A 213 ? N VAL A 211 O TYR A 240 ? O TYR A 238 
AA2 1 2 O LEU A 342 ? O LEU A 340 N TRP A 303 ? N TRP A 301 
AA2 2 3 O VAL A 304 ? O VAL A 302 N VAL A 274 ? N VAL A 272 
AA2 3 4 N PHE A 273 ? N PHE A 271 O GLY A 361 ? O GLY A 359 
AA2 4 5 N PHE A 362 ? N PHE A 360 O ILE A 382 ? O ILE A 380 
AA2 5 6 N ALA A 383 ? N ALA A 381 O LEU A 405 ? O LEU A 403 
# 
_pdbx_entry_details.entry_id                   8YP7 
_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_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLN 
_pdbx_validate_close_contact.auth_seq_id_1    297 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OE2 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   GLU 
_pdbx_validate_close_contact.auth_seq_id_2    427 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.13 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 220 ? ? -145.33 58.50  
2 1 ASN A 344 ? ? 73.30   -35.37 
3 1 CYS A 364 ? ? 70.25   30.59  
4 1 ASP A 398 ? ? -91.76  -70.80 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   CYS 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    364 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    365 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            149.54 
# 
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 GLY -1  ? A GLY 1   
2  1 Y 1 A ALA 0   ? A ALA 2   
3  1 Y 1 A MET 1   ? A MET 3   
4  1 Y 1 A ALA 2   ? A ALA 4   
5  1 Y 1 A VAL 74  ? A VAL 76  
6  1 Y 1 A VAL 75  ? A VAL 77  
7  1 Y 1 A SER 76  ? A SER 78  
8  1 Y 1 A GLN 77  ? A GLN 79  
9  1 Y 1 A SER 78  ? A SER 80  
10 1 Y 1 A PRO 79  ? A PRO 81  
11 1 Y 1 A ALA 80  ? A ALA 82  
12 1 Y 1 A HIS 81  ? A HIS 83  
13 1 Y 1 A THR 160 ? A THR 162 
14 1 Y 1 A CYS 161 ? A CYS 163 
15 1 Y 1 A GLU 162 ? A GLU 164 
16 1 Y 1 A PHE 163 ? A PHE 165 
17 1 Y 1 A ARG 164 ? A ARG 166 
18 1 Y 1 A HIS 165 ? A HIS 167 
19 1 Y 1 A MET 166 ? A MET 168 
20 1 Y 1 A THR 167 ? A THR 169 
21 1 Y 1 A MET 246 ? A MET 248 
22 1 Y 1 A ASP 247 ? A ASP 249 
23 1 Y 1 A TYR 248 ? A TYR 250 
24 1 Y 1 A ASP 249 ? A ASP 251 
25 1 Y 1 A VAL 250 ? A VAL 252 
26 1 Y 1 A ASP 251 ? A ASP 253 
27 1 Y 1 A ASP 252 ? A ASP 254 
28 1 Y 1 A LYS 471 ? A LYS 473 
29 1 Y 1 A HIS 472 ? A HIS 474 
# 
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           32200030 
_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   2vce 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YP7 
_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]   0.014453 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014119 
_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]   0.010792 
_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   . GLY A 1 5   ? 61.123  26.222 -0.384 1.00 57.71 ? 3   GLY A N   1 
ATOM   2    C CA  . GLY A 1 5   ? 61.584  27.185 0.655  1.00 58.45 ? 3   GLY A CA  1 
ATOM   3    C C   . GLY A 1 5   ? 63.040  26.950 1.051  1.00 62.33 ? 3   GLY A C   1 
ATOM   4    O O   . GLY A 1 5   ? 63.701  26.116 0.400  1.00 63.69 ? 3   GLY A O   1 
ATOM   5    N N   . THR A 1 6   ? 63.541  27.677 2.060  1.00 47.69 ? 4   THR A N   1 
ATOM   6    C CA  . THR A 1 6   ? 64.928  27.563 2.590  1.00 45.93 ? 4   THR A CA  1 
ATOM   7    C C   . THR A 1 6   ? 64.943  27.510 4.118  1.00 38.80 ? 4   THR A C   1 
ATOM   8    O O   . THR A 1 6   ? 64.035  27.994 4.800  1.00 31.51 ? 4   THR A O   1 
ATOM   9    C CB  . THR A 1 6   ? 65.814  28.741 2.182  1.00 50.22 ? 4   THR A CB  1 
ATOM   10   O OG1 . THR A 1 6   ? 65.178  29.883 2.757  1.00 49.79 ? 4   THR A OG1 1 
ATOM   11   C CG2 . THR A 1 6   ? 66.015  28.843 0.679  1.00 52.42 ? 4   THR A CG2 1 
ATOM   12   N N   . PRO A 1 7   ? 66.040  26.977 4.678  1.00 33.74 ? 5   PRO A N   1 
ATOM   13   C CA  . PRO A 1 7   ? 66.077  26.528 6.061  1.00 30.80 ? 5   PRO A CA  1 
ATOM   14   C C   . PRO A 1 7   ? 66.057  27.710 7.033  1.00 26.78 ? 5   PRO A C   1 
ATOM   15   O O   . PRO A 1 7   ? 66.604  28.734 6.736  1.00 26.19 ? 5   PRO A O   1 
ATOM   16   C CB  . PRO A 1 7   ? 67.419  25.774 6.158  1.00 33.46 ? 5   PRO A CB  1 
ATOM   17   C CG  . PRO A 1 7   ? 67.801  25.516 4.732  1.00 34.99 ? 5   PRO A CG  1 
ATOM   18   C CD  . PRO A 1 7   ? 67.318  26.733 3.993  1.00 35.99 ? 5   PRO A CD  1 
ATOM   19   N N   . HIS A 1 8   ? 65.440  27.498 8.180  1.00 27.10 ? 6   HIS A N   1 
ATOM   20   C CA  . HIS A 1 8   ? 65.330  28.499 9.264  1.00 21.96 ? 6   HIS A CA  1 
ATOM   21   C C   . HIS A 1 8   ? 65.868  27.857 10.543 1.00 23.87 ? 6   HIS A C   1 
ATOM   22   O O   . HIS A 1 8   ? 65.489  26.709 10.827 1.00 22.94 ? 6   HIS A O   1 
ATOM   23   C CB  . HIS A 1 8   ? 63.899  28.980 9.428  1.00 22.19 ? 6   HIS A CB  1 
ATOM   24   C CG  . HIS A 1 8   ? 63.806  30.200 10.284 1.00 24.64 ? 6   HIS A CG  1 
ATOM   25   N ND1 . HIS A 1 8   ? 63.993  31.476 9.751  1.00 23.91 ? 6   HIS A ND1 1 
ATOM   26   C CD2 . HIS A 1 8   ? 63.634  30.362 11.613 1.00 25.11 ? 6   HIS A CD2 1 
ATOM   27   C CE1 . HIS A 1 8   ? 63.873  32.363 10.724 1.00 23.88 ? 6   HIS A CE1 1 
ATOM   28   N NE2 . HIS A 1 8   ? 63.664  31.710 11.879 1.00 25.63 ? 6   HIS A NE2 1 
ATOM   29   N N   . ILE A 1 9   ? 66.700  28.568 11.292 1.00 19.91 ? 7   ILE A N   1 
ATOM   30   C CA  . ILE A 1 9   ? 67.254  28.027 12.565 1.00 21.14 ? 7   ILE A CA  1 
ATOM   31   C C   . ILE A 1 9   ? 66.848  28.971 13.680 1.00 21.80 ? 7   ILE A C   1 
ATOM   32   O O   . ILE A 1 9   ? 66.850  30.179 13.435 1.00 22.60 ? 7   ILE A O   1 
ATOM   33   C CB  . ILE A 1 9   ? 68.759  27.799 12.462 1.00 24.73 ? 7   ILE A CB  1 
ATOM   34   C CG1 . ILE A 1 9   ? 69.047  26.662 11.471 1.00 27.51 ? 7   ILE A CG1 1 
ATOM   35   C CG2 . ILE A 1 9   ? 69.347  27.470 13.817 1.00 30.02 ? 7   ILE A CG2 1 
ATOM   36   C CD1 . ILE A 1 9   ? 69.631  27.161 10.232 1.00 30.87 ? 7   ILE A CD1 1 
ATOM   37   N N   . ALA A 1 10  ? 66.401  28.419 14.803 1.00 22.82 ? 8   ALA A N   1 
ATOM   38   C CA  . ALA A 1 10  ? 66.171  29.179 16.049 1.00 21.86 ? 8   ALA A CA  1 
ATOM   39   C C   . ALA A 1 10  ? 67.426  29.066 16.894 1.00 22.07 ? 8   ALA A C   1 
ATOM   40   O O   . ALA A 1 10  ? 68.029  27.970 16.921 1.00 19.94 ? 8   ALA A O   1 
ATOM   41   C CB  . ALA A 1 10  ? 64.945  28.645 16.781 1.00 20.81 ? 8   ALA A CB  1 
ATOM   42   N N   . ILE A 1 11  ? 67.831  30.168 17.543 1.00 20.19 ? 9   ILE A N   1 
ATOM   43   C CA  . ILE A 1 11  ? 68.981  30.173 18.486 1.00 20.67 ? 9   ILE A CA  1 
ATOM   44   C C   . ILE A 1 11  ? 68.468  30.708 19.816 1.00 21.15 ? 9   ILE A C   1 
ATOM   45   O O   . ILE A 1 11  ? 67.824  31.801 19.826 1.00 22.59 ? 9   ILE A O   1 
ATOM   46   C CB  . ILE A 1 11  ? 70.179  30.978 17.926 1.00 21.36 ? 9   ILE A CB  1 
ATOM   47   C CG1 . ILE A 1 11  ? 70.681  30.404 16.594 1.00 24.45 ? 9   ILE A CG1 1 
ATOM   48   C CG2 . ILE A 1 11  ? 71.288  31.029 18.952 1.00 20.47 ? 9   ILE A CG2 1 
ATOM   49   C CD1 . ILE A 1 11  ? 71.733  31.234 15.914 1.00 23.91 ? 9   ILE A CD1 1 
ATOM   50   N N   . LEU A 1 12  ? 68.699  29.965 20.886 1.00 20.60 ? 10  LEU A N   1 
ATOM   51   C CA  . LEU A 1 12  ? 68.285  30.355 22.258 1.00 21.39 ? 10  LEU A CA  1 
ATOM   52   C C   . LEU A 1 12  ? 69.523  30.744 23.070 1.00 21.59 ? 10  LEU A C   1 
ATOM   53   O O   . LEU A 1 12  ? 70.189  29.870 23.616 1.00 23.27 ? 10  LEU A O   1 
ATOM   54   C CB  . LEU A 1 12  ? 67.580  29.147 22.887 1.00 22.37 ? 10  LEU A CB  1 
ATOM   55   C CG  . LEU A 1 12  ? 66.870  29.414 24.214 1.00 22.26 ? 10  LEU A CG  1 
ATOM   56   C CD1 . LEU A 1 12  ? 65.434  29.789 23.973 1.00 25.87 ? 10  LEU A CD1 1 
ATOM   57   C CD2 . LEU A 1 12  ? 66.934  28.207 25.110 1.00 26.50 ? 10  LEU A CD2 1 
ATOM   58   N N   . PRO A 1 13  ? 69.872  32.047 23.201 1.00 23.07 ? 11  PRO A N   1 
ATOM   59   C CA  . PRO A 1 13  ? 71.112  32.455 23.870 1.00 25.69 ? 11  PRO A CA  1 
ATOM   60   C C   . PRO A 1 13  ? 70.926  32.607 25.386 1.00 30.04 ? 11  PRO A C   1 
ATOM   61   O O   . PRO A 1 13  ? 69.798  32.698 25.834 1.00 30.54 ? 11  PRO A O   1 
ATOM   62   C CB  . PRO A 1 13  ? 71.384  33.814 23.239 1.00 25.62 ? 11  PRO A CB  1 
ATOM   63   C CG  . PRO A 1 13  ? 70.023  34.388 23.034 1.00 27.87 ? 11  PRO A CG  1 
ATOM   64   C CD  . PRO A 1 13  ? 69.173  33.197 22.623 1.00 26.43 ? 11  PRO A CD  1 
ATOM   65   N N   . SER A 1 14  ? 72.035  32.625 26.118 1.00 35.55 ? 12  SER A N   1 
ATOM   66   C CA  . SER A 1 14  ? 72.124  33.088 27.524 1.00 37.39 ? 12  SER A CA  1 
ATOM   67   C C   . SER A 1 14  ? 72.080  34.607 27.565 1.00 42.71 ? 12  SER A C   1 
ATOM   68   O O   . SER A 1 14  ? 72.339  35.299 26.566 1.00 38.89 ? 12  SER A O   1 
ATOM   69   C CB  . SER A 1 14  ? 73.349  32.531 28.164 1.00 43.93 ? 12  SER A CB  1 
ATOM   70   O OG  . SER A 1 14  ? 73.170  31.126 28.345 1.00 49.39 ? 12  SER A OG  1 
ATOM   71   N N   . PRO A 1 15  ? 71.737  35.157 28.748 1.00 48.16 ? 13  PRO A N   1 
ATOM   72   C CA  . PRO A 1 15  ? 71.939  36.576 29.013 1.00 49.83 ? 13  PRO A CA  1 
ATOM   73   C C   . PRO A 1 15  ? 73.459  36.808 29.025 1.00 43.45 ? 13  PRO A C   1 
ATOM   74   O O   . PRO A 1 15  ? 74.221  35.882 29.209 1.00 45.80 ? 13  PRO A O   1 
ATOM   75   C CB  . PRO A 1 15  ? 71.278  36.835 30.383 1.00 54.03 ? 13  PRO A CB  1 
ATOM   76   C CG  . PRO A 1 15  ? 70.672  35.490 30.828 1.00 51.95 ? 13  PRO A CG  1 
ATOM   77   C CD  . PRO A 1 15  ? 71.236  34.418 29.919 1.00 48.31 ? 13  PRO A CD  1 
ATOM   78   N N   . GLY A 1 16  ? 73.879  38.044 28.807 1.00 46.53 ? 14  GLY A N   1 
ATOM   79   C CA  . GLY A 1 16  ? 75.298  38.406 28.902 1.00 45.18 ? 14  GLY A CA  1 
ATOM   80   C C   . GLY A 1 16  ? 75.936  38.471 27.540 1.00 45.88 ? 14  GLY A C   1 
ATOM   81   O O   . GLY A 1 16  ? 75.817  37.509 26.726 1.00 45.55 ? 14  GLY A O   1 
ATOM   82   N N   . MET A 1 17  ? 76.626  39.572 27.324 1.00 43.63 ? 15  MET A N   1 
ATOM   83   C CA  . MET A 1 17  ? 77.329  39.869 26.064 1.00 46.93 ? 15  MET A CA  1 
ATOM   84   C C   . MET A 1 17  ? 78.256  38.702 25.705 1.00 41.44 ? 15  MET A C   1 
ATOM   85   O O   . MET A 1 17  ? 78.384  38.443 24.506 1.00 37.07 ? 15  MET A O   1 
ATOM   86   C CB  . MET A 1 17  ? 78.096  41.179 26.238 1.00 48.73 ? 15  MET A CB  1 
ATOM   87   C CG  . MET A 1 17  ? 77.166  42.306 26.637 1.00 49.30 ? 15  MET A CG  1 
ATOM   88   S SD  . MET A 1 17  ? 75.732  42.354 25.538 1.00 49.81 ? 15  MET A SD  1 
ATOM   89   C CE  . MET A 1 17  ? 76.557  42.807 24.024 1.00 45.30 ? 15  MET A CE  1 
ATOM   90   N N   . GLY A 1 18  ? 78.843  38.019 26.700 1.00 39.97 ? 16  GLY A N   1 
ATOM   91   C CA  . GLY A 1 18  ? 79.868  36.982 26.483 1.00 38.05 ? 16  GLY A CA  1 
ATOM   92   C C   . GLY A 1 18  ? 79.314  35.781 25.719 1.00 35.20 ? 16  GLY A C   1 
ATOM   93   O O   . GLY A 1 18  ? 80.057  35.162 24.962 1.00 38.60 ? 16  GLY A O   1 
ATOM   94   N N   . HIS A 1 19  ? 78.058  35.419 25.952 1.00 31.98 ? 17  HIS A N   1 
ATOM   95   C CA  . HIS A 1 19  ? 77.376  34.308 25.242 1.00 33.42 ? 17  HIS A CA  1 
ATOM   96   C C   . HIS A 1 19  ? 76.768  34.819 23.937 1.00 31.57 ? 17  HIS A C   1 
ATOM   97   O O   . HIS A 1 19  ? 76.794  34.060 22.941 1.00 29.66 ? 17  HIS A O   1 
ATOM   98   C CB  . HIS A 1 19  ? 76.316  33.666 26.144 1.00 37.10 ? 17  HIS A CB  1 
ATOM   99   C CG  . HIS A 1 19  ? 76.901  32.987 27.327 1.00 47.56 ? 17  HIS A CG  1 
ATOM   100  N ND1 . HIS A 1 19  ? 77.410  33.697 28.412 1.00 54.55 ? 17  HIS A ND1 1 
ATOM   101  C CD2 . HIS A 1 19  ? 77.087  31.677 27.597 1.00 50.69 ? 17  HIS A CD2 1 
ATOM   102  C CE1 . HIS A 1 19  ? 77.887  32.842 29.298 1.00 53.92 ? 17  HIS A CE1 1 
ATOM   103  N NE2 . HIS A 1 19  ? 77.708  31.599 28.815 1.00 49.43 ? 17  HIS A NE2 1 
ATOM   104  N N   . LEU A 1 20  ? 76.225  36.046 23.938 1.00 26.96 ? 18  LEU A N   1 
ATOM   105  C CA  . LEU A 1 20  ? 75.448  36.559 22.769 1.00 26.89 ? 18  LEU A CA  1 
ATOM   106  C C   . LEU A 1 20  ? 76.399  36.876 21.631 1.00 25.20 ? 18  LEU A C   1 
ATOM   107  O O   . LEU A 1 20  ? 76.079  36.511 20.484 1.00 24.90 ? 18  LEU A O   1 
ATOM   108  C CB  . LEU A 1 20  ? 74.642  37.822 23.114 1.00 25.78 ? 18  LEU A CB  1 
ATOM   109  C CG  . LEU A 1 20  ? 73.773  38.340 21.966 1.00 25.82 ? 18  LEU A CG  1 
ATOM   110  C CD1 . LEU A 1 20  ? 72.716  37.308 21.544 1.00 25.39 ? 18  LEU A CD1 1 
ATOM   111  C CD2 . LEU A 1 20  ? 73.070  39.634 22.344 1.00 27.84 ? 18  LEU A CD2 1 
ATOM   112  N N   . ILE A 1 21  ? 77.526  37.541 21.921 1.00 25.57 ? 19  ILE A N   1 
ATOM   113  C CA  . ILE A 1 21  ? 78.427  38.046 20.854 1.00 27.66 ? 19  ILE A CA  1 
ATOM   114  C C   . ILE A 1 21  ? 78.826  36.885 19.940 1.00 25.57 ? 19  ILE A C   1 
ATOM   115  O O   . ILE A 1 21  ? 78.705  36.999 18.716 1.00 21.72 ? 19  ILE A O   1 
ATOM   116  C CB  . ILE A 1 21  ? 79.630  38.813 21.436 1.00 29.25 ? 19  ILE A CB  1 
ATOM   117  C CG1 . ILE A 1 21  ? 79.154  40.172 21.960 1.00 32.77 ? 19  ILE A CG1 1 
ATOM   118  C CG2 . ILE A 1 21  ? 80.720  38.983 20.387 1.00 30.92 ? 19  ILE A CG2 1 
ATOM   119  C CD1 . ILE A 1 21  ? 80.055  40.800 22.993 1.00 35.54 ? 19  ILE A CD1 1 
ATOM   120  N N   . PRO A 1 22  ? 79.371  35.764 20.448 1.00 22.42 ? 20  PRO A N   1 
ATOM   121  C CA  . PRO A 1 22  ? 79.805  34.706 19.526 1.00 23.71 ? 20  PRO A CA  1 
ATOM   122  C C   . PRO A 1 22  ? 78.641  34.031 18.777 1.00 22.58 ? 20  PRO A C   1 
ATOM   123  O O   . PRO A 1 22  ? 78.820  33.635 17.633 1.00 23.98 ? 20  PRO A O   1 
ATOM   124  C CB  . PRO A 1 22  ? 80.555  33.672 20.396 1.00 25.17 ? 20  PRO A CB  1 
ATOM   125  C CG  . PRO A 1 22  ? 80.335  34.104 21.825 1.00 27.74 ? 20  PRO A CG  1 
ATOM   126  C CD  . PRO A 1 22  ? 79.714  35.491 21.845 1.00 26.33 ? 20  PRO A CD  1 
ATOM   127  N N   . MET A 1 23  ? 77.473  33.918 19.405 1.00 23.31 ? 21  MET A N   1 
ATOM   128  C CA  . MET A 1 23  ? 76.275  33.364 18.721 1.00 25.04 ? 21  MET A CA  1 
ATOM   129  C C   . MET A 1 23  ? 75.830  34.320 17.609 1.00 24.30 ? 21  MET A C   1 
ATOM   130  O O   . MET A 1 23  ? 75.453  33.843 16.517 1.00 21.10 ? 21  MET A O   1 
ATOM   131  C CB  . MET A 1 23  ? 75.114  33.138 19.687 1.00 24.88 ? 21  MET A CB  1 
ATOM   132  C CG  . MET A 1 23  ? 75.295  31.943 20.570 1.00 27.87 ? 21  MET A CG  1 
ATOM   133  S SD  . MET A 1 23  ? 73.844  31.788 21.663 1.00 30.79 ? 21  MET A SD  1 
ATOM   134  C CE  . MET A 1 23  ? 73.666  30.006 21.776 1.00 31.07 ? 21  MET A CE  1 
ATOM   135  N N   . ALA A 1 24  ? 75.868  35.628 17.866 1.00 20.92 ? 22  ALA A N   1 
ATOM   136  C CA  . ALA A 1 24  ? 75.540  36.632 16.833 1.00 22.42 ? 22  ALA A CA  1 
ATOM   137  C C   . ALA A 1 24  ? 76.531  36.521 15.690 1.00 20.71 ? 22  ALA A C   1 
ATOM   138  O O   . ALA A 1 24  ? 76.090  36.638 14.518 1.00 22.46 ? 22  ALA A O   1 
ATOM   139  C CB  . ALA A 1 24  ? 75.561  38.025 17.410 1.00 24.33 ? 22  ALA A CB  1 
ATOM   140  N N   . GLU A 1 25  ? 77.817  36.356 15.996 1.00 21.40 ? 23  GLU A N   1 
ATOM   141  C CA  . GLU A 1 25  ? 78.849  36.284 14.922 1.00 26.54 ? 23  GLU A CA  1 
ATOM   142  C C   . GLU A 1 25  ? 78.699  34.970 14.142 1.00 23.22 ? 23  GLU A C   1 
ATOM   143  O O   . GLU A 1 25  ? 78.845  34.974 12.915 1.00 22.05 ? 23  GLU A O   1 
ATOM   144  C CB  . GLU A 1 25  ? 80.260  36.456 15.489 1.00 29.56 ? 23  GLU A CB  1 
ATOM   145  C CG  . GLU A 1 25  ? 81.337  36.524 14.411 1.00 39.82 ? 23  GLU A CG  1 
ATOM   146  C CD  . GLU A 1 25  ? 81.163  37.585 13.322 1.00 42.03 ? 23  GLU A CD  1 
ATOM   147  O OE1 . GLU A 1 25  ? 81.491  37.294 12.134 1.00 41.16 ? 23  GLU A OE1 1 
ATOM   148  O OE2 . GLU A 1 25  ? 80.680  38.678 13.657 1.00 40.06 ? 23  GLU A OE2 1 
ATOM   149  N N   . PHE A 1 26  ? 78.398  33.875 14.832 1.00 21.74 ? 24  PHE A N   1 
ATOM   150  C CA  . PHE A 1 26  ? 78.031  32.620 14.137 1.00 21.07 ? 24  PHE A CA  1 
ATOM   151  C C   . PHE A 1 26  ? 76.877  32.892 13.154 1.00 20.15 ? 24  PHE A C   1 
ATOM   152  O O   . PHE A 1 26  ? 76.971  32.478 11.993 1.00 20.65 ? 24  PHE A O   1 
ATOM   153  C CB  . PHE A 1 26  ? 77.687  31.521 15.137 1.00 21.43 ? 24  PHE A CB  1 
ATOM   154  C CG  . PHE A 1 26  ? 77.276  30.259 14.412 1.00 23.40 ? 24  PHE A CG  1 
ATOM   155  C CD1 . PHE A 1 26  ? 78.230  29.430 13.835 1.00 26.72 ? 24  PHE A CD1 1 
ATOM   156  C CD2 . PHE A 1 26  ? 75.937  29.941 14.267 1.00 24.40 ? 24  PHE A CD2 1 
ATOM   157  C CE1 . PHE A 1 26  ? 77.844  28.272 13.158 1.00 26.40 ? 24  PHE A CE1 1 
ATOM   158  C CE2 . PHE A 1 26  ? 75.553  28.825 13.532 1.00 27.93 ? 24  PHE A CE2 1 
ATOM   159  C CZ  . PHE A 1 26  ? 76.511  27.998 12.969 1.00 24.96 ? 24  PHE A CZ  1 
ATOM   160  N N   . ALA A 1 27  ? 75.791  33.530 13.603 1.00 21.76 ? 25  ALA A N   1 
ATOM   161  C CA  . ALA A 1 27  ? 74.546  33.762 12.828 1.00 20.00 ? 25  ALA A CA  1 
ATOM   162  C C   . ALA A 1 27  ? 74.877  34.618 11.608 1.00 23.01 ? 25  ALA A C   1 
ATOM   163  O O   . ALA A 1 27  ? 74.467  34.245 10.478 1.00 21.02 ? 25  ALA A O   1 
ATOM   164  C CB  . ALA A 1 27  ? 73.476  34.397 13.708 1.00 20.50 ? 25  ALA A CB  1 
ATOM   165  N N   . LYS A 1 28  ? 75.664  35.680 11.817 1.00 22.93 ? 26  LYS A N   1 
ATOM   166  C CA  . LYS A 1 28  ? 76.114  36.547 10.705 1.00 24.53 ? 26  LYS A CA  1 
ATOM   167  C C   . LYS A 1 28  ? 76.941  35.745 9.697  1.00 22.51 ? 26  LYS A C   1 
ATOM   168  O O   . LYS A 1 28  ? 76.757  35.960 8.485  1.00 23.17 ? 26  LYS A O   1 
ATOM   169  C CB  . LYS A 1 28  ? 76.899  37.729 11.269 1.00 27.66 ? 26  LYS A CB  1 
ATOM   170  C CG  . LYS A 1 28  ? 75.926  38.774 11.800 1.00 32.47 ? 26  LYS A CG  1 
ATOM   171  C CD  . LYS A 1 28  ? 76.456  39.906 12.634 1.00 35.45 ? 26  LYS A CD  1 
ATOM   172  C CE  . LYS A 1 28  ? 77.942  39.997 12.773 1.00 40.76 ? 26  LYS A CE  1 
ATOM   173  N NZ  . LYS A 1 28  ? 78.281  41.238 13.516 1.00 46.49 ? 26  LYS A NZ  1 
ATOM   174  N N   . ARG A 1 29  ? 77.864  34.927 10.173 1.00 23.62 ? 27  ARG A N   1 
ATOM   175  C CA  . ARG A 1 29  ? 78.743  34.148 9.265  1.00 29.00 ? 27  ARG A CA  1 
ATOM   176  C C   . ARG A 1 29  ? 77.871  33.168 8.462  1.00 27.27 ? 27  ARG A C   1 
ATOM   177  O O   . ARG A 1 29  ? 78.098  33.035 7.223  1.00 25.64 ? 27  ARG A O   1 
ATOM   178  C CB  . ARG A 1 29  ? 79.842  33.440 10.057 1.00 32.40 ? 27  ARG A CB  1 
ATOM   179  C CG  . ARG A 1 29  ? 81.186  33.434 9.353  1.00 44.63 ? 27  ARG A CG  1 
ATOM   180  C CD  . ARG A 1 29  ? 82.339  33.130 10.260 1.00 46.37 ? 27  ARG A CD  1 
ATOM   181  N NE  . ARG A 1 29  ? 82.680  34.256 11.115 1.00 49.84 ? 27  ARG A NE  1 
ATOM   182  C CZ  . ARG A 1 29  ? 83.851  34.388 11.741 1.00 53.85 ? 27  ARG A CZ  1 
ATOM   183  N NH1 . ARG A 1 29  ? 84.070  35.426 12.525 1.00 55.42 ? 27  ARG A NH1 1 
ATOM   184  N NH2 . ARG A 1 29  ? 84.809  33.486 11.585 1.00 52.62 ? 27  ARG A NH2 1 
ATOM   185  N N   . LEU A 1 30  ? 76.873  32.534 9.093  1.00 25.06 ? 28  LEU A N   1 
ATOM   186  C CA  . LEU A 1 30  ? 76.007  31.559 8.378  1.00 23.65 ? 28  LEU A CA  1 
ATOM   187  C C   . LEU A 1 30  ? 75.191  32.252 7.279  1.00 25.41 ? 28  LEU A C   1 
ATOM   188  O O   . LEU A 1 30  ? 75.154  31.749 6.179  1.00 25.83 ? 28  LEU A O   1 
ATOM   189  C CB  . LEU A 1 30  ? 75.087  30.868 9.378  1.00 23.01 ? 28  LEU A CB  1 
ATOM   190  C CG  . LEU A 1 30  ? 74.147  29.853 8.752  1.00 25.01 ? 28  LEU A CG  1 
ATOM   191  C CD1 . LEU A 1 30  ? 74.978  28.663 8.246  1.00 23.71 ? 28  LEU A CD1 1 
ATOM   192  C CD2 . LEU A 1 30  ? 73.090  29.400 9.748  1.00 25.90 ? 28  LEU A CD2 1 
ATOM   193  N N   . VAL A 1 31  ? 74.533  33.372 7.564  1.00 24.13 ? 29  VAL A N   1 
ATOM   194  C CA  . VAL A 1 31  ? 73.646  34.036 6.578  1.00 24.06 ? 29  VAL A CA  1 
ATOM   195  C C   . VAL A 1 31  ? 74.494  34.793 5.547  1.00 26.93 ? 29  VAL A C   1 
ATOM   196  O O   . VAL A 1 31  ? 73.935  35.136 4.527  1.00 26.81 ? 29  VAL A O   1 
ATOM   197  C CB  . VAL A 1 31  ? 72.584  34.974 7.188  1.00 23.94 ? 29  VAL A CB  1 
ATOM   198  C CG1 . VAL A 1 31  ? 71.712  34.237 8.180  1.00 27.50 ? 29  VAL A CG1 1 
ATOM   199  C CG2 . VAL A 1 31  ? 73.153  36.248 7.780  1.00 25.93 ? 29  VAL A CG2 1 
ATOM   200  N N   . HIS A 1 32  ? 75.776  35.037 5.798  1.00 26.74 ? 30  HIS A N   1 
ATOM   201  C CA  . HIS A 1 32  ? 76.623  35.809 4.859  1.00 28.99 ? 30  HIS A CA  1 
ATOM   202  C C   . HIS A 1 32  ? 76.719  35.032 3.540  1.00 28.61 ? 30  HIS A C   1 
ATOM   203  O O   . HIS A 1 32  ? 76.503  35.646 2.463  1.00 25.57 ? 30  HIS A O   1 
ATOM   204  C CB  . HIS A 1 32  ? 78.010  36.064 5.455  1.00 33.81 ? 30  HIS A CB  1 
ATOM   205  C CG  . HIS A 1 32  ? 78.867  37.068 4.762  1.00 40.80 ? 30  HIS A CG  1 
ATOM   206  N ND1 . HIS A 1 32  ? 78.368  37.994 3.845  1.00 48.07 ? 30  HIS A ND1 1 
ATOM   207  C CD2 . HIS A 1 32  ? 80.177  37.354 4.929  1.00 44.67 ? 30  HIS A CD2 1 
ATOM   208  C CE1 . HIS A 1 32  ? 79.348  38.783 3.456  1.00 46.31 ? 30  HIS A CE1 1 
ATOM   209  N NE2 . HIS A 1 32  ? 80.474  38.391 4.089  1.00 49.06 ? 30  HIS A NE2 1 
ATOM   210  N N   . HIS A 1 33  ? 76.968  33.731 3.604  1.00 25.07 ? 31  HIS A N   1 
ATOM   211  C CA  . HIS A 1 33  ? 77.200  32.923 2.366  1.00 28.83 ? 31  HIS A CA  1 
ATOM   212  C C   . HIS A 1 33  ? 76.188  31.784 2.221  1.00 28.91 ? 31  HIS A C   1 
ATOM   213  O O   . HIS A 1 33  ? 76.495  30.874 1.448  1.00 26.10 ? 31  HIS A O   1 
ATOM   214  C CB  . HIS A 1 33  ? 78.644  32.416 2.315  1.00 33.95 ? 31  HIS A CB  1 
ATOM   215  C CG  . HIS A 1 33  ? 79.625  33.532 2.290  1.00 39.85 ? 31  HIS A CG  1 
ATOM   216  N ND1 . HIS A 1 33  ? 79.581  34.532 1.306  1.00 44.03 ? 31  HIS A ND1 1 
ATOM   217  C CD2 . HIS A 1 33  ? 80.609  33.876 3.150  1.00 44.25 ? 31  HIS A CD2 1 
ATOM   218  C CE1 . HIS A 1 33  ? 80.513  35.428 1.567  1.00 40.17 ? 31  HIS A CE1 1 
ATOM   219  N NE2 . HIS A 1 33  ? 81.159  35.043 2.679  1.00 44.86 ? 31  HIS A NE2 1 
ATOM   220  N N   . HIS A 1 34  ? 75.050  31.827 2.931  1.00 25.42 ? 32  HIS A N   1 
ATOM   221  C CA  . HIS A 1 34  ? 73.933  30.862 2.827  1.00 24.54 ? 32  HIS A CA  1 
ATOM   222  C C   . HIS A 1 34  ? 72.590  31.574 2.835  1.00 26.53 ? 32  HIS A C   1 
ATOM   223  O O   . HIS A 1 34  ? 72.385  32.464 3.669  1.00 26.30 ? 32  HIS A O   1 
ATOM   224  C CB  . HIS A 1 34  ? 74.014  29.818 3.944  1.00 24.36 ? 32  HIS A CB  1 
ATOM   225  C CG  . HIS A 1 34  ? 75.201  28.943 3.869  1.00 25.27 ? 32  HIS A CG  1 
ATOM   226  N ND1 . HIS A 1 34  ? 76.411  29.275 4.446  1.00 24.42 ? 32  HIS A ND1 1 
ATOM   227  C CD2 . HIS A 1 34  ? 75.368  27.726 3.309  1.00 24.24 ? 32  HIS A CD2 1 
ATOM   228  C CE1 . HIS A 1 34  ? 77.270  28.311 4.213  1.00 25.66 ? 32  HIS A CE1 1 
ATOM   229  N NE2 . HIS A 1 34  ? 76.660  27.373 3.506  1.00 23.02 ? 32  HIS A NE2 1 
ATOM   230  N N   . ASN A 1 35  ? 71.643  31.130 1.999  1.00 26.91 ? 33  ASN A N   1 
ATOM   231  C CA  . ASN A 1 35  ? 70.267  31.677 1.969  1.00 31.17 ? 33  ASN A CA  1 
ATOM   232  C C   . ASN A 1 35  ? 69.466  31.071 3.135  1.00 30.05 ? 33  ASN A C   1 
ATOM   233  O O   . ASN A 1 35  ? 68.467  30.400 2.886  1.00 35.63 ? 33  ASN A O   1 
ATOM   234  C CB  . ASN A 1 35  ? 69.590  31.371 0.629  1.00 35.73 ? 33  ASN A CB  1 
ATOM   235  C CG  . ASN A 1 35  ? 68.290  32.113 0.373  1.00 41.77 ? 33  ASN A CG  1 
ATOM   236  O OD1 . ASN A 1 35  ? 67.986  33.133 1.010  1.00 45.29 ? 33  ASN A OD1 1 
ATOM   237  N ND2 . ASN A 1 35  ? 67.560  31.644 -0.633 1.00 44.47 ? 33  ASN A ND2 1 
ATOM   238  N N   . PHE A 1 36  ? 69.930  31.224 4.366  1.00 26.01 ? 34  PHE A N   1 
ATOM   239  C CA  . PHE A 1 36  ? 69.231  30.719 5.564  1.00 23.63 ? 34  PHE A CA  1 
ATOM   240  C C   . PHE A 1 36  ? 68.665  31.933 6.290  1.00 26.45 ? 34  PHE A C   1 
ATOM   241  O O   . PHE A 1 36  ? 69.163  33.054 6.094  1.00 25.69 ? 34  PHE A O   1 
ATOM   242  C CB  . PHE A 1 36  ? 70.204  29.898 6.429  1.00 24.88 ? 34  PHE A CB  1 
ATOM   243  C CG  . PHE A 1 36  ? 70.576  28.545 5.877  1.00 26.25 ? 34  PHE A CG  1 
ATOM   244  C CD1 . PHE A 1 36  ? 70.437  28.244 4.524  1.00 35.36 ? 34  PHE A CD1 1 
ATOM   245  C CD2 . PHE A 1 36  ? 71.101  27.570 6.700  1.00 31.57 ? 34  PHE A CD2 1 
ATOM   246  C CE1 . PHE A 1 36  ? 70.794  26.999 4.020  1.00 34.02 ? 34  PHE A CE1 1 
ATOM   247  C CE2 . PHE A 1 36  ? 71.464  26.331 6.196  1.00 30.69 ? 34  PHE A CE2 1 
ATOM   248  C CZ  . PHE A 1 36  ? 71.319  26.048 4.865  1.00 31.89 ? 34  PHE A CZ  1 
ATOM   249  N N   . SER A 1 37  ? 67.678  31.745 7.153  1.00 23.22 ? 35  SER A N   1 
ATOM   250  C CA  . SER A 1 37  ? 67.217  32.847 8.031  1.00 22.58 ? 35  SER A CA  1 
ATOM   251  C C   . SER A 1 37  ? 67.227  32.310 9.463  1.00 22.99 ? 35  SER A C   1 
ATOM   252  O O   . SER A 1 37  ? 67.255  31.062 9.626  1.00 19.73 ? 35  SER A O   1 
ATOM   253  C CB  . SER A 1 37  ? 65.921  33.370 7.514  1.00 24.31 ? 35  SER A CB  1 
ATOM   254  O OG  . SER A 1 37  ? 64.956  32.355 7.440  1.00 25.62 ? 35  SER A OG  1 
ATOM   255  N N   . ILE A 1 38  ? 67.264  33.191 10.461 1.00 20.17 ? 36  ILE A N   1 
ATOM   256  C CA  . ILE A 1 38  ? 67.539  32.815 11.869 1.00 22.05 ? 36  ILE A CA  1 
ATOM   257  C C   . ILE A 1 38  ? 66.597  33.657 12.718 1.00 22.06 ? 36  ILE A C   1 
ATOM   258  O O   . ILE A 1 38  ? 66.429  34.829 12.342 1.00 23.12 ? 36  ILE A O   1 
ATOM   259  C CB  . ILE A 1 38  ? 69.021  33.061 12.241 1.00 21.84 ? 36  ILE A CB  1 
ATOM   260  C CG1 . ILE A 1 38  ? 69.992  32.151 11.480 1.00 24.41 ? 36  ILE A CG1 1 
ATOM   261  C CG2 . ILE A 1 38  ? 69.236  32.917 13.747 1.00 22.08 ? 36  ILE A CG2 1 
ATOM   262  C CD1 . ILE A 1 38  ? 71.442  32.542 11.629 1.00 26.19 ? 36  ILE A CD1 1 
ATOM   263  N N   . THR A 1 39  ? 66.089  33.094 13.815 1.00 22.91 ? 37  THR A N   1 
ATOM   264  C CA  . THR A 1 39  ? 65.419  33.830 14.918 1.00 22.62 ? 37  THR A CA  1 
ATOM   265  C C   . THR A 1 39  ? 66.145  33.542 16.223 1.00 21.79 ? 37  THR A C   1 
ATOM   266  O O   . THR A 1 39  ? 66.331  32.351 16.594 1.00 22.53 ? 37  THR A O   1 
ATOM   267  C CB  . THR A 1 39  ? 63.924  33.490 15.046 1.00 25.03 ? 37  THR A CB  1 
ATOM   268  O OG1 . THR A 1 39  ? 63.268  33.602 13.787 1.00 22.40 ? 37  THR A OG1 1 
ATOM   269  C CG2 . THR A 1 39  ? 63.190  34.351 16.053 1.00 23.80 ? 37  THR A CG2 1 
ATOM   270  N N   . PHE A 1 40  ? 66.619  34.586 16.870 1.00 19.27 ? 38  PHE A N   1 
ATOM   271  C CA  . PHE A 1 40  ? 67.062  34.519 18.279 1.00 21.72 ? 38  PHE A CA  1 
ATOM   272  C C   . PHE A 1 40  ? 65.795  34.545 19.140 1.00 22.51 ? 38  PHE A C   1 
ATOM   273  O O   . PHE A 1 40  ? 64.996  35.474 19.045 1.00 24.30 ? 38  PHE A O   1 
ATOM   274  C CB  . PHE A 1 40  ? 68.016  35.665 18.614 1.00 22.74 ? 38  PHE A CB  1 
ATOM   275  C CG  . PHE A 1 40  ? 69.429  35.415 18.206 1.00 22.37 ? 38  PHE A CG  1 
ATOM   276  C CD1 . PHE A 1 40  ? 69.828  35.674 16.909 1.00 24.35 ? 38  PHE A CD1 1 
ATOM   277  C CD2 . PHE A 1 40  ? 70.342  34.888 19.105 1.00 23.03 ? 38  PHE A CD2 1 
ATOM   278  C CE1 . PHE A 1 40  ? 71.114  35.380 16.498 1.00 22.38 ? 38  PHE A CE1 1 
ATOM   279  C CE2 . PHE A 1 40  ? 71.651  34.663 18.716 1.00 22.85 ? 38  PHE A CE2 1 
ATOM   280  C CZ  . PHE A 1 40  ? 72.037  34.943 17.424 1.00 23.25 ? 38  PHE A CZ  1 
ATOM   281  N N   . VAL A 1 41  ? 65.613  33.513 19.937 1.00 24.97 ? 39  VAL A N   1 
ATOM   282  C CA  . VAL A 1 41  ? 64.438  33.338 20.814 1.00 25.83 ? 39  VAL A CA  1 
ATOM   283  C C   . VAL A 1 41  ? 64.985  33.426 22.231 1.00 30.02 ? 39  VAL A C   1 
ATOM   284  O O   . VAL A 1 41  ? 65.809  32.597 22.586 1.00 29.26 ? 39  VAL A O   1 
ATOM   285  C CB  . VAL A 1 41  ? 63.687  32.019 20.558 1.00 26.64 ? 39  VAL A CB  1 
ATOM   286  C CG1 . VAL A 1 41  ? 62.586  31.823 21.589 1.00 28.78 ? 39  VAL A CG1 1 
ATOM   287  C CG2 . VAL A 1 41  ? 63.090  31.996 19.164 1.00 27.55 ? 39  VAL A CG2 1 
ATOM   288  N N   . ILE A 1 42  ? 64.641  34.497 22.942 1.00 28.00 ? 40  ILE A N   1 
ATOM   289  C CA  . ILE A 1 42  ? 65.420  34.945 24.115 1.00 26.92 ? 40  ILE A CA  1 
ATOM   290  C C   . ILE A 1 42  ? 64.570  34.757 25.366 1.00 26.53 ? 40  ILE A C   1 
ATOM   291  O O   . ILE A 1 42  ? 63.578  35.450 25.549 1.00 25.36 ? 40  ILE A O   1 
ATOM   292  C CB  . ILE A 1 42  ? 65.907  36.395 23.949 1.00 29.76 ? 40  ILE A CB  1 
ATOM   293  C CG1 . ILE A 1 42  ? 66.808  36.561 22.711 1.00 33.19 ? 40  ILE A CG1 1 
ATOM   294  C CG2 . ILE A 1 42  ? 66.607  36.843 25.217 1.00 31.24 ? 40  ILE A CG2 1 
ATOM   295  C CD1 . ILE A 1 42  ? 66.524  37.777 21.917 1.00 38.07 ? 40  ILE A CD1 1 
ATOM   296  N N   . PRO A 1 43  ? 64.955  33.809 26.243 1.00 28.42 ? 41  PRO A N   1 
ATOM   297  C CA  . PRO A 1 43  ? 64.316  33.655 27.550 1.00 29.67 ? 41  PRO A CA  1 
ATOM   298  C C   . PRO A 1 43  ? 64.844  34.770 28.460 1.00 28.11 ? 41  PRO A C   1 
ATOM   299  O O   . PRO A 1 43  ? 66.006  35.085 28.341 1.00 28.03 ? 41  PRO A O   1 
ATOM   300  C CB  . PRO A 1 43  ? 64.813  32.311 28.057 1.00 29.91 ? 41  PRO A CB  1 
ATOM   301  C CG  . PRO A 1 43  ? 65.447  31.683 26.824 1.00 35.04 ? 41  PRO A CG  1 
ATOM   302  C CD  . PRO A 1 43  ? 66.036  32.837 26.043 1.00 28.99 ? 41  PRO A CD  1 
ATOM   303  N N   . THR A 1 44  ? 64.021  35.314 29.359 1.00 31.39 ? 42  THR A N   1 
ATOM   304  C CA  . THR A 1 44  ? 64.438  36.450 30.226 1.00 33.77 ? 42  THR A CA  1 
ATOM   305  C C   . THR A 1 44  ? 63.816  36.279 31.611 1.00 31.65 ? 42  THR A C   1 
ATOM   306  O O   . THR A 1 44  ? 62.671  35.787 31.678 1.00 30.35 ? 42  THR A O   1 
ATOM   307  C CB  . THR A 1 44  ? 64.090  37.815 29.606 1.00 34.27 ? 42  THR A CB  1 
ATOM   308  O OG1 . THR A 1 44  ? 62.680  37.912 29.434 1.00 38.93 ? 42  THR A OG1 1 
ATOM   309  C CG2 . THR A 1 44  ? 64.769  38.026 28.270 1.00 40.74 ? 42  THR A CG2 1 
ATOM   310  N N   . ASP A 1 45  ? 64.538  36.687 32.647 1.00 34.69 ? 43  ASP A N   1 
ATOM   311  C CA  . ASP A 1 45  ? 63.976  36.817 34.025 1.00 36.79 ? 43  ASP A CA  1 
ATOM   312  C C   . ASP A 1 45  ? 63.911  38.298 34.426 1.00 41.65 ? 43  ASP A C   1 
ATOM   313  O O   . ASP A 1 45  ? 63.536  38.596 35.564 1.00 40.06 ? 43  ASP A O   1 
ATOM   314  C CB  . ASP A 1 45  ? 64.774  36.008 35.042 1.00 38.72 ? 43  ASP A CB  1 
ATOM   315  C CG  . ASP A 1 45  ? 66.173  36.530 35.304 1.00 40.61 ? 43  ASP A CG  1 
ATOM   316  O OD1 . ASP A 1 45  ? 66.646  37.362 34.524 1.00 44.92 ? 43  ASP A OD1 1 
ATOM   317  O OD2 . ASP A 1 45  ? 66.789  36.062 36.256 1.00 45.93 ? 43  ASP A OD2 1 
ATOM   318  N N   . GLY A 1 46  ? 64.156  39.195 33.486 1.00 41.99 ? 44  GLY A N   1 
ATOM   319  C CA  . GLY A 1 46  ? 64.141  40.643 33.725 1.00 43.32 ? 44  GLY A CA  1 
ATOM   320  C C   . GLY A 1 46  ? 64.505  41.370 32.441 1.00 41.28 ? 44  GLY A C   1 
ATOM   321  O O   . GLY A 1 46  ? 64.936  40.735 31.472 1.00 33.40 ? 44  GLY A O   1 
ATOM   322  N N   . PRO A 1 47  ? 64.422  42.711 32.429 1.00 36.63 ? 45  PRO A N   1 
ATOM   323  C CA  . PRO A 1 47  ? 64.638  43.461 31.190 1.00 35.21 ? 45  PRO A CA  1 
ATOM   324  C C   . PRO A 1 47  ? 66.048  43.189 30.678 1.00 31.37 ? 45  PRO A C   1 
ATOM   325  O O   . PRO A 1 47  ? 67.018  43.127 31.426 1.00 30.14 ? 45  PRO A O   1 
ATOM   326  C CB  . PRO A 1 47  ? 64.383  44.906 31.623 1.00 34.55 ? 45  PRO A CB  1 
ATOM   327  C CG  . PRO A 1 47  ? 64.668  44.913 33.098 1.00 37.11 ? 45  PRO A CG  1 
ATOM   328  C CD  . PRO A 1 47  ? 64.194  43.575 33.604 1.00 36.41 ? 45  PRO A CD  1 
ATOM   329  N N   . PRO A 1 48  ? 66.227  42.895 29.382 1.00 36.40 ? 46  PRO A N   1 
ATOM   330  C CA  . PRO A 1 48  ? 67.575  42.772 28.844 1.00 35.45 ? 46  PRO A CA  1 
ATOM   331  C C   . PRO A 1 48  ? 68.289  44.137 28.940 1.00 32.99 ? 46  PRO A C   1 
ATOM   332  O O   . PRO A 1 48  ? 67.620  45.171 28.916 1.00 34.99 ? 46  PRO A O   1 
ATOM   333  C CB  . PRO A 1 48  ? 67.376  42.334 27.388 1.00 38.86 ? 46  PRO A CB  1 
ATOM   334  C CG  . PRO A 1 48  ? 65.897  42.008 27.250 1.00 39.75 ? 46  PRO A CG  1 
ATOM   335  C CD  . PRO A 1 48  ? 65.159  42.659 28.401 1.00 39.65 ? 46  PRO A CD  1 
ATOM   336  N N   . SER A 1 49  ? 69.610  44.121 28.998 1.00 30.64 ? 47  SER A N   1 
ATOM   337  C CA  . SER A 1 49  ? 70.466  45.334 29.038 1.00 32.09 ? 47  SER A CA  1 
ATOM   338  C C   . SER A 1 49  ? 70.389  46.045 27.685 1.00 28.78 ? 47  SER A C   1 
ATOM   339  O O   . SER A 1 49  ? 70.094  45.394 26.660 1.00 23.72 ? 47  SER A O   1 
ATOM   340  C CB  . SER A 1 49  ? 71.885  45.020 29.420 1.00 32.45 ? 47  SER A CB  1 
ATOM   341  O OG  . SER A 1 49  ? 72.644  44.503 28.328 1.00 31.99 ? 47  SER A OG  1 
ATOM   342  N N   . SER A 1 50  ? 70.731  47.328 27.649 1.00 26.75 ? 48  SER A N   1 
ATOM   343  C CA  . SER A 1 50  ? 70.732  48.089 26.383 1.00 27.04 ? 48  SER A CA  1 
ATOM   344  C C   . SER A 1 50  ? 71.847  47.562 25.473 1.00 23.36 ? 48  SER A C   1 
ATOM   345  O O   . SER A 1 50  ? 71.642  47.587 24.265 1.00 23.36 ? 48  SER A O   1 
ATOM   346  C CB  . SER A 1 50  ? 70.841  49.594 26.632 1.00 27.60 ? 48  SER A CB  1 
ATOM   347  O OG  . SER A 1 50  ? 69.671  50.081 27.279 1.00 29.76 ? 48  SER A OG  1 
ATOM   348  N N   . ALA A 1 51  ? 72.969  47.081 26.025 1.00 28.48 ? 49  ALA A N   1 
ATOM   349  C CA  . ALA A 1 51  ? 74.091  46.502 25.235 1.00 28.33 ? 49  ALA A CA  1 
ATOM   350  C C   . ALA A 1 51  ? 73.591  45.225 24.533 1.00 25.10 ? 49  ALA A C   1 
ATOM   351  O O   . ALA A 1 51  ? 73.868  45.030 23.383 1.00 23.39 ? 49  ALA A O   1 
ATOM   352  C CB  . ALA A 1 51  ? 75.318  46.239 26.116 1.00 29.09 ? 49  ALA A CB  1 
ATOM   353  N N   . TYR A 1 52  ? 72.764  44.432 25.193 1.00 25.88 ? 50  TYR A N   1 
ATOM   354  C CA  . TYR A 1 52  ? 72.172  43.196 24.627 1.00 26.66 ? 50  TYR A CA  1 
ATOM   355  C C   . TYR A 1 52  ? 71.224  43.578 23.489 1.00 26.69 ? 50  TYR A C   1 
ATOM   356  O O   . TYR A 1 52  ? 71.332  43.036 22.394 1.00 27.51 ? 50  TYR A O   1 
ATOM   357  C CB  . TYR A 1 52  ? 71.443  42.472 25.761 1.00 30.17 ? 50  TYR A CB  1 
ATOM   358  C CG  . TYR A 1 52  ? 71.264  40.992 25.568 1.00 27.53 ? 50  TYR A CG  1 
ATOM   359  C CD1 . TYR A 1 52  ? 70.155  40.505 24.883 1.00 29.95 ? 50  TYR A CD1 1 
ATOM   360  C CD2 . TYR A 1 52  ? 72.194  40.090 26.066 1.00 27.59 ? 50  TYR A CD2 1 
ATOM   361  C CE1 . TYR A 1 52  ? 69.964  39.138 24.728 1.00 27.89 ? 50  TYR A CE1 1 
ATOM   362  C CE2 . TYR A 1 52  ? 72.039  38.720 25.875 1.00 29.04 ? 50  TYR A CE2 1 
ATOM   363  C CZ  . TYR A 1 52  ? 70.903  38.250 25.229 1.00 28.13 ? 50  TYR A CZ  1 
ATOM   364  O OH  . TYR A 1 52  ? 70.721  36.900 25.074 1.00 32.38 ? 50  TYR A OH  1 
ATOM   365  N N   . GLN A 1 53  ? 70.338  44.558 23.724 1.00 25.90 ? 51  GLN A N   1 
ATOM   366  C CA  . GLN A 1 53  ? 69.439  45.096 22.682 1.00 24.10 ? 51  GLN A CA  1 
ATOM   367  C C   . GLN A 1 53  ? 70.239  45.650 21.511 1.00 24.43 ? 51  GLN A C   1 
ATOM   368  O O   . GLN A 1 53  ? 69.754  45.527 20.357 1.00 25.56 ? 51  GLN A O   1 
ATOM   369  C CB  . GLN A 1 53  ? 68.502  46.150 23.262 1.00 26.82 ? 51  GLN A CB  1 
ATOM   370  C CG  . GLN A 1 53  ? 67.533  45.557 24.272 1.00 27.28 ? 51  GLN A CG  1 
ATOM   371  C CD  . GLN A 1 53  ? 66.296  44.978 23.628 1.00 28.62 ? 51  GLN A CD  1 
ATOM   372  O OE1 . GLN A 1 53  ? 66.228  44.695 22.423 1.00 24.78 ? 51  GLN A OE1 1 
ATOM   373  N NE2 . GLN A 1 53  ? 65.274  44.844 24.450 1.00 27.02 ? 51  GLN A NE2 1 
ATOM   374  N N   . GLN A 1 54  ? 71.368  46.313 21.784 1.00 24.78 ? 52  GLN A N   1 
ATOM   375  C CA  . GLN A 1 54  ? 72.199  46.951 20.731 1.00 26.51 ? 52  GLN A CA  1 
ATOM   376  C C   . GLN A 1 54  ? 72.641  45.842 19.761 1.00 24.10 ? 52  GLN A C   1 
ATOM   377  O O   . GLN A 1 54  ? 72.511  46.017 18.581 1.00 23.22 ? 52  GLN A O   1 
ATOM   378  C CB  . GLN A 1 54  ? 73.420  47.664 21.326 1.00 27.14 ? 52  GLN A CB  1 
ATOM   379  C CG  . GLN A 1 54  ? 74.260  48.457 20.319 1.00 29.28 ? 52  GLN A CG  1 
ATOM   380  C CD  . GLN A 1 54  ? 75.391  49.197 20.999 1.00 32.69 ? 52  GLN A CD  1 
ATOM   381  O OE1 . GLN A 1 54  ? 75.976  48.714 21.963 1.00 31.34 ? 52  GLN A OE1 1 
ATOM   382  N NE2 . GLN A 1 54  ? 75.689  50.404 20.530 1.00 36.73 ? 52  GLN A NE2 1 
ATOM   383  N N   . VAL A 1 55  ? 73.161  44.736 20.284 1.00 25.00 ? 53  VAL A N   1 
ATOM   384  C CA  . VAL A 1 55  ? 73.607  43.587 19.433 1.00 26.88 ? 53  VAL A CA  1 
ATOM   385  C C   . VAL A 1 55  ? 72.402  43.086 18.615 1.00 23.85 ? 53  VAL A C   1 
ATOM   386  O O   . VAL A 1 55  ? 72.522  42.993 17.377 1.00 25.87 ? 53  VAL A O   1 
ATOM   387  C CB  . VAL A 1 55  ? 74.239  42.474 20.281 1.00 27.90 ? 53  VAL A CB  1 
ATOM   388  C CG1 . VAL A 1 55  ? 74.481  41.225 19.432 1.00 31.39 ? 53  VAL A CG1 1 
ATOM   389  C CG2 . VAL A 1 55  ? 75.529  42.949 20.948 1.00 31.39 ? 53  VAL A CG2 1 
ATOM   390  N N   . LEU A 1 56  ? 71.260  42.808 19.252 1.00 24.21 ? 54  LEU A N   1 
ATOM   391  C CA  . LEU A 1 56  ? 70.095  42.203 18.519 1.00 27.37 ? 54  LEU A CA  1 
ATOM   392  C C   . LEU A 1 56  ? 69.594  43.145 17.428 1.00 29.68 ? 54  LEU A C   1 
ATOM   393  O O   . LEU A 1 56  ? 69.252  42.664 16.339 1.00 26.72 ? 54  LEU A O   1 
ATOM   394  C CB  . LEU A 1 56  ? 68.962  41.896 19.493 1.00 24.32 ? 54  LEU A CB  1 
ATOM   395  C CG  . LEU A 1 56  ? 69.350  40.879 20.548 1.00 26.11 ? 54  LEU A CG  1 
ATOM   396  C CD1 . LEU A 1 56  ? 68.296  40.809 21.618 1.00 29.09 ? 54  LEU A CD1 1 
ATOM   397  C CD2 . LEU A 1 56  ? 69.606  39.520 19.924 1.00 26.46 ? 54  LEU A CD2 1 
ATOM   398  N N   . THR A 1 57  ? 69.524  44.452 17.688 1.00 28.96 ? 55  THR A N   1 
ATOM   399  C CA  . THR A 1 57  ? 68.789  45.339 16.757 1.00 28.65 ? 55  THR A CA  1 
ATOM   400  C C   . THR A 1 57  ? 69.730  45.681 15.603 1.00 30.86 ? 55  THR A C   1 
ATOM   401  O O   . THR A 1 57  ? 69.217  46.187 14.609 1.00 35.13 ? 55  THR A O   1 
ATOM   402  C CB  . THR A 1 57  ? 68.157  46.544 17.480 1.00 33.20 ? 55  THR A CB  1 
ATOM   403  O OG1 . THR A 1 57  ? 69.185  47.305 18.087 1.00 29.78 ? 55  THR A OG1 1 
ATOM   404  C CG2 . THR A 1 57  ? 67.155  46.182 18.557 1.00 33.16 ? 55  THR A CG2 1 
ATOM   405  N N   . SER A 1 58  ? 71.030  45.390 15.700 1.00 30.61 ? 56  SER A N   1 
ATOM   406  C CA  . SER A 1 58  ? 72.060  45.697 14.670 1.00 34.77 ? 56  SER A CA  1 
ATOM   407  C C   . SER A 1 58  ? 72.269  44.525 13.714 1.00 34.02 ? 56  SER A C   1 
ATOM   408  O O   . SER A 1 58  ? 73.053  44.687 12.780 1.00 31.12 ? 56  SER A O   1 
ATOM   409  C CB  . SER A 1 58  ? 73.377  46.064 15.295 1.00 37.00 ? 56  SER A CB  1 
ATOM   410  O OG  . SER A 1 58  ? 74.050  44.889 15.721 1.00 53.22 ? 56  SER A OG  1 
ATOM   411  N N   . LEU A 1 59  ? 71.612  43.392 13.921 1.00 28.30 ? 57  LEU A N   1 
ATOM   412  C CA  . LEU A 1 59  ? 71.803  42.224 13.039 1.00 29.39 ? 57  LEU A CA  1 
ATOM   413  C C   . LEU A 1 59  ? 71.125  42.436 11.692 1.00 26.51 ? 57  LEU A C   1 
ATOM   414  O O   . LEU A 1 59  ? 70.118  43.126 11.570 1.00 27.09 ? 57  LEU A O   1 
ATOM   415  C CB  . LEU A 1 59  ? 71.255  40.975 13.725 1.00 27.72 ? 57  LEU A CB  1 
ATOM   416  C CG  . LEU A 1 59  ? 72.017  40.582 14.981 1.00 30.28 ? 57  LEU A CG  1 
ATOM   417  C CD1 . LEU A 1 59  ? 71.347  39.429 15.660 1.00 29.30 ? 57  LEU A CD1 1 
ATOM   418  C CD2 . LEU A 1 59  ? 73.478  40.291 14.708 1.00 33.51 ? 57  LEU A CD2 1 
ATOM   419  N N   . PRO A 1 60  ? 71.585  41.742 10.639 1.00 29.40 ? 58  PRO A N   1 
ATOM   420  C CA  . PRO A 1 60  ? 70.932  41.864 9.338  1.00 30.32 ? 58  PRO A CA  1 
ATOM   421  C C   . PRO A 1 60  ? 69.494  41.327 9.351  1.00 28.81 ? 58  PRO A C   1 
ATOM   422  O O   . PRO A 1 60  ? 69.103  40.594 10.267 1.00 25.63 ? 58  PRO A O   1 
ATOM   423  C CB  . PRO A 1 60  ? 71.877  41.088 8.416  1.00 31.34 ? 58  PRO A CB  1 
ATOM   424  C CG  . PRO A 1 60  ? 72.549  40.097 9.309  1.00 31.24 ? 58  PRO A CG  1 
ATOM   425  C CD  . PRO A 1 60  ? 72.766  40.862 10.603 1.00 31.39 ? 58  PRO A CD  1 
ATOM   426  N N   . SER A 1 61  ? 68.719  41.734 8.347  1.00 26.85 ? 59  SER A N   1 
ATOM   427  C CA  . SER A 1 61  ? 67.252  41.512 8.278  1.00 32.74 ? 59  SER A CA  1 
ATOM   428  C C   . SER A 1 61  ? 66.949  40.020 8.111  1.00 27.93 ? 59  SER A C   1 
ATOM   429  O O   . SER A 1 61  ? 65.840  39.663 8.409  1.00 29.88 ? 59  SER A O   1 
ATOM   430  C CB  . SER A 1 61  ? 66.589  42.329 7.192  1.00 33.87 ? 59  SER A CB  1 
ATOM   431  O OG  . SER A 1 61  ? 67.206  42.039 5.942  1.00 38.56 ? 59  SER A OG  1 
ATOM   432  N N   . SER A 1 62  ? 67.909  39.179 7.743  1.00 26.51 ? 60  SER A N   1 
ATOM   433  C CA  . SER A 1 62  ? 67.685  37.704 7.709  1.00 27.51 ? 60  SER A CA  1 
ATOM   434  C C   . SER A 1 62  ? 67.694  37.122 9.133  1.00 25.13 ? 60  SER A C   1 
ATOM   435  O O   . SER A 1 62  ? 67.374  35.899 9.282  1.00 26.25 ? 60  SER A O   1 
ATOM   436  C CB  . SER A 1 62  ? 68.717  37.042 6.864  1.00 27.96 ? 60  SER A CB  1 
ATOM   437  O OG  . SER A 1 62  ? 69.965  37.352 7.407  1.00 29.42 ? 60  SER A OG  1 
ATOM   438  N N   . ILE A 1 63  ? 68.109  37.891 10.138 1.00 24.89 ? 61  ILE A N   1 
ATOM   439  C CA  . ILE A 1 63  ? 68.229  37.454 11.561 1.00 23.75 ? 61  ILE A CA  1 
ATOM   440  C C   . ILE A 1 63  ? 67.276  38.278 12.427 1.00 31.32 ? 61  ILE A C   1 
ATOM   441  O O   . ILE A 1 63  ? 67.642  39.427 12.778 1.00 29.15 ? 61  ILE A O   1 
ATOM   442  C CB  . ILE A 1 63  ? 69.661  37.552 12.093 1.00 24.69 ? 61  ILE A CB  1 
ATOM   443  C CG1 . ILE A 1 63  ? 70.660  36.819 11.184 1.00 24.23 ? 61  ILE A CG1 1 
ATOM   444  C CG2 . ILE A 1 63  ? 69.708  37.025 13.525 1.00 23.88 ? 61  ILE A CG2 1 
ATOM   445  C CD1 . ILE A 1 63  ? 72.113  37.064 11.542 1.00 26.68 ? 61  ILE A CD1 1 
ATOM   446  N N   . ASP A 1 64  ? 66.142  37.712 12.858 1.00 27.73 ? 62  ASP A N   1 
ATOM   447  C CA  . ASP A 1 64  ? 65.204  38.464 13.741 1.00 27.47 ? 62  ASP A CA  1 
ATOM   448  C C   . ASP A 1 64  ? 65.326  37.927 15.151 1.00 24.97 ? 62  ASP A C   1 
ATOM   449  O O   . ASP A 1 64  ? 66.193  37.072 15.399 1.00 22.39 ? 62  ASP A O   1 
ATOM   450  C CB  . ASP A 1 64  ? 63.768  38.503 13.231 1.00 35.83 ? 62  ASP A CB  1 
ATOM   451  C CG  . ASP A 1 64  ? 63.238  37.164 12.836 1.00 40.55 ? 62  ASP A CG  1 
ATOM   452  O OD1 . ASP A 1 64  ? 63.554  36.209 13.546 1.00 49.70 ? 62  ASP A OD1 1 
ATOM   453  O OD2 . ASP A 1 64  ? 62.573  37.097 11.767 1.00 51.65 ? 62  ASP A OD2 1 
ATOM   454  N N   . HIS A 1 65  ? 64.558  38.491 16.074 1.00 21.79 ? 63  HIS A N   1 
ATOM   455  C CA  . HIS A 1 65  ? 64.607  38.043 17.487 1.00 23.40 ? 63  HIS A CA  1 
ATOM   456  C C   . HIS A 1 65  ? 63.225  38.238 18.105 1.00 25.34 ? 63  HIS A C   1 
ATOM   457  O O   . HIS A 1 65  ? 62.487  39.142 17.626 1.00 24.99 ? 63  HIS A O   1 
ATOM   458  C CB  . HIS A 1 65  ? 65.713  38.777 18.236 1.00 22.89 ? 63  HIS A CB  1 
ATOM   459  C CG  . HIS A 1 65  ? 65.500  40.245 18.297 1.00 24.18 ? 63  HIS A CG  1 
ATOM   460  N ND1 . HIS A 1 65  ? 65.791  41.090 17.231 1.00 27.66 ? 63  HIS A ND1 1 
ATOM   461  C CD2 . HIS A 1 65  ? 65.037  41.032 19.305 1.00 25.33 ? 63  HIS A CD2 1 
ATOM   462  C CE1 . HIS A 1 65  ? 65.496  42.337 17.578 1.00 25.12 ? 63  HIS A CE1 1 
ATOM   463  N NE2 . HIS A 1 65  ? 65.010  42.322 18.831 1.00 25.36 ? 63  HIS A NE2 1 
ATOM   464  N N   . ILE A 1 66  ? 62.907  37.350 19.036 1.00 28.11 ? 64  ILE A N   1 
ATOM   465  C CA  . ILE A 1 66  ? 61.655  37.272 19.831 1.00 27.30 ? 64  ILE A CA  1 
ATOM   466  C C   . ILE A 1 66  ? 62.073  37.074 21.281 1.00 28.25 ? 64  ILE A C   1 
ATOM   467  O O   . ILE A 1 66  ? 62.881  36.176 21.581 1.00 29.41 ? 64  ILE A O   1 
ATOM   468  C CB  . ILE A 1 66  ? 60.736  36.135 19.318 1.00 31.86 ? 64  ILE A CB  1 
ATOM   469  C CG1 . ILE A 1 66  ? 60.327  36.380 17.866 1.00 37.00 ? 64  ILE A CG1 1 
ATOM   470  C CG2 . ILE A 1 66  ? 59.500  35.979 20.215 1.00 36.03 ? 64  ILE A CG2 1 
ATOM   471  C CD1 . ILE A 1 66  ? 59.731  35.160 17.195 1.00 38.79 ? 64  ILE A CD1 1 
ATOM   472  N N   . PHE A 1 67  ? 61.521  37.886 22.176 1.00 25.85 ? 65  PHE A N   1 
ATOM   473  C CA  . PHE A 1 67  ? 61.623  37.707 23.638 1.00 27.33 ? 65  PHE A CA  1 
ATOM   474  C C   . PHE A 1 67  ? 60.438  36.877 24.108 1.00 25.19 ? 65  PHE A C   1 
ATOM   475  O O   . PHE A 1 67  ? 59.304  37.152 23.703 1.00 27.67 ? 65  PHE A O   1 
ATOM   476  C CB  . PHE A 1 67  ? 61.614  39.058 24.342 1.00 30.31 ? 65  PHE A CB  1 
ATOM   477  C CG  . PHE A 1 67  ? 62.822  39.875 24.004 1.00 29.09 ? 65  PHE A CG  1 
ATOM   478  C CD1 . PHE A 1 67  ? 64.008  39.678 24.678 1.00 31.77 ? 65  PHE A CD1 1 
ATOM   479  C CD2 . PHE A 1 67  ? 62.778  40.769 22.949 1.00 29.59 ? 65  PHE A CD2 1 
ATOM   480  C CE1 . PHE A 1 67  ? 65.130  40.410 24.340 1.00 31.43 ? 65  PHE A CE1 1 
ATOM   481  C CE2 . PHE A 1 67  ? 63.898  41.505 22.626 1.00 31.76 ? 65  PHE A CE2 1 
ATOM   482  C CZ  . PHE A 1 67  ? 65.062  41.337 23.336 1.00 27.15 ? 65  PHE A CZ  1 
ATOM   483  N N   . LEU A 1 68  ? 60.735  35.865 24.915 1.00 29.64 ? 66  LEU A N   1 
ATOM   484  C CA  . LEU A 1 68  ? 59.714  35.039 25.582 1.00 29.96 ? 66  LEU A CA  1 
ATOM   485  C C   . LEU A 1 68  ? 59.211  35.846 26.776 1.00 32.34 ? 66  LEU A C   1 
ATOM   486  O O   . LEU A 1 68  ? 59.949  36.679 27.306 1.00 30.21 ? 66  LEU A O   1 
ATOM   487  C CB  . LEU A 1 68  ? 60.355  33.719 26.029 1.00 27.33 ? 66  LEU A CB  1 
ATOM   488  C CG  . LEU A 1 68  ? 60.892  32.800 24.922 1.00 27.77 ? 66  LEU A CG  1 
ATOM   489  C CD1 . LEU A 1 68  ? 61.381  31.478 25.511 1.00 28.89 ? 66  LEU A CD1 1 
ATOM   490  C CD2 . LEU A 1 68  ? 59.866  32.525 23.833 1.00 27.05 ? 66  LEU A CD2 1 
ATOM   491  N N   . PRO A 1 69  ? 57.961  35.606 27.224 1.00 34.29 ? 67  PRO A N   1 
ATOM   492  C CA  . PRO A 1 69  ? 57.455  36.227 28.445 1.00 35.04 ? 67  PRO A CA  1 
ATOM   493  C C   . PRO A 1 69  ? 58.469  36.042 29.575 1.00 33.98 ? 67  PRO A C   1 
ATOM   494  O O   . PRO A 1 69  ? 58.982  34.957 29.809 1.00 33.39 ? 67  PRO A O   1 
ATOM   495  C CB  . PRO A 1 69  ? 56.115  35.502 28.710 1.00 34.82 ? 67  PRO A CB  1 
ATOM   496  C CG  . PRO A 1 69  ? 55.677  34.989 27.350 1.00 36.55 ? 67  PRO A CG  1 
ATOM   497  C CD  . PRO A 1 69  ? 56.942  34.799 26.532 1.00 35.49 ? 67  PRO A CD  1 
ATOM   498  N N   . GLN A 1 70  ? 58.732  37.135 30.277 1.00 34.10 ? 68  GLN A N   1 
ATOM   499  C CA  . GLN A 1 70  ? 59.647  37.175 31.422 1.00 37.07 ? 68  GLN A CA  1 
ATOM   500  C C   . GLN A 1 70  ? 59.200  36.172 32.489 1.00 37.50 ? 68  GLN A C   1 
ATOM   501  O O   . GLN A 1 70  ? 58.009  36.100 32.772 1.00 39.91 ? 68  GLN A O   1 
ATOM   502  C CB  . GLN A 1 70  ? 59.697  38.602 31.956 1.00 42.77 ? 68  GLN A CB  1 
ATOM   503  C CG  . GLN A 1 70  ? 60.934  38.864 32.776 1.00 46.43 ? 68  GLN A CG  1 
ATOM   504  C CD  . GLN A 1 70  ? 60.886  40.271 33.315 1.00 55.70 ? 68  GLN A CD  1 
ATOM   505  O OE1 . GLN A 1 70  ? 60.810  41.244 32.562 1.00 54.74 ? 68  GLN A OE1 1 
ATOM   506  N NE2 . GLN A 1 70  ? 60.915  40.374 34.635 1.00 53.67 ? 68  GLN A NE2 1 
ATOM   507  N N   . VAL A 1 71  ? 60.143  35.408 33.027 1.00 39.99 ? 69  VAL A N   1 
ATOM   508  C CA  . VAL A 1 71  ? 59.924  34.532 34.203 1.00 42.33 ? 69  VAL A CA  1 
ATOM   509  C C   . VAL A 1 71  ? 60.154  35.404 35.442 1.00 46.49 ? 69  VAL A C   1 
ATOM   510  O O   . VAL A 1 71  ? 61.112  36.176 35.467 1.00 43.66 ? 69  VAL A O   1 
ATOM   511  C CB  . VAL A 1 71  ? 60.827  33.281 34.172 1.00 45.26 ? 69  VAL A CB  1 
ATOM   512  C CG1 . VAL A 1 71  ? 60.678  32.522 32.857 1.00 44.80 ? 69  VAL A CG1 1 
ATOM   513  C CG2 . VAL A 1 71  ? 62.288  33.597 34.431 1.00 47.91 ? 69  VAL A CG2 1 
ATOM   514  N N   . ASP A 1 72  ? 59.253  35.324 36.405 1.00 46.62 ? 70  ASP A N   1 
ATOM   515  C CA  . ASP A 1 72  ? 59.448  35.856 37.778 1.00 51.70 ? 70  ASP A CA  1 
ATOM   516  C C   . ASP A 1 72  ? 60.236  34.829 38.604 1.00 44.18 ? 70  ASP A C   1 
ATOM   517  O O   . ASP A 1 72  ? 59.646  33.783 38.877 1.00 41.04 ? 70  ASP A O   1 
ATOM   518  C CB  . ASP A 1 72  ? 58.074  36.128 38.394 1.00 54.25 ? 70  ASP A CB  1 
ATOM   519  C CG  . ASP A 1 72  ? 58.090  37.166 39.490 1.00 59.52 ? 70  ASP A CG  1 
ATOM   520  O OD1 . ASP A 1 72  ? 59.170  37.370 40.083 1.00 57.92 ? 70  ASP A OD1 1 
ATOM   521  O OD2 . ASP A 1 72  ? 57.019  37.773 39.720 1.00 71.47 ? 70  ASP A OD2 1 
ATOM   522  N N   . LEU A 1 73  ? 61.504  35.089 38.958 1.00 41.19 ? 71  LEU A N   1 
ATOM   523  C CA  . LEU A 1 73  ? 62.343  34.176 39.816 1.00 50.13 ? 71  LEU A CA  1 
ATOM   524  C C   . LEU A 1 73  ? 62.417  34.625 41.296 1.00 53.77 ? 71  LEU A C   1 
ATOM   525  O O   . LEU A 1 73  ? 63.279  34.087 42.030 1.00 55.36 ? 71  LEU A O   1 
ATOM   526  C CB  . LEU A 1 73  ? 63.771  34.121 39.260 1.00 45.96 ? 71  LEU A CB  1 
ATOM   527  C CG  . LEU A 1 73  ? 63.933  33.454 37.901 1.00 47.70 ? 71  LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 73  ? 65.371  32.996 37.712 1.00 49.60 ? 71  LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 73  ? 62.972  32.290 37.729 1.00 47.58 ? 71  LEU A CD2 1 
ATOM   530  N N   . THR A 1 74  ? 61.570  35.561 41.736 1.00 61.59 ? 72  THR A N   1 
ATOM   531  C CA  . THR A 1 74  ? 61.655  36.234 43.067 1.00 67.35 ? 72  THR A CA  1 
ATOM   532  C C   . THR A 1 74  ? 61.879  35.214 44.205 1.00 69.59 ? 72  THR A C   1 
ATOM   533  O O   . THR A 1 74  ? 61.095  34.240 44.329 1.00 69.80 ? 72  THR A O   1 
ATOM   534  C CB  . THR A 1 74  ? 60.422  37.114 43.278 1.00 67.32 ? 72  THR A CB  1 
ATOM   535  O OG1 . THR A 1 74  ? 59.342  36.286 42.852 1.00 71.94 ? 72  THR A OG1 1 
ATOM   536  C CG2 . THR A 1 74  ? 60.458  38.416 42.505 1.00 61.40 ? 72  THR A CG2 1 
ATOM   537  N N   . ASP A 1 75  ? 62.918  35.480 45.005 1.00 74.73 ? 73  ASP A N   1 
ATOM   538  C CA  . ASP A 1 75  ? 63.549  34.622 46.050 1.00 82.14 ? 73  ASP A CA  1 
ATOM   539  C C   . ASP A 1 75  ? 65.061  34.926 46.043 1.00 75.80 ? 73  ASP A C   1 
ATOM   540  O O   . ASP A 1 75  ? 65.584  35.317 47.102 1.00 68.05 ? 73  ASP A O   1 
ATOM   541  C CB  . ASP A 1 75  ? 63.311  33.126 45.824 1.00 77.89 ? 73  ASP A CB  1 
ATOM   542  C CG  . ASP A 1 75  ? 64.371  32.516 44.934 1.00 72.56 ? 73  ASP A CG  1 
ATOM   543  O OD1 . ASP A 1 75  ? 65.566  32.704 45.237 1.00 67.10 ? 73  ASP A OD1 1 
ATOM   544  O OD2 . ASP A 1 75  ? 63.997  31.902 43.938 1.00 78.09 ? 73  ASP A OD2 1 
ATOM   545  N N   . PRO A 1 84  ? 71.267  32.624 44.228 1.00 72.11 ? 82  PRO A N   1 
ATOM   546  C CA  . PRO A 1 84  ? 72.117  33.665 43.647 1.00 68.70 ? 82  PRO A CA  1 
ATOM   547  C C   . PRO A 1 84  ? 72.758  33.351 42.277 1.00 60.47 ? 82  PRO A C   1 
ATOM   548  O O   . PRO A 1 84  ? 72.571  34.172 41.403 1.00 65.28 ? 82  PRO A O   1 
ATOM   549  C CB  . PRO A 1 84  ? 73.154  33.868 44.763 1.00 66.04 ? 82  PRO A CB  1 
ATOM   550  C CG  . PRO A 1 84  ? 72.294  33.874 46.009 1.00 70.73 ? 82  PRO A CG  1 
ATOM   551  C CD  . PRO A 1 84  ? 71.127  32.965 45.659 1.00 73.13 ? 82  PRO A CD  1 
ATOM   552  N N   . ARG A 1 85  ? 73.479  32.232 42.095 1.00 54.32 ? 83  ARG A N   1 
ATOM   553  C CA  . ARG A 1 85  ? 74.454  32.035 40.970 1.00 52.62 ? 83  ARG A CA  1 
ATOM   554  C C   . ARG A 1 85  ? 73.761  32.104 39.599 1.00 51.81 ? 83  ARG A C   1 
ATOM   555  O O   . ARG A 1 85  ? 72.631  31.572 39.481 1.00 44.11 ? 83  ARG A O   1 
ATOM   556  C CB  . ARG A 1 85  ? 75.208  30.708 41.106 1.00 53.01 ? 83  ARG A CB  1 
ATOM   557  C CG  . ARG A 1 85  ? 76.446  30.795 41.991 1.00 59.79 ? 83  ARG A CG  1 
ATOM   558  C CD  . ARG A 1 85  ? 77.579  29.859 41.594 1.00 61.79 ? 83  ARG A CD  1 
ATOM   559  N NE  . ARG A 1 85  ? 78.129  30.102 40.260 1.00 65.21 ? 83  ARG A NE  1 
ATOM   560  C CZ  . ARG A 1 85  ? 78.905  31.139 39.906 1.00 69.65 ? 83  ARG A CZ  1 
ATOM   561  N NH1 . ARG A 1 85  ? 79.229  32.070 40.784 1.00 67.55 ? 83  ARG A NH1 1 
ATOM   562  N NH2 . ARG A 1 85  ? 79.363  31.248 38.667 1.00 66.99 ? 83  ARG A NH2 1 
ATOM   563  N N   . ILE A 1 86  ? 74.425  32.706 38.597 1.00 52.65 ? 84  ILE A N   1 
ATOM   564  C CA  . ILE A 1 86  ? 73.802  33.103 37.288 1.00 53.49 ? 84  ILE A CA  1 
ATOM   565  C C   . ILE A 1 86  ? 73.347  31.854 36.512 1.00 51.07 ? 84  ILE A C   1 
ATOM   566  O O   . ILE A 1 86  ? 72.381  31.998 35.710 1.00 42.54 ? 84  ILE A O   1 
ATOM   567  C CB  . ILE A 1 86  ? 74.714  33.984 36.397 1.00 49.72 ? 84  ILE A CB  1 
ATOM   568  C CG1 . ILE A 1 86  ? 73.943  34.489 35.168 1.00 57.66 ? 84  ILE A CG1 1 
ATOM   569  C CG2 . ILE A 1 86  ? 75.986  33.251 35.979 1.00 50.21 ? 84  ILE A CG2 1 
ATOM   570  C CD1 . ILE A 1 86  ? 74.461  35.793 34.568 1.00 66.34 ? 84  ILE A CD1 1 
ATOM   571  N N   . GLU A 1 87  ? 74.035  30.718 36.714 1.00 46.02 ? 85  GLU A N   1 
ATOM   572  C CA  . GLU A 1 87  ? 73.792  29.417 36.026 1.00 51.83 ? 85  GLU A CA  1 
ATOM   573  C C   . GLU A 1 87  ? 72.509  28.780 36.560 1.00 49.53 ? 85  GLU A C   1 
ATOM   574  O O   . GLU A 1 87  ? 71.798  28.127 35.764 1.00 41.20 ? 85  GLU A O   1 
ATOM   575  C CB  . GLU A 1 87  ? 74.955  28.442 36.233 1.00 51.78 ? 85  GLU A CB  1 
ATOM   576  C CG  . GLU A 1 87  ? 76.265  28.947 35.636 1.00 57.82 ? 85  GLU A CG  1 
ATOM   577  C CD  . GLU A 1 87  ? 77.082  29.872 36.524 1.00 59.09 ? 85  GLU A CD  1 
ATOM   578  O OE1 . GLU A 1 87  ? 76.666  30.084 37.688 1.00 53.78 ? 85  GLU A OE1 1 
ATOM   579  O OE2 . GLU A 1 87  ? 78.132  30.369 36.050 1.00 60.37 ? 85  GLU A OE2 1 
ATOM   580  N N   . THR A 1 88  ? 72.272  28.898 37.869 1.00 45.33 ? 86  THR A N   1 
ATOM   581  C CA  . THR A 1 88  ? 71.001  28.460 38.505 1.00 39.64 ? 86  THR A CA  1 
ATOM   582  C C   . THR A 1 88  ? 69.893  29.325 37.935 1.00 35.88 ? 86  THR A C   1 
ATOM   583  O O   . THR A 1 88  ? 68.879  28.754 37.474 1.00 36.36 ? 86  THR A O   1 
ATOM   584  C CB  . THR A 1 88  ? 71.052  28.549 40.038 1.00 39.82 ? 86  THR A CB  1 
ATOM   585  O OG1 . THR A 1 88  ? 72.146  27.716 40.415 1.00 41.00 ? 86  THR A OG1 1 
ATOM   586  C CG2 . THR A 1 88  ? 69.770  28.095 40.701 1.00 42.25 ? 86  THR A CG2 1 
ATOM   587  N N   . LEU A 1 89  ? 70.099  30.650 37.904 1.00 36.65 ? 87  LEU A N   1 
ATOM   588  C CA  . LEU A 1 89  ? 69.098  31.626 37.382 1.00 37.37 ? 87  LEU A CA  1 
ATOM   589  C C   . LEU A 1 89  ? 68.796  31.349 35.891 1.00 37.64 ? 87  LEU A C   1 
ATOM   590  O O   . LEU A 1 89  ? 67.611  31.397 35.496 1.00 32.95 ? 87  LEU A O   1 
ATOM   591  C CB  . LEU A 1 89  ? 69.647  33.047 37.573 1.00 42.62 ? 87  LEU A CB  1 
ATOM   592  C CG  . LEU A 1 89  ? 69.807  33.543 39.018 1.00 44.59 ? 87  LEU A CG  1 
ATOM   593  C CD1 . LEU A 1 89  ? 70.336  34.969 39.028 1.00 43.97 ? 87  LEU A CD1 1 
ATOM   594  C CD2 . LEU A 1 89  ? 68.495  33.470 39.783 1.00 45.75 ? 87  LEU A CD2 1 
ATOM   595  N N   . ILE A 1 90  ? 69.829  31.093 35.078 1.00 38.37 ? 88  ILE A N   1 
ATOM   596  C CA  . ILE A 1 90  ? 69.670  30.799 33.622 1.00 38.01 ? 88  ILE A CA  1 
ATOM   597  C C   . ILE A 1 90  ? 68.853  29.507 33.497 1.00 30.25 ? 88  ILE A C   1 
ATOM   598  O O   . ILE A 1 90  ? 67.892  29.473 32.707 1.00 32.87 ? 88  ILE A O   1 
ATOM   599  C CB  . ILE A 1 90  ? 71.047  30.693 32.922 1.00 41.82 ? 88  ILE A CB  1 
ATOM   600  C CG1 . ILE A 1 90  ? 71.618  32.082 32.629 1.00 43.62 ? 88  ILE A CG1 1 
ATOM   601  C CG2 . ILE A 1 90  ? 70.968  29.848 31.650 1.00 42.71 ? 88  ILE A CG2 1 
ATOM   602  C CD1 . ILE A 1 90  ? 73.120  32.084 32.425 1.00 46.92 ? 88  ILE A CD1 1 
ATOM   603  N N   . SER A 1 91  ? 69.255  28.498 34.260 1.00 30.14 ? 89  SER A N   1 
ATOM   604  C CA  . SER A 1 91  ? 68.652  27.151 34.229 1.00 33.60 ? 89  SER A CA  1 
ATOM   605  C C   . SER A 1 91  ? 67.169  27.272 34.599 1.00 32.13 ? 89  SER A C   1 
ATOM   606  O O   . SER A 1 91  ? 66.347  26.707 33.916 1.00 31.15 ? 89  SER A O   1 
ATOM   607  C CB  . SER A 1 91  ? 69.398  26.203 35.134 1.00 33.39 ? 89  SER A CB  1 
ATOM   608  O OG  . SER A 1 91  ? 70.628  25.786 34.574 1.00 32.37 ? 89  SER A OG  1 
ATOM   609  N N   . LEU A 1 92  ? 66.831  27.985 35.668 1.00 31.23 ? 90  LEU A N   1 
ATOM   610  C CA  . LEU A 1 92  ? 65.420  28.212 36.070 1.00 32.04 ? 90  LEU A CA  1 
ATOM   611  C C   . LEU A 1 92  ? 64.689  29.040 35.018 1.00 29.37 ? 90  LEU A C   1 
ATOM   612  O O   . LEU A 1 92  ? 63.518  28.767 34.795 1.00 29.77 ? 90  LEU A O   1 
ATOM   613  C CB  . LEU A 1 92  ? 65.378  28.908 37.441 1.00 33.30 ? 90  LEU A CB  1 
ATOM   614  C CG  . LEU A 1 92  ? 65.780  27.998 38.601 1.00 34.30 ? 90  LEU A CG  1 
ATOM   615  C CD1 . LEU A 1 92  ? 65.856  28.775 39.898 1.00 36.70 ? 90  LEU A CD1 1 
ATOM   616  C CD2 . LEU A 1 92  ? 64.815  26.830 38.724 1.00 38.07 ? 90  LEU A CD2 1 
ATOM   617  N N   . THR A 1 93  ? 65.339  30.026 34.387 1.00 29.41 ? 91  THR A N   1 
ATOM   618  C CA  . THR A 1 93  ? 64.655  30.871 33.371 1.00 30.19 ? 91  THR A CA  1 
ATOM   619  C C   . THR A 1 93  ? 64.182  29.975 32.229 1.00 27.43 ? 91  THR A C   1 
ATOM   620  O O   . THR A 1 93  ? 63.011  30.090 31.821 1.00 34.26 ? 91  THR A O   1 
ATOM   621  C CB  . THR A 1 93  ? 65.537  32.031 32.893 1.00 32.84 ? 91  THR A CB  1 
ATOM   622  O OG1 . THR A 1 93  ? 65.913  32.769 34.065 1.00 35.51 ? 91  THR A OG1 1 
ATOM   623  C CG2 . THR A 1 93  ? 64.853  32.944 31.896 1.00 31.36 ? 91  THR A CG2 1 
ATOM   624  N N   . VAL A 1 94  ? 65.086  29.151 31.719 1.00 28.79 ? 92  VAL A N   1 
ATOM   625  C CA  . VAL A 1 94  ? 64.786  28.239 30.577 1.00 28.49 ? 92  VAL A CA  1 
ATOM   626  C C   . VAL A 1 94  ? 63.720  27.234 30.998 1.00 27.03 ? 92  VAL A C   1 
ATOM   627  O O   . VAL A 1 94  ? 62.730  27.079 30.273 1.00 26.90 ? 92  VAL A O   1 
ATOM   628  C CB  . VAL A 1 94  ? 66.035  27.512 30.053 1.00 27.78 ? 92  VAL A CB  1 
ATOM   629  C CG1 . VAL A 1 94  ? 65.626  26.573 28.914 1.00 25.42 ? 92  VAL A CG1 1 
ATOM   630  C CG2 . VAL A 1 94  ? 67.120  28.479 29.593 1.00 26.96 ? 92  VAL A CG2 1 
ATOM   631  N N   . ALA A 1 95  ? 63.901  26.565 32.140 1.00 32.78 ? 93  ALA A N   1 
ATOM   632  C CA  . ALA A 1 95  ? 62.949  25.525 32.609 1.00 32.13 ? 93  ALA A CA  1 
ATOM   633  C C   . ALA A 1 95  ? 61.542  26.136 32.745 1.00 31.41 ? 93  ALA A C   1 
ATOM   634  O O   . ALA A 1 95  ? 60.543  25.498 32.352 1.00 33.88 ? 93  ALA A O   1 
ATOM   635  C CB  . ALA A 1 95  ? 63.441  24.899 33.913 1.00 30.09 ? 93  ALA A CB  1 
ATOM   636  N N   . ARG A 1 96  ? 61.426  27.385 33.187 1.00 32.10 ? 94  ARG A N   1 
ATOM   637  C CA  . ARG A 1 96  ? 60.100  28.004 33.426 1.00 31.63 ? 94  ARG A CA  1 
ATOM   638  C C   . ARG A 1 96  ? 59.554  28.647 32.155 1.00 33.01 ? 94  ARG A C   1 
ATOM   639  O O   . ARG A 1 96  ? 58.442  29.200 32.187 1.00 32.65 ? 94  ARG A O   1 
ATOM   640  C CB  . ARG A 1 96  ? 60.231  29.020 34.558 1.00 39.53 ? 94  ARG A CB  1 
ATOM   641  C CG  . ARG A 1 96  ? 60.589  28.344 35.867 1.00 38.82 ? 94  ARG A CG  1 
ATOM   642  C CD  . ARG A 1 96  ? 60.531  29.276 37.049 1.00 45.78 ? 94  ARG A CD  1 
ATOM   643  N NE  . ARG A 1 96  ? 60.770  28.444 38.220 1.00 49.00 ? 94  ARG A NE  1 
ATOM   644  C CZ  . ARG A 1 96  ? 60.711  28.865 39.472 1.00 54.50 ? 94  ARG A CZ  1 
ATOM   645  N NH1 . ARG A 1 96  ? 60.411  30.124 39.735 1.00 55.25 ? 94  ARG A NH1 1 
ATOM   646  N NH2 . ARG A 1 96  ? 60.946  28.012 40.455 1.00 52.08 ? 94  ARG A NH2 1 
ATOM   647  N N   . SER A 1 97  ? 60.317  28.590 31.073 1.00 33.30 ? 95  SER A N   1 
ATOM   648  C CA  . SER A 1 97  ? 59.965  29.194 29.772 1.00 29.29 ? 95  SER A CA  1 
ATOM   649  C C   . SER A 1 97  ? 59.600  28.100 28.774 1.00 27.20 ? 95  SER A C   1 
ATOM   650  O O   . SER A 1 97  ? 59.401  28.442 27.603 1.00 27.32 ? 95  SER A O   1 
ATOM   651  C CB  . SER A 1 97  ? 61.131  30.013 29.223 1.00 32.50 ? 95  SER A CB  1 
ATOM   652  O OG  . SER A 1 97  ? 61.407  31.149 30.015 1.00 29.72 ? 95  SER A OG  1 
ATOM   653  N N   . LEU A 1 98  ? 59.511  26.832 29.171 1.00 28.12 ? 96  LEU A N   1 
ATOM   654  C CA  . LEU A 1 98  ? 59.444  25.762 28.144 1.00 29.53 ? 96  LEU A CA  1 
ATOM   655  C C   . LEU A 1 98  ? 58.096  25.819 27.423 1.00 28.71 ? 96  LEU A C   1 
ATOM   656  O O   . LEU A 1 98  ? 58.063  25.540 26.211 1.00 28.27 ? 96  LEU A O   1 
ATOM   657  C CB  . LEU A 1 98  ? 59.688  24.399 28.780 1.00 29.67 ? 96  LEU A CB  1 
ATOM   658  C CG  . LEU A 1 98  ? 61.129  24.119 29.198 1.00 31.50 ? 96  LEU A CG  1 
ATOM   659  C CD1 . LEU A 1 98  ? 61.260  22.672 29.647 1.00 31.91 ? 96  LEU A CD1 1 
ATOM   660  C CD2 . LEU A 1 98  ? 62.128  24.446 28.107 1.00 28.93 ? 96  LEU A CD2 1 
ATOM   661  N N   . SER A 1 99  ? 57.023  26.199 28.122 1.00 29.92 ? 97  SER A N   1 
ATOM   662  C CA  . SER A 1 99  ? 55.671  26.267 27.527 1.00 30.26 ? 97  SER A CA  1 
ATOM   663  C C   . SER A 1 99  ? 55.693  27.337 26.428 1.00 28.74 ? 97  SER A C   1 
ATOM   664  O O   . SER A 1 99  ? 55.233  27.071 25.318 1.00 27.68 ? 97  SER A O   1 
ATOM   665  C CB  . SER A 1 99  ? 54.602  26.540 28.546 1.00 33.19 ? 97  SER A CB  1 
ATOM   666  O OG  . SER A 1 99  ? 53.374  26.711 27.841 1.00 38.75 ? 97  SER A OG  1 
ATOM   667  N N   . SER A 1 100 ? 56.208  28.511 26.760 1.00 29.24 ? 98  SER A N   1 
ATOM   668  C CA  . SER A 1 100 ? 56.341  29.668 25.844 1.00 30.12 ? 98  SER A CA  1 
ATOM   669  C C   . SER A 1 100 ? 57.217  29.274 24.672 1.00 25.07 ? 98  SER A C   1 
ATOM   670  O O   . SER A 1 100 ? 56.889  29.644 23.553 1.00 26.57 ? 98  SER A O   1 
ATOM   671  C CB  . SER A 1 100 ? 56.951  30.850 26.537 1.00 32.02 ? 98  SER A CB  1 
ATOM   672  O OG  . SER A 1 100 ? 55.998  31.435 27.379 1.00 43.59 ? 98  SER A OG  1 
ATOM   673  N N   . LEU A 1 101 ? 58.354  28.638 24.959 1.00 27.97 ? 99  LEU A N   1 
ATOM   674  C CA  . LEU A 1 101 ? 59.278  28.210 23.885 1.00 24.98 ? 99  LEU A CA  1 
ATOM   675  C C   . LEU A 1 101 ? 58.529  27.288 22.917 1.00 24.37 ? 99  LEU A C   1 
ATOM   676  O O   . LEU A 1 101 ? 58.668  27.483 21.686 1.00 23.26 ? 99  LEU A O   1 
ATOM   677  C CB  . LEU A 1 101 ? 60.499  27.533 24.489 1.00 25.22 ? 99  LEU A CB  1 
ATOM   678  C CG  . LEU A 1 101 ? 61.512  27.071 23.459 1.00 26.13 ? 99  LEU A CG  1 
ATOM   679  C CD1 . LEU A 1 101 ? 61.967  28.260 22.599 1.00 24.23 ? 99  LEU A CD1 1 
ATOM   680  C CD2 . LEU A 1 101 ? 62.697  26.404 24.126 1.00 25.97 ? 99  LEU A CD2 1 
ATOM   681  N N   . ARG A 1 102 ? 57.800  26.277 23.403 1.00 25.62 ? 100 ARG A N   1 
ATOM   682  C CA  . ARG A 1 102 ? 57.138  25.350 22.443 1.00 29.09 ? 100 ARG A CA  1 
ATOM   683  C C   . ARG A 1 102 ? 56.141  26.136 21.568 1.00 29.71 ? 100 ARG A C   1 
ATOM   684  O O   . ARG A 1 102 ? 56.145  25.954 20.312 1.00 26.38 ? 100 ARG A O   1 
ATOM   685  C CB  . ARG A 1 102 ? 56.512  24.146 23.154 1.00 30.63 ? 100 ARG A CB  1 
ATOM   686  C CG  . ARG A 1 102 ? 55.996  23.099 22.170 1.00 31.97 ? 100 ARG A CG  1 
ATOM   687  C CD  . ARG A 1 102 ? 55.083  22.029 22.776 1.00 36.50 ? 100 ARG A CD  1 
ATOM   688  N NE  . ARG A 1 102 ? 53.868  22.677 23.270 1.00 39.17 ? 100 ARG A NE  1 
ATOM   689  C CZ  . ARG A 1 102 ? 52.856  23.093 22.500 1.00 41.92 ? 100 ARG A CZ  1 
ATOM   690  N NH1 . ARG A 1 102 ? 52.838  22.819 21.204 1.00 44.42 ? 100 ARG A NH1 1 
ATOM   691  N NH2 . ARG A 1 102 ? 51.839  23.736 23.046 1.00 43.87 ? 100 ARG A NH2 1 
ATOM   692  N N   . THR A 1 103 ? 55.331  27.011 22.162 1.00 28.94 ? 101 THR A N   1 
ATOM   693  C CA  . THR A 1 103 ? 54.316  27.765 21.381 1.00 32.47 ? 101 THR A CA  1 
ATOM   694  C C   . THR A 1 103 ? 55.034  28.733 20.419 1.00 28.34 ? 101 THR A C   1 
ATOM   695  O O   . THR A 1 103 ? 54.605  28.788 19.255 1.00 25.77 ? 101 THR A O   1 
ATOM   696  C CB  . THR A 1 103 ? 53.243  28.356 22.301 1.00 35.96 ? 101 THR A CB  1 
ATOM   697  O OG1 . THR A 1 103 ? 53.824  29.342 23.155 1.00 39.68 ? 101 THR A OG1 1 
ATOM   698  C CG2 . THR A 1 103 ? 52.612  27.271 23.148 1.00 37.26 ? 101 THR A CG2 1 
ATOM   699  N N   . THR A 1 104 ? 56.117  29.391 20.845 1.00 27.28 ? 102 THR A N   1 
ATOM   700  C CA  . THR A 1 104 ? 56.927  30.272 19.956 1.00 27.51 ? 102 THR A CA  1 
ATOM   701  C C   . THR A 1 104 ? 57.525  29.461 18.796 1.00 26.53 ? 102 THR A C   1 
ATOM   702  O O   . THR A 1 104 ? 57.466  29.941 17.683 1.00 24.42 ? 102 THR A O   1 
ATOM   703  C CB  . THR A 1 104 ? 58.016  31.033 20.708 1.00 27.47 ? 102 THR A CB  1 
ATOM   704  O OG1 . THR A 1 104 ? 57.282  31.798 21.657 1.00 26.29 ? 102 THR A OG1 1 
ATOM   705  C CG2 . THR A 1 104 ? 58.812  31.959 19.822 1.00 28.52 ? 102 THR A CG2 1 
ATOM   706  N N   . LEU A 1 105 ? 58.132  28.309 19.056 1.00 25.75 ? 103 LEU A N   1 
ATOM   707  C CA  . LEU A 1 105 ? 58.763  27.518 17.963 1.00 26.99 ? 103 LEU A CA  1 
ATOM   708  C C   . LEU A 1 105 ? 57.685  27.045 16.977 1.00 25.45 ? 103 LEU A C   1 
ATOM   709  O O   . LEU A 1 105 ? 57.915  27.036 15.727 1.00 24.80 ? 103 LEU A O   1 
ATOM   710  C CB  . LEU A 1 105 ? 59.522  26.349 18.580 1.00 28.91 ? 103 LEU A CB  1 
ATOM   711  C CG  . LEU A 1 105 ? 60.759  26.714 19.399 1.00 28.60 ? 103 LEU A CG  1 
ATOM   712  C CD1 . LEU A 1 105 ? 61.352  25.454 19.967 1.00 28.39 ? 103 LEU A CD1 1 
ATOM   713  C CD2 . LEU A 1 105 ? 61.787  27.471 18.551 1.00 31.01 ? 103 LEU A CD2 1 
ATOM   714  N N   . SER A 1 106 ? 56.520  26.667 17.501 1.00 27.81 ? 104 SER A N   1 
ATOM   715  C CA  . SER A 1 106 ? 55.375  26.278 16.646 1.00 28.29 ? 104 SER A CA  1 
ATOM   716  C C   . SER A 1 106 ? 54.935  27.465 15.775 1.00 25.07 ? 104 SER A C   1 
ATOM   717  O O   . SER A 1 106 ? 54.723  27.268 14.573 1.00 26.24 ? 104 SER A O   1 
ATOM   718  C CB  . SER A 1 106 ? 54.251  25.753 17.466 1.00 30.91 ? 104 SER A CB  1 
ATOM   719  O OG  . SER A 1 106 ? 53.372  25.091 16.602 1.00 33.46 ? 104 SER A OG  1 
ATOM   720  N N   . SER A 1 107 ? 54.831  28.664 16.341 1.00 27.44 ? 105 SER A N   1 
ATOM   721  C CA  . SER A 1 107 ? 54.469  29.879 15.560 1.00 30.68 ? 105 SER A CA  1 
ATOM   722  C C   . SER A 1 107 ? 55.528  30.179 14.470 1.00 29.83 ? 105 SER A C   1 
ATOM   723  O O   . SER A 1 107 ? 55.149  30.380 13.275 1.00 28.44 ? 105 SER A O   1 
ATOM   724  C CB  . SER A 1 107 ? 54.224  31.023 16.511 1.00 34.64 ? 105 SER A CB  1 
ATOM   725  O OG  . SER A 1 107 ? 53.754  32.143 15.786 1.00 45.75 ? 105 SER A OG  1 
ATOM   726  N N   . LEU A 1 108 ? 56.813  30.088 14.809 1.00 28.72 ? 106 LEU A N   1 
ATOM   727  C CA  . LEU A 1 108 ? 57.938  30.222 13.839 1.00 29.35 ? 106 LEU A CA  1 
ATOM   728  C C   . LEU A 1 108 ? 57.803  29.169 12.727 1.00 29.14 ? 106 LEU A C   1 
ATOM   729  O O   . LEU A 1 108 ? 57.906  29.536 11.556 1.00 27.78 ? 106 LEU A O   1 
ATOM   730  C CB  . LEU A 1 108 ? 59.233  30.007 14.609 1.00 32.00 ? 106 LEU A CB  1 
ATOM   731  C CG  . LEU A 1 108 ? 60.380  30.930 14.291 1.00 37.22 ? 106 LEU A CG  1 
ATOM   732  C CD1 . LEU A 1 108 ? 59.909  32.373 14.220 1.00 40.03 ? 106 LEU A CD1 1 
ATOM   733  C CD2 . LEU A 1 108 ? 61.438  30.756 15.353 1.00 36.28 ? 106 LEU A CD2 1 
ATOM   734  N N   . GLN A 1 109 ? 57.552  27.902 13.093 1.00 28.35 ? 107 GLN A N   1 
ATOM   735  C CA  . GLN A 1 109 ? 57.357  26.788 12.101 1.00 28.55 ? 107 GLN A CA  1 
ATOM   736  C C   . GLN A 1 109 ? 56.235  27.148 11.107 1.00 26.06 ? 107 GLN A C   1 
ATOM   737  O O   . GLN A 1 109 ? 56.304  26.673 9.963  1.00 27.50 ? 107 GLN A O   1 
ATOM   738  C CB  . GLN A 1 109 ? 57.143  25.481 12.873 1.00 28.15 ? 107 GLN A CB  1 
ATOM   739  C CG  . GLN A 1 109 ? 57.135  24.204 12.045 1.00 30.87 ? 107 GLN A CG  1 
ATOM   740  C CD  . GLN A 1 109 ? 56.647  23.033 12.864 1.00 30.11 ? 107 GLN A CD  1 
ATOM   741  O OE1 . GLN A 1 109 ? 55.485  22.995 13.329 1.00 40.04 ? 107 GLN A OE1 1 
ATOM   742  N NE2 . GLN A 1 109 ? 57.539  22.103 13.115 1.00 34.10 ? 107 GLN A NE2 1 
ATOM   743  N N   . SER A 1 110 ? 55.233  27.960 11.484 1.00 28.22 ? 108 SER A N   1 
ATOM   744  C CA  . SER A 1 110 ? 54.091  28.283 10.585 1.00 30.86 ? 108 SER A CA  1 
ATOM   745  C C   . SER A 1 110 ? 54.438  29.446 9.648  1.00 31.01 ? 108 SER A C   1 
ATOM   746  O O   . SER A 1 110 ? 53.921  29.445 8.545  1.00 31.19 ? 108 SER A O   1 
ATOM   747  C CB  . SER A 1 110 ? 52.787  28.426 11.324 1.00 37.91 ? 108 SER A CB  1 
ATOM   748  O OG  . SER A 1 110 ? 52.875  29.333 12.399 1.00 48.46 ? 108 SER A OG  1 
ATOM   749  N N   . SER A 1 111 ? 55.465  30.243 9.930  1.00 32.94 ? 109 SER A N   1 
ATOM   750  C CA  . SER A 1 111 ? 55.935  31.303 8.999  1.00 32.20 ? 109 SER A CA  1 
ATOM   751  C C   . SER A 1 111 ? 57.252  30.934 8.307  1.00 32.33 ? 109 SER A C   1 
ATOM   752  O O   . SER A 1 111 ? 57.488  31.468 7.212  1.00 31.92 ? 109 SER A O   1 
ATOM   753  C CB  . SER A 1 111 ? 56.025  32.644 9.695  1.00 35.49 ? 109 SER A CB  1 
ATOM   754  O OG  . SER A 1 111 ? 56.734  32.521 10.911 1.00 45.15 ? 109 SER A OG  1 
ATOM   755  N N   . LYS A 1 112 ? 58.077  30.050 8.878  1.00 29.10 ? 110 LYS A N   1 
ATOM   756  C CA  . LYS A 1 112 ? 59.443  29.721 8.364  1.00 27.24 ? 110 LYS A CA  1 
ATOM   757  C C   . LYS A 1 112 ? 59.661  28.203 8.356  1.00 24.51 ? 110 LYS A C   1 
ATOM   758  O O   . LYS A 1 112 ? 59.034  27.525 9.174  1.00 24.57 ? 110 LYS A O   1 
ATOM   759  C CB  . LYS A 1 112 ? 60.468  30.396 9.278  1.00 29.53 ? 110 LYS A CB  1 
ATOM   760  C CG  . LYS A 1 112 ? 60.483  31.919 9.242  1.00 30.83 ? 110 LYS A CG  1 
ATOM   761  C CD  . LYS A 1 112 ? 60.803  32.416 7.841  1.00 37.56 ? 110 LYS A CD  1 
ATOM   762  C CE  . LYS A 1 112 ? 61.421  33.802 7.793  1.00 45.01 ? 110 LYS A CE  1 
ATOM   763  N NZ  . LYS A 1 112 ? 60.624  34.759 8.592  1.00 43.20 ? 110 LYS A NZ  1 
ATOM   764  N N   . ASN A 1 113 ? 60.564  27.723 7.505  1.00 23.15 ? 111 ASN A N   1 
ATOM   765  C CA  . ASN A 1 113 ? 61.016  26.300 7.403  1.00 26.12 ? 111 ASN A CA  1 
ATOM   766  C C   . ASN A 1 113 ? 61.977  25.989 8.560  1.00 22.30 ? 111 ASN A C   1 
ATOM   767  O O   . ASN A 1 113 ? 63.161  25.741 8.325  1.00 22.90 ? 111 ASN A O   1 
ATOM   768  C CB  . ASN A 1 113 ? 61.623  26.058 6.034  1.00 27.90 ? 111 ASN A CB  1 
ATOM   769  C CG  . ASN A 1 113 ? 60.597  26.138 4.927  1.00 33.10 ? 111 ASN A CG  1 
ATOM   770  O OD1 . ASN A 1 113 ? 60.822  26.822 3.929  1.00 36.37 ? 111 ASN A OD1 1 
ATOM   771  N ND2 . ASN A 1 113 ? 59.488  25.428 5.087  1.00 26.79 ? 111 ASN A ND2 1 
ATOM   772  N N   . LEU A 1 114 ? 61.452  26.026 9.785  1.00 23.64 ? 112 LEU A N   1 
ATOM   773  C CA  . LEU A 1 114 ? 62.235  25.782 11.015 1.00 22.49 ? 112 LEU A CA  1 
ATOM   774  C C   . LEU A 1 114 ? 62.751  24.354 10.987 1.00 24.68 ? 112 LEU A C   1 
ATOM   775  O O   . LEU A 1 114 ? 61.920  23.448 10.942 1.00 23.09 ? 112 LEU A O   1 
ATOM   776  C CB  . LEU A 1 114 ? 61.331  26.010 12.214 1.00 22.72 ? 112 LEU A CB  1 
ATOM   777  C CG  . LEU A 1 114 ? 62.008  25.891 13.572 1.00 23.83 ? 112 LEU A CG  1 
ATOM   778  C CD1 . LEU A 1 114 ? 63.123  26.892 13.744 1.00 25.64 ? 112 LEU A CD1 1 
ATOM   779  C CD2 . LEU A 1 114 ? 60.990  26.057 14.687 1.00 25.06 ? 112 LEU A CD2 1 
ATOM   780  N N   . VAL A 1 115 ? 64.067  24.175 11.057 1.00 22.26 ? 113 VAL A N   1 
ATOM   781  C CA  . VAL A 1 115 ? 64.660  22.814 11.033 1.00 23.51 ? 113 VAL A CA  1 
ATOM   782  C C   . VAL A 1 115 ? 65.429  22.527 12.299 1.00 22.87 ? 113 VAL A C   1 
ATOM   783  O O   . VAL A 1 115 ? 65.714  21.325 12.570 1.00 22.04 ? 113 VAL A O   1 
ATOM   784  C CB  . VAL A 1 115 ? 65.560  22.623 9.807  1.00 25.79 ? 113 VAL A CB  1 
ATOM   785  C CG1 . VAL A 1 115 ? 64.698  22.606 8.562  1.00 25.32 ? 113 VAL A CG1 1 
ATOM   786  C CG2 . VAL A 1 115 ? 66.684  23.650 9.743  1.00 26.80 ? 113 VAL A CG2 1 
ATOM   787  N N   . SER A 1 116 ? 65.822  23.546 13.048 1.00 20.75 ? 114 SER A N   1 
ATOM   788  C CA  . SER A 1 116 ? 66.740  23.311 14.181 1.00 20.33 ? 114 SER A CA  1 
ATOM   789  C C   . SER A 1 116 ? 66.578  24.361 15.268 1.00 20.10 ? 114 SER A C   1 
ATOM   790  O O   . SER A 1 116 ? 66.151  25.492 14.978 1.00 19.47 ? 114 SER A O   1 
ATOM   791  C CB  . SER A 1 116 ? 68.159  23.224 13.659 1.00 21.93 ? 114 SER A CB  1 
ATOM   792  O OG  . SER A 1 116 ? 69.059  22.769 14.638 1.00 22.66 ? 114 SER A OG  1 
ATOM   793  N N   . LEU A 1 117 ? 66.915  23.961 16.488 1.00 18.78 ? 115 LEU A N   1 
ATOM   794  C CA  . LEU A 1 117 ? 67.108  24.860 17.645 1.00 19.36 ? 115 LEU A CA  1 
ATOM   795  C C   . LEU A 1 117 ? 68.531  24.688 18.162 1.00 18.94 ? 115 LEU A C   1 
ATOM   796  O O   . LEU A 1 117 ? 68.936  23.574 18.531 1.00 24.34 ? 115 LEU A O   1 
ATOM   797  C CB  . LEU A 1 117 ? 66.096  24.546 18.738 1.00 18.48 ? 115 LEU A CB  1 
ATOM   798  C CG  . LEU A 1 117 ? 66.276  25.349 20.024 1.00 19.85 ? 115 LEU A CG  1 
ATOM   799  C CD1 . LEU A 1 117 ? 65.993  26.839 19.772 1.00 20.41 ? 115 LEU A CD1 1 
ATOM   800  C CD2 . LEU A 1 117 ? 65.402  24.789 21.108 1.00 21.78 ? 115 LEU A CD2 1 
ATOM   801  N N   . VAL A 1 118 ? 69.263  25.782 18.231 1.00 21.01 ? 116 VAL A N   1 
ATOM   802  C CA  . VAL A 1 118 ? 70.632  25.858 18.809 1.00 19.60 ? 116 VAL A CA  1 
ATOM   803  C C   . VAL A 1 118 ? 70.510  26.483 20.199 1.00 20.36 ? 116 VAL A C   1 
ATOM   804  O O   . VAL A 1 118 ? 69.988  27.590 20.274 1.00 22.57 ? 116 VAL A O   1 
ATOM   805  C CB  . VAL A 1 118 ? 71.575  26.636 17.880 1.00 21.24 ? 116 VAL A CB  1 
ATOM   806  C CG1 . VAL A 1 118 ? 72.961  26.737 18.479 1.00 21.86 ? 116 VAL A CG1 1 
ATOM   807  C CG2 . VAL A 1 118 ? 71.611  26.046 16.460 1.00 24.08 ? 116 VAL A CG2 1 
ATOM   808  N N   . VAL A 1 119 ? 71.015  25.817 21.239 1.00 20.10 ? 117 VAL A N   1 
ATOM   809  C CA  . VAL A 1 119 ? 71.001  26.307 22.650 1.00 21.32 ? 117 VAL A CA  1 
ATOM   810  C C   . VAL A 1 119 ? 72.455  26.403 23.159 1.00 23.87 ? 117 VAL A C   1 
ATOM   811  O O   . VAL A 1 119 ? 73.316  25.755 22.591 1.00 26.47 ? 117 VAL A O   1 
ATOM   812  C CB  . VAL A 1 119 ? 70.169  25.371 23.546 1.00 22.98 ? 117 VAL A CB  1 
ATOM   813  C CG1 . VAL A 1 119 ? 68.797  25.091 22.951 1.00 25.31 ? 117 VAL A CG1 1 
ATOM   814  C CG2 . VAL A 1 119 ? 70.896  24.076 23.856 1.00 24.97 ? 117 VAL A CG2 1 
ATOM   815  N N   . ASP A 1 120 ? 72.697  27.165 24.235 1.00 29.00 ? 118 ASP A N   1 
ATOM   816  C CA  . ASP A 1 120 ? 73.972  27.262 25.008 1.00 34.47 ? 118 ASP A CA  1 
ATOM   817  C C   . ASP A 1 120 ? 74.101  26.046 25.916 1.00 34.99 ? 118 ASP A C   1 
ATOM   818  O O   . ASP A 1 120 ? 73.085  25.357 26.088 1.00 32.11 ? 118 ASP A O   1 
ATOM   819  C CB  . ASP A 1 120 ? 73.964  28.479 25.946 1.00 45.12 ? 118 ASP A CB  1 
ATOM   820  C CG  . ASP A 1 120 ? 74.726  29.708 25.474 1.00 55.37 ? 118 ASP A CG  1 
ATOM   821  O OD1 . ASP A 1 120 ? 75.893  29.560 25.049 1.00 59.20 ? 118 ASP A OD1 1 
ATOM   822  O OD2 . ASP A 1 120 ? 74.169  30.820 25.590 1.00 61.10 ? 118 ASP A OD2 1 
ATOM   823  N N   . LEU A 1 121 ? 75.231  25.913 26.618 1.00 34.44 ? 119 LEU A N   1 
ATOM   824  C CA  . LEU A 1 121 ? 75.535  24.801 27.560 1.00 41.76 ? 119 LEU A CA  1 
ATOM   825  C C   . LEU A 1 121 ? 74.461  24.727 28.634 1.00 35.62 ? 119 LEU A C   1 
ATOM   826  O O   . LEU A 1 121 ? 74.160  23.596 29.030 1.00 39.33 ? 119 LEU A O   1 
ATOM   827  C CB  . LEU A 1 121 ? 76.919  25.017 28.197 1.00 53.54 ? 119 LEU A CB  1 
ATOM   828  N N   . PHE A 1 122 ? 73.844  25.853 29.053 1.00 31.69 ? 120 PHE A N   1 
ATOM   829  C CA  . PHE A 1 122 ? 72.805  25.816 30.124 1.00 32.90 ? 120 PHE A CA  1 
ATOM   830  C C   . PHE A 1 122 ? 71.383  25.800 29.546 1.00 29.48 ? 120 PHE A C   1 
ATOM   831  O O   . PHE A 1 122 ? 70.453  26.107 30.282 1.00 28.66 ? 120 PHE A O   1 
ATOM   832  C CB  . PHE A 1 122 ? 73.001  26.964 31.114 1.00 34.42 ? 120 PHE A CB  1 
ATOM   833  C CG  . PHE A 1 122 ? 74.258  26.758 31.912 1.00 40.68 ? 120 PHE A CG  1 
ATOM   834  C CD1 . PHE A 1 122 ? 74.305  25.787 32.895 1.00 46.36 ? 120 PHE A CD1 1 
ATOM   835  C CD2 . PHE A 1 122 ? 75.422  27.423 31.592 1.00 44.12 ? 120 PHE A CD2 1 
ATOM   836  C CE1 . PHE A 1 122 ? 75.477  25.537 33.591 1.00 54.01 ? 120 PHE A CE1 1 
ATOM   837  C CE2 . PHE A 1 122 ? 76.586  27.183 32.301 1.00 41.30 ? 120 PHE A CE2 1 
ATOM   838  C CZ  . PHE A 1 122 ? 76.617  26.236 33.286 1.00 43.92 ? 120 PHE A CZ  1 
ATOM   839  N N   . GLY A 1 123 ? 71.230  25.471 28.262 1.00 27.73 ? 121 GLY A N   1 
ATOM   840  C CA  . GLY A 1 123 ? 69.926  25.482 27.588 1.00 25.21 ? 121 GLY A CA  1 
ATOM   841  C C   . GLY A 1 123 ? 69.422  24.082 27.279 1.00 24.22 ? 121 GLY A C   1 
ATOM   842  O O   . GLY A 1 123 ? 68.489  23.983 26.498 1.00 27.13 ? 121 GLY A O   1 
ATOM   843  N N   . THR A 1 124 ? 69.963  23.025 27.867 1.00 25.20 ? 122 THR A N   1 
ATOM   844  C CA  . THR A 1 124 ? 69.606  21.635 27.459 1.00 23.63 ? 122 THR A CA  1 
ATOM   845  C C   . THR A 1 124 ? 68.115  21.334 27.727 1.00 23.34 ? 122 THR A C   1 
ATOM   846  O O   . THR A 1 124 ? 67.572  20.413 27.059 1.00 22.81 ? 122 THR A O   1 
ATOM   847  C CB  . THR A 1 124 ? 70.502  20.541 28.048 1.00 24.52 ? 122 THR A CB  1 
ATOM   848  O OG1 . THR A 1 124 ? 70.163  20.359 29.427 1.00 24.60 ? 122 THR A OG1 1 
ATOM   849  C CG2 . THR A 1 124 ? 71.984  20.791 27.831 1.00 26.81 ? 122 THR A CG2 1 
ATOM   850  N N   . ASP A 1 125 ? 67.463  21.991 28.691 1.00 24.03 ? 123 ASP A N   1 
ATOM   851  C CA  . ASP A 1 125 ? 66.015  21.743 28.955 1.00 25.45 ? 123 ASP A CA  1 
ATOM   852  C C   . ASP A 1 125 ? 65.188  22.202 27.750 1.00 24.30 ? 123 ASP A C   1 
ATOM   853  O O   . ASP A 1 125 ? 64.118  21.615 27.507 1.00 20.40 ? 123 ASP A O   1 
ATOM   854  C CB  . ASP A 1 125 ? 65.542  22.345 30.285 1.00 23.24 ? 123 ASP A CB  1 
ATOM   855  C CG  . ASP A 1 125 ? 65.999  21.516 31.478 1.00 26.29 ? 123 ASP A CG  1 
ATOM   856  O OD1 . ASP A 1 125 ? 66.492  20.401 31.272 1.00 27.33 ? 123 ASP A OD1 1 
ATOM   857  O OD2 . ASP A 1 125 ? 65.967  22.047 32.582 1.00 29.10 ? 123 ASP A OD2 1 
ATOM   858  N N   . ALA A 1 126 ? 65.715  23.113 26.936 1.00 22.03 ? 124 ALA A N   1 
ATOM   859  C CA  . ALA A 1 126 ? 65.025  23.556 25.709 1.00 21.85 ? 124 ALA A CA  1 
ATOM   860  C C   . ALA A 1 126 ? 65.095  22.474 24.634 1.00 22.91 ? 124 ALA A C   1 
ATOM   861  O O   . ALA A 1 126 ? 64.351  22.610 23.653 1.00 22.65 ? 124 ALA A O   1 
ATOM   862  C CB  . ALA A 1 126 ? 65.566  24.876 25.208 1.00 21.56 ? 124 ALA A CB  1 
ATOM   863  N N   . PHE A 1 127 ? 65.925  21.432 24.787 1.00 23.27 ? 125 PHE A N   1 
ATOM   864  C CA  . PHE A 1 127 ? 65.883  20.281 23.850 1.00 24.85 ? 125 PHE A CA  1 
ATOM   865  C C   . PHE A 1 127 ? 64.475  19.662 23.794 1.00 25.21 ? 125 PHE A C   1 
ATOM   866  O O   . PHE A 1 127 ? 64.110  19.083 22.738 1.00 25.67 ? 125 PHE A O   1 
ATOM   867  C CB  . PHE A 1 127 ? 66.844  19.172 24.235 1.00 25.85 ? 125 PHE A CB  1 
ATOM   868  C CG  . PHE A 1 127 ? 68.316  19.485 24.141 1.00 23.23 ? 125 PHE A CG  1 
ATOM   869  C CD1 . PHE A 1 127 ? 68.806  20.509 23.335 1.00 24.29 ? 125 PHE A CD1 1 
ATOM   870  C CD2 . PHE A 1 127 ? 69.207  18.681 24.815 1.00 23.47 ? 125 PHE A CD2 1 
ATOM   871  C CE1 . PHE A 1 127 ? 70.168  20.701 23.203 1.00 24.64 ? 125 PHE A CE1 1 
ATOM   872  C CE2 . PHE A 1 127 ? 70.570  18.877 24.684 1.00 26.44 ? 125 PHE A CE2 1 
ATOM   873  C CZ  . PHE A 1 127 ? 71.044  19.903 23.897 1.00 23.44 ? 125 PHE A CZ  1 
ATOM   874  N N   . ASP A 1 128 ? 63.748  19.650 24.908 1.00 25.21 ? 126 ASP A N   1 
ATOM   875  C CA  . ASP A 1 128 ? 62.443  18.935 24.995 1.00 26.64 ? 126 ASP A CA  1 
ATOM   876  C C   . ASP A 1 128 ? 61.485  19.492 23.950 1.00 25.76 ? 126 ASP A C   1 
ATOM   877  O O   . ASP A 1 128 ? 61.011  18.747 23.101 1.00 25.64 ? 126 ASP A O   1 
ATOM   878  C CB  . ASP A 1 128 ? 61.872  18.939 26.416 1.00 28.43 ? 126 ASP A CB  1 
ATOM   879  C CG  . ASP A 1 128 ? 62.718  18.166 27.419 1.00 32.39 ? 126 ASP A CG  1 
ATOM   880  O OD1 . ASP A 1 128 ? 63.708  17.535 27.025 1.00 36.85 ? 126 ASP A OD1 1 
ATOM   881  O OD2 . ASP A 1 128 ? 62.419  18.292 28.615 1.00 47.10 ? 126 ASP A OD2 1 
ATOM   882  N N   . PRO A 1 129 ? 61.158  20.806 23.930 1.00 25.53 ? 127 PRO A N   1 
ATOM   883  C CA  . PRO A 1 129 ? 60.295  21.349 22.876 1.00 23.81 ? 127 PRO A CA  1 
ATOM   884  C C   . PRO A 1 129 ? 60.803  21.115 21.458 1.00 24.96 ? 127 PRO A C   1 
ATOM   885  O O   . PRO A 1 129 ? 59.992  20.939 20.574 1.00 25.34 ? 127 PRO A O   1 
ATOM   886  C CB  . PRO A 1 129 ? 60.279  22.863 23.122 1.00 26.62 ? 127 PRO A CB  1 
ATOM   887  C CG  . PRO A 1 129 ? 60.679  23.021 24.556 1.00 27.18 ? 127 PRO A CG  1 
ATOM   888  C CD  . PRO A 1 129 ? 61.497  21.808 24.946 1.00 25.04 ? 127 PRO A CD  1 
ATOM   889  N N   . ALA A 1 130 ? 62.117  21.178 21.249 1.00 22.88 ? 128 ALA A N   1 
ATOM   890  C CA  . ALA A 1 130 ? 62.701  20.920 19.912 1.00 22.22 ? 128 ALA A CA  1 
ATOM   891  C C   . ALA A 1 130 ? 62.376  19.472 19.484 1.00 19.95 ? 128 ALA A C   1 
ATOM   892  O O   . ALA A 1 130 ? 61.900  19.248 18.355 1.00 21.83 ? 128 ALA A O   1 
ATOM   893  C CB  . ALA A 1 130 ? 64.180  21.179 19.959 1.00 20.36 ? 128 ALA A CB  1 
ATOM   894  N N   . ILE A 1 131 ? 62.636  18.525 20.374 1.00 20.52 ? 129 ILE A N   1 
ATOM   895  C CA  . ILE A 1 131 ? 62.453  17.092 20.048 1.00 24.58 ? 129 ILE A CA  1 
ATOM   896  C C   . ILE A 1 131 ? 60.957  16.844 19.829 1.00 24.45 ? 129 ILE A C   1 
ATOM   897  O O   . ILE A 1 131 ? 60.580  16.169 18.826 1.00 24.15 ? 129 ILE A O   1 
ATOM   898  C CB  . ILE A 1 131 ? 63.044  16.221 21.162 1.00 25.89 ? 129 ILE A CB  1 
ATOM   899  C CG1 . ILE A 1 131 ? 64.567  16.322 21.220 1.00 27.63 ? 129 ILE A CG1 1 
ATOM   900  C CG2 . ILE A 1 131 ? 62.569  14.786 20.961 1.00 29.24 ? 129 ILE A CG2 1 
ATOM   901  C CD1 . ILE A 1 131 ? 65.166  15.697 22.469 1.00 27.33 ? 129 ILE A CD1 1 
ATOM   902  N N   . GLU A 1 132 ? 60.127  17.461 20.666 1.00 23.10 ? 130 GLU A N   1 
ATOM   903  C CA  . GLU A 1 132 ? 58.650  17.368 20.559 1.00 24.67 ? 130 GLU A CA  1 
ATOM   904  C C   . GLU A 1 132 ? 58.233  17.843 19.172 1.00 26.10 ? 130 GLU A C   1 
ATOM   905  O O   . GLU A 1 132 ? 57.416  17.142 18.522 1.00 23.70 ? 130 GLU A O   1 
ATOM   906  C CB  . GLU A 1 132 ? 57.964  18.198 21.640 1.00 24.58 ? 130 GLU A CB  1 
ATOM   907  C CG  . GLU A 1 132 ? 58.141  17.632 23.015 1.00 26.01 ? 130 GLU A CG  1 
ATOM   908  C CD  . GLU A 1 132 ? 57.955  18.583 24.173 1.00 26.37 ? 130 GLU A CD  1 
ATOM   909  O OE1 . GLU A 1 132 ? 57.542  19.727 23.960 1.00 27.93 ? 130 GLU A OE1 1 
ATOM   910  O OE2 . GLU A 1 132 ? 58.227  18.138 25.294 1.00 33.66 ? 130 GLU A OE2 1 
ATOM   911  N N   . LEU A 1 133 ? 58.792  18.968 18.696 1.00 25.09 ? 131 LEU A N   1 
ATOM   912  C CA  . LEU A 1 133 ? 58.315  19.577 17.425 1.00 24.63 ? 131 LEU A CA  1 
ATOM   913  C C   . LEU A 1 133 ? 58.965  18.890 16.220 1.00 26.52 ? 131 LEU A C   1 
ATOM   914  O O   . LEU A 1 133 ? 58.582  19.262 15.097 1.00 25.94 ? 131 LEU A O   1 
ATOM   915  C CB  . LEU A 1 133 ? 58.562  21.090 17.433 1.00 27.25 ? 131 LEU A CB  1 
ATOM   916  C CG  . LEU A 1 133 ? 57.588  21.864 18.323 1.00 30.86 ? 131 LEU A CG  1 
ATOM   917  C CD1 . LEU A 1 133 ? 58.028  23.304 18.555 1.00 31.25 ? 131 LEU A CD1 1 
ATOM   918  C CD2 . LEU A 1 133 ? 56.170  21.820 17.748 1.00 32.09 ? 131 LEU A CD2 1 
ATOM   919  N N   . GLY A 1 134 ? 59.942  17.994 16.440 1.00 27.17 ? 132 GLY A N   1 
ATOM   920  C CA  . GLY A 1 134 ? 60.639  17.237 15.382 1.00 27.27 ? 132 GLY A CA  1 
ATOM   921  C C   . GLY A 1 134 ? 61.751  18.040 14.709 1.00 28.76 ? 132 GLY A C   1 
ATOM   922  O O   . GLY A 1 134 ? 62.122  17.707 13.597 1.00 26.72 ? 132 GLY A O   1 
ATOM   923  N N   . ILE A 1 135 ? 62.272  19.062 15.372 1.00 24.79 ? 133 ILE A N   1 
ATOM   924  C CA  . ILE A 1 135 ? 63.442  19.833 14.871 1.00 25.49 ? 133 ILE A CA  1 
ATOM   925  C C   . ILE A 1 135 ? 64.696  19.387 15.604 1.00 21.90 ? 133 ILE A C   1 
ATOM   926  O O   . ILE A 1 135 ? 64.595  18.784 16.691 1.00 24.29 ? 133 ILE A O   1 
ATOM   927  C CB  . ILE A 1 135 ? 63.162  21.345 14.979 1.00 25.06 ? 133 ILE A CB  1 
ATOM   928  C CG1 . ILE A 1 135 ? 63.072  21.812 16.424 1.00 29.41 ? 133 ILE A CG1 1 
ATOM   929  C CG2 . ILE A 1 135 ? 61.915  21.719 14.185 1.00 27.14 ? 133 ILE A CG2 1 
ATOM   930  C CD1 . ILE A 1 135 ? 63.037  23.347 16.566 1.00 29.50 ? 133 ILE A CD1 1 
ATOM   931  N N   . SER A 1 136 ? 65.855  19.611 15.000 1.00 22.81 ? 134 SER A N   1 
ATOM   932  C CA  . SER A 1 136 ? 67.135  19.063 15.506 1.00 22.97 ? 134 SER A CA  1 
ATOM   933  C C   . SER A 1 136 ? 67.666  19.931 16.653 1.00 23.16 ? 134 SER A C   1 
ATOM   934  O O   . SER A 1 136 ? 67.847  21.138 16.483 1.00 25.37 ? 134 SER A O   1 
ATOM   935  C CB  . SER A 1 136 ? 68.077  18.968 14.374 1.00 24.64 ? 134 SER A CB  1 
ATOM   936  O OG  . SER A 1 136 ? 68.261  20.242 13.805 1.00 29.14 ? 134 SER A OG  1 
ATOM   937  N N   . PRO A 1 137 ? 67.907  19.365 17.849 1.00 21.11 ? 135 PRO A N   1 
ATOM   938  C CA  . PRO A 1 137 ? 68.549  20.103 18.928 1.00 22.67 ? 135 PRO A CA  1 
ATOM   939  C C   . PRO A 1 137 ? 70.076  20.101 18.739 1.00 21.55 ? 135 PRO A C   1 
ATOM   940  O O   . PRO A 1 137 ? 70.681  19.029 18.560 1.00 21.28 ? 135 PRO A O   1 
ATOM   941  C CB  . PRO A 1 137 ? 68.133  19.333 20.184 1.00 22.58 ? 135 PRO A CB  1 
ATOM   942  C CG  . PRO A 1 137 ? 68.027  17.887 19.690 1.00 24.01 ? 135 PRO A CG  1 
ATOM   943  C CD  . PRO A 1 137 ? 67.602  17.975 18.238 1.00 23.95 ? 135 PRO A CD  1 
ATOM   944  N N   . TYR A 1 138 ? 70.673  21.292 18.780 1.00 18.85 ? 136 TYR A N   1 
ATOM   945  C CA  . TYR A 1 138 ? 72.132  21.557 18.681 1.00 19.19 ? 136 TYR A CA  1 
ATOM   946  C C   . TYR A 1 138 ? 72.558  22.386 19.889 1.00 19.71 ? 136 TYR A C   1 
ATOM   947  O O   . TYR A 1 138 ? 71.710  23.103 20.423 1.00 21.54 ? 136 TYR A O   1 
ATOM   948  C CB  . TYR A 1 138 ? 72.530  22.296 17.396 1.00 19.81 ? 136 TYR A CB  1 
ATOM   949  C CG  . TYR A 1 138 ? 72.702  21.386 16.209 1.00 19.20 ? 136 TYR A CG  1 
ATOM   950  C CD1 . TYR A 1 138 ? 71.596  20.851 15.553 1.00 21.01 ? 136 TYR A CD1 1 
ATOM   951  C CD2 . TYR A 1 138 ? 73.960  21.105 15.689 1.00 22.84 ? 136 TYR A CD2 1 
ATOM   952  C CE1 . TYR A 1 138 ? 71.738  20.012 14.458 1.00 22.73 ? 136 TYR A CE1 1 
ATOM   953  C CE2 . TYR A 1 138 ? 74.111  20.283 14.584 1.00 21.29 ? 136 TYR A CE2 1 
ATOM   954  C CZ  . TYR A 1 138 ? 73.001  19.736 13.964 1.00 22.26 ? 136 TYR A CZ  1 
ATOM   955  O OH  . TYR A 1 138 ? 73.182  18.903 12.871 1.00 22.86 ? 136 TYR A OH  1 
ATOM   956  N N   . ILE A 1 139 ? 73.793  22.164 20.320 1.00 21.56 ? 137 ILE A N   1 
ATOM   957  C CA  . ILE A 1 139 ? 74.515  22.957 21.338 1.00 24.91 ? 137 ILE A CA  1 
ATOM   958  C C   . ILE A 1 139 ? 75.552  23.836 20.648 1.00 26.40 ? 137 ILE A C   1 
ATOM   959  O O   . ILE A 1 139 ? 76.305  23.351 19.772 1.00 28.09 ? 137 ILE A O   1 
ATOM   960  C CB  . ILE A 1 139 ? 75.229  22.094 22.387 1.00 29.50 ? 137 ILE A CB  1 
ATOM   961  C CG1 . ILE A 1 139 ? 74.265  21.288 23.233 1.00 30.75 ? 137 ILE A CG1 1 
ATOM   962  C CG2 . ILE A 1 139 ? 76.096  22.986 23.283 1.00 32.02 ? 137 ILE A CG2 1 
ATOM   963  C CD1 . ILE A 1 139 ? 74.991  20.345 24.169 1.00 33.66 ? 137 ILE A CD1 1 
ATOM   964  N N   . PHE A 1 140 ? 75.574  25.097 21.068 1.00 24.89 ? 138 PHE A N   1 
ATOM   965  C CA  . PHE A 1 140 ? 76.594  26.104 20.727 1.00 25.57 ? 138 PHE A CA  1 
ATOM   966  C C   . PHE A 1 140 ? 77.413  26.391 21.989 1.00 24.15 ? 138 PHE A C   1 
ATOM   967  O O   . PHE A 1 140 ? 76.793  26.744 23.026 1.00 23.67 ? 138 PHE A O   1 
ATOM   968  C CB  . PHE A 1 140 ? 75.954  27.397 20.256 1.00 26.77 ? 138 PHE A CB  1 
ATOM   969  C CG  . PHE A 1 140 ? 76.969  28.395 19.788 1.00 26.08 ? 138 PHE A CG  1 
ATOM   970  C CD1 . PHE A 1 140 ? 77.580  29.269 20.694 1.00 27.64 ? 138 PHE A CD1 1 
ATOM   971  C CD2 . PHE A 1 140 ? 77.305  28.487 18.448 1.00 26.21 ? 138 PHE A CD2 1 
ATOM   972  C CE1 . PHE A 1 140 ? 78.530  30.184 20.258 1.00 24.38 ? 138 PHE A CE1 1 
ATOM   973  C CE2 . PHE A 1 140 ? 78.273  29.389 18.024 1.00 25.97 ? 138 PHE A CE2 1 
ATOM   974  C CZ  . PHE A 1 140 ? 78.865  30.247 18.921 1.00 26.39 ? 138 PHE A CZ  1 
ATOM   975  N N   . PHE A 1 141 ? 78.730  26.197 21.931 1.00 20.42 ? 139 PHE A N   1 
ATOM   976  C CA  . PHE A 1 141 ? 79.628  26.398 23.098 1.00 23.36 ? 139 PHE A CA  1 
ATOM   977  C C   . PHE A 1 141 ? 80.497  27.609 22.803 1.00 23.54 ? 139 PHE A C   1 
ATOM   978  O O   . PHE A 1 141 ? 81.363  27.549 21.937 1.00 22.16 ? 139 PHE A O   1 
ATOM   979  C CB  . PHE A 1 141 ? 80.430  25.132 23.385 1.00 26.46 ? 139 PHE A CB  1 
ATOM   980  C CG  . PHE A 1 141 ? 80.921  25.068 24.807 1.00 33.76 ? 139 PHE A CG  1 
ATOM   981  C CD1 . PHE A 1 141 ? 82.136  25.642 25.175 1.00 33.17 ? 139 PHE A CD1 1 
ATOM   982  C CD2 . PHE A 1 141 ? 80.142  24.460 25.792 1.00 40.49 ? 139 PHE A CD2 1 
ATOM   983  C CE1 . PHE A 1 141 ? 82.551  25.627 26.498 1.00 37.01 ? 139 PHE A CE1 1 
ATOM   984  C CE2 . PHE A 1 141 ? 80.563  24.443 27.115 1.00 42.42 ? 139 PHE A CE2 1 
ATOM   985  C CZ  . PHE A 1 141 ? 81.771  25.014 27.459 1.00 42.03 ? 139 PHE A CZ  1 
ATOM   986  N N   . PRO A 1 142 ? 80.272  28.760 23.467 1.00 24.17 ? 140 PRO A N   1 
ATOM   987  C CA  . PRO A 1 142 ? 80.980  29.986 23.102 1.00 26.66 ? 140 PRO A CA  1 
ATOM   988  C C   . PRO A 1 142 ? 82.363  30.108 23.739 1.00 28.12 ? 140 PRO A C   1 
ATOM   989  O O   . PRO A 1 142 ? 83.069  31.005 23.364 1.00 31.32 ? 140 PRO A O   1 
ATOM   990  C CB  . PRO A 1 142 ? 80.047  31.070 23.686 1.00 28.74 ? 140 PRO A CB  1 
ATOM   991  C CG  . PRO A 1 142 ? 79.482  30.422 24.912 1.00 27.62 ? 140 PRO A CG  1 
ATOM   992  C CD  . PRO A 1 142 ? 79.273  28.971 24.532 1.00 26.67 ? 140 PRO A CD  1 
ATOM   993  N N   . SER A 1 143 ? 82.679  29.249 24.717 1.00 26.81 ? 141 SER A N   1 
ATOM   994  C CA  . SER A 1 143 ? 83.983  29.270 25.414 1.00 33.04 ? 141 SER A CA  1 
ATOM   995  C C   . SER A 1 143 ? 84.936  28.228 24.813 1.00 30.37 ? 141 SER A C   1 
ATOM   996  O O   . SER A 1 143 ? 84.735  27.810 23.648 1.00 25.76 ? 141 SER A O   1 
ATOM   997  C CB  . SER A 1 143 ? 83.832  29.135 26.916 1.00 38.47 ? 141 SER A CB  1 
ATOM   998  O OG  . SER A 1 143 ? 85.088  29.467 27.541 1.00 57.17 ? 141 SER A OG  1 
ATOM   999  N N   . THR A 1 144 ? 85.993  27.887 25.554 1.00 24.54 ? 142 THR A N   1 
ATOM   1000 C CA  . THR A 1 144 ? 87.098  27.044 25.059 1.00 24.30 ? 142 THR A CA  1 
ATOM   1001 C C   . THR A 1 144 ? 86.626  25.611 24.833 1.00 24.99 ? 142 THR A C   1 
ATOM   1002 O O   . THR A 1 144 ? 85.682  25.141 25.552 1.00 23.97 ? 142 THR A O   1 
ATOM   1003 C CB  . THR A 1 144 ? 88.299  27.093 25.999 1.00 26.32 ? 142 THR A CB  1 
ATOM   1004 O OG1 . THR A 1 144 ? 87.811  26.583 27.243 1.00 23.35 ? 142 THR A OG1 1 
ATOM   1005 C CG2 . THR A 1 144 ? 88.865  28.491 26.119 1.00 25.64 ? 142 THR A CG2 1 
ATOM   1006 N N   . ALA A 1 145 ? 87.365  24.892 23.991 1.00 23.52 ? 143 ALA A N   1 
ATOM   1007 C CA  . ALA A 1 145 ? 87.252  23.422 23.868 1.00 23.25 ? 143 ALA A CA  1 
ATOM   1008 C C   . ALA A 1 145 ? 87.689  22.770 25.192 1.00 23.44 ? 143 ALA A C   1 
ATOM   1009 O O   . ALA A 1 145 ? 87.136  21.708 25.552 1.00 22.44 ? 143 ALA A O   1 
ATOM   1010 C CB  . ALA A 1 145 ? 88.050  22.911 22.689 1.00 22.73 ? 143 ALA A CB  1 
ATOM   1011 N N   . MET A 1 146 ? 88.588  23.399 25.937 1.00 22.39 ? 144 MET A N   1 
ATOM   1012 C CA  . MET A 1 146 ? 88.977  22.876 27.274 1.00 25.57 ? 144 MET A CA  1 
ATOM   1013 C C   . MET A 1 146 ? 87.776  22.918 28.237 1.00 24.82 ? 144 MET A C   1 
ATOM   1014 O O   . MET A 1 146 ? 87.525  21.900 28.932 1.00 25.95 ? 144 MET A O   1 
ATOM   1015 C CB  . MET A 1 146 ? 90.161  23.661 27.839 1.00 28.22 ? 144 MET A CB  1 
ATOM   1016 C CG  . MET A 1 146 ? 90.362  23.491 29.336 1.00 31.36 ? 144 MET A CG  1 
ATOM   1017 S SD  . MET A 1 146 ? 91.599  24.715 29.991 1.00 37.15 ? 144 MET A SD  1 
ATOM   1018 C CE  . MET A 1 146 ? 93.051  23.967 29.255 1.00 38.07 ? 144 MET A CE  1 
ATOM   1019 N N   . THR A 1 147 ? 87.065  24.036 28.312 1.00 25.04 ? 145 THR A N   1 
ATOM   1020 C CA  . THR A 1 147 ? 85.828  24.168 29.121 1.00 25.90 ? 145 THR A CA  1 
ATOM   1021 C C   . THR A 1 147 ? 84.744  23.199 28.658 1.00 25.38 ? 145 THR A C   1 
ATOM   1022 O O   . THR A 1 147 ? 84.127  22.581 29.546 1.00 25.79 ? 145 THR A O   1 
ATOM   1023 C CB  . THR A 1 147 ? 85.317  25.606 29.184 1.00 30.47 ? 145 THR A CB  1 
ATOM   1024 O OG1 . THR A 1 147 ? 86.423  26.328 29.718 1.00 28.15 ? 145 THR A OG1 1 
ATOM   1025 C CG2 . THR A 1 147 ? 84.084  25.737 30.060 1.00 31.37 ? 145 THR A CG2 1 
ATOM   1026 N N   . LEU A 1 148 ? 84.592  22.975 27.352 1.00 24.39 ? 146 LEU A N   1 
ATOM   1027 C CA  . LEU A 1 148 ? 83.615  21.986 26.836 1.00 27.16 ? 146 LEU A CA  1 
ATOM   1028 C C   . LEU A 1 148 ? 83.997  20.592 27.346 1.00 29.99 ? 146 LEU A C   1 
ATOM   1029 O O   . LEU A 1 148 ? 83.106  19.864 27.852 1.00 29.82 ? 146 LEU A O   1 
ATOM   1030 C CB  . LEU A 1 148 ? 83.572  22.034 25.311 1.00 27.63 ? 146 LEU A CB  1 
ATOM   1031 C CG  . LEU A 1 148 ? 82.660  21.002 24.632 1.00 29.82 ? 146 LEU A CG  1 
ATOM   1032 C CD1 . LEU A 1 148 ? 81.266  21.050 25.225 1.00 32.06 ? 146 LEU A CD1 1 
ATOM   1033 C CD2 . LEU A 1 148 ? 82.615  21.222 23.126 1.00 31.43 ? 146 LEU A CD2 1 
ATOM   1034 N N   . SER A 1 149 ? 85.270  20.220 27.227 1.00 27.33 ? 147 SER A N   1 
ATOM   1035 C CA  . SER A 1 149 ? 85.768  18.902 27.682 1.00 30.03 ? 147 SER A CA  1 
ATOM   1036 C C   . SER A 1 149 ? 85.557  18.759 29.199 1.00 28.42 ? 147 SER A C   1 
ATOM   1037 O O   . SER A 1 149 ? 85.033  17.693 29.644 1.00 27.65 ? 147 SER A O   1 
ATOM   1038 C CB  . SER A 1 149 ? 87.189  18.694 27.294 1.00 29.54 ? 147 SER A CB  1 
ATOM   1039 O OG  . SER A 1 149 ? 87.578  17.422 27.756 1.00 33.47 ? 147 SER A OG  1 
ATOM   1040 N N   . LEU A 1 150 ? 85.867  19.791 29.968 1.00 26.02 ? 148 LEU A N   1 
ATOM   1041 C CA  . LEU A 1 150 ? 85.603  19.776 31.427 1.00 28.84 ? 148 LEU A CA  1 
ATOM   1042 C C   . LEU A 1 150 ? 84.089  19.596 31.691 1.00 29.95 ? 148 LEU A C   1 
ATOM   1043 O O   . LEU A 1 150 ? 83.736  18.750 32.532 1.00 31.67 ? 148 LEU A O   1 
ATOM   1044 C CB  . LEU A 1 150 ? 86.089  21.077 32.058 1.00 31.46 ? 148 LEU A CB  1 
ATOM   1045 C CG  . LEU A 1 150 ? 85.567  21.314 33.474 1.00 37.52 ? 148 LEU A CG  1 
ATOM   1046 C CD1 . LEU A 1 150 ? 86.037  20.194 34.392 1.00 39.39 ? 148 LEU A CD1 1 
ATOM   1047 C CD2 . LEU A 1 150 ? 85.979  22.691 34.010 1.00 36.67 ? 148 LEU A CD2 1 
ATOM   1048 N N   . PHE A 1 151 ? 83.224  20.390 31.056 1.00 31.05 ? 149 PHE A N   1 
ATOM   1049 C CA  . PHE A 1 151 ? 81.742  20.276 31.162 1.00 29.74 ? 149 PHE A CA  1 
ATOM   1050 C C   . PHE A 1 151 ? 81.340  18.802 30.961 1.00 30.59 ? 149 PHE A C   1 
ATOM   1051 O O   . PHE A 1 151 ? 80.732  18.230 31.881 1.00 32.56 ? 149 PHE A O   1 
ATOM   1052 C CB  . PHE A 1 151 ? 81.057  21.239 30.186 1.00 32.50 ? 149 PHE A CB  1 
ATOM   1053 C CG  . PHE A 1 151 ? 79.545  21.170 30.116 1.00 42.58 ? 149 PHE A CG  1 
ATOM   1054 C CD1 . PHE A 1 151 ? 78.751  21.764 31.085 1.00 47.89 ? 149 PHE A CD1 1 
ATOM   1055 C CD2 . PHE A 1 151 ? 78.909  20.562 29.032 1.00 50.57 ? 149 PHE A CD2 1 
ATOM   1056 C CE1 . PHE A 1 151 ? 77.365  21.694 31.010 1.00 52.63 ? 149 PHE A CE1 1 
ATOM   1057 C CE2 . PHE A 1 151 ? 77.523  20.525 28.939 1.00 52.78 ? 149 PHE A CE2 1 
ATOM   1058 C CZ  . PHE A 1 151 ? 76.756  21.087 29.934 1.00 51.88 ? 149 PHE A CZ  1 
ATOM   1059 N N   . LEU A 1 152 ? 81.702  18.191 29.836 1.00 28.82 ? 150 LEU A N   1 
ATOM   1060 C CA  . LEU A 1 152 ? 81.342  16.792 29.476 1.00 31.73 ? 150 LEU A CA  1 
ATOM   1061 C C   . LEU A 1 152 ? 81.863  15.815 30.524 1.00 34.98 ? 150 LEU A C   1 
ATOM   1062 O O   . LEU A 1 152 ? 81.152  14.847 30.815 1.00 39.23 ? 150 LEU A O   1 
ATOM   1063 C CB  . LEU A 1 152 ? 81.920  16.414 28.118 1.00 34.16 ? 150 LEU A CB  1 
ATOM   1064 C CG  . LEU A 1 152 ? 81.390  17.192 26.922 1.00 36.95 ? 150 LEU A CG  1 
ATOM   1065 C CD1 . LEU A 1 152 ? 81.769  16.496 25.625 1.00 36.74 ? 150 LEU A CD1 1 
ATOM   1066 C CD2 . LEU A 1 152 ? 79.892  17.383 27.018 1.00 42.12 ? 150 LEU A CD2 1 
ATOM   1067 N N   . TYR A 1 153 ? 83.041  16.082 31.080 1.00 35.10 ? 151 TYR A N   1 
ATOM   1068 C CA  . TYR A 1 153 ? 83.759  15.220 32.053 1.00 34.80 ? 151 TYR A CA  1 
ATOM   1069 C C   . TYR A 1 153 ? 83.189  15.357 33.484 1.00 37.38 ? 151 TYR A C   1 
ATOM   1070 O O   . TYR A 1 153 ? 83.465  14.434 34.276 1.00 40.01 ? 151 TYR A O   1 
ATOM   1071 C CB  . TYR A 1 153 ? 85.244  15.554 31.921 1.00 38.60 ? 151 TYR A CB  1 
ATOM   1072 C CG  . TYR A 1 153 ? 86.175  14.922 32.917 1.00 39.06 ? 151 TYR A CG  1 
ATOM   1073 C CD1 . TYR A 1 153 ? 86.386  13.555 32.944 1.00 43.22 ? 151 TYR A CD1 1 
ATOM   1074 C CD2 . TYR A 1 153 ? 86.897  15.717 33.796 1.00 49.70 ? 151 TYR A CD2 1 
ATOM   1075 C CE1 . TYR A 1 153 ? 87.266  12.984 33.853 1.00 47.59 ? 151 TYR A CE1 1 
ATOM   1076 C CE2 . TYR A 1 153 ? 87.784  15.168 34.702 1.00 50.35 ? 151 TYR A CE2 1 
ATOM   1077 C CZ  . TYR A 1 153 ? 87.968  13.796 34.726 1.00 50.45 ? 151 TYR A CZ  1 
ATOM   1078 O OH  . TYR A 1 153 ? 88.846  13.278 35.627 1.00 58.31 ? 151 TYR A OH  1 
ATOM   1079 N N   . MET A 1 154 ? 82.422  16.419 33.813 1.00 34.08 ? 152 MET A N   1 
ATOM   1080 C CA  . MET A 1 154 ? 81.911  16.730 35.186 1.00 37.54 ? 152 MET A CA  1 
ATOM   1081 C C   . MET A 1 154 ? 81.185  15.529 35.813 1.00 41.85 ? 152 MET A C   1 
ATOM   1082 O O   . MET A 1 154 ? 81.385  15.252 37.001 1.00 41.04 ? 152 MET A O   1 
ATOM   1083 C CB  . MET A 1 154 ? 80.947  17.926 35.205 1.00 40.22 ? 152 MET A CB  1 
ATOM   1084 C CG  . MET A 1 154 ? 81.626  19.287 35.150 1.00 41.08 ? 152 MET A CG  1 
ATOM   1085 S SD  . MET A 1 154 ? 83.067  19.440 36.219 1.00 39.73 ? 152 MET A SD  1 
ATOM   1086 C CE  . MET A 1 154 ? 82.333  19.175 37.839 1.00 38.09 ? 152 MET A CE  1 
ATOM   1087 N N   . PRO A 1 155 ? 80.287  14.800 35.108 1.00 38.68 ? 153 PRO A N   1 
ATOM   1088 C CA  . PRO A 1 155 ? 79.653  13.620 35.711 1.00 42.25 ? 153 PRO A CA  1 
ATOM   1089 C C   . PRO A 1 155 ? 80.670  12.575 36.210 1.00 42.82 ? 153 PRO A C   1 
ATOM   1090 O O   . PRO A 1 155 ? 80.520  12.065 37.313 1.00 45.45 ? 153 PRO A O   1 
ATOM   1091 C CB  . PRO A 1 155 ? 78.767  13.093 34.577 1.00 40.43 ? 153 PRO A CB  1 
ATOM   1092 C CG  . PRO A 1 155 ? 78.451  14.333 33.772 1.00 38.48 ? 153 PRO A CG  1 
ATOM   1093 C CD  . PRO A 1 155 ? 79.761  15.094 33.769 1.00 39.00 ? 153 PRO A CD  1 
ATOM   1094 N N   . GLN A 1 156 ? 81.700  12.298 35.415 1.00 46.05 ? 154 GLN A N   1 
ATOM   1095 C CA  . GLN A 1 156 ? 82.801  11.375 35.790 1.00 48.02 ? 154 GLN A CA  1 
ATOM   1096 C C   . GLN A 1 156 ? 83.571  11.972 36.987 1.00 48.95 ? 154 GLN A C   1 
ATOM   1097 O O   . GLN A 1 156 ? 83.732  11.261 38.019 1.00 47.00 ? 154 GLN A O   1 
ATOM   1098 C CB  . GLN A 1 156 ? 83.657  11.104 34.556 1.00 52.80 ? 154 GLN A CB  1 
ATOM   1099 C CG  . GLN A 1 156 ? 84.467  9.821  34.633 1.00 64.35 ? 154 GLN A CG  1 
ATOM   1100 C CD  . GLN A 1 156 ? 85.535  9.781  33.564 1.00 71.27 ? 154 GLN A CD  1 
ATOM   1101 O OE1 . GLN A 1 156 ? 85.498  10.535 32.591 1.00 71.62 ? 154 GLN A OE1 1 
ATOM   1102 N NE2 . GLN A 1 156 ? 86.510  8.902  33.742 1.00 74.87 ? 154 GLN A NE2 1 
ATOM   1103 N N   . LEU A 1 157 ? 84.007  13.240 36.911 1.00 47.81 ? 155 LEU A N   1 
ATOM   1104 C CA  . LEU A 1 157 ? 84.828  13.896 37.974 1.00 45.65 ? 155 LEU A CA  1 
ATOM   1105 C C   . LEU A 1 157 ? 84.060  13.859 39.295 1.00 49.41 ? 155 LEU A C   1 
ATOM   1106 O O   . LEU A 1 157 ? 84.700  13.646 40.356 1.00 48.63 ? 155 LEU A O   1 
ATOM   1107 C CB  . LEU A 1 157 ? 85.145  15.339 37.575 1.00 49.19 ? 155 LEU A CB  1 
ATOM   1108 C CG  . LEU A 1 157 ? 86.022  16.133 38.546 1.00 48.15 ? 155 LEU A CG  1 
ATOM   1109 C CD1 . LEU A 1 157 ? 87.382  15.478 38.735 1.00 49.62 ? 155 LEU A CD1 1 
ATOM   1110 C CD2 . LEU A 1 157 ? 86.208  17.546 38.040 1.00 49.86 ? 155 LEU A CD2 1 
ATOM   1111 N N   . ASP A 1 158 ? 82.739  14.064 39.214 1.00 47.76 ? 156 ASP A N   1 
ATOM   1112 C CA  . ASP A 1 158 ? 81.801  14.093 40.365 1.00 51.18 ? 156 ASP A CA  1 
ATOM   1113 C C   . ASP A 1 158 ? 81.804  12.731 41.086 1.00 52.41 ? 156 ASP A C   1 
ATOM   1114 O O   . ASP A 1 158 ? 81.797  12.727 42.331 1.00 51.73 ? 156 ASP A O   1 
ATOM   1115 C CB  . ASP A 1 158 ? 80.402  14.489 39.892 1.00 50.03 ? 156 ASP A CB  1 
ATOM   1116 C CG  . ASP A 1 158 ? 79.361  14.410 40.987 1.00 51.41 ? 156 ASP A CG  1 
ATOM   1117 O OD1 . ASP A 1 158 ? 79.300  15.364 41.779 1.00 49.10 ? 156 ASP A OD1 1 
ATOM   1118 O OD2 . ASP A 1 158 ? 78.673  13.363 41.060 1.00 48.00 ? 156 ASP A OD2 1 
ATOM   1119 N N   . LYS A 1 159 ? 81.802  11.625 40.334 1.00 60.33 ? 157 LYS A N   1 
ATOM   1120 C CA  . LYS A 1 159 ? 81.788  10.235 40.878 1.00 68.91 ? 157 LYS A CA  1 
ATOM   1121 C C   . LYS A 1 159 ? 83.205  9.844  41.346 1.00 72.89 ? 157 LYS A C   1 
ATOM   1122 O O   . LYS A 1 159 ? 83.307  8.920  42.174 1.00 73.27 ? 157 LYS A O   1 
ATOM   1123 C CB  . LYS A 1 159 ? 81.178  9.282  39.838 1.00 68.14 ? 157 LYS A CB  1 
ATOM   1124 C CG  . LYS A 1 159 ? 81.886  7.946  39.663 1.00 76.09 ? 157 LYS A CG  1 
ATOM   1125 C CD  . LYS A 1 159 ? 81.052  6.904  38.956 1.00 80.52 ? 157 LYS A CD  1 
ATOM   1126 C CE  . LYS A 1 159 ? 80.593  5.811  39.898 1.00 82.75 ? 157 LYS A CE  1 
ATOM   1127 N NZ  . LYS A 1 159 ? 79.639  4.892  39.237 1.00 87.18 ? 157 LYS A NZ  1 
ATOM   1128 N N   . SER A 1 160 ? 84.252  10.526 40.860 1.00 73.19 ? 158 SER A N   1 
ATOM   1129 C CA  . SER A 1 160 ? 85.685  10.232 41.152 1.00 75.00 ? 158 SER A CA  1 
ATOM   1130 C C   . SER A 1 160 ? 86.118  10.853 42.487 1.00 73.81 ? 158 SER A C   1 
ATOM   1131 O O   . SER A 1 160 ? 86.544  10.093 43.371 1.00 78.89 ? 158 SER A O   1 
ATOM   1132 C CB  . SER A 1 160 ? 86.593  10.707 40.039 1.00 72.49 ? 158 SER A CB  1 
ATOM   1133 O OG  . SER A 1 160 ? 86.678  9.743  39.006 1.00 72.02 ? 158 SER A OG  1 
ATOM   1134 N N   . VAL A 1 161 ? 86.047  12.186 42.604 1.00 68.30 ? 159 VAL A N   1 
ATOM   1135 C CA  . VAL A 1 161 ? 86.609  12.981 43.739 1.00 66.64 ? 159 VAL A CA  1 
ATOM   1136 C C   . VAL A 1 161 ? 85.552  13.134 44.839 1.00 66.21 ? 159 VAL A C   1 
ATOM   1137 O O   . VAL A 1 161 ? 84.525  13.778 44.543 1.00 61.10 ? 159 VAL A O   1 
ATOM   1138 C CB  . VAL A 1 161 ? 87.105  14.352 43.247 1.00 66.40 ? 159 VAL A CB  1 
ATOM   1139 C CG1 . VAL A 1 161 ? 87.654  15.197 44.388 1.00 64.81 ? 159 VAL A CG1 1 
ATOM   1140 C CG2 . VAL A 1 161 ? 88.130  14.204 42.128 1.00 63.04 ? 159 VAL A CG2 1 
ATOM   1141 N N   . ASP A 1 170 ? 96.083  14.905 41.910 1.00 64.42 ? 168 ASP A N   1 
ATOM   1142 C CA  . ASP A 1 170 ? 95.590  16.066 42.702 1.00 62.73 ? 168 ASP A CA  1 
ATOM   1143 C C   . ASP A 1 170 ? 95.275  17.242 41.754 1.00 58.30 ? 168 ASP A C   1 
ATOM   1144 O O   . ASP A 1 170 ? 94.347  18.005 42.072 1.00 54.00 ? 168 ASP A O   1 
ATOM   1145 C CB  . ASP A 1 170 ? 96.590  16.407 43.806 1.00 60.32 ? 168 ASP A CB  1 
ATOM   1146 C CG  . ASP A 1 170 ? 96.055  17.266 44.944 1.00 69.61 ? 168 ASP A CG  1 
ATOM   1147 O OD1 . ASP A 1 170 ? 94.866  17.117 45.340 1.00 70.39 ? 168 ASP A OD1 1 
ATOM   1148 O OD2 . ASP A 1 170 ? 96.841  18.081 45.436 1.00 73.79 ? 168 ASP A OD2 1 
ATOM   1149 N N   . LEU A 1 171 ? 96.011  17.401 40.646 1.00 57.23 ? 169 LEU A N   1 
ATOM   1150 C CA  . LEU A 1 171 ? 95.632  18.314 39.523 1.00 54.28 ? 169 LEU A CA  1 
ATOM   1151 C C   . LEU A 1 171 ? 94.511  17.640 38.720 1.00 53.72 ? 169 LEU A C   1 
ATOM   1152 O O   . LEU A 1 171 ? 94.505  16.409 38.657 1.00 54.93 ? 169 LEU A O   1 
ATOM   1153 C CB  . LEU A 1 171 ? 96.844  18.598 38.625 1.00 53.08 ? 169 LEU A CB  1 
ATOM   1154 C CG  . LEU A 1 171 ? 97.866  19.620 39.128 1.00 55.58 ? 169 LEU A CG  1 
ATOM   1155 C CD1 . LEU A 1 171 ? 98.893  19.902 38.035 1.00 57.38 ? 169 LEU A CD1 1 
ATOM   1156 C CD2 . LEU A 1 171 ? 97.213  20.921 39.576 1.00 49.77 ? 169 LEU A CD2 1 
ATOM   1157 N N   . VAL A 1 172 ? 93.593  18.412 38.125 1.00 52.56 ? 170 VAL A N   1 
ATOM   1158 C CA  . VAL A 1 172 ? 92.426  17.856 37.373 1.00 48.49 ? 170 VAL A CA  1 
ATOM   1159 C C   . VAL A 1 172 ? 92.871  17.531 35.948 1.00 45.03 ? 170 VAL A C   1 
ATOM   1160 O O   . VAL A 1 172 ? 93.428  18.432 35.297 1.00 46.45 ? 170 VAL A O   1 
ATOM   1161 C CB  . VAL A 1 172 ? 91.233  18.824 37.353 1.00 47.09 ? 170 VAL A CB  1 
ATOM   1162 C CG1 . VAL A 1 172 ? 90.106  18.235 36.519 1.00 44.41 ? 170 VAL A CG1 1 
ATOM   1163 C CG2 . VAL A 1 172 ? 90.773  19.189 38.760 1.00 46.82 ? 170 VAL A CG2 1 
ATOM   1164 N N   . ARG A 1 173 ? 92.634  16.303 35.488 1.00 42.99 ? 171 ARG A N   1 
ATOM   1165 C CA  . ARG A 1 173 ? 93.065  15.866 34.134 1.00 44.79 ? 171 ARG A CA  1 
ATOM   1166 C C   . ARG A 1 173 ? 91.865  16.022 33.194 1.00 39.38 ? 171 ARG A C   1 
ATOM   1167 O O   . ARG A 1 173 ? 91.149  15.055 32.970 1.00 37.85 ? 171 ARG A O   1 
ATOM   1168 C CB  . ARG A 1 173 ? 93.607  14.434 34.215 1.00 48.19 ? 171 ARG A CB  1 
ATOM   1169 N N   . ILE A 1 174 ? 91.614  17.220 32.673 1.00 41.76 ? 172 ILE A N   1 
ATOM   1170 C CA  . ILE A 1 174 ? 90.516  17.389 31.671 1.00 41.86 ? 172 ILE A CA  1 
ATOM   1171 C C   . ILE A 1 174 ? 90.934  16.661 30.384 1.00 39.31 ? 172 ILE A C   1 
ATOM   1172 O O   . ILE A 1 174 ? 92.011  16.929 29.844 1.00 35.59 ? 172 ILE A O   1 
ATOM   1173 C CB  . ILE A 1 174 ? 90.182  18.876 31.424 1.00 40.15 ? 172 ILE A CB  1 
ATOM   1174 C CG1 . ILE A 1 174 ? 89.783  19.612 32.705 1.00 40.83 ? 172 ILE A CG1 1 
ATOM   1175 C CG2 . ILE A 1 174 ? 89.098  18.992 30.363 1.00 44.40 ? 172 ILE A CG2 1 
ATOM   1176 C CD1 . ILE A 1 174 ? 89.923  21.106 32.613 1.00 41.20 ? 172 ILE A CD1 1 
ATOM   1177 N N   . PRO A 1 175 ? 90.139  15.693 29.866 1.00 44.69 ? 173 PRO A N   1 
ATOM   1178 C CA  . PRO A 1 175 ? 90.507  14.972 28.639 1.00 41.19 ? 173 PRO A CA  1 
ATOM   1179 C C   . PRO A 1 175 ? 90.957  15.902 27.502 1.00 43.56 ? 173 PRO A C   1 
ATOM   1180 O O   . PRO A 1 175 ? 90.240  16.851 27.200 1.00 45.12 ? 173 PRO A O   1 
ATOM   1181 C CB  . PRO A 1 175 ? 89.221  14.210 28.281 1.00 42.04 ? 173 PRO A CB  1 
ATOM   1182 C CG  . PRO A 1 175 ? 88.572  13.955 29.638 1.00 42.19 ? 173 PRO A CG  1 
ATOM   1183 C CD  . PRO A 1 175 ? 88.882  15.191 30.458 1.00 42.30 ? 173 PRO A CD  1 
ATOM   1184 N N   . GLY A 1 176 ? 92.143  15.611 26.941 1.00 43.32 ? 174 GLY A N   1 
ATOM   1185 C CA  . GLY A 1 176 ? 92.790  16.326 25.829 1.00 38.96 ? 174 GLY A CA  1 
ATOM   1186 C C   . GLY A 1 176 ? 93.547  17.569 26.267 1.00 44.21 ? 174 GLY A C   1 
ATOM   1187 O O   . GLY A 1 176 ? 94.140  18.233 25.401 1.00 48.24 ? 174 GLY A O   1 
ATOM   1188 N N   . CYS A 1 177 ? 93.515  17.946 27.542 1.00 39.25 ? 175 CYS A N   1 
ATOM   1189 C CA  . CYS A 1 177 ? 94.009  19.283 27.961 1.00 43.41 ? 175 CYS A CA  1 
ATOM   1190 C C   . CYS A 1 177 ? 95.287  19.146 28.789 1.00 44.41 ? 175 CYS A C   1 
ATOM   1191 O O   . CYS A 1 177 ? 95.526  18.066 29.324 1.00 45.60 ? 175 CYS A O   1 
ATOM   1192 C CB  . CYS A 1 177 ? 92.929  20.032 28.737 1.00 42.20 ? 175 CYS A CB  1 
ATOM   1193 S SG  . CYS A 1 177 ? 91.449  20.252 27.719 1.00 42.04 ? 175 CYS A SG  1 
ATOM   1194 N N   . VAL A 1 178 ? 96.041  20.235 28.885 1.00 42.79 ? 176 VAL A N   1 
ATOM   1195 C CA  . VAL A 1 178 ? 97.098  20.458 29.917 1.00 46.83 ? 176 VAL A CA  1 
ATOM   1196 C C   . VAL A 1 178 ? 96.420  20.389 31.290 1.00 52.10 ? 176 VAL A C   1 
ATOM   1197 O O   . VAL A 1 178 ? 95.286  20.850 31.452 1.00 47.64 ? 176 VAL A O   1 
ATOM   1198 C CB  . VAL A 1 178 ? 97.822  21.798 29.682 1.00 47.06 ? 176 VAL A CB  1 
ATOM   1199 C CG1 . VAL A 1 178 ? 98.376  21.901 28.265 1.00 47.32 ? 176 VAL A CG1 1 
ATOM   1200 C CG2 . VAL A 1 178 ? 96.931  22.993 29.982 1.00 44.54 ? 176 VAL A CG2 1 
ATOM   1201 N N   . PRO A 1 179 ? 97.059  19.801 32.329 1.00 48.94 ? 177 PRO A N   1 
ATOM   1202 C CA  . PRO A 1 179 ? 96.374  19.593 33.599 1.00 48.52 ? 177 PRO A CA  1 
ATOM   1203 C C   . PRO A 1 179 ? 96.122  20.967 34.238 1.00 47.61 ? 177 PRO A C   1 
ATOM   1204 O O   . PRO A 1 179 ? 96.759  21.945 33.872 1.00 46.00 ? 177 PRO A O   1 
ATOM   1205 C CB  . PRO A 1 179 ? 97.317  18.658 34.376 1.00 52.40 ? 177 PRO A CB  1 
ATOM   1206 C CG  . PRO A 1 179 ? 98.682  18.982 33.812 1.00 51.13 ? 177 PRO A CG  1 
ATOM   1207 C CD  . PRO A 1 179 ? 98.453  19.328 32.351 1.00 49.95 ? 177 PRO A CD  1 
ATOM   1208 N N   . VAL A 1 180 ? 95.133  21.021 35.126 1.00 48.07 ? 178 VAL A N   1 
ATOM   1209 C CA  . VAL A 1 180 ? 94.532  22.280 35.658 1.00 46.38 ? 178 VAL A CA  1 
ATOM   1210 C C   . VAL A 1 180 ? 94.313  22.089 37.170 1.00 45.28 ? 178 VAL A C   1 
ATOM   1211 O O   . VAL A 1 180 ? 93.918  20.985 37.564 1.00 43.24 ? 178 VAL A O   1 
ATOM   1212 C CB  . VAL A 1 180 ? 93.227  22.555 34.875 1.00 49.72 ? 178 VAL A CB  1 
ATOM   1213 C CG1 . VAL A 1 180 ? 92.250  23.451 35.617 1.00 47.50 ? 178 VAL A CG1 1 
ATOM   1214 C CG2 . VAL A 1 180 ? 93.535  23.084 33.465 1.00 46.80 ? 178 VAL A CG2 1 
ATOM   1215 N N   . ARG A 1 181 ? 94.592  23.096 38.000 1.00 43.37 ? 179 ARG A N   1 
ATOM   1216 C CA  . ARG A 1 181 ? 94.273  23.045 39.461 1.00 49.10 ? 179 ARG A CA  1 
ATOM   1217 C C   . ARG A 1 181 ? 92.747  22.928 39.658 1.00 44.81 ? 179 ARG A C   1 
ATOM   1218 O O   . ARG A 1 181 ? 91.979  23.542 38.861 1.00 42.16 ? 179 ARG A O   1 
ATOM   1219 C CB  . ARG A 1 181 ? 94.865  24.252 40.207 1.00 54.71 ? 179 ARG A CB  1 
ATOM   1220 C CG  . ARG A 1 181 ? 96.355  24.122 40.508 1.00 60.81 ? 179 ARG A CG  1 
ATOM   1221 C CD  . ARG A 1 181 ? 96.944  25.369 41.137 1.00 68.49 ? 179 ARG A CD  1 
ATOM   1222 N NE  . ARG A 1 181 ? 96.287  25.630 42.408 1.00 75.81 ? 179 ARG A NE  1 
ATOM   1223 C CZ  . ARG A 1 181 ? 96.638  25.112 43.585 1.00 77.41 ? 179 ARG A CZ  1 
ATOM   1224 N NH1 . ARG A 1 181 ? 97.683  24.304 43.691 1.00 76.88 ? 179 ARG A NH1 1 
ATOM   1225 N NH2 . ARG A 1 181 ? 95.934  25.418 44.664 1.00 77.50 ? 179 ARG A NH2 1 
ATOM   1226 N N   . GLY A 1 182 ? 92.321  22.151 40.666 1.00 44.64 ? 180 GLY A N   1 
ATOM   1227 C CA  . GLY A 1 182 ? 90.923  22.097 41.144 1.00 49.20 ? 180 GLY A CA  1 
ATOM   1228 C C   . GLY A 1 182 ? 90.384  23.503 41.383 1.00 47.61 ? 180 GLY A C   1 
ATOM   1229 O O   . GLY A 1 182 ? 89.226  23.783 41.018 1.00 48.33 ? 180 GLY A O   1 
ATOM   1230 N N   . SER A 1 183 ? 91.218  24.372 41.957 1.00 45.41 ? 181 SER A N   1 
ATOM   1231 C CA  . SER A 1 183 ? 90.880  25.771 42.303 1.00 48.76 ? 181 SER A CA  1 
ATOM   1232 C C   . SER A 1 183 ? 90.679  26.610 41.036 1.00 45.76 ? 181 SER A C   1 
ATOM   1233 O O   . SER A 1 183 ? 90.155  27.724 41.186 1.00 48.44 ? 181 SER A O   1 
ATOM   1234 C CB  . SER A 1 183 ? 91.926  26.385 43.209 1.00 49.21 ? 181 SER A CB  1 
ATOM   1235 O OG  . SER A 1 183 ? 93.236  26.186 42.699 1.00 55.35 ? 181 SER A OG  1 
ATOM   1236 N N   . ASP A 1 184 ? 91.067  26.118 39.845 1.00 45.14 ? 182 ASP A N   1 
ATOM   1237 C CA  . ASP A 1 184 ? 90.903  26.856 38.560 1.00 45.20 ? 182 ASP A CA  1 
ATOM   1238 C C   . ASP A 1 184 ? 89.646  26.414 37.793 1.00 47.45 ? 182 ASP A C   1 
ATOM   1239 O O   . ASP A 1 184 ? 89.383  27.053 36.739 1.00 46.08 ? 182 ASP A O   1 
ATOM   1240 C CB  . ASP A 1 184 ? 92.083  26.643 37.601 1.00 49.17 ? 182 ASP A CB  1 
ATOM   1241 C CG  . ASP A 1 184 ? 93.367  27.276 38.072 1.00 50.75 ? 182 ASP A CG  1 
ATOM   1242 O OD1 . ASP A 1 184 ? 93.270  28.319 38.750 1.00 49.93 ? 182 ASP A OD1 1 
ATOM   1243 O OD2 . ASP A 1 184 ? 94.440  26.699 37.769 1.00 53.32 ? 182 ASP A OD2 1 
ATOM   1244 N N   . LEU A 1 185 ? 88.947  25.343 38.207 1.00 42.36 ? 183 LEU A N   1 
ATOM   1245 C CA  . LEU A 1 185 ? 87.773  24.818 37.449 1.00 43.42 ? 183 LEU A CA  1 
ATOM   1246 C C   . LEU A 1 185 ? 86.696  25.916 37.407 1.00 43.78 ? 183 LEU A C   1 
ATOM   1247 O O   . LEU A 1 185 ? 86.528  26.600 38.461 1.00 39.47 ? 183 LEU A O   1 
ATOM   1248 C CB  . LEU A 1 185 ? 87.212  23.561 38.122 1.00 45.02 ? 183 LEU A CB  1 
ATOM   1249 C CG  . LEU A 1 185 ? 88.034  22.271 38.043 1.00 44.91 ? 183 LEU A CG  1 
ATOM   1250 C CD1 . LEU A 1 185 ? 87.138  21.082 38.406 1.00 40.45 ? 183 LEU A CD1 1 
ATOM   1251 C CD2 . LEU A 1 185 ? 88.687  22.073 36.684 1.00 43.31 ? 183 LEU A CD2 1 
ATOM   1252 N N   . PHE A 1 186 ? 86.015  26.103 36.259 1.00 39.13 ? 184 PHE A N   1 
ATOM   1253 C CA  . PHE A 1 186 ? 85.079  27.244 36.025 1.00 40.89 ? 184 PHE A CA  1 
ATOM   1254 C C   . PHE A 1 186 ? 84.096  27.354 37.197 1.00 42.40 ? 184 PHE A C   1 
ATOM   1255 O O   . PHE A 1 186 ? 83.758  26.305 37.813 1.00 41.87 ? 184 PHE A O   1 
ATOM   1256 C CB  . PHE A 1 186 ? 84.425  27.195 34.640 1.00 43.13 ? 184 PHE A CB  1 
ATOM   1257 C CG  . PHE A 1 186 ? 83.354  26.162 34.379 1.00 45.82 ? 184 PHE A CG  1 
ATOM   1258 C CD1 . PHE A 1 186 ? 83.401  24.891 34.943 1.00 41.04 ? 184 PHE A CD1 1 
ATOM   1259 C CD2 . PHE A 1 186 ? 82.326  26.448 33.479 1.00 48.64 ? 184 PHE A CD2 1 
ATOM   1260 C CE1 . PHE A 1 186 ? 82.409  23.957 34.664 1.00 45.62 ? 184 PHE A CE1 1 
ATOM   1261 C CE2 . PHE A 1 186 ? 81.348  25.503 33.192 1.00 45.76 ? 184 PHE A CE2 1 
ATOM   1262 C CZ  . PHE A 1 186 ? 81.386  24.264 33.790 1.00 42.95 ? 184 PHE A CZ  1 
ATOM   1263 N N   . ASP A 1 187 ? 83.663  28.592 37.474 1.00 43.37 ? 185 ASP A N   1 
ATOM   1264 C CA  . ASP A 1 187 ? 83.075  29.051 38.768 1.00 47.81 ? 185 ASP A CA  1 
ATOM   1265 C C   . ASP A 1 187 ? 81.803  28.278 39.120 1.00 48.12 ? 185 ASP A C   1 
ATOM   1266 O O   . ASP A 1 187 ? 81.581  27.983 40.299 1.00 42.65 ? 185 ASP A O   1 
ATOM   1267 C CB  . ASP A 1 187 ? 82.826  30.566 38.801 1.00 51.92 ? 185 ASP A CB  1 
ATOM   1268 C CG  . ASP A 1 187 ? 84.042  31.353 39.277 1.00 59.16 ? 185 ASP A CG  1 
ATOM   1269 O OD1 . ASP A 1 187 ? 84.637  30.949 40.337 1.00 59.71 ? 185 ASP A OD1 1 
ATOM   1270 O OD2 . ASP A 1 187 ? 84.415  32.340 38.576 1.00 47.46 ? 185 ASP A OD2 1 
ATOM   1271 N N   . PRO A 1 188 ? 80.931  27.880 38.158 1.00 44.34 ? 186 PRO A N   1 
ATOM   1272 C CA  . PRO A 1 188 ? 79.733  27.130 38.553 1.00 47.99 ? 186 PRO A CA  1 
ATOM   1273 C C   . PRO A 1 188 ? 79.986  25.792 39.291 1.00 46.09 ? 186 PRO A C   1 
ATOM   1274 O O   . PRO A 1 188 ? 79.026  25.279 39.846 1.00 43.73 ? 186 PRO A O   1 
ATOM   1275 C CB  . PRO A 1 188 ? 78.934  26.922 37.247 1.00 48.53 ? 186 PRO A CB  1 
ATOM   1276 C CG  . PRO A 1 188 ? 79.856  27.361 36.100 1.00 51.91 ? 186 PRO A CG  1 
ATOM   1277 C CD  . PRO A 1 188 ? 81.001  28.160 36.712 1.00 48.60 ? 186 PRO A CD  1 
ATOM   1278 N N   . VAL A 1 189 ? 81.214  25.229 39.280 1.00 46.02 ? 187 VAL A N   1 
ATOM   1279 C CA  . VAL A 1 189 ? 81.532  23.951 40.002 1.00 42.99 ? 187 VAL A CA  1 
ATOM   1280 C C   . VAL A 1 189 ? 82.443  24.209 41.211 1.00 45.91 ? 187 VAL A C   1 
ATOM   1281 O O   . VAL A 1 189 ? 82.877  23.205 41.804 1.00 41.41 ? 187 VAL A O   1 
ATOM   1282 C CB  . VAL A 1 189 ? 82.146  22.884 39.073 1.00 43.08 ? 187 VAL A CB  1 
ATOM   1283 C CG1 . VAL A 1 189 ? 81.407  22.832 37.746 1.00 46.00 ? 187 VAL A CG1 1 
ATOM   1284 C CG2 . VAL A 1 189 ? 83.643  23.067 38.846 1.00 41.94 ? 187 VAL A CG2 1 
ATOM   1285 N N   . GLN A 1 190 ? 82.722  25.474 41.569 1.00 48.81 ? 188 GLN A N   1 
ATOM   1286 C CA  . GLN A 1 190 ? 83.669  25.835 42.673 1.00 50.66 ? 188 GLN A CA  1 
ATOM   1287 C C   . GLN A 1 190 ? 82.968  25.697 44.039 1.00 51.48 ? 188 GLN A C   1 
ATOM   1288 O O   . GLN A 1 190 ? 83.630  25.953 45.064 1.00 47.43 ? 188 GLN A O   1 
ATOM   1289 C CB  . GLN A 1 190 ? 84.256  27.245 42.482 1.00 47.93 ? 188 GLN A CB  1 
ATOM   1290 C CG  . GLN A 1 190 ? 85.391  27.329 41.457 1.00 47.54 ? 188 GLN A CG  1 
ATOM   1291 C CD  . GLN A 1 190 ? 86.548  26.395 41.749 1.00 51.86 ? 188 GLN A CD  1 
ATOM   1292 O OE1 . GLN A 1 190 ? 86.935  26.196 42.904 1.00 50.45 ? 188 GLN A OE1 1 
ATOM   1293 N NE2 . GLN A 1 190 ? 87.120  25.815 40.699 1.00 39.98 ? 188 GLN A NE2 1 
ATOM   1294 N N   . ASP A 1 191 ? 81.681  25.321 44.059 1.00 54.03 ? 189 ASP A N   1 
ATOM   1295 C CA  . ASP A 1 191 ? 80.900  25.025 45.296 1.00 53.52 ? 189 ASP A CA  1 
ATOM   1296 C C   . ASP A 1 191 ? 79.891  23.893 45.023 1.00 48.12 ? 189 ASP A C   1 
ATOM   1297 O O   . ASP A 1 191 ? 78.808  24.196 44.491 1.00 43.68 ? 189 ASP A O   1 
ATOM   1298 C CB  . ASP A 1 191 ? 80.193  26.291 45.786 1.00 52.29 ? 189 ASP A CB  1 
ATOM   1299 C CG  . ASP A 1 191 ? 79.414  26.113 47.080 1.00 56.03 ? 189 ASP A CG  1 
ATOM   1300 O OD1 . ASP A 1 191 ? 79.279  24.957 47.541 1.00 49.93 ? 189 ASP A OD1 1 
ATOM   1301 O OD2 . ASP A 1 191 ? 78.919  27.134 47.599 1.00 54.83 ? 189 ASP A OD2 1 
ATOM   1302 N N   . ARG A 1 192 ? 80.205  22.651 45.420 1.00 46.80 ? 190 ARG A N   1 
ATOM   1303 C CA  . ARG A 1 192 ? 79.398  21.448 45.071 1.00 52.35 ? 190 ARG A CA  1 
ATOM   1304 C C   . ARG A 1 192 ? 78.051  21.475 45.794 1.00 55.39 ? 190 ARG A C   1 
ATOM   1305 O O   . ARG A 1 192 ? 77.075  20.909 45.245 1.00 70.53 ? 190 ARG A O   1 
ATOM   1306 C CB  . ARG A 1 192 ? 80.181  20.171 45.380 1.00 52.13 ? 190 ARG A CB  1 
ATOM   1307 C CG  . ARG A 1 192 ? 81.416  20.016 44.503 1.00 48.27 ? 190 ARG A CG  1 
ATOM   1308 C CD  . ARG A 1 192 ? 82.203  18.777 44.863 1.00 50.82 ? 190 ARG A CD  1 
ATOM   1309 N NE  . ARG A 1 192 ? 81.570  17.553 44.383 1.00 47.48 ? 190 ARG A NE  1 
ATOM   1310 C CZ  . ARG A 1 192 ? 82.201  16.396 44.227 1.00 49.01 ? 190 ARG A CZ  1 
ATOM   1311 N NH1 . ARG A 1 192 ? 81.551  15.333 43.778 1.00 50.52 ? 190 ARG A NH1 1 
ATOM   1312 N NH2 . ARG A 1 192 ? 83.493  16.300 44.502 1.00 53.78 ? 190 ARG A NH2 1 
ATOM   1313 N N   . THR A 1 193 ? 77.988  22.120 46.962 1.00 57.78 ? 191 THR A N   1 
ATOM   1314 C CA  . THR A 1 193 ? 76.747  22.224 47.786 1.00 59.11 ? 191 THR A CA  1 
ATOM   1315 C C   . THR A 1 193 ? 75.722  23.095 47.027 1.00 59.72 ? 191 THR A C   1 
ATOM   1316 O O   . THR A 1 193 ? 74.530  22.875 47.232 1.00 58.25 ? 191 THR A O   1 
ATOM   1317 C CB  . THR A 1 193 ? 77.060  22.677 49.229 1.00 53.26 ? 191 THR A CB  1 
ATOM   1318 O OG1 . THR A 1 193 ? 77.406  24.061 49.248 1.00 48.56 ? 191 THR A OG1 1 
ATOM   1319 C CG2 . THR A 1 193 ? 78.170  21.877 49.889 1.00 49.04 ? 191 THR A CG2 1 
ATOM   1320 N N   . ASP A 1 194 ? 76.173  23.993 46.137 1.00 57.01 ? 192 ASP A N   1 
ATOM   1321 C CA  . ASP A 1 194 ? 75.333  25.017 45.456 1.00 53.60 ? 192 ASP A CA  1 
ATOM   1322 C C   . ASP A 1 194 ? 74.437  24.346 44.398 1.00 56.34 ? 192 ASP A C   1 
ATOM   1323 O O   . ASP A 1 194 ? 74.788  23.238 43.882 1.00 59.83 ? 192 ASP A O   1 
ATOM   1324 C CB  . ASP A 1 194 ? 76.187  26.127 44.830 1.00 58.20 ? 192 ASP A CB  1 
ATOM   1325 C CG  . ASP A 1 194 ? 75.403  27.395 44.507 1.00 63.22 ? 192 ASP A CG  1 
ATOM   1326 O OD1 . ASP A 1 194 ? 74.767  27.464 43.415 1.00 64.38 ? 192 ASP A OD1 1 
ATOM   1327 O OD2 . ASP A 1 194 ? 75.413  28.303 45.359 1.00 59.80 ? 192 ASP A OD2 1 
ATOM   1328 N N   . GLU A 1 195 ? 73.308  24.995 44.104 1.00 48.53 ? 193 GLU A N   1 
ATOM   1329 C CA  . GLU A 1 195 ? 72.354  24.593 43.041 1.00 54.00 ? 193 GLU A CA  1 
ATOM   1330 C C   . GLU A 1 195 ? 73.077  24.621 41.685 1.00 45.91 ? 193 GLU A C   1 
ATOM   1331 O O   . GLU A 1 195 ? 72.827  23.724 40.901 1.00 40.64 ? 193 GLU A O   1 
ATOM   1332 C CB  . GLU A 1 195 ? 71.117  25.499 43.048 1.00 57.61 ? 193 GLU A CB  1 
ATOM   1333 C CG  . GLU A 1 195 ? 70.130  25.179 44.167 1.00 65.46 ? 193 GLU A CG  1 
ATOM   1334 C CD  . GLU A 1 195 ? 69.766  23.703 44.287 1.00 73.19 ? 193 GLU A CD  1 
ATOM   1335 O OE1 . GLU A 1 195 ? 68.949  23.222 43.469 1.00 77.39 ? 193 GLU A OE1 1 
ATOM   1336 O OE2 . GLU A 1 195 ? 70.335  23.021 45.168 1.00 80.40 ? 193 GLU A OE2 1 
ATOM   1337 N N   . ALA A 1 196 ? 73.962  25.598 41.450 1.00 45.88 ? 194 ALA A N   1 
ATOM   1338 C CA  . ALA A 1 196 ? 74.714  25.768 40.176 1.00 46.21 ? 194 ALA A CA  1 
ATOM   1339 C C   . ALA A 1 196 ? 75.443  24.463 39.815 1.00 41.63 ? 194 ALA A C   1 
ATOM   1340 O O   . ALA A 1 196 ? 75.465  24.102 38.640 1.00 39.43 ? 194 ALA A O   1 
ATOM   1341 C CB  . ALA A 1 196 ? 75.661  26.936 40.257 1.00 42.53 ? 194 ALA A CB  1 
ATOM   1342 N N   . TYR A 1 197 ? 75.941  23.733 40.805 1.00 37.24 ? 195 TYR A N   1 
ATOM   1343 C CA  . TYR A 1 197 ? 76.696  22.478 40.590 1.00 41.23 ? 195 TYR A CA  1 
ATOM   1344 C C   . TYR A 1 197 ? 75.758  21.365 40.089 1.00 41.67 ? 195 TYR A C   1 
ATOM   1345 O O   . TYR A 1 197 ? 76.096  20.596 39.157 1.00 34.80 ? 195 TYR A O   1 
ATOM   1346 C CB  . TYR A 1 197 ? 77.427  22.062 41.863 1.00 40.56 ? 195 TYR A CB  1 
ATOM   1347 C CG  . TYR A 1 197 ? 78.231  20.815 41.647 1.00 39.03 ? 195 TYR A CG  1 
ATOM   1348 C CD1 . TYR A 1 197 ? 79.483  20.878 41.051 1.00 37.91 ? 195 TYR A CD1 1 
ATOM   1349 C CD2 . TYR A 1 197 ? 77.735  19.574 42.020 1.00 41.56 ? 195 TYR A CD2 1 
ATOM   1350 C CE1 . TYR A 1 197 ? 80.209  19.727 40.803 1.00 37.12 ? 195 TYR A CE1 1 
ATOM   1351 C CE2 . TYR A 1 197 ? 78.457  18.415 41.790 1.00 42.49 ? 195 TYR A CE2 1 
ATOM   1352 C CZ  . TYR A 1 197 ? 79.701  18.497 41.185 1.00 40.17 ? 195 TYR A CZ  1 
ATOM   1353 O OH  . TYR A 1 197 ? 80.429  17.363 40.969 1.00 45.66 ? 195 TYR A OH  1 
ATOM   1354 N N   . LYS A 1 198 ? 74.594  21.240 40.703 1.00 39.74 ? 196 LYS A N   1 
ATOM   1355 C CA  . LYS A 1 198 ? 73.640  20.155 40.334 1.00 43.49 ? 196 LYS A CA  1 
ATOM   1356 C C   . LYS A 1 198 ? 73.099  20.459 38.923 1.00 34.72 ? 196 LYS A C   1 
ATOM   1357 O O   . LYS A 1 198 ? 72.816  19.544 38.180 1.00 32.94 ? 196 LYS A O   1 
ATOM   1358 C CB  . LYS A 1 198 ? 72.547  20.050 41.399 1.00 51.42 ? 196 LYS A CB  1 
ATOM   1359 C CG  . LYS A 1 198 ? 73.042  20.124 42.841 1.00 57.04 ? 196 LYS A CG  1 
ATOM   1360 C CD  . LYS A 1 198 ? 71.926  20.078 43.860 1.00 71.56 ? 196 LYS A CD  1 
ATOM   1361 C CE  . LYS A 1 198 ? 71.081  18.823 43.753 1.00 77.04 ? 196 LYS A CE  1 
ATOM   1362 N NZ  . LYS A 1 198 ? 70.279  18.604 44.980 1.00 82.03 ? 196 LYS A NZ  1 
ATOM   1363 N N   . TRP A 1 199 ? 72.989  21.732 38.573 1.00 33.37 ? 197 TRP A N   1 
ATOM   1364 C CA  . TRP A 1 199 ? 72.568  22.160 37.212 1.00 31.98 ? 197 TRP A CA  1 
ATOM   1365 C C   . TRP A 1 199 ? 73.651  21.792 36.172 1.00 30.46 ? 197 TRP A C   1 
ATOM   1366 O O   . TRP A 1 199 ? 73.319  21.207 35.096 1.00 35.69 ? 197 TRP A O   1 
ATOM   1367 C CB  . TRP A 1 199 ? 72.215  23.639 37.272 1.00 32.98 ? 197 TRP A CB  1 
ATOM   1368 C CG  . TRP A 1 199 ? 70.807  23.888 37.715 1.00 36.21 ? 197 TRP A CG  1 
ATOM   1369 C CD1 . TRP A 1 199 ? 70.377  24.560 38.825 1.00 37.26 ? 197 TRP A CD1 1 
ATOM   1370 C CD2 . TRP A 1 199 ? 69.619  23.478 37.013 1.00 35.98 ? 197 TRP A CD2 1 
ATOM   1371 N NE1 . TRP A 1 199 ? 69.004  24.598 38.856 1.00 37.86 ? 197 TRP A NE1 1 
ATOM   1372 C CE2 . TRP A 1 199 ? 68.510  23.939 37.758 1.00 38.01 ? 197 TRP A CE2 1 
ATOM   1373 C CE3 . TRP A 1 199 ? 69.392  22.782 35.821 1.00 36.70 ? 197 TRP A CE3 1 
ATOM   1374 C CZ2 . TRP A 1 199 ? 67.195  23.723 37.342 1.00 40.48 ? 197 TRP A CZ2 1 
ATOM   1375 C CZ3 . TRP A 1 199 ? 68.094  22.580 35.402 1.00 34.20 ? 197 TRP A CZ3 1 
ATOM   1376 C CH2 . TRP A 1 199 ? 67.014  23.046 36.155 1.00 39.55 ? 197 TRP A CH2 1 
ATOM   1377 N N   . VAL A 1 200 ? 74.921  22.030 36.476 1.00 31.53 ? 198 VAL A N   1 
ATOM   1378 C CA  . VAL A 1 200 ? 76.026  21.645 35.557 1.00 30.68 ? 198 VAL A CA  1 
ATOM   1379 C C   . VAL A 1 200 ? 75.926  20.126 35.309 1.00 31.23 ? 198 VAL A C   1 
ATOM   1380 O O   . VAL A 1 200 ? 76.095  19.659 34.158 1.00 27.82 ? 198 VAL A O   1 
ATOM   1381 C CB  . VAL A 1 200 ? 77.405  22.045 36.100 1.00 31.88 ? 198 VAL A CB  1 
ATOM   1382 C CG1 . VAL A 1 200 ? 78.505  21.411 35.252 1.00 32.98 ? 198 VAL A CG1 1 
ATOM   1383 C CG2 . VAL A 1 200 ? 77.587  23.559 36.192 1.00 35.40 ? 198 VAL A CG2 1 
ATOM   1384 N N   . ILE A 1 201 ? 75.707  19.332 36.347 1.00 30.80 ? 199 ILE A N   1 
ATOM   1385 C CA  . ILE A 1 201 ? 75.605  17.852 36.159 1.00 29.66 ? 199 ILE A CA  1 
ATOM   1386 C C   . ILE A 1 201 ? 74.397  17.506 35.283 1.00 26.44 ? 199 ILE A C   1 
ATOM   1387 O O   . ILE A 1 201 ? 74.508  16.604 34.414 1.00 25.77 ? 199 ILE A O   1 
ATOM   1388 C CB  . ILE A 1 201 ? 75.536  17.091 37.497 1.00 33.61 ? 199 ILE A CB  1 
ATOM   1389 C CG1 . ILE A 1 201 ? 76.767  17.353 38.370 1.00 36.78 ? 199 ILE A CG1 1 
ATOM   1390 C CG2 . ILE A 1 201 ? 75.357  15.608 37.213 1.00 30.35 ? 199 ILE A CG2 1 
ATOM   1391 C CD1 . ILE A 1 201 ? 78.059  16.912 37.752 1.00 40.35 ? 199 ILE A CD1 1 
ATOM   1392 N N   . HIS A 1 202 ? 73.276  18.151 35.542 1.00 25.72 ? 200 HIS A N   1 
ATOM   1393 C CA  . HIS A 1 202 ? 72.008  17.962 34.795 1.00 26.47 ? 200 HIS A CA  1 
ATOM   1394 C C   . HIS A 1 202 ? 72.253  18.201 33.304 1.00 26.41 ? 200 HIS A C   1 
ATOM   1395 O O   . HIS A 1 202 ? 71.897  17.344 32.501 1.00 26.33 ? 200 HIS A O   1 
ATOM   1396 C CB  . HIS A 1 202 ? 70.945  18.914 35.344 1.00 27.20 ? 200 HIS A CB  1 
ATOM   1397 C CG  . HIS A 1 202 ? 69.668  18.910 34.576 1.00 28.57 ? 200 HIS A CG  1 
ATOM   1398 N ND1 . HIS A 1 202 ? 68.706  17.930 34.758 1.00 28.79 ? 200 HIS A ND1 1 
ATOM   1399 C CD2 . HIS A 1 202 ? 69.228  19.717 33.579 1.00 25.13 ? 200 HIS A CD2 1 
ATOM   1400 C CE1 . HIS A 1 202 ? 67.703  18.156 33.932 1.00 32.02 ? 200 HIS A CE1 1 
ATOM   1401 N NE2 . HIS A 1 202 ? 67.990  19.275 33.214 1.00 28.16 ? 200 HIS A NE2 1 
ATOM   1402 N N   . HIS A 1 203 ? 72.856  19.334 32.950 1.00 25.67 ? 201 HIS A N   1 
ATOM   1403 C CA  . HIS A 1 203 ? 73.086  19.699 31.524 1.00 25.63 ? 201 HIS A CA  1 
ATOM   1404 C C   . HIS A 1 203 ? 74.106  18.775 30.879 1.00 24.16 ? 201 HIS A C   1 
ATOM   1405 O O   . HIS A 1 203 ? 73.923  18.371 29.706 1.00 24.00 ? 201 HIS A O   1 
ATOM   1406 C CB  . HIS A 1 203 ? 73.487  21.178 31.444 1.00 26.87 ? 201 HIS A CB  1 
ATOM   1407 C CG  . HIS A 1 203 ? 72.394  22.082 31.871 1.00 25.80 ? 201 HIS A CG  1 
ATOM   1408 N ND1 . HIS A 1 203 ? 71.150  22.057 31.278 1.00 26.27 ? 201 HIS A ND1 1 
ATOM   1409 C CD2 . HIS A 1 203 ? 72.385  23.098 32.763 1.00 25.72 ? 201 HIS A CD2 1 
ATOM   1410 C CE1 . HIS A 1 203 ? 70.400  22.976 31.837 1.00 28.34 ? 201 HIS A CE1 1 
ATOM   1411 N NE2 . HIS A 1 203 ? 71.134  23.612 32.783 1.00 26.73 ? 201 HIS A NE2 1 
ATOM   1412 N N   . SER A 1 204 ? 75.152  18.404 31.627 1.00 26.29 ? 202 SER A N   1 
ATOM   1413 C CA  . SER A 1 204 ? 76.263  17.580 31.128 1.00 27.58 ? 202 SER A CA  1 
ATOM   1414 C C   . SER A 1 204 ? 75.734  16.211 30.696 1.00 27.98 ? 202 SER A C   1 
ATOM   1415 O O   . SER A 1 204 ? 76.131  15.720 29.604 1.00 24.79 ? 202 SER A O   1 
ATOM   1416 C CB  . SER A 1 204 ? 77.379  17.416 32.103 1.00 27.87 ? 202 SER A CB  1 
ATOM   1417 O OG  . SER A 1 204 ? 78.397  16.708 31.430 1.00 28.79 ? 202 SER A OG  1 
ATOM   1418 N N   . ASN A 1 205 ? 74.881  15.611 31.521 1.00 29.37 ? 203 ASN A N   1 
ATOM   1419 C CA  . ASN A 1 205 ? 74.271  14.271 31.257 1.00 28.02 ? 203 ASN A CA  1 
ATOM   1420 C C   . ASN A 1 205 ? 73.341  14.340 30.046 1.00 27.06 ? 203 ASN A C   1 
ATOM   1421 O O   . ASN A 1 205 ? 73.162  13.306 29.409 1.00 27.97 ? 203 ASN A O   1 
ATOM   1422 C CB  . ASN A 1 205 ? 73.534  13.777 32.500 1.00 32.66 ? 203 ASN A CB  1 
ATOM   1423 C CG  . ASN A 1 205 ? 74.504  13.302 33.565 1.00 42.66 ? 203 ASN A CG  1 
ATOM   1424 O OD1 . ASN A 1 205 ? 75.546  12.701 33.250 1.00 44.45 ? 203 ASN A OD1 1 
ATOM   1425 N ND2 . ASN A 1 205 ? 74.192  13.603 34.819 1.00 48.26 ? 203 ASN A ND2 1 
ATOM   1426 N N   . ARG A 1 206 ? 72.836  15.529 29.690 1.00 24.26 ? 204 ARG A N   1 
ATOM   1427 C CA  . ARG A 1 206 ? 71.862  15.676 28.568 1.00 25.20 ? 204 ARG A CA  1 
ATOM   1428 C C   . ARG A 1 206 ? 72.571  15.998 27.242 1.00 27.12 ? 204 ARG A C   1 
ATOM   1429 O O   . ARG A 1 206 ? 71.922  15.939 26.181 1.00 26.13 ? 204 ARG A O   1 
ATOM   1430 C CB  . ARG A 1 206 ? 70.821  16.722 28.937 1.00 25.39 ? 204 ARG A CB  1 
ATOM   1431 C CG  . ARG A 1 206 ? 69.858  16.228 30.015 1.00 27.94 ? 204 ARG A CG  1 
ATOM   1432 C CD  . ARG A 1 206 ? 69.057  17.343 30.629 1.00 27.05 ? 204 ARG A CD  1 
ATOM   1433 N NE  . ARG A 1 206 ? 68.215  17.989 29.644 1.00 28.37 ? 204 ARG A NE  1 
ATOM   1434 C CZ  . ARG A 1 206 ? 67.046  17.513 29.197 1.00 28.22 ? 204 ARG A CZ  1 
ATOM   1435 N NH1 . ARG A 1 206 ? 66.601  16.342 29.604 1.00 26.64 ? 204 ARG A NH1 1 
ATOM   1436 N NH2 . ARG A 1 206 ? 66.365  18.159 28.274 1.00 26.78 ? 204 ARG A NH2 1 
ATOM   1437 N N   . TYR A 1 207 ? 73.862  16.309 27.288 1.00 24.64 ? 205 TYR A N   1 
ATOM   1438 C CA  . TYR A 1 207 ? 74.675  16.669 26.114 1.00 28.83 ? 205 TYR A CA  1 
ATOM   1439 C C   . TYR A 1 207 ? 74.471  15.698 24.944 1.00 25.45 ? 205 TYR A C   1 
ATOM   1440 O O   . TYR A 1 207 ? 74.407  16.120 23.790 1.00 25.44 ? 205 TYR A O   1 
ATOM   1441 C CB  . TYR A 1 207 ? 76.112  16.766 26.608 1.00 30.15 ? 205 TYR A CB  1 
ATOM   1442 C CG  . TYR A 1 207 ? 77.142  16.883 25.537 1.00 36.49 ? 205 TYR A CG  1 
ATOM   1443 C CD1 . TYR A 1 207 ? 77.496  18.135 25.052 1.00 43.11 ? 205 TYR A CD1 1 
ATOM   1444 C CD2 . TYR A 1 207 ? 77.820  15.766 25.070 1.00 41.61 ? 205 TYR A CD2 1 
ATOM   1445 C CE1 . TYR A 1 207 ? 78.479  18.263 24.082 1.00 45.79 ? 205 TYR A CE1 1 
ATOM   1446 C CE2 . TYR A 1 207 ? 78.807  15.877 24.102 1.00 44.32 ? 205 TYR A CE2 1 
ATOM   1447 C CZ  . TYR A 1 207 ? 79.138  17.135 23.611 1.00 46.21 ? 205 TYR A CZ  1 
ATOM   1448 O OH  . TYR A 1 207 ? 80.104  17.296 22.655 1.00 45.06 ? 205 TYR A OH  1 
ATOM   1449 N N   . PRO A 1 208 ? 74.452  14.364 25.148 1.00 24.39 ? 206 PRO A N   1 
ATOM   1450 C CA  . PRO A 1 208 ? 74.274  13.428 24.019 1.00 24.71 ? 206 PRO A CA  1 
ATOM   1451 C C   . PRO A 1 208 ? 72.923  13.509 23.292 1.00 24.03 ? 206 PRO A C   1 
ATOM   1452 O O   . PRO A 1 208 ? 72.755  12.968 22.189 1.00 23.51 ? 206 PRO A O   1 
ATOM   1453 C CB  . PRO A 1 208 ? 74.429  12.056 24.713 1.00 25.48 ? 206 PRO A CB  1 
ATOM   1454 C CG  . PRO A 1 208 ? 75.334  12.359 25.863 1.00 25.92 ? 206 PRO A CG  1 
ATOM   1455 C CD  . PRO A 1 208 ? 74.777  13.669 26.398 1.00 25.30 ? 206 PRO A CD  1 
ATOM   1456 N N   . MET A 1 209 ? 71.967  14.219 23.866 1.00 24.16 ? 207 MET A N   1 
ATOM   1457 C CA  . MET A 1 209 ? 70.700  14.466 23.139 1.00 24.80 ? 207 MET A CA  1 
ATOM   1458 C C   . MET A 1 209 ? 70.971  15.370 21.928 1.00 23.72 ? 207 MET A C   1 
ATOM   1459 O O   . MET A 1 209 ? 70.113  15.413 20.994 1.00 21.67 ? 207 MET A O   1 
ATOM   1460 C CB  . MET A 1 209 ? 69.651  15.094 24.063 1.00 27.41 ? 207 MET A CB  1 
ATOM   1461 C CG  . MET A 1 209 ? 69.114  14.102 25.110 1.00 32.67 ? 207 MET A CG  1 
ATOM   1462 S SD  . MET A 1 209 ? 68.171  14.900 26.455 1.00 31.32 ? 207 MET A SD  1 
ATOM   1463 C CE  . MET A 1 209 ? 66.788  15.354 25.427 1.00 25.82 ? 207 MET A CE  1 
ATOM   1464 N N   . ALA A 1 210 ? 72.083  16.121 21.937 1.00 23.19 ? 208 ALA A N   1 
ATOM   1465 C CA  . ALA A 1 210 ? 72.345  17.090 20.850 1.00 22.35 ? 208 ALA A CA  1 
ATOM   1466 C C   . ALA A 1 210 ? 72.675  16.302 19.577 1.00 24.33 ? 208 ALA A C   1 
ATOM   1467 O O   . ALA A 1 210 ? 73.379  15.302 19.679 1.00 23.96 ? 208 ALA A O   1 
ATOM   1468 C CB  . ALA A 1 210 ? 73.445  18.081 21.205 1.00 24.18 ? 208 ALA A CB  1 
ATOM   1469 N N   . GLU A 1 211 ? 72.194  16.754 18.413 1.00 23.36 ? 209 GLU A N   1 
ATOM   1470 C CA  . GLU A 1 211 ? 72.601  16.188 17.106 1.00 25.74 ? 209 GLU A CA  1 
ATOM   1471 C C   . GLU A 1 211 ? 73.987  16.692 16.725 1.00 27.03 ? 209 GLU A C   1 
ATOM   1472 O O   . GLU A 1 211 ? 74.612  16.089 15.880 1.00 22.16 ? 209 GLU A O   1 
ATOM   1473 C CB  . GLU A 1 211 ? 71.583  16.515 16.031 1.00 27.30 ? 209 GLU A CB  1 
ATOM   1474 C CG  . GLU A 1 211 ? 70.315  15.722 16.216 1.00 30.15 ? 209 GLU A CG  1 
ATOM   1475 C CD  . GLU A 1 211 ? 69.327  15.764 15.057 1.00 32.98 ? 209 GLU A CD  1 
ATOM   1476 O OE1 . GLU A 1 211 ? 69.757  16.076 13.900 1.00 30.07 ? 209 GLU A OE1 1 
ATOM   1477 O OE2 . GLU A 1 211 ? 68.118  15.530 15.336 1.00 33.94 ? 209 GLU A OE2 1 
ATOM   1478 N N   . GLY A 1 212 ? 74.449  17.789 17.312 1.00 22.87 ? 210 GLY A N   1 
ATOM   1479 C CA  . GLY A 1 212 ? 75.801  18.285 17.043 1.00 23.37 ? 210 GLY A CA  1 
ATOM   1480 C C   . GLY A 1 212 ? 76.132  19.396 18.010 1.00 20.12 ? 210 GLY A C   1 
ATOM   1481 O O   . GLY A 1 212 ? 75.189  19.927 18.648 1.00 20.15 ? 210 GLY A O   1 
ATOM   1482 N N   . VAL A 1 213 ? 77.419  19.646 18.155 1.00 22.23 ? 211 VAL A N   1 
ATOM   1483 C CA  . VAL A 1 213 ? 77.978  20.655 19.075 1.00 23.89 ? 211 VAL A CA  1 
ATOM   1484 C C   . VAL A 1 213 ? 78.841  21.614 18.268 1.00 23.16 ? 211 VAL A C   1 
ATOM   1485 O O   . VAL A 1 213 ? 79.762  21.169 17.566 1.00 21.99 ? 211 VAL A O   1 
ATOM   1486 C CB  . VAL A 1 213 ? 78.760  20.022 20.236 1.00 29.38 ? 211 VAL A CB  1 
ATOM   1487 C CG1 . VAL A 1 213 ? 79.290  21.081 21.181 1.00 27.25 ? 211 VAL A CG1 1 
ATOM   1488 C CG2 . VAL A 1 213 ? 77.866  19.015 20.969 1.00 29.59 ? 211 VAL A CG2 1 
ATOM   1489 N N   . ILE A 1 214 ? 78.497  22.896 18.347 1.00 21.62 ? 212 ILE A N   1 
ATOM   1490 C CA  . ILE A 1 214 ? 79.203  23.968 17.612 1.00 21.23 ? 212 ILE A CA  1 
ATOM   1491 C C   . ILE A 1 214 ? 80.187  24.631 18.587 1.00 20.57 ? 212 ILE A C   1 
ATOM   1492 O O   . ILE A 1 214 ? 79.702  25.299 19.510 1.00 23.07 ? 212 ILE A O   1 
ATOM   1493 C CB  . ILE A 1 214 ? 78.162  24.932 17.039 1.00 22.81 ? 212 ILE A CB  1 
ATOM   1494 C CG1 . ILE A 1 214 ? 77.084  24.207 16.228 1.00 25.08 ? 212 ILE A CG1 1 
ATOM   1495 C CG2 . ILE A 1 214 ? 78.834  26.002 16.201 1.00 22.78 ? 212 ILE A CG2 1 
ATOM   1496 C CD1 . ILE A 1 214 ? 75.866  25.066 15.962 1.00 24.60 ? 212 ILE A CD1 1 
ATOM   1497 N N   . GLU A 1 215 ? 81.484  24.446 18.395 1.00 19.00 ? 213 GLU A N   1 
ATOM   1498 C CA  . GLU A 1 215 ? 82.535  24.935 19.326 1.00 22.05 ? 213 GLU A CA  1 
ATOM   1499 C C   . GLU A 1 215 ? 83.213  26.165 18.723 1.00 20.50 ? 213 GLU A C   1 
ATOM   1500 O O   . GLU A 1 215 ? 83.817  26.052 17.640 1.00 22.18 ? 213 GLU A O   1 
ATOM   1501 C CB  . GLU A 1 215 ? 83.508  23.807 19.653 1.00 21.50 ? 213 GLU A CB  1 
ATOM   1502 C CG  . GLU A 1 215 ? 84.788  24.269 20.342 1.00 21.95 ? 213 GLU A CG  1 
ATOM   1503 C CD  . GLU A 1 215 ? 84.532  25.073 21.612 1.00 23.25 ? 213 GLU A CD  1 
ATOM   1504 O OE1 . GLU A 1 215 ? 83.555  24.762 22.320 1.00 24.91 ? 213 GLU A OE1 1 
ATOM   1505 O OE2 . GLU A 1 215 ? 85.281  26.024 21.871 1.00 23.32 ? 213 GLU A OE2 1 
ATOM   1506 N N   . ASN A 1 216 ? 83.271  27.243 19.508 1.00 20.71 ? 214 ASN A N   1 
ATOM   1507 C CA  . ASN A 1 216 ? 84.013  28.483 19.172 1.00 20.40 ? 214 ASN A CA  1 
ATOM   1508 C C   . ASN A 1 216 ? 85.516  28.345 19.428 1.00 21.30 ? 214 ASN A C   1 
ATOM   1509 O O   . ASN A 1 216 ? 86.077  29.003 20.302 1.00 20.69 ? 214 ASN A O   1 
ATOM   1510 C CB  . ASN A 1 216 ? 83.466  29.678 19.922 1.00 19.35 ? 214 ASN A CB  1 
ATOM   1511 C CG  . ASN A 1 216 ? 84.007  30.975 19.369 1.00 20.81 ? 214 ASN A CG  1 
ATOM   1512 O OD1 . ASN A 1 216 ? 84.565  31.025 18.272 1.00 23.21 ? 214 ASN A OD1 1 
ATOM   1513 N ND2 . ASN A 1 216 ? 83.821  32.033 20.129 1.00 20.38 ? 214 ASN A ND2 1 
ATOM   1514 N N   . SER A 1 217 ? 86.182  27.484 18.696 1.00 20.45 ? 215 SER A N   1 
ATOM   1515 C CA  . SER A 1 217 ? 87.652  27.334 18.781 1.00 20.23 ? 215 SER A CA  1 
ATOM   1516 C C   . SER A 1 217 ? 88.195  26.754 17.472 1.00 22.36 ? 215 SER A C   1 
ATOM   1517 O O   . SER A 1 217 ? 87.393  26.478 16.582 1.00 22.99 ? 215 SER A O   1 
ATOM   1518 C CB  . SER A 1 217 ? 88.045  26.523 19.971 1.00 21.44 ? 215 SER A CB  1 
ATOM   1519 O OG  . SER A 1 217 ? 89.436  26.620 20.204 1.00 24.17 ? 215 SER A OG  1 
ATOM   1520 N N   . PHE A 1 218 ? 89.521  26.581 17.375 1.00 21.05 ? 216 PHE A N   1 
ATOM   1521 C CA  . PHE A 1 218 ? 90.151  25.999 16.173 1.00 24.51 ? 216 PHE A CA  1 
ATOM   1522 C C   . PHE A 1 218 ? 91.365  25.171 16.612 1.00 23.83 ? 216 PHE A C   1 
ATOM   1523 O O   . PHE A 1 218 ? 91.918  25.421 17.674 1.00 21.94 ? 216 PHE A O   1 
ATOM   1524 C CB  . PHE A 1 218 ? 90.383  27.071 15.107 1.00 21.97 ? 216 PHE A CB  1 
ATOM   1525 C CG  . PHE A 1 218 ? 91.399  28.123 15.443 1.00 23.10 ? 216 PHE A CG  1 
ATOM   1526 C CD1 . PHE A 1 218 ? 91.044  29.215 16.218 1.00 23.28 ? 216 PHE A CD1 1 
ATOM   1527 C CD2 . PHE A 1 218 ? 92.692  28.056 14.930 1.00 24.99 ? 216 PHE A CD2 1 
ATOM   1528 C CE1 . PHE A 1 218 ? 91.985  30.202 16.515 1.00 23.52 ? 216 PHE A CE1 1 
ATOM   1529 C CE2 . PHE A 1 218 ? 93.619  29.057 15.205 1.00 26.16 ? 216 PHE A CE2 1 
ATOM   1530 C CZ  . PHE A 1 218 ? 93.272  30.117 16.018 1.00 25.84 ? 216 PHE A CZ  1 
ATOM   1531 N N   . MET A 1 219 ? 91.734  24.208 15.761 1.00 27.06 ? 217 MET A N   1 
ATOM   1532 C CA  . MET A 1 219 ? 92.758  23.161 16.019 1.00 25.99 ? 217 MET A CA  1 
ATOM   1533 C C   . MET A 1 219 ? 94.077  23.738 16.534 1.00 24.90 ? 217 MET A C   1 
ATOM   1534 O O   . MET A 1 219 ? 94.611  23.218 17.541 1.00 24.76 ? 217 MET A O   1 
ATOM   1535 C CB  . MET A 1 219 ? 93.012  22.388 14.717 1.00 30.23 ? 217 MET A CB  1 
ATOM   1536 C CG  . MET A 1 219 ? 94.030  21.286 14.869 1.00 35.82 ? 217 MET A CG  1 
ATOM   1537 S SD  . MET A 1 219 ? 93.500  20.078 16.138 1.00 43.46 ? 217 MET A SD  1 
ATOM   1538 C CE  . MET A 1 219 ? 91.860  19.591 15.595 1.00 40.21 ? 217 MET A CE  1 
ATOM   1539 N N   . GLU A 1 220 ? 94.651  24.752 15.883 1.00 24.67 ? 218 GLU A N   1 
ATOM   1540 C CA  . GLU A 1 220 ? 96.003  25.214 16.273 1.00 26.74 ? 218 GLU A CA  1 
ATOM   1541 C C   . GLU A 1 220 ? 95.931  25.886 17.642 1.00 28.89 ? 218 GLU A C   1 
ATOM   1542 O O   . GLU A 1 220 ? 96.965  26.004 18.292 1.00 26.91 ? 218 GLU A O   1 
ATOM   1543 C CB  . GLU A 1 220 ? 96.585  26.134 15.204 1.00 30.23 ? 218 GLU A CB  1 
ATOM   1544 C CG  . GLU A 1 220 ? 96.747  25.463 13.843 1.00 31.00 ? 218 GLU A CG  1 
ATOM   1545 C CD  . GLU A 1 220 ? 95.579  25.422 12.882 1.00 36.14 ? 218 GLU A CD  1 
ATOM   1546 O OE1 . GLU A 1 220 ? 94.415  25.628 13.295 1.00 33.29 ? 218 GLU A OE1 1 
ATOM   1547 O OE2 . GLU A 1 220 ? 95.838  25.191 11.662 1.00 44.54 ? 218 GLU A OE2 1 
ATOM   1548 N N   . LEU A 1 221 ? 94.745  26.323 18.080 1.00 25.75 ? 219 LEU A N   1 
ATOM   1549 C CA  . LEU A 1 221 ? 94.640  26.964 19.422 1.00 25.39 ? 219 LEU A CA  1 
ATOM   1550 C C   . LEU A 1 221 ? 94.480  25.896 20.514 1.00 23.32 ? 219 LEU A C   1 
ATOM   1551 O O   . LEU A 1 221 ? 94.968  26.127 21.646 1.00 25.72 ? 219 LEU A O   1 
ATOM   1552 C CB  . LEU A 1 221 ? 93.501  28.005 19.378 1.00 25.33 ? 219 LEU A CB  1 
ATOM   1553 C CG  . LEU A 1 221 ? 93.328  28.871 20.620 1.00 25.41 ? 219 LEU A CG  1 
ATOM   1554 C CD1 . LEU A 1 221 ? 94.659  29.369 21.160 1.00 29.48 ? 219 LEU A CD1 1 
ATOM   1555 C CD2 . LEU A 1 221 ? 92.415  30.053 20.328 1.00 27.76 ? 219 LEU A CD2 1 
ATOM   1556 N N   . GLU A 1 222 ? 93.777  24.807 20.236 1.00 21.62 ? 220 GLU A N   1 
ATOM   1557 C CA  . GLU A 1 222 ? 93.390  23.798 21.264 1.00 21.33 ? 220 GLU A CA  1 
ATOM   1558 C C   . GLU A 1 222 ? 93.406  22.408 20.626 1.00 23.28 ? 220 GLU A C   1 
ATOM   1559 O O   . GLU A 1 222 ? 92.341  21.737 20.600 1.00 26.44 ? 220 GLU A O   1 
ATOM   1560 C CB  . GLU A 1 222 ? 91.999  24.090 21.828 1.00 22.74 ? 220 GLU A CB  1 
ATOM   1561 C CG  . GLU A 1 222 ? 91.866  25.405 22.590 1.00 23.72 ? 220 GLU A CG  1 
ATOM   1562 C CD  . GLU A 1 222 ? 90.556  25.484 23.373 1.00 23.87 ? 220 GLU A CD  1 
ATOM   1563 O OE1 . GLU A 1 222 ? 89.568  26.066 22.852 1.00 23.62 ? 220 GLU A OE1 1 
ATOM   1564 O OE2 . GLU A 1 222 ? 90.518  24.922 24.508 1.00 24.92 ? 220 GLU A OE2 1 
ATOM   1565 N N   . HIS A 1 223 ? 94.561  22.008 20.095 1.00 24.87 ? 221 HIS A N   1 
ATOM   1566 C CA  . HIS A 1 223 ? 94.735  20.735 19.347 1.00 30.72 ? 221 HIS A CA  1 
ATOM   1567 C C   . HIS A 1 223 ? 94.321  19.576 20.257 1.00 28.45 ? 221 HIS A C   1 
ATOM   1568 O O   . HIS A 1 223 ? 93.469  18.785 19.830 1.00 31.93 ? 221 HIS A O   1 
ATOM   1569 C CB  . HIS A 1 223 ? 96.168  20.598 18.760 1.00 33.84 ? 221 HIS A CB  1 
ATOM   1570 C CG  . HIS A 1 223 ? 97.331  20.435 19.708 1.00 43.21 ? 221 HIS A CG  1 
ATOM   1571 N ND1 . HIS A 1 223 ? 98.366  21.398 19.801 1.00 51.04 ? 221 HIS A ND1 1 
ATOM   1572 C CD2 . HIS A 1 223 ? 97.725  19.394 20.490 1.00 45.59 ? 221 HIS A CD2 1 
ATOM   1573 C CE1 . HIS A 1 223 ? 99.288  20.975 20.645 1.00 49.36 ? 221 HIS A CE1 1 
ATOM   1574 N NE2 . HIS A 1 223 ? 98.918  19.746 21.078 1.00 47.43 ? 221 HIS A NE2 1 
ATOM   1575 N N   . GLY A 1 224 ? 94.832  19.543 21.486 1.00 31.00 ? 222 GLY A N   1 
ATOM   1576 C CA  . GLY A 1 224 ? 94.552  18.438 22.430 1.00 32.52 ? 222 GLY A CA  1 
ATOM   1577 C C   . GLY A 1 224 ? 93.058  18.259 22.674 1.00 31.21 ? 222 GLY A C   1 
ATOM   1578 O O   . GLY A 1 224 ? 92.536  17.132 22.535 1.00 32.47 ? 222 GLY A O   1 
ATOM   1579 N N   . ALA A 1 225 ? 92.360  19.329 23.046 1.00 28.21 ? 223 ALA A N   1 
ATOM   1580 C CA  . ALA A 1 225 ? 90.944  19.262 23.448 1.00 29.50 ? 223 ALA A CA  1 
ATOM   1581 C C   . ALA A 1 225 ? 90.098  18.878 22.241 1.00 29.44 ? 223 ALA A C   1 
ATOM   1582 O O   . ALA A 1 225 ? 89.183  18.012 22.378 1.00 28.51 ? 223 ALA A O   1 
ATOM   1583 C CB  . ALA A 1 225 ? 90.476  20.558 24.059 1.00 27.82 ? 223 ALA A CB  1 
ATOM   1584 N N   . LEU A 1 226 ? 90.324  19.556 21.116 1.00 30.65 ? 224 LEU A N   1 
ATOM   1585 C CA  . LEU A 1 226 ? 89.482  19.338 19.923 1.00 29.37 ? 224 LEU A CA  1 
ATOM   1586 C C   . LEU A 1 226 ? 89.698  17.912 19.402 1.00 29.87 ? 224 LEU A C   1 
ATOM   1587 O O   . LEU A 1 226 ? 88.694  17.317 19.008 1.00 32.72 ? 224 LEU A O   1 
ATOM   1588 C CB  . LEU A 1 226 ? 89.775  20.392 18.856 1.00 28.95 ? 224 LEU A CB  1 
ATOM   1589 C CG  . LEU A 1 226 ? 89.093  21.738 19.129 1.00 25.49 ? 224 LEU A CG  1 
ATOM   1590 C CD1 . LEU A 1 226 ? 89.591  22.822 18.188 1.00 28.00 ? 224 LEU A CD1 1 
ATOM   1591 C CD2 . LEU A 1 226 ? 87.591  21.608 19.034 1.00 25.32 ? 224 LEU A CD2 1 
ATOM   1592 N N   . LYS A 1 227 ? 90.940  17.440 19.355 1.00 32.45 ? 225 LYS A N   1 
ATOM   1593 C CA  . LYS A 1 227 ? 91.263  16.055 18.885 1.00 35.47 ? 225 LYS A CA  1 
ATOM   1594 C C   . LYS A 1 227 ? 90.462  15.071 19.739 1.00 34.95 ? 225 LYS A C   1 
ATOM   1595 O O   . LYS A 1 227 ? 89.822  14.169 19.176 1.00 38.85 ? 225 LYS A O   1 
ATOM   1596 C CB  . LYS A 1 227 ? 92.752  15.727 18.990 1.00 38.32 ? 225 LYS A CB  1 
ATOM   1597 C CG  . LYS A 1 227 ? 93.666  16.367 17.958 1.00 48.07 ? 225 LYS A CG  1 
ATOM   1598 C CD  . LYS A 1 227 ? 95.075  16.568 18.516 1.00 57.61 ? 225 LYS A CD  1 
ATOM   1599 C CE  . LYS A 1 227 ? 96.091  17.001 17.497 1.00 58.43 ? 225 LYS A CE  1 
ATOM   1600 N NZ  . LYS A 1 227 ? 96.357  15.902 16.540 1.00 66.83 ? 225 LYS A NZ  1 
ATOM   1601 N N   . TYR A 1 228 ? 90.474  15.255 21.056 1.00 36.81 ? 226 TYR A N   1 
ATOM   1602 C CA  . TYR A 1 228 ? 89.687  14.428 21.990 1.00 36.49 ? 226 TYR A CA  1 
ATOM   1603 C C   . TYR A 1 228 ? 88.195  14.512 21.644 1.00 39.86 ? 226 TYR A C   1 
ATOM   1604 O O   . TYR A 1 228 ? 87.597  13.465 21.382 1.00 36.05 ? 226 TYR A O   1 
ATOM   1605 C CB  . TYR A 1 228 ? 89.959  14.805 23.437 1.00 39.94 ? 226 TYR A CB  1 
ATOM   1606 C CG  . TYR A 1 228 ? 89.018  14.073 24.337 1.00 45.41 ? 226 TYR A CG  1 
ATOM   1607 C CD1 . TYR A 1 228 ? 89.186  12.716 24.576 1.00 48.24 ? 226 TYR A CD1 1 
ATOM   1608 C CD2 . TYR A 1 228 ? 87.894  14.699 24.851 1.00 46.38 ? 226 TYR A CD2 1 
ATOM   1609 C CE1 . TYR A 1 228 ? 88.295  12.017 25.372 1.00 46.53 ? 226 TYR A CE1 1 
ATOM   1610 C CE2 . TYR A 1 228 ? 86.998  14.010 25.653 1.00 49.64 ? 226 TYR A CE2 1 
ATOM   1611 C CZ  . TYR A 1 228 ? 87.187  12.662 25.903 1.00 50.91 ? 226 TYR A CZ  1 
ATOM   1612 O OH  . TYR A 1 228 ? 86.300  11.987 26.700 1.00 52.20 ? 226 TYR A OH  1 
ATOM   1613 N N   . LEU A 1 229 ? 87.617  15.720 21.587 1.00 33.66 ? 227 LEU A N   1 
ATOM   1614 C CA  . LEU A 1 229 ? 86.156  15.938 21.395 1.00 32.78 ? 227 LEU A CA  1 
ATOM   1615 C C   . LEU A 1 229 ? 85.707  15.449 20.012 1.00 29.73 ? 227 LEU A C   1 
ATOM   1616 O O   . LEU A 1 229 ? 84.515  15.088 19.861 1.00 32.64 ? 227 LEU A O   1 
ATOM   1617 C CB  . LEU A 1 229 ? 85.859  17.432 21.512 1.00 29.21 ? 227 LEU A CB  1 
ATOM   1618 C CG  . LEU A 1 229 ? 85.972  18.033 22.900 1.00 29.40 ? 227 LEU A CG  1 
ATOM   1619 C CD1 . LEU A 1 229 ? 85.957  19.559 22.824 1.00 29.25 ? 227 LEU A CD1 1 
ATOM   1620 C CD2 . LEU A 1 229 ? 84.827  17.519 23.754 1.00 31.24 ? 227 LEU A CD2 1 
ATOM   1621 N N   . GLN A 1 230 ? 86.612  15.468 19.043 1.00 31.72 ? 228 GLN A N   1 
ATOM   1622 C CA  . GLN A 1 230 ? 86.255  15.108 17.650 1.00 37.09 ? 228 GLN A CA  1 
ATOM   1623 C C   . GLN A 1 230 ? 86.551  13.634 17.384 1.00 43.19 ? 228 GLN A C   1 
ATOM   1624 O O   . GLN A 1 230 ? 86.284  13.198 16.269 1.00 46.33 ? 228 GLN A O   1 
ATOM   1625 C CB  . GLN A 1 230 ? 86.945  16.033 16.667 1.00 32.79 ? 228 GLN A CB  1 
ATOM   1626 C CG  . GLN A 1 230 ? 86.303  17.413 16.699 1.00 34.50 ? 228 GLN A CG  1 
ATOM   1627 C CD  . GLN A 1 230 ? 86.900  18.336 15.671 1.00 36.17 ? 228 GLN A CD  1 
ATOM   1628 O OE1 . GLN A 1 230 ? 88.085  18.251 15.400 1.00 40.07 ? 228 GLN A OE1 1 
ATOM   1629 N NE2 . GLN A 1 230 ? 86.083  19.218 15.096 1.00 36.61 ? 228 GLN A NE2 1 
ATOM   1630 N N   . THR A 1 231 ? 87.049  12.892 18.366 1.00 43.86 ? 229 THR A N   1 
ATOM   1631 C CA  . THR A 1 231 ? 87.233  11.429 18.224 1.00 44.04 ? 229 THR A CA  1 
ATOM   1632 C C   . THR A 1 231 ? 85.852  10.814 18.039 1.00 47.06 ? 229 THR A C   1 
ATOM   1633 O O   . THR A 1 231 ? 85.011  10.997 18.926 1.00 45.09 ? 229 THR A O   1 
ATOM   1634 C CB  . THR A 1 231 ? 87.986  10.829 19.410 1.00 47.17 ? 229 THR A CB  1 
ATOM   1635 O OG1 . THR A 1 231 ? 89.281  11.422 19.314 1.00 43.72 ? 229 THR A OG1 1 
ATOM   1636 C CG2 . THR A 1 231 ? 88.064  9.314  19.358 1.00 47.60 ? 229 THR A CG2 1 
ATOM   1637 N N   . VAL A 1 232 ? 85.608  10.177 16.891 1.00 46.88 ? 230 VAL A N   1 
ATOM   1638 C CA  . VAL A 1 232 ? 84.284  9.562  16.598 1.00 50.13 ? 230 VAL A CA  1 
ATOM   1639 C C   . VAL A 1 232 ? 84.066  8.490  17.665 1.00 47.65 ? 230 VAL A C   1 
ATOM   1640 O O   . VAL A 1 232 ? 84.979  7.707  17.957 1.00 49.80 ? 230 VAL A O   1 
ATOM   1641 C CB  . VAL A 1 232 ? 84.146  9.025  15.158 1.00 55.80 ? 230 VAL A CB  1 
ATOM   1642 C CG1 . VAL A 1 232 ? 82.886  8.174  15.001 1.00 57.98 ? 230 VAL A CG1 1 
ATOM   1643 C CG2 . VAL A 1 232 ? 84.126  10.166 14.146 1.00 54.85 ? 230 VAL A CG2 1 
ATOM   1644 N N   . GLN A 1 233 ? 82.932  8.564  18.335 1.00 43.15 ? 231 GLN A N   1 
ATOM   1645 C CA  . GLN A 1 233 ? 82.545  7.596  19.385 1.00 44.50 ? 231 GLN A CA  1 
ATOM   1646 C C   . GLN A 1 233 ? 81.042  7.421  19.215 1.00 41.98 ? 231 GLN A C   1 
ATOM   1647 O O   . GLN A 1 233 ? 80.330  8.435  19.058 1.00 35.83 ? 231 GLN A O   1 
ATOM   1648 C CB  . GLN A 1 233 ? 82.979  8.094  20.767 1.00 47.51 ? 231 GLN A CB  1 
ATOM   1649 C CG  . GLN A 1 233 ? 82.660  7.126  21.895 1.00 54.92 ? 231 GLN A CG  1 
ATOM   1650 C CD  . GLN A 1 233 ? 83.051  7.692  23.237 1.00 61.86 ? 231 GLN A CD  1 
ATOM   1651 O OE1 . GLN A 1 233 ? 83.951  8.529  23.346 1.00 67.12 ? 231 GLN A OE1 1 
ATOM   1652 N NE2 . GLN A 1 233 ? 82.362  7.240  24.274 1.00 63.27 ? 231 GLN A NE2 1 
ATOM   1653 N N   . SER A 1 234 ? 80.604  6.170  19.159 1.00 38.54 ? 232 SER A N   1 
ATOM   1654 C CA  . SER A 1 234 ? 79.186  5.789  19.016 1.00 34.52 ? 232 SER A CA  1 
ATOM   1655 C C   . SER A 1 234 ? 78.371  6.473  20.112 1.00 31.01 ? 232 SER A C   1 
ATOM   1656 O O   . SER A 1 234 ? 78.826  6.425  21.258 1.00 30.46 ? 232 SER A O   1 
ATOM   1657 C CB  . SER A 1 234 ? 79.055  4.296  19.060 1.00 36.07 ? 232 SER A CB  1 
ATOM   1658 O OG  . SER A 1 234 ? 77.942  3.924  18.287 1.00 41.69 ? 232 SER A OG  1 
ATOM   1659 N N   . GLY A 1 235 ? 77.264  7.139  19.735 1.00 30.18 ? 233 GLY A N   1 
ATOM   1660 C CA  . GLY A 1 235 ? 76.317  7.776  20.674 1.00 30.65 ? 233 GLY A CA  1 
ATOM   1661 C C   . GLY A 1 235 ? 76.809  9.106  21.232 1.00 33.72 ? 233 GLY A C   1 
ATOM   1662 O O   . GLY A 1 235 ? 76.168  9.573  22.148 1.00 32.83 ? 233 GLY A O   1 
ATOM   1663 N N   . LYS A 1 236 ? 77.961  9.652  20.784 1.00 34.78 ? 234 LYS A N   1 
ATOM   1664 C CA  . LYS A 1 236 ? 78.452  10.996 21.212 1.00 34.26 ? 234 LYS A CA  1 
ATOM   1665 C C   . LYS A 1 236 ? 78.252  11.913 20.012 1.00 32.44 ? 234 LYS A C   1 
ATOM   1666 O O   . LYS A 1 236 ? 78.548  11.501 18.897 1.00 32.45 ? 234 LYS A O   1 
ATOM   1667 C CB  . LYS A 1 236 ? 79.929  10.995 21.627 1.00 38.60 ? 234 LYS A CB  1 
ATOM   1668 C CG  . LYS A 1 236 ? 80.298  10.116 22.819 1.00 46.06 ? 234 LYS A CG  1 
ATOM   1669 C CD  . LYS A 1 236 ? 79.502  10.391 24.076 1.00 50.85 ? 234 LYS A CD  1 
ATOM   1670 C CE  . LYS A 1 236 ? 79.684  9.311  25.127 1.00 56.41 ? 234 LYS A CE  1 
ATOM   1671 N NZ  . LYS A 1 236 ? 78.814  9.543  26.309 1.00 58.26 ? 234 LYS A NZ  1 
ATOM   1672 N N   . PRO A 1 237 ? 77.769  13.167 20.176 1.00 30.31 ? 235 PRO A N   1 
ATOM   1673 C CA  . PRO A 1 237 ? 77.457  14.011 19.011 1.00 30.47 ? 235 PRO A CA  1 
ATOM   1674 C C   . PRO A 1 237 ? 78.732  14.473 18.323 1.00 25.77 ? 235 PRO A C   1 
ATOM   1675 O O   . PRO A 1 237 ? 79.740  14.656 18.989 1.00 26.06 ? 235 PRO A O   1 
ATOM   1676 C CB  . PRO A 1 237 ? 76.753  15.235 19.599 1.00 32.51 ? 235 PRO A CB  1 
ATOM   1677 C CG  . PRO A 1 237 ? 77.137  15.257 21.068 1.00 33.94 ? 235 PRO A CG  1 
ATOM   1678 C CD  . PRO A 1 237 ? 77.569  13.853 21.452 1.00 35.00 ? 235 PRO A CD  1 
ATOM   1679 N N   . PRO A 1 238 ? 78.728  14.717 16.998 1.00 26.35 ? 236 PRO A N   1 
ATOM   1680 C CA  . PRO A 1 238 ? 79.877  15.322 16.353 1.00 26.42 ? 236 PRO A CA  1 
ATOM   1681 C C   . PRO A 1 238 ? 80.093  16.766 16.855 1.00 25.54 ? 236 PRO A C   1 
ATOM   1682 O O   . PRO A 1 238 ? 79.150  17.427 17.230 1.00 22.33 ? 236 PRO A O   1 
ATOM   1683 C CB  . PRO A 1 238 ? 79.482  15.263 14.877 1.00 26.87 ? 236 PRO A CB  1 
ATOM   1684 C CG  . PRO A 1 238 ? 78.002  15.302 14.897 1.00 27.55 ? 236 PRO A CG  1 
ATOM   1685 C CD  . PRO A 1 238 ? 77.648  14.401 16.045 1.00 27.32 ? 236 PRO A CD  1 
ATOM   1686 N N   . VAL A 1 239 ? 81.355  17.184 16.894 1.00 26.82 ? 237 VAL A N   1 
ATOM   1687 C CA  . VAL A 1 239 ? 81.760  18.543 17.354 1.00 24.91 ? 237 VAL A CA  1 
ATOM   1688 C C   . VAL A 1 239 ? 82.330  19.278 16.149 1.00 24.19 ? 237 VAL A C   1 
ATOM   1689 O O   . VAL A 1 239 ? 83.226  18.750 15.494 1.00 26.12 ? 237 VAL A O   1 
ATOM   1690 C CB  . VAL A 1 239 ? 82.776  18.437 18.483 1.00 25.72 ? 237 VAL A CB  1 
ATOM   1691 C CG1 . VAL A 1 239 ? 83.293  19.821 18.848 1.00 25.91 ? 237 VAL A CG1 1 
ATOM   1692 C CG2 . VAL A 1 239 ? 82.156  17.698 19.683 1.00 28.41 ? 237 VAL A CG2 1 
ATOM   1693 N N   . TYR A 1 240 ? 81.784  20.441 15.866 1.00 22.52 ? 238 TYR A N   1 
ATOM   1694 C CA  . TYR A 1 240 ? 82.174  21.305 14.739 1.00 23.23 ? 238 TYR A CA  1 
ATOM   1695 C C   . TYR A 1 240 ? 82.970  22.484 15.293 1.00 23.85 ? 238 TYR A C   1 
ATOM   1696 O O   . TYR A 1 240 ? 82.358  23.294 16.028 1.00 23.54 ? 238 TYR A O   1 
ATOM   1697 C CB  . TYR A 1 240 ? 80.918  21.753 14.015 1.00 22.71 ? 238 TYR A CB  1 
ATOM   1698 C CG  . TYR A 1 240 ? 80.075  20.630 13.487 1.00 23.27 ? 238 TYR A CG  1 
ATOM   1699 C CD1 . TYR A 1 240 ? 79.134  20.009 14.284 1.00 26.30 ? 238 TYR A CD1 1 
ATOM   1700 C CD2 . TYR A 1 240 ? 80.204  20.202 12.179 1.00 24.88 ? 238 TYR A CD2 1 
ATOM   1701 C CE1 . TYR A 1 240 ? 78.324  18.993 13.801 1.00 27.67 ? 238 TYR A CE1 1 
ATOM   1702 C CE2 . TYR A 1 240 ? 79.406  19.179 11.677 1.00 26.77 ? 238 TYR A CE2 1 
ATOM   1703 C CZ  . TYR A 1 240 ? 78.463  18.568 12.485 1.00 27.96 ? 238 TYR A CZ  1 
ATOM   1704 O OH  . TYR A 1 240 ? 77.659  17.561 12.031 1.00 27.75 ? 238 TYR A OH  1 
ATOM   1705 N N   . ALA A 1 241 ? 84.259  22.547 14.952 1.00 22.69 ? 239 ALA A N   1 
ATOM   1706 C CA  . ALA A 1 241 ? 85.193  23.644 15.299 1.00 22.74 ? 239 ALA A CA  1 
ATOM   1707 C C   . ALA A 1 241 ? 84.972  24.790 14.310 1.00 23.06 ? 239 ALA A C   1 
ATOM   1708 O O   . ALA A 1 241 ? 85.378  24.703 13.136 1.00 23.26 ? 239 ALA A O   1 
ATOM   1709 C CB  . ALA A 1 241 ? 86.631  23.183 15.312 1.00 22.88 ? 239 ALA A CB  1 
ATOM   1710 N N   . VAL A 1 242 ? 84.258  25.818 14.745 1.00 21.08 ? 240 VAL A N   1 
ATOM   1711 C CA  . VAL A 1 242 ? 83.835  26.912 13.822 1.00 20.48 ? 240 VAL A CA  1 
ATOM   1712 C C   . VAL A 1 242 ? 84.594  28.205 14.144 1.00 21.42 ? 240 VAL A C   1 
ATOM   1713 O O   . VAL A 1 242 ? 84.331  29.188 13.457 1.00 20.65 ? 240 VAL A O   1 
ATOM   1714 C CB  . VAL A 1 242 ? 82.316  27.161 13.822 1.00 20.76 ? 240 VAL A CB  1 
ATOM   1715 C CG1 . VAL A 1 242 ? 81.491  25.982 13.303 1.00 21.46 ? 240 VAL A CG1 1 
ATOM   1716 C CG2 . VAL A 1 242 ? 81.844  27.605 15.193 1.00 19.71 ? 240 VAL A CG2 1 
ATOM   1717 N N   . GLY A 1 243 ? 85.446  28.208 15.165 1.00 20.26 ? 241 GLY A N   1 
ATOM   1718 C CA  . GLY A 1 243 ? 86.170  29.400 15.631 1.00 23.11 ? 241 GLY A CA  1 
ATOM   1719 C C   . GLY A 1 243 ? 87.322  29.762 14.705 1.00 24.09 ? 241 GLY A C   1 
ATOM   1720 O O   . GLY A 1 243 ? 87.695  28.976 13.837 1.00 24.99 ? 241 GLY A O   1 
ATOM   1721 N N   . PRO A 1 244 ? 87.891  30.972 14.840 1.00 26.43 ? 242 PRO A N   1 
ATOM   1722 C CA  . PRO A 1 244 ? 87.411  31.962 15.801 1.00 26.57 ? 242 PRO A CA  1 
ATOM   1723 C C   . PRO A 1 244 ? 86.215  32.806 15.311 1.00 28.84 ? 242 PRO A C   1 
ATOM   1724 O O   . PRO A 1 244 ? 86.259  33.290 14.213 1.00 35.62 ? 242 PRO A O   1 
ATOM   1725 C CB  . PRO A 1 244 ? 88.674  32.806 15.993 1.00 28.89 ? 242 PRO A CB  1 
ATOM   1726 C CG  . PRO A 1 244 ? 89.363  32.786 14.679 1.00 29.84 ? 242 PRO A CG  1 
ATOM   1727 C CD  . PRO A 1 244 ? 89.114  31.399 14.143 1.00 28.37 ? 242 PRO A CD  1 
ATOM   1728 N N   . LEU A 1 245 ? 85.168  32.927 16.125 1.00 27.01 ? 243 LEU A N   1 
ATOM   1729 C CA  . LEU A 1 245 ? 83.934  33.705 15.810 1.00 31.97 ? 243 LEU A CA  1 
ATOM   1730 C C   . LEU A 1 245 ? 84.037  35.126 16.402 1.00 35.14 ? 243 LEU A C   1 
ATOM   1731 O O   . LEU A 1 245 ? 83.535  35.340 17.520 1.00 47.06 ? 243 LEU A O   1 
ATOM   1732 C CB  . LEU A 1 245 ? 82.731  32.996 16.438 1.00 30.58 ? 243 LEU A CB  1 
ATOM   1733 C CG  . LEU A 1 245 ? 82.381  31.630 15.856 1.00 29.79 ? 243 LEU A CG  1 
ATOM   1734 C CD1 . LEU A 1 245 ? 81.284  30.994 16.686 1.00 34.32 ? 243 LEU A CD1 1 
ATOM   1735 C CD2 . LEU A 1 245 ? 81.951  31.747 14.404 1.00 32.33 ? 243 LEU A CD2 1 
ATOM   1736 N N   . ILE A 1 246 ? 84.576  36.086 15.673 1.00 37.30 ? 244 ILE A N   1 
ATOM   1737 C CA  . ILE A 1 246 ? 84.751  37.481 16.201 1.00 41.53 ? 244 ILE A CA  1 
ATOM   1738 C C   . ILE A 1 246 ? 84.239  38.541 15.202 1.00 41.12 ? 244 ILE A C   1 
ATOM   1739 O O   . ILE A 1 246 ? 84.249  38.257 14.004 1.00 42.44 ? 244 ILE A O   1 
ATOM   1740 C CB  . ILE A 1 246 ? 86.239  37.688 16.531 1.00 44.36 ? 244 ILE A CB  1 
ATOM   1741 C CG1 . ILE A 1 246 ? 87.098  37.829 15.273 1.00 43.45 ? 244 ILE A CG1 1 
ATOM   1742 C CG2 . ILE A 1 246 ? 86.787  36.624 17.451 1.00 46.23 ? 244 ILE A CG2 1 
ATOM   1743 C CD1 . ILE A 1 246 ? 87.443  39.269 14.987 1.00 45.28 ? 244 ILE A CD1 1 
ATOM   1744 N N   . LYS A 1 247 ? 83.897  39.750 15.680 1.00 51.08 ? 245 LYS A N   1 
ATOM   1745 C CA  . LYS A 1 247 ? 83.640  40.976 14.851 1.00 54.69 ? 245 LYS A CA  1 
ATOM   1746 C C   . LYS A 1 247 ? 84.852  41.345 13.974 1.00 57.10 ? 245 LYS A C   1 
ATOM   1747 O O   . LYS A 1 247 ? 85.048  40.694 12.920 1.00 57.27 ? 245 LYS A O   1 
ATOM   1748 C CB  . LYS A 1 247 ? 83.347  42.178 15.752 1.00 55.05 ? 245 LYS A CB  1 
ATOM   1749 N N   . SER A 1 255 ? 82.104  57.264 16.947 1.00 42.64 ? 253 SER A N   1 
ATOM   1750 C CA  . SER A 1 255 ? 82.031  57.474 18.420 1.00 44.95 ? 253 SER A CA  1 
ATOM   1751 C C   . SER A 1 255 ? 83.427  57.330 19.056 1.00 42.89 ? 253 SER A C   1 
ATOM   1752 O O   . SER A 1 255 ? 83.687  58.057 20.036 1.00 44.53 ? 253 SER A O   1 
ATOM   1753 C CB  . SER A 1 255 ? 81.042  56.544 19.095 1.00 46.20 ? 253 SER A CB  1 
ATOM   1754 O OG  . SER A 1 255 ? 81.058  56.781 20.495 1.00 49.40 ? 253 SER A OG  1 
ATOM   1755 N N   . GLY A 1 256 ? 84.279  56.419 18.552 1.00 36.40 ? 254 GLY A N   1 
ATOM   1756 C CA  . GLY A 1 256 ? 85.648  56.219 19.092 1.00 35.91 ? 254 GLY A CA  1 
ATOM   1757 C C   . GLY A 1 256 ? 86.718  56.955 18.282 1.00 38.10 ? 254 GLY A C   1 
ATOM   1758 O O   . GLY A 1 256 ? 87.891  56.617 18.465 1.00 32.69 ? 254 GLY A O   1 
ATOM   1759 N N   . SER A 1 257 ? 86.342  57.937 17.442 1.00 35.83 ? 255 SER A N   1 
ATOM   1760 C CA  . SER A 1 257 ? 87.239  58.577 16.438 1.00 38.90 ? 255 SER A CA  1 
ATOM   1761 C C   . SER A 1 257 ? 88.432  59.158 17.171 1.00 32.53 ? 255 SER A C   1 
ATOM   1762 O O   . SER A 1 257 ? 89.523  59.024 16.646 1.00 36.47 ? 255 SER A O   1 
ATOM   1763 C CB  . SER A 1 257 ? 86.612  59.707 15.612 1.00 41.58 ? 255 SER A CB  1 
ATOM   1764 O OG  . SER A 1 257 ? 85.347  59.350 15.119 1.00 43.47 ? 255 SER A OG  1 
ATOM   1765 N N   . LYS A 1 258 ? 88.188  59.870 18.266 1.00 33.04 ? 256 LYS A N   1 
ATOM   1766 C CA  . LYS A 1 258 ? 89.247  60.556 19.042 1.00 38.02 ? 256 LYS A CA  1 
ATOM   1767 C C   . LYS A 1 258 ? 90.210  59.519 19.608 1.00 34.18 ? 256 LYS A C   1 
ATOM   1768 O O   . LYS A 1 258 ? 91.410  59.829 19.711 1.00 28.25 ? 256 LYS A O   1 
ATOM   1769 C CB  . LYS A 1 258 ? 88.685  61.464 20.141 1.00 41.04 ? 256 LYS A CB  1 
ATOM   1770 C CG  . LYS A 1 258 ? 88.338  62.867 19.652 1.00 52.47 ? 256 LYS A CG  1 
ATOM   1771 C CD  . LYS A 1 258 ? 88.369  63.949 20.723 1.00 61.55 ? 256 LYS A CD  1 
ATOM   1772 C CE  . LYS A 1 258 ? 89.605  63.931 21.611 1.00 64.59 ? 256 LYS A CE  1 
ATOM   1773 N NZ  . LYS A 1 258 ? 89.586  65.036 22.603 1.00 65.63 ? 256 LYS A NZ  1 
ATOM   1774 N N   . ILE A 1 259 ? 89.733  58.327 19.967 1.00 30.08 ? 257 ILE A N   1 
ATOM   1775 C CA  . ILE A 1 259 ? 90.661  57.303 20.504 1.00 27.78 ? 257 ILE A CA  1 
ATOM   1776 C C   . ILE A 1 259 ? 91.547  56.859 19.343 1.00 27.35 ? 257 ILE A C   1 
ATOM   1777 O O   . ILE A 1 259 ? 92.760  56.711 19.539 1.00 29.60 ? 257 ILE A O   1 
ATOM   1778 C CB  . ILE A 1 259 ? 89.884  56.163 21.204 1.00 27.47 ? 257 ILE A CB  1 
ATOM   1779 C CG1 . ILE A 1 259 ? 89.140  56.719 22.422 1.00 28.80 ? 257 ILE A CG1 1 
ATOM   1780 C CG2 . ILE A 1 259 ? 90.822  55.032 21.553 1.00 25.91 ? 257 ILE A CG2 1 
ATOM   1781 C CD1 . ILE A 1 259 ? 88.057  55.782 23.004 1.00 31.26 ? 257 ILE A CD1 1 
ATOM   1782 N N   . ILE A 1 260 ? 90.971  56.656 18.163 1.00 28.61 ? 258 ILE A N   1 
ATOM   1783 C CA  . ILE A 1 260 ? 91.718  56.170 16.967 1.00 28.88 ? 258 ILE A CA  1 
ATOM   1784 C C   . ILE A 1 260 ? 92.717  57.247 16.534 1.00 32.69 ? 258 ILE A C   1 
ATOM   1785 O O   . ILE A 1 260 ? 93.863  56.878 16.157 1.00 28.69 ? 258 ILE A O   1 
ATOM   1786 C CB  . ILE A 1 260 ? 90.763  55.765 15.830 1.00 30.12 ? 258 ILE A CB  1 
ATOM   1787 C CG1 . ILE A 1 260 ? 89.804  54.656 16.283 1.00 31.68 ? 258 ILE A CG1 1 
ATOM   1788 C CG2 . ILE A 1 260 ? 91.546  55.371 14.585 1.00 32.82 ? 258 ILE A CG2 1 
ATOM   1789 C CD1 . ILE A 1 260 ? 90.489  53.363 16.681 1.00 32.45 ? 258 ILE A CD1 1 
ATOM   1790 N N   . GLU A 1 261 ? 92.306  58.520 16.568 1.00 31.87 ? 259 GLU A N   1 
ATOM   1791 C CA  . GLU A 1 261 ? 93.193  59.663 16.218 1.00 34.65 ? 259 GLU A CA  1 
ATOM   1792 C C   . GLU A 1 261 ? 94.401  59.673 17.150 1.00 29.95 ? 259 GLU A C   1 
ATOM   1793 O O   . GLU A 1 261 ? 95.487  59.924 16.689 1.00 27.45 ? 259 GLU A O   1 
ATOM   1794 C CB  . GLU A 1 261 ? 92.471  61.007 16.323 1.00 38.52 ? 259 GLU A CB  1 
ATOM   1795 C CG  . GLU A 1 261 ? 91.764  61.375 15.041 1.00 45.63 ? 259 GLU A CG  1 
ATOM   1796 C CD  . GLU A 1 261 ? 90.719  62.467 15.198 1.00 48.00 ? 259 GLU A CD  1 
ATOM   1797 O OE1 . GLU A 1 261 ? 90.871  63.329 16.116 1.00 45.10 ? 259 GLU A OE1 1 
ATOM   1798 O OE2 . GLU A 1 261 ? 89.745  62.429 14.424 1.00 55.62 ? 259 GLU A OE2 1 
ATOM   1799 N N   . TRP A 1 262 ? 94.211  59.393 18.432 1.00 28.86 ? 260 TRP A N   1 
ATOM   1800 C CA  . TRP A 1 262 ? 95.337  59.268 19.397 1.00 28.31 ? 260 TRP A CA  1 
ATOM   1801 C C   . TRP A 1 262 ? 96.283  58.162 18.936 1.00 25.81 ? 260 TRP A C   1 
ATOM   1802 O O   . TRP A 1 262 ? 97.499  58.383 18.848 1.00 24.19 ? 260 TRP A O   1 
ATOM   1803 C CB  . TRP A 1 262 ? 94.819  59.002 20.820 1.00 27.39 ? 260 TRP A CB  1 
ATOM   1804 C CG  . TRP A 1 262 ? 95.941  58.987 21.815 1.00 26.41 ? 260 TRP A CG  1 
ATOM   1805 C CD1 . TRP A 1 262 ? 96.525  60.075 22.388 1.00 28.15 ? 260 TRP A CD1 1 
ATOM   1806 C CD2 . TRP A 1 262 ? 96.694  57.844 22.255 1.00 24.04 ? 260 TRP A CD2 1 
ATOM   1807 N NE1 . TRP A 1 262 ? 97.541  59.680 23.201 1.00 25.22 ? 260 TRP A NE1 1 
ATOM   1808 C CE2 . TRP A 1 262 ? 97.681  58.323 23.129 1.00 25.70 ? 260 TRP A CE2 1 
ATOM   1809 C CE3 . TRP A 1 262 ? 96.608  56.465 22.020 1.00 25.60 ? 260 TRP A CE3 1 
ATOM   1810 C CZ2 . TRP A 1 262 ? 98.567  57.475 23.782 1.00 25.59 ? 260 TRP A CZ2 1 
ATOM   1811 C CZ3 . TRP A 1 262 ? 97.474  55.623 22.676 1.00 24.19 ? 260 TRP A CZ3 1 
ATOM   1812 C CH2 . TRP A 1 262 ? 98.441  56.128 23.548 1.00 26.55 ? 260 TRP A CH2 1 
ATOM   1813 N N   . LEU A 1 263 ? 95.721  56.983 18.656 1.00 25.20 ? 261 LEU A N   1 
ATOM   1814 C CA  . LEU A 1 263 ? 96.480  55.783 18.280 1.00 27.29 ? 261 LEU A CA  1 
ATOM   1815 C C   . LEU A 1 263 ? 97.262  56.068 16.988 1.00 29.01 ? 261 LEU A C   1 
ATOM   1816 O O   . LEU A 1 263 ? 98.459  55.701 16.936 1.00 25.08 ? 261 LEU A O   1 
ATOM   1817 C CB  . LEU A 1 263 ? 95.451  54.666 18.145 1.00 27.32 ? 261 LEU A CB  1 
ATOM   1818 C CG  . LEU A 1 263 ? 95.904  53.245 18.359 1.00 32.54 ? 261 LEU A CG  1 
ATOM   1819 C CD1 . LEU A 1 263 ? 96.774  53.078 19.593 1.00 31.89 ? 261 LEU A CD1 1 
ATOM   1820 C CD2 . LEU A 1 263 ? 94.672  52.361 18.425 1.00 32.90 ? 261 LEU A CD2 1 
ATOM   1821 N N   . ASP A 1 264 ? 96.632  56.738 16.024 1.00 29.41 ? 262 ASP A N   1 
ATOM   1822 C CA  . ASP A 1 264 ? 97.269  57.183 14.747 1.00 31.08 ? 262 ASP A CA  1 
ATOM   1823 C C   . ASP A 1 264 ? 98.564  57.957 15.003 1.00 31.32 ? 262 ASP A C   1 
ATOM   1824 O O   . ASP A 1 264 ? 99.455  57.925 14.129 1.00 30.20 ? 262 ASP A O   1 
ATOM   1825 C CB  . ASP A 1 264 ? 96.366  58.135 13.970 1.00 32.16 ? 262 ASP A CB  1 
ATOM   1826 C CG  . ASP A 1 264 ? 95.218  57.450 13.265 1.00 36.80 ? 262 ASP A CG  1 
ATOM   1827 O OD1 . ASP A 1 264 ? 95.287  56.215 13.083 1.00 35.10 ? 262 ASP A OD1 1 
ATOM   1828 O OD2 . ASP A 1 264 ? 94.292  58.169 12.890 1.00 32.11 ? 262 ASP A OD2 1 
ATOM   1829 N N   . ASP A 1 265 ? 98.662  58.673 16.128 1.00 31.11 ? 263 ASP A N   1 
ATOM   1830 C CA  . ASP A 1 265 ? 99.810  59.567 16.423 1.00 34.45 ? 263 ASP A CA  1 
ATOM   1831 C C   . ASP A 1 265 ? 100.904 58.812 17.190 1.00 32.30 ? 263 ASP A C   1 
ATOM   1832 O O   . ASP A 1 265 ? 101.836 59.470 17.631 1.00 31.71 ? 263 ASP A O   1 
ATOM   1833 C CB  . ASP A 1 265 ? 99.378  60.794 17.237 1.00 39.27 ? 263 ASP A CB  1 
ATOM   1834 C CG  . ASP A 1 265 ? 98.688  61.884 16.445 1.00 49.14 ? 263 ASP A CG  1 
ATOM   1835 O OD1 . ASP A 1 265 ? 98.755  61.843 15.208 1.00 54.63 ? 263 ASP A OD1 1 
ATOM   1836 O OD2 . ASP A 1 265 ? 98.079  62.761 17.085 1.00 58.23 ? 263 ASP A OD2 1 
ATOM   1837 N N   . GLN A 1 266 ? 100.787 57.502 17.403 1.00 25.88 ? 264 GLN A N   1 
ATOM   1838 C CA  . GLN A 1 266 ? 101.825 56.734 18.132 1.00 26.90 ? 264 GLN A CA  1 
ATOM   1839 C C   . GLN A 1 266 ? 102.581 55.863 17.144 1.00 25.13 ? 264 GLN A C   1 
ATOM   1840 O O   . GLN A 1 266 ? 102.009 55.460 16.137 1.00 26.64 ? 264 GLN A O   1 
ATOM   1841 C CB  . GLN A 1 266 ? 101.163 55.907 19.240 1.00 26.95 ? 264 GLN A CB  1 
ATOM   1842 C CG  . GLN A 1 266 ? 100.094 56.683 19.980 1.00 25.89 ? 264 GLN A CG  1 
ATOM   1843 C CD  . GLN A 1 266 ? 100.605 57.967 20.586 1.00 28.81 ? 264 GLN A CD  1 
ATOM   1844 O OE1 . GLN A 1 266 ? 101.725 58.043 21.082 1.00 28.30 ? 264 GLN A OE1 1 
ATOM   1845 N NE2 . GLN A 1 266 ? 99.754  58.967 20.586 1.00 24.14 ? 264 GLN A NE2 1 
ATOM   1846 N N   . PRO A 1 267 ? 103.874 55.559 17.390 1.00 27.65 ? 265 PRO A N   1 
ATOM   1847 C CA  . PRO A 1 267 ? 104.661 54.723 16.485 1.00 27.21 ? 265 PRO A CA  1 
ATOM   1848 C C   . PRO A 1 267 ? 104.120 53.300 16.434 1.00 29.06 ? 265 PRO A C   1 
ATOM   1849 O O   . PRO A 1 267 ? 103.467 52.801 17.422 1.00 25.04 ? 265 PRO A O   1 
ATOM   1850 C CB  . PRO A 1 267 ? 106.076 54.681 17.085 1.00 27.65 ? 265 PRO A CB  1 
ATOM   1851 C CG  . PRO A 1 267 ? 106.075 55.766 18.141 1.00 29.80 ? 265 PRO A CG  1 
ATOM   1852 C CD  . PRO A 1 267 ? 104.651 55.981 18.566 1.00 27.97 ? 265 PRO A CD  1 
ATOM   1853 N N   . VAL A 1 268 ? 104.456 52.632 15.345 1.00 26.43 ? 266 VAL A N   1 
ATOM   1854 C CA  . VAL A 1 268 ? 104.054 51.223 15.081 1.00 28.62 ? 266 VAL A CA  1 
ATOM   1855 C C   . VAL A 1 268 ? 104.492 50.365 16.270 1.00 29.16 ? 266 VAL A C   1 
ATOM   1856 O O   . VAL A 1 268 ? 105.618 50.526 16.735 1.00 28.05 ? 266 VAL A O   1 
ATOM   1857 C CB  . VAL A 1 268 ? 104.649 50.730 13.745 1.00 34.80 ? 266 VAL A CB  1 
ATOM   1858 C CG1 . VAL A 1 268 ? 104.463 49.236 13.563 1.00 35.77 ? 266 VAL A CG1 1 
ATOM   1859 C CG2 . VAL A 1 268 ? 104.076 51.519 12.567 1.00 38.54 ? 266 VAL A CG2 1 
ATOM   1860 N N   . GLY A 1 269 ? 103.597 49.506 16.761 1.00 28.20 ? 267 GLY A N   1 
ATOM   1861 C CA  . GLY A 1 269 ? 103.912 48.426 17.700 1.00 26.24 ? 267 GLY A CA  1 
ATOM   1862 C C   . GLY A 1 269 ? 104.162 48.930 19.108 1.00 24.04 ? 267 GLY A C   1 
ATOM   1863 O O   . GLY A 1 269 ? 104.640 48.121 19.885 1.00 24.55 ? 267 GLY A O   1 
ATOM   1864 N N   . SER A 1 270 ? 103.888 50.203 19.421 1.00 24.33 ? 268 SER A N   1 
ATOM   1865 C CA  . SER A 1 270 ? 104.362 50.871 20.668 1.00 23.26 ? 268 SER A CA  1 
ATOM   1866 C C   . SER A 1 270 ? 103.323 50.821 21.807 1.00 22.04 ? 268 SER A C   1 
ATOM   1867 O O   . SER A 1 270 ? 103.738 50.948 22.978 1.00 24.48 ? 268 SER A O   1 
ATOM   1868 C CB  . SER A 1 270 ? 104.740 52.299 20.379 1.00 22.65 ? 268 SER A CB  1 
ATOM   1869 O OG  . SER A 1 270 ? 103.598 53.051 19.983 1.00 25.95 ? 268 SER A OG  1 
ATOM   1870 N N   . VAL A 1 271 ? 102.039 50.630 21.513 1.00 20.97 ? 269 VAL A N   1 
ATOM   1871 C CA  . VAL A 1 271 ? 100.959 50.855 22.515 1.00 20.63 ? 269 VAL A CA  1 
ATOM   1872 C C   . VAL A 1 271 ? 100.574 49.561 23.171 1.00 19.74 ? 269 VAL A C   1 
ATOM   1873 O O   . VAL A 1 271 ? 100.204 48.628 22.436 1.00 20.15 ? 269 VAL A O   1 
ATOM   1874 C CB  . VAL A 1 271 ? 99.743  51.560 21.912 1.00 21.12 ? 269 VAL A CB  1 
ATOM   1875 C CG1 . VAL A 1 271 ? 98.650  51.770 22.957 1.00 23.03 ? 269 VAL A CG1 1 
ATOM   1876 C CG2 . VAL A 1 271 ? 100.173 52.891 21.291 1.00 23.23 ? 269 VAL A CG2 1 
ATOM   1877 N N   . LEU A 1 272 ? 100.586 49.530 24.514 1.00 19.19 ? 270 LEU A N   1 
ATOM   1878 C CA  . LEU A 1 272 ? 99.928  48.446 25.293 1.00 19.28 ? 270 LEU A CA  1 
ATOM   1879 C C   . LEU A 1 272 ? 98.457  48.827 25.495 1.00 20.70 ? 270 LEU A C   1 
ATOM   1880 O O   . LEU A 1 272 ? 98.142  49.809 26.183 1.00 20.63 ? 270 LEU A O   1 
ATOM   1881 C CB  . LEU A 1 272 ? 100.646 48.214 26.627 1.00 19.41 ? 270 LEU A CB  1 
ATOM   1882 C CG  . LEU A 1 272 ? 99.950  47.200 27.513 1.00 19.53 ? 270 LEU A CG  1 
ATOM   1883 C CD1 . LEU A 1 272 ? 99.953  45.836 26.834 1.00 20.27 ? 270 LEU A CD1 1 
ATOM   1884 C CD2 . LEU A 1 272 ? 100.609 47.144 28.866 1.00 21.26 ? 270 LEU A CD2 1 
ATOM   1885 N N   . PHE A 1 273 ? 97.565  48.076 24.881 1.00 19.55 ? 271 PHE A N   1 
ATOM   1886 C CA  . PHE A 1 273 ? 96.115  48.242 25.046 1.00 20.29 ? 271 PHE A CA  1 
ATOM   1887 C C   . PHE A 1 273 ? 95.682  47.464 26.283 1.00 18.46 ? 271 PHE A C   1 
ATOM   1888 O O   . PHE A 1 273 ? 95.663  46.238 26.179 1.00 20.50 ? 271 PHE A O   1 
ATOM   1889 C CB  . PHE A 1 273 ? 95.427  47.748 23.778 1.00 20.43 ? 271 PHE A CB  1 
ATOM   1890 C CG  . PHE A 1 273 ? 93.929  47.817 23.761 1.00 20.32 ? 271 PHE A CG  1 
ATOM   1891 C CD1 . PHE A 1 273 ? 93.233  48.720 24.535 1.00 21.13 ? 271 PHE A CD1 1 
ATOM   1892 C CD2 . PHE A 1 273 ? 93.215  46.993 22.898 1.00 21.71 ? 271 PHE A CD2 1 
ATOM   1893 C CE1 . PHE A 1 273 ? 91.854  48.793 24.506 1.00 21.43 ? 271 PHE A CE1 1 
ATOM   1894 C CE2 . PHE A 1 273 ? 91.831  47.091 22.829 1.00 21.94 ? 271 PHE A CE2 1 
ATOM   1895 C CZ  . PHE A 1 273 ? 91.151  47.984 23.644 1.00 21.71 ? 271 PHE A CZ  1 
ATOM   1896 N N   . VAL A 1 274 ? 95.372  48.171 27.363 1.00 19.00 ? 272 VAL A N   1 
ATOM   1897 C CA  . VAL A 1 274 ? 94.820  47.596 28.622 1.00 18.56 ? 272 VAL A CA  1 
ATOM   1898 C C   . VAL A 1 274 ? 93.295  47.627 28.508 1.00 20.18 ? 272 VAL A C   1 
ATOM   1899 O O   . VAL A 1 274 ? 92.641  48.668 28.778 1.00 19.08 ? 272 VAL A O   1 
ATOM   1900 C CB  . VAL A 1 274 ? 95.344  48.359 29.844 1.00 20.76 ? 272 VAL A CB  1 
ATOM   1901 C CG1 . VAL A 1 274 ? 94.861  47.716 31.140 1.00 20.95 ? 272 VAL A CG1 1 
ATOM   1902 C CG2 . VAL A 1 274 ? 96.862  48.422 29.788 1.00 23.26 ? 272 VAL A CG2 1 
ATOM   1903 N N   . SER A 1 275 ? 92.734  46.530 28.040 1.00 19.07 ? 273 SER A N   1 
ATOM   1904 C CA  . SER A 1 275 ? 91.315  46.449 27.632 1.00 22.16 ? 273 SER A CA  1 
ATOM   1905 C C   . SER A 1 275 ? 90.532  45.976 28.862 1.00 23.35 ? 273 SER A C   1 
ATOM   1906 O O   . SER A 1 275 ? 90.168  44.796 28.913 1.00 25.31 ? 273 SER A O   1 
ATOM   1907 C CB  . SER A 1 275 ? 91.177  45.511 26.433 1.00 24.90 ? 273 SER A CB  1 
ATOM   1908 O OG  . SER A 1 275 ? 89.859  45.482 25.944 1.00 27.29 ? 273 SER A OG  1 
ATOM   1909 N N   . PHE A 1 276 ? 90.364  46.844 29.843 1.00 24.00 ? 274 PHE A N   1 
ATOM   1910 C CA  . PHE A 1 276 ? 89.787  46.469 31.155 1.00 24.08 ? 274 PHE A CA  1 
ATOM   1911 C C   . PHE A 1 276 ? 88.373  47.048 31.274 1.00 26.56 ? 274 PHE A C   1 
ATOM   1912 O O   . PHE A 1 276 ? 87.919  47.199 32.427 1.00 30.91 ? 274 PHE A O   1 
ATOM   1913 C CB  . PHE A 1 276 ? 90.753  46.867 32.272 1.00 25.65 ? 274 PHE A CB  1 
ATOM   1914 C CG  . PHE A 1 276 ? 91.885  45.911 32.577 1.00 22.65 ? 274 PHE A CG  1 
ATOM   1915 C CD1 . PHE A 1 276 ? 92.192  44.828 31.763 1.00 21.17 ? 274 PHE A CD1 1 
ATOM   1916 C CD2 . PHE A 1 276 ? 92.666  46.123 33.705 1.00 21.52 ? 274 PHE A CD2 1 
ATOM   1917 C CE1 . PHE A 1 276 ? 93.247  43.985 32.061 1.00 21.77 ? 274 PHE A CE1 1 
ATOM   1918 C CE2 . PHE A 1 276 ? 93.724  45.274 33.999 1.00 21.37 ? 274 PHE A CE2 1 
ATOM   1919 C CZ  . PHE A 1 276 ? 94.021  44.208 33.169 1.00 20.35 ? 274 PHE A CZ  1 
ATOM   1920 N N   . GLY A 1 277 ? 87.728  47.356 30.140 1.00 29.62 ? 275 GLY A N   1 
ATOM   1921 C CA  . GLY A 1 277 ? 86.325  47.796 30.033 1.00 30.91 ? 275 GLY A CA  1 
ATOM   1922 C C   . GLY A 1 277 ? 85.326  46.679 30.280 1.00 36.40 ? 275 GLY A C   1 
ATOM   1923 O O   . GLY A 1 277 ? 84.160  46.992 30.534 1.00 42.28 ? 275 GLY A O   1 
ATOM   1924 N N   . SER A 1 278 ? 85.746  45.414 30.199 1.00 33.83 ? 276 SER A N   1 
ATOM   1925 C CA  . SER A 1 278 ? 84.886  44.241 30.478 1.00 32.92 ? 276 SER A CA  1 
ATOM   1926 C C   . SER A 1 278 ? 85.703  43.154 31.178 1.00 29.19 ? 276 SER A C   1 
ATOM   1927 O O   . SER A 1 278 ? 86.952  43.275 31.308 1.00 21.99 ? 276 SER A O   1 
ATOM   1928 C CB  . SER A 1 278 ? 84.207  43.760 29.237 1.00 35.09 ? 276 SER A CB  1 
ATOM   1929 O OG  . SER A 1 278 ? 85.099  43.041 28.430 1.00 41.89 ? 276 SER A OG  1 
ATOM   1930 N N   . GLY A 1 279 ? 85.004  42.184 31.739 1.00 25.14 ? 277 GLY A N   1 
ATOM   1931 C CA  . GLY A 1 279 ? 85.641  40.973 32.270 1.00 25.13 ? 277 GLY A CA  1 
ATOM   1932 C C   . GLY A 1 279 ? 85.955  41.096 33.737 1.00 24.75 ? 277 GLY A C   1 
ATOM   1933 O O   . GLY A 1 279 ? 86.662  40.223 34.271 1.00 25.59 ? 277 GLY A O   1 
ATOM   1934 N N   . GLY A 1 280 ? 85.421  42.114 34.404 1.00 27.62 ? 278 GLY A N   1 
ATOM   1935 C CA  . GLY A 1 280 ? 85.507  42.231 35.867 1.00 28.47 ? 278 GLY A CA  1 
ATOM   1936 C C   . GLY A 1 280 ? 86.139  43.532 36.312 1.00 28.01 ? 278 GLY A C   1 
ATOM   1937 O O   . GLY A 1 280 ? 86.654  44.282 35.497 1.00 29.64 ? 278 GLY A O   1 
ATOM   1938 N N   . THR A 1 281 ? 86.111  43.718 37.617 1.00 29.03 ? 279 THR A N   1 
ATOM   1939 C CA  . THR A 1 281 ? 86.439  44.957 38.347 1.00 31.77 ? 279 THR A CA  1 
ATOM   1940 C C   . THR A 1 281 ? 87.740  44.714 39.117 1.00 27.76 ? 279 THR A C   1 
ATOM   1941 O O   . THR A 1 281 ? 87.864  43.628 39.731 1.00 29.77 ? 279 THR A O   1 
ATOM   1942 C CB  . THR A 1 281 ? 85.275  45.248 39.311 1.00 34.26 ? 279 THR A CB  1 
ATOM   1943 O OG1 . THR A 1 281 ? 84.098  45.335 38.502 1.00 43.10 ? 279 THR A OG1 1 
ATOM   1944 C CG2 . THR A 1 281 ? 85.482  46.499 40.125 1.00 32.94 ? 279 THR A CG2 1 
ATOM   1945 N N   . LEU A 1 282 ? 88.639  45.688 39.141 1.00 23.96 ? 280 LEU A N   1 
ATOM   1946 C CA  . LEU A 1 282 ? 89.829  45.690 40.025 1.00 23.98 ? 280 LEU A CA  1 
ATOM   1947 C C   . LEU A 1 282 ? 89.456  46.283 41.381 1.00 21.57 ? 280 LEU A C   1 
ATOM   1948 O O   . LEU A 1 282 ? 88.583  47.172 41.446 1.00 21.99 ? 280 LEU A O   1 
ATOM   1949 C CB  . LEU A 1 282 ? 90.956  46.524 39.422 1.00 25.26 ? 280 LEU A CB  1 
ATOM   1950 C CG  . LEU A 1 282 ? 91.446  46.116 38.039 1.00 29.11 ? 280 LEU A CG  1 
ATOM   1951 C CD1 . LEU A 1 282 ? 92.518  47.085 37.571 1.00 31.95 ? 280 LEU A CD1 1 
ATOM   1952 C CD2 . LEU A 1 282 ? 91.955  44.692 38.040 1.00 29.23 ? 280 LEU A CD2 1 
ATOM   1953 N N   . SER A 1 283 ? 90.168  45.866 42.421 1.00 23.52 ? 281 SER A N   1 
ATOM   1954 C CA  . SER A 1 283 ? 90.158  46.581 43.723 1.00 21.70 ? 281 SER A CA  1 
ATOM   1955 C C   . SER A 1 283 ? 90.839  47.944 43.536 1.00 22.10 ? 281 SER A C   1 
ATOM   1956 O O   . SER A 1 283 ? 91.660  48.123 42.642 1.00 21.74 ? 281 SER A O   1 
ATOM   1957 C CB  . SER A 1 283 ? 90.823  45.760 44.792 1.00 20.55 ? 281 SER A CB  1 
ATOM   1958 O OG  . SER A 1 283 ? 92.238  45.670 44.573 1.00 21.52 ? 281 SER A OG  1 
ATOM   1959 N N   . TYR A 1 284 ? 90.486  48.892 44.368 1.00 22.73 ? 282 TYR A N   1 
ATOM   1960 C CA  . TYR A 1 284 ? 91.140  50.210 44.459 1.00 21.44 ? 282 TYR A CA  1 
ATOM   1961 C C   . TYR A 1 284 ? 92.642  50.020 44.627 1.00 21.66 ? 282 TYR A C   1 
ATOM   1962 O O   . TYR A 1 284 ? 93.443  50.695 43.960 1.00 23.27 ? 282 TYR A O   1 
ATOM   1963 C CB  . TYR A 1 284 ? 90.492  51.012 45.582 1.00 22.38 ? 282 TYR A CB  1 
ATOM   1964 C CG  . TYR A 1 284 ? 91.216  52.301 45.828 1.00 24.08 ? 282 TYR A CG  1 
ATOM   1965 C CD1 . TYR A 1 284 ? 91.076  53.378 44.971 1.00 27.63 ? 282 TYR A CD1 1 
ATOM   1966 C CD2 . TYR A 1 284 ? 92.116  52.407 46.874 1.00 26.36 ? 282 TYR A CD2 1 
ATOM   1967 C CE1 . TYR A 1 284 ? 91.780  54.553 45.185 1.00 26.80 ? 282 TYR A CE1 1 
ATOM   1968 C CE2 . TYR A 1 284 ? 92.796  53.587 47.129 1.00 26.83 ? 282 TYR A CE2 1 
ATOM   1969 C CZ  . TYR A 1 284 ? 92.632  54.656 46.273 1.00 29.35 ? 282 TYR A CZ  1 
ATOM   1970 O OH  . TYR A 1 284 ? 93.353  55.778 46.510 1.00 31.54 ? 282 TYR A OH  1 
ATOM   1971 N N   . GLU A 1 285 ? 93.042  49.094 45.486 1.00 20.22 ? 283 GLU A N   1 
ATOM   1972 C CA  . GLU A 1 285 ? 94.466  48.799 45.734 1.00 22.26 ? 283 GLU A CA  1 
ATOM   1973 C C   . GLU A 1 285 ? 95.100  48.313 44.424 1.00 21.73 ? 283 GLU A C   1 
ATOM   1974 O O   . GLU A 1 285 ? 96.232  48.759 44.085 1.00 22.26 ? 283 GLU A O   1 
ATOM   1975 C CB  . GLU A 1 285 ? 94.587  47.773 46.871 1.00 22.78 ? 283 GLU A CB  1 
ATOM   1976 C CG  . GLU A 1 285 ? 95.986  47.290 47.055 1.00 23.97 ? 283 GLU A CG  1 
ATOM   1977 C CD  . GLU A 1 285 ? 96.206  46.243 48.130 1.00 23.30 ? 283 GLU A CD  1 
ATOM   1978 O OE1 . GLU A 1 285 ? 95.235  45.558 48.512 1.00 24.16 ? 283 GLU A OE1 1 
ATOM   1979 O OE2 . GLU A 1 285 ? 97.356  46.108 48.527 1.00 27.80 ? 283 GLU A OE2 1 
ATOM   1980 N N   . GLN A 1 286 ? 94.437  47.406 43.715 1.00 20.13 ? 284 GLN A N   1 
ATOM   1981 C CA  . GLN A 1 286 ? 95.058  46.785 42.523 1.00 20.31 ? 284 GLN A CA  1 
ATOM   1982 C C   . GLN A 1 286 ? 95.156  47.882 41.458 1.00 20.37 ? 284 GLN A C   1 
ATOM   1983 O O   . GLN A 1 286 ? 96.173  47.956 40.717 1.00 21.69 ? 284 GLN A O   1 
ATOM   1984 C CB  . GLN A 1 286 ? 94.273  45.577 42.036 1.00 20.44 ? 284 GLN A CB  1 
ATOM   1985 C CG  . GLN A 1 286 ? 94.871  44.980 40.775 1.00 22.90 ? 284 GLN A CG  1 
ATOM   1986 C CD  . GLN A 1 286 ? 96.226  44.385 41.034 1.00 21.84 ? 284 GLN A CD  1 
ATOM   1987 O OE1 . GLN A 1 286 ? 96.325  43.243 41.430 1.00 21.28 ? 284 GLN A OE1 1 
ATOM   1988 N NE2 . GLN A 1 286 ? 97.283  45.143 40.833 1.00 21.69 ? 284 GLN A NE2 1 
ATOM   1989 N N   . MET A 1 287 ? 94.120  48.690 41.367 1.00 21.23 ? 285 MET A N   1 
ATOM   1990 C CA  . MET A 1 287 ? 94.073  49.762 40.349 1.00 23.54 ? 285 MET A CA  1 
ATOM   1991 C C   . MET A 1 287 ? 95.229  50.741 40.613 1.00 21.27 ? 285 MET A C   1 
ATOM   1992 O O   . MET A 1 287 ? 95.848  51.214 39.670 1.00 19.62 ? 285 MET A O   1 
ATOM   1993 C CB  . MET A 1 287 ? 92.725  50.477 40.365 1.00 23.16 ? 285 MET A CB  1 
ATOM   1994 C CG  . MET A 1 287 ? 92.672  51.693 39.438 1.00 26.02 ? 285 MET A CG  1 
ATOM   1995 S SD  . MET A 1 287 ? 91.029  52.405 39.437 1.00 29.71 ? 285 MET A SD  1 
ATOM   1996 C CE  . MET A 1 287 ? 91.146  53.682 38.189 1.00 37.88 ? 285 MET A CE  1 
ATOM   1997 N N   . THR A 1 288 ? 95.486  51.103 41.864 1.00 21.56 ? 286 THR A N   1 
ATOM   1998 C CA  . THR A 1 288 ? 96.631  51.966 42.255 1.00 22.56 ? 286 THR A CA  1 
ATOM   1999 C C   . THR A 1 288 ? 97.948  51.313 41.806 1.00 21.74 ? 286 THR A C   1 
ATOM   2000 O O   . THR A 1 288 ? 98.770  51.991 41.203 1.00 21.63 ? 286 THR A O   1 
ATOM   2001 C CB  . THR A 1 288 ? 96.564  52.189 43.784 1.00 26.44 ? 286 THR A CB  1 
ATOM   2002 O OG1 . THR A 1 288 ? 95.334  52.828 44.113 1.00 27.55 ? 286 THR A OG1 1 
ATOM   2003 C CG2 . THR A 1 288 ? 97.718  53.008 44.314 1.00 25.61 ? 286 THR A CG2 1 
ATOM   2004 N N   . GLU A 1 289 ? 98.174  50.024 42.073 1.00 19.81 ? 287 GLU A N   1 
ATOM   2005 C CA  . GLU A 1 289 ? 99.422  49.331 41.666 1.00 20.97 ? 287 GLU A CA  1 
ATOM   2006 C C   . GLU A 1 289 ? 99.543  49.279 40.140 1.00 21.87 ? 287 GLU A C   1 
ATOM   2007 O O   . GLU A 1 289 ? 100.682 49.375 39.649 1.00 20.71 ? 287 GLU A O   1 
ATOM   2008 C CB  . GLU A 1 289 ? 99.499  47.926 42.225 1.00 23.20 ? 287 GLU A CB  1 
ATOM   2009 C CG  . GLU A 1 289 ? 99.593  47.963 43.743 1.00 25.12 ? 287 GLU A CG  1 
ATOM   2010 C CD  . GLU A 1 289 ? 100.749 48.800 44.240 1.00 24.34 ? 287 GLU A CD  1 
ATOM   2011 O OE1 . GLU A 1 289 ? 101.933 48.432 43.928 1.00 24.23 ? 287 GLU A OE1 1 
ATOM   2012 O OE2 . GLU A 1 289 ? 100.467 49.827 44.930 1.00 24.16 ? 287 GLU A OE2 1 
ATOM   2013 N N   . LEU A 1 290 ? 98.426  49.106 39.434 1.00 20.25 ? 288 LEU A N   1 
ATOM   2014 C CA  . LEU A 1 290 ? 98.475  49.021 37.953 1.00 19.76 ? 288 LEU A CA  1 
ATOM   2015 C C   . LEU A 1 290 ? 98.879  50.405 37.390 1.00 20.00 ? 288 LEU A C   1 
ATOM   2016 O O   . LEU A 1 290 ? 99.724  50.453 36.477 1.00 21.00 ? 288 LEU A O   1 
ATOM   2017 C CB  . LEU A 1 290 ? 97.121  48.548 37.434 1.00 20.45 ? 288 LEU A CB  1 
ATOM   2018 C CG  . LEU A 1 290 ? 96.960  48.543 35.908 1.00 22.05 ? 288 LEU A CG  1 
ATOM   2019 C CD1 . LEU A 1 290 ? 98.038  47.714 35.218 1.00 24.25 ? 288 LEU A CD1 1 
ATOM   2020 C CD2 . LEU A 1 290 ? 95.577  48.025 35.533 1.00 21.44 ? 288 LEU A CD2 1 
ATOM   2021 N N   . ALA A 1 291 ? 98.320  51.495 37.903 1.00 19.05 ? 289 ALA A N   1 
ATOM   2022 C CA  . ALA A 1 291 ? 98.669  52.857 37.452 1.00 20.34 ? 289 ALA A CA  1 
ATOM   2023 C C   . ALA A 1 291 ? 100.176 53.094 37.641 1.00 22.73 ? 289 ALA A C   1 
ATOM   2024 O O   . ALA A 1 291 ? 100.836 53.502 36.694 1.00 22.00 ? 289 ALA A O   1 
ATOM   2025 C CB  . ALA A 1 291 ? 97.842  53.875 38.203 1.00 20.25 ? 289 ALA A CB  1 
ATOM   2026 N N   . HIS A 1 292 ? 100.736 52.793 38.815 1.00 23.17 ? 290 HIS A N   1 
ATOM   2027 C CA  . HIS A 1 292 ? 102.199 52.983 39.065 1.00 24.38 ? 290 HIS A CA  1 
ATOM   2028 C C   . HIS A 1 292 ? 103.037 52.081 38.158 1.00 22.66 ? 290 HIS A C   1 
ATOM   2029 O O   . HIS A 1 292 ? 104.055 52.526 37.627 1.00 22.83 ? 290 HIS A O   1 
ATOM   2030 C CB  . HIS A 1 292 ? 102.544 52.731 40.541 1.00 23.66 ? 290 HIS A CB  1 
ATOM   2031 C CG  . HIS A 1 292 ? 102.044 53.810 41.434 1.00 26.98 ? 290 HIS A CG  1 
ATOM   2032 N ND1 . HIS A 1 292 ? 102.555 55.103 41.383 1.00 30.78 ? 290 HIS A ND1 1 
ATOM   2033 C CD2 . HIS A 1 292 ? 101.073 53.830 42.374 1.00 31.61 ? 290 HIS A CD2 1 
ATOM   2034 C CE1 . HIS A 1 292 ? 101.895 55.864 42.248 1.00 30.16 ? 290 HIS A CE1 1 
ATOM   2035 N NE2 . HIS A 1 292 ? 100.994 55.119 42.876 1.00 30.52 ? 290 HIS A NE2 1 
ATOM   2036 N N   . GLY A 1 293 ? 102.630 50.830 37.996 1.00 24.07 ? 291 GLY A N   1 
ATOM   2037 C CA  . GLY A 1 293 ? 103.367 49.872 37.187 1.00 23.66 ? 291 GLY A CA  1 
ATOM   2038 C C   . GLY A 1 293 ? 103.405 50.282 35.722 1.00 23.95 ? 291 GLY A C   1 
ATOM   2039 O O   . GLY A 1 293 ? 104.463 50.138 35.127 1.00 23.56 ? 291 GLY A O   1 
ATOM   2040 N N   . LEU A 1 294 ? 102.290 50.792 35.179 1.00 24.56 ? 292 LEU A N   1 
ATOM   2041 C CA  . LEU A 1 294 ? 102.239 51.318 33.793 1.00 23.29 ? 292 LEU A CA  1 
ATOM   2042 C C   . LEU A 1 294 ? 103.132 52.552 33.691 1.00 23.82 ? 292 LEU A C   1 
ATOM   2043 O O   . LEU A 1 294 ? 103.934 52.648 32.728 1.00 23.02 ? 292 LEU A O   1 
ATOM   2044 C CB  . LEU A 1 294 ? 100.798 51.661 33.391 1.00 23.38 ? 292 LEU A CB  1 
ATOM   2045 C CG  . LEU A 1 294 ? 99.895  50.449 33.132 1.00 23.19 ? 292 LEU A CG  1 
ATOM   2046 C CD1 . LEU A 1 294 ? 98.450  50.874 33.022 1.00 20.82 ? 292 LEU A CD1 1 
ATOM   2047 C CD2 . LEU A 1 294 ? 100.311 49.684 31.876 1.00 23.67 ? 292 LEU A CD2 1 
ATOM   2048 N N   . GLU A 1 295 ? 102.966 53.512 34.596 1.00 25.03 ? 293 GLU A N   1 
ATOM   2049 C CA  . GLU A 1 295 ? 103.776 54.760 34.541 1.00 24.71 ? 293 GLU A CA  1 
ATOM   2050 C C   . GLU A 1 295 ? 105.268 54.387 34.576 1.00 25.34 ? 293 GLU A C   1 
ATOM   2051 O O   . GLU A 1 295 ? 106.005 54.852 33.696 1.00 25.98 ? 293 GLU A O   1 
ATOM   2052 C CB  . GLU A 1 295 ? 103.367 55.678 35.679 1.00 25.06 ? 293 GLU A CB  1 
ATOM   2053 C CG  . GLU A 1 295 ? 104.234 56.894 35.735 1.00 26.60 ? 293 GLU A CG  1 
ATOM   2054 C CD  . GLU A 1 295 ? 103.824 57.965 36.708 1.00 29.55 ? 293 GLU A CD  1 
ATOM   2055 O OE1 . GLU A 1 295 ? 102.993 57.686 37.620 1.00 30.28 ? 293 GLU A OE1 1 
ATOM   2056 O OE2 . GLU A 1 295 ? 104.331 59.099 36.542 1.00 32.11 ? 293 GLU A OE2 1 
ATOM   2057 N N   . SER A 1 296 ? 105.707 53.513 35.495 1.00 25.84 ? 294 SER A N   1 
ATOM   2058 C CA  . SER A 1 296 ? 107.137 53.172 35.696 1.00 26.69 ? 294 SER A CA  1 
ATOM   2059 C C   . SER A 1 296 ? 107.697 52.389 34.499 1.00 29.71 ? 294 SER A C   1 
ATOM   2060 O O   . SER A 1 296 ? 108.925 52.391 34.313 1.00 26.11 ? 294 SER A O   1 
ATOM   2061 C CB  . SER A 1 296 ? 107.403 52.451 37.009 1.00 31.23 ? 294 SER A CB  1 
ATOM   2062 O OG  . SER A 1 296 ? 107.163 53.328 38.103 1.00 31.73 ? 294 SER A OG  1 
ATOM   2063 N N   . SER A 1 297 ? 106.850 51.773 33.683 1.00 24.63 ? 295 SER A N   1 
ATOM   2064 C CA  . SER A 1 297 ? 107.295 51.032 32.468 1.00 23.59 ? 295 SER A CA  1 
ATOM   2065 C C   . SER A 1 297 ? 107.810 52.017 31.409 1.00 23.35 ? 295 SER A C   1 
ATOM   2066 O O   . SER A 1 297 ? 108.570 51.606 30.504 1.00 25.34 ? 295 SER A O   1 
ATOM   2067 C CB  . SER A 1 297 ? 106.167 50.164 31.946 1.00 22.44 ? 295 SER A CB  1 
ATOM   2068 O OG  . SER A 1 297 ? 105.185 50.930 31.252 1.00 20.70 ? 295 SER A OG  1 
ATOM   2069 N N   . GLN A 1 298 ? 107.343 53.256 31.455 1.00 23.20 ? 296 GLN A N   1 
ATOM   2070 C CA  . GLN A 1 298 ? 107.633 54.288 30.425 1.00 26.03 ? 296 GLN A CA  1 
ATOM   2071 C C   . GLN A 1 298 ? 107.082 53.863 29.061 1.00 25.42 ? 296 GLN A C   1 
ATOM   2072 O O   . GLN A 1 298 ? 107.381 54.536 28.080 1.00 30.30 ? 296 GLN A O   1 
ATOM   2073 C CB  . GLN A 1 298 ? 109.151 54.514 30.308 1.00 28.77 ? 296 GLN A CB  1 
ATOM   2074 C CG  . GLN A 1 298 ? 109.753 55.094 31.583 1.00 33.95 ? 296 GLN A CG  1 
ATOM   2075 C CD  . GLN A 1 298 ? 109.278 56.490 31.919 1.00 33.27 ? 296 GLN A CD  1 
ATOM   2076 O OE1 . GLN A 1 298 ? 108.786 57.244 31.084 1.00 38.50 ? 296 GLN A OE1 1 
ATOM   2077 N NE2 . GLN A 1 298 ? 109.430 56.863 33.177 1.00 42.93 ? 296 GLN A NE2 1 
ATOM   2078 N N   . GLN A 1 299 ? 106.284 52.814 28.972 1.00 24.00 ? 297 GLN A N   1 
ATOM   2079 C CA  . GLN A 1 299 ? 105.688 52.392 27.678 1.00 23.87 ? 297 GLN A CA  1 
ATOM   2080 C C   . GLN A 1 299 ? 104.435 53.213 27.408 1.00 22.83 ? 297 GLN A C   1 
ATOM   2081 O O   . GLN A 1 299 ? 103.755 53.639 28.353 1.00 22.71 ? 297 GLN A O   1 
ATOM   2082 C CB  . GLN A 1 299 ? 105.330 50.913 27.727 1.00 26.63 ? 297 GLN A CB  1 
ATOM   2083 C CG  . GLN A 1 299 ? 106.505 50.035 28.140 1.00 34.17 ? 297 GLN A CG  1 
ATOM   2084 C CD  . GLN A 1 299 ? 107.609 50.112 27.111 1.00 37.18 ? 297 GLN A CD  1 
ATOM   2085 O OE1 . GLN A 1 299 ? 108.761 50.467 27.406 1.00 48.29 ? 297 GLN A OE1 1 
ATOM   2086 N NE2 . GLN A 1 299 ? 107.218 49.894 25.886 1.00 29.22 ? 297 GLN A NE2 1 
ATOM   2087 N N   . ARG A 1 300 ? 104.096 53.369 26.137 1.00 22.00 ? 298 ARG A N   1 
ATOM   2088 C CA  . ARG A 1 300 ? 102.798 53.901 25.705 1.00 22.61 ? 298 ARG A CA  1 
ATOM   2089 C C   . ARG A 1 300 ? 101.685 52.915 26.074 1.00 20.91 ? 298 ARG A C   1 
ATOM   2090 O O   . ARG A 1 300 ? 101.902 51.704 25.959 1.00 21.37 ? 298 ARG A O   1 
ATOM   2091 C CB  . ARG A 1 300 ? 102.791 54.141 24.213 1.00 23.88 ? 298 ARG A CB  1 
ATOM   2092 C CG  . ARG A 1 300 ? 103.645 55.348 23.850 1.00 27.15 ? 298 ARG A CG  1 
ATOM   2093 C CD  . ARG A 1 300 ? 103.625 55.480 22.354 1.00 26.83 ? 298 ARG A CD  1 
ATOM   2094 N NE  . ARG A 1 300 ? 104.149 56.760 21.960 1.00 26.58 ? 298 ARG A NE  1 
ATOM   2095 C CZ  . ARG A 1 300 ? 105.432 57.054 21.839 1.00 31.23 ? 298 ARG A CZ  1 
ATOM   2096 N NH1 . ARG A 1 300 ? 106.376 56.163 22.085 1.00 36.34 ? 298 ARG A NH1 1 
ATOM   2097 N NH2 . ARG A 1 300 ? 105.763 58.265 21.458 1.00 35.88 ? 298 ARG A NH2 1 
ATOM   2098 N N   . PHE A 1 301 ? 100.549 53.434 26.491 1.00 20.20 ? 299 PHE A N   1 
ATOM   2099 C CA  . PHE A 1 301 ? 99.396  52.600 26.867 1.00 21.00 ? 299 PHE A CA  1 
ATOM   2100 C C   . PHE A 1 301 ? 98.103  53.326 26.535 1.00 21.01 ? 299 PHE A C   1 
ATOM   2101 O O   . PHE A 1 301 ? 98.047  54.556 26.583 1.00 21.63 ? 299 PHE A O   1 
ATOM   2102 C CB  . PHE A 1 301 ? 99.518  52.181 28.334 1.00 19.04 ? 299 PHE A CB  1 
ATOM   2103 C CG  . PHE A 1 301 ? 99.490  53.309 29.317 1.00 19.89 ? 299 PHE A CG  1 
ATOM   2104 C CD1 . PHE A 1 301 ? 98.295  53.822 29.780 1.00 23.04 ? 299 PHE A CD1 1 
ATOM   2105 C CD2 . PHE A 1 301 ? 100.673 53.875 29.769 1.00 20.01 ? 299 PHE A CD2 1 
ATOM   2106 C CE1 . PHE A 1 301 ? 98.277  54.864 30.697 1.00 22.15 ? 299 PHE A CE1 1 
ATOM   2107 C CE2 . PHE A 1 301 ? 100.655 54.929 30.664 1.00 19.35 ? 299 PHE A CE2 1 
ATOM   2108 C CZ  . PHE A 1 301 ? 99.457  55.426 31.132 1.00 23.12 ? 299 PHE A CZ  1 
ATOM   2109 N N   . LEU A 1 302 ? 97.083  52.524 26.279 1.00 21.30 ? 300 LEU A N   1 
ATOM   2110 C CA  . LEU A 1 302 ? 95.670  52.927 26.116 1.00 20.01 ? 300 LEU A CA  1 
ATOM   2111 C C   . LEU A 1 302 ? 94.883  52.113 27.122 1.00 20.97 ? 300 LEU A C   1 
ATOM   2112 O O   . LEU A 1 302 ? 94.799  50.889 26.943 1.00 19.77 ? 300 LEU A O   1 
ATOM   2113 C CB  . LEU A 1 302 ? 95.272  52.623 24.683 1.00 21.69 ? 300 LEU A CB  1 
ATOM   2114 C CG  . LEU A 1 302 ? 94.001  53.315 24.201 1.00 24.83 ? 300 LEU A CG  1 
ATOM   2115 C CD1 . LEU A 1 302 ? 93.718  53.005 22.734 1.00 28.10 ? 300 LEU A CD1 1 
ATOM   2116 C CD2 . LEU A 1 302 ? 92.803  52.984 25.018 1.00 25.99 ? 300 LEU A CD2 1 
ATOM   2117 N N   . TRP A 1 303 ? 94.443  52.723 28.199 1.00 18.99 ? 301 TRP A N   1 
ATOM   2118 C CA  . TRP A 1 303 ? 93.890  51.967 29.331 1.00 19.21 ? 301 TRP A CA  1 
ATOM   2119 C C   . TRP A 1 303 ? 92.399  52.269 29.382 1.00 21.00 ? 301 TRP A C   1 
ATOM   2120 O O   . TRP A 1 303 ? 92.001  53.459 29.597 1.00 21.52 ? 301 TRP A O   1 
ATOM   2121 C CB  . TRP A 1 303 ? 94.618  52.319 30.624 1.00 20.38 ? 301 TRP A CB  1 
ATOM   2122 C CG  . TRP A 1 303 ? 94.115  51.627 31.841 1.00 21.43 ? 301 TRP A CG  1 
ATOM   2123 C CD1 . TRP A 1 303 ? 93.194  50.622 31.950 1.00 20.52 ? 301 TRP A CD1 1 
ATOM   2124 C CD2 . TRP A 1 303 ? 94.544  51.940 33.171 1.00 19.55 ? 301 TRP A CD2 1 
ATOM   2125 N NE1 . TRP A 1 303 ? 92.985  50.331 33.272 1.00 21.99 ? 301 TRP A NE1 1 
ATOM   2126 C CE2 . TRP A 1 303 ? 93.852  51.075 34.037 1.00 20.66 ? 301 TRP A CE2 1 
ATOM   2127 C CE3 . TRP A 1 303 ? 95.454  52.867 33.686 1.00 21.64 ? 301 TRP A CE3 1 
ATOM   2128 C CZ2 . TRP A 1 303 ? 94.024  51.137 35.422 1.00 20.69 ? 301 TRP A CZ2 1 
ATOM   2129 C CZ3 . TRP A 1 303 ? 95.607  52.940 35.056 1.00 23.03 ? 301 TRP A CZ3 1 
ATOM   2130 C CH2 . TRP A 1 303 ? 94.918  52.057 35.901 1.00 22.51 ? 301 TRP A CH2 1 
ATOM   2131 N N   . VAL A 1 304 ? 91.601  51.232 29.187 1.00 19.02 ? 302 VAL A N   1 
ATOM   2132 C CA  . VAL A 1 304 ? 90.123  51.350 29.364 1.00 21.82 ? 302 VAL A CA  1 
ATOM   2133 C C   . VAL A 1 304 ? 89.837  50.994 30.827 1.00 23.18 ? 302 VAL A C   1 
ATOM   2134 O O   . VAL A 1 304 ? 89.991  49.823 31.181 1.00 25.25 ? 302 VAL A O   1 
ATOM   2135 C CB  . VAL A 1 304 ? 89.341  50.481 28.378 1.00 21.50 ? 302 VAL A CB  1 
ATOM   2136 C CG1 . VAL A 1 304 ? 87.823  50.655 28.596 1.00 23.68 ? 302 VAL A CG1 1 
ATOM   2137 C CG2 . VAL A 1 304 ? 89.721  50.782 26.937 1.00 21.54 ? 302 VAL A CG2 1 
ATOM   2138 N N   . VAL A 1 305 ? 89.383  51.963 31.606 1.00 22.45 ? 303 VAL A N   1 
ATOM   2139 C CA  . VAL A 1 305 ? 89.236  51.822 33.080 1.00 24.74 ? 303 VAL A CA  1 
ATOM   2140 C C   . VAL A 1 305 ? 87.754  51.673 33.447 1.00 26.14 ? 303 VAL A C   1 
ATOM   2141 O O   . VAL A 1 305 ? 86.888  52.379 32.897 1.00 25.69 ? 303 VAL A O   1 
ATOM   2142 C CB  . VAL A 1 305 ? 89.947  52.964 33.825 1.00 29.97 ? 303 VAL A CB  1 
ATOM   2143 C CG1 . VAL A 1 305 ? 89.491  54.344 33.414 1.00 34.01 ? 303 VAL A CG1 1 
ATOM   2144 C CG2 . VAL A 1 305 ? 89.774  52.823 35.318 1.00 31.34 ? 303 VAL A CG2 1 
ATOM   2145 N N   . ARG A 1 306 ? 87.448  50.788 34.383 1.00 26.02 ? 304 ARG A N   1 
ATOM   2146 C CA  . ARG A 1 306 ? 86.105  50.816 35.022 1.00 31.70 ? 304 ARG A CA  1 
ATOM   2147 C C   . ARG A 1 306 ? 86.303  51.118 36.499 1.00 29.84 ? 304 ARG A C   1 
ATOM   2148 O O   . ARG A 1 306 ? 87.444  51.021 36.985 1.00 28.11 ? 304 ARG A O   1 
ATOM   2149 C CB  . ARG A 1 306 ? 85.293  49.553 34.738 1.00 40.47 ? 304 ARG A CB  1 
ATOM   2150 C CG  . ARG A 1 306 ? 85.769  48.292 35.438 1.00 49.86 ? 304 ARG A CG  1 
ATOM   2151 C CD  . ARG A 1 306 ? 84.691  47.221 35.345 1.00 61.46 ? 304 ARG A CD  1 
ATOM   2152 N NE  . ARG A 1 306 ? 84.073  47.219 34.020 1.00 75.33 ? 304 ARG A NE  1 
ATOM   2153 C CZ  . ARG A 1 306 ? 82.764  47.122 33.780 1.00 77.62 ? 304 ARG A CZ  1 
ATOM   2154 N NH1 . ARG A 1 306 ? 81.895  47.013 34.773 1.00 74.65 ? 304 ARG A NH1 1 
ATOM   2155 N NH2 . ARG A 1 306 ? 82.325  47.146 32.535 1.00 80.60 ? 304 ARG A NH2 1 
ATOM   2156 N N   . SER A 1 307 ? 85.250  51.610 37.137 1.00 27.76 ? 305 SER A N   1 
ATOM   2157 C CA  . SER A 1 307 ? 85.293  52.050 38.549 1.00 29.61 ? 305 SER A CA  1 
ATOM   2158 C C   . SER A 1 307 ? 85.793  50.859 39.356 1.00 24.56 ? 305 SER A C   1 
ATOM   2159 O O   . SER A 1 307 ? 85.340  49.756 39.151 1.00 22.26 ? 305 SER A O   1 
ATOM   2160 C CB  . SER A 1 307 ? 83.933  52.557 39.017 1.00 31.61 ? 305 SER A CB  1 
ATOM   2161 O OG  . SER A 1 307 ? 83.800  53.899 38.575 1.00 43.79 ? 305 SER A OG  1 
ATOM   2162 N N   . PRO A 1 308 ? 86.780  51.027 40.248 1.00 23.96 ? 306 PRO A N   1 
ATOM   2163 C CA  . PRO A 1 308 ? 87.175  49.920 41.091 1.00 24.48 ? 306 PRO A CA  1 
ATOM   2164 C C   . PRO A 1 308 ? 86.114  49.608 42.154 1.00 25.21 ? 306 PRO A C   1 
ATOM   2165 O O   . PRO A 1 308 ? 85.260  50.417 42.414 1.00 25.51 ? 306 PRO A O   1 
ATOM   2166 C CB  . PRO A 1 308 ? 88.459  50.458 41.692 1.00 22.08 ? 306 PRO A CB  1 
ATOM   2167 C CG  . PRO A 1 308 ? 88.151  51.912 41.867 1.00 24.83 ? 306 PRO A CG  1 
ATOM   2168 C CD  . PRO A 1 308 ? 87.423  52.291 40.613 1.00 22.00 ? 306 PRO A CD  1 
ATOM   2169 N N   . ASN A 1 309 ? 86.250  48.463 42.801 1.00 26.20 ? 307 ASN A N   1 
ATOM   2170 C CA  . ASN A 1 309 ? 85.492  48.170 44.040 1.00 25.51 ? 307 ASN A CA  1 
ATOM   2171 C C   . ASN A 1 309 ? 86.473  48.226 45.202 1.00 26.33 ? 307 ASN A C   1 
ATOM   2172 O O   . ASN A 1 309 ? 87.609  48.719 45.035 1.00 24.00 ? 307 ASN A O   1 
ATOM   2173 C CB  . ASN A 1 309 ? 84.768  46.824 43.999 1.00 25.48 ? 307 ASN A CB  1 
ATOM   2174 C CG  . ASN A 1 309 ? 85.675  45.613 43.977 1.00 27.13 ? 307 ASN A CG  1 
ATOM   2175 O OD1 . ASN A 1 309 ? 86.925  45.691 44.013 1.00 29.42 ? 307 ASN A OD1 1 
ATOM   2176 N ND2 . ASN A 1 309 ? 85.049  44.456 43.894 1.00 31.32 ? 307 ASN A ND2 1 
ATOM   2177 N N   . GLN A 1 310 ? 85.994  47.875 46.395 1.00 22.41 ? 308 GLN A N   1 
ATOM   2178 C CA  . GLN A 1 310 ? 86.877  47.782 47.558 1.00 23.44 ? 308 GLN A CA  1 
ATOM   2179 C C   . GLN A 1 310 ? 87.473  49.163 47.827 1.00 25.70 ? 308 GLN A C   1 
ATOM   2180 O O   . GLN A 1 310 ? 88.678  49.227 48.096 1.00 28.22 ? 308 GLN A O   1 
ATOM   2181 C CB  . GLN A 1 310 ? 87.893  46.690 47.252 1.00 24.18 ? 308 GLN A CB  1 
ATOM   2182 C CG  . GLN A 1 310 ? 88.447  46.028 48.477 1.00 25.23 ? 308 GLN A CG  1 
ATOM   2183 C CD  . GLN A 1 310 ? 89.533  45.054 48.128 1.00 23.68 ? 308 GLN A CD  1 
ATOM   2184 O OE1 . GLN A 1 310 ? 90.722  45.401 48.100 1.00 25.71 ? 308 GLN A OE1 1 
ATOM   2185 N NE2 . GLN A 1 310 ? 89.137  43.819 47.933 1.00 22.65 ? 308 GLN A NE2 1 
ATOM   2186 N N   . ILE A 1 311 ? 86.650  50.220 47.755 1.00 24.91 ? 309 ILE A N   1 
ATOM   2187 C CA  . ILE A 1 311 ? 87.138  51.625 47.813 1.00 26.94 ? 309 ILE A CA  1 
ATOM   2188 C C   . ILE A 1 311 ? 87.042  52.125 49.250 1.00 30.12 ? 309 ILE A C   1 
ATOM   2189 O O   . ILE A 1 311 ? 85.963  52.096 49.812 1.00 28.13 ? 309 ILE A O   1 
ATOM   2190 C CB  . ILE A 1 311 ? 86.353  52.585 46.910 1.00 29.95 ? 309 ILE A CB  1 
ATOM   2191 C CG1 . ILE A 1 311 ? 86.326  52.126 45.447 1.00 27.95 ? 309 ILE A CG1 1 
ATOM   2192 C CG2 . ILE A 1 311 ? 86.946  53.978 47.056 1.00 33.31 ? 309 ILE A CG2 1 
ATOM   2193 C CD1 . ILE A 1 311 ? 85.298  52.801 44.598 1.00 30.65 ? 309 ILE A CD1 1 
ATOM   2194 N N   . PRO A 1 312 ? 88.138  52.648 49.829 1.00 33.16 ? 310 PRO A N   1 
ATOM   2195 C CA  . PRO A 1 312 ? 88.124  53.186 51.197 1.00 37.37 ? 310 PRO A CA  1 
ATOM   2196 C C   . PRO A 1 312 ? 87.198  54.403 51.326 1.00 41.10 ? 310 PRO A C   1 
ATOM   2197 O O   . PRO A 1 312 ? 87.126  55.208 50.380 1.00 36.64 ? 310 PRO A O   1 
ATOM   2198 C CB  . PRO A 1 312 ? 89.587  53.566 51.439 1.00 39.56 ? 310 PRO A CB  1 
ATOM   2199 C CG  . PRO A 1 312 ? 90.356  52.756 50.404 1.00 39.96 ? 310 PRO A CG  1 
ATOM   2200 C CD  . PRO A 1 312 ? 89.451  52.767 49.196 1.00 36.12 ? 310 PRO A CD  1 
ATOM   2201 N N   . ASN A 1 313 ? 86.494  54.513 52.457 1.00 42.89 ? 311 ASN A N   1 
ATOM   2202 C CA  . ASN A 1 313 ? 85.508  55.605 52.717 1.00 48.75 ? 311 ASN A CA  1 
ATOM   2203 C C   . ASN A 1 313 ? 86.079  56.990 52.399 1.00 43.19 ? 311 ASN A C   1 
ATOM   2204 O O   . ASN A 1 313 ? 85.360  57.782 51.748 1.00 47.25 ? 311 ASN A O   1 
ATOM   2205 C CB  . ASN A 1 313 ? 85.084  55.677 54.178 1.00 49.24 ? 311 ASN A CB  1 
ATOM   2206 C CG  . ASN A 1 313 ? 84.059  54.633 54.515 1.00 51.16 ? 311 ASN A CG  1 
ATOM   2207 O OD1 . ASN A 1 313 ? 83.373  54.119 53.627 1.00 46.70 ? 311 ASN A OD1 1 
ATOM   2208 N ND2 . ASN A 1 313 ? 83.966  54.328 55.798 1.00 52.71 ? 311 ASN A ND2 1 
ATOM   2209 N N   . SER A 1 314 ? 87.283  57.279 52.895 1.00 45.35 ? 312 SER A N   1 
ATOM   2210 C CA  . SER A 1 314 ? 88.008  58.563 52.702 1.00 50.33 ? 312 SER A CA  1 
ATOM   2211 C C   . SER A 1 314 ? 88.128  58.876 51.197 1.00 50.60 ? 312 SER A C   1 
ATOM   2212 O O   . SER A 1 314 ? 87.855  60.025 50.796 1.00 50.18 ? 312 SER A O   1 
ATOM   2213 C CB  . SER A 1 314 ? 89.348  58.511 53.385 1.00 49.67 ? 312 SER A CB  1 
ATOM   2214 O OG  . SER A 1 314 ? 89.956  57.256 53.151 1.00 58.23 ? 312 SER A OG  1 
ATOM   2215 N N   . THR A 1 315 ? 88.503  57.893 50.372 1.00 47.03 ? 313 THR A N   1 
ATOM   2216 C CA  . THR A 1 315 ? 88.568  58.071 48.897 1.00 42.95 ? 313 THR A CA  1 
ATOM   2217 C C   . THR A 1 315 ? 87.159  58.316 48.346 1.00 38.17 ? 313 THR A C   1 
ATOM   2218 O O   . THR A 1 315 ? 86.950  59.331 47.640 1.00 42.76 ? 313 THR A O   1 
ATOM   2219 C CB  . THR A 1 315 ? 89.203  56.854 48.222 1.00 44.15 ? 313 THR A CB  1 
ATOM   2220 O OG1 . THR A 1 315 ? 90.503  56.732 48.796 1.00 47.94 ? 313 THR A OG1 1 
ATOM   2221 C CG2 . THR A 1 315 ? 89.283  57.006 46.721 1.00 42.14 ? 313 THR A CG2 1 
ATOM   2222 N N   . TYR A 1 316 ? 86.227  57.410 48.648 1.00 34.16 ? 314 TYR A N   1 
ATOM   2223 C CA  . TYR A 1 316 ? 84.887  57.360 48.021 1.00 39.27 ? 314 TYR A CA  1 
ATOM   2224 C C   . TYR A 1 316 ? 84.177  58.700 48.198 1.00 43.30 ? 314 TYR A C   1 
ATOM   2225 O O   . TYR A 1 316 ? 83.544  59.193 47.246 1.00 46.32 ? 314 TYR A O   1 
ATOM   2226 C CB  . TYR A 1 316 ? 84.075  56.208 48.612 1.00 40.49 ? 314 TYR A CB  1 
ATOM   2227 C CG  . TYR A 1 316 ? 82.782  55.977 47.889 1.00 43.23 ? 314 TYR A CG  1 
ATOM   2228 C CD1 . TYR A 1 316 ? 82.783  55.595 46.553 1.00 48.48 ? 314 TYR A CD1 1 
ATOM   2229 C CD2 . TYR A 1 316 ? 81.571  56.140 48.528 1.00 43.18 ? 314 TYR A CD2 1 
ATOM   2230 C CE1 . TYR A 1 316 ? 81.606  55.375 45.860 1.00 48.20 ? 314 TYR A CE1 1 
ATOM   2231 C CE2 . TYR A 1 316 ? 80.382  55.940 47.849 1.00 51.07 ? 314 TYR A CE2 1 
ATOM   2232 C CZ  . TYR A 1 316 ? 80.400  55.555 46.516 1.00 53.52 ? 314 TYR A CZ  1 
ATOM   2233 O OH  . TYR A 1 316 ? 79.228  55.348 45.852 1.00 59.98 ? 314 TYR A OH  1 
ATOM   2234 N N   . PHE A 1 317 ? 84.291  59.290 49.386 1.00 46.73 ? 315 PHE A N   1 
ATOM   2235 C CA  . PHE A 1 317 ? 83.506  60.487 49.778 1.00 51.87 ? 315 PHE A CA  1 
ATOM   2236 C C   . PHE A 1 317 ? 84.272  61.745 49.371 1.00 49.07 ? 315 PHE A C   1 
ATOM   2237 O O   . PHE A 1 317 ? 83.675  62.829 49.492 1.00 60.77 ? 315 PHE A O   1 
ATOM   2238 C CB  . PHE A 1 317 ? 83.156  60.442 51.275 1.00 52.33 ? 315 PHE A CB  1 
ATOM   2239 C CG  . PHE A 1 317 ? 81.916  59.638 51.570 1.00 53.85 ? 315 PHE A CG  1 
ATOM   2240 C CD1 . PHE A 1 317 ? 80.659  60.180 51.353 1.00 60.04 ? 315 PHE A CD1 1 
ATOM   2241 C CD2 . PHE A 1 317 ? 82.003  58.328 52.019 1.00 54.34 ? 315 PHE A CD2 1 
ATOM   2242 C CE1 . PHE A 1 317 ? 79.519  59.431 51.595 1.00 63.08 ? 315 PHE A CE1 1 
ATOM   2243 C CE2 . PHE A 1 317 ? 80.864  57.577 52.247 1.00 57.80 ? 315 PHE A CE2 1 
ATOM   2244 C CZ  . PHE A 1 317 ? 79.624  58.129 52.034 1.00 63.74 ? 315 PHE A CZ  1 
ATOM   2245 N N   . SER A 1 318 ? 85.513  61.621 48.882 1.00 48.05 ? 316 SER A N   1 
ATOM   2246 C CA  . SER A 1 318 ? 86.386  62.788 48.568 1.00 49.18 ? 316 SER A CA  1 
ATOM   2247 C C   . SER A 1 318 ? 86.498  63.044 47.055 1.00 45.01 ? 316 SER A C   1 
ATOM   2248 O O   . SER A 1 318 ? 86.878  64.165 46.682 1.00 45.15 ? 316 SER A O   1 
ATOM   2249 C CB  . SER A 1 318 ? 87.747  62.634 49.191 1.00 49.74 ? 316 SER A CB  1 
ATOM   2250 O OG  . SER A 1 318 ? 88.491  61.622 48.523 1.00 54.20 ? 316 SER A OG  1 
ATOM   2251 N N   . VAL A 1 319 ? 86.209  62.063 46.198 1.00 40.39 ? 317 VAL A N   1 
ATOM   2252 C CA  . VAL A 1 319 ? 86.309  62.250 44.719 1.00 38.14 ? 317 VAL A CA  1 
ATOM   2253 C C   . VAL A 1 319 ? 85.223  63.216 44.240 1.00 37.11 ? 317 VAL A C   1 
ATOM   2254 O O   . VAL A 1 319 ? 84.156  63.299 44.871 1.00 33.22 ? 317 VAL A O   1 
ATOM   2255 C CB  . VAL A 1 319 ? 86.235  60.915 43.960 1.00 35.22 ? 317 VAL A CB  1 
ATOM   2256 C CG1 . VAL A 1 319 ? 87.472  60.072 44.221 1.00 38.30 ? 317 VAL A CG1 1 
ATOM   2257 C CG2 . VAL A 1 319 ? 84.963  60.162 44.278 1.00 33.60 ? 317 VAL A CG2 1 
ATOM   2258 N N   . GLN A 1 320 ? 85.471  63.895 43.120 1.00 40.54 ? 318 GLN A N   1 
ATOM   2259 C CA  . GLN A 1 320 ? 84.576  64.961 42.597 1.00 43.69 ? 318 GLN A CA  1 
ATOM   2260 C C   . GLN A 1 320 ? 83.286  64.282 42.125 1.00 42.18 ? 318 GLN A C   1 
ATOM   2261 O O   . GLN A 1 320 ? 82.195  64.716 42.511 1.00 37.54 ? 318 GLN A O   1 
ATOM   2262 C CB  . GLN A 1 320 ? 85.322  65.759 41.517 1.00 49.27 ? 318 GLN A CB  1 
ATOM   2263 C CG  . GLN A 1 320 ? 84.468  66.749 40.737 1.00 55.57 ? 318 GLN A CG  1 
ATOM   2264 C CD  . GLN A 1 320 ? 83.714  67.703 41.628 1.00 58.11 ? 318 GLN A CD  1 
ATOM   2265 O OE1 . GLN A 1 320 ? 84.077  67.919 42.783 1.00 67.96 ? 318 GLN A OE1 1 
ATOM   2266 N NE2 . GLN A 1 320 ? 82.649  68.291 41.095 1.00 55.12 ? 318 GLN A NE2 1 
ATOM   2267 N N   . SER A 1 321 ? 83.427  63.158 41.433 1.00 35.14 ? 319 SER A N   1 
ATOM   2268 C CA  . SER A 1 321 ? 82.310  62.348 40.907 1.00 31.15 ? 319 SER A CA  1 
ATOM   2269 C C   . SER A 1 321 ? 82.599  60.898 41.249 1.00 29.42 ? 319 SER A C   1 
ATOM   2270 O O   . SER A 1 321 ? 83.697  60.445 40.839 1.00 24.93 ? 319 SER A O   1 
ATOM   2271 C CB  . SER A 1 321 ? 82.199  62.534 39.406 1.00 32.28 ? 319 SER A CB  1 
ATOM   2272 O OG  . SER A 1 321 ? 81.378  61.541 38.831 1.00 31.91 ? 319 SER A OG  1 
ATOM   2273 N N   . GLN A 1 322 ? 81.663  60.241 41.932 1.00 27.48 ? 320 GLN A N   1 
ATOM   2274 C CA  . GLN A 1 322 ? 81.719  58.799 42.262 1.00 32.28 ? 320 GLN A CA  1 
ATOM   2275 C C   . GLN A 1 322 ? 81.621  57.968 40.983 1.00 31.25 ? 320 GLN A C   1 
ATOM   2276 O O   . GLN A 1 322 ? 82.089  56.830 41.007 1.00 29.58 ? 320 GLN A O   1 
ATOM   2277 C CB  . GLN A 1 322 ? 80.622  58.398 43.250 1.00 40.18 ? 320 GLN A CB  1 
ATOM   2278 C CG  . GLN A 1 322 ? 80.977  58.686 44.710 1.00 43.82 ? 320 GLN A CG  1 
ATOM   2279 C CD  . GLN A 1 322 ? 80.892  60.147 45.078 1.00 52.39 ? 320 GLN A CD  1 
ATOM   2280 O OE1 . GLN A 1 322 ? 80.092  60.913 44.524 1.00 57.12 ? 320 GLN A OE1 1 
ATOM   2281 N NE2 . GLN A 1 322 ? 81.747  60.565 46.006 1.00 58.09 ? 320 GLN A NE2 1 
ATOM   2282 N N   . LYS A 1 323 ? 81.019  58.514 39.923 1.00 31.27 ? 321 LYS A N   1 
ATOM   2283 C CA  . LYS A 1 323 ? 80.776  57.761 38.667 1.00 29.23 ? 321 LYS A CA  1 
ATOM   2284 C C   . LYS A 1 323 ? 82.009  57.791 37.756 1.00 29.85 ? 321 LYS A C   1 
ATOM   2285 O O   . LYS A 1 323 ? 81.959  57.148 36.697 1.00 31.63 ? 321 LYS A O   1 
ATOM   2286 C CB  . LYS A 1 323 ? 79.573  58.357 37.938 1.00 30.31 ? 321 LYS A CB  1 
ATOM   2287 C CG  . LYS A 1 323 ? 78.236  58.162 38.645 1.00 31.86 ? 321 LYS A CG  1 
ATOM   2288 C CD  . LYS A 1 323 ? 77.806  56.727 38.865 1.00 31.82 ? 321 LYS A CD  1 
ATOM   2289 C CE  . LYS A 1 323 ? 77.547  56.008 37.564 1.00 35.34 ? 321 LYS A CE  1 
ATOM   2290 N NZ  . LYS A 1 323 ? 76.870  54.704 37.763 1.00 34.06 ? 321 LYS A NZ  1 
ATOM   2291 N N   . ASP A 1 324 ? 83.025  58.581 38.090 1.00 26.91 ? 322 ASP A N   1 
ATOM   2292 C CA  . ASP A 1 324 ? 84.198  58.794 37.204 1.00 27.86 ? 322 ASP A CA  1 
ATOM   2293 C C   . ASP A 1 324 ? 85.285  57.773 37.555 1.00 26.42 ? 322 ASP A C   1 
ATOM   2294 O O   . ASP A 1 324 ? 85.934  57.921 38.585 1.00 23.43 ? 322 ASP A O   1 
ATOM   2295 C CB  . ASP A 1 324 ? 84.714  60.222 37.354 1.00 28.86 ? 322 ASP A CB  1 
ATOM   2296 C CG  . ASP A 1 324 ? 85.952  60.502 36.512 1.00 31.55 ? 322 ASP A CG  1 
ATOM   2297 O OD1 . ASP A 1 324 ? 86.258  59.643 35.674 1.00 31.97 ? 322 ASP A OD1 1 
ATOM   2298 O OD2 . ASP A 1 324 ? 86.570  61.571 36.700 1.00 30.66 ? 322 ASP A OD2 1 
ATOM   2299 N N   . PRO A 1 325 ? 85.557  56.717 36.744 1.00 27.32 ? 323 PRO A N   1 
ATOM   2300 C CA  . PRO A 1 325 ? 86.595  55.734 37.102 1.00 26.83 ? 323 PRO A CA  1 
ATOM   2301 C C   . PRO A 1 325 ? 87.962  56.400 37.245 1.00 27.88 ? 323 PRO A C   1 
ATOM   2302 O O   . PRO A 1 325 ? 88.722  55.989 38.073 1.00 28.55 ? 323 PRO A O   1 
ATOM   2303 C CB  . PRO A 1 325 ? 86.626  54.741 35.921 1.00 27.63 ? 323 PRO A CB  1 
ATOM   2304 C CG  . PRO A 1 325 ? 85.282  54.921 35.244 1.00 24.78 ? 323 PRO A CG  1 
ATOM   2305 C CD  . PRO A 1 325 ? 84.900  56.376 35.465 1.00 26.02 ? 323 PRO A CD  1 
ATOM   2306 N N   . LEU A 1 326 ? 88.220  57.463 36.477 1.00 25.60 ? 324 LEU A N   1 
ATOM   2307 C CA  . LEU A 1 326 ? 89.537  58.145 36.449 1.00 27.37 ? 324 LEU A CA  1 
ATOM   2308 C C   . LEU A 1 326 ? 89.779  58.876 37.779 1.00 25.34 ? 324 LEU A C   1 
ATOM   2309 O O   . LEU A 1 326 ? 90.945  59.167 38.088 1.00 26.67 ? 324 LEU A O   1 
ATOM   2310 C CB  . LEU A 1 326 ? 89.624  59.096 35.240 1.00 25.31 ? 324 LEU A CB  1 
ATOM   2311 C CG  . LEU A 1 326 ? 89.958  58.412 33.906 1.00 29.47 ? 324 LEU A CG  1 
ATOM   2312 C CD1 . LEU A 1 326 ? 88.793  57.596 33.365 1.00 30.66 ? 324 LEU A CD1 1 
ATOM   2313 C CD2 . LEU A 1 326 ? 90.376  59.440 32.874 1.00 27.68 ? 324 LEU A CD2 1 
ATOM   2314 N N   . ALA A 1 327 ? 88.743  59.095 38.578 1.00 26.44 ? 325 ALA A N   1 
ATOM   2315 C CA  . ALA A 1 327 ? 88.877  59.854 39.850 1.00 29.07 ? 325 ALA A CA  1 
ATOM   2316 C C   . ALA A 1 327 ? 89.612  59.032 40.918 1.00 26.64 ? 325 ALA A C   1 
ATOM   2317 O O   . ALA A 1 327 ? 90.106  59.638 41.851 1.00 24.51 ? 325 ALA A O   1 
ATOM   2318 C CB  . ALA A 1 327 ? 87.525  60.303 40.348 1.00 31.99 ? 325 ALA A CB  1 
ATOM   2319 N N   . TYR A 1 328 ? 89.717  57.717 40.747 1.00 26.31 ? 326 TYR A N   1 
ATOM   2320 C CA  . TYR A 1 328 ? 90.309  56.776 41.738 1.00 26.24 ? 326 TYR A CA  1 
ATOM   2321 C C   . TYR A 1 328 ? 91.793  56.526 41.426 1.00 28.17 ? 326 TYR A C   1 
ATOM   2322 O O   . TYR A 1 328 ? 92.466  55.842 42.225 1.00 29.81 ? 326 TYR A O   1 
ATOM   2323 C CB  . TYR A 1 328 ? 89.459  55.515 41.806 1.00 27.01 ? 326 TYR A CB  1 
ATOM   2324 C CG  . TYR A 1 328 ? 88.007  55.762 42.168 1.00 26.93 ? 326 TYR A CG  1 
ATOM   2325 C CD1 . TYR A 1 328 ? 87.620  55.996 43.471 1.00 30.95 ? 326 TYR A CD1 1 
ATOM   2326 C CD2 . TYR A 1 328 ? 87.011  55.767 41.206 1.00 30.03 ? 326 TYR A CD2 1 
ATOM   2327 C CE1 . TYR A 1 328 ? 86.299  56.244 43.812 1.00 28.80 ? 326 TYR A CE1 1 
ATOM   2328 C CE2 . TYR A 1 328 ? 85.675  55.986 41.532 1.00 30.81 ? 326 TYR A CE2 1 
ATOM   2329 C CZ  . TYR A 1 328 ? 85.312  56.224 42.847 1.00 32.68 ? 326 TYR A CZ  1 
ATOM   2330 O OH  . TYR A 1 328 ? 83.985  56.396 43.190 1.00 32.48 ? 326 TYR A OH  1 
ATOM   2331 N N   . LEU A 1 329 ? 92.320  57.133 40.354 1.00 26.02 ? 327 LEU A N   1 
ATOM   2332 C CA  . LEU A 1 329 ? 93.748  56.993 39.968 1.00 25.14 ? 327 LEU A CA  1 
ATOM   2333 C C   . LEU A 1 329 ? 94.630  57.802 40.909 1.00 26.11 ? 327 LEU A C   1 
ATOM   2334 O O   . LEU A 1 329 ? 94.178  58.782 41.490 1.00 26.35 ? 327 LEU A O   1 
ATOM   2335 C CB  . LEU A 1 329 ? 93.940  57.444 38.518 1.00 24.76 ? 327 LEU A CB  1 
ATOM   2336 C CG  . LEU A 1 329 ? 93.229  56.543 37.514 1.00 26.33 ? 327 LEU A CG  1 
ATOM   2337 C CD1 . LEU A 1 329 ? 93.157  57.233 36.177 1.00 25.37 ? 327 LEU A CD1 1 
ATOM   2338 C CD2 . LEU A 1 329 ? 93.916  55.177 37.418 1.00 28.40 ? 327 LEU A CD2 1 
ATOM   2339 N N   . PRO A 1 330 ? 95.926  57.459 41.007 1.00 25.90 ? 328 PRO A N   1 
ATOM   2340 C CA  . PRO A 1 330 ? 96.860  58.195 41.860 1.00 27.24 ? 328 PRO A CA  1 
ATOM   2341 C C   . PRO A 1 330 ? 96.957  59.668 41.447 1.00 29.64 ? 328 PRO A C   1 
ATOM   2342 O O   . PRO A 1 330 ? 96.891  59.982 40.256 1.00 27.69 ? 328 PRO A O   1 
ATOM   2343 C CB  . PRO A 1 330 ? 98.186  57.493 41.622 1.00 25.03 ? 328 PRO A CB  1 
ATOM   2344 C CG  . PRO A 1 330 ? 97.752  56.088 41.250 1.00 26.47 ? 328 PRO A CG  1 
ATOM   2345 C CD  . PRO A 1 330 ? 96.560  56.314 40.346 1.00 26.33 ? 328 PRO A CD  1 
ATOM   2346 N N   . GLU A 1 331 ? 97.172  60.529 42.439 1.00 29.76 ? 329 GLU A N   1 
ATOM   2347 C CA  . GLU A 1 331 ? 97.415  61.985 42.255 1.00 35.45 ? 329 GLU A CA  1 
ATOM   2348 C C   . GLU A 1 331 ? 98.539  62.190 41.228 1.00 27.66 ? 329 GLU A C   1 
ATOM   2349 O O   . GLU A 1 331 ? 99.623  61.644 41.413 1.00 28.31 ? 329 GLU A O   1 
ATOM   2350 C CB  . GLU A 1 331 ? 97.776  62.651 43.593 1.00 43.31 ? 329 GLU A CB  1 
ATOM   2351 C CG  . GLU A 1 331 ? 97.722  64.175 43.552 1.00 54.45 ? 329 GLU A CG  1 
ATOM   2352 C CD  . GLU A 1 331 ? 96.328  64.771 43.430 1.00 64.16 ? 329 GLU A CD  1 
ATOM   2353 O OE1 . GLU A 1 331 ? 95.582  64.764 44.441 1.00 69.75 ? 329 GLU A OE1 1 
ATOM   2354 O OE2 . GLU A 1 331 ? 95.981  65.249 42.321 1.00 75.12 ? 329 GLU A OE2 1 
ATOM   2355 N N   . GLY A 1 332 ? 98.272  62.972 40.187 1.00 29.97 ? 330 GLY A N   1 
ATOM   2356 C CA  . GLY A 1 332 ? 99.298  63.387 39.215 1.00 30.51 ? 330 GLY A CA  1 
ATOM   2357 C C   . GLY A 1 332 ? 99.509  62.358 38.110 1.00 31.78 ? 330 GLY A C   1 
ATOM   2358 O O   . GLY A 1 332 ? 100.161 62.707 37.150 1.00 27.75 ? 330 GLY A O   1 
ATOM   2359 N N   . PHE A 1 333 ? 99.005  61.125 38.233 1.00 27.77 ? 331 PHE A N   1 
ATOM   2360 C CA  . PHE A 1 333 ? 99.289  60.031 37.269 1.00 23.60 ? 331 PHE A CA  1 
ATOM   2361 C C   . PHE A 1 333 ? 98.849  60.426 35.856 1.00 22.45 ? 331 PHE A C   1 
ATOM   2362 O O   . PHE A 1 333 ? 99.648  60.238 34.883 1.00 25.04 ? 331 PHE A O   1 
ATOM   2363 C CB  . PHE A 1 333 ? 98.625  58.722 37.708 1.00 25.15 ? 331 PHE A CB  1 
ATOM   2364 C CG  . PHE A 1 333 ? 98.514  57.684 36.622 1.00 23.98 ? 331 PHE A CG  1 
ATOM   2365 C CD1 . PHE A 1 333 ? 99.605  56.918 36.252 1.00 23.77 ? 331 PHE A CD1 1 
ATOM   2366 C CD2 . PHE A 1 333 ? 97.289  57.433 36.025 1.00 26.26 ? 331 PHE A CD2 1 
ATOM   2367 C CE1 . PHE A 1 333 ? 99.483  55.943 35.270 1.00 24.64 ? 331 PHE A CE1 1 
ATOM   2368 C CE2 . PHE A 1 333 ? 97.171  56.489 35.013 1.00 26.20 ? 331 PHE A CE2 1 
ATOM   2369 C CZ  . PHE A 1 333 ? 98.263  55.731 34.653 1.00 24.75 ? 331 PHE A CZ  1 
ATOM   2370 N N   . LEU A 1 334 ? 97.638  60.955 35.713 1.00 22.45 ? 332 LEU A N   1 
ATOM   2371 C CA  . LEU A 1 334 ? 97.098  61.340 34.385 1.00 27.12 ? 332 LEU A CA  1 
ATOM   2372 C C   . LEU A 1 334 ? 97.932  62.503 33.831 1.00 27.84 ? 332 LEU A C   1 
ATOM   2373 O O   . LEU A 1 334 ? 98.207  62.523 32.633 1.00 29.45 ? 332 LEU A O   1 
ATOM   2374 C CB  . LEU A 1 334 ? 95.617  61.733 34.497 1.00 31.31 ? 332 LEU A CB  1 
ATOM   2375 C CG  . LEU A 1 334 ? 94.641  60.587 34.764 1.00 30.30 ? 332 LEU A CG  1 
ATOM   2376 C CD1 . LEU A 1 334 ? 93.240  61.107 35.002 1.00 31.68 ? 332 LEU A CD1 1 
ATOM   2377 C CD2 . LEU A 1 334 ? 94.625  59.595 33.623 1.00 33.68 ? 332 LEU A CD2 1 
ATOM   2378 N N   . ASN A 1 335 ? 98.323  63.458 34.670 1.00 31.77 ? 333 ASN A N   1 
ATOM   2379 C CA  . ASN A 1 335 ? 99.107  64.632 34.194 1.00 30.30 ? 333 ASN A CA  1 
ATOM   2380 C C   . ASN A 1 335 ? 100.489 64.149 33.749 1.00 30.69 ? 333 ASN A C   1 
ATOM   2381 O O   . ASN A 1 335 ? 100.910 64.518 32.649 1.00 30.06 ? 333 ASN A O   1 
ATOM   2382 C CB  . ASN A 1 335 ? 99.181  65.737 35.245 1.00 35.79 ? 333 ASN A CB  1 
ATOM   2383 C CG  . ASN A 1 335 ? 97.837  66.385 35.515 1.00 41.88 ? 333 ASN A CG  1 
ATOM   2384 O OD1 . ASN A 1 335 ? 96.979  66.480 34.648 1.00 47.27 ? 333 ASN A OD1 1 
ATOM   2385 N ND2 . ASN A 1 335 ? 97.623  66.822 36.739 1.00 48.45 ? 333 ASN A ND2 1 
ATOM   2386 N N   . ARG A 1 336 ? 101.150 63.314 34.542 1.00 27.28 ? 334 ARG A N   1 
ATOM   2387 C CA  . ARG A 1 336 ? 102.543 62.864 34.277 1.00 28.13 ? 334 ARG A CA  1 
ATOM   2388 C C   . ARG A 1 336 ? 102.581 61.972 33.026 1.00 29.64 ? 334 ARG A C   1 
ATOM   2389 O O   . ARG A 1 336 ? 103.575 62.104 32.332 1.00 26.99 ? 334 ARG A O   1 
ATOM   2390 C CB  . ARG A 1 336 ? 103.143 62.096 35.447 1.00 28.88 ? 334 ARG A CB  1 
ATOM   2391 C CG  . ARG A 1 336 ? 103.306 62.947 36.707 1.00 31.38 ? 334 ARG A CG  1 
ATOM   2392 C CD  . ARG A 1 336 ? 104.183 62.264 37.741 1.00 31.16 ? 334 ARG A CD  1 
ATOM   2393 N NE  . ARG A 1 336 ? 103.571 61.016 38.164 1.00 32.06 ? 334 ARG A NE  1 
ATOM   2394 C CZ  . ARG A 1 336 ? 102.672 60.879 39.142 1.00 32.60 ? 334 ARG A CZ  1 
ATOM   2395 N NH1 . ARG A 1 336 ? 102.290 61.923 39.859 1.00 31.87 ? 334 ARG A NH1 1 
ATOM   2396 N NH2 . ARG A 1 336 ? 102.156 59.689 39.397 1.00 28.88 ? 334 ARG A NH2 1 
ATOM   2397 N N   . THR A 1 337 ? 101.518 61.206 32.708 1.00 23.71 ? 335 THR A N   1 
ATOM   2398 C CA  . THR A 1 337 ? 101.543 60.189 31.615 1.00 22.76 ? 335 THR A CA  1 
ATOM   2399 C C   . THR A 1 337 ? 100.839 60.699 30.373 1.00 24.63 ? 335 THR A C   1 
ATOM   2400 O O   . THR A 1 337 ? 100.665 59.908 29.433 1.00 24.88 ? 335 THR A O   1 
ATOM   2401 C CB  . THR A 1 337 ? 100.954 58.845 32.056 1.00 23.89 ? 335 THR A CB  1 
ATOM   2402 O OG1 . THR A 1 337 ? 99.592  58.990 32.453 1.00 23.13 ? 335 THR A OG1 1 
ATOM   2403 C CG2 . THR A 1 337 ? 101.752 58.266 33.193 1.00 23.77 ? 335 THR A CG2 1 
ATOM   2404 N N   . GLU A 1 338 ? 100.386 61.945 30.367 1.00 26.13 ? 336 GLU A N   1 
ATOM   2405 C CA  . GLU A 1 338 ? 99.430  62.370 29.320 1.00 29.30 ? 336 GLU A CA  1 
ATOM   2406 C C   . GLU A 1 338 ? 100.135 62.350 27.958 1.00 26.32 ? 336 GLU A C   1 
ATOM   2407 O O   . GLU A 1 338 ? 99.453  62.178 26.979 1.00 27.31 ? 336 GLU A O   1 
ATOM   2408 C CB  . GLU A 1 338 ? 98.830  63.744 29.603 1.00 36.92 ? 336 GLU A CB  1 
ATOM   2409 C CG  . GLU A 1 338 ? 99.805  64.878 29.478 1.00 38.83 ? 336 GLU A CG  1 
ATOM   2410 C CD  . GLU A 1 338 ? 99.138  66.224 29.706 1.00 54.71 ? 336 GLU A CD  1 
ATOM   2411 O OE1 . GLU A 1 338 ? 98.427  66.689 28.772 1.00 61.18 ? 336 GLU A OE1 1 
ATOM   2412 O OE2 . GLU A 1 338 ? 99.314  66.792 30.812 1.00 58.87 ? 336 GLU A OE2 1 
ATOM   2413 N N   . GLY A 1 339 ? 101.450 62.440 27.899 1.00 25.98 ? 337 GLY A N   1 
ATOM   2414 C CA  . GLY A 1 339 ? 102.153 62.332 26.600 1.00 28.82 ? 337 GLY A CA  1 
ATOM   2415 C C   . GLY A 1 339 ? 102.200 60.921 26.035 1.00 31.67 ? 337 GLY A C   1 
ATOM   2416 O O   . GLY A 1 339 ? 102.335 60.790 24.810 1.00 38.46 ? 337 GLY A O   1 
ATOM   2417 N N   . ARG A 1 340 ? 102.163 59.868 26.847 1.00 26.57 ? 338 ARG A N   1 
ATOM   2418 C CA  . ARG A 1 340 ? 102.373 58.489 26.336 1.00 24.86 ? 338 ARG A CA  1 
ATOM   2419 C C   . ARG A 1 340 ? 101.194 57.567 26.677 1.00 23.92 ? 338 ARG A C   1 
ATOM   2420 O O   . ARG A 1 340 ? 101.189 56.415 26.191 1.00 24.42 ? 338 ARG A O   1 
ATOM   2421 C CB  . ARG A 1 340 ? 103.659 57.929 26.924 1.00 23.78 ? 338 ARG A CB  1 
ATOM   2422 C CG  . ARG A 1 340 ? 103.569 57.702 28.422 1.00 23.23 ? 338 ARG A CG  1 
ATOM   2423 C CD  . ARG A 1 340 ? 104.951 57.450 28.966 1.00 23.48 ? 338 ARG A CD  1 
ATOM   2424 N NE  . ARG A 1 340 ? 105.084 57.116 30.373 1.00 25.22 ? 338 ARG A NE  1 
ATOM   2425 C CZ  . ARG A 1 340 ? 105.359 57.980 31.340 1.00 27.97 ? 338 ARG A CZ  1 
ATOM   2426 N NH1 . ARG A 1 340 ? 105.445 59.270 31.082 1.00 29.04 ? 338 ARG A NH1 1 
ATOM   2427 N NH2 . ARG A 1 340 ? 105.558 57.557 32.578 1.00 28.18 ? 338 ARG A NH2 1 
ATOM   2428 N N   . GLY A 1 341 ? 100.255 58.018 27.515 1.00 24.17 ? 339 GLY A N   1 
ATOM   2429 C CA  . GLY A 1 341 ? 99.136  57.177 27.956 1.00 27.01 ? 339 GLY A CA  1 
ATOM   2430 C C   . GLY A 1 341 ? 97.804  57.850 27.710 1.00 28.56 ? 339 GLY A C   1 
ATOM   2431 O O   . GLY A 1 341 ? 97.650  59.009 28.110 1.00 28.76 ? 339 GLY A O   1 
ATOM   2432 N N   . LEU A 1 342 ? 96.868  57.137 27.110 1.00 24.19 ? 340 LEU A N   1 
ATOM   2433 C CA  . LEU A 1 342 ? 95.469  57.590 26.949 1.00 23.31 ? 340 LEU A CA  1 
ATOM   2434 C C   . LEU A 1 342 ? 94.623  56.720 27.881 1.00 23.83 ? 340 LEU A C   1 
ATOM   2435 O O   . LEU A 1 342 ? 94.617  55.455 27.711 1.00 20.48 ? 340 LEU A O   1 
ATOM   2436 C CB  . LEU A 1 342 ? 95.000  57.506 25.497 1.00 25.74 ? 340 LEU A CB  1 
ATOM   2437 C CG  . LEU A 1 342 ? 93.511  57.806 25.287 1.00 27.29 ? 340 LEU A CG  1 
ATOM   2438 C CD1 . LEU A 1 342 ? 93.191  59.255 25.632 1.00 34.63 ? 340 LEU A CD1 1 
ATOM   2439 C CD2 . LEU A 1 342 ? 93.088  57.507 23.858 1.00 30.66 ? 340 LEU A CD2 1 
ATOM   2440 N N   . VAL A 1 343 ? 93.970  57.355 28.852 1.00 24.11 ? 341 VAL A N   1 
ATOM   2441 C CA  . VAL A 1 343 ? 93.059  56.661 29.810 1.00 23.35 ? 341 VAL A CA  1 
ATOM   2442 C C   . VAL A 1 343 ? 91.617  57.049 29.481 1.00 26.50 ? 341 VAL A C   1 
ATOM   2443 O O   . VAL A 1 343 ? 91.287  58.261 29.486 1.00 23.50 ? 341 VAL A O   1 
ATOM   2444 C CB  . VAL A 1 343 ? 93.474  56.937 31.269 1.00 23.95 ? 341 VAL A CB  1 
ATOM   2445 C CG1 . VAL A 1 343 ? 92.579  56.178 32.241 1.00 22.94 ? 341 VAL A CG1 1 
ATOM   2446 C CG2 . VAL A 1 343 ? 94.952  56.590 31.484 1.00 24.99 ? 341 VAL A CG2 1 
ATOM   2447 N N   . VAL A 1 344 ? 90.787  56.064 29.145 1.00 25.11 ? 342 VAL A N   1 
ATOM   2448 C CA  . VAL A 1 344 ? 89.363  56.344 28.790 1.00 25.21 ? 342 VAL A CA  1 
ATOM   2449 C C   . VAL A 1 344 ? 88.445  55.542 29.694 1.00 24.35 ? 342 VAL A C   1 
ATOM   2450 O O   . VAL A 1 344 ? 88.785  54.419 30.084 1.00 24.56 ? 342 VAL A O   1 
ATOM   2451 C CB  . VAL A 1 344 ? 89.050  56.085 27.315 1.00 27.79 ? 342 VAL A CB  1 
ATOM   2452 C CG1 . VAL A 1 344 ? 90.009  56.900 26.442 1.00 31.91 ? 342 VAL A CG1 1 
ATOM   2453 C CG2 . VAL A 1 344 ? 89.086  54.622 26.957 1.00 24.95 ? 342 VAL A CG2 1 
ATOM   2454 N N   . SER A 1 345 ? 87.303  56.153 29.969 1.00 25.07 ? 343 SER A N   1 
ATOM   2455 C CA  . SER A 1 345 ? 86.221  55.603 30.791 1.00 25.00 ? 343 SER A CA  1 
ATOM   2456 C C   . SER A 1 345 ? 85.446  54.515 30.064 1.00 23.10 ? 343 SER A C   1 
ATOM   2457 O O   . SER A 1 345 ? 84.861  54.773 29.010 1.00 24.36 ? 343 SER A O   1 
ATOM   2458 C CB  . SER A 1 345 ? 85.336  56.725 31.298 1.00 26.48 ? 343 SER A CB  1 
ATOM   2459 O OG  . SER A 1 345 ? 84.286  56.136 32.030 1.00 32.84 ? 343 SER A OG  1 
ATOM   2460 N N   . ASN A 1 346 ? 85.493  53.304 30.602 1.00 21.86 ? 344 ASN A N   1 
ATOM   2461 C CA  . ASN A 1 346 ? 84.507  52.214 30.404 1.00 22.24 ? 344 ASN A CA  1 
ATOM   2462 C C   . ASN A 1 346 ? 84.597  51.572 29.023 1.00 21.84 ? 344 ASN A C   1 
ATOM   2463 O O   . ASN A 1 346 ? 84.285  50.404 28.937 1.00 24.35 ? 344 ASN A O   1 
ATOM   2464 C CB  . ASN A 1 346 ? 83.062  52.696 30.574 1.00 25.71 ? 344 ASN A CB  1 
ATOM   2465 C CG  . ASN A 1 346 ? 82.588  52.589 32.005 1.00 34.92 ? 344 ASN A CG  1 
ATOM   2466 O OD1 . ASN A 1 346 ? 82.167  51.508 32.428 1.00 36.08 ? 344 ASN A OD1 1 
ATOM   2467 N ND2 . ASN A 1 346 ? 82.693  53.690 32.746 1.00 35.79 ? 344 ASN A ND2 1 
ATOM   2468 N N   . TRP A 1 347 ? 84.897  52.310 27.955 1.00 25.70 ? 345 TRP A N   1 
ATOM   2469 C CA  . TRP A 1 347 ? 84.823  51.704 26.596 1.00 26.66 ? 345 TRP A CA  1 
ATOM   2470 C C   . TRP A 1 347 ? 85.894  52.259 25.648 1.00 25.39 ? 345 TRP A C   1 
ATOM   2471 O O   . TRP A 1 347 ? 86.224  53.457 25.737 1.00 26.26 ? 345 TRP A O   1 
ATOM   2472 C CB  . TRP A 1 347 ? 83.431  51.933 26.000 1.00 27.11 ? 345 TRP A CB  1 
ATOM   2473 C CG  . TRP A 1 347 ? 83.294  51.456 24.583 1.00 25.88 ? 345 TRP A CG  1 
ATOM   2474 C CD1 . TRP A 1 347 ? 82.872  50.228 24.183 1.00 28.17 ? 345 TRP A CD1 1 
ATOM   2475 C CD2 . TRP A 1 347 ? 83.491  52.229 23.387 1.00 26.24 ? 345 TRP A CD2 1 
ATOM   2476 N NE1 . TRP A 1 347 ? 82.832  50.173 22.807 1.00 28.96 ? 345 TRP A NE1 1 
ATOM   2477 C CE2 . TRP A 1 347 ? 83.220  51.383 22.298 1.00 27.72 ? 345 TRP A CE2 1 
ATOM   2478 C CE3 . TRP A 1 347 ? 83.933  53.534 23.126 1.00 28.29 ? 345 TRP A CE3 1 
ATOM   2479 C CZ2 . TRP A 1 347 ? 83.325  51.821 20.984 1.00 29.34 ? 345 TRP A CZ2 1 
ATOM   2480 C CZ3 . TRP A 1 347 ? 84.065  53.957 21.828 1.00 31.38 ? 345 TRP A CZ3 1 
ATOM   2481 C CH2 . TRP A 1 347 ? 83.741  53.116 20.768 1.00 27.71 ? 345 TRP A CH2 1 
ATOM   2482 N N   . ALA A 1 348 ? 86.381  51.384 24.764 1.00 28.38 ? 346 ALA A N   1 
ATOM   2483 C CA  . ALA A 1 348 ? 87.120  51.742 23.537 1.00 24.66 ? 346 ALA A CA  1 
ATOM   2484 C C   . ALA A 1 348 ? 86.766  50.719 22.460 1.00 26.85 ? 346 ALA A C   1 
ATOM   2485 O O   . ALA A 1 348 ? 86.249  49.640 22.754 1.00 25.21 ? 346 ALA A O   1 
ATOM   2486 C CB  . ALA A 1 348 ? 88.617  51.825 23.819 1.00 25.29 ? 346 ALA A CB  1 
ATOM   2487 N N   . PRO A 1 349 ? 86.927  51.082 21.177 1.00 24.33 ? 347 PRO A N   1 
ATOM   2488 C CA  . PRO A 1 349 ? 86.595  50.172 20.070 1.00 25.81 ? 347 PRO A CA  1 
ATOM   2489 C C   . PRO A 1 349 ? 87.673  49.092 19.925 1.00 27.04 ? 347 PRO A C   1 
ATOM   2490 O O   . PRO A 1 349 ? 88.618  49.300 19.191 1.00 27.64 ? 347 PRO A O   1 
ATOM   2491 C CB  . PRO A 1 349 ? 86.511  51.153 18.886 1.00 25.51 ? 347 PRO A CB  1 
ATOM   2492 C CG  . PRO A 1 349 ? 87.529  52.228 19.247 1.00 25.78 ? 347 PRO A CG  1 
ATOM   2493 C CD  . PRO A 1 349 ? 87.329  52.420 20.730 1.00 26.04 ? 347 PRO A CD  1 
ATOM   2494 N N   . GLN A 1 350 ? 87.501  47.992 20.672 1.00 26.83 ? 348 GLN A N   1 
ATOM   2495 C CA  . GLN A 1 350 ? 88.492  46.919 20.903 1.00 26.88 ? 348 GLN A CA  1 
ATOM   2496 C C   . GLN A 1 350 ? 88.968  46.313 19.572 1.00 27.02 ? 348 GLN A C   1 
ATOM   2497 O O   . GLN A 1 350 ? 90.219  46.163 19.402 1.00 24.45 ? 348 GLN A O   1 
ATOM   2498 C CB  . GLN A 1 350 ? 87.897  45.844 21.804 1.00 28.05 ? 348 GLN A CB  1 
ATOM   2499 C CG  . GLN A 1 350 ? 88.880  44.751 22.156 1.00 27.91 ? 348 GLN A CG  1 
ATOM   2500 C CD  . GLN A 1 350 ? 88.275  43.625 22.963 1.00 31.90 ? 348 GLN A CD  1 
ATOM   2501 O OE1 . GLN A 1 350 ? 87.553  42.779 22.441 1.00 36.95 ? 348 GLN A OE1 1 
ATOM   2502 N NE2 . GLN A 1 350 ? 88.592  43.595 24.242 1.00 29.65 ? 348 GLN A NE2 1 
ATOM   2503 N N   . ALA A 1 351 ? 88.063  45.948 18.661 1.00 30.73 ? 349 ALA A N   1 
ATOM   2504 C CA  . ALA A 1 351 ? 88.430  45.321 17.362 1.00 30.67 ? 349 ALA A CA  1 
ATOM   2505 C C   . ALA A 1 351 ? 89.252  46.306 16.525 1.00 32.29 ? 349 ALA A C   1 
ATOM   2506 O O   . ALA A 1 351 ? 90.327  45.910 16.021 1.00 30.62 ? 349 ALA A O   1 
ATOM   2507 C CB  . ALA A 1 351 ? 87.204  44.845 16.618 1.00 33.92 ? 349 ALA A CB  1 
ATOM   2508 N N   . GLN A 1 352 ? 88.788  47.550 16.386 1.00 27.73 ? 350 GLN A N   1 
ATOM   2509 C CA  . GLN A 1 352 ? 89.520  48.605 15.652 1.00 30.02 ? 350 GLN A CA  1 
ATOM   2510 C C   . GLN A 1 352 ? 90.904  48.858 16.281 1.00 26.67 ? 350 GLN A C   1 
ATOM   2511 O O   . GLN A 1 352 ? 91.861  48.999 15.533 1.00 27.77 ? 350 GLN A O   1 
ATOM   2512 C CB  . GLN A 1 352 ? 88.664  49.866 15.549 1.00 35.48 ? 350 GLN A CB  1 
ATOM   2513 C CG  . GLN A 1 352 ? 89.146  50.786 14.439 1.00 45.73 ? 350 GLN A CG  1 
ATOM   2514 C CD  . GLN A 1 352 ? 88.247  51.981 14.228 1.00 46.09 ? 350 GLN A CD  1 
ATOM   2515 O OE1 . GLN A 1 352 ? 87.166  52.059 14.807 1.00 43.58 ? 350 GLN A OE1 1 
ATOM   2516 N NE2 . GLN A 1 352 ? 88.716  52.926 13.421 1.00 44.37 ? 350 GLN A NE2 1 
ATOM   2517 N N   . ILE A 1 353 ? 91.046  48.868 17.606 1.00 22.49 ? 351 ILE A N   1 
ATOM   2518 C CA  . ILE A 1 353 ? 92.360  49.119 18.269 1.00 25.42 ? 351 ILE A CA  1 
ATOM   2519 C C   . ILE A 1 353 ? 93.289  47.943 17.964 1.00 20.99 ? 351 ILE A C   1 
ATOM   2520 O O   . ILE A 1 353 ? 94.493  48.137 17.654 1.00 25.70 ? 351 ILE A O   1 
ATOM   2521 C CB  . ILE A 1 353 ? 92.186  49.264 19.794 1.00 25.68 ? 351 ILE A CB  1 
ATOM   2522 C CG1 . ILE A 1 353 ? 91.322  50.462 20.199 1.00 32.82 ? 351 ILE A CG1 1 
ATOM   2523 C CG2 . ILE A 1 353 ? 93.548  49.282 20.486 1.00 28.32 ? 351 ILE A CG2 1 
ATOM   2524 C CD1 . ILE A 1 353 ? 91.812  51.739 19.696 1.00 39.49 ? 351 ILE A CD1 1 
ATOM   2525 N N   . LEU A 1 354 ? 92.785  46.743 18.133 1.00 21.28 ? 352 LEU A N   1 
ATOM   2526 C CA  . LEU A 1 354 ? 93.635  45.548 17.908 1.00 22.13 ? 352 LEU A CA  1 
ATOM   2527 C C   . LEU A 1 354 ? 94.065  45.474 16.443 1.00 22.37 ? 352 LEU A C   1 
ATOM   2528 O O   . LEU A 1 354 ? 95.136  44.923 16.203 1.00 21.46 ? 352 LEU A O   1 
ATOM   2529 C CB  . LEU A 1 354 ? 92.907  44.293 18.370 1.00 23.32 ? 352 LEU A CB  1 
ATOM   2530 C CG  . LEU A 1 354 ? 92.900  44.058 19.882 1.00 21.56 ? 352 LEU A CG  1 
ATOM   2531 C CD1 . LEU A 1 354 ? 91.927  42.944 20.213 1.00 21.65 ? 352 LEU A CD1 1 
ATOM   2532 C CD2 . LEU A 1 354 ? 94.274  43.734 20.435 1.00 21.41 ? 352 LEU A CD2 1 
ATOM   2533 N N   . SER A 1 355 ? 93.300  46.043 15.514 1.00 24.06 ? 353 SER A N   1 
ATOM   2534 C CA  . SER A 1 355 ? 93.677  46.083 14.069 1.00 28.83 ? 353 SER A CA  1 
ATOM   2535 C C   . SER A 1 355 ? 94.709  47.168 13.772 1.00 28.23 ? 353 SER A C   1 
ATOM   2536 O O   . SER A 1 355 ? 95.214  47.180 12.645 1.00 29.49 ? 353 SER A O   1 
ATOM   2537 C CB  . SER A 1 355 ? 92.474  46.321 13.192 1.00 28.39 ? 353 SER A CB  1 
ATOM   2538 O OG  . SER A 1 355 ? 91.558  45.265 13.390 1.00 39.30 ? 353 SER A OG  1 
ATOM   2539 N N   . HIS A 1 356 ? 94.893  48.128 14.667 1.00 25.23 ? 354 HIS A N   1 
ATOM   2540 C CA  . HIS A 1 356 ? 95.730  49.315 14.398 1.00 26.66 ? 354 HIS A CA  1 
ATOM   2541 C C   . HIS A 1 356 ? 97.217  48.924 14.488 1.00 26.56 ? 354 HIS A C   1 
ATOM   2542 O O   . HIS A 1 356 ? 97.609  48.217 15.434 1.00 25.61 ? 354 HIS A O   1 
ATOM   2543 C CB  . HIS A 1 356 ? 95.319  50.426 15.354 1.00 28.50 ? 354 HIS A CB  1 
ATOM   2544 C CG  . HIS A 1 356 ? 95.813  51.774 14.955 1.00 27.71 ? 354 HIS A CG  1 
ATOM   2545 N ND1 . HIS A 1 356 ? 97.160  52.080 14.929 1.00 26.94 ? 354 HIS A ND1 1 
ATOM   2546 C CD2 . HIS A 1 356 ? 95.136  52.877 14.544 1.00 31.12 ? 354 HIS A CD2 1 
ATOM   2547 C CE1 . HIS A 1 356 ? 97.294  53.334 14.497 1.00 31.31 ? 354 HIS A CE1 1 
ATOM   2548 N NE2 . HIS A 1 356 ? 96.038  53.866 14.306 1.00 26.82 ? 354 HIS A NE2 1 
ATOM   2549 N N   . GLY A 1 357 ? 98.046  49.397 13.562 1.00 25.31 ? 355 GLY A N   1 
ATOM   2550 C CA  . GLY A 1 357 ? 99.492  49.048 13.551 1.00 27.24 ? 355 GLY A CA  1 
ATOM   2551 C C   . GLY A 1 357 ? 100.224 49.583 14.789 1.00 25.34 ? 355 GLY A C   1 
ATOM   2552 O O   . GLY A 1 357 ? 101.272 49.054 15.130 1.00 23.72 ? 355 GLY A O   1 
ATOM   2553 N N   . SER A 1 358 ? 99.680  50.590 15.476 1.00 23.88 ? 356 SER A N   1 
ATOM   2554 C CA  . SER A 1 358 ? 100.345 51.199 16.662 1.00 23.57 ? 356 SER A CA  1 
ATOM   2555 C C   . SER A 1 358 ? 100.211 50.326 17.922 1.00 22.17 ? 356 SER A C   1 
ATOM   2556 O O   . SER A 1 358 ? 100.962 50.584 18.905 1.00 24.14 ? 356 SER A O   1 
ATOM   2557 C CB  . SER A 1 358 ? 99.826  52.577 16.888 1.00 25.78 ? 356 SER A CB  1 
ATOM   2558 O OG  . SER A 1 358 ? 100.106 53.386 15.741 1.00 28.40 ? 356 SER A OG  1 
ATOM   2559 N N   . THR A 1 359 ? 99.300  49.353 17.898 1.00 21.50 ? 357 THR A N   1 
ATOM   2560 C CA  . THR A 1 359 ? 99.027  48.432 19.024 1.00 23.46 ? 357 THR A CA  1 
ATOM   2561 C C   . THR A 1 359 ? 100.082 47.335 19.059 1.00 25.65 ? 357 THR A C   1 
ATOM   2562 O O   . THR A 1 359 ? 100.153 46.594 18.072 1.00 25.80 ? 357 THR A O   1 
ATOM   2563 C CB  . THR A 1 359 ? 97.610  47.870 18.938 1.00 23.66 ? 357 THR A CB  1 
ATOM   2564 O OG1 . THR A 1 359 ? 96.692  48.970 18.948 1.00 23.21 ? 357 THR A OG1 1 
ATOM   2565 C CG2 . THR A 1 359 ? 97.326  46.899 20.073 1.00 20.80 ? 357 THR A CG2 1 
ATOM   2566 N N   . GLY A 1 360 ? 100.900 47.260 20.115 1.00 23.14 ? 358 GLY A N   1 
ATOM   2567 C CA  . GLY A 1 360 ? 101.918 46.199 20.220 1.00 24.28 ? 358 GLY A CA  1 
ATOM   2568 C C   . GLY A 1 360 ? 101.613 45.157 21.288 1.00 23.46 ? 358 GLY A C   1 
ATOM   2569 O O   . GLY A 1 360 ? 102.281 44.150 21.314 1.00 23.82 ? 358 GLY A O   1 
ATOM   2570 N N   . GLY A 1 361 ? 100.627 45.389 22.144 1.00 20.93 ? 359 GLY A N   1 
ATOM   2571 C CA  . GLY A 1 361 ? 100.275 44.473 23.237 1.00 20.33 ? 359 GLY A CA  1 
ATOM   2572 C C   . GLY A 1 361 ? 98.833  44.595 23.660 1.00 19.99 ? 359 GLY A C   1 
ATOM   2573 O O   . GLY A 1 361 ? 98.219  45.683 23.465 1.00 20.23 ? 359 GLY A O   1 
ATOM   2574 N N   . PHE A 1 362 ? 98.301  43.515 24.228 1.00 18.95 ? 360 PHE A N   1 
ATOM   2575 C CA  . PHE A 1 362 ? 96.910  43.466 24.736 1.00 19.69 ? 360 PHE A CA  1 
ATOM   2576 C C   . PHE A 1 362 ? 96.853  42.868 26.142 1.00 19.68 ? 360 PHE A C   1 
ATOM   2577 O O   . PHE A 1 362 ? 97.093  41.663 26.321 1.00 20.74 ? 360 PHE A O   1 
ATOM   2578 C CB  . PHE A 1 362 ? 96.101  42.622 23.765 1.00 20.33 ? 360 PHE A CB  1 
ATOM   2579 C CG  . PHE A 1 362 ? 94.635  42.531 24.015 1.00 18.99 ? 360 PHE A CG  1 
ATOM   2580 C CD1 . PHE A 1 362 ? 93.841  43.666 23.977 1.00 22.66 ? 360 PHE A CD1 1 
ATOM   2581 C CD2 . PHE A 1 362 ? 94.036  41.283 24.196 1.00 20.22 ? 360 PHE A CD2 1 
ATOM   2582 C CE1 . PHE A 1 362 ? 92.459  43.562 24.125 1.00 24.71 ? 360 PHE A CE1 1 
ATOM   2583 C CE2 . PHE A 1 362 ? 92.665  41.182 24.323 1.00 19.89 ? 360 PHE A CE2 1 
ATOM   2584 C CZ  . PHE A 1 362 ? 91.876  42.325 24.299 1.00 23.40 ? 360 PHE A CZ  1 
ATOM   2585 N N   . MET A 1 363 ? 96.545  43.690 27.120 1.00 19.51 ? 361 MET A N   1 
ATOM   2586 C CA  . MET A 1 363 ? 96.358  43.250 28.523 1.00 20.76 ? 361 MET A CA  1 
ATOM   2587 C C   . MET A 1 363 ? 94.848  43.118 28.742 1.00 20.71 ? 361 MET A C   1 
ATOM   2588 O O   . MET A 1 363 ? 94.122  44.111 28.522 1.00 19.65 ? 361 MET A O   1 
ATOM   2589 C CB  . MET A 1 363 ? 96.956  44.255 29.519 1.00 21.73 ? 361 MET A CB  1 
ATOM   2590 C CG  . MET A 1 363 ? 96.886  43.801 30.965 1.00 24.97 ? 361 MET A CG  1 
ATOM   2591 S SD  . MET A 1 363 ? 97.619  45.040 32.148 1.00 31.79 ? 361 MET A SD  1 
ATOM   2592 C CE  . MET A 1 363 ? 99.216  44.322 31.974 1.00 23.05 ? 361 MET A CE  1 
ATOM   2593 N N   . SER A 1 364 ? 94.384  41.913 29.102 1.00 21.26 ? 362 SER A N   1 
ATOM   2594 C CA  . SER A 1 364 ? 92.949  41.540 29.103 1.00 22.29 ? 362 SER A CA  1 
ATOM   2595 C C   . SER A 1 364 ? 92.628  40.663 30.308 1.00 20.61 ? 362 SER A C   1 
ATOM   2596 O O   . SER A 1 364 ? 93.532  39.905 30.713 1.00 20.87 ? 362 SER A O   1 
ATOM   2597 C CB  . SER A 1 364 ? 92.679  40.827 27.793 1.00 25.45 ? 362 SER A CB  1 
ATOM   2598 O OG  . SER A 1 364 ? 91.478  40.121 27.814 1.00 24.78 ? 362 SER A OG  1 
ATOM   2599 N N   . HIS A 1 365 ? 91.360  40.630 30.741 1.00 20.64 ? 363 HIS A N   1 
ATOM   2600 C CA  . HIS A 1 365 ? 90.909  39.687 31.799 1.00 21.14 ? 363 HIS A CA  1 
ATOM   2601 C C   . HIS A 1 365 ? 90.710  38.286 31.190 1.00 20.50 ? 363 HIS A C   1 
ATOM   2602 O O   . HIS A 1 365 ? 90.432  37.373 31.946 1.00 20.38 ? 363 HIS A O   1 
ATOM   2603 C CB  . HIS A 1 365 ? 89.721  40.255 32.583 1.00 20.83 ? 363 HIS A CB  1 
ATOM   2604 C CG  . HIS A 1 365 ? 90.070  41.494 33.334 1.00 22.07 ? 363 HIS A CG  1 
ATOM   2605 N ND1 . HIS A 1 365 ? 91.219  41.565 34.119 1.00 20.01 ? 363 HIS A ND1 1 
ATOM   2606 C CD2 . HIS A 1 365 ? 89.446  42.676 33.471 1.00 21.24 ? 363 HIS A CD2 1 
ATOM   2607 C CE1 . HIS A 1 365 ? 91.279  42.739 34.688 1.00 19.02 ? 363 HIS A CE1 1 
ATOM   2608 N NE2 . HIS A 1 365 ? 90.248  43.460 34.277 1.00 20.54 ? 363 HIS A NE2 1 
ATOM   2609 N N   . CYS A 1 366 ? 90.930  38.097 29.890 1.00 22.92 ? 364 CYS A N   1 
ATOM   2610 C CA  . CYS A 1 366 ? 90.998  36.759 29.236 1.00 21.33 ? 364 CYS A CA  1 
ATOM   2611 C C   . CYS A 1 366 ? 89.637  36.050 29.163 1.00 19.55 ? 364 CYS A C   1 
ATOM   2612 O O   . CYS A 1 366 ? 89.643  34.757 29.129 1.00 22.63 ? 364 CYS A O   1 
ATOM   2613 C CB  . CYS A 1 366 ? 91.952  35.845 29.978 1.00 26.22 ? 364 CYS A CB  1 
ATOM   2614 S SG  . CYS A 1 366 ? 93.660  36.383 29.773 1.00 31.68 ? 364 CYS A SG  1 
ATOM   2615 N N   . GLY A 1 367 ? 88.555  36.813 29.065 1.00 20.87 ? 365 GLY A N   1 
ATOM   2616 C CA  . GLY A 1 367 ? 87.330  36.386 28.365 1.00 22.05 ? 365 GLY A CA  1 
ATOM   2617 C C   . GLY A 1 367 ? 87.725  35.768 27.023 1.00 23.17 ? 365 GLY A C   1 
ATOM   2618 O O   . GLY A 1 367 ? 88.618  36.292 26.359 1.00 20.57 ? 365 GLY A O   1 
ATOM   2619 N N   . TRP A 1 368 ? 87.060  34.702 26.593 1.00 21.73 ? 366 TRP A N   1 
ATOM   2620 C CA  . TRP A 1 368 ? 87.444  33.977 25.359 1.00 22.18 ? 366 TRP A CA  1 
ATOM   2621 C C   . TRP A 1 368 ? 87.255  34.876 24.143 1.00 22.76 ? 366 TRP A C   1 
ATOM   2622 O O   . TRP A 1 368 ? 88.127  34.852 23.255 1.00 20.23 ? 366 TRP A O   1 
ATOM   2623 C CB  . TRP A 1 368 ? 86.664  32.671 25.246 1.00 22.10 ? 366 TRP A CB  1 
ATOM   2624 C CG  . TRP A 1 368 ? 87.223  31.744 24.220 1.00 23.79 ? 366 TRP A CG  1 
ATOM   2625 C CD1 . TRP A 1 368 ? 86.529  31.151 23.210 1.00 22.47 ? 366 TRP A CD1 1 
ATOM   2626 C CD2 . TRP A 1 368 ? 88.561  31.235 24.152 1.00 21.67 ? 366 TRP A CD2 1 
ATOM   2627 N NE1 . TRP A 1 368 ? 87.359  30.314 22.516 1.00 22.80 ? 366 TRP A NE1 1 
ATOM   2628 C CE2 . TRP A 1 368 ? 88.614  30.360 23.052 1.00 22.53 ? 366 TRP A CE2 1 
ATOM   2629 C CE3 . TRP A 1 368 ? 89.731  31.453 24.880 1.00 24.31 ? 366 TRP A CE3 1 
ATOM   2630 C CZ2 . TRP A 1 368 ? 89.781  29.687 22.691 1.00 23.69 ? 366 TRP A CZ2 1 
ATOM   2631 C CZ3 . TRP A 1 368 ? 90.890  30.803 24.520 1.00 27.51 ? 366 TRP A CZ3 1 
ATOM   2632 C CH2 . TRP A 1 368 ? 90.919  29.933 23.430 1.00 26.69 ? 366 TRP A CH2 1 
ATOM   2633 N N   . ASN A 1 369 ? 86.183  35.674 24.113 1.00 23.41 ? 367 ASN A N   1 
ATOM   2634 C CA  . ASN A 1 369 ? 85.940  36.621 22.987 1.00 25.16 ? 367 ASN A CA  1 
ATOM   2635 C C   . ASN A 1 369 ? 87.153  37.562 22.810 1.00 23.57 ? 367 ASN A C   1 
ATOM   2636 O O   . ASN A 1 369 ? 87.551  37.817 21.668 1.00 21.92 ? 367 ASN A O   1 
ATOM   2637 C CB  . ASN A 1 369 ? 84.652  37.412 23.191 1.00 27.14 ? 367 ASN A CB  1 
ATOM   2638 C CG  . ASN A 1 369 ? 83.459  36.483 23.230 1.00 36.74 ? 367 ASN A CG  1 
ATOM   2639 O OD1 . ASN A 1 369 ? 83.334  35.609 22.369 1.00 37.79 ? 367 ASN A OD1 1 
ATOM   2640 N ND2 . ASN A 1 369 ? 82.599  36.621 24.230 1.00 36.98 ? 367 ASN A ND2 1 
ATOM   2641 N N   . SER A 1 370 ? 87.611  38.174 23.898 1.00 23.32 ? 368 SER A N   1 
ATOM   2642 C CA  . SER A 1 370 ? 88.775  39.083 23.942 1.00 23.72 ? 368 SER A CA  1 
ATOM   2643 C C   . SER A 1 370 ? 90.034  38.371 23.427 1.00 21.67 ? 368 SER A C   1 
ATOM   2644 O O   . SER A 1 370 ? 90.778  38.980 22.612 1.00 22.59 ? 368 SER A O   1 
ATOM   2645 C CB  . SER A 1 370 ? 88.961  39.577 25.340 1.00 26.86 ? 368 SER A CB  1 
ATOM   2646 O OG  . SER A 1 370 ? 87.950  40.503 25.624 1.00 29.29 ? 368 SER A OG  1 
ATOM   2647 N N   . ILE A 1 371 ? 90.330  37.171 23.944 1.00 20.17 ? 369 ILE A N   1 
ATOM   2648 C CA  . ILE A 1 371 ? 91.509  36.368 23.496 1.00 20.46 ? 369 ILE A CA  1 
ATOM   2649 C C   . ILE A 1 371 ? 91.408  36.174 21.975 1.00 23.78 ? 369 ILE A C   1 
ATOM   2650 O O   . ILE A 1 371 ? 92.383  36.426 21.278 1.00 23.25 ? 369 ILE A O   1 
ATOM   2651 C CB  . ILE A 1 371 ? 91.615  35.055 24.269 1.00 20.88 ? 369 ILE A CB  1 
ATOM   2652 C CG1 . ILE A 1 371 ? 92.117  35.328 25.690 1.00 24.41 ? 369 ILE A CG1 1 
ATOM   2653 C CG2 . ILE A 1 371 ? 92.484  34.068 23.526 1.00 22.63 ? 369 ILE A CG2 1 
ATOM   2654 C CD1 . ILE A 1 371 ? 92.151  34.111 26.593 1.00 24.09 ? 369 ILE A CD1 1 
ATOM   2655 N N   . LEU A 1 372 ? 90.274  35.714 21.478 1.00 23.03 ? 370 LEU A N   1 
ATOM   2656 C CA  . LEU A 1 372 ? 90.125  35.385 20.034 1.00 22.54 ? 370 LEU A CA  1 
ATOM   2657 C C   . LEU A 1 372 ? 90.325  36.662 19.189 1.00 21.83 ? 370 LEU A C   1 
ATOM   2658 O O   . LEU A 1 372 ? 90.977  36.571 18.132 1.00 22.51 ? 370 LEU A O   1 
ATOM   2659 C CB  . LEU A 1 372 ? 88.754  34.776 19.773 1.00 22.69 ? 370 LEU A CB  1 
ATOM   2660 C CG  . LEU A 1 372 ? 88.519  33.388 20.356 1.00 21.90 ? 370 LEU A CG  1 
ATOM   2661 C CD1 . LEU A 1 372 ? 87.104  32.921 20.071 1.00 23.19 ? 370 LEU A CD1 1 
ATOM   2662 C CD2 . LEU A 1 372 ? 89.540  32.401 19.843 1.00 24.82 ? 370 LEU A CD2 1 
ATOM   2663 N N   . GLU A 1 373 ? 89.840  37.811 19.650 1.00 22.21 ? 371 GLU A N   1 
ATOM   2664 C CA  . GLU A 1 373 ? 90.073  39.081 18.936 1.00 21.46 ? 371 GLU A CA  1 
ATOM   2665 C C   . GLU A 1 373 ? 91.585  39.317 18.839 1.00 22.33 ? 371 GLU A C   1 
ATOM   2666 O O   . GLU A 1 373 ? 92.065  39.798 17.807 1.00 21.81 ? 371 GLU A O   1 
ATOM   2667 C CB  . GLU A 1 373 ? 89.414  40.247 19.673 1.00 27.12 ? 371 GLU A CB  1 
ATOM   2668 C CG  . GLU A 1 373 ? 87.914  40.277 19.498 1.00 31.91 ? 371 GLU A CG  1 
ATOM   2669 C CD  . GLU A 1 373 ? 87.501  40.971 18.210 1.00 42.50 ? 371 GLU A CD  1 
ATOM   2670 O OE1 . GLU A 1 373 ? 86.291  41.001 17.933 1.00 45.51 ? 371 GLU A OE1 1 
ATOM   2671 O OE2 . GLU A 1 373 ? 88.389  41.457 17.479 1.00 45.53 ? 371 GLU A OE2 1 
ATOM   2672 N N   . SER A 1 374 ? 92.284  39.132 19.944 1.00 21.41 ? 372 SER A N   1 
ATOM   2673 C CA  . SER A 1 374 ? 93.721  39.451 20.003 1.00 21.79 ? 372 SER A CA  1 
ATOM   2674 C C   . SER A 1 374 ? 94.462  38.479 19.072 1.00 23.70 ? 372 SER A C   1 
ATOM   2675 O O   . SER A 1 374 ? 95.400  38.929 18.344 1.00 20.79 ? 372 SER A O   1 
ATOM   2676 C CB  . SER A 1 374 ? 94.252  39.432 21.413 1.00 20.72 ? 372 SER A CB  1 
ATOM   2677 O OG  . SER A 1 374 ? 95.408  40.249 21.473 1.00 22.26 ? 372 SER A OG  1 
ATOM   2678 N N   . VAL A 1 375 ? 94.018  37.222 19.067 1.00 20.50 ? 373 VAL A N   1 
ATOM   2679 C CA  . VAL A 1 375 ? 94.638  36.162 18.227 1.00 20.47 ? 373 VAL A CA  1 
ATOM   2680 C C   . VAL A 1 375 ? 94.458  36.507 16.737 1.00 22.21 ? 373 VAL A C   1 
ATOM   2681 O O   . VAL A 1 375 ? 95.470  36.430 15.967 1.00 22.77 ? 373 VAL A O   1 
ATOM   2682 C CB  . VAL A 1 375 ? 94.088  34.773 18.549 1.00 22.95 ? 373 VAL A CB  1 
ATOM   2683 C CG1 . VAL A 1 375 ? 94.533  33.779 17.470 1.00 24.01 ? 373 VAL A CG1 1 
ATOM   2684 C CG2 . VAL A 1 375 ? 94.582  34.335 19.911 1.00 21.29 ? 373 VAL A CG2 1 
ATOM   2685 N N   . VAL A 1 376 ? 93.239  36.848 16.327 1.00 21.35 ? 374 VAL A N   1 
ATOM   2686 C CA  . VAL A 1 376 ? 92.926  37.114 14.892 1.00 22.37 ? 374 VAL A CA  1 
ATOM   2687 C C   . VAL A 1 376 ? 93.770  38.292 14.390 1.00 25.25 ? 374 VAL A C   1 
ATOM   2688 O O   . VAL A 1 376 ? 94.135  38.276 13.178 1.00 23.35 ? 374 VAL A O   1 
ATOM   2689 C CB  . VAL A 1 376 ? 91.410  37.340 14.719 1.00 25.09 ? 374 VAL A CB  1 
ATOM   2690 C CG1 . VAL A 1 376 ? 91.038  38.063 13.462 1.00 30.73 ? 374 VAL A CG1 1 
ATOM   2691 C CG2 . VAL A 1 376 ? 90.682  36.022 14.791 1.00 25.08 ? 374 VAL A CG2 1 
ATOM   2692 N N   . HIS A 1 377 ? 94.086  39.278 15.257 1.00 22.36 ? 375 HIS A N   1 
ATOM   2693 C CA  . HIS A 1 377 ? 94.879  40.488 14.907 1.00 23.52 ? 375 HIS A CA  1 
ATOM   2694 C C   . HIS A 1 377 ? 96.367  40.311 15.211 1.00 23.98 ? 375 HIS A C   1 
ATOM   2695 O O   . HIS A 1 377 ? 97.146  41.234 14.949 1.00 23.43 ? 375 HIS A O   1 
ATOM   2696 C CB  . HIS A 1 377 ? 94.270  41.680 15.642 1.00 24.33 ? 375 HIS A CB  1 
ATOM   2697 C CG  . HIS A 1 377 ? 92.939  42.011 15.075 1.00 26.59 ? 375 HIS A CG  1 
ATOM   2698 N ND1 . HIS A 1 377 ? 91.761  41.765 15.750 1.00 31.05 ? 375 HIS A ND1 1 
ATOM   2699 C CD2 . HIS A 1 377 ? 92.589  42.428 13.838 1.00 28.47 ? 375 HIS A CD2 1 
ATOM   2700 C CE1 . HIS A 1 377 ? 90.748  42.151 15.003 1.00 26.14 ? 375 HIS A CE1 1 
ATOM   2701 N NE2 . HIS A 1 377 ? 91.233  42.547 13.831 1.00 27.97 ? 375 HIS A NE2 1 
ATOM   2702 N N   . GLY A 1 378 ? 96.761  39.184 15.787 1.00 21.31 ? 376 GLY A N   1 
ATOM   2703 C CA  . GLY A 1 378 ? 98.168  38.855 16.019 1.00 22.30 ? 376 GLY A CA  1 
ATOM   2704 C C   . GLY A 1 378 ? 98.792  39.737 17.090 1.00 23.37 ? 376 GLY A C   1 
ATOM   2705 O O   . GLY A 1 378 ? 99.993  39.922 17.044 1.00 21.65 ? 376 GLY A O   1 
ATOM   2706 N N   . VAL A 1 379 ? 98.027  40.144 18.099 1.00 21.18 ? 377 VAL A N   1 
ATOM   2707 C CA  . VAL A 1 379 ? 98.557  41.003 19.196 1.00 21.02 ? 377 VAL A CA  1 
ATOM   2708 C C   . VAL A 1 379 ? 98.882  40.134 20.396 1.00 22.39 ? 377 VAL A C   1 
ATOM   2709 O O   . VAL A 1 379 ? 98.000  39.438 20.915 1.00 21.06 ? 377 VAL A O   1 
ATOM   2710 C CB  . VAL A 1 379 ? 97.598  42.145 19.547 1.00 20.99 ? 377 VAL A CB  1 
ATOM   2711 C CG1 . VAL A 1 379 ? 98.206  43.074 20.616 1.00 21.81 ? 377 VAL A CG1 1 
ATOM   2712 C CG2 . VAL A 1 379 ? 97.274  42.956 18.303 1.00 23.13 ? 377 VAL A CG2 1 
ATOM   2713 N N   . PRO A 1 380 ? 100.167 40.123 20.836 1.00 22.12 ? 378 PRO A N   1 
ATOM   2714 C CA  . PRO A 1 380 ? 100.546 39.348 22.011 1.00 23.32 ? 378 PRO A CA  1 
ATOM   2715 C C   . PRO A 1 380 ? 99.832  39.853 23.274 1.00 20.40 ? 378 PRO A C   1 
ATOM   2716 O O   . PRO A 1 380 ? 99.544  41.042 23.397 1.00 20.35 ? 378 PRO A O   1 
ATOM   2717 C CB  . PRO A 1 380 ? 102.083 39.467 22.069 1.00 21.61 ? 378 PRO A CB  1 
ATOM   2718 C CG  . PRO A 1 380 ? 102.392 40.732 21.322 1.00 22.46 ? 378 PRO A CG  1 
ATOM   2719 C CD  . PRO A 1 380 ? 101.312 40.861 20.259 1.00 22.57 ? 378 PRO A CD  1 
ATOM   2720 N N   . ILE A 1 381 ? 99.591  38.921 24.204 1.00 20.94 ? 379 ILE A N   1 
ATOM   2721 C CA  . ILE A 1 381 ? 98.678  39.140 25.359 1.00 21.27 ? 379 ILE A CA  1 
ATOM   2722 C C   . ILE A 1 381 ? 99.513  39.246 26.641 1.00 20.30 ? 379 ILE A C   1 
ATOM   2723 O O   . ILE A 1 381 ? 100.467 38.492 26.788 1.00 19.88 ? 379 ILE A O   1 
ATOM   2724 C CB  . ILE A 1 381 ? 97.631  38.012 25.437 1.00 20.87 ? 379 ILE A CB  1 
ATOM   2725 C CG1 . ILE A 1 381 ? 96.721  37.997 24.208 1.00 23.28 ? 379 ILE A CG1 1 
ATOM   2726 C CG2 . ILE A 1 381 ? 96.771  38.124 26.691 1.00 21.02 ? 379 ILE A CG2 1 
ATOM   2727 C CD1 . ILE A 1 381 ? 95.928  36.727 24.070 1.00 23.64 ? 379 ILE A CD1 1 
ATOM   2728 N N   . ILE A 1 382 ? 99.097  40.101 27.554 1.00 19.14 ? 380 ILE A N   1 
ATOM   2729 C CA  . ILE A 1 382 ? 99.355  39.936 29.005 1.00 20.38 ? 380 ILE A CA  1 
ATOM   2730 C C   . ILE A 1 382 ? 98.048  39.485 29.655 1.00 19.33 ? 380 ILE A C   1 
ATOM   2731 O O   . ILE A 1 382 ? 97.057  40.274 29.641 1.00 20.27 ? 380 ILE A O   1 
ATOM   2732 C CB  . ILE A 1 382 ? 99.885  41.242 29.635 1.00 20.52 ? 380 ILE A CB  1 
ATOM   2733 C CG1 . ILE A 1 382 ? 101.224 41.644 29.004 1.00 22.20 ? 380 ILE A CG1 1 
ATOM   2734 C CG2 . ILE A 1 382 ? 99.975  41.055 31.144 1.00 21.24 ? 380 ILE A CG2 1 
ATOM   2735 C CD1 . ILE A 1 382 ? 101.700 43.058 29.356 1.00 22.33 ? 380 ILE A CD1 1 
ATOM   2736 N N   . ALA A 1 383 ? 98.047  38.289 30.235 1.00 19.66 ? 381 ALA A N   1 
ATOM   2737 C CA  . ALA A 1 383 ? 96.872  37.626 30.832 1.00 20.94 ? 381 ALA A CA  1 
ATOM   2738 C C   . ALA A 1 383 ? 96.646  38.189 32.244 1.00 22.99 ? 381 ALA A C   1 
ATOM   2739 O O   . ALA A 1 383 ? 97.569  38.086 33.093 1.00 22.52 ? 381 ALA A O   1 
ATOM   2740 C CB  . ALA A 1 383 ? 97.131  36.149 30.845 1.00 21.48 ? 381 ALA A CB  1 
ATOM   2741 N N   . TRP A 1 384 ? 95.472  38.757 32.484 1.00 22.22 ? 382 TRP A N   1 
ATOM   2742 C CA  . TRP A 1 384 ? 95.041  39.252 33.815 1.00 21.19 ? 382 TRP A CA  1 
ATOM   2743 C C   . TRP A 1 384 ? 93.717  38.597 34.222 1.00 22.38 ? 382 TRP A C   1 
ATOM   2744 O O   . TRP A 1 384 ? 92.701  39.268 34.427 1.00 19.66 ? 382 TRP A O   1 
ATOM   2745 C CB  . TRP A 1 384 ? 94.935  40.774 33.807 1.00 21.53 ? 382 TRP A CB  1 
ATOM   2746 C CG  . TRP A 1 384 ? 95.036  41.342 35.193 1.00 21.53 ? 382 TRP A CG  1 
ATOM   2747 C CD1 . TRP A 1 384 ? 94.228  41.087 36.264 1.00 22.46 ? 382 TRP A CD1 1 
ATOM   2748 C CD2 . TRP A 1 384 ? 96.090  42.180 35.672 1.00 20.85 ? 382 TRP A CD2 1 
ATOM   2749 N NE1 . TRP A 1 384 ? 94.678  41.781 37.365 1.00 20.73 ? 382 TRP A NE1 1 
ATOM   2750 C CE2 . TRP A 1 384 ? 95.836  42.425 37.033 1.00 20.75 ? 382 TRP A CE2 1 
ATOM   2751 C CE3 . TRP A 1 384 ? 97.222  42.754 35.074 1.00 23.18 ? 382 TRP A CE3 1 
ATOM   2752 C CZ2 . TRP A 1 384 ? 96.672  43.249 37.791 1.00 25.79 ? 382 TRP A CZ2 1 
ATOM   2753 C CZ3 . TRP A 1 384 ? 98.076  43.522 35.844 1.00 27.10 ? 382 TRP A CZ3 1 
ATOM   2754 C CH2 . TRP A 1 384 ? 97.802  43.753 37.195 1.00 24.69 ? 382 TRP A CH2 1 
ATOM   2755 N N   . PRO A 1 385 ? 93.667  37.260 34.403 1.00 22.06 ? 383 PRO A N   1 
ATOM   2756 C CA  . PRO A 1 385 ? 92.420  36.604 34.795 1.00 22.10 ? 383 PRO A CA  1 
ATOM   2757 C C   . PRO A 1 385 ? 91.973  36.963 36.230 1.00 22.54 ? 383 PRO A C   1 
ATOM   2758 O O   . PRO A 1 385 ? 92.830  37.101 37.097 1.00 23.50 ? 383 PRO A O   1 
ATOM   2759 C CB  . PRO A 1 385 ? 92.790  35.124 34.683 1.00 20.45 ? 383 PRO A CB  1 
ATOM   2760 C CG  . PRO A 1 385 ? 94.272  35.095 34.944 1.00 22.61 ? 383 PRO A CG  1 
ATOM   2761 C CD  . PRO A 1 385 ? 94.778  36.306 34.204 1.00 22.36 ? 383 PRO A CD  1 
ATOM   2762 N N   . LEU A 1 386 ? 90.675  37.194 36.419 1.00 23.01 ? 384 LEU A N   1 
ATOM   2763 C CA  . LEU A 1 386 ? 90.036  37.463 37.742 1.00 23.96 ? 384 LEU A CA  1 
ATOM   2764 C C   . LEU A 1 386 ? 89.127  36.292 38.145 1.00 29.34 ? 384 LEU A C   1 
ATOM   2765 O O   . LEU A 1 386 ? 89.166  35.888 39.309 1.00 29.73 ? 384 LEU A O   1 
ATOM   2766 C CB  . LEU A 1 386 ? 89.264  38.778 37.658 1.00 27.87 ? 384 LEU A CB  1 
ATOM   2767 C CG  . LEU A 1 386 ? 90.104  40.030 37.369 1.00 25.50 ? 384 LEU A CG  1 
ATOM   2768 C CD1 . LEU A 1 386 ? 89.202  41.233 37.220 1.00 28.06 ? 384 LEU A CD1 1 
ATOM   2769 C CD2 . LEU A 1 386 ? 91.114  40.279 38.480 1.00 25.70 ? 384 LEU A CD2 1 
ATOM   2770 N N   . TYR A 1 387 ? 88.376  35.715 37.219 1.00 27.92 ? 385 TYR A N   1 
ATOM   2771 C CA  . TYR A 1 387 ? 87.406  34.610 37.474 1.00 29.70 ? 385 TYR A CA  1 
ATOM   2772 C C   . TYR A 1 387 ? 88.018  33.274 37.055 1.00 28.10 ? 385 TYR A C   1 
ATOM   2773 O O   . TYR A 1 387 ? 88.987  33.233 36.266 1.00 29.44 ? 385 TYR A O   1 
ATOM   2774 C CB  . TYR A 1 387 ? 86.124  34.884 36.694 1.00 32.60 ? 385 TYR A CB  1 
ATOM   2775 C CG  . TYR A 1 387 ? 85.410  36.120 37.166 1.00 37.59 ? 385 TYR A CG  1 
ATOM   2776 C CD1 . TYR A 1 387 ? 84.710  36.099 38.364 1.00 46.02 ? 385 TYR A CD1 1 
ATOM   2777 C CD2 . TYR A 1 387 ? 85.450  37.308 36.465 1.00 40.24 ? 385 TYR A CD2 1 
ATOM   2778 C CE1 . TYR A 1 387 ? 84.038  37.219 38.835 1.00 53.30 ? 385 TYR A CE1 1 
ATOM   2779 C CE2 . TYR A 1 387 ? 84.774  38.436 36.911 1.00 46.07 ? 385 TYR A CE2 1 
ATOM   2780 C CZ  . TYR A 1 387 ? 84.074  38.393 38.109 1.00 54.07 ? 385 TYR A CZ  1 
ATOM   2781 O OH  . TYR A 1 387 ? 83.421  39.483 38.597 1.00 52.94 ? 385 TYR A OH  1 
ATOM   2782 N N   . ALA A 1 388 ? 87.502  32.172 37.607 1.00 30.90 ? 386 ALA A N   1 
ATOM   2783 C CA  . ALA A 1 388 ? 88.061  30.824 37.400 1.00 30.06 ? 386 ALA A CA  1 
ATOM   2784 C C   . ALA A 1 388 ? 88.060  30.523 35.893 1.00 29.58 ? 386 ALA A C   1 
ATOM   2785 O O   . ALA A 1 388 ? 89.041  29.982 35.420 1.00 26.52 ? 386 ALA A O   1 
ATOM   2786 C CB  . ALA A 1 388 ? 87.317  29.775 38.205 1.00 34.42 ? 386 ALA A CB  1 
ATOM   2787 N N   . GLU A 1 389 ? 87.005  30.850 35.149 1.00 27.71 ? 387 GLU A N   1 
ATOM   2788 C CA  . GLU A 1 389 ? 87.000  30.459 33.718 1.00 28.70 ? 387 GLU A CA  1 
ATOM   2789 C C   . GLU A 1 389 ? 88.074  31.263 32.981 1.00 24.77 ? 387 GLU A C   1 
ATOM   2790 O O   . GLU A 1 389 ? 88.668  30.741 32.033 1.00 22.88 ? 387 GLU A O   1 
ATOM   2791 C CB  . GLU A 1 389 ? 85.628  30.636 33.088 1.00 31.20 ? 387 GLU A CB  1 
ATOM   2792 C CG  . GLU A 1 389 ? 85.608  30.120 31.649 1.00 34.25 ? 387 GLU A CG  1 
ATOM   2793 C CD  . GLU A 1 389 ? 84.231  30.206 31.014 1.00 37.80 ? 387 GLU A CD  1 
ATOM   2794 O OE1 . GLU A 1 389 ? 83.249  30.229 31.759 1.00 43.21 ? 387 GLU A OE1 1 
ATOM   2795 O OE2 . GLU A 1 389 ? 84.151  30.191 29.790 1.00 41.51 ? 387 GLU A OE2 1 
ATOM   2796 N N   . GLN A 1 390 ? 88.291  32.521 33.376 1.00 24.92 ? 388 GLN A N   1 
ATOM   2797 C CA  . GLN A 1 390 ? 89.375  33.357 32.773 1.00 23.56 ? 388 GLN A CA  1 
ATOM   2798 C C   . GLN A 1 390 ? 90.742  32.734 33.066 1.00 22.36 ? 388 GLN A C   1 
ATOM   2799 O O   . GLN A 1 390 ? 91.632  32.793 32.194 1.00 22.25 ? 388 GLN A O   1 
ATOM   2800 C CB  . GLN A 1 390 ? 89.272  34.781 33.313 1.00 21.78 ? 388 GLN A CB  1 
ATOM   2801 C CG  . GLN A 1 390 ? 88.000  35.494 32.887 1.00 22.92 ? 388 GLN A CG  1 
ATOM   2802 C CD  . GLN A 1 390 ? 87.884  36.821 33.577 1.00 23.34 ? 388 GLN A CD  1 
ATOM   2803 O OE1 . GLN A 1 390 ? 88.417  36.996 34.671 1.00 22.32 ? 388 GLN A OE1 1 
ATOM   2804 N NE2 . GLN A 1 390 ? 87.155  37.722 32.961 1.00 22.05 ? 388 GLN A NE2 1 
ATOM   2805 N N   . LYS A 1 391 ? 90.925  32.163 34.272 1.00 23.12 ? 389 LYS A N   1 
ATOM   2806 C CA  . LYS A 1 391 ? 92.174  31.480 34.678 1.00 24.41 ? 389 LYS A CA  1 
ATOM   2807 C C   . LYS A 1 391 ? 92.387  30.264 33.788 1.00 24.02 ? 389 LYS A C   1 
ATOM   2808 O O   . LYS A 1 391 ? 93.499  30.098 33.354 1.00 23.80 ? 389 LYS A O   1 
ATOM   2809 C CB  . LYS A 1 391 ? 92.191  31.027 36.149 1.00 27.81 ? 389 LYS A CB  1 
ATOM   2810 C CG  . LYS A 1 391 ? 92.164  32.172 37.144 1.00 32.06 ? 389 LYS A CG  1 
ATOM   2811 C CD  . LYS A 1 391 ? 92.034  31.725 38.602 1.00 33.05 ? 389 LYS A CD  1 
ATOM   2812 C CE  . LYS A 1 391 ? 91.622  32.873 39.481 1.00 32.78 ? 389 LYS A CE  1 
ATOM   2813 N NZ  . LYS A 1 391 ? 91.494  32.442 40.887 1.00 37.74 ? 389 LYS A NZ  1 
ATOM   2814 N N   . MET A 1 392 ? 91.347  29.478 33.489 1.00 25.90 ? 390 MET A N   1 
ATOM   2815 C CA  . MET A 1 392 ? 91.515  28.337 32.553 1.00 24.82 ? 390 MET A CA  1 
ATOM   2816 C C   . MET A 1 392 ? 91.893  28.882 31.172 1.00 22.88 ? 390 MET A C   1 
ATOM   2817 O O   . MET A 1 392 ? 92.809  28.309 30.483 1.00 24.44 ? 390 MET A O   1 
ATOM   2818 C CB  . MET A 1 392 ? 90.225  27.522 32.419 1.00 28.83 ? 390 MET A CB  1 
ATOM   2819 C CG  . MET A 1 392 ? 89.876  26.725 33.684 1.00 33.68 ? 390 MET A CG  1 
ATOM   2820 S SD  . MET A 1 392 ? 88.157  26.054 33.587 1.00 39.02 ? 390 MET A SD  1 
ATOM   2821 C CE  . MET A 1 392 ? 88.375  25.028 32.129 1.00 39.05 ? 390 MET A CE  1 
ATOM   2822 N N   . ASN A 1 393 ? 91.215  29.934 30.737 1.00 22.48 ? 391 ASN A N   1 
ATOM   2823 C CA  . ASN A 1 393 ? 91.546  30.548 29.417 1.00 22.14 ? 391 ASN A CA  1 
ATOM   2824 C C   . ASN A 1 393 ? 93.009  31.005 29.413 1.00 25.05 ? 391 ASN A C   1 
ATOM   2825 O O   . ASN A 1 393 ? 93.709  30.876 28.352 1.00 21.20 ? 391 ASN A O   1 
ATOM   2826 C CB  . ASN A 1 393 ? 90.622  31.714 29.065 1.00 22.19 ? 391 ASN A CB  1 
ATOM   2827 C CG  . ASN A 1 393 ? 89.151  31.333 28.928 1.00 24.17 ? 391 ASN A CG  1 
ATOM   2828 O OD1 . ASN A 1 393 ? 88.813  30.159 28.935 1.00 23.39 ? 391 ASN A OD1 1 
ATOM   2829 N ND2 . ASN A 1 393 ? 88.272  32.327 28.794 1.00 19.97 ? 391 ASN A ND2 1 
ATOM   2830 N N   . SER A 1 394 ? 93.478  31.586 30.517 1.00 23.67 ? 392 SER A N   1 
ATOM   2831 C CA  . SER A 1 394 ? 94.845  32.141 30.612 1.00 24.76 ? 392 SER A CA  1 
ATOM   2832 C C   . SER A 1 394 ? 95.870  30.990 30.575 1.00 26.98 ? 392 SER A C   1 
ATOM   2833 O O   . SER A 1 394 ? 96.945  31.169 30.018 1.00 27.11 ? 392 SER A O   1 
ATOM   2834 C CB  . SER A 1 394 ? 94.995  33.013 31.822 1.00 27.33 ? 392 SER A CB  1 
ATOM   2835 O OG  . SER A 1 394 ? 95.175  32.226 32.986 1.00 30.78 ? 392 SER A OG  1 
ATOM   2836 N N   . ILE A 1 395 ? 95.513  29.789 31.022 1.00 26.37 ? 393 ILE A N   1 
ATOM   2837 C CA  . ILE A 1 395 ? 96.412  28.600 30.926 1.00 26.88 ? 393 ILE A CA  1 
ATOM   2838 C C   . ILE A 1 395 ? 96.616  28.240 29.453 1.00 26.97 ? 393 ILE A C   1 
ATOM   2839 O O   . ILE A 1 395 ? 97.760  27.894 29.092 1.00 25.76 ? 393 ILE A O   1 
ATOM   2840 C CB  . ILE A 1 395 ? 95.880  27.412 31.759 1.00 28.23 ? 393 ILE A CB  1 
ATOM   2841 C CG1 . ILE A 1 395 ? 95.978  27.693 33.260 1.00 31.56 ? 393 ILE A CG1 1 
ATOM   2842 C CG2 . ILE A 1 395 ? 96.579  26.106 31.398 1.00 28.24 ? 393 ILE A CG2 1 
ATOM   2843 C CD1 . ILE A 1 395 ? 95.233  26.667 34.098 1.00 37.14 ? 393 ILE A CD1 1 
ATOM   2844 N N   . ILE A 1 396 ? 95.576  28.340 28.623 1.00 25.92 ? 394 ILE A N   1 
ATOM   2845 C CA  . ILE A 1 396 ? 95.688  28.077 27.161 1.00 25.29 ? 394 ILE A CA  1 
ATOM   2846 C C   . ILE A 1 396 ? 96.720  29.037 26.566 1.00 25.93 ? 394 ILE A C   1 
ATOM   2847 O O   . ILE A 1 396 ? 97.661  28.570 25.910 1.00 23.93 ? 394 ILE A O   1 
ATOM   2848 C CB  . ILE A 1 396 ? 94.337  28.166 26.433 1.00 25.10 ? 394 ILE A CB  1 
ATOM   2849 C CG1 . ILE A 1 396 ? 93.388  27.056 26.888 1.00 27.95 ? 394 ILE A CG1 1 
ATOM   2850 C CG2 . ILE A 1 396 ? 94.536  28.133 24.919 1.00 25.75 ? 394 ILE A CG2 1 
ATOM   2851 C CD1 . ILE A 1 396 ? 91.990  27.224 26.344 1.00 28.98 ? 394 ILE A CD1 1 
ATOM   2852 N N   . VAL A 1 397 ? 96.583  30.340 26.806 1.00 22.75 ? 395 VAL A N   1 
ATOM   2853 C CA  . VAL A 1 397 ? 97.452  31.309 26.080 1.00 23.45 ? 395 VAL A CA  1 
ATOM   2854 C C   . VAL A 1 397 ? 98.834  31.432 26.732 1.00 21.66 ? 395 VAL A C   1 
ATOM   2855 O O   . VAL A 1 397 ? 99.800  31.653 25.992 1.00 20.97 ? 395 VAL A O   1 
ATOM   2856 C CB  . VAL A 1 397 ? 96.728  32.646 25.892 1.00 21.93 ? 395 VAL A CB  1 
ATOM   2857 C CG1 . VAL A 1 397 ? 95.628  32.480 24.862 1.00 22.15 ? 395 VAL A CG1 1 
ATOM   2858 C CG2 . VAL A 1 397 ? 96.170  33.203 27.187 1.00 21.87 ? 395 VAL A CG2 1 
ATOM   2859 N N   . VAL A 1 398 ? 98.947  31.361 28.062 1.00 22.67 ? 396 VAL A N   1 
ATOM   2860 C CA  . VAL A 1 398 ? 100.268 31.477 28.736 1.00 24.72 ? 396 VAL A CA  1 
ATOM   2861 C C   . VAL A 1 398 ? 101.060 30.162 28.618 1.00 27.30 ? 396 VAL A C   1 
ATOM   2862 O O   . VAL A 1 398 ? 102.251 30.220 28.290 1.00 25.66 ? 396 VAL A O   1 
ATOM   2863 C CB  . VAL A 1 398 ? 100.114 31.919 30.200 1.00 25.46 ? 396 VAL A CB  1 
ATOM   2864 C CG1 . VAL A 1 398 ? 101.471 31.946 30.901 1.00 25.10 ? 396 VAL A CG1 1 
ATOM   2865 C CG2 . VAL A 1 398 ? 99.435  33.288 30.253 1.00 24.96 ? 396 VAL A CG2 1 
ATOM   2866 N N   . GLU A 1 399 ? 100.463 29.039 28.995 1.00 27.92 ? 397 GLU A N   1 
ATOM   2867 C CA  . GLU A 1 399 ? 101.201 27.781 29.264 1.00 28.62 ? 397 GLU A CA  1 
ATOM   2868 C C   . GLU A 1 399 ? 101.167 26.849 28.058 1.00 28.19 ? 397 GLU A C   1 
ATOM   2869 O O   . GLU A 1 399 ? 102.158 26.179 27.862 1.00 29.82 ? 397 GLU A O   1 
ATOM   2870 C CB  . GLU A 1 399 ? 100.619 27.102 30.498 1.00 31.41 ? 397 GLU A CB  1 
ATOM   2871 C CG  . GLU A 1 399 ? 100.841 27.949 31.735 1.00 36.00 ? 397 GLU A CG  1 
ATOM   2872 C CD  . GLU A 1 399 ? 100.258 27.347 32.994 1.00 42.48 ? 397 GLU A CD  1 
ATOM   2873 O OE1 . GLU A 1 399 ? 100.030 26.120 33.014 1.00 44.98 ? 397 GLU A OE1 1 
ATOM   2874 O OE2 . GLU A 1 399 ? 100.033 28.108 33.953 1.00 47.03 ? 397 GLU A OE2 1 
ATOM   2875 N N   . ASP A 1 400 ? 100.092 26.822 27.267 1.00 30.12 ? 398 ASP A N   1 
ATOM   2876 C CA  . ASP A 1 400 ? 99.931  25.828 26.167 1.00 33.33 ? 398 ASP A CA  1 
ATOM   2877 C C   . ASP A 1 400 ? 100.482 26.397 24.858 1.00 31.99 ? 398 ASP A C   1 
ATOM   2878 O O   . ASP A 1 400 ? 101.485 25.855 24.390 1.00 32.58 ? 398 ASP A O   1 
ATOM   2879 C CB  . ASP A 1 400 ? 98.496  25.333 26.033 1.00 31.33 ? 398 ASP A CB  1 
ATOM   2880 C CG  . ASP A 1 400 ? 98.344  24.132 25.106 1.00 40.59 ? 398 ASP A CG  1 
ATOM   2881 O OD1 . ASP A 1 400 ? 99.338  23.773 24.414 1.00 42.77 ? 398 ASP A OD1 1 
ATOM   2882 O OD2 . ASP A 1 400 ? 97.203  23.572 25.049 1.00 41.28 ? 398 ASP A OD2 1 
ATOM   2883 N N   . VAL A 1 401 ? 99.835  27.384 24.232 1.00 29.78 ? 399 VAL A N   1 
ATOM   2884 C CA  . VAL A 1 401 ? 100.322 27.948 22.940 1.00 25.12 ? 399 VAL A CA  1 
ATOM   2885 C C   . VAL A 1 401 ? 101.342 29.077 23.167 1.00 26.49 ? 399 VAL A C   1 
ATOM   2886 O O   . VAL A 1 401 ? 101.993 29.470 22.175 1.00 23.29 ? 399 VAL A O   1 
ATOM   2887 C CB  . VAL A 1 401 ? 99.174  28.359 22.003 1.00 27.99 ? 399 VAL A CB  1 
ATOM   2888 C CG1 . VAL A 1 401 ? 98.359  27.131 21.644 1.00 28.03 ? 399 VAL A CG1 1 
ATOM   2889 C CG2 . VAL A 1 401 ? 98.257  29.447 22.573 1.00 27.04 ? 399 VAL A CG2 1 
ATOM   2890 N N   . LYS A 1 402 ? 101.445 29.610 24.390 1.00 24.33 ? 400 LYS A N   1 
ATOM   2891 C CA  . LYS A 1 402 ? 102.513 30.568 24.791 1.00 25.38 ? 400 LYS A CA  1 
ATOM   2892 C C   . LYS A 1 402 ? 102.483 31.804 23.887 1.00 24.61 ? 400 LYS A C   1 
ATOM   2893 O O   . LYS A 1 402 ? 103.568 32.210 23.386 1.00 23.40 ? 400 LYS A O   1 
ATOM   2894 C CB  . LYS A 1 402 ? 103.891 29.880 24.749 1.00 30.39 ? 400 LYS A CB  1 
ATOM   2895 C CG  . LYS A 1 402 ? 103.999 28.646 25.653 1.00 35.05 ? 400 LYS A CG  1 
ATOM   2896 C CD  . LYS A 1 402 ? 105.335 27.934 25.570 1.00 40.32 ? 400 LYS A CD  1 
ATOM   2897 C CE  . LYS A 1 402 ? 105.479 26.833 26.601 1.00 43.89 ? 400 LYS A CE  1 
ATOM   2898 N NZ  . LYS A 1 402 ? 104.528 25.724 26.357 1.00 48.06 ? 400 LYS A NZ  1 
ATOM   2899 N N   . VAL A 1 403 ? 101.310 32.445 23.753 1.00 22.11 ? 401 VAL A N   1 
ATOM   2900 C CA  . VAL A 1 403 ? 101.143 33.724 23.000 1.00 22.83 ? 401 VAL A CA  1 
ATOM   2901 C C   . VAL A 1 403 ? 100.860 34.843 24.001 1.00 21.79 ? 401 VAL A C   1 
ATOM   2902 O O   . VAL A 1 403 ? 100.463 35.932 23.586 1.00 21.87 ? 401 VAL A O   1 
ATOM   2903 C CB  . VAL A 1 403 ? 100.037 33.617 21.941 1.00 24.05 ? 401 VAL A CB  1 
ATOM   2904 C CG1 . VAL A 1 403 ? 100.438 32.607 20.854 1.00 24.93 ? 401 VAL A CG1 1 
ATOM   2905 C CG2 . VAL A 1 403 ? 98.708  33.277 22.561 1.00 23.53 ? 401 VAL A CG2 1 
ATOM   2906 N N   . ALA A 1 404 ? 101.041 34.540 25.274 1.00 22.77 ? 402 ALA A N   1 
ATOM   2907 C CA  . ALA A 1 404 ? 100.678 35.435 26.385 1.00 22.21 ? 402 ALA A CA  1 
ATOM   2908 C C   . ALA A 1 404 ? 101.736 35.332 27.484 1.00 23.44 ? 402 ALA A C   1 
ATOM   2909 O O   . ALA A 1 404 ? 102.248 34.223 27.712 1.00 22.76 ? 402 ALA A O   1 
ATOM   2910 C CB  . ALA A 1 404 ? 99.334  35.068 26.904 1.00 21.17 ? 402 ALA A CB  1 
ATOM   2911 N N   . LEU A 1 405 ? 102.071 36.456 28.112 1.00 22.72 ? 403 LEU A N   1 
ATOM   2912 C CA  . LEU A 1 405 ? 102.791 36.465 29.419 1.00 23.99 ? 403 LEU A CA  1 
ATOM   2913 C C   . LEU A 1 405 ? 101.793 36.741 30.544 1.00 23.93 ? 403 LEU A C   1 
ATOM   2914 O O   . LEU A 1 405 ? 100.637 37.178 30.289 1.00 24.74 ? 403 LEU A O   1 
ATOM   2915 C CB  . LEU A 1 405 ? 103.883 37.530 29.399 1.00 23.70 ? 403 LEU A CB  1 
ATOM   2916 C CG  . LEU A 1 405 ? 104.893 37.420 28.258 1.00 26.88 ? 403 LEU A CG  1 
ATOM   2917 C CD1 . LEU A 1 405 ? 105.856 38.601 28.244 1.00 29.62 ? 403 LEU A CD1 1 
ATOM   2918 C CD2 . LEU A 1 405 ? 105.650 36.124 28.367 1.00 27.31 ? 403 LEU A CD2 1 
ATOM   2919 N N   . ARG A 1 406 ? 102.161 36.437 31.774 1.00 26.93 ? 404 ARG A N   1 
ATOM   2920 C CA  . ARG A 1 406 ? 101.245 36.698 32.908 1.00 30.86 ? 404 ARG A CA  1 
ATOM   2921 C C   . ARG A 1 406 ? 102.099 37.348 33.984 1.00 34.37 ? 404 ARG A C   1 
ATOM   2922 O O   . ARG A 1 406 ? 103.264 36.979 34.113 1.00 29.01 ? 404 ARG A O   1 
ATOM   2923 C CB  . ARG A 1 406 ? 100.576 35.400 33.369 1.00 35.62 ? 404 ARG A CB  1 
ATOM   2924 C CG  . ARG A 1 406 ? 101.519 34.430 34.059 1.00 42.94 ? 404 ARG A CG  1 
ATOM   2925 C CD  . ARG A 1 406 ? 100.968 33.059 34.469 1.00 46.78 ? 404 ARG A CD  1 
ATOM   2926 N NE  . ARG A 1 406 ? 99.526  33.069 34.664 1.00 47.46 ? 404 ARG A NE  1 
ATOM   2927 C CZ  . ARG A 1 406 ? 98.741  32.001 34.545 1.00 50.59 ? 404 ARG A CZ  1 
ATOM   2928 N NH1 . ARG A 1 406 ? 99.272  30.817 34.267 1.00 41.24 ? 404 ARG A NH1 1 
ATOM   2929 N NH2 . ARG A 1 406 ? 97.428  32.133 34.713 1.00 46.59 ? 404 ARG A NH2 1 
ATOM   2930 N N   . PRO A 1 407 ? 101.582 38.376 34.693 1.00 32.02 ? 405 PRO A N   1 
ATOM   2931 C CA  . PRO A 1 407 ? 102.269 38.931 35.854 1.00 32.19 ? 405 PRO A CA  1 
ATOM   2932 C C   . PRO A 1 407 ? 102.254 37.895 36.980 1.00 31.12 ? 405 PRO A C   1 
ATOM   2933 O O   . PRO A 1 407 ? 101.307 37.140 37.084 1.00 25.45 ? 405 PRO A O   1 
ATOM   2934 C CB  . PRO A 1 407 ? 101.428 40.115 36.325 1.00 31.65 ? 405 PRO A CB  1 
ATOM   2935 C CG  . PRO A 1 407 ? 100.311 40.258 35.311 1.00 33.85 ? 405 PRO A CG  1 
ATOM   2936 C CD  . PRO A 1 407 ? 100.273 38.997 34.477 1.00 30.93 ? 405 PRO A CD  1 
ATOM   2937 N N   . ALA A 1 408 ? 103.296 37.894 37.810 1.00 32.72 ? 406 ALA A N   1 
ATOM   2938 C CA  . ALA A 1 408 ? 103.384 37.029 39.004 1.00 33.20 ? 406 ALA A CA  1 
ATOM   2939 C C   . ALA A 1 408 ? 102.189 37.311 39.924 1.00 32.16 ? 406 ALA A C   1 
ATOM   2940 O O   . ALA A 1 408 ? 101.866 38.503 40.190 1.00 33.94 ? 406 ALA A O   1 
ATOM   2941 C CB  . ALA A 1 408 ? 104.720 37.256 39.695 1.00 35.76 ? 406 ALA A CB  1 
ATOM   2942 N N   . GLY A 1 409 ? 101.494 36.242 40.280 1.00 29.11 ? 407 GLY A N   1 
ATOM   2943 C CA  . GLY A 1 409 ? 100.422 36.197 41.272 1.00 28.52 ? 407 GLY A CA  1 
ATOM   2944 C C   . GLY A 1 409 ? 99.033  36.469 40.743 1.00 27.12 ? 407 GLY A C   1 
ATOM   2945 O O   . GLY A 1 409 ? 98.075  36.375 41.512 1.00 25.97 ? 407 GLY A O   1 
ATOM   2946 N N   . VAL A 1 410 ? 98.888  36.802 39.471 1.00 26.49 ? 408 VAL A N   1 
ATOM   2947 C CA  . VAL A 1 410 ? 97.585  37.313 38.979 1.00 25.81 ? 408 VAL A CA  1 
ATOM   2948 C C   . VAL A 1 410 ? 96.499  36.245 39.168 1.00 26.91 ? 408 VAL A C   1 
ATOM   2949 O O   . VAL A 1 410 ? 96.758  35.082 38.906 1.00 32.50 ? 408 VAL A O   1 
ATOM   2950 C CB  . VAL A 1 410 ? 97.706  37.785 37.522 1.00 25.68 ? 408 VAL A CB  1 
ATOM   2951 C CG1 . VAL A 1 410 ? 97.836  36.604 36.576 1.00 26.38 ? 408 VAL A CG1 1 
ATOM   2952 C CG2 . VAL A 1 410 ? 96.540  38.704 37.184 1.00 28.09 ? 408 VAL A CG2 1 
ATOM   2953 N N   . GLY A 1 411 ? 95.311  36.657 39.555 1.00 25.02 ? 409 GLY A N   1 
ATOM   2954 C CA  . GLY A 1 411 ? 94.168  35.778 39.854 1.00 30.61 ? 409 GLY A CA  1 
ATOM   2955 C C   . GLY A 1 411 ? 94.180  35.236 41.280 1.00 30.97 ? 409 GLY A C   1 
ATOM   2956 O O   . GLY A 1 411 ? 93.119  34.819 41.709 1.00 35.95 ? 409 GLY A O   1 
ATOM   2957 N N   . GLU A 1 412 ? 95.329  35.220 41.971 1.00 33.39 ? 410 GLU A N   1 
ATOM   2958 C CA  . GLU A 1 412 ? 95.461  34.695 43.374 1.00 33.53 ? 410 GLU A CA  1 
ATOM   2959 C C   . GLU A 1 412 ? 95.619  35.854 44.396 1.00 34.51 ? 410 GLU A C   1 
ATOM   2960 O O   . GLU A 1 412 ? 95.227  35.690 45.568 1.00 32.52 ? 410 GLU A O   1 
ATOM   2961 C CB  . GLU A 1 412 ? 96.681  33.780 43.491 1.00 39.88 ? 410 GLU A CB  1 
ATOM   2962 C CG  . GLU A 1 412 ? 96.842  32.700 42.421 1.00 51.68 ? 410 GLU A CG  1 
ATOM   2963 C CD  . GLU A 1 412 ? 98.037  31.783 42.689 1.00 64.45 ? 410 GLU A CD  1 
ATOM   2964 O OE1 . GLU A 1 412 ? 97.895  30.838 43.514 1.00 69.93 ? 410 GLU A OE1 1 
ATOM   2965 O OE2 . GLU A 1 412 ? 99.135  32.036 42.121 1.00 72.07 ? 410 GLU A OE2 1 
ATOM   2966 N N   . ARG A 1 413 ? 96.199  36.992 44.005 1.00 29.67 ? 411 ARG A N   1 
ATOM   2967 C CA  . ARG A 1 413 ? 96.643  38.036 44.975 1.00 28.84 ? 411 ARG A CA  1 
ATOM   2968 C C   . ARG A 1 413 ? 96.742  39.365 44.242 1.00 28.90 ? 411 ARG A C   1 
ATOM   2969 O O   . ARG A 1 413 ? 96.686  39.367 42.982 1.00 28.18 ? 411 ARG A O   1 
ATOM   2970 C CB  . ARG A 1 413 ? 97.969  37.645 45.649 1.00 26.42 ? 411 ARG A CB  1 
ATOM   2971 C CG  . ARG A 1 413 ? 99.138  37.432 44.716 1.00 30.47 ? 411 ARG A CG  1 
ATOM   2972 C CD  . ARG A 1 413 ? 100.454 37.409 45.452 1.00 32.95 ? 411 ARG A CD  1 
ATOM   2973 N NE  . ARG A 1 413 ? 101.590 37.115 44.599 1.00 30.79 ? 411 ARG A NE  1 
ATOM   2974 C CZ  . ARG A 1 413 ? 102.251 37.996 43.876 1.00 32.30 ? 411 ARG A CZ  1 
ATOM   2975 N NH1 . ARG A 1 413 ? 101.915 39.286 43.869 1.00 31.28 ? 411 ARG A NH1 1 
ATOM   2976 N NH2 . ARG A 1 413 ? 103.296 37.577 43.203 1.00 30.10 ? 411 ARG A NH2 1 
ATOM   2977 N N   . VAL A 1 414 ? 96.846  40.451 44.992 1.00 22.12 ? 412 VAL A N   1 
ATOM   2978 C CA  . VAL A 1 414 ? 97.239  41.767 44.404 1.00 22.01 ? 412 VAL A CA  1 
ATOM   2979 C C   . VAL A 1 414 ? 98.593  41.619 43.734 1.00 22.66 ? 412 VAL A C   1 
ATOM   2980 O O   . VAL A 1 414 ? 99.478  40.991 44.300 1.00 24.25 ? 412 VAL A O   1 
ATOM   2981 C CB  . VAL A 1 414 ? 97.297  42.835 45.497 1.00 23.75 ? 412 VAL A CB  1 
ATOM   2982 C CG1 . VAL A 1 414 ? 97.879  44.159 45.000 1.00 25.66 ? 412 VAL A CG1 1 
ATOM   2983 C CG2 . VAL A 1 414 ? 95.920  42.986 46.090 1.00 25.52 ? 412 VAL A CG2 1 
ATOM   2984 N N   . VAL A 1 415 ? 98.705  42.119 42.502 1.00 20.35 ? 413 VAL A N   1 
ATOM   2985 C CA  . VAL A 1 415 ? 99.957  42.215 41.717 1.00 24.24 ? 413 VAL A CA  1 
ATOM   2986 C C   . VAL A 1 415 ? 100.597 43.570 42.029 1.00 22.92 ? 413 VAL A C   1 
ATOM   2987 O O   . VAL A 1 415 ? 99.900  44.590 41.901 1.00 23.05 ? 413 VAL A O   1 
ATOM   2988 C CB  . VAL A 1 415 ? 99.679  42.038 40.214 1.00 24.88 ? 413 VAL A CB  1 
ATOM   2989 C CG1 . VAL A 1 415 ? 100.947 41.977 39.395 1.00 26.15 ? 413 VAL A CG1 1 
ATOM   2990 C CG2 . VAL A 1 415 ? 98.828  40.804 39.954 1.00 26.54 ? 413 VAL A CG2 1 
ATOM   2991 N N   . GLU A 1 416 ? 101.845 43.520 42.483 1.00 23.17 ? 414 GLU A N   1 
ATOM   2992 C CA  . GLU A 1 416 ? 102.681 44.655 42.915 1.00 27.72 ? 414 GLU A CA  1 
ATOM   2993 C C   . GLU A 1 416 ? 103.074 45.468 41.679 1.00 28.33 ? 414 GLU A C   1 
ATOM   2994 O O   . GLU A 1 416 ? 103.280 44.885 40.570 1.00 23.61 ? 414 GLU A O   1 
ATOM   2995 C CB  . GLU A 1 416 ? 103.933 44.176 43.662 1.00 28.50 ? 414 GLU A CB  1 
ATOM   2996 C CG  . GLU A 1 416 ? 103.627 43.452 44.968 1.00 31.72 ? 414 GLU A CG  1 
ATOM   2997 C CD  . GLU A 1 416 ? 102.961 44.332 45.998 1.00 31.75 ? 414 GLU A CD  1 
ATOM   2998 O OE1 . GLU A 1 416 ? 103.443 45.437 46.187 1.00 32.16 ? 414 GLU A OE1 1 
ATOM   2999 O OE2 . GLU A 1 416 ? 101.937 43.942 46.585 1.00 35.28 ? 414 GLU A OE2 1 
ATOM   3000 N N   . ARG A 1 417 ? 103.210 46.779 41.857 1.00 27.89 ? 415 ARG A N   1 
ATOM   3001 C CA  . ARG A 1 417 ? 103.581 47.683 40.743 1.00 26.59 ? 415 ARG A CA  1 
ATOM   3002 C C   . ARG A 1 417 ? 104.864 47.155 40.076 1.00 29.05 ? 415 ARG A C   1 
ATOM   3003 O O   . ARG A 1 417 ? 104.924 47.161 38.841 1.00 27.28 ? 415 ARG A O   1 
ATOM   3004 C CB  . ARG A 1 417 ? 103.721 49.118 41.250 1.00 26.46 ? 415 ARG A CB  1 
ATOM   3005 C CG  . ARG A 1 417 ? 104.800 49.281 42.320 1.00 25.64 ? 415 ARG A CG  1 
ATOM   3006 C CD  . ARG A 1 417 ? 104.751 50.627 42.998 1.00 25.72 ? 415 ARG A CD  1 
ATOM   3007 N NE  . ARG A 1 417 ? 103.561 50.792 43.817 1.00 28.83 ? 415 ARG A NE  1 
ATOM   3008 C CZ  . ARG A 1 417 ? 103.244 51.905 44.484 1.00 30.10 ? 415 ARG A CZ  1 
ATOM   3009 N NH1 . ARG A 1 417 ? 104.016 52.969 44.409 1.00 30.45 ? 415 ARG A NH1 1 
ATOM   3010 N NH2 . ARG A 1 417 ? 102.143 51.960 45.207 1.00 30.30 ? 415 ARG A NH2 1 
ATOM   3011 N N   . SER A 1 418 ? 105.855 46.647 40.827 1.00 27.16 ? 416 SER A N   1 
ATOM   3012 C CA  . SER A 1 418 ? 107.140 46.214 40.213 1.00 29.17 ? 416 SER A CA  1 
ATOM   3013 C C   . SER A 1 418 ? 106.882 45.013 39.306 1.00 24.90 ? 416 SER A C   1 
ATOM   3014 O O   . SER A 1 418 ? 107.525 44.911 38.262 1.00 27.35 ? 416 SER A O   1 
ATOM   3015 C CB  . SER A 1 418 ? 108.222 45.915 41.252 1.00 33.25 ? 416 SER A CB  1 
ATOM   3016 O OG  . SER A 1 418 ? 107.742 44.985 42.216 1.00 32.55 ? 416 SER A OG  1 
ATOM   3017 N N   . GLU A 1 419 ? 105.966 44.128 39.691 1.00 26.80 ? 417 GLU A N   1 
ATOM   3018 C CA  . GLU A 1 419 ? 105.619 42.936 38.872 1.00 24.61 ? 417 GLU A CA  1 
ATOM   3019 C C   . GLU A 1 419 ? 104.933 43.403 37.583 1.00 24.00 ? 417 GLU A C   1 
ATOM   3020 O O   . GLU A 1 419 ? 105.111 42.783 36.521 1.00 24.86 ? 417 GLU A O   1 
ATOM   3021 C CB  . GLU A 1 419 ? 104.725 42.012 39.691 1.00 26.90 ? 417 GLU A CB  1 
ATOM   3022 C CG  . GLU A 1 419 ? 105.480 41.381 40.841 1.00 29.23 ? 417 GLU A CG  1 
ATOM   3023 C CD  . GLU A 1 419 ? 104.629 40.636 41.857 1.00 33.13 ? 417 GLU A CD  1 
ATOM   3024 O OE1 . GLU A 1 419 ? 103.478 41.030 42.131 1.00 33.56 ? 417 GLU A OE1 1 
ATOM   3025 O OE2 . GLU A 1 419 ? 105.148 39.657 42.421 1.00 34.03 ? 417 GLU A OE2 1 
ATOM   3026 N N   . ILE A 1 420 ? 104.105 44.429 37.698 1.00 23.18 ? 418 ILE A N   1 
ATOM   3027 C CA  . ILE A 1 420 ? 103.412 45.007 36.511 1.00 24.07 ? 418 ILE A CA  1 
ATOM   3028 C C   . ILE A 1 420 ? 104.452 45.635 35.598 1.00 24.82 ? 418 ILE A C   1 
ATOM   3029 O O   . ILE A 1 420 ? 104.426 45.301 34.387 1.00 24.89 ? 418 ILE A O   1 
ATOM   3030 C CB  . ILE A 1 420 ? 102.296 45.972 36.932 1.00 23.22 ? 418 ILE A CB  1 
ATOM   3031 C CG1 . ILE A 1 420 ? 101.265 45.191 37.747 1.00 24.21 ? 418 ILE A CG1 1 
ATOM   3032 C CG2 . ILE A 1 420 ? 101.730 46.681 35.707 1.00 22.29 ? 418 ILE A CG2 1 
ATOM   3033 C CD1 . ILE A 1 420 ? 100.267 46.010 38.508 1.00 23.73 ? 418 ILE A CD1 1 
ATOM   3034 N N   . THR A 1 421 ? 105.346 46.484 36.124 1.00 23.29 ? 419 THR A N   1 
ATOM   3035 C CA  . THR A 1 421 ? 106.437 47.068 35.315 1.00 24.53 ? 419 THR A CA  1 
ATOM   3036 C C   . THR A 1 421 ? 107.202 45.952 34.608 1.00 25.44 ? 419 THR A C   1 
ATOM   3037 O O   . THR A 1 421 ? 107.444 46.060 33.419 1.00 24.31 ? 419 THR A O   1 
ATOM   3038 C CB  . THR A 1 421 ? 107.356 47.966 36.149 1.00 26.76 ? 419 THR A CB  1 
ATOM   3039 O OG1 . THR A 1 421 ? 106.479 48.972 36.636 1.00 29.08 ? 419 THR A OG1 1 
ATOM   3040 C CG2 . THR A 1 421 ? 108.501 48.576 35.357 1.00 27.79 ? 419 THR A CG2 1 
ATOM   3041 N N   . ALA A 1 422 ? 107.570 44.906 35.327 1.00 24.56 ? 420 ALA A N   1 
ATOM   3042 C CA  . ALA A 1 422 ? 108.381 43.804 34.769 1.00 28.00 ? 420 ALA A CA  1 
ATOM   3043 C C   . ALA A 1 422 ? 107.660 43.145 33.582 1.00 23.59 ? 420 ALA A C   1 
ATOM   3044 O O   . ALA A 1 422 ? 108.330 42.853 32.579 1.00 25.53 ? 420 ALA A O   1 
ATOM   3045 C CB  . ALA A 1 422 ? 108.682 42.796 35.855 1.00 29.64 ? 420 ALA A CB  1 
ATOM   3046 N N   . VAL A 1 423 ? 106.366 42.817 33.692 1.00 25.15 ? 421 VAL A N   1 
ATOM   3047 C CA  . VAL A 1 423 ? 105.705 42.032 32.607 1.00 25.33 ? 421 VAL A CA  1 
ATOM   3048 C C   . VAL A 1 423 ? 105.479 42.958 31.396 1.00 23.82 ? 421 VAL A C   1 
ATOM   3049 O O   . VAL A 1 423 ? 105.584 42.507 30.272 1.00 24.81 ? 421 VAL A O   1 
ATOM   3050 C CB  . VAL A 1 423 ? 104.430 41.312 33.101 1.00 25.85 ? 421 VAL A CB  1 
ATOM   3051 C CG1 . VAL A 1 423 ? 103.275 42.250 33.441 1.00 27.30 ? 421 VAL A CG1 1 
ATOM   3052 C CG2 . VAL A 1 423 ? 103.986 40.285 32.086 1.00 28.45 ? 421 VAL A CG2 1 
ATOM   3053 N N   . VAL A 1 424 ? 105.144 44.219 31.617 1.00 22.98 ? 422 VAL A N   1 
ATOM   3054 C CA  . VAL A 1 424 ? 104.960 45.202 30.508 1.00 25.40 ? 422 VAL A CA  1 
ATOM   3055 C C   . VAL A 1 424 ? 106.278 45.356 29.726 1.00 28.37 ? 422 VAL A C   1 
ATOM   3056 O O   . VAL A 1 424 ? 106.288 45.308 28.436 1.00 24.85 ? 422 VAL A O   1 
ATOM   3057 C CB  . VAL A 1 424 ? 104.444 46.521 31.106 1.00 24.43 ? 422 VAL A CB  1 
ATOM   3058 C CG1 . VAL A 1 424 ? 104.439 47.634 30.069 1.00 27.44 ? 422 VAL A CG1 1 
ATOM   3059 C CG2 . VAL A 1 424 ? 103.051 46.320 31.725 1.00 22.92 ? 422 VAL A CG2 1 
ATOM   3060 N N   . LYS A 1 425 ? 107.391 45.484 30.446 1.00 28.40 ? 423 LYS A N   1 
ATOM   3061 C CA  . LYS A 1 425 ? 108.722 45.592 29.789 1.00 32.20 ? 423 LYS A CA  1 
ATOM   3062 C C   . LYS A 1 425 ? 109.016 44.277 29.063 1.00 28.98 ? 423 LYS A C   1 
ATOM   3063 O O   . LYS A 1 425 ? 109.495 44.335 27.925 1.00 29.62 ? 423 LYS A O   1 
ATOM   3064 C CB  . LYS A 1 425 ? 109.809 45.953 30.806 1.00 34.08 ? 423 LYS A CB  1 
ATOM   3065 C CG  . LYS A 1 425 ? 109.694 47.381 31.347 1.00 42.02 ? 423 LYS A CG  1 
ATOM   3066 C CD  . LYS A 1 425 ? 110.872 47.833 32.255 1.00 46.95 ? 423 LYS A CD  1 
ATOM   3067 C CE  . LYS A 1 425 ? 110.693 49.282 32.682 1.00 50.57 ? 423 LYS A CE  1 
ATOM   3068 N NZ  . LYS A 1 425 ? 111.742 49.793 33.606 1.00 56.22 ? 423 LYS A NZ  1 
ATOM   3069 N N   . ALA A 1 426 ? 108.733 43.134 29.682 1.00 25.71 ? 424 ALA A N   1 
ATOM   3070 C CA  . ALA A 1 426 ? 109.044 41.829 29.066 1.00 28.68 ? 424 ALA A CA  1 
ATOM   3071 C C   . ALA A 1 426 ? 108.324 41.741 27.708 1.00 26.52 ? 424 ALA A C   1 
ATOM   3072 O O   . ALA A 1 426 ? 108.962 41.328 26.738 1.00 27.54 ? 424 ALA A O   1 
ATOM   3073 C CB  . ALA A 1 426 ? 108.660 40.689 29.973 1.00 28.69 ? 424 ALA A CB  1 
ATOM   3074 N N   . LEU A 1 427 ? 107.041 42.110 27.657 1.00 26.09 ? 425 LEU A N   1 
ATOM   3075 C CA  . LEU A 1 427 ? 106.230 41.970 26.422 1.00 25.20 ? 425 LEU A CA  1 
ATOM   3076 C C   . LEU A 1 427 ? 106.711 42.998 25.405 1.00 27.89 ? 425 LEU A C   1 
ATOM   3077 O O   . LEU A 1 427 ? 106.888 42.617 24.219 1.00 27.74 ? 425 LEU A O   1 
ATOM   3078 C CB  . LEU A 1 427 ? 104.748 42.191 26.727 1.00 26.41 ? 425 LEU A CB  1 
ATOM   3079 C CG  . LEU A 1 427 ? 103.846 41.916 25.533 1.00 29.90 ? 425 LEU A CG  1 
ATOM   3080 C CD1 . LEU A 1 427 ? 103.649 40.425 25.436 1.00 32.70 ? 425 LEU A CD1 1 
ATOM   3081 C CD2 . LEU A 1 427 ? 102.529 42.650 25.667 1.00 32.91 ? 425 LEU A CD2 1 
ATOM   3082 N N   . MET A 1 428 ? 106.816 44.254 25.830 1.00 28.95 ? 426 MET A N   1 
ATOM   3083 C CA  . MET A 1 428 ? 106.992 45.378 24.878 1.00 30.99 ? 426 MET A CA  1 
ATOM   3084 C C   . MET A 1 428 ? 108.472 45.541 24.458 1.00 32.46 ? 426 MET A C   1 
ATOM   3085 O O   . MET A 1 428 ? 108.678 45.987 23.329 1.00 32.13 ? 426 MET A O   1 
ATOM   3086 C CB  . MET A 1 428 ? 106.431 46.685 25.435 1.00 30.60 ? 426 MET A CB  1 
ATOM   3087 C CG  . MET A 1 428 ? 104.969 46.604 25.817 1.00 31.42 ? 426 MET A CG  1 
ATOM   3088 S SD  . MET A 1 428 ? 103.881 46.136 24.439 1.00 33.02 ? 426 MET A SD  1 
ATOM   3089 C CE  . MET A 1 428 ? 103.818 47.663 23.503 1.00 33.37 ? 426 MET A CE  1 
ATOM   3090 N N   . GLU A 1 429 ? 109.468 45.160 25.257 1.00 33.03 ? 427 GLU A N   1 
ATOM   3091 C CA  . GLU A 1 429 ? 110.902 45.393 24.907 1.00 35.55 ? 427 GLU A CA  1 
ATOM   3092 C C   . GLU A 1 429 ? 111.751 44.128 25.092 1.00 38.89 ? 427 GLU A C   1 
ATOM   3093 O O   . GLU A 1 429 ? 112.810 44.070 24.512 1.00 44.56 ? 427 GLU A O   1 
ATOM   3094 C CB  . GLU A 1 429 ? 111.532 46.487 25.776 1.00 43.20 ? 427 GLU A CB  1 
ATOM   3095 C CG  . GLU A 1 429 ? 110.563 47.507 26.326 1.00 47.65 ? 427 GLU A CG  1 
ATOM   3096 C CD  . GLU A 1 429 ? 111.168 48.448 27.355 1.00 57.30 ? 427 GLU A CD  1 
ATOM   3097 O OE1 . GLU A 1 429 ? 112.122 48.043 28.078 1.00 64.93 ? 427 GLU A OE1 1 
ATOM   3098 O OE2 . GLU A 1 429 ? 110.706 49.596 27.418 1.00 69.95 ? 427 GLU A OE2 1 
ATOM   3099 N N   . GLY A 1 430 ? 111.300 43.135 25.842 1.00 35.01 ? 428 GLY A N   1 
ATOM   3100 C CA  . GLY A 1 430 ? 112.147 42.012 26.285 1.00 34.82 ? 428 GLY A CA  1 
ATOM   3101 C C   . GLY A 1 430 ? 112.240 40.877 25.282 1.00 35.77 ? 428 GLY A C   1 
ATOM   3102 O O   . GLY A 1 430 ? 111.405 40.811 24.334 1.00 33.04 ? 428 GLY A O   1 
ATOM   3103 N N   . GLU A 1 431 ? 113.174 39.956 25.545 1.00 35.50 ? 429 GLU A N   1 
ATOM   3104 C CA  . GLU A 1 431 ? 113.395 38.720 24.756 1.00 38.49 ? 429 GLU A CA  1 
ATOM   3105 C C   . GLU A 1 431 ? 112.146 37.857 24.847 1.00 35.11 ? 429 GLU A C   1 
ATOM   3106 O O   . GLU A 1 431 ? 111.805 37.284 23.834 1.00 33.66 ? 429 GLU A O   1 
ATOM   3107 C CB  . GLU A 1 431 ? 114.586 37.887 25.258 1.00 39.21 ? 429 GLU A CB  1 
ATOM   3108 N N   . GLU A 1 432 ? 111.572 37.698 26.044 1.00 34.42 ? 430 GLU A N   1 
ATOM   3109 C CA  . GLU A 1 432 ? 110.279 36.967 26.258 1.00 42.16 ? 430 GLU A CA  1 
ATOM   3110 C C   . GLU A 1 432 ? 109.170 37.512 25.352 1.00 32.52 ? 430 GLU A C   1 
ATOM   3111 O O   . GLU A 1 432 ? 108.411 36.703 24.791 1.00 29.75 ? 430 GLU A O   1 
ATOM   3112 C CB  . GLU A 1 432 ? 109.716 37.161 27.664 1.00 44.44 ? 430 GLU A CB  1 
ATOM   3113 C CG  . GLU A 1 432 ? 110.278 36.239 28.713 1.00 52.66 ? 430 GLU A CG  1 
ATOM   3114 C CD  . GLU A 1 432 ? 109.903 36.716 30.111 1.00 59.84 ? 430 GLU A CD  1 
ATOM   3115 O OE1 . GLU A 1 432 ? 108.992 36.107 30.736 1.00 63.28 ? 430 GLU A OE1 1 
ATOM   3116 O OE2 . GLU A 1 432 ? 110.504 37.721 30.559 1.00 64.48 ? 430 GLU A OE2 1 
ATOM   3117 N N   . GLY A 1 433 ? 109.038 38.843 25.271 1.00 29.16 ? 431 GLY A N   1 
ATOM   3118 C CA  . GLY A 1 433 ? 108.045 39.498 24.394 1.00 29.30 ? 431 GLY A CA  1 
ATOM   3119 C C   . GLY A 1 433 ? 108.222 39.074 22.943 1.00 33.12 ? 431 GLY A C   1 
ATOM   3120 O O   . GLY A 1 433 ? 107.222 38.790 22.255 1.00 27.92 ? 431 GLY A O   1 
ATOM   3121 N N   . LYS A 1 434 ? 109.472 39.049 22.481 1.00 31.81 ? 432 LYS A N   1 
ATOM   3122 C CA  . LYS A 1 434 ? 109.814 38.775 21.069 1.00 35.33 ? 432 LYS A CA  1 
ATOM   3123 C C   . LYS A 1 434 ? 109.329 37.371 20.706 1.00 29.13 ? 432 LYS A C   1 
ATOM   3124 O O   . LYS A 1 434 ? 108.773 37.229 19.625 1.00 30.50 ? 432 LYS A O   1 
ATOM   3125 C CB  . LYS A 1 434 ? 111.325 38.925 20.861 1.00 42.50 ? 432 LYS A CB  1 
ATOM   3126 C CG  . LYS A 1 434 ? 111.811 40.351 21.074 1.00 47.20 ? 432 LYS A CG  1 
ATOM   3127 C CD  . LYS A 1 434 ? 113.266 40.585 20.768 1.00 53.83 ? 432 LYS A CD  1 
ATOM   3128 C CE  . LYS A 1 434 ? 113.632 42.047 20.924 1.00 54.19 ? 432 LYS A CE  1 
ATOM   3129 N NZ  . LYS A 1 434 ? 115.101 42.212 20.884 1.00 62.54 ? 432 LYS A NZ  1 
ATOM   3130 N N   . LYS A 1 435 ? 109.551 36.405 21.590 1.00 30.14 ? 433 LYS A N   1 
ATOM   3131 C CA  . LYS A 1 435 ? 109.186 34.981 21.382 1.00 34.82 ? 433 LYS A CA  1 
ATOM   3132 C C   . LYS A 1 435 ? 107.661 34.879 21.326 1.00 30.38 ? 433 LYS A C   1 
ATOM   3133 O O   . LYS A 1 435 ? 107.138 34.208 20.445 1.00 29.05 ? 433 LYS A O   1 
ATOM   3134 C CB  . LYS A 1 435 ? 109.770 34.124 22.507 1.00 40.29 ? 433 LYS A CB  1 
ATOM   3135 C CG  . LYS A 1 435 ? 111.255 33.816 22.339 1.00 49.59 ? 433 LYS A CG  1 
ATOM   3136 C CD  . LYS A 1 435 ? 111.929 33.331 23.589 1.00 61.00 ? 433 LYS A CD  1 
ATOM   3137 C CE  . LYS A 1 435 ? 113.208 34.093 23.883 1.00 69.56 ? 433 LYS A CE  1 
ATOM   3138 N NZ  . LYS A 1 435 ? 114.190 33.247 24.599 1.00 77.20 ? 433 LYS A NZ  1 
ATOM   3139 N N   . VAL A 1 436 ? 106.977 35.552 22.245 1.00 27.16 ? 434 VAL A N   1 
ATOM   3140 C CA  . VAL A 1 436 ? 105.499 35.465 22.366 1.00 30.26 ? 434 VAL A CA  1 
ATOM   3141 C C   . VAL A 1 436 ? 104.898 36.116 21.118 1.00 26.30 ? 434 VAL A C   1 
ATOM   3142 O O   . VAL A 1 436 ? 103.948 35.570 20.522 1.00 26.80 ? 434 VAL A O   1 
ATOM   3143 C CB  . VAL A 1 436 ? 105.059 36.077 23.714 1.00 31.79 ? 434 VAL A CB  1 
ATOM   3144 C CG1 . VAL A 1 436 ? 103.651 36.567 23.642 1.00 36.33 ? 434 VAL A CG1 1 
ATOM   3145 C CG2 . VAL A 1 436 ? 105.222 35.062 24.842 1.00 35.69 ? 434 VAL A CG2 1 
ATOM   3146 N N   . ARG A 1 437 ? 105.487 37.225 20.682 1.00 26.65 ? 435 ARG A N   1 
ATOM   3147 C CA  . ARG A 1 437 ? 105.026 37.992 19.500 1.00 28.01 ? 435 ARG A CA  1 
ATOM   3148 C C   . ARG A 1 437 ? 105.189 37.133 18.234 1.00 29.95 ? 435 ARG A C   1 
ATOM   3149 O O   . ARG A 1 437 ? 104.275 37.125 17.403 1.00 27.04 ? 435 ARG A O   1 
ATOM   3150 C CB  . ARG A 1 437 ? 105.784 39.330 19.418 1.00 28.63 ? 435 ARG A CB  1 
ATOM   3151 C CG  . ARG A 1 437 ? 105.388 40.203 18.237 1.00 32.84 ? 435 ARG A CG  1 
ATOM   3152 C CD  . ARG A 1 437 ? 105.948 41.623 18.314 1.00 37.28 ? 435 ARG A CD  1 
ATOM   3153 N NE  . ARG A 1 437 ? 105.255 42.398 19.340 1.00 44.98 ? 435 ARG A NE  1 
ATOM   3154 C CZ  . ARG A 1 437 ? 105.737 42.684 20.542 1.00 44.91 ? 435 ARG A CZ  1 
ATOM   3155 N NH1 . ARG A 1 437 ? 106.962 42.305 20.877 1.00 54.02 ? 435 ARG A NH1 1 
ATOM   3156 N NH2 . ARG A 1 437 ? 105.003 43.380 21.395 1.00 36.90 ? 435 ARG A NH2 1 
ATOM   3157 N N   . ASN A 1 438 ? 106.302 36.416 18.086 1.00 30.66 ? 436 ASN A N   1 
ATOM   3158 C CA  . ASN A 1 438 ? 106.524 35.494 16.938 1.00 32.45 ? 436 ASN A CA  1 
ATOM   3159 C C   . ASN A 1 438 ? 105.511 34.342 16.966 1.00 26.47 ? 436 ASN A C   1 
ATOM   3160 O O   . ASN A 1 438 ? 105.000 34.012 15.918 1.00 26.27 ? 436 ASN A O   1 
ATOM   3161 C CB  . ASN A 1 438 ? 107.913 34.863 16.956 1.00 38.04 ? 436 ASN A CB  1 
ATOM   3162 C CG  . ASN A 1 438 ? 109.003 35.838 16.580 1.00 46.76 ? 436 ASN A CG  1 
ATOM   3163 O OD1 . ASN A 1 438 ? 108.763 36.760 15.806 1.00 47.50 ? 436 ASN A OD1 1 
ATOM   3164 N ND2 . ASN A 1 438 ? 110.201 35.620 17.110 1.00 50.57 ? 436 ASN A ND2 1 
ATOM   3165 N N   . ARG A 1 439 ? 105.243 33.764 18.131 1.00 26.57 ? 437 ARG A N   1 
ATOM   3166 C CA  . ARG A 1 439 ? 104.288 32.637 18.247 1.00 26.93 ? 437 ARG A CA  1 
ATOM   3167 C C   . ARG A 1 439 ? 102.889 33.169 17.937 1.00 27.65 ? 437 ARG A C   1 
ATOM   3168 O O   . ARG A 1 439 ? 102.130 32.464 17.260 1.00 23.06 ? 437 ARG A O   1 
ATOM   3169 C CB  . ARG A 1 439 ? 104.437 31.941 19.598 1.00 28.43 ? 437 ARG A CB  1 
ATOM   3170 C CG  . ARG A 1 439 ? 105.738 31.165 19.704 1.00 31.80 ? 437 ARG A CG  1 
ATOM   3171 C CD  . ARG A 1 439 ? 105.767 30.305 20.938 1.00 32.96 ? 437 ARG A CD  1 
ATOM   3172 N NE  . ARG A 1 439 ? 105.812 31.103 22.135 1.00 37.32 ? 437 ARG A NE  1 
ATOM   3173 C CZ  . ARG A 1 439 ? 106.848 31.248 22.951 1.00 41.33 ? 437 ARG A CZ  1 
ATOM   3174 N NH1 . ARG A 1 439 ? 106.714 32.003 24.026 1.00 39.81 ? 437 ARG A NH1 1 
ATOM   3175 N NH2 . ARG A 1 439 ? 108.001 30.646 22.713 1.00 47.78 ? 437 ARG A NH2 1 
ATOM   3176 N N   . MET A 1 440 ? 102.562 34.391 18.393 1.00 25.16 ? 438 MET A N   1 
ATOM   3177 C CA  . MET A 1 440 ? 101.223 34.978 18.160 1.00 24.01 ? 438 MET A CA  1 
ATOM   3178 C C   . MET A 1 440 ? 101.050 35.289 16.673 1.00 23.93 ? 438 MET A C   1 
ATOM   3179 O O   . MET A 1 440 ? 99.926  35.099 16.167 1.00 22.61 ? 438 MET A O   1 
ATOM   3180 C CB  . MET A 1 440 ? 100.982 36.251 18.980 1.00 24.34 ? 438 MET A CB  1 
ATOM   3181 C CG  . MET A 1 440 ? 99.549  36.767 18.819 1.00 24.92 ? 438 MET A CG  1 
ATOM   3182 S SD  . MET A 1 440 ? 98.274  35.619 19.288 1.00 24.46 ? 438 MET A SD  1 
ATOM   3183 C CE  . MET A 1 440 ? 97.830  36.273 20.897 1.00 23.19 ? 438 MET A CE  1 
ATOM   3184 N N   . LYS A 1 441 ? 102.111 35.696 15.965 1.00 23.13 ? 439 LYS A N   1 
ATOM   3185 C CA  . LYS A 1 441 ? 102.027 35.948 14.516 1.00 25.58 ? 439 LYS A CA  1 
ATOM   3186 C C   . LYS A 1 441 ? 101.671 34.649 13.803 1.00 23.65 ? 439 LYS A C   1 
ATOM   3187 O O   . LYS A 1 441 ? 100.859 34.686 12.891 1.00 26.62 ? 439 LYS A O   1 
ATOM   3188 C CB  . LYS A 1 441 ? 103.341 36.494 13.964 1.00 33.64 ? 439 LYS A CB  1 
ATOM   3189 C CG  . LYS A 1 441 ? 103.307 36.837 12.482 1.00 39.86 ? 439 LYS A CG  1 
ATOM   3190 C CD  . LYS A 1 441 ? 104.638 37.352 11.948 1.00 48.41 ? 439 LYS A CD  1 
ATOM   3191 C CE  . LYS A 1 441 ? 105.012 36.797 10.591 1.00 55.36 ? 439 LYS A CE  1 
ATOM   3192 N NZ  . LYS A 1 441 ? 106.466 36.500 10.515 1.00 61.70 ? 439 LYS A NZ  1 
ATOM   3193 N N   . GLU A 1 442 ? 102.308 33.553 14.179 1.00 25.09 ? 440 GLU A N   1 
ATOM   3194 C CA  . GLU A 1 442 ? 102.069 32.229 13.552 1.00 24.17 ? 440 GLU A CA  1 
ATOM   3195 C C   . GLU A 1 442 ? 100.634 31.778 13.853 1.00 24.44 ? 440 GLU A C   1 
ATOM   3196 O O   . GLU A 1 442 ? 99.976  31.248 12.948 1.00 22.25 ? 440 GLU A O   1 
ATOM   3197 C CB  . GLU A 1 442 ? 103.119 31.232 14.030 1.00 27.86 ? 440 GLU A CB  1 
ATOM   3198 C CG  . GLU A 1 442 ? 104.512 31.502 13.469 1.00 30.30 ? 440 GLU A CG  1 
ATOM   3199 C CD  . GLU A 1 442 ? 104.597 31.535 11.946 1.00 34.43 ? 440 GLU A CD  1 
ATOM   3200 O OE1 . GLU A 1 442 ? 103.845 30.814 11.274 1.00 38.07 ? 440 GLU A OE1 1 
ATOM   3201 O OE2 . GLU A 1 442 ? 105.349 32.358 11.428 1.00 41.98 ? 440 GLU A OE2 1 
ATOM   3202 N N   . LEU A 1 443 ? 100.144 31.951 15.080 1.00 24.16 ? 441 LEU A N   1 
ATOM   3203 C CA  . LEU A 1 443 ? 98.738  31.627 15.433 1.00 25.04 ? 441 LEU A CA  1 
ATOM   3204 C C   . LEU A 1 443 ? 97.751  32.522 14.636 1.00 23.91 ? 441 LEU A C   1 
ATOM   3205 O O   . LEU A 1 443 ? 96.709  32.009 14.149 1.00 24.56 ? 441 LEU A O   1 
ATOM   3206 C CB  . LEU A 1 443 ? 98.582  31.739 16.957 1.00 23.47 ? 441 LEU A CB  1 
ATOM   3207 C CG  . LEU A 1 443 ? 97.261  31.209 17.520 1.00 27.06 ? 441 LEU A CG  1 
ATOM   3208 C CD1 . LEU A 1 443 ? 97.108  29.707 17.270 1.00 27.80 ? 441 LEU A CD1 1 
ATOM   3209 C CD2 . LEU A 1 443 ? 97.176  31.488 19.023 1.00 27.90 ? 441 LEU A CD2 1 
ATOM   3210 N N   . LYS A 1 444 ? 98.043  33.809 14.451 1.00 22.24 ? 442 LYS A N   1 
ATOM   3211 C CA  . LYS A 1 444 ? 97.185  34.711 13.644 1.00 24.68 ? 442 LYS A CA  1 
ATOM   3212 C C   . LYS A 1 444 ? 97.077  34.143 12.225 1.00 22.50 ? 442 LYS A C   1 
ATOM   3213 O O   . LYS A 1 444 ? 95.991  34.171 11.660 1.00 22.48 ? 442 LYS A O   1 
ATOM   3214 C CB  . LYS A 1 444 ? 97.735  36.141 13.607 1.00 26.29 ? 442 LYS A CB  1 
ATOM   3215 C CG  . LYS A 1 444 ? 97.199  37.024 12.493 1.00 28.51 ? 442 LYS A CG  1 
ATOM   3216 C CD  . LYS A 1 444 ? 98.101  38.232 12.293 1.00 34.00 ? 442 LYS A CD  1 
ATOM   3217 C CE  . LYS A 1 444 ? 97.473  39.396 11.565 1.00 41.01 ? 442 LYS A CE  1 
ATOM   3218 N NZ  . LYS A 1 444 ? 97.436  39.168 10.103 1.00 47.73 ? 442 LYS A NZ  1 
ATOM   3219 N N   . GLU A 1 445 ? 98.177  33.656 11.670 1.00 24.95 ? 443 GLU A N   1 
ATOM   3220 C CA  . GLU A 1 445 ? 98.198  33.107 10.292 1.00 23.48 ? 443 GLU A CA  1 
ATOM   3221 C C   . GLU A 1 445 ? 97.354  31.829 10.252 1.00 22.63 ? 443 GLU A C   1 
ATOM   3222 O O   . GLU A 1 445 ? 96.618  31.633 9.272  1.00 22.30 ? 443 GLU A O   1 
ATOM   3223 C CB  . GLU A 1 445 ? 99.643  32.912 9.847  1.00 26.46 ? 443 GLU A CB  1 
ATOM   3224 C CG  . GLU A 1 445 ? 100.325 34.217 9.540  1.00 34.22 ? 443 GLU A CG  1 
ATOM   3225 C CD  . GLU A 1 445 ? 101.841 34.120 9.382  1.00 45.39 ? 443 GLU A CD  1 
ATOM   3226 O OE1 . GLU A 1 445 ? 102.390 32.994 9.552  1.00 50.30 ? 443 GLU A OE1 1 
ATOM   3227 O OE2 . GLU A 1 445 ? 102.482 35.176 9.089  1.00 48.82 ? 443 GLU A OE2 1 
ATOM   3228 N N   . ALA A 1 446 ? 97.481  30.951 11.252 1.00 22.81 ? 444 ALA A N   1 
ATOM   3229 C CA  . ALA A 1 446 ? 96.613  29.746 11.377 1.00 24.51 ? 444 ALA A CA  1 
ATOM   3230 C C   . ALA A 1 446 ? 95.125  30.143 11.463 1.00 24.42 ? 444 ALA A C   1 
ATOM   3231 O O   . ALA A 1 446 ? 94.295  29.422 10.887 1.00 23.03 ? 444 ALA A O   1 
ATOM   3232 C CB  . ALA A 1 446 ? 97.044  28.912 12.570 1.00 26.67 ? 444 ALA A CB  1 
ATOM   3233 N N   . ALA A 1 447 ? 94.777  31.215 12.202 1.00 22.32 ? 445 ALA A N   1 
ATOM   3234 C CA  . ALA A 1 447 ? 93.394  31.702 12.332 1.00 21.51 ? 445 ALA A CA  1 
ATOM   3235 C C   . ALA A 1 447 ? 92.893  32.183 10.965 1.00 22.82 ? 445 ALA A C   1 
ATOM   3236 O O   . ALA A 1 447 ? 91.749  31.871 10.604 1.00 23.92 ? 445 ALA A O   1 
ATOM   3237 C CB  . ALA A 1 447 ? 93.266  32.770 13.394 1.00 20.97 ? 445 ALA A CB  1 
ATOM   3238 N N   . ALA A 1 448 ? 93.701  32.925 10.224 1.00 21.79 ? 446 ALA A N   1 
ATOM   3239 C CA  . ALA A 1 448 ? 93.324  33.405 8.882  1.00 21.95 ? 446 ALA A CA  1 
ATOM   3240 C C   . ALA A 1 448 ? 93.091  32.202 7.950  1.00 24.51 ? 446 ALA A C   1 
ATOM   3241 O O   . ALA A 1 448 ? 92.085  32.205 7.180  1.00 26.01 ? 446 ALA A O   1 
ATOM   3242 C CB  . ALA A 1 448 ? 94.389  34.343 8.356  1.00 24.28 ? 446 ALA A CB  1 
ATOM   3243 N N   . ARG A 1 449 ? 93.999  31.231 7.968  1.00 26.92 ? 447 ARG A N   1 
ATOM   3244 C CA  . ARG A 1 449 ? 93.790  29.969 7.201  1.00 28.10 ? 447 ARG A CA  1 
ATOM   3245 C C   . ARG A 1 449 ? 92.462  29.329 7.625  1.00 26.27 ? 447 ARG A C   1 
ATOM   3246 O O   . ARG A 1 449 ? 91.723  28.928 6.748  1.00 22.69 ? 447 ARG A O   1 
ATOM   3247 C CB  . ARG A 1 449 ? 94.980  29.028 7.348  1.00 28.89 ? 447 ARG A CB  1 
ATOM   3248 C CG  . ARG A 1 449 ? 96.223  29.520 6.613  1.00 34.67 ? 447 ARG A CG  1 
ATOM   3249 C CD  . ARG A 1 449 ? 97.286  28.439 6.477  1.00 35.36 ? 447 ARG A CD  1 
ATOM   3250 N NE  . ARG A 1 449 ? 97.776  28.003 7.776  1.00 31.95 ? 447 ARG A NE  1 
ATOM   3251 C CZ  . ARG A 1 449 ? 98.802  28.535 8.427  1.00 33.16 ? 447 ARG A CZ  1 
ATOM   3252 N NH1 . ARG A 1 449 ? 99.510  29.519 7.907  1.00 36.04 ? 447 ARG A NH1 1 
ATOM   3253 N NH2 . ARG A 1 449 ? 99.164  28.037 9.581  1.00 31.57 ? 447 ARG A NH2 1 
ATOM   3254 N N   . ALA A 1 450 ? 92.168  29.201 8.930  1.00 24.54 ? 448 ALA A N   1 
ATOM   3255 C CA  . ALA A 1 450 ? 90.947  28.519 9.397  1.00 23.62 ? 448 ALA A CA  1 
ATOM   3256 C C   . ALA A 1 450 ? 89.679  29.151 8.783  1.00 24.76 ? 448 ALA A C   1 
ATOM   3257 O O   . ALA A 1 450 ? 88.704  28.415 8.576  1.00 25.81 ? 448 ALA A O   1 
ATOM   3258 C CB  . ALA A 1 450 ? 90.899  28.514 10.899 1.00 24.68 ? 448 ALA A CB  1 
ATOM   3259 N N   . VAL A 1 451 ? 89.647  30.456 8.533  1.00 22.75 ? 449 VAL A N   1 
ATOM   3260 C CA  . VAL A 1 451 ? 88.404  31.159 8.107  1.00 25.37 ? 449 VAL A CA  1 
ATOM   3261 C C   . VAL A 1 451 ? 88.457  31.428 6.599  1.00 27.05 ? 449 VAL A C   1 
ATOM   3262 O O   . VAL A 1 451 ? 87.519  32.018 6.108  1.00 27.88 ? 449 VAL A O   1 
ATOM   3263 C CB  . VAL A 1 451 ? 88.112  32.433 8.922  1.00 26.54 ? 449 VAL A CB  1 
ATOM   3264 C CG1 . VAL A 1 451 ? 87.927  32.078 10.388 1.00 28.52 ? 449 VAL A CG1 1 
ATOM   3265 C CG2 . VAL A 1 451 ? 89.156  33.530 8.742  1.00 27.22 ? 449 VAL A CG2 1 
ATOM   3266 N N   . SER A 1 452 ? 89.470  30.914 5.906  1.00 28.37 ? 450 SER A N   1 
ATOM   3267 C CA  . SER A 1 452 ? 89.640  31.060 4.438  1.00 29.93 ? 450 SER A CA  1 
ATOM   3268 C C   . SER A 1 452 ? 88.587  30.166 3.775  1.00 32.95 ? 450 SER A C   1 
ATOM   3269 O O   . SER A 1 452 ? 87.983  29.361 4.484  1.00 27.55 ? 450 SER A O   1 
ATOM   3270 C CB  . SER A 1 452 ? 91.060  30.695 4.025  1.00 28.42 ? 450 SER A CB  1 
ATOM   3271 O OG  . SER A 1 452 ? 91.292  29.282 4.167  1.00 28.08 ? 450 SER A OG  1 
ATOM   3272 N N   . ASP A 1 453 ? 88.386  30.294 2.466  1.00 31.52 ? 451 ASP A N   1 
ATOM   3273 C CA  . ASP A 1 453 ? 87.428  29.460 1.693  1.00 33.94 ? 451 ASP A CA  1 
ATOM   3274 C C   . ASP A 1 453 ? 87.670  27.971 1.930  1.00 29.18 ? 451 ASP A C   1 
ATOM   3275 O O   . ASP A 1 453 ? 86.690  27.203 1.908  1.00 29.98 ? 451 ASP A O   1 
ATOM   3276 C CB  . ASP A 1 453 ? 87.580  29.677 0.191  1.00 42.63 ? 451 ASP A CB  1 
ATOM   3277 C CG  . ASP A 1 453 ? 86.537  30.618 -0.357 1.00 55.48 ? 451 ASP A CG  1 
ATOM   3278 O OD1 . ASP A 1 453 ? 85.340  30.414 -0.028 1.00 61.41 ? 451 ASP A OD1 1 
ATOM   3279 O OD2 . ASP A 1 453 ? 86.929  31.527 -1.118 1.00 62.19 ? 451 ASP A OD2 1 
ATOM   3280 N N   . ASP A 1 454 ? 88.929  27.564 2.055  1.00 24.81 ? 452 ASP A N   1 
ATOM   3281 C CA  . ASP A 1 454 ? 89.288  26.133 2.188  1.00 25.64 ? 452 ASP A CA  1 
ATOM   3282 C C   . ASP A 1 454 ? 89.683  25.812 3.633  1.00 26.41 ? 452 ASP A C   1 
ATOM   3283 O O   . ASP A 1 454 ? 90.305  24.771 3.833  1.00 26.30 ? 452 ASP A O   1 
ATOM   3284 C CB  . ASP A 1 454 ? 90.358  25.746 1.165  1.00 28.33 ? 452 ASP A CB  1 
ATOM   3285 C CG  . ASP A 1 454 ? 90.503  24.239 1.011  1.00 29.92 ? 452 ASP A CG  1 
ATOM   3286 O OD1 . ASP A 1 454 ? 89.473  23.523 1.045  1.00 32.35 ? 452 ASP A OD1 1 
ATOM   3287 O OD2 . ASP A 1 454 ? 91.640  23.787 0.959  1.00 34.78 ? 452 ASP A OD2 1 
ATOM   3288 N N   . GLY A 1 455 ? 89.345  26.671 4.601  1.00 27.37 ? 453 GLY A N   1 
ATOM   3289 C CA  . GLY A 1 455 ? 89.756  26.482 6.007  1.00 26.40 ? 453 GLY A CA  1 
ATOM   3290 C C   . GLY A 1 455 ? 88.796  25.621 6.825  1.00 24.60 ? 453 GLY A C   1 
ATOM   3291 O O   . GLY A 1 455 ? 87.610  25.560 6.507  1.00 25.54 ? 453 GLY A O   1 
ATOM   3292 N N   . ALA A 1 456 ? 89.288  25.040 7.921  1.00 25.19 ? 454 ALA A N   1 
ATOM   3293 C CA  . ALA A 1 456 ? 88.555  24.125 8.810  1.00 25.15 ? 454 ALA A CA  1 
ATOM   3294 C C   . ALA A 1 456 ? 87.285  24.795 9.347  1.00 25.68 ? 454 ALA A C   1 
ATOM   3295 O O   . ALA A 1 456 ? 86.293  24.136 9.446  1.00 24.21 ? 454 ALA A O   1 
ATOM   3296 C CB  . ALA A 1 456 ? 89.446  23.663 9.939  1.00 28.92 ? 454 ALA A CB  1 
ATOM   3297 N N   . SER A 1 457 ? 87.278  26.087 9.673  1.00 26.00 ? 455 SER A N   1 
ATOM   3298 C CA  . SER A 1 457 ? 86.077  26.710 10.268 1.00 25.70 ? 455 SER A CA  1 
ATOM   3299 C C   . SER A 1 457 ? 85.008  26.898 9.183  1.00 26.67 ? 455 SER A C   1 
ATOM   3300 O O   . SER A 1 457 ? 83.863  26.564 9.416  1.00 22.68 ? 455 SER A O   1 
ATOM   3301 C CB  . SER A 1 457 ? 86.465  27.952 10.948 1.00 27.34 ? 455 SER A CB  1 
ATOM   3302 O OG  . SER A 1 457 ? 87.448  27.609 11.934 1.00 31.61 ? 455 SER A OG  1 
ATOM   3303 N N   . THR A 1 458 ? 85.407  27.402 8.016  1.00 24.36 ? 456 THR A N   1 
ATOM   3304 C CA  . THR A 1 458 ? 84.509  27.540 6.861  1.00 25.85 ? 456 THR A CA  1 
ATOM   3305 C C   . THR A 1 458 ? 83.901  26.162 6.516  1.00 22.07 ? 456 THR A C   1 
ATOM   3306 O O   . THR A 1 458 ? 82.708  26.122 6.210  1.00 23.73 ? 456 THR A O   1 
ATOM   3307 C CB  . THR A 1 458 ? 85.260  28.198 5.698  1.00 26.22 ? 456 THR A CB  1 
ATOM   3308 O OG1 . THR A 1 458 ? 85.884  29.374 6.229  1.00 24.16 ? 456 THR A OG1 1 
ATOM   3309 C CG2 . THR A 1 458 ? 84.351  28.529 4.543  1.00 28.13 ? 456 THR A CG2 1 
ATOM   3310 N N   . ILE A 1 459 ? 84.689  25.107 6.537  1.00 23.28 ? 457 ILE A N   1 
ATOM   3311 C CA  . ILE A 1 459 ? 84.232  23.736 6.174  1.00 22.72 ? 457 ILE A CA  1 
ATOM   3312 C C   . ILE A 1 459 ? 83.203  23.282 7.219  1.00 24.49 ? 457 ILE A C   1 
ATOM   3313 O O   . ILE A 1 459 ? 82.134  22.718 6.832  1.00 23.77 ? 457 ILE A O   1 
ATOM   3314 C CB  . ILE A 1 459 ? 85.427  22.796 6.042  1.00 22.99 ? 457 ILE A CB  1 
ATOM   3315 C CG1 . ILE A 1 459 ? 86.257  23.114 4.795  1.00 24.03 ? 457 ILE A CG1 1 
ATOM   3316 C CG2 . ILE A 1 459 ? 84.973  21.351 6.086  1.00 23.68 ? 457 ILE A CG2 1 
ATOM   3317 C CD1 . ILE A 1 459 ? 87.590  22.408 4.719  1.00 25.06 ? 457 ILE A CD1 1 
ATOM   3318 N N   . ALA A 1 460 ? 83.472  23.561 8.508  1.00 23.86 ? 458 ALA A N   1 
ATOM   3319 C CA  . ALA A 1 460 ? 82.582  23.176 9.622  1.00 22.98 ? 458 ALA A CA  1 
ATOM   3320 C C   . ALA A 1 460 ? 81.244  23.890 9.447  1.00 21.39 ? 458 ALA A C   1 
ATOM   3321 O O   . ALA A 1 460 ? 80.213  23.229 9.551  1.00 25.01 ? 458 ALA A O   1 
ATOM   3322 C CB  . ALA A 1 460 ? 83.271  23.442 10.969 1.00 23.22 ? 458 ALA A CB  1 
ATOM   3323 N N   . ILE A 1 461 ? 81.232  25.191 9.127  1.00 23.52 ? 459 ILE A N   1 
ATOM   3324 C CA  . ILE A 1 461 ? 79.985  25.959 8.876  1.00 24.65 ? 459 ILE A CA  1 
ATOM   3325 C C   . ILE A 1 461 ? 79.221  25.354 7.687  1.00 24.19 ? 459 ILE A C   1 
ATOM   3326 O O   . ILE A 1 461 ? 77.971  25.229 7.785  1.00 20.91 ? 459 ILE A O   1 
ATOM   3327 C CB  . ILE A 1 461 ? 80.258  27.476 8.736  1.00 25.28 ? 459 ILE A CB  1 
ATOM   3328 C CG1 . ILE A 1 461 ? 80.737  28.080 10.067 1.00 27.01 ? 459 ILE A CG1 1 
ATOM   3329 C CG2 . ILE A 1 461 ? 78.992  28.167 8.239  1.00 27.72 ? 459 ILE A CG2 1 
ATOM   3330 C CD1 . ILE A 1 461 ? 81.305  29.474 9.937  1.00 29.79 ? 459 ILE A CD1 1 
ATOM   3331 N N   . ALA A 1 462 ? 79.910  25.038 6.595  1.00 24.82 ? 460 ALA A N   1 
ATOM   3332 C CA  . ALA A 1 462 ? 79.320  24.371 5.407  1.00 24.81 ? 460 ALA A CA  1 
ATOM   3333 C C   . ALA A 1 462 ? 78.721  23.013 5.787  1.00 22.96 ? 460 ALA A C   1 
ATOM   3334 O O   . ALA A 1 462 ? 77.610  22.693 5.339  1.00 23.89 ? 460 ALA A O   1 
ATOM   3335 C CB  . ALA A 1 462 ? 80.356  24.204 4.312  1.00 25.69 ? 460 ALA A CB  1 
ATOM   3336 N N   . ASP A 1 463 ? 79.431  22.231 6.583  1.00 24.85 ? 461 ASP A N   1 
ATOM   3337 C CA  . ASP A 1 463 ? 78.956  20.932 7.118  1.00 24.24 ? 461 ASP A CA  1 
ATOM   3338 C C   . ASP A 1 463 ? 77.639  21.124 7.863  1.00 23.35 ? 461 ASP A C   1 
ATOM   3339 O O   . ASP A 1 463 ? 76.675  20.396 7.563  1.00 22.20 ? 461 ASP A O   1 
ATOM   3340 C CB  . ASP A 1 463 ? 79.962  20.303 8.076  1.00 29.79 ? 461 ASP A CB  1 
ATOM   3341 C CG  . ASP A 1 463 ? 81.192  19.686 7.444  1.00 40.03 ? 461 ASP A CG  1 
ATOM   3342 O OD1 . ASP A 1 463 ? 81.271  19.664 6.178  1.00 40.51 ? 461 ASP A OD1 1 
ATOM   3343 O OD2 . ASP A 1 463 ? 82.091  19.257 8.238  1.00 52.18 ? 461 ASP A OD2 1 
ATOM   3344 N N   . LEU A 1 464 ? 77.591  22.045 8.828  1.00 22.97 ? 462 LEU A N   1 
ATOM   3345 C CA  . LEU A 1 464 ? 76.332  22.374 9.539  1.00 24.16 ? 462 LEU A CA  1 
ATOM   3346 C C   . LEU A 1 464 ? 75.248  22.802 8.552  1.00 23.22 ? 462 LEU A C   1 
ATOM   3347 O O   . LEU A 1 464 ? 74.085  22.323 8.691  1.00 23.71 ? 462 LEU A O   1 
ATOM   3348 C CB  . LEU A 1 464 ? 76.550  23.483 10.579 1.00 23.34 ? 462 LEU A CB  1 
ATOM   3349 C CG  . LEU A 1 464 ? 77.428  23.088 11.751 1.00 25.10 ? 462 LEU A CG  1 
ATOM   3350 C CD1 . LEU A 1 464 ? 77.946  24.340 12.495 1.00 23.97 ? 462 LEU A CD1 1 
ATOM   3351 C CD2 . LEU A 1 464 ? 76.635  22.166 12.677 1.00 23.44 ? 462 LEU A CD2 1 
ATOM   3352 N N   . ALA A 1 465 ? 75.567  23.708 7.610  1.00 24.22 ? 463 ALA A N   1 
ATOM   3353 C CA  . ALA A 1 465 ? 74.589  24.145 6.589  1.00 22.29 ? 463 ALA A CA  1 
ATOM   3354 C C   . ALA A 1 465 ? 74.004  22.913 5.875  1.00 25.21 ? 463 ALA A C   1 
ATOM   3355 O O   . ALA A 1 465 ? 72.786  22.884 5.638  1.00 25.16 ? 463 ALA A O   1 
ATOM   3356 C CB  . ALA A 1 465 ? 75.200  25.130 5.632  1.00 22.32 ? 463 ALA A CB  1 
ATOM   3357 N N   . GLN A 1 466 ? 74.826  21.933 5.517  1.00 25.53 ? 464 GLN A N   1 
ATOM   3358 C CA  . GLN A 1 466 ? 74.339  20.745 4.765  1.00 26.20 ? 464 GLN A CA  1 
ATOM   3359 C C   . GLN A 1 466 ? 73.441  19.893 5.671  1.00 25.59 ? 464 GLN A C   1 
ATOM   3360 O O   . GLN A 1 466 ? 72.426  19.397 5.218  1.00 25.52 ? 464 GLN A O   1 
ATOM   3361 C CB  . GLN A 1 466 ? 75.520  19.931 4.242  1.00 28.20 ? 464 GLN A CB  1 
ATOM   3362 C CG  . GLN A 1 466 ? 76.269  20.605 3.096  1.00 29.48 ? 464 GLN A CG  1 
ATOM   3363 C CD  . GLN A 1 466 ? 77.244  19.703 2.365  1.00 35.83 ? 464 GLN A CD  1 
ATOM   3364 O OE1 . GLN A 1 466 ? 78.324  19.368 2.843  1.00 40.02 ? 464 GLN A OE1 1 
ATOM   3365 N NE2 . GLN A 1 466 ? 76.877  19.334 1.148  1.00 40.79 ? 464 GLN A NE2 1 
ATOM   3366 N N   . LYS A 1 467 ? 73.785  19.763 6.935  1.00 25.18 ? 465 LYS A N   1 
ATOM   3367 C CA  . LYS A 1 467 ? 72.930  19.062 7.933  1.00 28.33 ? 465 LYS A CA  1 
ATOM   3368 C C   . LYS A 1 467 ? 71.554  19.738 8.027  1.00 25.82 ? 465 LYS A C   1 
ATOM   3369 O O   . LYS A 1 467 ? 70.519  19.049 7.941  1.00 23.31 ? 465 LYS A O   1 
ATOM   3370 C CB  . LYS A 1 467 ? 73.623  19.052 9.295  1.00 31.70 ? 465 LYS A CB  1 
ATOM   3371 C CG  . LYS A 1 467 ? 74.915  18.251 9.346  1.00 36.34 ? 465 LYS A CG  1 
ATOM   3372 C CD  . LYS A 1 467 ? 74.675  16.776 9.316  1.00 45.01 ? 465 LYS A CD  1 
ATOM   3373 C CE  . LYS A 1 467 ? 75.944  15.969 9.480  1.00 51.89 ? 465 LYS A CE  1 
ATOM   3374 N NZ  . LYS A 1 467 ? 76.601  15.731 8.176  1.00 56.43 ? 465 LYS A NZ  1 
ATOM   3375 N N   . TRP A 1 468 ? 71.524  21.051 8.192  1.00 21.61 ? 466 TRP A N   1 
ATOM   3376 C CA  . TRP A 1 468 ? 70.248  21.772 8.309  1.00 23.00 ? 466 TRP A CA  1 
ATOM   3377 C C   . TRP A 1 468 ? 69.435  21.690 7.009  1.00 23.45 ? 466 TRP A C   1 
ATOM   3378 O O   . TRP A 1 468 ? 68.205  21.492 7.058  1.00 25.95 ? 466 TRP A O   1 
ATOM   3379 C CB  . TRP A 1 468 ? 70.527  23.194 8.791  1.00 21.53 ? 466 TRP A CB  1 
ATOM   3380 C CG  . TRP A 1 468 ? 70.965  23.215 10.225 1.00 23.80 ? 466 TRP A CG  1 
ATOM   3381 C CD1 . TRP A 1 468 ? 70.528  22.400 11.238 1.00 27.70 ? 466 TRP A CD1 1 
ATOM   3382 C CD2 . TRP A 1 468 ? 71.889  24.131 10.834 1.00 22.40 ? 466 TRP A CD2 1 
ATOM   3383 N NE1 . TRP A 1 468 ? 71.135  22.738 12.425 1.00 25.00 ? 466 TRP A NE1 1 
ATOM   3384 C CE2 . TRP A 1 468 ? 71.969  23.797 12.205 1.00 24.14 ? 466 TRP A CE2 1 
ATOM   3385 C CE3 . TRP A 1 468 ? 72.668  25.191 10.353 1.00 22.86 ? 466 TRP A CE3 1 
ATOM   3386 C CZ2 . TRP A 1 468 ? 72.784  24.500 13.095 1.00 25.07 ? 466 TRP A CZ2 1 
ATOM   3387 C CZ3 . TRP A 1 468 ? 73.486  25.870 11.234 1.00 24.09 ? 466 TRP A CZ3 1 
ATOM   3388 C CH2 . TRP A 1 468 ? 73.539  25.525 12.584 1.00 24.21 ? 466 TRP A CH2 1 
ATOM   3389 N N   . ARG A 1 469 ? 70.063  21.882 5.866  1.00 23.36 ? 467 ARG A N   1 
ATOM   3390 C CA  . ARG A 1 469 ? 69.332  21.731 4.589  1.00 23.65 ? 467 ARG A CA  1 
ATOM   3391 C C   . ARG A 1 469 ? 68.721  20.323 4.434  1.00 23.83 ? 467 ARG A C   1 
ATOM   3392 O O   . ARG A 1 469 ? 67.603  20.232 3.854  1.00 23.78 ? 467 ARG A O   1 
ATOM   3393 C CB  . ARG A 1 469 ? 70.289  22.062 3.436  1.00 25.77 ? 467 ARG A CB  1 
ATOM   3394 C CG  . ARG A 1 469 ? 69.612  22.051 2.068  1.00 27.66 ? 467 ARG A CG  1 
ATOM   3395 C CD  . ARG A 1 469 ? 70.666  22.161 0.983  1.00 27.95 ? 467 ARG A CD  1 
ATOM   3396 N NE  . ARG A 1 469 ? 71.234  23.498 1.038  1.00 27.14 ? 467 ARG A NE  1 
ATOM   3397 C CZ  . ARG A 1 469 ? 72.477  23.804 1.401  1.00 25.68 ? 467 ARG A CZ  1 
ATOM   3398 N NH1 . ARG A 1 469 ? 73.361  22.870 1.701  1.00 26.36 ? 467 ARG A NH1 1 
ATOM   3399 N NH2 . ARG A 1 469 ? 72.860  25.069 1.414  1.00 27.82 ? 467 ARG A NH2 1 
ATOM   3400 N N   . SER A 1 470 ? 69.409  19.260 4.863  1.00 27.92 ? 468 SER A N   1 
ATOM   3401 C CA  . SER A 1 470 ? 68.918  17.862 4.700  1.00 31.74 ? 468 SER A CA  1 
ATOM   3402 C C   . SER A 1 470 ? 67.631  17.643 5.515  1.00 32.39 ? 468 SER A C   1 
ATOM   3403 O O   . SER A 1 470 ? 66.852  16.767 5.141  1.00 29.77 ? 468 SER A O   1 
ATOM   3404 C CB  . SER A 1 470 ? 69.957  16.843 5.037  1.00 31.73 ? 468 SER A CB  1 
ATOM   3405 O OG  . SER A 1 470 ? 70.164  16.814 6.427  1.00 35.64 ? 468 SER A OG  1 
ATOM   3406 N N   . SER A 1 471 ? 67.393  18.446 6.556  1.00 32.24 ? 469 SER A N   1 
ATOM   3407 C CA  . SER A 1 471 ? 66.161  18.408 7.382  1.00 32.70 ? 469 SER A CA  1 
ATOM   3408 C C   . SER A 1 471 ? 64.964  19.029 6.675  1.00 34.47 ? 469 SER A C   1 
ATOM   3409 O O   . SER A 1 471 ? 63.879  18.947 7.266  1.00 36.59 ? 469 SER A O   1 
ATOM   3410 C CB  . SER A 1 471 ? 66.372  19.106 8.692  1.00 34.67 ? 469 SER A CB  1 
ATOM   3411 O OG  . SER A 1 471 ? 67.308  18.403 9.452  1.00 35.25 ? 469 SER A OG  1 
ATOM   3412 N N   . MET A 1 472 ? 65.119  19.639 5.492  1.00 33.49 ? 470 MET A N   1 
ATOM   3413 C CA  . MET A 1 472 ? 63.983  20.293 4.771  1.00 34.68 ? 470 MET A CA  1 
ATOM   3414 C C   . MET A 1 472 ? 62.983  19.245 4.265  1.00 38.25 ? 470 MET A C   1 
ATOM   3415 O O   . MET A 1 472 ? 63.523  18.182 3.987  1.00 41.92 ? 470 MET A O   1 
ATOM   3416 C CB  . MET A 1 472 ? 64.494  21.125 3.597  1.00 31.85 ? 470 MET A CB  1 
ATOM   3417 C CG  . MET A 1 472 ? 65.299  22.305 4.096  1.00 33.07 ? 470 MET A CG  1 
ATOM   3418 S SD  . MET A 1 472 ? 64.169  23.528 4.800  1.00 37.01 ? 470 MET A SD  1 
ATOM   3419 C CE  . MET A 1 472 ? 63.819  24.427 3.291  1.00 40.20 ? 470 MET A CE  1 
HETATM 3420 O O   . HOH B 2 .   ? 83.248  48.491 28.088 1.00 42.45 ? 501 HOH A O   1 
HETATM 3421 O O   . HOH B 2 .   ? 72.577  28.834 28.361 1.00 44.51 ? 502 HOH A O   1 
HETATM 3422 O O   . HOH B 2 .   ? 49.918  24.539 21.850 1.00 54.10 ? 503 HOH A O   1 
HETATM 3423 O O   . HOH B 2 .   ? 84.330  31.316 36.332 1.00 31.71 ? 504 HOH A O   1 
HETATM 3424 O O   . HOH B 2 .   ? 53.524  24.503 13.096 1.00 36.09 ? 505 HOH A O   1 
HETATM 3425 O O   . HOH B 2 .   ? 59.689  21.944 11.866 1.00 36.40 ? 506 HOH A O   1 
HETATM 3426 O O   . HOH B 2 .   ? 80.587  14.789 21.332 1.00 37.59 ? 507 HOH A O   1 
HETATM 3427 O O   . HOH B 2 .   ? 65.853  15.818 14.307 1.00 46.50 ? 508 HOH A O   1 
HETATM 3428 O O   . HOH B 2 .   ? 78.143  31.219 5.499  1.00 33.30 ? 509 HOH A O   1 
HETATM 3429 O O   . HOH B 2 .   ? 97.465  45.526 15.467 1.00 30.22 ? 510 HOH A O   1 
HETATM 3430 O O   . HOH B 2 .   ? 68.877  19.413 11.171 1.00 32.03 ? 511 HOH A O   1 
HETATM 3431 O O   . HOH B 2 .   ? 84.833  13.105 28.443 1.00 43.78 ? 512 HOH A O   1 
HETATM 3432 O O   . HOH B 2 .   ? 102.134 30.572 8.811  1.00 34.88 ? 513 HOH A O   1 
HETATM 3433 O O   . HOH B 2 .   ? 106.568 46.718 43.665 1.00 38.72 ? 514 HOH A O   1 
HETATM 3434 O O   . HOH B 2 .   ? 92.976  44.231 47.867 1.00 34.06 ? 515 HOH A O   1 
HETATM 3435 O O   . HOH B 2 .   ? 71.086  17.601 12.225 1.00 31.13 ? 516 HOH A O   1 
HETATM 3436 O O   . HOH B 2 .   ? 100.579 41.779 46.669 1.00 26.66 ? 517 HOH A O   1 
HETATM 3437 O O   . HOH B 2 .   ? 106.107 59.504 34.719 1.00 37.36 ? 518 HOH A O   1 
HETATM 3438 O O   . HOH B 2 .   ? 52.325  27.823 7.332  1.00 35.56 ? 519 HOH A O   1 
HETATM 3439 O O   . HOH B 2 .   ? 94.856  55.172 42.929 1.00 31.34 ? 520 HOH A O   1 
HETATM 3440 O O   . HOH B 2 .   ? 58.254  32.476 29.697 1.00 37.64 ? 521 HOH A O   1 
HETATM 3441 O O   . HOH B 2 .   ? 95.308  63.882 40.225 1.00 43.36 ? 522 HOH A O   1 
HETATM 3442 O O   . HOH B 2 .   ? 91.262  34.261 5.833  1.00 38.74 ? 523 HOH A O   1 
HETATM 3443 O O   . HOH B 2 .   ? 98.629  50.342 46.686 1.00 40.88 ? 524 HOH A O   1 
HETATM 3444 O O   . HOH B 2 .   ? 94.098  26.919 10.224 1.00 37.82 ? 525 HOH A O   1 
HETATM 3445 O O   . HOH B 2 .   ? 89.123  42.341 41.613 1.00 30.66 ? 526 HOH A O   1 
HETATM 3446 O O   . HOH B 2 .   ? 103.909 32.137 27.678 1.00 32.15 ? 527 HOH A O   1 
HETATM 3447 O O   . HOH B 2 .   ? 95.207  24.960 24.093 1.00 32.56 ? 528 HOH A O   1 
HETATM 3448 O O   . HOH B 2 .   ? 101.093 29.418 11.448 1.00 30.14 ? 529 HOH A O   1 
HETATM 3449 O O   . HOH B 2 .   ? 64.857  20.779 34.598 1.00 39.71 ? 530 HOH A O   1 
HETATM 3450 O O   . HOH B 2 .   ? 88.159  43.370 43.947 1.00 31.89 ? 531 HOH A O   1 
HETATM 3451 O O   . HOH B 2 .   ? 67.826  42.000 12.217 1.00 34.24 ? 532 HOH A O   1 
HETATM 3452 O O   . HOH B 2 .   ? 95.058  39.115 40.910 1.00 27.96 ? 533 HOH A O   1 
HETATM 3453 O O   . HOH B 2 .   ? 66.591  13.594 16.299 1.00 48.77 ? 534 HOH A O   1 
HETATM 3454 O O   . HOH B 2 .   ? 73.009  12.685 19.514 1.00 35.75 ? 535 HOH A O   1 
HETATM 3455 O O   . HOH B 2 .   ? 104.261 54.472 30.816 1.00 20.72 ? 536 HOH A O   1 
HETATM 3456 O O   . HOH B 2 .   ? 106.343 52.176 40.343 1.00 37.01 ? 537 HOH A O   1 
HETATM 3457 O O   . HOH B 2 .   ? 65.558  45.845 27.393 1.00 36.42 ? 538 HOH A O   1 
HETATM 3458 O O   . HOH B 2 .   ? 89.464  27.409 29.147 1.00 30.72 ? 539 HOH A O   1 
HETATM 3459 O O   . HOH B 2 .   ? 85.551  15.506 28.232 1.00 32.84 ? 540 HOH A O   1 
HETATM 3460 O O   . HOH B 2 .   ? 77.551  57.177 44.904 1.00 47.71 ? 541 HOH A O   1 
HETATM 3461 O O   . HOH B 2 .   ? 102.306 28.417 19.756 1.00 30.27 ? 542 HOH A O   1 
HETATM 3462 O O   . HOH B 2 .   ? 75.356  17.168 13.298 1.00 25.62 ? 543 HOH A O   1 
HETATM 3463 O O   . HOH B 2 .   ? 67.675  40.553 15.434 1.00 33.69 ? 544 HOH A O   1 
HETATM 3464 O O   . HOH B 2 .   ? 93.965  36.093 11.661 1.00 29.47 ? 545 HOH A O   1 
HETATM 3465 O O   . HOH B 2 .   ? 93.930  14.853 22.584 1.00 32.62 ? 546 HOH A O   1 
HETATM 3466 O O   . HOH B 2 .   ? 92.687  61.173 38.420 1.00 34.16 ? 547 HOH A O   1 
HETATM 3467 O O   . HOH B 2 .   ? 64.447  44.419 20.401 1.00 27.84 ? 548 HOH A O   1 
HETATM 3468 O O   . HOH B 2 .   ? 75.925  38.394 7.717  1.00 36.44 ? 549 HOH A O   1 
HETATM 3469 O O   . HOH B 2 .   ? 78.512  14.498 29.858 1.00 35.88 ? 550 HOH A O   1 
HETATM 3470 O O   . HOH B 2 .   ? 111.000 42.498 32.595 1.00 41.70 ? 551 HOH A O   1 
HETATM 3471 O O   . HOH B 2 .   ? 76.611  8.989  24.860 1.00 41.06 ? 552 HOH A O   1 
HETATM 3472 O O   . HOH B 2 .   ? 102.108 29.769 17.338 1.00 24.29 ? 553 HOH A O   1 
HETATM 3473 O O   . HOH B 2 .   ? 95.769  61.051 38.048 1.00 29.45 ? 554 HOH A O   1 
HETATM 3474 O O   . HOH B 2 .   ? 93.131  19.857 32.741 1.00 44.86 ? 555 HOH A O   1 
HETATM 3475 O O   . HOH B 2 .   ? 89.006  62.407 35.881 1.00 44.35 ? 556 HOH A O   1 
HETATM 3476 O O   . HOH B 2 .   ? 59.718  15.934 25.768 1.00 49.17 ? 557 HOH A O   1 
HETATM 3477 O O   . HOH B 2 .   ? 104.184 55.937 39.393 1.00 41.14 ? 558 HOH A O   1 
HETATM 3478 O O   . HOH B 2 .   ? 91.303  48.014 47.720 1.00 24.15 ? 559 HOH A O   1 
HETATM 3479 O O   . HOH B 2 .   ? 96.589  62.835 19.340 1.00 57.12 ? 560 HOH A O   1 
HETATM 3480 O O   . HOH B 2 .   ? 106.103 62.893 32.899 1.00 31.68 ? 561 HOH A O   1 
HETATM 3481 O O   . HOH B 2 .   ? 85.707  59.855 20.239 1.00 40.82 ? 562 HOH A O   1 
HETATM 3482 O O   . HOH B 2 .   ? 59.357  19.595 12.519 1.00 31.58 ? 563 HOH A O   1 
HETATM 3483 O O   . HOH B 2 .   ? 67.201  24.491 32.594 1.00 29.67 ? 564 HOH A O   1 
HETATM 3484 O O   . HOH B 2 .   ? 70.541  28.408 25.881 1.00 34.71 ? 565 HOH A O   1 
HETATM 3485 O O   . HOH B 2 .   ? 89.075  20.842 1.286  1.00 30.05 ? 566 HOH A O   1 
HETATM 3486 O O   . HOH B 2 .   ? 92.813  23.702 25.315 1.00 24.65 ? 567 HOH A O   1 
HETATM 3487 O O   . HOH B 2 .   ? 101.495 34.425 37.106 1.00 40.76 ? 568 HOH A O   1 
HETATM 3488 O O   . HOH B 2 .   ? 84.956  55.771 26.408 1.00 35.05 ? 569 HOH A O   1 
HETATM 3489 O O   . HOH B 2 .   ? 81.197  54.695 35.784 1.00 38.06 ? 570 HOH A O   1 
HETATM 3490 O O   . HOH B 2 .   ? 62.339  29.761 5.998  1.00 29.19 ? 571 HOH A O   1 
HETATM 3491 O O   . HOH B 2 .   ? 64.405  16.060 16.848 1.00 34.30 ? 572 HOH A O   1 
HETATM 3492 O O   . HOH B 2 .   ? 51.574  23.421 17.810 1.00 25.14 ? 573 HOH A O   1 
HETATM 3493 O O   . HOH B 2 .   ? 77.459  12.047 31.406 1.00 49.16 ? 574 HOH A O   1 
HETATM 3494 O O   . HOH B 2 .   ? 64.454  19.138 11.508 1.00 37.21 ? 575 HOH A O   1 
HETATM 3495 O O   . HOH B 2 .   ? 88.974  45.721 35.152 1.00 25.59 ? 576 HOH A O   1 
HETATM 3496 O O   . HOH B 2 .   ? 99.532  25.848 17.341 1.00 31.88 ? 577 HOH A O   1 
HETATM 3497 O O   . HOH B 2 .   ? 69.280  16.104 36.726 1.00 50.67 ? 578 HOH A O   1 
HETATM 3498 O O   . HOH B 2 .   ? 88.042  47.265 26.989 1.00 20.25 ? 579 HOH A O   1 
HETATM 3499 O O   . HOH B 2 .   ? 61.608  33.807 29.254 1.00 26.69 ? 580 HOH A O   1 
HETATM 3500 O O   . HOH B 2 .   ? 67.372  36.864 31.882 1.00 40.84 ? 581 HOH A O   1 
HETATM 3501 O O   . HOH B 2 .   ? 97.148  23.809 20.480 1.00 35.38 ? 582 HOH A O   1 
HETATM 3502 O O   . HOH B 2 .   ? 68.998  31.202 28.048 1.00 36.57 ? 583 HOH A O   1 
HETATM 3503 O O   . HOH B 2 .   ? 106.950 49.748 39.279 1.00 36.61 ? 584 HOH A O   1 
HETATM 3504 O O   . HOH B 2 .   ? 63.394  40.837 15.094 1.00 37.84 ? 585 HOH A O   1 
HETATM 3505 O O   . HOH B 2 .   ? 111.996 39.291 28.775 1.00 39.76 ? 586 HOH A O   1 
HETATM 3506 O O   . HOH B 2 .   ? 101.154 52.874 13.188 1.00 45.69 ? 587 HOH A O   1 
HETATM 3507 O O   . HOH B 2 .   ? 104.357 60.859 29.038 1.00 31.36 ? 588 HOH A O   1 
HETATM 3508 O O   . HOH B 2 .   ? 70.229  15.253 33.371 1.00 34.37 ? 589 HOH A O   1 
HETATM 3509 O O   . HOH B 2 .   ? 103.282 63.373 29.823 1.00 31.39 ? 590 HOH A O   1 
HETATM 3510 O O   . HOH B 2 .   ? 97.429  59.794 30.808 1.00 30.87 ? 591 HOH A O   1 
HETATM 3511 O O   . HOH B 2 .   ? 96.438  21.508 23.281 1.00 32.87 ? 592 HOH A O   1 
HETATM 3512 O O   . HOH B 2 .   ? 82.889  33.439 24.795 1.00 45.47 ? 593 HOH A O   1 
HETATM 3513 O O   . HOH B 2 .   ? 67.866  15.191 11.982 1.00 51.24 ? 594 HOH A O   1 
HETATM 3514 O O   . HOH B 2 .   ? 68.089  24.528 30.184 1.00 22.79 ? 595 HOH A O   1 
HETATM 3515 O O   . HOH B 2 .   ? 99.194  62.278 24.144 1.00 46.51 ? 596 HOH A O   1 
HETATM 3516 O O   . HOH B 2 .   ? 89.169  42.169 29.765 1.00 25.47 ? 597 HOH A O   1 
HETATM 3517 O O   . HOH B 2 .   ? 103.337 55.524 45.490 1.00 44.30 ? 598 HOH A O   1 
HETATM 3518 O O   . HOH B 2 .   ? 72.424  19.203 2.366  1.00 41.21 ? 599 HOH A O   1 
HETATM 3519 O O   . HOH B 2 .   ? 87.233  66.714 45.424 1.00 58.58 ? 600 HOH A O   1 
HETATM 3520 O O   . HOH B 2 .   ? 85.349  41.467 39.350 1.00 43.83 ? 601 HOH A O   1 
HETATM 3521 O O   . HOH B 2 .   ? 90.231  24.017 13.326 1.00 29.23 ? 602 HOH A O   1 
HETATM 3522 O O   . HOH B 2 .   ? 90.908  14.621 37.100 1.00 42.25 ? 603 HOH A O   1 
HETATM 3523 O O   . HOH B 2 .   ? 85.321  20.760 12.801 1.00 29.71 ? 604 HOH A O   1 
HETATM 3524 O O   . HOH B 2 .   ? 83.140  43.824 34.082 1.00 48.00 ? 605 HOH A O   1 
HETATM 3525 O O   . HOH B 2 .   ? 84.693  14.913 47.174 1.00 54.61 ? 606 HOH A O   1 
HETATM 3526 O O   . HOH B 2 .   ? 93.794  21.662 23.911 1.00 34.22 ? 607 HOH A O   1 
HETATM 3527 O O   . HOH B 2 .   ? 100.885 18.318 22.617 1.00 28.11 ? 608 HOH A O   1 
HETATM 3528 O O   . HOH B 2 .   ? 101.062 59.235 42.061 1.00 40.50 ? 609 HOH A O   1 
HETATM 3529 O O   . HOH B 2 .   ? 110.137 46.064 37.851 1.00 36.76 ? 610 HOH A O   1 
HETATM 3530 O O   . HOH B 2 .   ? 82.356  13.593 18.385 1.00 36.73 ? 611 HOH A O   1 
HETATM 3531 O O   . HOH B 2 .   ? 109.522 42.661 23.036 1.00 42.48 ? 612 HOH A O   1 
HETATM 3532 O O   . HOH B 2 .   ? 105.472 39.938 36.933 1.00 29.66 ? 613 HOH A O   1 
HETATM 3533 O O   . HOH B 2 .   ? 89.111  60.174 29.392 1.00 47.77 ? 614 HOH A O   1 
HETATM 3534 O O   . HOH B 2 .   ? 99.307  56.112 45.016 1.00 38.99 ? 615 HOH A O   1 
HETATM 3535 O O   . HOH B 2 .   ? 56.960  26.135 31.024 1.00 46.18 ? 616 HOH A O   1 
HETATM 3536 O O   . HOH B 2 .   ? 89.560  42.357 27.194 1.00 29.59 ? 617 HOH A O   1 
HETATM 3537 O O   . HOH B 2 .   ? 83.317  15.326 15.795 1.00 42.07 ? 618 HOH A O   1 
HETATM 3538 O O   . HOH B 2 .   ? 85.200  45.729 19.181 1.00 36.51 ? 619 HOH A O   1 
HETATM 3539 O O   . HOH B 2 .   ? 64.469  35.573 10.128 1.00 32.87 ? 620 HOH A O   1 
HETATM 3540 O O   . HOH B 2 .   ? 104.608 34.825 31.918 1.00 32.64 ? 621 HOH A O   1 
HETATM 3541 O O   . HOH B 2 .   ? 94.141  41.662 40.250 1.00 23.33 ? 622 HOH A O   1 
HETATM 3542 O O   . HOH B 2 .   ? 56.525  29.014 29.641 1.00 34.38 ? 623 HOH A O   1 
HETATM 3543 O O   . HOH B 2 .   ? 69.593  43.909 6.568  1.00 45.45 ? 624 HOH A O   1 
HETATM 3544 O O   . HOH B 2 .   ? 107.143 37.649 32.438 1.00 47.98 ? 625 HOH A O   1 
HETATM 3545 O O   . HOH B 2 .   ? 82.737  52.057 35.661 1.00 35.34 ? 626 HOH A O   1 
HETATM 3546 O O   . HOH B 2 .   ? 97.024  50.932 11.246 1.00 36.71 ? 627 HOH A O   1 
HETATM 3547 O O   . HOH B 2 .   ? 96.726  63.636 37.170 1.00 38.68 ? 628 HOH A O   1 
HETATM 3548 O O   . HOH B 2 .   ? 93.582  13.106 27.702 1.00 49.91 ? 629 HOH A O   1 
HETATM 3549 O O   . HOH B 2 .   ? 73.973  47.878 28.726 1.00 37.79 ? 630 HOH A O   1 
HETATM 3550 O O   . HOH B 2 .   ? 87.841  39.715 29.158 1.00 29.60 ? 631 HOH A O   1 
HETATM 3551 O O   . HOH B 2 .   ? 85.352  32.946 28.586 1.00 28.96 ? 632 HOH A O   1 
HETATM 3552 O O   . HOH B 2 .   ? 83.487  16.284 13.807 1.00 54.89 ? 633 HOH A O   1 
HETATM 3553 O O   . HOH B 2 .   ? 59.762  40.068 21.076 1.00 28.03 ? 634 HOH A O   1 
HETATM 3554 O O   . HOH B 2 .   ? 56.641  33.840 36.136 1.00 54.92 ? 635 HOH A O   1 
HETATM 3555 O O   . HOH B 2 .   ? 94.573  60.225 29.558 1.00 30.24 ? 636 HOH A O   1 
HETATM 3556 O O   . HOH B 2 .   ? 82.658  3.966  19.412 1.00 37.69 ? 637 HOH A O   1 
HETATM 3557 O O   . HOH B 2 .   ? 80.682  27.909 4.836  1.00 27.43 ? 638 HOH A O   1 
HETATM 3558 O O   . HOH B 2 .   ? 85.909  48.006 17.245 1.00 35.31 ? 639 HOH A O   1 
HETATM 3559 O O   . HOH B 2 .   ? 81.398  11.380 17.823 1.00 39.90 ? 640 HOH A O   1 
HETATM 3560 O O   . HOH B 2 .   ? 85.673  38.591 26.325 1.00 27.97 ? 641 HOH A O   1 
HETATM 3561 O O   . HOH B 2 .   ? 87.038  52.415 54.636 1.00 44.04 ? 642 HOH A O   1 
HETATM 3562 O O   . HOH B 2 .   ? 92.285  25.378 8.566  1.00 31.33 ? 643 HOH A O   1 
HETATM 3563 O O   . HOH B 2 .   ? 102.749 64.973 39.627 1.00 39.06 ? 644 HOH A O   1 
HETATM 3564 O O   . HOH B 2 .   ? 106.456 53.497 42.563 1.00 37.65 ? 645 HOH A O   1 
HETATM 3565 O O   . HOH B 2 .   ? 77.015  34.276 39.451 1.00 47.72 ? 646 HOH A O   1 
HETATM 3566 O O   . HOH B 2 .   ? 85.739  48.309 25.567 1.00 34.61 ? 647 HOH A O   1 
HETATM 3567 O O   . HOH B 2 .   ? 84.487  37.769 20.342 1.00 53.59 ? 648 HOH A O   1 
HETATM 3568 O O   . HOH B 2 .   ? 101.626 24.229 21.606 1.00 45.78 ? 649 HOH A O   1 
HETATM 3569 O O   . HOH B 2 .   ? 56.721  39.635 29.889 1.00 43.73 ? 650 HOH A O   1 
HETATM 3570 O O   . HOH B 2 .   ? 84.743  46.935 23.722 1.00 49.48 ? 651 HOH A O   1 
HETATM 3571 O O   . HOH B 2 .   ? 91.870  43.162 41.777 1.00 18.03 ? 652 HOH A O   1 
HETATM 3572 O O   . HOH B 2 .   ? 79.932  53.409 38.482 1.00 43.77 ? 653 HOH A O   1 
HETATM 3573 O O   . HOH B 2 .   ? 71.014  14.533 35.967 1.00 44.54 ? 654 HOH A O   1 
HETATM 3574 O O   . HOH B 2 .   ? 100.213 28.432 15.813 1.00 35.71 ? 655 HOH A O   1 
HETATM 3575 O O   . HOH B 2 .   ? 85.368  50.870 55.345 1.00 44.35 ? 656 HOH A O   1 
HETATM 3576 O O   . HOH B 2 .   ? 106.062 61.237 26.942 1.00 33.61 ? 657 HOH A O   1 
HETATM 3577 O O   . HOH B 2 .   ? 80.810  30.514 5.130  1.00 46.98 ? 658 HOH A O   1 
HETATM 3578 O O   . HOH B 2 .   ? 109.874 48.330 39.321 1.00 52.33 ? 659 HOH A O   1 
HETATM 3579 O O   . HOH B 2 .   ? 85.009  34.465 30.984 1.00 41.02 ? 660 HOH A O   1 
# 
