data_9H5Z
# 
_entry.id   9H5Z 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9H5Z         pdb_00009h5z 10.2210/pdb9h5z/pdb 
WWPDB D_1292142710 ?            ?                   
# 
_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       2025-01-22 
# 
_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                        9H5Z 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9H5P unspecified 
PDB . 9H5Q unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              claudia.binda@unipv.it 
_pdbx_contact_author.name_first         Claudia 
_pdbx_contact_author.name_last          Binda 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2038-9845 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Basile, L.'      1 0009-0004-6724-0110 
'Poli, C.'        2 ?                   
'Santema, L.L.'   3 ?                   
'Lesenciuc, R.C.' 4 ?                   
'Fraaije, M.W.'   5 0000-0001-6346-5014 
'Binda, C.'       6 0000-0003-2038-9845 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Arch.Biochem.Biophys. 
_citation.journal_id_ASTM           ABBIA4 
_citation.journal_id_CSD            0158 
_citation.journal_id_ISSN           1096-0384 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            764 
_citation.language                  ? 
_citation.page_first                110276 
_citation.page_last                 110276 
_citation.title                     
'Altering substrate specificity of a thermostable bacterial monoamine oxidase by structure-based mutagenesis.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.abb.2024.110276 
_citation.pdbx_database_id_PubMed   39706511 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Basile, L.'      1 ? 
primary 'Poli, C.'        2 ? 
primary 'Santema, L.L.'   3 ? 
primary 'Lesenciuc, R.C.' 4 ? 
primary 'Fraaije, M.W.'   5 ? 
primary 'Binda, C.'       6 ? 
# 
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 'Monoamine oxidase'           50089.773 2   ? ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   2   ? ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'               24.305    2   ? ? ? ? 
4 non-polymer syn BENZYLAMINE                   107.153   1   ? ? ? ? 
5 water       nat water                         18.015    237 ? ? ? ? 
# 
_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       
;MGSSHHHHHHGSGLVPRGSAGMPSEQVDVVVVGAGFAGLTAARAVHEAGRSVLVLEARDRVGGRTCTEEHHGTWIDLGGQ
WIGPGQDRVAALAAELGVETYPQPTEGDDVVLFGDGEPQRAPDVALAFSDEELTAYLELAGALEAIAEKVPLDAPWLAPE
AAAWDATTLREWVAGTGVPDRVAGLFEVAVQAVFAATSAQLSLLHAAHYVHSAGGWSKLTDTEGGAQQDRLVGGVQPLAE
RLAARLPDGALRLSTPVRGLAQDGDGVTVRTAGGEVRARRAIVAVPPTLAGRIDHDPPLPPQRDQLLQHMPQGSVVKFHV
IYDEPWWRAEGLSGTVLCPDEPIGVTFDGTPPAGTPGIVTGFFEGPAAVAAGARTREERRDVVVDVLARTLGERARDVRD
YIDRDWSAEPWTRGCYGAHLPPGAWTVYGPALRVPVGRVHWAGTETAERWTGYIDGAIESGQRAAAEVLAALGS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHGSGLVPRGSAGMPSEQVDVVVVGAGFAGLTAARAVHEAGRSVLVLEARDRVGGRTCTEEHHGTWIDLGGQ
WIGPGQDRVAALAAELGVETYPQPTEGDDVVLFGDGEPQRAPDVALAFSDEELTAYLELAGALEAIAEKVPLDAPWLAPE
AAAWDATTLREWVAGTGVPDRVAGLFEVAVQAVFAATSAQLSLLHAAHYVHSAGGWSKLTDTEGGAQQDRLVGGVQPLAE
RLAARLPDGALRLSTPVRGLAQDGDGVTVRTAGGEVRARRAIVAVPPTLAGRIDHDPPLPPQRDQLLQHMPQGSVVKFHV
IYDEPWWRAEGLSGTVLCPDEPIGVTFDGTPPAGTPGIVTGFFEGPAAVAAGARTREERRDVVVDVLARTLGERARDVRD
YIDRDWSAEPWTRGCYGAHLPPGAWTVYGPALRVPVGRVHWAGTETAERWTGYIDGAIESGQRAAAEVLAALGS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 'MAGNESIUM ION'               MG  
4 BENZYLAMINE                   ABN 
5 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  GLY n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  ALA n 
1 21  GLY n 
1 22  MET n 
1 23  PRO n 
1 24  SER n 
1 25  GLU n 
1 26  GLN n 
1 27  VAL n 
1 28  ASP n 
1 29  VAL n 
1 30  VAL n 
1 31  VAL n 
1 32  VAL n 
1 33  GLY n 
1 34  ALA n 
1 35  GLY n 
1 36  PHE n 
1 37  ALA n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  ALA n 
1 42  ALA n 
1 43  ARG n 
1 44  ALA n 
1 45  VAL n 
1 46  HIS n 
1 47  GLU n 
1 48  ALA n 
1 49  GLY n 
1 50  ARG n 
1 51  SER n 
1 52  VAL n 
1 53  LEU n 
1 54  VAL n 
1 55  LEU n 
1 56  GLU n 
1 57  ALA n 
1 58  ARG n 
1 59  ASP n 
1 60  ARG n 
1 61  VAL n 
1 62  GLY n 
1 63  GLY n 
1 64  ARG n 
1 65  THR n 
1 66  CYS n 
1 67  THR n 
1 68  GLU n 
1 69  GLU n 
1 70  HIS n 
1 71  HIS n 
1 72  GLY n 
1 73  THR n 
1 74  TRP n 
1 75  ILE n 
1 76  ASP n 
1 77  LEU n 
1 78  GLY n 
1 79  GLY n 
1 80  GLN n 
1 81  TRP n 
1 82  ILE n 
1 83  GLY n 
1 84  PRO n 
1 85  GLY n 
1 86  GLN n 
1 87  ASP n 
1 88  ARG n 
1 89  VAL n 
1 90  ALA n 
1 91  ALA n 
1 92  LEU n 
1 93  ALA n 
1 94  ALA n 
1 95  GLU n 
1 96  LEU n 
1 97  GLY n 
1 98  VAL n 
1 99  GLU n 
1 100 THR n 
1 101 TYR n 
1 102 PRO n 
1 103 GLN n 
1 104 PRO n 
1 105 THR n 
1 106 GLU n 
1 107 GLY n 
1 108 ASP n 
1 109 ASP n 
1 110 VAL n 
1 111 VAL n 
1 112 LEU n 
1 113 PHE n 
1 114 GLY n 
1 115 ASP n 
1 116 GLY n 
1 117 GLU n 
1 118 PRO n 
1 119 GLN n 
1 120 ARG n 
1 121 ALA n 
1 122 PRO n 
1 123 ASP n 
1 124 VAL n 
1 125 ALA n 
1 126 LEU n 
1 127 ALA n 
1 128 PHE n 
1 129 SER n 
1 130 ASP n 
1 131 GLU n 
1 132 GLU n 
1 133 LEU n 
1 134 THR n 
1 135 ALA n 
1 136 TYR n 
1 137 LEU n 
1 138 GLU n 
1 139 LEU n 
1 140 ALA n 
1 141 GLY n 
1 142 ALA n 
1 143 LEU n 
1 144 GLU n 
1 145 ALA n 
1 146 ILE n 
1 147 ALA n 
1 148 GLU n 
1 149 LYS n 
1 150 VAL n 
1 151 PRO n 
1 152 LEU n 
1 153 ASP n 
1 154 ALA n 
1 155 PRO n 
1 156 TRP n 
1 157 LEU n 
1 158 ALA n 
1 159 PRO n 
1 160 GLU n 
1 161 ALA n 
1 162 ALA n 
1 163 ALA n 
1 164 TRP n 
1 165 ASP n 
1 166 ALA n 
1 167 THR n 
1 168 THR n 
1 169 LEU n 
1 170 ARG n 
1 171 GLU n 
1 172 TRP n 
1 173 VAL n 
1 174 ALA n 
1 175 GLY n 
1 176 THR n 
1 177 GLY n 
1 178 VAL n 
1 179 PRO n 
1 180 ASP n 
1 181 ARG n 
1 182 VAL n 
1 183 ALA n 
1 184 GLY n 
1 185 LEU n 
1 186 PHE n 
1 187 GLU n 
1 188 VAL n 
1 189 ALA n 
1 190 VAL n 
1 191 GLN n 
1 192 ALA n 
1 193 VAL n 
1 194 PHE n 
1 195 ALA n 
1 196 ALA n 
1 197 THR n 
1 198 SER n 
1 199 ALA n 
1 200 GLN n 
1 201 LEU n 
1 202 SER n 
1 203 LEU n 
1 204 LEU n 
1 205 HIS n 
1 206 ALA n 
1 207 ALA n 
1 208 HIS n 
1 209 TYR n 
1 210 VAL n 
1 211 HIS n 
1 212 SER n 
1 213 ALA n 
1 214 GLY n 
1 215 GLY n 
1 216 TRP n 
1 217 SER n 
1 218 LYS n 
1 219 LEU n 
1 220 THR n 
1 221 ASP n 
1 222 THR n 
1 223 GLU n 
1 224 GLY n 
1 225 GLY n 
1 226 ALA n 
1 227 GLN n 
1 228 GLN n 
1 229 ASP n 
1 230 ARG n 
1 231 LEU n 
1 232 VAL n 
1 233 GLY n 
1 234 GLY n 
1 235 VAL n 
1 236 GLN n 
1 237 PRO n 
1 238 LEU n 
1 239 ALA n 
1 240 GLU n 
1 241 ARG n 
1 242 LEU n 
1 243 ALA n 
1 244 ALA n 
1 245 ARG n 
1 246 LEU n 
1 247 PRO n 
1 248 ASP n 
1 249 GLY n 
1 250 ALA n 
1 251 LEU n 
1 252 ARG n 
1 253 LEU n 
1 254 SER n 
1 255 THR n 
1 256 PRO n 
1 257 VAL n 
1 258 ARG n 
1 259 GLY n 
1 260 LEU n 
1 261 ALA n 
1 262 GLN n 
1 263 ASP n 
1 264 GLY n 
1 265 ASP n 
1 266 GLY n 
1 267 VAL n 
1 268 THR n 
1 269 VAL n 
1 270 ARG n 
1 271 THR n 
1 272 ALA n 
1 273 GLY n 
1 274 GLY n 
1 275 GLU n 
1 276 VAL n 
1 277 ARG n 
1 278 ALA n 
1 279 ARG n 
1 280 ARG n 
1 281 ALA n 
1 282 ILE n 
1 283 VAL n 
1 284 ALA n 
1 285 VAL n 
1 286 PRO n 
1 287 PRO n 
1 288 THR n 
1 289 LEU n 
1 290 ALA n 
1 291 GLY n 
1 292 ARG n 
1 293 ILE n 
1 294 ASP n 
1 295 HIS n 
1 296 ASP n 
1 297 PRO n 
1 298 PRO n 
1 299 LEU n 
1 300 PRO n 
1 301 PRO n 
1 302 GLN n 
1 303 ARG n 
1 304 ASP n 
1 305 GLN n 
1 306 LEU n 
1 307 LEU n 
1 308 GLN n 
1 309 HIS n 
1 310 MET n 
1 311 PRO n 
1 312 GLN n 
1 313 GLY n 
1 314 SER n 
1 315 VAL n 
1 316 VAL n 
1 317 LYS n 
1 318 PHE n 
1 319 HIS n 
1 320 VAL n 
1 321 ILE n 
1 322 TYR n 
1 323 ASP n 
1 324 GLU n 
1 325 PRO n 
1 326 TRP n 
1 327 TRP n 
1 328 ARG n 
1 329 ALA n 
1 330 GLU n 
1 331 GLY n 
1 332 LEU n 
1 333 SER n 
1 334 GLY n 
1 335 THR n 
1 336 VAL n 
1 337 LEU n 
1 338 CYS n 
1 339 PRO n 
1 340 ASP n 
1 341 GLU n 
1 342 PRO n 
1 343 ILE n 
1 344 GLY n 
1 345 VAL n 
1 346 THR n 
1 347 PHE n 
1 348 ASP n 
1 349 GLY n 
1 350 THR n 
1 351 PRO n 
1 352 PRO n 
1 353 ALA n 
1 354 GLY n 
1 355 THR n 
1 356 PRO n 
1 357 GLY n 
1 358 ILE n 
1 359 VAL n 
1 360 THR n 
1 361 GLY n 
1 362 PHE n 
1 363 PHE n 
1 364 GLU n 
1 365 GLY n 
1 366 PRO n 
1 367 ALA n 
1 368 ALA n 
1 369 VAL n 
1 370 ALA n 
1 371 ALA n 
1 372 GLY n 
1 373 ALA n 
1 374 ARG n 
1 375 THR n 
1 376 ARG n 
1 377 GLU n 
1 378 GLU n 
1 379 ARG n 
1 380 ARG n 
1 381 ASP n 
1 382 VAL n 
1 383 VAL n 
1 384 VAL n 
1 385 ASP n 
1 386 VAL n 
1 387 LEU n 
1 388 ALA n 
1 389 ARG n 
1 390 THR n 
1 391 LEU n 
1 392 GLY n 
1 393 GLU n 
1 394 ARG n 
1 395 ALA n 
1 396 ARG n 
1 397 ASP n 
1 398 VAL n 
1 399 ARG n 
1 400 ASP n 
1 401 TYR n 
1 402 ILE n 
1 403 ASP n 
1 404 ARG n 
1 405 ASP n 
1 406 TRP n 
1 407 SER n 
1 408 ALA n 
1 409 GLU n 
1 410 PRO n 
1 411 TRP n 
1 412 THR n 
1 413 ARG n 
1 414 GLY n 
1 415 CYS n 
1 416 TYR n 
1 417 GLY n 
1 418 ALA n 
1 419 HIS n 
1 420 LEU n 
1 421 PRO n 
1 422 PRO n 
1 423 GLY n 
1 424 ALA n 
1 425 TRP n 
1 426 THR n 
1 427 VAL n 
1 428 TYR n 
1 429 GLY n 
1 430 PRO n 
1 431 ALA n 
1 432 LEU n 
1 433 ARG n 
1 434 VAL n 
1 435 PRO n 
1 436 VAL n 
1 437 GLY n 
1 438 ARG n 
1 439 VAL n 
1 440 HIS n 
1 441 TRP n 
1 442 ALA n 
1 443 GLY n 
1 444 THR n 
1 445 GLU n 
1 446 THR n 
1 447 ALA n 
1 448 GLU n 
1 449 ARG n 
1 450 TRP n 
1 451 THR n 
1 452 GLY n 
1 453 TYR n 
1 454 ILE n 
1 455 ASP n 
1 456 GLY n 
1 457 ALA n 
1 458 ILE n 
1 459 GLU n 
1 460 SER n 
1 461 GLY n 
1 462 GLN n 
1 463 ARG n 
1 464 ALA n 
1 465 ALA n 
1 466 ALA n 
1 467 GLU n 
1 468 VAL n 
1 469 LEU n 
1 470 ALA n 
1 471 ALA n 
1 472 LEU n 
1 473 GLY n 
1 474 SER 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               ? 
_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      'Thermoanaerobacterales bacterium' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2304039 
_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 
ABN non-polymer         . BENZYLAMINE                   ? 'C7 H9 N'           107.153 
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 
ASP 'L-peptide linking' y 'ASPARTIC ACID'               ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                      ? 'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking' y GLUTAMINE                     ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                       ? 'C2 H5 N O2'        75.067  
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 
MG  non-polymer         . 'MAGNESIUM ION'               ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE                 ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                     ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -20 ?   ?   ?   A . n 
A 1 2   GLY 2   -19 ?   ?   ?   A . n 
A 1 3   SER 3   -18 ?   ?   ?   A . n 
A 1 4   SER 4   -17 ?   ?   ?   A . n 
A 1 5   HIS 5   -16 ?   ?   ?   A . n 
A 1 6   HIS 6   -15 ?   ?   ?   A . n 
A 1 7   HIS 7   -14 ?   ?   ?   A . n 
A 1 8   HIS 8   -13 ?   ?   ?   A . n 
A 1 9   HIS 9   -12 ?   ?   ?   A . n 
A 1 10  HIS 10  -11 ?   ?   ?   A . n 
A 1 11  GLY 11  -10 ?   ?   ?   A . n 
A 1 12  SER 12  -9  ?   ?   ?   A . n 
A 1 13  GLY 13  -8  ?   ?   ?   A . n 
A 1 14  LEU 14  -7  ?   ?   ?   A . n 
A 1 15  VAL 15  -6  ?   ?   ?   A . n 
A 1 16  PRO 16  -5  ?   ?   ?   A . n 
A 1 17  ARG 17  -4  ?   ?   ?   A . n 
A 1 18  GLY 18  -3  ?   ?   ?   A . n 
A 1 19  SER 19  -2  ?   ?   ?   A . n 
A 1 20  ALA 20  -1  ?   ?   ?   A . n 
A 1 21  GLY 21  0   ?   ?   ?   A . n 
A 1 22  MET 22  1   ?   ?   ?   A . n 
A 1 23  PRO 23  2   ?   ?   ?   A . n 
A 1 24  SER 24  3   ?   ?   ?   A . n 
A 1 25  GLU 25  4   ?   ?   ?   A . n 
A 1 26  GLN 26  5   5   GLN GLN A . n 
A 1 27  VAL 27  6   6   VAL VAL A . n 
A 1 28  ASP 28  7   7   ASP ASP A . n 
A 1 29  VAL 29  8   8   VAL VAL A . n 
A 1 30  VAL 30  9   9   VAL VAL A . n 
A 1 31  VAL 31  10  10  VAL VAL A . n 
A 1 32  VAL 32  11  11  VAL VAL A . n 
A 1 33  GLY 33  12  12  GLY GLY A . n 
A 1 34  ALA 34  13  13  ALA ALA A . n 
A 1 35  GLY 35  14  14  GLY GLY A . n 
A 1 36  PHE 36  15  15  PHE PHE A . n 
A 1 37  ALA 37  16  16  ALA ALA A . n 
A 1 38  GLY 38  17  17  GLY GLY A . n 
A 1 39  LEU 39  18  18  LEU LEU A . n 
A 1 40  THR 40  19  19  THR THR A . n 
A 1 41  ALA 41  20  20  ALA ALA A . n 
A 1 42  ALA 42  21  21  ALA ALA A . n 
A 1 43  ARG 43  22  22  ARG ARG A . n 
A 1 44  ALA 44  23  23  ALA ALA A . n 
A 1 45  VAL 45  24  24  VAL VAL A . n 
A 1 46  HIS 46  25  25  HIS HIS A . n 
A 1 47  GLU 47  26  26  GLU GLU A . n 
A 1 48  ALA 48  27  27  ALA ALA A . n 
A 1 49  GLY 49  28  28  GLY GLY A . n 
A 1 50  ARG 50  29  29  ARG ARG A . n 
A 1 51  SER 51  30  30  SER SER A . n 
A 1 52  VAL 52  31  31  VAL VAL A . n 
A 1 53  LEU 53  32  32  LEU LEU A . n 
A 1 54  VAL 54  33  33  VAL VAL A . n 
A 1 55  LEU 55  34  34  LEU LEU A . n 
A 1 56  GLU 56  35  35  GLU GLU A . n 
A 1 57  ALA 57  36  36  ALA ALA A . n 
A 1 58  ARG 58  37  37  ARG ARG A . n 
A 1 59  ASP 59  38  38  ASP ASP A . n 
A 1 60  ARG 60  39  39  ARG ARG A . n 
A 1 61  VAL 61  40  40  VAL VAL A . n 
A 1 62  GLY 62  41  41  GLY GLY A . n 
A 1 63  GLY 63  42  42  GLY GLY A . n 
A 1 64  ARG 64  43  43  ARG ARG A . n 
A 1 65  THR 65  44  44  THR THR A . n 
A 1 66  CYS 66  45  45  CYS CYS A . n 
A 1 67  THR 67  46  46  THR THR A . n 
A 1 68  GLU 68  47  47  GLU GLU A . n 
A 1 69  GLU 69  48  48  GLU GLU A . n 
A 1 70  HIS 70  49  49  HIS HIS A . n 
A 1 71  HIS 71  50  50  HIS HIS A . n 
A 1 72  GLY 72  51  51  GLY GLY A . n 
A 1 73  THR 73  52  52  THR THR A . n 
A 1 74  TRP 74  53  53  TRP TRP A . n 
A 1 75  ILE 75  54  54  ILE ILE A . n 
A 1 76  ASP 76  55  55  ASP ASP A . n 
A 1 77  LEU 77  56  56  LEU LEU A . n 
A 1 78  GLY 78  57  57  GLY GLY A . n 
A 1 79  GLY 79  58  58  GLY GLY A . n 
A 1 80  GLN 80  59  59  GLN GLN A . n 
A 1 81  TRP 81  60  60  TRP TRP A . n 
A 1 82  ILE 82  61  61  ILE ILE A . n 
A 1 83  GLY 83  62  62  GLY GLY A . n 
A 1 84  PRO 84  63  63  PRO PRO A . n 
A 1 85  GLY 85  64  64  GLY GLY A . n 
A 1 86  GLN 86  65  65  GLN GLN A . n 
A 1 87  ASP 87  66  66  ASP ASP A . n 
A 1 88  ARG 88  67  67  ARG ARG A . n 
A 1 89  VAL 89  68  68  VAL VAL A . n 
A 1 90  ALA 90  69  69  ALA ALA A . n 
A 1 91  ALA 91  70  70  ALA ALA A . n 
A 1 92  LEU 92  71  71  LEU LEU A . n 
A 1 93  ALA 93  72  72  ALA ALA A . n 
A 1 94  ALA 94  73  73  ALA ALA A . n 
A 1 95  GLU 95  74  74  GLU GLU A . n 
A 1 96  LEU 96  75  75  LEU LEU A . n 
A 1 97  GLY 97  76  76  GLY GLY A . n 
A 1 98  VAL 98  77  77  VAL VAL A . n 
A 1 99  GLU 99  78  78  GLU GLU A . n 
A 1 100 THR 100 79  79  THR THR A . n 
A 1 101 TYR 101 80  80  TYR TYR A . n 
A 1 102 PRO 102 81  81  PRO PRO A . n 
A 1 103 GLN 103 82  82  GLN GLN A . n 
A 1 104 PRO 104 83  83  PRO PRO A . n 
A 1 105 THR 105 84  84  THR THR A . n 
A 1 106 GLU 106 85  85  GLU GLU A . n 
A 1 107 GLY 107 86  86  GLY GLY A . n 
A 1 108 ASP 108 87  87  ASP ASP A . n 
A 1 109 ASP 109 88  88  ASP ASP A . n 
A 1 110 VAL 110 89  89  VAL VAL A . n 
A 1 111 VAL 111 90  90  VAL VAL A . n 
A 1 112 LEU 112 91  91  LEU LEU A . n 
A 1 113 PHE 113 92  92  PHE PHE A . n 
A 1 114 GLY 114 93  93  GLY GLY A . n 
A 1 115 ASP 115 94  94  ASP ASP A . n 
A 1 116 GLY 116 95  95  GLY GLY A . n 
A 1 117 GLU 117 96  96  GLU GLU A . n 
A 1 118 PRO 118 97  97  PRO PRO A . n 
A 1 119 GLN 119 98  98  GLN GLN A . n 
A 1 120 ARG 120 99  99  ARG ARG A . n 
A 1 121 ALA 121 100 100 ALA ALA A . n 
A 1 122 PRO 122 101 101 PRO PRO A . n 
A 1 123 ASP 123 102 102 ASP ASP A . n 
A 1 124 VAL 124 103 103 VAL VAL A . n 
A 1 125 ALA 125 104 104 ALA ALA A . n 
A 1 126 LEU 126 105 105 LEU LEU A . n 
A 1 127 ALA 127 106 106 ALA ALA A . n 
A 1 128 PHE 128 107 107 PHE PHE A . n 
A 1 129 SER 129 108 108 SER SER A . n 
A 1 130 ASP 130 109 109 ASP ASP A . n 
A 1 131 GLU 131 110 110 GLU GLU A . n 
A 1 132 GLU 132 111 111 GLU GLU A . n 
A 1 133 LEU 133 112 112 LEU LEU A . n 
A 1 134 THR 134 113 113 THR THR A . n 
A 1 135 ALA 135 114 114 ALA ALA A . n 
A 1 136 TYR 136 115 115 TYR TYR A . n 
A 1 137 LEU 137 116 116 LEU LEU A . n 
A 1 138 GLU 138 117 117 GLU GLU A . n 
A 1 139 LEU 139 118 118 LEU LEU A . n 
A 1 140 ALA 140 119 119 ALA ALA A . n 
A 1 141 GLY 141 120 120 GLY GLY A . n 
A 1 142 ALA 142 121 121 ALA ALA A . n 
A 1 143 LEU 143 122 122 LEU LEU A . n 
A 1 144 GLU 144 123 123 GLU GLU A . n 
A 1 145 ALA 145 124 124 ALA ALA A . n 
A 1 146 ILE 146 125 125 ILE ILE A . n 
A 1 147 ALA 147 126 126 ALA ALA A . n 
A 1 148 GLU 148 127 127 GLU GLU A . n 
A 1 149 LYS 149 128 128 LYS LYS A . n 
A 1 150 VAL 150 129 129 VAL VAL A . n 
A 1 151 PRO 151 130 130 PRO PRO A . n 
A 1 152 LEU 152 131 131 LEU LEU A . n 
A 1 153 ASP 153 132 132 ASP ASP A . n 
A 1 154 ALA 154 133 133 ALA ALA A . n 
A 1 155 PRO 155 134 134 PRO PRO A . n 
A 1 156 TRP 156 135 135 TRP TRP A . n 
A 1 157 LEU 157 136 136 LEU LEU A . n 
A 1 158 ALA 158 137 137 ALA ALA A . n 
A 1 159 PRO 159 138 138 PRO PRO A . n 
A 1 160 GLU 160 139 139 GLU GLU A . n 
A 1 161 ALA 161 140 140 ALA ALA A . n 
A 1 162 ALA 162 141 141 ALA ALA A . n 
A 1 163 ALA 163 142 142 ALA ALA A . n 
A 1 164 TRP 164 143 143 TRP TRP A . n 
A 1 165 ASP 165 144 144 ASP ASP A . n 
A 1 166 ALA 166 145 145 ALA ALA A . n 
A 1 167 THR 167 146 146 THR THR A . n 
A 1 168 THR 168 147 147 THR THR A . n 
A 1 169 LEU 169 148 148 LEU LEU A . n 
A 1 170 ARG 170 149 149 ARG ARG A . n 
A 1 171 GLU 171 150 150 GLU GLU A . n 
A 1 172 TRP 172 151 151 TRP TRP A . n 
A 1 173 VAL 173 152 152 VAL VAL A . n 
A 1 174 ALA 174 153 153 ALA ALA A . n 
A 1 175 GLY 175 154 154 GLY GLY A . n 
A 1 176 THR 176 155 155 THR THR A . n 
A 1 177 GLY 177 156 156 GLY GLY A . n 
A 1 178 VAL 178 157 157 VAL VAL A . n 
A 1 179 PRO 179 158 158 PRO PRO A . n 
A 1 180 ASP 180 159 159 ASP ASP A . n 
A 1 181 ARG 181 160 160 ARG ARG A . n 
A 1 182 VAL 182 161 161 VAL VAL A . n 
A 1 183 ALA 183 162 162 ALA ALA A . n 
A 1 184 GLY 184 163 163 GLY GLY A . n 
A 1 185 LEU 185 164 164 LEU LEU A . n 
A 1 186 PHE 186 165 165 PHE PHE A . n 
A 1 187 GLU 187 166 166 GLU GLU A . n 
A 1 188 VAL 188 167 167 VAL VAL A . n 
A 1 189 ALA 189 168 168 ALA ALA A . n 
A 1 190 VAL 190 169 169 VAL VAL A . n 
A 1 191 GLN 191 170 170 GLN GLN A . n 
A 1 192 ALA 192 171 171 ALA ALA A . n 
A 1 193 VAL 193 172 172 VAL VAL A . n 
A 1 194 PHE 194 173 173 PHE PHE A . n 
A 1 195 ALA 195 174 174 ALA ALA A . n 
A 1 196 ALA 196 175 175 ALA ALA A . n 
A 1 197 THR 197 176 176 THR THR A . n 
A 1 198 SER 198 177 177 SER SER A . n 
A 1 199 ALA 199 178 178 ALA ALA A . n 
A 1 200 GLN 200 179 179 GLN GLN A . n 
A 1 201 LEU 201 180 180 LEU LEU A . n 
A 1 202 SER 202 181 181 SER SER A . n 
A 1 203 LEU 203 182 182 LEU LEU A . n 
A 1 204 LEU 204 183 183 LEU LEU A . n 
A 1 205 HIS 205 184 184 HIS HIS A . n 
A 1 206 ALA 206 185 185 ALA ALA A . n 
A 1 207 ALA 207 186 186 ALA ALA A . n 
A 1 208 HIS 208 187 187 HIS HIS A . n 
A 1 209 TYR 209 188 188 TYR TYR A . n 
A 1 210 VAL 210 189 189 VAL VAL A . n 
A 1 211 HIS 211 190 190 HIS HIS A . n 
A 1 212 SER 212 191 191 SER SER A . n 
A 1 213 ALA 213 192 192 ALA ALA A . n 
A 1 214 GLY 214 193 193 GLY GLY A . n 
A 1 215 GLY 215 194 194 GLY GLY A . n 
A 1 216 TRP 216 195 195 TRP TRP A . n 
A 1 217 SER 217 196 196 SER SER A . n 
A 1 218 LYS 218 197 197 LYS LYS A . n 
A 1 219 LEU 219 198 198 LEU LEU A . n 
A 1 220 THR 220 199 199 THR THR A . n 
A 1 221 ASP 221 200 200 ASP ASP A . n 
A 1 222 THR 222 201 201 THR THR A . n 
A 1 223 GLU 223 202 202 GLU GLU A . n 
A 1 224 GLY 224 203 203 GLY GLY A . n 
A 1 225 GLY 225 204 204 GLY GLY A . n 
A 1 226 ALA 226 205 205 ALA ALA A . n 
A 1 227 GLN 227 206 206 GLN GLN A . n 
A 1 228 GLN 228 207 207 GLN GLN A . n 
A 1 229 ASP 229 208 208 ASP ASP A . n 
A 1 230 ARG 230 209 209 ARG ARG A . n 
A 1 231 LEU 231 210 210 LEU LEU A . n 
A 1 232 VAL 232 211 211 VAL VAL A . n 
A 1 233 GLY 233 212 212 GLY GLY A . n 
A 1 234 GLY 234 213 213 GLY GLY A . n 
A 1 235 VAL 235 214 214 VAL VAL A . n 
A 1 236 GLN 236 215 215 GLN GLN A . n 
A 1 237 PRO 237 216 216 PRO PRO A . n 
A 1 238 LEU 238 217 217 LEU LEU A . n 
A 1 239 ALA 239 218 218 ALA ALA A . n 
A 1 240 GLU 240 219 219 GLU GLU A . n 
A 1 241 ARG 241 220 220 ARG ARG A . n 
A 1 242 LEU 242 221 221 LEU LEU A . n 
A 1 243 ALA 243 222 222 ALA ALA A . n 
A 1 244 ALA 244 223 223 ALA ALA A . n 
A 1 245 ARG 245 224 224 ARG ARG A . n 
A 1 246 LEU 246 225 225 LEU LEU A . n 
A 1 247 PRO 247 226 226 PRO PRO A . n 
A 1 248 ASP 248 227 227 ASP ASP A . n 
A 1 249 GLY 249 228 228 GLY GLY A . n 
A 1 250 ALA 250 229 229 ALA ALA A . n 
A 1 251 LEU 251 230 230 LEU LEU A . n 
A 1 252 ARG 252 231 231 ARG ARG A . n 
A 1 253 LEU 253 232 232 LEU LEU A . n 
A 1 254 SER 254 233 233 SER SER A . n 
A 1 255 THR 255 234 234 THR THR A . n 
A 1 256 PRO 256 235 235 PRO PRO A . n 
A 1 257 VAL 257 236 236 VAL VAL A . n 
A 1 258 ARG 258 237 237 ARG ARG A . n 
A 1 259 GLY 259 238 238 GLY GLY A . n 
A 1 260 LEU 260 239 239 LEU LEU A . n 
A 1 261 ALA 261 240 240 ALA ALA A . n 
A 1 262 GLN 262 241 241 GLN GLN A . n 
A 1 263 ASP 263 242 242 ASP ASP A . n 
A 1 264 GLY 264 243 243 GLY GLY A . n 
A 1 265 ASP 265 244 244 ASP ASP A . n 
A 1 266 GLY 266 245 245 GLY GLY A . n 
A 1 267 VAL 267 246 246 VAL VAL A . n 
A 1 268 THR 268 247 247 THR THR A . n 
A 1 269 VAL 269 248 248 VAL VAL A . n 
A 1 270 ARG 270 249 249 ARG ARG A . n 
A 1 271 THR 271 250 250 THR THR A . n 
A 1 272 ALA 272 251 251 ALA ALA A . n 
A 1 273 GLY 273 252 252 GLY GLY A . n 
A 1 274 GLY 274 253 253 GLY GLY A . n 
A 1 275 GLU 275 254 254 GLU GLU A . n 
A 1 276 VAL 276 255 255 VAL VAL A . n 
A 1 277 ARG 277 256 256 ARG ARG A . n 
A 1 278 ALA 278 257 257 ALA ALA A . n 
A 1 279 ARG 279 258 258 ARG ARG A . n 
A 1 280 ARG 280 259 259 ARG ARG A . n 
A 1 281 ALA 281 260 260 ALA ALA A . n 
A 1 282 ILE 282 261 261 ILE ILE A . n 
A 1 283 VAL 283 262 262 VAL VAL A . n 
A 1 284 ALA 284 263 263 ALA ALA A . n 
A 1 285 VAL 285 264 264 VAL VAL A . n 
A 1 286 PRO 286 265 265 PRO PRO A . n 
A 1 287 PRO 287 266 266 PRO PRO A . n 
A 1 288 THR 288 267 267 THR THR A . n 
A 1 289 LEU 289 268 268 LEU LEU A . n 
A 1 290 ALA 290 269 269 ALA ALA A . n 
A 1 291 GLY 291 270 270 GLY GLY A . n 
A 1 292 ARG 292 271 271 ARG ARG A . n 
A 1 293 ILE 293 272 272 ILE ILE A . n 
A 1 294 ASP 294 273 273 ASP ASP A . n 
A 1 295 HIS 295 274 274 HIS HIS A . n 
A 1 296 ASP 296 275 275 ASP ASP A . n 
A 1 297 PRO 297 276 276 PRO PRO A . n 
A 1 298 PRO 298 277 277 PRO PRO A . n 
A 1 299 LEU 299 278 278 LEU LEU A . n 
A 1 300 PRO 300 279 279 PRO PRO A . n 
A 1 301 PRO 301 280 280 PRO PRO A . n 
A 1 302 GLN 302 281 281 GLN GLN A . n 
A 1 303 ARG 303 282 282 ARG ARG A . n 
A 1 304 ASP 304 283 283 ASP ASP A . n 
A 1 305 GLN 305 284 284 GLN GLN A . n 
A 1 306 LEU 306 285 285 LEU LEU A . n 
A 1 307 LEU 307 286 286 LEU LEU A . n 
A 1 308 GLN 308 287 287 GLN GLN A . n 
A 1 309 HIS 309 288 288 HIS HIS A . n 
A 1 310 MET 310 289 289 MET MET A . n 
A 1 311 PRO 311 290 290 PRO PRO A . n 
A 1 312 GLN 312 291 291 GLN GLN A . n 
A 1 313 GLY 313 292 292 GLY GLY A . n 
A 1 314 SER 314 293 293 SER SER A . n 
A 1 315 VAL 315 294 294 VAL VAL A . n 
A 1 316 VAL 316 295 295 VAL VAL A . n 
A 1 317 LYS 317 296 296 LYS LYS A . n 
A 1 318 PHE 318 297 297 PHE PHE A . n 
A 1 319 HIS 319 298 298 HIS HIS A . n 
A 1 320 VAL 320 299 299 VAL VAL A . n 
A 1 321 ILE 321 300 300 ILE ILE A . n 
A 1 322 TYR 322 301 301 TYR TYR A . n 
A 1 323 ASP 323 302 302 ASP ASP A . n 
A 1 324 GLU 324 303 303 GLU GLU A . n 
A 1 325 PRO 325 304 304 PRO PRO A . n 
A 1 326 TRP 326 305 305 TRP TRP A . n 
A 1 327 TRP 327 306 306 TRP TRP A . n 
A 1 328 ARG 328 307 307 ARG ARG A . n 
A 1 329 ALA 329 308 308 ALA ALA A . n 
A 1 330 GLU 330 309 309 GLU GLU A . n 
A 1 331 GLY 331 310 310 GLY GLY A . n 
A 1 332 LEU 332 311 311 LEU LEU A . n 
A 1 333 SER 333 312 312 SER SER A . n 
A 1 334 GLY 334 313 313 GLY GLY A . n 
A 1 335 THR 335 314 314 THR THR A . n 
A 1 336 VAL 336 315 315 VAL VAL A . n 
A 1 337 LEU 337 316 316 LEU LEU A . n 
A 1 338 CYS 338 317 317 CYS CYS A . n 
A 1 339 PRO 339 318 318 PRO PRO A . n 
A 1 340 ASP 340 319 319 ASP ASP A . n 
A 1 341 GLU 341 320 320 GLU GLU A . n 
A 1 342 PRO 342 321 321 PRO PRO A . n 
A 1 343 ILE 343 322 322 ILE ILE A . n 
A 1 344 GLY 344 323 323 GLY GLY A . n 
A 1 345 VAL 345 324 324 VAL VAL A . n 
A 1 346 THR 346 325 325 THR THR A . n 
A 1 347 PHE 347 326 326 PHE PHE A . n 
A 1 348 ASP 348 327 327 ASP ASP A . n 
A 1 349 GLY 349 328 328 GLY GLY A . n 
A 1 350 THR 350 329 329 THR THR A . n 
A 1 351 PRO 351 330 330 PRO PRO A . n 
A 1 352 PRO 352 331 331 PRO PRO A . n 
A 1 353 ALA 353 332 332 ALA ALA A . n 
A 1 354 GLY 354 333 333 GLY GLY A . n 
A 1 355 THR 355 334 334 THR THR A . n 
A 1 356 PRO 356 335 335 PRO PRO A . n 
A 1 357 GLY 357 336 336 GLY GLY A . n 
A 1 358 ILE 358 337 337 ILE ILE A . n 
A 1 359 VAL 359 338 338 VAL VAL A . n 
A 1 360 THR 360 339 339 THR THR A . n 
A 1 361 GLY 361 340 340 GLY GLY A . n 
A 1 362 PHE 362 341 341 PHE PHE A . n 
A 1 363 PHE 363 342 342 PHE PHE A . n 
A 1 364 GLU 364 343 343 GLU GLU A . n 
A 1 365 GLY 365 344 344 GLY GLY A . n 
A 1 366 PRO 366 345 345 PRO PRO A . n 
A 1 367 ALA 367 346 346 ALA ALA A . n 
A 1 368 ALA 368 347 347 ALA ALA A . n 
A 1 369 VAL 369 348 348 VAL VAL A . n 
A 1 370 ALA 370 349 349 ALA ALA A . n 
A 1 371 ALA 371 350 350 ALA ALA A . n 
A 1 372 GLY 372 351 351 GLY GLY A . n 
A 1 373 ALA 373 352 352 ALA ALA A . n 
A 1 374 ARG 374 353 353 ARG ARG A . n 
A 1 375 THR 375 354 354 THR THR A . n 
A 1 376 ARG 376 355 355 ARG ARG A . n 
A 1 377 GLU 377 356 356 GLU GLU A . n 
A 1 378 GLU 378 357 357 GLU GLU A . n 
A 1 379 ARG 379 358 358 ARG ARG A . n 
A 1 380 ARG 380 359 359 ARG ARG A . n 
A 1 381 ASP 381 360 360 ASP ASP A . n 
A 1 382 VAL 382 361 361 VAL VAL A . n 
A 1 383 VAL 383 362 362 VAL VAL A . n 
A 1 384 VAL 384 363 363 VAL VAL A . n 
A 1 385 ASP 385 364 364 ASP ASP A . n 
A 1 386 VAL 386 365 365 VAL VAL A . n 
A 1 387 LEU 387 366 366 LEU LEU A . n 
A 1 388 ALA 388 367 367 ALA ALA A . n 
A 1 389 ARG 389 368 368 ARG ARG A . n 
A 1 390 THR 390 369 369 THR THR A . n 
A 1 391 LEU 391 370 370 LEU LEU A . n 
A 1 392 GLY 392 371 371 GLY GLY A . n 
A 1 393 GLU 393 372 372 GLU GLU A . n 
A 1 394 ARG 394 373 373 ARG ARG A . n 
A 1 395 ALA 395 374 374 ALA ALA A . n 
A 1 396 ARG 396 375 375 ARG ARG A . n 
A 1 397 ASP 397 376 376 ASP ASP A . n 
A 1 398 VAL 398 377 377 VAL VAL A . n 
A 1 399 ARG 399 378 378 ARG ARG A . n 
A 1 400 ASP 400 379 379 ASP ASP A . n 
A 1 401 TYR 401 380 380 TYR TYR A . n 
A 1 402 ILE 402 381 381 ILE ILE A . n 
A 1 403 ASP 403 382 382 ASP ASP A . n 
A 1 404 ARG 404 383 383 ARG ARG A . n 
A 1 405 ASP 405 384 384 ASP ASP A . n 
A 1 406 TRP 406 385 385 TRP TRP A . n 
A 1 407 SER 407 386 386 SER SER A . n 
A 1 408 ALA 408 387 387 ALA ALA A . n 
A 1 409 GLU 409 388 388 GLU GLU A . n 
A 1 410 PRO 410 389 389 PRO PRO A . n 
A 1 411 TRP 411 390 390 TRP TRP A . n 
A 1 412 THR 412 391 391 THR THR A . n 
A 1 413 ARG 413 392 392 ARG ARG A . n 
A 1 414 GLY 414 393 393 GLY GLY A . n 
A 1 415 CYS 415 394 394 CYS CYS A . n 
A 1 416 TYR 416 395 395 TYR TYR A . n 
A 1 417 GLY 417 396 396 GLY GLY A . n 
A 1 418 ALA 418 397 397 ALA ALA A . n 
A 1 419 HIS 419 398 398 HIS HIS A . n 
A 1 420 LEU 420 399 399 LEU LEU A . n 
A 1 421 PRO 421 400 400 PRO PRO A . n 
A 1 422 PRO 422 401 401 PRO PRO A . n 
A 1 423 GLY 423 402 402 GLY GLY A . n 
A 1 424 ALA 424 403 403 ALA ALA A . n 
A 1 425 TRP 425 404 404 TRP TRP A . n 
A 1 426 THR 426 405 405 THR THR A . n 
A 1 427 VAL 427 406 406 VAL VAL A . n 
A 1 428 TYR 428 407 407 TYR TYR A . n 
A 1 429 GLY 429 408 408 GLY GLY A . n 
A 1 430 PRO 430 409 409 PRO PRO A . n 
A 1 431 ALA 431 410 410 ALA ALA A . n 
A 1 432 LEU 432 411 411 LEU LEU A . n 
A 1 433 ARG 433 412 412 ARG ARG A . n 
A 1 434 VAL 434 413 413 VAL VAL A . n 
A 1 435 PRO 435 414 414 PRO PRO A . n 
A 1 436 VAL 436 415 415 VAL VAL A . n 
A 1 437 GLY 437 416 416 GLY GLY A . n 
A 1 438 ARG 438 417 417 ARG ARG A . n 
A 1 439 VAL 439 418 418 VAL VAL A . n 
A 1 440 HIS 440 419 419 HIS HIS A . n 
A 1 441 TRP 441 420 420 TRP TRP A . n 
A 1 442 ALA 442 421 421 ALA ALA A . n 
A 1 443 GLY 443 422 422 GLY GLY A . n 
A 1 444 THR 444 423 423 THR THR A . n 
A 1 445 GLU 445 424 424 GLU GLU A . n 
A 1 446 THR 446 425 425 THR THR A . n 
A 1 447 ALA 447 426 426 ALA ALA A . n 
A 1 448 GLU 448 427 427 GLU GLU A . n 
A 1 449 ARG 449 428 428 ARG ARG A . n 
A 1 450 TRP 450 429 429 TRP TRP A . n 
A 1 451 THR 451 430 430 THR THR A . n 
A 1 452 GLY 452 431 431 GLY GLY A . n 
A 1 453 TYR 453 432 432 TYR TYR A . n 
A 1 454 ILE 454 433 433 ILE ILE A . n 
A 1 455 ASP 455 434 434 ASP ASP A . n 
A 1 456 GLY 456 435 435 GLY GLY A . n 
A 1 457 ALA 457 436 436 ALA ALA A . n 
A 1 458 ILE 458 437 437 ILE ILE A . n 
A 1 459 GLU 459 438 438 GLU GLU A . n 
A 1 460 SER 460 439 439 SER SER A . n 
A 1 461 GLY 461 440 440 GLY GLY A . n 
A 1 462 GLN 462 441 441 GLN GLN A . n 
A 1 463 ARG 463 442 442 ARG ARG A . n 
A 1 464 ALA 464 443 443 ALA ALA A . n 
A 1 465 ALA 465 444 444 ALA ALA A . n 
A 1 466 ALA 466 445 445 ALA ALA A . n 
A 1 467 GLU 467 446 446 GLU GLU A . n 
A 1 468 VAL 468 447 447 VAL VAL A . n 
A 1 469 LEU 469 448 448 LEU LEU A . n 
A 1 470 ALA 470 449 449 ALA ALA A . n 
A 1 471 ALA 471 450 450 ALA ALA A . n 
A 1 472 LEU 472 451 451 LEU LEU A . n 
A 1 473 GLY 473 452 452 GLY GLY A . n 
A 1 474 SER 474 453 ?   ?   ?   A . n 
B 1 1   MET 1   -20 ?   ?   ?   B . n 
B 1 2   GLY 2   -19 ?   ?   ?   B . n 
B 1 3   SER 3   -18 ?   ?   ?   B . n 
B 1 4   SER 4   -17 ?   ?   ?   B . n 
B 1 5   HIS 5   -16 ?   ?   ?   B . n 
B 1 6   HIS 6   -15 ?   ?   ?   B . n 
B 1 7   HIS 7   -14 ?   ?   ?   B . n 
B 1 8   HIS 8   -13 ?   ?   ?   B . n 
B 1 9   HIS 9   -12 ?   ?   ?   B . n 
B 1 10  HIS 10  -11 ?   ?   ?   B . n 
B 1 11  GLY 11  -10 ?   ?   ?   B . n 
B 1 12  SER 12  -9  ?   ?   ?   B . n 
B 1 13  GLY 13  -8  ?   ?   ?   B . n 
B 1 14  LEU 14  -7  ?   ?   ?   B . n 
B 1 15  VAL 15  -6  ?   ?   ?   B . n 
B 1 16  PRO 16  -5  ?   ?   ?   B . n 
B 1 17  ARG 17  -4  ?   ?   ?   B . n 
B 1 18  GLY 18  -3  ?   ?   ?   B . n 
B 1 19  SER 19  -2  ?   ?   ?   B . n 
B 1 20  ALA 20  -1  ?   ?   ?   B . n 
B 1 21  GLY 21  0   ?   ?   ?   B . n 
B 1 22  MET 22  1   ?   ?   ?   B . n 
B 1 23  PRO 23  2   ?   ?   ?   B . n 
B 1 24  SER 24  3   ?   ?   ?   B . n 
B 1 25  GLU 25  4   ?   ?   ?   B . n 
B 1 26  GLN 26  5   5   GLN GLN B . n 
B 1 27  VAL 27  6   6   VAL VAL B . n 
B 1 28  ASP 28  7   7   ASP ASP B . n 
B 1 29  VAL 29  8   8   VAL VAL B . n 
B 1 30  VAL 30  9   9   VAL VAL B . n 
B 1 31  VAL 31  10  10  VAL VAL B . n 
B 1 32  VAL 32  11  11  VAL VAL B . n 
B 1 33  GLY 33  12  12  GLY GLY B . n 
B 1 34  ALA 34  13  13  ALA ALA B . n 
B 1 35  GLY 35  14  14  GLY GLY B . n 
B 1 36  PHE 36  15  15  PHE PHE B . n 
B 1 37  ALA 37  16  16  ALA ALA B . n 
B 1 38  GLY 38  17  17  GLY GLY B . n 
B 1 39  LEU 39  18  18  LEU LEU B . n 
B 1 40  THR 40  19  19  THR THR B . n 
B 1 41  ALA 41  20  20  ALA ALA B . n 
B 1 42  ALA 42  21  21  ALA ALA B . n 
B 1 43  ARG 43  22  22  ARG ARG B . n 
B 1 44  ALA 44  23  23  ALA ALA B . n 
B 1 45  VAL 45  24  24  VAL VAL B . n 
B 1 46  HIS 46  25  25  HIS HIS B . n 
B 1 47  GLU 47  26  26  GLU GLU B . n 
B 1 48  ALA 48  27  27  ALA ALA B . n 
B 1 49  GLY 49  28  28  GLY GLY B . n 
B 1 50  ARG 50  29  29  ARG ARG B . n 
B 1 51  SER 51  30  30  SER SER B . n 
B 1 52  VAL 52  31  31  VAL VAL B . n 
B 1 53  LEU 53  32  32  LEU LEU B . n 
B 1 54  VAL 54  33  33  VAL VAL B . n 
B 1 55  LEU 55  34  34  LEU LEU B . n 
B 1 56  GLU 56  35  35  GLU GLU B . n 
B 1 57  ALA 57  36  36  ALA ALA B . n 
B 1 58  ARG 58  37  37  ARG ARG B . n 
B 1 59  ASP 59  38  38  ASP ASP B . n 
B 1 60  ARG 60  39  39  ARG ARG B . n 
B 1 61  VAL 61  40  40  VAL VAL B . n 
B 1 62  GLY 62  41  41  GLY GLY B . n 
B 1 63  GLY 63  42  42  GLY GLY B . n 
B 1 64  ARG 64  43  43  ARG ARG B . n 
B 1 65  THR 65  44  44  THR THR B . n 
B 1 66  CYS 66  45  45  CYS CYS B . n 
B 1 67  THR 67  46  46  THR THR B . n 
B 1 68  GLU 68  47  47  GLU GLU B . n 
B 1 69  GLU 69  48  48  GLU GLU B . n 
B 1 70  HIS 70  49  49  HIS HIS B . n 
B 1 71  HIS 71  50  50  HIS HIS B . n 
B 1 72  GLY 72  51  51  GLY GLY B . n 
B 1 73  THR 73  52  52  THR THR B . n 
B 1 74  TRP 74  53  53  TRP TRP B . n 
B 1 75  ILE 75  54  54  ILE ILE B . n 
B 1 76  ASP 76  55  55  ASP ASP B . n 
B 1 77  LEU 77  56  56  LEU LEU B . n 
B 1 78  GLY 78  57  57  GLY GLY B . n 
B 1 79  GLY 79  58  58  GLY GLY B . n 
B 1 80  GLN 80  59  59  GLN GLN B . n 
B 1 81  TRP 81  60  60  TRP TRP B . n 
B 1 82  ILE 82  61  61  ILE ILE B . n 
B 1 83  GLY 83  62  62  GLY GLY B . n 
B 1 84  PRO 84  63  63  PRO PRO B . n 
B 1 85  GLY 85  64  64  GLY GLY B . n 
B 1 86  GLN 86  65  65  GLN GLN B . n 
B 1 87  ASP 87  66  66  ASP ASP B . n 
B 1 88  ARG 88  67  67  ARG ARG B . n 
B 1 89  VAL 89  68  68  VAL VAL B . n 
B 1 90  ALA 90  69  69  ALA ALA B . n 
B 1 91  ALA 91  70  70  ALA ALA B . n 
B 1 92  LEU 92  71  71  LEU LEU B . n 
B 1 93  ALA 93  72  72  ALA ALA B . n 
B 1 94  ALA 94  73  73  ALA ALA B . n 
B 1 95  GLU 95  74  74  GLU GLU B . n 
B 1 96  LEU 96  75  75  LEU LEU B . n 
B 1 97  GLY 97  76  76  GLY GLY B . n 
B 1 98  VAL 98  77  77  VAL VAL B . n 
B 1 99  GLU 99  78  78  GLU GLU B . n 
B 1 100 THR 100 79  79  THR THR B . n 
B 1 101 TYR 101 80  80  TYR TYR B . n 
B 1 102 PRO 102 81  81  PRO PRO B . n 
B 1 103 GLN 103 82  82  GLN GLN B . n 
B 1 104 PRO 104 83  83  PRO PRO B . n 
B 1 105 THR 105 84  84  THR THR B . n 
B 1 106 GLU 106 85  85  GLU GLU B . n 
B 1 107 GLY 107 86  86  GLY GLY B . n 
B 1 108 ASP 108 87  87  ASP ASP B . n 
B 1 109 ASP 109 88  88  ASP ASP B . n 
B 1 110 VAL 110 89  89  VAL VAL B . n 
B 1 111 VAL 111 90  90  VAL VAL B . n 
B 1 112 LEU 112 91  91  LEU LEU B . n 
B 1 113 PHE 113 92  92  PHE PHE B . n 
B 1 114 GLY 114 93  93  GLY GLY B . n 
B 1 115 ASP 115 94  94  ASP ASP B . n 
B 1 116 GLY 116 95  95  GLY GLY B . n 
B 1 117 GLU 117 96  96  GLU GLU B . n 
B 1 118 PRO 118 97  97  PRO PRO B . n 
B 1 119 GLN 119 98  98  GLN GLN B . n 
B 1 120 ARG 120 99  99  ARG ARG B . n 
B 1 121 ALA 121 100 100 ALA ALA B . n 
B 1 122 PRO 122 101 101 PRO PRO B . n 
B 1 123 ASP 123 102 102 ASP ASP B . n 
B 1 124 VAL 124 103 103 VAL VAL B . n 
B 1 125 ALA 125 104 104 ALA ALA B . n 
B 1 126 LEU 126 105 105 LEU LEU B . n 
B 1 127 ALA 127 106 106 ALA ALA B . n 
B 1 128 PHE 128 107 107 PHE PHE B . n 
B 1 129 SER 129 108 108 SER SER B . n 
B 1 130 ASP 130 109 109 ASP ASP B . n 
B 1 131 GLU 131 110 110 GLU GLU B . n 
B 1 132 GLU 132 111 111 GLU GLU B . n 
B 1 133 LEU 133 112 112 LEU LEU B . n 
B 1 134 THR 134 113 113 THR THR B . n 
B 1 135 ALA 135 114 114 ALA ALA B . n 
B 1 136 TYR 136 115 115 TYR TYR B . n 
B 1 137 LEU 137 116 116 LEU LEU B . n 
B 1 138 GLU 138 117 117 GLU GLU B . n 
B 1 139 LEU 139 118 118 LEU LEU B . n 
B 1 140 ALA 140 119 119 ALA ALA B . n 
B 1 141 GLY 141 120 120 GLY GLY B . n 
B 1 142 ALA 142 121 121 ALA ALA B . n 
B 1 143 LEU 143 122 122 LEU LEU B . n 
B 1 144 GLU 144 123 123 GLU GLU B . n 
B 1 145 ALA 145 124 124 ALA ALA B . n 
B 1 146 ILE 146 125 125 ILE ILE B . n 
B 1 147 ALA 147 126 126 ALA ALA B . n 
B 1 148 GLU 148 127 127 GLU GLU B . n 
B 1 149 LYS 149 128 128 LYS LYS B . n 
B 1 150 VAL 150 129 129 VAL VAL B . n 
B 1 151 PRO 151 130 130 PRO PRO B . n 
B 1 152 LEU 152 131 131 LEU LEU B . n 
B 1 153 ASP 153 132 132 ASP ASP B . n 
B 1 154 ALA 154 133 133 ALA ALA B . n 
B 1 155 PRO 155 134 134 PRO PRO B . n 
B 1 156 TRP 156 135 135 TRP TRP B . n 
B 1 157 LEU 157 136 136 LEU LEU B . n 
B 1 158 ALA 158 137 137 ALA ALA B . n 
B 1 159 PRO 159 138 138 PRO PRO B . n 
B 1 160 GLU 160 139 139 GLU GLU B . n 
B 1 161 ALA 161 140 140 ALA ALA B . n 
B 1 162 ALA 162 141 141 ALA ALA B . n 
B 1 163 ALA 163 142 142 ALA ALA B . n 
B 1 164 TRP 164 143 143 TRP TRP B . n 
B 1 165 ASP 165 144 144 ASP ASP B . n 
B 1 166 ALA 166 145 145 ALA ALA B . n 
B 1 167 THR 167 146 146 THR THR B . n 
B 1 168 THR 168 147 147 THR THR B . n 
B 1 169 LEU 169 148 148 LEU LEU B . n 
B 1 170 ARG 170 149 149 ARG ARG B . n 
B 1 171 GLU 171 150 150 GLU GLU B . n 
B 1 172 TRP 172 151 151 TRP TRP B . n 
B 1 173 VAL 173 152 152 VAL VAL B . n 
B 1 174 ALA 174 153 153 ALA ALA B . n 
B 1 175 GLY 175 154 154 GLY GLY B . n 
B 1 176 THR 176 155 155 THR THR B . n 
B 1 177 GLY 177 156 156 GLY GLY B . n 
B 1 178 VAL 178 157 157 VAL VAL B . n 
B 1 179 PRO 179 158 158 PRO PRO B . n 
B 1 180 ASP 180 159 159 ASP ASP B . n 
B 1 181 ARG 181 160 160 ARG ARG B . n 
B 1 182 VAL 182 161 161 VAL VAL B . n 
B 1 183 ALA 183 162 162 ALA ALA B . n 
B 1 184 GLY 184 163 163 GLY GLY B . n 
B 1 185 LEU 185 164 164 LEU LEU B . n 
B 1 186 PHE 186 165 165 PHE PHE B . n 
B 1 187 GLU 187 166 166 GLU GLU B . n 
B 1 188 VAL 188 167 167 VAL VAL B . n 
B 1 189 ALA 189 168 168 ALA ALA B . n 
B 1 190 VAL 190 169 169 VAL VAL B . n 
B 1 191 GLN 191 170 170 GLN GLN B . n 
B 1 192 ALA 192 171 171 ALA ALA B . n 
B 1 193 VAL 193 172 172 VAL VAL B . n 
B 1 194 PHE 194 173 173 PHE PHE B . n 
B 1 195 ALA 195 174 174 ALA ALA B . n 
B 1 196 ALA 196 175 175 ALA ALA B . n 
B 1 197 THR 197 176 176 THR THR B . n 
B 1 198 SER 198 177 177 SER SER B . n 
B 1 199 ALA 199 178 178 ALA ALA B . n 
B 1 200 GLN 200 179 179 GLN GLN B . n 
B 1 201 LEU 201 180 180 LEU LEU B . n 
B 1 202 SER 202 181 181 SER SER B . n 
B 1 203 LEU 203 182 182 LEU LEU B . n 
B 1 204 LEU 204 183 183 LEU LEU B . n 
B 1 205 HIS 205 184 184 HIS HIS B . n 
B 1 206 ALA 206 185 185 ALA ALA B . n 
B 1 207 ALA 207 186 186 ALA ALA B . n 
B 1 208 HIS 208 187 187 HIS HIS B . n 
B 1 209 TYR 209 188 188 TYR TYR B . n 
B 1 210 VAL 210 189 189 VAL VAL B . n 
B 1 211 HIS 211 190 190 HIS HIS B . n 
B 1 212 SER 212 191 191 SER SER B . n 
B 1 213 ALA 213 192 192 ALA ALA B . n 
B 1 214 GLY 214 193 193 GLY GLY B . n 
B 1 215 GLY 215 194 194 GLY GLY B . n 
B 1 216 TRP 216 195 195 TRP TRP B . n 
B 1 217 SER 217 196 196 SER SER B . n 
B 1 218 LYS 218 197 197 LYS LYS B . n 
B 1 219 LEU 219 198 198 LEU LEU B . n 
B 1 220 THR 220 199 199 THR THR B . n 
B 1 221 ASP 221 200 200 ASP ASP B . n 
B 1 222 THR 222 201 201 THR THR B . n 
B 1 223 GLU 223 202 202 GLU GLU B . n 
B 1 224 GLY 224 203 203 GLY GLY B . n 
B 1 225 GLY 225 204 204 GLY GLY B . n 
B 1 226 ALA 226 205 205 ALA ALA B . n 
B 1 227 GLN 227 206 206 GLN GLN B . n 
B 1 228 GLN 228 207 207 GLN GLN B . n 
B 1 229 ASP 229 208 208 ASP ASP B . n 
B 1 230 ARG 230 209 209 ARG ARG B . n 
B 1 231 LEU 231 210 210 LEU LEU B . n 
B 1 232 VAL 232 211 211 VAL VAL B . n 
B 1 233 GLY 233 212 212 GLY GLY B . n 
B 1 234 GLY 234 213 213 GLY GLY B . n 
B 1 235 VAL 235 214 214 VAL VAL B . n 
B 1 236 GLN 236 215 215 GLN GLN B . n 
B 1 237 PRO 237 216 216 PRO PRO B . n 
B 1 238 LEU 238 217 217 LEU LEU B . n 
B 1 239 ALA 239 218 218 ALA ALA B . n 
B 1 240 GLU 240 219 219 GLU GLU B . n 
B 1 241 ARG 241 220 220 ARG ARG B . n 
B 1 242 LEU 242 221 221 LEU LEU B . n 
B 1 243 ALA 243 222 222 ALA ALA B . n 
B 1 244 ALA 244 223 223 ALA ALA B . n 
B 1 245 ARG 245 224 224 ARG ARG B . n 
B 1 246 LEU 246 225 225 LEU LEU B . n 
B 1 247 PRO 247 226 226 PRO PRO B . n 
B 1 248 ASP 248 227 227 ASP ASP B . n 
B 1 249 GLY 249 228 228 GLY GLY B . n 
B 1 250 ALA 250 229 229 ALA ALA B . n 
B 1 251 LEU 251 230 230 LEU LEU B . n 
B 1 252 ARG 252 231 231 ARG ARG B . n 
B 1 253 LEU 253 232 232 LEU LEU B . n 
B 1 254 SER 254 233 233 SER SER B . n 
B 1 255 THR 255 234 234 THR THR B . n 
B 1 256 PRO 256 235 235 PRO PRO B . n 
B 1 257 VAL 257 236 236 VAL VAL B . n 
B 1 258 ARG 258 237 237 ARG ARG B . n 
B 1 259 GLY 259 238 238 GLY GLY B . n 
B 1 260 LEU 260 239 239 LEU LEU B . n 
B 1 261 ALA 261 240 240 ALA ALA B . n 
B 1 262 GLN 262 241 241 GLN GLN B . n 
B 1 263 ASP 263 242 242 ASP ASP B . n 
B 1 264 GLY 264 243 243 GLY GLY B . n 
B 1 265 ASP 265 244 244 ASP ASP B . n 
B 1 266 GLY 266 245 245 GLY GLY B . n 
B 1 267 VAL 267 246 246 VAL VAL B . n 
B 1 268 THR 268 247 247 THR THR B . n 
B 1 269 VAL 269 248 248 VAL VAL B . n 
B 1 270 ARG 270 249 249 ARG ARG B . n 
B 1 271 THR 271 250 250 THR THR B . n 
B 1 272 ALA 272 251 251 ALA ALA B . n 
B 1 273 GLY 273 252 252 GLY GLY B . n 
B 1 274 GLY 274 253 253 GLY GLY B . n 
B 1 275 GLU 275 254 254 GLU GLU B . n 
B 1 276 VAL 276 255 255 VAL VAL B . n 
B 1 277 ARG 277 256 256 ARG ARG B . n 
B 1 278 ALA 278 257 257 ALA ALA B . n 
B 1 279 ARG 279 258 258 ARG ARG B . n 
B 1 280 ARG 280 259 259 ARG ARG B . n 
B 1 281 ALA 281 260 260 ALA ALA B . n 
B 1 282 ILE 282 261 261 ILE ILE B . n 
B 1 283 VAL 283 262 262 VAL VAL B . n 
B 1 284 ALA 284 263 263 ALA ALA B . n 
B 1 285 VAL 285 264 264 VAL VAL B . n 
B 1 286 PRO 286 265 265 PRO PRO B . n 
B 1 287 PRO 287 266 266 PRO PRO B . n 
B 1 288 THR 288 267 267 THR THR B . n 
B 1 289 LEU 289 268 268 LEU LEU B . n 
B 1 290 ALA 290 269 269 ALA ALA B . n 
B 1 291 GLY 291 270 270 GLY GLY B . n 
B 1 292 ARG 292 271 271 ARG ARG B . n 
B 1 293 ILE 293 272 272 ILE ILE B . n 
B 1 294 ASP 294 273 273 ASP ASP B . n 
B 1 295 HIS 295 274 274 HIS HIS B . n 
B 1 296 ASP 296 275 275 ASP ASP B . n 
B 1 297 PRO 297 276 276 PRO PRO B . n 
B 1 298 PRO 298 277 277 PRO PRO B . n 
B 1 299 LEU 299 278 278 LEU LEU B . n 
B 1 300 PRO 300 279 279 PRO PRO B . n 
B 1 301 PRO 301 280 280 PRO PRO B . n 
B 1 302 GLN 302 281 281 GLN GLN B . n 
B 1 303 ARG 303 282 282 ARG ARG B . n 
B 1 304 ASP 304 283 283 ASP ASP B . n 
B 1 305 GLN 305 284 284 GLN GLN B . n 
B 1 306 LEU 306 285 285 LEU LEU B . n 
B 1 307 LEU 307 286 286 LEU LEU B . n 
B 1 308 GLN 308 287 287 GLN GLN B . n 
B 1 309 HIS 309 288 288 HIS HIS B . n 
B 1 310 MET 310 289 289 MET MET B . n 
B 1 311 PRO 311 290 290 PRO PRO B . n 
B 1 312 GLN 312 291 291 GLN GLN B . n 
B 1 313 GLY 313 292 292 GLY GLY B . n 
B 1 314 SER 314 293 293 SER SER B . n 
B 1 315 VAL 315 294 294 VAL VAL B . n 
B 1 316 VAL 316 295 295 VAL VAL B . n 
B 1 317 LYS 317 296 296 LYS LYS B . n 
B 1 318 PHE 318 297 297 PHE PHE B . n 
B 1 319 HIS 319 298 298 HIS HIS B . n 
B 1 320 VAL 320 299 299 VAL VAL B . n 
B 1 321 ILE 321 300 300 ILE ILE B . n 
B 1 322 TYR 322 301 301 TYR TYR B . n 
B 1 323 ASP 323 302 302 ASP ASP B . n 
B 1 324 GLU 324 303 303 GLU GLU B . n 
B 1 325 PRO 325 304 304 PRO PRO B . n 
B 1 326 TRP 326 305 305 TRP TRP B . n 
B 1 327 TRP 327 306 306 TRP TRP B . n 
B 1 328 ARG 328 307 307 ARG ARG B . n 
B 1 329 ALA 329 308 308 ALA ALA B . n 
B 1 330 GLU 330 309 309 GLU GLU B . n 
B 1 331 GLY 331 310 310 GLY GLY B . n 
B 1 332 LEU 332 311 311 LEU LEU B . n 
B 1 333 SER 333 312 312 SER SER B . n 
B 1 334 GLY 334 313 313 GLY GLY B . n 
B 1 335 THR 335 314 314 THR THR B . n 
B 1 336 VAL 336 315 315 VAL VAL B . n 
B 1 337 LEU 337 316 316 LEU LEU B . n 
B 1 338 CYS 338 317 317 CYS CYS B . n 
B 1 339 PRO 339 318 318 PRO PRO B . n 
B 1 340 ASP 340 319 319 ASP ASP B . n 
B 1 341 GLU 341 320 320 GLU GLU B . n 
B 1 342 PRO 342 321 321 PRO PRO B . n 
B 1 343 ILE 343 322 322 ILE ILE B . n 
B 1 344 GLY 344 323 323 GLY GLY B . n 
B 1 345 VAL 345 324 324 VAL VAL B . n 
B 1 346 THR 346 325 325 THR THR B . n 
B 1 347 PHE 347 326 326 PHE PHE B . n 
B 1 348 ASP 348 327 327 ASP ASP B . n 
B 1 349 GLY 349 328 328 GLY GLY B . n 
B 1 350 THR 350 329 329 THR THR B . n 
B 1 351 PRO 351 330 330 PRO PRO B . n 
B 1 352 PRO 352 331 331 PRO PRO B . n 
B 1 353 ALA 353 332 332 ALA ALA B . n 
B 1 354 GLY 354 333 333 GLY GLY B . n 
B 1 355 THR 355 334 334 THR THR B . n 
B 1 356 PRO 356 335 335 PRO PRO B . n 
B 1 357 GLY 357 336 336 GLY GLY B . n 
B 1 358 ILE 358 337 337 ILE ILE B . n 
B 1 359 VAL 359 338 338 VAL VAL B . n 
B 1 360 THR 360 339 339 THR THR B . n 
B 1 361 GLY 361 340 340 GLY GLY B . n 
B 1 362 PHE 362 341 341 PHE PHE B . n 
B 1 363 PHE 363 342 342 PHE PHE B . n 
B 1 364 GLU 364 343 343 GLU GLU B . n 
B 1 365 GLY 365 344 344 GLY GLY B . n 
B 1 366 PRO 366 345 345 PRO PRO B . n 
B 1 367 ALA 367 346 346 ALA ALA B . n 
B 1 368 ALA 368 347 347 ALA ALA B . n 
B 1 369 VAL 369 348 348 VAL VAL B . n 
B 1 370 ALA 370 349 349 ALA ALA B . n 
B 1 371 ALA 371 350 350 ALA ALA B . n 
B 1 372 GLY 372 351 351 GLY GLY B . n 
B 1 373 ALA 373 352 352 ALA ALA B . n 
B 1 374 ARG 374 353 353 ARG ARG B . n 
B 1 375 THR 375 354 354 THR THR B . n 
B 1 376 ARG 376 355 355 ARG ARG B . n 
B 1 377 GLU 377 356 356 GLU GLU B . n 
B 1 378 GLU 378 357 357 GLU GLU B . n 
B 1 379 ARG 379 358 358 ARG ARG B . n 
B 1 380 ARG 380 359 359 ARG ARG B . n 
B 1 381 ASP 381 360 360 ASP ASP B . n 
B 1 382 VAL 382 361 361 VAL VAL B . n 
B 1 383 VAL 383 362 362 VAL VAL B . n 
B 1 384 VAL 384 363 363 VAL VAL B . n 
B 1 385 ASP 385 364 364 ASP ASP B . n 
B 1 386 VAL 386 365 365 VAL VAL B . n 
B 1 387 LEU 387 366 366 LEU LEU B . n 
B 1 388 ALA 388 367 367 ALA ALA B . n 
B 1 389 ARG 389 368 368 ARG ARG B . n 
B 1 390 THR 390 369 369 THR THR B . n 
B 1 391 LEU 391 370 370 LEU LEU B . n 
B 1 392 GLY 392 371 371 GLY GLY B . n 
B 1 393 GLU 393 372 372 GLU GLU B . n 
B 1 394 ARG 394 373 373 ARG ARG B . n 
B 1 395 ALA 395 374 374 ALA ALA B . n 
B 1 396 ARG 396 375 375 ARG ARG B . n 
B 1 397 ASP 397 376 376 ASP ASP B . n 
B 1 398 VAL 398 377 377 VAL VAL B . n 
B 1 399 ARG 399 378 378 ARG ARG B . n 
B 1 400 ASP 400 379 379 ASP ASP B . n 
B 1 401 TYR 401 380 380 TYR TYR B . n 
B 1 402 ILE 402 381 381 ILE ILE B . n 
B 1 403 ASP 403 382 382 ASP ASP B . n 
B 1 404 ARG 404 383 383 ARG ARG B . n 
B 1 405 ASP 405 384 384 ASP ASP B . n 
B 1 406 TRP 406 385 385 TRP TRP B . n 
B 1 407 SER 407 386 386 SER SER B . n 
B 1 408 ALA 408 387 387 ALA ALA B . n 
B 1 409 GLU 409 388 388 GLU GLU B . n 
B 1 410 PRO 410 389 389 PRO PRO B . n 
B 1 411 TRP 411 390 390 TRP TRP B . n 
B 1 412 THR 412 391 391 THR THR B . n 
B 1 413 ARG 413 392 392 ARG ARG B . n 
B 1 414 GLY 414 393 393 GLY GLY B . n 
B 1 415 CYS 415 394 394 CYS CYS B . n 
B 1 416 TYR 416 395 395 TYR TYR B . n 
B 1 417 GLY 417 396 396 GLY GLY B . n 
B 1 418 ALA 418 397 397 ALA ALA B . n 
B 1 419 HIS 419 398 398 HIS HIS B . n 
B 1 420 LEU 420 399 399 LEU LEU B . n 
B 1 421 PRO 421 400 400 PRO PRO B . n 
B 1 422 PRO 422 401 401 PRO PRO B . n 
B 1 423 GLY 423 402 402 GLY GLY B . n 
B 1 424 ALA 424 403 403 ALA ALA B . n 
B 1 425 TRP 425 404 404 TRP TRP B . n 
B 1 426 THR 426 405 405 THR THR B . n 
B 1 427 VAL 427 406 406 VAL VAL B . n 
B 1 428 TYR 428 407 407 TYR TYR B . n 
B 1 429 GLY 429 408 408 GLY GLY B . n 
B 1 430 PRO 430 409 409 PRO PRO B . n 
B 1 431 ALA 431 410 410 ALA ALA B . n 
B 1 432 LEU 432 411 411 LEU LEU B . n 
B 1 433 ARG 433 412 412 ARG ARG B . n 
B 1 434 VAL 434 413 413 VAL VAL B . n 
B 1 435 PRO 435 414 414 PRO PRO B . n 
B 1 436 VAL 436 415 415 VAL VAL B . n 
B 1 437 GLY 437 416 416 GLY GLY B . n 
B 1 438 ARG 438 417 417 ARG ARG B . n 
B 1 439 VAL 439 418 418 VAL VAL B . n 
B 1 440 HIS 440 419 419 HIS HIS B . n 
B 1 441 TRP 441 420 420 TRP TRP B . n 
B 1 442 ALA 442 421 421 ALA ALA B . n 
B 1 443 GLY 443 422 422 GLY GLY B . n 
B 1 444 THR 444 423 423 THR THR B . n 
B 1 445 GLU 445 424 424 GLU GLU B . n 
B 1 446 THR 446 425 425 THR THR B . n 
B 1 447 ALA 447 426 426 ALA ALA B . n 
B 1 448 GLU 448 427 427 GLU GLU B . n 
B 1 449 ARG 449 428 428 ARG ARG B . n 
B 1 450 TRP 450 429 429 TRP TRP B . n 
B 1 451 THR 451 430 430 THR THR B . n 
B 1 452 GLY 452 431 431 GLY GLY B . n 
B 1 453 TYR 453 432 432 TYR TYR B . n 
B 1 454 ILE 454 433 433 ILE ILE B . n 
B 1 455 ASP 455 434 434 ASP ASP B . n 
B 1 456 GLY 456 435 435 GLY GLY B . n 
B 1 457 ALA 457 436 436 ALA ALA B . n 
B 1 458 ILE 458 437 437 ILE ILE B . n 
B 1 459 GLU 459 438 438 GLU GLU B . n 
B 1 460 SER 460 439 439 SER SER B . n 
B 1 461 GLY 461 440 440 GLY GLY B . n 
B 1 462 GLN 462 441 441 GLN GLN B . n 
B 1 463 ARG 463 442 442 ARG ARG B . n 
B 1 464 ALA 464 443 443 ALA ALA B . n 
B 1 465 ALA 465 444 444 ALA ALA B . n 
B 1 466 ALA 466 445 445 ALA ALA B . n 
B 1 467 GLU 467 446 446 GLU GLU B . n 
B 1 468 VAL 468 447 447 VAL VAL B . n 
B 1 469 LEU 469 448 448 LEU LEU B . n 
B 1 470 ALA 470 449 449 ALA ALA B . n 
B 1 471 ALA 471 450 450 ALA ALA B . n 
B 1 472 LEU 472 451 451 LEU LEU B . n 
B 1 473 GLY 473 452 452 GLY GLY B . n 
B 1 474 SER 474 453 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 FAD ? ? FAD ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ABN ? ? ABN ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 FAD 1   501 600 FAD FAD A . 
D 3 MG  1   502 603 MG  MG  A . 
E 2 FAD 1   501 600 FAD FAD B . 
F 4 ABN 1   502 606 ABN LIG B . 
G 3 MG  1   503 604 MG  MG  B . 
H 5 HOH 1   601 181 HOH HOH A . 
H 5 HOH 2   602 187 HOH HOH A . 
H 5 HOH 3   603 235 HOH HOH A . 
H 5 HOH 4   604 212 HOH HOH A . 
H 5 HOH 5   605 230 HOH HOH A . 
H 5 HOH 6   606 192 HOH HOH A . 
H 5 HOH 7   607 65  HOH HOH A . 
H 5 HOH 8   608 90  HOH HOH A . 
H 5 HOH 9   609 184 HOH HOH A . 
H 5 HOH 10  610 86  HOH HOH A . 
H 5 HOH 11  611 125 HOH HOH A . 
H 5 HOH 12  612 225 HOH HOH A . 
H 5 HOH 13  613 232 HOH HOH A . 
H 5 HOH 14  614 144 HOH HOH A . 
H 5 HOH 15  615 52  HOH HOH A . 
H 5 HOH 16  616 226 HOH HOH A . 
H 5 HOH 17  617 113 HOH HOH A . 
H 5 HOH 18  618 97  HOH HOH A . 
H 5 HOH 19  619 130 HOH HOH A . 
H 5 HOH 20  620 57  HOH HOH A . 
H 5 HOH 21  621 101 HOH HOH A . 
H 5 HOH 22  622 233 HOH HOH A . 
H 5 HOH 23  623 69  HOH HOH A . 
H 5 HOH 24  624 103 HOH HOH A . 
H 5 HOH 25  625 8   HOH HOH A . 
H 5 HOH 26  626 18  HOH HOH A . 
H 5 HOH 27  627 133 HOH HOH A . 
H 5 HOH 28  628 7   HOH HOH A . 
H 5 HOH 29  629 186 HOH HOH A . 
H 5 HOH 30  630 128 HOH HOH A . 
H 5 HOH 31  631 209 HOH HOH A . 
H 5 HOH 32  632 50  HOH HOH A . 
H 5 HOH 33  633 107 HOH HOH A . 
H 5 HOH 34  634 56  HOH HOH A . 
H 5 HOH 35  635 83  HOH HOH A . 
H 5 HOH 36  636 234 HOH HOH A . 
H 5 HOH 37  637 98  HOH HOH A . 
H 5 HOH 38  638 110 HOH HOH A . 
H 5 HOH 39  639 80  HOH HOH A . 
H 5 HOH 40  640 229 HOH HOH A . 
H 5 HOH 41  641 211 HOH HOH A . 
H 5 HOH 42  642 121 HOH HOH A . 
H 5 HOH 43  643 183 HOH HOH A . 
H 5 HOH 44  644 228 HOH HOH A . 
H 5 HOH 45  645 162 HOH HOH A . 
H 5 HOH 46  646 72  HOH HOH A . 
H 5 HOH 47  647 143 HOH HOH A . 
H 5 HOH 48  648 84  HOH HOH A . 
H 5 HOH 49  649 15  HOH HOH A . 
H 5 HOH 50  650 126 HOH HOH A . 
H 5 HOH 51  651 19  HOH HOH A . 
H 5 HOH 52  652 22  HOH HOH A . 
H 5 HOH 53  653 208 HOH HOH A . 
H 5 HOH 54  654 182 HOH HOH A . 
H 5 HOH 55  655 28  HOH HOH A . 
H 5 HOH 56  656 5   HOH HOH A . 
H 5 HOH 57  657 58  HOH HOH A . 
H 5 HOH 58  658 78  HOH HOH A . 
H 5 HOH 59  659 210 HOH HOH A . 
H 5 HOH 60  660 138 HOH HOH A . 
H 5 HOH 61  661 46  HOH HOH A . 
H 5 HOH 62  662 91  HOH HOH A . 
H 5 HOH 63  663 156 HOH HOH A . 
H 5 HOH 64  664 119 HOH HOH A . 
H 5 HOH 65  665 64  HOH HOH A . 
H 5 HOH 66  666 4   HOH HOH A . 
H 5 HOH 67  667 54  HOH HOH A . 
H 5 HOH 68  668 12  HOH HOH A . 
H 5 HOH 69  669 153 HOH HOH A . 
H 5 HOH 70  670 127 HOH HOH A . 
H 5 HOH 71  671 32  HOH HOH A . 
H 5 HOH 72  672 124 HOH HOH A . 
H 5 HOH 73  673 136 HOH HOH A . 
H 5 HOH 74  674 53  HOH HOH A . 
H 5 HOH 75  675 134 HOH HOH A . 
H 5 HOH 76  676 21  HOH HOH A . 
H 5 HOH 77  677 167 HOH HOH A . 
H 5 HOH 78  678 111 HOH HOH A . 
H 5 HOH 79  679 122 HOH HOH A . 
H 5 HOH 80  680 6   HOH HOH A . 
H 5 HOH 81  681 75  HOH HOH A . 
H 5 HOH 82  682 108 HOH HOH A . 
H 5 HOH 83  683 48  HOH HOH A . 
H 5 HOH 84  684 89  HOH HOH A . 
H 5 HOH 85  685 104 HOH HOH A . 
H 5 HOH 86  686 36  HOH HOH A . 
H 5 HOH 87  687 73  HOH HOH A . 
H 5 HOH 88  688 16  HOH HOH A . 
H 5 HOH 89  689 151 HOH HOH A . 
H 5 HOH 90  690 74  HOH HOH A . 
H 5 HOH 91  691 60  HOH HOH A . 
H 5 HOH 92  692 193 HOH HOH A . 
H 5 HOH 93  693 92  HOH HOH A . 
H 5 HOH 94  694 175 HOH HOH A . 
H 5 HOH 95  695 70  HOH HOH A . 
H 5 HOH 96  696 123 HOH HOH A . 
H 5 HOH 97  697 49  HOH HOH A . 
H 5 HOH 98  698 20  HOH HOH A . 
H 5 HOH 99  699 38  HOH HOH A . 
H 5 HOH 100 700 102 HOH HOH A . 
H 5 HOH 101 701 145 HOH HOH A . 
H 5 HOH 102 702 17  HOH HOH A . 
H 5 HOH 103 703 25  HOH HOH A . 
H 5 HOH 104 704 148 HOH HOH A . 
H 5 HOH 105 705 164 HOH HOH A . 
H 5 HOH 106 706 137 HOH HOH A . 
H 5 HOH 107 707 2   HOH HOH A . 
H 5 HOH 108 708 158 HOH HOH A . 
H 5 HOH 109 709 29  HOH HOH A . 
H 5 HOH 110 710 231 HOH HOH A . 
H 5 HOH 111 711 140 HOH HOH A . 
H 5 HOH 112 712 224 HOH HOH A . 
H 5 HOH 113 713 47  HOH HOH A . 
H 5 HOH 114 714 87  HOH HOH A . 
H 5 HOH 115 715 37  HOH HOH A . 
H 5 HOH 116 716 131 HOH HOH A . 
H 5 HOH 117 717 185 HOH HOH A . 
H 5 HOH 118 718 168 HOH HOH A . 
H 5 HOH 119 719 217 HOH HOH A . 
H 5 HOH 120 720 188 HOH HOH A . 
H 5 HOH 121 721 152 HOH HOH A . 
H 5 HOH 122 722 94  HOH HOH A . 
H 5 HOH 123 723 207 HOH HOH A . 
H 5 HOH 124 724 31  HOH HOH A . 
H 5 HOH 125 725 180 HOH HOH A . 
H 5 HOH 126 726 149 HOH HOH A . 
H 5 HOH 127 727 166 HOH HOH A . 
H 5 HOH 128 728 114 HOH HOH A . 
H 5 HOH 129 729 200 HOH HOH A . 
H 5 HOH 130 730 154 HOH HOH A . 
H 5 HOH 131 731 206 HOH HOH A . 
H 5 HOH 132 732 172 HOH HOH A . 
H 5 HOH 133 733 177 HOH HOH A . 
H 5 HOH 134 734 173 HOH HOH A . 
H 5 HOH 135 735 157 HOH HOH A . 
H 5 HOH 136 736 147 HOH HOH A . 
H 5 HOH 137 737 132 HOH HOH A . 
H 5 HOH 138 738 170 HOH HOH A . 
I 5 HOH 1   601 13  HOH HOH B . 
I 5 HOH 2   602 191 HOH HOH B . 
I 5 HOH 3   603 100 HOH HOH B . 
I 5 HOH 4   604 165 HOH HOH B . 
I 5 HOH 5   605 118 HOH HOH B . 
I 5 HOH 6   606 219 HOH HOH B . 
I 5 HOH 7   607 195 HOH HOH B . 
I 5 HOH 8   608 82  HOH HOH B . 
I 5 HOH 9   609 40  HOH HOH B . 
I 5 HOH 10  610 62  HOH HOH B . 
I 5 HOH 11  611 129 HOH HOH B . 
I 5 HOH 12  612 77  HOH HOH B . 
I 5 HOH 13  613 214 HOH HOH B . 
I 5 HOH 14  614 88  HOH HOH B . 
I 5 HOH 15  615 1   HOH HOH B . 
I 5 HOH 16  616 23  HOH HOH B . 
I 5 HOH 17  617 146 HOH HOH B . 
I 5 HOH 18  618 237 HOH HOH B . 
I 5 HOH 19  619 139 HOH HOH B . 
I 5 HOH 20  620 160 HOH HOH B . 
I 5 HOH 21  621 63  HOH HOH B . 
I 5 HOH 22  622 35  HOH HOH B . 
I 5 HOH 23  623 30  HOH HOH B . 
I 5 HOH 24  624 203 HOH HOH B . 
I 5 HOH 25  625 106 HOH HOH B . 
I 5 HOH 26  626 96  HOH HOH B . 
I 5 HOH 27  627 95  HOH HOH B . 
I 5 HOH 28  628 201 HOH HOH B . 
I 5 HOH 29  629 55  HOH HOH B . 
I 5 HOH 30  630 43  HOH HOH B . 
I 5 HOH 31  631 85  HOH HOH B . 
I 5 HOH 32  632 135 HOH HOH B . 
I 5 HOH 33  633 150 HOH HOH B . 
I 5 HOH 34  634 194 HOH HOH B . 
I 5 HOH 35  635 14  HOH HOH B . 
I 5 HOH 36  636 220 HOH HOH B . 
I 5 HOH 37  637 24  HOH HOH B . 
I 5 HOH 38  638 76  HOH HOH B . 
I 5 HOH 39  639 116 HOH HOH B . 
I 5 HOH 40  640 109 HOH HOH B . 
I 5 HOH 41  641 45  HOH HOH B . 
I 5 HOH 42  642 141 HOH HOH B . 
I 5 HOH 43  643 204 HOH HOH B . 
I 5 HOH 44  644 216 HOH HOH B . 
I 5 HOH 45  645 159 HOH HOH B . 
I 5 HOH 46  646 61  HOH HOH B . 
I 5 HOH 47  647 163 HOH HOH B . 
I 5 HOH 48  648 202 HOH HOH B . 
I 5 HOH 49  649 68  HOH HOH B . 
I 5 HOH 50  650 71  HOH HOH B . 
I 5 HOH 51  651 117 HOH HOH B . 
I 5 HOH 52  652 115 HOH HOH B . 
I 5 HOH 53  653 39  HOH HOH B . 
I 5 HOH 54  654 10  HOH HOH B . 
I 5 HOH 55  655 81  HOH HOH B . 
I 5 HOH 56  656 161 HOH HOH B . 
I 5 HOH 57  657 99  HOH HOH B . 
I 5 HOH 58  658 59  HOH HOH B . 
I 5 HOH 59  659 93  HOH HOH B . 
I 5 HOH 60  660 34  HOH HOH B . 
I 5 HOH 61  661 11  HOH HOH B . 
I 5 HOH 62  662 3   HOH HOH B . 
I 5 HOH 63  663 44  HOH HOH B . 
I 5 HOH 64  664 112 HOH HOH B . 
I 5 HOH 65  665 218 HOH HOH B . 
I 5 HOH 66  666 236 HOH HOH B . 
I 5 HOH 67  667 221 HOH HOH B . 
I 5 HOH 68  668 51  HOH HOH B . 
I 5 HOH 69  669 120 HOH HOH B . 
I 5 HOH 70  670 66  HOH HOH B . 
I 5 HOH 71  671 105 HOH HOH B . 
I 5 HOH 72  672 227 HOH HOH B . 
I 5 HOH 73  673 79  HOH HOH B . 
I 5 HOH 74  674 178 HOH HOH B . 
I 5 HOH 75  675 155 HOH HOH B . 
I 5 HOH 76  676 67  HOH HOH B . 
I 5 HOH 77  677 41  HOH HOH B . 
I 5 HOH 78  678 33  HOH HOH B . 
I 5 HOH 79  679 27  HOH HOH B . 
I 5 HOH 80  680 189 HOH HOH B . 
I 5 HOH 81  681 42  HOH HOH B . 
I 5 HOH 82  682 197 HOH HOH B . 
I 5 HOH 83  683 9   HOH HOH B . 
I 5 HOH 84  684 213 HOH HOH B . 
I 5 HOH 85  685 199 HOH HOH B . 
I 5 HOH 86  686 26  HOH HOH B . 
I 5 HOH 87  687 222 HOH HOH B . 
I 5 HOH 88  688 174 HOH HOH B . 
I 5 HOH 89  689 169 HOH HOH B . 
I 5 HOH 90  690 171 HOH HOH B . 
I 5 HOH 91  691 205 HOH HOH B . 
I 5 HOH 92  692 179 HOH HOH B . 
I 5 HOH 93  693 198 HOH HOH B . 
I 5 HOH 94  694 196 HOH HOH B . 
I 5 HOH 95  695 215 HOH HOH B . 
I 5 HOH 96  696 223 HOH HOH B . 
I 5 HOH 97  697 142 HOH HOH B . 
I 5 HOH 98  698 190 HOH HOH B . 
I 5 HOH 99  699 176 HOH HOH B . 
# 
_software.citation_id            ? 
_software.classification         refinement 
_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                   REFMAC 
_software.os                     ? 
_software.os_version             ? 
_software.type                   ? 
_software.version                5.8.0267 
_software.pdbx_ordinal           1 
# 
_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                     9H5Z 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     69.473 
_cell.length_a_esd                 ? 
_cell.length_b                     100.242 
_cell.length_b_esd                 ? 
_cell.length_c                     120.901 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9H5Z 
_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                   9H5Z 
_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             2.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.46 
_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    '30% PEG4000, 100 mM TRIS/HCl buffer pH 8.5, 200 mM MgCl2' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER R 1M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-29 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.873128 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID23-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.873128 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-2 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H5Z 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.14 
_reflns.d_resolution_low                               77.17 
_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                                     43665 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.2 
_reflns_shell.d_res_low                                     2.257 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3723 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.813 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -2.93 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            4.56 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.63 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               38.629 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.932 
_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                                 9H5Z 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.20 
_refine.ls_d_res_low                             77.17 
_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                     41489 
_refine.ls_number_reflns_R_free                  2051 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.84 
_refine.ls_percent_reflns_R_free                 4.7 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18151 
_refine.ls_R_factor_R_free                       0.23956 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17871 
_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                       0.292 
_refine.pdbx_overall_ESU_R_Free                  0.221 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             7.952 
_refine.overall_SU_ML                            0.187 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        77.17 
_refine_hist.number_atoms_solvent             237 
_refine_hist.number_atoms_total               7053 
_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        6700 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         116 
_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' ? 0.009  0.013  7006  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  6463  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.637  1.669  9612  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.802  1.588  14804 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.728  5.000  896   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 27.755 20.317 378   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.479 15.000 953   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.838 15.000 71    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.068  0.200  885   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  8080  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1612  ? 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' ? 2.952  3.948  3587  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.949  3.946  3585  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.153  5.915  4482  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.151  5.915  4482  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.545  4.275  3419  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.545  4.275  3420  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.333  6.268  5131  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.672  45.634 7404  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.673  45.610 7386  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.200 
_refine_ls_shell.d_res_low                        2.257 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             136 
_refine_ls_shell.number_reflns_R_work             3053 
_refine_ls_shell.percent_reflns_obs               99.97 
_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                  0.319 
_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                  0.360 
# 
_struct.entry_id                     9H5Z 
_struct.title                        
'Crystal structure of Thermoanaerobacterales bacterium monoamine oxidase in complex with benzylamine' 
_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        9H5Z 
_struct_keywords.text            'monoamine oxidase, Thermoanaerobacterales bacterium, enzyme, benzylamine, FLAVOPROTEIN' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 3 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0AAJ6N6J2_9FIRM 
_struct_ref.pdbx_db_accession          A0AAJ6N6J2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPSEQVDVVVVGAGFAGLTAARAVHEAGRSVLVLEARDRVGGRTCTEEHHGTWIDLGGQWIGPGQDRVAALAAELGVETY
PQPTEGDDVVLFGDGEPQRAPDVALAFSDEELTAYLELAGALEAIAEKVPLDAPWLAPEAAAWDATTLREWVAGTGVPDR
VAGLFEVAVQAVFAATSAQLSLLHAAHYVHSAGGWSKLTDTEGGAQQDRLVGGVQPLAERLAARLPDGALRLSTPVRGLA
QDGDGVTVRTAGGEVRARRAIVAVPPTLAGRIDHDPPLPPQRDQLLQHMPQGSVVKFHVIYDEPWWRAEGLSGTVLCPDE
PIGVTFDGTPPAGTPGIVTGFFEGPAAVAAGARTREERRDVVVDVLARTLGERARDVRDYIDRDWSAEPWTRGCYGAHLP
PGAWTVYGPALRVPVGRVHWAGTETAERWTGYIDGAIESGQRAAAEVLAALGS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9H5Z A 22 ? 474 ? A0AAJ6N6J2 1 ? 453 ? 1 453 
2 1 9H5Z B 22 ? 474 ? A0AAJ6N6J2 1 ? 453 ? 1 453 
# 
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 9H5Z MET A 1  ? UNP A0AAJ6N6J2 ? ? 'initiating methionine' -20 1  
1 9H5Z GLY A 2  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -19 2  
1 9H5Z SER A 3  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -18 3  
1 9H5Z SER A 4  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -17 4  
1 9H5Z HIS A 5  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -16 5  
1 9H5Z HIS A 6  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -15 6  
1 9H5Z HIS A 7  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -14 7  
1 9H5Z HIS A 8  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -13 8  
1 9H5Z HIS A 9  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -12 9  
1 9H5Z HIS A 10 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -11 10 
1 9H5Z GLY A 11 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -10 11 
1 9H5Z SER A 12 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -9  12 
1 9H5Z GLY A 13 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -8  13 
1 9H5Z LEU A 14 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -7  14 
1 9H5Z VAL A 15 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -6  15 
1 9H5Z PRO A 16 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -5  16 
1 9H5Z ARG A 17 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -4  17 
1 9H5Z GLY A 18 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -3  18 
1 9H5Z SER A 19 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -2  19 
1 9H5Z ALA A 20 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -1  20 
1 9H5Z GLY A 21 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        0   21 
2 9H5Z MET B 1  ? UNP A0AAJ6N6J2 ? ? 'initiating methionine' -20 22 
2 9H5Z GLY B 2  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -19 23 
2 9H5Z SER B 3  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -18 24 
2 9H5Z SER B 4  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -17 25 
2 9H5Z HIS B 5  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -16 26 
2 9H5Z HIS B 6  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -15 27 
2 9H5Z HIS B 7  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -14 28 
2 9H5Z HIS B 8  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -13 29 
2 9H5Z HIS B 9  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -12 30 
2 9H5Z HIS B 10 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -11 31 
2 9H5Z GLY B 11 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -10 32 
2 9H5Z SER B 12 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -9  33 
2 9H5Z GLY B 13 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -8  34 
2 9H5Z LEU B 14 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -7  35 
2 9H5Z VAL B 15 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -6  36 
2 9H5Z PRO B 16 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -5  37 
2 9H5Z ARG B 17 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -4  38 
2 9H5Z GLY B 18 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -3  39 
2 9H5Z SER B 19 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -2  40 
2 9H5Z ALA B 20 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -1  41 
2 9H5Z GLY B 21 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        0   42 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6750  ? 
1 MORE         -37   ? 
1 'SSA (A^2)'  30360 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_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 35  ? ALA A 48  ? GLY A 14  ALA A 27  1 ? 14 
HELX_P HELX_P2  AA2 GLN A 86  ? LEU A 96  ? GLN A 65  LEU A 75  1 ? 11 
HELX_P HELX_P3  AA3 ASP A 123 ? PHE A 128 ? ASP A 102 PHE A 107 5 ? 6  
HELX_P HELX_P4  AA4 SER A 129 ? GLU A 148 ? SER A 108 GLU A 127 1 ? 20 
HELX_P HELX_P5  AA5 ALA A 154 ? ALA A 158 ? ALA A 133 ALA A 137 5 ? 5  
HELX_P HELX_P6  AA6 GLU A 160 ? ASP A 165 ? GLU A 139 ASP A 144 1 ? 6  
HELX_P HELX_P7  AA7 THR A 168 ? GLY A 177 ? THR A 147 GLY A 156 1 ? 10 
HELX_P HELX_P8  AA8 PRO A 179 ? ALA A 195 ? PRO A 158 ALA A 174 1 ? 17 
HELX_P HELX_P9  AA9 SER A 202 ? GLY A 214 ? SER A 181 GLY A 193 1 ? 13 
HELX_P HELX_P10 AB1 GLY A 215 ? ASP A 221 ? GLY A 194 ASP A 200 1 ? 7  
HELX_P HELX_P11 AB2 VAL A 235 ? ALA A 244 ? VAL A 214 ALA A 223 1 ? 10 
HELX_P HELX_P12 AB3 PRO A 286 ? GLY A 291 ? PRO A 265 GLY A 270 1 ? 6  
HELX_P HELX_P13 AB4 PRO A 300 ? HIS A 309 ? PRO A 279 HIS A 288 1 ? 10 
HELX_P HELX_P14 AB5 TRP A 327 ? GLU A 330 ? TRP A 306 GLU A 309 5 ? 4  
HELX_P HELX_P15 AB6 GLY A 365 ? ALA A 373 ? GLY A 344 ALA A 352 1 ? 9  
HELX_P HELX_P16 AB7 THR A 375 ? LEU A 391 ? THR A 354 LEU A 370 1 ? 17 
HELX_P HELX_P17 AB8 GLY A 392 ? ASP A 397 ? GLY A 371 ASP A 376 5 ? 6  
HELX_P HELX_P18 AB9 TYR A 428 ? LEU A 432 ? TYR A 407 LEU A 411 5 ? 5  
HELX_P HELX_P19 AC1 GLY A 443 ? ALA A 447 ? GLY A 422 ALA A 426 5 ? 5  
HELX_P HELX_P20 AC2 TYR A 453 ? GLY A 473 ? TYR A 432 GLY A 452 1 ? 21 
HELX_P HELX_P21 AC3 GLY B 35  ? ALA B 48  ? GLY B 14  ALA B 27  1 ? 14 
HELX_P HELX_P22 AC4 GLN B 86  ? LEU B 96  ? GLN B 65  LEU B 75  1 ? 11 
HELX_P HELX_P23 AC5 ASP B 123 ? PHE B 128 ? ASP B 102 PHE B 107 5 ? 6  
HELX_P HELX_P24 AC6 SER B 129 ? LYS B 149 ? SER B 108 LYS B 128 1 ? 21 
HELX_P HELX_P25 AC7 ALA B 154 ? ALA B 158 ? ALA B 133 ALA B 137 5 ? 5  
HELX_P HELX_P26 AC8 GLU B 160 ? ALA B 166 ? GLU B 139 ALA B 145 1 ? 7  
HELX_P HELX_P27 AC9 THR B 168 ? THR B 176 ? THR B 147 THR B 155 1 ? 9  
HELX_P HELX_P28 AD1 PRO B 179 ? ALA B 195 ? PRO B 158 ALA B 174 1 ? 17 
HELX_P HELX_P29 AD2 SER B 202 ? GLY B 214 ? SER B 181 GLY B 193 1 ? 13 
HELX_P HELX_P30 AD3 GLY B 215 ? ASP B 221 ? GLY B 194 ASP B 200 1 ? 7  
HELX_P HELX_P31 AD4 GLY B 234 ? ARG B 245 ? GLY B 213 ARG B 224 1 ? 12 
HELX_P HELX_P32 AD5 PRO B 286 ? GLY B 291 ? PRO B 265 GLY B 270 1 ? 6  
HELX_P HELX_P33 AD6 PRO B 300 ? HIS B 309 ? PRO B 279 HIS B 288 1 ? 10 
HELX_P HELX_P34 AD7 PRO B 325 ? GLU B 330 ? PRO B 304 GLU B 309 5 ? 6  
HELX_P HELX_P35 AD8 GLY B 365 ? ALA B 373 ? GLY B 344 ALA B 352 1 ? 9  
HELX_P HELX_P36 AD9 THR B 375 ? LEU B 391 ? THR B 354 LEU B 370 1 ? 17 
HELX_P HELX_P37 AE1 GLY B 392 ? ASP B 397 ? GLY B 371 ASP B 376 5 ? 6  
HELX_P HELX_P38 AE2 GLY B 423 ? TYR B 428 ? GLY B 402 TYR B 407 1 ? 6  
HELX_P HELX_P39 AE3 GLY B 429 ? LEU B 432 ? GLY B 408 LEU B 411 5 ? 4  
HELX_P HELX_P40 AE4 GLY B 443 ? ALA B 447 ? GLY B 422 ALA B 426 5 ? 5  
HELX_P HELX_P41 AE5 TYR B 453 ? GLY B 473 ? TYR B 432 GLY B 452 1 ? 21 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale none ? A CYS 415 SG ? ? ? 1_555 C FAD . C8M ? ? A CYS 394 A FAD 501 1_555 ? ? ? ? ? ? ? 1.650 ? ? 
covale2  covale none ? B CYS 415 SG ? ? ? 1_555 E FAD . C8M ? ? B CYS 394 B FAD 501 1_555 ? ? ? ? ? ? ? 1.676 ? ? 
metalc1  metalc ?    ? A THR 105 O  ? ? ? 1_555 D MG  . MG  ? ? A THR 84  A MG  502 1_555 ? ? ? ? ? ? ? 2.482 ? ? 
metalc2  metalc ?    ? D MG  .   MG ? ? ? 1_555 H HOH . O   ? ? A MG  502 A HOH 603 1_555 ? ? ? ? ? ? ? 2.140 ? ? 
metalc3  metalc ?    ? D MG  .   MG ? ? ? 1_555 H HOH . O   ? ? A MG  502 A HOH 613 1_555 ? ? ? ? ? ? ? 1.985 ? ? 
metalc4  metalc ?    ? D MG  .   MG ? ? ? 1_555 H HOH . O   ? ? A MG  502 A HOH 622 1_555 ? ? ? ? ? ? ? 2.421 ? ? 
metalc5  metalc ?    ? D MG  .   MG ? ? ? 1_555 H HOH . O   ? ? A MG  502 A HOH 636 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc6  metalc ?    ? B THR 105 O  ? ? ? 1_555 G MG  . MG  ? ? B THR 84  B MG  503 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
metalc7  metalc ?    ? G MG  .   MG ? ? ? 1_555 I HOH . O   ? ? B MG  503 B HOH 606 1_555 ? ? ? ? ? ? ? 1.882 ? ? 
metalc8  metalc ?    ? G MG  .   MG ? ? ? 1_555 I HOH . O   ? ? B MG  503 B HOH 618 1_555 ? ? ? ? ? ? ? 1.929 ? ? 
metalc9  metalc ?    ? G MG  .   MG ? ? ? 1_555 I HOH . O   ? ? B MG  503 B HOH 636 1_555 ? ? ? ? ? ? ? 2.158 ? ? 
metalc10 metalc ?    ? G MG  .   MG ? ? ? 1_555 I HOH . O   ? ? B MG  503 B HOH 666 1_555 ? ? ? ? ? ? ? 2.201 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O ? A THR 105 ? A THR 84  ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? H HOH . ? A HOH 603 ? 1_555 80.6  ? 
2  O ? A THR 105 ? A THR 84  ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? H HOH . ? A HOH 613 ? 1_555 77.2  ? 
3  O ? H HOH .   ? A HOH 603 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? H HOH . ? A HOH 613 ? 1_555 152.2 ? 
4  O ? A THR 105 ? A THR 84  ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? H HOH . ? A HOH 622 ? 1_555 90.8  ? 
5  O ? H HOH .   ? A HOH 603 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? H HOH . ? A HOH 622 ? 1_555 79.9  ? 
6  O ? H HOH .   ? A HOH 613 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? H HOH . ? A HOH 622 ? 1_555 83.9  ? 
7  O ? A THR 105 ? A THR 84  ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? H HOH . ? A HOH 636 ? 1_555 173.7 ? 
8  O ? H HOH .   ? A HOH 603 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? H HOH . ? A HOH 636 ? 1_555 94.7  ? 
9  O ? H HOH .   ? A HOH 613 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? H HOH . ? A HOH 636 ? 1_555 108.6 ? 
10 O ? H HOH .   ? A HOH 622 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? H HOH . ? A HOH 636 ? 1_555 92.5  ? 
11 O ? B THR 105 ? B THR 84  ? 1_555 MG ? G MG . ? B MG 503 ? 1_555 O ? I HOH . ? B HOH 606 ? 1_555 79.9  ? 
12 O ? B THR 105 ? B THR 84  ? 1_555 MG ? G MG . ? B MG 503 ? 1_555 O ? I HOH . ? B HOH 618 ? 1_555 92.6  ? 
13 O ? I HOH .   ? B HOH 606 ? 1_555 MG ? G MG . ? B MG 503 ? 1_555 O ? I HOH . ? B HOH 618 ? 1_555 98.7  ? 
14 O ? B THR 105 ? B THR 84  ? 1_555 MG ? G MG . ? B MG 503 ? 1_555 O ? I HOH . ? B HOH 636 ? 1_555 89.2  ? 
15 O ? I HOH .   ? B HOH 606 ? 1_555 MG ? G MG . ? B MG 503 ? 1_555 O ? I HOH . ? B HOH 636 ? 1_555 163.1 ? 
16 O ? I HOH .   ? B HOH 618 ? 1_555 MG ? G MG . ? B MG 503 ? 1_555 O ? I HOH . ? B HOH 636 ? 1_555 94.6  ? 
17 O ? B THR 105 ? B THR 84  ? 1_555 MG ? G MG . ? B MG 503 ? 1_555 O ? I HOH . ? B HOH 666 ? 1_555 85.6  ? 
18 O ? I HOH .   ? B HOH 606 ? 1_555 MG ? G MG . ? B MG 503 ? 1_555 O ? I HOH . ? B HOH 666 ? 1_555 85.0  ? 
19 O ? I HOH .   ? B HOH 618 ? 1_555 MG ? G MG . ? B MG 503 ? 1_555 O ? I HOH . ? B HOH 666 ? 1_555 175.6 ? 
20 O ? I HOH .   ? B HOH 636 ? 1_555 MG ? G MG . ? B MG 503 ? 1_555 O ? I HOH . ? B HOH 666 ? 1_555 81.4  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 FAD C . ? CYS A 415 ? FAD A 501 ? 1_555 CYS A 394 ? 1_555 C8M SG CYS 3 FAD None Flavin 
2 FAD E . ? CYS B 415 ? FAD B 501 ? 1_555 CYS B 394 ? 1_555 C8M SG CYS 3 FAD None Flavin 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASP 296 A . ? ASP 275 A PRO 297 A ? PRO 276 A 1 -5.61 
2 THR 355 A . ? THR 334 A PRO 356 A ? PRO 335 A 1 -2.38 
3 CYS 415 A . ? CYS 394 A TYR 416 A ? TYR 395 A 1 0.52  
4 ASP 296 B . ? ASP 275 B PRO 297 B ? PRO 276 B 1 -6.12 
5 THR 355 B . ? THR 334 B PRO 356 B ? PRO 335 B 1 -8.48 
6 CYS 415 B . ? CYS 394 B TYR 416 B ? TYR 395 B 1 -3.27 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 3 ? 
AA6 ? 4 ? 
AA7 ? 7 ? 
AA8 ? 5 ? 
AA9 ? 2 ? 
AB1 ? 3 ? 
AB2 ? 3 ? 
AB3 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA7 6 7 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? parallel      
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 251 ? ARG A 252 ? LEU A 230 ARG A 231 
AA1 2 VAL A 52  ? LEU A 55  ? VAL A 31  LEU A 34  
AA1 3 VAL A 27  ? VAL A 32  ? VAL A 6   VAL A 11  
AA1 4 GLU A 275 ? VAL A 283 ? GLU A 254 VAL A 262 
AA1 5 VAL A 267 ? ARG A 270 ? VAL A 246 ARG A 249 
AA1 6 GLY A 259 ? GLN A 262 ? GLY A 238 GLN A 241 
AA1 7 ASP A 294 ? ASP A 296 ? ASP A 273 ASP A 275 
AA2 1 LEU A 251 ? ARG A 252 ? LEU A 230 ARG A 231 
AA2 2 VAL A 52  ? LEU A 55  ? VAL A 31  LEU A 34  
AA2 3 VAL A 27  ? VAL A 32  ? VAL A 6   VAL A 11  
AA2 4 GLU A 275 ? VAL A 283 ? GLU A 254 VAL A 262 
AA2 5 VAL A 439 ? TRP A 441 ? VAL A 418 TRP A 420 
AA3 1 THR A 67  ? HIS A 70  ? THR A 46  HIS A 49  
AA3 2 THR A 73  ? ASP A 76  ? THR A 52  ASP A 55  
AA4 1 TRP A 81  ? ILE A 82  ? TRP A 60  ILE A 61  
AA4 2 ASP A 229 ? LEU A 231 ? ASP A 208 LEU A 210 
AA4 3 THR A 100 ? PRO A 102 ? THR A 79  PRO A 81  
AA5 1 GLN A 119 ? ALA A 121 ? GLN A 98  ALA A 100 
AA5 2 ASP A 108 ? VAL A 111 ? ASP A 87  VAL A 90  
AA5 3 LEU A 332 ? LEU A 337 ? LEU A 311 LEU A 316 
AA6 1 PHE A 347 ? ASP A 348 ? PHE A 326 ASP A 327 
AA6 2 GLY A 357 ? GLU A 364 ? GLY A 336 GLU A 343 
AA6 3 VAL A 315 ? TYR A 322 ? VAL A 294 TYR A 301 
AA6 4 ASP A 400 ? ASP A 405 ? ASP A 379 ASP A 384 
AA7 1 LEU B 251 ? ARG B 252 ? LEU B 230 ARG B 231 
AA7 2 VAL B 52  ? LEU B 55  ? VAL B 31  LEU B 34  
AA7 3 VAL B 27  ? VAL B 32  ? VAL B 6   VAL B 11  
AA7 4 GLU B 275 ? VAL B 283 ? GLU B 254 VAL B 262 
AA7 5 GLY B 266 ? ARG B 270 ? GLY B 245 ARG B 249 
AA7 6 GLY B 259 ? ASP B 263 ? GLY B 238 ASP B 242 
AA7 7 ASP B 294 ? ASP B 296 ? ASP B 273 ASP B 275 
AA8 1 LEU B 251 ? ARG B 252 ? LEU B 230 ARG B 231 
AA8 2 VAL B 52  ? LEU B 55  ? VAL B 31  LEU B 34  
AA8 3 VAL B 27  ? VAL B 32  ? VAL B 6   VAL B 11  
AA8 4 GLU B 275 ? VAL B 283 ? GLU B 254 VAL B 262 
AA8 5 VAL B 439 ? TRP B 441 ? VAL B 418 TRP B 420 
AA9 1 THR B 67  ? HIS B 70  ? THR B 46  HIS B 49  
AA9 2 THR B 73  ? ASP B 76  ? THR B 52  ASP B 55  
AB1 1 TRP B 81  ? ILE B 82  ? TRP B 60  ILE B 61  
AB1 2 ASP B 229 ? LEU B 231 ? ASP B 208 LEU B 210 
AB1 3 THR B 100 ? PRO B 102 ? THR B 79  PRO B 81  
AB2 1 GLN B 119 ? ALA B 121 ? GLN B 98  ALA B 100 
AB2 2 ASP B 108 ? VAL B 111 ? ASP B 87  VAL B 90  
AB2 3 LEU B 332 ? LEU B 337 ? LEU B 311 LEU B 316 
AB3 1 ILE B 343 ? ASP B 348 ? ILE B 322 ASP B 327 
AB3 2 GLY B 357 ? GLU B 364 ? GLY B 336 GLU B 343 
AB3 3 VAL B 315 ? TYR B 322 ? VAL B 294 TYR B 301 
AB3 4 ASP B 400 ? ASP B 405 ? ASP B 379 ASP B 384 
# 
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 ARG A 252 ? O ARG A 231 N VAL A 54  ? N VAL A 33  
AA1 2 3 O LEU A 53  ? O LEU A 32  N VAL A 31  ? N VAL A 10  
AA1 3 4 N VAL A 32  ? N VAL A 11  O ILE A 282 ? O ILE A 261 
AA1 4 5 O ALA A 278 ? O ALA A 257 N VAL A 267 ? N VAL A 246 
AA1 5 6 O THR A 268 ? O THR A 247 N ALA A 261 ? N ALA A 240 
AA1 6 7 N LEU A 260 ? N LEU A 239 O ASP A 294 ? O ASP A 273 
AA2 1 2 O ARG A 252 ? O ARG A 231 N VAL A 54  ? N VAL A 33  
AA2 2 3 O LEU A 53  ? O LEU A 32  N VAL A 31  ? N VAL A 10  
AA2 3 4 N VAL A 32  ? N VAL A 11  O ILE A 282 ? O ILE A 261 
AA2 4 5 N ALA A 281 ? N ALA A 260 O HIS A 440 ? O HIS A 419 
AA3 1 2 N GLU A 68  ? N GLU A 47  O ILE A 75  ? O ILE A 54  
AA4 1 2 N ILE A 82  ? N ILE A 61  O ASP A 229 ? O ASP A 208 
AA4 2 3 O ARG A 230 ? O ARG A 209 N TYR A 101 ? N TYR A 80  
AA5 1 2 O GLN A 119 ? O GLN A 98  N VAL A 111 ? N VAL A 90  
AA5 2 3 N ASP A 108 ? N ASP A 87  O SER A 333 ? O SER A 312 
AA6 1 2 N PHE A 347 ? N PHE A 326 O THR A 360 ? O THR A 339 
AA6 2 3 O GLY A 357 ? O GLY A 336 N TYR A 322 ? N TYR A 301 
AA6 3 4 N HIS A 319 ? N HIS A 298 O ILE A 402 ? O ILE A 381 
AA7 1 2 O ARG B 252 ? O ARG B 231 N VAL B 54  ? N VAL B 33  
AA7 2 3 O LEU B 53  ? O LEU B 32  N VAL B 31  ? N VAL B 10  
AA7 3 4 N VAL B 32  ? N VAL B 11  O ILE B 282 ? O ILE B 261 
AA7 4 5 O VAL B 276 ? O VAL B 255 N VAL B 269 ? N VAL B 248 
AA7 5 6 O THR B 268 ? O THR B 247 N ALA B 261 ? N ALA B 240 
AA7 6 7 N LEU B 260 ? N LEU B 239 O ASP B 294 ? O ASP B 273 
AA8 1 2 O ARG B 252 ? O ARG B 231 N VAL B 54  ? N VAL B 33  
AA8 2 3 O LEU B 53  ? O LEU B 32  N VAL B 31  ? N VAL B 10  
AA8 3 4 N VAL B 32  ? N VAL B 11  O ILE B 282 ? O ILE B 261 
AA8 4 5 N VAL B 283 ? N VAL B 262 O HIS B 440 ? O HIS B 419 
AA9 1 2 N GLU B 68  ? N GLU B 47  O ILE B 75  ? O ILE B 54  
AB1 1 2 N ILE B 82  ? N ILE B 61  O ASP B 229 ? O ASP B 208 
AB1 2 3 O ARG B 230 ? O ARG B 209 N TYR B 101 ? N TYR B 80  
AB2 1 2 O GLN B 119 ? O GLN B 98  N VAL B 111 ? N VAL B 90  
AB2 2 3 N ASP B 108 ? N ASP B 87  O SER B 333 ? O SER B 312 
AB3 1 2 N PHE B 347 ? N PHE B 326 O THR B 360 ? O THR B 339 
AB3 2 3 O GLY B 357 ? O GLY B 336 N TYR B 322 ? N TYR B 301 
AB3 3 4 N ILE B 321 ? N ILE B 300 O ASP B 400 ? O ASP B 379 
# 
_pdbx_entry_details.entry_id                   9H5Z 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 MG  B MG  503 ? ? O B HOH 667 ? ? 1.68 
2 1 OE1 B GLU 127 ? ? O B HOH 601 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 VAL A 103 ? ? -16.11  -57.58  
2  1 SER A 108 ? ? -49.71  164.84  
3  1 ALA A 133 ? ? -153.85 67.86   
4  1 GLU A 139 ? ? -102.36 43.37   
5  1 VAL A 157 ? ? -35.12  158.42  
6  1 ALA A 175 ? ? -176.31 144.79  
7  1 THR A 201 ? ? -83.99  -89.54  
8  1 THR A 391 ? ? -133.88 -63.78  
9  1 ARG A 392 ? ? 72.98   39.28   
10 1 ALA B 13  ? ? -102.52 45.30   
11 1 ASP B 38  ? ? -77.35  21.21   
12 1 GLN B 59  ? ? -145.13 -27.10  
13 1 ALA B 133 ? ? -161.89 67.15   
14 1 THR B 201 ? ? -77.52  -84.64  
15 1 THR B 250 ? ? -116.47 -167.73 
16 1 THR B 369 ? ? -121.70 -54.15  
17 1 THR B 391 ? ? -135.06 -54.37  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -20 ? A MET 1   
2  1 Y 1 A GLY -19 ? A GLY 2   
3  1 Y 1 A SER -18 ? A SER 3   
4  1 Y 1 A SER -17 ? A SER 4   
5  1 Y 1 A HIS -16 ? A HIS 5   
6  1 Y 1 A HIS -15 ? A HIS 6   
7  1 Y 1 A HIS -14 ? A HIS 7   
8  1 Y 1 A HIS -13 ? A HIS 8   
9  1 Y 1 A HIS -12 ? A HIS 9   
10 1 Y 1 A HIS -11 ? A HIS 10  
11 1 Y 1 A GLY -10 ? A GLY 11  
12 1 Y 1 A SER -9  ? A SER 12  
13 1 Y 1 A GLY -8  ? A GLY 13  
14 1 Y 1 A LEU -7  ? A LEU 14  
15 1 Y 1 A VAL -6  ? A VAL 15  
16 1 Y 1 A PRO -5  ? A PRO 16  
17 1 Y 1 A ARG -4  ? A ARG 17  
18 1 Y 1 A GLY -3  ? A GLY 18  
19 1 Y 1 A SER -2  ? A SER 19  
20 1 Y 1 A ALA -1  ? A ALA 20  
21 1 Y 1 A GLY 0   ? A GLY 21  
22 1 Y 1 A MET 1   ? A MET 22  
23 1 Y 1 A PRO 2   ? A PRO 23  
24 1 Y 1 A SER 3   ? A SER 24  
25 1 Y 1 A GLU 4   ? A GLU 25  
26 1 Y 1 A SER 453 ? A SER 474 
27 1 Y 1 B MET -20 ? B MET 1   
28 1 Y 1 B GLY -19 ? B GLY 2   
29 1 Y 1 B SER -18 ? B SER 3   
30 1 Y 1 B SER -17 ? B SER 4   
31 1 Y 1 B HIS -16 ? B HIS 5   
32 1 Y 1 B HIS -15 ? B HIS 6   
33 1 Y 1 B HIS -14 ? B HIS 7   
34 1 Y 1 B HIS -13 ? B HIS 8   
35 1 Y 1 B HIS -12 ? B HIS 9   
36 1 Y 1 B HIS -11 ? B HIS 10  
37 1 Y 1 B GLY -10 ? B GLY 11  
38 1 Y 1 B SER -9  ? B SER 12  
39 1 Y 1 B GLY -8  ? B GLY 13  
40 1 Y 1 B LEU -7  ? B LEU 14  
41 1 Y 1 B VAL -6  ? B VAL 15  
42 1 Y 1 B PRO -5  ? B PRO 16  
43 1 Y 1 B ARG -4  ? B ARG 17  
44 1 Y 1 B GLY -3  ? B GLY 18  
45 1 Y 1 B SER -2  ? B SER 19  
46 1 Y 1 B ALA -1  ? B ALA 20  
47 1 Y 1 B GLY 0   ? B GLY 21  
48 1 Y 1 B MET 1   ? B MET 22  
49 1 Y 1 B PRO 2   ? B PRO 23  
50 1 Y 1 B SER 3   ? B SER 24  
51 1 Y 1 B GLU 4   ? B GLU 25  
52 1 Y 1 B SER 453 ? B SER 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 
ABN N      N  N N 1   
ABN C      C  N N 2   
ABN C1     C  Y N 3   
ABN C2     C  Y N 4   
ABN C3     C  Y N 5   
ABN C4     C  Y N 6   
ABN C5     C  Y N 7   
ABN C6     C  Y N 8   
ABN HN1    H  N N 9   
ABN HN2    H  N N 10  
ABN H1     H  N N 11  
ABN H2A    H  N N 12  
ABN H2     H  N N 13  
ABN H3     H  N N 14  
ABN H4     H  N N 15  
ABN H5     H  N N 16  
ABN H6     H  N N 17  
ALA N      N  N N 18  
ALA CA     C  N S 19  
ALA C      C  N N 20  
ALA O      O  N N 21  
ALA CB     C  N N 22  
ALA OXT    O  N N 23  
ALA H      H  N N 24  
ALA H2     H  N N 25  
ALA HA     H  N N 26  
ALA HB1    H  N N 27  
ALA HB2    H  N N 28  
ALA HB3    H  N N 29  
ALA HXT    H  N N 30  
ARG N      N  N N 31  
ARG CA     C  N S 32  
ARG C      C  N N 33  
ARG O      O  N N 34  
ARG CB     C  N N 35  
ARG CG     C  N N 36  
ARG CD     C  N N 37  
ARG NE     N  N N 38  
ARG CZ     C  N N 39  
ARG NH1    N  N N 40  
ARG NH2    N  N N 41  
ARG OXT    O  N N 42  
ARG H      H  N N 43  
ARG H2     H  N N 44  
ARG HA     H  N N 45  
ARG HB2    H  N N 46  
ARG HB3    H  N N 47  
ARG HG2    H  N N 48  
ARG HG3    H  N N 49  
ARG HD2    H  N N 50  
ARG HD3    H  N N 51  
ARG HE     H  N N 52  
ARG HH11   H  N N 53  
ARG HH12   H  N N 54  
ARG HH21   H  N N 55  
ARG HH22   H  N N 56  
ARG HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
FAD PA     P  N R 88  
FAD O1A    O  N N 89  
FAD O2A    O  N N 90  
FAD O5B    O  N N 91  
FAD C5B    C  N N 92  
FAD C4B    C  N R 93  
FAD O4B    O  N N 94  
FAD C3B    C  N S 95  
FAD O3B    O  N N 96  
FAD C2B    C  N R 97  
FAD O2B    O  N N 98  
FAD C1B    C  N R 99  
FAD N9A    N  Y N 100 
FAD C8A    C  Y N 101 
FAD N7A    N  Y N 102 
FAD C5A    C  Y N 103 
FAD C6A    C  Y N 104 
FAD N6A    N  N N 105 
FAD N1A    N  Y N 106 
FAD C2A    C  Y N 107 
FAD N3A    N  Y N 108 
FAD C4A    C  Y N 109 
FAD N1     N  N N 110 
FAD C2     C  N N 111 
FAD O2     O  N N 112 
FAD N3     N  N N 113 
FAD C4     C  N N 114 
FAD O4     O  N N 115 
FAD C4X    C  N N 116 
FAD N5     N  N N 117 
FAD C5X    C  Y N 118 
FAD C6     C  Y N 119 
FAD C7     C  Y N 120 
FAD C7M    C  N N 121 
FAD C8     C  Y N 122 
FAD C8M    C  N N 123 
FAD C9     C  Y N 124 
FAD C9A    C  Y N 125 
FAD N10    N  N N 126 
FAD C10    C  N N 127 
FAD "C1'"  C  N N 128 
FAD "C2'"  C  N S 129 
FAD "O2'"  O  N N 130 
FAD "C3'"  C  N S 131 
FAD "O3'"  O  N N 132 
FAD "C4'"  C  N R 133 
FAD "O4'"  O  N N 134 
FAD "C5'"  C  N N 135 
FAD "O5'"  O  N N 136 
FAD P      P  N R 137 
FAD O1P    O  N N 138 
FAD O2P    O  N N 139 
FAD O3P    O  N N 140 
FAD HOA2   H  N N 141 
FAD H51A   H  N N 142 
FAD H52A   H  N N 143 
FAD H4B    H  N N 144 
FAD H3B    H  N N 145 
FAD HO3A   H  N N 146 
FAD H2B    H  N N 147 
FAD HO2A   H  N N 148 
FAD H1B    H  N N 149 
FAD H8A    H  N N 150 
FAD H61A   H  N N 151 
FAD H62A   H  N N 152 
FAD H2A    H  N N 153 
FAD HN3    H  N N 154 
FAD H6     H  N N 155 
FAD HM71   H  N N 156 
FAD HM72   H  N N 157 
FAD HM73   H  N N 158 
FAD HM81   H  N N 159 
FAD HM82   H  N N 160 
FAD HM83   H  N N 161 
FAD H9     H  N N 162 
FAD "H1'1" H  N N 163 
FAD "H1'2" H  N N 164 
FAD "H2'"  H  N N 165 
FAD "HO2'" H  N N 166 
FAD "H3'"  H  N N 167 
FAD "HO3'" H  N N 168 
FAD "H4'"  H  N N 169 
FAD "HO4'" H  N N 170 
FAD "H5'1" H  N N 171 
FAD "H5'2" H  N N 172 
FAD HOP2   H  N N 173 
GLN N      N  N N 174 
GLN CA     C  N S 175 
GLN C      C  N N 176 
GLN O      O  N N 177 
GLN CB     C  N N 178 
GLN CG     C  N N 179 
GLN CD     C  N N 180 
GLN OE1    O  N N 181 
GLN NE2    N  N N 182 
GLN OXT    O  N N 183 
GLN H      H  N N 184 
GLN H2     H  N N 185 
GLN HA     H  N N 186 
GLN HB2    H  N N 187 
GLN HB3    H  N N 188 
GLN HG2    H  N N 189 
GLN HG3    H  N N 190 
GLN HE21   H  N N 191 
GLN HE22   H  N N 192 
GLN HXT    H  N N 193 
GLU N      N  N N 194 
GLU CA     C  N S 195 
GLU C      C  N N 196 
GLU O      O  N N 197 
GLU CB     C  N N 198 
GLU CG     C  N N 199 
GLU CD     C  N N 200 
GLU OE1    O  N N 201 
GLU OE2    O  N N 202 
GLU OXT    O  N N 203 
GLU H      H  N N 204 
GLU H2     H  N N 205 
GLU HA     H  N N 206 
GLU HB2    H  N N 207 
GLU HB3    H  N N 208 
GLU HG2    H  N N 209 
GLU HG3    H  N N 210 
GLU HE2    H  N N 211 
GLU HXT    H  N N 212 
GLY N      N  N N 213 
GLY CA     C  N N 214 
GLY C      C  N N 215 
GLY O      O  N N 216 
GLY OXT    O  N N 217 
GLY H      H  N N 218 
GLY H2     H  N N 219 
GLY HA2    H  N N 220 
GLY HA3    H  N N 221 
GLY HXT    H  N N 222 
HIS N      N  N N 223 
HIS CA     C  N S 224 
HIS C      C  N N 225 
HIS O      O  N N 226 
HIS CB     C  N N 227 
HIS CG     C  Y N 228 
HIS ND1    N  Y N 229 
HIS CD2    C  Y N 230 
HIS CE1    C  Y N 231 
HIS NE2    N  Y N 232 
HIS OXT    O  N N 233 
HIS H      H  N N 234 
HIS H2     H  N N 235 
HIS HA     H  N N 236 
HIS HB2    H  N N 237 
HIS HB3    H  N N 238 
HIS HD1    H  N N 239 
HIS HD2    H  N N 240 
HIS HE1    H  N N 241 
HIS HE2    H  N N 242 
HIS HXT    H  N N 243 
HOH O      O  N N 244 
HOH H1     H  N N 245 
HOH H2     H  N N 246 
ILE N      N  N N 247 
ILE CA     C  N S 248 
ILE C      C  N N 249 
ILE O      O  N N 250 
ILE CB     C  N S 251 
ILE CG1    C  N N 252 
ILE CG2    C  N N 253 
ILE CD1    C  N N 254 
ILE OXT    O  N N 255 
ILE H      H  N N 256 
ILE H2     H  N N 257 
ILE HA     H  N N 258 
ILE HB     H  N N 259 
ILE HG12   H  N N 260 
ILE HG13   H  N N 261 
ILE HG21   H  N N 262 
ILE HG22   H  N N 263 
ILE HG23   H  N N 264 
ILE HD11   H  N N 265 
ILE HD12   H  N N 266 
ILE HD13   H  N N 267 
ILE HXT    H  N N 268 
LEU N      N  N N 269 
LEU CA     C  N S 270 
LEU C      C  N N 271 
LEU O      O  N N 272 
LEU CB     C  N N 273 
LEU CG     C  N N 274 
LEU CD1    C  N N 275 
LEU CD2    C  N N 276 
LEU OXT    O  N N 277 
LEU H      H  N N 278 
LEU H2     H  N N 279 
LEU HA     H  N N 280 
LEU HB2    H  N N 281 
LEU HB3    H  N N 282 
LEU HG     H  N N 283 
LEU HD11   H  N N 284 
LEU HD12   H  N N 285 
LEU HD13   H  N N 286 
LEU HD21   H  N N 287 
LEU HD22   H  N N 288 
LEU HD23   H  N N 289 
LEU HXT    H  N N 290 
LYS N      N  N N 291 
LYS CA     C  N S 292 
LYS C      C  N N 293 
LYS O      O  N N 294 
LYS CB     C  N N 295 
LYS CG     C  N N 296 
LYS CD     C  N N 297 
LYS CE     C  N N 298 
LYS NZ     N  N N 299 
LYS OXT    O  N N 300 
LYS H      H  N N 301 
LYS H2     H  N N 302 
LYS HA     H  N N 303 
LYS HB2    H  N N 304 
LYS HB3    H  N N 305 
LYS HG2    H  N N 306 
LYS HG3    H  N N 307 
LYS HD2    H  N N 308 
LYS HD3    H  N N 309 
LYS HE2    H  N N 310 
LYS HE3    H  N N 311 
LYS HZ1    H  N N 312 
LYS HZ2    H  N N 313 
LYS HZ3    H  N N 314 
LYS HXT    H  N N 315 
MET N      N  N N 316 
MET CA     C  N S 317 
MET C      C  N N 318 
MET O      O  N N 319 
MET CB     C  N N 320 
MET CG     C  N N 321 
MET SD     S  N N 322 
MET CE     C  N N 323 
MET OXT    O  N N 324 
MET H      H  N N 325 
MET H2     H  N N 326 
MET HA     H  N N 327 
MET HB2    H  N N 328 
MET HB3    H  N N 329 
MET HG2    H  N N 330 
MET HG3    H  N N 331 
MET HE1    H  N N 332 
MET HE2    H  N N 333 
MET HE3    H  N N 334 
MET HXT    H  N N 335 
MG  MG     MG N N 336 
PHE N      N  N N 337 
PHE CA     C  N S 338 
PHE C      C  N N 339 
PHE O      O  N N 340 
PHE CB     C  N N 341 
PHE CG     C  Y N 342 
PHE CD1    C  Y N 343 
PHE CD2    C  Y N 344 
PHE CE1    C  Y N 345 
PHE CE2    C  Y N 346 
PHE CZ     C  Y N 347 
PHE OXT    O  N N 348 
PHE H      H  N N 349 
PHE H2     H  N N 350 
PHE HA     H  N N 351 
PHE HB2    H  N N 352 
PHE HB3    H  N N 353 
PHE HD1    H  N N 354 
PHE HD2    H  N N 355 
PHE HE1    H  N N 356 
PHE HE2    H  N N 357 
PHE HZ     H  N N 358 
PHE HXT    H  N N 359 
PRO N      N  N N 360 
PRO CA     C  N S 361 
PRO C      C  N N 362 
PRO O      O  N N 363 
PRO CB     C  N N 364 
PRO CG     C  N N 365 
PRO CD     C  N N 366 
PRO OXT    O  N N 367 
PRO H      H  N N 368 
PRO HA     H  N N 369 
PRO HB2    H  N N 370 
PRO HB3    H  N N 371 
PRO HG2    H  N N 372 
PRO HG3    H  N N 373 
PRO HD2    H  N N 374 
PRO HD3    H  N N 375 
PRO HXT    H  N N 376 
SER N      N  N N 377 
SER CA     C  N S 378 
SER C      C  N N 379 
SER O      O  N N 380 
SER CB     C  N N 381 
SER OG     O  N N 382 
SER OXT    O  N N 383 
SER H      H  N N 384 
SER H2     H  N N 385 
SER HA     H  N N 386 
SER HB2    H  N N 387 
SER HB3    H  N N 388 
SER HG     H  N N 389 
SER HXT    H  N N 390 
THR N      N  N N 391 
THR CA     C  N S 392 
THR C      C  N N 393 
THR O      O  N N 394 
THR CB     C  N R 395 
THR OG1    O  N N 396 
THR CG2    C  N N 397 
THR OXT    O  N N 398 
THR H      H  N N 399 
THR H2     H  N N 400 
THR HA     H  N N 401 
THR HB     H  N N 402 
THR HG1    H  N N 403 
THR HG21   H  N N 404 
THR HG22   H  N N 405 
THR HG23   H  N N 406 
THR HXT    H  N N 407 
TRP N      N  N N 408 
TRP CA     C  N S 409 
TRP C      C  N N 410 
TRP O      O  N N 411 
TRP CB     C  N N 412 
TRP CG     C  Y N 413 
TRP CD1    C  Y N 414 
TRP CD2    C  Y N 415 
TRP NE1    N  Y N 416 
TRP CE2    C  Y N 417 
TRP CE3    C  Y N 418 
TRP CZ2    C  Y N 419 
TRP CZ3    C  Y N 420 
TRP CH2    C  Y N 421 
TRP OXT    O  N N 422 
TRP H      H  N N 423 
TRP H2     H  N N 424 
TRP HA     H  N N 425 
TRP HB2    H  N N 426 
TRP HB3    H  N N 427 
TRP HD1    H  N N 428 
TRP HE1    H  N N 429 
TRP HE3    H  N N 430 
TRP HZ2    H  N N 431 
TRP HZ3    H  N N 432 
TRP HH2    H  N N 433 
TRP HXT    H  N N 434 
TYR N      N  N N 435 
TYR CA     C  N S 436 
TYR C      C  N N 437 
TYR O      O  N N 438 
TYR CB     C  N N 439 
TYR CG     C  Y N 440 
TYR CD1    C  Y N 441 
TYR CD2    C  Y N 442 
TYR CE1    C  Y N 443 
TYR CE2    C  Y N 444 
TYR CZ     C  Y N 445 
TYR OH     O  N N 446 
TYR OXT    O  N N 447 
TYR H      H  N N 448 
TYR H2     H  N N 449 
TYR HA     H  N N 450 
TYR HB2    H  N N 451 
TYR HB3    H  N N 452 
TYR HD1    H  N N 453 
TYR HD2    H  N N 454 
TYR HE1    H  N N 455 
TYR HE2    H  N N 456 
TYR HH     H  N N 457 
TYR HXT    H  N N 458 
VAL N      N  N N 459 
VAL CA     C  N S 460 
VAL C      C  N N 461 
VAL O      O  N N 462 
VAL CB     C  N N 463 
VAL CG1    C  N N 464 
VAL CG2    C  N N 465 
VAL OXT    O  N N 466 
VAL H      H  N N 467 
VAL H2     H  N N 468 
VAL HA     H  N N 469 
VAL HB     H  N N 470 
VAL HG11   H  N N 471 
VAL HG12   H  N N 472 
VAL HG13   H  N N 473 
VAL HG21   H  N N 474 
VAL HG22   H  N N 475 
VAL HG23   H  N N 476 
VAL HXT    H  N N 477 
# 
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 
ABN N     C      sing N N 1   
ABN N     HN1    sing N N 2   
ABN N     HN2    sing N N 3   
ABN C     C1     sing N N 4   
ABN C     H1     sing N N 5   
ABN C     H2A    sing N N 6   
ABN C1    C2     doub Y N 7   
ABN C1    C6     sing Y N 8   
ABN C2    C3     sing Y N 9   
ABN C2    H2     sing N N 10  
ABN C3    C4     doub Y N 11  
ABN C3    H3     sing N N 12  
ABN C4    C5     sing Y N 13  
ABN C4    H4     sing N N 14  
ABN C5    C6     doub Y N 15  
ABN C5    H5     sing N N 16  
ABN C6    H6     sing N N 17  
ALA N     CA     sing N N 18  
ALA N     H      sing N N 19  
ALA N     H2     sing N N 20  
ALA CA    C      sing N N 21  
ALA CA    CB     sing N N 22  
ALA CA    HA     sing N N 23  
ALA C     O      doub N N 24  
ALA C     OXT    sing N N 25  
ALA CB    HB1    sing N N 26  
ALA CB    HB2    sing N N 27  
ALA CB    HB3    sing N N 28  
ALA OXT   HXT    sing N N 29  
ARG N     CA     sing N N 30  
ARG N     H      sing N N 31  
ARG N     H2     sing N N 32  
ARG CA    C      sing N N 33  
ARG CA    CB     sing N N 34  
ARG CA    HA     sing N N 35  
ARG C     O      doub N N 36  
ARG C     OXT    sing N N 37  
ARG CB    CG     sing N N 38  
ARG CB    HB2    sing N N 39  
ARG CB    HB3    sing N N 40  
ARG CG    CD     sing N N 41  
ARG CG    HG2    sing N N 42  
ARG CG    HG3    sing N N 43  
ARG CD    NE     sing N N 44  
ARG CD    HD2    sing N N 45  
ARG CD    HD3    sing N N 46  
ARG NE    CZ     sing N N 47  
ARG NE    HE     sing N N 48  
ARG CZ    NH1    sing N N 49  
ARG CZ    NH2    doub N N 50  
ARG NH1   HH11   sing N N 51  
ARG NH1   HH12   sing N N 52  
ARG NH2   HH21   sing N N 53  
ARG NH2   HH22   sing N N 54  
ARG OXT   HXT    sing N N 55  
ASP N     CA     sing N N 56  
ASP N     H      sing N N 57  
ASP N     H2     sing N N 58  
ASP CA    C      sing N N 59  
ASP CA    CB     sing N N 60  
ASP CA    HA     sing N N 61  
ASP C     O      doub N N 62  
ASP C     OXT    sing N N 63  
ASP CB    CG     sing N N 64  
ASP CB    HB2    sing N N 65  
ASP CB    HB3    sing N N 66  
ASP CG    OD1    doub N N 67  
ASP CG    OD2    sing N N 68  
ASP OD2   HD2    sing N N 69  
ASP OXT   HXT    sing N N 70  
CYS N     CA     sing N N 71  
CYS N     H      sing N N 72  
CYS N     H2     sing N N 73  
CYS CA    C      sing N N 74  
CYS CA    CB     sing N N 75  
CYS CA    HA     sing N N 76  
CYS C     O      doub N N 77  
CYS C     OXT    sing N N 78  
CYS CB    SG     sing N N 79  
CYS CB    HB2    sing N N 80  
CYS CB    HB3    sing N N 81  
CYS SG    HG     sing N N 82  
CYS OXT   HXT    sing N N 83  
FAD PA    O1A    doub N N 84  
FAD PA    O2A    sing N N 85  
FAD PA    O5B    sing N N 86  
FAD PA    O3P    sing N N 87  
FAD O2A   HOA2   sing N N 88  
FAD O5B   C5B    sing N N 89  
FAD C5B   C4B    sing N N 90  
FAD C5B   H51A   sing N N 91  
FAD C5B   H52A   sing N N 92  
FAD C4B   O4B    sing N N 93  
FAD C4B   C3B    sing N N 94  
FAD C4B   H4B    sing N N 95  
FAD O4B   C1B    sing N N 96  
FAD C3B   O3B    sing N N 97  
FAD C3B   C2B    sing N N 98  
FAD C3B   H3B    sing N N 99  
FAD O3B   HO3A   sing N N 100 
FAD C2B   O2B    sing N N 101 
FAD C2B   C1B    sing N N 102 
FAD C2B   H2B    sing N N 103 
FAD O2B   HO2A   sing N N 104 
FAD C1B   N9A    sing N N 105 
FAD C1B   H1B    sing N N 106 
FAD N9A   C8A    sing Y N 107 
FAD N9A   C4A    sing Y N 108 
FAD C8A   N7A    doub Y N 109 
FAD C8A   H8A    sing N N 110 
FAD N7A   C5A    sing Y N 111 
FAD C5A   C6A    sing Y N 112 
FAD C5A   C4A    doub Y N 113 
FAD C6A   N6A    sing N N 114 
FAD C6A   N1A    doub Y N 115 
FAD N6A   H61A   sing N N 116 
FAD N6A   H62A   sing N N 117 
FAD N1A   C2A    sing Y N 118 
FAD C2A   N3A    doub Y N 119 
FAD C2A   H2A    sing N N 120 
FAD N3A   C4A    sing Y N 121 
FAD N1    C2     sing N N 122 
FAD N1    C10    doub N N 123 
FAD C2    O2     doub N N 124 
FAD C2    N3     sing N N 125 
FAD N3    C4     sing N N 126 
FAD N3    HN3    sing N N 127 
FAD C4    O4     doub N N 128 
FAD C4    C4X    sing N N 129 
FAD C4X   N5     doub N N 130 
FAD C4X   C10    sing N N 131 
FAD N5    C5X    sing N N 132 
FAD C5X   C6     doub Y N 133 
FAD C5X   C9A    sing Y N 134 
FAD C6    C7     sing Y N 135 
FAD C6    H6     sing N N 136 
FAD C7    C7M    sing N N 137 
FAD C7    C8     doub Y N 138 
FAD C7M   HM71   sing N N 139 
FAD C7M   HM72   sing N N 140 
FAD C7M   HM73   sing N N 141 
FAD C8    C8M    sing N N 142 
FAD C8    C9     sing Y N 143 
FAD C8M   HM81   sing N N 144 
FAD C8M   HM82   sing N N 145 
FAD C8M   HM83   sing N N 146 
FAD C9    C9A    doub Y N 147 
FAD C9    H9     sing N N 148 
FAD C9A   N10    sing N N 149 
FAD N10   C10    sing N N 150 
FAD N10   "C1'"  sing N N 151 
FAD "C1'" "C2'"  sing N N 152 
FAD "C1'" "H1'1" sing N N 153 
FAD "C1'" "H1'2" sing N N 154 
FAD "C2'" "O2'"  sing N N 155 
FAD "C2'" "C3'"  sing N N 156 
FAD "C2'" "H2'"  sing N N 157 
FAD "O2'" "HO2'" sing N N 158 
FAD "C3'" "O3'"  sing N N 159 
FAD "C3'" "C4'"  sing N N 160 
FAD "C3'" "H3'"  sing N N 161 
FAD "O3'" "HO3'" sing N N 162 
FAD "C4'" "O4'"  sing N N 163 
FAD "C4'" "C5'"  sing N N 164 
FAD "C4'" "H4'"  sing N N 165 
FAD "O4'" "HO4'" sing N N 166 
FAD "C5'" "O5'"  sing N N 167 
FAD "C5'" "H5'1" sing N N 168 
FAD "C5'" "H5'2" sing N N 169 
FAD "O5'" P      sing N N 170 
FAD P     O1P    doub N N 171 
FAD P     O2P    sing N N 172 
FAD P     O3P    sing N N 173 
FAD O2P   HOP2   sing N N 174 
GLN N     CA     sing N N 175 
GLN N     H      sing N N 176 
GLN N     H2     sing N N 177 
GLN CA    C      sing N N 178 
GLN CA    CB     sing N N 179 
GLN CA    HA     sing N N 180 
GLN C     O      doub N N 181 
GLN C     OXT    sing N N 182 
GLN CB    CG     sing N N 183 
GLN CB    HB2    sing N N 184 
GLN CB    HB3    sing N N 185 
GLN CG    CD     sing N N 186 
GLN CG    HG2    sing N N 187 
GLN CG    HG3    sing N N 188 
GLN CD    OE1    doub N N 189 
GLN CD    NE2    sing N N 190 
GLN NE2   HE21   sing N N 191 
GLN NE2   HE22   sing N N 192 
GLN OXT   HXT    sing N N 193 
GLU N     CA     sing N N 194 
GLU N     H      sing N N 195 
GLU N     H2     sing N N 196 
GLU CA    C      sing N N 197 
GLU CA    CB     sing N N 198 
GLU CA    HA     sing N N 199 
GLU C     O      doub N N 200 
GLU C     OXT    sing N N 201 
GLU CB    CG     sing N N 202 
GLU CB    HB2    sing N N 203 
GLU CB    HB3    sing N N 204 
GLU CG    CD     sing N N 205 
GLU CG    HG2    sing N N 206 
GLU CG    HG3    sing N N 207 
GLU CD    OE1    doub N N 208 
GLU CD    OE2    sing N N 209 
GLU OE2   HE2    sing N N 210 
GLU OXT   HXT    sing N N 211 
GLY N     CA     sing N N 212 
GLY N     H      sing N N 213 
GLY N     H2     sing N N 214 
GLY CA    C      sing N N 215 
GLY CA    HA2    sing N N 216 
GLY CA    HA3    sing N N 217 
GLY C     O      doub N N 218 
GLY C     OXT    sing N N 219 
GLY OXT   HXT    sing N N 220 
HIS N     CA     sing N N 221 
HIS N     H      sing N N 222 
HIS N     H2     sing N N 223 
HIS CA    C      sing N N 224 
HIS CA    CB     sing N N 225 
HIS CA    HA     sing N N 226 
HIS C     O      doub N N 227 
HIS C     OXT    sing N N 228 
HIS CB    CG     sing N N 229 
HIS CB    HB2    sing N N 230 
HIS CB    HB3    sing N N 231 
HIS CG    ND1    sing Y N 232 
HIS CG    CD2    doub Y N 233 
HIS ND1   CE1    doub Y N 234 
HIS ND1   HD1    sing N N 235 
HIS CD2   NE2    sing Y N 236 
HIS CD2   HD2    sing N N 237 
HIS CE1   NE2    sing Y N 238 
HIS CE1   HE1    sing N N 239 
HIS NE2   HE2    sing N N 240 
HIS OXT   HXT    sing N N 241 
HOH O     H1     sing N N 242 
HOH O     H2     sing N N 243 
ILE N     CA     sing N N 244 
ILE N     H      sing N N 245 
ILE N     H2     sing N N 246 
ILE CA    C      sing N N 247 
ILE CA    CB     sing N N 248 
ILE CA    HA     sing N N 249 
ILE C     O      doub N N 250 
ILE C     OXT    sing N N 251 
ILE CB    CG1    sing N N 252 
ILE CB    CG2    sing N N 253 
ILE CB    HB     sing N N 254 
ILE CG1   CD1    sing N N 255 
ILE CG1   HG12   sing N N 256 
ILE CG1   HG13   sing N N 257 
ILE CG2   HG21   sing N N 258 
ILE CG2   HG22   sing N N 259 
ILE CG2   HG23   sing N N 260 
ILE CD1   HD11   sing N N 261 
ILE CD1   HD12   sing N N 262 
ILE CD1   HD13   sing N N 263 
ILE OXT   HXT    sing N N 264 
LEU N     CA     sing N N 265 
LEU N     H      sing N N 266 
LEU N     H2     sing N N 267 
LEU CA    C      sing N N 268 
LEU CA    CB     sing N N 269 
LEU CA    HA     sing N N 270 
LEU C     O      doub N N 271 
LEU C     OXT    sing N N 272 
LEU CB    CG     sing N N 273 
LEU CB    HB2    sing N N 274 
LEU CB    HB3    sing N N 275 
LEU CG    CD1    sing N N 276 
LEU CG    CD2    sing N N 277 
LEU CG    HG     sing N N 278 
LEU CD1   HD11   sing N N 279 
LEU CD1   HD12   sing N N 280 
LEU CD1   HD13   sing N N 281 
LEU CD2   HD21   sing N N 282 
LEU CD2   HD22   sing N N 283 
LEU CD2   HD23   sing N N 284 
LEU OXT   HXT    sing N N 285 
LYS N     CA     sing N N 286 
LYS N     H      sing N N 287 
LYS N     H2     sing N N 288 
LYS CA    C      sing N N 289 
LYS CA    CB     sing N N 290 
LYS CA    HA     sing N N 291 
LYS C     O      doub N N 292 
LYS C     OXT    sing N N 293 
LYS CB    CG     sing N N 294 
LYS CB    HB2    sing N N 295 
LYS CB    HB3    sing N N 296 
LYS CG    CD     sing N N 297 
LYS CG    HG2    sing N N 298 
LYS CG    HG3    sing N N 299 
LYS CD    CE     sing N N 300 
LYS CD    HD2    sing N N 301 
LYS CD    HD3    sing N N 302 
LYS CE    NZ     sing N N 303 
LYS CE    HE2    sing N N 304 
LYS CE    HE3    sing N N 305 
LYS NZ    HZ1    sing N N 306 
LYS NZ    HZ2    sing N N 307 
LYS NZ    HZ3    sing N N 308 
LYS OXT   HXT    sing N N 309 
MET N     CA     sing N N 310 
MET N     H      sing N N 311 
MET N     H2     sing N N 312 
MET CA    C      sing N N 313 
MET CA    CB     sing N N 314 
MET CA    HA     sing N N 315 
MET C     O      doub N N 316 
MET C     OXT    sing N N 317 
MET CB    CG     sing N N 318 
MET CB    HB2    sing N N 319 
MET CB    HB3    sing N N 320 
MET CG    SD     sing N N 321 
MET CG    HG2    sing N N 322 
MET CG    HG3    sing N N 323 
MET SD    CE     sing N N 324 
MET CE    HE1    sing N N 325 
MET CE    HE2    sing N N 326 
MET CE    HE3    sing N N 327 
MET OXT   HXT    sing N N 328 
PHE N     CA     sing N N 329 
PHE N     H      sing N N 330 
PHE N     H2     sing N N 331 
PHE CA    C      sing N N 332 
PHE CA    CB     sing N N 333 
PHE CA    HA     sing N N 334 
PHE C     O      doub N N 335 
PHE C     OXT    sing N N 336 
PHE CB    CG     sing N N 337 
PHE CB    HB2    sing N N 338 
PHE CB    HB3    sing N N 339 
PHE CG    CD1    doub Y N 340 
PHE CG    CD2    sing Y N 341 
PHE CD1   CE1    sing Y N 342 
PHE CD1   HD1    sing N N 343 
PHE CD2   CE2    doub Y N 344 
PHE CD2   HD2    sing N N 345 
PHE CE1   CZ     doub Y N 346 
PHE CE1   HE1    sing N N 347 
PHE CE2   CZ     sing Y N 348 
PHE CE2   HE2    sing N N 349 
PHE CZ    HZ     sing N N 350 
PHE OXT   HXT    sing N N 351 
PRO N     CA     sing N N 352 
PRO N     CD     sing N N 353 
PRO N     H      sing N N 354 
PRO CA    C      sing N N 355 
PRO CA    CB     sing N N 356 
PRO CA    HA     sing N N 357 
PRO C     O      doub N N 358 
PRO C     OXT    sing N N 359 
PRO CB    CG     sing N N 360 
PRO CB    HB2    sing N N 361 
PRO CB    HB3    sing N N 362 
PRO CG    CD     sing N N 363 
PRO CG    HG2    sing N N 364 
PRO CG    HG3    sing N N 365 
PRO CD    HD2    sing N N 366 
PRO CD    HD3    sing N N 367 
PRO OXT   HXT    sing N N 368 
SER N     CA     sing N N 369 
SER N     H      sing N N 370 
SER N     H2     sing N N 371 
SER CA    C      sing N N 372 
SER CA    CB     sing N N 373 
SER CA    HA     sing N N 374 
SER C     O      doub N N 375 
SER C     OXT    sing N N 376 
SER CB    OG     sing N N 377 
SER CB    HB2    sing N N 378 
SER CB    HB3    sing N N 379 
SER OG    HG     sing N N 380 
SER OXT   HXT    sing N N 381 
THR N     CA     sing N N 382 
THR N     H      sing N N 383 
THR N     H2     sing N N 384 
THR CA    C      sing N N 385 
THR CA    CB     sing N N 386 
THR CA    HA     sing N N 387 
THR C     O      doub N N 388 
THR C     OXT    sing N N 389 
THR CB    OG1    sing N N 390 
THR CB    CG2    sing N N 391 
THR CB    HB     sing N N 392 
THR OG1   HG1    sing N N 393 
THR CG2   HG21   sing N N 394 
THR CG2   HG22   sing N N 395 
THR CG2   HG23   sing N N 396 
THR OXT   HXT    sing N N 397 
TRP N     CA     sing N N 398 
TRP N     H      sing N N 399 
TRP N     H2     sing N N 400 
TRP CA    C      sing N N 401 
TRP CA    CB     sing N N 402 
TRP CA    HA     sing N N 403 
TRP C     O      doub N N 404 
TRP C     OXT    sing N N 405 
TRP CB    CG     sing N N 406 
TRP CB    HB2    sing N N 407 
TRP CB    HB3    sing N N 408 
TRP CG    CD1    doub Y N 409 
TRP CG    CD2    sing Y N 410 
TRP CD1   NE1    sing Y N 411 
TRP CD1   HD1    sing N N 412 
TRP CD2   CE2    doub Y N 413 
TRP CD2   CE3    sing Y N 414 
TRP NE1   CE2    sing Y N 415 
TRP NE1   HE1    sing N N 416 
TRP CE2   CZ2    sing Y N 417 
TRP CE3   CZ3    doub Y N 418 
TRP CE3   HE3    sing N N 419 
TRP CZ2   CH2    doub Y N 420 
TRP CZ2   HZ2    sing N N 421 
TRP CZ3   CH2    sing Y N 422 
TRP CZ3   HZ3    sing N N 423 
TRP CH2   HH2    sing N N 424 
TRP OXT   HXT    sing N N 425 
TYR N     CA     sing N N 426 
TYR N     H      sing N N 427 
TYR N     H2     sing N N 428 
TYR CA    C      sing N N 429 
TYR CA    CB     sing N N 430 
TYR CA    HA     sing N N 431 
TYR C     O      doub N N 432 
TYR C     OXT    sing N N 433 
TYR CB    CG     sing N N 434 
TYR CB    HB2    sing N N 435 
TYR CB    HB3    sing N N 436 
TYR CG    CD1    doub Y N 437 
TYR CG    CD2    sing Y N 438 
TYR CD1   CE1    sing Y N 439 
TYR CD1   HD1    sing N N 440 
TYR CD2   CE2    doub Y N 441 
TYR CD2   HD2    sing N N 442 
TYR CE1   CZ     doub Y N 443 
TYR CE1   HE1    sing N N 444 
TYR CE2   CZ     sing Y N 445 
TYR CE2   HE2    sing N N 446 
TYR CZ    OH     sing N N 447 
TYR OH    HH     sing N N 448 
TYR OXT   HXT    sing N N 449 
VAL N     CA     sing N N 450 
VAL N     H      sing N N 451 
VAL N     H2     sing N N 452 
VAL CA    C      sing N N 453 
VAL CA    CB     sing N N 454 
VAL CA    HA     sing N N 455 
VAL C     O      doub N N 456 
VAL C     OXT    sing N N 457 
VAL CB    CG1    sing N N 458 
VAL CB    CG2    sing N N 459 
VAL CB    HB     sing N N 460 
VAL CG1   HG11   sing N N 461 
VAL CG1   HG12   sing N N 462 
VAL CG1   HG13   sing N N 463 
VAL CG2   HG21   sing N N 464 
VAL CG2   HG22   sing N N 465 
VAL CG2   HG23   sing N N 466 
VAL OXT   HXT    sing N N 467 
# 
_pdbx_audit_support.funding_organization   'Italian Ministry of Education' 
_pdbx_audit_support.country                Italy 
_pdbx_audit_support.grant_number           'MUR PNRR NODES' 
_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   8p84 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9H5Z 
_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]   0.014394 
_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]   0.009976 
_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]   0.008271 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLN A 1 26  ? 61.485 3.683   -2.912  1.00 45.97  ? 5   GLN A N     1 
ATOM   2    C  CA    . GLN A 1 26  ? 60.660 3.834   -4.148  1.00 50.05  ? 5   GLN A CA    1 
ATOM   3    C  C     . GLN A 1 26  ? 61.053 2.784   -5.197  1.00 46.96  ? 5   GLN A C     1 
ATOM   4    O  O     . GLN A 1 26  ? 62.212 2.756   -5.570  1.00 53.37  ? 5   GLN A O     1 
ATOM   5    C  CB    . GLN A 1 26  ? 60.792 5.222   -4.790  1.00 52.41  ? 5   GLN A CB    1 
ATOM   6    C  CG    . GLN A 1 26  ? 59.769 5.428   -5.913  1.00 54.93  ? 5   GLN A CG    1 
ATOM   7    C  CD    . GLN A 1 26  ? 59.886 6.706   -6.717  1.00 59.54  ? 5   GLN A CD    1 
ATOM   8    O  OE1   . GLN A 1 26  ? 60.862 6.937   -7.436  1.00 62.82  ? 5   GLN A OE1   1 
ATOM   9    N  NE2   . GLN A 1 26  ? 58.836 7.512   -6.678  1.00 57.32  ? 5   GLN A NE2   1 
ATOM   10   N  N     . VAL A 1 27  ? 60.096 2.020   -5.717  1.00 43.25  ? 6   VAL A N     1 
ATOM   11   C  CA    . VAL A 1 27  ? 60.329 1.037   -6.818  1.00 42.45  ? 6   VAL A CA    1 
ATOM   12   C  C     . VAL A 1 27  ? 59.783 1.614   -8.130  1.00 41.48  ? 6   VAL A C     1 
ATOM   13   O  O     . VAL A 1 27  ? 59.182 2.706   -8.103  1.00 40.43  ? 6   VAL A O     1 
ATOM   14   C  CB    . VAL A 1 27  ? 59.738 -0.344  -6.477  1.00 42.81  ? 6   VAL A CB    1 
ATOM   15   C  CG1   . VAL A 1 27  ? 60.429 -0.900  -5.246  1.00 45.17  ? 6   VAL A CG1   1 
ATOM   16   C  CG2   . VAL A 1 27  ? 58.230 -0.329  -6.283  1.00 44.02  ? 6   VAL A CG2   1 
ATOM   17   N  N     . ASP A 1 28  ? 60.026 0.938   -9.252  1.00 37.02  ? 7   ASP A N     1 
ATOM   18   C  CA    . ASP A 1 28  ? 59.590 1.453   -10.573 1.00 39.30  ? 7   ASP A CA    1 
ATOM   19   C  C     . ASP A 1 28  ? 58.065 1.289   -10.652 1.00 38.16  ? 7   ASP A C     1 
ATOM   20   O  O     . ASP A 1 28  ? 57.350 2.290   -10.903 1.00 35.87  ? 7   ASP A O     1 
ATOM   21   C  CB    . ASP A 1 28  ? 60.373 0.821   -11.726 1.00 37.27  ? 7   ASP A CB    1 
ATOM   22   C  CG    . ASP A 1 28  ? 61.824 1.288   -11.834 1.00 45.82  ? 7   ASP A CG    1 
ATOM   23   O  OD1   . ASP A 1 28  ? 62.082 2.518   -11.626 1.00 50.45  ? 7   ASP A OD1   1 
ATOM   24   O  OD2   . ASP A 1 28  ? 62.701 0.430   -12.139 1.00 43.83  ? 7   ASP A OD2   1 
ATOM   25   N  N     . VAL A 1 29  ? 57.580 0.098   -10.335 1.00 34.47  ? 8   VAL A N     1 
ATOM   26   C  CA    . VAL A 1 29  ? 56.172 -0.296  -10.599 1.00 33.76  ? 8   VAL A CA    1 
ATOM   27   C  C     . VAL A 1 29  ? 55.640 -1.024  -9.375  1.00 31.51  ? 8   VAL A C     1 
ATOM   28   O  O     . VAL A 1 29  ? 56.331 -1.951  -8.898  1.00 34.91  ? 8   VAL A O     1 
ATOM   29   C  CB    . VAL A 1 29  ? 56.109 -1.152  -11.879 1.00 34.16  ? 8   VAL A CB    1 
ATOM   30   C  CG1   . VAL A 1 29  ? 54.692 -1.504  -12.275 1.00 33.05  ? 8   VAL A CG1   1 
ATOM   31   C  CG2   . VAL A 1 29  ? 56.810 -0.454  -13.039 1.00 32.72  ? 8   VAL A CG2   1 
ATOM   32   N  N     . VAL A 1 30  ? 54.468 -0.604  -8.884  1.00 30.99  ? 9   VAL A N     1 
ATOM   33   C  CA    . VAL A 1 30  ? 53.655 -1.370  -7.903  1.00 28.61  ? 9   VAL A CA    1 
ATOM   34   C  C     . VAL A 1 30  ? 52.445 -1.960  -8.637  1.00 31.77  ? 9   VAL A C     1 
ATOM   35   O  O     . VAL A 1 30  ? 51.662 -1.216  -9.255  1.00 34.75  ? 9   VAL A O     1 
ATOM   36   C  CB    . VAL A 1 30  ? 53.257 -0.532  -6.679  1.00 32.57  ? 9   VAL A CB    1 
ATOM   37   C  CG1   . VAL A 1 30  ? 52.375 0.655   -7.036  1.00 36.23  ? 9   VAL A CG1   1 
ATOM   38   C  CG2   . VAL A 1 30  ? 52.575 -1.370  -5.606  1.00 35.12  ? 9   VAL A CG2   1 
ATOM   39   N  N     . VAL A 1 31  ? 52.316 -3.277  -8.576  1.00 30.77  ? 10  VAL A N     1 
ATOM   40   C  CA    . VAL A 1 31  ? 51.168 -4.046  -9.119  1.00 32.14  ? 10  VAL A CA    1 
ATOM   41   C  C     . VAL A 1 31  ? 50.229 -4.444  -7.970  1.00 30.67  ? 10  VAL A C     1 
ATOM   42   O  O     . VAL A 1 31  ? 50.713 -5.036  -7.003  1.00 28.52  ? 10  VAL A O     1 
ATOM   43   C  CB    . VAL A 1 31  ? 51.685 -5.290  -9.852  1.00 31.94  ? 10  VAL A CB    1 
ATOM   44   C  CG1   . VAL A 1 31  ? 50.548 -6.024  -10.543 1.00 32.12  ? 10  VAL A CG1   1 
ATOM   45   C  CG2   . VAL A 1 31  ? 52.809 -4.933  -10.817 1.00 32.62  ? 10  VAL A CG2   1 
ATOM   46   N  N     . VAL A 1 32  ? 48.932 -4.152  -8.099  1.00 30.50  ? 11  VAL A N     1 
ATOM   47   C  CA    . VAL A 1 32  ? 47.867 -4.595  -7.155  1.00 33.12  ? 11  VAL A CA    1 
ATOM   48   C  C     . VAL A 1 32  ? 47.208 -5.849  -7.739  1.00 32.36  ? 11  VAL A C     1 
ATOM   49   O  O     . VAL A 1 32  ? 46.605 -5.731  -8.788  1.00 32.93  ? 11  VAL A O     1 
ATOM   50   C  CB    . VAL A 1 32  ? 46.834 -3.483  -6.927  1.00 33.98  ? 11  VAL A CB    1 
ATOM   51   C  CG1   . VAL A 1 32  ? 46.019 -3.780  -5.689  1.00 34.28  ? 11  VAL A CG1   1 
ATOM   52   C  CG2   . VAL A 1 32  ? 47.490 -2.104  -6.830  1.00 36.21  ? 11  VAL A CG2   1 
ATOM   53   N  N     . GLY A 1 33  ? 47.376 -7.004  -7.099  1.00 33.00  ? 12  GLY A N     1 
ATOM   54   C  CA    . GLY A 1 33  ? 46.775 -8.285  -7.530  1.00 33.00  ? 12  GLY A CA    1 
ATOM   55   C  C     . GLY A 1 33  ? 47.794 -9.274  -8.088  1.00 30.27  ? 12  GLY A C     1 
ATOM   56   O  O     . GLY A 1 33  ? 48.595 -8.898  -8.938  1.00 33.86  ? 12  GLY A O     1 
ATOM   57   N  N     . ALA A 1 34  ? 47.729 -10.515 -7.633  1.00 28.60  ? 13  ALA A N     1 
ATOM   58   C  CA    . ALA A 1 34  ? 48.595 -11.640 -8.029  1.00 28.09  ? 13  ALA A CA    1 
ATOM   59   C  C     . ALA A 1 34  ? 47.712 -12.725 -8.643  1.00 28.88  ? 13  ALA A C     1 
ATOM   60   O  O     . ALA A 1 34  ? 47.934 -13.899 -8.341  1.00 27.09  ? 13  ALA A O     1 
ATOM   61   C  CB    . ALA A 1 34  ? 49.353 -12.166 -6.833  1.00 30.45  ? 13  ALA A CB    1 
ATOM   62   N  N     . GLY A 1 35  ? 46.730 -12.319 -9.451  1.00 29.50  ? 14  GLY A N     1 
ATOM   63   C  CA    . GLY A 1 35  ? 46.120 -13.177 -10.487 1.00 32.64  ? 14  GLY A CA    1 
ATOM   64   C  C     . GLY A 1 35  ? 47.047 -13.284 -11.687 1.00 32.52  ? 14  GLY A C     1 
ATOM   65   O  O     . GLY A 1 35  ? 48.148 -12.714 -11.642 1.00 34.57  ? 14  GLY A O     1 
ATOM   66   N  N     . PHE A 1 36  ? 46.627 -13.967 -12.739 1.00 30.52  ? 15  PHE A N     1 
ATOM   67   C  CA    . PHE A 1 36  ? 47.434 -14.117 -13.976 1.00 30.35  ? 15  PHE A CA    1 
ATOM   68   C  C     . PHE A 1 36  ? 47.753 -12.720 -14.541 1.00 33.47  ? 15  PHE A C     1 
ATOM   69   O  O     . PHE A 1 36  ? 48.854 -12.549 -15.051 1.00 32.24  ? 15  PHE A O     1 
ATOM   70   C  CB    . PHE A 1 36  ? 46.727 -15.074 -14.938 1.00 27.08  ? 15  PHE A CB    1 
ATOM   71   C  CG    . PHE A 1 36  ? 47.004 -16.524 -14.620 1.00 26.44  ? 15  PHE A CG    1 
ATOM   72   C  CD1   . PHE A 1 36  ? 48.160 -17.137 -15.075 1.00 28.31  ? 15  PHE A CD1   1 
ATOM   73   C  CD2   . PHE A 1 36  ? 46.142 -17.268 -13.828 1.00 26.11  ? 15  PHE A CD2   1 
ATOM   74   C  CE1   . PHE A 1 36  ? 48.408 -18.479 -14.798 1.00 27.66  ? 15  PHE A CE1   1 
ATOM   75   C  CE2   . PHE A 1 36  ? 46.406 -18.601 -13.533 1.00 26.17  ? 15  PHE A CE2   1 
ATOM   76   C  CZ    . PHE A 1 36  ? 47.540 -19.201 -14.013 1.00 25.77  ? 15  PHE A CZ    1 
ATOM   77   N  N     . ALA A 1 37  ? 46.841 -11.744 -14.446 1.00 33.47  ? 16  ALA A N     1 
ATOM   78   C  CA    . ALA A 1 37  ? 47.069 -10.388 -14.996 1.00 34.32  ? 16  ALA A CA    1 
ATOM   79   C  C     . ALA A 1 37  ? 48.212 -9.703  -14.229 1.00 30.46  ? 16  ALA A C     1 
ATOM   80   O  O     . ALA A 1 37  ? 49.136 -9.207  -14.873 1.00 31.89  ? 16  ALA A O     1 
ATOM   81   C  CB    . ALA A 1 37  ? 45.801 -9.568  -14.956 1.00 35.30  ? 16  ALA A CB    1 
ATOM   82   N  N     . GLY A 1 38  ? 48.152 -9.667  -12.900 1.00 29.75  ? 17  GLY A N     1 
ATOM   83   C  CA    . GLY A 1 38  ? 49.183 -9.005  -12.075 1.00 29.68  ? 17  GLY A CA    1 
ATOM   84   C  C     . GLY A 1 38  ? 50.538 -9.686  -12.165 1.00 30.29  ? 17  GLY A C     1 
ATOM   85   O  O     . GLY A 1 38  ? 51.542 -8.975  -12.255 1.00 27.06  ? 17  GLY A O     1 
ATOM   86   N  N     . LEU A 1 39  ? 50.572 -11.016 -12.089 1.00 28.08  ? 18  LEU A N     1 
ATOM   87   C  CA    . LEU A 1 39  ? 51.834 -11.795 -12.119 1.00 30.53  ? 18  LEU A CA    1 
ATOM   88   C  C     . LEU A 1 39  ? 52.479 -11.696 -13.512 1.00 30.67  ? 18  LEU A C     1 
ATOM   89   O  O     . LEU A 1 39  ? 53.702 -11.568 -13.551 1.00 29.57  ? 18  LEU A O     1 
ATOM   90   C  CB    . LEU A 1 39  ? 51.558 -13.252 -11.710 1.00 29.78  ? 18  LEU A CB    1 
ATOM   91   C  CG    . LEU A 1 39  ? 51.341 -13.486 -10.213 1.00 28.52  ? 18  LEU A CG    1 
ATOM   92   C  CD1   . LEU A 1 39  ? 51.029 -14.940 -9.905  1.00 29.94  ? 18  LEU A CD1   1 
ATOM   93   C  CD2   . LEU A 1 39  ? 52.530 -13.042 -9.397  1.00 30.74  ? 18  LEU A CD2   1 
ATOM   94   N  N     . THR A 1 40  ? 51.695 -11.690 -14.602 1.00 29.54  ? 19  THR A N     1 
ATOM   95   C  CA    . THR A 1 40  ? 52.188 -11.495 -15.988 1.00 28.36  ? 19  THR A CA    1 
ATOM   96   C  C     . THR A 1 40  ? 52.785 -10.079 -16.108 1.00 32.76  ? 19  THR A C     1 
ATOM   97   O  O     . THR A 1 40  ? 53.895 -9.958  -16.673 1.00 31.87  ? 19  THR A O     1 
ATOM   98   C  CB    . THR A 1 40  ? 51.094 -11.781 -17.032 1.00 28.97  ? 19  THR A CB    1 
ATOM   99   O  OG1   . THR A 1 40  ? 50.726 -13.164 -17.008 1.00 27.62  ? 19  THR A OG1   1 
ATOM   100  C  CG2   . THR A 1 40  ? 51.535 -11.460 -18.439 1.00 27.79  ? 19  THR A CG2   1 
ATOM   101  N  N     . ALA A 1 41  ? 52.095 -9.035  -15.622 1.00 27.19  ? 20  ALA A N     1 
ATOM   102  C  CA    . ALA A 1 41  ? 52.610 -7.654  -15.694 1.00 27.76  ? 20  ALA A CA    1 
ATOM   103  C  C     . ALA A 1 41  ? 53.897 -7.562  -14.868 1.00 29.08  ? 20  ALA A C     1 
ATOM   104  O  O     . ALA A 1 41  ? 54.852 -6.906  -15.330 1.00 31.64  ? 20  ALA A O     1 
ATOM   105  C  CB    . ALA A 1 41  ? 51.588 -6.642  -15.221 1.00 28.26  ? 20  ALA A CB    1 
ATOM   106  N  N     . ALA A 1 42  ? 53.949 -8.188  -13.693 1.00 26.33  ? 21  ALA A N     1 
ATOM   107  C  CA    . ALA A 1 42  ? 55.134 -8.051  -12.835 1.00 29.79  ? 21  ALA A CA    1 
ATOM   108  C  C     . ALA A 1 42  ? 56.321 -8.774  -13.477 1.00 29.67  ? 21  ALA A C     1 
ATOM   109  O  O     . ALA A 1 42  ? 57.423 -8.216  -13.405 1.00 26.61  ? 21  ALA A O     1 
ATOM   110  C  CB    . ALA A 1 42  ? 54.873 -8.505  -11.432 1.00 28.11  ? 21  ALA A CB    1 
ATOM   111  N  N     . ARG A 1 43  ? 56.128 -9.975  -14.017 1.00 30.12  ? 22  ARG A N     1 
ATOM   112  C  CA    . ARG A 1 43  ? 57.250 -10.753 -14.618 1.00 32.52  ? 22  ARG A CA    1 
ATOM   113  C  C     . ARG A 1 43  ? 57.795 -9.995  -15.833 1.00 34.98  ? 22  ARG A C     1 
ATOM   114  O  O     . ARG A 1 43  ? 59.004 -9.996  -16.029 1.00 34.74  ? 22  ARG A O     1 
ATOM   115  C  CB    . ARG A 1 43  ? 56.807 -12.156 -15.028 1.00 34.35  ? 22  ARG A CB    1 
ATOM   116  C  CG    . ARG A 1 43  ? 57.966 -13.082 -15.371 1.00 39.72  ? 22  ARG A CG    1 
ATOM   117  C  CD    . ARG A 1 43  ? 58.282 -13.128 -16.837 1.00 42.12  ? 22  ARG A CD    1 
ATOM   118  N  NE    . ARG A 1 43  ? 57.251 -13.869 -17.536 1.00 47.10  ? 22  ARG A NE    1 
ATOM   119  C  CZ    . ARG A 1 43  ? 57.349 -15.132 -17.925 1.00 46.78  ? 22  ARG A CZ    1 
ATOM   120  N  NH1   . ARG A 1 43  ? 58.456 -15.823 -17.725 1.00 46.46  ? 22  ARG A NH1   1 
ATOM   121  N  NH2   . ARG A 1 43  ? 56.329 -15.695 -18.536 1.00 44.80  ? 22  ARG A NH2   1 
ATOM   122  N  N     . ALA A 1 44  ? 56.931 -9.404  -16.657 1.00 32.70  ? 23  ALA A N     1 
ATOM   123  C  CA    . ALA A 1 44  ? 57.367 -8.676  -17.862 1.00 33.62  ? 23  ALA A CA    1 
ATOM   124  C  C     . ALA A 1 44  ? 58.113 -7.412  -17.415 1.00 33.70  ? 23  ALA A C     1 
ATOM   125  O  O     . ALA A 1 44  ? 59.133 -7.107  -18.055 1.00 31.31  ? 23  ALA A O     1 
ATOM   126  C  CB    . ALA A 1 44  ? 56.204 -8.381  -18.783 1.00 34.95  ? 23  ALA A CB    1 
ATOM   127  N  N     . VAL A 1 45  ? 57.674 -6.714  -16.355 1.00 33.21  ? 24  VAL A N     1 
ATOM   128  C  CA    . VAL A 1 45  ? 58.418 -5.517  -15.847 1.00 34.32  ? 24  VAL A CA    1 
ATOM   129  C  C     . VAL A 1 45  ? 59.788 -5.966  -15.309 1.00 40.48  ? 24  VAL A C     1 
ATOM   130  O  O     . VAL A 1 45  ? 60.796 -5.221  -15.546 1.00 37.36  ? 24  VAL A O     1 
ATOM   131  C  CB    . VAL A 1 45  ? 57.660 -4.720  -14.773 1.00 35.35  ? 24  VAL A CB    1 
ATOM   132  C  CG1   . VAL A 1 45  ? 58.566 -3.686  -14.120 1.00 35.46  ? 24  VAL A CG1   1 
ATOM   133  C  CG2   . VAL A 1 45  ? 56.429 -4.019  -15.333 1.00 35.91  ? 24  VAL A CG2   1 
ATOM   134  N  N     . HIS A 1 46  ? 59.827 -7.103  -14.595 1.00 38.23  ? 25  HIS A N     1 
ATOM   135  C  CA    . HIS A 1 46  ? 61.059 -7.718  -14.035 1.00 39.77  ? 25  HIS A CA    1 
ATOM   136  C  C     . HIS A 1 46  ? 62.022 -8.099  -15.167 1.00 40.12  ? 25  HIS A C     1 
ATOM   137  O  O     . HIS A 1 46  ? 63.192 -7.773  -15.003 1.00 38.51  ? 25  HIS A O     1 
ATOM   138  C  CB    . HIS A 1 46  ? 60.772 -8.916  -13.123 1.00 38.96  ? 25  HIS A CB    1 
ATOM   139  C  CG    . HIS A 1 46  ? 62.022 -9.622  -12.688 1.00 40.24  ? 25  HIS A CG    1 
ATOM   140  N  ND1   . HIS A 1 46  ? 62.917 -9.059  -11.805 1.00 41.31  ? 25  HIS A ND1   1 
ATOM   141  C  CD2   . HIS A 1 46  ? 62.541 -10.824 -13.028 1.00 37.86  ? 25  HIS A CD2   1 
ATOM   142  C  CE1   . HIS A 1 46  ? 63.922 -9.891  -11.598 1.00 37.51  ? 25  HIS A CE1   1 
ATOM   143  N  NE2   . HIS A 1 46  ? 63.711 -10.980 -12.331 1.00 39.34  ? 25  HIS A NE2   1 
ATOM   144  N  N     . GLU A 1 47  ? 61.558 -8.723  -16.263 1.00 42.77  ? 26  GLU A N     1 
ATOM   145  C  CA    . GLU A 1 47  ? 62.414 -9.155  -17.416 1.00 46.48  ? 26  GLU A CA    1 
ATOM   146  C  C     . GLU A 1 47  ? 63.025 -7.930  -18.127 1.00 42.79  ? 26  GLU A C     1 
ATOM   147  O  O     . GLU A 1 47  ? 64.113 -8.070  -18.718 1.00 39.00  ? 26  GLU A O     1 
ATOM   148  C  CB    . GLU A 1 47  ? 61.659 -10.030 -18.427 1.00 52.76  ? 26  GLU A CB    1 
ATOM   149  C  CG    . GLU A 1 47  ? 61.674 -11.521 -18.087 1.00 63.43  ? 26  GLU A CG    1 
ATOM   150  C  CD    . GLU A 1 47  ? 61.332 -12.466 -19.237 1.00 69.63  ? 26  GLU A CD    1 
ATOM   151  O  OE1   . GLU A 1 47  ? 61.606 -13.683 -19.113 1.00 71.95  ? 26  GLU A OE1   1 
ATOM   152  O  OE2   . GLU A 1 47  ? 60.793 -11.991 -20.257 1.00 70.56  ? 26  GLU A OE2   1 
ATOM   153  N  N     . ALA A 1 48  ? 62.358 -6.779  -18.091 1.00 36.72  ? 27  ALA A N     1 
ATOM   154  C  CA    . ALA A 1 48  ? 62.804 -5.528  -18.748 1.00 34.70  ? 27  ALA A CA    1 
ATOM   155  C  C     . ALA A 1 48  ? 63.824 -4.773  -17.881 1.00 35.11  ? 27  ALA A C     1 
ATOM   156  O  O     . ALA A 1 48  ? 64.227 -3.700  -18.288 1.00 40.11  ? 27  ALA A O     1 
ATOM   157  C  CB    . ALA A 1 48  ? 61.598 -4.669  -19.032 1.00 36.73  ? 27  ALA A CB    1 
ATOM   158  N  N     . GLY A 1 49  ? 64.174 -5.274  -16.692 1.00 34.90  ? 28  GLY A N     1 
ATOM   159  C  CA    . GLY A 1 49  ? 65.223 -4.710  -15.826 1.00 35.35  ? 28  GLY A CA    1 
ATOM   160  C  C     . GLY A 1 49  ? 64.729 -3.678  -14.813 1.00 38.29  ? 28  GLY A C     1 
ATOM   161  O  O     . GLY A 1 49  ? 65.588 -2.970  -14.230 1.00 37.57  ? 28  GLY A O     1 
ATOM   162  N  N     . ARG A 1 50  ? 63.417 -3.573  -14.574 1.00 39.19  ? 29  ARG A N     1 
ATOM   163  C  CA    . ARG A 1 50  ? 62.849 -2.572  -13.630 1.00 36.28  ? 29  ARG A CA    1 
ATOM   164  C  C     . ARG A 1 50  ? 62.454 -3.283  -12.324 1.00 34.64  ? 29  ARG A C     1 
ATOM   165  O  O     . ARG A 1 50  ? 62.199 -4.492  -12.341 1.00 33.34  ? 29  ARG A O     1 
ATOM   166  C  CB    . ARG A 1 50  ? 61.711 -1.806  -14.314 1.00 39.60  ? 29  ARG A CB    1 
ATOM   167  C  CG    . ARG A 1 50  ? 62.090 -1.147  -15.637 1.00 47.60  ? 29  ARG A CG    1 
ATOM   168  C  CD    . ARG A 1 50  ? 63.353 -0.310  -15.532 1.00 54.10  ? 29  ARG A CD    1 
ATOM   169  N  NE    . ARG A 1 50  ? 63.572 0.712   -16.560 1.00 58.48  ? 29  ARG A NE    1 
ATOM   170  C  CZ    . ARG A 1 50  ? 63.595 2.037   -16.340 1.00 63.44  ? 29  ARG A CZ    1 
ATOM   171  N  NH1   . ARG A 1 50  ? 63.367 2.538   -15.135 1.00 64.42  ? 29  ARG A NH1   1 
ATOM   172  N  NH2   . ARG A 1 50  ? 63.830 2.872   -17.334 1.00 62.42  ? 29  ARG A NH2   1 
ATOM   173  N  N     . SER A 1 51  ? 62.445 -2.537  -11.222 1.00 36.20  ? 30  SER A N     1 
ATOM   174  C  CA    . SER A 1 51  ? 62.074 -2.994  -9.864  1.00 35.53  ? 30  SER A CA    1 
ATOM   175  C  C     . SER A 1 51  ? 60.545 -3.040  -9.764  1.00 36.50  ? 30  SER A C     1 
ATOM   176  O  O     . SER A 1 51  ? 59.862 -2.150  -10.290 1.00 31.52  ? 30  SER A O     1 
ATOM   177  C  CB    . SER A 1 51  ? 62.683 -2.121  -8.800  1.00 36.47  ? 30  SER A CB    1 
ATOM   178  O  OG    . SER A 1 51  ? 62.374 -0.756  -9.018  1.00 34.53  ? 30  SER A OG    1 
ATOM   179  N  N     . VAL A 1 52  ? 60.025 -4.096  -9.154  1.00 35.99  ? 31  VAL A N     1 
ATOM   180  C  CA    . VAL A 1 52  ? 58.568 -4.346  -9.112  1.00 37.65  ? 31  VAL A CA    1 
ATOM   181  C  C     . VAL A 1 52  ? 58.223 -4.891  -7.723  1.00 34.54  ? 31  VAL A C     1 
ATOM   182  O  O     . VAL A 1 52  ? 59.044 -5.607  -7.140  1.00 34.88  ? 31  VAL A O     1 
ATOM   183  C  CB    . VAL A 1 52  ? 58.168 -5.269  -10.276 1.00 38.48  ? 31  VAL A CB    1 
ATOM   184  C  CG1   . VAL A 1 52  ? 58.708 -6.692  -10.094 1.00 40.18  ? 31  VAL A CG1   1 
ATOM   185  C  CG2   . VAL A 1 52  ? 56.666 -5.251  -10.492 1.00 37.91  ? 31  VAL A CG2   1 
ATOM   186  N  N     . LEU A 1 53  ? 57.089 -4.451  -7.181  1.00 33.69  ? 32  LEU A N     1 
ATOM   187  C  CA    . LEU A 1 53  ? 56.457 -4.989  -5.955  1.00 32.49  ? 32  LEU A CA    1 
ATOM   188  C  C     . LEU A 1 53  ? 55.034 -5.409  -6.329  1.00 33.53  ? 32  LEU A C     1 
ATOM   189  O  O     . LEU A 1 53  ? 54.369 -4.605  -7.029  1.00 35.61  ? 32  LEU A O     1 
ATOM   190  C  CB    . LEU A 1 53  ? 56.469 -3.882  -4.904  1.00 37.62  ? 32  LEU A CB    1 
ATOM   191  C  CG    . LEU A 1 53  ? 57.056 -4.230  -3.544  1.00 41.31  ? 32  LEU A CG    1 
ATOM   192  C  CD1   . LEU A 1 53  ? 58.438 -4.846  -3.678  1.00 43.48  ? 32  LEU A CD1   1 
ATOM   193  C  CD2   . LEU A 1 53  ? 57.120 -2.971  -2.697  1.00 43.33  ? 32  LEU A CD2   1 
ATOM   194  N  N     . VAL A 1 54  ? 54.601 -6.607  -5.915  1.00 30.26  ? 33  VAL A N     1 
ATOM   195  C  CA    . VAL A 1 54  ? 53.227 -7.150  -6.151  1.00 31.91  ? 33  VAL A CA    1 
ATOM   196  C  C     . VAL A 1 54  ? 52.521 -7.299  -4.800  1.00 31.71  ? 33  VAL A C     1 
ATOM   197  O  O     . VAL A 1 54  ? 53.012 -8.051  -3.956  1.00 31.39  ? 33  VAL A O     1 
ATOM   198  C  CB    . VAL A 1 54  ? 53.250 -8.494  -6.904  1.00 32.34  ? 33  VAL A CB    1 
ATOM   199  C  CG1   . VAL A 1 54  ? 51.841 -9.068  -7.042  1.00 33.19  ? 33  VAL A CG1   1 
ATOM   200  C  CG2   . VAL A 1 54  ? 53.904 -8.360  -8.266  1.00 31.17  ? 33  VAL A CG2   1 
ATOM   201  N  N     . LEU A 1 55  ? 51.431 -6.566  -4.585  1.00 32.48  ? 34  LEU A N     1 
ATOM   202  C  CA    . LEU A 1 55  ? 50.698 -6.594  -3.297  1.00 32.12  ? 34  LEU A CA    1 
ATOM   203  C  C     . LEU A 1 55  ? 49.405 -7.383  -3.504  1.00 32.59  ? 34  LEU A C     1 
ATOM   204  O  O     . LEU A 1 55  ? 48.615 -6.988  -4.383  1.00 36.52  ? 34  LEU A O     1 
ATOM   205  C  CB    . LEU A 1 55  ? 50.435 -5.150  -2.867  1.00 35.75  ? 34  LEU A CB    1 
ATOM   206  C  CG    . LEU A 1 55  ? 51.672 -4.275  -2.686  1.00 36.64  ? 34  LEU A CG    1 
ATOM   207  C  CD1   . LEU A 1 55  ? 51.270 -2.837  -2.380  1.00 38.57  ? 34  LEU A CD1   1 
ATOM   208  C  CD2   . LEU A 1 55  ? 52.575 -4.823  -1.599  1.00 36.05  ? 34  LEU A CD2   1 
ATOM   209  N  N     . GLU A 1 56  ? 49.230 -8.482  -2.778  1.00 29.70  ? 35  GLU A N     1 
ATOM   210  C  CA    . GLU A 1 56  ? 48.096 -9.422  -2.950  1.00 29.77  ? 35  GLU A CA    1 
ATOM   211  C  C     . GLU A 1 56  ? 47.323 -9.549  -1.626  1.00 28.96  ? 35  GLU A C     1 
ATOM   212  O  O     . GLU A 1 56  ? 47.986 -9.719  -0.576  1.00 29.51  ? 35  GLU A O     1 
ATOM   213  C  CB    . GLU A 1 56  ? 48.685 -10.750 -3.420  1.00 30.07  ? 35  GLU A CB    1 
ATOM   214  C  CG    . GLU A 1 56  ? 47.704 -11.904 -3.410  1.00 29.14  ? 35  GLU A CG    1 
ATOM   215  C  CD    . GLU A 1 56  ? 46.412 -11.735 -4.184  1.00 30.91  ? 35  GLU A CD    1 
ATOM   216  O  OE1   . GLU A 1 56  ? 46.456 -11.228 -5.321  1.00 27.98  ? 35  GLU A OE1   1 
ATOM   217  O  OE2   . GLU A 1 56  ? 45.336 -12.141 -3.637  1.00 37.39  ? 35  GLU A OE2   1 
ATOM   218  N  N     . ALA A 1 57  ? 45.986 -9.467  -1.647  1.00 27.00  ? 36  ALA A N     1 
ATOM   219  C  CA    . ALA A 1 57  ? 45.126 -9.471  -0.425  1.00 27.90  ? 36  ALA A CA    1 
ATOM   220  C  C     . ALA A 1 57  ? 45.058 -10.862 0.233   1.00 26.85  ? 36  ALA A C     1 
ATOM   221  O  O     . ALA A 1 57  ? 44.939 -10.940 1.467   1.00 26.85  ? 36  ALA A O     1 
ATOM   222  C  CB    . ALA A 1 57  ? 43.741 -9.018  -0.776  1.00 28.31  ? 36  ALA A CB    1 
ATOM   223  N  N     . ARG A 1 58  ? 45.049 -11.921 -0.558  1.00 25.16  ? 37  ARG A N     1 
ATOM   224  C  CA    . ARG A 1 58  ? 44.953 -13.305 -0.035  1.00 28.17  ? 37  ARG A CA    1 
ATOM   225  C  C     . ARG A 1 58  ? 46.325 -13.780 0.440   1.00 29.48  ? 37  ARG A C     1 
ATOM   226  O  O     . ARG A 1 58  ? 47.315 -13.142 0.161   1.00 28.25  ? 37  ARG A O     1 
ATOM   227  C  CB    . ARG A 1 58  ? 44.470 -14.270 -1.107  1.00 26.79  ? 37  ARG A CB    1 
ATOM   228  C  CG    . ARG A 1 58  ? 43.012 -14.057 -1.460  1.00 31.35  ? 37  ARG A CG    1 
ATOM   229  C  CD    . ARG A 1 58  ? 42.627 -14.927 -2.621  1.00 31.48  ? 37  ARG A CD    1 
ATOM   230  N  NE    . ARG A 1 58  ? 41.183 -15.001 -2.840  1.00 33.80  ? 37  ARG A NE    1 
ATOM   231  C  CZ    . ARG A 1 58  ? 40.520 -14.520 -3.886  1.00 33.82  ? 37  ARG A CZ    1 
ATOM   232  N  NH1   . ARG A 1 58  ? 41.134 -13.849 -4.850  1.00 35.78  ? 37  ARG A NH1   1 
ATOM   233  N  NH2   . ARG A 1 58  ? 39.218 -14.711 -3.964  1.00 38.42  ? 37  ARG A NH2   1 
ATOM   234  N  N     . ASP A 1 59  ? 46.348 -14.909 1.117   1.00 31.58  ? 38  ASP A N     1 
ATOM   235  C  CA    . ASP A 1 59  ? 47.595 -15.562 1.566   1.00 32.17  ? 38  ASP A CA    1 
ATOM   236  C  C     . ASP A 1 59  ? 48.135 -16.457 0.435   1.00 30.47  ? 38  ASP A C     1 
ATOM   237  O  O     . ASP A 1 59  ? 49.045 -17.232 0.698   1.00 33.66  ? 38  ASP A O     1 
ATOM   238  C  CB    . ASP A 1 59  ? 47.298 -16.294 2.870   1.00 29.80  ? 38  ASP A CB    1 
ATOM   239  C  CG    . ASP A 1 59  ? 46.396 -17.498 2.688   1.00 33.90  ? 38  ASP A CG    1 
ATOM   240  O  OD1   . ASP A 1 59  ? 45.928 -17.682 1.567   1.00 38.95  ? 38  ASP A OD1   1 
ATOM   241  O  OD2   . ASP A 1 59  ? 46.181 -18.267 3.677   1.00 36.20  ? 38  ASP A OD2   1 
ATOM   242  N  N     . ARG A 1 60  ? 47.636 -16.325 -0.793  1.00 30.99  ? 39  ARG A N     1 
ATOM   243  C  CA    . ARG A 1 60  ? 48.034 -17.168 -1.957  1.00 31.77  ? 39  ARG A CA    1 
ATOM   244  C  C     . ARG A 1 60  ? 47.962 -16.358 -3.246  1.00 32.33  ? 39  ARG A C     1 
ATOM   245  O  O     . ARG A 1 60  ? 47.205 -15.334 -3.280  1.00 32.54  ? 39  ARG A O     1 
ATOM   246  C  CB    . ARG A 1 60  ? 47.092 -18.369 -2.125  1.00 33.86  ? 39  ARG A CB    1 
ATOM   247  C  CG    . ARG A 1 60  ? 45.640 -17.976 -2.380  1.00 34.97  ? 39  ARG A CG    1 
ATOM   248  C  CD    . ARG A 1 60  ? 44.741 -19.181 -2.603  1.00 35.85  ? 39  ARG A CD    1 
ATOM   249  N  NE    . ARG A 1 60  ? 43.433 -18.735 -3.064  1.00 33.40  ? 39  ARG A NE    1 
ATOM   250  C  CZ    . ARG A 1 60  ? 43.106 -18.498 -4.329  1.00 35.61  ? 39  ARG A CZ    1 
ATOM   251  N  NH1   . ARG A 1 60  ? 43.991 -18.649 -5.306  1.00 35.85  ? 39  ARG A NH1   1 
ATOM   252  N  NH2   . ARG A 1 60  ? 41.882 -18.085 -4.621  1.00 36.78  ? 39  ARG A NH2   1 
ATOM   253  N  N     . VAL A 1 61  ? 48.651 -16.824 -4.295  1.00 31.03  ? 40  VAL A N     1 
ATOM   254  C  CA    . VAL A 1 61  ? 48.504 -16.252 -5.667  1.00 28.62  ? 40  VAL A CA    1 
ATOM   255  C  C     . VAL A 1 61  ? 47.376 -16.992 -6.392  1.00 26.73  ? 40  VAL A C     1 
ATOM   256  O  O     . VAL A 1 61  ? 46.904 -18.010 -5.854  1.00 31.30  ? 40  VAL A O     1 
ATOM   257  C  CB    . VAL A 1 61  ? 49.833 -16.282 -6.442  1.00 31.05  ? 40  VAL A CB    1 
ATOM   258  C  CG1   . VAL A 1 61  ? 50.934 -15.552 -5.710  1.00 30.38  ? 40  VAL A CG1   1 
ATOM   259  C  CG2   . VAL A 1 61  ? 50.284 -17.686 -6.806  1.00 31.96  ? 40  VAL A CG2   1 
ATOM   260  N  N     . GLY A 1 62  ? 46.930 -16.495 -7.552  1.00 27.22  ? 41  GLY A N     1 
ATOM   261  C  CA    . GLY A 1 62  ? 46.000 -17.215 -8.449  1.00 27.56  ? 41  GLY A CA    1 
ATOM   262  C  C     . GLY A 1 62  ? 44.656 -16.536 -8.669  1.00 27.72  ? 41  GLY A C     1 
ATOM   263  O  O     . GLY A 1 62  ? 44.043 -16.770 -9.746  1.00 29.96  ? 41  GLY A O     1 
ATOM   264  N  N     . GLY A 1 63  ? 44.163 -15.783 -7.684  1.00 29.15  ? 42  GLY A N     1 
ATOM   265  C  CA    . GLY A 1 63  ? 42.872 -15.060 -7.747  1.00 27.75  ? 42  GLY A CA    1 
ATOM   266  C  C     . GLY A 1 63  ? 41.707 -15.995 -8.056  1.00 27.32  ? 42  GLY A C     1 
ATOM   267  O  O     . GLY A 1 63  ? 41.404 -16.871 -7.206  1.00 27.21  ? 42  GLY A O     1 
ATOM   268  N  N     . ARG A 1 64  ? 41.108 -15.866 -9.243  1.00 25.88  ? 43  ARG A N     1 
ATOM   269  C  CA    . ARG A 1 64  ? 39.929 -16.669 -9.663  1.00 25.83  ? 43  ARG A CA    1 
ATOM   270  C  C     . ARG A 1 64  ? 40.335 -18.078 -10.128 1.00 28.59  ? 43  ARG A C     1 
ATOM   271  O  O     . ARG A 1 64  ? 39.460 -18.832 -10.580 1.00 30.19  ? 43  ARG A O     1 
ATOM   272  C  CB    . ARG A 1 64  ? 39.161 -15.942 -10.759 1.00 25.46  ? 43  ARG A CB    1 
ATOM   273  C  CG    . ARG A 1 64  ? 38.284 -14.815 -10.246 1.00 28.14  ? 43  ARG A CG    1 
ATOM   274  C  CD    . ARG A 1 64  ? 37.672 -14.030 -11.383 1.00 27.04  ? 43  ARG A CD    1 
ATOM   275  N  NE    . ARG A 1 64  ? 38.455 -12.839 -11.631 1.00 27.31  ? 43  ARG A NE    1 
ATOM   276  C  CZ    . ARG A 1 64  ? 38.094 -11.869 -12.468 1.00 29.93  ? 43  ARG A CZ    1 
ATOM   277  N  NH1   . ARG A 1 64  ? 36.986 -11.982 -13.190 1.00 29.41  ? 43  ARG A NH1   1 
ATOM   278  N  NH2   . ARG A 1 64  ? 38.851 -10.794 -12.590 1.00 30.58  ? 43  ARG A NH2   1 
ATOM   279  N  N     . THR A 1 65  ? 41.611 -18.431 -10.057 1.00 28.20  ? 44  THR A N     1 
ATOM   280  C  CA    . THR A 1 65  ? 42.072 -19.837 -10.103 1.00 29.11  ? 44  THR A CA    1 
ATOM   281  C  C     . THR A 1 65  ? 42.528 -20.178 -8.690  1.00 31.38  ? 44  THR A C     1 
ATOM   282  O  O     . THR A 1 65  ? 43.144 -19.305 -8.035  1.00 30.15  ? 44  THR A O     1 
ATOM   283  C  CB    . THR A 1 65  ? 43.162 -20.052 -11.159 1.00 28.07  ? 44  THR A CB    1 
ATOM   284  O  OG1   . THR A 1 65  ? 44.344 -19.380 -10.718 1.00 28.32  ? 44  THR A OG1   1 
ATOM   285  C  CG2   . THR A 1 65  ? 42.711 -19.566 -12.518 1.00 28.32  ? 44  THR A CG2   1 
ATOM   286  N  N     . CYS A 1 66  ? 42.200 -21.388 -8.260  1.00 31.75  ? 45  CYS A N     1 
ATOM   287  C  CA    . CYS A 1 66  ? 42.344 -21.884 -6.879  1.00 32.40  ? 45  CYS A CA    1 
ATOM   288  C  C     . CYS A 1 66  ? 42.240 -23.414 -6.902  1.00 33.04  ? 45  CYS A C     1 
ATOM   289  O  O     . CYS A 1 66  ? 41.190 -23.931 -7.363  1.00 29.84  ? 45  CYS A O     1 
ATOM   290  C  CB    . CYS A 1 66  ? 41.263 -21.305 -5.987  1.00 31.27  ? 45  CYS A CB    1 
ATOM   291  S  SG    . CYS A 1 66  ? 41.519 -21.712 -4.240  1.00 34.48  ? 45  CYS A SG    1 
ATOM   292  N  N     . THR A 1 67  ? 43.282 -24.092 -6.422  1.00 29.67  ? 46  THR A N     1 
ATOM   293  C  CA    . THR A 1 67  ? 43.447 -25.552 -6.562  1.00 31.85  ? 46  THR A CA    1 
ATOM   294  C  C     . THR A 1 67  ? 43.681 -26.087 -5.159  1.00 30.52  ? 46  THR A C     1 
ATOM   295  O  O     . THR A 1 67  ? 44.591 -25.571 -4.528  1.00 28.27  ? 46  THR A O     1 
ATOM   296  C  CB    . THR A 1 67  ? 44.591 -25.911 -7.536  1.00 33.95  ? 46  THR A CB    1 
ATOM   297  O  OG1   . THR A 1 67  ? 44.414 -25.293 -8.815  1.00 31.37  ? 46  THR A OG1   1 
ATOM   298  C  CG2   . THR A 1 67  ? 44.709 -27.407 -7.753  1.00 33.49  ? 46  THR A CG2   1 
ATOM   299  N  N     . GLU A 1 68  ? 42.868 -27.042 -4.697  1.00 30.34  ? 47  GLU A N     1 
ATOM   300  C  CA    . GLU A 1 68  ? 43.077 -27.724 -3.397  1.00 31.67  ? 47  GLU A CA    1 
ATOM   301  C  C     . GLU A 1 68  ? 43.209 -29.233 -3.600  1.00 31.18  ? 47  GLU A C     1 
ATOM   302  O  O     . GLU A 1 68  ? 42.659 -29.758 -4.587  1.00 30.96  ? 47  GLU A O     1 
ATOM   303  C  CB    . GLU A 1 68  ? 41.897 -27.472 -2.471  1.00 35.75  ? 47  GLU A CB    1 
ATOM   304  C  CG    . GLU A 1 68  ? 41.991 -26.152 -1.728  1.00 40.65  ? 47  GLU A CG    1 
ATOM   305  C  CD    . GLU A 1 68  ? 40.671 -25.684 -1.143  1.00 44.92  ? 47  GLU A CD    1 
ATOM   306  O  OE1   . GLU A 1 68  ? 39.786 -26.550 -0.847  1.00 38.65  ? 47  GLU A OE1   1 
ATOM   307  O  OE2   . GLU A 1 68  ? 40.521 -24.448 -1.017  1.00 50.09  ? 47  GLU A OE2   1 
ATOM   308  N  N     . GLU A 1 69  ? 43.870 -29.902 -2.662  1.00 31.85  ? 48  GLU A N     1 
ATOM   309  C  CA    . GLU A 1 69  ? 44.112 -31.371 -2.704  1.00 36.89  ? 48  GLU A CA    1 
ATOM   310  C  C     . GLU A 1 69  ? 43.025 -32.060 -1.885  1.00 31.26  ? 48  GLU A C     1 
ATOM   311  O  O     . GLU A 1 69  ? 42.961 -31.806 -0.682  1.00 30.48  ? 48  GLU A O     1 
ATOM   312  C  CB    . GLU A 1 69  ? 45.507 -31.695 -2.156  1.00 43.63  ? 48  GLU A CB    1 
ATOM   313  C  CG    . GLU A 1 69  ? 45.933 -33.151 -2.329  1.00 56.64  ? 48  GLU A CG    1 
ATOM   314  C  CD    . GLU A 1 69  ? 46.583 -33.542 -3.658  1.00 72.95  ? 48  GLU A CD    1 
ATOM   315  O  OE1   . GLU A 1 69  ? 46.868 -32.625 -4.501  1.00 76.09  ? 48  GLU A OE1   1 
ATOM   316  O  OE2   . GLU A 1 69  ? 46.822 -34.777 -3.853  1.00 69.70  ? 48  GLU A OE2   1 
ATOM   317  N  N     . HIS A 1 70  ? 42.190 -32.895 -2.508  1.00 34.16  ? 49  HIS A N     1 
ATOM   318  C  CA    . HIS A 1 70  ? 41.212 -33.774 -1.810  1.00 36.18  ? 49  HIS A CA    1 
ATOM   319  C  C     . HIS A 1 70  ? 41.180 -35.153 -2.464  1.00 36.10  ? 49  HIS A C     1 
ATOM   320  O  O     . HIS A 1 70  ? 41.254 -35.212 -3.675  1.00 40.40  ? 49  HIS A O     1 
ATOM   321  C  CB    . HIS A 1 70  ? 39.819 -33.156 -1.862  1.00 38.13  ? 49  HIS A CB    1 
ATOM   322  C  CG    . HIS A 1 70  ? 39.713 -31.825 -1.210  1.00 36.87  ? 49  HIS A CG    1 
ATOM   323  N  ND1   . HIS A 1 70  ? 39.993 -30.645 -1.880  1.00 38.14  ? 49  HIS A ND1   1 
ATOM   324  C  CD2   . HIS A 1 70  ? 39.318 -31.476 0.030   1.00 42.09  ? 49  HIS A CD2   1 
ATOM   325  C  CE1   . HIS A 1 70  ? 39.799 -29.627 -1.066  1.00 37.55  ? 49  HIS A CE1   1 
ATOM   326  N  NE2   . HIS A 1 70  ? 39.385 -30.109 0.111   1.00 40.69  ? 49  HIS A NE2   1 
ATOM   327  N  N     . HIS A 1 71  ? 41.084 -36.229 -1.695  1.00 35.54  ? 50  HIS A N     1 
ATOM   328  C  CA    . HIS A 1 71  ? 40.950 -37.603 -2.253  1.00 37.17  ? 50  HIS A CA    1 
ATOM   329  C  C     . HIS A 1 71  ? 42.095 -37.911 -3.235  1.00 36.58  ? 50  HIS A C     1 
ATOM   330  O  O     . HIS A 1 71  ? 41.804 -38.415 -4.349  1.00 35.81  ? 50  HIS A O     1 
ATOM   331  C  CB    . HIS A 1 71  ? 39.563 -37.743 -2.891  1.00 37.02  ? 50  HIS A CB    1 
ATOM   332  C  CG    . HIS A 1 71  ? 38.487 -37.472 -1.896  1.00 39.08  ? 50  HIS A CG    1 
ATOM   333  N  ND1   . HIS A 1 71  ? 37.668 -36.357 -1.973  1.00 40.79  ? 50  HIS A ND1   1 
ATOM   334  C  CD2   . HIS A 1 71  ? 38.160 -38.110 -0.754  1.00 36.09  ? 50  HIS A CD2   1 
ATOM   335  C  CE1   . HIS A 1 71  ? 36.892 -36.325 -0.915  1.00 38.33  ? 50  HIS A CE1   1 
ATOM   336  N  NE2   . HIS A 1 71  ? 37.180 -37.381 -0.157  1.00 32.98  ? 50  HIS A NE2   1 
ATOM   337  N  N     . GLY A 1 72  ? 43.327 -37.546 -2.865  1.00 34.16  ? 51  GLY A N     1 
ATOM   338  C  CA    . GLY A 1 72  ? 44.568 -37.822 -3.618  1.00 36.43  ? 51  GLY A CA    1 
ATOM   339  C  C     . GLY A 1 72  ? 44.622 -37.193 -5.010  1.00 40.98  ? 51  GLY A C     1 
ATOM   340  O  O     . GLY A 1 72  ? 45.445 -37.678 -5.819  1.00 43.83  ? 51  GLY A O     1 
ATOM   341  N  N     . THR A 1 73  ? 43.862 -36.119 -5.293  1.00 39.96  ? 52  THR A N     1 
ATOM   342  C  CA    . THR A 1 73  ? 43.907 -35.409 -6.607  1.00 37.33  ? 52  THR A CA    1 
ATOM   343  C  C     . THR A 1 73  ? 43.665 -33.906 -6.415  1.00 36.79  ? 52  THR A C     1 
ATOM   344  O  O     . THR A 1 73  ? 43.361 -33.461 -5.286  1.00 37.61  ? 52  THR A O     1 
ATOM   345  C  CB    . THR A 1 73  ? 42.943 -36.045 -7.628  1.00 41.53  ? 52  THR A CB    1 
ATOM   346  O  OG1   . THR A 1 73  ? 43.265 -35.583 -8.948  1.00 39.29  ? 52  THR A OG1   1 
ATOM   347  C  CG2   . THR A 1 73  ? 41.478 -35.768 -7.334  1.00 41.52  ? 52  THR A CG2   1 
ATOM   348  N  N     . TRP A 1 74  ? 43.825 -33.145 -7.488  1.00 31.73  ? 53  TRP A N     1 
ATOM   349  C  CA    . TRP A 1 74  ? 43.633 -31.673 -7.512  1.00 33.80  ? 53  TRP A CA    1 
ATOM   350  C  C     . TRP A 1 74  ? 42.158 -31.359 -7.761  1.00 34.21  ? 53  TRP A C     1 
ATOM   351  O  O     . TRP A 1 74  ? 41.554 -32.017 -8.654  1.00 30.41  ? 53  TRP A O     1 
ATOM   352  C  CB    . TRP A 1 74  ? 44.510 -31.005 -8.583  1.00 33.05  ? 53  TRP A CB    1 
ATOM   353  C  CG    . TRP A 1 74  ? 44.356 -31.594 -9.952  1.00 32.18  ? 53  TRP A CG    1 
ATOM   354  C  CD1   . TRP A 1 74  ? 43.540 -31.149 -10.948 1.00 33.40  ? 53  TRP A CD1   1 
ATOM   355  C  CD2   . TRP A 1 74  ? 45.043 -32.744 -10.487 1.00 33.79  ? 53  TRP A CD2   1 
ATOM   356  N  NE1   . TRP A 1 74  ? 43.681 -31.922 -12.070 1.00 33.21  ? 53  TRP A NE1   1 
ATOM   357  C  CE2   . TRP A 1 74  ? 44.573 -32.926 -11.812 1.00 31.98  ? 53  TRP A CE2   1 
ATOM   358  C  CE3   . TRP A 1 74  ? 46.010 -33.634 -9.986  1.00 35.69  ? 53  TRP A CE3   1 
ATOM   359  C  CZ2   . TRP A 1 74  ? 45.031 -33.958 -12.628 1.00 31.26  ? 53  TRP A CZ2   1 
ATOM   360  C  CZ3   . TRP A 1 74  ? 46.465 -34.659 -10.796 1.00 32.72  ? 53  TRP A CZ3   1 
ATOM   361  C  CH2   . TRP A 1 74  ? 45.976 -34.817 -12.096 1.00 33.19  ? 53  TRP A CH2   1 
ATOM   362  N  N     . ILE A 1 75  ? 41.628 -30.382 -7.010  1.00 32.49  ? 54  ILE A N     1 
ATOM   363  C  CA    . ILE A 1 75  ? 40.272 -29.794 -7.210  1.00 32.84  ? 54  ILE A CA    1 
ATOM   364  C  C     . ILE A 1 75  ? 40.450 -28.339 -7.647  1.00 33.18  ? 54  ILE A C     1 
ATOM   365  O  O     . ILE A 1 75  ? 40.876 -27.514 -6.804  1.00 34.56  ? 54  ILE A O     1 
ATOM   366  C  CB    . ILE A 1 75  ? 39.400 -29.901 -5.938  1.00 32.84  ? 54  ILE A CB    1 
ATOM   367  C  CG1   . ILE A 1 75  ? 39.347 -31.332 -5.394  1.00 31.46  ? 54  ILE A CG1   1 
ATOM   368  C  CG2   . ILE A 1 75  ? 38.006 -29.348 -6.207  1.00 31.86  ? 54  ILE A CG2   1 
ATOM   369  C  CD1   . ILE A 1 75  ? 38.811 -32.342 -6.382  1.00 31.97  ? 54  ILE A CD1   1 
ATOM   370  N  N     . ASP A 1 76  ? 40.150 -28.056 -8.921  1.00 32.40  ? 55  ASP A N     1 
ATOM   371  C  CA    . ASP A 1 76  ? 40.070 -26.677 -9.466  1.00 33.52  ? 55  ASP A CA    1 
ATOM   372  C  C     . ASP A 1 76  ? 38.739 -26.049 -9.006  1.00 33.29  ? 55  ASP A C     1 
ATOM   373  O  O     . ASP A 1 76  ? 37.657 -26.313 -9.601  1.00 32.15  ? 55  ASP A O     1 
ATOM   374  C  CB    . ASP A 1 76  ? 40.329 -26.631 -10.980 1.00 31.24  ? 55  ASP A CB    1 
ATOM   375  C  CG    . ASP A 1 76  ? 41.808 -26.686 -11.353 1.00 31.24  ? 55  ASP A CG    1 
ATOM   376  O  OD1   . ASP A 1 76  ? 42.644 -25.980 -10.709 1.00 32.47  ? 55  ASP A OD1   1 
ATOM   377  O  OD2   . ASP A 1 76  ? 42.120 -27.422 -12.283 1.00 29.09  ? 55  ASP A OD2   1 
ATOM   378  N  N     . LEU A 1 77  ? 38.811 -25.231 -7.961  1.00 29.82  ? 56  LEU A N     1 
ATOM   379  C  CA    . LEU A 1 77  ? 37.618 -24.513 -7.478  1.00 31.09  ? 56  LEU A CA    1 
ATOM   380  C  C     . LEU A 1 77  ? 37.347 -23.327 -8.388  1.00 28.65  ? 56  LEU A C     1 
ATOM   381  O  O     . LEU A 1 77  ? 36.175 -22.951 -8.465  1.00 26.65  ? 56  LEU A O     1 
ATOM   382  C  CB    . LEU A 1 77  ? 37.841 -24.112 -6.026  1.00 34.39  ? 56  LEU A CB    1 
ATOM   383  C  CG    . LEU A 1 77  ? 37.932 -25.330 -5.110  1.00 37.53  ? 56  LEU A CG    1 
ATOM   384  C  CD1   . LEU A 1 77  ? 38.750 -25.012 -3.882  1.00 44.56  ? 56  LEU A CD1   1 
ATOM   385  C  CD2   . LEU A 1 77  ? 36.553 -25.819 -4.740  1.00 39.38  ? 56  LEU A CD2   1 
ATOM   386  N  N     . GLY A 1 78  ? 38.380 -22.818 -9.071  1.00 29.38  ? 57  GLY A N     1 
ATOM   387  C  CA    . GLY A 1 78  ? 38.269 -21.705 -10.033 1.00 31.01  ? 57  GLY A CA    1 
ATOM   388  C  C     . GLY A 1 78  ? 38.434 -22.139 -11.485 1.00 31.12  ? 57  GLY A C     1 
ATOM   389  O  O     . GLY A 1 78  ? 38.048 -23.272 -11.835 1.00 29.68  ? 57  GLY A O     1 
ATOM   390  N  N     . GLY A 1 79  ? 38.980 -21.256 -12.315 1.00 29.55  ? 58  GLY A N     1 
ATOM   391  C  CA    . GLY A 1 79  ? 39.265 -21.562 -13.729 1.00 31.71  ? 58  GLY A CA    1 
ATOM   392  C  C     . GLY A 1 79  ? 40.035 -22.856 -13.883 1.00 28.93  ? 58  GLY A C     1 
ATOM   393  O  O     . GLY A 1 79  ? 40.998 -23.043 -13.125 1.00 28.41  ? 58  GLY A O     1 
ATOM   394  N  N     . GLN A 1 80  ? 39.641 -23.718 -14.824 1.00 30.03  ? 59  GLN A N     1 
ATOM   395  C  CA    . GLN A 1 80  ? 40.304 -25.041 -14.985 1.00 32.47  ? 59  GLN A CA    1 
ATOM   396  C  C     . GLN A 1 80  ? 40.631 -25.378 -16.452 1.00 32.03  ? 59  GLN A C     1 
ATOM   397  O  O     . GLN A 1 80  ? 41.486 -26.254 -16.640 1.00 26.95  ? 59  GLN A O     1 
ATOM   398  C  CB    . GLN A 1 80  ? 39.457 -26.121 -14.330 1.00 30.25  ? 59  GLN A CB    1 
ATOM   399  C  CG    . GLN A 1 80  ? 38.239 -26.536 -15.128 1.00 31.59  ? 59  GLN A CG    1 
ATOM   400  C  CD    . GLN A 1 80  ? 37.484 -27.624 -14.395 1.00 33.79  ? 59  GLN A CD    1 
ATOM   401  O  OE1   . GLN A 1 80  ? 37.506 -27.694 -13.166 1.00 35.16  ? 59  GLN A OE1   1 
ATOM   402  N  NE2   . GLN A 1 80  ? 36.837 -28.503 -15.143 1.00 35.92  ? 59  GLN A NE2   1 
ATOM   403  N  N     . TRP A 1 81  ? 39.958 -24.757 -17.428 1.00 31.05  ? 60  TRP A N     1 
ATOM   404  C  CA    . TRP A 1 81  ? 40.001 -25.157 -18.859 1.00 31.27  ? 60  TRP A CA    1 
ATOM   405  C  C     . TRP A 1 81  ? 40.819 -24.176 -19.700 1.00 32.47  ? 60  TRP A C     1 
ATOM   406  O  O     . TRP A 1 81  ? 40.727 -22.944 -19.456 1.00 34.54  ? 60  TRP A O     1 
ATOM   407  C  CB    . TRP A 1 81  ? 38.615 -25.279 -19.457 1.00 30.62  ? 60  TRP A CB    1 
ATOM   408  C  CG    . TRP A 1 81  ? 37.863 -26.515 -19.103 1.00 29.98  ? 60  TRP A CG    1 
ATOM   409  C  CD1   . TRP A 1 81  ? 38.214 -27.808 -19.351 1.00 29.68  ? 60  TRP A CD1   1 
ATOM   410  C  CD2   . TRP A 1 81  ? 36.560 -26.559 -18.494 1.00 32.45  ? 60  TRP A CD2   1 
ATOM   411  N  NE1   . TRP A 1 81  ? 37.220 -28.661 -18.940 1.00 29.22  ? 60  TRP A NE1   1 
ATOM   412  C  CE2   . TRP A 1 81  ? 36.201 -27.926 -18.392 1.00 30.87  ? 60  TRP A CE2   1 
ATOM   413  C  CE3   . TRP A 1 81  ? 35.663 -25.583 -18.033 1.00 31.16  ? 60  TRP A CE3   1 
ATOM   414  C  CZ2   . TRP A 1 81  ? 34.992 -28.327 -17.825 1.00 31.04  ? 60  TRP A CZ2   1 
ATOM   415  C  CZ3   . TRP A 1 81  ? 34.453 -25.983 -17.503 1.00 30.90  ? 60  TRP A CZ3   1 
ATOM   416  C  CH2   . TRP A 1 81  ? 34.131 -27.340 -17.390 1.00 30.06  ? 60  TRP A CH2   1 
ATOM   417  N  N     . ILE A 1 82  ? 41.572 -24.734 -20.662 1.00 32.11  ? 61  ILE A N     1 
ATOM   418  C  CA    . ILE A 1 82  ? 42.155 -24.003 -21.832 1.00 33.21  ? 61  ILE A CA    1 
ATOM   419  C  C     . ILE A 1 82  ? 41.750 -24.747 -23.114 1.00 32.77  ? 61  ILE A C     1 
ATOM   420  O  O     . ILE A 1 82  ? 41.498 -25.979 -23.064 1.00 30.16  ? 61  ILE A O     1 
ATOM   421  C  CB    . ILE A 1 82  ? 43.679 -23.847 -21.677 1.00 34.28  ? 61  ILE A CB    1 
ATOM   422  C  CG1   . ILE A 1 82  ? 44.424 -25.185 -21.727 1.00 41.05  ? 61  ILE A CG1   1 
ATOM   423  C  CG2   . ILE A 1 82  ? 44.014 -23.111 -20.391 1.00 35.25  ? 61  ILE A CG2   1 
ATOM   424  C  CD1   . ILE A 1 82  ? 45.951 -25.036 -21.821 1.00 43.74  ? 61  ILE A CD1   1 
ATOM   425  N  N     . GLY A 1 83  ? 41.682 -24.020 -24.219 1.00 31.05  ? 62  GLY A N     1 
ATOM   426  C  CA    . GLY A 1 83  ? 41.365 -24.586 -25.534 1.00 34.48  ? 62  GLY A CA    1 
ATOM   427  C  C     . GLY A 1 83  ? 42.196 -23.967 -26.645 1.00 37.26  ? 62  GLY A C     1 
ATOM   428  O  O     . GLY A 1 83  ? 42.944 -23.014 -26.434 1.00 39.59  ? 62  GLY A O     1 
ATOM   429  N  N     . PRO A 1 84  ? 42.055 -24.506 -27.870 1.00 42.09  ? 63  PRO A N     1 
ATOM   430  C  CA    . PRO A 1 84  ? 42.647 -23.911 -29.066 1.00 44.24  ? 63  PRO A CA    1 
ATOM   431  C  C     . PRO A 1 84  ? 42.124 -22.491 -29.279 1.00 39.81  ? 63  PRO A C     1 
ATOM   432  O  O     . PRO A 1 84  ? 40.966 -22.238 -28.952 1.00 45.77  ? 63  PRO A O     1 
ATOM   433  C  CB    . PRO A 1 84  ? 42.165 -24.777 -30.239 1.00 44.88  ? 63  PRO A CB    1 
ATOM   434  C  CG    . PRO A 1 84  ? 41.001 -25.581 -29.663 1.00 46.22  ? 63  PRO A CG    1 
ATOM   435  C  CD    . PRO A 1 84  ? 41.289 -25.725 -28.177 1.00 48.72  ? 63  PRO A CD    1 
ATOM   436  N  N     . GLY A 1 85  ? 42.994 -21.632 -29.796 1.00 34.44  ? 64  GLY A N     1 
ATOM   437  C  CA    . GLY A 1 85  ? 42.780 -20.179 -29.886 1.00 36.07  ? 64  GLY A CA    1 
ATOM   438  C  C     . GLY A 1 85  ? 43.462 -19.435 -28.748 1.00 34.94  ? 64  GLY A C     1 
ATOM   439  O  O     . GLY A 1 85  ? 43.733 -18.239 -28.939 1.00 34.18  ? 64  GLY A O     1 
ATOM   440  N  N     . GLN A 1 86  ? 43.697 -20.095 -27.605 1.00 34.71  ? 65  GLN A N     1 
ATOM   441  C  CA    . GLN A 1 86  ? 44.166 -19.428 -26.357 1.00 37.52  ? 65  GLN A CA    1 
ATOM   442  C  C     . GLN A 1 86  ? 45.687 -19.583 -26.292 1.00 34.98  ? 65  GLN A C     1 
ATOM   443  O  O     . GLN A 1 86  ? 46.185 -20.459 -25.588 1.00 38.15  ? 65  GLN A O     1 
ATOM   444  C  CB    . GLN A 1 86  ? 43.472 -20.004 -25.120 1.00 36.54  ? 65  GLN A CB    1 
ATOM   445  C  CG    . GLN A 1 86  ? 41.990 -19.668 -24.995 1.00 36.43  ? 65  GLN A CG    1 
ATOM   446  C  CD    . GLN A 1 86  ? 41.342 -20.465 -23.883 1.00 36.96  ? 65  GLN A CD    1 
ATOM   447  O  OE1   . GLN A 1 86  ? 42.009 -21.172 -23.130 1.00 36.65  ? 65  GLN A OE1   1 
ATOM   448  N  NE2   . GLN A 1 86  ? 40.033 -20.347 -23.746 1.00 37.32  ? 65  GLN A NE2   1 
ATOM   449  N  N     . ASP A 1 87  ? 46.406 -18.762 -27.033 1.00 40.38  ? 66  ASP A N     1 
ATOM   450  C  CA    . ASP A 1 87  ? 47.823 -19.069 -27.345 1.00 43.58  ? 66  ASP A CA    1 
ATOM   451  C  C     . ASP A 1 87  ? 48.713 -18.533 -26.218 1.00 41.93  ? 66  ASP A C     1 
ATOM   452  O  O     . ASP A 1 87  ? 49.817 -19.077 -26.047 1.00 39.19  ? 66  ASP A O     1 
ATOM   453  C  CB    . ASP A 1 87  ? 48.194 -18.669 -28.778 1.00 45.45  ? 66  ASP A CB    1 
ATOM   454  C  CG    . ASP A 1 87  ? 47.681 -17.344 -29.295 1.00 50.10  ? 66  ASP A CG    1 
ATOM   455  O  OD1   . ASP A 1 87  ? 48.167 -16.302 -28.824 1.00 58.06  ? 66  ASP A OD1   1 
ATOM   456  O  OD2   . ASP A 1 87  ? 46.851 -17.374 -30.227 1.00 57.11  ? 66  ASP A OD2   1 
ATOM   457  N  N     . ARG A 1 88  ? 48.225 -17.578 -25.425 1.00 39.92  ? 67  ARG A N     1 
ATOM   458  C  CA    . ARG A 1 88  ? 49.016 -16.995 -24.316 1.00 40.08  ? 67  ARG A CA    1 
ATOM   459  C  C     . ARG A 1 88  ? 49.030 -17.985 -23.148 1.00 34.29  ? 67  ARG A C     1 
ATOM   460  O  O     . ARG A 1 88  ? 50.089 -18.188 -22.569 1.00 34.38  ? 67  ARG A O     1 
ATOM   461  C  CB    . ARG A 1 88  ? 48.495 -15.591 -24.029 1.00 40.44  ? 67  ARG A CB    1 
ATOM   462  C  CG    . ARG A 1 88  ? 48.733 -14.678 -25.222 1.00 50.57  ? 67  ARG A CG    1 
ATOM   463  C  CD    . ARG A 1 88  ? 47.990 -13.369 -25.200 1.00 59.53  ? 67  ARG A CD    1 
ATOM   464  N  NE    . ARG A 1 88  ? 46.560 -13.613 -25.051 1.00 75.21  ? 67  ARG A NE    1 
ATOM   465  C  CZ    . ARG A 1 88  ? 45.594 -13.259 -25.900 1.00 68.17  ? 67  ARG A CZ    1 
ATOM   466  N  NH1   . ARG A 1 88  ? 45.867 -12.602 -27.017 1.00 66.57  ? 67  ARG A NH1   1 
ATOM   467  N  NH2   . ARG A 1 88  ? 44.340 -13.556 -25.591 1.00 57.28  ? 67  ARG A NH2   1 
ATOM   468  N  N     . VAL A 1 89  ? 47.917 -18.620 -22.816 1.00 32.95  ? 68  VAL A N     1 
ATOM   469  C  CA    . VAL A 1 89  ? 47.931 -19.554 -21.660 1.00 32.51  ? 68  VAL A CA    1 
ATOM   470  C  C     . VAL A 1 89  ? 48.683 -20.813 -22.112 1.00 29.95  ? 68  VAL A C     1 
ATOM   471  O  O     . VAL A 1 89  ? 49.458 -21.346 -21.314 1.00 29.14  ? 68  VAL A O     1 
ATOM   472  C  CB    . VAL A 1 89  ? 46.531 -19.854 -21.074 1.00 34.26  ? 68  VAL A CB    1 
ATOM   473  C  CG1   . VAL A 1 89  ? 45.619 -20.586 -22.042 1.00 34.18  ? 68  VAL A CG1   1 
ATOM   474  C  CG2   . VAL A 1 89  ? 46.627 -20.662 -19.780 1.00 33.42  ? 68  VAL A CG2   1 
ATOM   475  N  N     . ALA A 1 90  ? 48.498 -21.257 -23.356 1.00 33.92  ? 69  ALA A N     1 
ATOM   476  C  CA    . ALA A 1 90  ? 49.175 -22.471 -23.895 1.00 36.26  ? 69  ALA A CA    1 
ATOM   477  C  C     . ALA A 1 90  ? 50.710 -22.305 -23.841 1.00 37.58  ? 69  ALA A C     1 
ATOM   478  O  O     . ALA A 1 90  ? 51.389 -23.235 -23.349 1.00 36.68  ? 69  ALA A O     1 
ATOM   479  C  CB    . ALA A 1 90  ? 48.677 -22.785 -25.279 1.00 35.44  ? 69  ALA A CB    1 
ATOM   480  N  N     . ALA A 1 91  ? 51.241 -21.167 -24.306 1.00 34.69  ? 70  ALA A N     1 
ATOM   481  C  CA    . ALA A 1 91  ? 52.680 -20.817 -24.253 1.00 35.13  ? 70  ALA A CA    1 
ATOM   482  C  C     . ALA A 1 91  ? 53.163 -20.705 -22.790 1.00 35.99  ? 70  ALA A C     1 
ATOM   483  O  O     . ALA A 1 91  ? 54.300 -21.113 -22.498 1.00 30.28  ? 70  ALA A O     1 
ATOM   484  C  CB    . ALA A 1 91  ? 52.928 -19.531 -25.011 1.00 34.96  ? 70  ALA A CB    1 
ATOM   485  N  N     . LEU A 1 92  ? 52.361 -20.148 -21.875 1.00 35.51  ? 71  LEU A N     1 
ATOM   486  C  CA    . LEU A 1 92  ? 52.810 -20.082 -20.467 1.00 33.69  ? 71  LEU A CA    1 
ATOM   487  C  C     . LEU A 1 92  ? 52.903 -21.513 -19.925 1.00 31.39  ? 71  LEU A C     1 
ATOM   488  O  O     . LEU A 1 92  ? 53.903 -21.814 -19.302 1.00 33.94  ? 71  LEU A O     1 
ATOM   489  C  CB    . LEU A 1 92  ? 51.868 -19.221 -19.626 1.00 39.96  ? 71  LEU A CB    1 
ATOM   490  C  CG    . LEU A 1 92  ? 52.340 -18.986 -18.187 1.00 41.23  ? 71  LEU A CG    1 
ATOM   491  C  CD1   . LEU A 1 92  ? 53.567 -18.070 -18.148 1.00 40.29  ? 71  LEU A CD1   1 
ATOM   492  C  CD2   . LEU A 1 92  ? 51.229 -18.393 -17.354 1.00 40.19  ? 71  LEU A CD2   1 
ATOM   493  N  N     . ALA A 1 93  ? 51.904 -22.365 -20.128 1.00 27.94  ? 72  ALA A N     1 
ATOM   494  C  CA    . ALA A 1 93  ? 51.913 -23.731 -19.563 1.00 30.77  ? 72  ALA A CA    1 
ATOM   495  C  C     . ALA A 1 93  ? 53.148 -24.484 -20.064 1.00 35.20  ? 72  ALA A C     1 
ATOM   496  O  O     . ALA A 1 93  ? 53.848 -25.064 -19.237 1.00 37.47  ? 72  ALA A O     1 
ATOM   497  C  CB    . ALA A 1 93  ? 50.660 -24.470 -19.913 1.00 32.15  ? 72  ALA A CB    1 
ATOM   498  N  N     . ALA A 1 94  ? 53.443 -24.408 -21.361 1.00 41.12  ? 73  ALA A N     1 
ATOM   499  C  CA    . ALA A 1 94  ? 54.590 -25.087 -22.023 1.00 42.59  ? 73  ALA A CA    1 
ATOM   500  C  C     . ALA A 1 94  ? 55.920 -24.615 -21.425 1.00 39.70  ? 73  ALA A C     1 
ATOM   501  O  O     . ALA A 1 94  ? 56.754 -25.479 -21.095 1.00 35.28  ? 73  ALA A O     1 
ATOM   502  C  CB    . ALA A 1 94  ? 54.547 -24.834 -23.516 1.00 42.68  ? 73  ALA A CB    1 
ATOM   503  N  N     . GLU A 1 95  ? 56.078 -23.298 -21.271 1.00 35.73  ? 74  GLU A N     1 
ATOM   504  C  CA    . GLU A 1 95  ? 57.314 -22.626 -20.780 1.00 36.61  ? 74  GLU A CA    1 
ATOM   505  C  C     . GLU A 1 95  ? 57.619 -23.014 -19.324 1.00 36.19  ? 74  GLU A C     1 
ATOM   506  O  O     . GLU A 1 95  ? 58.796 -23.189 -19.008 1.00 38.41  ? 74  GLU A O     1 
ATOM   507  C  CB    . GLU A 1 95  ? 57.128 -21.109 -20.926 1.00 35.32  ? 74  GLU A CB    1 
ATOM   508  C  CG    . GLU A 1 95  ? 58.079 -20.284 -20.085 1.00 39.76  ? 74  GLU A CG    1 
ATOM   509  C  CD    . GLU A 1 95  ? 57.729 -18.799 -20.007 1.00 45.04  ? 74  GLU A CD    1 
ATOM   510  O  OE1   . GLU A 1 95  ? 56.536 -18.453 -20.206 1.00 46.32  ? 74  GLU A OE1   1 
ATOM   511  O  OE2   . GLU A 1 95  ? 58.643 -17.986 -19.748 1.00 42.30  ? 74  GLU A OE2   1 
ATOM   512  N  N     . LEU A 1 96  ? 56.617 -23.075 -18.434 1.00 34.82  ? 75  LEU A N     1 
ATOM   513  C  CA    . LEU A 1 96  ? 56.839 -23.379 -16.994 1.00 32.93  ? 75  LEU A CA    1 
ATOM   514  C  C     . LEU A 1 96  ? 56.600 -24.869 -16.736 1.00 33.51  ? 75  LEU A C     1 
ATOM   515  O  O     . LEU A 1 96  ? 56.602 -25.254 -15.572 1.00 45.16  ? 75  LEU A O     1 
ATOM   516  C  CB    . LEU A 1 96  ? 55.925 -22.503 -16.132 1.00 31.82  ? 75  LEU A CB    1 
ATOM   517  C  CG    . LEU A 1 96  ? 55.957 -20.995 -16.407 1.00 30.51  ? 75  LEU A CG    1 
ATOM   518  C  CD1   . LEU A 1 96  ? 54.971 -20.287 -15.488 1.00 30.78  ? 75  LEU A CD1   1 
ATOM   519  C  CD2   . LEU A 1 96  ? 57.350 -20.413 -16.211 1.00 29.42  ? 75  LEU A CD2   1 
ATOM   520  N  N     . GLY A 1 97  ? 56.426 -25.668 -17.786 1.00 33.29  ? 76  GLY A N     1 
ATOM   521  C  CA    . GLY A 1 97  ? 56.524 -27.141 -17.743 1.00 36.05  ? 76  GLY A CA    1 
ATOM   522  C  C     . GLY A 1 97  ? 55.287 -27.777 -17.129 1.00 37.55  ? 76  GLY A C     1 
ATOM   523  O  O     . GLY A 1 97  ? 55.435 -28.752 -16.428 1.00 34.00  ? 76  GLY A O     1 
ATOM   524  N  N     . VAL A 1 98  ? 54.087 -27.253 -17.373 1.00 39.03  ? 77  VAL A N     1 
ATOM   525  C  CA    . VAL A 1 98  ? 52.844 -27.881 -16.840 1.00 37.18  ? 77  VAL A CA    1 
ATOM   526  C  C     . VAL A 1 98  ? 52.184 -28.624 -17.992 1.00 37.46  ? 77  VAL A C     1 
ATOM   527  O  O     . VAL A 1 98  ? 51.917 -27.974 -19.012 1.00 38.86  ? 77  VAL A O     1 
ATOM   528  C  CB    . VAL A 1 98  ? 51.883 -26.853 -16.210 1.00 35.91  ? 77  VAL A CB    1 
ATOM   529  C  CG1   . VAL A 1 98  ? 50.619 -27.545 -15.731 1.00 35.59  ? 77  VAL A CG1   1 
ATOM   530  C  CG2   . VAL A 1 98  ? 52.523 -26.055 -15.069 1.00 32.29  ? 77  VAL A CG2   1 
ATOM   531  N  N     . GLU A 1 99  ? 51.900 -29.912 -17.804 1.00 39.80  ? 78  GLU A N     1 
ATOM   532  C  CA    . GLU A 1 99  ? 51.296 -30.793 -18.832 1.00 40.39  ? 78  GLU A CA    1 
ATOM   533  C  C     . GLU A 1 99  ? 49.776 -30.565 -18.889 1.00 37.82  ? 78  GLU A C     1 
ATOM   534  O  O     . GLU A 1 99  ? 49.173 -30.110 -17.868 1.00 35.69  ? 78  GLU A O     1 
ATOM   535  C  CB    . GLU A 1 99  ? 51.669 -32.242 -18.527 1.00 45.78  ? 78  GLU A CB    1 
ATOM   536  C  CG    . GLU A 1 99  ? 51.191 -33.220 -19.591 1.00 58.61  ? 78  GLU A CG    1 
ATOM   537  C  CD    . GLU A 1 99  ? 51.687 -34.663 -19.493 1.00 70.60  ? 78  GLU A CD    1 
ATOM   538  O  OE1   . GLU A 1 99  ? 52.853 -34.868 -19.073 1.00 73.26  ? 78  GLU A OE1   1 
ATOM   539  O  OE2   . GLU A 1 99  ? 50.901 -35.588 -19.840 1.00 73.39  ? 78  GLU A OE2   1 
ATOM   540  N  N     . THR A 1 100 ? 49.175 -30.831 -20.052 1.00 34.71  ? 79  THR A N     1 
ATOM   541  C  CA    . THR A 1 100 ? 47.700 -30.820 -20.289 1.00 38.49  ? 79  THR A CA    1 
ATOM   542  C  C     . THR A 1 100 ? 47.175 -32.260 -20.368 1.00 34.39  ? 79  THR A C     1 
ATOM   543  O  O     . THR A 1 100 ? 47.940 -33.180 -20.666 1.00 38.65  ? 79  THR A O     1 
ATOM   544  C  CB    . THR A 1 100 ? 47.298 -30.023 -21.545 1.00 39.59  ? 79  THR A CB    1 
ATOM   545  O  OG1   . THR A 1 100 ? 47.702 -30.696 -22.738 1.00 35.11  ? 79  THR A OG1   1 
ATOM   546  C  CG2   . THR A 1 100 ? 47.862 -28.619 -21.570 1.00 38.70  ? 79  THR A CG2   1 
ATOM   547  N  N     . TYR A 1 101 ? 45.908 -32.462 -20.058 1.00 35.78  ? 80  TYR A N     1 
ATOM   548  C  CA    . TYR A 1 101 ? 45.172 -33.726 -20.343 1.00 31.90  ? 80  TYR A CA    1 
ATOM   549  C  C     . TYR A 1 101 ? 43.837 -33.346 -20.976 1.00 34.31  ? 80  TYR A C     1 
ATOM   550  O  O     . TYR A 1 101 ? 43.321 -32.260 -20.674 1.00 32.75  ? 80  TYR A O     1 
ATOM   551  C  CB    . TYR A 1 101 ? 45.036 -34.591 -19.090 1.00 31.52  ? 80  TYR A CB    1 
ATOM   552  C  CG    . TYR A 1 101 ? 44.200 -34.052 -17.945 1.00 33.72  ? 80  TYR A CG    1 
ATOM   553  C  CD1   . TYR A 1 101 ? 44.701 -33.089 -17.086 1.00 34.73  ? 80  TYR A CD1   1 
ATOM   554  C  CD2   . TYR A 1 101 ? 42.967 -34.600 -17.625 1.00 35.08  ? 80  TYR A CD2   1 
ATOM   555  C  CE1   . TYR A 1 101 ? 43.974 -32.628 -16.005 1.00 38.32  ? 80  TYR A CE1   1 
ATOM   556  C  CE2   . TYR A 1 101 ? 42.234 -34.168 -16.530 1.00 38.02  ? 80  TYR A CE2   1 
ATOM   557  C  CZ    . TYR A 1 101 ? 42.737 -33.171 -15.716 1.00 38.27  ? 80  TYR A CZ    1 
ATOM   558  O  OH    . TYR A 1 101 ? 42.047 -32.709 -14.628 1.00 37.48  ? 80  TYR A OH    1 
ATOM   559  N  N     . PRO A 1 102 ? 43.284 -34.192 -21.890 1.00 33.34  ? 81  PRO A N     1 
ATOM   560  C  CA    . PRO A 1 102 ? 42.013 -33.888 -22.547 1.00 33.13  ? 81  PRO A CA    1 
ATOM   561  C  C     . PRO A 1 102 ? 40.806 -34.037 -21.600 1.00 33.86  ? 81  PRO A C     1 
ATOM   562  O  O     . PRO A 1 102 ? 40.772 -34.982 -20.846 1.00 34.54  ? 81  PRO A O     1 
ATOM   563  C  CB    . PRO A 1 102 ? 41.954 -34.896 -23.722 1.00 32.41  ? 81  PRO A CB    1 
ATOM   564  C  CG    . PRO A 1 102 ? 42.814 -36.084 -23.278 1.00 30.49  ? 81  PRO A CG    1 
ATOM   565  C  CD    . PRO A 1 102 ? 43.862 -35.470 -22.362 1.00 32.60  ? 81  PRO A CD    1 
ATOM   566  N  N     . GLN A 1 103 ? 39.862 -33.089 -21.663 1.00 31.71  ? 82  GLN A N     1 
ATOM   567  C  CA    . GLN A 1 103 ? 38.489 -33.226 -21.115 1.00 33.92  ? 82  GLN A CA    1 
ATOM   568  C  C     . GLN A 1 103 ? 37.870 -34.463 -21.768 1.00 36.75  ? 82  GLN A C     1 
ATOM   569  O  O     . GLN A 1 103 ? 37.742 -34.507 -22.992 1.00 36.24  ? 82  GLN A O     1 
ATOM   570  C  CB    . GLN A 1 103 ? 37.728 -31.916 -21.385 1.00 32.89  ? 82  GLN A CB    1 
ATOM   571  C  CG    . GLN A 1 103 ? 36.295 -31.856 -20.883 1.00 28.90  ? 82  GLN A CG    1 
ATOM   572  C  CD    . GLN A 1 103 ? 36.163 -32.058 -19.395 1.00 28.42  ? 82  GLN A CD    1 
ATOM   573  O  OE1   . GLN A 1 103 ? 36.858 -31.456 -18.583 1.00 32.47  ? 82  GLN A OE1   1 
ATOM   574  N  NE2   . GLN A 1 103 ? 35.268 -32.937 -19.022 1.00 27.74  ? 82  GLN A NE2   1 
ATOM   575  N  N     . PRO A 1 104 ? 37.499 -35.511 -20.995 1.00 40.53  ? 83  PRO A N     1 
ATOM   576  C  CA    . PRO A 1 104 ? 36.793 -36.670 -21.549 1.00 44.48  ? 83  PRO A CA    1 
ATOM   577  C  C     . PRO A 1 104 ? 35.499 -36.269 -22.281 1.00 50.97  ? 83  PRO A C     1 
ATOM   578  O  O     . PRO A 1 104 ? 34.861 -35.323 -21.866 1.00 50.69  ? 83  PRO A O     1 
ATOM   579  C  CB    . PRO A 1 104 ? 36.449 -37.514 -20.313 1.00 42.69  ? 83  PRO A CB    1 
ATOM   580  C  CG    . PRO A 1 104 ? 37.496 -37.127 -19.317 1.00 41.93  ? 83  PRO A CG    1 
ATOM   581  C  CD    . PRO A 1 104 ? 37.697 -35.638 -19.546 1.00 41.34  ? 83  PRO A CD    1 
ATOM   582  N  N     . THR A 1 105 ? 35.142 -36.997 -23.344 1.00 58.00  ? 84  THR A N     1 
ATOM   583  C  CA    . THR A 1 105 ? 34.042 -36.639 -24.281 1.00 60.17  ? 84  THR A CA    1 
ATOM   584  C  C     . THR A 1 105 ? 33.186 -37.862 -24.680 1.00 54.92  ? 84  THR A C     1 
ATOM   585  O  O     . THR A 1 105 ? 32.015 -37.665 -25.058 1.00 56.91  ? 84  THR A O     1 
ATOM   586  C  CB    . THR A 1 105 ? 34.636 -35.877 -25.471 1.00 61.98  ? 84  THR A CB    1 
ATOM   587  O  OG1   . THR A 1 105 ? 33.642 -35.864 -26.494 1.00 67.32  ? 84  THR A OG1   1 
ATOM   588  C  CG2   . THR A 1 105 ? 35.925 -36.475 -25.987 1.00 59.06  ? 84  THR A CG2   1 
ATOM   589  N  N     . GLU A 1 106 ? 33.712 -39.079 -24.577 1.00 51.41  ? 85  GLU A N     1 
ATOM   590  C  CA    . GLU A 1 106 ? 33.045 -40.320 -25.045 1.00 49.46  ? 85  GLU A CA    1 
ATOM   591  C  C     . GLU A 1 106 ? 31.917 -40.708 -24.083 1.00 47.29  ? 85  GLU A C     1 
ATOM   592  O  O     . GLU A 1 106 ? 31.945 -40.277 -22.923 1.00 46.10  ? 85  GLU A O     1 
ATOM   593  C  CB    . GLU A 1 106 ? 34.072 -41.449 -25.155 1.00 57.43  ? 85  GLU A CB    1 
ATOM   594  C  CG    . GLU A 1 106 ? 35.216 -41.132 -26.111 1.00 68.15  ? 85  GLU A CG    1 
ATOM   595  C  CD    . GLU A 1 106 ? 34.948 -41.312 -27.605 1.00 73.98  ? 85  GLU A CD    1 
ATOM   596  O  OE1   . GLU A 1 106 ? 35.900 -41.700 -28.331 1.00 78.32  ? 85  GLU A OE1   1 
ATOM   597  O  OE2   . GLU A 1 106 ? 33.802 -41.063 -28.047 1.00 75.13  ? 85  GLU A OE2   1 
ATOM   598  N  N     . GLY A 1 107 ? 30.981 -41.533 -24.566 1.00 43.48  ? 86  GLY A N     1 
ATOM   599  C  CA    . GLY A 1 107 ? 29.764 -41.968 -23.859 1.00 40.42  ? 86  GLY A CA    1 
ATOM   600  C  C     . GLY A 1 107 ? 28.540 -41.150 -24.258 1.00 38.19  ? 86  GLY A C     1 
ATOM   601  O  O     . GLY A 1 107 ? 28.685 -40.059 -24.845 1.00 35.42  ? 86  GLY A O     1 
ATOM   602  N  N     . ASP A 1 108 ? 27.345 -41.638 -23.937 1.00 42.23  ? 87  ASP A N     1 
ATOM   603  C  CA    . ASP A 1 108 ? 26.086 -40.944 -24.310 1.00 45.09  ? 87  ASP A CA    1 
ATOM   604  C  C     . ASP A 1 108 ? 25.861 -39.793 -23.331 1.00 40.09  ? 87  ASP A C     1 
ATOM   605  O  O     . ASP A 1 108 ? 26.018 -39.988 -22.118 1.00 38.48  ? 87  ASP A O     1 
ATOM   606  C  CB    . ASP A 1 108 ? 24.920 -41.935 -24.398 1.00 52.88  ? 87  ASP A CB    1 
ATOM   607  C  CG    . ASP A 1 108 ? 25.146 -43.062 -25.404 1.00 54.86  ? 87  ASP A CG    1 
ATOM   608  O  OD1   . ASP A 1 108 ? 25.846 -42.822 -26.417 1.00 56.56  ? 87  ASP A OD1   1 
ATOM   609  O  OD2   . ASP A 1 108 ? 24.655 -44.186 -25.145 1.00 54.84  ? 87  ASP A OD2   1 
ATOM   610  N  N     . ASP A 1 109 ? 25.559 -38.617 -23.860 1.00 44.12  ? 88  ASP A N     1 
ATOM   611  C  CA    . ASP A 1 109 ? 25.035 -37.475 -23.069 1.00 44.72  ? 88  ASP A CA    1 
ATOM   612  C  C     . ASP A 1 109 ? 23.582 -37.790 -22.691 1.00 45.22  ? 88  ASP A C     1 
ATOM   613  O  O     . ASP A 1 109 ? 22.947 -38.629 -23.393 1.00 56.45  ? 88  ASP A O     1 
ATOM   614  C  CB    . ASP A 1 109 ? 25.205 -36.177 -23.855 1.00 48.07  ? 88  ASP A CB    1 
ATOM   615  C  CG    . ASP A 1 109 ? 26.661 -35.878 -24.192 1.00 53.22  ? 88  ASP A CG    1 
ATOM   616  O  OD1   . ASP A 1 109 ? 27.546 -36.542 -23.601 1.00 58.68  ? 88  ASP A OD1   1 
ATOM   617  O  OD2   . ASP A 1 109 ? 26.906 -34.979 -25.037 1.00 55.80  ? 88  ASP A OD2   1 
ATOM   618  N  N     . VAL A 1 110 ? 23.082 -37.211 -21.596 1.00 40.41  ? 89  VAL A N     1 
ATOM   619  C  CA    . VAL A 1 110 ? 21.656 -37.335 -21.172 1.00 41.56  ? 89  VAL A CA    1 
ATOM   620  C  C     . VAL A 1 110 ? 21.021 -35.940 -21.247 1.00 45.86  ? 89  VAL A C     1 
ATOM   621  O  O     . VAL A 1 110 ? 21.585 -34.992 -20.670 1.00 43.76  ? 89  VAL A O     1 
ATOM   622  C  CB    . VAL A 1 110 ? 21.524 -37.971 -19.771 1.00 41.83  ? 89  VAL A CB    1 
ATOM   623  C  CG1   . VAL A 1 110 ? 20.085 -37.983 -19.262 1.00 37.41  ? 89  VAL A CG1   1 
ATOM   624  C  CG2   . VAL A 1 110 ? 22.111 -39.378 -19.726 1.00 42.72  ? 89  VAL A CG2   1 
ATOM   625  N  N     . VAL A 1 111 ? 19.887 -35.824 -21.940 1.00 45.86  ? 90  VAL A N     1 
ATOM   626  C  CA    . VAL A 1 111 ? 19.057 -34.590 -21.976 1.00 46.32  ? 90  VAL A CA    1 
ATOM   627  C  C     . VAL A 1 111 ? 17.703 -34.883 -21.305 1.00 48.87  ? 90  VAL A C     1 
ATOM   628  O  O     . VAL A 1 111 ? 17.187 -36.000 -21.481 1.00 54.73  ? 90  VAL A O     1 
ATOM   629  C  CB    . VAL A 1 111 ? 18.929 -34.086 -23.423 1.00 49.98  ? 90  VAL A CB    1 
ATOM   630  C  CG1   . VAL A 1 111 ? 17.950 -32.931 -23.547 1.00 53.35  ? 90  VAL A CG1   1 
ATOM   631  C  CG2   . VAL A 1 111 ? 20.285 -33.692 -23.992 1.00 43.94  ? 90  VAL A CG2   1 
ATOM   632  N  N     . LEU A 1 112 ? 17.190 -33.923 -20.528 1.00 46.03  ? 91  LEU A N     1 
ATOM   633  C  CA    . LEU A 1 112 ? 15.936 -33.996 -19.727 1.00 47.54  ? 91  LEU A CA    1 
ATOM   634  C  C     . LEU A 1 112 ? 15.215 -32.651 -19.844 1.00 53.49  ? 91  LEU A C     1 
ATOM   635  O  O     . LEU A 1 112 ? 15.846 -31.622 -19.487 1.00 43.84  ? 91  LEU A O     1 
ATOM   636  C  CB    . LEU A 1 112 ? 16.266 -34.265 -18.258 1.00 47.01  ? 91  LEU A CB    1 
ATOM   637  C  CG    . LEU A 1 112 ? 15.083 -34.216 -17.288 1.00 49.32  ? 91  LEU A CG    1 
ATOM   638  C  CD1   . LEU A 1 112 ? 14.336 -35.546 -17.263 1.00 52.87  ? 91  LEU A CD1   1 
ATOM   639  C  CD2   . LEU A 1 112 ? 15.542 -33.858 -15.885 1.00 49.82  ? 91  LEU A CD2   1 
ATOM   640  N  N     . PHE A 1 113 ? 13.945 -32.681 -20.280 1.00 57.56  ? 92  PHE A N     1 
ATOM   641  C  CA    . PHE A 1 113 ? 13.074 -31.502 -20.530 1.00 55.56  ? 92  PHE A CA    1 
ATOM   642  C  C     . PHE A 1 113 ? 11.850 -31.527 -19.614 1.00 55.87  ? 92  PHE A C     1 
ATOM   643  O  O     . PHE A 1 113 ? 11.022 -32.431 -19.801 1.00 57.52  ? 92  PHE A O     1 
ATOM   644  C  CB    . PHE A 1 113 ? 12.528 -31.534 -21.953 1.00 57.00  ? 92  PHE A CB    1 
ATOM   645  C  CG    . PHE A 1 113 ? 13.543 -31.333 -23.043 1.00 60.72  ? 92  PHE A CG    1 
ATOM   646  C  CD1   . PHE A 1 113 ? 14.208 -30.120 -23.176 1.00 60.65  ? 92  PHE A CD1   1 
ATOM   647  C  CD2   . PHE A 1 113 ? 13.803 -32.345 -23.954 1.00 56.90  ? 92  PHE A CD2   1 
ATOM   648  C  CE1   . PHE A 1 113 ? 15.133 -29.934 -24.194 1.00 65.50  ? 92  PHE A CE1   1 
ATOM   649  C  CE2   . PHE A 1 113 ? 14.714 -32.151 -24.981 1.00 60.46  ? 92  PHE A CE2   1 
ATOM   650  C  CZ    . PHE A 1 113 ? 15.378 -30.947 -25.099 1.00 62.40  ? 92  PHE A CZ    1 
ATOM   651  N  N     . GLY A 1 114 ? 11.721 -30.551 -18.705 1.00 57.24  ? 93  GLY A N     1 
ATOM   652  C  CA    . GLY A 1 114 ? 10.586 -30.402 -17.760 1.00 60.41  ? 93  GLY A CA    1 
ATOM   653  C  C     . GLY A 1 114 ? 10.245 -31.695 -17.032 1.00 55.96  ? 93  GLY A C     1 
ATOM   654  O  O     . GLY A 1 114 ? 11.186 -32.403 -16.608 1.00 60.21  ? 93  GLY A O     1 
ATOM   655  N  N     . ASP A 1 115 ? 8.951  -32.025 -16.950 1.00 58.92  ? 94  ASP A N     1 
ATOM   656  C  CA    . ASP A 1 115 ? 8.386  -33.203 -16.224 1.00 66.19  ? 94  ASP A CA    1 
ATOM   657  C  C     . ASP A 1 115 ? 8.752  -34.521 -16.934 1.00 67.99  ? 94  ASP A C     1 
ATOM   658  O  O     . ASP A 1 115 ? 8.527  -35.590 -16.328 1.00 67.82  ? 94  ASP A O     1 
ATOM   659  C  CB    . ASP A 1 115 ? 6.861  -33.079 -16.055 1.00 69.27  ? 94  ASP A CB    1 
ATOM   660  C  CG    . ASP A 1 115 ? 6.412  -32.097 -14.969 1.00 77.25  ? 94  ASP A CG    1 
ATOM   661  O  OD1   . ASP A 1 115 ? 7.152  -31.119 -14.706 1.00 72.80  ? 94  ASP A OD1   1 
ATOM   662  O  OD2   . ASP A 1 115 ? 5.318  -32.310 -14.381 1.00 73.40  ? 94  ASP A OD2   1 
ATOM   663  N  N     . GLY A 1 116 ? 9.307  -34.456 -18.154 1.00 69.54  ? 95  GLY A N     1 
ATOM   664  C  CA    . GLY A 1 116 ? 9.558  -35.607 -19.051 1.00 67.22  ? 95  GLY A CA    1 
ATOM   665  C  C     . GLY A 1 116 ? 10.562 -36.588 -18.478 1.00 62.70  ? 95  GLY A C     1 
ATOM   666  O  O     . GLY A 1 116 ? 11.118 -36.295 -17.415 1.00 73.30  ? 95  GLY A O     1 
ATOM   667  N  N     . GLU A 1 117 ? 10.780 -37.719 -19.151 1.00 61.55  ? 96  GLU A N     1 
ATOM   668  C  CA    . GLU A 1 117 ? 11.781 -38.737 -18.737 1.00 60.55  ? 96  GLU A CA    1 
ATOM   669  C  C     . GLU A 1 117 ? 13.117 -38.383 -19.392 1.00 55.19  ? 96  GLU A C     1 
ATOM   670  O  O     . GLU A 1 117 ? 13.164 -37.593 -20.336 1.00 53.06  ? 96  GLU A O     1 
ATOM   671  C  CB    . GLU A 1 117 ? 11.280 -40.153 -19.046 1.00 64.46  ? 96  GLU A CB    1 
ATOM   672  C  CG    . GLU A 1 117 ? 10.182 -40.639 -18.093 1.00 74.64  ? 96  GLU A CG    1 
ATOM   673  C  CD    . GLU A 1 117 ? 10.568 -40.875 -16.629 1.00 88.06  ? 96  GLU A CD    1 
ATOM   674  O  OE1   . GLU A 1 117 ? 11.328 -41.830 -16.349 1.00 80.68  ? 96  GLU A OE1   1 
ATOM   675  O  OE2   . GLU A 1 117 ? 10.098 -40.107 -15.751 1.00 91.41  ? 96  GLU A OE2   1 
ATOM   676  N  N     . PRO A 1 118 ? 14.246 -38.877 -18.843 1.00 49.22  ? 97  PRO A N     1 
ATOM   677  C  CA    . PRO A 1 118 ? 15.571 -38.600 -19.398 1.00 53.20  ? 97  PRO A CA    1 
ATOM   678  C  C     . PRO A 1 118 ? 15.869 -39.380 -20.682 1.00 47.96  ? 97  PRO A C     1 
ATOM   679  O  O     . PRO A 1 118 ? 15.489 -40.530 -20.763 1.00 49.13  ? 97  PRO A O     1 
ATOM   680  C  CB    . PRO A 1 118 ? 16.558 -39.070 -18.311 1.00 56.34  ? 97  PRO A CB    1 
ATOM   681  C  CG    . PRO A 1 118 ? 15.776 -40.075 -17.477 1.00 56.37  ? 97  PRO A CG    1 
ATOM   682  C  CD    . PRO A 1 118 ? 14.316 -39.675 -17.607 1.00 54.23  ? 97  PRO A CD    1 
ATOM   683  N  N     . GLN A 1 119 ? 16.602 -38.756 -21.603 1.00 47.60  ? 98  GLN A N     1 
ATOM   684  C  CA    . GLN A 1 119 ? 16.906 -39.316 -22.945 1.00 50.83  ? 98  GLN A CA    1 
ATOM   685  C  C     . GLN A 1 119 ? 18.422 -39.412 -23.168 1.00 46.44  ? 98  GLN A C     1 
ATOM   686  O  O     . GLN A 1 119 ? 19.101 -38.377 -23.077 1.00 39.44  ? 98  GLN A O     1 
ATOM   687  C  CB    . GLN A 1 119 ? 16.226 -38.450 -23.999 1.00 55.25  ? 98  GLN A CB    1 
ATOM   688  C  CG    . GLN A 1 119 ? 14.729 -38.722 -24.091 1.00 68.68  ? 98  GLN A CG    1 
ATOM   689  C  CD    . GLN A 1 119 ? 13.981 -37.615 -24.798 1.00 75.38  ? 98  GLN A CD    1 
ATOM   690  O  OE1   . GLN A 1 119 ? 14.567 -36.775 -25.490 1.00 68.72  ? 98  GLN A OE1   1 
ATOM   691  N  NE2   . GLN A 1 119 ? 12.668 -37.602 -24.607 1.00 78.94  ? 98  GLN A NE2   1 
ATOM   692  N  N     . ARG A 1 120 ? 18.922 -40.622 -23.448 1.00 50.03  ? 99  ARG A N     1 
ATOM   693  C  CA    . ARG A 1 120 ? 20.319 -40.868 -23.894 1.00 57.03  ? 99  ARG A CA    1 
ATOM   694  C  C     . ARG A 1 120 ? 20.449 -40.550 -25.389 1.00 59.58  ? 99  ARG A C     1 
ATOM   695  O  O     . ARG A 1 120 ? 19.567 -40.959 -26.169 1.00 66.35  ? 99  ARG A O     1 
ATOM   696  C  CB    . ARG A 1 120 ? 20.713 -42.327 -23.645 1.00 59.05  ? 99  ARG A CB    1 
ATOM   697  C  CG    . ARG A 1 120 ? 20.761 -42.722 -22.177 1.00 61.94  ? 99  ARG A CG    1 
ATOM   698  C  CD    . ARG A 1 120 ? 21.145 -44.175 -21.956 1.00 58.50  ? 99  ARG A CD    1 
ATOM   699  N  NE    . ARG A 1 120 ? 22.458 -44.470 -22.504 1.00 57.42  ? 99  ARG A NE    1 
ATOM   700  C  CZ    . ARG A 1 120 ? 23.407 -45.186 -21.903 1.00 57.54  ? 99  ARG A CZ    1 
ATOM   701  N  NH1   . ARG A 1 120 ? 23.219 -45.715 -20.704 1.00 54.77  ? 99  ARG A NH1   1 
ATOM   702  N  NH2   . ARG A 1 120 ? 24.568 -45.360 -22.507 1.00 57.16  ? 99  ARG A NH2   1 
ATOM   703  N  N     . ALA A 1 121 ? 21.517 -39.861 -25.784 1.00 56.86  ? 100 ALA A N     1 
ATOM   704  C  CA    . ALA A 1 121 ? 21.939 -39.754 -27.197 1.00 54.97  ? 100 ALA A CA    1 
ATOM   705  C  C     . ALA A 1 121 ? 23.462 -39.713 -27.253 1.00 61.84  ? 100 ALA A C     1 
ATOM   706  O  O     . ALA A 1 121 ? 24.096 -39.433 -26.235 1.00 61.95  ? 100 ALA A O     1 
ATOM   707  C  CB    . ALA A 1 121 ? 21.312 -38.548 -27.828 1.00 56.45  ? 100 ALA A CB    1 
ATOM   708  N  N     . PRO A 1 122 ? 24.089 -40.021 -28.418 1.00 63.91  ? 101 PRO A N     1 
ATOM   709  C  CA    . PRO A 1 122 ? 25.548 -39.948 -28.567 1.00 66.86  ? 101 PRO A CA    1 
ATOM   710  C  C     . PRO A 1 122 ? 26.106 -38.535 -28.337 1.00 66.45  ? 101 PRO A C     1 
ATOM   711  O  O     . PRO A 1 122 ? 27.251 -38.401 -27.955 1.00 63.14  ? 101 PRO A O     1 
ATOM   712  C  CB    . PRO A 1 122 ? 25.804 -40.354 -30.026 1.00 63.93  ? 101 PRO A CB    1 
ATOM   713  C  CG    . PRO A 1 122 ? 24.567 -41.146 -30.402 1.00 68.71  ? 101 PRO A CG    1 
ATOM   714  C  CD    . PRO A 1 122 ? 23.433 -40.476 -29.653 1.00 66.10  ? 101 PRO A CD    1 
ATOM   715  N  N     . ASP A 1 123 ? 25.271 -37.524 -28.585 1.00 65.12  ? 102 ASP A N     1 
ATOM   716  C  CA    . ASP A 1 123 ? 25.600 -36.088 -28.402 1.00 66.61  ? 102 ASP A CA    1 
ATOM   717  C  C     . ASP A 1 123 ? 24.311 -35.327 -28.046 1.00 62.26  ? 102 ASP A C     1 
ATOM   718  O  O     . ASP A 1 123 ? 23.299 -35.523 -28.727 1.00 67.07  ? 102 ASP A O     1 
ATOM   719  C  CB    . ASP A 1 123 ? 26.277 -35.527 -29.655 1.00 65.52  ? 102 ASP A CB    1 
ATOM   720  C  CG    . ASP A 1 123 ? 26.961 -34.189 -29.430 1.00 74.06  ? 102 ASP A CG    1 
ATOM   721  O  OD1   . ASP A 1 123 ? 26.292 -33.247 -28.925 1.00 71.70  ? 102 ASP A OD1   1 
ATOM   722  O  OD2   . ASP A 1 123 ? 28.165 -34.100 -29.746 1.00 82.50  ? 102 ASP A OD2   1 
ATOM   723  N  N     . VAL A 1 124 ? 24.359 -34.526 -26.985 1.00 56.97  ? 103 VAL A N     1 
ATOM   724  C  CA    . VAL A 1 124 ? 23.391 -33.443 -26.644 1.00 57.69  ? 103 VAL A CA    1 
ATOM   725  C  C     . VAL A 1 124 ? 22.525 -33.073 -27.863 1.00 54.52  ? 103 VAL A C     1 
ATOM   726  O  O     . VAL A 1 124 ? 21.271 -33.152 -27.745 1.00 47.38  ? 103 VAL A O     1 
ATOM   727  C  CB    . VAL A 1 124 ? 24.170 -32.230 -26.100 1.00 57.53  ? 103 VAL A CB    1 
ATOM   728  C  CG1   . VAL A 1 124 ? 23.425 -30.918 -26.277 1.00 62.78  ? 103 VAL A CG1   1 
ATOM   729  C  CG2   . VAL A 1 124 ? 24.558 -32.425 -24.640 1.00 60.70  ? 103 VAL A CG2   1 
ATOM   730  N  N     . ALA A 1 125 ? 23.143 -32.669 -28.982 1.00 57.03  ? 104 ALA A N     1 
ATOM   731  C  CA    . ALA A 1 125 ? 22.469 -32.020 -30.137 1.00 62.33  ? 104 ALA A CA    1 
ATOM   732  C  C     . ALA A 1 125 ? 21.531 -32.997 -30.876 1.00 63.69  ? 104 ALA A C     1 
ATOM   733  O  O     . ALA A 1 125 ? 20.732 -32.513 -31.712 1.00 58.24  ? 104 ALA A O     1 
ATOM   734  C  CB    . ALA A 1 125 ? 23.497 -31.416 -31.067 1.00 64.39  ? 104 ALA A CB    1 
ATOM   735  N  N     . LEU A 1 126 ? 21.578 -34.296 -30.545 1.00 61.51  ? 105 LEU A N     1 
ATOM   736  C  CA    . LEU A 1 126 ? 20.799 -35.383 -31.196 1.00 64.14  ? 105 LEU A CA    1 
ATOM   737  C  C     . LEU A 1 126 ? 19.587 -35.805 -30.344 1.00 65.82  ? 105 LEU A C     1 
ATOM   738  O  O     . LEU A 1 126 ? 19.199 -36.993 -30.432 1.00 62.41  ? 105 LEU A O     1 
ATOM   739  C  CB    . LEU A 1 126 ? 21.750 -36.560 -31.433 1.00 69.88  ? 105 LEU A CB    1 
ATOM   740  C  CG    . LEU A 1 126 ? 23.105 -36.211 -32.062 1.00 77.86  ? 105 LEU A CG    1 
ATOM   741  C  CD1   . LEU A 1 126 ? 23.889 -37.480 -32.388 1.00 75.04  ? 105 LEU A CD1   1 
ATOM   742  C  CD2   . LEU A 1 126 ? 22.955 -35.341 -33.313 1.00 74.18  ? 105 LEU A CD2   1 
ATOM   743  N  N     . ALA A 1 127 ? 19.020 -34.886 -29.546 1.00 65.58  ? 106 ALA A N     1 
ATOM   744  C  CA    . ALA A 1 127 ? 17.719 -35.025 -28.839 1.00 60.86  ? 106 ALA A CA    1 
ATOM   745  C  C     . ALA A 1 127 ? 16.798 -33.891 -29.281 1.00 59.83  ? 106 ALA A C     1 
ATOM   746  O  O     . ALA A 1 127 ? 15.752 -33.683 -28.635 1.00 62.02  ? 106 ALA A O     1 
ATOM   747  C  CB    . ALA A 1 127 ? 17.909 -35.005 -27.343 1.00 61.39  ? 106 ALA A CB    1 
ATOM   748  N  N     . PHE A 1 128 ? 17.187 -33.213 -30.360 1.00 60.17  ? 107 PHE A N     1 
ATOM   749  C  CA    . PHE A 1 128 ? 16.493 -32.051 -30.969 1.00 67.88  ? 107 PHE A CA    1 
ATOM   750  C  C     . PHE A 1 128 ? 16.178 -32.357 -32.443 1.00 67.57  ? 107 PHE A C     1 
ATOM   751  O  O     . PHE A 1 128 ? 17.069 -32.814 -33.171 1.00 66.37  ? 107 PHE A O     1 
ATOM   752  C  CB    . PHE A 1 128 ? 17.360 -30.796 -30.836 1.00 68.88  ? 107 PHE A CB    1 
ATOM   753  C  CG    . PHE A 1 128 ? 17.668 -30.403 -29.414 1.00 75.40  ? 107 PHE A CG    1 
ATOM   754  C  CD1   . PHE A 1 128 ? 18.590 -31.117 -28.664 1.00 79.92  ? 107 PHE A CD1   1 
ATOM   755  C  CD2   . PHE A 1 128 ? 17.021 -29.329 -28.820 1.00 81.42  ? 107 PHE A CD2   1 
ATOM   756  C  CE1   . PHE A 1 128 ? 18.859 -30.764 -27.350 1.00 85.54  ? 107 PHE A CE1   1 
ATOM   757  C  CE2   . PHE A 1 128 ? 17.295 -28.975 -27.508 1.00 82.55  ? 107 PHE A CE2   1 
ATOM   758  C  CZ    . PHE A 1 128 ? 18.215 -29.690 -26.776 1.00 85.23  ? 107 PHE A CZ    1 
ATOM   759  N  N     . SER A 1 129 ? 14.941 -32.088 -32.868 1.00 64.84  ? 108 SER A N     1 
ATOM   760  C  CA    . SER A 1 129 ? 14.473 -32.185 -34.272 1.00 64.80  ? 108 SER A CA    1 
ATOM   761  C  C     . SER A 1 129 ? 15.442 -31.446 -35.202 1.00 71.89  ? 108 SER A C     1 
ATOM   762  O  O     . SER A 1 129 ? 16.265 -30.634 -34.725 1.00 73.01  ? 108 SER A O     1 
ATOM   763  C  CB    . SER A 1 129 ? 13.073 -31.640 -34.420 1.00 62.75  ? 108 SER A CB    1 
ATOM   764  O  OG    . SER A 1 129 ? 13.063 -30.218 -34.374 1.00 61.51  ? 108 SER A OG    1 
ATOM   765  N  N     . ASP A 1 130 ? 15.324 -31.709 -36.498 1.00 70.96  ? 109 ASP A N     1 
ATOM   766  C  CA    . ASP A 1 130 ? 16.219 -31.138 -37.531 1.00 71.72  ? 109 ASP A CA    1 
ATOM   767  C  C     . ASP A 1 130 ? 15.924 -29.639 -37.644 1.00 69.69  ? 109 ASP A C     1 
ATOM   768  O  O     . ASP A 1 130 ? 16.892 -28.879 -37.821 1.00 67.06  ? 109 ASP A O     1 
ATOM   769  C  CB    . ASP A 1 130 ? 16.054 -31.884 -38.857 1.00 72.61  ? 109 ASP A CB    1 
ATOM   770  C  CG    . ASP A 1 130 ? 16.447 -33.352 -38.773 1.00 75.64  ? 109 ASP A CG    1 
ATOM   771  O  OD1   . ASP A 1 130 ? 17.582 -33.630 -38.321 1.00 75.95  ? 109 ASP A OD1   1 
ATOM   772  O  OD2   . ASP A 1 130 ? 15.614 -34.208 -39.149 1.00 69.89  ? 109 ASP A OD2   1 
ATOM   773  N  N     . GLU A 1 131 ? 14.651 -29.237 -37.524 1.00 64.11  ? 110 GLU A N     1 
ATOM   774  C  CA    . GLU A 1 131 ? 14.195 -27.825 -37.694 1.00 70.67  ? 110 GLU A CA    1 
ATOM   775  C  C     . GLU A 1 131 ? 14.680 -27.015 -36.479 1.00 64.81  ? 110 GLU A C     1 
ATOM   776  O  O     . GLU A 1 131 ? 14.987 -25.811 -36.668 1.00 60.44  ? 110 GLU A O     1 
ATOM   777  C  CB    . GLU A 1 131 ? 12.673 -27.734 -37.919 1.00 75.94  ? 110 GLU A CB    1 
ATOM   778  C  CG    . GLU A 1 131 ? 12.226 -26.498 -38.722 1.00 86.20  ? 110 GLU A CG    1 
ATOM   779  C  CD    . GLU A 1 131 ? 10.751 -26.386 -39.131 1.00 93.58  ? 110 GLU A CD    1 
ATOM   780  O  OE1   . GLU A 1 131 ? 9.946  -27.281 -38.772 1.00 89.69  ? 110 GLU A OE1   1 
ATOM   781  O  OE2   . GLU A 1 131 ? 10.396 -25.395 -39.824 1.00 88.27  ? 110 GLU A OE2   1 
ATOM   782  N  N     . GLU A 1 132 ? 14.764 -27.668 -35.306 1.00 62.42  ? 111 GLU A N     1 
ATOM   783  C  CA    . GLU A 1 132 ? 15.249 -27.109 -34.010 1.00 63.96  ? 111 GLU A CA    1 
ATOM   784  C  C     . GLU A 1 132 ? 16.762 -26.865 -34.074 1.00 66.39  ? 111 GLU A C     1 
ATOM   785  O  O     . GLU A 1 132 ? 17.162 -25.684 -33.964 1.00 64.52  ? 111 GLU A O     1 
ATOM   786  C  CB    . GLU A 1 132 ? 14.898 -28.045 -32.853 1.00 62.10  ? 111 GLU A CB    1 
ATOM   787  C  CG    . GLU A 1 132 ? 13.450 -27.908 -32.413 1.00 65.61  ? 111 GLU A CG    1 
ATOM   788  C  CD    . GLU A 1 132 ? 13.002 -28.835 -31.297 1.00 61.27  ? 111 GLU A CD    1 
ATOM   789  O  OE1   . GLU A 1 132 ? 13.772 -29.747 -30.942 1.00 58.83  ? 111 GLU A OE1   1 
ATOM   790  O  OE2   . GLU A 1 132 ? 11.889 -28.624 -30.776 1.00 54.23  ? 111 GLU A OE2   1 
ATOM   791  N  N     . LEU A 1 133 ? 17.557 -27.929 -34.263 1.00 63.81  ? 112 LEU A N     1 
ATOM   792  C  CA    . LEU A 1 133 ? 19.034 -27.871 -34.460 1.00 61.75  ? 112 LEU A CA    1 
ATOM   793  C  C     . LEU A 1 133 ? 19.411 -26.781 -35.478 1.00 59.33  ? 112 LEU A C     1 
ATOM   794  O  O     . LEU A 1 133 ? 20.447 -26.120 -35.284 1.00 56.19  ? 112 LEU A O     1 
ATOM   795  C  CB    . LEU A 1 133 ? 19.525 -29.248 -34.909 1.00 65.93  ? 112 LEU A CB    1 
ATOM   796  C  CG    . LEU A 1 133 ? 21.043 -29.409 -34.927 1.00 73.76  ? 112 LEU A CG    1 
ATOM   797  C  CD1   . LEU A 1 133 ? 21.466 -30.652 -34.159 1.00 71.72  ? 112 LEU A CD1   1 
ATOM   798  C  CD2   . LEU A 1 133 ? 21.588 -29.423 -36.354 1.00 75.45  ? 112 LEU A CD2   1 
ATOM   799  N  N     . THR A 1 134 ? 18.577 -26.573 -36.500 1.00 54.96  ? 113 THR A N     1 
ATOM   800  C  CA    . THR A 1 134 ? 18.773 -25.595 -37.605 1.00 57.30  ? 113 THR A CA    1 
ATOM   801  C  C     . THR A 1 134 ? 18.469 -24.163 -37.154 1.00 54.24  ? 113 THR A C     1 
ATOM   802  O  O     . THR A 1 134 ? 19.177 -23.224 -37.608 1.00 55.39  ? 113 THR A O     1 
ATOM   803  C  CB    . THR A 1 134 ? 17.851 -25.935 -38.784 1.00 60.01  ? 113 THR A CB    1 
ATOM   804  O  OG1   . THR A 1 134 ? 18.290 -27.209 -39.263 1.00 55.78  ? 113 THR A OG1   1 
ATOM   805  C  CG2   . THR A 1 134 ? 17.856 -24.883 -39.876 1.00 60.76  ? 113 THR A CG2   1 
ATOM   806  N  N     . ALA A 1 135 ? 17.392 -23.979 -36.391 1.00 48.92  ? 114 ALA A N     1 
ATOM   807  C  CA    . ALA A 1 135 ? 17.035 -22.668 -35.820 1.00 51.41  ? 114 ALA A CA    1 
ATOM   808  C  C     . ALA A 1 135 ? 18.174 -22.254 -34.879 1.00 49.01  ? 114 ALA A C     1 
ATOM   809  O  O     . ALA A 1 135 ? 18.626 -21.101 -34.986 1.00 51.70  ? 114 ALA A O     1 
ATOM   810  C  CB    . ALA A 1 135 ? 15.694 -22.739 -35.135 1.00 52.82  ? 114 ALA A CB    1 
ATOM   811  N  N     . TYR A 1 136 ? 18.673 -23.183 -34.055 1.00 50.84  ? 115 TYR A N     1 
ATOM   812  C  CA    . TYR A 1 136 ? 19.791 -22.949 -33.095 1.00 53.43  ? 115 TYR A CA    1 
ATOM   813  C  C     . TYR A 1 136 ? 21.019 -22.374 -33.820 1.00 62.42  ? 115 TYR A C     1 
ATOM   814  O  O     . TYR A 1 136 ? 21.612 -21.403 -33.298 1.00 61.44  ? 115 TYR A O     1 
ATOM   815  C  CB    . TYR A 1 136 ? 20.170 -24.218 -32.327 1.00 52.59  ? 115 TYR A CB    1 
ATOM   816  C  CG    . TYR A 1 136 ? 21.256 -23.968 -31.313 1.00 53.04  ? 115 TYR A CG    1 
ATOM   817  C  CD1   . TYR A 1 136 ? 20.966 -23.409 -30.076 1.00 50.72  ? 115 TYR A CD1   1 
ATOM   818  C  CD2   . TYR A 1 136 ? 22.587 -24.210 -31.616 1.00 56.61  ? 115 TYR A CD2   1 
ATOM   819  C  CE1   . TYR A 1 136 ? 21.962 -23.125 -29.153 1.00 50.72  ? 115 TYR A CE1   1 
ATOM   820  C  CE2   . TYR A 1 136 ? 23.598 -23.932 -30.706 1.00 55.21  ? 115 TYR A CE2   1 
ATOM   821  C  CZ    . TYR A 1 136 ? 23.285 -23.384 -29.472 1.00 53.14  ? 115 TYR A CZ    1 
ATOM   822  O  OH    . TYR A 1 136 ? 24.277 -23.102 -28.578 1.00 55.00  ? 115 TYR A OH    1 
ATOM   823  N  N     . LEU A 1 137 ? 21.369 -22.907 -35.001 1.00 64.95  ? 116 LEU A N     1 
ATOM   824  C  CA    . LEU A 1 137 ? 22.643 -22.571 -35.698 1.00 61.19  ? 116 LEU A CA    1 
ATOM   825  C  C     . LEU A 1 137 ? 22.528 -21.272 -36.511 1.00 63.68  ? 116 LEU A C     1 
ATOM   826  O  O     . LEU A 1 137 ? 23.573 -20.582 -36.598 1.00 60.79  ? 116 LEU A O     1 
ATOM   827  C  CB    . LEU A 1 137 ? 23.078 -23.768 -36.546 1.00 68.05  ? 116 LEU A CB    1 
ATOM   828  C  CG    . LEU A 1 137 ? 23.437 -25.021 -35.736 1.00 67.66  ? 116 LEU A CG    1 
ATOM   829  C  CD1   . LEU A 1 137 ? 23.469 -26.252 -36.629 1.00 73.28  ? 116 LEU A CD1   1 
ATOM   830  C  CD2   . LEU A 1 137 ? 24.761 -24.858 -34.994 1.00 63.61  ? 116 LEU A CD2   1 
ATOM   831  N  N     . GLU A 1 138 ? 21.337 -20.912 -37.031 1.00 61.23  ? 117 GLU A N     1 
ATOM   832  C  CA    . GLU A 1 138 ? 21.039 -19.557 -37.594 1.00 61.98  ? 117 GLU A CA    1 
ATOM   833  C  C     . GLU A 1 138 ? 21.121 -18.503 -36.471 1.00 56.13  ? 117 GLU A C     1 
ATOM   834  O  O     . GLU A 1 138 ? 21.613 -17.369 -36.747 1.00 49.01  ? 117 GLU A O     1 
ATOM   835  C  CB    . GLU A 1 138 ? 19.669 -19.525 -38.299 1.00 74.48  ? 117 GLU A CB    1 
ATOM   836  C  CG    . GLU A 1 138 ? 19.093 -18.120 -38.605 1.00 77.17  ? 117 GLU A CG    1 
ATOM   837  C  CD    . GLU A 1 138 ? 19.490 -17.427 -39.915 1.00 84.56  ? 117 GLU A CD    1 
ATOM   838  O  OE1   . GLU A 1 138 ? 20.058 -18.115 -40.803 1.00 80.91  ? 117 GLU A OE1   1 
ATOM   839  O  OE2   . GLU A 1 138 ? 19.222 -16.186 -40.066 1.00 73.23  ? 117 GLU A OE2   1 
ATOM   840  N  N     . LEU A 1 139 ? 20.643 -18.832 -35.262 1.00 51.75  ? 118 LEU A N     1 
ATOM   841  C  CA    . LEU A 1 139 ? 20.677 -17.929 -34.069 1.00 48.86  ? 118 LEU A CA    1 
ATOM   842  C  C     . LEU A 1 139 ? 22.144 -17.640 -33.694 1.00 44.82  ? 118 LEU A C     1 
ATOM   843  O  O     . LEU A 1 139 ? 22.569 -16.449 -33.785 1.00 42.86  ? 118 LEU A O     1 
ATOM   844  C  CB    . LEU A 1 139 ? 19.888 -18.577 -32.924 1.00 48.86  ? 118 LEU A CB    1 
ATOM   845  C  CG    . LEU A 1 139 ? 19.573 -17.692 -31.718 1.00 47.85  ? 118 LEU A CG    1 
ATOM   846  C  CD1   . LEU A 1 139 ? 19.086 -16.315 -32.149 1.00 45.79  ? 118 LEU A CD1   1 
ATOM   847  C  CD2   . LEU A 1 139 ? 18.529 -18.360 -30.833 1.00 49.00  ? 118 LEU A CD2   1 
ATOM   848  N  N     . ALA A 1 140 ? 22.921 -18.687 -33.398 1.00 41.26  ? 119 ALA A N     1 
ATOM   849  C  CA    . ALA A 1 140 ? 24.391 -18.616 -33.240 1.00 44.16  ? 119 ALA A CA    1 
ATOM   850  C  C     . ALA A 1 140 ? 24.997 -17.823 -34.411 1.00 49.19  ? 119 ALA A C     1 
ATOM   851  O  O     . ALA A 1 140 ? 25.768 -16.862 -34.139 1.00 54.05  ? 119 ALA A O     1 
ATOM   852  C  CB    . ALA A 1 140 ? 24.965 -20.007 -33.153 1.00 44.24  ? 119 ALA A CB    1 
ATOM   853  N  N     . GLY A 1 141 ? 24.640 -18.182 -35.658 1.00 45.86  ? 120 GLY A N     1 
ATOM   854  C  CA    . GLY A 1 141 ? 25.155 -17.559 -36.894 1.00 35.81  ? 120 GLY A CA    1 
ATOM   855  C  C     . GLY A 1 141 ? 24.885 -16.066 -36.911 1.00 39.45  ? 120 GLY A C     1 
ATOM   856  O  O     . GLY A 1 141 ? 25.816 -15.304 -37.189 1.00 38.67  ? 120 GLY A O     1 
ATOM   857  N  N     . ALA A 1 142 ? 23.650 -15.660 -36.601 1.00 40.33  ? 121 ALA A N     1 
ATOM   858  C  CA    . ALA A 1 142 ? 23.198 -14.247 -36.549 1.00 40.83  ? 121 ALA A CA    1 
ATOM   859  C  C     . ALA A 1 142 ? 24.005 -13.469 -35.504 1.00 39.02  ? 121 ALA A C     1 
ATOM   860  O  O     . ALA A 1 142 ? 24.434 -12.322 -35.803 1.00 40.89  ? 121 ALA A O     1 
ATOM   861  C  CB    . ALA A 1 142 ? 21.721 -14.185 -36.235 1.00 42.16  ? 121 ALA A CB    1 
ATOM   862  N  N     . LEU A 1 143 ? 24.235 -14.072 -34.330 1.00 41.30  ? 122 LEU A N     1 
ATOM   863  C  CA    . LEU A 1 143 ? 24.995 -13.421 -33.225 1.00 39.30  ? 122 LEU A CA    1 
ATOM   864  C  C     . LEU A 1 143 ? 26.423 -13.161 -33.734 1.00 38.23  ? 122 LEU A C     1 
ATOM   865  O  O     . LEU A 1 143 ? 26.912 -12.015 -33.568 1.00 36.59  ? 122 LEU A O     1 
ATOM   866  C  CB    . LEU A 1 143 ? 24.920 -14.290 -31.954 1.00 41.77  ? 122 LEU A CB    1 
ATOM   867  C  CG    . LEU A 1 143 ? 25.601 -13.756 -30.678 1.00 40.68  ? 122 LEU A CG    1 
ATOM   868  C  CD1   . LEU A 1 143 ? 25.138 -12.366 -30.300 1.00 41.77  ? 122 LEU A CD1   1 
ATOM   869  C  CD2   . LEU A 1 143 ? 25.378 -14.691 -29.504 1.00 41.87  ? 122 LEU A CD2   1 
ATOM   870  N  N     . GLU A 1 144 ? 27.040 -14.142 -34.414 1.00 40.08  ? 123 GLU A N     1 
ATOM   871  C  CA    . GLU A 1 144 ? 28.422 -14.021 -34.952 1.00 38.14  ? 123 GLU A CA    1 
ATOM   872  C  C     . GLU A 1 144 ? 28.482 -12.887 -35.980 1.00 41.18  ? 123 GLU A C     1 
ATOM   873  O  O     . GLU A 1 144 ? 29.480 -12.109 -35.951 1.00 37.14  ? 123 GLU A O     1 
ATOM   874  C  CB    . GLU A 1 144 ? 28.893 -15.333 -35.553 1.00 38.28  ? 123 GLU A CB    1 
ATOM   875  C  CG    . GLU A 1 144 ? 29.343 -16.310 -34.490 1.00 41.77  ? 123 GLU A CG    1 
ATOM   876  C  CD    . GLU A 1 144 ? 29.603 -17.715 -35.004 1.00 41.88  ? 123 GLU A CD    1 
ATOM   877  O  OE1   . GLU A 1 144 ? 29.567 -17.914 -36.238 1.00 46.92  ? 123 GLU A OE1   1 
ATOM   878  O  OE2   . GLU A 1 144 ? 29.814 -18.609 -34.169 1.00 44.22  ? 123 GLU A OE2   1 
ATOM   879  N  N     . ALA A 1 145 ? 27.451 -12.790 -36.831 1.00 40.59  ? 124 ALA A N     1 
ATOM   880  C  CA    . ALA A 1 145 ? 27.296 -11.738 -37.861 1.00 40.19  ? 124 ALA A CA    1 
ATOM   881  C  C     . ALA A 1 145 ? 27.369 -10.357 -37.199 1.00 36.65  ? 124 ALA A C     1 
ATOM   882  O  O     . ALA A 1 145 ? 28.086 -9.467  -37.717 1.00 35.01  ? 124 ALA A O     1 
ATOM   883  C  CB    . ALA A 1 145 ? 26.007 -11.945 -38.621 1.00 41.22  ? 124 ALA A CB    1 
ATOM   884  N  N     . ILE A 1 146 ? 26.706 -10.171 -36.061 1.00 38.79  ? 125 ILE A N     1 
ATOM   885  C  CA    . ILE A 1 146 ? 26.781 -8.865  -35.334 1.00 40.85  ? 125 ILE A CA    1 
ATOM   886  C  C     . ILE A 1 146 ? 28.168 -8.731  -34.696 1.00 36.40  ? 125 ILE A C     1 
ATOM   887  O  O     . ILE A 1 146 ? 28.811 -7.664  -34.847 1.00 37.44  ? 125 ILE A O     1 
ATOM   888  C  CB    . ILE A 1 146 ? 25.635 -8.742  -34.319 1.00 47.47  ? 125 ILE A CB    1 
ATOM   889  C  CG1   . ILE A 1 146 ? 24.287 -8.742  -35.050 1.00 50.74  ? 125 ILE A CG1   1 
ATOM   890  C  CG2   . ILE A 1 146 ? 25.806 -7.501  -33.444 1.00 48.29  ? 125 ILE A CG2   1 
ATOM   891  C  CD1   . ILE A 1 146 ? 23.102 -9.140  -34.196 1.00 53.55  ? 125 ILE A CD1   1 
ATOM   892  N  N     . ALA A 1 147 ? 28.609 -9.783  -34.017 1.00 39.67  ? 126 ALA A N     1 
ATOM   893  C  CA    . ALA A 1 147 ? 29.920 -9.874  -33.323 1.00 40.43  ? 126 ALA A CA    1 
ATOM   894  C  C     . ALA A 1 147 ? 31.040 -9.313  -34.210 1.00 41.78  ? 126 ALA A C     1 
ATOM   895  O  O     . ALA A 1 147 ? 31.779 -8.405  -33.724 1.00 37.01  ? 126 ALA A O     1 
ATOM   896  C  CB    . ALA A 1 147 ? 30.186 -11.303 -32.923 1.00 37.76  ? 126 ALA A CB    1 
ATOM   897  N  N     . GLU A 1 148 ? 31.147 -9.789  -35.462 1.00 41.98  ? 127 GLU A N     1 
ATOM   898  C  CA    . GLU A 1 148 ? 32.295 -9.474  -36.360 1.00 43.63  ? 127 GLU A CA    1 
ATOM   899  C  C     . GLU A 1 148 ? 32.268 -8.001  -36.762 1.00 40.06  ? 127 GLU A C     1 
ATOM   900  O  O     . GLU A 1 148 ? 33.323 -7.542  -37.192 1.00 35.47  ? 127 GLU A O     1 
ATOM   901  C  CB    . GLU A 1 148 ? 32.372 -10.391 -37.582 1.00 51.75  ? 127 GLU A CB    1 
ATOM   902  C  CG    . GLU A 1 148 ? 31.152 -10.360 -38.481 1.00 62.80  ? 127 GLU A CG    1 
ATOM   903  C  CD    . GLU A 1 148 ? 30.951 -11.635 -39.291 1.00 76.41  ? 127 GLU A CD    1 
ATOM   904  O  OE1   . GLU A 1 148 ? 31.866 -12.497 -39.260 1.00 75.33  ? 127 GLU A OE1   1 
ATOM   905  O  OE2   . GLU A 1 148 ? 29.881 -11.771 -39.953 1.00 74.72  ? 127 GLU A OE2   1 
ATOM   906  N  N     . LYS A 1 149 ? 31.164 -7.273  -36.544 1.00 42.34  ? 128 LYS A N     1 
ATOM   907  C  CA    . LYS A 1 149 ? 31.076 -5.804  -36.818 1.00 45.52  ? 128 LYS A CA    1 
ATOM   908  C  C     . LYS A 1 149 ? 31.591 -4.986  -35.627 1.00 42.83  ? 128 LYS A C     1 
ATOM   909  O  O     . LYS A 1 149 ? 31.680 -3.736  -35.773 1.00 42.36  ? 128 LYS A O     1 
ATOM   910  C  CB    . LYS A 1 149 ? 29.637 -5.348  -37.100 1.00 49.01  ? 128 LYS A CB    1 
ATOM   911  C  CG    . LYS A 1 149 ? 28.875 -6.136  -38.157 1.00 59.34  ? 128 LYS A CG    1 
ATOM   912  C  CD    . LYS A 1 149 ? 29.234 -5.768  -39.574 1.00 66.20  ? 128 LYS A CD    1 
ATOM   913  C  CE    . LYS A 1 149 ? 28.663 -4.432  -39.995 1.00 75.67  ? 128 LYS A CE    1 
ATOM   914  N  NZ    . LYS A 1 149 ? 27.186 -4.425  -39.890 1.00 82.31  ? 128 LYS A NZ    1 
ATOM   915  N  N     . VAL A 1 150 ? 31.871 -5.639  -34.490 1.00 37.64  ? 129 VAL A N     1 
ATOM   916  C  CA    . VAL A 1 150 ? 32.173 -4.978  -33.182 1.00 36.67  ? 129 VAL A CA    1 
ATOM   917  C  C     . VAL A 1 150 ? 33.676 -4.985  -32.966 1.00 32.53  ? 129 VAL A C     1 
ATOM   918  O  O     . VAL A 1 150 ? 34.248 -6.035  -32.705 1.00 38.49  ? 129 VAL A O     1 
ATOM   919  C  CB    . VAL A 1 150 ? 31.441 -5.651  -32.006 1.00 36.97  ? 129 VAL A CB    1 
ATOM   920  C  CG1   . VAL A 1 150 ? 31.819 -5.048  -30.669 1.00 40.76  ? 129 VAL A CG1   1 
ATOM   921  C  CG2   . VAL A 1 150 ? 29.948 -5.591  -32.190 1.00 39.96  ? 129 VAL A CG2   1 
ATOM   922  N  N     . PRO A 1 151 ? 34.349 -3.815  -33.019 1.00 31.96  ? 130 PRO A N     1 
ATOM   923  C  CA    . PRO A 1 151 ? 35.799 -3.767  -32.852 1.00 34.38  ? 130 PRO A CA    1 
ATOM   924  C  C     . PRO A 1 151 ? 36.210 -4.194  -31.435 1.00 34.75  ? 130 PRO A C     1 
ATOM   925  O  O     . PRO A 1 151 ? 35.629 -3.716  -30.485 1.00 36.54  ? 130 PRO A O     1 
ATOM   926  C  CB    . PRO A 1 151 ? 36.166 -2.299  -33.123 1.00 33.39  ? 130 PRO A CB    1 
ATOM   927  C  CG    . PRO A 1 151 ? 34.938 -1.708  -33.782 1.00 35.31  ? 130 PRO A CG    1 
ATOM   928  C  CD    . PRO A 1 151 ? 33.766 -2.482  -33.225 1.00 31.98  ? 130 PRO A CD    1 
ATOM   929  N  N     . LEU A 1 152 ? 37.224 -5.046  -31.324 1.00 33.83  ? 131 LEU A N     1 
ATOM   930  C  CA    . LEU A 1 152 ? 37.610 -5.712  -30.057 1.00 37.04  ? 131 LEU A CA    1 
ATOM   931  C  C     . LEU A 1 152 ? 38.181 -4.688  -29.083 1.00 38.20  ? 131 LEU A C     1 
ATOM   932  O  O     . LEU A 1 152 ? 38.045 -4.900  -27.881 1.00 45.37  ? 131 LEU A O     1 
ATOM   933  C  CB    . LEU A 1 152 ? 38.618 -6.822  -30.363 1.00 36.37  ? 131 LEU A CB    1 
ATOM   934  C  CG    . LEU A 1 152 ? 38.012 -7.983  -31.137 1.00 38.57  ? 131 LEU A CG    1 
ATOM   935  C  CD1   . LEU A 1 152 ? 39.033 -9.098  -31.332 1.00 44.83  ? 131 LEU A CD1   1 
ATOM   936  C  CD2   . LEU A 1 152 ? 36.784 -8.525  -30.418 1.00 36.98  ? 131 LEU A CD2   1 
ATOM   937  N  N     . ASP A 1 153 ? 38.766 -3.610  -29.580 1.00 39.06  ? 132 ASP A N     1 
ATOM   938  C  CA    . ASP A 1 153 ? 39.429 -2.583  -28.736 1.00 43.36  ? 132 ASP A CA    1 
ATOM   939  C  C     . ASP A 1 153 ? 38.478 -1.399  -28.487 1.00 40.70  ? 132 ASP A C     1 
ATOM   940  O  O     . ASP A 1 153 ? 38.777 -0.636  -27.584 1.00 42.86  ? 132 ASP A O     1 
ATOM   941  C  CB    . ASP A 1 153 ? 40.786 -2.178  -29.338 1.00 48.51  ? 132 ASP A CB    1 
ATOM   942  C  CG    . ASP A 1 153 ? 40.753 -1.376  -30.635 1.00 52.49  ? 132 ASP A CG    1 
ATOM   943  O  OD1   . ASP A 1 153 ? 39.685 -1.378  -31.337 1.00 51.06  ? 132 ASP A OD1   1 
ATOM   944  O  OD2   . ASP A 1 153 ? 41.813 -0.749  -30.952 1.00 57.25  ? 132 ASP A OD2   1 
ATOM   945  N  N     . ALA A 1 154 ? 37.368 -1.244  -29.219 1.00 38.32  ? 133 ALA A N     1 
ATOM   946  C  CA    . ALA A 1 154 ? 36.457 -0.086  -29.029 1.00 36.66  ? 133 ALA A CA    1 
ATOM   947  C  C     . ALA A 1 154 ? 35.041 -0.436  -29.459 1.00 34.72  ? 133 ALA A C     1 
ATOM   948  O  O     . ALA A 1 154 ? 34.543 0.117   -30.439 1.00 37.32  ? 133 ALA A O     1 
ATOM   949  C  CB    . ALA A 1 154 ? 36.978 1.109   -29.792 1.00 38.50  ? 133 ALA A CB    1 
ATOM   950  N  N     . PRO A 1 155 ? 34.353 -1.342  -28.728 1.00 34.83  ? 134 PRO A N     1 
ATOM   951  C  CA    . PRO A 1 155 ? 32.990 -1.763  -29.072 1.00 35.06  ? 134 PRO A CA    1 
ATOM   952  C  C     . PRO A 1 155 ? 32.010 -0.578  -29.194 1.00 36.42  ? 134 PRO A C     1 
ATOM   953  O  O     . PRO A 1 155 ? 31.067 -0.653  -29.984 1.00 37.46  ? 134 PRO A O     1 
ATOM   954  C  CB    . PRO A 1 155 ? 32.554 -2.675  -27.918 1.00 33.56  ? 134 PRO A CB    1 
ATOM   955  C  CG    . PRO A 1 155 ? 33.561 -2.437  -26.815 1.00 35.13  ? 134 PRO A CG    1 
ATOM   956  C  CD    . PRO A 1 155 ? 34.828 -1.963  -27.484 1.00 35.06  ? 134 PRO A CD    1 
ATOM   957  N  N     . TRP A 1 156 ? 32.301 0.521   -28.493 1.00 36.96  ? 135 TRP A N     1 
ATOM   958  C  CA    . TRP A 1 156 ? 31.531 1.790   -28.611 1.00 38.77  ? 135 TRP A CA    1 
ATOM   959  C  C     . TRP A 1 156 ? 31.640 2.412   -30.009 1.00 39.48  ? 135 TRP A C     1 
ATOM   960  O  O     . TRP A 1 156 ? 30.892 3.374   -30.235 1.00 40.48  ? 135 TRP A O     1 
ATOM   961  C  CB    . TRP A 1 156 ? 31.972 2.795   -27.551 1.00 37.08  ? 135 TRP A CB    1 
ATOM   962  C  CG    . TRP A 1 156 ? 33.412 3.185   -27.593 1.00 39.30  ? 135 TRP A CG    1 
ATOM   963  C  CD1   . TRP A 1 156 ? 33.956 4.228   -28.282 1.00 40.20  ? 135 TRP A CD1   1 
ATOM   964  C  CD2   . TRP A 1 156 ? 34.481 2.581   -26.844 1.00 40.88  ? 135 TRP A CD2   1 
ATOM   965  N  NE1   . TRP A 1 156 ? 35.296 4.297   -28.028 1.00 42.98  ? 135 TRP A NE1   1 
ATOM   966  C  CE2   . TRP A 1 156 ? 35.651 3.293   -27.164 1.00 40.41  ? 135 TRP A CE2   1 
ATOM   967  C  CE3   . TRP A 1 156 ? 34.564 1.517   -25.935 1.00 41.22  ? 135 TRP A CE3   1 
ATOM   968  C  CZ2   . TRP A 1 156 ? 36.890 2.974   -26.608 1.00 39.35  ? 135 TRP A CZ2   1 
ATOM   969  C  CZ3   . TRP A 1 156 ? 35.789 1.195   -25.398 1.00 40.64  ? 135 TRP A CZ3   1 
ATOM   970  C  CH2   . TRP A 1 156 ? 36.934 1.920   -25.728 1.00 40.29  ? 135 TRP A CH2   1 
ATOM   971  N  N     . LEU A 1 157 ? 32.540 1.924   -30.881 1.00 37.54  ? 136 LEU A N     1 
ATOM   972  C  CA    . LEU A 1 157 ? 32.726 2.418   -32.274 1.00 37.61  ? 136 LEU A CA    1 
ATOM   973  C  C     . LEU A 1 157 ? 32.055 1.489   -33.296 1.00 35.58  ? 136 LEU A C     1 
ATOM   974  O  O     . LEU A 1 157 ? 32.225 1.717   -34.497 1.00 38.67  ? 136 LEU A O     1 
ATOM   975  C  CB    . LEU A 1 157 ? 34.228 2.572   -32.550 1.00 41.28  ? 136 LEU A CB    1 
ATOM   976  C  CG    . LEU A 1 157 ? 34.892 3.727   -31.809 1.00 42.03  ? 136 LEU A CG    1 
ATOM   977  C  CD1   . LEU A 1 157 ? 36.373 3.834   -32.153 1.00 40.24  ? 136 LEU A CD1   1 
ATOM   978  C  CD2   . LEU A 1 157 ? 34.167 5.030   -32.118 1.00 45.02  ? 136 LEU A CD2   1 
ATOM   979  N  N     . ALA A 1 158 ? 31.314 0.475   -32.872 1.00 35.75  ? 137 ALA A N     1 
ATOM   980  C  CA    . ALA A 1 158 ? 30.597 -0.404  -33.826 1.00 39.79  ? 137 ALA A CA    1 
ATOM   981  C  C     . ALA A 1 158 ? 29.568 0.439   -34.593 1.00 45.09  ? 137 ALA A C     1 
ATOM   982  O  O     . ALA A 1 158 ? 28.980 1.380   -34.056 1.00 42.91  ? 137 ALA A O     1 
ATOM   983  C  CB    . ALA A 1 158 ? 29.979 -1.581  -33.103 1.00 36.60  ? 137 ALA A CB    1 
ATOM   984  N  N     . PRO A 1 159 ? 29.333 0.160   -35.891 1.00 46.35  ? 138 PRO A N     1 
ATOM   985  C  CA    . PRO A 1 159 ? 28.426 0.978   -36.698 1.00 48.15  ? 138 PRO A CA    1 
ATOM   986  C  C     . PRO A 1 159 ? 27.021 1.203   -36.092 1.00 46.90  ? 138 PRO A C     1 
ATOM   987  O  O     . PRO A 1 159 ? 26.573 2.309   -36.090 1.00 46.58  ? 138 PRO A O     1 
ATOM   988  C  CB    . PRO A 1 159 ? 28.285 0.199   -38.012 1.00 48.54  ? 138 PRO A CB    1 
ATOM   989  C  CG    . PRO A 1 159 ? 29.489 -0.720  -38.067 1.00 51.47  ? 138 PRO A CG    1 
ATOM   990  C  CD    . PRO A 1 159 ? 29.916 -0.965  -36.635 1.00 50.14  ? 138 PRO A CD    1 
ATOM   991  N  N     . GLU A 1 160 ? 26.349 0.173   -35.586 1.00 46.50  ? 139 GLU A N     1 
ATOM   992  C  CA    . GLU A 1 160 ? 25.050 0.355   -34.884 1.00 51.83  ? 139 GLU A CA    1 
ATOM   993  C  C     . GLU A 1 160 ? 25.255 0.270   -33.353 1.00 50.91  ? 139 GLU A C     1 
ATOM   994  O  O     . GLU A 1 160 ? 24.413 -0.343  -32.666 1.00 50.41  ? 139 GLU A O     1 
ATOM   995  C  CB    . GLU A 1 160 ? 24.045 -0.641  -35.478 1.00 59.93  ? 139 GLU A CB    1 
ATOM   996  C  CG    . GLU A 1 160 ? 23.602 -0.291  -36.905 1.00 62.32  ? 139 GLU A CG    1 
ATOM   997  C  CD    . GLU A 1 160 ? 23.095 1.141   -37.109 1.00 63.63  ? 139 GLU A CD    1 
ATOM   998  O  OE1   . GLU A 1 160 ? 22.300 1.612   -36.266 1.00 69.62  ? 139 GLU A OE1   1 
ATOM   999  O  OE2   . GLU A 1 160 ? 23.508 1.802   -38.093 1.00 50.57  ? 139 GLU A OE2   1 
ATOM   1000 N  N     . ALA A 1 161 ? 26.306 0.906   -32.816 1.00 42.98  ? 140 ALA A N     1 
ATOM   1001 C  CA    . ALA A 1 161 ? 26.669 0.824   -31.381 1.00 41.53  ? 140 ALA A CA    1 
ATOM   1002 C  C     . ALA A 1 161 ? 25.489 1.322   -30.533 1.00 43.08  ? 140 ALA A C     1 
ATOM   1003 O  O     . ALA A 1 161 ? 25.083 0.591   -29.609 1.00 39.24  ? 140 ALA A O     1 
ATOM   1004 C  CB    . ALA A 1 161 ? 27.926 1.594   -31.085 1.00 37.01  ? 140 ALA A CB    1 
ATOM   1005 N  N     . ALA A 1 162 ? 24.931 2.495   -30.858 1.00 43.83  ? 141 ALA A N     1 
ATOM   1006 C  CA    . ALA A 1 162 ? 23.807 3.110   -30.110 1.00 44.34  ? 141 ALA A CA    1 
ATOM   1007 C  C     . ALA A 1 162 ? 22.660 2.095   -29.992 1.00 42.35  ? 141 ALA A C     1 
ATOM   1008 O  O     . ALA A 1 162 ? 22.231 1.798   -28.841 1.00 40.12  ? 141 ALA A O     1 
ATOM   1009 C  CB    . ALA A 1 162 ? 23.385 4.397   -30.772 1.00 46.03  ? 141 ALA A CB    1 
ATOM   1010 N  N     . ALA A 1 163 ? 22.246 1.505   -31.114 1.00 38.47  ? 142 ALA A N     1 
ATOM   1011 C  CA    . ALA A 1 163 ? 21.134 0.526   -31.171 1.00 41.21  ? 142 ALA A CA    1 
ATOM   1012 C  C     . ALA A 1 163 ? 21.478 -0.767  -30.420 1.00 43.96  ? 142 ALA A C     1 
ATOM   1013 O  O     . ALA A 1 163 ? 20.576 -1.306  -29.728 1.00 44.45  ? 142 ALA A O     1 
ATOM   1014 C  CB    . ALA A 1 163 ? 20.743 0.228   -32.598 1.00 42.69  ? 142 ALA A CB    1 
ATOM   1015 N  N     . TRP A 1 164 ? 22.692 -1.305  -30.541 1.00 44.19  ? 143 TRP A N     1 
ATOM   1016 C  CA    . TRP A 1 164 ? 23.001 -2.617  -29.891 1.00 43.56  ? 143 TRP A CA    1 
ATOM   1017 C  C     . TRP A 1 164 ? 23.211 -2.433  -28.373 1.00 40.72  ? 143 TRP A C     1 
ATOM   1018 O  O     . TRP A 1 164 ? 23.012 -3.417  -27.633 1.00 36.40  ? 143 TRP A O     1 
ATOM   1019 C  CB    . TRP A 1 164 ? 24.181 -3.323  -30.582 1.00 47.40  ? 143 TRP A CB    1 
ATOM   1020 C  CG    . TRP A 1 164 ? 23.941 -3.616  -32.036 1.00 51.50  ? 143 TRP A CG    1 
ATOM   1021 C  CD1   . TRP A 1 164 ? 22.730 -3.834  -32.628 1.00 52.82  ? 143 TRP A CD1   1 
ATOM   1022 C  CD2   . TRP A 1 164 ? 24.922 -3.764  -33.079 1.00 49.38  ? 143 TRP A CD2   1 
ATOM   1023 N  NE1   . TRP A 1 164 ? 22.885 -4.058  -33.965 1.00 50.38  ? 143 TRP A NE1   1 
ATOM   1024 C  CE2   . TRP A 1 164 ? 24.220 -4.044  -34.269 1.00 56.55  ? 143 TRP A CE2   1 
ATOM   1025 C  CE3   . TRP A 1 164 ? 26.317 -3.705  -33.132 1.00 52.65  ? 143 TRP A CE3   1 
ATOM   1026 C  CZ2   . TRP A 1 164 ? 24.870 -4.249  -35.491 1.00 57.79  ? 143 TRP A CZ2   1 
ATOM   1027 C  CZ3   . TRP A 1 164 ? 26.960 -3.914  -34.336 1.00 53.76  ? 143 TRP A CZ3   1 
ATOM   1028 C  CH2   . TRP A 1 164 ? 26.245 -4.177  -35.501 1.00 53.38  ? 143 TRP A CH2   1 
ATOM   1029 N  N     . ASP A 1 165 ? 23.550 -1.229  -27.899 1.00 36.16  ? 144 ASP A N     1 
ATOM   1030 C  CA    . ASP A 1 165 ? 23.775 -0.968  -26.451 1.00 39.39  ? 144 ASP A CA    1 
ATOM   1031 C  C     . ASP A 1 165 ? 22.476 -0.579  -25.728 1.00 43.98  ? 144 ASP A C     1 
ATOM   1032 O  O     . ASP A 1 165 ? 22.495 -0.419  -24.497 1.00 51.74  ? 144 ASP A O     1 
ATOM   1033 C  CB    . ASP A 1 165 ? 24.780 0.153   -26.216 1.00 39.01  ? 144 ASP A CB    1 
ATOM   1034 C  CG    . ASP A 1 165 ? 25.503 0.000   -24.889 1.00 41.80  ? 144 ASP A CG    1 
ATOM   1035 O  OD1   . ASP A 1 165 ? 25.625 -1.172  -24.409 1.00 44.94  ? 144 ASP A OD1   1 
ATOM   1036 O  OD2   . ASP A 1 165 ? 25.960 1.034   -24.360 1.00 40.37  ? 144 ASP A OD2   1 
ATOM   1037 N  N     . ALA A 1 166 ? 21.386 -0.407  -26.458 1.00 41.51  ? 145 ALA A N     1 
ATOM   1038 C  CA    . ALA A 1 166 ? 20.095 0.053   -25.911 1.00 40.15  ? 145 ALA A CA    1 
ATOM   1039 C  C     . ALA A 1 166 ? 19.157 -1.150  -25.795 1.00 41.35  ? 145 ALA A C     1 
ATOM   1040 O  O     . ALA A 1 166 ? 17.995 -0.937  -25.372 1.00 51.27  ? 145 ALA A O     1 
ATOM   1041 C  CB    . ALA A 1 166 ? 19.539 1.143   -26.801 1.00 36.93  ? 145 ALA A CB    1 
ATOM   1042 N  N     . THR A 1 167 ? 19.672 -2.348  -26.101 1.00 35.86  ? 146 THR A N     1 
ATOM   1043 C  CA    . THR A 1 167 ? 18.921 -3.619  -26.270 1.00 40.15  ? 146 THR A CA    1 
ATOM   1044 C  C     . THR A 1 167 ? 19.534 -4.702  -25.372 1.00 34.53  ? 146 THR A C     1 
ATOM   1045 O  O     . THR A 1 167 ? 20.737 -4.810  -25.324 1.00 34.50  ? 146 THR A O     1 
ATOM   1046 C  CB    . THR A 1 167 ? 19.007 -4.131  -27.720 1.00 42.96  ? 146 THR A CB    1 
ATOM   1047 O  OG1   . THR A 1 167 ? 18.772 -3.031  -28.592 1.00 49.18  ? 146 THR A OG1   1 
ATOM   1048 C  CG2   . THR A 1 167 ? 18.030 -5.240  -28.045 1.00 42.57  ? 146 THR A CG2   1 
ATOM   1049 N  N     . THR A 1 168 ? 18.735 -5.544  -24.749 1.00 34.90  ? 147 THR A N     1 
ATOM   1050 C  CA    . THR A 1 168 ? 19.263 -6.745  -24.069 1.00 37.17  ? 147 THR A CA    1 
ATOM   1051 C  C     . THR A 1 168 ? 19.478 -7.841  -25.117 1.00 36.20  ? 147 THR A C     1 
ATOM   1052 O  O     . THR A 1 168 ? 18.822 -7.814  -26.163 1.00 31.88  ? 147 THR A O     1 
ATOM   1053 C  CB    . THR A 1 168 ? 18.319 -7.203  -22.959 1.00 37.86  ? 147 THR A CB    1 
ATOM   1054 O  OG1   . THR A 1 168 ? 17.152 -7.685  -23.611 1.00 37.59  ? 147 THR A OG1   1 
ATOM   1055 C  CG2   . THR A 1 168 ? 17.980 -6.098  -21.985 1.00 39.46  ? 147 THR A CG2   1 
ATOM   1056 N  N     . LEU A 1 169 ? 20.340 -8.802  -24.814 1.00 36.28  ? 148 LEU A N     1 
ATOM   1057 C  CA    . LEU A 1 169 ? 20.455 -10.053 -25.596 1.00 36.22  ? 148 LEU A CA    1 
ATOM   1058 C  C     . LEU A 1 169 ? 19.082 -10.740 -25.628 1.00 36.81  ? 148 LEU A C     1 
ATOM   1059 O  O     . LEU A 1 169 ? 18.725 -11.283 -26.701 1.00 42.35  ? 148 LEU A O     1 
ATOM   1060 C  CB    . LEU A 1 169 ? 21.533 -10.959 -24.991 1.00 35.57  ? 148 LEU A CB    1 
ATOM   1061 C  CG    . LEU A 1 169 ? 21.813 -12.252 -25.754 1.00 34.18  ? 148 LEU A CG    1 
ATOM   1062 C  CD1   . LEU A 1 169 ? 22.455 -11.949 -27.109 1.00 33.84  ? 148 LEU A CD1   1 
ATOM   1063 C  CD2   . LEU A 1 169 ? 22.697 -13.181 -24.923 1.00 34.83  ? 148 LEU A CD2   1 
ATOM   1064 N  N     . ARG A 1 170 ? 18.313 -10.684 -24.537 1.00 36.00  ? 149 ARG A N     1 
ATOM   1065 C  CA    . ARG A 1 170 ? 16.993 -11.362 -24.464 1.00 38.45  ? 149 ARG A CA    1 
ATOM   1066 C  C     . ARG A 1 170 ? 16.058 -10.756 -25.512 1.00 39.30  ? 149 ARG A C     1 
ATOM   1067 O  O     . ARG A 1 170 ? 15.393 -11.528 -26.204 1.00 43.51  ? 149 ARG A O     1 
ATOM   1068 C  CB    . ARG A 1 170 ? 16.317 -11.279 -23.095 1.00 39.55  ? 149 ARG A CB    1 
ATOM   1069 C  CG    . ARG A 1 170 ? 14.920 -11.882 -23.131 1.00 40.89  ? 149 ARG A CG    1 
ATOM   1070 C  CD    . ARG A 1 170 ? 14.494 -12.589 -21.885 1.00 47.05  ? 149 ARG A CD    1 
ATOM   1071 N  NE    . ARG A 1 170 ? 15.529 -13.432 -21.284 1.00 47.80  ? 149 ARG A NE    1 
ATOM   1072 C  CZ    . ARG A 1 170 ? 15.536 -13.829 -20.007 1.00 44.45  ? 149 ARG A CZ    1 
ATOM   1073 N  NH1   . ARG A 1 170 ? 14.552 -13.476 -19.184 1.00 42.81  ? 149 ARG A NH1   1 
ATOM   1074 N  NH2   . ARG A 1 170 ? 16.526 -14.583 -19.559 1.00 44.19  ? 149 ARG A NH2   1 
ATOM   1075 N  N     . GLU A 1 171 ? 16.028 -9.432  -25.627 1.00 39.95  ? 150 GLU A N     1 
ATOM   1076 C  CA    . GLU A 1 171 ? 15.143 -8.735  -26.595 1.00 42.57  ? 150 GLU A CA    1 
ATOM   1077 C  C     . GLU A 1 171 ? 15.571 -9.105  -28.031 1.00 44.62  ? 150 GLU A C     1 
ATOM   1078 O  O     . GLU A 1 171 ? 14.684 -9.375  -28.850 1.00 43.81  ? 150 GLU A O     1 
ATOM   1079 C  CB    . GLU A 1 171 ? 15.154 -7.235  -26.315 1.00 41.00  ? 150 GLU A CB    1 
ATOM   1080 C  CG    . GLU A 1 171 ? 14.124 -6.468  -27.118 1.00 47.81  ? 150 GLU A CG    1 
ATOM   1081 C  CD    . GLU A 1 171 ? 14.345 -4.962  -27.210 1.00 52.69  ? 150 GLU A CD    1 
ATOM   1082 O  OE1   . GLU A 1 171 ? 15.069 -4.405  -26.353 1.00 54.11  ? 150 GLU A OE1   1 
ATOM   1083 O  OE2   . GLU A 1 171 ? 13.771 -4.352  -28.135 1.00 58.21  ? 150 GLU A OE2   1 
ATOM   1084 N  N     . TRP A 1 172 ? 16.877 -9.165  -28.329 1.00 42.70  ? 151 TRP A N     1 
ATOM   1085 C  CA    . TRP A 1 172 ? 17.393 -9.648  -29.638 1.00 40.41  ? 151 TRP A CA    1 
ATOM   1086 C  C     . TRP A 1 172 ? 16.997 -11.113 -29.873 1.00 38.47  ? 151 TRP A C     1 
ATOM   1087 O  O     . TRP A 1 172 ? 16.560 -11.403 -30.991 1.00 47.28  ? 151 TRP A O     1 
ATOM   1088 C  CB    . TRP A 1 172 ? 18.907 -9.435  -29.770 1.00 42.65  ? 151 TRP A CB    1 
ATOM   1089 C  CG    . TRP A 1 172 ? 19.502 -10.058 -30.991 1.00 44.03  ? 151 TRP A CG    1 
ATOM   1090 C  CD1   . TRP A 1 172 ? 19.639 -9.476  -32.218 1.00 42.28  ? 151 TRP A CD1   1 
ATOM   1091 C  CD2   . TRP A 1 172 ? 20.004 -11.402 -31.122 1.00 42.08  ? 151 TRP A CD2   1 
ATOM   1092 N  NE1   . TRP A 1 172 ? 20.210 -10.358 -33.091 1.00 42.21  ? 151 TRP A NE1   1 
ATOM   1093 C  CE2   . TRP A 1 172 ? 20.430 -11.550 -32.453 1.00 41.11  ? 151 TRP A CE2   1 
ATOM   1094 C  CE3   . TRP A 1 172 ? 20.169 -12.478 -30.243 1.00 45.45  ? 151 TRP A CE3   1 
ATOM   1095 C  CZ2   . TRP A 1 172 ? 21.009 -12.728 -32.923 1.00 43.67  ? 151 TRP A CZ2   1 
ATOM   1096 C  CZ3   . TRP A 1 172 ? 20.733 -13.644 -30.711 1.00 46.07  ? 151 TRP A CZ3   1 
ATOM   1097 C  CH2   . TRP A 1 172 ? 21.156 -13.763 -32.035 1.00 41.27  ? 151 TRP A CH2   1 
ATOM   1098 N  N     . VAL A 1 173 ? 17.122 -12.017 -28.902 1.00 41.30  ? 152 VAL A N     1 
ATOM   1099 C  CA    . VAL A 1 173 ? 16.709 -13.444 -29.113 1.00 42.01  ? 152 VAL A CA    1 
ATOM   1100 C  C     . VAL A 1 173 ? 15.221 -13.484 -29.485 1.00 47.72  ? 152 VAL A C     1 
ATOM   1101 O  O     . VAL A 1 173 ? 14.874 -14.239 -30.409 1.00 48.37  ? 152 VAL A O     1 
ATOM   1102 C  CB    . VAL A 1 173 ? 16.977 -14.351 -27.901 1.00 38.68  ? 152 VAL A CB    1 
ATOM   1103 C  CG1   . VAL A 1 173 ? 16.320 -15.714 -28.035 1.00 39.50  ? 152 VAL A CG1   1 
ATOM   1104 C  CG2   . VAL A 1 173 ? 18.457 -14.515 -27.641 1.00 39.57  ? 152 VAL A CG2   1 
ATOM   1105 N  N     . ALA A 1 174 ? 14.366 -12.713 -28.800 1.00 47.65  ? 153 ALA A N     1 
ATOM   1106 C  CA    . ALA A 1 174 ? 12.893 -12.767 -29.005 1.00 47.58  ? 153 ALA A CA    1 
ATOM   1107 C  C     . ALA A 1 174 ? 12.517 -12.171 -30.375 1.00 46.16  ? 153 ALA A C     1 
ATOM   1108 O  O     . ALA A 1 174 ? 11.784 -12.832 -31.086 1.00 48.22  ? 153 ALA A O     1 
ATOM   1109 C  CB    . ALA A 1 174 ? 12.163 -12.094 -27.863 1.00 43.44  ? 153 ALA A CB    1 
ATOM   1110 N  N     . GLY A 1 175 ? 13.001 -10.970 -30.716 1.00 52.31  ? 154 GLY A N     1 
ATOM   1111 C  CA    . GLY A 1 175 ? 12.729 -10.249 -31.979 1.00 53.74  ? 154 GLY A CA    1 
ATOM   1112 C  C     . GLY A 1 175 ? 13.403 -10.886 -33.194 1.00 61.81  ? 154 GLY A C     1 
ATOM   1113 O  O     . GLY A 1 175 ? 13.224 -10.389 -34.335 1.00 57.60  ? 154 GLY A O     1 
ATOM   1114 N  N     . THR A 1 176 ? 14.193 -11.929 -32.964 1.00 66.83  ? 155 THR A N     1 
ATOM   1115 C  CA    . THR A 1 176 ? 14.733 -12.836 -34.002 1.00 63.23  ? 155 THR A CA    1 
ATOM   1116 C  C     . THR A 1 176 ? 13.594 -13.770 -34.415 1.00 62.82  ? 155 THR A C     1 
ATOM   1117 O  O     . THR A 1 176 ? 13.503 -14.092 -35.609 1.00 65.57  ? 155 THR A O     1 
ATOM   1118 C  CB    . THR A 1 176 ? 16.003 -13.520 -33.475 1.00 63.29  ? 155 THR A CB    1 
ATOM   1119 O  OG1   . THR A 1 176 ? 17.103 -12.903 -34.150 1.00 64.83  ? 155 THR A OG1   1 
ATOM   1120 C  CG2   . THR A 1 176 ? 16.000 -15.023 -33.643 1.00 58.36  ? 155 THR A CG2   1 
ATOM   1121 N  N     . GLY A 1 177 ? 12.766 -14.183 -33.454 1.00 63.73  ? 156 GLY A N     1 
ATOM   1122 C  CA    . GLY A 1 177 ? 11.500 -14.907 -33.686 1.00 60.96  ? 156 GLY A CA    1 
ATOM   1123 C  C     . GLY A 1 177 ? 11.658 -16.413 -33.616 1.00 60.15  ? 156 GLY A C     1 
ATOM   1124 O  O     . GLY A 1 177 ? 10.640 -17.114 -33.780 1.00 59.50  ? 156 GLY A O     1 
ATOM   1125 N  N     . VAL A 1 178 ? 12.875 -16.904 -33.378 1.00 62.52  ? 157 VAL A N     1 
ATOM   1126 C  CA    . VAL A 1 178 ? 13.169 -18.331 -33.021 1.00 67.10  ? 157 VAL A CA    1 
ATOM   1127 C  C     . VAL A 1 178 ? 12.045 -18.910 -32.152 1.00 63.78  ? 157 VAL A C     1 
ATOM   1128 O  O     . VAL A 1 178 ? 11.294 -18.164 -31.534 1.00 67.34  ? 157 VAL A O     1 
ATOM   1129 C  CB    . VAL A 1 178 ? 14.558 -18.388 -32.348 1.00 71.83  ? 157 VAL A CB    1 
ATOM   1130 C  CG1   . VAL A 1 178 ? 14.741 -19.515 -31.338 1.00 70.77  ? 157 VAL A CG1   1 
ATOM   1131 C  CG2   . VAL A 1 178 ? 15.644 -18.447 -33.406 1.00 74.21  ? 157 VAL A CG2   1 
ATOM   1132 N  N     . PRO A 1 179 ? 11.866 -20.253 -32.075 1.00 64.05  ? 158 PRO A N     1 
ATOM   1133 C  CA    . PRO A 1 179 ? 10.913 -20.861 -31.141 1.00 62.51  ? 158 PRO A CA    1 
ATOM   1134 C  C     . PRO A 1 179 ? 11.397 -21.065 -29.699 1.00 73.26  ? 158 PRO A C     1 
ATOM   1135 O  O     . PRO A 1 179 ? 12.582 -20.928 -29.459 1.00 76.30  ? 158 PRO A O     1 
ATOM   1136 C  CB    . PRO A 1 179 ? 10.671 -22.247 -31.753 1.00 61.33  ? 158 PRO A CB    1 
ATOM   1137 C  CG    . PRO A 1 179 ? 11.992 -22.583 -32.395 1.00 64.43  ? 158 PRO A CG    1 
ATOM   1138 C  CD    . PRO A 1 179 ? 12.484 -21.260 -32.954 1.00 64.01  ? 158 PRO A CD    1 
ATOM   1139 N  N     . ASP A 1 180 ? 10.468 -21.469 -28.816 1.00 79.92  ? 159 ASP A N     1 
ATOM   1140 C  CA    . ASP A 1 180 ? 10.580 -21.447 -27.327 1.00 78.46  ? 159 ASP A CA    1 
ATOM   1141 C  C     . ASP A 1 180 ? 11.605 -22.469 -26.836 1.00 72.63  ? 159 ASP A C     1 
ATOM   1142 O  O     . ASP A 1 180 ? 12.316 -22.175 -25.868 1.00 69.26  ? 159 ASP A O     1 
ATOM   1143 C  CB    . ASP A 1 180 ? 9.253  -21.787 -26.629 1.00 81.81  ? 159 ASP A CB    1 
ATOM   1144 C  CG    . ASP A 1 180 ? 8.215  -20.671 -26.627 1.00 85.43  ? 159 ASP A CG    1 
ATOM   1145 O  OD1   . ASP A 1 180 ? 8.538  -19.548 -27.081 1.00 86.12  ? 159 ASP A OD1   1 
ATOM   1146 O  OD2   . ASP A 1 180 ? 7.084  -20.931 -26.172 1.00 86.40  ? 159 ASP A OD2   1 
ATOM   1147 N  N     . ARG A 1 181 ? 11.636 -23.648 -27.449 1.00 67.86  ? 160 ARG A N     1 
ATOM   1148 C  CA    . ARG A 1 181 ? 12.415 -24.797 -26.932 1.00 62.01  ? 160 ARG A CA    1 
ATOM   1149 C  C     . ARG A 1 181 ? 13.893 -24.648 -27.309 1.00 60.09  ? 160 ARG A C     1 
ATOM   1150 O  O     . ARG A 1 181 ? 14.719 -25.367 -26.742 1.00 64.15  ? 160 ARG A O     1 
ATOM   1151 C  CB    . ARG A 1 181 ? 11.808 -26.080 -27.483 1.00 64.49  ? 160 ARG A CB    1 
ATOM   1152 C  CG    . ARG A 1 181 ? 11.850 -27.223 -26.488 1.00 66.30  ? 160 ARG A CG    1 
ATOM   1153 C  CD    . ARG A 1 181 ? 12.937 -28.219 -26.798 1.00 65.18  ? 160 ARG A CD    1 
ATOM   1154 N  NE    . ARG A 1 181 ? 12.365 -29.480 -27.238 1.00 67.88  ? 160 ARG A NE    1 
ATOM   1155 C  CZ    . ARG A 1 181 ? 11.564 -30.247 -26.502 1.00 70.37  ? 160 ARG A CZ    1 
ATOM   1156 N  NH1   . ARG A 1 181 ? 11.201 -29.876 -25.285 1.00 65.19  ? 160 ARG A NH1   1 
ATOM   1157 N  NH2   . ARG A 1 181 ? 11.118 -31.390 -26.993 1.00 75.91  ? 160 ARG A NH2   1 
ATOM   1158 N  N     . VAL A 1 182 ? 14.185 -23.739 -28.237 1.00 57.28  ? 161 VAL A N     1 
ATOM   1159 C  CA    . VAL A 1 182 ? 15.538 -23.409 -28.761 1.00 53.60  ? 161 VAL A CA    1 
ATOM   1160 C  C     . VAL A 1 182 ? 16.090 -22.193 -28.008 1.00 51.64  ? 161 VAL A C     1 
ATOM   1161 O  O     . VAL A 1 182 ? 17.303 -22.192 -27.725 1.00 47.79  ? 161 VAL A O     1 
ATOM   1162 C  CB    . VAL A 1 182 ? 15.464 -23.133 -30.269 1.00 51.76  ? 161 VAL A CB    1 
ATOM   1163 C  CG1   . VAL A 1 182 ? 16.687 -22.380 -30.757 1.00 51.33  ? 161 VAL A CG1   1 
ATOM   1164 C  CG2   . VAL A 1 182 ? 15.263 -24.415 -31.059 1.00 53.32  ? 161 VAL A CG2   1 
ATOM   1165 N  N     . ALA A 1 183 ? 15.253 -21.188 -27.720 1.00 46.48  ? 162 ALA A N     1 
ATOM   1166 C  CA    . ALA A 1 183 ? 15.632 -20.025 -26.883 1.00 48.77  ? 162 ALA A CA    1 
ATOM   1167 C  C     . ALA A 1 183 ? 16.003 -20.523 -25.474 1.00 47.87  ? 162 ALA A C     1 
ATOM   1168 O  O     . ALA A 1 183 ? 16.901 -19.901 -24.860 1.00 46.02  ? 162 ALA A O     1 
ATOM   1169 C  CB    . ALA A 1 183 ? 14.548 -18.968 -26.864 1.00 47.31  ? 162 ALA A CB    1 
ATOM   1170 N  N     . GLY A 1 184 ? 15.397 -21.630 -25.018 1.00 40.33  ? 163 GLY A N     1 
ATOM   1171 C  CA    . GLY A 1 184 ? 15.723 -22.304 -23.750 1.00 40.57  ? 163 GLY A CA    1 
ATOM   1172 C  C     . GLY A 1 184 ? 17.058 -23.042 -23.787 1.00 44.73  ? 163 GLY A C     1 
ATOM   1173 O  O     . GLY A 1 184 ? 17.780 -23.040 -22.744 1.00 46.47  ? 163 GLY A O     1 
ATOM   1174 N  N     . LEU A 1 185 ? 17.372 -23.711 -24.897 1.00 43.95  ? 164 LEU A N     1 
ATOM   1175 C  CA    . LEU A 1 185 ? 18.702 -24.336 -25.100 1.00 44.74  ? 164 LEU A CA    1 
ATOM   1176 C  C     . LEU A 1 185 ? 19.737 -23.214 -25.120 1.00 39.21  ? 164 LEU A C     1 
ATOM   1177 O  O     . LEU A 1 185 ? 20.810 -23.373 -24.527 1.00 42.28  ? 164 LEU A O     1 
ATOM   1178 C  CB    . LEU A 1 185 ? 18.749 -25.136 -26.409 1.00 51.18  ? 164 LEU A CB    1 
ATOM   1179 C  CG    . LEU A 1 185 ? 20.140 -25.656 -26.797 1.00 54.26  ? 164 LEU A CG    1 
ATOM   1180 C  CD1   . LEU A 1 185 ? 20.704 -26.556 -25.701 1.00 56.18  ? 164 LEU A CD1   1 
ATOM   1181 C  CD2   . LEU A 1 185 ? 20.116 -26.386 -28.132 1.00 54.01  ? 164 LEU A CD2   1 
ATOM   1182 N  N     . PHE A 1 186 ? 19.427 -22.131 -25.808 1.00 33.83  ? 165 PHE A N     1 
ATOM   1183 C  CA    . PHE A 1 186 ? 20.350 -20.989 -25.975 1.00 38.76  ? 165 PHE A CA    1 
ATOM   1184 C  C     . PHE A 1 186 ? 20.607 -20.355 -24.599 1.00 37.99  ? 165 PHE A C     1 
ATOM   1185 O  O     . PHE A 1 186 ? 21.776 -20.061 -24.324 1.00 38.05  ? 165 PHE A O     1 
ATOM   1186 C  CB    . PHE A 1 186 ? 19.783 -20.010 -27.000 1.00 38.36  ? 165 PHE A CB    1 
ATOM   1187 C  CG    . PHE A 1 186 ? 20.722 -18.887 -27.312 1.00 38.19  ? 165 PHE A CG    1 
ATOM   1188 C  CD1   . PHE A 1 186 ? 21.893 -19.132 -28.011 1.00 41.93  ? 165 PHE A CD1   1 
ATOM   1189 C  CD2   . PHE A 1 186 ? 20.450 -17.601 -26.888 1.00 39.63  ? 165 PHE A CD2   1 
ATOM   1190 C  CE1   . PHE A 1 186 ? 22.767 -18.098 -28.299 1.00 42.85  ? 165 PHE A CE1   1 
ATOM   1191 C  CE2   . PHE A 1 186 ? 21.333 -16.568 -27.160 1.00 40.82  ? 165 PHE A CE2   1 
ATOM   1192 C  CZ    . PHE A 1 186 ? 22.487 -16.818 -27.863 1.00 44.42  ? 165 PHE A CZ    1 
ATOM   1193 N  N     . GLU A 1 187 ? 19.565 -20.203 -23.763 1.00 39.02  ? 166 GLU A N     1 
ATOM   1194 C  CA    . GLU A 1 187 ? 19.647 -19.602 -22.400 1.00 42.01  ? 166 GLU A CA    1 
ATOM   1195 C  C     . GLU A 1 187 ? 20.628 -20.404 -21.537 1.00 40.01  ? 166 GLU A C     1 
ATOM   1196 O  O     . GLU A 1 187 ? 21.393 -19.765 -20.768 1.00 40.51  ? 166 GLU A O     1 
ATOM   1197 C  CB    . GLU A 1 187 ? 18.279 -19.536 -21.709 1.00 43.82  ? 166 GLU A CB    1 
ATOM   1198 C  CG    . GLU A 1 187 ? 18.275 -18.673 -20.460 1.00 45.89  ? 166 GLU A CG    1 
ATOM   1199 C  CD    . GLU A 1 187 ? 18.531 -17.186 -20.688 1.00 53.86  ? 166 GLU A CD    1 
ATOM   1200 O  OE1   . GLU A 1 187 ? 18.199 -16.679 -21.798 1.00 58.11  ? 166 GLU A OE1   1 
ATOM   1201 O  OE2   . GLU A 1 187 ? 19.055 -16.518 -19.756 1.00 48.05  ? 166 GLU A OE2   1 
ATOM   1202 N  N     . VAL A 1 188 ? 20.598 -21.742 -21.629 1.00 36.45  ? 167 VAL A N     1 
ATOM   1203 C  CA    . VAL A 1 188 ? 21.558 -22.620 -20.904 1.00 35.76  ? 167 VAL A CA    1 
ATOM   1204 C  C     . VAL A 1 188 ? 22.980 -22.189 -21.290 1.00 36.06  ? 167 VAL A C     1 
ATOM   1205 O  O     . VAL A 1 188 ? 23.829 -21.973 -20.381 1.00 37.70  ? 167 VAL A O     1 
ATOM   1206 C  CB    . VAL A 1 188 ? 21.337 -24.119 -21.189 1.00 36.72  ? 167 VAL A CB    1 
ATOM   1207 C  CG1   . VAL A 1 188 ? 22.438 -24.943 -20.564 1.00 36.92  ? 167 VAL A CG1   1 
ATOM   1208 C  CG2   . VAL A 1 188 ? 19.987 -24.618 -20.685 1.00 37.24  ? 167 VAL A CG2   1 
ATOM   1209 N  N     . ALA A 1 189 ? 23.244 -22.057 -22.587 1.00 33.57  ? 168 ALA A N     1 
ATOM   1210 C  CA    . ALA A 1 189 ? 24.588 -21.729 -23.097 1.00 36.23  ? 168 ALA A CA    1 
ATOM   1211 C  C     . ALA A 1 189 ? 24.969 -20.301 -22.663 1.00 35.74  ? 168 ALA A C     1 
ATOM   1212 O  O     . ALA A 1 189 ? 26.141 -20.100 -22.258 1.00 32.67  ? 168 ALA A O     1 
ATOM   1213 C  CB    . ALA A 1 189 ? 24.607 -21.893 -24.586 1.00 40.28  ? 168 ALA A CB    1 
ATOM   1214 N  N     . VAL A 1 190 ? 24.033 -19.347 -22.743 1.00 31.57  ? 169 VAL A N     1 
ATOM   1215 C  CA    . VAL A 1 190 ? 24.296 -17.939 -22.353 1.00 33.64  ? 169 VAL A CA    1 
ATOM   1216 C  C     . VAL A 1 190 ? 24.745 -17.912 -20.890 1.00 33.26  ? 169 VAL A C     1 
ATOM   1217 O  O     . VAL A 1 190 ? 25.755 -17.238 -20.622 1.00 31.67  ? 169 VAL A O     1 
ATOM   1218 C  CB    . VAL A 1 190 ? 23.085 -17.032 -22.587 1.00 34.24  ? 169 VAL A CB    1 
ATOM   1219 C  CG1   . VAL A 1 190 ? 23.217 -15.718 -21.812 1.00 34.42  ? 169 VAL A CG1   1 
ATOM   1220 C  CG2   . VAL A 1 190 ? 22.901 -16.776 -24.073 1.00 35.66  ? 169 VAL A CG2   1 
ATOM   1221 N  N     . GLN A 1 191 ? 24.066 -18.676 -20.033 1.00 34.29  ? 170 GLN A N     1 
ATOM   1222 C  CA    . GLN A 1 191 ? 24.327 -18.790 -18.569 1.00 35.87  ? 170 GLN A CA    1 
ATOM   1223 C  C     . GLN A 1 191 ? 25.616 -19.588 -18.305 1.00 35.72  ? 170 GLN A C     1 
ATOM   1224 O  O     . GLN A 1 191 ? 26.309 -19.258 -17.324 1.00 31.72  ? 170 GLN A O     1 
ATOM   1225 C  CB    . GLN A 1 191 ? 23.109 -19.393 -17.862 1.00 37.10  ? 170 GLN A CB    1 
ATOM   1226 C  CG    . GLN A 1 191 ? 21.906 -18.454 -17.878 1.00 41.57  ? 170 GLN A CG    1 
ATOM   1227 C  CD    . GLN A 1 191 ? 20.772 -18.842 -16.950 1.00 43.56  ? 170 GLN A CD    1 
ATOM   1228 O  OE1   . GLN A 1 191 ? 20.846 -19.807 -16.197 1.00 44.01  ? 170 GLN A OE1   1 
ATOM   1229 N  NE2   . GLN A 1 191 ? 19.687 -18.082 -17.012 1.00 45.96  ? 170 GLN A NE2   1 
ATOM   1230 N  N     . ALA A 1 192 ? 25.944 -20.601 -19.115 1.00 34.32  ? 171 ALA A N     1 
ATOM   1231 C  CA    . ALA A 1 192 ? 27.236 -21.334 -19.016 1.00 35.16  ? 171 ALA A CA    1 
ATOM   1232 C  C     . ALA A 1 192 ? 28.417 -20.397 -19.321 1.00 34.72  ? 171 ALA A C     1 
ATOM   1233 O  O     . ALA A 1 192 ? 29.469 -20.549 -18.653 1.00 32.03  ? 171 ALA A O     1 
ATOM   1234 C  CB    . ALA A 1 192 ? 27.266 -22.502 -19.968 1.00 37.81  ? 171 ALA A CB    1 
ATOM   1235 N  N     . VAL A 1 193 ? 28.245 -19.481 -20.281 1.00 32.64  ? 172 VAL A N     1 
ATOM   1236 C  CA    . VAL A 1 193 ? 29.320 -18.596 -20.816 1.00 34.70  ? 172 VAL A CA    1 
ATOM   1237 C  C     . VAL A 1 193 ? 29.468 -17.345 -19.944 1.00 33.41  ? 172 VAL A C     1 
ATOM   1238 O  O     . VAL A 1 193 ? 30.598 -16.917 -19.774 1.00 31.89  ? 172 VAL A O     1 
ATOM   1239 C  CB    . VAL A 1 193 ? 29.057 -18.190 -22.274 1.00 35.26  ? 172 VAL A CB    1 
ATOM   1240 C  CG1   . VAL A 1 193 ? 30.021 -17.103 -22.698 1.00 40.08  ? 172 VAL A CG1   1 
ATOM   1241 C  CG2   . VAL A 1 193 ? 29.126 -19.359 -23.232 1.00 37.74  ? 172 VAL A CG2   1 
ATOM   1242 N  N     . PHE A 1 194 ? 28.363 -16.731 -19.500 1.00 33.80  ? 173 PHE A N     1 
ATOM   1243 C  CA    . PHE A 1 194 ? 28.312 -15.345 -18.936 1.00 31.63  ? 173 PHE A CA    1 
ATOM   1244 C  C     . PHE A 1 194 ? 28.053 -15.331 -17.419 1.00 30.04  ? 173 PHE A C     1 
ATOM   1245 O  O     . PHE A 1 194 ? 28.300 -14.293 -16.802 1.00 29.24  ? 173 PHE A O     1 
ATOM   1246 C  CB    . PHE A 1 194 ? 27.228 -14.515 -19.641 1.00 31.33  ? 173 PHE A CB    1 
ATOM   1247 C  CG    . PHE A 1 194 ? 27.543 -14.147 -21.069 1.00 30.58  ? 173 PHE A CG    1 
ATOM   1248 C  CD1   . PHE A 1 194 ? 28.416 -13.107 -21.352 1.00 28.23  ? 173 PHE A CD1   1 
ATOM   1249 C  CD2   . PHE A 1 194 ? 26.934 -14.799 -22.127 1.00 32.94  ? 173 PHE A CD2   1 
ATOM   1250 C  CE1   . PHE A 1 194 ? 28.702 -12.754 -22.659 1.00 26.42  ? 173 PHE A CE1   1 
ATOM   1251 C  CE2   . PHE A 1 194 ? 27.230 -14.452 -23.441 1.00 32.62  ? 173 PHE A CE2   1 
ATOM   1252 C  CZ    . PHE A 1 194 ? 28.105 -13.418 -23.698 1.00 29.75  ? 173 PHE A CZ    1 
ATOM   1253 N  N     . ALA A 1 195 ? 27.519 -16.418 -16.844 1.00 31.03  ? 174 ALA A N     1 
ATOM   1254 C  CA    . ALA A 1 195 ? 27.120 -16.520 -15.417 1.00 32.53  ? 174 ALA A CA    1 
ATOM   1255 C  C     . ALA A 1 195 ? 26.141 -15.384 -15.062 1.00 32.75  ? 174 ALA A C     1 
ATOM   1256 O  O     . ALA A 1 195 ? 26.299 -14.732 -14.014 1.00 34.30  ? 174 ALA A O     1 
ATOM   1257 C  CB    . ALA A 1 195 ? 28.348 -16.535 -14.538 1.00 33.42  ? 174 ALA A CB    1 
ATOM   1258 N  N     . ALA A 1 196 ? 25.122 -15.223 -15.897 1.00 32.63  ? 175 ALA A N     1 
ATOM   1259 C  CA    . ALA A 1 196 ? 24.175 -14.093 -15.962 1.00 32.89  ? 175 ALA A CA    1 
ATOM   1260 C  C     . ALA A 1 196 ? 23.136 -14.420 -17.025 1.00 33.27  ? 175 ALA A C     1 
ATOM   1261 O  O     . ALA A 1 196 ? 23.506 -15.033 -18.028 1.00 36.51  ? 175 ALA A O     1 
ATOM   1262 C  CB    . ALA A 1 196 ? 24.927 -12.835 -16.306 1.00 33.12  ? 175 ALA A CB    1 
ATOM   1263 N  N     . THR A 1 197 ? 21.884 -14.022 -16.837 1.00 38.38  ? 176 THR A N     1 
ATOM   1264 C  CA    . THR A 1 197 ? 20.804 -14.338 -17.804 1.00 35.27  ? 176 THR A CA    1 
ATOM   1265 C  C     . THR A 1 197 ? 20.940 -13.415 -19.009 1.00 36.79  ? 176 THR A C     1 
ATOM   1266 O  O     . THR A 1 197 ? 21.623 -12.351 -18.905 1.00 35.49  ? 176 THR A O     1 
ATOM   1267 C  CB    . THR A 1 197 ? 19.368 -14.145 -17.280 1.00 34.49  ? 176 THR A CB    1 
ATOM   1268 O  OG1   . THR A 1 197 ? 19.143 -12.737 -17.209 1.00 34.90  ? 176 THR A OG1   1 
ATOM   1269 C  CG2   . THR A 1 197 ? 19.107 -14.817 -15.955 1.00 34.66  ? 176 THR A CG2   1 
ATOM   1270 N  N     . SER A 1 198 ? 20.254 -13.817 -20.080 1.00 37.13  ? 177 SER A N     1 
ATOM   1271 C  CA    . SER A 1 198 ? 19.984 -13.061 -21.326 1.00 38.40  ? 177 SER A CA    1 
ATOM   1272 C  C     . SER A 1 198 ? 19.463 -11.642 -21.013 1.00 35.54  ? 177 SER A C     1 
ATOM   1273 O  O     . SER A 1 198 ? 19.778 -10.660 -21.747 1.00 32.83  ? 177 SER A O     1 
ATOM   1274 C  CB    . SER A 1 198 ? 18.991 -13.874 -22.113 1.00 38.58  ? 177 SER A CB    1 
ATOM   1275 O  OG    . SER A 1 198 ? 18.764 -13.263 -23.349 1.00 54.15  ? 177 SER A OG    1 
ATOM   1276 N  N     . ALA A 1 199 ? 18.654 -11.501 -19.972 1.00 36.47  ? 178 ALA A N     1 
ATOM   1277 C  CA    . ALA A 1 199 ? 18.037 -10.200 -19.640 1.00 35.47  ? 178 ALA A CA    1 
ATOM   1278 C  C     . ALA A 1 199 ? 19.060 -9.234  -19.049 1.00 33.88  ? 178 ALA A C     1 
ATOM   1279 O  O     . ALA A 1 199 ? 18.817 -8.032  -19.157 1.00 38.76  ? 178 ALA A O     1 
ATOM   1280 C  CB    . ALA A 1 199 ? 16.877 -10.403 -18.706 1.00 37.35  ? 178 ALA A CB    1 
ATOM   1281 N  N     . GLN A 1 200 ? 20.125 -9.706  -18.397 1.00 37.11  ? 179 GLN A N     1 
ATOM   1282 C  CA    . GLN A 1 200 ? 21.060 -8.802  -17.654 1.00 36.64  ? 179 GLN A CA    1 
ATOM   1283 C  C     . GLN A 1 200 ? 22.124 -8.194  -18.591 1.00 36.16  ? 179 GLN A C     1 
ATOM   1284 O  O     . GLN A 1 200 ? 22.801 -7.206  -18.171 1.00 37.81  ? 179 GLN A O     1 
ATOM   1285 C  CB    . GLN A 1 200 ? 21.757 -9.546  -16.510 1.00 38.48  ? 179 GLN A CB    1 
ATOM   1286 C  CG    . GLN A 1 200 ? 20.836 -10.176 -15.468 1.00 36.48  ? 179 GLN A CG    1 
ATOM   1287 C  CD    . GLN A 1 200 ? 21.674 -11.051 -14.569 1.00 37.36  ? 179 GLN A CD    1 
ATOM   1288 O  OE1   . GLN A 1 200 ? 21.736 -12.278 -14.715 1.00 37.49  ? 179 GLN A OE1   1 
ATOM   1289 N  NE2   . GLN A 1 200 ? 22.414 -10.409 -13.684 1.00 37.93  ? 179 GLN A NE2   1 
ATOM   1290 N  N     . LEU A 1 201 ? 22.302 -8.770  -19.787 1.00 34.94  ? 180 LEU A N     1 
ATOM   1291 C  CA    . LEU A 1 201 ? 23.397 -8.451  -20.742 1.00 36.83  ? 180 LEU A CA    1 
ATOM   1292 C  C     . LEU A 1 201 ? 22.890 -7.541  -21.862 1.00 31.62  ? 180 LEU A C     1 
ATOM   1293 O  O     . LEU A 1 201 ? 21.871 -7.919  -22.477 1.00 30.16  ? 180 LEU A O     1 
ATOM   1294 C  CB    . LEU A 1 201 ? 23.877 -9.749  -21.406 1.00 38.31  ? 180 LEU A CB    1 
ATOM   1295 C  CG    . LEU A 1 201 ? 24.382 -10.834 -20.476 1.00 40.12  ? 180 LEU A CG    1 
ATOM   1296 C  CD1   . LEU A 1 201 ? 24.607 -12.118 -21.246 1.00 42.41  ? 180 LEU A CD1   1 
ATOM   1297 C  CD2   . LEU A 1 201 ? 25.655 -10.384 -19.796 1.00 42.98  ? 180 LEU A CD2   1 
ATOM   1298 N  N     . SER A 1 202 ? 23.654 -6.521  -22.254 1.00 29.36  ? 181 SER A N     1 
ATOM   1299 C  CA    . SER A 1 202 ? 23.437 -5.797  -23.540 1.00 33.82  ? 181 SER A CA    1 
ATOM   1300 C  C     . SER A 1 202 ? 23.884 -6.667  -24.713 1.00 34.13  ? 181 SER A C     1 
ATOM   1301 O  O     . SER A 1 202 ? 24.815 -7.477  -24.530 1.00 36.81  ? 181 SER A O     1 
ATOM   1302 C  CB    . SER A 1 202 ? 24.147 -4.476  -23.603 1.00 37.73  ? 181 SER A CB    1 
ATOM   1303 O  OG    . SER A 1 202 ? 25.508 -4.667  -23.886 1.00 40.26  ? 181 SER A OG    1 
ATOM   1304 N  N     . LEU A 1 203 ? 23.252 -6.479  -25.871 1.00 34.52  ? 182 LEU A N     1 
ATOM   1305 C  CA    . LEU A 1 203 ? 23.595 -7.166  -27.142 1.00 36.55  ? 182 LEU A CA    1 
ATOM   1306 C  C     . LEU A 1 203 ? 25.031 -6.830  -27.536 1.00 34.74  ? 182 LEU A C     1 
ATOM   1307 O  O     . LEU A 1 203 ? 25.765 -7.760  -27.978 1.00 32.23  ? 182 LEU A O     1 
ATOM   1308 C  CB    . LEU A 1 203 ? 22.635 -6.713  -28.248 1.00 38.78  ? 182 LEU A CB    1 
ATOM   1309 C  CG    . LEU A 1 203 ? 22.901 -7.325  -29.621 1.00 35.20  ? 182 LEU A CG    1 
ATOM   1310 C  CD1   . LEU A 1 203 ? 22.781 -8.842  -29.567 1.00 33.05  ? 182 LEU A CD1   1 
ATOM   1311 C  CD2   . LEU A 1 203 ? 21.957 -6.709  -30.642 1.00 33.80  ? 182 LEU A CD2   1 
ATOM   1312 N  N     . LEU A 1 204 ? 25.398 -5.553  -27.393 1.00 33.13  ? 183 LEU A N     1 
ATOM   1313 C  CA    . LEU A 1 204 ? 26.770 -5.067  -27.683 1.00 34.67  ? 183 LEU A CA    1 
ATOM   1314 C  C     . LEU A 1 204 ? 27.793 -5.803  -26.805 1.00 36.37  ? 183 LEU A C     1 
ATOM   1315 O  O     . LEU A 1 204 ? 28.879 -6.145  -27.343 1.00 34.87  ? 183 LEU A O     1 
ATOM   1316 C  CB    . LEU A 1 204 ? 26.853 -3.556  -27.466 1.00 34.90  ? 183 LEU A CB    1 
ATOM   1317 C  CG    . LEU A 1 204 ? 28.159 -2.910  -27.922 1.00 35.42  ? 183 LEU A CG    1 
ATOM   1318 C  CD1   . LEU A 1 204 ? 28.563 -3.387  -29.311 1.00 38.03  ? 183 LEU A CD1   1 
ATOM   1319 C  CD2   . LEU A 1 204 ? 28.027 -1.393  -27.905 1.00 36.10  ? 183 LEU A CD2   1 
ATOM   1320 N  N     . HIS A 1 205 ? 27.504 -5.994  -25.510 1.00 33.52  ? 184 HIS A N     1 
ATOM   1321 C  CA    . HIS A 1 205 ? 28.424 -6.710  -24.591 1.00 32.22  ? 184 HIS A CA    1 
ATOM   1322 C  C     . HIS A 1 205 ? 28.548 -8.157  -25.073 1.00 30.21  ? 184 HIS A C     1 
ATOM   1323 O  O     . HIS A 1 205 ? 29.678 -8.628  -25.191 1.00 29.39  ? 184 HIS A O     1 
ATOM   1324 C  CB    . HIS A 1 205 ? 28.010 -6.639  -23.102 1.00 33.12  ? 184 HIS A CB    1 
ATOM   1325 C  CG    . HIS A 1 205 ? 28.905 -7.469  -22.236 1.00 30.29  ? 184 HIS A CG    1 
ATOM   1326 N  ND1   . HIS A 1 205 ? 28.599 -8.776  -21.888 1.00 34.88  ? 184 HIS A ND1   1 
ATOM   1327 C  CD2   . HIS A 1 205 ? 30.136 -7.238  -21.728 1.00 29.61  ? 184 HIS A CD2   1 
ATOM   1328 C  CE1   . HIS A 1 205 ? 29.602 -9.298  -21.202 1.00 29.94  ? 184 HIS A CE1   1 
ATOM   1329 N  NE2   . HIS A 1 205 ? 30.541 -8.380  -21.091 1.00 29.08  ? 184 HIS A NE2   1 
ATOM   1330 N  N     . ALA A 1 206 ? 27.430 -8.828  -25.347 1.00 30.39  ? 185 ALA A N     1 
ATOM   1331 C  CA    . ALA A 1 206 ? 27.398 -10.259 -25.735 1.00 30.34  ? 185 ALA A CA    1 
ATOM   1332 C  C     . ALA A 1 206 ? 28.124 -10.424 -27.069 1.00 31.01  ? 185 ALA A C     1 
ATOM   1333 O  O     . ALA A 1 206 ? 28.901 -11.377 -27.198 1.00 32.23  ? 185 ALA A O     1 
ATOM   1334 C  CB    . ALA A 1 206 ? 25.981 -10.766 -25.799 1.00 30.06  ? 185 ALA A CB    1 
ATOM   1335 N  N     . ALA A 1 207 ? 27.926 -9.493  -28.008 1.00 33.39  ? 186 ALA A N     1 
ATOM   1336 C  CA    . ALA A 1 207 ? 28.536 -9.553  -29.356 1.00 35.32  ? 186 ALA A CA    1 
ATOM   1337 C  C     . ALA A 1 207 ? 30.063 -9.417  -29.245 1.00 35.29  ? 186 ALA A C     1 
ATOM   1338 O  O     . ALA A 1 207 ? 30.762 -10.246 -29.826 1.00 36.03  ? 186 ALA A O     1 
ATOM   1339 C  CB    . ALA A 1 207 ? 27.958 -8.488  -30.244 1.00 36.12  ? 186 ALA A CB    1 
ATOM   1340 N  N     . HIS A 1 208 ? 30.552 -8.394  -28.538 1.00 36.54  ? 187 HIS A N     1 
ATOM   1341 C  CA    . HIS A 1 208 ? 31.993 -8.171  -28.228 1.00 36.31  ? 187 HIS A CA    1 
ATOM   1342 C  C     . HIS A 1 208 ? 32.611 -9.458  -27.684 1.00 36.56  ? 187 HIS A C     1 
ATOM   1343 O  O     . HIS A 1 208 ? 33.602 -9.936  -28.240 1.00 38.91  ? 187 HIS A O     1 
ATOM   1344 C  CB    . HIS A 1 208 ? 32.157 -7.033  -27.233 1.00 35.51  ? 187 HIS A CB    1 
ATOM   1345 C  CG    . HIS A 1 208 ? 33.557 -6.859  -26.756 1.00 38.18  ? 187 HIS A CG    1 
ATOM   1346 N  ND1   . HIS A 1 208 ? 34.568 -6.372  -27.567 1.00 41.04  ? 187 HIS A ND1   1 
ATOM   1347 C  CD2   . HIS A 1 208 ? 34.108 -7.052  -25.540 1.00 40.48  ? 187 HIS A CD2   1 
ATOM   1348 C  CE1   . HIS A 1 208 ? 35.682 -6.304  -26.878 1.00 38.91  ? 187 HIS A CE1   1 
ATOM   1349 N  NE2   . HIS A 1 208 ? 35.424 -6.695  -25.624 1.00 40.24  ? 187 HIS A NE2   1 
ATOM   1350 N  N     . TYR A 1 209 ? 32.008 -10.032 -26.654 1.00 33.93  ? 188 TYR A N     1 
ATOM   1351 C  CA    . TYR A 1 209 ? 32.517 -11.269 -26.016 1.00 33.56  ? 188 TYR A CA    1 
ATOM   1352 C  C     . TYR A 1 209 ? 32.737 -12.347 -27.068 1.00 33.67  ? 188 TYR A C     1 
ATOM   1353 O  O     . TYR A 1 209 ? 33.719 -13.144 -26.912 1.00 34.02  ? 188 TYR A O     1 
ATOM   1354 C  CB    . TYR A 1 209 ? 31.510 -11.797 -24.996 1.00 32.39  ? 188 TYR A CB    1 
ATOM   1355 C  CG    . TYR A 1 209 ? 32.105 -12.443 -23.777 1.00 31.40  ? 188 TYR A CG    1 
ATOM   1356 C  CD1   . TYR A 1 209 ? 32.634 -11.673 -22.748 1.00 32.32  ? 188 TYR A CD1   1 
ATOM   1357 C  CD2   . TYR A 1 209 ? 32.119 -13.823 -23.646 1.00 31.31  ? 188 TYR A CD2   1 
ATOM   1358 C  CE1   . TYR A 1 209 ? 33.149 -12.259 -21.601 1.00 33.64  ? 188 TYR A CE1   1 
ATOM   1359 C  CE2   . TYR A 1 209 ? 32.641 -14.424 -22.515 1.00 31.43  ? 188 TYR A CE2   1 
ATOM   1360 C  CZ    . TYR A 1 209 ? 33.157 -13.643 -21.494 1.00 33.43  ? 188 TYR A CZ    1 
ATOM   1361 O  OH    . TYR A 1 209 ? 33.677 -14.230 -20.382 1.00 35.00  ? 188 TYR A OH    1 
ATOM   1362 N  N     . VAL A 1 210 ? 31.783 -12.460 -28.004 1.00 33.39  ? 189 VAL A N     1 
ATOM   1363 C  CA    . VAL A 1 210 ? 31.728 -13.568 -29.008 1.00 36.89  ? 189 VAL A CA    1 
ATOM   1364 C  C     . VAL A 1 210 ? 32.839 -13.313 -30.033 1.00 35.70  ? 189 VAL A C     1 
ATOM   1365 O  O     . VAL A 1 210 ? 33.636 -14.234 -30.299 1.00 37.96  ? 189 VAL A O     1 
ATOM   1366 C  CB    . VAL A 1 210 ? 30.341 -13.715 -29.671 1.00 38.12  ? 189 VAL A CB    1 
ATOM   1367 C  CG1   . VAL A 1 210 ? 30.378 -14.631 -30.889 1.00 38.94  ? 189 VAL A CG1   1 
ATOM   1368 C  CG2   . VAL A 1 210 ? 29.296 -14.203 -28.685 1.00 37.30  ? 189 VAL A CG2   1 
ATOM   1369 N  N     . HIS A 1 211 ? 32.904 -12.097 -30.558 1.00 33.32  ? 190 HIS A N     1 
ATOM   1370 C  CA    . HIS A 1 211 ? 34.033 -11.641 -31.396 1.00 35.07  ? 190 HIS A CA    1 
ATOM   1371 C  C     . HIS A 1 211 ? 35.336 -11.975 -30.653 1.00 39.80  ? 190 HIS A C     1 
ATOM   1372 O  O     . HIS A 1 211 ? 36.182 -12.672 -31.255 1.00 43.94  ? 190 HIS A O     1 
ATOM   1373 C  CB    . HIS A 1 211 ? 33.905 -10.152 -31.739 1.00 32.05  ? 190 HIS A CB    1 
ATOM   1374 C  CG    . HIS A 1 211 ? 34.744 -9.743  -32.903 1.00 34.10  ? 190 HIS A CG    1 
ATOM   1375 N  ND1   . HIS A 1 211 ? 35.099 -8.418  -33.131 1.00 37.24  ? 190 HIS A ND1   1 
ATOM   1376 C  CD2   . HIS A 1 211 ? 35.310 -10.469 -33.898 1.00 32.46  ? 190 HIS A CD2   1 
ATOM   1377 C  CE1   . HIS A 1 211 ? 35.844 -8.345  -34.223 1.00 36.44  ? 190 HIS A CE1   1 
ATOM   1378 N  NE2   . HIS A 1 211 ? 35.988 -9.596  -34.707 1.00 39.82  ? 190 HIS A NE2   1 
ATOM   1379 N  N     . SER A 1 212 ? 35.472 -11.516 -29.399 1.00 35.03  ? 191 SER A N     1 
ATOM   1380 C  CA    . SER A 1 212 ? 36.705 -11.602 -28.569 1.00 35.65  ? 191 SER A CA    1 
ATOM   1381 C  C     . SER A 1 212 ? 37.252 -13.033 -28.564 1.00 33.39  ? 191 SER A C     1 
ATOM   1382 O  O     . SER A 1 212 ? 38.468 -13.169 -28.637 1.00 32.19  ? 191 SER A O     1 
ATOM   1383 C  CB    . SER A 1 212 ? 36.464 -11.124 -27.156 1.00 36.08  ? 191 SER A CB    1 
ATOM   1384 O  OG    . SER A 1 212 ? 37.608 -11.260 -26.320 1.00 34.17  ? 191 SER A OG    1 
ATOM   1385 N  N     . ALA A 1 213 ? 36.371 -14.030 -28.471 1.00 32.45  ? 192 ALA A N     1 
ATOM   1386 C  CA    . ALA A 1 213 ? 36.712 -15.466 -28.389 1.00 35.07  ? 192 ALA A CA    1 
ATOM   1387 C  C     . ALA A 1 213 ? 36.806 -16.085 -29.787 1.00 38.14  ? 192 ALA A C     1 
ATOM   1388 O  O     . ALA A 1 213 ? 37.247 -17.249 -29.886 1.00 39.38  ? 192 ALA A O     1 
ATOM   1389 C  CB    . ALA A 1 213 ? 35.667 -16.171 -27.573 1.00 34.64  ? 192 ALA A CB    1 
ATOM   1390 N  N     . GLY A 1 214 ? 36.347 -15.371 -30.822 1.00 40.96  ? 193 GLY A N     1 
ATOM   1391 C  CA    . GLY A 1 214 ? 36.360 -15.856 -32.220 1.00 42.60  ? 193 GLY A CA    1 
ATOM   1392 C  C     . GLY A 1 214 ? 35.193 -16.782 -32.558 1.00 42.08  ? 193 GLY A C     1 
ATOM   1393 O  O     . GLY A 1 214 ? 35.406 -17.665 -33.384 1.00 43.86  ? 193 GLY A O     1 
ATOM   1394 N  N     . GLY A 1 215 ? 33.992 -16.566 -32.002 1.00 40.02  ? 194 GLY A N     1 
ATOM   1395 C  CA    . GLY A 1 215 ? 32.774 -17.305 -32.392 1.00 37.35  ? 194 GLY A CA    1 
ATOM   1396 C  C     . GLY A 1 215 ? 32.183 -18.123 -31.259 1.00 37.34  ? 194 GLY A C     1 
ATOM   1397 O  O     . GLY A 1 215 ? 32.829 -18.231 -30.183 1.00 36.61  ? 194 GLY A O     1 
ATOM   1398 N  N     . TRP A 1 216 ? 30.985 -18.662 -31.495 1.00 36.33  ? 195 TRP A N     1 
ATOM   1399 C  CA    . TRP A 1 216 ? 30.086 -19.271 -30.486 1.00 38.01  ? 195 TRP A CA    1 
ATOM   1400 C  C     . TRP A 1 216 ? 30.505 -20.712 -30.199 1.00 38.75  ? 195 TRP A C     1 
ATOM   1401 O  O     . TRP A 1 216 ? 30.377 -21.150 -29.035 1.00 39.22  ? 195 TRP A O     1 
ATOM   1402 C  CB    . TRP A 1 216 ? 28.634 -19.196 -30.967 1.00 42.11  ? 195 TRP A CB    1 
ATOM   1403 C  CG    . TRP A 1 216 ? 27.624 -19.642 -29.956 1.00 41.80  ? 195 TRP A CG    1 
ATOM   1404 C  CD1   . TRP A 1 216 ? 26.853 -20.766 -30.000 1.00 46.23  ? 195 TRP A CD1   1 
ATOM   1405 C  CD2   . TRP A 1 216 ? 27.262 -18.955 -28.745 1.00 44.59  ? 195 TRP A CD2   1 
ATOM   1406 N  NE1   . TRP A 1 216 ? 26.045 -20.828 -28.897 1.00 49.49  ? 195 TRP A NE1   1 
ATOM   1407 C  CE2   . TRP A 1 216 ? 26.267 -19.726 -28.115 1.00 42.16  ? 195 TRP A CE2   1 
ATOM   1408 C  CE3   . TRP A 1 216 ? 27.686 -17.771 -28.128 1.00 47.43  ? 195 TRP A CE3   1 
ATOM   1409 C  CZ2   . TRP A 1 216 ? 25.712 -19.359 -26.893 1.00 44.93  ? 195 TRP A CZ2   1 
ATOM   1410 C  CZ3   . TRP A 1 216 ? 27.111 -17.392 -26.934 1.00 44.42  ? 195 TRP A CZ3   1 
ATOM   1411 C  CH2   . TRP A 1 216 ? 26.145 -18.184 -26.321 1.00 43.79  ? 195 TRP A CH2   1 
ATOM   1412 N  N     . SER A 1 217 ? 30.940 -21.455 -31.208 1.00 37.94  ? 196 SER A N     1 
ATOM   1413 C  CA    . SER A 1 217 ? 31.474 -22.832 -31.007 1.00 41.68  ? 196 SER A CA    1 
ATOM   1414 C  C     . SER A 1 217 ? 32.741 -22.752 -30.154 1.00 40.64  ? 196 SER A C     1 
ATOM   1415 O  O     . SER A 1 217 ? 32.979 -23.691 -29.387 1.00 36.96  ? 196 SER A O     1 
ATOM   1416 C  CB    . SER A 1 217 ? 31.767 -23.534 -32.292 1.00 41.33  ? 196 SER A CB    1 
ATOM   1417 O  OG    . SER A 1 217 ? 30.741 -23.296 -33.226 1.00 48.21  ? 196 SER A OG    1 
ATOM   1418 N  N     . LYS A 1 218 ? 33.533 -21.688 -30.318 1.00 38.12  ? 197 LYS A N     1 
ATOM   1419 C  CA    . LYS A 1 218 ? 34.766 -21.469 -29.522 1.00 39.96  ? 197 LYS A CA    1 
ATOM   1420 C  C     . LYS A 1 218 ? 34.422 -21.420 -28.021 1.00 40.26  ? 197 LYS A C     1 
ATOM   1421 O  O     . LYS A 1 218 ? 35.140 -22.121 -27.233 1.00 35.44  ? 197 LYS A O     1 
ATOM   1422 C  CB    . LYS A 1 218 ? 35.478 -20.212 -30.014 1.00 43.24  ? 197 LYS A CB    1 
ATOM   1423 C  CG    . LYS A 1 218 ? 36.238 -20.420 -31.310 1.00 47.32  ? 197 LYS A CG    1 
ATOM   1424 C  CD    . LYS A 1 218 ? 37.382 -21.406 -31.139 1.00 55.33  ? 197 LYS A CD    1 
ATOM   1425 C  CE    . LYS A 1 218 ? 38.331 -21.445 -32.318 1.00 61.46  ? 197 LYS A CE    1 
ATOM   1426 N  NZ    . LYS A 1 218 ? 39.620 -22.071 -31.941 1.00 59.16  ? 197 LYS A NZ    1 
ATOM   1427 N  N     . LEU A 1 219 ? 33.331 -20.716 -27.659 1.00 35.53  ? 198 LEU A N     1 
ATOM   1428 C  CA    . LEU A 1 219 ? 32.845 -20.515 -26.263 1.00 33.81  ? 198 LEU A CA    1 
ATOM   1429 C  C     . LEU A 1 219 ? 32.158 -21.770 -25.694 1.00 34.75  ? 198 LEU A C     1 
ATOM   1430 O  O     . LEU A 1 219 ? 32.274 -21.988 -24.466 1.00 31.00  ? 198 LEU A O     1 
ATOM   1431 C  CB    . LEU A 1 219 ? 31.865 -19.342 -26.242 1.00 31.99  ? 198 LEU A CB    1 
ATOM   1432 C  CG    . LEU A 1 219 ? 32.434 -17.993 -26.658 1.00 34.44  ? 198 LEU A CG    1 
ATOM   1433 C  CD1   . LEU A 1 219 ? 31.323 -16.964 -26.773 1.00 38.34  ? 198 LEU A CD1   1 
ATOM   1434 C  CD2   . LEU A 1 219 ? 33.475 -17.518 -25.678 1.00 36.07  ? 198 LEU A CD2   1 
ATOM   1435 N  N     . THR A 1 220 ? 31.441 -22.540 -26.520 1.00 34.88  ? 199 THR A N     1 
ATOM   1436 C  CA    . THR A 1 220 ? 30.495 -23.600 -26.071 1.00 37.44  ? 199 THR A CA    1 
ATOM   1437 C  C     . THR A 1 220 ? 31.114 -24.998 -26.197 1.00 40.88  ? 199 THR A C     1 
ATOM   1438 O  O     . THR A 1 220 ? 30.725 -25.875 -25.415 1.00 38.68  ? 199 THR A O     1 
ATOM   1439 C  CB    . THR A 1 220 ? 29.178 -23.536 -26.860 1.00 39.45  ? 199 THR A CB    1 
ATOM   1440 O  OG1   . THR A 1 220 ? 29.475 -23.418 -28.250 1.00 43.22  ? 199 THR A OG1   1 
ATOM   1441 C  CG2   . THR A 1 220 ? 28.307 -22.357 -26.489 1.00 40.38  ? 199 THR A CG2   1 
ATOM   1442 N  N     . ASP A 1 221 ? 32.017 -25.237 -27.151 1.00 42.22  ? 200 ASP A N     1 
ATOM   1443 C  CA    . ASP A 1 221 ? 32.399 -26.631 -27.522 1.00 45.29  ? 200 ASP A CA    1 
ATOM   1444 C  C     . ASP A 1 221 ? 33.482 -27.156 -26.582 1.00 42.15  ? 200 ASP A C     1 
ATOM   1445 O  O     . ASP A 1 221 ? 34.269 -26.337 -26.069 1.00 40.71  ? 200 ASP A O     1 
ATOM   1446 C  CB    . ASP A 1 221 ? 32.908 -26.730 -28.961 1.00 50.83  ? 200 ASP A CB    1 
ATOM   1447 C  CG    . ASP A 1 221 ? 31.829 -26.618 -30.027 1.00 54.36  ? 200 ASP A CG    1 
ATOM   1448 O  OD1   . ASP A 1 221 ? 30.617 -26.627 -29.661 1.00 55.25  ? 200 ASP A OD1   1 
ATOM   1449 O  OD2   . ASP A 1 221 ? 32.218 -26.523 -31.217 1.00 58.67  ? 200 ASP A OD2   1 
ATOM   1450 N  N     . THR A 1 222 ? 33.548 -28.480 -26.436 1.00 42.23  ? 201 THR A N     1 
ATOM   1451 C  CA    . THR A 1 222 ? 34.628 -29.221 -25.722 1.00 40.15  ? 201 THR A CA    1 
ATOM   1452 C  C     . THR A 1 222 ? 35.794 -29.425 -26.700 1.00 43.01  ? 201 THR A C     1 
ATOM   1453 O  O     . THR A 1 222 ? 36.672 -28.523 -26.759 1.00 49.11  ? 201 THR A O     1 
ATOM   1454 C  CB    . THR A 1 222 ? 34.045 -30.492 -25.094 1.00 37.18  ? 201 THR A CB    1 
ATOM   1455 O  OG1   . THR A 1 222 ? 33.078 -30.043 -24.142 1.00 32.98  ? 201 THR A OG1   1 
ATOM   1456 C  CG2   . THR A 1 222 ? 35.068 -31.405 -24.446 1.00 36.73  ? 201 THR A CG2   1 
ATOM   1457 N  N     . GLU A 1 223 ? 35.801 -30.524 -27.458 1.00 44.75  ? 202 GLU A N     1 
ATOM   1458 C  CA    . GLU A 1 223 ? 36.746 -30.735 -28.590 1.00 48.03  ? 202 GLU A CA    1 
ATOM   1459 C  C     . GLU A 1 223 ? 36.635 -29.537 -29.545 1.00 40.49  ? 202 GLU A C     1 
ATOM   1460 O  O     . GLU A 1 223 ? 35.535 -29.281 -30.028 1.00 38.75  ? 202 GLU A O     1 
ATOM   1461 C  CB    . GLU A 1 223 ? 36.469 -32.078 -29.277 1.00 55.48  ? 202 GLU A CB    1 
ATOM   1462 C  CG    . GLU A 1 223 ? 37.213 -33.252 -28.639 1.00 65.81  ? 202 GLU A CG    1 
ATOM   1463 C  CD    . GLU A 1 223 ? 36.946 -34.642 -29.222 1.00 78.86  ? 202 GLU A CD    1 
ATOM   1464 O  OE1   . GLU A 1 223 ? 35.892 -34.830 -29.873 1.00 76.07  ? 202 GLU A OE1   1 
ATOM   1465 O  OE2   . GLU A 1 223 ? 37.793 -35.555 -29.016 1.00 85.12  ? 202 GLU A OE2   1 
ATOM   1466 N  N     . GLY A 1 224 ? 37.724 -28.797 -29.754 1.00 37.87  ? 203 GLY A N     1 
ATOM   1467 C  CA    . GLY A 1 224 ? 37.745 -27.632 -30.658 1.00 34.93  ? 203 GLY A CA    1 
ATOM   1468 C  C     . GLY A 1 224 ? 37.440 -26.301 -29.990 1.00 37.40  ? 203 GLY A C     1 
ATOM   1469 O  O     . GLY A 1 224 ? 37.612 -25.273 -30.678 1.00 36.81  ? 203 GLY A O     1 
ATOM   1470 N  N     . GLY A 1 225 ? 36.993 -26.267 -28.724 1.00 38.67  ? 204 GLY A N     1 
ATOM   1471 C  CA    . GLY A 1 225 ? 36.662 -25.004 -28.022 1.00 36.11  ? 204 GLY A CA    1 
ATOM   1472 C  C     . GLY A 1 225 ? 37.309 -24.839 -26.637 1.00 38.16  ? 204 GLY A C     1 
ATOM   1473 O  O     . GLY A 1 225 ? 38.252 -25.605 -26.255 1.00 27.91  ? 204 GLY A O     1 
ATOM   1474 N  N     . ALA A 1 226 ? 36.771 -23.891 -25.862 1.00 35.72  ? 205 ALA A N     1 
ATOM   1475 C  CA    . ALA A 1 226 ? 37.350 -23.394 -24.596 1.00 35.08  ? 205 ALA A CA    1 
ATOM   1476 C  C     . ALA A 1 226 ? 37.401 -24.487 -23.521 1.00 32.70  ? 205 ALA A C     1 
ATOM   1477 O  O     . ALA A 1 226 ? 38.150 -24.272 -22.562 1.00 35.55  ? 205 ALA A O     1 
ATOM   1478 C  CB    . ALA A 1 226 ? 36.583 -22.179 -24.121 1.00 36.26  ? 205 ALA A CB    1 
ATOM   1479 N  N     . GLN A 1 227 ? 36.651 -25.592 -23.626 1.00 31.20  ? 206 GLN A N     1 
ATOM   1480 C  CA    . GLN A 1 227 ? 36.658 -26.660 -22.582 1.00 30.20  ? 206 GLN A CA    1 
ATOM   1481 C  C     . GLN A 1 227 ? 37.393 -27.920 -23.064 1.00 31.29  ? 206 GLN A C     1 
ATOM   1482 O  O     . GLN A 1 227 ? 37.116 -29.020 -22.518 1.00 29.53  ? 206 GLN A O     1 
ATOM   1483 C  CB    . GLN A 1 227 ? 35.231 -27.020 -22.157 1.00 33.45  ? 206 GLN A CB    1 
ATOM   1484 C  CG    . GLN A 1 227 ? 34.572 -25.986 -21.267 1.00 34.20  ? 206 GLN A CG    1 
ATOM   1485 C  CD    . GLN A 1 227 ? 34.027 -24.833 -22.066 1.00 38.84  ? 206 GLN A CD    1 
ATOM   1486 O  OE1   . GLN A 1 227 ? 33.137 -25.003 -22.917 1.00 37.48  ? 206 GLN A OE1   1 
ATOM   1487 N  NE2   . GLN A 1 227 ? 34.588 -23.656 -21.810 1.00 35.80  ? 206 GLN A NE2   1 
ATOM   1488 N  N     . GLN A 1 228 ? 38.351 -27.783 -23.984 1.00 35.64  ? 207 GLN A N     1 
ATOM   1489 C  CA    . GLN A 1 228 ? 39.020 -28.942 -24.629 1.00 33.63  ? 207 GLN A CA    1 
ATOM   1490 C  C     . GLN A 1 228 ? 39.992 -29.582 -23.640 1.00 35.77  ? 207 GLN A C     1 
ATOM   1491 O  O     . GLN A 1 228 ? 39.954 -30.823 -23.500 1.00 36.38  ? 207 GLN A O     1 
ATOM   1492 C  CB    . GLN A 1 228 ? 39.765 -28.515 -25.889 1.00 35.16  ? 207 GLN A CB    1 
ATOM   1493 C  CG    . GLN A 1 228 ? 40.379 -29.691 -26.640 1.00 35.90  ? 207 GLN A CG    1 
ATOM   1494 C  CD    . GLN A 1 228 ? 41.113 -29.271 -27.895 1.00 34.81  ? 207 GLN A CD    1 
ATOM   1495 O  OE1   . GLN A 1 228 ? 40.527 -28.953 -28.921 1.00 41.03  ? 207 GLN A OE1   1 
ATOM   1496 N  NE2   . GLN A 1 228 ? 42.423 -29.304 -27.837 1.00 35.30  ? 207 GLN A NE2   1 
ATOM   1497 N  N     . ASP A 1 229 ? 40.830 -28.767 -22.984 1.00 35.19  ? 208 ASP A N     1 
ATOM   1498 C  CA    . ASP A 1 229 ? 41.997 -29.262 -22.206 1.00 35.73  ? 208 ASP A CA    1 
ATOM   1499 C  C     . ASP A 1 229 ? 41.933 -28.761 -20.770 1.00 35.30  ? 208 ASP A C     1 
ATOM   1500 O  O     . ASP A 1 229 ? 41.263 -27.738 -20.507 1.00 33.16  ? 208 ASP A O     1 
ATOM   1501 C  CB    . ASP A 1 229 ? 43.316 -28.895 -22.888 1.00 39.30  ? 208 ASP A CB    1 
ATOM   1502 C  CG    . ASP A 1 229 ? 43.497 -29.653 -24.201 1.00 43.20  ? 208 ASP A CG    1 
ATOM   1503 O  OD1   . ASP A 1 229 ? 43.467 -30.927 -24.158 1.00 47.92  ? 208 ASP A OD1   1 
ATOM   1504 O  OD2   . ASP A 1 229 ? 43.603 -28.986 -25.263 1.00 37.95  ? 208 ASP A OD2   1 
ATOM   1505 N  N     . ARG A 1 230 ? 42.602 -29.514 -19.900 1.00 35.74  ? 209 ARG A N     1 
ATOM   1506 C  CA    . ARG A 1 230 ? 42.852 -29.255 -18.461 1.00 34.71  ? 209 ARG A CA    1 
ATOM   1507 C  C     . ARG A 1 230 ? 44.369 -29.307 -18.231 1.00 34.61  ? 209 ARG A C     1 
ATOM   1508 O  O     . ARG A 1 230 ? 45.096 -29.821 -19.100 1.00 33.72  ? 209 ARG A O     1 
ATOM   1509 C  CB    . ARG A 1 230 ? 42.232 -30.355 -17.588 1.00 36.76  ? 209 ARG A CB    1 
ATOM   1510 C  CG    . ARG A 1 230 ? 40.713 -30.444 -17.585 1.00 36.33  ? 209 ARG A CG    1 
ATOM   1511 C  CD    . ARG A 1 230 ? 39.933 -29.607 -16.583 1.00 35.70  ? 209 ARG A CD    1 
ATOM   1512 N  NE    . ARG A 1 230 ? 40.496 -29.457 -15.240 1.00 38.63  ? 209 ARG A NE    1 
ATOM   1513 C  CZ    . ARG A 1 230 ? 40.136 -30.106 -14.119 1.00 38.86  ? 209 ARG A CZ    1 
ATOM   1514 N  NH1   . ARG A 1 230 ? 39.233 -31.075 -14.127 1.00 38.71  ? 209 ARG A NH1   1 
ATOM   1515 N  NH2   . ARG A 1 230 ? 40.736 -29.802 -12.970 1.00 39.06  ? 209 ARG A NH2   1 
ATOM   1516 N  N     . LEU A 1 231 ? 44.816 -28.852 -17.066 1.00 35.58  ? 210 LEU A N     1 
ATOM   1517 C  CA    . LEU A 1 231 ? 46.228 -28.874 -16.621 1.00 34.48  ? 210 LEU A CA    1 
ATOM   1518 C  C     . LEU A 1 231 ? 46.418 -29.967 -15.558 1.00 33.64  ? 210 LEU A C     1 
ATOM   1519 O  O     . LEU A 1 231 ? 45.727 -29.902 -14.533 1.00 30.49  ? 210 LEU A O     1 
ATOM   1520 C  CB    . LEU A 1 231 ? 46.576 -27.494 -16.065 1.00 34.57  ? 210 LEU A CB    1 
ATOM   1521 C  CG    . LEU A 1 231 ? 46.895 -26.435 -17.119 1.00 39.72  ? 210 LEU A CG    1 
ATOM   1522 C  CD1   . LEU A 1 231 ? 45.734 -26.235 -18.062 1.00 44.84  ? 210 LEU A CD1   1 
ATOM   1523 C  CD2   . LEU A 1 231 ? 47.258 -25.102 -16.477 1.00 41.10  ? 210 LEU A CD2   1 
ATOM   1524 N  N     . VAL A 1 232 ? 47.341 -30.918 -15.784 1.00 32.56  ? 211 VAL A N     1 
ATOM   1525 C  CA    . VAL A 1 232 ? 47.777 -31.924 -14.768 1.00 32.09  ? 211 VAL A CA    1 
ATOM   1526 C  C     . VAL A 1 232 ? 48.240 -31.173 -13.506 1.00 34.50  ? 211 VAL A C     1 
ATOM   1527 O  O     . VAL A 1 232 ? 49.240 -30.373 -13.601 1.00 29.42  ? 211 VAL A O     1 
ATOM   1528 C  CB    . VAL A 1 232 ? 48.904 -32.846 -15.289 1.00 34.80  ? 211 VAL A CB    1 
ATOM   1529 C  CG1   . VAL A 1 232 ? 49.385 -33.792 -14.199 1.00 34.61  ? 211 VAL A CG1   1 
ATOM   1530 C  CG2   . VAL A 1 232 ? 48.505 -33.641 -16.528 1.00 35.52  ? 211 VAL A CG2   1 
ATOM   1531 N  N     . GLY A 1 233 ? 47.597 -31.462 -12.364 1.00 32.42  ? 212 GLY A N     1 
ATOM   1532 C  CA    . GLY A 1 233 ? 47.897 -30.839 -11.055 1.00 34.35  ? 212 GLY A CA    1 
ATOM   1533 C  C     . GLY A 1 233 ? 47.099 -29.550 -10.785 1.00 33.68  ? 212 GLY A C     1 
ATOM   1534 O  O     . GLY A 1 233 ? 47.228 -29.002 -9.681  1.00 35.99  ? 212 GLY A O     1 
ATOM   1535 N  N     . GLY A 1 234 ? 46.327 -29.059 -11.750 1.00 30.19  ? 213 GLY A N     1 
ATOM   1536 C  CA    . GLY A 1 234 ? 45.427 -27.901 -11.592 1.00 29.78  ? 213 GLY A CA    1 
ATOM   1537 C  C     . GLY A 1 234 ? 46.098 -26.607 -12.006 1.00 29.63  ? 213 GLY A C     1 
ATOM   1538 O  O     . GLY A 1 234 ? 47.261 -26.636 -12.435 1.00 30.78  ? 213 GLY A O     1 
ATOM   1539 N  N     . VAL A 1 235 ? 45.387 -25.498 -11.909 1.00 31.50  ? 214 VAL A N     1 
ATOM   1540 C  CA    . VAL A 1 235 ? 45.814 -24.208 -12.520 1.00 30.96  ? 214 VAL A CA    1 
ATOM   1541 C  C     . VAL A 1 235 ? 46.610 -23.389 -11.492 1.00 30.26  ? 214 VAL A C     1 
ATOM   1542 O  O     . VAL A 1 235 ? 47.555 -22.730 -11.889 1.00 34.40  ? 214 VAL A O     1 
ATOM   1543 C  CB    . VAL A 1 235 ? 44.592 -23.465 -13.088 1.00 30.86  ? 214 VAL A CB    1 
ATOM   1544 C  CG1   . VAL A 1 235 ? 44.937 -22.129 -13.724 1.00 31.44  ? 214 VAL A CG1   1 
ATOM   1545 C  CG2   . VAL A 1 235 ? 43.874 -24.350 -14.089 1.00 31.32  ? 214 VAL A CG2   1 
ATOM   1546 N  N     . GLN A 1 236 ? 46.279 -23.420 -10.209 1.00 32.59  ? 215 GLN A N     1 
ATOM   1547 C  CA    . GLN A 1 236 ? 47.007 -22.580 -9.223  1.00 36.79  ? 215 GLN A CA    1 
ATOM   1548 C  C     . GLN A 1 236 ? 48.518 -22.853 -9.252  1.00 35.17  ? 215 GLN A C     1 
ATOM   1549 O  O     . GLN A 1 236 ? 49.290 -21.896 -9.122  1.00 32.24  ? 215 GLN A O     1 
ATOM   1550 C  CB    . GLN A 1 236 ? 46.469 -22.745 -7.798  1.00 38.94  ? 215 GLN A CB    1 
ATOM   1551 C  CG    . GLN A 1 236 ? 46.895 -21.613 -6.875  1.00 40.35  ? 215 GLN A CG    1 
ATOM   1552 C  CD    . GLN A 1 236 ? 46.358 -21.864 -5.495  1.00 44.34  ? 215 GLN A CD    1 
ATOM   1553 O  OE1   . GLN A 1 236 ? 45.248 -22.351 -5.338  1.00 39.13  ? 215 GLN A OE1   1 
ATOM   1554 N  NE2   . GLN A 1 236 ? 47.163 -21.579 -4.487  1.00 50.24  ? 215 GLN A NE2   1 
ATOM   1555 N  N     . PRO A 1 237 ? 49.008 -24.123 -9.334  1.00 29.82  ? 216 PRO A N     1 
ATOM   1556 C  CA    . PRO A 1 237 ? 50.446 -24.365 -9.454  1.00 31.68  ? 216 PRO A CA    1 
ATOM   1557 C  C     . PRO A 1 237 ? 51.130 -23.601 -10.609 1.00 29.12  ? 216 PRO A C     1 
ATOM   1558 O  O     . PRO A 1 237 ? 52.237 -23.155 -10.426 1.00 32.39  ? 216 PRO A O     1 
ATOM   1559 C  CB    . PRO A 1 237 ? 50.559 -25.904 -9.597  1.00 29.98  ? 216 PRO A CB    1 
ATOM   1560 C  CG    . PRO A 1 237 ? 49.337 -26.409 -8.883  1.00 29.72  ? 216 PRO A CG    1 
ATOM   1561 C  CD    . PRO A 1 237 ? 48.259 -25.381 -9.207  1.00 29.76  ? 216 PRO A CD    1 
ATOM   1562 N  N     . LEU A 1 238 ? 50.475 -23.408 -11.750 1.00 30.06  ? 217 LEU A N     1 
ATOM   1563 C  CA    . LEU A 1 238 ? 51.053 -22.638 -12.889 1.00 31.90  ? 217 LEU A CA    1 
ATOM   1564 C  C     . LEU A 1 238 ? 51.253 -21.169 -12.450 1.00 33.46  ? 217 LEU A C     1 
ATOM   1565 O  O     . LEU A 1 238 ? 52.298 -20.579 -12.764 1.00 30.78  ? 217 LEU A O     1 
ATOM   1566 C  CB    . LEU A 1 238 ? 50.120 -22.746 -14.093 1.00 34.57  ? 217 LEU A CB    1 
ATOM   1567 C  CG    . LEU A 1 238 ? 50.504 -21.911 -15.315 1.00 35.80  ? 217 LEU A CG    1 
ATOM   1568 C  CD1   . LEU A 1 238 ? 51.847 -22.342 -15.860 1.00 39.96  ? 217 LEU A CD1   1 
ATOM   1569 C  CD2   . LEU A 1 238 ? 49.451 -22.030 -16.403 1.00 37.06  ? 217 LEU A CD2   1 
ATOM   1570 N  N     . ALA A 1 239 ? 50.275 -20.596 -11.748 1.00 31.50  ? 218 ALA A N     1 
ATOM   1571 C  CA    . ALA A 1 239 ? 50.346 -19.229 -11.195 1.00 34.52  ? 218 ALA A CA    1 
ATOM   1572 C  C     . ALA A 1 239 ? 51.509 -19.186 -10.199 1.00 36.70  ? 218 ALA A C     1 
ATOM   1573 O  O     . ALA A 1 239 ? 52.187 -18.132 -10.116 1.00 34.95  ? 218 ALA A O     1 
ATOM   1574 C  CB    . ALA A 1 239 ? 49.029 -18.851 -10.553 1.00 31.32  ? 218 ALA A CB    1 
ATOM   1575 N  N     . GLU A 1 240 ? 51.745 -20.289 -9.487  1.00 34.68  ? 219 GLU A N     1 
ATOM   1576 C  CA    . GLU A 1 240 ? 52.844 -20.357 -8.486  1.00 41.77  ? 219 GLU A CA    1 
ATOM   1577 C  C     . GLU A 1 240 ? 54.189 -20.352 -9.223  1.00 37.70  ? 219 GLU A C     1 
ATOM   1578 O  O     . GLU A 1 240 ? 55.093 -19.626 -8.791  1.00 31.74  ? 219 GLU A O     1 
ATOM   1579 C  CB    . GLU A 1 240 ? 52.651 -21.538 -7.531  1.00 49.40  ? 219 GLU A CB    1 
ATOM   1580 C  CG    . GLU A 1 240 ? 51.835 -21.162 -6.291  1.00 60.61  ? 219 GLU A CG    1 
ATOM   1581 C  CD    . GLU A 1 240 ? 51.170 -22.276 -5.485  1.00 68.91  ? 219 GLU A CD    1 
ATOM   1582 O  OE1   . GLU A 1 240 ? 51.286 -23.470 -5.875  1.00 80.08  ? 219 GLU A OE1   1 
ATOM   1583 O  OE2   . GLU A 1 240 ? 50.520 -21.944 -4.459  1.00 67.22  ? 219 GLU A OE2   1 
ATOM   1584 N  N     . ARG A 1 241 ? 54.309 -21.104 -10.318 1.00 39.71  ? 220 ARG A N     1 
ATOM   1585 C  CA    . ARG A 1 241 ? 55.566 -21.187 -11.117 1.00 35.82  ? 220 ARG A CA    1 
ATOM   1586 C  C     . ARG A 1 241 ? 55.843 -19.810 -11.736 1.00 36.13  ? 220 ARG A C     1 
ATOM   1587 O  O     . ARG A 1 241 ? 57.016 -19.367 -11.694 1.00 33.72  ? 220 ARG A O     1 
ATOM   1588 C  CB    . ARG A 1 241 ? 55.455 -22.334 -12.119 1.00 35.71  ? 220 ARG A CB    1 
ATOM   1589 C  CG    . ARG A 1 241 ? 55.279 -23.687 -11.446 1.00 33.27  ? 220 ARG A CG    1 
ATOM   1590 C  CD    . ARG A 1 241 ? 55.362 -24.803 -12.446 1.00 37.88  ? 220 ARG A CD    1 
ATOM   1591 N  NE    . ARG A 1 241 ? 55.418 -26.091 -11.798 1.00 42.15  ? 220 ARG A NE    1 
ATOM   1592 C  CZ    . ARG A 1 241 ? 55.687 -27.246 -12.403 1.00 46.38  ? 220 ARG A CZ    1 
ATOM   1593 N  NH1   . ARG A 1 241 ? 55.934 -27.307 -13.702 1.00 50.41  ? 220 ARG A NH1   1 
ATOM   1594 N  NH2   . ARG A 1 241 ? 55.696 -28.356 -11.692 1.00 46.59  ? 220 ARG A NH2   1 
ATOM   1595 N  N     . LEU A 1 242 ? 54.807 -19.099 -12.193 1.00 33.19  ? 221 LEU A N     1 
ATOM   1596 C  CA    . LEU A 1 242 ? 54.985 -17.709 -12.710 1.00 35.02  ? 221 LEU A CA    1 
ATOM   1597 C  C     . LEU A 1 242 ? 55.475 -16.797 -11.565 1.00 35.51  ? 221 LEU A C     1 
ATOM   1598 O  O     . LEU A 1 242 ? 56.446 -16.006 -11.805 1.00 32.54  ? 221 LEU A O     1 
ATOM   1599 C  CB    . LEU A 1 242 ? 53.698 -17.215 -13.385 1.00 35.01  ? 221 LEU A CB    1 
ATOM   1600 C  CG    . LEU A 1 242 ? 53.731 -15.781 -13.932 1.00 40.41  ? 221 LEU A CG    1 
ATOM   1601 C  CD1   . LEU A 1 242 ? 54.989 -15.517 -14.760 1.00 40.06  ? 221 LEU A CD1   1 
ATOM   1602 C  CD2   . LEU A 1 242 ? 52.484 -15.470 -14.763 1.00 38.97  ? 221 LEU A CD2   1 
ATOM   1603 N  N     . ALA A 1 243 ? 54.932 -16.948 -10.345 1.00 31.93  ? 222 ALA A N     1 
ATOM   1604 C  CA    . ALA A 1 243 ? 55.285 -16.108 -9.174  1.00 30.81  ? 222 ALA A CA    1 
ATOM   1605 C  C     . ALA A 1 243 ? 56.756 -16.323 -8.775  1.00 32.58  ? 222 ALA A C     1 
ATOM   1606 O  O     . ALA A 1 243 ? 57.437 -15.323 -8.431  1.00 29.73  ? 222 ALA A O     1 
ATOM   1607 C  CB    . ALA A 1 243 ? 54.349 -16.371 -8.019  1.00 32.43  ? 222 ALA A CB    1 
ATOM   1608 N  N     . ALA A 1 244 ? 57.245 -17.566 -8.828  1.00 33.34  ? 223 ALA A N     1 
ATOM   1609 C  CA    . ALA A 1 244 ? 58.648 -17.956 -8.532  1.00 32.03  ? 223 ALA A CA    1 
ATOM   1610 C  C     . ALA A 1 244 ? 59.671 -17.293 -9.488  1.00 32.68  ? 223 ALA A C     1 
ATOM   1611 O  O     . ALA A 1 244 ? 60.839 -17.269 -9.140  1.00 32.74  ? 223 ALA A O     1 
ATOM   1612 C  CB    . ALA A 1 244 ? 58.767 -19.465 -8.584  1.00 33.06  ? 223 ALA A CB    1 
ATOM   1613 N  N     . ARG A 1 245 ? 59.266 -16.711 -10.620 1.00 35.16  ? 224 ARG A N     1 
ATOM   1614 C  CA    . ARG A 1 245 ? 60.183 -15.950 -11.514 1.00 35.56  ? 224 ARG A CA    1 
ATOM   1615 C  C     . ARG A 1 245 ? 60.532 -14.585 -10.925 1.00 34.38  ? 224 ARG A C     1 
ATOM   1616 O  O     . ARG A 1 245 ? 61.503 -13.973 -11.441 1.00 32.08  ? 224 ARG A O     1 
ATOM   1617 C  CB    . ARG A 1 245 ? 59.584 -15.731 -12.904 1.00 36.08  ? 224 ARG A CB    1 
ATOM   1618 C  CG    . ARG A 1 245 ? 59.478 -16.994 -13.749 1.00 36.75  ? 224 ARG A CG    1 
ATOM   1619 C  CD    . ARG A 1 245 ? 60.743 -17.814 -13.757 1.00 38.63  ? 224 ARG A CD    1 
ATOM   1620 N  NE    . ARG A 1 245 ? 60.510 -19.132 -14.337 1.00 45.61  ? 224 ARG A NE    1 
ATOM   1621 C  CZ    . ARG A 1 245 ? 60.879 -19.508 -15.567 1.00 47.26  ? 224 ARG A CZ    1 
ATOM   1622 N  NH1   . ARG A 1 245 ? 61.507 -18.672 -16.381 1.00 52.01  ? 224 ARG A NH1   1 
ATOM   1623 N  NH2   . ARG A 1 245 ? 60.604 -20.726 -15.985 1.00 48.31  ? 224 ARG A NH2   1 
ATOM   1624 N  N     . LEU A 1 246 ? 59.827 -14.141 -9.874  1.00 33.85  ? 225 LEU A N     1 
ATOM   1625 C  CA    . LEU A 1 246 ? 60.130 -12.849 -9.202  1.00 34.32  ? 225 LEU A CA    1 
ATOM   1626 C  C     . LEU A 1 246 ? 61.162 -13.056 -8.096  1.00 35.53  ? 225 LEU A C     1 
ATOM   1627 O  O     . LEU A 1 246 ? 61.188 -14.102 -7.457  1.00 36.47  ? 225 LEU A O     1 
ATOM   1628 C  CB    . LEU A 1 246 ? 58.840 -12.270 -8.642  1.00 32.57  ? 225 LEU A CB    1 
ATOM   1629 C  CG    . LEU A 1 246 ? 57.777 -11.979 -9.690  1.00 38.05  ? 225 LEU A CG    1 
ATOM   1630 C  CD1   . LEU A 1 246 ? 56.464 -11.630 -9.021  1.00 42.25  ? 225 LEU A CD1   1 
ATOM   1631 C  CD2   . LEU A 1 246 ? 58.218 -10.846 -10.596 1.00 40.53  ? 225 LEU A CD2   1 
ATOM   1632 N  N     . PRO A 1 247 ? 62.003 -12.046 -7.790  1.00 33.56  ? 226 PRO A N     1 
ATOM   1633 C  CA    . PRO A 1 247 ? 62.897 -12.121 -6.638  1.00 35.92  ? 226 PRO A CA    1 
ATOM   1634 C  C     . PRO A 1 247 ? 62.206 -12.190 -5.264  1.00 36.79  ? 226 PRO A C     1 
ATOM   1635 O  O     . PRO A 1 247 ? 61.050 -11.794 -5.123  1.00 32.10  ? 226 PRO A O     1 
ATOM   1636 C  CB    . PRO A 1 247 ? 63.771 -10.844 -6.719  1.00 37.95  ? 226 PRO A CB    1 
ATOM   1637 C  CG    . PRO A 1 247 ? 63.091 -9.939  -7.715  1.00 38.02  ? 226 PRO A CG    1 
ATOM   1638 C  CD    . PRO A 1 247 ? 62.167 -10.806 -8.558  1.00 38.76  ? 226 PRO A CD    1 
ATOM   1639 N  N     . ASP A 1 248 ? 62.948 -12.691 -4.267  1.00 34.54  ? 227 ASP A N     1 
ATOM   1640 C  CA    . ASP A 1 248 ? 62.501 -12.716 -2.850  1.00 35.64  ? 227 ASP A CA    1 
ATOM   1641 C  C     . ASP A 1 248 ? 62.169 -11.262 -2.457  1.00 34.10  ? 227 ASP A C     1 
ATOM   1642 O  O     . ASP A 1 248 ? 62.936 -10.363 -2.846  1.00 35.07  ? 227 ASP A O     1 
ATOM   1643 C  CB    . ASP A 1 248 ? 63.540 -13.412 -1.964  1.00 31.35  ? 227 ASP A CB    1 
ATOM   1644 C  CG    . ASP A 1 248 ? 63.675 -14.917 -2.219  1.00 34.94  ? 227 ASP A CG    1 
ATOM   1645 O  OD1   . ASP A 1 248 ? 62.925 -15.457 -3.053  1.00 34.78  ? 227 ASP A OD1   1 
ATOM   1646 O  OD2   . ASP A 1 248 ? 64.541 -15.546 -1.603  1.00 34.99  ? 227 ASP A OD2   1 
ATOM   1647 N  N     . GLY A 1 249 ? 61.029 -11.032 -1.804  1.00 33.92  ? 228 GLY A N     1 
ATOM   1648 C  CA    . GLY A 1 249 ? 60.645 -9.701  -1.288  1.00 36.28  ? 228 GLY A CA    1 
ATOM   1649 C  C     . GLY A 1 249 ? 59.764 -8.922  -2.247  1.00 36.36  ? 228 GLY A C     1 
ATOM   1650 O  O     . GLY A 1 249 ? 59.112 -7.944  -1.798  1.00 38.43  ? 228 GLY A O     1 
ATOM   1651 N  N     . ALA A 1 250 ? 59.711 -9.324  -3.514  1.00 33.40  ? 229 ALA A N     1 
ATOM   1652 C  CA    . ALA A 1 250 ? 58.875 -8.662  -4.539  1.00 35.49  ? 229 ALA A CA    1 
ATOM   1653 C  C     . ALA A 1 250 ? 57.396 -8.992  -4.302  1.00 37.77  ? 229 ALA A C     1 
ATOM   1654 O  O     . ALA A 1 250 ? 56.599 -8.056  -4.389  1.00 35.58  ? 229 ALA A O     1 
ATOM   1655 C  CB    . ALA A 1 250 ? 59.311 -9.037  -5.931  1.00 35.59  ? 229 ALA A CB    1 
ATOM   1656 N  N     . LEU A 1 251 ? 57.044 -10.248 -3.992  1.00 34.96  ? 230 LEU A N     1 
ATOM   1657 C  CA    . LEU A 1 251 ? 55.632 -10.629 -3.691  1.00 36.63  ? 230 LEU A CA    1 
ATOM   1658 C  C     . LEU A 1 251 ? 55.341 -10.467 -2.187  1.00 36.54  ? 230 LEU A C     1 
ATOM   1659 O  O     . LEU A 1 251 ? 56.044 -11.054 -1.380  1.00 34.89  ? 230 LEU A O     1 
ATOM   1660 C  CB    . LEU A 1 251 ? 55.365 -12.061 -4.164  1.00 37.31  ? 230 LEU A CB    1 
ATOM   1661 C  CG    . LEU A 1 251 ? 53.958 -12.617 -3.917  1.00 38.34  ? 230 LEU A CG    1 
ATOM   1662 C  CD1   . LEU A 1 251 ? 52.921 -11.894 -4.770  1.00 36.87  ? 230 LEU A CD1   1 
ATOM   1663 C  CD2   . LEU A 1 251 ? 53.937 -14.112 -4.216  1.00 38.35  ? 230 LEU A CD2   1 
ATOM   1664 N  N     . ARG A 1 252 ? 54.298 -9.706  -1.851  1.00 36.71  ? 231 ARG A N     1 
ATOM   1665 C  CA    . ARG A 1 252 ? 53.780 -9.519  -0.471  1.00 35.04  ? 231 ARG A CA    1 
ATOM   1666 C  C     . ARG A 1 252 ? 52.346 -10.058 -0.404  1.00 34.02  ? 231 ARG A C     1 
ATOM   1667 O  O     . ARG A 1 252 ? 51.448 -9.512  -1.076  1.00 33.53  ? 231 ARG A O     1 
ATOM   1668 C  CB    . ARG A 1 252 ? 53.832 -8.040  -0.088  1.00 36.47  ? 231 ARG A CB    1 
ATOM   1669 C  CG    . ARG A 1 252 ? 55.143 -7.344  -0.431  1.00 38.77  ? 231 ARG A CG    1 
ATOM   1670 C  CD    . ARG A 1 252 ? 56.224 -7.559  0.604   1.00 39.99  ? 231 ARG A CD    1 
ATOM   1671 N  NE    . ARG A 1 252 ? 57.446 -6.904  0.166   1.00 40.83  ? 231 ARG A NE    1 
ATOM   1672 C  CZ    . ARG A 1 252 ? 57.725 -5.608  0.307   1.00 40.72  ? 231 ARG A CZ    1 
ATOM   1673 N  NH1   . ARG A 1 252 ? 56.863 -4.790  0.893   1.00 36.30  ? 231 ARG A NH1   1 
ATOM   1674 N  NH2   . ARG A 1 252 ? 58.876 -5.145  -0.156  1.00 39.74  ? 231 ARG A NH2   1 
ATOM   1675 N  N     . LEU A 1 253 ? 52.136 -11.114 0.364   1.00 32.21  ? 232 LEU A N     1 
ATOM   1676 C  CA    . LEU A 1 253 ? 50.814 -11.776 0.497   1.00 29.83  ? 232 LEU A CA    1 
ATOM   1677 C  C     . LEU A 1 253 ? 50.149 -11.211 1.759   1.00 31.62  ? 232 LEU A C     1 
ATOM   1678 O  O     . LEU A 1 253 ? 50.826 -10.499 2.572   1.00 29.89  ? 232 LEU A O     1 
ATOM   1679 C  CB    . LEU A 1 253 ? 51.013 -13.297 0.554   1.00 26.47  ? 232 LEU A CB    1 
ATOM   1680 C  CG    . LEU A 1 253 ? 51.560 -13.912 -0.736  1.00 28.31  ? 232 LEU A CG    1 
ATOM   1681 C  CD1   . LEU A 1 253 ? 52.023 -15.351 -0.560  1.00 28.04  ? 232 LEU A CD1   1 
ATOM   1682 C  CD2   . LEU A 1 253 ? 50.531 -13.865 -1.842  1.00 26.22  ? 232 LEU A CD2   1 
ATOM   1683 N  N     . SER A 1 254 ? 48.863 -11.496 1.916   1.00 29.10  ? 233 SER A N     1 
ATOM   1684 C  CA    . SER A 1 254 ? 48.057 -10.998 3.045   1.00 31.03  ? 233 SER A CA    1 
ATOM   1685 C  C     . SER A 1 254 ? 48.275 -9.479  3.198   1.00 30.39  ? 233 SER A C     1 
ATOM   1686 O  O     . SER A 1 254 ? 48.264 -9.006  4.310   1.00 33.47  ? 233 SER A O     1 
ATOM   1687 C  CB    . SER A 1 254 ? 48.395 -11.793 4.250   1.00 31.19  ? 233 SER A CB    1 
ATOM   1688 O  OG    . SER A 1 254 ? 48.061 -13.169 4.026   1.00 33.97  ? 233 SER A OG    1 
ATOM   1689 N  N     . THR A 1 255 ? 48.420 -8.746  2.092   1.00 30.71  ? 234 THR A N     1 
ATOM   1690 C  CA    . THR A 1 255 ? 48.663 -7.264  2.071   1.00 30.77  ? 234 THR A CA    1 
ATOM   1691 C  C     . THR A 1 255 ? 47.623 -6.616  1.153   1.00 29.86  ? 234 THR A C     1 
ATOM   1692 O  O     . THR A 1 255 ? 47.913 -6.304  -0.005  1.00 30.95  ? 234 THR A O     1 
ATOM   1693 C  CB    . THR A 1 255 ? 50.117 -6.957  1.670   1.00 31.52  ? 234 THR A CB    1 
ATOM   1694 O  OG1   . THR A 1 255 ? 50.978 -7.744  2.495   1.00 29.25  ? 234 THR A OG1   1 
ATOM   1695 C  CG2   . THR A 1 255 ? 50.505 -5.497  1.837   1.00 31.55  ? 234 THR A CG2   1 
ATOM   1696 N  N     . PRO A 1 256 ? 46.347 -6.503  1.600   1.00 28.85  ? 235 PRO A N     1 
ATOM   1697 C  CA    . PRO A 1 256 ? 45.315 -5.831  0.811   1.00 29.74  ? 235 PRO A CA    1 
ATOM   1698 C  C     . PRO A 1 256 ? 45.727 -4.366  0.556   1.00 30.75  ? 235 PRO A C     1 
ATOM   1699 O  O     . PRO A 1 256 ? 46.326 -3.788  1.463   1.00 28.78  ? 235 PRO A O     1 
ATOM   1700 C  CB    . PRO A 1 256 ? 44.059 -5.890  1.693   1.00 31.72  ? 235 PRO A CB    1 
ATOM   1701 C  CG    . PRO A 1 256 ? 44.344 -6.992  2.735   1.00 32.43  ? 235 PRO A CG    1 
ATOM   1702 C  CD    . PRO A 1 256 ? 45.847 -7.001  2.899   1.00 31.68  ? 235 PRO A CD    1 
ATOM   1703 N  N     . VAL A 1 257 ? 45.473 -3.817  -0.645  1.00 30.85  ? 236 VAL A N     1 
ATOM   1704 C  CA    . VAL A 1 257 ? 45.739 -2.371  -0.933  1.00 31.82  ? 236 VAL A CA    1 
ATOM   1705 C  C     . VAL A 1 257 ? 44.489 -1.616  -0.513  1.00 33.40  ? 236 VAL A C     1 
ATOM   1706 O  O     . VAL A 1 257 ? 43.403 -2.026  -0.951  1.00 36.42  ? 236 VAL A O     1 
ATOM   1707 C  CB    . VAL A 1 257 ? 46.143 -2.084  -2.392  1.00 31.70  ? 236 VAL A CB    1 
ATOM   1708 C  CG1   . VAL A 1 257 ? 46.089 -0.608  -2.730  1.00 31.34  ? 236 VAL A CG1   1 
ATOM   1709 C  CG2   . VAL A 1 257 ? 47.546 -2.608  -2.685  1.00 32.82  ? 236 VAL A CG2   1 
ATOM   1710 N  N     . ARG A 1 258 ? 44.637 -0.627  0.370   1.00 31.09  ? 237 ARG A N     1 
ATOM   1711 C  CA    . ARG A 1 258 ? 43.495 0.176   0.885   1.00 32.50  ? 237 ARG A CA    1 
ATOM   1712 C  C     . ARG A 1 258 ? 43.453 1.538   0.201   1.00 30.18  ? 237 ARG A C     1 
ATOM   1713 O  O     . ARG A 1 258 ? 42.368 2.073   0.041   1.00 32.25  ? 237 ARG A O     1 
ATOM   1714 C  CB    . ARG A 1 258 ? 43.602 0.372   2.394   1.00 35.46  ? 237 ARG A CB    1 
ATOM   1715 C  CG    . ARG A 1 258 ? 43.258 -0.868  3.197   1.00 38.07  ? 237 ARG A CG    1 
ATOM   1716 C  CD    . ARG A 1 258 ? 43.717 -0.649  4.609   1.00 42.92  ? 237 ARG A CD    1 
ATOM   1717 N  NE    . ARG A 1 258 ? 43.246 -1.667  5.536   1.00 45.96  ? 237 ARG A NE    1 
ATOM   1718 C  CZ    . ARG A 1 258 ? 43.361 -1.568  6.854   1.00 45.94  ? 237 ARG A CZ    1 
ATOM   1719 N  NH1   . ARG A 1 258 ? 43.922 -0.494  7.395   1.00 49.08  ? 237 ARG A NH1   1 
ATOM   1720 N  NH2   . ARG A 1 258 ? 42.928 -2.546  7.624   1.00 45.04  ? 237 ARG A NH2   1 
ATOM   1721 N  N     . GLY A 1 259 ? 44.602 2.077   -0.174  1.00 30.34  ? 238 GLY A N     1 
ATOM   1722 C  CA    . GLY A 1 259 ? 44.700 3.461   -0.677  1.00 29.91  ? 238 GLY A CA    1 
ATOM   1723 C  C     . GLY A 1 259 ? 45.691 3.521   -1.807  1.00 29.27  ? 238 GLY A C     1 
ATOM   1724 O  O     . GLY A 1 259 ? 46.700 2.783   -1.758  1.00 32.61  ? 238 GLY A O     1 
ATOM   1725 N  N     . LEU A 1 260 ? 45.414 4.331   -2.813  1.00 29.23  ? 239 LEU A N     1 
ATOM   1726 C  CA    . LEU A 1 260 ? 46.371 4.594   -3.908  1.00 29.92  ? 239 LEU A CA    1 
ATOM   1727 C  C     . LEU A 1 260 ? 46.344 6.097   -4.227  1.00 31.66  ? 239 LEU A C     1 
ATOM   1728 O  O     . LEU A 1 260 ? 45.360 6.625   -4.798  1.00 31.80  ? 239 LEU A O     1 
ATOM   1729 C  CB    . LEU A 1 260 ? 45.992 3.674   -5.066  1.00 33.48  ? 239 LEU A CB    1 
ATOM   1730 C  CG    . LEU A 1 260 ? 46.796 3.802   -6.355  1.00 36.35  ? 239 LEU A CG    1 
ATOM   1731 C  CD1   . LEU A 1 260 ? 48.275 3.505   -6.141  1.00 40.95  ? 239 LEU A CD1   1 
ATOM   1732 C  CD2   . LEU A 1 260 ? 46.203 2.862   -7.388  1.00 35.96  ? 239 LEU A CD2   1 
ATOM   1733 N  N     . ALA A 1 261 ? 47.390 6.791   -3.822  1.00 29.25  ? 240 ALA A N     1 
ATOM   1734 C  CA    . ALA A 1 261 ? 47.526 8.248   -4.007  1.00 32.03  ? 240 ALA A CA    1 
ATOM   1735 C  C     . ALA A 1 261 ? 48.579 8.482   -5.093  1.00 36.63  ? 240 ALA A C     1 
ATOM   1736 O  O     . ALA A 1 261 ? 49.480 7.632   -5.263  1.00 36.69  ? 240 ALA A O     1 
ATOM   1737 C  CB    . ALA A 1 261 ? 47.911 8.902   -2.687  1.00 32.75  ? 240 ALA A CB    1 
ATOM   1738 N  N     . GLN A 1 262 ? 48.472 9.596   -5.808  1.00 35.75  ? 241 GLN A N     1 
ATOM   1739 C  CA    . GLN A 1 262 ? 49.430 9.931   -6.876  1.00 35.74  ? 241 GLN A CA    1 
ATOM   1740 C  C     . GLN A 1 262 ? 49.588 11.444  -6.966  1.00 36.16  ? 241 GLN A C     1 
ATOM   1741 O  O     . GLN A 1 262 ? 48.663 12.156  -6.583  1.00 38.55  ? 241 GLN A O     1 
ATOM   1742 C  CB    . GLN A 1 262 ? 48.967 9.335   -8.198  1.00 34.73  ? 241 GLN A CB    1 
ATOM   1743 C  CG    . GLN A 1 262 ? 47.748 10.013  -8.794  1.00 34.93  ? 241 GLN A CG    1 
ATOM   1744 C  CD    . GLN A 1 262 ? 47.514 9.500   -10.191 1.00 37.21  ? 241 GLN A CD    1 
ATOM   1745 O  OE1   . GLN A 1 262 ? 46.444 8.960   -10.519 1.00 39.37  ? 241 GLN A OE1   1 
ATOM   1746 N  NE2   . GLN A 1 262 ? 48.550 9.613   -11.007 1.00 35.06  ? 241 GLN A NE2   1 
ATOM   1747 N  N     . ASP A 1 263 ? 50.727 11.872  -7.494  1.00 38.58  ? 242 ASP A N     1 
ATOM   1748 C  CA    . ASP A 1 263 ? 51.108 13.294  -7.696  1.00 44.80  ? 242 ASP A CA    1 
ATOM   1749 C  C     . ASP A 1 263 ? 51.985 13.330  -8.949  1.00 44.18  ? 242 ASP A C     1 
ATOM   1750 O  O     . ASP A 1 263 ? 51.988 12.312  -9.687  1.00 44.55  ? 242 ASP A O     1 
ATOM   1751 C  CB    . ASP A 1 263 ? 51.789 13.860  -6.437  1.00 45.61  ? 242 ASP A CB    1 
ATOM   1752 C  CG    . ASP A 1 263 ? 53.095 13.166  -6.087  1.00 46.29  ? 242 ASP A CG    1 
ATOM   1753 O  OD1   . ASP A 1 263 ? 53.730 12.610  -7.013  1.00 44.45  ? 242 ASP A OD1   1 
ATOM   1754 O  OD2   . ASP A 1 263 ? 53.463 13.175  -4.902  1.00 51.94  ? 242 ASP A OD2   1 
ATOM   1755 N  N     . GLY A 1 264 ? 52.730 14.419  -9.153  1.00 44.13  ? 243 GLY A N     1 
ATOM   1756 C  CA    . GLY A 1 264 ? 53.555 14.641  -10.356 1.00 43.71  ? 243 GLY A CA    1 
ATOM   1757 C  C     . GLY A 1 264 ? 54.832 13.812  -10.354 1.00 43.18  ? 243 GLY A C     1 
ATOM   1758 O  O     . GLY A 1 264 ? 55.480 13.760  -11.408 1.00 47.89  ? 243 GLY A O     1 
ATOM   1759 N  N     . ASP A 1 265 ? 55.185 13.175  -9.233  1.00 42.51  ? 244 ASP A N     1 
ATOM   1760 C  CA    . ASP A 1 265 ? 56.467 12.444  -9.071  1.00 45.91  ? 244 ASP A CA    1 
ATOM   1761 C  C     . ASP A 1 265 ? 56.250 10.939  -8.833  1.00 42.54  ? 244 ASP A C     1 
ATOM   1762 O  O     . ASP A 1 265 ? 57.224 10.201  -8.948  1.00 43.49  ? 244 ASP A O     1 
ATOM   1763 C  CB    . ASP A 1 265 ? 57.309 13.117  -7.986  1.00 52.59  ? 244 ASP A CB    1 
ATOM   1764 C  CG    . ASP A 1 265 ? 57.946 14.410  -8.472  1.00 64.83  ? 244 ASP A CG    1 
ATOM   1765 O  OD1   . ASP A 1 265 ? 58.687 14.355  -9.504  1.00 66.88  ? 244 ASP A OD1   1 
ATOM   1766 O  OD2   . ASP A 1 265 ? 57.677 15.469  -7.843  1.00 73.51  ? 244 ASP A OD2   1 
ATOM   1767 N  N     . GLY A 1 266 ? 55.043 10.467  -8.539  1.00 41.05  ? 245 GLY A N     1 
ATOM   1768 C  CA    . GLY A 1 266 ? 54.840 9.020   -8.316  1.00 41.91  ? 245 GLY A CA    1 
ATOM   1769 C  C     . GLY A 1 266 ? 53.549 8.705   -7.591  1.00 39.63  ? 245 GLY A C     1 
ATOM   1770 O  O     . GLY A 1 266 ? 52.638 9.568   -7.559  1.00 33.75  ? 245 GLY A O     1 
ATOM   1771 N  N     . VAL A 1 267 ? 53.484 7.493   -7.041  1.00 35.57  ? 246 VAL A N     1 
ATOM   1772 C  CA    . VAL A 1 267 ? 52.265 6.938   -6.400  1.00 36.79  ? 246 VAL A CA    1 
ATOM   1773 C  C     . VAL A 1 267 ? 52.647 6.425   -5.016  1.00 34.45  ? 246 VAL A C     1 
ATOM   1774 O  O     . VAL A 1 267 ? 53.760 5.963   -4.857  1.00 35.64  ? 246 VAL A O     1 
ATOM   1775 C  CB    . VAL A 1 267 ? 51.639 5.815   -7.249  1.00 38.65  ? 246 VAL A CB    1 
ATOM   1776 C  CG1   . VAL A 1 267 ? 51.383 6.261   -8.676  1.00 38.51  ? 246 VAL A CG1   1 
ATOM   1777 C  CG2   . VAL A 1 267 ? 52.484 4.546   -7.237  1.00 37.09  ? 246 VAL A CG2   1 
ATOM   1778 N  N     . THR A 1 268 ? 51.706 6.472   -4.087  1.00 35.36  ? 247 THR A N     1 
ATOM   1779 C  CA    . THR A 1 268 ? 51.835 5.956   -2.707  1.00 36.83  ? 247 THR A CA    1 
ATOM   1780 C  C     . THR A 1 268 ? 50.681 4.993   -2.471  1.00 35.80  ? 247 THR A C     1 
ATOM   1781 O  O     . THR A 1 268 ? 49.547 5.368   -2.770  1.00 36.24  ? 247 THR A O     1 
ATOM   1782 C  CB    . THR A 1 268 ? 51.897 7.092   -1.688  1.00 35.40  ? 247 THR A CB    1 
ATOM   1783 O  OG1   . THR A 1 268 ? 52.972 7.888   -2.187  1.00 43.63  ? 247 THR A OG1   1 
ATOM   1784 C  CG2   . THR A 1 268 ? 52.169 6.634   -0.273  1.00 35.82  ? 247 THR A CG2   1 
ATOM   1785 N  N     . VAL A 1 269 ? 51.018 3.772   -2.059  1.00 34.90  ? 248 VAL A N     1 
ATOM   1786 C  CA    . VAL A 1 269 ? 50.071 2.682   -1.716  1.00 33.95  ? 248 VAL A CA    1 
ATOM   1787 C  C     . VAL A 1 269 ? 50.024 2.611   -0.195  1.00 33.68  ? 248 VAL A C     1 
ATOM   1788 O  O     . VAL A 1 269 ? 51.091 2.389   0.380   1.00 37.06  ? 248 VAL A O     1 
ATOM   1789 C  CB    . VAL A 1 269 ? 50.528 1.353   -2.339  1.00 36.85  ? 248 VAL A CB    1 
ATOM   1790 C  CG1   . VAL A 1 269 ? 49.677 0.189   -1.867  1.00 38.94  ? 248 VAL A CG1   1 
ATOM   1791 C  CG2   . VAL A 1 269 ? 50.530 1.426   -3.852  1.00 39.51  ? 248 VAL A CG2   1 
ATOM   1792 N  N     . ARG A 1 270 ? 48.838 2.815   0.403   1.00 33.96  ? 249 ARG A N     1 
ATOM   1793 C  CA    . ARG A 1 270 ? 48.555 2.599   1.844   1.00 33.37  ? 249 ARG A CA    1 
ATOM   1794 C  C     . ARG A 1 270 ? 47.976 1.185   2.034   1.00 31.09  ? 249 ARG A C     1 
ATOM   1795 O  O     . ARG A 1 270 ? 46.971 0.886   1.398   1.00 34.50  ? 249 ARG A O     1 
ATOM   1796 C  CB    . ARG A 1 270 ? 47.577 3.652   2.375   1.00 35.27  ? 249 ARG A CB    1 
ATOM   1797 C  CG    . ARG A 1 270 ? 47.454 3.661   3.899   1.00 38.42  ? 249 ARG A CG    1 
ATOM   1798 C  CD    . ARG A 1 270 ? 46.394 4.594   4.462   1.00 38.21  ? 249 ARG A CD    1 
ATOM   1799 N  NE    . ARG A 1 270 ? 45.023 4.127   4.231   1.00 42.85  ? 249 ARG A NE    1 
ATOM   1800 C  CZ    . ARG A 1 270 ? 44.158 4.628   3.339   1.00 45.43  ? 249 ARG A CZ    1 
ATOM   1801 N  NH1   . ARG A 1 270 ? 44.481 5.661   2.576   1.00 46.39  ? 249 ARG A NH1   1 
ATOM   1802 N  NH2   . ARG A 1 270 ? 42.946 4.106   3.235   1.00 45.25  ? 249 ARG A NH2   1 
ATOM   1803 N  N     . THR A 1 271 ? 48.584 0.375   2.902   1.00 30.12  ? 250 THR A N     1 
ATOM   1804 C  CA    . THR A 1 271 ? 48.126 -0.972  3.361   1.00 32.20  ? 250 THR A CA    1 
ATOM   1805 C  C     . THR A 1 271 ? 48.017 -0.919  4.890   1.00 34.99  ? 250 THR A C     1 
ATOM   1806 O  O     . THR A 1 271 ? 48.533 0.077   5.447   1.00 35.34  ? 250 THR A O     1 
ATOM   1807 C  CB    . THR A 1 271 ? 49.138 -2.065  2.987   1.00 28.84  ? 250 THR A CB    1 
ATOM   1808 O  OG1   . THR A 1 271 ? 50.245 -1.945  3.865   1.00 31.15  ? 250 THR A OG1   1 
ATOM   1809 C  CG2   . THR A 1 271 ? 49.691 -1.952  1.590   1.00 30.64  ? 250 THR A CG2   1 
ATOM   1810 N  N     . ALA A 1 272 ? 47.442 -1.932  5.550   1.00 35.08  ? 251 ALA A N     1 
ATOM   1811 C  CA    . ALA A 1 272 ? 47.358 -1.990  7.034   1.00 41.82  ? 251 ALA A CA    1 
ATOM   1812 C  C     . ALA A 1 272 ? 48.762 -1.810  7.611   1.00 45.15  ? 251 ALA A C     1 
ATOM   1813 O  O     . ALA A 1 272 ? 48.875 -1.075  8.586   1.00 49.71  ? 251 ALA A O     1 
ATOM   1814 C  CB    . ALA A 1 272 ? 46.754 -3.284  7.534   1.00 40.03  ? 251 ALA A CB    1 
ATOM   1815 N  N     . GLY A 1 273 ? 49.775 -2.452  7.007   1.00 48.92  ? 252 GLY A N     1 
ATOM   1816 C  CA    . GLY A 1 273 ? 51.169 -2.498  7.494   1.00 50.87  ? 252 GLY A CA    1 
ATOM   1817 C  C     . GLY A 1 273 ? 51.907 -1.165  7.385   1.00 52.64  ? 252 GLY A C     1 
ATOM   1818 O  O     . GLY A 1 273 ? 52.755 -0.901  8.249   1.00 61.74  ? 252 GLY A O     1 
ATOM   1819 N  N     . GLY A 1 274 ? 51.641 -0.366  6.353   1.00 50.86  ? 253 GLY A N     1 
ATOM   1820 C  CA    . GLY A 1 274 ? 52.341 0.909   6.104   1.00 48.35  ? 253 GLY A CA    1 
ATOM   1821 C  C     . GLY A 1 274 ? 52.220 1.343   4.653   1.00 45.32  ? 253 GLY A C     1 
ATOM   1822 O  O     . GLY A 1 274 ? 51.166 1.103   4.046   1.00 50.44  ? 253 GLY A O     1 
ATOM   1823 N  N     . GLU A 1 275 ? 53.259 1.968   4.117   1.00 43.63  ? 254 GLU A N     1 
ATOM   1824 C  CA    . GLU A 1 275 ? 53.240 2.622   2.786   1.00 48.79  ? 254 GLU A CA    1 
ATOM   1825 C  C     . GLU A 1 275 ? 54.214 1.915   1.855   1.00 45.97  ? 254 GLU A C     1 
ATOM   1826 O  O     . GLU A 1 275 ? 55.228 1.388   2.339   1.00 46.55  ? 254 GLU A O     1 
ATOM   1827 C  CB    . GLU A 1 275 ? 53.705 4.075   2.857   1.00 52.48  ? 254 GLU A CB    1 
ATOM   1828 C  CG    . GLU A 1 275 ? 52.670 5.032   3.410   1.00 64.59  ? 254 GLU A CG    1 
ATOM   1829 C  CD    . GLU A 1 275 ? 53.067 6.494   3.241   1.00 68.77  ? 254 GLU A CD    1 
ATOM   1830 O  OE1   . GLU A 1 275 ? 54.277 6.759   2.965   1.00 66.93  ? 254 GLU A OE1   1 
ATOM   1831 O  OE2   . GLU A 1 275 ? 52.168 7.362   3.365   1.00 65.31  ? 254 GLU A OE2   1 
ATOM   1832 N  N     . VAL A 1 276 ? 53.948 1.999   0.561   1.00 41.20  ? 255 VAL A N     1 
ATOM   1833 C  CA    . VAL A 1 276 ? 54.906 1.615   -0.508  1.00 40.28  ? 255 VAL A CA    1 
ATOM   1834 C  C     . VAL A 1 276 ? 54.823 2.720   -1.553  1.00 34.76  ? 255 VAL A C     1 
ATOM   1835 O  O     . VAL A 1 276 ? 53.721 3.089   -1.874  1.00 34.06  ? 255 VAL A O     1 
ATOM   1836 C  CB    . VAL A 1 276 ? 54.539 0.236   -1.103  1.00 44.83  ? 255 VAL A CB    1 
ATOM   1837 C  CG1   . VAL A 1 276 ? 55.361 -0.083  -2.341  1.00 47.50  ? 255 VAL A CG1   1 
ATOM   1838 C  CG2   . VAL A 1 276 ? 54.660 -0.884  -0.081  1.00 43.74  ? 255 VAL A CG2   1 
ATOM   1839 N  N     A ARG A 1 277 ? 55.954 3.243   -2.041  0.50 33.66  ? 256 ARG A N     1 
ATOM   1840 N  N     B ARG A 1 277 ? 55.968 3.144   -2.083  0.50 32.62  ? 256 ARG A N     1 
ATOM   1841 C  CA    A ARG A 1 277 ? 56.000 4.331   -3.062  0.50 34.33  ? 256 ARG A CA    1 
ATOM   1842 C  CA    B ARG A 1 277 ? 56.079 4.257   -3.054  0.50 32.88  ? 256 ARG A CA    1 
ATOM   1843 C  C     A ARG A 1 277 ? 56.612 3.744   -4.342  0.50 33.25  ? 256 ARG A C     1 
ATOM   1844 C  C     B ARG A 1 277 ? 56.617 3.684   -4.367  0.50 32.36  ? 256 ARG A C     1 
ATOM   1845 O  O     A ARG A 1 277 ? 57.510 2.898   -4.240  0.50 35.39  ? 256 ARG A O     1 
ATOM   1846 O  O     B ARG A 1 277 ? 57.473 2.791   -4.318  0.50 34.32  ? 256 ARG A O     1 
ATOM   1847 C  CB    A ARG A 1 277 ? 56.711 5.573   -2.495  0.50 34.76  ? 256 ARG A CB    1 
ATOM   1848 C  CB    B ARG A 1 277 ? 56.922 5.376   -2.434  0.50 32.50  ? 256 ARG A CB    1 
ATOM   1849 C  CG    A ARG A 1 277 ? 57.003 6.712   -3.478  0.50 37.21  ? 256 ARG A CG    1 
ATOM   1850 C  CG    B ARG A 1 277 ? 56.149 6.210   -1.423  0.50 33.20  ? 256 ARG A CG    1 
ATOM   1851 C  CD    A ARG A 1 277 ? 55.837 7.480   -4.109  0.50 34.08  ? 256 ARG A CD    1 
ATOM   1852 C  CD    B ARG A 1 277 ? 56.909 7.400   -0.867  0.50 33.74  ? 256 ARG A CD    1 
ATOM   1853 N  NE    A ARG A 1 277 ? 56.104 8.884   -4.387  0.50 33.87  ? 256 ARG A NE    1 
ATOM   1854 N  NE    B ARG A 1 277 ? 58.199 7.025   -0.324  0.50 34.64  ? 256 ARG A NE    1 
ATOM   1855 C  CZ    A ARG A 1 277 ? 55.172 9.821   -4.580  0.50 35.02  ? 256 ARG A CZ    1 
ATOM   1856 C  CZ    B ARG A 1 277 ? 59.370 7.397   -0.830  0.50 37.16  ? 256 ARG A CZ    1 
ATOM   1857 N  NH1   A ARG A 1 277 ? 53.888 9.510   -4.550  0.50 39.16  ? 256 ARG A NH1   1 
ATOM   1858 N  NH1   B ARG A 1 277 ? 59.415 8.143   -1.916  0.50 39.49  ? 256 ARG A NH1   1 
ATOM   1859 N  NH2   A ARG A 1 277 ? 55.518 11.073  -4.803  0.50 33.00  ? 256 ARG A NH2   1 
ATOM   1860 N  NH2   B ARG A 1 277 ? 60.497 7.018   -0.258  0.50 38.01  ? 256 ARG A NH2   1 
ATOM   1861 N  N     . ALA A 1 278 ? 56.081 4.142   -5.499  1.00 31.21  ? 257 ALA A N     1 
ATOM   1862 C  CA    . ALA A 1 278 ? 56.528 3.723   -6.834  1.00 31.64  ? 257 ALA A CA    1 
ATOM   1863 C  C     . ALA A 1 278 ? 56.370 4.907   -7.782  1.00 32.05  ? 257 ALA A C     1 
ATOM   1864 O  O     . ALA A 1 278 ? 55.731 5.891   -7.369  1.00 36.55  ? 257 ALA A O     1 
ATOM   1865 C  CB    . ALA A 1 278 ? 55.724 2.538   -7.285  1.00 31.53  ? 257 ALA A CB    1 
ATOM   1866 N  N     . ARG A 1 279 ? 56.946 4.797   -8.978  1.00 29.26  ? 258 ARG A N     1 
ATOM   1867 C  CA    . ARG A 1 279 ? 56.757 5.749   -10.089 1.00 35.12  ? 258 ARG A CA    1 
ATOM   1868 C  C     . ARG A 1 279 ? 55.387 5.550   -10.760 1.00 35.73  ? 258 ARG A C     1 
ATOM   1869 O  O     . ARG A 1 279 ? 54.767 6.574   -11.127 1.00 34.04  ? 258 ARG A O     1 
ATOM   1870 C  CB    . ARG A 1 279 ? 57.943 5.607   -11.041 1.00 39.20  ? 258 ARG A CB    1 
ATOM   1871 C  CG    . ARG A 1 279 ? 59.223 6.099   -10.384 1.00 45.34  ? 258 ARG A CG    1 
ATOM   1872 C  CD    . ARG A 1 279 ? 60.457 5.625   -11.084 1.00 50.15  ? 258 ARG A CD    1 
ATOM   1873 N  NE    . ARG A 1 279 ? 60.642 6.356   -12.319 1.00 61.60  ? 258 ARG A NE    1 
ATOM   1874 C  CZ    . ARG A 1 279 ? 61.644 6.130   -13.161 1.00 71.60  ? 258 ARG A CZ    1 
ATOM   1875 N  NH1   . ARG A 1 279 ? 62.537 5.187   -12.880 1.00 68.39  ? 258 ARG A NH1   1 
ATOM   1876 N  NH2   . ARG A 1 279 ? 61.742 6.839   -14.277 1.00 69.36  ? 258 ARG A NH2   1 
ATOM   1877 N  N     . ARG A 1 280 ? 54.953 4.296   -10.937 1.00 32.35  ? 259 ARG A N     1 
ATOM   1878 C  CA    . ARG A 1 280 ? 53.704 3.940   -11.646 1.00 30.88  ? 259 ARG A CA    1 
ATOM   1879 C  C     . ARG A 1 280 ? 53.060 2.722   -10.972 1.00 29.96  ? 259 ARG A C     1 
ATOM   1880 O  O     . ARG A 1 280 ? 53.767 1.889   -10.341 1.00 29.66  ? 259 ARG A O     1 
ATOM   1881 C  CB    . ARG A 1 280 ? 53.975 3.580   -13.108 1.00 32.68  ? 259 ARG A CB    1 
ATOM   1882 C  CG    . ARG A 1 280 ? 54.785 4.597   -13.890 1.00 38.25  ? 259 ARG A CG    1 
ATOM   1883 C  CD    . ARG A 1 280 ? 54.009 5.310   -14.976 1.00 42.26  ? 259 ARG A CD    1 
ATOM   1884 N  NE    . ARG A 1 280 ? 54.569 6.620   -15.268 1.00 45.61  ? 259 ARG A NE    1 
ATOM   1885 C  CZ    . ARG A 1 280 ? 53.907 7.605   -15.856 1.00 47.38  ? 259 ARG A CZ    1 
ATOM   1886 N  NH1   . ARG A 1 280 ? 52.652 7.438   -16.241 1.00 51.52  ? 259 ARG A NH1   1 
ATOM   1887 N  NH2   . ARG A 1 280 ? 54.507 8.763   -16.037 1.00 51.78  ? 259 ARG A NH2   1 
ATOM   1888 N  N     . ALA A 1 281 ? 51.752 2.597   -11.145 1.00 30.85  ? 260 ALA A N     1 
ATOM   1889 C  CA    . ALA A 1 281 ? 50.928 1.527   -10.554 1.00 32.11  ? 260 ALA A CA    1 
ATOM   1890 C  C     . ALA A 1 281 ? 50.230 0.784   -11.689 1.00 33.89  ? 260 ALA A C     1 
ATOM   1891 O  O     . ALA A 1 281 ? 49.846 1.430   -12.677 1.00 34.57  ? 260 ALA A O     1 
ATOM   1892 C  CB    . ALA A 1 281 ? 49.933 2.106   -9.591  1.00 31.72  ? 260 ALA A CB    1 
ATOM   1893 N  N     . ILE A 1 282 ? 50.119 -0.532  -11.554 1.00 31.29  ? 261 ILE A N     1 
ATOM   1894 C  CA    . ILE A 1 282 ? 49.164 -1.345  -12.347 1.00 32.10  ? 261 ILE A CA    1 
ATOM   1895 C  C     . ILE A 1 282 ? 48.156 -1.942  -11.373 1.00 29.58  ? 261 ILE A C     1 
ATOM   1896 O  O     . ILE A 1 282 ? 48.597 -2.617  -10.452 1.00 31.69  ? 261 ILE A O     1 
ATOM   1897 C  CB    . ILE A 1 282 ? 49.892 -2.436  -13.137 1.00 33.03  ? 261 ILE A CB    1 
ATOM   1898 C  CG1   . ILE A 1 282 ? 50.901 -1.834  -14.115 1.00 31.46  ? 261 ILE A CG1   1 
ATOM   1899 C  CG2   . ILE A 1 282 ? 48.878 -3.347  -13.823 1.00 33.84  ? 261 ILE A CG2   1 
ATOM   1900 C  CD1   . ILE A 1 282 ? 51.819 -2.859  -14.760 1.00 33.12  ? 261 ILE A CD1   1 
ATOM   1901 N  N     . VAL A 1 283 ? 46.863 -1.693  -11.586 1.00 29.25  ? 262 VAL A N     1 
ATOM   1902 C  CA    . VAL A 1 283 ? 45.746 -2.284  -10.793 1.00 28.38  ? 262 VAL A CA    1 
ATOM   1903 C  C     . VAL A 1 283 ? 45.164 -3.411  -11.647 1.00 28.00  ? 262 VAL A C     1 
ATOM   1904 O  O     . VAL A 1 283 ? 44.630 -3.105  -12.709 1.00 32.93  ? 262 VAL A O     1 
ATOM   1905 C  CB    . VAL A 1 283 ? 44.682 -1.235  -10.404 1.00 29.11  ? 262 VAL A CB    1 
ATOM   1906 C  CG1   . VAL A 1 283 ? 43.630 -1.812  -9.479  1.00 28.43  ? 262 VAL A CG1   1 
ATOM   1907 C  CG2   . VAL A 1 283 ? 45.306 -0.002  -9.772  1.00 30.55  ? 262 VAL A CG2   1 
ATOM   1908 N  N     . ALA A 1 284 ? 45.313 -4.649  -11.193 1.00 26.12  ? 263 ALA A N     1 
ATOM   1909 C  CA    . ALA A 1 284 ? 44.947 -5.898  -11.891 1.00 28.47  ? 263 ALA A CA    1 
ATOM   1910 C  C     . ALA A 1 284 ? 43.961 -6.681  -11.024 1.00 29.65  ? 263 ALA A C     1 
ATOM   1911 O  O     . ALA A 1 284 ? 44.192 -7.877  -10.804 1.00 29.07  ? 263 ALA A O     1 
ATOM   1912 C  CB    . ALA A 1 284 ? 46.192 -6.711  -12.141 1.00 27.89  ? 263 ALA A CB    1 
ATOM   1913 N  N     . VAL A 1 285 ? 42.946 -5.999  -10.501 1.00 30.54  ? 264 VAL A N     1 
ATOM   1914 C  CA    . VAL A 1 285 ? 41.844 -6.589  -9.689  1.00 32.99  ? 264 VAL A CA    1 
ATOM   1915 C  C     . VAL A 1 285 ? 40.551 -6.512  -10.489 1.00 35.11  ? 264 VAL A C     1 
ATOM   1916 O  O     . VAL A 1 285 ? 40.476 -5.763  -11.468 1.00 32.45  ? 264 VAL A O     1 
ATOM   1917 C  CB    . VAL A 1 285 ? 41.738 -5.893  -8.320  1.00 34.00  ? 264 VAL A CB    1 
ATOM   1918 C  CG1   . VAL A 1 285 ? 43.095 -5.894  -7.634  1.00 35.51  ? 264 VAL A CG1   1 
ATOM   1919 C  CG2   . VAL A 1 285 ? 41.180 -4.474  -8.397  1.00 31.82  ? 264 VAL A CG2   1 
ATOM   1920 N  N     . PRO A 1 286 ? 39.499 -7.281  -10.102 1.00 33.62  ? 265 PRO A N     1 
ATOM   1921 C  CA    . PRO A 1 286 ? 38.189 -7.148  -10.727 1.00 35.00  ? 265 PRO A CA    1 
ATOM   1922 C  C     . PRO A 1 286 ? 37.617 -5.731  -10.556 1.00 33.42  ? 265 PRO A C     1 
ATOM   1923 O  O     . PRO A 1 286 ? 37.839 -5.044  -9.554  1.00 28.41  ? 265 PRO A O     1 
ATOM   1924 C  CB    . PRO A 1 286 ? 37.313 -8.207  -10.042 1.00 36.99  ? 265 PRO A CB    1 
ATOM   1925 C  CG    . PRO A 1 286 ? 38.278 -9.137  -9.338  1.00 36.98  ? 265 PRO A CG    1 
ATOM   1926 C  CD    . PRO A 1 286 ? 39.511 -8.303  -9.052  1.00 36.88  ? 265 PRO A CD    1 
ATOM   1927 N  N     . PRO A 1 287 ? 36.887 -5.242  -11.577 1.00 36.30  ? 266 PRO A N     1 
ATOM   1928 C  CA    . PRO A 1 287 ? 36.371 -3.867  -11.593 1.00 38.09  ? 266 PRO A CA    1 
ATOM   1929 C  C     . PRO A 1 287 ? 35.665 -3.368  -10.321 1.00 37.31  ? 266 PRO A C     1 
ATOM   1930 O  O     . PRO A 1 287 ? 35.956 -2.239  -9.905  1.00 36.38  ? 266 PRO A O     1 
ATOM   1931 C  CB    . PRO A 1 287 ? 35.356 -3.924  -12.743 1.00 39.26  ? 266 PRO A CB    1 
ATOM   1932 C  CG    . PRO A 1 287 ? 35.987 -4.913  -13.704 1.00 41.28  ? 266 PRO A CG    1 
ATOM   1933 C  CD    . PRO A 1 287 ? 36.548 -5.992  -12.800 1.00 36.12  ? 266 PRO A CD    1 
ATOM   1934 N  N     . THR A 1 288 ? 34.781 -4.185  -9.733  1.00 33.63  ? 267 THR A N     1 
ATOM   1935 C  CA    . THR A 1 288 ? 34.083 -3.863  -8.456  1.00 33.34  ? 267 THR A CA    1 
ATOM   1936 C  C     . THR A 1 288 ? 35.103 -3.533  -7.355  1.00 33.47  ? 267 THR A C     1 
ATOM   1937 O  O     . THR A 1 288 ? 34.882 -2.536  -6.643  1.00 36.07  ? 267 THR A O     1 
ATOM   1938 C  CB    . THR A 1 288 ? 33.091 -4.968  -8.071  1.00 36.84  ? 267 THR A CB    1 
ATOM   1939 O  OG1   . THR A 1 288 ? 32.336 -4.469  -6.972  1.00 39.10  ? 267 THR A OG1   1 
ATOM   1940 C  CG2   . THR A 1 288 ? 33.739 -6.286  -7.711  1.00 37.95  ? 267 THR A CG2   1 
ATOM   1941 N  N     . LEU A 1 289 ? 36.229 -4.253  -7.264  1.00 29.46  ? 268 LEU A N     1 
ATOM   1942 C  CA    . LEU A 1 289 ? 37.209 -4.085  -6.157  1.00 29.08  ? 268 LEU A CA    1 
ATOM   1943 C  C     . LEU A 1 289 ? 38.140 -2.884  -6.438  1.00 30.47  ? 268 LEU A C     1 
ATOM   1944 O  O     . LEU A 1 289 ? 38.582 -2.217  -5.499  1.00 29.25  ? 268 LEU A O     1 
ATOM   1945 C  CB    . LEU A 1 289 ? 37.942 -5.421  -5.980  1.00 31.09  ? 268 LEU A CB    1 
ATOM   1946 C  CG    . LEU A 1 289 ? 37.026 -6.613  -5.653  1.00 31.19  ? 268 LEU A CG    1 
ATOM   1947 C  CD1   . LEU A 1 289 ? 37.784 -7.901  -5.409  1.00 32.04  ? 268 LEU A CD1   1 
ATOM   1948 C  CD2   . LEU A 1 289 ? 36.190 -6.322  -4.426  1.00 36.64  ? 268 LEU A CD2   1 
ATOM   1949 N  N     . ALA A 1 290 ? 38.402 -2.578  -7.695  1.00 29.62  ? 269 ALA A N     1 
ATOM   1950 C  CA    . ALA A 1 290 ? 39.238 -1.435  -8.088  1.00 31.83  ? 269 ALA A CA    1 
ATOM   1951 C  C     . ALA A 1 290 ? 38.566 -0.148  -7.599  1.00 32.40  ? 269 ALA A C     1 
ATOM   1952 O  O     . ALA A 1 290 ? 39.287 0.778   -7.193  1.00 32.64  ? 269 ALA A O     1 
ATOM   1953 C  CB    . ALA A 1 290 ? 39.440 -1.460  -9.590  1.00 33.39  ? 269 ALA A CB    1 
ATOM   1954 N  N     . GLY A 1 291 ? 37.234 -0.101  -7.653  1.00 33.38  ? 270 GLY A N     1 
ATOM   1955 C  CA    . GLY A 1 291 ? 36.412 1.053   -7.247  1.00 34.02  ? 270 GLY A CA    1 
ATOM   1956 C  C     . GLY A 1 291 ? 36.399 1.275   -5.735  1.00 34.87  ? 270 GLY A C     1 
ATOM   1957 O  O     . GLY A 1 291 ? 36.168 2.427   -5.328  1.00 38.16  ? 270 GLY A O     1 
ATOM   1958 N  N     . ARG A 1 292 ? 36.683 0.237   -4.943  1.00 32.64  ? 271 ARG A N     1 
ATOM   1959 C  CA    . ARG A 1 292 ? 36.650 0.233   -3.452  1.00 35.15  ? 271 ARG A CA    1 
ATOM   1960 C  C     . ARG A 1 292 ? 37.991 0.690   -2.871  1.00 34.33  ? 271 ARG A C     1 
ATOM   1961 O  O     . ARG A 1 292 ? 38.091 0.863   -1.655  1.00 43.31  ? 271 ARG A O     1 
ATOM   1962 C  CB    . ARG A 1 292 ? 36.349 -1.180  -2.935  1.00 36.92  ? 271 ARG A CB    1 
ATOM   1963 C  CG    . ARG A 1 292 ? 35.085 -1.788  -3.531  1.00 37.80  ? 271 ARG A CG    1 
ATOM   1964 C  CD    . ARG A 1 292 ? 34.611 -3.051  -2.842  1.00 36.92  ? 271 ARG A CD    1 
ATOM   1965 N  NE    . ARG A 1 292 ? 33.596 -3.677  -3.674  1.00 38.76  ? 271 ARG A NE    1 
ATOM   1966 C  CZ    . ARG A 1 292 ? 32.790 -4.660  -3.304  1.00 35.93  ? 271 ARG A CZ    1 
ATOM   1967 N  NH1   . ARG A 1 292 ? 32.848 -5.165  -2.092  1.00 35.85  ? 271 ARG A NH1   1 
ATOM   1968 N  NH2   . ARG A 1 292 ? 31.949 -5.170  -4.180  1.00 43.69  ? 271 ARG A NH2   1 
ATOM   1969 N  N     . ILE A 1 293 ? 39.011 0.814   -3.698  1.00 32.87  ? 272 ILE A N     1 
ATOM   1970 C  CA    . ILE A 1 293 ? 40.305 1.410   -3.277  1.00 31.07  ? 272 ILE A CA    1 
ATOM   1971 C  C     . ILE A 1 293 ? 40.079 2.915   -3.048  1.00 34.25  ? 272 ILE A C     1 
ATOM   1972 O  O     . ILE A 1 293 ? 39.433 3.543   -3.893  1.00 29.00  ? 272 ILE A O     1 
ATOM   1973 C  CB    . ILE A 1 293 ? 41.377 1.135   -4.337  1.00 27.23  ? 272 ILE A CB    1 
ATOM   1974 C  CG1   . ILE A 1 293 ? 41.625 -0.361  -4.513  1.00 27.82  ? 272 ILE A CG1   1 
ATOM   1975 C  CG2   . ILE A 1 293 ? 42.646 1.878   -3.977  1.00 30.58  ? 272 ILE A CG2   1 
ATOM   1976 C  CD1   . ILE A 1 293 ? 42.779 -0.688  -5.427  1.00 28.35  ? 272 ILE A CD1   1 
ATOM   1977 N  N     . ASP A 1 294 ? 40.623 3.458   -1.950  1.00 37.44  ? 273 ASP A N     1 
ATOM   1978 C  CA    . ASP A 1 294 ? 40.619 4.906   -1.629  1.00 36.63  ? 273 ASP A CA    1 
ATOM   1979 C  C     . ASP A 1 294 ? 41.592 5.582   -2.600  1.00 36.18  ? 273 ASP A C     1 
ATOM   1980 O  O     . ASP A 1 294 ? 42.792 5.593   -2.292  1.00 36.16  ? 273 ASP A O     1 
ATOM   1981 C  CB    . ASP A 1 294 ? 40.939 5.117   -0.139  1.00 39.81  ? 273 ASP A CB    1 
ATOM   1982 C  CG    . ASP A 1 294 ? 41.189 6.560   0.322   1.00 41.44  ? 273 ASP A CG    1 
ATOM   1983 O  OD1   . ASP A 1 294 ? 40.701 7.496   -0.340  1.00 44.20  ? 273 ASP A OD1   1 
ATOM   1984 O  OD2   . ASP A 1 294 ? 41.862 6.737   1.367   1.00 47.78  ? 273 ASP A OD2   1 
ATOM   1985 N  N     . HIS A 1 295 ? 41.105 6.099   -3.737  1.00 31.43  ? 274 HIS A N     1 
ATOM   1986 C  CA    . HIS A 1 295 ? 41.934 6.809   -4.745  1.00 31.57  ? 274 HIS A CA    1 
ATOM   1987 C  C     . HIS A 1 295 ? 42.093 8.268   -4.330  1.00 33.51  ? 274 HIS A C     1 
ATOM   1988 O  O     . HIS A 1 295 ? 41.161 8.828   -3.776  1.00 29.56  ? 274 HIS A O     1 
ATOM   1989 C  CB    . HIS A 1 295 ? 41.380 6.674   -6.166  1.00 34.70  ? 274 HIS A CB    1 
ATOM   1990 C  CG    . HIS A 1 295 ? 41.494 5.285   -6.700  1.00 35.35  ? 274 HIS A CG    1 
ATOM   1991 N  ND1   . HIS A 1 295 ? 40.453 4.374   -6.615  1.00 36.21  ? 274 HIS A ND1   1 
ATOM   1992 C  CD2   . HIS A 1 295 ? 42.530 4.628   -7.263  1.00 34.78  ? 274 HIS A CD2   1 
ATOM   1993 C  CE1   . HIS A 1 295 ? 40.824 3.231   -7.150  1.00 35.72  ? 274 HIS A CE1   1 
ATOM   1994 N  NE2   . HIS A 1 295 ? 42.103 3.347   -7.533  1.00 37.99  ? 274 HIS A NE2   1 
ATOM   1995 N  N     . ASP A 1 296 ? 43.261 8.847   -4.595  1.00 37.16  ? 275 ASP A N     1 
ATOM   1996 C  CA    . ASP A 1 296 ? 43.595 10.252  -4.246  1.00 39.08  ? 275 ASP A CA    1 
ATOM   1997 C  C     . ASP A 1 296 ? 44.556 10.766  -5.313  1.00 38.20  ? 275 ASP A C     1 
ATOM   1998 O  O     . ASP A 1 296 ? 45.638 10.213  -5.468  1.00 38.66  ? 275 ASP A O     1 
ATOM   1999 C  CB    . ASP A 1 296 ? 44.198 10.332  -2.841  1.00 41.71  ? 275 ASP A CB    1 
ATOM   2000 C  CG    . ASP A 1 296 ? 44.396 11.755  -2.358  1.00 49.36  ? 275 ASP A CG    1 
ATOM   2001 O  OD1   . ASP A 1 296 ? 43.501 12.576  -2.603  1.00 56.00  ? 275 ASP A OD1   1 
ATOM   2002 O  OD2   . ASP A 1 296 ? 45.443 12.025  -1.726  1.00 61.83  ? 275 ASP A OD2   1 
ATOM   2003 N  N     . PRO A 1 297 ? 44.161 11.736  -6.166  1.00 36.85  ? 276 PRO A N     1 
ATOM   2004 C  CA    . PRO A 1 297 ? 42.795 12.251  -6.200  1.00 39.47  ? 276 PRO A CA    1 
ATOM   2005 C  C     . PRO A 1 297 ? 41.723 11.208  -6.497  1.00 37.27  ? 276 PRO A C     1 
ATOM   2006 O  O     . PRO A 1 297 ? 42.012 10.108  -6.973  1.00 34.54  ? 276 PRO A O     1 
ATOM   2007 C  CB    . PRO A 1 297 ? 42.803 13.245  -7.378  1.00 39.87  ? 276 PRO A CB    1 
ATOM   2008 C  CG    . PRO A 1 297 ? 44.257 13.626  -7.537  1.00 38.30  ? 276 PRO A CG    1 
ATOM   2009 C  CD    . PRO A 1 297 ? 45.013 12.362  -7.183  1.00 38.92  ? 276 PRO A CD    1 
ATOM   2010 N  N     . PRO A 1 298 ? 40.438 11.546  -6.257  1.00 38.17  ? 277 PRO A N     1 
ATOM   2011 C  CA    . PRO A 1 298 ? 39.340 10.660  -6.638  1.00 40.16  ? 277 PRO A CA    1 
ATOM   2012 C  C     . PRO A 1 298 ? 39.454 10.320  -8.134  1.00 41.14  ? 277 PRO A C     1 
ATOM   2013 O  O     . PRO A 1 298 ? 39.871 11.180  -8.878  1.00 38.81  ? 277 PRO A O     1 
ATOM   2014 C  CB    . PRO A 1 298 ? 38.096 11.509  -6.342  1.00 40.45  ? 277 PRO A CB    1 
ATOM   2015 C  CG    . PRO A 1 298 ? 38.548 12.451  -5.265  1.00 39.31  ? 277 PRO A CG    1 
ATOM   2016 C  CD    . PRO A 1 298 ? 39.980 12.782  -5.602  1.00 36.95  ? 277 PRO A CD    1 
ATOM   2017 N  N     . LEU A 1 299 ? 39.117 9.091   -8.532  1.00 37.93  ? 278 LEU A N     1 
ATOM   2018 C  CA    . LEU A 1 299 ? 39.006 8.696   -9.956  1.00 36.65  ? 278 LEU A CA    1 
ATOM   2019 C  C     . LEU A 1 299 ? 38.113 9.706   -10.659 1.00 39.30  ? 278 LEU A C     1 
ATOM   2020 O  O     . LEU A 1 299 ? 37.151 10.190  -10.048 1.00 38.86  ? 278 LEU A O     1 
ATOM   2021 C  CB    . LEU A 1 299 ? 38.355 7.318   -10.094 1.00 34.90  ? 278 LEU A CB    1 
ATOM   2022 C  CG    . LEU A 1 299 ? 39.136 6.108   -9.592  1.00 36.41  ? 278 LEU A CG    1 
ATOM   2023 C  CD1   . LEU A 1 299 ? 38.467 4.844   -10.115 1.00 34.32  ? 278 LEU A CD1   1 
ATOM   2024 C  CD2   . LEU A 1 299 ? 40.610 6.159   -9.982  1.00 35.03  ? 278 LEU A CD2   1 
ATOM   2025 N  N     . PRO A 1 300 ? 38.360 9.976   -11.965 1.00 40.12  ? 279 PRO A N     1 
ATOM   2026 C  CA    . PRO A 1 300 ? 37.437 10.759  -12.789 1.00 40.21  ? 279 PRO A CA    1 
ATOM   2027 C  C     . PRO A 1 300 ? 36.043 10.126  -12.867 1.00 38.87  ? 279 PRO A C     1 
ATOM   2028 O  O     . PRO A 1 300 ? 35.914 8.897   -12.905 1.00 36.95  ? 279 PRO A O     1 
ATOM   2029 C  CB    . PRO A 1 300 ? 38.088 10.774  -14.178 1.00 39.81  ? 279 PRO A CB    1 
ATOM   2030 C  CG    . PRO A 1 300 ? 39.535 10.418  -13.922 1.00 38.12  ? 279 PRO A CG    1 
ATOM   2031 C  CD    . PRO A 1 300 ? 39.510 9.486   -12.737 1.00 38.44  ? 279 PRO A CD    1 
ATOM   2032 N  N     . PRO A 1 301 ? 34.965 10.953  -12.898 1.00 35.61  ? 280 PRO A N     1 
ATOM   2033 C  CA    . PRO A 1 301 ? 33.591 10.454  -12.811 1.00 36.02  ? 280 PRO A CA    1 
ATOM   2034 C  C     . PRO A 1 301 ? 33.215 9.381   -13.838 1.00 33.64  ? 280 PRO A C     1 
ATOM   2035 O  O     . PRO A 1 301 ? 32.423 8.507   -13.489 1.00 35.53  ? 280 PRO A O     1 
ATOM   2036 C  CB    . PRO A 1 301 ? 32.696 11.690  -13.012 1.00 36.04  ? 280 PRO A CB    1 
ATOM   2037 C  CG    . PRO A 1 301 ? 33.626 12.774  -13.522 1.00 37.23  ? 280 PRO A CG    1 
ATOM   2038 C  CD    . PRO A 1 301 ? 35.005 12.421  -12.998 1.00 35.44  ? 280 PRO A CD    1 
ATOM   2039 N  N     . GLN A 1 302 ? 33.727 9.465   -15.066 1.00 31.88  ? 281 GLN A N     1 
ATOM   2040 C  CA    . GLN A 1 302 ? 33.384 8.459   -16.104 1.00 31.45  ? 281 GLN A CA    1 
ATOM   2041 C  C     . GLN A 1 302 ? 33.922 7.085   -15.661 1.00 32.56  ? 281 GLN A C     1 
ATOM   2042 O  O     . GLN A 1 302 ? 33.227 6.040   -15.909 1.00 29.41  ? 281 GLN A O     1 
ATOM   2043 C  CB    . GLN A 1 302 ? 33.928 8.847   -17.474 1.00 30.28  ? 281 GLN A CB    1 
ATOM   2044 C  CG    . GLN A 1 302 ? 33.293 8.038   -18.602 1.00 31.04  ? 281 GLN A CG    1 
ATOM   2045 C  CD    . GLN A 1 302 ? 33.905 8.285   -19.959 1.00 29.59  ? 281 GLN A CD    1 
ATOM   2046 O  OE1   . GLN A 1 302 ? 35.064 8.624   -20.083 1.00 34.29  ? 281 GLN A OE1   1 
ATOM   2047 N  NE2   . GLN A 1 302 ? 33.153 8.034   -21.006 1.00 32.76  ? 281 GLN A NE2   1 
ATOM   2048 N  N     . ARG A 1 303 ? 35.103 7.057   -15.039 1.00 29.95  ? 282 ARG A N     1 
ATOM   2049 C  CA    . ARG A 1 303 ? 35.696 5.755   -14.658 1.00 35.88  ? 282 ARG A CA    1 
ATOM   2050 C  C     . ARG A 1 303 ? 35.028 5.232   -13.380 1.00 31.89  ? 282 ARG A C     1 
ATOM   2051 O  O     . ARG A 1 303 ? 34.674 4.038   -13.344 1.00 30.77  ? 282 ARG A O     1 
ATOM   2052 C  CB    . ARG A 1 303 ? 37.219 5.777   -14.542 1.00 34.72  ? 282 ARG A CB    1 
ATOM   2053 C  CG    . ARG A 1 303 ? 37.725 4.360   -14.333 1.00 36.69  ? 282 ARG A CG    1 
ATOM   2054 C  CD    . ARG A 1 303 ? 39.030 3.928   -14.990 1.00 40.72  ? 282 ARG A CD    1 
ATOM   2055 N  NE    . ARG A 1 303 ? 39.337 2.754   -14.198 1.00 40.90  ? 282 ARG A NE    1 
ATOM   2056 C  CZ    . ARG A 1 303 ? 39.365 1.515   -14.617 1.00 40.81  ? 282 ARG A CZ    1 
ATOM   2057 N  NH1   . ARG A 1 303 ? 39.614 0.569   -13.736 1.00 48.55  ? 282 ARG A NH1   1 
ATOM   2058 N  NH2   . ARG A 1 303 ? 39.216 1.211   -15.891 1.00 42.74  ? 282 ARG A NH2   1 
ATOM   2059 N  N     . ASP A 1 304 ? 34.744 6.078   -12.397 1.00 33.19  ? 283 ASP A N     1 
ATOM   2060 C  CA    . ASP A 1 304 ? 34.027 5.580   -11.193 1.00 31.73  ? 283 ASP A CA    1 
ATOM   2061 C  C     . ASP A 1 304 ? 32.658 4.984   -11.551 1.00 29.18  ? 283 ASP A C     1 
ATOM   2062 O  O     . ASP A 1 304 ? 32.325 3.899   -11.055 1.00 32.22  ? 283 ASP A O     1 
ATOM   2063 C  CB    . ASP A 1 304 ? 33.793 6.647   -10.143 1.00 35.52  ? 283 ASP A CB    1 
ATOM   2064 C  CG    . ASP A 1 304 ? 33.368 5.970   -8.847  1.00 36.62  ? 283 ASP A CG    1 
ATOM   2065 O  OD1   . ASP A 1 304 ? 34.232 5.346   -8.199  1.00 36.70  ? 283 ASP A OD1   1 
ATOM   2066 O  OD2   . ASP A 1 304 ? 32.165 5.984   -8.561  1.00 39.59  ? 283 ASP A OD2   1 
ATOM   2067 N  N     . GLN A 1 305 ? 31.888 5.682   -12.370 1.00 27.08  ? 284 GLN A N     1 
ATOM   2068 C  CA    . GLN A 1 305 ? 30.544 5.241   -12.801 1.00 30.31  ? 284 GLN A CA    1 
ATOM   2069 C  C     . GLN A 1 305 ? 30.643 4.027   -13.735 1.00 29.53  ? 284 GLN A C     1 
ATOM   2070 O  O     . GLN A 1 305 ? 29.692 3.237   -13.696 1.00 27.16  ? 284 GLN A O     1 
ATOM   2071 C  CB    . GLN A 1 305 ? 29.774 6.407   -13.426 1.00 31.83  ? 284 GLN A CB    1 
ATOM   2072 C  CG    . GLN A 1 305 ? 29.499 7.521   -12.420 1.00 31.84  ? 284 GLN A CG    1 
ATOM   2073 C  CD    . GLN A 1 305 ? 28.185 8.204   -12.699 1.00 29.43  ? 284 GLN A CD    1 
ATOM   2074 O  OE1   . GLN A 1 305 ? 27.941 8.691   -13.799 1.00 31.66  ? 284 GLN A OE1   1 
ATOM   2075 N  NE2   . GLN A 1 305 ? 27.334 8.268   -11.693 1.00 30.08  ? 284 GLN A NE2   1 
ATOM   2076 N  N     . LEU A 1 306 ? 31.724 3.867   -14.516 1.00 29.57  ? 285 LEU A N     1 
ATOM   2077 C  CA    . LEU A 1 306 ? 31.920 2.632   -15.327 1.00 31.46  ? 285 LEU A CA    1 
ATOM   2078 C  C     . LEU A 1 306 ? 31.954 1.433   -14.385 1.00 29.22  ? 285 LEU A C     1 
ATOM   2079 O  O     . LEU A 1 306 ? 31.263 0.468   -14.645 1.00 28.00  ? 285 LEU A O     1 
ATOM   2080 C  CB    . LEU A 1 306 ? 33.202 2.673   -16.165 1.00 31.50  ? 285 LEU A CB    1 
ATOM   2081 C  CG    . LEU A 1 306 ? 33.525 1.386   -16.947 1.00 31.80  ? 285 LEU A CG    1 
ATOM   2082 C  CD1   . LEU A 1 306 ? 32.419 1.020   -17.894 1.00 31.37  ? 285 LEU A CD1   1 
ATOM   2083 C  CD2   . LEU A 1 306 ? 34.817 1.506   -17.740 1.00 31.13  ? 285 LEU A CD2   1 
ATOM   2084 N  N     . LEU A 1 307 ? 32.721 1.530   -13.309 1.00 32.17  ? 286 LEU A N     1 
ATOM   2085 C  CA    . LEU A 1 307 ? 32.939 0.408   -12.360 1.00 31.50  ? 286 LEU A CA    1 
ATOM   2086 C  C     . LEU A 1 307 ? 31.611 0.081   -11.666 1.00 32.19  ? 286 LEU A C     1 
ATOM   2087 O  O     . LEU A 1 307 ? 31.321 -1.129  -11.519 1.00 32.92  ? 286 LEU A O     1 
ATOM   2088 C  CB    . LEU A 1 307 ? 34.065 0.762   -11.384 1.00 31.98  ? 286 LEU A CB    1 
ATOM   2089 C  CG    . LEU A 1 307 ? 35.393 1.197   -12.019 1.00 31.72  ? 286 LEU A CG    1 
ATOM   2090 C  CD1   . LEU A 1 307 ? 36.416 1.483   -10.947 1.00 34.20  ? 286 LEU A CD1   1 
ATOM   2091 C  CD2   . LEU A 1 307 ? 35.930 0.141   -12.960 1.00 32.50  ? 286 LEU A CD2   1 
ATOM   2092 N  N     . GLN A 1 308 ? 30.787 1.098   -11.375 1.00 29.63  ? 287 GLN A N     1 
ATOM   2093 C  CA    . GLN A 1 308 ? 29.402 0.932   -10.849 1.00 28.21  ? 287 GLN A CA    1 
ATOM   2094 C  C     . GLN A 1 308 ? 28.548 0.172   -11.884 1.00 29.08  ? 287 GLN A C     1 
ATOM   2095 O  O     . GLN A 1 308 ? 27.514 -0.411  -11.488 1.00 30.05  ? 287 GLN A O     1 
ATOM   2096 C  CB    . GLN A 1 308 ? 28.737 2.282   -10.531 1.00 30.07  ? 287 GLN A CB    1 
ATOM   2097 C  CG    . GLN A 1 308 ? 29.391 3.098   -9.416  1.00 29.67  ? 287 GLN A CG    1 
ATOM   2098 C  CD    . GLN A 1 308 ? 28.646 4.388   -9.122  1.00 32.22  ? 287 GLN A CD    1 
ATOM   2099 O  OE1   . GLN A 1 308 ? 29.220 5.454   -8.857  1.00 31.05  ? 287 GLN A OE1   1 
ATOM   2100 N  NE2   . GLN A 1 308 ? 27.333 4.317   -9.183  1.00 31.70  ? 287 GLN A NE2   1 
ATOM   2101 N  N     . HIS A 1 309 ? 28.901 0.197   -13.172 1.00 28.45  ? 288 HIS A N     1 
ATOM   2102 C  CA    . HIS A 1 309 ? 28.108 -0.467  -14.252 1.00 30.55  ? 288 HIS A CA    1 
ATOM   2103 C  C     . HIS A 1 309 ? 28.822 -1.726  -14.783 1.00 31.37  ? 288 HIS A C     1 
ATOM   2104 O  O     . HIS A 1 309 ? 28.470 -2.128  -15.902 1.00 29.47  ? 288 HIS A O     1 
ATOM   2105 C  CB    . HIS A 1 309 ? 27.818 0.501   -15.406 1.00 27.80  ? 288 HIS A CB    1 
ATOM   2106 C  CG    . HIS A 1 309 ? 26.748 1.514   -15.144 1.00 29.75  ? 288 HIS A CG    1 
ATOM   2107 N  ND1   . HIS A 1 309 ? 27.020 2.788   -14.664 1.00 31.44  ? 288 HIS A ND1   1 
ATOM   2108 C  CD2   . HIS A 1 309 ? 25.417 1.475   -15.336 1.00 29.49  ? 288 HIS A CD2   1 
ATOM   2109 C  CE1   . HIS A 1 309 ? 25.900 3.468   -14.541 1.00 28.12  ? 288 HIS A CE1   1 
ATOM   2110 N  NE2   . HIS A 1 309 ? 24.907 2.690   -14.954 1.00 31.06  ? 288 HIS A NE2   1 
ATOM   2111 N  N     . MET A 1 310 ? 29.749 -2.332  -14.027 1.00 29.86  ? 289 MET A N     1 
ATOM   2112 C  CA    . MET A 1 310 ? 30.495 -3.547  -14.452 1.00 29.75  ? 289 MET A CA    1 
ATOM   2113 C  C     . MET A 1 310 ? 30.413 -4.596  -13.347 1.00 31.47  ? 289 MET A C     1 
ATOM   2114 O  O     . MET A 1 310 ? 31.409 -4.970  -12.743 1.00 31.35  ? 289 MET A O     1 
ATOM   2115 C  CB    . MET A 1 310 ? 31.954 -3.218  -14.742 1.00 31.91  ? 289 MET A CB    1 
ATOM   2116 C  CG    . MET A 1 310 ? 32.165 -2.578  -16.074 1.00 33.99  ? 289 MET A CG    1 
ATOM   2117 S  SD    . MET A 1 310 ? 33.909 -2.296  -16.428 1.00 36.54  ? 289 MET A SD    1 
ATOM   2118 C  CE    . MET A 1 310 ? 34.367 -3.949  -16.953 1.00 33.66  ? 289 MET A CE    1 
ATOM   2119 N  N     . PRO A 1 311 ? 29.197 -5.070  -13.020 1.00 31.20  ? 290 PRO A N     1 
ATOM   2120 C  CA    . PRO A 1 311 ? 29.019 -6.089  -12.001 1.00 33.31  ? 290 PRO A CA    1 
ATOM   2121 C  C     . PRO A 1 311 ? 29.517 -7.485  -12.418 1.00 33.00  ? 290 PRO A C     1 
ATOM   2122 O  O     . PRO A 1 311 ? 29.383 -7.842  -13.550 1.00 32.68  ? 290 PRO A O     1 
ATOM   2123 C  CB    . PRO A 1 311 ? 27.487 -6.086  -11.809 1.00 32.06  ? 290 PRO A CB    1 
ATOM   2124 C  CG    . PRO A 1 311 ? 26.969 -5.714  -13.168 1.00 32.53  ? 290 PRO A CG    1 
ATOM   2125 C  CD    . PRO A 1 311 ? 27.920 -4.614  -13.589 1.00 33.10  ? 290 PRO A CD    1 
ATOM   2126 N  N     . GLN A 1 312 ? 30.068 -8.235  -11.466 1.00 31.14  ? 291 GLN A N     1 
ATOM   2127 C  CA    . GLN A 1 312 ? 30.541 -9.626  -11.662 1.00 32.86  ? 291 GLN A CA    1 
ATOM   2128 C  C     . GLN A 1 312 ? 29.352 -10.572 -11.836 1.00 29.81  ? 291 GLN A C     1 
ATOM   2129 O  O     . GLN A 1 312 ? 28.299 -10.329 -11.245 1.00 30.53  ? 291 GLN A O     1 
ATOM   2130 C  CB    . GLN A 1 312 ? 31.359 -10.111 -10.457 1.00 34.18  ? 291 GLN A CB    1 
ATOM   2131 C  CG    . GLN A 1 312 ? 32.514 -9.208  -10.048 1.00 36.07  ? 291 GLN A CG    1 
ATOM   2132 C  CD    . GLN A 1 312 ? 33.674 -9.292  -11.004 1.00 40.58  ? 291 GLN A CD    1 
ATOM   2133 O  OE1   . GLN A 1 312 ? 34.028 -8.314  -11.661 1.00 46.50  ? 291 GLN A OE1   1 
ATOM   2134 N  NE2   . GLN A 1 312 ? 34.279 -10.469 -11.088 1.00 42.94  ? 291 GLN A NE2   1 
ATOM   2135 N  N     . GLY A 1 313 ? 29.583 -11.704 -12.500 1.00 32.74  ? 292 GLY A N     1 
ATOM   2136 C  CA    . GLY A 1 313 ? 28.582 -12.774 -12.684 1.00 29.16  ? 292 GLY A CA    1 
ATOM   2137 C  C     . GLY A 1 313 ? 28.276 -13.467 -11.383 1.00 26.31  ? 292 GLY A C     1 
ATOM   2138 O  O     . GLY A 1 313 ? 28.921 -13.138 -10.355 1.00 25.63  ? 292 GLY A O     1 
ATOM   2139 N  N     . SER A 1 314 ? 27.371 -14.436 -11.407 1.00 25.82  ? 293 SER A N     1 
ATOM   2140 C  CA    . SER A 1 314 ? 27.037 -15.225 -10.195 1.00 30.26  ? 293 SER A CA    1 
ATOM   2141 C  C     . SER A 1 314 ? 27.192 -16.705 -10.514 1.00 33.08  ? 293 SER A C     1 
ATOM   2142 O  O     . SER A 1 314 ? 26.473 -17.207 -11.437 1.00 31.15  ? 293 SER A O     1 
ATOM   2143 C  CB    . SER A 1 314 ? 25.663 -14.857 -9.659  1.00 33.01  ? 293 SER A CB    1 
ATOM   2144 O  OG    . SER A 1 314 ? 25.543 -13.429 -9.521  1.00 36.14  ? 293 SER A OG    1 
ATOM   2145 N  N     . VAL A 1 315 ? 28.095 -17.378 -9.793  1.00 31.12  ? 294 VAL A N     1 
ATOM   2146 C  CA    . VAL A 1 315 ? 28.417 -18.806 -10.072 1.00 31.66  ? 294 VAL A CA    1 
ATOM   2147 C  C     . VAL A 1 315 ? 28.818 -19.486 -8.767  1.00 31.94  ? 294 VAL A C     1 
ATOM   2148 O  O     . VAL A 1 315 ? 29.554 -18.884 -7.927  1.00 29.66  ? 294 VAL A O     1 
ATOM   2149 C  CB    . VAL A 1 315 ? 29.490 -18.997 -11.167 1.00 34.51  ? 294 VAL A CB    1 
ATOM   2150 C  CG1   . VAL A 1 315 ? 30.840 -18.446 -10.772 1.00 38.12  ? 294 VAL A CG1   1 
ATOM   2151 C  CG2   . VAL A 1 315 ? 29.651 -20.453 -11.548 1.00 38.35  ? 294 VAL A CG2   1 
ATOM   2152 N  N     . VAL A 1 316 ? 28.282 -20.679 -8.604  1.00 27.27  ? 295 VAL A N     1 
ATOM   2153 C  CA    . VAL A 1 316 ? 28.727 -21.660 -7.592  1.00 32.91  ? 295 VAL A CA    1 
ATOM   2154 C  C     . VAL A 1 316 ? 29.205 -22.880 -8.370  1.00 30.64  ? 295 VAL A C     1 
ATOM   2155 O  O     . VAL A 1 316 ? 28.415 -23.428 -9.133  1.00 30.23  ? 295 VAL A O     1 
ATOM   2156 C  CB    . VAL A 1 316 ? 27.587 -22.036 -6.637  1.00 33.28  ? 295 VAL A CB    1 
ATOM   2157 C  CG1   . VAL A 1 316 ? 28.081 -23.000 -5.575  1.00 33.29  ? 295 VAL A CG1   1 
ATOM   2158 C  CG2   . VAL A 1 316 ? 26.932 -20.794 -6.027  1.00 35.42  ? 295 VAL A CG2   1 
ATOM   2159 N  N     . LYS A 1 317 ? 30.476 -23.233 -8.216  1.00 33.96  ? 296 LYS A N     1 
ATOM   2160 C  CA    . LYS A 1 317 ? 31.120 -24.342 -8.966  1.00 30.66  ? 296 LYS A CA    1 
ATOM   2161 C  C     . LYS A 1 317 ? 31.283 -25.487 -7.993  1.00 28.31  ? 296 LYS A C     1 
ATOM   2162 O  O     . LYS A 1 317 ? 31.735 -25.220 -6.868  1.00 27.64  ? 296 LYS A O     1 
ATOM   2163 C  CB    . LYS A 1 317 ? 32.465 -23.923 -9.551  1.00 29.75  ? 296 LYS A CB    1 
ATOM   2164 C  CG    . LYS A 1 317 ? 33.152 -25.034 -10.321 1.00 31.17  ? 296 LYS A CG    1 
ATOM   2165 C  CD    . LYS A 1 317 ? 34.413 -24.642 -11.044 1.00 31.23  ? 296 LYS A CD    1 
ATOM   2166 C  CE    . LYS A 1 317 ? 35.141 -25.884 -11.532 1.00 31.35  ? 296 LYS A CE    1 
ATOM   2167 N  NZ    . LYS A 1 317 ? 36.436 -25.537 -12.159 1.00 30.30  ? 296 LYS A NZ    1 
ATOM   2168 N  N     . PHE A 1 318 ? 30.914 -26.690 -8.417  1.00 27.29  ? 297 PHE A N     1 
ATOM   2169 C  CA    . PHE A 1 318 ? 30.907 -27.893 -7.560  1.00 26.96  ? 297 PHE A CA    1 
ATOM   2170 C  C     . PHE A 1 318 ? 31.597 -29.061 -8.260  1.00 28.25  ? 297 PHE A C     1 
ATOM   2171 O  O     . PHE A 1 318 ? 31.623 -29.148 -9.496  1.00 32.25  ? 297 PHE A O     1 
ATOM   2172 C  CB    . PHE A 1 318 ? 29.483 -28.254 -7.109  1.00 28.81  ? 297 PHE A CB    1 
ATOM   2173 C  CG    . PHE A 1 318 ? 28.520 -28.646 -8.204  1.00 29.73  ? 297 PHE A CG    1 
ATOM   2174 C  CD1   . PHE A 1 318 ? 28.531 -29.927 -8.735  1.00 28.80  ? 297 PHE A CD1   1 
ATOM   2175 C  CD2   . PHE A 1 318 ? 27.557 -27.752 -8.654  1.00 28.37  ? 297 PHE A CD2   1 
ATOM   2176 C  CE1   . PHE A 1 318 ? 27.663 -30.271 -9.756  1.00 28.53  ? 297 PHE A CE1   1 
ATOM   2177 C  CE2   . PHE A 1 318 ? 26.692 -28.099 -9.673  1.00 27.49  ? 297 PHE A CE2   1 
ATOM   2178 C  CZ    . PHE A 1 318 ? 26.738 -29.363 -10.214 1.00 31.40  ? 297 PHE A CZ    1 
ATOM   2179 N  N     . HIS A 1 319 ? 32.141 -29.944 -7.429  1.00 29.68  ? 298 HIS A N     1 
ATOM   2180 C  CA    . HIS A 1 319 ? 32.672 -31.288 -7.766  1.00 31.60  ? 298 HIS A CA    1 
ATOM   2181 C  C     . HIS A 1 319 ? 32.010 -32.304 -6.815  1.00 30.85  ? 298 HIS A C     1 
ATOM   2182 O  O     . HIS A 1 319 ? 32.216 -32.202 -5.579  1.00 31.33  ? 298 HIS A O     1 
ATOM   2183 C  CB    . HIS A 1 319 ? 34.204 -31.315 -7.644  1.00 28.72  ? 298 HIS A CB    1 
ATOM   2184 C  CG    . HIS A 1 319 ? 34.954 -30.403 -8.553  1.00 31.60  ? 298 HIS A CG    1 
ATOM   2185 N  ND1   . HIS A 1 319 ? 35.309 -29.096 -8.176  1.00 36.53  ? 298 HIS A ND1   1 
ATOM   2186 C  CD2   . HIS A 1 319 ? 35.464 -30.589 -9.795  1.00 33.66  ? 298 HIS A CD2   1 
ATOM   2187 C  CE1   . HIS A 1 319 ? 36.010 -28.535 -9.141  1.00 34.08  ? 298 HIS A CE1   1 
ATOM   2188 N  NE2   . HIS A 1 319 ? 36.109 -29.420 -10.156 1.00 38.65  ? 298 HIS A NE2   1 
ATOM   2189 N  N     . VAL A 1 320 ? 31.198 -33.210 -7.365  1.00 32.38  ? 299 VAL A N     1 
ATOM   2190 C  CA    . VAL A 1 320 ? 30.641 -34.397 -6.643  1.00 30.20  ? 299 VAL A CA    1 
ATOM   2191 C  C     . VAL A 1 320 ? 31.642 -35.554 -6.778  1.00 30.64  ? 299 VAL A C     1 
ATOM   2192 O  O     . VAL A 1 320 ? 31.946 -35.933 -7.913  1.00 28.90  ? 299 VAL A O     1 
ATOM   2193 C  CB    . VAL A 1 320 ? 29.275 -34.793 -7.217  1.00 28.22  ? 299 VAL A CB    1 
ATOM   2194 C  CG1   . VAL A 1 320 ? 28.551 -35.774 -6.308  1.00 26.98  ? 299 VAL A CG1   1 
ATOM   2195 C  CG2   . VAL A 1 320 ? 28.425 -33.567 -7.496  1.00 28.77  ? 299 VAL A CG2   1 
ATOM   2196 N  N     . ILE A 1 321 ? 32.118 -36.092 -5.658  1.00 33.33  ? 300 ILE A N     1 
ATOM   2197 C  CA    . ILE A 1 321 ? 33.178 -37.134 -5.589  1.00 31.87  ? 300 ILE A CA    1 
ATOM   2198 C  C     . ILE A 1 321 ? 32.509 -38.496 -5.387  1.00 31.42  ? 300 ILE A C     1 
ATOM   2199 O  O     . ILE A 1 321 ? 31.710 -38.610 -4.491  1.00 32.80  ? 300 ILE A O     1 
ATOM   2200 C  CB    . ILE A 1 321 ? 34.154 -36.826 -4.435  1.00 33.81  ? 300 ILE A CB    1 
ATOM   2201 C  CG1   . ILE A 1 321 ? 34.636 -35.371 -4.449  1.00 32.16  ? 300 ILE A CG1   1 
ATOM   2202 C  CG2   . ILE A 1 321 ? 35.326 -37.808 -4.425  1.00 33.27  ? 300 ILE A CG2   1 
ATOM   2203 C  CD1   . ILE A 1 321 ? 35.156 -34.913 -5.782  1.00 31.70  ? 300 ILE A CD1   1 
ATOM   2204 N  N     . TYR A 1 322 ? 32.863 -39.488 -6.190  1.00 33.79  ? 301 TYR A N     1 
ATOM   2205 C  CA    . TYR A 1 322 ? 32.481 -40.919 -6.033  1.00 33.88  ? 301 TYR A CA    1 
ATOM   2206 C  C     . TYR A 1 322 ? 33.771 -41.743 -6.004  1.00 34.72  ? 301 TYR A C     1 
ATOM   2207 O  O     . TYR A 1 322 ? 34.819 -41.258 -6.474  1.00 31.01  ? 301 TYR A O     1 
ATOM   2208 C  CB    . TYR A 1 322 ? 31.550 -41.353 -7.174  1.00 31.20  ? 301 TYR A CB    1 
ATOM   2209 C  CG    . TYR A 1 322 ? 30.266 -40.572 -7.251  1.00 30.28  ? 301 TYR A CG    1 
ATOM   2210 C  CD1   . TYR A 1 322 ? 29.180 -40.929 -6.480  1.00 32.16  ? 301 TYR A CD1   1 
ATOM   2211 C  CD2   . TYR A 1 322 ? 30.146 -39.434 -8.029  1.00 33.76  ? 301 TYR A CD2   1 
ATOM   2212 C  CE1   . TYR A 1 322 ? 27.990 -40.220 -6.527  1.00 32.49  ? 301 TYR A CE1   1 
ATOM   2213 C  CE2   . TYR A 1 322 ? 28.975 -38.686 -8.065  1.00 35.09  ? 301 TYR A CE2   1 
ATOM   2214 C  CZ    . TYR A 1 322 ? 27.878 -39.089 -7.315  1.00 34.20  ? 301 TYR A CZ    1 
ATOM   2215 O  OH    . TYR A 1 322 ? 26.701 -38.374 -7.311  1.00 29.68  ? 301 TYR A OH    1 
ATOM   2216 N  N     . ASP A 1 323 ? 33.706 -42.969 -5.494  1.00 41.15  ? 302 ASP A N     1 
ATOM   2217 C  CA    . ASP A 1 323 ? 34.879 -43.884 -5.462  1.00 42.67  ? 302 ASP A CA    1 
ATOM   2218 C  C     . ASP A 1 323 ? 35.339 -44.093 -6.912  1.00 41.98  ? 302 ASP A C     1 
ATOM   2219 O  O     . ASP A 1 323 ? 36.531 -43.908 -7.210  1.00 39.58  ? 302 ASP A O     1 
ATOM   2220 C  CB    . ASP A 1 323 ? 34.554 -45.135 -4.641  1.00 47.46  ? 302 ASP A CB    1 
ATOM   2221 C  CG    . ASP A 1 323 ? 34.266 -44.822 -3.171  1.00 57.34  ? 302 ASP A CG    1 
ATOM   2222 O  OD1   . ASP A 1 323 ? 34.873 -43.863 -2.620  1.00 61.90  ? 302 ASP A OD1   1 
ATOM   2223 O  OD2   . ASP A 1 323 ? 33.418 -45.508 -2.578  1.00 56.59  ? 302 ASP A OD2   1 
ATOM   2224 N  N     . GLU A 1 324 ? 34.401 -44.337 -7.812  1.00 44.36  ? 303 GLU A N     1 
ATOM   2225 C  CA    . GLU A 1 324 ? 34.704 -44.675 -9.217  1.00 47.48  ? 303 GLU A CA    1 
ATOM   2226 C  C     . GLU A 1 324 ? 33.801 -43.847 -10.101 1.00 41.15  ? 303 GLU A C     1 
ATOM   2227 O  O     . GLU A 1 324 ? 32.752 -43.396 -9.647  1.00 35.08  ? 303 GLU A O     1 
ATOM   2228 C  CB    . GLU A 1 324 ? 34.432 -46.151 -9.498  1.00 55.71  ? 303 GLU A CB    1 
ATOM   2229 C  CG    . GLU A 1 324 ? 35.329 -47.089 -8.715  1.00 67.90  ? 303 GLU A CG    1 
ATOM   2230 C  CD    . GLU A 1 324 ? 34.949 -48.551 -8.879  1.00 78.89  ? 303 GLU A CD    1 
ATOM   2231 O  OE1   . GLU A 1 324 ? 34.606 -48.942 -10.015 1.00 82.96  ? 303 GLU A OE1   1 
ATOM   2232 O  OE2   . GLU A 1 324 ? 34.976 -49.292 -7.869  1.00 83.59  ? 303 GLU A OE2   1 
ATOM   2233 N  N     . PRO A 1 325 ? 34.192 -43.651 -11.374 1.00 35.48  ? 304 PRO A N     1 
ATOM   2234 C  CA    . PRO A 1 325 ? 33.317 -43.042 -12.362 1.00 39.54  ? 304 PRO A CA    1 
ATOM   2235 C  C     . PRO A 1 325 ? 32.317 -44.085 -12.886 1.00 39.92  ? 304 PRO A C     1 
ATOM   2236 O  O     . PRO A 1 325 ? 32.387 -44.461 -14.025 1.00 39.46  ? 304 PRO A O     1 
ATOM   2237 C  CB    . PRO A 1 325 ? 34.354 -42.526 -13.363 1.00 38.97  ? 304 PRO A CB    1 
ATOM   2238 C  CG    . PRO A 1 325 ? 35.409 -43.605 -13.362 1.00 33.81  ? 304 PRO A CG    1 
ATOM   2239 C  CD    . PRO A 1 325 ? 35.522 -43.961 -11.904 1.00 35.08  ? 304 PRO A CD    1 
ATOM   2240 N  N     . TRP A 1 326 ? 31.368 -44.466 -12.026 1.00 44.61  ? 305 TRP A N     1 
ATOM   2241 C  CA    . TRP A 1 326 ? 30.415 -45.593 -12.218 1.00 41.08  ? 305 TRP A CA    1 
ATOM   2242 C  C     . TRP A 1 326 ? 29.590 -45.362 -13.488 1.00 43.06  ? 305 TRP A C     1 
ATOM   2243 O  O     . TRP A 1 326 ? 29.040 -46.336 -13.992 1.00 49.40  ? 305 TRP A O     1 
ATOM   2244 C  CB    . TRP A 1 326 ? 29.528 -45.793 -10.970 1.00 39.67  ? 305 TRP A CB    1 
ATOM   2245 C  CG    . TRP A 1 326 ? 28.839 -44.540 -10.506 1.00 40.50  ? 305 TRP A CG    1 
ATOM   2246 C  CD1   . TRP A 1 326 ? 29.235 -43.716 -9.494  1.00 39.94  ? 305 TRP A CD1   1 
ATOM   2247 C  CD2   . TRP A 1 326 ? 27.630 -43.955 -11.032 1.00 38.98  ? 305 TRP A CD2   1 
ATOM   2248 N  NE1   . TRP A 1 326 ? 28.370 -42.666 -9.361  1.00 38.93  ? 305 TRP A NE1   1 
ATOM   2249 C  CE2   . TRP A 1 326 ? 27.385 -42.774 -10.297 1.00 35.93  ? 305 TRP A CE2   1 
ATOM   2250 C  CE3   . TRP A 1 326 ? 26.725 -44.314 -12.037 1.00 36.37  ? 305 TRP A CE3   1 
ATOM   2251 C  CZ2   . TRP A 1 326 ? 26.290 -41.955 -10.540 1.00 36.46  ? 305 TRP A CZ2   1 
ATOM   2252 C  CZ3   . TRP A 1 326 ? 25.633 -43.509 -12.278 1.00 36.28  ? 305 TRP A CZ3   1 
ATOM   2253 C  CH2   . TRP A 1 326 ? 25.420 -42.348 -11.535 1.00 38.48  ? 305 TRP A CH2   1 
ATOM   2254 N  N     . TRP A 1 327 ? 29.491 -44.128 -13.988 1.00 41.91  ? 306 TRP A N     1 
ATOM   2255 C  CA    . TRP A 1 327 ? 28.610 -43.801 -15.147 1.00 40.94  ? 306 TRP A CA    1 
ATOM   2256 C  C     . TRP A 1 327 ? 29.192 -44.296 -16.478 1.00 41.29  ? 306 TRP A C     1 
ATOM   2257 O  O     . TRP A 1 327 ? 28.373 -44.618 -17.376 1.00 39.98  ? 306 TRP A O     1 
ATOM   2258 C  CB    . TRP A 1 327 ? 28.322 -42.302 -15.231 1.00 38.57  ? 306 TRP A CB    1 
ATOM   2259 C  CG    . TRP A 1 327 ? 29.537 -41.441 -15.130 1.00 36.00  ? 306 TRP A CG    1 
ATOM   2260 C  CD1   . TRP A 1 327 ? 30.300 -40.985 -16.154 1.00 34.97  ? 306 TRP A CD1   1 
ATOM   2261 C  CD2   . TRP A 1 327 ? 30.129 -40.921 -13.927 1.00 36.66  ? 306 TRP A CD2   1 
ATOM   2262 N  NE1   . TRP A 1 327 ? 31.333 -40.232 -15.671 1.00 34.25  ? 306 TRP A NE1   1 
ATOM   2263 C  CE2   . TRP A 1 327 ? 31.244 -40.149 -14.316 1.00 34.61  ? 306 TRP A CE2   1 
ATOM   2264 C  CE3   . TRP A 1 327 ? 29.810 -41.005 -12.571 1.00 35.25  ? 306 TRP A CE3   1 
ATOM   2265 C  CZ2   . TRP A 1 327 ? 32.046 -39.471 -13.405 1.00 36.81  ? 306 TRP A CZ2   1 
ATOM   2266 C  CZ3   . TRP A 1 327 ? 30.611 -40.346 -11.664 1.00 37.46  ? 306 TRP A CZ3   1 
ATOM   2267 C  CH2   . TRP A 1 327 ? 31.708 -39.583 -12.076 1.00 37.61  ? 306 TRP A CH2   1 
ATOM   2268 N  N     . ARG A 1 328 ? 30.521 -44.268 -16.632 1.00 42.41  ? 307 ARG A N     1 
ATOM   2269 C  CA    . ARG A 1 328 ? 31.255 -44.813 -17.815 1.00 43.03  ? 307 ARG A CA    1 
ATOM   2270 C  C     . ARG A 1 328 ? 30.846 -46.278 -18.033 1.00 42.04  ? 307 ARG A C     1 
ATOM   2271 O  O     . ARG A 1 328 ? 30.514 -46.611 -19.165 1.00 43.37  ? 307 ARG A O     1 
ATOM   2272 C  CB    . ARG A 1 328 ? 32.778 -44.720 -17.620 1.00 44.80  ? 307 ARG A CB    1 
ATOM   2273 C  CG    . ARG A 1 328 ? 33.318 -43.296 -17.544 1.00 41.98  ? 307 ARG A CG    1 
ATOM   2274 C  CD    . ARG A 1 328 ? 34.789 -43.206 -17.166 1.00 41.41  ? 307 ARG A CD    1 
ATOM   2275 N  NE    . ARG A 1 328 ? 35.239 -41.803 -17.095 1.00 43.79  ? 307 ARG A NE    1 
ATOM   2276 C  CZ    . ARG A 1 328 ? 36.510 -41.392 -17.021 1.00 40.91  ? 307 ARG A CZ    1 
ATOM   2277 N  NH1   . ARG A 1 328 ? 37.501 -42.266 -17.027 1.00 40.03  ? 307 ARG A NH1   1 
ATOM   2278 N  NH2   . ARG A 1 328 ? 36.795 -40.105 -16.975 1.00 41.18  ? 307 ARG A NH2   1 
ATOM   2279 N  N     . ALA A 1 329 ? 30.834 -47.111 -16.983 1.00 40.52  ? 308 ALA A N     1 
ATOM   2280 C  CA    . ALA A 1 329 ? 30.411 -48.531 -17.045 1.00 44.07  ? 308 ALA A CA    1 
ATOM   2281 C  C     . ALA A 1 329 ? 29.031 -48.659 -17.709 1.00 47.42  ? 308 ALA A C     1 
ATOM   2282 O  O     . ALA A 1 329 ? 28.748 -49.747 -18.222 1.00 47.31  ? 308 ALA A O     1 
ATOM   2283 C  CB    . ALA A 1 329 ? 30.404 -49.157 -15.672 1.00 46.26  ? 308 ALA A CB    1 
ATOM   2284 N  N     . GLU A 1 330 ? 28.211 -47.603 -17.730 1.00 44.41  ? 309 GLU A N     1 
ATOM   2285 C  CA    . GLU A 1 330 ? 26.872 -47.613 -18.389 1.00 44.62  ? 309 GLU A CA    1 
ATOM   2286 C  C     . GLU A 1 330 ? 26.926 -46.974 -19.793 1.00 37.93  ? 309 GLU A C     1 
ATOM   2287 O  O     . GLU A 1 330 ? 25.868 -46.822 -20.395 1.00 39.34  ? 309 GLU A O     1 
ATOM   2288 C  CB    . GLU A 1 330 ? 25.844 -46.884 -17.512 1.00 50.61  ? 309 GLU A CB    1 
ATOM   2289 C  CG    . GLU A 1 330 ? 25.778 -47.384 -16.077 1.00 57.29  ? 309 GLU A CG    1 
ATOM   2290 C  CD    . GLU A 1 330 ? 24.851 -48.566 -15.843 1.00 64.97  ? 309 GLU A CD    1 
ATOM   2291 O  OE1   . GLU A 1 330 ? 23.704 -48.499 -16.322 1.00 68.20  ? 309 GLU A OE1   1 
ATOM   2292 O  OE2   . GLU A 1 330 ? 25.280 -49.554 -15.184 1.00 66.04  ? 309 GLU A OE2   1 
ATOM   2293 N  N     . GLY A 1 331 ? 28.095 -46.566 -20.290 1.00 34.91  ? 310 GLY A N     1 
ATOM   2294 C  CA    . GLY A 1 331 ? 28.244 -45.862 -21.578 1.00 33.83  ? 310 GLY A CA    1 
ATOM   2295 C  C     . GLY A 1 331 ? 27.798 -44.402 -21.528 1.00 36.53  ? 310 GLY A C     1 
ATOM   2296 O  O     . GLY A 1 331 ? 27.576 -43.810 -22.608 1.00 35.07  ? 310 GLY A O     1 
ATOM   2297 N  N     . LEU A 1 332 ? 27.662 -43.803 -20.344 1.00 36.51  ? 311 LEU A N     1 
ATOM   2298 C  CA    . LEU A 1 332 ? 27.334 -42.351 -20.225 1.00 40.16  ? 311 LEU A CA    1 
ATOM   2299 C  C     . LEU A 1 332 ? 28.633 -41.536 -20.234 1.00 36.75  ? 311 LEU A C     1 
ATOM   2300 O  O     . LEU A 1 332 ? 29.636 -42.033 -19.724 1.00 36.92  ? 311 LEU A O     1 
ATOM   2301 C  CB    . LEU A 1 332 ? 26.509 -42.126 -18.953 1.00 38.95  ? 311 LEU A CB    1 
ATOM   2302 C  CG    . LEU A 1 332 ? 25.224 -42.957 -18.890 1.00 40.69  ? 311 LEU A CG    1 
ATOM   2303 C  CD1   . LEU A 1 332 ? 24.613 -42.934 -17.496 1.00 42.86  ? 311 LEU A CD1   1 
ATOM   2304 C  CD2   . LEU A 1 332 ? 24.216 -42.479 -19.915 1.00 39.63  ? 311 LEU A CD2   1 
ATOM   2305 N  N     . SER A 1 333 ? 28.612 -40.333 -20.804 1.00 36.87  ? 312 SER A N     1 
ATOM   2306 C  CA    . SER A 1 333 ? 29.739 -39.362 -20.759 1.00 36.94  ? 312 SER A CA    1 
ATOM   2307 C  C     . SER A 1 333 ? 29.869 -38.763 -19.349 1.00 41.76  ? 312 SER A C     1 
ATOM   2308 O  O     . SER A 1 333 ? 31.003 -38.403 -18.956 1.00 39.69  ? 312 SER A O     1 
ATOM   2309 C  CB    . SER A 1 333 ? 29.529 -38.295 -21.776 1.00 38.23  ? 312 SER A CB    1 
ATOM   2310 O  OG    . SER A 1 333 ? 28.410 -37.505 -21.406 1.00 38.80  ? 312 SER A OG    1 
ATOM   2311 N  N     . GLY A 1 334 ? 28.742 -38.652 -18.625 1.00 42.49  ? 313 GLY A N     1 
ATOM   2312 C  CA    . GLY A 1 334 ? 28.610 -37.896 -17.366 1.00 40.51  ? 313 GLY A CA    1 
ATOM   2313 C  C     . GLY A 1 334 ? 28.180 -36.460 -17.608 1.00 40.52  ? 313 GLY A C     1 
ATOM   2314 O  O     . GLY A 1 334 ? 28.121 -35.662 -16.637 1.00 38.89  ? 313 GLY A O     1 
ATOM   2315 N  N     . THR A 1 335 ? 27.899 -36.102 -18.856 1.00 43.26  ? 314 THR A N     1 
ATOM   2316 C  CA    . THR A 1 335 ? 27.371 -34.757 -19.205 1.00 45.27  ? 314 THR A CA    1 
ATOM   2317 C  C     . THR A 1 335 ? 25.848 -34.859 -19.261 1.00 44.09  ? 314 THR A C     1 
ATOM   2318 O  O     . THR A 1 335 ? 25.348 -35.766 -19.939 1.00 39.07  ? 314 THR A O     1 
ATOM   2319 C  CB    . THR A 1 335 ? 27.949 -34.199 -20.513 1.00 44.55  ? 314 THR A CB    1 
ATOM   2320 O  OG1   . THR A 1 335 ? 29.231 -33.616 -20.234 1.00 42.02  ? 314 THR A OG1   1 
ATOM   2321 C  CG2   . THR A 1 335 ? 27.021 -33.176 -21.139 1.00 43.82  ? 314 THR A CG2   1 
ATOM   2322 N  N     . VAL A 1 336 ? 25.162 -33.979 -18.530 1.00 45.71  ? 315 VAL A N     1 
ATOM   2323 C  CA    . VAL A 1 336 ? 23.677 -33.846 -18.568 1.00 40.75  ? 315 VAL A CA    1 
ATOM   2324 C  C     . VAL A 1 336 ? 23.365 -32.412 -18.981 1.00 39.87  ? 315 VAL A C     1 
ATOM   2325 O  O     . VAL A 1 336 ? 24.068 -31.501 -18.502 1.00 41.30  ? 315 VAL A O     1 
ATOM   2326 C  CB    . VAL A 1 336 ? 23.002 -34.240 -17.236 1.00 40.49  ? 315 VAL A CB    1 
ATOM   2327 C  CG1   . VAL A 1 336 ? 23.523 -35.578 -16.713 1.00 42.63  ? 315 VAL A CG1   1 
ATOM   2328 C  CG2   . VAL A 1 336 ? 23.108 -33.156 -16.169 1.00 40.01  ? 315 VAL A CG2   1 
ATOM   2329 N  N     . LEU A 1 337 ? 22.374 -32.240 -19.856 1.00 42.43  ? 316 LEU A N     1 
ATOM   2330 C  CA    . LEU A 1 337 ? 21.745 -30.924 -20.140 1.00 47.72  ? 316 LEU A CA    1 
ATOM   2331 C  C     . LEU A 1 337 ? 20.272 -31.002 -19.721 1.00 47.10  ? 316 LEU A C     1 
ATOM   2332 O  O     . LEU A 1 337 ? 19.582 -31.930 -20.178 1.00 45.81  ? 316 LEU A O     1 
ATOM   2333 C  CB    . LEU A 1 337 ? 21.901 -30.566 -21.621 1.00 50.17  ? 316 LEU A CB    1 
ATOM   2334 C  CG    . LEU A 1 337 ? 21.390 -29.175 -22.003 1.00 57.29  ? 316 LEU A CG    1 
ATOM   2335 C  CD1   . LEU A 1 337 ? 22.533 -28.213 -22.327 1.00 57.92  ? 316 LEU A CD1   1 
ATOM   2336 C  CD2   . LEU A 1 337 ? 20.442 -29.267 -23.189 1.00 67.12  ? 316 LEU A CD2   1 
ATOM   2337 N  N     . CYS A 1 338 ? 19.843 -30.074 -18.860 1.00 42.64  ? 317 CYS A N     1 
ATOM   2338 C  CA    . CYS A 1 338 ? 18.523 -30.027 -18.182 1.00 43.65  ? 317 CYS A CA    1 
ATOM   2339 C  C     . CYS A 1 338 ? 18.063 -28.581 -18.158 1.00 43.45  ? 317 CYS A C     1 
ATOM   2340 O  O     . CYS A 1 338 ? 18.330 -27.872 -17.195 1.00 39.48  ? 317 CYS A O     1 
ATOM   2341 C  CB    . CYS A 1 338 ? 18.611 -30.502 -16.739 1.00 45.93  ? 317 CYS A CB    1 
ATOM   2342 S  SG    . CYS A 1 338 ? 19.075 -32.239 -16.556 1.00 56.83  ? 317 CYS A SG    1 
ATOM   2343 N  N     . PRO A 1 339 ? 17.421 -28.075 -19.228 1.00 48.16  ? 318 PRO A N     1 
ATOM   2344 C  CA    . PRO A 1 339 ? 17.181 -26.639 -19.340 1.00 49.79  ? 318 PRO A CA    1 
ATOM   2345 C  C     . PRO A 1 339 ? 16.296 -26.061 -18.227 1.00 46.12  ? 318 PRO A C     1 
ATOM   2346 O  O     . PRO A 1 339 ? 16.308 -24.865 -18.103 1.00 48.96  ? 318 PRO A O     1 
ATOM   2347 C  CB    . PRO A 1 339 ? 16.504 -26.492 -20.717 1.00 49.38  ? 318 PRO A CB    1 
ATOM   2348 C  CG    . PRO A 1 339 ? 16.927 -27.736 -21.474 1.00 49.03  ? 318 PRO A CG    1 
ATOM   2349 C  CD    . PRO A 1 339 ? 16.967 -28.817 -20.415 1.00 49.55  ? 318 PRO A CD    1 
ATOM   2350 N  N     . ASP A 1 340 ? 15.573 -26.902 -17.476 1.00 43.67  ? 319 ASP A N     1 
ATOM   2351 C  CA    . ASP A 1 340 ? 14.520 -26.482 -16.507 1.00 47.58  ? 319 ASP A CA    1 
ATOM   2352 C  C     . ASP A 1 340 ? 14.985 -26.655 -15.062 1.00 47.08  ? 319 ASP A C     1 
ATOM   2353 O  O     . ASP A 1 340 ? 14.201 -26.334 -14.179 1.00 55.42  ? 319 ASP A O     1 
ATOM   2354 C  CB    . ASP A 1 340 ? 13.226 -27.261 -16.747 1.00 47.95  ? 319 ASP A CB    1 
ATOM   2355 C  CG    . ASP A 1 340 ? 12.615 -26.882 -18.087 1.00 57.62  ? 319 ASP A CG    1 
ATOM   2356 O  OD1   . ASP A 1 340 ? 12.403 -25.675 -18.286 1.00 59.23  ? 319 ASP A OD1   1 
ATOM   2357 O  OD2   . ASP A 1 340 ? 12.425 -27.780 -18.951 1.00 66.95  ? 319 ASP A OD2   1 
ATOM   2358 N  N     . GLU A 1 341 ? 16.211 -27.131 -14.839 1.00 44.69  ? 320 GLU A N     1 
ATOM   2359 C  CA    . GLU A 1 341 ? 16.723 -27.502 -13.499 1.00 45.09  ? 320 GLU A CA    1 
ATOM   2360 C  C     . GLU A 1 341 ? 17.624 -26.388 -12.997 1.00 40.05  ? 320 GLU A C     1 
ATOM   2361 O  O     . GLU A 1 341 ? 18.044 -25.554 -13.772 1.00 40.77  ? 320 GLU A O     1 
ATOM   2362 C  CB    . GLU A 1 341 ? 17.472 -28.829 -13.600 1.00 50.12  ? 320 GLU A CB    1 
ATOM   2363 C  CG    . GLU A 1 341 ? 16.559 -29.984 -13.970 1.00 50.94  ? 320 GLU A CG    1 
ATOM   2364 C  CD    . GLU A 1 341 ? 15.550 -30.302 -12.895 1.00 49.35  ? 320 GLU A CD    1 
ATOM   2365 O  OE1   . GLU A 1 341 ? 15.949 -30.219 -11.732 1.00 52.41  ? 320 GLU A OE1   1 
ATOM   2366 O  OE2   . GLU A 1 341 ? 14.373 -30.586 -13.224 1.00 50.29  ? 320 GLU A OE2   1 
ATOM   2367 N  N     . PRO A 1 342 ? 17.975 -26.342 -11.699 1.00 42.24  ? 321 PRO A N     1 
ATOM   2368 C  CA    . PRO A 1 342 ? 18.811 -25.262 -11.178 1.00 41.10  ? 321 PRO A CA    1 
ATOM   2369 C  C     . PRO A 1 342 ? 20.269 -25.319 -11.675 1.00 41.32  ? 321 PRO A C     1 
ATOM   2370 O  O     . PRO A 1 342 ? 20.887 -24.287 -11.769 1.00 39.74  ? 321 PRO A O     1 
ATOM   2371 C  CB    . PRO A 1 342 ? 18.756 -25.421 -9.649  1.00 38.54  ? 321 PRO A CB    1 
ATOM   2372 C  CG    . PRO A 1 342 ? 17.675 -26.474 -9.391  1.00 42.63  ? 321 PRO A CG    1 
ATOM   2373 C  CD    . PRO A 1 342 ? 17.565 -27.297 -10.658 1.00 44.40  ? 321 PRO A CD    1 
ATOM   2374 N  N     . ILE A 1 343 ? 20.805 -26.502 -11.978 1.00 41.00  ? 322 ILE A N     1 
ATOM   2375 C  CA    . ILE A 1 343 ? 22.236 -26.644 -12.389 1.00 41.42  ? 322 ILE A CA    1 
ATOM   2376 C  C     . ILE A 1 343 ? 22.317 -26.554 -13.917 1.00 39.73  ? 322 ILE A C     1 
ATOM   2377 O  O     . ILE A 1 343 ? 21.449 -27.098 -14.566 1.00 36.30  ? 322 ILE A O     1 
ATOM   2378 C  CB    . ILE A 1 343 ? 22.864 -27.943 -11.827 1.00 45.44  ? 322 ILE A CB    1 
ATOM   2379 C  CG1   . ILE A 1 343 ? 22.342 -29.209 -12.508 1.00 45.46  ? 322 ILE A CG1   1 
ATOM   2380 C  CG2   . ILE A 1 343 ? 22.704 -28.025 -10.311 1.00 41.82  ? 322 ILE A CG2   1 
ATOM   2381 C  CD1   . ILE A 1 343 ? 23.061 -30.454 -12.075 1.00 49.00  ? 322 ILE A CD1   1 
ATOM   2382 N  N     . GLY A 1 344 ? 23.320 -25.859 -14.459 1.00 44.65  ? 323 GLY A N     1 
ATOM   2383 C  CA    . GLY A 1 344 ? 23.651 -25.893 -15.893 1.00 42.33  ? 323 GLY A CA    1 
ATOM   2384 C  C     . GLY A 1 344 ? 24.197 -27.250 -16.317 1.00 44.56  ? 323 GLY A C     1 
ATOM   2385 O  O     . GLY A 1 344 ? 23.821 -28.274 -15.720 1.00 44.15  ? 323 GLY A O     1 
ATOM   2386 N  N     . VAL A 1 345 ? 25.087 -27.245 -17.304 1.00 45.84  ? 324 VAL A N     1 
ATOM   2387 C  CA    . VAL A 1 345 ? 25.704 -28.455 -17.922 1.00 45.65  ? 324 VAL A CA    1 
ATOM   2388 C  C     . VAL A 1 345 ? 26.668 -29.086 -16.909 1.00 40.74  ? 324 VAL A C     1 
ATOM   2389 O  O     . VAL A 1 345 ? 27.274 -28.315 -16.161 1.00 47.13  ? 324 VAL A O     1 
ATOM   2390 C  CB    . VAL A 1 345 ? 26.411 -28.033 -19.227 1.00 45.00  ? 324 VAL A CB    1 
ATOM   2391 C  CG1   . VAL A 1 345 ? 27.099 -29.190 -19.928 1.00 48.87  ? 324 VAL A CG1   1 
ATOM   2392 C  CG2   . VAL A 1 345 ? 25.440 -27.363 -20.178 1.00 46.67  ? 324 VAL A CG2   1 
ATOM   2393 N  N     . THR A 1 346 ? 26.776 -30.421 -16.858 1.00 36.93  ? 325 THR A N     1 
ATOM   2394 C  CA    . THR A 1 346 ? 27.812 -31.159 -16.070 1.00 35.24  ? 325 THR A CA    1 
ATOM   2395 C  C     . THR A 1 346 ? 28.899 -31.739 -16.989 1.00 35.29  ? 325 THR A C     1 
ATOM   2396 O  O     . THR A 1 346 ? 28.664 -31.845 -18.192 1.00 35.80  ? 325 THR A O     1 
ATOM   2397 C  CB    . THR A 1 346 ? 27.228 -32.310 -15.248 1.00 34.07  ? 325 THR A CB    1 
ATOM   2398 O  OG1   . THR A 1 346 ? 26.674 -33.251 -16.163 1.00 30.73  ? 325 THR A OG1   1 
ATOM   2399 C  CG2   . THR A 1 346 ? 26.209 -31.826 -14.241 1.00 36.18  ? 325 THR A CG2   1 
ATOM   2400 N  N     . PHE A 1 347 ? 30.048 -32.101 -16.417 1.00 33.84  ? 326 PHE A N     1 
ATOM   2401 C  CA    . PHE A 1 347 ? 31.210 -32.693 -17.117 1.00 32.94  ? 326 PHE A CA    1 
ATOM   2402 C  C     . PHE A 1 347 ? 31.775 -33.837 -16.277 1.00 33.21  ? 326 PHE A C     1 
ATOM   2403 O  O     . PHE A 1 347 ? 31.595 -33.840 -15.077 1.00 34.72  ? 326 PHE A O     1 
ATOM   2404 C  CB    . PHE A 1 347 ? 32.295 -31.642 -17.353 1.00 35.04  ? 326 PHE A CB    1 
ATOM   2405 C  CG    . PHE A 1 347 ? 31.880 -30.505 -18.256 1.00 36.68  ? 326 PHE A CG    1 
ATOM   2406 C  CD1   . PHE A 1 347 ? 31.176 -29.414 -17.756 1.00 35.39  ? 326 PHE A CD1   1 
ATOM   2407 C  CD2   . PHE A 1 347 ? 32.198 -30.516 -19.607 1.00 37.88  ? 326 PHE A CD2   1 
ATOM   2408 C  CE1   . PHE A 1 347 ? 30.781 -28.375 -18.590 1.00 35.64  ? 326 PHE A CE1   1 
ATOM   2409 C  CE2   . PHE A 1 347 ? 31.807 -29.468 -20.436 1.00 40.30  ? 326 PHE A CE2   1 
ATOM   2410 C  CZ    . PHE A 1 347 ? 31.113 -28.390 -19.925 1.00 36.70  ? 326 PHE A CZ    1 
ATOM   2411 N  N     . ASP A 1 348 ? 32.472 -34.771 -16.914 1.00 33.10  ? 327 ASP A N     1 
ATOM   2412 C  CA    . ASP A 1 348 ? 33.301 -35.786 -16.222 1.00 35.41  ? 327 ASP A CA    1 
ATOM   2413 C  C     . ASP A 1 348 ? 34.600 -35.086 -15.817 1.00 35.72  ? 327 ASP A C     1 
ATOM   2414 O  O     . ASP A 1 348 ? 35.350 -34.737 -16.711 1.00 36.89  ? 327 ASP A O     1 
ATOM   2415 C  CB    . ASP A 1 348 ? 33.458 -37.001 -17.135 1.00 38.95  ? 327 ASP A CB    1 
ATOM   2416 C  CG    . ASP A 1 348 ? 34.122 -38.203 -16.509 1.00 41.74  ? 327 ASP A CG    1 
ATOM   2417 O  OD1   . ASP A 1 348 ? 34.918 -38.012 -15.580 1.00 41.33  ? 327 ASP A OD1   1 
ATOM   2418 O  OD2   . ASP A 1 348 ? 33.817 -39.324 -16.972 1.00 43.26  ? 327 ASP A OD2   1 
ATOM   2419 N  N     . GLY A 1 349 ? 34.792 -34.815 -14.518 1.00 34.64  ? 328 GLY A N     1 
ATOM   2420 C  CA    . GLY A 1 349 ? 36.008 -34.202 -13.954 1.00 32.27  ? 328 GLY A CA    1 
ATOM   2421 C  C     . GLY A 1 349 ? 36.957 -35.238 -13.359 1.00 31.74  ? 328 GLY A C     1 
ATOM   2422 O  O     . GLY A 1 349 ? 37.835 -34.861 -12.537 1.00 31.09  ? 328 GLY A O     1 
ATOM   2423 N  N     . THR A 1 350 ? 36.778 -36.514 -13.690 1.00 30.76  ? 329 THR A N     1 
ATOM   2424 C  CA    . THR A 1 350 ? 37.653 -37.608 -13.205 1.00 30.32  ? 329 THR A CA    1 
ATOM   2425 C  C     . THR A 1 350 ? 39.046 -37.354 -13.761 1.00 28.97  ? 329 THR A C     1 
ATOM   2426 O  O     . THR A 1 350 ? 39.166 -37.135 -14.958 1.00 28.24  ? 329 THR A O     1 
ATOM   2427 C  CB    . THR A 1 350 ? 37.144 -38.980 -13.675 1.00 31.88  ? 329 THR A CB    1 
ATOM   2428 O  OG1   . THR A 1 350 ? 35.784 -39.123 -13.253 1.00 31.81  ? 329 THR A OG1   1 
ATOM   2429 C  CG2   . THR A 1 350 ? 37.989 -40.126 -13.148 1.00 32.46  ? 329 THR A CG2   1 
ATOM   2430 N  N     . PRO A 1 351 ? 40.131 -37.392 -12.960 1.00 30.84  ? 330 PRO A N     1 
ATOM   2431 C  CA    . PRO A 1 351 ? 41.485 -37.222 -13.499 1.00 33.75  ? 330 PRO A CA    1 
ATOM   2432 C  C     . PRO A 1 351 ? 42.035 -38.428 -14.267 1.00 34.71  ? 330 PRO A C     1 
ATOM   2433 O  O     . PRO A 1 351 ? 41.409 -39.486 -14.307 1.00 37.65  ? 330 PRO A O     1 
ATOM   2434 C  CB    . PRO A 1 351 ? 42.303 -36.986 -12.222 1.00 32.28  ? 330 PRO A CB    1 
ATOM   2435 C  CG    . PRO A 1 351 ? 41.607 -37.837 -11.205 1.00 31.39  ? 330 PRO A CG    1 
ATOM   2436 C  CD    . PRO A 1 351 ? 40.136 -37.613 -11.505 1.00 33.18  ? 330 PRO A CD    1 
ATOM   2437 N  N     . PRO A 1 352 ? 43.205 -38.302 -14.931 1.00 36.04  ? 331 PRO A N     1 
ATOM   2438 C  CA    . PRO A 1 352 ? 43.702 -39.352 -15.826 1.00 39.35  ? 331 PRO A CA    1 
ATOM   2439 C  C     . PRO A 1 352 ? 43.925 -40.743 -15.212 1.00 37.84  ? 331 PRO A C     1 
ATOM   2440 O  O     . PRO A 1 352 ? 43.747 -41.661 -15.911 1.00 40.45  ? 331 PRO A O     1 
ATOM   2441 C  CB    . PRO A 1 352 ? 45.012 -38.778 -16.390 1.00 39.93  ? 331 PRO A CB    1 
ATOM   2442 C  CG    . PRO A 1 352 ? 44.802 -37.267 -16.301 1.00 38.46  ? 331 PRO A CG    1 
ATOM   2443 C  CD    . PRO A 1 352 ? 44.032 -37.086 -15.001 1.00 40.03  ? 331 PRO A CD    1 
ATOM   2444 N  N     . ALA A 1 353 ? 44.270 -40.846 -13.933 1.00 42.16  ? 332 ALA A N     1 
ATOM   2445 C  CA    . ALA A 1 353 ? 44.420 -42.113 -13.183 1.00 39.98  ? 332 ALA A CA    1 
ATOM   2446 C  C     . ALA A 1 353 ? 43.086 -42.863 -13.127 1.00 44.04  ? 332 ALA A C     1 
ATOM   2447 O  O     . ALA A 1 353 ? 43.112 -44.071 -12.816 1.00 41.94  ? 332 ALA A O     1 
ATOM   2448 C  CB    . ALA A 1 353 ? 44.921 -41.824 -11.788 1.00 42.50  ? 332 ALA A CB    1 
ATOM   2449 N  N     . GLY A 1 354 ? 41.964 -42.166 -13.354 1.00 44.61  ? 333 GLY A N     1 
ATOM   2450 C  CA    . GLY A 1 354 ? 40.621 -42.771 -13.507 1.00 45.70  ? 333 GLY A CA    1 
ATOM   2451 C  C     . GLY A 1 354 ? 39.860 -42.892 -12.188 1.00 44.88  ? 333 GLY A C     1 
ATOM   2452 O  O     . GLY A 1 354 ? 38.746 -43.434 -12.207 1.00 48.55  ? 333 GLY A O     1 
ATOM   2453 N  N     . THR A 1 355 ? 40.432 -42.422 -11.076 1.00 44.65  ? 334 THR A N     1 
ATOM   2454 C  CA    . THR A 1 355 ? 39.765 -42.349 -9.745  1.00 41.25  ? 334 THR A CA    1 
ATOM   2455 C  C     . THR A 1 355 ? 40.349 -41.163 -8.983  1.00 40.75  ? 334 THR A C     1 
ATOM   2456 O  O     . THR A 1 355 ? 41.483 -40.767 -9.235  1.00 39.02  ? 334 THR A O     1 
ATOM   2457 C  CB    . THR A 1 355 ? 39.903 -43.666 -8.978  1.00 42.59  ? 334 THR A CB    1 
ATOM   2458 O  OG1   . THR A 1 355 ? 41.267 -43.773 -8.581  1.00 44.69  ? 334 THR A OG1   1 
ATOM   2459 C  CG2   . THR A 1 355 ? 39.519 -44.878 -9.797  1.00 44.41  ? 334 THR A CG2   1 
ATOM   2460 N  N     . PRO A 1 356 ? 39.576 -40.501 -8.094  1.00 41.35  ? 335 PRO A N     1 
ATOM   2461 C  CA    . PRO A 1 356 ? 38.162 -40.835 -7.852  1.00 38.95  ? 335 PRO A CA    1 
ATOM   2462 C  C     . PRO A 1 356 ? 37.225 -40.475 -9.015  1.00 36.91  ? 335 PRO A C     1 
ATOM   2463 O  O     . PRO A 1 356 ? 37.651 -39.776 -9.912  1.00 37.15  ? 335 PRO A O     1 
ATOM   2464 C  CB    . PRO A 1 356 ? 37.803 -39.951 -6.656  1.00 37.09  ? 335 PRO A CB    1 
ATOM   2465 C  CG    . PRO A 1 356 ? 38.703 -38.741 -6.843  1.00 40.75  ? 335 PRO A CG    1 
ATOM   2466 C  CD    . PRO A 1 356 ? 40.017 -39.341 -7.312  1.00 39.61  ? 335 PRO A CD    1 
ATOM   2467 N  N     . GLY A 1 357 ? 35.977 -40.950 -8.976  1.00 37.11  ? 336 GLY A N     1 
ATOM   2468 C  CA    . GLY A 1 357 ? 34.913 -40.453 -9.867  1.00 36.94  ? 336 GLY A CA    1 
ATOM   2469 C  C     . GLY A 1 357 ? 34.534 -39.030 -9.473  1.00 34.24  ? 336 GLY A C     1 
ATOM   2470 O  O     . GLY A 1 357 ? 34.368 -38.795 -8.259  1.00 32.64  ? 336 GLY A O     1 
ATOM   2471 N  N     . ILE A 1 358 ? 34.474 -38.107 -10.436 1.00 33.72  ? 337 ILE A N     1 
ATOM   2472 C  CA    . ILE A 1 358 ? 34.080 -36.685 -10.189 1.00 29.49  ? 337 ILE A CA    1 
ATOM   2473 C  C     . ILE A 1 358 ? 33.047 -36.270 -11.232 1.00 30.22  ? 337 ILE A C     1 
ATOM   2474 O  O     . ILE A 1 358 ? 33.245 -36.554 -12.430 1.00 30.59  ? 337 ILE A O     1 
ATOM   2475 C  CB    . ILE A 1 358 ? 35.292 -35.738 -10.162 1.00 28.56  ? 337 ILE A CB    1 
ATOM   2476 C  CG1   . ILE A 1 358 ? 36.256 -36.101 -9.029  1.00 29.25  ? 337 ILE A CG1   1 
ATOM   2477 C  CG2   . ILE A 1 358 ? 34.856 -34.267 -10.072 1.00 29.00  ? 337 ILE A CG2   1 
ATOM   2478 C  CD1   . ILE A 1 358 ? 37.554 -35.299 -9.037  1.00 30.88  ? 337 ILE A CD1   1 
ATOM   2479 N  N     . VAL A 1 359 ? 31.974 -35.626 -10.772 1.00 29.99  ? 338 VAL A N     1 
ATOM   2480 C  CA    . VAL A 1 359 ? 31.051 -34.848 -11.639 1.00 29.67  ? 338 VAL A CA    1 
ATOM   2481 C  C     . VAL A 1 359 ? 31.207 -33.357 -11.297 1.00 31.49  ? 338 VAL A C     1 
ATOM   2482 O  O     . VAL A 1 359 ? 30.978 -32.971 -10.129 1.00 30.66  ? 338 VAL A O     1 
ATOM   2483 C  CB    . VAL A 1 359 ? 29.600 -35.330 -11.501 1.00 29.85  ? 338 VAL A CB    1 
ATOM   2484 C  CG1   . VAL A 1 359 ? 28.733 -34.599 -12.518 1.00 33.22  ? 338 VAL A CG1   1 
ATOM   2485 C  CG2   . VAL A 1 359 ? 29.483 -36.842 -11.687 1.00 31.39  ? 338 VAL A CG2   1 
ATOM   2486 N  N     . THR A 1 360 ? 31.570 -32.559 -12.297 1.00 33.02  ? 339 THR A N     1 
ATOM   2487 C  CA    . THR A 1 360 ? 31.776 -31.094 -12.194 1.00 35.62  ? 339 THR A CA    1 
ATOM   2488 C  C     . THR A 1 360 ? 30.566 -30.370 -12.775 1.00 33.67  ? 339 THR A C     1 
ATOM   2489 O  O     . THR A 1 360 ? 30.099 -30.759 -13.874 1.00 37.35  ? 339 THR A O     1 
ATOM   2490 C  CB    . THR A 1 360 ? 33.050 -30.645 -12.926 1.00 36.28  ? 339 THR A CB    1 
ATOM   2491 O  OG1   . THR A 1 360 ? 34.132 -31.393 -12.383 1.00 36.18  ? 339 THR A OG1   1 
ATOM   2492 C  CG2   . THR A 1 360 ? 33.336 -29.162 -12.798 1.00 35.93  ? 339 THR A CG2   1 
ATOM   2493 N  N     . GLY A 1 361 ? 30.115 -29.313 -12.107 1.00 30.58  ? 340 GLY A N     1 
ATOM   2494 C  CA    . GLY A 1 361 ? 29.084 -28.437 -12.683 1.00 29.93  ? 340 GLY A CA    1 
ATOM   2495 C  C     . GLY A 1 361 ? 28.984 -27.120 -11.949 1.00 32.24  ? 340 GLY A C     1 
ATOM   2496 O  O     . GLY A 1 361 ? 29.861 -26.851 -11.114 1.00 31.58  ? 340 GLY A O     1 
ATOM   2497 N  N     . PHE A 1 362 ? 27.920 -26.370 -12.257 1.00 33.50  ? 341 PHE A N     1 
ATOM   2498 C  CA    . PHE A 1 362 ? 27.714 -24.945 -11.920 1.00 34.90  ? 341 PHE A CA    1 
ATOM   2499 C  C     . PHE A 1 362 ? 26.234 -24.658 -11.704 1.00 34.14  ? 341 PHE A C     1 
ATOM   2500 O  O     . PHE A 1 362 ? 25.377 -25.147 -12.460 1.00 34.37  ? 341 PHE A O     1 
ATOM   2501 C  CB    . PHE A 1 362 ? 28.201 -24.033 -13.048 1.00 36.25  ? 341 PHE A CB    1 
ATOM   2502 C  CG    . PHE A 1 362 ? 29.541 -24.418 -13.607 1.00 35.69  ? 341 PHE A CG    1 
ATOM   2503 C  CD1   . PHE A 1 362 ? 29.646 -25.444 -14.543 1.00 37.73  ? 341 PHE A CD1   1 
ATOM   2504 C  CD2   . PHE A 1 362 ? 30.696 -23.796 -13.168 1.00 34.35  ? 341 PHE A CD2   1 
ATOM   2505 C  CE1   . PHE A 1 362 ? 30.880 -25.827 -15.048 1.00 35.33  ? 341 PHE A CE1   1 
ATOM   2506 C  CE2   . PHE A 1 362 ? 31.926 -24.170 -13.688 1.00 35.34  ? 341 PHE A CE2   1 
ATOM   2507 C  CZ    . PHE A 1 362 ? 32.019 -25.186 -14.613 1.00 37.43  ? 341 PHE A CZ    1 
ATOM   2508 N  N     . PHE A 1 363 ? 25.968 -23.885 -10.660 1.00 33.22  ? 342 PHE A N     1 
ATOM   2509 C  CA    . PHE A 1 363 ? 24.785 -23.012 -10.532 1.00 32.36  ? 342 PHE A CA    1 
ATOM   2510 C  C     . PHE A 1 363 ? 25.181 -21.685 -11.176 1.00 31.23  ? 342 PHE A C     1 
ATOM   2511 O  O     . PHE A 1 363 ? 26.269 -21.218 -10.889 1.00 32.52  ? 342 PHE A O     1 
ATOM   2512 C  CB    . PHE A 1 363 ? 24.415 -22.839 -9.059  1.00 34.99  ? 342 PHE A CB    1 
ATOM   2513 C  CG    . PHE A 1 363 ? 24.063 -24.097 -8.296  1.00 32.84  ? 342 PHE A CG    1 
ATOM   2514 C  CD1   . PHE A 1 363 ? 22.743 -24.533 -8.216  1.00 34.61  ? 342 PHE A CD1   1 
ATOM   2515 C  CD2   . PHE A 1 363 ? 25.027 -24.797 -7.590  1.00 32.00  ? 342 PHE A CD2   1 
ATOM   2516 C  CE1   . PHE A 1 363 ? 22.401 -25.650 -7.467  1.00 33.68  ? 342 PHE A CE1   1 
ATOM   2517 C  CE2   . PHE A 1 363 ? 24.697 -25.942 -6.882  1.00 35.33  ? 342 PHE A CE2   1 
ATOM   2518 C  CZ    . PHE A 1 363 ? 23.387 -26.366 -6.820  1.00 36.32  ? 342 PHE A CZ    1 
ATOM   2519 N  N     . GLU A 1 364 ? 24.348 -21.135 -12.044 1.00 32.65  ? 343 GLU A N     1 
ATOM   2520 C  CA    . GLU A 1 364 ? 24.614 -19.900 -12.821 1.00 36.02  ? 343 GLU A CA    1 
ATOM   2521 C  C     . GLU A 1 364 ? 23.527 -18.853 -12.560 1.00 33.88  ? 343 GLU A C     1 
ATOM   2522 O  O     . GLU A 1 364 ? 22.362 -19.226 -12.395 1.00 34.06  ? 343 GLU A O     1 
ATOM   2523 C  CB    . GLU A 1 364 ? 24.596 -20.195 -14.324 1.00 40.85  ? 343 GLU A CB    1 
ATOM   2524 C  CG    . GLU A 1 364 ? 25.528 -21.312 -14.766 1.00 47.35  ? 343 GLU A CG    1 
ATOM   2525 C  CD    . GLU A 1 364 ? 27.007 -20.969 -14.748 1.00 53.13  ? 343 GLU A CD    1 
ATOM   2526 O  OE1   . GLU A 1 364 ? 27.378 -19.902 -14.188 1.00 55.72  ? 343 GLU A OE1   1 
ATOM   2527 O  OE2   . GLU A 1 364 ? 27.790 -21.760 -15.302 1.00 56.56  ? 343 GLU A OE2   1 
ATOM   2528 N  N     . GLY A 1 365 ? 23.894 -17.576 -12.614 1.00 34.45  ? 344 GLY A N     1 
ATOM   2529 C  CA    . GLY A 1 365 ? 22.950 -16.448 -12.517 1.00 32.80  ? 344 GLY A CA    1 
ATOM   2530 C  C     . GLY A 1 365 ? 22.028 -16.589 -11.305 1.00 33.16  ? 344 GLY A C     1 
ATOM   2531 O  O     . GLY A 1 365 ? 22.505 -16.813 -10.178 1.00 31.25  ? 344 GLY A O     1 
ATOM   2532 N  N     . PRO A 1 366 ? 20.691 -16.453 -11.515 1.00 31.77  ? 345 PRO A N     1 
ATOM   2533 C  CA    . PRO A 1 366 ? 19.702 -16.504 -10.436 1.00 31.89  ? 345 PRO A CA    1 
ATOM   2534 C  C     . PRO A 1 366 ? 19.787 -17.756 -9.548  1.00 32.00  ? 345 PRO A C     1 
ATOM   2535 O  O     . PRO A 1 366 ? 19.651 -17.622 -8.368  1.00 34.89  ? 345 PRO A O     1 
ATOM   2536 C  CB    . PRO A 1 366 ? 18.344 -16.510 -11.164 1.00 34.51  ? 345 PRO A CB    1 
ATOM   2537 C  CG    . PRO A 1 366 ? 18.613 -15.880 -12.510 1.00 35.00  ? 345 PRO A CG    1 
ATOM   2538 C  CD    . PRO A 1 366 ? 20.061 -16.217 -12.826 1.00 35.03  ? 345 PRO A CD    1 
ATOM   2539 N  N     . ALA A 1 367 ? 19.987 -18.941 -10.129 1.00 31.94  ? 346 ALA A N     1 
ATOM   2540 C  CA    . ALA A 1 367 ? 20.069 -20.196 -9.364  1.00 32.62  ? 346 ALA A CA    1 
ATOM   2541 C  C     . ALA A 1 367 ? 21.338 -20.164 -8.494  1.00 32.28  ? 346 ALA A C     1 
ATOM   2542 O  O     . ALA A 1 367 ? 21.321 -20.793 -7.426  1.00 32.14  ? 346 ALA A O     1 
ATOM   2543 C  CB    . ALA A 1 367 ? 20.047 -21.382 -10.312 1.00 33.65  ? 346 ALA A CB    1 
ATOM   2544 N  N     . ALA A 1 368 ? 22.401 -19.456 -8.901  1.00 31.86  ? 347 ALA A N     1 
ATOM   2545 C  CA    . ALA A 1 368 ? 23.645 -19.350 -8.085  1.00 30.19  ? 347 ALA A CA    1 
ATOM   2546 C  C     . ALA A 1 368 ? 23.390 -18.468 -6.867  1.00 29.16  ? 347 ALA A C     1 
ATOM   2547 O  O     . ALA A 1 368 ? 23.895 -18.790 -5.775  1.00 27.88  ? 347 ALA A O     1 
ATOM   2548 C  CB    . ALA A 1 368 ? 24.809 -18.816 -8.871  1.00 30.61  ? 347 ALA A CB    1 
ATOM   2549 N  N     . VAL A 1 369 ? 22.645 -17.378 -7.041  1.00 28.51  ? 348 VAL A N     1 
ATOM   2550 C  CA    . VAL A 1 369 ? 22.274 -16.487 -5.915  1.00 26.78  ? 348 VAL A CA    1 
ATOM   2551 C  C     . VAL A 1 369 ? 21.349 -17.249 -4.963  1.00 28.81  ? 348 VAL A C     1 
ATOM   2552 O  O     . VAL A 1 369 ? 21.607 -17.196 -3.775  1.00 29.84  ? 348 VAL A O     1 
ATOM   2553 C  CB    . VAL A 1 369 ? 21.616 -15.189 -6.404  1.00 30.28  ? 348 VAL A CB    1 
ATOM   2554 C  CG1   . VAL A 1 369 ? 21.174 -14.355 -5.217  1.00 29.97  ? 348 VAL A CG1   1 
ATOM   2555 C  CG2   . VAL A 1 369 ? 22.532 -14.393 -7.330  1.00 27.92  ? 348 VAL A CG2   1 
ATOM   2556 N  N     . ALA A 1 370 ? 20.310 -17.944 -5.439  1.00 31.51  ? 349 ALA A N     1 
ATOM   2557 C  CA    . ALA A 1 370 ? 19.436 -18.764 -4.550  1.00 32.79  ? 349 ALA A CA    1 
ATOM   2558 C  C     . ALA A 1 370 ? 20.268 -19.855 -3.846  1.00 34.96  ? 349 ALA A C     1 
ATOM   2559 O  O     . ALA A 1 370 ? 19.975 -20.168 -2.689  1.00 30.83  ? 349 ALA A O     1 
ATOM   2560 C  CB    . ALA A 1 370 ? 18.271 -19.370 -5.308  1.00 31.95  ? 349 ALA A CB    1 
ATOM   2561 N  N     . ALA A 1 371 ? 21.268 -20.452 -4.491  1.00 34.20  ? 350 ALA A N     1 
ATOM   2562 C  CA    . ALA A 1 371 ? 21.985 -21.596 -3.868  1.00 35.17  ? 350 ALA A CA    1 
ATOM   2563 C  C     . ALA A 1 371 ? 23.019 -21.080 -2.857  1.00 35.38  ? 350 ALA A C     1 
ATOM   2564 O  O     . ALA A 1 371 ? 23.261 -21.772 -1.845  1.00 29.87  ? 350 ALA A O     1 
ATOM   2565 C  CB    . ALA A 1 371 ? 22.616 -22.468 -4.910  1.00 34.97  ? 350 ALA A CB    1 
ATOM   2566 N  N     . GLY A 1 372 ? 23.577 -19.887 -3.115  1.00 38.09  ? 351 GLY A N     1 
ATOM   2567 C  CA    . GLY A 1 372 ? 24.556 -19.218 -2.247  1.00 32.31  ? 351 GLY A CA    1 
ATOM   2568 C  C     . GLY A 1 372 ? 23.954 -18.917 -0.886  1.00 35.63  ? 351 GLY A C     1 
ATOM   2569 O  O     . GLY A 1 372 ? 24.731 -18.836 0.113   1.00 31.58  ? 351 GLY A O     1 
ATOM   2570 N  N     . ALA A 1 373 ? 22.629 -18.738 -0.836  1.00 35.23  ? 352 ALA A N     1 
ATOM   2571 C  CA    . ALA A 1 373 ? 21.893 -18.328 0.387   1.00 39.23  ? 352 ALA A CA    1 
ATOM   2572 C  C     . ALA A 1 373 ? 21.625 -19.557 1.264   1.00 34.93  ? 352 ALA A C     1 
ATOM   2573 O  O     . ALA A 1 373 ? 21.302 -19.364 2.442   1.00 38.07  ? 352 ALA A O     1 
ATOM   2574 C  CB    . ALA A 1 373 ? 20.618 -17.577 0.034   1.00 35.75  ? 352 ALA A CB    1 
ATOM   2575 N  N     . ARG A 1 374 ? 21.795 -20.758 0.710   1.00 33.87  ? 353 ARG A N     1 
ATOM   2576 C  CA    . ARG A 1 374 ? 21.517 -22.068 1.367   1.00 34.44  ? 353 ARG A CA    1 
ATOM   2577 C  C     . ARG A 1 374 ? 22.835 -22.645 1.906   1.00 34.97  ? 353 ARG A C     1 
ATOM   2578 O  O     . ARG A 1 374 ? 23.863 -22.027 1.675   1.00 34.62  ? 353 ARG A O     1 
ATOM   2579 C  CB    . ARG A 1 374 ? 20.801 -22.961 0.342   1.00 36.70  ? 353 ARG A CB    1 
ATOM   2580 C  CG    . ARG A 1 374 ? 19.466 -22.377 -0.117  1.00 40.74  ? 353 ARG A CG    1 
ATOM   2581 C  CD    . ARG A 1 374 ? 18.695 -23.190 -1.147  1.00 43.33  ? 353 ARG A CD    1 
ATOM   2582 N  NE    . ARG A 1 374 ? 17.981 -24.258 -0.478  1.00 52.45  ? 353 ARG A NE    1 
ATOM   2583 C  CZ    . ARG A 1 374 ? 17.576 -25.404 -1.027  1.00 55.75  ? 353 ARG A CZ    1 
ATOM   2584 N  NH1   . ARG A 1 374 ? 17.773 -25.657 -2.313  1.00 56.04  ? 353 ARG A NH1   1 
ATOM   2585 N  NH2   . ARG A 1 374 ? 16.986 -26.304 -0.254  1.00 52.08  ? 353 ARG A NH2   1 
ATOM   2586 N  N     . THR A 1 375 ? 22.816 -23.795 2.590   1.00 35.33  ? 354 THR A N     1 
ATOM   2587 C  CA    . THR A 1 375 ? 24.019 -24.461 3.156   1.00 31.93  ? 354 THR A CA    1 
ATOM   2588 C  C     . THR A 1 375 ? 24.655 -25.395 2.121   1.00 34.83  ? 354 THR A C     1 
ATOM   2589 O  O     . THR A 1 375 ? 23.972 -25.764 1.144   1.00 35.85  ? 354 THR A O     1 
ATOM   2590 C  CB    . THR A 1 375 ? 23.674 -25.310 4.384   1.00 34.72  ? 354 THR A CB    1 
ATOM   2591 O  OG1   . THR A 1 375 ? 22.853 -26.406 3.945   1.00 31.75  ? 354 THR A OG1   1 
ATOM   2592 C  CG2   . THR A 1 375 ? 22.998 -24.502 5.476   1.00 33.09  ? 354 THR A CG2   1 
ATOM   2593 N  N     . ARG A 1 376 ? 25.884 -25.838 2.405   1.00 33.04  ? 355 ARG A N     1 
ATOM   2594 C  CA    . ARG A 1 376 ? 26.627 -26.859 1.631   1.00 34.11  ? 355 ARG A CA    1 
ATOM   2595 C  C     . ARG A 1 376 ? 25.743 -28.102 1.469   1.00 31.72  ? 355 ARG A C     1 
ATOM   2596 O  O     . ARG A 1 376 ? 25.650 -28.599 0.316   1.00 31.57  ? 355 ARG A O     1 
ATOM   2597 C  CB    . ARG A 1 376 ? 27.971 -27.201 2.288   1.00 34.07  ? 355 ARG A CB    1 
ATOM   2598 C  CG    . ARG A 1 376 ? 28.897 -27.976 1.360   1.00 35.94  ? 355 ARG A CG    1 
ATOM   2599 C  CD    . ARG A 1 376 ? 29.989 -28.761 2.070   1.00 38.43  ? 355 ARG A CD    1 
ATOM   2600 N  NE    . ARG A 1 376 ? 29.451 -29.819 2.931   1.00 38.55  ? 355 ARG A NE    1 
ATOM   2601 C  CZ    . ARG A 1 376 ? 29.386 -31.119 2.625   1.00 39.72  ? 355 ARG A CZ    1 
ATOM   2602 N  NH1   . ARG A 1 376 ? 29.795 -31.586 1.453   1.00 37.93  ? 355 ARG A NH1   1 
ATOM   2603 N  NH2   . ARG A 1 376 ? 28.881 -31.955 3.507   1.00 36.66  ? 355 ARG A NH2   1 
ATOM   2604 N  N     . GLU A 1 377 ? 25.063 -28.540 2.530   1.00 33.12  ? 356 GLU A N     1 
ATOM   2605 C  CA    . GLU A 1 377 ? 24.229 -29.789 2.502   1.00 38.86  ? 356 GLU A CA    1 
ATOM   2606 C  C     . GLU A 1 377 ? 22.984 -29.614 1.618   1.00 37.86  ? 356 GLU A C     1 
ATOM   2607 O  O     . GLU A 1 377 ? 22.645 -30.565 0.905   1.00 35.54  ? 356 GLU A O     1 
ATOM   2608 C  CB    . GLU A 1 377 ? 23.766 -30.236 3.890   1.00 37.24  ? 356 GLU A CB    1 
ATOM   2609 C  CG    . GLU A 1 377 ? 24.892 -30.817 4.729   1.00 39.20  ? 356 GLU A CG    1 
ATOM   2610 C  CD    . GLU A 1 377 ? 25.816 -29.765 5.310   1.00 40.77  ? 356 GLU A CD    1 
ATOM   2611 O  OE1   . GLU A 1 377 ? 25.447 -28.562 5.270   1.00 39.32  ? 356 GLU A OE1   1 
ATOM   2612 O  OE2   . GLU A 1 377 ? 26.902 -30.141 5.802   1.00 47.54  ? 356 GLU A OE2   1 
ATOM   2613 N  N     . GLU A 1 378 ? 22.302 -28.469 1.699   1.00 38.12  ? 357 GLU A N     1 
ATOM   2614 C  CA    . GLU A 1 378 ? 21.154 -28.162 0.812   1.00 35.95  ? 357 GLU A CA    1 
ATOM   2615 C  C     . GLU A 1 378 ? 21.641 -28.174 -0.645  1.00 35.21  ? 357 GLU A C     1 
ATOM   2616 O  O     . GLU A 1 378 ? 20.936 -28.761 -1.460  1.00 32.69  ? 357 GLU A O     1 
ATOM   2617 C  CB    . GLU A 1 378 ? 20.488 -26.835 1.171   1.00 35.46  ? 357 GLU A CB    1 
ATOM   2618 C  CG    . GLU A 1 378 ? 19.597 -26.888 2.406   1.00 39.77  ? 357 GLU A CG    1 
ATOM   2619 C  CD    . GLU A 1 378 ? 19.190 -25.509 2.928   1.00 43.27  ? 357 GLU A CD    1 
ATOM   2620 O  OE1   . GLU A 1 378 ? 20.078 -24.690 3.185   1.00 42.78  ? 357 GLU A OE1   1 
ATOM   2621 O  OE2   . GLU A 1 378 ? 17.986 -25.245 3.072   1.00 52.68  ? 357 GLU A OE2   1 
ATOM   2622 N  N     . ARG A 1 379 ? 22.790 -27.562 -0.973  1.00 33.57  ? 358 ARG A N     1 
ATOM   2623 C  CA    . ARG A 1 379 ? 23.268 -27.500 -2.384  1.00 33.74  ? 358 ARG A CA    1 
ATOM   2624 C  C     . ARG A 1 379 ? 23.556 -28.932 -2.857  1.00 32.78  ? 358 ARG A C     1 
ATOM   2625 O  O     . ARG A 1 379 ? 23.164 -29.272 -3.991  1.00 34.42  ? 358 ARG A O     1 
ATOM   2626 C  CB    . ARG A 1 379 ? 24.472 -26.555 -2.543  1.00 33.59  ? 358 ARG A CB    1 
ATOM   2627 C  CG    . ARG A 1 379 ? 24.131 -25.090 -2.265  1.00 37.76  ? 358 ARG A CG    1 
ATOM   2628 C  CD    . ARG A 1 379 ? 25.098 -24.103 -2.901  1.00 35.74  ? 358 ARG A CD    1 
ATOM   2629 N  NE    . ARG A 1 379 ? 26.360 -24.122 -2.190  1.00 33.64  ? 358 ARG A NE    1 
ATOM   2630 C  CZ    . ARG A 1 379 ? 26.565 -23.569 -1.004  1.00 30.89  ? 358 ARG A CZ    1 
ATOM   2631 N  NH1   . ARG A 1 379 ? 25.594 -22.920 -0.393  1.00 31.89  ? 358 ARG A NH1   1 
ATOM   2632 N  NH2   . ARG A 1 379 ? 27.747 -23.657 -0.429  1.00 31.13  ? 358 ARG A NH2   1 
ATOM   2633 N  N     . ARG A 1 380 ? 24.208 -29.733 -2.017  1.00 33.66  ? 359 ARG A N     1 
ATOM   2634 C  CA    . ARG A 1 380 ? 24.570 -31.148 -2.305  1.00 34.33  ? 359 ARG A CA    1 
ATOM   2635 C  C     . ARG A 1 380 ? 23.302 -31.931 -2.680  1.00 36.59  ? 359 ARG A C     1 
ATOM   2636 O  O     . ARG A 1 380 ? 23.306 -32.582 -3.742  1.00 33.50  ? 359 ARG A O     1 
ATOM   2637 C  CB    . ARG A 1 380 ? 25.272 -31.764 -1.099  1.00 32.80  ? 359 ARG A CB    1 
ATOM   2638 C  CG    . ARG A 1 380 ? 25.527 -33.262 -1.218  1.00 32.96  ? 359 ARG A CG    1 
ATOM   2639 C  CD    . ARG A 1 380 ? 25.659 -33.839 0.178   1.00 32.58  ? 359 ARG A CD    1 
ATOM   2640 N  NE    . ARG A 1 380 ? 24.393 -33.741 0.898   1.00 30.95  ? 359 ARG A NE    1 
ATOM   2641 C  CZ    . ARG A 1 380 ? 24.267 -33.898 2.195   1.00 33.36  ? 359 ARG A CZ    1 
ATOM   2642 N  NH1   . ARG A 1 380 ? 25.336 -34.103 2.948   1.00 32.66  ? 359 ARG A NH1   1 
ATOM   2643 N  NH2   . ARG A 1 380 ? 23.069 -33.839 2.737   1.00 36.34  ? 359 ARG A NH2   1 
ATOM   2644 N  N     . ASP A 1 381 ? 22.245 -31.799 -1.877  1.00 37.47  ? 360 ASP A N     1 
ATOM   2645 C  CA    . ASP A 1 381 ? 20.932 -32.476 -2.068  1.00 36.89  ? 360 ASP A CA    1 
ATOM   2646 C  C     . ASP A 1 381 ? 20.356 -32.102 -3.436  1.00 36.51  ? 360 ASP A C     1 
ATOM   2647 O  O     . ASP A 1 381 ? 19.999 -33.030 -4.158  1.00 33.51  ? 360 ASP A O     1 
ATOM   2648 C  CB    . ASP A 1 381 ? 20.016 -32.162 -0.895  1.00 36.90  ? 360 ASP A CB    1 
ATOM   2649 C  CG    . ASP A 1 381 ? 20.522 -32.761 0.419   1.00 41.55  ? 360 ASP A CG    1 
ATOM   2650 O  OD1   . ASP A 1 381 ? 21.549 -33.480 0.406   1.00 43.37  ? 360 ASP A OD1   1 
ATOM   2651 O  OD2   . ASP A 1 381 ? 19.893 -32.517 1.450   1.00 47.59  ? 360 ASP A OD2   1 
ATOM   2652 N  N     . VAL A 1 382 ? 20.370 -30.824 -3.828  1.00 32.70  ? 361 VAL A N     1 
ATOM   2653 C  CA    . VAL A 1 382 ? 19.811 -30.362 -5.139  1.00 36.32  ? 361 VAL A CA    1 
ATOM   2654 C  C     . VAL A 1 382 ? 20.593 -31.004 -6.308  1.00 37.39  ? 361 VAL A C     1 
ATOM   2655 O  O     . VAL A 1 382 ? 19.964 -31.482 -7.263  1.00 34.76  ? 361 VAL A O     1 
ATOM   2656 C  CB    . VAL A 1 382 ? 19.822 -28.830 -5.265  1.00 38.65  ? 361 VAL A CB    1 
ATOM   2657 C  CG1   . VAL A 1 382 ? 19.415 -28.394 -6.655  1.00 42.04  ? 361 VAL A CG1   1 
ATOM   2658 C  CG2   . VAL A 1 382 ? 18.920 -28.165 -4.243  1.00 44.35  ? 361 VAL A CG2   1 
ATOM   2659 N  N     . VAL A 1 383 ? 21.926 -30.987 -6.255  1.00 34.42  ? 362 VAL A N     1 
ATOM   2660 C  CA    . VAL A 1 383 ? 22.806 -31.563 -7.315  1.00 33.47  ? 362 VAL A CA    1 
ATOM   2661 C  C     . VAL A 1 383 ? 22.566 -33.079 -7.417  1.00 30.67  ? 362 VAL A C     1 
ATOM   2662 O  O     . VAL A 1 383 ? 22.385 -33.579 -8.524  1.00 26.57  ? 362 VAL A O     1 
ATOM   2663 C  CB    . VAL A 1 383 ? 24.286 -31.257 -7.016  1.00 34.21  ? 362 VAL A CB    1 
ATOM   2664 C  CG1   . VAL A 1 383 ? 25.218 -32.054 -7.912  1.00 33.23  ? 362 VAL A CG1   1 
ATOM   2665 C  CG2   . VAL A 1 383 ? 24.589 -29.770 -7.111  1.00 34.36  ? 362 VAL A CG2   1 
ATOM   2666 N  N     . VAL A 1 384 ? 22.598 -33.792 -6.295  1.00 29.85  ? 363 VAL A N     1 
ATOM   2667 C  CA    . VAL A 1 384 ? 22.480 -35.274 -6.281  1.00 34.77  ? 363 VAL A CA    1 
ATOM   2668 C  C     . VAL A 1 384 ? 21.101 -35.671 -6.823  1.00 36.09  ? 363 VAL A C     1 
ATOM   2669 O  O     . VAL A 1 384 ? 20.996 -36.738 -7.471  1.00 38.40  ? 363 VAL A O     1 
ATOM   2670 C  CB    . VAL A 1 384 ? 22.759 -35.821 -4.873  1.00 36.88  ? 363 VAL A CB    1 
ATOM   2671 C  CG1   . VAL A 1 384 ? 22.087 -37.156 -4.634  1.00 36.03  ? 363 VAL A CG1   1 
ATOM   2672 C  CG2   . VAL A 1 384 ? 24.260 -35.915 -4.630  1.00 36.72  ? 363 VAL A CG2   1 
ATOM   2673 N  N     . ASP A 1 385 ? 20.094 -34.830 -6.600  1.00 33.97  ? 364 ASP A N     1 
ATOM   2674 C  CA    . ASP A 1 385 ? 18.712 -35.068 -7.069  1.00 35.23  ? 364 ASP A CA    1 
ATOM   2675 C  C     . ASP A 1 385 ? 18.676 -34.972 -8.599  1.00 34.34  ? 364 ASP A C     1 
ATOM   2676 O  O     . ASP A 1 385 ? 18.124 -35.871 -9.243  1.00 31.51  ? 364 ASP A O     1 
ATOM   2677 C  CB    . ASP A 1 385 ? 17.719 -34.080 -6.454  1.00 37.56  ? 364 ASP A CB    1 
ATOM   2678 C  CG    . ASP A 1 385 ? 16.331 -34.270 -7.037  1.00 40.75  ? 364 ASP A CG    1 
ATOM   2679 O  OD1   . ASP A 1 385 ? 15.738 -35.335 -6.748  1.00 44.34  ? 364 ASP A OD1   1 
ATOM   2680 O  OD2   . ASP A 1 385 ? 15.889 -33.401 -7.847  1.00 41.86  ? 364 ASP A OD2   1 
ATOM   2681 N  N     . VAL A 1 386 ? 19.249 -33.917 -9.169  1.00 33.42  ? 365 VAL A N     1 
ATOM   2682 C  CA    . VAL A 1 386 ? 19.360 -33.776 -10.653 1.00 35.19  ? 365 VAL A CA    1 
ATOM   2683 C  C     . VAL A 1 386 ? 20.108 -34.992 -11.246 1.00 32.36  ? 365 VAL A C     1 
ATOM   2684 O  O     . VAL A 1 386 ? 19.655 -35.492 -12.262 1.00 32.13  ? 365 VAL A O     1 
ATOM   2685 C  CB    . VAL A 1 386 ? 20.009 -32.434 -11.038 1.00 36.07  ? 365 VAL A CB    1 
ATOM   2686 C  CG1   . VAL A 1 386 ? 20.352 -32.363 -12.518 1.00 37.24  ? 365 VAL A CG1   1 
ATOM   2687 C  CG2   . VAL A 1 386 ? 19.099 -31.276 -10.642 1.00 36.89  ? 365 VAL A CG2   1 
ATOM   2688 N  N     . LEU A 1 387 ? 21.204 -35.452 -10.638 1.00 28.70  ? 366 LEU A N     1 
ATOM   2689 C  CA    . LEU A 1 387 ? 22.054 -36.513 -11.212 1.00 28.85  ? 366 LEU A CA    1 
ATOM   2690 C  C     . LEU A 1 387 ? 21.342 -37.864 -11.064 1.00 31.09  ? 366 LEU A C     1 
ATOM   2691 O  O     . LEU A 1 387 ? 21.515 -38.708 -11.962 1.00 29.08  ? 366 LEU A O     1 
ATOM   2692 C  CB    . LEU A 1 387 ? 23.434 -36.528 -10.550 1.00 29.43  ? 366 LEU A CB    1 
ATOM   2693 C  CG    . LEU A 1 387 ? 24.291 -35.272 -10.741 1.00 31.21  ? 366 LEU A CG    1 
ATOM   2694 C  CD1   . LEU A 1 387 ? 25.656 -35.448 -10.102 1.00 31.53  ? 366 LEU A CD1   1 
ATOM   2695 C  CD2   . LEU A 1 387 ? 24.438 -34.904 -12.198 1.00 34.74  ? 366 LEU A CD2   1 
ATOM   2696 N  N     . ALA A 1 388 ? 20.569 -38.045 -9.989  1.00 35.17  ? 367 ALA A N     1 
ATOM   2697 C  CA    . ALA A 1 388 ? 19.785 -39.264 -9.702  1.00 37.56  ? 367 ALA A CA    1 
ATOM   2698 C  C     . ALA A 1 388 ? 18.780 -39.490 -10.832 1.00 36.29  ? 367 ALA A C     1 
ATOM   2699 O  O     . ALA A 1 388 ? 18.646 -40.614 -11.291 1.00 40.69  ? 367 ALA A O     1 
ATOM   2700 C  CB    . ALA A 1 388 ? 19.103 -39.151 -8.362  1.00 39.21  ? 367 ALA A CB    1 
ATOM   2701 N  N     . ARG A 1 389 ? 18.137 -38.434 -11.295 1.00 37.53  ? 368 ARG A N     1 
ATOM   2702 C  CA    . ARG A 1 389 ? 17.042 -38.527 -12.287 1.00 41.56  ? 368 ARG A CA    1 
ATOM   2703 C  C     . ARG A 1 389 ? 17.626 -38.565 -13.709 1.00 42.50  ? 368 ARG A C     1 
ATOM   2704 O  O     . ARG A 1 389 ? 16.857 -38.878 -14.649 1.00 42.05  ? 368 ARG A O     1 
ATOM   2705 C  CB    . ARG A 1 389 ? 16.070 -37.364 -12.059 1.00 46.34  ? 368 ARG A CB    1 
ATOM   2706 C  CG    . ARG A 1 389 ? 15.388 -37.383 -10.696 1.00 45.96  ? 368 ARG A CG    1 
ATOM   2707 C  CD    . ARG A 1 389 ? 14.288 -36.338 -10.601 1.00 47.07  ? 368 ARG A CD    1 
ATOM   2708 N  NE    . ARG A 1 389 ? 14.838 -35.049 -10.226 1.00 44.86  ? 368 ARG A NE    1 
ATOM   2709 C  CZ    . ARG A 1 389 ? 14.924 -33.967 -11.000 1.00 47.73  ? 368 ARG A CZ    1 
ATOM   2710 N  NH1   . ARG A 1 389 ? 14.495 -33.973 -12.250 1.00 45.11  ? 368 ARG A NH1   1 
ATOM   2711 N  NH2   . ARG A 1 389 ? 15.477 -32.869 -10.508 1.00 45.64  ? 368 ARG A NH2   1 
ATOM   2712 N  N     . THR A 1 390 ? 18.924 -38.282 -13.885 1.00 42.61  ? 369 THR A N     1 
ATOM   2713 C  CA    . THR A 1 390 ? 19.574 -38.235 -15.229 1.00 40.68  ? 369 THR A CA    1 
ATOM   2714 C  C     . THR A 1 390 ? 20.597 -39.374 -15.388 1.00 41.83  ? 369 THR A C     1 
ATOM   2715 O  O     . THR A 1 390 ? 20.314 -40.291 -16.172 1.00 41.10  ? 369 THR A O     1 
ATOM   2716 C  CB    . THR A 1 390 ? 20.131 -36.836 -15.495 1.00 39.46  ? 369 THR A CB    1 
ATOM   2717 O  OG1   . THR A 1 390 ? 20.923 -36.409 -14.392 1.00 39.38  ? 369 THR A OG1   1 
ATOM   2718 C  CG2   . THR A 1 390 ? 19.027 -35.826 -15.722 1.00 42.32  ? 369 THR A CG2   1 
ATOM   2719 N  N     . LEU A 1 391 ? 21.716 -39.343 -14.654 1.00 40.32  ? 370 LEU A N     1 
ATOM   2720 C  CA    . LEU A 1 391 ? 22.773 -40.394 -14.695 1.00 39.78  ? 370 LEU A CA    1 
ATOM   2721 C  C     . LEU A 1 391 ? 22.299 -41.673 -13.990 1.00 36.71  ? 370 LEU A C     1 
ATOM   2722 O  O     . LEU A 1 391 ? 22.873 -42.733 -14.267 1.00 32.96  ? 370 LEU A O     1 
ATOM   2723 C  CB    . LEU A 1 391 ? 24.052 -39.895 -14.011 1.00 38.82  ? 370 LEU A CB    1 
ATOM   2724 C  CG    . LEU A 1 391 ? 24.804 -38.750 -14.678 1.00 39.96  ? 370 LEU A CG    1 
ATOM   2725 C  CD1   . LEU A 1 391 ? 26.133 -38.519 -13.948 1.00 40.50  ? 370 LEU A CD1   1 
ATOM   2726 C  CD2   . LEU A 1 391 ? 25.038 -39.023 -16.163 1.00 40.81  ? 370 LEU A CD2   1 
ATOM   2727 N  N     . GLY A 1 392 ? 21.366 -41.568 -13.042 1.00 39.05  ? 371 GLY A N     1 
ATOM   2728 C  CA    . GLY A 1 392 ? 20.825 -42.739 -12.323 1.00 37.98  ? 371 GLY A CA    1 
ATOM   2729 C  C     . GLY A 1 392 ? 21.001 -42.667 -10.810 1.00 40.43  ? 371 GLY A C     1 
ATOM   2730 O  O     . GLY A 1 392 ? 21.847 -41.875 -10.292 1.00 33.32  ? 371 GLY A O     1 
ATOM   2731 N  N     . GLU A 1 393 ? 20.299 -43.582 -10.146 1.00 36.86  ? 372 GLU A N     1 
ATOM   2732 C  CA    . GLU A 1 393 ? 19.883 -43.499 -8.728  1.00 40.46  ? 372 GLU A CA    1 
ATOM   2733 C  C     . GLU A 1 393 ? 21.128 -43.769 -7.872  1.00 37.22  ? 372 GLU A C     1 
ATOM   2734 O  O     . GLU A 1 393 ? 21.136 -43.426 -6.668  1.00 32.20  ? 372 GLU A O     1 
ATOM   2735 C  CB    . GLU A 1 393 ? 18.698 -44.455 -8.579  1.00 43.75  ? 372 GLU A CB    1 
ATOM   2736 C  CG    . GLU A 1 393 ? 17.613 -44.014 -7.613  1.00 52.66  ? 372 GLU A CG    1 
ATOM   2737 C  CD    . GLU A 1 393 ? 17.043 -42.607 -7.699  1.00 52.05  ? 372 GLU A CD    1 
ATOM   2738 O  OE1   . GLU A 1 393 ? 16.434 -42.252 -8.712  1.00 50.67  ? 372 GLU A OE1   1 
ATOM   2739 O  OE2   . GLU A 1 393 ? 17.167 -41.893 -6.705  1.00 58.11  ? 372 GLU A OE2   1 
ATOM   2740 N  N     . ARG A 1 394 ? 22.187 -44.272 -8.509  1.00 35.57  ? 373 ARG A N     1 
ATOM   2741 C  CA    . ARG A 1 394 ? 23.483 -44.543 -7.852  1.00 37.38  ? 373 ARG A CA    1 
ATOM   2742 C  C     . ARG A 1 394 ? 24.155 -43.216 -7.464  1.00 34.35  ? 373 ARG A C     1 
ATOM   2743 O  O     . ARG A 1 394 ? 24.987 -43.257 -6.582  1.00 33.48  ? 373 ARG A O     1 
ATOM   2744 C  CB    . ARG A 1 394 ? 24.360 -45.395 -8.771  1.00 45.18  ? 373 ARG A CB    1 
ATOM   2745 C  CG    . ARG A 1 394 ? 25.753 -45.633 -8.210  1.00 58.25  ? 373 ARG A CG    1 
ATOM   2746 C  CD    . ARG A 1 394 ? 26.378 -46.923 -8.685  1.00 70.29  ? 373 ARG A CD    1 
ATOM   2747 N  NE    . ARG A 1 394 ? 27.709 -47.081 -8.101  1.00 83.22  ? 373 ARG A NE    1 
ATOM   2748 C  CZ    . ARG A 1 394 ? 28.560 -48.065 -8.401  1.00 86.55  ? 373 ARG A CZ    1 
ATOM   2749 N  NH1   . ARG A 1 394 ? 28.222 -48.989 -9.286  1.00 84.16  ? 373 ARG A NH1   1 
ATOM   2750 N  NH2   . ARG A 1 394 ? 29.745 -48.123 -7.813  1.00 85.04  ? 373 ARG A NH2   1 
ATOM   2751 N  N     . ALA A 1 395 ? 23.794 -42.085 -8.076  1.00 30.84  ? 374 ALA A N     1 
ATOM   2752 C  CA    . ALA A 1 395 ? 24.323 -40.736 -7.743  1.00 34.22  ? 374 ALA A CA    1 
ATOM   2753 C  C     . ALA A 1 395 ? 24.034 -40.334 -6.276  1.00 36.79  ? 374 ALA A C     1 
ATOM   2754 O  O     . ALA A 1 395 ? 24.766 -39.445 -5.752  1.00 36.37  ? 374 ALA A O     1 
ATOM   2755 C  CB    . ALA A 1 395 ? 23.763 -39.712 -8.711  1.00 32.78  ? 374 ALA A CB    1 
ATOM   2756 N  N     . ARG A 1 396 ? 23.041 -40.939 -5.611  1.00 34.07  ? 375 ARG A N     1 
ATOM   2757 C  CA    . ARG A 1 396 ? 22.671 -40.545 -4.221  1.00 35.24  ? 375 ARG A CA    1 
ATOM   2758 C  C     . ARG A 1 396 ? 23.691 -41.100 -3.209  1.00 37.58  ? 375 ARG A C     1 
ATOM   2759 O  O     . ARG A 1 396 ? 23.727 -40.518 -2.082  1.00 35.80  ? 375 ARG A O     1 
ATOM   2760 C  CB    . ARG A 1 396 ? 21.233 -40.937 -3.848  1.00 31.71  ? 375 ARG A CB    1 
ATOM   2761 C  CG    . ARG A 1 396 ? 20.169 -40.337 -4.752  1.00 30.26  ? 375 ARG A CG    1 
ATOM   2762 C  CD    . ARG A 1 396 ? 18.729 -40.560 -4.315  1.00 29.70  ? 375 ARG A CD    1 
ATOM   2763 N  NE    . ARG A 1 396 ? 17.744 -39.907 -5.176  1.00 29.58  ? 375 ARG A NE    1 
ATOM   2764 C  CZ    . ARG A 1 396 ? 17.484 -38.597 -5.210  1.00 34.38  ? 375 ARG A CZ    1 
ATOM   2765 N  NH1   . ARG A 1 396 ? 18.132 -37.747 -4.428  1.00 35.21  ? 375 ARG A NH1   1 
ATOM   2766 N  NH2   . ARG A 1 396 ? 16.558 -38.134 -6.030  1.00 37.47  ? 375 ARG A NH2   1 
ATOM   2767 N  N     . ASP A 1 397 ? 24.480 -42.135 -3.568  1.00 37.52  ? 376 ASP A N     1 
ATOM   2768 C  CA    . ASP A 1 397 ? 25.584 -42.701 -2.720  1.00 42.20  ? 376 ASP A CA    1 
ATOM   2769 C  C     . ASP A 1 397 ? 26.894 -41.931 -2.992  1.00 40.26  ? 376 ASP A C     1 
ATOM   2770 O  O     . ASP A 1 397 ? 27.759 -42.437 -3.703  1.00 40.10  ? 376 ASP A O     1 
ATOM   2771 C  CB    . ASP A 1 397 ? 25.778 -44.215 -2.924  1.00 42.20  ? 376 ASP A CB    1 
ATOM   2772 C  CG    . ASP A 1 397 ? 26.835 -44.865 -2.023  1.00 43.95  ? 376 ASP A CG    1 
ATOM   2773 O  OD1   . ASP A 1 397 ? 27.373 -44.198 -1.113  1.00 47.30  ? 376 ASP A OD1   1 
ATOM   2774 O  OD2   . ASP A 1 397 ? 27.109 -46.054 -2.225  1.00 48.19  ? 376 ASP A OD2   1 
ATOM   2775 N  N     . VAL A 1 398 ? 27.023 -40.735 -2.431  1.00 38.87  ? 377 VAL A N     1 
ATOM   2776 C  CA    . VAL A 1 398 ? 28.095 -39.764 -2.769  1.00 38.44  ? 377 VAL A CA    1 
ATOM   2777 C  C     . VAL A 1 398 ? 29.146 -39.861 -1.660  1.00 36.68  ? 377 VAL A C     1 
ATOM   2778 O  O     . VAL A 1 398 ? 28.750 -39.902 -0.494  1.00 37.15  ? 377 VAL A O     1 
ATOM   2779 C  CB    . VAL A 1 398 ? 27.515 -38.344 -2.943  1.00 38.62  ? 377 VAL A CB    1 
ATOM   2780 C  CG1   . VAL A 1 398 ? 26.632 -37.918 -1.784  1.00 43.66  ? 377 VAL A CG1   1 
ATOM   2781 C  CG2   . VAL A 1 398 ? 28.603 -37.319 -3.124  1.00 41.56  ? 377 VAL A CG2   1 
ATOM   2782 N  N     . ARG A 1 399 ? 30.429 -39.950 -1.995  1.00 36.53  ? 378 ARG A N     1 
ATOM   2783 C  CA    . ARG A 1 399 ? 31.498 -39.958 -0.967  1.00 37.73  ? 378 ARG A CA    1 
ATOM   2784 C  C     . ARG A 1 399 ? 31.716 -38.526 -0.460  1.00 34.19  ? 378 ARG A C     1 
ATOM   2785 O  O     . ARG A 1 399 ? 31.812 -38.348 0.725   1.00 40.02  ? 378 ARG A O     1 
ATOM   2786 C  CB    . ARG A 1 399 ? 32.788 -40.582 -1.505  1.00 45.76  ? 378 ARG A CB    1 
ATOM   2787 C  CG    . ARG A 1 399 ? 33.855 -40.822 -0.437  1.00 52.40  ? 378 ARG A CG    1 
ATOM   2788 C  CD    . ARG A 1 399 ? 35.228 -41.100 -1.038  1.00 62.23  ? 378 ARG A CD    1 
ATOM   2789 N  NE    . ARG A 1 399 ? 36.099 -41.930 -0.195  1.00 74.14  ? 378 ARG A NE    1 
ATOM   2790 C  CZ    . ARG A 1 399 ? 37.359 -42.288 -0.492  1.00 79.09  ? 378 ARG A CZ    1 
ATOM   2791 N  NH1   . ARG A 1 399 ? 37.925 -41.909 -1.628  1.00 81.09  ? 378 ARG A NH1   1 
ATOM   2792 N  NH2   . ARG A 1 399 ? 38.054 -43.026 0.358   1.00 75.53  ? 378 ARG A NH2   1 
ATOM   2793 N  N     . ASP A 1 400 ? 31.746 -37.511 -1.309  1.00 34.98  ? 379 ASP A N     1 
ATOM   2794 C  CA    . ASP A 1 400 ? 31.962 -36.121 -0.831  1.00 36.46  ? 379 ASP A CA    1 
ATOM   2795 C  C     . ASP A 1 400 ? 31.348 -35.143 -1.837  1.00 33.66  ? 379 ASP A C     1 
ATOM   2796 O  O     . ASP A 1 400 ? 30.974 -35.564 -2.931  1.00 36.24  ? 379 ASP A O     1 
ATOM   2797 C  CB    . ASP A 1 400 ? 33.451 -35.884 -0.538  1.00 36.99  ? 379 ASP A CB    1 
ATOM   2798 C  CG    . ASP A 1 400 ? 33.772 -34.669 0.331   1.00 36.57  ? 379 ASP A CG    1 
ATOM   2799 O  OD1   . ASP A 1 400 ? 32.861 -33.864 0.562   1.00 46.31  ? 379 ASP A OD1   1 
ATOM   2800 O  OD2   . ASP A 1 400 ? 34.939 -34.523 0.762   1.00 39.80  ? 379 ASP A OD2   1 
ATOM   2801 N  N     . TYR A 1 401 ? 31.179 -33.895 -1.419  1.00 33.72  ? 380 TYR A N     1 
ATOM   2802 C  CA    . TYR A 1 401 ? 30.690 -32.771 -2.253  1.00 34.72  ? 380 TYR A CA    1 
ATOM   2803 C  C     . TYR A 1 401 ? 31.483 -31.519 -1.859  1.00 34.96  ? 380 TYR A C     1 
ATOM   2804 O  O     . TYR A 1 401 ? 31.436 -31.138 -0.682  1.00 34.64  ? 380 TYR A O     1 
ATOM   2805 C  CB    . TYR A 1 401 ? 29.169 -32.632 -2.122  1.00 32.38  ? 380 TYR A CB    1 
ATOM   2806 C  CG    . TYR A 1 401 ? 28.594 -31.408 -2.782  1.00 30.68  ? 380 TYR A CG    1 
ATOM   2807 C  CD1   . TYR A 1 401 ? 28.222 -31.433 -4.111  1.00 31.30  ? 380 TYR A CD1   1 
ATOM   2808 C  CD2   . TYR A 1 401 ? 28.458 -30.218 -2.092  1.00 29.24  ? 380 TYR A CD2   1 
ATOM   2809 C  CE1   . TYR A 1 401 ? 27.735 -30.305 -4.745  1.00 31.09  ? 380 TYR A CE1   1 
ATOM   2810 C  CE2   . TYR A 1 401 ? 27.990 -29.075 -2.711  1.00 30.06  ? 380 TYR A CE2   1 
ATOM   2811 C  CZ    . TYR A 1 401 ? 27.644 -29.115 -4.046  1.00 32.51  ? 380 TYR A CZ    1 
ATOM   2812 O  OH    . TYR A 1 401 ? 27.176 -28.004 -4.675  1.00 31.64  ? 380 TYR A OH    1 
ATOM   2813 N  N     . ILE A 1 402 ? 32.205 -30.935 -2.824  1.00 34.85  ? 381 ILE A N     1 
ATOM   2814 C  CA    . ILE A 1 402 ? 33.050 -29.724 -2.636  1.00 34.10  ? 381 ILE A CA    1 
ATOM   2815 C  C     . ILE A 1 402 ? 32.558 -28.618 -3.574  1.00 34.79  ? 381 ILE A C     1 
ATOM   2816 O  O     . ILE A 1 402 ? 32.507 -28.872 -4.798  1.00 35.85  ? 381 ILE A O     1 
ATOM   2817 C  CB    . ILE A 1 402 ? 34.529 -30.066 -2.888  1.00 36.52  ? 381 ILE A CB    1 
ATOM   2818 C  CG1   . ILE A 1 402 ? 34.968 -31.316 -2.124  1.00 40.04  ? 381 ILE A CG1   1 
ATOM   2819 C  CG2   . ILE A 1 402 ? 35.409 -28.889 -2.518  1.00 36.62  ? 381 ILE A CG2   1 
ATOM   2820 C  CD1   . ILE A 1 402 ? 36.106 -32.068 -2.774  1.00 39.73  ? 381 ILE A CD1   1 
ATOM   2821 N  N     . ASP A 1 403 ? 32.235 -27.425 -3.060  1.00 31.15  ? 382 ASP A N     1 
ATOM   2822 C  CA    . ASP A 1 403 ? 31.842 -26.299 -3.939  1.00 33.36  ? 382 ASP A CA    1 
ATOM   2823 C  C     . ASP A 1 403 ? 32.457 -24.991 -3.444  1.00 32.58  ? 382 ASP A C     1 
ATOM   2824 O  O     . ASP A 1 403 ? 33.106 -25.019 -2.397  1.00 29.49  ? 382 ASP A O     1 
ATOM   2825 C  CB    . ASP A 1 403 ? 30.330 -26.244 -4.167  1.00 38.01  ? 382 ASP A CB    1 
ATOM   2826 C  CG    . ASP A 1 403 ? 29.426 -25.860 -3.005  1.00 41.47  ? 382 ASP A CG    1 
ATOM   2827 O  OD1   . ASP A 1 403 ? 29.930 -25.308 -2.013  1.00 37.29  ? 382 ASP A OD1   1 
ATOM   2828 O  OD2   . ASP A 1 403 ? 28.180 -26.110 -3.135  1.00 41.88  ? 382 ASP A OD2   1 
ATOM   2829 N  N     . ARG A 1 404 ? 32.334 -23.931 -4.249  1.00 30.02  ? 383 ARG A N     1 
ATOM   2830 C  CA    . ARG A 1 404 ? 32.753 -22.560 -3.901  1.00 30.73  ? 383 ARG A CA    1 
ATOM   2831 C  C     . ARG A 1 404 ? 31.794 -21.549 -4.542  1.00 31.56  ? 383 ARG A C     1 
ATOM   2832 O  O     . ARG A 1 404 ? 31.635 -21.574 -5.763  1.00 30.43  ? 383 ARG A O     1 
ATOM   2833 C  CB    . ARG A 1 404 ? 34.204 -22.291 -4.311  1.00 31.91  ? 383 ARG A CB    1 
ATOM   2834 C  CG    . ARG A 1 404 ? 34.654 -20.910 -3.872  1.00 38.40  ? 383 ARG A CG    1 
ATOM   2835 C  CD    . ARG A 1 404 ? 36.112 -20.749 -3.508  1.00 42.78  ? 383 ARG A CD    1 
ATOM   2836 N  NE    . ARG A 1 404 ? 36.489 -21.571 -2.379  1.00 48.72  ? 383 ARG A NE    1 
ATOM   2837 C  CZ    . ARG A 1 404 ? 37.747 -21.835 -2.027  1.00 51.47  ? 383 ARG A CZ    1 
ATOM   2838 N  NH1   . ARG A 1 404 ? 38.758 -21.307 -2.692  1.00 49.90  ? 383 ARG A NH1   1 
ATOM   2839 N  NH2   . ARG A 1 404 ? 37.985 -22.629 -1.000  1.00 58.39  ? 383 ARG A NH2   1 
ATOM   2840 N  N     . ASP A 1 405 ? 31.163 -20.709 -3.711  1.00 33.15  ? 384 ASP A N     1 
ATOM   2841 C  CA    . ASP A 1 405 ? 30.379 -19.516 -4.133  1.00 32.33  ? 384 ASP A CA    1 
ATOM   2842 C  C     . ASP A 1 405 ? 31.364 -18.356 -4.261  1.00 29.19  ? 384 ASP A C     1 
ATOM   2843 O  O     . ASP A 1 405 ? 31.740 -17.776 -3.229  1.00 25.78  ? 384 ASP A O     1 
ATOM   2844 C  CB    . ASP A 1 405 ? 29.265 -19.158 -3.134  1.00 36.94  ? 384 ASP A CB    1 
ATOM   2845 C  CG    . ASP A 1 405 ? 28.342 -18.020 -3.578  1.00 37.70  ? 384 ASP A CG    1 
ATOM   2846 O  OD1   . ASP A 1 405 ? 28.521 -17.514 -4.704  1.00 36.97  ? 384 ASP A OD1   1 
ATOM   2847 O  OD2   . ASP A 1 405 ? 27.410 -17.683 -2.817  1.00 39.65  ? 384 ASP A OD2   1 
ATOM   2848 N  N     . TRP A 1 406 ? 31.799 -18.073 -5.482  1.00 27.29  ? 385 TRP A N     1 
ATOM   2849 C  CA    . TRP A 1 406 ? 32.795 -17.015 -5.776  1.00 28.06  ? 385 TRP A CA    1 
ATOM   2850 C  C     . TRP A 1 406 ? 32.194 -15.628 -5.502  1.00 29.75  ? 385 TRP A C     1 
ATOM   2851 O  O     . TRP A 1 406 ? 32.972 -14.661 -5.412  1.00 29.40  ? 385 TRP A O     1 
ATOM   2852 C  CB    . TRP A 1 406 ? 33.314 -17.187 -7.213  1.00 29.17  ? 385 TRP A CB    1 
ATOM   2853 C  CG    . TRP A 1 406 ? 34.326 -18.289 -7.310  1.00 26.89  ? 385 TRP A CG    1 
ATOM   2854 C  CD1   . TRP A 1 406 ? 34.085 -19.602 -7.577  1.00 28.53  ? 385 TRP A CD1   1 
ATOM   2855 C  CD2   . TRP A 1 406 ? 35.731 -18.193 -7.021  1.00 26.37  ? 385 TRP A CD2   1 
ATOM   2856 N  NE1   . TRP A 1 406 ? 35.250 -20.322 -7.525  1.00 28.13  ? 385 TRP A NE1   1 
ATOM   2857 C  CE2   . TRP A 1 406 ? 36.274 -19.486 -7.172  1.00 29.23  ? 385 TRP A CE2   1 
ATOM   2858 C  CE3   . TRP A 1 406 ? 36.583 -17.133 -6.699  1.00 29.31  ? 385 TRP A CE3   1 
ATOM   2859 C  CZ2   . TRP A 1 406 ? 37.635 -19.751 -7.014  1.00 30.41  ? 385 TRP A CZ2   1 
ATOM   2860 C  CZ3   . TRP A 1 406 ? 37.922 -17.395 -6.528  1.00 32.55  ? 385 TRP A CZ3   1 
ATOM   2861 C  CH2   . TRP A 1 406 ? 38.444 -18.685 -6.699  1.00 31.18  ? 385 TRP A CH2   1 
ATOM   2862 N  N     . SER A 1 407 ? 30.867 -15.540 -5.346  1.00 29.24  ? 386 SER A N     1 
ATOM   2863 C  CA    . SER A 1 407 ? 30.144 -14.331 -4.889  1.00 30.10  ? 386 SER A CA    1 
ATOM   2864 C  C     . SER A 1 407 ? 30.471 -14.038 -3.425  1.00 30.54  ? 386 SER A C     1 
ATOM   2865 O  O     . SER A 1 407 ? 30.407 -12.863 -3.055  1.00 28.17  ? 386 SER A O     1 
ATOM   2866 C  CB    . SER A 1 407 ? 28.661 -14.475 -5.084  1.00 30.80  ? 386 SER A CB    1 
ATOM   2867 O  OG    . SER A 1 407 ? 28.329 -14.475 -6.466  1.00 31.99  ? 386 SER A OG    1 
ATOM   2868 N  N     . ALA A 1 408 ? 30.770 -15.067 -2.621  1.00 29.68  ? 387 ALA A N     1 
ATOM   2869 C  CA    . ALA A 1 408 ? 31.018 -14.954 -1.159  1.00 34.04  ? 387 ALA A CA    1 
ATOM   2870 C  C     . ALA A 1 408 ? 32.507 -14.712 -0.852  1.00 34.60  ? 387 ALA A C     1 
ATOM   2871 O  O     . ALA A 1 408 ? 32.834 -14.601 0.329   1.00 35.12  ? 387 ALA A O     1 
ATOM   2872 C  CB    . ALA A 1 408 ? 30.512 -16.190 -0.449  1.00 33.14  ? 387 ALA A CB    1 
ATOM   2873 N  N     . GLU A 1 409 ? 33.372 -14.659 -1.870  1.00 33.37  ? 388 GLU A N     1 
ATOM   2874 C  CA    . GLU A 1 409 ? 34.831 -14.373 -1.737  1.00 33.66  ? 388 GLU A CA    1 
ATOM   2875 C  C     . GLU A 1 409 ? 35.050 -12.860 -1.670  1.00 30.71  ? 388 GLU A C     1 
ATOM   2876 O  O     . GLU A 1 409 ? 34.877 -12.148 -2.670  1.00 31.15  ? 388 GLU A O     1 
ATOM   2877 C  CB    . GLU A 1 409 ? 35.575 -15.014 -2.915  1.00 30.78  ? 388 GLU A CB    1 
ATOM   2878 C  CG    . GLU A 1 409 ? 35.528 -16.539 -2.886  1.00 31.68  ? 388 GLU A CG    1 
ATOM   2879 C  CD    . GLU A 1 409 ? 36.639 -17.167 -2.076  1.00 34.00  ? 388 GLU A CD    1 
ATOM   2880 O  OE1   . GLU A 1 409 ? 37.771 -16.627 -2.075  1.00 38.27  ? 388 GLU A OE1   1 
ATOM   2881 O  OE2   . GLU A 1 409 ? 36.361 -18.156 -1.408  1.00 42.76  ? 388 GLU A OE2   1 
ATOM   2882 N  N     . PRO A 1 410 ? 35.461 -12.295 -0.517  1.00 30.73  ? 389 PRO A N     1 
ATOM   2883 C  CA    . PRO A 1 410 ? 35.640 -10.843 -0.436  1.00 30.87  ? 389 PRO A CA    1 
ATOM   2884 C  C     . PRO A 1 410 ? 36.600 -10.327 -1.531  1.00 28.77  ? 389 PRO A C     1 
ATOM   2885 O  O     . PRO A 1 410 ? 36.420 -9.201  -1.970  1.00 27.28  ? 389 PRO A O     1 
ATOM   2886 C  CB    . PRO A 1 410 ? 36.179 -10.582 0.991   1.00 31.73  ? 389 PRO A CB    1 
ATOM   2887 C  CG    . PRO A 1 410 ? 36.644 -11.968 1.488   1.00 34.26  ? 389 PRO A CG    1 
ATOM   2888 C  CD    . PRO A 1 410 ? 35.789 -12.986 0.745   1.00 32.85  ? 389 PRO A CD    1 
ATOM   2889 N  N     . TRP A 1 411 ? 37.541 -11.147 -2.021  1.00 27.99  ? 390 TRP A N     1 
ATOM   2890 C  CA    . TRP A 1 411 ? 38.612 -10.652 -2.938  1.00 29.68  ? 390 TRP A CA    1 
ATOM   2891 C  C     . TRP A 1 411 ? 38.326 -10.993 -4.406  1.00 27.71  ? 390 TRP A C     1 
ATOM   2892 O  O     . TRP A 1 411 ? 39.231 -10.787 -5.237  1.00 28.48  ? 390 TRP A O     1 
ATOM   2893 C  CB    . TRP A 1 411 ? 39.994 -11.115 -2.465  1.00 27.86  ? 390 TRP A CB    1 
ATOM   2894 C  CG    . TRP A 1 411 ? 40.269 -10.595 -1.096  1.00 27.64  ? 390 TRP A CG    1 
ATOM   2895 C  CD1   . TRP A 1 411 ? 40.418 -11.339 0.034   1.00 29.87  ? 390 TRP A CD1   1 
ATOM   2896 C  CD2   . TRP A 1 411 ? 40.333 -9.215  -0.680  1.00 30.15  ? 390 TRP A CD2   1 
ATOM   2897 N  NE1   . TRP A 1 411 ? 40.561 -10.526 1.128   1.00 28.16  ? 390 TRP A NE1   1 
ATOM   2898 C  CE2   . TRP A 1 411 ? 40.542 -9.215  0.721   1.00 32.10  ? 390 TRP A CE2   1 
ATOM   2899 C  CE3   . TRP A 1 411 ? 40.223 -7.982  -1.336  1.00 32.43  ? 390 TRP A CE3   1 
ATOM   2900 C  CZ2   . TRP A 1 411 ? 40.641 -8.036  1.467   1.00 31.42  ? 390 TRP A CZ2   1 
ATOM   2901 C  CZ3   . TRP A 1 411 ? 40.335 -6.818  -0.602  1.00 34.16  ? 390 TRP A CZ3   1 
ATOM   2902 C  CH2   . TRP A 1 411 ? 40.525 -6.845  0.784   1.00 32.81  ? 390 TRP A CH2   1 
ATOM   2903 N  N     . THR A 1 412 ? 37.098 -11.399 -4.735  1.00 28.37  ? 391 THR A N     1 
ATOM   2904 C  CA    . THR A 1 412 ? 36.625 -11.609 -6.134  1.00 25.81  ? 391 THR A CA    1 
ATOM   2905 C  C     . THR A 1 412 ? 35.245 -10.955 -6.290  1.00 26.41  ? 391 THR A C     1 
ATOM   2906 O  O     . THR A 1 412 ? 35.129 -10.035 -7.103  1.00 28.05  ? 391 THR A O     1 
ATOM   2907 C  CB    . THR A 1 412 ? 36.595 -13.108 -6.516  1.00 27.76  ? 391 THR A CB    1 
ATOM   2908 O  OG1   . THR A 1 412 ? 37.822 -13.806 -6.263  1.00 26.18  ? 391 THR A OG1   1 
ATOM   2909 C  CG2   . THR A 1 412 ? 36.290 -13.316 -7.990  1.00 25.79  ? 391 THR A CG2   1 
ATOM   2910 N  N     . ARG A 1 413 ? 34.235 -11.452 -5.554  1.00 27.90  ? 392 ARG A N     1 
ATOM   2911 C  CA    . ARG A 1 413 ? 32.852 -10.903 -5.483  1.00 29.92  ? 392 ARG A CA    1 
ATOM   2912 C  C     . ARG A 1 413 ? 32.122 -11.222 -6.795  1.00 32.23  ? 392 ARG A C     1 
ATOM   2913 O  O     . ARG A 1 413 ? 31.359 -10.362 -7.275  1.00 27.02  ? 392 ARG A O     1 
ATOM   2914 C  CB    . ARG A 1 413 ? 32.867 -9.402  -5.135  1.00 30.58  ? 392 ARG A CB    1 
ATOM   2915 C  CG    . ARG A 1 413 ? 33.163 -9.110  -3.672  1.00 31.04  ? 392 ARG A CG    1 
ATOM   2916 C  CD    . ARG A 1 413 ? 32.334 -9.977  -2.726  1.00 33.05  ? 392 ARG A CD    1 
ATOM   2917 N  NE    . ARG A 1 413 ? 32.303 -9.481  -1.352  1.00 31.66  ? 392 ARG A NE    1 
ATOM   2918 C  CZ    . ARG A 1 413 ? 31.477 -9.926  -0.406  1.00 31.89  ? 392 ARG A CZ    1 
ATOM   2919 N  NH1   . ARG A 1 413 ? 30.610 -10.896 -0.663  1.00 32.88  ? 392 ARG A NH1   1 
ATOM   2920 N  NH2   . ARG A 1 413 ? 31.520 -9.401  0.805   1.00 33.25  ? 392 ARG A NH2   1 
ATOM   2921 N  N     . GLY A 1 414 ? 32.350 -12.428 -7.332  1.00 30.98  ? 393 GLY A N     1 
ATOM   2922 C  CA    . GLY A 1 414 ? 31.604 -13.006 -8.462  1.00 33.08  ? 393 GLY A CA    1 
ATOM   2923 C  C     . GLY A 1 414 ? 32.496 -13.487 -9.598  1.00 31.87  ? 393 GLY A C     1 
ATOM   2924 O  O     . GLY A 1 414 ? 33.381 -12.761 -10.020 1.00 32.34  ? 393 GLY A O     1 
ATOM   2925 N  N     . CYS A 1 415 ? 32.224 -14.679 -10.107 1.00 31.05  ? 394 CYS A N     1 
ATOM   2926 C  CA    . CYS A 1 415 ? 32.846 -15.230 -11.333 1.00 32.06  ? 394 CYS A CA    1 
ATOM   2927 C  C     . CYS A 1 415 ? 31.797 -15.260 -12.446 1.00 34.97  ? 394 CYS A C     1 
ATOM   2928 O  O     . CYS A 1 415 ? 30.600 -15.120 -12.161 1.00 32.40  ? 394 CYS A O     1 
ATOM   2929 C  CB    . CYS A 1 415 ? 33.429 -16.606 -11.037 1.00 32.31  ? 394 CYS A CB    1 
ATOM   2930 S  SG    . CYS A 1 415 ? 35.187 -16.525 -10.605 1.00 36.17  ? 394 CYS A SG    1 
ATOM   2931 N  N     . TYR A 1 416 ? 32.229 -15.464 -13.707 1.00 32.41  ? 395 TYR A N     1 
ATOM   2932 C  CA    . TYR A 1 416 ? 33.610 -15.669 -14.098 1.00 31.59  ? 395 TYR A CA    1 
ATOM   2933 C  C     . TYR A 1 416 ? 34.294 -14.301 -14.195 1.00 34.13  ? 395 TYR A C     1 
ATOM   2934 O  O     . TYR A 1 416 ? 35.530 -14.191 -13.974 1.00 32.40  ? 395 TYR A O     1 
ATOM   2935 C  CB    . TYR A 1 416 ? 33.689 -16.381 -15.450 1.00 32.82  ? 395 TYR A CB    1 
ATOM   2936 C  CG    . TYR A 1 416 ? 32.780 -17.568 -15.583 1.00 34.28  ? 395 TYR A CG    1 
ATOM   2937 C  CD1   . TYR A 1 416 ? 32.969 -18.699 -14.803 1.00 34.67  ? 395 TYR A CD1   1 
ATOM   2938 C  CD2   . TYR A 1 416 ? 31.715 -17.558 -16.466 1.00 35.86  ? 395 TYR A CD2   1 
ATOM   2939 C  CE1   . TYR A 1 416 ? 32.139 -19.803 -14.904 1.00 35.09  ? 395 TYR A CE1   1 
ATOM   2940 C  CE2   . TYR A 1 416 ? 30.880 -18.660 -16.586 1.00 37.68  ? 395 TYR A CE2   1 
ATOM   2941 C  CZ    . TYR A 1 416 ? 31.095 -19.790 -15.810 1.00 37.17  ? 395 TYR A CZ    1 
ATOM   2942 O  OH    . TYR A 1 416 ? 30.256 -20.862 -15.897 1.00 37.45  ? 395 TYR A OH    1 
ATOM   2943 N  N     . GLY A 1 417 ? 33.506 -13.287 -14.557 1.00 32.99  ? 396 GLY A N     1 
ATOM   2944 C  CA    . GLY A 1 417 ? 33.927 -11.875 -14.525 1.00 31.68  ? 396 GLY A CA    1 
ATOM   2945 C  C     . GLY A 1 417 ? 32.760 -10.947 -14.773 1.00 32.70  ? 396 GLY A C     1 
ATOM   2946 O  O     . GLY A 1 417 ? 31.600 -11.426 -14.718 1.00 34.05  ? 396 GLY A O     1 
ATOM   2947 N  N     . ALA A 1 418 ? 33.073 -9.694  -15.089 1.00 30.11  ? 397 ALA A N     1 
ATOM   2948 C  CA    . ALA A 1 418 ? 32.127 -8.574  -15.241 1.00 30.48  ? 397 ALA A CA    1 
ATOM   2949 C  C     . ALA A 1 418 ? 31.348 -8.719  -16.544 1.00 33.65  ? 397 ALA A C     1 
ATOM   2950 O  O     . ALA A 1 418 ? 31.939 -9.153  -17.562 1.00 35.81  ? 397 ALA A O     1 
ATOM   2951 C  CB    . ALA A 1 418 ? 32.858 -7.259  -15.221 1.00 28.76  ? 397 ALA A CB    1 
ATOM   2952 N  N     . HIS A 1 419 ? 30.087 -8.291  -16.513 1.00 33.74  ? 398 HIS A N     1 
ATOM   2953 C  CA    . HIS A 1 419 ? 29.229 -8.038  -17.696 1.00 34.71  ? 398 HIS A CA    1 
ATOM   2954 C  C     . HIS A 1 419 ? 28.745 -6.587  -17.645 1.00 32.68  ? 398 HIS A C     1 
ATOM   2955 O  O     . HIS A 1 419 ? 28.889 -5.947  -16.598 1.00 34.55  ? 398 HIS A O     1 
ATOM   2956 C  CB    . HIS A 1 419 ? 28.086 -9.051  -17.748 1.00 32.54  ? 398 HIS A CB    1 
ATOM   2957 C  CG    . HIS A 1 419 ? 27.169 -8.995  -16.573 1.00 37.73  ? 398 HIS A CG    1 
ATOM   2958 N  ND1   . HIS A 1 419 ? 26.123 -8.073  -16.487 1.00 38.85  ? 398 HIS A ND1   1 
ATOM   2959 C  CD2   . HIS A 1 419 ? 27.099 -9.756  -15.454 1.00 37.49  ? 398 HIS A CD2   1 
ATOM   2960 C  CE1   . HIS A 1 419 ? 25.463 -8.271  -15.361 1.00 38.31  ? 398 HIS A CE1   1 
ATOM   2961 N  NE2   . HIS A 1 419 ? 26.041 -9.298  -14.706 1.00 35.89  ? 398 HIS A NE2   1 
ATOM   2962 N  N     . LEU A 1 420 ? 28.246 -6.064  -18.755 1.00 34.49  ? 399 LEU A N     1 
ATOM   2963 C  CA    . LEU A 1 420 ? 27.770 -4.661  -18.858 1.00 34.87  ? 399 LEU A CA    1 
ATOM   2964 C  C     . LEU A 1 420 ? 26.307 -4.707  -19.289 1.00 37.02  ? 399 LEU A C     1 
ATOM   2965 O  O     . LEU A 1 420 ? 25.947 -5.418  -20.229 1.00 34.35  ? 399 LEU A O     1 
ATOM   2966 C  CB    . LEU A 1 420 ? 28.655 -3.860  -19.825 1.00 34.72  ? 399 LEU A CB    1 
ATOM   2967 C  CG    . LEU A 1 420 ? 29.977 -3.368  -19.234 1.00 35.68  ? 399 LEU A CG    1 
ATOM   2968 C  CD1   . LEU A 1 420 ? 31.043 -4.459  -19.272 1.00 34.62  ? 399 LEU A CD1   1 
ATOM   2969 C  CD2   . LEU A 1 420 ? 30.463 -2.135  -19.953 1.00 34.50  ? 399 LEU A CD2   1 
ATOM   2970 N  N     . PRO A 1 421 ? 25.416 -3.977  -18.586 1.00 38.91  ? 400 PRO A N     1 
ATOM   2971 C  CA    . PRO A 1 421 ? 23.996 -3.978  -18.912 1.00 39.22  ? 400 PRO A CA    1 
ATOM   2972 C  C     . PRO A 1 421 ? 23.791 -2.922  -19.996 1.00 38.14  ? 400 PRO A C     1 
ATOM   2973 O  O     . PRO A 1 421 ? 24.689 -2.126  -20.262 1.00 37.20  ? 400 PRO A O     1 
ATOM   2974 C  CB    . PRO A 1 421 ? 23.392 -3.615  -17.551 1.00 37.01  ? 400 PRO A CB    1 
ATOM   2975 C  CG    . PRO A 1 421 ? 24.340 -2.524  -17.093 1.00 42.50  ? 400 PRO A CG    1 
ATOM   2976 C  CD    . PRO A 1 421 ? 25.712 -3.063  -17.472 1.00 40.69  ? 400 PRO A CD    1 
ATOM   2977 N  N     . PRO A 1 422 ? 22.586 -2.843  -20.602 1.00 37.13  ? 401 PRO A N     1 
ATOM   2978 C  CA    . PRO A 1 422 ? 22.296 -1.822  -21.606 1.00 37.10  ? 401 PRO A CA    1 
ATOM   2979 C  C     . PRO A 1 422 ? 22.693 -0.399  -21.181 1.00 38.42  ? 401 PRO A C     1 
ATOM   2980 O  O     . PRO A 1 422 ? 22.377 -0.028  -20.070 1.00 34.38  ? 401 PRO A O     1 
ATOM   2981 C  CB    . PRO A 1 422 ? 20.768 -1.877  -21.733 1.00 38.16  ? 401 PRO A CB    1 
ATOM   2982 C  CG    . PRO A 1 422 ? 20.385 -3.293  -21.309 1.00 37.92  ? 401 PRO A CG    1 
ATOM   2983 C  CD    . PRO A 1 422 ? 21.426 -3.697  -20.290 1.00 36.83  ? 401 PRO A CD    1 
ATOM   2984 N  N     . GLY A 1 423 ? 23.376 0.333   -22.069 1.00 35.54  ? 402 GLY A N     1 
ATOM   2985 C  CA    . GLY A 1 423 ? 23.673 1.771   -21.939 1.00 35.39  ? 402 GLY A CA    1 
ATOM   2986 C  C     . GLY A 1 423 ? 25.053 2.037   -21.364 1.00 36.84  ? 402 GLY A C     1 
ATOM   2987 O  O     . GLY A 1 423 ? 25.394 3.228   -21.222 1.00 43.67  ? 402 GLY A O     1 
ATOM   2988 N  N     . ALA A 1 424 ? 25.832 0.988   -21.048 1.00 36.58  ? 403 ALA A N     1 
ATOM   2989 C  CA    . ALA A 1 424 ? 27.117 1.088   -20.307 1.00 33.99  ? 403 ALA A CA    1 
ATOM   2990 C  C     . ALA A 1 424 ? 28.329 1.163   -21.265 1.00 35.47  ? 403 ALA A C     1 
ATOM   2991 O  O     . ALA A 1 424 ? 29.190 2.062   -21.097 1.00 30.13  ? 403 ALA A O     1 
ATOM   2992 C  CB    . ALA A 1 424 ? 27.208 -0.055  -19.344 1.00 29.90  ? 403 ALA A CB    1 
ATOM   2993 N  N     . TRP A 1 425 ? 28.405 0.262   -22.248 1.00 36.97  ? 404 TRP A N     1 
ATOM   2994 C  CA    . TRP A 1 425 ? 29.540 0.216   -23.201 1.00 33.08  ? 404 TRP A CA    1 
ATOM   2995 C  C     . TRP A 1 425 ? 29.714 1.570   -23.891 1.00 34.73  ? 404 TRP A C     1 
ATOM   2996 O  O     . TRP A 1 425 ? 30.868 2.006   -24.053 1.00 37.99  ? 404 TRP A O     1 
ATOM   2997 C  CB    . TRP A 1 425 ? 29.350 -0.903  -24.216 1.00 32.24  ? 404 TRP A CB    1 
ATOM   2998 C  CG    . TRP A 1 425 ? 30.089 -2.141  -23.836 1.00 32.68  ? 404 TRP A CG    1 
ATOM   2999 C  CD1   . TRP A 1 425 ? 29.575 -3.385  -23.645 1.00 33.97  ? 404 TRP A CD1   1 
ATOM   3000 C  CD2   . TRP A 1 425 ? 31.487 -2.229  -23.526 1.00 31.15  ? 404 TRP A CD2   1 
ATOM   3001 N  NE1   . TRP A 1 425 ? 30.568 -4.251  -23.261 1.00 36.01  ? 404 TRP A NE1   1 
ATOM   3002 C  CE2   . TRP A 1 425 ? 31.752 -3.572  -23.188 1.00 34.71  ? 404 TRP A CE2   1 
ATOM   3003 C  CE3   . TRP A 1 425 ? 32.532 -1.306  -23.493 1.00 28.39  ? 404 TRP A CE3   1 
ATOM   3004 C  CZ2   . TRP A 1 425 ? 33.030 -4.022  -22.851 1.00 35.00  ? 404 TRP A CZ2   1 
ATOM   3005 C  CZ3   . TRP A 1 425 ? 33.785 -1.747  -23.148 1.00 31.22  ? 404 TRP A CZ3   1 
ATOM   3006 C  CH2   . TRP A 1 425 ? 34.033 -3.088  -22.831 1.00 31.26  ? 404 TRP A CH2   1 
ATOM   3007 N  N     . THR A 1 426 ? 28.629 2.192   -24.348 1.00 33.96  ? 405 THR A N     1 
ATOM   3008 C  CA    . THR A 1 426 ? 28.729 3.385   -25.230 1.00 35.39  ? 405 THR A CA    1 
ATOM   3009 C  C     . THR A 1 426 ? 28.959 4.641   -24.387 1.00 35.45  ? 405 THR A C     1 
ATOM   3010 O  O     . THR A 1 426 ? 29.575 5.583   -24.919 1.00 38.21  ? 405 THR A O     1 
ATOM   3011 C  CB    . THR A 1 426 ? 27.521 3.538   -26.166 1.00 36.62  ? 405 THR A CB    1 
ATOM   3012 O  OG1   . THR A 1 426 ? 26.336 3.432   -25.377 1.00 36.26  ? 405 THR A OG1   1 
ATOM   3013 C  CG2   . THR A 1 426 ? 27.520 2.503   -27.278 1.00 34.95  ? 405 THR A CG2   1 
ATOM   3014 N  N     . VAL A 1 427 ? 28.501 4.666   -23.133 1.00 33.94  ? 406 VAL A N     1 
ATOM   3015 C  CA    . VAL A 1 427 ? 28.464 5.914   -22.315 1.00 36.53  ? 406 VAL A CA    1 
ATOM   3016 C  C     . VAL A 1 427 ? 29.673 5.943   -21.364 1.00 36.00  ? 406 VAL A C     1 
ATOM   3017 O  O     . VAL A 1 427 ? 30.383 6.974   -21.337 1.00 41.82  ? 406 VAL A O     1 
ATOM   3018 C  CB    . VAL A 1 427 ? 27.094 6.030   -21.606 1.00 37.25  ? 406 VAL A CB    1 
ATOM   3019 C  CG1   . VAL A 1 427 ? 27.081 7.060   -20.496 1.00 38.50  ? 406 VAL A CG1   1 
ATOM   3020 C  CG2   . VAL A 1 427 ? 25.993 6.331   -22.611 1.00 37.39  ? 406 VAL A CG2   1 
ATOM   3021 N  N     . TYR A 1 428 ? 29.922 4.849   -20.647 1.00 33.41  ? 407 TYR A N     1 
ATOM   3022 C  CA    . TYR A 1 428 ? 30.994 4.714   -19.626 1.00 30.81  ? 407 TYR A CA    1 
ATOM   3023 C  C     . TYR A 1 428 ? 32.170 3.894   -20.177 1.00 29.77  ? 407 TYR A C     1 
ATOM   3024 O  O     . TYR A 1 428 ? 33.277 4.087   -19.677 1.00 30.08  ? 407 TYR A O     1 
ATOM   3025 C  CB    . TYR A 1 428 ? 30.417 4.092   -18.343 1.00 32.13  ? 407 TYR A CB    1 
ATOM   3026 C  CG    . TYR A 1 428 ? 29.188 4.800   -17.822 1.00 32.65  ? 407 TYR A CG    1 
ATOM   3027 C  CD1   . TYR A 1 428 ? 29.268 6.001   -17.110 1.00 33.41  ? 407 TYR A CD1   1 
ATOM   3028 C  CD2   . TYR A 1 428 ? 27.926 4.308   -18.102 1.00 32.90  ? 407 TYR A CD2   1 
ATOM   3029 C  CE1   . TYR A 1 428 ? 28.130 6.659   -16.657 1.00 32.20  ? 407 TYR A CE1   1 
ATOM   3030 C  CE2   . TYR A 1 428 ? 26.782 4.963   -17.675 1.00 35.76  ? 407 TYR A CE2   1 
ATOM   3031 C  CZ    . TYR A 1 428 ? 26.875 6.137   -16.938 1.00 35.83  ? 407 TYR A CZ    1 
ATOM   3032 O  OH    . TYR A 1 428 ? 25.715 6.769   -16.560 1.00 37.15  ? 407 TYR A OH    1 
ATOM   3033 N  N     . GLY A 1 429 ? 31.953 3.017   -21.158 1.00 28.97  ? 408 GLY A N     1 
ATOM   3034 C  CA    . GLY A 1 429 ? 32.948 2.036   -21.656 1.00 30.77  ? 408 GLY A CA    1 
ATOM   3035 C  C     . GLY A 1 429 ? 34.277 2.643   -22.118 1.00 31.92  ? 408 GLY A C     1 
ATOM   3036 O  O     . GLY A 1 429 ? 35.333 2.024   -21.931 1.00 29.37  ? 408 GLY A O     1 
ATOM   3037 N  N     . PRO A 1 430 ? 34.294 3.828   -22.783 1.00 33.11  ? 409 PRO A N     1 
ATOM   3038 C  CA    . PRO A 1 430 ? 35.541 4.371   -23.332 1.00 32.08  ? 409 PRO A CA    1 
ATOM   3039 C  C     . PRO A 1 430 ? 36.643 4.587   -22.278 1.00 30.93  ? 409 PRO A C     1 
ATOM   3040 O  O     . PRO A 1 430 ? 37.771 4.632   -22.682 1.00 37.77  ? 409 PRO A O     1 
ATOM   3041 C  CB    . PRO A 1 430 ? 35.119 5.688   -24.017 1.00 31.98  ? 409 PRO A CB    1 
ATOM   3042 C  CG    . PRO A 1 430 ? 33.637 5.508   -24.302 1.00 32.58  ? 409 PRO A CG    1 
ATOM   3043 C  CD    . PRO A 1 430 ? 33.120 4.630   -23.181 1.00 34.45  ? 409 PRO A CD    1 
ATOM   3044 N  N     . ALA A 1 431 ? 36.316 4.701   -20.980 1.00 30.74  ? 410 ALA A N     1 
ATOM   3045 C  CA    . ALA A 1 431 ? 37.314 4.815   -19.888 1.00 33.36  ? 410 ALA A CA    1 
ATOM   3046 C  C     . ALA A 1 431 ? 37.903 3.450   -19.432 1.00 31.93  ? 410 ALA A C     1 
ATOM   3047 O  O     . ALA A 1 431 ? 38.738 3.486   -18.518 1.00 33.50  ? 410 ALA A O     1 
ATOM   3048 C  CB    . ALA A 1 431 ? 36.708 5.569   -18.733 1.00 33.00  ? 410 ALA A CB    1 
ATOM   3049 N  N     . LEU A 1 432 ? 37.527 2.298   -20.016 1.00 31.93  ? 411 LEU A N     1 
ATOM   3050 C  CA    . LEU A 1 432 ? 37.946 0.941   -19.525 1.00 32.94  ? 411 LEU A CA    1 
ATOM   3051 C  C     . LEU A 1 432 ? 39.477 0.837   -19.367 1.00 32.95  ? 411 LEU A C     1 
ATOM   3052 O  O     . LEU A 1 432 ? 39.900 0.395   -18.305 1.00 36.69  ? 411 LEU A O     1 
ATOM   3053 C  CB    . LEU A 1 432 ? 37.426 -0.127  -20.487 1.00 33.59  ? 411 LEU A CB    1 
ATOM   3054 C  CG    . LEU A 1 432 ? 37.853 -1.571  -20.203 1.00 36.93  ? 411 LEU A CG    1 
ATOM   3055 C  CD1   . LEU A 1 432 ? 37.301 -2.074  -18.884 1.00 38.00  ? 411 LEU A CD1   1 
ATOM   3056 C  CD2   . LEU A 1 432 ? 37.423 -2.488  -21.337 1.00 36.24  ? 411 LEU A CD2   1 
ATOM   3057 N  N     . ARG A 1 433 ? 40.271 1.269   -20.356 1.00 34.96  ? 412 ARG A N     1 
ATOM   3058 C  CA    . ARG A 1 433 ? 41.743 1.036   -20.435 1.00 40.00  ? 412 ARG A CA    1 
ATOM   3059 C  C     . ARG A 1 433 ? 42.533 2.334   -20.262 1.00 41.22  ? 412 ARG A C     1 
ATOM   3060 O  O     . ARG A 1 433 ? 43.765 2.245   -20.091 1.00 44.77  ? 412 ARG A O     1 
ATOM   3061 C  CB    . ARG A 1 433 ? 42.132 0.384   -21.771 1.00 42.75  ? 412 ARG A CB    1 
ATOM   3062 C  CG    . ARG A 1 433 ? 42.230 -1.135  -21.706 1.00 48.25  ? 412 ARG A CG    1 
ATOM   3063 C  CD    . ARG A 1 433 ? 42.665 -1.786  -23.003 1.00 44.05  ? 412 ARG A CD    1 
ATOM   3064 N  NE    . ARG A 1 433 ? 41.745 -1.351  -24.028 1.00 50.53  ? 412 ARG A NE    1 
ATOM   3065 C  CZ    . ARG A 1 433 ? 40.612 -1.949  -24.360 1.00 49.25  ? 412 ARG A CZ    1 
ATOM   3066 N  NH1   . ARG A 1 433 ? 40.223 -3.061  -23.764 1.00 48.10  ? 412 ARG A NH1   1 
ATOM   3067 N  NH2   . ARG A 1 433 ? 39.883 -1.437  -25.328 1.00 52.67  ? 412 ARG A NH2   1 
ATOM   3068 N  N     . VAL A 1 434 ? 41.886 3.496   -20.300 1.00 40.01  ? 413 VAL A N     1 
ATOM   3069 C  CA    . VAL A 1 434 ? 42.607 4.801   -20.295 1.00 37.76  ? 413 VAL A CA    1 
ATOM   3070 C  C     . VAL A 1 434 ? 43.311 4.952   -18.943 1.00 40.41  ? 413 VAL A C     1 
ATOM   3071 O  O     . VAL A 1 434 ? 42.680 4.925   -17.884 1.00 39.57  ? 413 VAL A O     1 
ATOM   3072 C  CB    . VAL A 1 434 ? 41.651 5.966   -20.631 1.00 38.43  ? 413 VAL A CB    1 
ATOM   3073 C  CG1   . VAL A 1 434 ? 42.318 7.337   -20.527 1.00 35.73  ? 413 VAL A CG1   1 
ATOM   3074 C  CG2   . VAL A 1 434 ? 41.063 5.770   -22.019 1.00 39.59  ? 413 VAL A CG2   1 
ATOM   3075 N  N     . PRO A 1 435 ? 44.658 5.084   -18.914 1.00 40.54  ? 414 PRO A N     1 
ATOM   3076 C  CA    . PRO A 1 435 ? 45.361 5.287   -17.647 1.00 40.18  ? 414 PRO A CA    1 
ATOM   3077 C  C     . PRO A 1 435 ? 44.910 6.610   -17.002 1.00 39.68  ? 414 PRO A C     1 
ATOM   3078 O  O     . PRO A 1 435 ? 44.558 7.525   -17.719 1.00 38.31  ? 414 PRO A O     1 
ATOM   3079 C  CB    . PRO A 1 435 ? 46.858 5.291   -18.007 1.00 41.10  ? 414 PRO A CB    1 
ATOM   3080 C  CG    . PRO A 1 435 ? 46.917 5.497   -19.516 1.00 44.21  ? 414 PRO A CG    1 
ATOM   3081 C  CD    . PRO A 1 435 ? 45.569 5.065   -20.074 1.00 42.80  ? 414 PRO A CD    1 
ATOM   3082 N  N     . VAL A 1 436 ? 44.869 6.650   -15.671 1.00 34.82  ? 415 VAL A N     1 
ATOM   3083 C  CA    . VAL A 1 436 ? 44.545 7.874   -14.893 1.00 34.08  ? 415 VAL A CA    1 
ATOM   3084 C  C     . VAL A 1 436 ? 45.851 8.343   -14.250 1.00 33.00  ? 415 VAL A C     1 
ATOM   3085 O  O     . VAL A 1 436 ? 46.204 7.798   -13.167 1.00 31.17  ? 415 VAL A O     1 
ATOM   3086 C  CB    . VAL A 1 436 ? 43.439 7.632   -13.853 1.00 34.54  ? 415 VAL A CB    1 
ATOM   3087 C  CG1   . VAL A 1 436 ? 43.178 8.907   -13.052 1.00 34.81  ? 415 VAL A CG1   1 
ATOM   3088 C  CG2   . VAL A 1 436 ? 42.149 7.107   -14.484 1.00 32.43  ? 415 VAL A CG2   1 
ATOM   3089 N  N     . GLY A 1 437 ? 46.561 9.235   -14.960 1.00 30.02  ? 416 GLY A N     1 
ATOM   3090 C  CA    . GLY A 1 437 ? 47.920 9.725   -14.630 1.00 32.87  ? 416 GLY A CA    1 
ATOM   3091 C  C     . GLY A 1 437 ? 48.957 8.602   -14.609 1.00 29.30  ? 416 GLY A C     1 
ATOM   3092 O  O     . GLY A 1 437 ? 49.312 8.100   -15.676 1.00 30.52  ? 416 GLY A O     1 
ATOM   3093 N  N     . ARG A 1 438 ? 49.426 8.231   -13.426 1.00 29.97  ? 417 ARG A N     1 
ATOM   3094 C  CA    . ARG A 1 438 ? 50.441 7.168   -13.203 1.00 30.83  ? 417 ARG A CA    1 
ATOM   3095 C  C     . ARG A 1 438 ? 49.752 5.828   -12.900 1.00 32.35  ? 417 ARG A C     1 
ATOM   3096 O  O     . ARG A 1 438 ? 50.470 4.850   -12.619 1.00 33.75  ? 417 ARG A O     1 
ATOM   3097 C  CB    . ARG A 1 438 ? 51.365 7.606   -12.065 1.00 32.67  ? 417 ARG A CB    1 
ATOM   3098 C  CG    . ARG A 1 438 ? 52.199 8.830   -12.422 1.00 35.07  ? 417 ARG A CG    1 
ATOM   3099 C  CD    . ARG A 1 438 ? 52.918 9.482   -11.260 1.00 35.90  ? 417 ARG A CD    1 
ATOM   3100 N  NE    . ARG A 1 438 ? 53.911 10.412  -11.764 1.00 34.44  ? 417 ARG A NE    1 
ATOM   3101 C  CZ    . ARG A 1 438 ? 55.081 10.042  -12.281 1.00 37.76  ? 417 ARG A CZ    1 
ATOM   3102 N  NH1   . ARG A 1 438 ? 55.435 8.772   -12.314 1.00 40.77  ? 417 ARG A NH1   1 
ATOM   3103 N  NH2   . ARG A 1 438 ? 55.920 10.945  -12.736 1.00 40.02  ? 417 ARG A NH2   1 
ATOM   3104 N  N     . VAL A 1 439 ? 48.418 5.736   -12.970 1.00 32.02  ? 418 VAL A N     1 
ATOM   3105 C  CA    . VAL A 1 439 ? 47.709 4.472   -12.605 1.00 29.62  ? 418 VAL A CA    1 
ATOM   3106 C  C     . VAL A 1 439 ? 47.205 3.832   -13.901 1.00 32.92  ? 418 VAL A C     1 
ATOM   3107 O  O     . VAL A 1 439 ? 46.375 4.453   -14.604 1.00 31.07  ? 418 VAL A O     1 
ATOM   3108 C  CB    . VAL A 1 439 ? 46.576 4.713   -11.590 1.00 28.63  ? 418 VAL A CB    1 
ATOM   3109 C  CG1   . VAL A 1 439 ? 45.882 3.428   -11.213 1.00 28.25  ? 418 VAL A CG1   1 
ATOM   3110 C  CG2   . VAL A 1 439 ? 47.069 5.389   -10.329 1.00 29.42  ? 418 VAL A CG2   1 
ATOM   3111 N  N     . HIS A 1 440 ? 47.718 2.642   -14.209 1.00 33.43  ? 419 HIS A N     1 
ATOM   3112 C  CA    . HIS A 1 440 ? 47.360 1.844   -15.404 1.00 32.68  ? 419 HIS A CA    1 
ATOM   3113 C  C     . HIS A 1 440 ? 46.441 0.709   -14.938 1.00 33.15  ? 419 HIS A C     1 
ATOM   3114 O  O     . HIS A 1 440 ? 46.423 0.452   -13.700 1.00 31.51  ? 419 HIS A O     1 
ATOM   3115 C  CB    . HIS A 1 440 ? 48.648 1.380   -16.094 1.00 35.27  ? 419 HIS A CB    1 
ATOM   3116 C  CG    . HIS A 1 440 ? 49.452 2.492   -16.670 1.00 33.44  ? 419 HIS A CG    1 
ATOM   3117 N  ND1   . HIS A 1 440 ? 50.236 3.322   -15.886 1.00 41.50  ? 419 HIS A ND1   1 
ATOM   3118 C  CD2   . HIS A 1 440 ? 49.650 2.873   -17.947 1.00 33.78  ? 419 HIS A CD2   1 
ATOM   3119 C  CE1   . HIS A 1 440 ? 50.856 4.201   -16.654 1.00 41.83  ? 419 HIS A CE1   1 
ATOM   3120 N  NE2   . HIS A 1 440 ? 50.509 3.948   -17.927 1.00 39.40  ? 419 HIS A NE2   1 
ATOM   3121 N  N     . TRP A 1 441 ? 45.694 0.094   -15.868 1.00 34.75  ? 420 TRP A N     1 
ATOM   3122 C  CA    . TRP A 1 441 ? 44.587 -0.873  -15.598 1.00 35.18  ? 420 TRP A CA    1 
ATOM   3123 C  C     . TRP A 1 441 ? 44.893 -2.194  -16.291 1.00 34.47  ? 420 TRP A C     1 
ATOM   3124 O  O     . TRP A 1 441 ? 45.291 -2.175  -17.452 1.00 37.42  ? 420 TRP A O     1 
ATOM   3125 C  CB    . TRP A 1 441 ? 43.222 -0.333  -16.065 1.00 36.37  ? 420 TRP A CB    1 
ATOM   3126 C  CG    . TRP A 1 441 ? 42.972 1.035   -15.533 1.00 34.53  ? 420 TRP A CG    1 
ATOM   3127 C  CD1   . TRP A 1 441 ? 43.092 2.208   -16.206 1.00 34.35  ? 420 TRP A CD1   1 
ATOM   3128 C  CD2   . TRP A 1 441 ? 42.695 1.375   -14.168 1.00 32.51  ? 420 TRP A CD2   1 
ATOM   3129 N  NE1   . TRP A 1 441 ? 42.858 3.258   -15.358 1.00 33.39  ? 420 TRP A NE1   1 
ATOM   3130 C  CE2   . TRP A 1 441 ? 42.644 2.781   -14.097 1.00 33.19  ? 420 TRP A CE2   1 
ATOM   3131 C  CE3   . TRP A 1 441 ? 42.478 0.638   -13.003 1.00 34.37  ? 420 TRP A CE3   1 
ATOM   3132 C  CZ2   . TRP A 1 441 ? 42.357 3.462   -12.912 1.00 33.05  ? 420 TRP A CZ2   1 
ATOM   3133 C  CZ3   . TRP A 1 441 ? 42.216 1.311   -11.825 1.00 35.91  ? 420 TRP A CZ3   1 
ATOM   3134 C  CH2   . TRP A 1 441 ? 42.156 2.706   -11.781 1.00 35.16  ? 420 TRP A CH2   1 
ATOM   3135 N  N     . ALA A 1 442 ? 44.657 -3.304  -15.619 1.00 30.70  ? 421 ALA A N     1 
ATOM   3136 C  CA    . ALA A 1 442 ? 44.764 -4.638  -16.237 1.00 31.24  ? 421 ALA A CA    1 
ATOM   3137 C  C     . ALA A 1 442 ? 43.677 -5.517  -15.633 1.00 32.37  ? 421 ALA A C     1 
ATOM   3138 O  O     . ALA A 1 442 ? 42.909 -5.008  -14.803 1.00 29.08  ? 421 ALA A O     1 
ATOM   3139 C  CB    . ALA A 1 442 ? 46.143 -5.197  -15.982 1.00 30.34  ? 421 ALA A CB    1 
ATOM   3140 N  N     . GLY A 1 443 ? 43.725 -6.812  -15.943 1.00 33.53  ? 422 GLY A N     1 
ATOM   3141 C  CA    . GLY A 1 443 ? 42.701 -7.798  -15.555 1.00 29.45  ? 422 GLY A CA    1 
ATOM   3142 C  C     . GLY A 1 443 ? 41.961 -8.244  -16.790 1.00 27.28  ? 422 GLY A C     1 
ATOM   3143 O  O     . GLY A 1 443 ? 41.916 -7.459  -17.766 1.00 26.69  ? 422 GLY A O     1 
ATOM   3144 N  N     . THR A 1 444 ? 41.418 -9.459  -16.775 1.00 26.85  ? 423 THR A N     1 
ATOM   3145 C  CA    . THR A 1 444 ? 40.845 -10.104 -17.983 1.00 27.46  ? 423 THR A CA    1 
ATOM   3146 C  C     . THR A 1 444 ? 39.747 -9.222  -18.594 1.00 28.51  ? 423 THR A C     1 
ATOM   3147 O  O     . THR A 1 444 ? 39.499 -9.301  -19.827 1.00 28.58  ? 423 THR A O     1 
ATOM   3148 C  CB    . THR A 1 444 ? 40.351 -11.510 -17.640 1.00 26.10  ? 423 THR A CB    1 
ATOM   3149 O  OG1   . THR A 1 444 ? 40.037 -12.089 -18.899 1.00 24.81  ? 423 THR A OG1   1 
ATOM   3150 C  CG2   . THR A 1 444 ? 39.139 -11.510 -16.737 1.00 28.20  ? 423 THR A CG2   1 
ATOM   3151 N  N     . GLU A 1 445 ? 39.093 -8.404  -17.777 1.00 32.13  ? 424 GLU A N     1 
ATOM   3152 C  CA    . GLU A 1 445 ? 38.038 -7.462  -18.246 1.00 33.88  ? 424 GLU A CA    1 
ATOM   3153 C  C     . GLU A 1 445 ? 38.617 -6.388  -19.189 1.00 34.14  ? 424 GLU A C     1 
ATOM   3154 O  O     . GLU A 1 445 ? 37.806 -5.792  -19.927 1.00 37.99  ? 424 GLU A O     1 
ATOM   3155 C  CB    . GLU A 1 445 ? 37.324 -6.835  -17.046 1.00 33.87  ? 424 GLU A CB    1 
ATOM   3156 C  CG    . GLU A 1 445 ? 36.391 -7.790  -16.334 1.00 34.33  ? 424 GLU A CG    1 
ATOM   3157 C  CD    . GLU A 1 445 ? 36.980 -8.795  -15.343 1.00 41.99  ? 424 GLU A CD    1 
ATOM   3158 O  OE1   . GLU A 1 445 ? 38.213 -8.692  -14.962 1.00 41.70  ? 424 GLU A OE1   1 
ATOM   3159 O  OE2   . GLU A 1 445 ? 36.199 -9.701  -14.941 1.00 40.18  ? 424 GLU A OE2   1 
ATOM   3160 N  N     . THR A 1 446 ? 39.928 -6.125  -19.201 1.00 32.15  ? 425 THR A N     1 
ATOM   3161 C  CA    . THR A 1 446 ? 40.543 -5.142  -20.146 1.00 33.58  ? 425 THR A CA    1 
ATOM   3162 C  C     . THR A 1 446 ? 41.133 -5.802  -21.409 1.00 32.83  ? 425 THR A C     1 
ATOM   3163 O  O     . THR A 1 446 ? 41.580 -5.070  -22.312 1.00 31.21  ? 425 THR A O     1 
ATOM   3164 C  CB    . THR A 1 446 ? 41.610 -4.307  -19.449 1.00 32.80  ? 425 THR A CB    1 
ATOM   3165 O  OG1   . THR A 1 446 ? 42.621 -5.227  -19.050 1.00 34.04  ? 425 THR A OG1   1 
ATOM   3166 C  CG2   . THR A 1 446 ? 41.047 -3.509  -18.296 1.00 35.33  ? 425 THR A CG2   1 
ATOM   3167 N  N     . ALA A 1 447 ? 41.137 -7.124  -21.489 1.00 33.68  ? 426 ALA A N     1 
ATOM   3168 C  CA    . ALA A 1 447 ? 41.589 -7.894  -22.667 1.00 34.98  ? 426 ALA A CA    1 
ATOM   3169 C  C     . ALA A 1 447 ? 40.725 -7.571  -23.912 1.00 36.41  ? 426 ALA A C     1 
ATOM   3170 O  O     . ALA A 1 447 ? 39.537 -7.230  -23.774 1.00 41.89  ? 426 ALA A O     1 
ATOM   3171 C  CB    . ALA A 1 447 ? 41.546 -9.364  -22.331 1.00 35.52  ? 426 ALA A CB    1 
ATOM   3172 N  N     . GLU A 1 448 ? 41.344 -7.661  -25.093 1.00 35.25  ? 427 GLU A N     1 
ATOM   3173 C  CA    . GLU A 1 448 ? 40.729 -7.634  -26.438 1.00 37.12  ? 427 GLU A CA    1 
ATOM   3174 C  C     . GLU A 1 448 ? 40.421 -9.063  -26.899 1.00 40.53  ? 427 GLU A C     1 
ATOM   3175 O  O     . GLU A 1 448 ? 39.343 -9.250  -27.502 1.00 45.94  ? 427 GLU A O     1 
ATOM   3176 C  CB    . GLU A 1 448 ? 41.676 -6.912  -27.385 1.00 39.53  ? 427 GLU A CB    1 
ATOM   3177 C  CG    . GLU A 1 448 ? 41.638 -5.415  -27.165 1.00 46.80  ? 427 GLU A CG    1 
ATOM   3178 C  CD    . GLU A 1 448 ? 42.824 -4.633  -27.702 1.00 54.43  ? 427 GLU A CD    1 
ATOM   3179 O  OE1   . GLU A 1 448 ? 42.986 -4.571  -28.950 1.00 55.73  ? 427 GLU A OE1   1 
ATOM   3180 O  OE2   . GLU A 1 448 ? 43.573 -4.077  -26.862 1.00 64.40  ? 427 GLU A OE2   1 
ATOM   3181 N  N     . ARG A 1 449 ? 41.298 -10.037 -26.612 1.00 37.72  ? 428 ARG A N     1 
ATOM   3182 C  CA    . ARG A 1 449 ? 41.096 -11.457 -27.019 1.00 36.79  ? 428 ARG A CA    1 
ATOM   3183 C  C     . ARG A 1 449 ? 40.898 -12.323 -25.771 1.00 32.34  ? 428 ARG A C     1 
ATOM   3184 O  O     . ARG A 1 449 ? 41.687 -12.229 -24.820 1.00 28.79  ? 428 ARG A O     1 
ATOM   3185 C  CB    . ARG A 1 449 ? 42.247 -11.994 -27.886 1.00 37.16  ? 428 ARG A CB    1 
ATOM   3186 C  CG    . ARG A 1 449 ? 42.183 -11.557 -29.339 1.00 43.59  ? 428 ARG A CG    1 
ATOM   3187 C  CD    . ARG A 1 449 ? 43.143 -12.313 -30.240 1.00 44.49  ? 428 ARG A CD    1 
ATOM   3188 N  NE    . ARG A 1 449 ? 42.678 -13.687 -30.414 1.00 43.39  ? 428 ARG A NE    1 
ATOM   3189 C  CZ    . ARG A 1 449 ? 43.266 -14.770 -29.909 1.00 41.35  ? 428 ARG A CZ    1 
ATOM   3190 N  NH1   . ARG A 1 449 ? 42.738 -15.970 -30.107 1.00 42.40  ? 428 ARG A NH1   1 
ATOM   3191 N  NH2   . ARG A 1 449 ? 44.376 -14.660 -29.204 1.00 44.16  ? 428 ARG A NH2   1 
ATOM   3192 N  N     . TRP A 1 450 ? 39.879 -13.173 -25.817 1.00 31.94  ? 429 TRP A N     1 
ATOM   3193 C  CA    . TRP A 1 450 ? 39.492 -14.088 -24.719 1.00 29.31  ? 429 TRP A CA    1 
ATOM   3194 C  C     . TRP A 1 450 ? 39.249 -13.294 -23.429 1.00 27.74  ? 429 TRP A C     1 
ATOM   3195 O  O     . TRP A 1 450 ? 39.642 -13.753 -22.333 1.00 25.33  ? 429 TRP A O     1 
ATOM   3196 C  CB    . TRP A 1 450 ? 40.570 -15.166 -24.621 1.00 28.12  ? 429 TRP A CB    1 
ATOM   3197 C  CG    . TRP A 1 450 ? 40.391 -16.186 -25.701 1.00 29.64  ? 429 TRP A CG    1 
ATOM   3198 C  CD1   . TRP A 1 450 ? 41.137 -16.320 -26.836 1.00 32.02  ? 429 TRP A CD1   1 
ATOM   3199 C  CD2   . TRP A 1 450 ? 39.373 -17.199 -25.778 1.00 31.84  ? 429 TRP A CD2   1 
ATOM   3200 N  NE1   . TRP A 1 450 ? 40.678 -17.367 -27.588 1.00 30.87  ? 429 TRP A NE1   1 
ATOM   3201 C  CE2   . TRP A 1 450 ? 39.591 -17.915 -26.975 1.00 28.87  ? 429 TRP A CE2   1 
ATOM   3202 C  CE3   . TRP A 1 450 ? 38.307 -17.588 -24.950 1.00 34.32  ? 429 TRP A CE3   1 
ATOM   3203 C  CZ2   . TRP A 1 450 ? 38.803 -18.997 -27.347 1.00 28.57  ? 429 TRP A CZ2   1 
ATOM   3204 C  CZ3   . TRP A 1 450 ? 37.515 -18.655 -25.331 1.00 31.68  ? 429 TRP A CZ3   1 
ATOM   3205 C  CH2   . TRP A 1 450 ? 37.759 -19.341 -26.516 1.00 29.40  ? 429 TRP A CH2   1 
ATOM   3206 N  N     . THR A 1 451 ? 38.600 -12.127 -23.545 1.00 28.23  ? 430 THR A N     1 
ATOM   3207 C  CA    . THR A 1 451 ? 38.138 -11.358 -22.362 1.00 27.56  ? 430 THR A CA    1 
ATOM   3208 C  C     . THR A 1 451 ? 37.278 -12.300 -21.537 1.00 26.35  ? 430 THR A C     1 
ATOM   3209 O  O     . THR A 1 451 ? 36.428 -13.000 -22.121 1.00 26.15  ? 430 THR A O     1 
ATOM   3210 C  CB    . THR A 1 451 ? 37.412 -10.049 -22.724 1.00 31.19  ? 430 THR A CB    1 
ATOM   3211 O  OG1   . THR A 1 451 ? 37.305 -9.309  -21.513 1.00 28.86  ? 430 THR A OG1   1 
ATOM   3212 C  CG2   . THR A 1 451 ? 36.025 -10.239 -23.299 1.00 32.15  ? 430 THR A CG2   1 
ATOM   3213 N  N     . GLY A 1 452 ? 37.558 -12.389 -20.245 1.00 26.13  ? 431 GLY A N     1 
ATOM   3214 C  CA    . GLY A 1 452 ? 36.790 -13.242 -19.319 1.00 27.10  ? 431 GLY A CA    1 
ATOM   3215 C  C     . GLY A 1 452 ? 37.487 -14.569 -19.049 1.00 27.59  ? 431 GLY A C     1 
ATOM   3216 O  O     . GLY A 1 452 ? 36.960 -15.361 -18.222 1.00 30.89  ? 431 GLY A O     1 
ATOM   3217 N  N     . TYR A 1 453 ? 38.644 -14.813 -19.670 1.00 28.58  ? 432 TYR A N     1 
ATOM   3218 C  CA    . TYR A 1 453 ? 39.414 -16.090 -19.515 1.00 28.56  ? 432 TYR A CA    1 
ATOM   3219 C  C     . TYR A 1 453 ? 40.830 -15.818 -19.001 1.00 26.31  ? 432 TYR A C     1 
ATOM   3220 O  O     . TYR A 1 453 ? 41.275 -14.627 -18.923 1.00 23.46  ? 432 TYR A O     1 
ATOM   3221 C  CB    . TYR A 1 453 ? 39.433 -16.856 -20.836 1.00 27.72  ? 432 TYR A CB    1 
ATOM   3222 C  CG    . TYR A 1 453 ? 38.083 -17.354 -21.264 1.00 26.73  ? 432 TYR A CG    1 
ATOM   3223 C  CD1   . TYR A 1 453 ? 37.177 -16.496 -21.865 1.00 32.56  ? 432 TYR A CD1   1 
ATOM   3224 C  CD2   . TYR A 1 453 ? 37.688 -18.657 -21.044 1.00 26.33  ? 432 TYR A CD2   1 
ATOM   3225 C  CE1   . TYR A 1 453 ? 35.913 -16.923 -22.245 1.00 27.52  ? 432 TYR A CE1   1 
ATOM   3226 C  CE2   . TYR A 1 453 ? 36.426 -19.097 -21.405 1.00 28.00  ? 432 TYR A CE2   1 
ATOM   3227 C  CZ    . TYR A 1 453 ? 35.540 -18.232 -22.034 1.00 26.56  ? 432 TYR A CZ    1 
ATOM   3228 O  OH    . TYR A 1 453 ? 34.273 -18.635 -22.384 1.00 24.78  ? 432 TYR A OH    1 
ATOM   3229 N  N     . ILE A 1 454 ? 41.496 -16.893 -18.588 1.00 24.93  ? 433 ILE A N     1 
ATOM   3230 C  CA    . ILE A 1 454 ? 42.930 -16.869 -18.145 1.00 28.03  ? 433 ILE A CA    1 
ATOM   3231 C  C     . ILE A 1 454 ? 43.762 -16.227 -19.270 1.00 27.73  ? 433 ILE A C     1 
ATOM   3232 O  O     . ILE A 1 454 ? 44.601 -15.333 -18.962 1.00 25.81  ? 433 ILE A O     1 
ATOM   3233 C  CB    . ILE A 1 454 ? 43.428 -18.281 -17.757 1.00 29.91  ? 433 ILE A CB    1 
ATOM   3234 C  CG1   . ILE A 1 454 ? 42.574 -18.906 -16.647 1.00 33.41  ? 433 ILE A CG1   1 
ATOM   3235 C  CG2   . ILE A 1 454 ? 44.900 -18.276 -17.364 1.00 28.41  ? 433 ILE A CG2   1 
ATOM   3236 C  CD1   . ILE A 1 454 ? 42.613 -20.425 -16.596 1.00 35.80  ? 433 ILE A CD1   1 
ATOM   3237 N  N     . ASP A 1 455 ? 43.551 -16.667 -20.525 1.00 27.40  ? 434 ASP A N     1 
ATOM   3238 C  CA    . ASP A 1 455 ? 44.253 -16.162 -21.732 1.00 27.78  ? 434 ASP A CA    1 
ATOM   3239 C  C     . ASP A 1 455 ? 44.159 -14.638 -21.800 1.00 29.04  ? 434 ASP A C     1 
ATOM   3240 O  O     . ASP A 1 455 ? 45.181 -14.015 -22.086 1.00 30.69  ? 434 ASP A O     1 
ATOM   3241 C  CB    . ASP A 1 455 ? 43.653 -16.698 -23.024 1.00 30.42  ? 434 ASP A CB    1 
ATOM   3242 C  CG    . ASP A 1 455 ? 44.616 -16.684 -24.201 1.00 31.11  ? 434 ASP A CG    1 
ATOM   3243 O  OD1   . ASP A 1 455 ? 45.666 -17.382 -24.123 1.00 34.92  ? 434 ASP A OD1   1 
ATOM   3244 O  OD2   . ASP A 1 455 ? 44.310 -16.007 -25.188 1.00 35.33  ? 434 ASP A OD2   1 
ATOM   3245 N  N     . GLY A 1 456 ? 42.971 -14.085 -21.548 1.00 26.76  ? 435 GLY A N     1 
ATOM   3246 C  CA    . GLY A 1 456 ? 42.721 -12.637 -21.524 1.00 28.15  ? 435 GLY A CA    1 
ATOM   3247 C  C     . GLY A 1 456 ? 43.402 -11.950 -20.358 1.00 26.70  ? 435 GLY A C     1 
ATOM   3248 O  O     . GLY A 1 456 ? 43.835 -10.773 -20.518 1.00 28.16  ? 435 GLY A O     1 
ATOM   3249 N  N     . ALA A 1 457 ? 43.515 -12.624 -19.220 1.00 26.15  ? 436 ALA A N     1 
ATOM   3250 C  CA    . ALA A 1 457 ? 44.208 -12.057 -18.039 1.00 30.01  ? 436 ALA A CA    1 
ATOM   3251 C  C     . ALA A 1 457 ? 45.672 -11.774 -18.435 1.00 33.15  ? 436 ALA A C     1 
ATOM   3252 O  O     . ALA A 1 457 ? 46.196 -10.580 -18.297 1.00 29.86  ? 436 ALA A O     1 
ATOM   3253 C  CB    . ALA A 1 457 ? 44.050 -12.992 -16.853 1.00 31.03  ? 436 ALA A CB    1 
ATOM   3254 N  N     . ILE A 1 458 ? 46.285 -12.792 -19.044 1.00 32.17  ? 437 ILE A N     1 
ATOM   3255 C  CA    . ILE A 1 458 ? 47.683 -12.738 -19.543 1.00 30.30  ? 437 ILE A CA    1 
ATOM   3256 C  C     . ILE A 1 458 ? 47.824 -11.614 -20.578 1.00 29.76  ? 437 ILE A C     1 
ATOM   3257 O  O     . ILE A 1 458 ? 48.742 -10.816 -20.420 1.00 27.95  ? 437 ILE A O     1 
ATOM   3258 C  CB    . ILE A 1 458 ? 48.143 -14.099 -20.066 1.00 29.78  ? 437 ILE A CB    1 
ATOM   3259 C  CG1   . ILE A 1 458 ? 48.067 -15.151 -18.957 1.00 28.90  ? 437 ILE A CG1   1 
ATOM   3260 C  CG2   . ILE A 1 458 ? 49.549 -13.971 -20.653 1.00 31.87  ? 437 ILE A CG2   1 
ATOM   3261 C  CD1   . ILE A 1 458 ? 48.128 -16.579 -19.446 1.00 29.63  ? 437 ILE A CD1   1 
ATOM   3262 N  N     . GLU A 1 459 ? 46.964 -11.522 -21.586 1.00 31.73  ? 438 GLU A N     1 
ATOM   3263 C  CA    . GLU A 1 459 ? 47.065 -10.409 -22.564 1.00 33.42  ? 438 GLU A CA    1 
ATOM   3264 C  C     . GLU A 1 459 ? 47.041 -9.058  -21.835 1.00 29.96  ? 438 GLU A C     1 
ATOM   3265 O  O     . GLU A 1 459 ? 47.832 -8.190  -22.178 1.00 32.58  ? 438 GLU A O     1 
ATOM   3266 C  CB    . GLU A 1 459 ? 45.922 -10.400 -23.575 1.00 38.21  ? 438 GLU A CB    1 
ATOM   3267 C  CG    . GLU A 1 459 ? 45.990 -9.184  -24.503 1.00 42.15  ? 438 GLU A CG    1 
ATOM   3268 C  CD    . GLU A 1 459 ? 44.668 -8.810  -25.149 1.00 46.97  ? 438 GLU A CD    1 
ATOM   3269 O  OE1   . GLU A 1 459 ? 44.035 -9.737  -25.701 1.00 46.06  ? 438 GLU A OE1   1 
ATOM   3270 O  OE2   . GLU A 1 459 ? 44.277 -7.589  -25.104 1.00 44.10  ? 438 GLU A OE2   1 
ATOM   3271 N  N     . SER A 1 460 ? 46.147 -8.870  -20.875 1.00 29.95  ? 439 SER A N     1 
ATOM   3272 C  CA    . SER A 1 460 ? 45.981 -7.572  -20.170 1.00 29.38  ? 439 SER A CA    1 
ATOM   3273 C  C     . SER A 1 460 ? 47.288 -7.202  -19.449 1.00 30.00  ? 439 SER A C     1 
ATOM   3274 O  O     . SER A 1 460 ? 47.686 -5.986  -19.487 1.00 28.92  ? 439 SER A O     1 
ATOM   3275 C  CB    . SER A 1 460 ? 44.801 -7.608  -19.249 1.00 28.82  ? 439 SER A CB    1 
ATOM   3276 O  OG    . SER A 1 460 ? 45.099 -8.351  -18.085 1.00 30.44  ? 439 SER A OG    1 
ATOM   3277 N  N     . GLY A 1 461 ? 47.942 -8.190  -18.830 1.00 29.05  ? 440 GLY A N     1 
ATOM   3278 C  CA    . GLY A 1 461 ? 49.211 -7.993  -18.099 1.00 30.09  ? 440 GLY A CA    1 
ATOM   3279 C  C     . GLY A 1 461 ? 50.352 -7.606  -19.042 1.00 34.77  ? 440 GLY A C     1 
ATOM   3280 O  O     . GLY A 1 461 ? 51.047 -6.573  -18.772 1.00 32.15  ? 440 GLY A O     1 
ATOM   3281 N  N     . GLN A 1 462 ? 50.516 -8.342  -20.152 1.00 33.44  ? 441 GLN A N     1 
ATOM   3282 C  CA    . GLN A 1 462 ? 51.470 -7.978  -21.244 1.00 34.02  ? 441 GLN A CA    1 
ATOM   3283 C  C     . GLN A 1 462 ? 51.228 -6.529  -21.693 1.00 32.89  ? 441 GLN A C     1 
ATOM   3284 O  O     . GLN A 1 462 ? 52.216 -5.773  -21.724 1.00 31.16  ? 441 GLN A O     1 
ATOM   3285 C  CB    . GLN A 1 462 ? 51.371 -8.931  -22.430 1.00 34.20  ? 441 GLN A CB    1 
ATOM   3286 C  CG    . GLN A 1 462 ? 52.014 -10.288 -22.177 1.00 37.87  ? 441 GLN A CG    1 
ATOM   3287 C  CD    . GLN A 1 462 ? 51.572 -11.356 -23.157 1.00 39.77  ? 441 GLN A CD    1 
ATOM   3288 O  OE1   . GLN A 1 462 ? 50.907 -11.078 -24.164 1.00 38.96  ? 441 GLN A OE1   1 
ATOM   3289 N  NE2   . GLN A 1 462 ? 51.966 -12.601 -22.878 1.00 38.03  ? 441 GLN A NE2   1 
ATOM   3290 N  N     . ARG A 1 463 ? 49.985 -6.133  -22.010 1.00 31.46  ? 442 ARG A N     1 
ATOM   3291 C  CA    . ARG A 1 463 ? 49.708 -4.766  -22.535 1.00 31.01  ? 442 ARG A CA    1 
ATOM   3292 C  C     . ARG A 1 463 ? 50.006 -3.736  -21.429 1.00 31.68  ? 442 ARG A C     1 
ATOM   3293 O  O     . ARG A 1 463 ? 50.622 -2.699  -21.733 1.00 37.62  ? 442 ARG A O     1 
ATOM   3294 C  CB    . ARG A 1 463 ? 48.282 -4.598  -23.084 1.00 32.65  ? 442 ARG A CB    1 
ATOM   3295 C  CG    . ARG A 1 463 ? 47.922 -3.112  -23.218 1.00 33.75  ? 442 ARG A CG    1 
ATOM   3296 C  CD    . ARG A 1 463 ? 46.473 -2.702  -23.194 1.00 32.96  ? 442 ARG A CD    1 
ATOM   3297 N  NE    . ARG A 1 463 ? 45.681 -3.326  -22.127 1.00 40.49  ? 442 ARG A NE    1 
ATOM   3298 C  CZ    . ARG A 1 463 ? 45.494 -2.845  -20.894 1.00 36.01  ? 442 ARG A CZ    1 
ATOM   3299 N  NH1   . ARG A 1 463 ? 46.053 -1.706  -20.503 1.00 38.04  ? 442 ARG A NH1   1 
ATOM   3300 N  NH2   . ARG A 1 463 ? 44.706 -3.495  -20.061 1.00 34.05  ? 442 ARG A NH2   1 
ATOM   3301 N  N     . ALA A 1 464 ? 49.603 -4.002  -20.185 1.00 31.46  ? 443 ALA A N     1 
ATOM   3302 C  CA    . ALA A 1 464 ? 49.798 -3.081  -19.034 1.00 35.49  ? 443 ALA A CA    1 
ATOM   3303 C  C     . ALA A 1 464 ? 51.295 -2.849  -18.765 1.00 33.35  ? 443 ALA A C     1 
ATOM   3304 O  O     . ALA A 1 464 ? 51.686 -1.673  -18.581 1.00 31.10  ? 443 ALA A O     1 
ATOM   3305 C  CB    . ALA A 1 464 ? 49.091 -3.608  -17.810 1.00 36.67  ? 443 ALA A CB    1 
ATOM   3306 N  N     . ALA A 1 465 ? 52.106 -3.909  -18.780 1.00 31.25  ? 444 ALA A N     1 
ATOM   3307 C  CA    . ALA A 1 465 ? 53.583 -3.838  -18.640 1.00 32.34  ? 444 ALA A CA    1 
ATOM   3308 C  C     . ALA A 1 465 ? 54.217 -3.034  -19.778 1.00 32.91  ? 444 ALA A C     1 
ATOM   3309 O  O     . ALA A 1 465 ? 55.013 -2.112  -19.470 1.00 35.89  ? 444 ALA A O     1 
ATOM   3310 C  CB    . ALA A 1 465 ? 54.188 -5.209  -18.568 1.00 36.19  ? 444 ALA A CB    1 
ATOM   3311 N  N     . ALA A 1 466 ? 53.893 -3.320  -21.038 1.00 32.36  ? 445 ALA A N     1 
ATOM   3312 C  CA    . ALA A 1 466 ? 54.341 -2.487  -22.189 1.00 33.61  ? 445 ALA A CA    1 
ATOM   3313 C  C     . ALA A 1 466 ? 54.020 -0.992  -21.942 1.00 34.12  ? 445 ALA A C     1 
ATOM   3314 O  O     . ALA A 1 466 ? 54.947 -0.175  -22.030 1.00 32.57  ? 445 ALA A O     1 
ATOM   3315 C  CB    . ALA A 1 466 ? 53.714 -2.964  -23.475 1.00 33.37  ? 445 ALA A CB    1 
ATOM   3316 N  N     . GLU A 1 467 ? 52.766 -0.634  -21.624 1.00 36.41  ? 446 GLU A N     1 
ATOM   3317 C  CA    . GLU A 1 467 ? 52.332 0.782   -21.423 1.00 36.59  ? 446 GLU A CA    1 
ATOM   3318 C  C     . GLU A 1 467 ? 53.191 1.451   -20.349 1.00 34.61  ? 446 GLU A C     1 
ATOM   3319 O  O     . GLU A 1 467 ? 53.645 2.581   -20.558 1.00 38.43  ? 446 GLU A O     1 
ATOM   3320 C  CB    . GLU A 1 467 ? 50.892 0.897   -20.938 1.00 41.28  ? 446 GLU A CB    1 
ATOM   3321 C  CG    . GLU A 1 467 ? 49.837 0.785   -22.020 1.00 43.14  ? 446 GLU A CG    1 
ATOM   3322 C  CD    . GLU A 1 467 ? 48.407 0.877   -21.487 1.00 40.68  ? 446 GLU A CD    1 
ATOM   3323 O  OE1   . GLU A 1 467 ? 48.235 1.226   -20.301 1.00 34.14  ? 446 GLU A OE1   1 
ATOM   3324 O  OE2   . GLU A 1 467 ? 47.469 0.583   -22.259 1.00 46.94  ? 446 GLU A OE2   1 
ATOM   3325 N  N     . VAL A 1 468 ? 53.421 0.767   -19.237 1.00 34.80  ? 447 VAL A N     1 
ATOM   3326 C  CA    . VAL A 1 468 ? 54.116 1.368   -18.063 1.00 36.75  ? 447 VAL A CA    1 
ATOM   3327 C  C     . VAL A 1 468 ? 55.615 1.531   -18.373 1.00 36.21  ? 447 VAL A C     1 
ATOM   3328 O  O     . VAL A 1 468 ? 56.148 2.623   -18.067 1.00 34.76  ? 447 VAL A O     1 
ATOM   3329 C  CB    . VAL A 1 468 ? 53.807 0.580   -16.778 1.00 37.22  ? 447 VAL A CB    1 
ATOM   3330 C  CG1   . VAL A 1 468 ? 54.788 0.868   -15.667 1.00 40.73  ? 447 VAL A CG1   1 
ATOM   3331 C  CG2   . VAL A 1 468 ? 52.389 0.879   -16.300 1.00 39.19  ? 447 VAL A CG2   1 
ATOM   3332 N  N     . LEU A 1 469 ? 56.261 0.542   -19.000 1.00 33.07  ? 448 LEU A N     1 
ATOM   3333 C  CA    . LEU A 1 469 ? 57.688 0.651   -19.402 1.00 34.15  ? 448 LEU A CA    1 
ATOM   3334 C  C     . LEU A 1 469 ? 57.886 1.842   -20.360 1.00 36.53  ? 448 LEU A C     1 
ATOM   3335 O  O     . LEU A 1 469 ? 58.819 2.599   -20.117 1.00 43.18  ? 448 LEU A O     1 
ATOM   3336 C  CB    . LEU A 1 469 ? 58.154 -0.697  -19.959 1.00 33.13  ? 448 LEU A CB    1 
ATOM   3337 C  CG    . LEU A 1 469 ? 58.206 -1.804  -18.898 1.00 32.58  ? 448 LEU A CG    1 
ATOM   3338 C  CD1   . LEU A 1 469 ? 58.308 -3.181  -19.516 1.00 37.01  ? 448 LEU A CD1   1 
ATOM   3339 C  CD2   . LEU A 1 469 ? 59.355 -1.596  -17.935 1.00 32.67  ? 448 LEU A CD2   1 
ATOM   3340 N  N     . ALA A 1 470 ? 56.998 2.085   -21.329 1.00 33.77  ? 449 ALA A N     1 
ATOM   3341 C  CA    . ALA A 1 470 ? 57.034 3.273   -22.224 1.00 35.34  ? 449 ALA A CA    1 
ATOM   3342 C  C     . ALA A 1 470 ? 56.873 4.589   -21.429 1.00 40.88  ? 449 ALA A C     1 
ATOM   3343 O  O     . ALA A 1 470 ? 57.556 5.554   -21.748 1.00 41.71  ? 449 ALA A O     1 
ATOM   3344 C  CB    . ALA A 1 470 ? 55.970 3.156   -23.287 1.00 34.89  ? 449 ALA A CB    1 
ATOM   3345 N  N     . ALA A 1 471 ? 56.023 4.632   -20.401 1.00 45.01  ? 450 ALA A N     1 
ATOM   3346 C  CA    . ALA A 1 471 ? 55.663 5.868   -19.659 1.00 48.89  ? 450 ALA A CA    1 
ATOM   3347 C  C     . ALA A 1 471 ? 56.741 6.259   -18.631 1.00 47.23  ? 450 ALA A C     1 
ATOM   3348 O  O     . ALA A 1 471 ? 56.751 7.429   -18.211 1.00 47.50  ? 450 ALA A O     1 
ATOM   3349 C  CB    . ALA A 1 471 ? 54.306 5.684   -19.005 1.00 51.29  ? 450 ALA A CB    1 
ATOM   3350 N  N     . LEU A 1 472 ? 57.598 5.322   -18.221 1.00 48.60  ? 451 LEU A N     1 
ATOM   3351 C  CA    . LEU A 1 472 ? 58.731 5.566   -17.283 1.00 50.88  ? 451 LEU A CA    1 
ATOM   3352 C  C     . LEU A 1 472 ? 59.783 6.475   -17.933 1.00 57.33  ? 451 LEU A C     1 
ATOM   3353 O  O     . LEU A 1 472 ? 60.251 7.399   -17.247 1.00 59.73  ? 451 LEU A O     1 
ATOM   3354 C  CB    . LEU A 1 472 ? 59.358 4.219   -16.911 1.00 47.95  ? 451 LEU A CB    1 
ATOM   3355 C  CG    . LEU A 1 472 ? 58.500 3.323   -16.029 1.00 43.81  ? 451 LEU A CG    1 
ATOM   3356 C  CD1   . LEU A 1 472 ? 59.029 1.898   -16.019 1.00 47.92  ? 451 LEU A CD1   1 
ATOM   3357 C  CD2   . LEU A 1 472 ? 58.433 3.876   -14.625 1.00 43.03  ? 451 LEU A CD2   1 
ATOM   3358 N  N     . GLY A 1 473 ? 60.143 6.201   -19.196 1.00 67.03  ? 452 GLY A N     1 
ATOM   3359 C  CA    . GLY A 1 473 ? 61.198 6.902   -19.964 1.00 75.57  ? 452 GLY A CA    1 
ATOM   3360 C  C     . GLY A 1 473 ? 60.821 8.340   -20.311 1.00 77.32  ? 452 GLY A C     1 
ATOM   3361 O  O     . GLY A 1 473 ? 59.865 8.629   -21.039 1.00 67.16  ? 452 GLY A O     1 
ATOM   3362 N  N     . GLN B 1 26  ? 32.852 4.051   24.104  1.00 67.69  ? 5   GLN B N     1 
ATOM   3363 C  CA    . GLN B 1 26  ? 31.632 3.226   24.217  1.00 66.77  ? 5   GLN B CA    1 
ATOM   3364 C  C     . GLN B 1 26  ? 30.381 4.089   23.981  1.00 68.04  ? 5   GLN B C     1 
ATOM   3365 O  O     . GLN B 1 26  ? 30.244 5.125   24.674  1.00 59.24  ? 5   GLN B O     1 
ATOM   3366 C  CB    . GLN B 1 26  ? 31.565 2.572   25.600  1.00 72.49  ? 5   GLN B CB    1 
ATOM   3367 C  CG    . GLN B 1 26  ? 30.488 1.505   25.688  1.00 75.10  ? 5   GLN B CG    1 
ATOM   3368 C  CD    . GLN B 1 26  ? 30.627 0.562   24.519  1.00 73.75  ? 5   GLN B CD    1 
ATOM   3369 O  OE1   . GLN B 1 26  ? 31.737 0.152   24.189  1.00 76.73  ? 5   GLN B OE1   1 
ATOM   3370 N  NE2   . GLN B 1 26  ? 29.518 0.231   23.871  1.00 69.91  ? 5   GLN B NE2   1 
ATOM   3371 N  N     . VAL B 1 27  ? 29.502 3.671   23.054  1.00 61.50  ? 6   VAL B N     1 
ATOM   3372 C  CA    . VAL B 1 27  ? 28.149 4.269   22.813  1.00 56.68  ? 6   VAL B CA    1 
ATOM   3373 C  C     . VAL B 1 27  ? 27.208 3.142   22.403  1.00 48.00  ? 6   VAL B C     1 
ATOM   3374 O  O     . VAL B 1 27  ? 27.712 2.051   22.147  1.00 52.96  ? 6   VAL B O     1 
ATOM   3375 C  CB    . VAL B 1 27  ? 28.157 5.392   21.755  1.00 55.60  ? 6   VAL B CB    1 
ATOM   3376 C  CG1   . VAL B 1 27  ? 28.945 6.614   22.223  1.00 54.41  ? 6   VAL B CG1   1 
ATOM   3377 C  CG2   . VAL B 1 27  ? 28.659 4.889   20.407  1.00 57.12  ? 6   VAL B CG2   1 
ATOM   3378 N  N     . ASP B 1 28  ? 25.901 3.404   22.354  1.00 47.94  ? 7   ASP B N     1 
ATOM   3379 C  CA    . ASP B 1 28  ? 24.867 2.393   22.003  1.00 51.55  ? 7   ASP B CA    1 
ATOM   3380 C  C     . ASP B 1 28  ? 24.759 2.239   20.486  1.00 50.73  ? 7   ASP B C     1 
ATOM   3381 O  O     . ASP B 1 28  ? 24.688 1.092   20.017  1.00 49.70  ? 7   ASP B O     1 
ATOM   3382 C  CB    . ASP B 1 28  ? 23.479 2.787   22.506  1.00 58.20  ? 7   ASP B CB    1 
ATOM   3383 C  CG    . ASP B 1 28  ? 23.373 2.860   24.018  1.00 61.26  ? 7   ASP B CG    1 
ATOM   3384 O  OD1   . ASP B 1 28  ? 23.163 1.799   24.629  1.00 55.49  ? 7   ASP B OD1   1 
ATOM   3385 O  OD2   . ASP B 1 28  ? 23.503 3.983   24.559  1.00 58.01  ? 7   ASP B OD2   1 
ATOM   3386 N  N     . VAL B 1 29  ? 24.675 3.359   19.759  1.00 45.44  ? 8   VAL B N     1 
ATOM   3387 C  CA    . VAL B 1 29  ? 24.432 3.361   18.289  1.00 44.95  ? 8   VAL B CA    1 
ATOM   3388 C  C     . VAL B 1 29  ? 25.441 4.288   17.619  1.00 41.08  ? 8   VAL B C     1 
ATOM   3389 O  O     . VAL B 1 29  ? 25.557 5.438   18.049  1.00 42.01  ? 8   VAL B O     1 
ATOM   3390 C  CB    . VAL B 1 29  ? 22.978 3.737   17.941  1.00 46.51  ? 8   VAL B CB    1 
ATOM   3391 C  CG1   . VAL B 1 29  ? 22.703 3.636   16.444  1.00 43.27  ? 8   VAL B CG1   1 
ATOM   3392 C  CG2   . VAL B 1 29  ? 21.995 2.867   18.716  1.00 47.05  ? 8   VAL B CG2   1 
ATOM   3393 N  N     . VAL B 1 30  ? 26.155 3.767   16.612  1.00 41.57  ? 9   VAL B N     1 
ATOM   3394 C  CA    . VAL B 1 30  ? 26.914 4.583   15.615  1.00 39.19  ? 9   VAL B CA    1 
ATOM   3395 C  C     . VAL B 1 30  ? 26.132 4.587   14.287  1.00 36.60  ? 9   VAL B C     1 
ATOM   3396 O  O     . VAL B 1 30  ? 25.694 3.490   13.777  1.00 31.80  ? 9   VAL B O     1 
ATOM   3397 C  CB    . VAL B 1 30  ? 28.374 4.136   15.460  1.00 39.39  ? 9   VAL B CB    1 
ATOM   3398 C  CG1   . VAL B 1 30  ? 28.487 2.712   14.924  1.00 44.48  ? 9   VAL B CG1   1 
ATOM   3399 C  CG2   . VAL B 1 30  ? 29.144 5.110   14.594  1.00 39.99  ? 9   VAL B CG2   1 
ATOM   3400 N  N     . VAL B 1 31  ? 25.879 5.807   13.815  1.00 34.10  ? 10  VAL B N     1 
ATOM   3401 C  CA    . VAL B 1 31  ? 25.252 6.133   12.510  1.00 36.86  ? 10  VAL B CA    1 
ATOM   3402 C  C     . VAL B 1 31  ? 26.364 6.617   11.562  1.00 34.43  ? 10  VAL B C     1 
ATOM   3403 O  O     . VAL B 1 31  ? 27.159 7.522   11.946  1.00 39.43  ? 10  VAL B O     1 
ATOM   3404 C  CB    . VAL B 1 31  ? 24.133 7.176   12.695  1.00 40.10  ? 10  VAL B CB    1 
ATOM   3405 C  CG1   . VAL B 1 31  ? 23.597 7.646   11.349  1.00 38.10  ? 10  VAL B CG1   1 
ATOM   3406 C  CG2   . VAL B 1 31  ? 23.008 6.649   13.593  1.00 39.01  ? 10  VAL B CG2   1 
ATOM   3407 N  N     . VAL B 1 32  ? 26.439 6.031   10.374  1.00 32.42  ? 11  VAL B N     1 
ATOM   3408 C  CA    . VAL B 1 32  ? 27.434 6.403   9.322   1.00 35.72  ? 11  VAL B CA    1 
ATOM   3409 C  C     . VAL B 1 32  ? 26.692 7.245   8.283   1.00 32.71  ? 11  VAL B C     1 
ATOM   3410 O  O     . VAL B 1 32  ? 25.790 6.687   7.667   1.00 34.59  ? 11  VAL B O     1 
ATOM   3411 C  CB    . VAL B 1 32  ? 28.055 5.146   8.683   1.00 36.37  ? 11  VAL B CB    1 
ATOM   3412 C  CG1   . VAL B 1 32  ? 29.253 5.469   7.794   1.00 39.80  ? 11  VAL B CG1   1 
ATOM   3413 C  CG2   . VAL B 1 32  ? 28.443 4.123   9.730   1.00 40.10  ? 11  VAL B CG2   1 
ATOM   3414 N  N     . GLY B 1 33  ? 27.013 8.536   8.163   1.00 34.71  ? 12  GLY B N     1 
ATOM   3415 C  CA    . GLY B 1 33  ? 26.399 9.478   7.198   1.00 33.90  ? 12  GLY B CA    1 
ATOM   3416 C  C     . GLY B 1 33  ? 25.466 10.464  7.884   1.00 34.73  ? 12  GLY B C     1 
ATOM   3417 O  O     . GLY B 1 33  ? 24.547 10.006  8.555   1.00 34.97  ? 12  GLY B O     1 
ATOM   3418 N  N     . ALA B 1 34  ? 25.716 11.769  7.732   1.00 34.26  ? 13  ALA B N     1 
ATOM   3419 C  CA    . ALA B 1 34  ? 24.892 12.874  8.271   1.00 36.00  ? 13  ALA B CA    1 
ATOM   3420 C  C     . ALA B 1 34  ? 24.042 13.468  7.138   1.00 39.05  ? 13  ALA B C     1 
ATOM   3421 O  O     . ALA B 1 34  ? 23.963 14.709  7.005   1.00 36.01  ? 13  ALA B O     1 
ATOM   3422 C  CB    . ALA B 1 34  ? 25.791 13.906  8.910   1.00 37.04  ? 13  ALA B CB    1 
ATOM   3423 N  N     . GLY B 1 35  ? 23.422 12.602  6.334   1.00 41.43  ? 14  GLY B N     1 
ATOM   3424 C  CA    . GLY B 1 35  ? 22.363 13.001  5.391   1.00 38.33  ? 14  GLY B CA    1 
ATOM   3425 C  C     . GLY B 1 35  ? 21.074 13.171  6.156   1.00 40.17  ? 14  GLY B C     1 
ATOM   3426 O  O     . GLY B 1 35  ? 21.121 13.121  7.393   1.00 41.99  ? 14  GLY B O     1 
ATOM   3427 N  N     . PHE B 1 36  ? 19.962 13.376  5.465   1.00 35.87  ? 15  PHE B N     1 
ATOM   3428 C  CA    . PHE B 1 36  ? 18.632 13.459  6.108   1.00 36.26  ? 15  PHE B CA    1 
ATOM   3429 C  C     . PHE B 1 36  ? 18.318 12.098  6.750   1.00 36.38  ? 15  PHE B C     1 
ATOM   3430 O  O     . PHE B 1 36  ? 17.677 12.084  7.797   1.00 34.29  ? 15  PHE B O     1 
ATOM   3431 C  CB    . PHE B 1 36  ? 17.586 13.980  5.115   1.00 35.19  ? 15  PHE B CB    1 
ATOM   3432 C  CG    . PHE B 1 36  ? 17.452 15.486  5.132   1.00 37.37  ? 15  PHE B CG    1 
ATOM   3433 C  CD1   . PHE B 1 36  ? 16.660 16.116  6.089   1.00 38.55  ? 15  PHE B CD1   1 
ATOM   3434 C  CD2   . PHE B 1 36  ? 18.154 16.274  4.235   1.00 34.58  ? 15  PHE B CD2   1 
ATOM   3435 C  CE1   . PHE B 1 36  ? 16.527 17.492  6.112   1.00 37.81  ? 15  PHE B CE1   1 
ATOM   3436 C  CE2   . PHE B 1 36  ? 18.027 17.652  4.266   1.00 36.96  ? 15  PHE B CE2   1 
ATOM   3437 C  CZ    . PHE B 1 36  ? 17.217 18.261  5.202   1.00 39.76  ? 15  PHE B CZ    1 
ATOM   3438 N  N     . ALA B 1 37  ? 18.765 10.989  6.159   1.00 30.96  ? 16  ALA B N     1 
ATOM   3439 C  CA    . ALA B 1 37  ? 18.526 9.632   6.706   1.00 32.35  ? 16  ALA B CA    1 
ATOM   3440 C  C     . ALA B 1 37  ? 19.297 9.448   8.017   1.00 36.22  ? 16  ALA B C     1 
ATOM   3441 O  O     . ALA B 1 37  ? 18.676 9.058   9.036   1.00 38.20  ? 16  ALA B O     1 
ATOM   3442 C  CB    . ALA B 1 37  ? 18.917 8.586   5.701   1.00 32.12  ? 16  ALA B CB    1 
ATOM   3443 N  N     . GLY B 1 38  ? 20.616 9.655   7.978   1.00 39.86  ? 17  GLY B N     1 
ATOM   3444 C  CA    . GLY B 1 38  ? 21.516 9.508   9.131   1.00 37.51  ? 17  GLY B CA    1 
ATOM   3445 C  C     . GLY B 1 38  ? 21.061 10.355  10.303  1.00 38.58  ? 17  GLY B C     1 
ATOM   3446 O  O     . GLY B 1 38  ? 21.086 9.848   11.460  1.00 36.48  ? 17  GLY B O     1 
ATOM   3447 N  N     . LEU B 1 39  ? 20.678 11.603  10.023  1.00 37.01  ? 18  LEU B N     1 
ATOM   3448 C  CA    . LEU B 1 39  ? 20.341 12.620  11.047  1.00 36.65  ? 18  LEU B CA    1 
ATOM   3449 C  C     . LEU B 1 39  ? 19.015 12.237  11.712  1.00 39.30  ? 18  LEU B C     1 
ATOM   3450 O  O     . LEU B 1 39  ? 18.910 12.334  12.948  1.00 44.89  ? 18  LEU B O     1 
ATOM   3451 C  CB    . LEU B 1 39  ? 20.252 14.000  10.391  1.00 34.66  ? 18  LEU B CB    1 
ATOM   3452 C  CG    . LEU B 1 39  ? 21.575 14.718  10.153  1.00 36.28  ? 18  LEU B CG    1 
ATOM   3453 C  CD1   . LEU B 1 39  ? 21.323 16.185  9.819   1.00 44.15  ? 18  LEU B CD1   1 
ATOM   3454 C  CD2   . LEU B 1 39  ? 22.489 14.623  11.357  1.00 36.12  ? 18  LEU B CD2   1 
ATOM   3455 N  N     . THR B 1 40  ? 18.041 11.835  10.908  1.00 36.72  ? 19  THR B N     1 
ATOM   3456 C  CA    . THR B 1 40  ? 16.709 11.387  11.351  1.00 38.67  ? 19  THR B CA    1 
ATOM   3457 C  C     . THR B 1 40  ? 16.911 10.252  12.354  1.00 43.72  ? 19  THR B C     1 
ATOM   3458 O  O     . THR B 1 40  ? 16.363 10.353  13.463  1.00 49.11  ? 19  THR B O     1 
ATOM   3459 C  CB    . THR B 1 40  ? 15.850 10.956  10.150  1.00 37.90  ? 19  THR B CB    1 
ATOM   3460 O  OG1   . THR B 1 40  ? 15.645 12.086  9.303   1.00 36.40  ? 19  THR B OG1   1 
ATOM   3461 C  CG2   . THR B 1 40  ? 14.500 10.400  10.552  1.00 39.07  ? 19  THR B CG2   1 
ATOM   3462 N  N     . ALA B 1 41  ? 17.656 9.213   11.962  1.00 40.45  ? 20  ALA B N     1 
ATOM   3463 C  CA    . ALA B 1 41  ? 17.901 8.018   12.788  1.00 40.57  ? 20  ALA B CA    1 
ATOM   3464 C  C     . ALA B 1 41  ? 18.578 8.445   14.091  1.00 39.39  ? 20  ALA B C     1 
ATOM   3465 O  O     . ALA B 1 41  ? 18.128 7.997   15.129  1.00 38.41  ? 20  ALA B O     1 
ATOM   3466 C  CB    . ALA B 1 41  ? 18.730 7.001   12.057  1.00 43.63  ? 20  ALA B CB    1 
ATOM   3467 N  N     . ALA B 1 42  ? 19.601 9.295   14.049  1.00 35.94  ? 21  ALA B N     1 
ATOM   3468 C  CA    . ALA B 1 42  ? 20.404 9.620   15.250  1.00 37.19  ? 21  ALA B CA    1 
ATOM   3469 C  C     . ALA B 1 42  ? 19.525 10.380  16.241  1.00 42.56  ? 21  ALA B C     1 
ATOM   3470 O  O     . ALA B 1 42  ? 19.651 10.114  17.451  1.00 36.75  ? 21  ALA B O     1 
ATOM   3471 C  CB    . ALA B 1 42  ? 21.644 10.415  14.925  1.00 39.50  ? 21  ALA B CB    1 
ATOM   3472 N  N     . ARG B 1 43  ? 18.687 11.290  15.732  1.00 44.84  ? 22  ARG B N     1 
ATOM   3473 C  CA    . ARG B 1 43  ? 17.766 12.111  16.554  1.00 44.59  ? 22  ARG B CA    1 
ATOM   3474 C  C     . ARG B 1 43  ? 16.733 11.204  17.242  1.00 41.14  ? 22  ARG B C     1 
ATOM   3475 O  O     . ARG B 1 43  ? 16.548 11.376  18.467  1.00 41.62  ? 22  ARG B O     1 
ATOM   3476 C  CB    . ARG B 1 43  ? 17.118 13.202  15.705  1.00 48.73  ? 22  ARG B CB    1 
ATOM   3477 C  CG    . ARG B 1 43  ? 16.503 14.327  16.524  1.00 52.34  ? 22  ARG B CG    1 
ATOM   3478 C  CD    . ARG B 1 43  ? 15.211 14.799  15.886  1.00 54.74  ? 22  ARG B CD    1 
ATOM   3479 N  NE    . ARG B 1 43  ? 14.677 15.936  16.608  1.00 59.67  ? 22  ARG B NE    1 
ATOM   3480 C  CZ    . ARG B 1 43  ? 13.533 16.547  16.336  1.00 55.88  ? 22  ARG B CZ    1 
ATOM   3481 N  NH1   . ARG B 1 43  ? 12.784 16.157  15.320  1.00 48.76  ? 22  ARG B NH1   1 
ATOM   3482 N  NH2   . ARG B 1 43  ? 13.162 17.573  17.078  1.00 60.70  ? 22  ARG B NH2   1 
ATOM   3483 N  N     . ALA B 1 44  ? 16.125 10.239  16.544  1.00 35.44  ? 23  ALA B N     1 
ATOM   3484 C  CA    . ALA B 1 44  ? 15.169 9.303   17.178  1.00 37.27  ? 23  ALA B CA    1 
ATOM   3485 C  C     . ALA B 1 44  ? 15.873 8.601   18.352  1.00 48.44  ? 23  ALA B C     1 
ATOM   3486 O  O     . ALA B 1 44  ? 15.281 8.519   19.451  1.00 57.98  ? 23  ALA B O     1 
ATOM   3487 C  CB    . ALA B 1 44  ? 14.587 8.329   16.182  1.00 31.87  ? 23  ALA B CB    1 
ATOM   3488 N  N     . VAL B 1 45  ? 17.126 8.188   18.157  1.00 49.34  ? 24  VAL B N     1 
ATOM   3489 C  CA    . VAL B 1 45  ? 17.914 7.370   19.126  1.00 50.13  ? 24  VAL B CA    1 
ATOM   3490 C  C     . VAL B 1 45  ? 18.287 8.215   20.367  1.00 48.34  ? 24  VAL B C     1 
ATOM   3491 O  O     . VAL B 1 45  ? 18.174 7.678   21.494  1.00 46.33  ? 24  VAL B O     1 
ATOM   3492 C  CB    . VAL B 1 45  ? 19.126 6.753   18.392  1.00 54.25  ? 24  VAL B CB    1 
ATOM   3493 C  CG1   . VAL B 1 45  ? 20.216 6.265   19.332  1.00 59.72  ? 24  VAL B CG1   1 
ATOM   3494 C  CG2   . VAL B 1 45  ? 18.689 5.630   17.466  1.00 48.99  ? 24  VAL B CG2   1 
ATOM   3495 N  N     . HIS B 1 46  ? 18.698 9.478   20.194  1.00 46.13  ? 25  HIS B N     1 
ATOM   3496 C  CA    . HIS B 1 46  ? 19.053 10.443  21.278  1.00 57.51  ? 25  HIS B CA    1 
ATOM   3497 C  C     . HIS B 1 46  ? 17.835 10.797  22.153  1.00 58.87  ? 25  HIS B C     1 
ATOM   3498 O  O     . HIS B 1 46  ? 18.044 11.077  23.368  1.00 55.17  ? 25  HIS B O     1 
ATOM   3499 C  CB    . HIS B 1 46  ? 19.722 11.688  20.673  1.00 65.18  ? 25  HIS B CB    1 
ATOM   3500 C  CG    . HIS B 1 46  ? 19.364 12.984  21.320  1.00 74.13  ? 25  HIS B CG    1 
ATOM   3501 N  ND1   . HIS B 1 46  ? 18.557 13.934  20.700  1.00 79.17  ? 25  HIS B ND1   1 
ATOM   3502 C  CD2   . HIS B 1 46  ? 19.722 13.510  22.508  1.00 73.18  ? 25  HIS B CD2   1 
ATOM   3503 C  CE1   . HIS B 1 46  ? 18.425 14.975  21.494  1.00 77.31  ? 25  HIS B CE1   1 
ATOM   3504 N  NE2   . HIS B 1 46  ? 19.136 14.743  22.605  1.00 74.14  ? 25  HIS B NE2   1 
ATOM   3505 N  N     . GLU B 1 47  ? 16.631 10.766  21.568  1.00 57.32  ? 26  GLU B N     1 
ATOM   3506 C  CA    . GLU B 1 47  ? 15.335 11.132  22.206  1.00 62.35  ? 26  GLU B CA    1 
ATOM   3507 C  C     . GLU B 1 47  ? 14.803 9.989   23.078  1.00 65.08  ? 26  GLU B C     1 
ATOM   3508 O  O     . GLU B 1 47  ? 14.034 10.294  24.016  1.00 62.91  ? 26  GLU B O     1 
ATOM   3509 C  CB    . GLU B 1 47  ? 14.272 11.455  21.156  1.00 63.06  ? 26  GLU B CB    1 
ATOM   3510 C  CG    . GLU B 1 47  ? 14.358 12.876  20.630  1.00 66.78  ? 26  GLU B CG    1 
ATOM   3511 C  CD    . GLU B 1 47  ? 13.166 13.287  19.791  1.00 63.54  ? 26  GLU B CD    1 
ATOM   3512 O  OE1   . GLU B 1 47  ? 12.201 12.505  19.724  1.00 70.03  ? 26  GLU B OE1   1 
ATOM   3513 O  OE2   . GLU B 1 47  ? 13.199 14.391  19.226  1.00 67.90  ? 26  GLU B OE2   1 
ATOM   3514 N  N     . ALA B 1 48  ? 15.149 8.739   22.752  1.00 57.27  ? 27  ALA B N     1 
ATOM   3515 C  CA    . ALA B 1 48  ? 14.938 7.563   23.634  1.00 58.00  ? 27  ALA B CA    1 
ATOM   3516 C  C     . ALA B 1 48  ? 16.083 7.471   24.660  1.00 54.17  ? 27  ALA B C     1 
ATOM   3517 O  O     . ALA B 1 48  ? 16.118 6.497   25.389  1.00 56.49  ? 27  ALA B O     1 
ATOM   3518 C  CB    . ALA B 1 48  ? 14.785 6.309   22.808  1.00 55.71  ? 27  ALA B CB    1 
ATOM   3519 N  N     . GLY B 1 49  ? 16.992 8.463   24.703  1.00 65.74  ? 28  GLY B N     1 
ATOM   3520 C  CA    . GLY B 1 49  ? 18.001 8.681   25.767  1.00 60.77  ? 28  GLY B CA    1 
ATOM   3521 C  C     . GLY B 1 49  ? 19.242 7.801   25.632  1.00 65.90  ? 28  GLY B C     1 
ATOM   3522 O  O     . GLY B 1 49  ? 20.019 7.720   26.638  1.00 56.55  ? 28  GLY B O     1 
ATOM   3523 N  N     . ARG B 1 50  ? 19.431 7.166   24.457  1.00 66.46  ? 29  ARG B N     1 
ATOM   3524 C  CA    . ARG B 1 50  ? 20.570 6.256   24.125  1.00 53.11  ? 29  ARG B CA    1 
ATOM   3525 C  C     . ARG B 1 50  ? 21.726 7.107   23.610  1.00 46.19  ? 29  ARG B C     1 
ATOM   3526 O  O     . ARG B 1 50  ? 21.475 8.175   23.036  1.00 43.88  ? 29  ARG B O     1 
ATOM   3527 C  CB    . ARG B 1 50  ? 20.188 5.236   23.054  1.00 47.94  ? 29  ARG B CB    1 
ATOM   3528 C  CG    . ARG B 1 50  ? 19.001 4.361   23.412  1.00 48.11  ? 29  ARG B CG    1 
ATOM   3529 C  CD    . ARG B 1 50  ? 19.337 3.309   24.451  1.00 49.16  ? 29  ARG B CD    1 
ATOM   3530 N  NE    . ARG B 1 50  ? 18.276 2.306   24.484  1.00 51.36  ? 29  ARG B NE    1 
ATOM   3531 C  CZ    . ARG B 1 50  ? 18.258 1.243   25.284  1.00 54.65  ? 29  ARG B CZ    1 
ATOM   3532 N  NH1   . ARG B 1 50  ? 19.263 1.041   26.123  1.00 56.28  ? 29  ARG B NH1   1 
ATOM   3533 N  NH2   . ARG B 1 50  ? 17.234 0.401   25.254  1.00 48.11  ? 29  ARG B NH2   1 
ATOM   3534 N  N     . SER B 1 51  ? 22.957 6.680   23.838  1.00 46.20  ? 30  SER B N     1 
ATOM   3535 C  CA    . SER B 1 51  ? 24.132 7.419   23.317  1.00 49.64  ? 30  SER B CA    1 
ATOM   3536 C  C     . SER B 1 51  ? 24.254 7.114   21.809  1.00 51.17  ? 30  SER B C     1 
ATOM   3537 O  O     . SER B 1 51  ? 23.874 5.994   21.351  1.00 44.60  ? 30  SER B O     1 
ATOM   3538 C  CB    . SER B 1 51  ? 25.379 7.122   24.109  1.00 45.86  ? 30  SER B CB    1 
ATOM   3539 O  OG    . SER B 1 51  ? 25.486 5.735   24.341  1.00 51.11  ? 30  SER B OG    1 
ATOM   3540 N  N     . VAL B 1 52  ? 24.673 8.117   21.041  1.00 49.38  ? 31  VAL B N     1 
ATOM   3541 C  CA    . VAL B 1 52  ? 24.750 8.027   19.561  1.00 47.74  ? 31  VAL B CA    1 
ATOM   3542 C  C     . VAL B 1 52  ? 25.963 8.832   19.123  1.00 49.02  ? 31  VAL B C     1 
ATOM   3543 O  O     . VAL B 1 52  ? 26.155 9.935   19.679  1.00 49.74  ? 31  VAL B O     1 
ATOM   3544 C  CB    . VAL B 1 52  ? 23.447 8.537   18.930  1.00 48.42  ? 31  VAL B CB    1 
ATOM   3545 C  CG1   . VAL B 1 52  ? 23.396 10.057  18.911  1.00 45.21  ? 31  VAL B CG1   1 
ATOM   3546 C  CG2   . VAL B 1 52  ? 23.225 7.947   17.550  1.00 47.92  ? 31  VAL B CG2   1 
ATOM   3547 N  N     . LEU B 1 53  ? 26.769 8.268   18.223  1.00 47.55  ? 32  LEU B N     1 
ATOM   3548 C  CA    . LEU B 1 53  ? 27.764 9.012   17.408  1.00 48.49  ? 32  LEU B CA    1 
ATOM   3549 C  C     . LEU B 1 53  ? 27.298 9.011   15.944  1.00 48.11  ? 32  LEU B C     1 
ATOM   3550 O  O     . LEU B 1 53  ? 26.810 7.966   15.467  1.00 46.11  ? 32  LEU B O     1 
ATOM   3551 C  CB    . LEU B 1 53  ? 29.145 8.368   17.549  1.00 51.96  ? 32  LEU B CB    1 
ATOM   3552 C  CG    . LEU B 1 53  ? 29.961 8.801   18.768  1.00 61.66  ? 32  LEU B CG    1 
ATOM   3553 C  CD1   . LEU B 1 53  ? 31.268 8.020   18.841  1.00 62.52  ? 32  LEU B CD1   1 
ATOM   3554 C  CD2   . LEU B 1 53  ? 30.253 10.301  18.766  1.00 60.36  ? 32  LEU B CD2   1 
ATOM   3555 N  N     . VAL B 1 54  ? 27.393 10.165  15.292  1.00 42.22  ? 33  VAL B N     1 
ATOM   3556 C  CA    . VAL B 1 54  ? 27.203 10.321  13.829  1.00 41.53  ? 33  VAL B CA    1 
ATOM   3557 C  C     . VAL B 1 54  ? 28.569 10.617  13.222  1.00 42.70  ? 33  VAL B C     1 
ATOM   3558 O  O     . VAL B 1 54  ? 29.084 11.722  13.474  1.00 39.70  ? 33  VAL B O     1 
ATOM   3559 C  CB    . VAL B 1 54  ? 26.198 11.434  13.514  1.00 41.65  ? 33  VAL B CB    1 
ATOM   3560 C  CG1   . VAL B 1 54  ? 25.883 11.473  12.036  1.00 40.14  ? 33  VAL B CG1   1 
ATOM   3561 C  CG2   . VAL B 1 54  ? 24.925 11.282  14.338  1.00 44.38  ? 33  VAL B CG2   1 
ATOM   3562 N  N     . LEU B 1 55  ? 29.108 9.663   12.455  1.00 39.62  ? 34  LEU B N     1 
ATOM   3563 C  CA    . LEU B 1 55  ? 30.359 9.812   11.672  1.00 37.90  ? 34  LEU B CA    1 
ATOM   3564 C  C     . LEU B 1 55  ? 30.010 10.229  10.225  1.00 38.06  ? 34  LEU B C     1 
ATOM   3565 O  O     . LEU B 1 55  ? 29.345 9.468   9.503   1.00 39.13  ? 34  LEU B O     1 
ATOM   3566 C  CB    . LEU B 1 55  ? 31.111 8.479   11.768  1.00 42.12  ? 34  LEU B CB    1 
ATOM   3567 C  CG    . LEU B 1 55  ? 31.363 7.975   13.197  1.00 44.64  ? 34  LEU B CG    1 
ATOM   3568 C  CD1   . LEU B 1 55  ? 31.918 6.558   13.226  1.00 46.09  ? 34  LEU B CD1   1 
ATOM   3569 C  CD2   . LEU B 1 55  ? 32.304 8.899   13.950  1.00 43.72  ? 34  LEU B CD2   1 
ATOM   3570 N  N     . GLU B 1 56  ? 30.411 11.432  9.828   1.00 35.18  ? 35  GLU B N     1 
ATOM   3571 C  CA    . GLU B 1 56  ? 30.161 12.033  8.496   1.00 36.65  ? 35  GLU B CA    1 
ATOM   3572 C  C     . GLU B 1 56  ? 31.515 12.294  7.816   1.00 39.85  ? 35  GLU B C     1 
ATOM   3573 O  O     . GLU B 1 56  ? 32.393 12.970  8.453   1.00 39.44  ? 35  GLU B O     1 
ATOM   3574 C  CB    . GLU B 1 56  ? 29.346 13.321  8.672   1.00 37.22  ? 35  GLU B CB    1 
ATOM   3575 C  CG    . GLU B 1 56  ? 29.301 14.219  7.442   1.00 35.92  ? 35  GLU B CG    1 
ATOM   3576 C  CD    . GLU B 1 56  ? 28.739 13.548  6.201   1.00 36.62  ? 35  GLU B CD    1 
ATOM   3577 O  OE1   . GLU B 1 56  ? 27.659 12.902  6.298   1.00 35.52  ? 35  GLU B OE1   1 
ATOM   3578 O  OE2   . GLU B 1 56  ? 29.395 13.643  5.148   1.00 37.21  ? 35  GLU B OE2   1 
ATOM   3579 N  N     . ALA B 1 57  ? 31.706 11.782  6.592   1.00 34.83  ? 36  ALA B N     1 
ATOM   3580 C  CA    . ALA B 1 57  ? 32.958 11.969  5.809   1.00 36.48  ? 36  ALA B CA    1 
ATOM   3581 C  C     . ALA B 1 57  ? 33.243 13.456  5.524   1.00 36.80  ? 36  ALA B C     1 
ATOM   3582 O  O     . ALA B 1 57  ? 34.416 13.830  5.498   1.00 37.12  ? 36  ALA B O     1 
ATOM   3583 C  CB    . ALA B 1 57  ? 32.887 11.207  4.511   1.00 32.02  ? 36  ALA B CB    1 
ATOM   3584 N  N     . ARG B 1 58  ? 32.218 14.254  5.240   1.00 33.97  ? 37  ARG B N     1 
ATOM   3585 C  CA    . ARG B 1 58  ? 32.382 15.641  4.734   1.00 35.33  ? 37  ARG B CA    1 
ATOM   3586 C  C     . ARG B 1 58  ? 32.561 16.664  5.868   1.00 35.64  ? 37  ARG B C     1 
ATOM   3587 O  O     . ARG B 1 58  ? 32.158 16.384  7.008   1.00 36.09  ? 37  ARG B O     1 
ATOM   3588 C  CB    . ARG B 1 58  ? 31.136 16.045  3.947   1.00 32.58  ? 37  ARG B CB    1 
ATOM   3589 C  CG    . ARG B 1 58  ? 31.145 15.610  2.490   1.00 32.63  ? 37  ARG B CG    1 
ATOM   3590 C  CD    . ARG B 1 58  ? 29.844 16.096  1.895   1.00 34.36  ? 37  ARG B CD    1 
ATOM   3591 N  NE    . ARG B 1 58  ? 29.679 15.937  0.463   1.00 32.88  ? 37  ARG B NE    1 
ATOM   3592 C  CZ    . ARG B 1 58  ? 28.914 15.034  -0.126  1.00 34.42  ? 37  ARG B CZ    1 
ATOM   3593 N  NH1   . ARG B 1 58  ? 28.271 14.131  0.597   1.00 34.09  ? 37  ARG B NH1   1 
ATOM   3594 N  NH2   . ARG B 1 58  ? 28.827 15.022  -1.448  1.00 32.78  ? 37  ARG B NH2   1 
ATOM   3595 N  N     . ASP B 1 59  ? 33.027 17.868  5.541   1.00 36.52  ? 38  ASP B N     1 
ATOM   3596 C  CA    . ASP B 1 59  ? 33.143 18.987  6.521   1.00 41.77  ? 38  ASP B CA    1 
ATOM   3597 C  C     . ASP B 1 59  ? 31.756 19.623  6.779   1.00 40.62  ? 38  ASP B C     1 
ATOM   3598 O  O     . ASP B 1 59  ? 31.724 20.756  7.276   1.00 42.00  ? 38  ASP B O     1 
ATOM   3599 C  CB    . ASP B 1 59  ? 34.229 19.991  6.093   1.00 45.57  ? 38  ASP B CB    1 
ATOM   3600 C  CG    . ASP B 1 59  ? 33.963 20.775  4.809   1.00 52.94  ? 38  ASP B CG    1 
ATOM   3601 O  OD1   . ASP B 1 59  ? 32.830 20.680  4.267   1.00 59.36  ? 38  ASP B OD1   1 
ATOM   3602 O  OD2   . ASP B 1 59  ? 34.891 21.490  4.351   1.00 56.99  ? 38  ASP B OD2   1 
ATOM   3603 N  N     . ARG B 1 60  ? 30.648 18.921  6.512   1.00 35.45  ? 39  ARG B N     1 
ATOM   3604 C  CA    . ARG B 1 60  ? 29.280 19.487  6.602   1.00 37.08  ? 39  ARG B CA    1 
ATOM   3605 C  C     . ARG B 1 60  ? 28.253 18.348  6.636   1.00 38.73  ? 39  ARG B C     1 
ATOM   3606 O  O     . ARG B 1 60  ? 28.609 17.196  6.300   1.00 35.60  ? 39  ARG B O     1 
ATOM   3607 C  CB    . ARG B 1 60  ? 28.995 20.418  5.417   1.00 38.76  ? 39  ARG B CB    1 
ATOM   3608 C  CG    . ARG B 1 60  ? 28.906 19.708  4.069   1.00 37.98  ? 39  ARG B CG    1 
ATOM   3609 C  CD    . ARG B 1 60  ? 28.383 20.556  2.917   1.00 39.95  ? 39  ARG B CD    1 
ATOM   3610 N  NE    . ARG B 1 60  ? 28.268 19.752  1.704   1.00 41.20  ? 39  ARG B NE    1 
ATOM   3611 C  CZ    . ARG B 1 60  ? 27.231 18.967  1.372   1.00 37.91  ? 39  ARG B CZ    1 
ATOM   3612 N  NH1   . ARG B 1 60  ? 26.148 18.869  2.133   1.00 34.12  ? 39  ARG B NH1   1 
ATOM   3613 N  NH2   . ARG B 1 60  ? 27.286 18.276  0.244   1.00 38.60  ? 39  ARG B NH2   1 
ATOM   3614 N  N     . VAL B 1 61  ? 27.019 18.685  7.008   1.00 37.98  ? 40  VAL B N     1 
ATOM   3615 C  CA    . VAL B 1 61  ? 25.830 17.784  6.969   1.00 37.58  ? 40  VAL B CA    1 
ATOM   3616 C  C     . VAL B 1 61  ? 25.046 18.115  5.689   1.00 35.56  ? 40  VAL B C     1 
ATOM   3617 O  O     . VAL B 1 61  ? 25.357 19.166  5.068   1.00 36.80  ? 40  VAL B O     1 
ATOM   3618 C  CB    . VAL B 1 61  ? 24.977 17.960  8.244   1.00 42.08  ? 40  VAL B CB    1 
ATOM   3619 C  CG1   . VAL B 1 61  ? 25.801 17.774  9.509   1.00 43.81  ? 40  VAL B CG1   1 
ATOM   3620 C  CG2   . VAL B 1 61  ? 24.261 19.312  8.293   1.00 44.26  ? 40  VAL B CG2   1 
ATOM   3621 N  N     . GLY B 1 62  ? 24.052 17.298  5.342   1.00 31.01  ? 41  GLY B N     1 
ATOM   3622 C  CA    . GLY B 1 62  ? 23.125 17.533  4.213   1.00 34.75  ? 41  GLY B CA    1 
ATOM   3623 C  C     . GLY B 1 62  ? 23.278 16.516  3.084   1.00 33.76  ? 41  GLY B C     1 
ATOM   3624 O  O     . GLY B 1 62  ? 22.249 16.199  2.390   1.00 32.56  ? 41  GLY B O     1 
ATOM   3625 N  N     . GLY B 1 63  ? 24.507 16.027  2.883   1.00 33.92  ? 42  GLY B N     1 
ATOM   3626 C  CA    . GLY B 1 63  ? 24.847 15.005  1.870   1.00 35.75  ? 42  GLY B CA    1 
ATOM   3627 C  C     . GLY B 1 63  ? 24.481 15.422  0.450   1.00 32.85  ? 42  GLY B C     1 
ATOM   3628 O  O     . GLY B 1 63  ? 25.145 16.332  -0.126  1.00 27.76  ? 42  GLY B O     1 
ATOM   3629 N  N     . ARG B 1 64  ? 23.476 14.762  -0.121  1.00 28.24  ? 43  ARG B N     1 
ATOM   3630 C  CA    . ARG B 1 64  ? 22.974 15.098  -1.477  1.00 29.83  ? 43  ARG B CA    1 
ATOM   3631 C  C     . ARG B 1 64  ? 22.118 16.381  -1.439  1.00 30.35  ? 43  ARG B C     1 
ATOM   3632 O  O     . ARG B 1 64  ? 21.605 16.770  -2.501  1.00 30.46  ? 43  ARG B O     1 
ATOM   3633 C  CB    . ARG B 1 64  ? 22.214 13.911  -2.085  1.00 27.64  ? 43  ARG B CB    1 
ATOM   3634 C  CG    . ARG B 1 64  ? 23.137 12.846  -2.657  1.00 28.13  ? 43  ARG B CG    1 
ATOM   3635 C  CD    . ARG B 1 64  ? 22.378 11.625  -3.137  1.00 27.55  ? 43  ARG B CD    1 
ATOM   3636 N  NE    . ARG B 1 64  ? 22.253 10.628  -2.117  1.00 27.38  ? 43  ARG B NE    1 
ATOM   3637 C  CZ    . ARG B 1 64  ? 21.573 9.483   -2.257  1.00 29.24  ? 43  ARG B CZ    1 
ATOM   3638 N  NH1   . ARG B 1 64  ? 20.907 9.224   -3.365  1.00 26.78  ? 43  ARG B NH1   1 
ATOM   3639 N  NH2   . ARG B 1 64  ? 21.582 8.587   -1.284  1.00 29.46  ? 43  ARG B NH2   1 
ATOM   3640 N  N     . THR B 1 65  ? 21.947 17.016  -0.282  1.00 31.44  ? 44  THR B N     1 
ATOM   3641 C  CA    . THR B 1 65  ? 21.486 18.427  -0.206  1.00 31.61  ? 44  THR B CA    1 
ATOM   3642 C  C     . THR B 1 65  ? 22.686 19.302  0.148   1.00 35.60  ? 44  THR B C     1 
ATOM   3643 O  O     . THR B 1 65  ? 23.441 18.964  1.065   1.00 41.55  ? 44  THR B O     1 
ATOM   3644 C  CB    . THR B 1 65  ? 20.297 18.594  0.746   1.00 33.18  ? 44  THR B CB    1 
ATOM   3645 O  OG1   . THR B 1 65  ? 20.775 18.434  2.077   1.00 30.81  ? 44  THR B OG1   1 
ATOM   3646 C  CG2   . THR B 1 65  ? 19.165 17.625  0.468   1.00 32.67  ? 44  THR B CG2   1 
ATOM   3647 N  N     . CYS B 1 66  ? 22.873 20.375  -0.603  1.00 36.70  ? 45  CYS B N     1 
ATOM   3648 C  CA    . CYS B 1 66  ? 24.033 21.274  -0.485  1.00 39.93  ? 45  CYS B CA    1 
ATOM   3649 C  C     . CYS B 1 66  ? 23.573 22.675  -0.887  1.00 38.36  ? 45  CYS B C     1 
ATOM   3650 O  O     . CYS B 1 66  ? 23.009 22.796  -1.982  1.00 36.72  ? 45  CYS B O     1 
ATOM   3651 C  CB    . CYS B 1 66  ? 25.172 20.798  -1.376  1.00 40.13  ? 45  CYS B CB    1 
ATOM   3652 S  SG    . CYS B 1 66  ? 26.726 21.701  -1.127  1.00 43.22  ? 45  CYS B SG    1 
ATOM   3653 N  N     . THR B 1 67  ? 23.805 23.664  -0.027  1.00 37.82  ? 46  THR B N     1 
ATOM   3654 C  CA    . THR B 1 67  ? 23.382 25.079  -0.226  1.00 41.04  ? 46  THR B CA    1 
ATOM   3655 C  C     . THR B 1 67  ? 24.587 26.014  -0.086  1.00 41.06  ? 46  THR B C     1 
ATOM   3656 O  O     . THR B 1 67  ? 25.315 25.895  0.904   1.00 38.30  ? 46  THR B O     1 
ATOM   3657 C  CB    . THR B 1 67  ? 22.256 25.440  0.751   1.00 39.80  ? 46  THR B CB    1 
ATOM   3658 O  OG1   . THR B 1 67  ? 21.232 24.434  0.611   1.00 38.52  ? 46  THR B OG1   1 
ATOM   3659 C  CG2   . THR B 1 67  ? 21.724 26.834  0.493   1.00 35.39  ? 46  THR B CG2   1 
ATOM   3660 N  N     . GLU B 1 68  ? 24.820 26.871  -1.073  1.00 44.77  ? 47  GLU B N     1 
ATOM   3661 C  CA    . GLU B 1 68  ? 25.880 27.911  -1.029  1.00 47.83  ? 47  GLU B CA    1 
ATOM   3662 C  C     . GLU B 1 68  ? 25.219 29.290  -1.193  1.00 48.68  ? 47  GLU B C     1 
ATOM   3663 O  O     . GLU B 1 68  ? 24.170 29.373  -1.872  1.00 45.06  ? 47  GLU B O     1 
ATOM   3664 C  CB    . GLU B 1 68  ? 26.950 27.624  -2.092  1.00 48.82  ? 47  GLU B CB    1 
ATOM   3665 C  CG    . GLU B 1 68  ? 28.054 26.694  -1.603  1.00 52.80  ? 47  GLU B CG    1 
ATOM   3666 C  CD    . GLU B 1 68  ? 29.137 26.241  -2.585  1.00 54.12  ? 47  GLU B CD    1 
ATOM   3667 O  OE1   . GLU B 1 68  ? 29.083 26.591  -3.789  1.00 49.39  ? 47  GLU B OE1   1 
ATOM   3668 O  OE2   . GLU B 1 68  ? 30.057 25.531  -2.131  1.00 62.03  ? 47  GLU B OE2   1 
ATOM   3669 N  N     . GLU B 1 69  ? 25.822 30.318  -0.587  1.00 45.63  ? 48  GLU B N     1 
ATOM   3670 C  CA    . GLU B 1 69  ? 25.373 31.735  -0.622  1.00 49.63  ? 48  GLU B CA    1 
ATOM   3671 C  C     . GLU B 1 69  ? 26.158 32.450  -1.733  1.00 46.08  ? 48  GLU B C     1 
ATOM   3672 O  O     . GLU B 1 69  ? 27.384 32.538  -1.600  1.00 49.58  ? 48  GLU B O     1 
ATOM   3673 C  CB    . GLU B 1 69  ? 25.585 32.353  0.766   1.00 52.92  ? 48  GLU B CB    1 
ATOM   3674 C  CG    . GLU B 1 69  ? 25.330 33.857  0.847   1.00 59.04  ? 48  GLU B CG    1 
ATOM   3675 C  CD    . GLU B 1 69  ? 23.871 34.297  0.878   1.00 65.95  ? 48  GLU B CD    1 
ATOM   3676 O  OE1   . GLU B 1 69  ? 22.991 33.431  1.082   1.00 76.10  ? 48  GLU B OE1   1 
ATOM   3677 O  OE2   . GLU B 1 69  ? 23.611 35.512  0.703   1.00 66.86  ? 48  GLU B OE2   1 
ATOM   3678 N  N     . HIS B 1 70  ? 25.490 32.865  -2.815  1.00 41.77  ? 49  HIS B N     1 
ATOM   3679 C  CA    . HIS B 1 70  ? 26.081 33.595  -3.972  1.00 42.66  ? 49  HIS B CA    1 
ATOM   3680 C  C     . HIS B 1 70  ? 25.150 34.747  -4.332  1.00 40.60  ? 49  HIS B C     1 
ATOM   3681 O  O     . HIS B 1 70  ? 23.924 34.560  -4.216  1.00 41.28  ? 49  HIS B O     1 
ATOM   3682 C  CB    . HIS B 1 70  ? 26.259 32.699  -5.208  1.00 44.20  ? 49  HIS B CB    1 
ATOM   3683 C  CG    . HIS B 1 70  ? 27.384 31.724  -5.124  1.00 48.83  ? 49  HIS B CG    1 
ATOM   3684 N  ND1   . HIS B 1 70  ? 27.193 30.393  -4.776  1.00 49.11  ? 49  HIS B ND1   1 
ATOM   3685 C  CD2   . HIS B 1 70  ? 28.703 31.860  -5.369  1.00 49.55  ? 49  HIS B CD2   1 
ATOM   3686 C  CE1   . HIS B 1 70  ? 28.353 29.766  -4.793  1.00 46.34  ? 49  HIS B CE1   1 
ATOM   3687 N  NE2   . HIS B 1 70  ? 29.290 30.641  -5.144  1.00 44.25  ? 49  HIS B NE2   1 
ATOM   3688 N  N     . HIS B 1 71  ? 25.707 35.878  -4.759  1.00 40.26  ? 50  HIS B N     1 
ATOM   3689 C  CA    . HIS B 1 71  ? 24.944 37.084  -5.182  1.00 42.46  ? 50  HIS B CA    1 
ATOM   3690 C  C     . HIS B 1 71  ? 23.791 37.351  -4.208  1.00 41.86  ? 50  HIS B C     1 
ATOM   3691 O  O     . HIS B 1 71  ? 22.666 37.531  -4.678  1.00 40.73  ? 50  HIS B O     1 
ATOM   3692 C  CB    . HIS B 1 71  ? 24.452 36.915  -6.624  1.00 46.32  ? 50  HIS B CB    1 
ATOM   3693 C  CG    . HIS B 1 71  ? 25.575 36.579  -7.542  1.00 52.87  ? 50  HIS B CG    1 
ATOM   3694 N  ND1   . HIS B 1 71  ? 25.839 35.272  -7.926  1.00 52.66  ? 50  HIS B ND1   1 
ATOM   3695 C  CD2   . HIS B 1 71  ? 26.556 37.352  -8.064  1.00 52.84  ? 50  HIS B CD2   1 
ATOM   3696 C  CE1   . HIS B 1 71  ? 26.923 35.263  -8.673  1.00 54.48  ? 50  HIS B CE1   1 
ATOM   3697 N  NE2   . HIS B 1 71  ? 27.379 36.529  -8.778  1.00 54.07  ? 50  HIS B NE2   1 
ATOM   3698 N  N     . GLY B 1 72  ? 24.075 37.313  -2.905  1.00 40.76  ? 51  GLY B N     1 
ATOM   3699 C  CA    . GLY B 1 72  ? 23.126 37.631  -1.822  1.00 41.56  ? 51  GLY B CA    1 
ATOM   3700 C  C     . GLY B 1 72  ? 21.921 36.702  -1.752  1.00 43.68  ? 51  GLY B C     1 
ATOM   3701 O  O     . GLY B 1 72  ? 20.873 37.152  -1.248  1.00 51.45  ? 51  GLY B O     1 
ATOM   3702 N  N     . THR B 1 73  ? 22.013 35.467  -2.238  1.00 44.51  ? 52  THR B N     1 
ATOM   3703 C  CA    . THR B 1 73  ? 20.883 34.508  -2.155  1.00 43.16  ? 52  THR B CA    1 
ATOM   3704 C  C     . THR B 1 73  ? 21.426 33.094  -2.007  1.00 41.71  ? 52  THR B C     1 
ATOM   3705 O  O     . THR B 1 73  ? 22.641 32.928  -1.958  1.00 46.67  ? 52  THR B O     1 
ATOM   3706 C  CB    . THR B 1 73  ? 19.903 34.652  -3.330  1.00 45.65  ? 52  THR B CB    1 
ATOM   3707 O  OG1   . THR B 1 73  ? 18.682 34.007  -2.946  1.00 43.20  ? 52  THR B OG1   1 
ATOM   3708 C  CG2   . THR B 1 73  ? 20.420 34.076  -4.629  1.00 44.39  ? 52  THR B CG2   1 
ATOM   3709 N  N     . TRP B 1 74  ? 20.535 32.124  -1.868  1.00 39.67  ? 53  TRP B N     1 
ATOM   3710 C  CA    . TRP B 1 74  ? 20.926 30.719  -1.608  1.00 40.78  ? 53  TRP B CA    1 
ATOM   3711 C  C     . TRP B 1 74  ? 20.945 29.983  -2.943  1.00 41.17  ? 53  TRP B C     1 
ATOM   3712 O  O     . TRP B 1 74  ? 20.076 30.239  -3.808  1.00 40.28  ? 53  TRP B O     1 
ATOM   3713 C  CB    . TRP B 1 74  ? 19.997 30.060  -0.587  1.00 37.76  ? 53  TRP B CB    1 
ATOM   3714 C  CG    . TRP B 1 74  ? 18.557 30.107  -0.986  1.00 38.58  ? 53  TRP B CG    1 
ATOM   3715 C  CD1   . TRP B 1 74  ? 17.871 29.195  -1.738  1.00 39.63  ? 53  TRP B CD1   1 
ATOM   3716 C  CD2   . TRP B 1 74  ? 17.632 31.158  -0.676  1.00 38.03  ? 53  TRP B CD2   1 
ATOM   3717 N  NE1   . TRP B 1 74  ? 16.570 29.586  -1.887  1.00 39.45  ? 53  TRP B NE1   1 
ATOM   3718 C  CE2   . TRP B 1 74  ? 16.398 30.796  -1.260  1.00 39.24  ? 53  TRP B CE2   1 
ATOM   3719 C  CE3   . TRP B 1 74  ? 17.730 32.364  0.035   1.00 38.07  ? 53  TRP B CE3   1 
ATOM   3720 C  CZ2   . TRP B 1 74  ? 15.267 31.605  -1.140  1.00 39.34  ? 53  TRP B CZ2   1 
ATOM   3721 C  CZ3   . TRP B 1 74  ? 16.610 33.161  0.154   1.00 38.58  ? 53  TRP B CZ3   1 
ATOM   3722 C  CH2   . TRP B 1 74  ? 15.395 32.781  -0.421  1.00 38.14  ? 53  TRP B CH2   1 
ATOM   3723 N  N     . ILE B 1 75  ? 21.949 29.147  -3.122  1.00 40.00  ? 54  ILE B N     1 
ATOM   3724 C  CA    . ILE B 1 75  ? 22.066 28.292  -4.333  1.00 39.69  ? 54  ILE B CA    1 
ATOM   3725 C  C     . ILE B 1 75  ? 22.009 26.830  -3.889  1.00 33.67  ? 54  ILE B C     1 
ATOM   3726 O  O     . ILE B 1 75  ? 22.979 26.358  -3.296  1.00 31.24  ? 54  ILE B O     1 
ATOM   3727 C  CB    . ILE B 1 75  ? 23.347 28.637  -5.103  1.00 37.19  ? 54  ILE B CB    1 
ATOM   3728 C  CG1   . ILE B 1 75  ? 23.358 30.104  -5.549  1.00 40.02  ? 54  ILE B CG1   1 
ATOM   3729 C  CG2   . ILE B 1 75  ? 23.508 27.687  -6.269  1.00 42.81  ? 54  ILE B CG2   1 
ATOM   3730 C  CD1   . ILE B 1 75  ? 22.270 30.468  -6.537  1.00 38.25  ? 54  ILE B CD1   1 
ATOM   3731 N  N     . ASP B 1 76  ? 20.888 26.164  -4.143  1.00 31.96  ? 55  ASP B N     1 
ATOM   3732 C  CA    . ASP B 1 76  ? 20.736 24.706  -3.889  1.00 33.16  ? 55  ASP B CA    1 
ATOM   3733 C  C     . ASP B 1 76  ? 21.472 23.948  -5.016  1.00 32.85  ? 55  ASP B C     1 
ATOM   3734 O  O     . ASP B 1 76  ? 20.981 23.897  -6.122  1.00 34.99  ? 55  ASP B O     1 
ATOM   3735 C  CB    . ASP B 1 76  ? 19.257 24.330  -3.710  1.00 33.26  ? 55  ASP B CB    1 
ATOM   3736 C  CG    . ASP B 1 76  ? 18.707 24.558  -2.288  1.00 33.85  ? 55  ASP B CG    1 
ATOM   3737 O  OD1   . ASP B 1 76  ? 19.390 24.181  -1.309  1.00 30.50  ? 55  ASP B OD1   1 
ATOM   3738 O  OD2   . ASP B 1 76  ? 17.590 25.100  -2.156  1.00 32.12  ? 55  ASP B OD2   1 
ATOM   3739 N  N     . LEU B 1 77  ? 22.629 23.365  -4.726  1.00 32.26  ? 56  LEU B N     1 
ATOM   3740 C  CA    . LEU B 1 77  ? 23.414 22.567  -5.693  1.00 32.76  ? 56  LEU B CA    1 
ATOM   3741 C  C     . LEU B 1 77  ? 22.900 21.124  -5.741  1.00 30.11  ? 56  LEU B C     1 
ATOM   3742 O  O     . LEU B 1 77  ? 23.158 20.464  -6.746  1.00 30.90  ? 56  LEU B O     1 
ATOM   3743 C  CB    . LEU B 1 77  ? 24.882 22.641  -5.272  1.00 34.06  ? 56  LEU B CB    1 
ATOM   3744 C  CG    . LEU B 1 77  ? 25.507 24.020  -5.420  1.00 36.71  ? 56  LEU B CG    1 
ATOM   3745 C  CD1   . LEU B 1 77  ? 26.880 24.051  -4.775  1.00 45.06  ? 56  LEU B CD1   1 
ATOM   3746 C  CD2   . LEU B 1 77  ? 25.602 24.393  -6.887  1.00 38.44  ? 56  LEU B CD2   1 
ATOM   3747 N  N     . GLY B 1 78  ? 22.189 20.669  -4.706  1.00 30.97  ? 57  GLY B N     1 
ATOM   3748 C  CA    . GLY B 1 78  ? 21.545 19.335  -4.653  1.00 28.80  ? 57  GLY B CA    1 
ATOM   3749 C  C     . GLY B 1 78  ? 20.050 19.464  -4.517  1.00 29.26  ? 57  GLY B C     1 
ATOM   3750 O  O     . GLY B 1 78  ? 19.526 20.450  -5.007  1.00 30.00  ? 57  GLY B O     1 
ATOM   3751 N  N     . GLY B 1 79  ? 19.397 18.521  -3.839  1.00 31.89  ? 58  GLY B N     1 
ATOM   3752 C  CA    . GLY B 1 79  ? 17.944 18.538  -3.557  1.00 34.41  ? 58  GLY B CA    1 
ATOM   3753 C  C     . GLY B 1 79  ? 17.413 19.902  -3.130  1.00 31.14  ? 58  GLY B C     1 
ATOM   3754 O  O     . GLY B 1 79  ? 18.062 20.556  -2.302  1.00 36.36  ? 58  GLY B O     1 
ATOM   3755 N  N     . GLN B 1 80  ? 16.264 20.316  -3.669  1.00 34.77  ? 59  GLN B N     1 
ATOM   3756 C  CA    . GLN B 1 80  ? 15.739 21.703  -3.497  1.00 36.38  ? 59  GLN B CA    1 
ATOM   3757 C  C     . GLN B 1 80  ? 14.197 21.786  -3.404  1.00 36.63  ? 59  GLN B C     1 
ATOM   3758 O  O     . GLN B 1 80  ? 13.714 22.781  -2.787  1.00 33.96  ? 59  GLN B O     1 
ATOM   3759 C  CB    . GLN B 1 80  ? 16.304 22.586  -4.613  1.00 36.78  ? 59  GLN B CB    1 
ATOM   3760 C  CG    . GLN B 1 80  ? 15.644 22.423  -5.966  1.00 36.96  ? 59  GLN B CG    1 
ATOM   3761 C  CD    . GLN B 1 80  ? 15.984 23.571  -6.884  1.00 39.68  ? 59  GLN B CD    1 
ATOM   3762 O  OE1   . GLN B 1 80  ? 17.104 24.072  -6.901  1.00 37.17  ? 59  GLN B OE1   1 
ATOM   3763 N  NE2   . GLN B 1 80  ? 15.002 24.024  -7.641  1.00 45.39  ? 59  GLN B NE2   1 
ATOM   3764 N  N     . TRP B 1 81  ? 13.455 20.839  -3.999  1.00 35.70  ? 60  TRP B N     1 
ATOM   3765 C  CA    . TRP B 1 81  ? 11.969 20.841  -4.091  1.00 36.29  ? 60  TRP B CA    1 
ATOM   3766 C  C     . TRP B 1 81  ? 11.324 19.869  -3.099  1.00 34.18  ? 60  TRP B C     1 
ATOM   3767 O  O     . TRP B 1 81  ? 11.834 18.739  -2.980  1.00 34.15  ? 60  TRP B O     1 
ATOM   3768 C  CB    . TRP B 1 81  ? 11.518 20.474  -5.496  1.00 35.29  ? 60  TRP B CB    1 
ATOM   3769 C  CG    . TRP B 1 81  ? 11.694 21.560  -6.500  1.00 41.35  ? 60  TRP B CG    1 
ATOM   3770 C  CD1   . TRP B 1 81  ? 11.204 22.832  -6.441  1.00 38.82  ? 60  TRP B CD1   1 
ATOM   3771 C  CD2   . TRP B 1 81  ? 12.354 21.430  -7.765  1.00 38.80  ? 60  TRP B CD2   1 
ATOM   3772 N  NE1   . TRP B 1 81  ? 11.533 23.508  -7.580  1.00 39.76  ? 60  TRP B NE1   1 
ATOM   3773 C  CE2   . TRP B 1 81  ? 12.235 22.673  -8.413  1.00 42.42  ? 60  TRP B CE2   1 
ATOM   3774 C  CE3   . TRP B 1 81  ? 13.025 20.389  -8.411  1.00 47.62  ? 60  TRP B CE3   1 
ATOM   3775 C  CZ2   . TRP B 1 81  ? 12.801 22.907  -9.669  1.00 45.48  ? 60  TRP B CZ2   1 
ATOM   3776 C  CZ3   . TRP B 1 81  ? 13.571 20.617  -9.662  1.00 46.99  ? 60  TRP B CZ3   1 
ATOM   3777 C  CH2   . TRP B 1 81  ? 13.457 21.860  -10.278 1.00 44.01  ? 60  TRP B CH2   1 
ATOM   3778 N  N     . ILE B 1 82  ? 10.191 20.268  -2.501  1.00 33.65  ? 61  ILE B N     1 
ATOM   3779 C  CA    . ILE B 1 82  ? 9.225  19.362  -1.787  1.00 36.43  ? 61  ILE B CA    1 
ATOM   3780 C  C     . ILE B 1 82  ? 7.835  19.601  -2.384  1.00 43.51  ? 61  ILE B C     1 
ATOM   3781 O  O     . ILE B 1 82  ? 7.608  20.698  -2.954  1.00 45.73  ? 61  ILE B O     1 
ATOM   3782 C  CB    . ILE B 1 82  ? 9.235  19.575  -0.259  1.00 36.62  ? 61  ILE B CB    1 
ATOM   3783 C  CG1   . ILE B 1 82  ? 8.456  20.836  0.138   1.00 35.81  ? 61  ILE B CG1   1 
ATOM   3784 C  CG2   . ILE B 1 82  ? 10.662 19.581  0.287   1.00 34.59  ? 61  ILE B CG2   1 
ATOM   3785 C  CD1   . ILE B 1 82  ? 8.443  21.100  1.620   1.00 37.03  ? 61  ILE B CD1   1 
ATOM   3786 N  N     . GLY B 1 83  ? 6.941  18.617  -2.277  1.00 41.02  ? 62  GLY B N     1 
ATOM   3787 C  CA    . GLY B 1 83  ? 5.620  18.648  -2.927  1.00 40.44  ? 62  GLY B CA    1 
ATOM   3788 C  C     . GLY B 1 83  ? 4.552  17.972  -2.075  1.00 39.96  ? 62  GLY B C     1 
ATOM   3789 O  O     . GLY B 1 83  ? 4.874  17.432  -1.037  1.00 37.49  ? 62  GLY B O     1 
ATOM   3790 N  N     . PRO B 1 84  ? 3.255  18.065  -2.446  1.00 45.28  ? 63  PRO B N     1 
ATOM   3791 C  CA    . PRO B 1 84  ? 2.190  17.308  -1.789  1.00 45.77  ? 63  PRO B CA    1 
ATOM   3792 C  C     . PRO B 1 84  ? 2.370  15.780  -1.765  1.00 46.40  ? 63  PRO B C     1 
ATOM   3793 O  O     . PRO B 1 84  ? 2.724  15.202  -2.773  1.00 47.72  ? 63  PRO B O     1 
ATOM   3794 C  CB    . PRO B 1 84  ? 0.930  17.635  -2.623  1.00 46.76  ? 63  PRO B CB    1 
ATOM   3795 C  CG    . PRO B 1 84  ? 1.437  18.303  -3.882  1.00 49.17  ? 63  PRO B CG    1 
ATOM   3796 C  CD    . PRO B 1 84  ? 2.732  18.975  -3.477  1.00 47.66  ? 63  PRO B CD    1 
ATOM   3797 N  N     . GLY B 1 85  ? 2.045  15.156  -0.626  1.00 42.91  ? 64  GLY B N     1 
ATOM   3798 C  CA    . GLY B 1 85  ? 2.211  13.706  -0.405  1.00 41.67  ? 64  GLY B CA    1 
ATOM   3799 C  C     . GLY B 1 85  ? 3.533  13.428  0.290   1.00 38.35  ? 64  GLY B C     1 
ATOM   3800 O  O     . GLY B 1 85  ? 3.743  12.293  0.683   1.00 43.45  ? 64  GLY B O     1 
ATOM   3801 N  N     . GLN B 1 86  ? 4.393  14.442  0.422   1.00 36.07  ? 65  GLN B N     1 
ATOM   3802 C  CA    . GLN B 1 86  ? 5.714  14.366  1.092   1.00 36.52  ? 65  GLN B CA    1 
ATOM   3803 C  C     . GLN B 1 86  ? 5.524  14.897  2.517   1.00 38.19  ? 65  GLN B C     1 
ATOM   3804 O  O     . GLN B 1 86  ? 6.021  15.987  2.829   1.00 36.16  ? 65  GLN B O     1 
ATOM   3805 C  CB    . GLN B 1 86  ? 6.794  15.101  0.286   1.00 35.95  ? 65  GLN B CB    1 
ATOM   3806 C  CG    . GLN B 1 86  ? 7.136  14.441  -1.053  1.00 35.52  ? 65  GLN B CG    1 
ATOM   3807 C  CD    . GLN B 1 86  ? 8.033  15.284  -1.934  1.00 36.99  ? 65  GLN B CD    1 
ATOM   3808 O  OE1   . GLN B 1 86  ? 8.575  16.318  -1.524  1.00 36.39  ? 65  GLN B OE1   1 
ATOM   3809 N  NE2   . GLN B 1 86  ? 8.215  14.835  -3.161  1.00 36.25  ? 65  GLN B NE2   1 
ATOM   3810 N  N     . ASP B 1 87  ? 4.828  14.114  3.347   1.00 39.08  ? 66  ASP B N     1 
ATOM   3811 C  CA    . ASP B 1 87  ? 4.316  14.529  4.681   1.00 40.86  ? 66  ASP B CA    1 
ATOM   3812 C  C     . ASP B 1 87  ? 5.480  14.671  5.674   1.00 42.10  ? 66  ASP B C     1 
ATOM   3813 O  O     . ASP B 1 87  ? 5.401  15.556  6.543   1.00 44.07  ? 66  ASP B O     1 
ATOM   3814 C  CB    . ASP B 1 87  ? 3.198  13.574  5.117   1.00 43.62  ? 66  ASP B CB    1 
ATOM   3815 C  CG    . ASP B 1 87  ? 2.041  13.579  4.128   1.00 46.22  ? 66  ASP B CG    1 
ATOM   3816 O  OD1   . ASP B 1 87  ? 1.637  14.685  3.714   1.00 51.27  ? 66  ASP B OD1   1 
ATOM   3817 O  OD2   . ASP B 1 87  ? 1.599  12.493  3.715   1.00 49.83  ? 66  ASP B OD2   1 
ATOM   3818 N  N     . ARG B 1 88  ? 6.553  13.884  5.540   1.00 38.91  ? 67  ARG B N     1 
ATOM   3819 C  CA    . ARG B 1 88  ? 7.618  13.833  6.573   1.00 37.90  ? 67  ARG B CA    1 
ATOM   3820 C  C     . ARG B 1 88  ? 8.504  15.073  6.468   1.00 37.69  ? 67  ARG B C     1 
ATOM   3821 O  O     . ARG B 1 88  ? 8.858  15.632  7.526   1.00 36.14  ? 67  ARG B O     1 
ATOM   3822 C  CB    . ARG B 1 88  ? 8.407  12.526  6.471   1.00 42.10  ? 67  ARG B CB    1 
ATOM   3823 C  CG    . ARG B 1 88  ? 7.563  11.290  6.763   1.00 43.87  ? 67  ARG B CG    1 
ATOM   3824 C  CD    . ARG B 1 88  ? 8.312  10.039  6.371   1.00 49.93  ? 67  ARG B CD    1 
ATOM   3825 N  NE    . ARG B 1 88  ? 7.448  8.913   6.049   1.00 55.69  ? 67  ARG B NE    1 
ATOM   3826 C  CZ    . ARG B 1 88  ? 6.983  8.039   6.930   1.00 56.88  ? 67  ARG B CZ    1 
ATOM   3827 N  NH1   . ARG B 1 88  ? 7.281  8.156   8.211   1.00 60.54  ? 67  ARG B NH1   1 
ATOM   3828 N  NH2   . ARG B 1 88  ? 6.218  7.042   6.527   1.00 60.67  ? 67  ARG B NH2   1 
ATOM   3829 N  N     . VAL B 1 89  ? 8.867  15.493  5.250   1.00 37.39  ? 68  VAL B N     1 
ATOM   3830 C  CA    . VAL B 1 89  ? 9.776  16.662  5.049   1.00 34.48  ? 68  VAL B CA    1 
ATOM   3831 C  C     . VAL B 1 89  ? 8.975  17.958  5.314   1.00 33.66  ? 68  VAL B C     1 
ATOM   3832 O  O     . VAL B 1 89  ? 9.568  18.906  5.862   1.00 33.63  ? 68  VAL B O     1 
ATOM   3833 C  CB    . VAL B 1 89  ? 10.480 16.631  3.674   1.00 33.80  ? 68  VAL B CB    1 
ATOM   3834 C  CG1   . VAL B 1 89  ? 9.506  16.658  2.502   1.00 32.43  ? 68  VAL B CG1   1 
ATOM   3835 C  CG2   . VAL B 1 89  ? 11.498 17.752  3.535   1.00 33.73  ? 68  VAL B CG2   1 
ATOM   3836 N  N     . ALA B 1 90  ? 7.685  18.000  4.977   1.00 32.88  ? 69  ALA B N     1 
ATOM   3837 C  CA    . ALA B 1 90  ? 6.771  19.114  5.340   1.00 41.54  ? 69  ALA B CA    1 
ATOM   3838 C  C     . ALA B 1 90  ? 6.635  19.189  6.879   1.00 42.27  ? 69  ALA B C     1 
ATOM   3839 O  O     . ALA B 1 90  ? 6.749  20.295  7.430   1.00 38.13  ? 69  ALA B O     1 
ATOM   3840 C  CB    . ALA B 1 90  ? 5.425  18.966  4.646   1.00 39.13  ? 69  ALA B CB    1 
ATOM   3841 N  N     . ALA B 1 91  ? 6.428  18.059  7.567   1.00 39.91  ? 70  ALA B N     1 
ATOM   3842 C  CA    . ALA B 1 91  ? 6.352  18.018  9.041   1.00 37.68  ? 70  ALA B CA    1 
ATOM   3843 C  C     . ALA B 1 91  ? 7.666  18.567  9.616   1.00 44.88  ? 70  ALA B C     1 
ATOM   3844 O  O     . ALA B 1 91  ? 7.619  19.442  10.495  1.00 52.08  ? 70  ALA B O     1 
ATOM   3845 C  CB    . ALA B 1 91  ? 6.061  16.618  9.496   1.00 37.08  ? 70  ALA B CB    1 
ATOM   3846 N  N     . LEU B 1 92  ? 8.808  18.149  9.071   1.00 41.27  ? 71  LEU B N     1 
ATOM   3847 C  CA    . LEU B 1 92  ? 10.142 18.481  9.624   1.00 42.52  ? 71  LEU B CA    1 
ATOM   3848 C  C     . LEU B 1 92  ? 10.417 19.976  9.433   1.00 41.23  ? 71  LEU B C     1 
ATOM   3849 O  O     . LEU B 1 92  ? 11.053 20.562  10.309  1.00 37.61  ? 71  LEU B O     1 
ATOM   3850 C  CB    . LEU B 1 92  ? 11.208 17.628  8.921   1.00 42.91  ? 71  LEU B CB    1 
ATOM   3851 C  CG    . LEU B 1 92  ? 12.648 17.894  9.350   1.00 46.12  ? 71  LEU B CG    1 
ATOM   3852 C  CD1   . LEU B 1 92  ? 12.822 17.690  10.844  1.00 49.26  ? 71  LEU B CD1   1 
ATOM   3853 C  CD2   . LEU B 1 92  ? 13.614 17.007  8.587   1.00 47.01  ? 71  LEU B CD2   1 
ATOM   3854 N  N     . ALA B 1 93  ? 9.968  20.557  8.320   1.00 42.36  ? 72  ALA B N     1 
ATOM   3855 C  CA    . ALA B 1 93  ? 10.217 21.975  7.949   1.00 49.19  ? 72  ALA B CA    1 
ATOM   3856 C  C     . ALA B 1 93  ? 9.412  22.908  8.877   1.00 46.00  ? 72  ALA B C     1 
ATOM   3857 O  O     . ALA B 1 93  ? 9.974  23.942  9.336   1.00 42.28  ? 72  ALA B O     1 
ATOM   3858 C  CB    . ALA B 1 93  ? 9.905  22.201  6.477   1.00 47.92  ? 72  ALA B CB    1 
ATOM   3859 N  N     . ALA B 1 94  ? 8.149  22.553  9.139   1.00 43.24  ? 73  ALA B N     1 
ATOM   3860 C  CA    . ALA B 1 94  ? 7.229  23.238  10.085  1.00 45.47  ? 73  ALA B CA    1 
ATOM   3861 C  C     . ALA B 1 94  ? 7.808  23.177  11.512  1.00 42.70  ? 73  ALA B C     1 
ATOM   3862 O  O     . ALA B 1 94  ? 8.054  24.227  12.113  1.00 46.50  ? 73  ALA B O     1 
ATOM   3863 C  CB    . ALA B 1 94  ? 5.862  22.602  9.992   1.00 41.15  ? 73  ALA B CB    1 
ATOM   3864 N  N     . GLU B 1 95  ? 8.134  21.985  11.993  1.00 49.04  ? 74  GLU B N     1 
ATOM   3865 C  CA    . GLU B 1 95  ? 8.722  21.790  13.344  1.00 51.97  ? 74  GLU B CA    1 
ATOM   3866 C  C     . GLU B 1 95  ? 10.002 22.625  13.532  1.00 47.82  ? 74  GLU B C     1 
ATOM   3867 O  O     . GLU B 1 95  ? 10.160 23.172  14.628  1.00 40.56  ? 74  GLU B O     1 
ATOM   3868 C  CB    . GLU B 1 95  ? 9.019  20.320  13.600  1.00 56.12  ? 74  GLU B CB    1 
ATOM   3869 C  CG    . GLU B 1 95  ? 9.516  20.066  15.005  1.00 65.65  ? 74  GLU B CG    1 
ATOM   3870 C  CD    . GLU B 1 95  ? 10.344 18.803  15.121  1.00 79.34  ? 74  GLU B CD    1 
ATOM   3871 O  OE1   . GLU B 1 95  ? 9.787  17.706  14.865  1.00 80.69  ? 74  GLU B OE1   1 
ATOM   3872 O  OE2   . GLU B 1 95  ? 11.553 18.926  15.433  1.00 96.69  ? 74  GLU B OE2   1 
ATOM   3873 N  N     . LEU B 1 96  ? 10.894 22.725  12.542  1.00 43.48  ? 75  LEU B N     1 
ATOM   3874 C  CA    . LEU B 1 96  ? 12.201 23.418  12.726  1.00 41.67  ? 75  LEU B CA    1 
ATOM   3875 C  C     . LEU B 1 96  ? 12.117 24.892  12.300  1.00 40.58  ? 75  LEU B C     1 
ATOM   3876 O  O     . LEU B 1 96  ? 13.160 25.540  12.337  1.00 41.55  ? 75  LEU B O     1 
ATOM   3877 C  CB    . LEU B 1 96  ? 13.296 22.680  11.950  1.00 42.63  ? 75  LEU B CB    1 
ATOM   3878 C  CG    . LEU B 1 96  ? 13.694 21.301  12.486  1.00 47.33  ? 75  LEU B CG    1 
ATOM   3879 C  CD1   . LEU B 1 96  ? 14.880 20.749  11.694  1.00 46.77  ? 75  LEU B CD1   1 
ATOM   3880 C  CD2   . LEU B 1 96  ? 14.025 21.341  13.980  1.00 48.60  ? 75  LEU B CD2   1 
ATOM   3881 N  N     . GLY B 1 97  ? 10.941 25.398  11.899  1.00 46.85  ? 76  GLY B N     1 
ATOM   3882 C  CA    . GLY B 1 97  ? 10.695 26.837  11.657  1.00 49.48  ? 76  GLY B CA    1 
ATOM   3883 C  C     . GLY B 1 97  ? 11.154 27.336  10.284  1.00 55.25  ? 76  GLY B C     1 
ATOM   3884 O  O     . GLY B 1 97  ? 11.320 28.576  10.134  1.00 59.21  ? 76  GLY B O     1 
ATOM   3885 N  N     . VAL B 1 98  ? 11.311 26.443  9.296   1.00 52.40  ? 77  VAL B N     1 
ATOM   3886 C  CA    . VAL B 1 98  ? 11.671 26.807  7.890   1.00 52.47  ? 77  VAL B CA    1 
ATOM   3887 C  C     . VAL B 1 98  ? 10.386 26.935  7.062   1.00 50.12  ? 77  VAL B C     1 
ATOM   3888 O  O     . VAL B 1 98  ? 9.652  25.927  6.941   1.00 46.70  ? 77  VAL B O     1 
ATOM   3889 C  CB    . VAL B 1 98  ? 12.625 25.789  7.240   1.00 48.72  ? 77  VAL B CB    1 
ATOM   3890 C  CG1   . VAL B 1 98  ? 13.025 26.224  5.840   1.00 48.07  ? 77  VAL B CG1   1 
ATOM   3891 C  CG2   . VAL B 1 98  ? 13.853 25.542  8.097   1.00 51.73  ? 77  VAL B CG2   1 
ATOM   3892 N  N     . GLU B 1 99  ? 10.161 28.118  6.483   1.00 47.70  ? 78  GLU B N     1 
ATOM   3893 C  CA    . GLU B 1 99  ? 9.010  28.392  5.576   1.00 50.75  ? 78  GLU B CA    1 
ATOM   3894 C  C     . GLU B 1 99  ? 9.354  27.953  4.142   1.00 44.13  ? 78  GLU B C     1 
ATOM   3895 O  O     . GLU B 1 99  ? 10.568 27.860  3.774   1.00 38.58  ? 78  GLU B O     1 
ATOM   3896 C  CB    . GLU B 1 99  ? 8.583  29.870  5.606   1.00 53.23  ? 78  GLU B CB    1 
ATOM   3897 C  CG    . GLU B 1 99  ? 8.360  30.453  7.010   1.00 55.21  ? 78  GLU B CG    1 
ATOM   3898 C  CD    . GLU B 1 99  ? 7.280  29.804  7.875   1.00 57.89  ? 78  GLU B CD    1 
ATOM   3899 O  OE1   . GLU B 1 99  ? 6.201  29.465  7.332   1.00 47.68  ? 78  GLU B OE1   1 
ATOM   3900 O  OE2   . GLU B 1 99  ? 7.517  29.639  9.107   1.00 65.66  ? 78  GLU B OE2   1 
ATOM   3901 N  N     . THR B 1 100 ? 8.304  27.714  3.363   1.00 40.61  ? 79  THR B N     1 
ATOM   3902 C  CA    . THR B 1 100 ? 8.353  27.335  1.938   1.00 43.17  ? 79  THR B CA    1 
ATOM   3903 C  C     . THR B 1 100 ? 7.936  28.525  1.069   1.00 44.45  ? 79  THR B C     1 
ATOM   3904 O  O     . THR B 1 100 ? 7.108  29.314  1.532   1.00 47.61  ? 79  THR B O     1 
ATOM   3905 C  CB    . THR B 1 100 ? 7.428  26.139  1.691   1.00 45.11  ? 79  THR B CB    1 
ATOM   3906 O  OG1   . THR B 1 100 ? 6.082  26.609  1.651   1.00 41.76  ? 79  THR B OG1   1 
ATOM   3907 C  CG2   . THR B 1 100 ? 7.564  25.065  2.747   1.00 49.77  ? 79  THR B CG2   1 
ATOM   3908 N  N     . TYR B 1 101 ? 8.437  28.602  -0.168  1.00 45.14  ? 80  TYR B N     1 
ATOM   3909 C  CA    . TYR B 1 101 ? 7.869  29.461  -1.243  1.00 47.86  ? 80  TYR B CA    1 
ATOM   3910 C  C     . TYR B 1 101 ? 7.556  28.584  -2.456  1.00 46.55  ? 80  TYR B C     1 
ATOM   3911 O  O     . TYR B 1 101 ? 8.208  27.563  -2.649  1.00 42.59  ? 80  TYR B O     1 
ATOM   3912 C  CB    . TYR B 1 101 ? 8.807  30.624  -1.567  1.00 47.85  ? 80  TYR B CB    1 
ATOM   3913 C  CG    . TYR B 1 101 ? 10.167 30.234  -2.089  1.00 47.41  ? 80  TYR B CG    1 
ATOM   3914 C  CD1   . TYR B 1 101 ? 11.146 29.715  -1.256  1.00 44.82  ? 80  TYR B CD1   1 
ATOM   3915 C  CD2   . TYR B 1 101 ? 10.482 30.404  -3.422  1.00 42.87  ? 80  TYR B CD2   1 
ATOM   3916 C  CE1   . TYR B 1 101 ? 12.395 29.361  -1.739  1.00 42.03  ? 80  TYR B CE1   1 
ATOM   3917 C  CE2   . TYR B 1 101 ? 11.736 30.083  -3.912  1.00 45.39  ? 80  TYR B CE2   1 
ATOM   3918 C  CZ    . TYR B 1 101 ? 12.702 29.567  -3.069  1.00 42.25  ? 80  TYR B CZ    1 
ATOM   3919 O  OH    . TYR B 1 101 ? 13.936 29.250  -3.571  1.00 38.03  ? 80  TYR B OH    1 
ATOM   3920 N  N     . PRO B 1 102 ? 6.540  28.926  -3.291  1.00 46.27  ? 81  PRO B N     1 
ATOM   3921 C  CA    . PRO B 1 102 ? 6.165  28.088  -4.423  1.00 45.83  ? 81  PRO B CA    1 
ATOM   3922 C  C     . PRO B 1 102 ? 7.146  28.307  -5.588  1.00 47.35  ? 81  PRO B C     1 
ATOM   3923 O  O     . PRO B 1 102 ? 7.693  29.395  -5.733  1.00 47.50  ? 81  PRO B O     1 
ATOM   3924 C  CB    . PRO B 1 102 ? 4.727  28.524  -4.771  1.00 45.07  ? 81  PRO B CB    1 
ATOM   3925 C  CG    . PRO B 1 102 ? 4.567  29.923  -4.183  1.00 44.26  ? 81  PRO B CG    1 
ATOM   3926 C  CD    . PRO B 1 102 ? 5.737  30.163  -3.248  1.00 46.65  ? 81  PRO B CD    1 
ATOM   3927 N  N     . GLN B 1 103 ? 7.383  27.245  -6.355  1.00 44.17  ? 82  GLN B N     1 
ATOM   3928 C  CA    . GLN B 1 103 ? 8.095  27.276  -7.659  1.00 40.60  ? 82  GLN B CA    1 
ATOM   3929 C  C     . GLN B 1 103 ? 7.273  28.143  -8.617  1.00 36.36  ? 82  GLN B C     1 
ATOM   3930 O  O     . GLN B 1 103 ? 6.127  27.804  -8.889  1.00 35.08  ? 82  GLN B O     1 
ATOM   3931 C  CB    . GLN B 1 103 ? 8.263  25.825  -8.142  1.00 38.59  ? 82  GLN B CB    1 
ATOM   3932 C  CG    . GLN B 1 103 ? 8.786  25.666  -9.568  1.00 35.17  ? 82  GLN B CG    1 
ATOM   3933 C  CD    . GLN B 1 103 ? 10.149 26.289  -9.739  1.00 32.84  ? 82  GLN B CD    1 
ATOM   3934 O  OE1   . GLN B 1 103 ? 11.114 26.011  -9.030  1.00 30.95  ? 82  GLN B OE1   1 
ATOM   3935 N  NE2   . GLN B 1 103 ? 10.241 27.176  -10.700 1.00 39.14  ? 82  GLN B NE2   1 
ATOM   3936 N  N     . PRO B 1 104 ? 7.791  29.291  -9.131  1.00 40.07  ? 83  PRO B N     1 
ATOM   3937 C  CA    . PRO B 1 104 ? 7.096  30.049  -10.181 1.00 40.36  ? 83  PRO B CA    1 
ATOM   3938 C  C     . PRO B 1 104 ? 6.549  29.095  -11.255 1.00 43.42  ? 83  PRO B C     1 
ATOM   3939 O  O     . PRO B 1 104 ? 7.255  28.144  -11.625 1.00 39.90  ? 83  PRO B O     1 
ATOM   3940 C  CB    . PRO B 1 104 ? 8.175  30.994  -10.725 1.00 40.37  ? 83  PRO B CB    1 
ATOM   3941 C  CG    . PRO B 1 104 ? 9.125  31.210  -9.561  1.00 39.11  ? 83  PRO B CG    1 
ATOM   3942 C  CD    . PRO B 1 104 ? 9.040  29.953  -8.711  1.00 40.93  ? 83  PRO B CD    1 
ATOM   3943 N  N     . THR B 1 105 ? 5.304  29.324  -11.680 1.00 43.25  ? 84  THR B N     1 
ATOM   3944 C  CA    . THR B 1 105 ? 4.505  28.407  -12.537 1.00 45.05  ? 84  THR B CA    1 
ATOM   3945 C  C     . THR B 1 105 ? 3.959  29.141  -13.763 1.00 47.08  ? 84  THR B C     1 
ATOM   3946 O  O     . THR B 1 105 ? 3.488  28.465  -14.704 1.00 45.50  ? 84  THR B O     1 
ATOM   3947 C  CB    . THR B 1 105 ? 3.313  27.828  -11.759 1.00 51.30  ? 84  THR B CB    1 
ATOM   3948 O  OG1   . THR B 1 105 ? 2.336  28.850  -11.574 1.00 48.52  ? 84  THR B OG1   1 
ATOM   3949 C  CG2   . THR B 1 105 ? 3.682  27.280  -10.398 1.00 53.15  ? 84  THR B CG2   1 
ATOM   3950 N  N     . GLU B 1 106 ? 4.015  30.473  -13.748 1.00 53.17  ? 85  GLU B N     1 
ATOM   3951 C  CA    . GLU B 1 106 ? 3.170  31.360  -14.586 1.00 53.51  ? 85  GLU B CA    1 
ATOM   3952 C  C     . GLU B 1 106 ? 3.931  31.696  -15.882 1.00 56.88  ? 85  GLU B C     1 
ATOM   3953 O  O     . GLU B 1 106 ? 5.184  31.878  -15.833 1.00 49.97  ? 85  GLU B O     1 
ATOM   3954 C  CB    . GLU B 1 106 ? 2.805  32.592  -13.753 1.00 59.80  ? 85  GLU B CB    1 
ATOM   3955 C  CG    . GLU B 1 106 ? 1.499  33.254  -14.158 1.00 70.62  ? 85  GLU B CG    1 
ATOM   3956 C  CD    . GLU B 1 106 ? 0.249  32.410  -13.960 1.00 75.39  ? 85  GLU B CD    1 
ATOM   3957 O  OE1   . GLU B 1 106 ? 0.337  31.378  -13.251 1.00 75.56  ? 85  GLU B OE1   1 
ATOM   3958 O  OE2   . GLU B 1 106 ? -0.811 32.787  -14.517 1.00 80.36  ? 85  GLU B OE2   1 
ATOM   3959 N  N     . GLY B 1 107 ? 3.207  31.778  -17.003 1.00 48.24  ? 86  GLY B N     1 
ATOM   3960 C  CA    . GLY B 1 107 ? 3.758  32.212  -18.293 1.00 47.10  ? 86  GLY B CA    1 
ATOM   3961 C  C     . GLY B 1 107 ? 4.126  31.031  -19.158 1.00 46.24  ? 86  GLY B C     1 
ATOM   3962 O  O     . GLY B 1 107 ? 4.029  29.907  -18.673 1.00 50.30  ? 86  GLY B O     1 
ATOM   3963 N  N     . ASP B 1 108 ? 4.577  31.301  -20.382 1.00 44.03  ? 87  ASP B N     1 
ATOM   3964 C  CA    . ASP B 1 108 ? 4.728  30.308  -21.471 1.00 43.63  ? 87  ASP B CA    1 
ATOM   3965 C  C     . ASP B 1 108 ? 5.988  29.457  -21.257 1.00 44.21  ? 87  ASP B C     1 
ATOM   3966 O  O     . ASP B 1 108 ? 7.070  30.025  -21.013 1.00 43.55  ? 87  ASP B O     1 
ATOM   3967 C  CB    . ASP B 1 108 ? 4.818  31.000  -22.831 1.00 48.00  ? 87  ASP B CB    1 
ATOM   3968 C  CG    . ASP B 1 108 ? 3.490  31.411  -23.437 1.00 53.91  ? 87  ASP B CG    1 
ATOM   3969 O  OD1   . ASP B 1 108 ? 2.430  30.997  -22.898 1.00 56.97  ? 87  ASP B OD1   1 
ATOM   3970 O  OD2   . ASP B 1 108 ? 3.531  32.136  -24.459 1.00 56.21  ? 87  ASP B OD2   1 
ATOM   3971 N  N     . ASP B 1 109 ? 5.825  28.145  -21.372 1.00 39.99  ? 88  ASP B N     1 
ATOM   3972 C  CA    . ASP B 1 109 ? 6.910  27.145  -21.544 1.00 44.48  ? 88  ASP B CA    1 
ATOM   3973 C  C     . ASP B 1 109 ? 7.282  27.126  -23.037 1.00 40.89  ? 88  ASP B C     1 
ATOM   3974 O  O     . ASP B 1 109 ? 6.379  27.332  -23.890 1.00 39.31  ? 88  ASP B O     1 
ATOM   3975 C  CB    . ASP B 1 109 ? 6.476  25.745  -21.067 1.00 45.84  ? 88  ASP B CB    1 
ATOM   3976 C  CG    . ASP B 1 109 ? 5.926  25.645  -19.641 1.00 49.23  ? 88  ASP B CG    1 
ATOM   3977 O  OD1   . ASP B 1 109 ? 6.466  26.301  -18.726 1.00 46.89  ? 88  ASP B OD1   1 
ATOM   3978 O  OD2   . ASP B 1 109 ? 4.974  24.879  -19.444 1.00 56.80  ? 88  ASP B OD2   1 
ATOM   3979 N  N     . VAL B 1 110 ? 8.556  26.887  -23.351 1.00 36.61  ? 89  VAL B N     1 
ATOM   3980 C  CA    . VAL B 1 110 ? 9.042  26.664  -24.744 1.00 35.47  ? 89  VAL B CA    1 
ATOM   3981 C  C     . VAL B 1 110 ? 9.398  25.181  -24.917 1.00 35.44  ? 89  VAL B C     1 
ATOM   3982 O  O     . VAL B 1 110 ? 10.161 24.644  -24.091 1.00 36.14  ? 89  VAL B O     1 
ATOM   3983 C  CB    . VAL B 1 110 ? 10.236 27.580  -25.050 1.00 35.94  ? 89  VAL B CB    1 
ATOM   3984 C  CG1   . VAL B 1 110 ? 10.843 27.277  -26.423 1.00 37.72  ? 89  VAL B CG1   1 
ATOM   3985 C  CG2   . VAL B 1 110 ? 9.838  29.047  -24.919 1.00 34.82  ? 89  VAL B CG2   1 
ATOM   3986 N  N     . VAL B 1 111 ? 8.870  24.555  -25.963 1.00 34.46  ? 90  VAL B N     1 
ATOM   3987 C  CA    . VAL B 1 111 ? 9.241  23.182  -26.406 1.00 37.19  ? 90  VAL B CA    1 
ATOM   3988 C  C     . VAL B 1 111 ? 9.910  23.303  -27.778 1.00 38.65  ? 90  VAL B C     1 
ATOM   3989 O  O     . VAL B 1 111 ? 9.346  23.985  -28.654 1.00 36.88  ? 90  VAL B O     1 
ATOM   3990 C  CB    . VAL B 1 111 ? 8.021  22.251  -26.495 1.00 37.49  ? 90  VAL B CB    1 
ATOM   3991 C  CG1   . VAL B 1 111 ? 8.448  20.849  -26.891 1.00 40.39  ? 90  VAL B CG1   1 
ATOM   3992 C  CG2   . VAL B 1 111 ? 7.229  22.220  -25.197 1.00 40.38  ? 90  VAL B CG2   1 
ATOM   3993 N  N     . LEU B 1 112 ? 11.050 22.641  -27.949 1.00 36.65  ? 91  LEU B N     1 
ATOM   3994 C  CA    . LEU B 1 112 ? 11.795 22.551  -29.229 1.00 39.79  ? 91  LEU B CA    1 
ATOM   3995 C  C     . LEU B 1 112 ? 12.081 21.085  -29.566 1.00 39.57  ? 91  LEU B C     1 
ATOM   3996 O  O     . LEU B 1 112 ? 12.926 20.500  -28.886 1.00 41.09  ? 91  LEU B O     1 
ATOM   3997 C  CB    . LEU B 1 112 ? 13.108 23.303  -29.039 1.00 42.19  ? 91  LEU B CB    1 
ATOM   3998 C  CG    . LEU B 1 112 ? 14.074 23.226  -30.211 1.00 44.92  ? 91  LEU B CG    1 
ATOM   3999 C  CD1   . LEU B 1 112 ? 13.512 24.003  -31.395 1.00 39.93  ? 91  LEU B CD1   1 
ATOM   4000 C  CD2   . LEU B 1 112 ? 15.442 23.743  -29.786 1.00 46.78  ? 91  LEU B CD2   1 
ATOM   4001 N  N     . PHE B 1 113 ? 11.426 20.523  -30.581 1.00 42.02  ? 92  PHE B N     1 
ATOM   4002 C  CA    . PHE B 1 113 ? 11.628 19.124  -31.035 1.00 44.32  ? 92  PHE B CA    1 
ATOM   4003 C  C     . PHE B 1 113 ? 12.814 19.090  -31.996 1.00 47.61  ? 92  PHE B C     1 
ATOM   4004 O  O     . PHE B 1 113 ? 13.294 20.167  -32.387 1.00 53.63  ? 92  PHE B O     1 
ATOM   4005 C  CB    . PHE B 1 113 ? 10.355 18.593  -31.697 1.00 48.46  ? 92  PHE B CB    1 
ATOM   4006 C  CG    . PHE B 1 113 ? 9.152  18.528  -30.786 1.00 52.96  ? 92  PHE B CG    1 
ATOM   4007 C  CD1   . PHE B 1 113 ? 9.086  17.592  -29.760 1.00 56.81  ? 92  PHE B CD1   1 
ATOM   4008 C  CD2   . PHE B 1 113 ? 8.073  19.384  -30.967 1.00 56.33  ? 92  PHE B CD2   1 
ATOM   4009 C  CE1   . PHE B 1 113 ? 7.972  17.520  -28.938 1.00 56.18  ? 92  PHE B CE1   1 
ATOM   4010 C  CE2   . PHE B 1 113 ? 6.954  19.308  -30.153 1.00 55.13  ? 92  PHE B CE2   1 
ATOM   4011 C  CZ    . PHE B 1 113 ? 6.908  18.377  -29.140 1.00 60.66  ? 92  PHE B CZ    1 
ATOM   4012 N  N     . GLY B 1 114 ? 13.248 17.890  -32.382 1.00 52.74  ? 93  GLY B N     1 
ATOM   4013 C  CA    . GLY B 1 114 ? 14.393 17.661  -33.285 1.00 59.08  ? 93  GLY B CA    1 
ATOM   4014 C  C     . GLY B 1 114 ? 14.296 18.472  -34.567 1.00 60.90  ? 93  GLY B C     1 
ATOM   4015 O  O     . GLY B 1 114 ? 15.368 18.819  -35.131 1.00 55.38  ? 93  GLY B O     1 
ATOM   4016 N  N     . ASP B 1 115 ? 13.065 18.754  -35.014 1.00 65.84  ? 94  ASP B N     1 
ATOM   4017 C  CA    . ASP B 1 115 ? 12.743 19.545  -36.235 1.00 69.49  ? 94  ASP B CA    1 
ATOM   4018 C  C     . ASP B 1 115 ? 11.704 20.621  -35.886 1.00 64.36  ? 94  ASP B C     1 
ATOM   4019 O  O     . ASP B 1 115 ? 10.955 20.434  -34.909 1.00 60.41  ? 94  ASP B O     1 
ATOM   4020 C  CB    . ASP B 1 115 ? 12.238 18.631  -37.358 1.00 75.34  ? 94  ASP B CB    1 
ATOM   4021 C  CG    . ASP B 1 115 ? 11.266 17.563  -36.875 1.00 73.77  ? 94  ASP B CG    1 
ATOM   4022 O  OD1   . ASP B 1 115 ? 11.723 16.608  -36.201 1.00 82.40  ? 94  ASP B OD1   1 
ATOM   4023 O  OD2   . ASP B 1 115 ? 10.063 17.709  -37.141 1.00 68.18  ? 94  ASP B OD2   1 
ATOM   4024 N  N     . GLY B 1 116 ? 11.645 21.694  -36.679 1.00 60.33  ? 95  GLY B N     1 
ATOM   4025 C  CA    . GLY B 1 116 ? 10.689 22.809  -36.505 1.00 54.74  ? 95  GLY B CA    1 
ATOM   4026 C  C     . GLY B 1 116 ? 11.226 23.862  -35.541 1.00 49.69  ? 95  GLY B C     1 
ATOM   4027 O  O     . GLY B 1 116 ? 12.331 23.678  -34.977 1.00 39.65  ? 95  GLY B O     1 
ATOM   4028 N  N     . GLU B 1 117 ? 10.463 24.933  -35.349 1.00 51.36  ? 96  GLU B N     1 
ATOM   4029 C  CA    . GLU B 1 117 ? 10.858 26.101  -34.518 1.00 57.30  ? 96  GLU B CA    1 
ATOM   4030 C  C     . GLU B 1 117 ? 10.498 25.846  -33.062 1.00 56.74  ? 96  GLU B C     1 
ATOM   4031 O  O     . GLU B 1 117 ? 9.655  24.998  -32.788 1.00 58.65  ? 96  GLU B O     1 
ATOM   4032 C  CB    . GLU B 1 117 ? 10.101 27.338  -34.973 1.00 52.53  ? 96  GLU B CB    1 
ATOM   4033 C  CG    . GLU B 1 117 ? 10.028 27.470  -36.470 1.00 54.37  ? 96  GLU B CG    1 
ATOM   4034 C  CD    . GLU B 1 117 ? 9.548  28.843  -36.878 1.00 57.27  ? 96  GLU B CD    1 
ATOM   4035 O  OE1   . GLU B 1 117 ? 10.239 29.844  -36.530 1.00 65.07  ? 96  GLU B OE1   1 
ATOM   4036 O  OE2   . GLU B 1 117 ? 8.474  28.914  -37.494 1.00 53.53  ? 96  GLU B OE2   1 
ATOM   4037 N  N     . PRO B 1 118 ? 11.100 26.581  -32.098 1.00 56.25  ? 97  PRO B N     1 
ATOM   4038 C  CA    . PRO B 1 118 ? 10.605 26.584  -30.719 1.00 53.50  ? 97  PRO B CA    1 
ATOM   4039 C  C     . PRO B 1 118 ? 9.142  27.046  -30.616 1.00 55.37  ? 97  PRO B C     1 
ATOM   4040 O  O     . PRO B 1 118 ? 8.817  28.054  -31.213 1.00 58.64  ? 97  PRO B O     1 
ATOM   4041 C  CB    . PRO B 1 118 ? 11.531 27.566  -29.986 1.00 57.22  ? 97  PRO B CB    1 
ATOM   4042 C  CG    . PRO B 1 118 ? 12.275 28.316  -31.074 1.00 57.35  ? 97  PRO B CG    1 
ATOM   4043 C  CD    . PRO B 1 118 ? 12.314 27.393  -32.273 1.00 56.13  ? 97  PRO B CD    1 
ATOM   4044 N  N     . GLN B 1 119 ? 8.303  26.294  -29.888 1.00 55.53  ? 98  GLN B N     1 
ATOM   4045 C  CA    . GLN B 1 119 ? 6.850  26.571  -29.669 1.00 50.68  ? 98  GLN B CA    1 
ATOM   4046 C  C     . GLN B 1 119 ? 6.613  27.154  -28.266 1.00 49.61  ? 98  GLN B C     1 
ATOM   4047 O  O     . GLN B 1 119 ? 7.107  26.560  -27.284 1.00 41.13  ? 98  GLN B O     1 
ATOM   4048 C  CB    . GLN B 1 119 ? 6.034  25.288  -29.764 1.00 51.75  ? 98  GLN B CB    1 
ATOM   4049 C  CG    . GLN B 1 119 ? 6.407  24.403  -30.935 1.00 57.29  ? 98  GLN B CG    1 
ATOM   4050 C  CD    . GLN B 1 119 ? 6.026  25.070  -32.231 1.00 65.01  ? 98  GLN B CD    1 
ATOM   4051 O  OE1   . GLN B 1 119 ? 4.963  25.677  -32.334 1.00 71.78  ? 98  GLN B OE1   1 
ATOM   4052 N  NE2   . GLN B 1 119 ? 6.901  24.985  -33.222 1.00 63.81  ? 98  GLN B NE2   1 
ATOM   4053 N  N     . ARG B 1 120 ? 5.850  28.246  -28.173 1.00 50.30  ? 99  ARG B N     1 
ATOM   4054 C  CA    . ARG B 1 120 ? 5.385  28.837  -26.887 1.00 52.58  ? 99  ARG B CA    1 
ATOM   4055 C  C     . ARG B 1 120 ? 3.955  28.390  -26.578 1.00 53.21  ? 99  ARG B C     1 
ATOM   4056 O  O     . ARG B 1 120 ? 3.098  28.498  -27.461 1.00 56.77  ? 99  ARG B O     1 
ATOM   4057 C  CB    . ARG B 1 120 ? 5.390  30.362  -26.928 1.00 51.45  ? 99  ARG B CB    1 
ATOM   4058 C  CG    . ARG B 1 120 ? 6.779  30.974  -26.882 1.00 55.53  ? 99  ARG B CG    1 
ATOM   4059 C  CD    . ARG B 1 120 ? 6.705  32.421  -27.329 1.00 56.33  ? 99  ARG B CD    1 
ATOM   4060 N  NE    . ARG B 1 120 ? 5.866  33.215  -26.432 1.00 56.62  ? 99  ARG B NE    1 
ATOM   4061 C  CZ    . ARG B 1 120 ? 6.285  34.250  -25.701 1.00 53.18  ? 99  ARG B CZ    1 
ATOM   4062 N  NH1   . ARG B 1 120 ? 7.544  34.640  -25.743 1.00 54.70  ? 99  ARG B NH1   1 
ATOM   4063 N  NH2   . ARG B 1 120 ? 5.440  34.904  -24.927 1.00 55.00  ? 99  ARG B NH2   1 
ATOM   4064 N  N     . ALA B 1 121 ? 3.700  27.941  -25.348 1.00 55.71  ? 100 ALA B N     1 
ATOM   4065 C  CA    . ALA B 1 121 ? 2.340  27.609  -24.871 1.00 57.49  ? 100 ALA B CA    1 
ATOM   4066 C  C     . ALA B 1 121 ? 2.324  27.675  -23.350 1.00 60.77  ? 100 ALA B C     1 
ATOM   4067 O  O     . ALA B 1 121 ? 3.327  27.376  -22.705 1.00 57.73  ? 100 ALA B O     1 
ATOM   4068 C  CB    . ALA B 1 121 ? 1.920  26.254  -25.387 1.00 57.47  ? 100 ALA B CB    1 
ATOM   4069 N  N     . PRO B 1 122 ? 1.187  28.064  -22.727 1.00 62.21  ? 101 PRO B N     1 
ATOM   4070 C  CA    . PRO B 1 122 ? 1.123  28.128  -21.271 1.00 58.78  ? 101 PRO B CA    1 
ATOM   4071 C  C     . PRO B 1 122 ? 1.281  26.726  -20.649 1.00 56.87  ? 101 PRO B C     1 
ATOM   4072 O  O     . PRO B 1 122 ? 1.627  26.646  -19.483 1.00 51.34  ? 101 PRO B O     1 
ATOM   4073 C  CB    . PRO B 1 122 ? -0.219 28.828  -20.984 1.00 59.39  ? 101 PRO B CB    1 
ATOM   4074 C  CG    . PRO B 1 122 ? -1.046 28.651  -22.241 1.00 56.00  ? 101 PRO B CG    1 
ATOM   4075 C  CD    . PRO B 1 122 ? -0.071 28.461  -23.382 1.00 58.22  ? 101 PRO B CD    1 
ATOM   4076 N  N     . ASP B 1 123 ? 1.098  25.658  -21.430 1.00 54.22  ? 102 ASP B N     1 
ATOM   4077 C  CA    . ASP B 1 123 ? 1.345  24.269  -20.956 1.00 60.15  ? 102 ASP B CA    1 
ATOM   4078 C  C     . ASP B 1 123 ? 2.131  23.485  -22.019 1.00 54.21  ? 102 ASP B C     1 
ATOM   4079 O  O     . ASP B 1 123 ? 1.819  23.615  -23.213 1.00 48.04  ? 102 ASP B O     1 
ATOM   4080 C  CB    . ASP B 1 123 ? 0.034  23.580  -20.548 1.00 71.59  ? 102 ASP B CB    1 
ATOM   4081 C  CG    . ASP B 1 123 ? 0.207  22.350  -19.655 1.00 80.71  ? 102 ASP B CG    1 
ATOM   4082 O  OD1   . ASP B 1 123 ? 1.338  22.123  -19.153 1.00 86.24  ? 102 ASP B OD1   1 
ATOM   4083 O  OD2   . ASP B 1 123 ? -0.791 21.616  -19.463 1.00 82.91  ? 102 ASP B OD2   1 
ATOM   4084 N  N     . VAL B 1 124 ? 3.122  22.710  -21.564 1.00 55.03  ? 103 VAL B N     1 
ATOM   4085 C  CA    . VAL B 1 124 ? 3.934  21.750  -22.369 1.00 51.85  ? 103 VAL B CA    1 
ATOM   4086 C  C     . VAL B 1 124 ? 2.983  20.891  -23.202 1.00 50.16  ? 103 VAL B C     1 
ATOM   4087 O  O     . VAL B 1 124 ? 3.245  20.767  -24.401 1.00 49.03  ? 103 VAL B O     1 
ATOM   4088 C  CB    . VAL B 1 124 ? 4.859  20.891  -21.481 1.00 52.13  ? 103 VAL B CB    1 
ATOM   4089 C  CG1   . VAL B 1 124 ? 5.420  19.688  -22.228 1.00 49.37  ? 103 VAL B CG1   1 
ATOM   4090 C  CG2   . VAL B 1 124 ? 5.993  21.722  -20.883 1.00 49.04  ? 103 VAL B CG2   1 
ATOM   4091 N  N     . ALA B 1 125 ? 1.896  20.387  -22.606 1.00 51.84  ? 104 ALA B N     1 
ATOM   4092 C  CA    . ALA B 1 125 ? 0.872  19.541  -23.275 1.00 55.34  ? 104 ALA B CA    1 
ATOM   4093 C  C     . ALA B 1 125 ? 0.386  20.169  -24.594 1.00 54.07  ? 104 ALA B C     1 
ATOM   4094 O  O     . ALA B 1 125 ? 0.173  19.398  -25.547 1.00 47.90  ? 104 ALA B O     1 
ATOM   4095 C  CB    . ALA B 1 125 ? -0.305 19.283  -22.357 1.00 57.96  ? 104 ALA B CB    1 
ATOM   4096 N  N     . LEU B 1 126 ? 0.175  21.489  -24.654 1.00 51.10  ? 105 LEU B N     1 
ATOM   4097 C  CA    . LEU B 1 126 ? -0.465 22.156  -25.826 1.00 54.35  ? 105 LEU B CA    1 
ATOM   4098 C  C     . LEU B 1 126 ? 0.471  22.129  -27.048 1.00 55.64  ? 105 LEU B C     1 
ATOM   4099 O  O     . LEU B 1 126 ? -0.035 22.291  -28.174 1.00 56.26  ? 105 LEU B O     1 
ATOM   4100 C  CB    . LEU B 1 126 ? -0.826 23.604  -25.476 1.00 60.40  ? 105 LEU B CB    1 
ATOM   4101 C  CG    . LEU B 1 126 ? -1.755 23.808  -24.279 1.00 61.67  ? 105 LEU B CG    1 
ATOM   4102 C  CD1   . LEU B 1 126 ? -1.919 25.294  -24.008 1.00 63.24  ? 105 LEU B CD1   1 
ATOM   4103 C  CD2   . LEU B 1 126 ? -3.113 23.148  -24.490 1.00 62.93  ? 105 LEU B CD2   1 
ATOM   4104 N  N     . ALA B 1 127 ? 1.780  21.940  -26.855 1.00 54.71  ? 106 ALA B N     1 
ATOM   4105 C  CA    . ALA B 1 127 ? 2.769  21.751  -27.947 1.00 55.42  ? 106 ALA B CA    1 
ATOM   4106 C  C     . ALA B 1 127 ? 2.469  20.482  -28.772 1.00 60.18  ? 106 ALA B C     1 
ATOM   4107 O  O     . ALA B 1 127 ? 2.839  20.464  -29.961 1.00 64.54  ? 106 ALA B O     1 
ATOM   4108 C  CB    . ALA B 1 127 ? 4.164  21.718  -27.377 1.00 56.82  ? 106 ALA B CB    1 
ATOM   4109 N  N     . PHE B 1 128 ? 1.834  19.453  -28.192 1.00 60.83  ? 107 PHE B N     1 
ATOM   4110 C  CA    . PHE B 1 128 ? 1.477  18.181  -28.886 1.00 60.10  ? 107 PHE B CA    1 
ATOM   4111 C  C     . PHE B 1 128 ? 0.205  18.359  -29.724 1.00 58.73  ? 107 PHE B C     1 
ATOM   4112 O  O     . PHE B 1 128 ? -0.639 19.190  -29.356 1.00 56.69  ? 107 PHE B O     1 
ATOM   4113 C  CB    . PHE B 1 128 ? 1.170  17.041  -27.908 1.00 62.44  ? 107 PHE B CB    1 
ATOM   4114 C  CG    . PHE B 1 128 ? 2.338  16.305  -27.301 1.00 65.58  ? 107 PHE B CG    1 
ATOM   4115 C  CD1   . PHE B 1 128 ? 3.506  16.081  -28.010 1.00 66.53  ? 107 PHE B CD1   1 
ATOM   4116 C  CD2   . PHE B 1 128 ? 2.229  15.765  -26.025 1.00 72.56  ? 107 PHE B CD2   1 
ATOM   4117 C  CE1   . PHE B 1 128 ? 4.554  15.375  -27.438 1.00 72.03  ? 107 PHE B CE1   1 
ATOM   4118 C  CE2   . PHE B 1 128 ? 3.277  15.056  -25.455 1.00 68.97  ? 107 PHE B CE2   1 
ATOM   4119 C  CZ    . PHE B 1 128 ? 4.437  14.861  -26.164 1.00 68.07  ? 107 PHE B CZ    1 
ATOM   4120 N  N     . SER B 1 129 ? 0.041  17.533  -30.763 1.00 57.52  ? 108 SER B N     1 
ATOM   4121 C  CA    . SER B 1 129 ? -1.209 17.408  -31.559 1.00 58.47  ? 108 SER B CA    1 
ATOM   4122 C  C     . SER B 1 129 ? -2.269 16.660  -30.743 1.00 63.01  ? 108 SER B C     1 
ATOM   4123 O  O     . SER B 1 129 ? -1.932 16.134  -29.657 1.00 57.39  ? 108 SER B O     1 
ATOM   4124 C  CB    . SER B 1 129 ? -0.971 16.727  -32.889 1.00 56.38  ? 108 SER B CB    1 
ATOM   4125 O  OG    . SER B 1 129 ? -0.783 15.325  -32.740 1.00 53.12  ? 108 SER B OG    1 
ATOM   4126 N  N     . ASP B 1 130 ? -3.500 16.626  -31.270 1.00 67.38  ? 109 ASP B N     1 
ATOM   4127 C  CA    . ASP B 1 130 ? -4.656 15.850  -30.747 1.00 66.24  ? 109 ASP B CA    1 
ATOM   4128 C  C     . ASP B 1 130 ? -4.240 14.386  -30.536 1.00 57.75  ? 109 ASP B C     1 
ATOM   4129 O  O     . ASP B 1 130 ? -4.320 13.925  -29.394 1.00 59.00  ? 109 ASP B O     1 
ATOM   4130 C  CB    . ASP B 1 130 ? -5.860 15.954  -31.693 1.00 73.26  ? 109 ASP B CB    1 
ATOM   4131 C  CG    . ASP B 1 130 ? -6.541 17.319  -31.737 1.00 77.05  ? 109 ASP B CG    1 
ATOM   4132 O  OD1   . ASP B 1 130 ? -6.396 18.092  -30.766 1.00 80.89  ? 109 ASP B OD1   1 
ATOM   4133 O  OD2   . ASP B 1 130 ? -7.226 17.596  -32.742 1.00 78.30  ? 109 ASP B OD2   1 
ATOM   4134 N  N     . GLU B 1 131 ? -3.802 13.698  -31.593 1.00 58.09  ? 110 GLU B N     1 
ATOM   4135 C  CA    . GLU B 1 131 ? -3.463 12.247  -31.572 1.00 67.90  ? 110 GLU B CA    1 
ATOM   4136 C  C     . GLU B 1 131 ? -2.312 12.007  -30.579 1.00 68.19  ? 110 GLU B C     1 
ATOM   4137 O  O     . GLU B 1 131 ? -2.332 10.973  -29.840 1.00 61.93  ? 110 GLU B O     1 
ATOM   4138 C  CB    . GLU B 1 131 ? -3.129 11.767  -32.992 1.00 74.77  ? 110 GLU B CB    1 
ATOM   4139 C  CG    . GLU B 1 131 ? -2.811 10.277  -33.092 1.00 87.61  ? 110 GLU B CG    1 
ATOM   4140 C  CD    . GLU B 1 131 ? -1.342 9.882   -32.964 1.00 99.23  ? 110 GLU B CD    1 
ATOM   4141 O  OE1   . GLU B 1 131 ? -0.511 10.409  -33.742 1.00 95.23  ? 110 GLU B OE1   1 
ATOM   4142 O  OE2   . GLU B 1 131 ? -1.025 9.039   -32.089 1.00 103.76 ? 110 GLU B OE2   1 
ATOM   4143 N  N     . GLU B 1 132 ? -1.359 12.942  -30.545 1.00 57.79  ? 111 GLU B N     1 
ATOM   4144 C  CA    . GLU B 1 132 ? -0.100 12.819  -29.771 1.00 55.77  ? 111 GLU B CA    1 
ATOM   4145 C  C     . GLU B 1 132 ? -0.397 12.947  -28.282 1.00 53.13  ? 111 GLU B C     1 
ATOM   4146 O  O     . GLU B 1 132 ? 0.118  12.120  -27.527 1.00 57.54  ? 111 GLU B O     1 
ATOM   4147 C  CB    . GLU B 1 132 ? 0.911  13.873  -30.213 1.00 53.73  ? 111 GLU B CB    1 
ATOM   4148 C  CG    . GLU B 1 132 ? 1.646  13.480  -31.477 1.00 49.70  ? 111 GLU B CG    1 
ATOM   4149 C  CD    . GLU B 1 132 ? 2.492  14.615  -32.017 1.00 56.69  ? 111 GLU B CD    1 
ATOM   4150 O  OE1   . GLU B 1 132 ? 2.310  15.771  -31.528 1.00 53.33  ? 111 GLU B OE1   1 
ATOM   4151 O  OE2   . GLU B 1 132 ? 3.328  14.348  -32.913 1.00 53.72  ? 111 GLU B OE2   1 
ATOM   4152 N  N     . LEU B 1 133 ? -1.187 13.940  -27.876 1.00 50.72  ? 112 LEU B N     1 
ATOM   4153 C  CA    . LEU B 1 133 ? -1.582 14.099  -26.450 1.00 49.61  ? 112 LEU B CA    1 
ATOM   4154 C  C     . LEU B 1 133 ? -2.370 12.862  -25.998 1.00 45.85  ? 112 LEU B C     1 
ATOM   4155 O  O     . LEU B 1 133 ? -2.131 12.428  -24.864 1.00 45.30  ? 112 LEU B O     1 
ATOM   4156 C  CB    . LEU B 1 133 ? -2.396 15.381  -26.256 1.00 51.41  ? 112 LEU B CB    1 
ATOM   4157 C  CG    . LEU B 1 133 ? -2.849 15.646  -24.823 1.00 52.56  ? 112 LEU B CG    1 
ATOM   4158 C  CD1   . LEU B 1 133 ? -1.674 15.972  -23.917 1.00 53.18  ? 112 LEU B CD1   1 
ATOM   4159 C  CD2   . LEU B 1 133 ? -3.878 16.764  -24.783 1.00 56.49  ? 112 LEU B CD2   1 
ATOM   4160 N  N     . THR B 1 134 ? -3.244 12.294  -26.843 1.00 44.44  ? 113 THR B N     1 
ATOM   4161 C  CA    . THR B 1 134 ? -4.037 11.078  -26.494 1.00 48.14  ? 113 THR B CA    1 
ATOM   4162 C  C     . THR B 1 134 ? -3.079 9.906   -26.240 1.00 47.22  ? 113 THR B C     1 
ATOM   4163 O  O     . THR B 1 134 ? -3.241 9.242   -25.209 1.00 47.64  ? 113 THR B O     1 
ATOM   4164 C  CB    . THR B 1 134 ? -5.101 10.757  -27.549 1.00 49.01  ? 113 THR B CB    1 
ATOM   4165 O  OG1   . THR B 1 134 ? -5.655 11.998  -27.973 1.00 48.04  ? 113 THR B OG1   1 
ATOM   4166 C  CG2   . THR B 1 134 ? -6.216 9.876   -27.026 1.00 51.30  ? 113 THR B CG2   1 
ATOM   4167 N  N     . ALA B 1 135 ? -2.079 9.719   -27.108 1.00 50.45  ? 114 ALA B N     1 
ATOM   4168 C  CA    . ALA B 1 135 ? -1.019 8.683   -26.992 1.00 45.34  ? 114 ALA B CA    1 
ATOM   4169 C  C     . ALA B 1 135 ? -0.224 8.878   -25.692 1.00 41.36  ? 114 ALA B C     1 
ATOM   4170 O  O     . ALA B 1 135 ? 0.013  7.883   -25.006 1.00 41.72  ? 114 ALA B O     1 
ATOM   4171 C  CB    . ALA B 1 135 ? -0.119 8.730   -28.204 1.00 47.61  ? 114 ALA B CB    1 
ATOM   4172 N  N     . TYR B 1 136 ? 0.130  10.112  -25.331 1.00 40.88  ? 115 TYR B N     1 
ATOM   4173 C  CA    . TYR B 1 136 ? 0.968  10.412  -24.142 1.00 40.82  ? 115 TYR B CA    1 
ATOM   4174 C  C     . TYR B 1 136 ? 0.204  10.095  -22.856 1.00 42.02  ? 115 TYR B C     1 
ATOM   4175 O  O     . TYR B 1 136 ? 0.837  9.654   -21.882 1.00 43.25  ? 115 TYR B O     1 
ATOM   4176 C  CB    . TYR B 1 136 ? 1.426  11.868  -24.083 1.00 41.81  ? 115 TYR B CB    1 
ATOM   4177 C  CG    . TYR B 1 136 ? 2.127  12.219  -22.793 1.00 43.26  ? 115 TYR B CG    1 
ATOM   4178 C  CD1   . TYR B 1 136 ? 3.440  11.832  -22.560 1.00 47.65  ? 115 TYR B CD1   1 
ATOM   4179 C  CD2   . TYR B 1 136 ? 1.468  12.894  -21.783 1.00 44.97  ? 115 TYR B CD2   1 
ATOM   4180 C  CE1   . TYR B 1 136 ? 4.091  12.140  -21.374 1.00 45.52  ? 115 TYR B CE1   1 
ATOM   4181 C  CE2   . TYR B 1 136 ? 2.094  13.188  -20.581 1.00 45.57  ? 115 TYR B CE2   1 
ATOM   4182 C  CZ    . TYR B 1 136 ? 3.414  12.825  -20.382 1.00 45.86  ? 115 TYR B CZ    1 
ATOM   4183 O  OH    . TYR B 1 136 ? 4.043  13.160  -19.219 1.00 47.61  ? 115 TYR B OH    1 
ATOM   4184 N  N     . LEU B 1 137 ? -1.109 10.313  -22.841 1.00 47.12  ? 116 LEU B N     1 
ATOM   4185 C  CA    . LEU B 1 137 ? -1.954 10.045  -21.641 1.00 47.19  ? 116 LEU B CA    1 
ATOM   4186 C  C     . LEU B 1 137 ? -2.245 8.537   -21.547 1.00 48.16  ? 116 LEU B C     1 
ATOM   4187 O  O     . LEU B 1 137 ? -2.210 7.999   -20.414 1.00 44.81  ? 116 LEU B O     1 
ATOM   4188 C  CB    . LEU B 1 137 ? -3.212 10.915  -21.724 1.00 46.61  ? 116 LEU B CB    1 
ATOM   4189 C  CG    . LEU B 1 137 ? -2.952 12.425  -21.597 1.00 48.16  ? 116 LEU B CG    1 
ATOM   4190 C  CD1   . LEU B 1 137 ? -4.216 13.235  -21.893 1.00 47.83  ? 116 LEU B CD1   1 
ATOM   4191 C  CD2   . LEU B 1 137 ? -2.398 12.782  -20.216 1.00 45.77  ? 116 LEU B CD2   1 
ATOM   4192 N  N     . GLU B 1 138 ? -2.446 7.863   -22.687 1.00 47.01  ? 117 GLU B N     1 
ATOM   4193 C  CA    . GLU B 1 138 ? -2.544 6.378   -22.745 1.00 51.60  ? 117 GLU B CA    1 
ATOM   4194 C  C     . GLU B 1 138 ? -1.278 5.773   -22.104 1.00 50.71  ? 117 GLU B C     1 
ATOM   4195 O  O     . GLU B 1 138 ? -1.427 4.998   -21.143 1.00 49.02  ? 117 GLU B O     1 
ATOM   4196 C  CB    . GLU B 1 138 ? -2.733 5.898   -24.187 1.00 54.11  ? 117 GLU B CB    1 
ATOM   4197 C  CG    . GLU B 1 138 ? -4.162 5.981   -24.710 1.00 63.81  ? 117 GLU B CG    1 
ATOM   4198 C  CD    . GLU B 1 138 ? -4.365 5.384   -26.106 1.00 70.60  ? 117 GLU B CD    1 
ATOM   4199 O  OE1   . GLU B 1 138 ? -3.553 5.670   -27.010 1.00 72.89  ? 117 GLU B OE1   1 
ATOM   4200 O  OE2   . GLU B 1 138 ? -5.329 4.617   -26.294 1.00 71.56  ? 117 GLU B OE2   1 
ATOM   4201 N  N     . LEU B 1 139 ? -0.086 6.142   -22.604 1.00 50.66  ? 118 LEU B N     1 
ATOM   4202 C  CA    . LEU B 1 139 ? 1.258  5.675   -22.137 1.00 46.87  ? 118 LEU B CA    1 
ATOM   4203 C  C     . LEU B 1 139 ? 1.422  5.900   -20.625 1.00 45.71  ? 118 LEU B C     1 
ATOM   4204 O  O     . LEU B 1 139 ? 1.798  4.942   -19.900 1.00 40.77  ? 118 LEU B O     1 
ATOM   4205 C  CB    . LEU B 1 139 ? 2.341  6.437   -22.910 1.00 46.39  ? 118 LEU B CB    1 
ATOM   4206 C  CG    . LEU B 1 139 ? 3.790  6.021   -22.638 1.00 49.47  ? 118 LEU B CG    1 
ATOM   4207 C  CD1   . LEU B 1 139 ? 3.987  4.536   -22.903 1.00 48.38  ? 118 LEU B CD1   1 
ATOM   4208 C  CD2   . LEU B 1 139 ? 4.751  6.823   -23.499 1.00 48.44  ? 118 LEU B CD2   1 
ATOM   4209 N  N     . ALA B 1 140 ? 1.157  7.122   -20.155 1.00 45.12  ? 119 ALA B N     1 
ATOM   4210 C  CA    . ALA B 1 140 ? 1.275  7.499   -18.726 1.00 47.50  ? 119 ALA B CA    1 
ATOM   4211 C  C     . ALA B 1 140 ? 0.323  6.640   -17.868 1.00 48.03  ? 119 ALA B C     1 
ATOM   4212 O  O     . ALA B 1 140 ? 0.763  6.167   -16.801 1.00 46.89  ? 119 ALA B O     1 
ATOM   4213 C  CB    . ALA B 1 140 ? 1.024  8.978   -18.558 1.00 47.62  ? 119 ALA B CB    1 
ATOM   4214 N  N     . GLY B 1 141 ? -0.921 6.425   -18.327 1.00 49.33  ? 120 GLY B N     1 
ATOM   4215 C  CA    . GLY B 1 141 ? -1.938 5.584   -17.659 1.00 45.16  ? 120 GLY B CA    1 
ATOM   4216 C  C     . GLY B 1 141 ? -1.537 4.113   -17.660 1.00 41.65  ? 120 GLY B C     1 
ATOM   4217 O  O     . GLY B 1 141 ? -1.686 3.465   -16.625 1.00 38.29  ? 120 GLY B O     1 
ATOM   4218 N  N     . ALA B 1 142 ? -1.031 3.599   -18.781 1.00 41.52  ? 121 ALA B N     1 
ATOM   4219 C  CA    . ALA B 1 142 ? -0.592 2.192   -18.914 1.00 42.84  ? 121 ALA B CA    1 
ATOM   4220 C  C     . ALA B 1 142 ? 0.534  1.921   -17.908 1.00 43.26  ? 121 ALA B C     1 
ATOM   4221 O  O     . ALA B 1 142 ? 0.525  0.844   -17.293 1.00 49.83  ? 121 ALA B O     1 
ATOM   4222 C  CB    . ALA B 1 142 ? -0.175 1.928   -20.326 1.00 42.50  ? 121 ALA B CB    1 
ATOM   4223 N  N     . LEU B 1 143 ? 1.421  2.897   -17.690 1.00 44.37  ? 122 LEU B N     1 
ATOM   4224 C  CA    . LEU B 1 143 ? 2.586  2.773   -16.767 1.00 42.07  ? 122 LEU B CA    1 
ATOM   4225 C  C     . LEU B 1 143 ? 2.141  2.789   -15.298 1.00 39.55  ? 122 LEU B C     1 
ATOM   4226 O  O     . LEU B 1 143 ? 2.728  2.020   -14.508 1.00 34.79  ? 122 LEU B O     1 
ATOM   4227 C  CB    . LEU B 1 143 ? 3.574  3.909   -17.029 1.00 43.42  ? 122 LEU B CB    1 
ATOM   4228 C  CG    . LEU B 1 143 ? 4.804  3.930   -16.116 1.00 45.84  ? 122 LEU B CG    1 
ATOM   4229 C  CD1   . LEU B 1 143 ? 5.546  2.599   -16.139 1.00 44.51  ? 122 LEU B CD1   1 
ATOM   4230 C  CD2   . LEU B 1 143 ? 5.736  5.063   -16.514 1.00 48.11  ? 122 LEU B CD2   1 
ATOM   4231 N  N     . GLU B 1 144 ? 1.205  3.670   -14.915 1.00 41.04  ? 123 GLU B N     1 
ATOM   4232 C  CA    . GLU B 1 144 ? 0.660  3.736   -13.525 1.00 43.76  ? 123 GLU B CA    1 
ATOM   4233 C  C     . GLU B 1 144 ? -0.092 2.441   -13.189 1.00 39.41  ? 123 GLU B C     1 
ATOM   4234 O  O     . GLU B 1 144 ? -0.110 2.041   -12.008 1.00 42.98  ? 123 GLU B O     1 
ATOM   4235 C  CB    . GLU B 1 144 ? -0.305 4.900   -13.341 1.00 47.51  ? 123 GLU B CB    1 
ATOM   4236 C  CG    . GLU B 1 144 ? 0.370  6.248   -13.361 1.00 57.02  ? 123 GLU B CG    1 
ATOM   4237 C  CD    . GLU B 1 144 ? -0.617 7.394   -13.453 1.00 61.87  ? 123 GLU B CD    1 
ATOM   4238 O  OE1   . GLU B 1 144 ? -1.809 7.118   -13.736 1.00 71.65  ? 123 GLU B OE1   1 
ATOM   4239 O  OE2   . GLU B 1 144 ? -0.195 8.558   -13.256 1.00 76.31  ? 123 GLU B OE2   1 
ATOM   4240 N  N     . ALA B 1 145 ? -0.710 1.815   -14.178 1.00 34.85  ? 124 ALA B N     1 
ATOM   4241 C  CA    . ALA B 1 145 ? -1.457 0.557   -13.987 1.00 39.36  ? 124 ALA B CA    1 
ATOM   4242 C  C     . ALA B 1 145 ? -0.470 -0.544  -13.566 1.00 38.54  ? 124 ALA B C     1 
ATOM   4243 O  O     . ALA B 1 145 ? -0.750 -1.290  -12.607 1.00 35.51  ? 124 ALA B O     1 
ATOM   4244 C  CB    . ALA B 1 145 ? -2.235 0.220   -15.248 1.00 40.74  ? 124 ALA B CB    1 
ATOM   4245 N  N     . ILE B 1 146 ? 0.682  -0.618  -14.224 1.00 40.94  ? 125 ILE B N     1 
ATOM   4246 C  CA    . ILE B 1 146 ? 1.765  -1.569  -13.838 1.00 38.35  ? 125 ILE B CA    1 
ATOM   4247 C  C     . ILE B 1 146 ? 2.270  -1.182  -12.446 1.00 38.44  ? 125 ILE B C     1 
ATOM   4248 O  O     . ILE B 1 146 ? 2.323  -2.081  -11.564 1.00 36.97  ? 125 ILE B O     1 
ATOM   4249 C  CB    . ILE B 1 146 ? 2.861  -1.582  -14.913 1.00 41.64  ? 125 ILE B CB    1 
ATOM   4250 C  CG1   . ILE B 1 146 ? 2.310  -2.140  -16.225 1.00 40.71  ? 125 ILE B CG1   1 
ATOM   4251 C  CG2   . ILE B 1 146 ? 4.075  -2.364  -14.435 1.00 44.24  ? 125 ILE B CG2   1 
ATOM   4252 C  CD1   . ILE B 1 146 ? 3.075  -1.712  -17.442 1.00 42.83  ? 125 ILE B CD1   1 
ATOM   4253 N  N     . ALA B 1 147 ? 2.508  0.116   -12.226 1.00 32.45  ? 126 ALA B N     1 
ATOM   4254 C  CA    . ALA B 1 147 ? 3.040  0.660   -10.959 1.00 37.32  ? 126 ALA B CA    1 
ATOM   4255 C  C     . ALA B 1 147 ? 2.192  0.193   -9.769  1.00 36.42  ? 126 ALA B C     1 
ATOM   4256 O  O     . ALA B 1 147 ? 2.777  -0.122  -8.693  1.00 35.76  ? 126 ALA B O     1 
ATOM   4257 C  CB    . ALA B 1 147 ? 3.102  2.180   -11.021 1.00 39.50  ? 126 ALA B CB    1 
ATOM   4258 N  N     . GLU B 1 148 ? 0.858  0.225   -9.907  1.00 44.54  ? 127 GLU B N     1 
ATOM   4259 C  CA    . GLU B 1 148 ? -0.077 -0.039  -8.775  1.00 41.01  ? 127 GLU B CA    1 
ATOM   4260 C  C     . GLU B 1 148 ? -0.024 -1.514  -8.393  1.00 38.20  ? 127 GLU B C     1 
ATOM   4261 O  O     . GLU B 1 148 ? -0.346 -1.771  -7.239  1.00 42.11  ? 127 GLU B O     1 
ATOM   4262 C  CB    . GLU B 1 148 ? -1.521 0.352   -9.067  1.00 43.41  ? 127 GLU B CB    1 
ATOM   4263 C  CG    . GLU B 1 148 ? -1.818 1.838   -8.905  1.00 44.28  ? 127 GLU B CG    1 
ATOM   4264 C  CD    . GLU B 1 148 ? -1.653 2.494   -7.537  1.00 42.39  ? 127 GLU B CD    1 
ATOM   4265 O  OE1   . GLU B 1 148 ? -1.742 1.829   -6.485  1.00 38.96  ? 127 GLU B OE1   1 
ATOM   4266 O  OE2   . GLU B 1 148 ? -1.413 3.720   -7.537  1.00 52.47  ? 127 GLU B OE2   1 
ATOM   4267 N  N     . LYS B 1 149 ? 0.415  -2.408  -9.286  1.00 39.25  ? 128 LYS B N     1 
ATOM   4268 C  CA    . LYS B 1 149 ? 0.590  -3.859  -8.980  1.00 45.23  ? 128 LYS B CA    1 
ATOM   4269 C  C     . LYS B 1 149 ? 1.938  -4.163  -8.289  1.00 42.40  ? 128 LYS B C     1 
ATOM   4270 O  O     . LYS B 1 149 ? 2.141  -5.336  -7.903  1.00 50.91  ? 128 LYS B O     1 
ATOM   4271 C  CB    . LYS B 1 149 ? 0.459  -4.704  -10.249 1.00 47.48  ? 128 LYS B CB    1 
ATOM   4272 C  CG    . LYS B 1 149 ? -0.938 -4.807  -10.848 1.00 54.38  ? 128 LYS B CG    1 
ATOM   4273 C  CD    . LYS B 1 149 ? -1.053 -6.012  -11.778 1.00 65.38  ? 128 LYS B CD    1 
ATOM   4274 C  CE    . LYS B 1 149 ? -2.027 -5.828  -12.921 1.00 75.35  ? 128 LYS B CE    1 
ATOM   4275 N  NZ    . LYS B 1 149 ? -3.426 -6.074  -12.485 1.00 85.69  ? 128 LYS B NZ    1 
ATOM   4276 N  N     . VAL B 1 150 ? 2.836  -3.194  -8.109  1.00 39.18  ? 129 VAL B N     1 
ATOM   4277 C  CA    . VAL B 1 150 ? 4.212  -3.442  -7.575  1.00 39.37  ? 129 VAL B CA    1 
ATOM   4278 C  C     . VAL B 1 150 ? 4.273  -3.047  -6.099  1.00 37.85  ? 129 VAL B C     1 
ATOM   4279 O  O     . VAL B 1 150 ? 4.223  -1.871  -5.770  1.00 43.52  ? 129 VAL B O     1 
ATOM   4280 C  CB    . VAL B 1 150 ? 5.274  -2.716  -8.438  1.00 43.72  ? 129 VAL B CB    1 
ATOM   4281 C  CG1   . VAL B 1 150 ? 6.684  -2.773  -7.865  1.00 43.22  ? 129 VAL B CG1   1 
ATOM   4282 C  CG2   . VAL B 1 150 ? 5.294  -3.261  -9.858  1.00 41.75  ? 129 VAL B CG2   1 
ATOM   4283 N  N     . PRO B 1 151 ? 4.382  -4.009  -5.151  1.00 37.99  ? 130 PRO B N     1 
ATOM   4284 C  CA    . PRO B 1 151 ? 4.383  -3.687  -3.725  1.00 39.57  ? 130 PRO B CA    1 
ATOM   4285 C  C     . PRO B 1 151 ? 5.604  -2.851  -3.332  1.00 41.25  ? 130 PRO B C     1 
ATOM   4286 O  O     . PRO B 1 151 ? 6.710  -3.228  -3.676  1.00 43.90  ? 130 PRO B O     1 
ATOM   4287 C  CB    . PRO B 1 151 ? 4.427  -5.041  -2.980  1.00 39.09  ? 130 PRO B CB    1 
ATOM   4288 C  CG    . PRO B 1 151 ? 4.190  -6.107  -4.032  1.00 34.75  ? 130 PRO B CG    1 
ATOM   4289 C  CD    . PRO B 1 151 ? 4.463  -5.463  -5.381  1.00 37.80  ? 130 PRO B CD    1 
ATOM   4290 N  N     . LEU B 1 152 ? 5.383  -1.770  -2.592  1.00 42.00  ? 131 LEU B N     1 
ATOM   4291 C  CA    . LEU B 1 152 ? 6.441  -0.792  -2.238  1.00 43.76  ? 131 LEU B CA    1 
ATOM   4292 C  C     . LEU B 1 152 ? 7.530  -1.430  -1.356  1.00 46.37  ? 131 LEU B C     1 
ATOM   4293 O  O     . LEU B 1 152 ? 8.671  -0.936  -1.396  1.00 46.23  ? 131 LEU B O     1 
ATOM   4294 C  CB    . LEU B 1 152 ? 5.776  0.396   -1.534  1.00 43.07  ? 131 LEU B CB    1 
ATOM   4295 C  CG    . LEU B 1 152 ? 4.760  1.162   -2.374  1.00 40.82  ? 131 LEU B CG    1 
ATOM   4296 C  CD1   . LEU B 1 152 ? 4.247  2.356   -1.601  1.00 45.29  ? 131 LEU B CD1   1 
ATOM   4297 C  CD2   . LEU B 1 152 ? 5.368  1.623   -3.691  1.00 40.98  ? 131 LEU B CD2   1 
ATOM   4298 N  N     . ASP B 1 153 ? 7.205  -2.465  -0.570  1.00 48.48  ? 132 ASP B N     1 
ATOM   4299 C  CA    . ASP B 1 153 ? 8.149  -3.070  0.413   1.00 48.68  ? 132 ASP B CA    1 
ATOM   4300 C  C     . ASP B 1 153 ? 8.833  -4.298  -0.209  1.00 45.01  ? 132 ASP B C     1 
ATOM   4301 O  O     . ASP B 1 153 ? 9.787  -4.811  0.389   1.00 48.42  ? 132 ASP B O     1 
ATOM   4302 C  CB    . ASP B 1 153 ? 7.453  -3.339  1.756   1.00 51.93  ? 132 ASP B CB    1 
ATOM   4303 C  CG    . ASP B 1 153 ? 6.349  -4.394  1.782   1.00 59.11  ? 132 ASP B CG    1 
ATOM   4304 O  OD1   . ASP B 1 153 ? 5.806  -4.736  0.706   1.00 54.19  ? 132 ASP B OD1   1 
ATOM   4305 O  OD2   . ASP B 1 153 ? 6.010  -4.846  2.909   1.00 73.44  ? 132 ASP B OD2   1 
ATOM   4306 N  N     . ALA B 1 154 ? 8.377  -4.749  -1.374  1.00 43.18  ? 133 ALA B N     1 
ATOM   4307 C  CA    . ALA B 1 154 ? 8.783  -6.038  -1.981  1.00 40.70  ? 133 ALA B CA    1 
ATOM   4308 C  C     . ALA B 1 154 ? 8.436  -6.021  -3.465  1.00 37.79  ? 133 ALA B C     1 
ATOM   4309 O  O     . ALA B 1 154 ? 7.554  -6.764  -3.888  1.00 39.28  ? 133 ALA B O     1 
ATOM   4310 C  CB    . ALA B 1 154 ? 8.094  -7.173  -1.261  1.00 40.05  ? 133 ALA B CB    1 
ATOM   4311 N  N     . PRO B 1 155 ? 9.103  -5.170  -4.286  1.00 36.22  ? 134 PRO B N     1 
ATOM   4312 C  CA    . PRO B 1 155 ? 8.803  -5.059  -5.710  1.00 36.93  ? 134 PRO B CA    1 
ATOM   4313 C  C     . PRO B 1 155 ? 8.942  -6.410  -6.412  1.00 35.29  ? 134 PRO B C     1 
ATOM   4314 O  O     . PRO B 1 155 ? 8.297  -6.614  -7.402  1.00 36.10  ? 134 PRO B O     1 
ATOM   4315 C  CB    . PRO B 1 155 ? 9.797  -4.020  -6.269  1.00 36.39  ? 134 PRO B CB    1 
ATOM   4316 C  CG    . PRO B 1 155 ? 10.803 -3.808  -5.178  1.00 37.54  ? 134 PRO B CG    1 
ATOM   4317 C  CD    . PRO B 1 155 ? 10.123 -4.197  -3.882  1.00 37.57  ? 134 PRO B CD    1 
ATOM   4318 N  N     . TRP B 1 156 ? 9.759  -7.302  -5.862  1.00 38.26  ? 135 TRP B N     1 
ATOM   4319 C  CA    . TRP B 1 156 ? 10.016 -8.651  -6.443  1.00 36.08  ? 135 TRP B CA    1 
ATOM   4320 C  C     . TRP B 1 156 ? 8.864  -9.618  -6.185  1.00 38.56  ? 135 TRP B C     1 
ATOM   4321 O  O     . TRP B 1 156 ? 8.969  -10.735 -6.708  1.00 38.60  ? 135 TRP B O     1 
ATOM   4322 C  CB    . TRP B 1 156 ? 11.313 -9.222  -5.873  1.00 36.55  ? 135 TRP B CB    1 
ATOM   4323 C  CG    . TRP B 1 156 ? 11.302 -9.266  -4.381  1.00 33.69  ? 135 TRP B CG    1 
ATOM   4324 C  CD1   . TRP B 1 156 ? 10.758 -10.245 -3.608  1.00 34.21  ? 135 TRP B CD1   1 
ATOM   4325 C  CD2   . TRP B 1 156 ? 11.793 -8.257  -3.484  1.00 33.22  ? 135 TRP B CD2   1 
ATOM   4326 N  NE1   . TRP B 1 156 ? 10.907 -9.923  -2.291  1.00 38.55  ? 135 TRP B NE1   1 
ATOM   4327 C  CE2   . TRP B 1 156 ? 11.540 -8.713  -2.180  1.00 34.28  ? 135 TRP B CE2   1 
ATOM   4328 C  CE3   . TRP B 1 156 ? 12.427 -7.022  -3.646  1.00 34.34  ? 135 TRP B CE3   1 
ATOM   4329 C  CZ2   . TRP B 1 156 ? 11.903 -7.981  -1.048  1.00 35.33  ? 135 TRP B CZ2   1 
ATOM   4330 C  CZ3   . TRP B 1 156 ? 12.789 -6.299  -2.526  1.00 34.04  ? 135 TRP B CZ3   1 
ATOM   4331 C  CH2   . TRP B 1 156 ? 12.529 -6.771  -1.241  1.00 32.88  ? 135 TRP B CH2   1 
ATOM   4332 N  N     . LEU B 1 157 ? 7.862  -9.242  -5.367  1.00 42.20  ? 136 LEU B N     1 
ATOM   4333 C  CA    . LEU B 1 157 ? 6.659  -10.087 -5.076  1.00 42.20  ? 136 LEU B CA    1 
ATOM   4334 C  C     . LEU B 1 157 ? 5.465  -9.669  -5.945  1.00 44.23  ? 136 LEU B C     1 
ATOM   4335 O  O     . LEU B 1 157 ? 4.421  -10.303 -5.829  1.00 49.50  ? 136 LEU B O     1 
ATOM   4336 C  CB    . LEU B 1 157 ? 6.312  -10.031 -3.587  1.00 40.17  ? 136 LEU B CB    1 
ATOM   4337 C  CG    . LEU B 1 157 ? 7.304  -10.736 -2.657  1.00 44.40  ? 136 LEU B CG    1 
ATOM   4338 C  CD1   . LEU B 1 157 ? 6.888  -10.606 -1.198  1.00 43.99  ? 136 LEU B CD1   1 
ATOM   4339 C  CD2   . LEU B 1 157 ? 7.488  -12.217 -3.030  1.00 42.28  ? 136 LEU B CD2   1 
ATOM   4340 N  N     . ALA B 1 158 ? 5.623  -8.675  -6.821  1.00 48.06  ? 137 ALA B N     1 
ATOM   4341 C  CA    . ALA B 1 158 ? 4.634  -8.330  -7.870  1.00 44.00  ? 137 ALA B CA    1 
ATOM   4342 C  C     . ALA B 1 158 ? 4.321  -9.597  -8.655  1.00 45.12  ? 137 ALA B C     1 
ATOM   4343 O  O     . ALA B 1 158 ? 5.205  -10.415 -8.869  1.00 43.30  ? 137 ALA B O     1 
ATOM   4344 C  CB    . ALA B 1 158 ? 5.176  -7.240  -8.758  1.00 41.76  ? 137 ALA B CB    1 
ATOM   4345 N  N     . PRO B 1 159 ? 3.054  -9.833  -9.057  1.00 51.05  ? 138 PRO B N     1 
ATOM   4346 C  CA    . PRO B 1 159 ? 2.672  -11.104 -9.680  1.00 50.01  ? 138 PRO B CA    1 
ATOM   4347 C  C     . PRO B 1 159 ? 3.389  -11.431 -11.000 1.00 49.88  ? 138 PRO B C     1 
ATOM   4348 O  O     . PRO B 1 159 ? 3.554  -12.609 -11.274 1.00 50.81  ? 138 PRO B O     1 
ATOM   4349 C  CB    . PRO B 1 159 ? 1.160  -10.979 -9.953  1.00 55.30  ? 138 PRO B CB    1 
ATOM   4350 C  CG    . PRO B 1 159 ? 0.795  -9.515  -9.711  1.00 57.57  ? 138 PRO B CG    1 
ATOM   4351 C  CD    . PRO B 1 159 ? 1.921  -8.910  -8.895  1.00 57.40  ? 138 PRO B CD    1 
ATOM   4352 N  N     . GLU B 1 160 ? 3.765  -10.402 -11.775 1.00 49.01  ? 139 GLU B N     1 
ATOM   4353 C  CA    . GLU B 1 160 ? 4.480  -10.498 -13.080 1.00 48.55  ? 139 GLU B CA    1 
ATOM   4354 C  C     . GLU B 1 160 ? 5.915  -9.982  -12.934 1.00 41.15  ? 139 GLU B C     1 
ATOM   4355 O  O     . GLU B 1 160 ? 6.499  -9.585  -13.937 1.00 38.64  ? 139 GLU B O     1 
ATOM   4356 C  CB    . GLU B 1 160 ? 3.757  -9.665  -14.140 1.00 56.37  ? 139 GLU B CB    1 
ATOM   4357 C  CG    . GLU B 1 160 ? 2.380  -10.200 -14.487 1.00 66.85  ? 139 GLU B CG    1 
ATOM   4358 C  CD    . GLU B 1 160 ? 2.383  -11.460 -15.336 1.00 69.58  ? 139 GLU B CD    1 
ATOM   4359 O  OE1   . GLU B 1 160 ? 3.043  -11.452 -16.391 1.00 77.35  ? 139 GLU B OE1   1 
ATOM   4360 O  OE2   . GLU B 1 160 ? 1.718  -12.442 -14.947 1.00 78.28  ? 139 GLU B OE2   1 
ATOM   4361 N  N     . ALA B 1 161 ? 6.459  -9.989  -11.717 1.00 41.19  ? 140 ALA B N     1 
ATOM   4362 C  CA    . ALA B 1 161 ? 7.801  -9.457  -11.381 1.00 39.77  ? 140 ALA B CA    1 
ATOM   4363 C  C     . ALA B 1 161 ? 8.876  -10.016 -12.336 1.00 42.16  ? 140 ALA B C     1 
ATOM   4364 O  O     . ALA B 1 161 ? 9.731  -9.204  -12.800 1.00 38.77  ? 140 ALA B O     1 
ATOM   4365 C  CB    . ALA B 1 161 ? 8.112  -9.745  -9.936  1.00 35.52  ? 140 ALA B CB    1 
ATOM   4366 N  N     . ALA B 1 162 ? 8.802  -11.309 -12.687 1.00 41.84  ? 141 ALA B N     1 
ATOM   4367 C  CA    . ALA B 1 162 ? 9.814  -12.050 -13.484 1.00 44.47  ? 141 ALA B CA    1 
ATOM   4368 C  C     . ALA B 1 162 ? 9.909  -11.492 -14.913 1.00 46.16  ? 141 ALA B C     1 
ATOM   4369 O  O     . ALA B 1 162 ? 11.039 -11.283 -15.393 1.00 57.92  ? 141 ALA B O     1 
ATOM   4370 C  CB    . ALA B 1 162 ? 9.488  -13.530 -13.488 1.00 46.30  ? 141 ALA B CB    1 
ATOM   4371 N  N     . ALA B 1 163 ? 8.778  -11.249 -15.572 1.00 45.64  ? 142 ALA B N     1 
ATOM   4372 C  CA    . ALA B 1 163 ? 8.687  -10.675 -16.939 1.00 43.06  ? 142 ALA B CA    1 
ATOM   4373 C  C     . ALA B 1 163 ? 9.003  -9.175  -16.928 1.00 41.89  ? 142 ALA B C     1 
ATOM   4374 O  O     . ALA B 1 163 ? 9.652  -8.707  -17.870 1.00 49.21  ? 142 ALA B O     1 
ATOM   4375 C  CB    . ALA B 1 163 ? 7.306  -10.912 -17.492 1.00 41.63  ? 142 ALA B CB    1 
ATOM   4376 N  N     . TRP B 1 164 ? 8.520  -8.439  -15.927 1.00 41.58  ? 143 TRP B N     1 
ATOM   4377 C  CA    . TRP B 1 164 ? 8.717  -6.968  -15.794 1.00 43.18  ? 143 TRP B CA    1 
ATOM   4378 C  C     . TRP B 1 164 ? 10.188 -6.632  -15.461 1.00 41.78  ? 143 TRP B C     1 
ATOM   4379 O  O     . TRP B 1 164 ? 10.679 -5.600  -15.947 1.00 40.91  ? 143 TRP B O     1 
ATOM   4380 C  CB    . TRP B 1 164 ? 7.750  -6.395  -14.745 1.00 40.97  ? 143 TRP B CB    1 
ATOM   4381 C  CG    . TRP B 1 164 ? 6.309  -6.362  -15.161 1.00 46.76  ? 143 TRP B CG    1 
ATOM   4382 C  CD1   . TRP B 1 164 ? 5.809  -6.573  -16.415 1.00 47.65  ? 143 TRP B CD1   1 
ATOM   4383 C  CD2   . TRP B 1 164 ? 5.170  -6.021  -14.339 1.00 46.13  ? 143 TRP B CD2   1 
ATOM   4384 N  NE1   . TRP B 1 164 ? 4.447  -6.420  -16.421 1.00 43.72  ? 143 TRP B NE1   1 
ATOM   4385 C  CE2   . TRP B 1 164 ? 4.022  -6.079  -15.168 1.00 45.34  ? 143 TRP B CE2   1 
ATOM   4386 C  CE3   . TRP B 1 164 ? 4.999  -5.670  -12.992 1.00 45.08  ? 143 TRP B CE3   1 
ATOM   4387 C  CZ2   . TRP B 1 164 ? 2.731  -5.825  -14.694 1.00 44.75  ? 143 TRP B CZ2   1 
ATOM   4388 C  CZ3   . TRP B 1 164 ? 3.721  -5.417  -12.523 1.00 48.35  ? 143 TRP B CZ3   1 
ATOM   4389 C  CH2   . TRP B 1 164 ? 2.603  -5.504  -13.361 1.00 43.97  ? 143 TRP B CH2   1 
ATOM   4390 N  N     . ASP B 1 165 ? 10.866 -7.454  -14.659 1.00 38.94  ? 144 ASP B N     1 
ATOM   4391 C  CA    . ASP B 1 165 ? 12.305 -7.305  -14.339 1.00 40.05  ? 144 ASP B CA    1 
ATOM   4392 C  C     . ASP B 1 165 ? 13.169 -7.713  -15.545 1.00 43.10  ? 144 ASP B C     1 
ATOM   4393 O  O     . ASP B 1 165 ? 14.306 -7.224  -15.619 1.00 49.43  ? 144 ASP B O     1 
ATOM   4394 C  CB    . ASP B 1 165 ? 12.650 -8.106  -13.089 1.00 40.01  ? 144 ASP B CB    1 
ATOM   4395 C  CG    . ASP B 1 165 ? 13.866 -7.643  -12.311 1.00 42.93  ? 144 ASP B CG    1 
ATOM   4396 O  OD1   . ASP B 1 165 ? 14.094 -6.383  -12.193 1.00 44.36  ? 144 ASP B OD1   1 
ATOM   4397 O  OD2   . ASP B 1 165 ? 14.559 -8.548  -11.793 1.00 42.57  ? 144 ASP B OD2   1 
ATOM   4398 N  N     . ALA B 1 166 ? 12.654 -8.520  -16.483 1.00 44.87  ? 145 ALA B N     1 
ATOM   4399 C  CA    . ALA B 1 166 ? 13.390 -9.048  -17.668 1.00 42.86  ? 145 ALA B CA    1 
ATOM   4400 C  C     . ALA B 1 166 ? 13.318 -8.076  -18.858 1.00 43.92  ? 145 ALA B C     1 
ATOM   4401 O  O     . ALA B 1 166 ? 13.865 -8.425  -19.922 1.00 43.28  ? 145 ALA B O     1 
ATOM   4402 C  CB    . ALA B 1 166 ? 12.855 -10.412 -18.056 1.00 37.86  ? 145 ALA B CB    1 
ATOM   4403 N  N     . THR B 1 167 ? 12.665 -6.919  -18.695 1.00 43.91  ? 146 THR B N     1 
ATOM   4404 C  CA    . THR B 1 167 ? 12.362 -5.925  -19.766 1.00 43.74  ? 146 THR B CA    1 
ATOM   4405 C  C     . THR B 1 167 ? 12.936 -4.565  -19.365 1.00 38.70  ? 146 THR B C     1 
ATOM   4406 O  O     . THR B 1 167 ? 12.758 -4.183  -18.182 1.00 36.26  ? 146 THR B O     1 
ATOM   4407 C  CB    . THR B 1 167 ? 10.846 -5.718  -19.938 1.00 45.78  ? 146 THR B CB    1 
ATOM   4408 O  OG1   . THR B 1 167 ? 10.192 -6.985  -19.918 1.00 58.57  ? 146 THR B OG1   1 
ATOM   4409 C  CG2   . THR B 1 167 ? 10.466 -4.996  -21.208 1.00 45.90  ? 146 THR B CG2   1 
ATOM   4410 N  N     . THR B 1 168 ? 13.504 -3.820  -20.311 1.00 35.21  ? 147 THR B N     1 
ATOM   4411 C  CA    . THR B 1 168 ? 13.879 -2.401  -20.086 1.00 37.71  ? 147 THR B CA    1 
ATOM   4412 C  C     . THR B 1 168 ? 12.608 -1.528  -20.175 1.00 39.53  ? 147 THR B C     1 
ATOM   4413 O  O     . THR B 1 168 ? 11.612 -1.966  -20.802 1.00 38.44  ? 147 THR B O     1 
ATOM   4414 C  CB    . THR B 1 168 ? 14.955 -1.913  -21.068 1.00 36.04  ? 147 THR B CB    1 
ATOM   4415 O  OG1   . THR B 1 168 ? 14.345 -1.773  -22.344 1.00 36.15  ? 147 THR B OG1   1 
ATOM   4416 C  CG2   . THR B 1 168 ? 16.178 -2.800  -21.139 1.00 34.98  ? 147 THR B CG2   1 
ATOM   4417 N  N     . LEU B 1 169 ? 12.636 -0.318  -19.614 1.00 37.32  ? 148 LEU B N     1 
ATOM   4418 C  CA    . LEU B 1 169 ? 11.543 0.672   -19.787 1.00 38.19  ? 148 LEU B CA    1 
ATOM   4419 C  C     . LEU B 1 169 ? 11.455 1.034   -21.273 1.00 37.08  ? 148 LEU B C     1 
ATOM   4420 O  O     . LEU B 1 169 ? 10.338 1.260   -21.733 1.00 43.19  ? 148 LEU B O     1 
ATOM   4421 C  CB    . LEU B 1 169 ? 11.768 1.924   -18.919 1.00 39.11  ? 148 LEU B CB    1 
ATOM   4422 C  CG    . LEU B 1 169 ? 10.674 3.002   -19.023 1.00 36.46  ? 148 LEU B CG    1 
ATOM   4423 C  CD1   . LEU B 1 169 ? 9.315  2.432   -18.639 1.00 38.11  ? 148 LEU B CD1   1 
ATOM   4424 C  CD2   . LEU B 1 169 ? 10.989 4.208   -18.149 1.00 34.95  ? 148 LEU B CD2   1 
ATOM   4425 N  N     . ARG B 1 170 ? 12.582 1.051   -21.998 1.00 38.13  ? 149 ARG B N     1 
ATOM   4426 C  CA    . ARG B 1 170 ? 12.643 1.523   -23.403 1.00 35.80  ? 149 ARG B CA    1 
ATOM   4427 C  C     . ARG B 1 170 ? 11.943 0.536   -24.330 1.00 37.72  ? 149 ARG B C     1 
ATOM   4428 O  O     . ARG B 1 170 ? 11.296 0.998   -25.286 1.00 39.25  ? 149 ARG B O     1 
ATOM   4429 C  CB    . ARG B 1 170 ? 14.074 1.712   -23.895 1.00 36.68  ? 149 ARG B CB    1 
ATOM   4430 C  CG    . ARG B 1 170 ? 14.109 2.193   -25.336 1.00 37.74  ? 149 ARG B CG    1 
ATOM   4431 C  CD    . ARG B 1 170 ? 15.372 2.846   -25.783 1.00 40.38  ? 149 ARG B CD    1 
ATOM   4432 N  NE    . ARG B 1 170 ? 15.663 4.019   -24.986 1.00 46.75  ? 149 ARG B NE    1 
ATOM   4433 C  CZ    . ARG B 1 170 ? 16.758 4.751   -25.136 1.00 52.01  ? 149 ARG B CZ    1 
ATOM   4434 N  NH1   . ARG B 1 170 ? 17.640 4.415   -26.064 1.00 55.31  ? 149 ARG B NH1   1 
ATOM   4435 N  NH2   . ARG B 1 170 ? 16.980 5.803   -24.358 1.00 51.97  ? 149 ARG B NH2   1 
ATOM   4436 N  N     . GLU B 1 171 ? 12.092 -0.761  -24.066 1.00 42.21  ? 150 GLU B N     1 
ATOM   4437 C  CA    . GLU B 1 171 ? 11.457 -1.865  -24.841 1.00 44.99  ? 150 GLU B CA    1 
ATOM   4438 C  C     . GLU B 1 171 ? 9.939  -1.868  -24.621 1.00 44.46  ? 150 GLU B C     1 
ATOM   4439 O  O     . GLU B 1 171 ? 9.177  -2.080  -25.583 1.00 49.87  ? 150 GLU B O     1 
ATOM   4440 C  CB    . GLU B 1 171 ? 12.080 -3.183  -24.412 1.00 47.96  ? 150 GLU B CB    1 
ATOM   4441 C  CG    . GLU B 1 171 ? 11.332 -4.402  -24.905 1.00 56.21  ? 150 GLU B CG    1 
ATOM   4442 C  CD    . GLU B 1 171 ? 11.919 -5.689  -24.350 1.00 66.05  ? 150 GLU B CD    1 
ATOM   4443 O  OE1   . GLU B 1 171 ? 12.912 -5.609  -23.556 1.00 70.87  ? 150 GLU B OE1   1 
ATOM   4444 O  OE2   . GLU B 1 171 ? 11.400 -6.768  -24.710 1.00 74.45  ? 150 GLU B OE2   1 
ATOM   4445 N  N     . TRP B 1 172 ? 9.499  -1.660  -23.388 1.00 41.54  ? 151 TRP B N     1 
ATOM   4446 C  CA    . TRP B 1 172 ? 8.061  -1.490  -23.080 1.00 43.63  ? 151 TRP B CA    1 
ATOM   4447 C  C     . TRP B 1 172 ? 7.496  -0.289  -23.864 1.00 44.39  ? 151 TRP B C     1 
ATOM   4448 O  O     . TRP B 1 172 ? 6.464  -0.473  -24.528 1.00 46.00  ? 151 TRP B O     1 
ATOM   4449 C  CB    . TRP B 1 172 ? 7.866  -1.355  -21.572 1.00 45.74  ? 151 TRP B CB    1 
ATOM   4450 C  CG    . TRP B 1 172 ? 6.438  -1.141  -21.192 1.00 44.66  ? 151 TRP B CG    1 
ATOM   4451 C  CD1   . TRP B 1 172 ? 5.480  -2.102  -21.045 1.00 40.86  ? 151 TRP B CD1   1 
ATOM   4452 C  CD2   . TRP B 1 172 ? 5.801  0.125   -20.959 1.00 38.94  ? 151 TRP B CD2   1 
ATOM   4453 N  NE1   . TRP B 1 172 ? 4.287  -1.514  -20.735 1.00 40.79  ? 151 TRP B NE1   1 
ATOM   4454 C  CE2   . TRP B 1 172 ? 4.450  -0.152  -20.679 1.00 39.23  ? 151 TRP B CE2   1 
ATOM   4455 C  CE3   . TRP B 1 172 ? 6.226  1.457   -20.981 1.00 40.39  ? 151 TRP B CE3   1 
ATOM   4456 C  CZ2   . TRP B 1 172 ? 3.534  0.859   -20.399 1.00 37.20  ? 151 TRP B CZ2   1 
ATOM   4457 C  CZ3   . TRP B 1 172 ? 5.319  2.455   -20.701 1.00 38.16  ? 151 TRP B CZ3   1 
ATOM   4458 C  CH2   . TRP B 1 172 ? 3.989  2.158   -20.423 1.00 36.41  ? 151 TRP B CH2   1 
ATOM   4459 N  N     . VAL B 1 173 ? 8.142  0.885   -23.817 1.00 38.85  ? 152 VAL B N     1 
ATOM   4460 C  CA    . VAL B 1 173 ? 7.697  2.095   -24.573 1.00 39.78  ? 152 VAL B CA    1 
ATOM   4461 C  C     . VAL B 1 173 ? 7.613  1.773   -26.072 1.00 43.86  ? 152 VAL B C     1 
ATOM   4462 O  O     . VAL B 1 173 ? 6.609  2.147   -26.702 1.00 43.75  ? 152 VAL B O     1 
ATOM   4463 C  CB    . VAL B 1 173 ? 8.611  3.306   -24.335 1.00 42.33  ? 152 VAL B CB    1 
ATOM   4464 C  CG1   . VAL B 1 173 ? 8.423  4.380   -25.397 1.00 42.90  ? 152 VAL B CG1   1 
ATOM   4465 C  CG2   . VAL B 1 173 ? 8.419  3.895   -22.947 1.00 42.32  ? 152 VAL B CG2   1 
ATOM   4466 N  N     . ALA B 1 174 ? 8.629  1.133   -26.654 1.00 44.70  ? 153 ALA B N     1 
ATOM   4467 C  CA    . ALA B 1 174 ? 8.587  0.693   -28.069 1.00 44.76  ? 153 ALA B CA    1 
ATOM   4468 C  C     . ALA B 1 174 ? 7.363  -0.219  -28.297 1.00 47.04  ? 153 ALA B C     1 
ATOM   4469 O  O     . ALA B 1 174 ? 6.716  -0.101  -29.346 1.00 48.49  ? 153 ALA B O     1 
ATOM   4470 C  CB    . ALA B 1 174 ? 9.883  0.016   -28.455 1.00 43.90  ? 153 ALA B CB    1 
ATOM   4471 N  N     . GLY B 1 175 ? 7.003  -1.063  -27.329 1.00 48.74  ? 154 GLY B N     1 
ATOM   4472 C  CA    . GLY B 1 175 ? 5.930  -2.062  -27.494 1.00 49.80  ? 154 GLY B CA    1 
ATOM   4473 C  C     . GLY B 1 175 ? 4.538  -1.455  -27.592 1.00 55.25  ? 154 GLY B C     1 
ATOM   4474 O  O     . GLY B 1 175 ? 3.647  -2.189  -28.051 1.00 54.71  ? 154 GLY B O     1 
ATOM   4475 N  N     . THR B 1 176 ? 4.342  -0.193  -27.168 1.00 56.24  ? 155 THR B N     1 
ATOM   4476 C  CA    . THR B 1 176 ? 3.006  0.463   -27.029 1.00 56.76  ? 155 THR B CA    1 
ATOM   4477 C  C     . THR B 1 176 ? 2.563  1.130   -28.338 1.00 60.33  ? 155 THR B C     1 
ATOM   4478 O  O     . THR B 1 176 ? 1.382  1.570   -28.376 1.00 55.44  ? 155 THR B O     1 
ATOM   4479 C  CB    . THR B 1 176 ? 2.970  1.543   -25.937 1.00 55.28  ? 155 THR B CB    1 
ATOM   4480 O  OG1   . THR B 1 176 ? 3.884  2.585   -26.295 1.00 56.65  ? 155 THR B OG1   1 
ATOM   4481 C  CG2   . THR B 1 176 ? 3.284  1.011   -24.556 1.00 52.10  ? 155 THR B CG2   1 
ATOM   4482 N  N     . GLY B 1 177 ? 3.466  1.245   -29.325 1.00 60.84  ? 156 GLY B N     1 
ATOM   4483 C  CA    . GLY B 1 177 ? 3.167  1.699   -30.701 1.00 62.73  ? 156 GLY B CA    1 
ATOM   4484 C  C     . GLY B 1 177 ? 3.038  3.211   -30.789 1.00 62.22  ? 156 GLY B C     1 
ATOM   4485 O  O     . GLY B 1 177 ? 2.306  3.711   -31.659 1.00 72.73  ? 156 GLY B O     1 
ATOM   4486 N  N     . VAL B 1 178 ? 3.761  3.922   -29.933 1.00 59.78  ? 157 VAL B N     1 
ATOM   4487 C  CA    . VAL B 1 178 ? 3.610  5.383   -29.688 1.00 54.15  ? 157 VAL B CA    1 
ATOM   4488 C  C     . VAL B 1 178 ? 4.476  6.138   -30.694 1.00 51.16  ? 157 VAL B C     1 
ATOM   4489 O  O     . VAL B 1 178 ? 5.567  5.698   -31.016 1.00 52.18  ? 157 VAL B O     1 
ATOM   4490 C  CB    . VAL B 1 178 ? 3.973  5.666   -28.218 1.00 58.72  ? 157 VAL B CB    1 
ATOM   4491 C  CG1   . VAL B 1 178 ? 4.191  7.132   -27.916 1.00 56.26  ? 157 VAL B CG1   1 
ATOM   4492 C  CG2   . VAL B 1 178 ? 2.923  5.090   -27.279 1.00 62.48  ? 157 VAL B CG2   1 
ATOM   4493 N  N     . PRO B 1 179 ? 4.019  7.272   -31.268 1.00 52.69  ? 158 PRO B N     1 
ATOM   4494 C  CA    . PRO B 1 179 ? 4.851  8.035   -32.199 1.00 54.40  ? 158 PRO B CA    1 
ATOM   4495 C  C     . PRO B 1 179 ? 6.132  8.623   -31.578 1.00 57.70  ? 158 PRO B C     1 
ATOM   4496 O  O     . PRO B 1 179 ? 6.232  8.731   -30.375 1.00 53.67  ? 158 PRO B O     1 
ATOM   4497 C  CB    . PRO B 1 179 ? 3.923  9.152   -32.703 1.00 54.37  ? 158 PRO B CB    1 
ATOM   4498 C  CG    . PRO B 1 179 ? 2.786  9.227   -31.695 1.00 53.35  ? 158 PRO B CG    1 
ATOM   4499 C  CD    . PRO B 1 179 ? 2.664  7.835   -31.117 1.00 54.08  ? 158 PRO B CD    1 
ATOM   4500 N  N     . ASP B 1 180 ? 7.091  8.978   -32.434 1.00 59.21  ? 159 ASP B N     1 
ATOM   4501 C  CA    . ASP B 1 180 ? 8.460  9.412   -32.045 1.00 62.63  ? 159 ASP B CA    1 
ATOM   4502 C  C     . ASP B 1 180 ? 8.393  10.658  -31.161 1.00 62.29  ? 159 ASP B C     1 
ATOM   4503 O  O     . ASP B 1 180 ? 9.103  10.687  -30.137 1.00 62.00  ? 159 ASP B O     1 
ATOM   4504 C  CB    . ASP B 1 180 ? 9.326  9.652   -33.280 1.00 61.44  ? 159 ASP B CB    1 
ATOM   4505 C  CG    . ASP B 1 180 ? 9.716  8.349   -33.958 1.00 67.60  ? 159 ASP B CG    1 
ATOM   4506 O  OD1   . ASP B 1 180 ? 9.055  7.316   -33.692 1.00 68.05  ? 159 ASP B OD1   1 
ATOM   4507 O  OD2   . ASP B 1 180 ? 10.692 8.368   -34.722 1.00 75.81  ? 159 ASP B OD2   1 
ATOM   4508 N  N     . ARG B 1 181 ? 7.577  11.643  -31.533 1.00 54.66  ? 160 ARG B N     1 
ATOM   4509 C  CA    . ARG B 1 181 ? 7.474  12.913  -30.774 1.00 54.75  ? 160 ARG B CA    1 
ATOM   4510 C  C     . ARG B 1 181 ? 6.947  12.651  -29.362 1.00 52.42  ? 160 ARG B C     1 
ATOM   4511 O  O     . ARG B 1 181 ? 7.281  13.461  -28.475 1.00 51.91  ? 160 ARG B O     1 
ATOM   4512 C  CB    . ARG B 1 181 ? 6.573  13.923  -31.481 1.00 60.43  ? 160 ARG B CB    1 
ATOM   4513 C  CG    . ARG B 1 181 ? 7.336  14.986  -32.254 1.00 59.18  ? 160 ARG B CG    1 
ATOM   4514 C  CD    . ARG B 1 181 ? 6.414  16.093  -32.700 1.00 54.53  ? 160 ARG B CD    1 
ATOM   4515 N  NE    . ARG B 1 181 ? 7.210  17.147  -33.289 1.00 57.06  ? 160 ARG B NE    1 
ATOM   4516 C  CZ    . ARG B 1 181 ? 6.741  18.323  -33.661 1.00 60.20  ? 160 ARG B CZ    1 
ATOM   4517 N  NH1   . ARG B 1 181 ? 5.458  18.601  -33.507 1.00 64.07  ? 160 ARG B NH1   1 
ATOM   4518 N  NH2   . ARG B 1 181 ? 7.560  19.230  -34.166 1.00 62.89  ? 160 ARG B NH2   1 
ATOM   4519 N  N     . VAL B 1 182 ? 6.156  11.592  -29.153 1.00 47.31  ? 161 VAL B N     1 
ATOM   4520 C  CA    . VAL B 1 182 ? 5.665  11.219  -27.789 1.00 47.98  ? 161 VAL B CA    1 
ATOM   4521 C  C     . VAL B 1 182 ? 6.806  10.515  -27.033 1.00 51.51  ? 161 VAL B C     1 
ATOM   4522 O  O     . VAL B 1 182 ? 7.058  10.907  -25.850 1.00 47.62  ? 161 VAL B O     1 
ATOM   4523 C  CB    . VAL B 1 182 ? 4.365  10.383  -27.820 1.00 43.98  ? 161 VAL B CB    1 
ATOM   4524 C  CG1   . VAL B 1 182 ? 3.964  9.888   -26.431 1.00 43.01  ? 161 VAL B CG1   1 
ATOM   4525 C  CG2   . VAL B 1 182 ? 3.221  11.177  -28.428 1.00 45.87  ? 161 VAL B CG2   1 
ATOM   4526 N  N     . ALA B 1 183 ? 7.494  9.557   -27.673 1.00 46.67  ? 162 ALA B N     1 
ATOM   4527 C  CA    . ALA B 1 183 ? 8.628  8.821   -27.058 1.00 49.63  ? 162 ALA B CA    1 
ATOM   4528 C  C     . ALA B 1 183 ? 9.723  9.835   -26.705 1.00 46.49  ? 162 ALA B C     1 
ATOM   4529 O  O     . ALA B 1 183 ? 10.325 9.687   -25.631 1.00 48.31  ? 162 ALA B O     1 
ATOM   4530 C  CB    . ALA B 1 183 ? 9.145  7.708   -27.942 1.00 40.56  ? 162 ALA B CB    1 
ATOM   4531 N  N     . GLY B 1 184 ? 9.903  10.860  -27.540 1.00 45.15  ? 163 GLY B N     1 
ATOM   4532 C  CA    . GLY B 1 184 ? 10.869 11.950  -27.319 1.00 46.01  ? 163 GLY B CA    1 
ATOM   4533 C  C     . GLY B 1 184 ? 10.613 12.669  -26.002 1.00 49.77  ? 163 GLY B C     1 
ATOM   4534 O  O     . GLY B 1 184 ? 11.548 12.738  -25.177 1.00 51.28  ? 163 GLY B O     1 
ATOM   4535 N  N     . LEU B 1 185 ? 9.400  13.190  -25.797 1.00 44.04  ? 164 LEU B N     1 
ATOM   4536 C  CA    . LEU B 1 185 ? 9.083  14.049  -24.629 1.00 48.23  ? 164 LEU B CA    1 
ATOM   4537 C  C     . LEU B 1 185 ? 8.988  13.181  -23.375 1.00 46.99  ? 164 LEU B C     1 
ATOM   4538 O  O     . LEU B 1 185 ? 9.373  13.670  -22.290 1.00 46.43  ? 164 LEU B O     1 
ATOM   4539 C  CB    . LEU B 1 185 ? 7.780  14.823  -24.859 1.00 53.07  ? 164 LEU B CB    1 
ATOM   4540 C  CG    . LEU B 1 185 ? 7.869  16.322  -24.556 1.00 54.67  ? 164 LEU B CG    1 
ATOM   4541 C  CD1   . LEU B 1 185 ? 9.092  16.953  -25.225 1.00 52.06  ? 164 LEU B CD1   1 
ATOM   4542 C  CD2   . LEU B 1 185 ? 6.598  17.037  -24.998 1.00 58.43  ? 164 LEU B CD2   1 
ATOM   4543 N  N     . PHE B 1 186 ? 8.515  11.944  -23.522 1.00 43.88  ? 165 PHE B N     1 
ATOM   4544 C  CA    . PHE B 1 186 ? 8.474  10.938  -22.435 1.00 39.51  ? 165 PHE B CA    1 
ATOM   4545 C  C     . PHE B 1 186 ? 9.903  10.708  -21.923 1.00 39.71  ? 165 PHE B C     1 
ATOM   4546 O  O     . PHE B 1 186 ? 10.114 10.857  -20.699 1.00 35.73  ? 165 PHE B O     1 
ATOM   4547 C  CB    . PHE B 1 186 ? 7.781  9.659   -22.904 1.00 38.31  ? 165 PHE B CB    1 
ATOM   4548 C  CG    . PHE B 1 186 ? 7.649  8.641   -21.804 1.00 41.17  ? 165 PHE B CG    1 
ATOM   4549 C  CD1   . PHE B 1 186 ? 6.743  8.834   -20.773 1.00 42.15  ? 165 PHE B CD1   1 
ATOM   4550 C  CD2   . PHE B 1 186 ? 8.469  7.528   -21.770 1.00 41.30  ? 165 PHE B CD2   1 
ATOM   4551 C  CE1   . PHE B 1 186 ? 6.643  7.911   -19.747 1.00 46.70  ? 165 PHE B CE1   1 
ATOM   4552 C  CE2   . PHE B 1 186 ? 8.363  6.602   -20.748 1.00 41.31  ? 165 PHE B CE2   1 
ATOM   4553 C  CZ    . PHE B 1 186 ? 7.456  6.799   -19.735 1.00 45.06  ? 165 PHE B CZ    1 
ATOM   4554 N  N     . GLU B 1 187 ? 10.863 10.456  -22.831 1.00 41.44  ? 166 GLU B N     1 
ATOM   4555 C  CA    . GLU B 1 187 ? 12.300 10.217  -22.498 1.00 39.71  ? 166 GLU B CA    1 
ATOM   4556 C  C     . GLU B 1 187 ? 12.905 11.446  -21.785 1.00 37.70  ? 166 GLU B C     1 
ATOM   4557 O  O     . GLU B 1 187 ? 13.627 11.239  -20.794 1.00 38.91  ? 166 GLU B O     1 
ATOM   4558 C  CB    . GLU B 1 187 ? 13.076 9.865   -23.762 1.00 42.13  ? 166 GLU B CB    1 
ATOM   4559 C  CG    . GLU B 1 187 ? 14.506 9.434   -23.505 1.00 45.87  ? 166 GLU B CG    1 
ATOM   4560 C  CD    . GLU B 1 187 ? 14.652 8.028   -22.947 1.00 50.53  ? 166 GLU B CD    1 
ATOM   4561 O  OE1   . GLU B 1 187 ? 13.674 7.229   -23.053 1.00 50.17  ? 166 GLU B OE1   1 
ATOM   4562 O  OE2   . GLU B 1 187 ? 15.751 7.726   -22.427 1.00 45.97  ? 166 GLU B OE2   1 
ATOM   4563 N  N     . VAL B 1 188 ? 12.620 12.679  -22.221 1.00 32.65  ? 167 VAL B N     1 
ATOM   4564 C  CA    . VAL B 1 188 ? 13.022 13.898  -21.450 1.00 35.30  ? 167 VAL B CA    1 
ATOM   4565 C  C     . VAL B 1 188 ? 12.527 13.773  -19.991 1.00 36.19  ? 167 VAL B C     1 
ATOM   4566 O  O     . VAL B 1 188 ? 13.308 14.017  -19.053 1.00 37.62  ? 167 VAL B O     1 
ATOM   4567 C  CB    . VAL B 1 188 ? 12.503 15.189  -22.111 1.00 37.82  ? 167 VAL B CB    1 
ATOM   4568 C  CG1   . VAL B 1 188 ? 12.600 16.385  -21.179 1.00 39.21  ? 167 VAL B CG1   1 
ATOM   4569 C  CG2   . VAL B 1 188 ? 13.228 15.482  -23.408 1.00 38.39  ? 167 VAL B CG2   1 
ATOM   4570 N  N     . ALA B 1 189 ? 11.273 13.394  -19.769 1.00 37.52  ? 168 ALA B N     1 
ATOM   4571 C  CA    . ALA B 1 189 ? 10.689 13.291  -18.402 1.00 38.32  ? 168 ALA B CA    1 
ATOM   4572 C  C     . ALA B 1 189 ? 11.377 12.154  -17.627 1.00 36.21  ? 168 ALA B C     1 
ATOM   4573 O  O     . ALA B 1 189 ? 11.740 12.370  -16.453 1.00 38.06  ? 168 ALA B O     1 
ATOM   4574 C  CB    . ALA B 1 189 ? 9.183  13.103  -18.480 1.00 36.52  ? 168 ALA B CB    1 
ATOM   4575 N  N     . VAL B 1 190 ? 11.575 11.001  -18.269 1.00 31.75  ? 169 VAL B N     1 
ATOM   4576 C  CA    . VAL B 1 190 ? 12.298 9.845   -17.671 1.00 33.36  ? 169 VAL B CA    1 
ATOM   4577 C  C     . VAL B 1 190 ? 13.697 10.260  -17.236 1.00 32.64  ? 169 VAL B C     1 
ATOM   4578 O  O     . VAL B 1 190 ? 14.075 9.993   -16.092 1.00 35.54  ? 169 VAL B O     1 
ATOM   4579 C  CB    . VAL B 1 190 ? 12.372 8.661   -18.639 1.00 31.24  ? 169 VAL B CB    1 
ATOM   4580 C  CG1   . VAL B 1 190 ? 13.378 7.637   -18.171 1.00 32.43  ? 169 VAL B CG1   1 
ATOM   4581 C  CG2   . VAL B 1 190 ? 11.003 8.046   -18.815 1.00 29.81  ? 169 VAL B CG2   1 
ATOM   4582 N  N     . GLN B 1 191 ? 14.467 10.868  -18.116 1.00 35.28  ? 170 GLN B N     1 
ATOM   4583 C  CA    . GLN B 1 191 ? 15.830 11.327  -17.741 1.00 37.60  ? 170 GLN B CA    1 
ATOM   4584 C  C     . GLN B 1 191 ? 15.749 12.437  -16.670 1.00 37.52  ? 170 GLN B C     1 
ATOM   4585 O  O     . GLN B 1 191 ? 16.612 12.436  -15.763 1.00 35.86  ? 170 GLN B O     1 
ATOM   4586 C  CB    . GLN B 1 191 ? 16.588 11.712  -19.005 1.00 42.76  ? 170 GLN B CB    1 
ATOM   4587 C  CG    . GLN B 1 191 ? 16.802 10.518  -19.920 1.00 44.34  ? 170 GLN B CG    1 
ATOM   4588 C  CD    . GLN B 1 191 ? 17.680 10.815  -21.109 1.00 45.56  ? 170 GLN B CD    1 
ATOM   4589 O  OE1   . GLN B 1 191 ? 17.851 9.966   -21.980 1.00 47.16  ? 170 GLN B OE1   1 
ATOM   4590 N  NE2   . GLN B 1 191 ? 18.241 12.011  -21.160 1.00 41.41  ? 170 GLN B NE2   1 
ATOM   4591 N  N     . ALA B 1 192 ? 14.741 13.313  -16.691 1.00 33.19  ? 171 ALA B N     1 
ATOM   4592 C  CA    . ALA B 1 192 ? 14.599 14.350  -15.641 1.00 34.97  ? 171 ALA B CA    1 
ATOM   4593 C  C     . ALA B 1 192 ? 14.394 13.682  -14.276 1.00 37.86  ? 171 ALA B C     1 
ATOM   4594 O  O     . ALA B 1 192 ? 14.896 14.238  -13.284 1.00 36.87  ? 171 ALA B O     1 
ATOM   4595 C  CB    . ALA B 1 192 ? 13.453 15.281  -15.944 1.00 37.81  ? 171 ALA B CB    1 
ATOM   4596 N  N     . VAL B 1 193 ? 13.663 12.554  -14.228 1.00 35.68  ? 172 VAL B N     1 
ATOM   4597 C  CA    . VAL B 1 193 ? 13.252 11.874  -12.956 1.00 36.28  ? 172 VAL B CA    1 
ATOM   4598 C  C     . VAL B 1 193 ? 14.335 10.886  -12.478 1.00 32.65  ? 172 VAL B C     1 
ATOM   4599 O  O     . VAL B 1 193 ? 14.540 10.827  -11.282 1.00 32.48  ? 172 VAL B O     1 
ATOM   4600 C  CB    . VAL B 1 193 ? 11.905 11.139  -13.108 1.00 36.92  ? 172 VAL B CB    1 
ATOM   4601 C  CG1   . VAL B 1 193 ? 11.620 10.243  -11.914 1.00 38.08  ? 172 VAL B CG1   1 
ATOM   4602 C  CG2   . VAL B 1 193 ? 10.743 12.083  -13.359 1.00 37.10  ? 172 VAL B CG2   1 
ATOM   4603 N  N     . PHE B 1 194 ? 14.929 10.084  -13.362 1.00 32.86  ? 173 PHE B N     1 
ATOM   4604 C  CA    . PHE B 1 194 ? 15.793 8.923   -13.004 1.00 35.14  ? 173 PHE B CA    1 
ATOM   4605 C  C     . PHE B 1 194 ? 17.275 9.214   -13.221 1.00 35.14  ? 173 PHE B C     1 
ATOM   4606 O  O     . PHE B 1 194 ? 18.065 8.402   -12.772 1.00 37.06  ? 173 PHE B O     1 
ATOM   4607 C  CB    . PHE B 1 194 ? 15.445 7.690   -13.832 1.00 35.20  ? 173 PHE B CB    1 
ATOM   4608 C  CG    . PHE B 1 194 ? 14.084 7.128   -13.533 1.00 37.91  ? 173 PHE B CG    1 
ATOM   4609 C  CD1   . PHE B 1 194 ? 13.895 6.308   -12.429 1.00 36.60  ? 173 PHE B CD1   1 
ATOM   4610 C  CD2   . PHE B 1 194 ? 13.002 7.412   -14.360 1.00 37.78  ? 173 PHE B CD2   1 
ATOM   4611 C  CE1   . PHE B 1 194 ? 12.638 5.800   -12.151 1.00 41.80  ? 173 PHE B CE1   1 
ATOM   4612 C  CE2   . PHE B 1 194 ? 11.748 6.896   -14.079 1.00 41.08  ? 173 PHE B CE2   1 
ATOM   4613 C  CZ    . PHE B 1 194 ? 11.568 6.091   -12.978 1.00 41.44  ? 173 PHE B CZ    1 
ATOM   4614 N  N     . ALA B 1 195 ? 17.635 10.289  -13.920 1.00 37.87  ? 174 ALA B N     1 
ATOM   4615 C  CA    . ALA B 1 195 ? 19.041 10.650  -14.191 1.00 39.38  ? 174 ALA B CA    1 
ATOM   4616 C  C     . ALA B 1 195 ? 19.718 9.487   -14.929 1.00 37.94  ? 174 ALA B C     1 
ATOM   4617 O  O     . ALA B 1 195 ? 20.910 9.235   -14.694 1.00 38.35  ? 174 ALA B O     1 
ATOM   4618 C  CB    . ALA B 1 195 ? 19.722 10.968  -12.878 1.00 41.18  ? 174 ALA B CB    1 
ATOM   4619 N  N     . ALA B 1 196 ? 18.930 8.782   -15.741 1.00 36.31  ? 175 ALA B N     1 
ATOM   4620 C  CA    . ALA B 1 196 ? 19.298 7.601   -16.546 1.00 34.44  ? 175 ALA B CA    1 
ATOM   4621 C  C     . ALA B 1 196 ? 18.331 7.537   -17.748 1.00 39.30  ? 175 ALA B C     1 
ATOM   4622 O  O     . ALA B 1 196 ? 17.277 8.223   -17.712 1.00 37.21  ? 175 ALA B O     1 
ATOM   4623 C  CB    . ALA B 1 196 ? 19.236 6.367   -15.690 1.00 32.60  ? 175 ALA B CB    1 
ATOM   4624 N  N     . THR B 1 197 ? 18.707 6.818   -18.810 1.00 36.75  ? 176 THR B N     1 
ATOM   4625 C  CA    . THR B 1 197 ? 17.890 6.610   -20.025 1.00 33.01  ? 176 THR B CA    1 
ATOM   4626 C  C     . THR B 1 197 ? 16.900 5.479   -19.751 1.00 29.45  ? 176 THR B C     1 
ATOM   4627 O  O     . THR B 1 197 ? 17.182 4.621   -18.914 1.00 29.35  ? 176 THR B O     1 
ATOM   4628 C  CB    . THR B 1 197 ? 18.736 6.304   -21.274 1.00 31.46  ? 176 THR B CB    1 
ATOM   4629 O  OG1   . THR B 1 197 ? 19.170 4.945   -21.256 1.00 32.35  ? 176 THR B OG1   1 
ATOM   4630 C  CG2   . THR B 1 197 ? 19.923 7.222   -21.414 1.00 32.19  ? 176 THR B CG2   1 
ATOM   4631 N  N     . SER B 1 198 ? 15.795 5.458   -20.487 1.00 32.05  ? 177 SER B N     1 
ATOM   4632 C  CA    . SER B 1 198 ? 14.793 4.367   -20.462 1.00 34.58  ? 177 SER B CA    1 
ATOM   4633 C  C     . SER B 1 198 ? 15.486 3.021   -20.725 1.00 35.01  ? 177 SER B C     1 
ATOM   4634 O  O     . SER B 1 198 ? 14.949 2.025   -20.213 1.00 36.62  ? 177 SER B O     1 
ATOM   4635 C  CB    . SER B 1 198 ? 13.688 4.629   -21.440 1.00 33.89  ? 177 SER B CB    1 
ATOM   4636 O  OG    . SER B 1 198 ? 14.198 4.970   -22.714 1.00 33.83  ? 177 SER B OG    1 
ATOM   4637 N  N     . ALA B 1 199 ? 16.623 2.994   -21.459 1.00 33.13  ? 178 ALA B N     1 
ATOM   4638 C  CA    . ALA B 1 199 ? 17.371 1.753   -21.787 1.00 35.38  ? 178 ALA B CA    1 
ATOM   4639 C  C     . ALA B 1 199 ? 18.094 1.201   -20.555 1.00 36.17  ? 178 ALA B C     1 
ATOM   4640 O  O     . ALA B 1 199 ? 18.252 -0.037  -20.473 1.00 37.35  ? 178 ALA B O     1 
ATOM   4641 C  CB    . ALA B 1 199 ? 18.345 1.977   -22.923 1.00 38.38  ? 178 ALA B CB    1 
ATOM   4642 N  N     . GLN B 1 200 ? 18.505 2.054   -19.613 1.00 35.90  ? 179 GLN B N     1 
ATOM   4643 C  CA    . GLN B 1 200 ? 19.265 1.582   -18.425 1.00 34.72  ? 179 GLN B CA    1 
ATOM   4644 C  C     . GLN B 1 200 ? 18.326 0.977   -17.374 1.00 34.33  ? 179 GLN B C     1 
ATOM   4645 O  O     . GLN B 1 200 ? 18.818 0.167   -16.596 1.00 32.38  ? 179 GLN B O     1 
ATOM   4646 C  CB    . GLN B 1 200 ? 20.097 2.707   -17.818 1.00 32.38  ? 179 GLN B CB    1 
ATOM   4647 C  CG    . GLN B 1 200 ? 21.168 3.234   -18.760 1.00 32.71  ? 179 GLN B CG    1 
ATOM   4648 C  CD    . GLN B 1 200 ? 21.765 4.508   -18.215 1.00 33.56  ? 179 GLN B CD    1 
ATOM   4649 O  OE1   . GLN B 1 200 ? 21.283 5.609   -18.460 1.00 35.06  ? 179 GLN B OE1   1 
ATOM   4650 N  NE2   . GLN B 1 200 ? 22.800 4.369   -17.405 1.00 37.80  ? 179 GLN B NE2   1 
ATOM   4651 N  N     . LEU B 1 201 ? 17.047 1.365   -17.317 1.00 34.78  ? 180 LEU B N     1 
ATOM   4652 C  CA    . LEU B 1 201 ? 16.125 0.989   -16.205 1.00 33.24  ? 180 LEU B CA    1 
ATOM   4653 C  C     . LEU B 1 201 ? 15.342 -0.275  -16.579 1.00 32.76  ? 180 LEU B C     1 
ATOM   4654 O  O     . LEU B 1 201 ? 14.810 -0.329  -17.698 1.00 29.20  ? 180 LEU B O     1 
ATOM   4655 C  CB    . LEU B 1 201 ? 15.123 2.125   -15.953 1.00 34.67  ? 180 LEU B CB    1 
ATOM   4656 C  CG    . LEU B 1 201 ? 15.698 3.533   -15.880 1.00 37.33  ? 180 LEU B CG    1 
ATOM   4657 C  CD1   . LEU B 1 201 ? 14.587 4.565   -15.947 1.00 40.34  ? 180 LEU B CD1   1 
ATOM   4658 C  CD2   . LEU B 1 201 ? 16.522 3.720   -14.625 1.00 39.92  ? 180 LEU B CD2   1 
ATOM   4659 N  N     . SER B 1 202 ? 15.176 -1.213  -15.650 1.00 32.79  ? 181 SER B N     1 
ATOM   4660 C  CA    . SER B 1 202 ? 14.161 -2.285  -15.795 1.00 34.96  ? 181 SER B CA    1 
ATOM   4661 C  C     . SER B 1 202 ? 12.757 -1.664  -15.664 1.00 36.02  ? 181 SER B C     1 
ATOM   4662 O  O     . SER B 1 202 ? 12.626 -0.611  -14.996 1.00 31.37  ? 181 SER B O     1 
ATOM   4663 C  CB    . SER B 1 202 ? 14.381 -3.380  -14.780 1.00 35.65  ? 181 SER B CB    1 
ATOM   4664 O  OG    . SER B 1 202 ? 13.767 -3.077  -13.539 1.00 34.90  ? 181 SER B OG    1 
ATOM   4665 N  N     . LEU B 1 203 ? 11.747 -2.288  -16.275 1.00 36.83  ? 182 LEU B N     1 
ATOM   4666 C  CA    . LEU B 1 203 ? 10.339 -1.806  -16.243 1.00 37.36  ? 182 LEU B CA    1 
ATOM   4667 C  C     . LEU B 1 203 ? 9.862  -1.833  -14.787 1.00 37.30  ? 182 LEU B C     1 
ATOM   4668 O  O     . LEU B 1 203 ? 9.249  -0.842  -14.292 1.00 32.57  ? 182 LEU B O     1 
ATOM   4669 C  CB    . LEU B 1 203 ? 9.481  -2.692  -17.152 1.00 39.81  ? 182 LEU B CB    1 
ATOM   4670 C  CG    . LEU B 1 203 ? 7.972  -2.497  -17.039 1.00 40.66  ? 182 LEU B CG    1 
ATOM   4671 C  CD1   . LEU B 1 203 ? 7.591  -1.036  -17.205 1.00 41.50  ? 182 LEU B CD1   1 
ATOM   4672 C  CD2   . LEU B 1 203 ? 7.253  -3.343  -18.062 1.00 39.40  ? 182 LEU B CD2   1 
ATOM   4673 N  N     . LEU B 1 204 ? 10.191 -2.911  -14.099 1.00 31.40  ? 183 LEU B N     1 
ATOM   4674 C  CA    . LEU B 1 204 ? 9.837  -3.089  -12.670 1.00 32.33  ? 183 LEU B CA    1 
ATOM   4675 C  C     . LEU B 1 204 ? 10.444 -1.965  -11.800 1.00 32.23  ? 183 LEU B C     1 
ATOM   4676 O  O     . LEU B 1 204 ? 9.794  -1.510  -10.832 1.00 32.77  ? 183 LEU B O     1 
ATOM   4677 C  CB    . LEU B 1 204 ? 10.331 -4.479  -12.252 1.00 32.09  ? 183 LEU B CB    1 
ATOM   4678 C  CG    . LEU B 1 204 ? 10.001 -4.885  -10.819 1.00 31.52  ? 183 LEU B CG    1 
ATOM   4679 C  CD1   . LEU B 1 204 ? 8.499  -4.803  -10.578 1.00 32.88  ? 183 LEU B CD1   1 
ATOM   4680 C  CD2   . LEU B 1 204 ? 10.505 -6.282  -10.546 1.00 31.20  ? 183 LEU B CD2   1 
ATOM   4681 N  N     . HIS B 1 205 ? 11.683 -1.558  -12.039 1.00 30.44  ? 184 HIS B N     1 
ATOM   4682 C  CA    . HIS B 1 205 ? 12.279 -0.459  -11.229 1.00 32.54  ? 184 HIS B CA    1 
ATOM   4683 C  C     . HIS B 1 205 ? 11.472 0.830   -11.448 1.00 27.00  ? 184 HIS B C     1 
ATOM   4684 O  O     . HIS B 1 205 ? 11.140 1.467   -10.437 1.00 26.42  ? 184 HIS B O     1 
ATOM   4685 C  CB    . HIS B 1 205 ? 13.773 -0.245  -11.510 1.00 31.70  ? 184 HIS B CB    1 
ATOM   4686 C  CG    . HIS B 1 205 ? 14.262 0.957   -10.798 1.00 30.52  ? 184 HIS B CG    1 
ATOM   4687 N  ND1   . HIS B 1 205 ? 14.428 0.960   -9.456  1.00 31.09  ? 184 HIS B ND1   1 
ATOM   4688 C  CD2   . HIS B 1 205 ? 14.510 2.211   -11.230 1.00 32.19  ? 184 HIS B CD2   1 
ATOM   4689 C  CE1   . HIS B 1 205 ? 14.818 2.158   -9.078  1.00 31.78  ? 184 HIS B CE1   1 
ATOM   4690 N  NE2   . HIS B 1 205 ? 14.876 2.944   -10.151 1.00 33.31  ? 184 HIS B NE2   1 
ATOM   4691 N  N     . ALA B 1 206 ? 11.146 1.162   -12.701 1.00 25.72  ? 185 ALA B N     1 
ATOM   4692 C  CA    . ALA B 1 206 ? 10.400 2.386   -13.097 1.00 30.93  ? 185 ALA B CA    1 
ATOM   4693 C  C     . ALA B 1 206 ? 8.976  2.354   -12.503 1.00 33.29  ? 185 ALA B C     1 
ATOM   4694 O  O     . ALA B 1 206 ? 8.574  3.331   -11.825 1.00 34.72  ? 185 ALA B O     1 
ATOM   4695 C  CB    . ALA B 1 206 ? 10.411 2.525   -14.592 1.00 32.39  ? 185 ALA B CB    1 
ATOM   4696 N  N     . ALA B 1 207 ? 8.265  1.238   -12.670 1.00 33.53  ? 186 ALA B N     1 
ATOM   4697 C  CA    . ALA B 1 207 ? 6.954  0.961   -12.055 1.00 32.69  ? 186 ALA B CA    1 
ATOM   4698 C  C     . ALA B 1 207 ? 7.009  1.201   -10.539 1.00 34.80  ? 186 ALA B C     1 
ATOM   4699 O  O     . ALA B 1 207 ? 6.191  1.989   -10.009 1.00 34.20  ? 186 ALA B O     1 
ATOM   4700 C  CB    . ALA B 1 207 ? 6.569  -0.459  -12.376 1.00 38.86  ? 186 ALA B CB    1 
ATOM   4701 N  N     . HIS B 1 208 ? 7.924  0.540   -9.829  1.00 33.10  ? 187 HIS B N     1 
ATOM   4702 C  CA    . HIS B 1 208 ? 8.046  0.678   -8.352  1.00 30.65  ? 187 HIS B CA    1 
ATOM   4703 C  C     . HIS B 1 208 ? 8.251  2.144   -7.972  1.00 30.76  ? 187 HIS B C     1 
ATOM   4704 O  O     . HIS B 1 208 ? 7.754  2.550   -6.887  1.00 31.30  ? 187 HIS B O     1 
ATOM   4705 C  CB    . HIS B 1 208 ? 9.208  -0.147  -7.793  1.00 32.03  ? 187 HIS B CB    1 
ATOM   4706 C  CG    . HIS B 1 208 ? 9.574  0.203   -6.387  1.00 31.30  ? 187 HIS B CG    1 
ATOM   4707 N  ND1   . HIS B 1 208 ? 8.914  -0.336  -5.299  1.00 33.00  ? 187 HIS B ND1   1 
ATOM   4708 C  CD2   . HIS B 1 208 ? 10.542 1.008   -5.888  1.00 34.26  ? 187 HIS B CD2   1 
ATOM   4709 C  CE1   . HIS B 1 208 ? 9.444  0.144   -4.185  1.00 32.62  ? 187 HIS B CE1   1 
ATOM   4710 N  NE2   . HIS B 1 208 ? 10.444 0.980   -4.517  1.00 34.24  ? 187 HIS B NE2   1 
ATOM   4711 N  N     . TYR B 1 209 ? 9.059  2.877   -8.741  1.00 30.80  ? 188 TYR B N     1 
ATOM   4712 C  CA    . TYR B 1 209 ? 9.425  4.287   -8.418  1.00 33.08  ? 188 TYR B CA    1 
ATOM   4713 C  C     . TYR B 1 209 ? 8.180  5.159   -8.557  1.00 29.81  ? 188 TYR B C     1 
ATOM   4714 O  O     . TYR B 1 209 ? 7.952  6.019   -7.694  1.00 34.44  ? 188 TYR B O     1 
ATOM   4715 C  CB    . TYR B 1 209 ? 10.496 4.834   -9.361  1.00 32.60  ? 188 TYR B CB    1 
ATOM   4716 C  CG    . TYR B 1 209 ? 11.344 5.963   -8.836  1.00 30.39  ? 188 TYR B CG    1 
ATOM   4717 C  CD1   . TYR B 1 209 ? 12.497 5.703   -8.102  1.00 31.98  ? 188 TYR B CD1   1 
ATOM   4718 C  CD2   . TYR B 1 209 ? 11.058 7.276   -9.176  1.00 28.82  ? 188 TYR B CD2   1 
ATOM   4719 C  CE1   . TYR B 1 209 ? 13.327 6.733   -7.685  1.00 32.82  ? 188 TYR B CE1   1 
ATOM   4720 C  CE2   . TYR B 1 209 ? 11.877 8.322   -8.769  1.00 30.91  ? 188 TYR B CE2   1 
ATOM   4721 C  CZ    . TYR B 1 209 ? 12.999 8.046   -8.002  1.00 32.38  ? 188 TYR B CZ    1 
ATOM   4722 O  OH    . TYR B 1 209 ? 13.811 9.063   -7.617  1.00 30.59  ? 188 TYR B OH    1 
ATOM   4723 N  N     . VAL B 1 210 ? 7.399  4.901   -9.601  1.00 32.21  ? 189 VAL B N     1 
ATOM   4724 C  CA    . VAL B 1 210 ? 6.138  5.631   -9.905  1.00 36.56  ? 189 VAL B CA    1 
ATOM   4725 C  C     . VAL B 1 210 ? 5.176  5.398   -8.743  1.00 37.78  ? 189 VAL B C     1 
ATOM   4726 O  O     . VAL B 1 210 ? 4.610  6.414   -8.204  1.00 36.11  ? 189 VAL B O     1 
ATOM   4727 C  CB    . VAL B 1 210 ? 5.538  5.201   -11.256 1.00 40.20  ? 189 VAL B CB    1 
ATOM   4728 C  CG1   . VAL B 1 210 ? 4.115  5.733   -11.445 1.00 40.24  ? 189 VAL B CG1   1 
ATOM   4729 C  CG2   . VAL B 1 210 ? 6.454  5.625   -12.407 1.00 40.04  ? 189 VAL B CG2   1 
ATOM   4730 N  N     . HIS B 1 211 ? 5.062  4.140   -8.320  1.00 33.07  ? 190 HIS B N     1 
ATOM   4731 C  CA    . HIS B 1 211 ? 4.123  3.721   -7.250  1.00 34.59  ? 190 HIS B CA    1 
ATOM   4732 C  C     . HIS B 1 211 ? 4.549  4.398   -5.941  1.00 36.74  ? 190 HIS B C     1 
ATOM   4733 O  O     . HIS B 1 211 ? 3.687  4.946   -5.229  1.00 39.51  ? 190 HIS B O     1 
ATOM   4734 C  CB    . HIS B 1 211 ? 4.019  2.198   -7.188  1.00 35.08  ? 190 HIS B CB    1 
ATOM   4735 C  CG    . HIS B 1 211 ? 2.908  1.745   -6.304  1.00 44.07  ? 190 HIS B CG    1 
ATOM   4736 N  ND1   . HIS B 1 211 ? 2.803  0.435   -5.857  1.00 41.72  ? 190 HIS B ND1   1 
ATOM   4737 C  CD2   . HIS B 1 211 ? 1.869  2.431   -5.763  1.00 38.60  ? 190 HIS B CD2   1 
ATOM   4738 C  CE1   . HIS B 1 211 ? 1.754  0.344   -5.063  1.00 40.79  ? 190 HIS B CE1   1 
ATOM   4739 N  NE2   . HIS B 1 211 ? 1.153  1.550   -5.008  1.00 43.61  ? 190 HIS B NE2   1 
ATOM   4740 N  N     . SER B 1 212 ? 5.852  4.464   -5.688  1.00 35.59  ? 191 SER B N     1 
ATOM   4741 C  CA    . SER B 1 212 ? 6.430  5.059   -4.458  1.00 33.71  ? 191 SER B CA    1 
ATOM   4742 C  C     . SER B 1 212 ? 6.123  6.567   -4.387  1.00 33.63  ? 191 SER B C     1 
ATOM   4743 O  O     . SER B 1 212 ? 6.095  7.083   -3.262  1.00 35.50  ? 191 SER B O     1 
ATOM   4744 C  CB    . SER B 1 212 ? 7.900  4.761   -4.382  1.00 30.42  ? 191 SER B CB    1 
ATOM   4745 O  OG    . SER B 1 212 ? 8.530  5.451   -3.320  1.00 33.35  ? 191 SER B OG    1 
ATOM   4746 N  N     . ALA B 1 213 ? 5.951  7.243   -5.523  1.00 32.69  ? 192 ALA B N     1 
ATOM   4747 C  CA    . ALA B 1 213 ? 5.671  8.700   -5.593  1.00 40.72  ? 192 ALA B CA    1 
ATOM   4748 C  C     . ALA B 1 213 ? 4.150  8.973   -5.531  1.00 38.62  ? 192 ALA B C     1 
ATOM   4749 O  O     . ALA B 1 213 ? 3.775  10.117  -5.203  1.00 40.45  ? 192 ALA B O     1 
ATOM   4750 C  CB    . ALA B 1 213 ? 6.291  9.280   -6.850  1.00 38.75  ? 192 ALA B CB    1 
ATOM   4751 N  N     . GLY B 1 214 ? 3.319  7.966   -5.831  1.00 36.20  ? 193 GLY B N     1 
ATOM   4752 C  CA    . GLY B 1 214 ? 1.854  8.080   -5.953  1.00 35.65  ? 193 GLY B CA    1 
ATOM   4753 C  C     . GLY B 1 214 ? 1.411  8.384   -7.386  1.00 40.93  ? 193 GLY B C     1 
ATOM   4754 O  O     . GLY B 1 214 ? 0.350  8.989   -7.546  1.00 48.07  ? 193 GLY B O     1 
ATOM   4755 N  N     . GLY B 1 215 ? 2.192  8.011   -8.407  1.00 37.34  ? 194 GLY B N     1 
ATOM   4756 C  CA    . GLY B 1 215 ? 1.813  8.159   -9.823  1.00 37.02  ? 194 GLY B CA    1 
ATOM   4757 C  C     . GLY B 1 215 ? 2.738  9.083   -10.615 1.00 38.22  ? 194 GLY B C     1 
ATOM   4758 O  O     . GLY B 1 215 ? 3.589  9.773   -10.002 1.00 34.28  ? 194 GLY B O     1 
ATOM   4759 N  N     . TRP B 1 216 ? 2.518  9.116   -11.934 1.00 38.24  ? 195 TRP B N     1 
ATOM   4760 C  CA    . TRP B 1 216 ? 3.313  9.831   -12.962 1.00 39.70  ? 195 TRP B CA    1 
ATOM   4761 C  C     . TRP B 1 216 ? 3.138  11.354  -12.830 1.00 41.33  ? 195 TRP B C     1 
ATOM   4762 O  O     . TRP B 1 216 ? 4.166  12.089  -12.899 1.00 39.49  ? 195 TRP B O     1 
ATOM   4763 C  CB    . TRP B 1 216 ? 2.934  9.313   -14.347 1.00 39.11  ? 195 TRP B CB    1 
ATOM   4764 C  CG    . TRP B 1 216 ? 3.817  9.879   -15.409 1.00 48.09  ? 195 TRP B CG    1 
ATOM   4765 C  CD1   . TRP B 1 216 ? 3.506  10.869  -16.301 1.00 51.11  ? 195 TRP B CD1   1 
ATOM   4766 C  CD2   . TRP B 1 216 ? 5.202  9.558   -15.634 1.00 48.30  ? 195 TRP B CD2   1 
ATOM   4767 N  NE1   . TRP B 1 216 ? 4.594  11.156  -17.082 1.00 50.57  ? 195 TRP B NE1   1 
ATOM   4768 C  CE2   . TRP B 1 216 ? 5.646  10.367  -16.700 1.00 48.80  ? 195 TRP B CE2   1 
ATOM   4769 C  CE3   . TRP B 1 216 ? 6.105  8.676   -15.041 1.00 49.70  ? 195 TRP B CE3   1 
ATOM   4770 C  CZ2   . TRP B 1 216 ? 6.944  10.300  -17.198 1.00 51.02  ? 195 TRP B CZ2   1 
ATOM   4771 C  CZ3   . TRP B 1 216 ? 7.388  8.605   -15.536 1.00 54.78  ? 195 TRP B CZ3   1 
ATOM   4772 C  CH2   . TRP B 1 216 ? 7.800  9.406   -16.603 1.00 52.94  ? 195 TRP B CH2   1 
ATOM   4773 N  N     . SER B 1 217 ? 1.919  11.819  -12.556 1.00 41.76  ? 196 SER B N     1 
ATOM   4774 C  CA    . SER B 1 217 ? 1.601  13.263  -12.371 1.00 42.46  ? 196 SER B CA    1 
ATOM   4775 C  C     . SER B 1 217 ? 2.384  13.785  -11.173 1.00 42.14  ? 196 SER B C     1 
ATOM   4776 O  O     . SER B 1 217 ? 2.972  14.857  -11.279 1.00 37.40  ? 196 SER B O     1 
ATOM   4777 C  CB    . SER B 1 217 ? 0.138  13.501  -12.194 1.00 40.94  ? 196 SER B CB    1 
ATOM   4778 O  OG    . SER B 1 217 ? -0.543 13.232  -13.403 1.00 44.07  ? 196 SER B OG    1 
ATOM   4779 N  N     . LYS B 1 218 ? 2.446  12.995  -10.103 1.00 41.88  ? 197 LYS B N     1 
ATOM   4780 C  CA    . LYS B 1 218 ? 3.175  13.362  -8.864  1.00 42.31  ? 197 LYS B CA    1 
ATOM   4781 C  C     . LYS B 1 218 ? 4.668  13.584  -9.158  1.00 41.32  ? 197 LYS B C     1 
ATOM   4782 O  O     . LYS B 1 218 ? 5.235  14.515  -8.516  1.00 41.16  ? 197 LYS B O     1 
ATOM   4783 C  CB    . LYS B 1 218 ? 2.922  12.324  -7.769  1.00 45.47  ? 197 LYS B CB    1 
ATOM   4784 C  CG    . LYS B 1 218 ? 1.695  12.590  -6.906  1.00 47.16  ? 197 LYS B CG    1 
ATOM   4785 C  CD    . LYS B 1 218 ? 1.896  13.782  -5.990  1.00 53.82  ? 197 LYS B CD    1 
ATOM   4786 C  CE    . LYS B 1 218 ? 0.607  14.393  -5.489  1.00 56.78  ? 197 LYS B CE    1 
ATOM   4787 N  NZ    . LYS B 1 218 ? 0.076  13.609  -4.356  1.00 63.10  ? 197 LYS B NZ    1 
ATOM   4788 N  N     . LEU B 1 219 ? 5.266  12.804  -10.082 1.00 38.25  ? 198 LEU B N     1 
ATOM   4789 C  CA    . LEU B 1 219 ? 6.715  12.876  -10.453 1.00 36.65  ? 198 LEU B CA    1 
ATOM   4790 C  C     . LEU B 1 219 ? 7.006  14.088  -11.363 1.00 34.64  ? 198 LEU B C     1 
ATOM   4791 O  O     . LEU B 1 219 ? 8.045  14.736  -11.121 1.00 32.44  ? 198 LEU B O     1 
ATOM   4792 C  CB    . LEU B 1 219 ? 7.172  11.569  -11.121 1.00 34.06  ? 198 LEU B CB    1 
ATOM   4793 C  CG    . LEU B 1 219 ? 7.310  10.359  -10.198 1.00 34.40  ? 198 LEU B CG    1 
ATOM   4794 C  CD1   . LEU B 1 219 ? 7.641  9.102   -10.992 1.00 36.40  ? 198 LEU B CD1   1 
ATOM   4795 C  CD2   . LEU B 1 219 ? 8.359  10.571  -9.125  1.00 34.27  ? 198 LEU B CD2   1 
ATOM   4796 N  N     . THR B 1 220 ? 6.135  14.388  -12.336 1.00 34.26  ? 199 THR B N     1 
ATOM   4797 C  CA    . THR B 1 220 ? 6.385  15.332  -13.465 1.00 37.38  ? 199 THR B CA    1 
ATOM   4798 C  C     . THR B 1 220 ? 5.795  16.716  -13.166 1.00 36.72  ? 199 THR B C     1 
ATOM   4799 O  O     . THR B 1 220 ? 6.362  17.706  -13.625 1.00 34.87  ? 199 THR B O     1 
ATOM   4800 C  CB    . THR B 1 220 ? 5.830  14.789  -14.795 1.00 38.33  ? 199 THR B CB    1 
ATOM   4801 O  OG1   . THR B 1 220 ? 4.471  14.371  -14.679 1.00 39.16  ? 199 THR B OG1   1 
ATOM   4802 C  CG2   . THR B 1 220 ? 6.576  13.578  -15.296 1.00 39.50  ? 199 THR B CG2   1 
ATOM   4803 N  N     . ASP B 1 221 ? 4.720  16.804  -12.387 1.00 39.65  ? 200 ASP B N     1 
ATOM   4804 C  CA    . ASP B 1 221 ? 3.985  18.085  -12.188 1.00 37.49  ? 200 ASP B CA    1 
ATOM   4805 C  C     . ASP B 1 221 ? 4.740  19.031  -11.245 1.00 39.14  ? 200 ASP B C     1 
ATOM   4806 O  O     . ASP B 1 221 ? 5.360  18.574  -10.244 1.00 37.08  ? 200 ASP B O     1 
ATOM   4807 C  CB    . ASP B 1 221 ? 2.564  17.841  -11.680 1.00 39.52  ? 200 ASP B CB    1 
ATOM   4808 C  CG    . ASP B 1 221 ? 1.629  17.312  -12.763 1.00 44.04  ? 200 ASP B CG    1 
ATOM   4809 O  OD1   . ASP B 1 221 ? 2.104  17.140  -13.904 1.00 40.38  ? 200 ASP B OD1   1 
ATOM   4810 O  OD2   . ASP B 1 221 ? 0.423  17.083  -12.457 1.00 47.49  ? 200 ASP B OD2   1 
ATOM   4811 N  N     . THR B 1 222 ? 4.635  20.330  -11.525 1.00 39.25  ? 201 THR B N     1 
ATOM   4812 C  CA    . THR B 1 222 ? 4.980  21.421  -10.587 1.00 39.22  ? 201 THR B CA    1 
ATOM   4813 C  C     . THR B 1 222 ? 3.820  21.543  -9.578  1.00 44.80  ? 201 THR B C     1 
ATOM   4814 O  O     . THR B 1 222 ? 3.916  20.937  -8.466  1.00 44.27  ? 201 THR B O     1 
ATOM   4815 C  CB    . THR B 1 222 ? 5.322  22.692  -11.384 1.00 39.44  ? 201 THR B CB    1 
ATOM   4816 O  OG1   . THR B 1 222 ? 6.466  22.408  -12.194 1.00 38.22  ? 201 THR B OG1   1 
ATOM   4817 C  CG2   . THR B 1 222 ? 5.617  23.889  -10.509 1.00 36.72  ? 201 THR B CG2   1 
ATOM   4818 N  N     . GLU B 1 223 ? 2.765  22.289  -9.934  1.00 46.23  ? 202 GLU B N     1 
ATOM   4819 C  CA    . GLU B 1 223 ? 1.522  22.435  -9.129  1.00 48.97  ? 202 GLU B CA    1 
ATOM   4820 C  C     . GLU B 1 223 ? 0.892  21.046  -8.958  1.00 45.69  ? 202 GLU B C     1 
ATOM   4821 O  O     . GLU B 1 223 ? 0.586  20.373  -9.981  1.00 41.30  ? 202 GLU B O     1 
ATOM   4822 C  CB    . GLU B 1 223 ? 0.549  23.475  -9.706  1.00 53.47  ? 202 GLU B CB    1 
ATOM   4823 C  CG    . GLU B 1 223 ? 0.328  23.383  -11.212 1.00 67.34  ? 202 GLU B CG    1 
ATOM   4824 C  CD    . GLU B 1 223 ? 1.233  24.263  -12.073 1.00 75.37  ? 202 GLU B CD    1 
ATOM   4825 O  OE1   . GLU B 1 223 ? 1.087  25.516  -11.967 1.00 71.90  ? 202 GLU B OE1   1 
ATOM   4826 O  OE2   . GLU B 1 223 ? 2.089  23.693  -12.855 1.00 58.84  ? 202 GLU B OE2   1 
ATOM   4827 N  N     . GLY B 1 224 ? 0.743  20.637  -7.692  1.00 47.24  ? 203 GLY B N     1 
ATOM   4828 C  CA    . GLY B 1 224 ? 0.173  19.341  -7.284  1.00 45.86  ? 203 GLY B CA    1 
ATOM   4829 C  C     . GLY B 1 224 ? 1.162  18.188  -7.374  1.00 43.15  ? 203 GLY B C     1 
ATOM   4830 O  O     . GLY B 1 224 ? 0.677  17.044  -7.259  1.00 40.38  ? 203 GLY B O     1 
ATOM   4831 N  N     . GLY B 1 225 ? 2.475  18.469  -7.516  1.00 41.82  ? 204 GLY B N     1 
ATOM   4832 C  CA    . GLY B 1 225 ? 3.530  17.457  -7.758  1.00 36.79  ? 204 GLY B CA    1 
ATOM   4833 C  C     . GLY B 1 225 ? 4.827  17.753  -7.027  1.00 36.73  ? 204 GLY B C     1 
ATOM   4834 O  O     . GLY B 1 225 ? 4.883  18.740  -6.286  1.00 35.52  ? 204 GLY B O     1 
ATOM   4835 N  N     . ALA B 1 226 ? 5.866  16.937  -7.262  1.00 37.74  ? 205 ALA B N     1 
ATOM   4836 C  CA    . ALA B 1 226 ? 7.149  16.949  -6.517  1.00 32.42  ? 205 ALA B CA    1 
ATOM   4837 C  C     . ALA B 1 226 ? 7.887  18.285  -6.667  1.00 29.72  ? 205 ALA B C     1 
ATOM   4838 O  O     . ALA B 1 226 ? 8.739  18.580  -5.802  1.00 29.07  ? 205 ALA B O     1 
ATOM   4839 C  CB    . ALA B 1 226 ? 8.040  15.842  -6.998  1.00 32.85  ? 205 ALA B CB    1 
ATOM   4840 N  N     . GLN B 1 227 ? 7.616  19.058  -7.712  1.00 29.18  ? 206 GLN B N     1 
ATOM   4841 C  CA    . GLN B 1 227 ? 8.367  20.325  -7.955  1.00 33.59  ? 206 GLN B CA    1 
ATOM   4842 C  C     . GLN B 1 227 ? 7.573  21.559  -7.483  1.00 34.85  ? 206 GLN B C     1 
ATOM   4843 O  O     . GLN B 1 227 ? 7.970  22.690  -7.875  1.00 36.40  ? 206 GLN B O     1 
ATOM   4844 C  CB    . GLN B 1 227 ? 8.808  20.395  -9.424  1.00 32.91  ? 206 GLN B CB    1 
ATOM   4845 C  CG    . GLN B 1 227 ? 10.028 19.516  -9.720  1.00 32.82  ? 206 GLN B CG    1 
ATOM   4846 C  CD    . GLN B 1 227 ? 9.671  18.058  -9.926  1.00 32.02  ? 206 GLN B CD    1 
ATOM   4847 O  OE1   . GLN B 1 227 ? 8.868  17.701  -10.790 1.00 31.00  ? 206 GLN B OE1   1 
ATOM   4848 N  NE2   . GLN B 1 227 ? 10.260 17.198  -9.119  1.00 34.04  ? 206 GLN B NE2   1 
ATOM   4849 N  N     . GLN B 1 228 ? 6.591  21.395  -6.587  1.00 35.86  ? 207 GLN B N     1 
ATOM   4850 C  CA    . GLN B 1 228 ? 5.654  22.501  -6.206  1.00 39.20  ? 207 GLN B CA    1 
ATOM   4851 C  C     . GLN B 1 228 ? 6.331  23.633  -5.409  1.00 33.39  ? 207 GLN B C     1 
ATOM   4852 O  O     . GLN B 1 228 ? 5.987  24.818  -5.669  1.00 37.27  ? 207 GLN B O     1 
ATOM   4853 C  CB    . GLN B 1 228 ? 4.459  21.987  -5.402  1.00 39.62  ? 207 GLN B CB    1 
ATOM   4854 C  CG    . GLN B 1 228 ? 3.290  22.969  -5.463  1.00 41.91  ? 207 GLN B CG    1 
ATOM   4855 C  CD    . GLN B 1 228 ? 2.099  22.547  -4.644  1.00 38.18  ? 207 GLN B CD    1 
ATOM   4856 O  OE1   . GLN B 1 228 ? 1.114  22.058  -5.169  1.00 38.25  ? 207 GLN B OE1   1 
ATOM   4857 N  NE2   . GLN B 1 228 ? 2.214  22.697  -3.341  1.00 35.29  ? 207 GLN B NE2   1 
ATOM   4858 N  N     . ASP B 1 229 ? 7.192  23.314  -4.442  1.00 31.54  ? 208 ASP B N     1 
ATOM   4859 C  CA    . ASP B 1 229 ? 7.684  24.272  -3.415  1.00 36.61  ? 208 ASP B CA    1 
ATOM   4860 C  C     . ASP B 1 229 ? 9.191  24.136  -3.193  1.00 39.41  ? 208 ASP B C     1 
ATOM   4861 O  O     . ASP B 1 229 ? 9.746  23.029  -3.395  1.00 38.67  ? 208 ASP B O     1 
ATOM   4862 C  CB    . ASP B 1 229 ? 6.971  24.106  -2.061  1.00 40.17  ? 208 ASP B CB    1 
ATOM   4863 C  CG    . ASP B 1 229 ? 5.509  24.575  -2.061  1.00 48.16  ? 208 ASP B CG    1 
ATOM   4864 O  OD1   . ASP B 1 229 ? 5.244  25.777  -2.357  1.00 50.12  ? 208 ASP B OD1   1 
ATOM   4865 O  OD2   . ASP B 1 229 ? 4.623  23.726  -1.810  1.00 49.37  ? 208 ASP B OD2   1 
ATOM   4866 N  N     . ARG B 1 230 ? 9.787  25.232  -2.712  1.00 35.81  ? 209 ARG B N     1 
ATOM   4867 C  CA    . ARG B 1 230 ? 11.197 25.376  -2.294  1.00 35.08  ? 209 ARG B CA    1 
ATOM   4868 C  C     . ARG B 1 230 ? 11.221 25.779  -0.819  1.00 35.88  ? 209 ARG B C     1 
ATOM   4869 O  O     . ARG B 1 230 ? 10.182 26.125  -0.272  1.00 38.43  ? 209 ARG B O     1 
ATOM   4870 C  CB    . ARG B 1 230 ? 11.879 26.480  -3.104  1.00 38.02  ? 209 ARG B CB    1 
ATOM   4871 C  CG    . ARG B 1 230 ? 11.902 26.282  -4.616  1.00 41.08  ? 209 ARG B CG    1 
ATOM   4872 C  CD    . ARG B 1 230 ? 13.088 25.489  -5.140  1.00 36.74  ? 209 ARG B CD    1 
ATOM   4873 N  NE    . ARG B 1 230 ? 14.371 25.886  -4.586  1.00 36.31  ? 209 ARG B NE    1 
ATOM   4874 C  CZ    . ARG B 1 230 ? 15.284 26.693  -5.153  1.00 36.55  ? 209 ARG B CZ    1 
ATOM   4875 N  NH1   . ARG B 1 230 ? 15.088 27.266  -6.324  1.00 33.19  ? 209 ARG B NH1   1 
ATOM   4876 N  NH2   . ARG B 1 230 ? 16.418 26.940  -4.522  1.00 36.89  ? 209 ARG B NH2   1 
ATOM   4877 N  N     . LEU B 1 231 ? 12.394 25.768  -0.203  1.00 40.01  ? 210 LEU B N     1 
ATOM   4878 C  CA    . LEU B 1 231 ? 12.598 26.135  1.219   1.00 37.35  ? 210 LEU B CA    1 
ATOM   4879 C  C     . LEU B 1 231 ? 13.303 27.489  1.214   1.00 41.31  ? 210 LEU B C     1 
ATOM   4880 O  O     . LEU B 1 231 ? 14.222 27.654  0.393   1.00 40.26  ? 210 LEU B O     1 
ATOM   4881 C  CB    . LEU B 1 231 ? 13.417 25.035  1.916   1.00 39.06  ? 210 LEU B CB    1 
ATOM   4882 C  CG    . LEU B 1 231 ? 12.634 23.895  2.605   1.00 43.14  ? 210 LEU B CG    1 
ATOM   4883 C  CD1   . LEU B 1 231 ? 11.374 23.480  1.865   1.00 43.94  ? 210 LEU B CD1   1 
ATOM   4884 C  CD2   . LEU B 1 231 ? 13.493 22.657  2.810   1.00 42.32  ? 210 LEU B CD2   1 
ATOM   4885 N  N     . VAL B 1 232 ? 12.827 28.440  2.023   1.00 40.21  ? 211 VAL B N     1 
ATOM   4886 C  CA    . VAL B 1 232 ? 13.446 29.789  2.171   1.00 40.39  ? 211 VAL B CA    1 
ATOM   4887 C  C     . VAL B 1 232 ? 14.808 29.608  2.870   1.00 41.72  ? 211 VAL B C     1 
ATOM   4888 O  O     . VAL B 1 232 ? 14.860 29.040  3.969   1.00 39.70  ? 211 VAL B O     1 
ATOM   4889 C  CB    . VAL B 1 232 ? 12.486 30.750  2.911   1.00 40.16  ? 211 VAL B CB    1 
ATOM   4890 C  CG1   . VAL B 1 232 ? 13.157 32.050  3.350   1.00 37.29  ? 211 VAL B CG1   1 
ATOM   4891 C  CG2   . VAL B 1 232 ? 11.249 31.048  2.071   1.00 38.15  ? 211 VAL B CG2   1 
ATOM   4892 N  N     . GLY B 1 233 ? 15.889 30.056  2.231   1.00 43.14  ? 212 GLY B N     1 
ATOM   4893 C  CA    . GLY B 1 233 ? 17.277 29.841  2.681   1.00 39.85  ? 212 GLY B CA    1 
ATOM   4894 C  C     . GLY B 1 233 ? 17.883 28.562  2.110   1.00 38.53  ? 212 GLY B C     1 
ATOM   4895 O  O     . GLY B 1 233 ? 19.087 28.355  2.319   1.00 35.82  ? 212 GLY B O     1 
ATOM   4896 N  N     . GLY B 1 234 ? 17.090 27.705  1.458   1.00 38.39  ? 213 GLY B N     1 
ATOM   4897 C  CA    . GLY B 1 234 ? 17.580 26.430  0.896   1.00 38.89  ? 213 GLY B CA    1 
ATOM   4898 C  C     . GLY B 1 234 ? 17.493 25.278  1.881   1.00 36.58  ? 213 GLY B C     1 
ATOM   4899 O  O     . GLY B 1 234 ? 17.009 25.471  2.999   1.00 37.91  ? 213 GLY B O     1 
ATOM   4900 N  N     . VAL B 1 235 ? 17.945 24.095  1.467   1.00 40.27  ? 214 VAL B N     1 
ATOM   4901 C  CA    . VAL B 1 235 ? 17.698 22.798  2.173   1.00 39.05  ? 214 VAL B CA    1 
ATOM   4902 C  C     . VAL B 1 235 ? 18.843 22.477  3.143   1.00 37.47  ? 214 VAL B C     1 
ATOM   4903 O  O     . VAL B 1 235 ? 18.554 21.950  4.225   1.00 37.96  ? 214 VAL B O     1 
ATOM   4904 C  CB    . VAL B 1 235 ? 17.475 21.664  1.165   1.00 39.04  ? 214 VAL B CB    1 
ATOM   4905 C  CG1   . VAL B 1 235 ? 17.291 20.322  1.868   1.00 38.81  ? 214 VAL B CG1   1 
ATOM   4906 C  CG2   . VAL B 1 235 ? 16.300 21.972  0.248   1.00 39.53  ? 214 VAL B CG2   1 
ATOM   4907 N  N     . GLN B 1 236 ? 20.099 22.772  2.815   1.00 41.92  ? 215 GLN B N     1 
ATOM   4908 C  CA    . GLN B 1 236 ? 21.206 22.411  3.740   1.00 45.11  ? 215 GLN B CA    1 
ATOM   4909 C  C     . GLN B 1 236 ? 20.968 23.072  5.097   1.00 48.46  ? 215 GLN B C     1 
ATOM   4910 O  O     . GLN B 1 236 ? 21.290 22.469  6.116   1.00 45.61  ? 215 GLN B O     1 
ATOM   4911 C  CB    . GLN B 1 236 ? 22.604 22.776  3.241   1.00 47.31  ? 215 GLN B CB    1 
ATOM   4912 C  CG    . GLN B 1 236 ? 23.695 22.404  4.247   1.00 44.50  ? 215 GLN B CG    1 
ATOM   4913 C  CD    . GLN B 1 236 ? 25.098 22.685  3.778   1.00 44.58  ? 215 GLN B CD    1 
ATOM   4914 O  OE1   . GLN B 1 236 ? 25.371 22.899  2.591   1.00 43.07  ? 215 GLN B OE1   1 
ATOM   4915 N  NE2   . GLN B 1 236 ? 26.011 22.665  4.732   1.00 42.96  ? 215 GLN B NE2   1 
ATOM   4916 N  N     . PRO B 1 237 ? 20.507 24.348  5.172   1.00 47.12  ? 216 PRO B N     1 
ATOM   4917 C  CA    . PRO B 1 237 ? 20.134 24.947  6.458   1.00 44.78  ? 216 PRO B CA    1 
ATOM   4918 C  C     . PRO B 1 237 ? 19.085 24.151  7.251   1.00 41.82  ? 216 PRO B C     1 
ATOM   4919 O  O     . PRO B 1 237 ? 19.260 24.034  8.443   1.00 43.52  ? 216 PRO B O     1 
ATOM   4920 C  CB    . PRO B 1 237 ? 19.674 26.349  6.052   1.00 45.01  ? 216 PRO B CB    1 
ATOM   4921 C  CG    . PRO B 1 237 ? 20.588 26.642  4.881   1.00 45.30  ? 216 PRO B CG    1 
ATOM   4922 C  CD    . PRO B 1 237 ? 20.525 25.346  4.092   1.00 45.22  ? 216 PRO B CD    1 
ATOM   4923 N  N     . LEU B 1 238 ? 18.085 23.565  6.594   1.00 39.99  ? 217 LEU B N     1 
ATOM   4924 C  CA    . LEU B 1 238 ? 17.116 22.666  7.275   1.00 40.66  ? 217 LEU B CA    1 
ATOM   4925 C  C     . LEU B 1 238 ? 17.891 21.523  7.945   1.00 43.96  ? 217 LEU B C     1 
ATOM   4926 O  O     . LEU B 1 238 ? 17.599 21.242  9.110   1.00 45.95  ? 217 LEU B O     1 
ATOM   4927 C  CB    . LEU B 1 238 ? 16.064 22.138  6.293   1.00 38.18  ? 217 LEU B CB    1 
ATOM   4928 C  CG    . LEU B 1 238 ? 15.049 21.143  6.867   1.00 40.58  ? 217 LEU B CG    1 
ATOM   4929 C  CD1   . LEU B 1 238 ? 14.407 21.652  8.155   1.00 44.99  ? 217 LEU B CD1   1 
ATOM   4930 C  CD2   . LEU B 1 238 ? 13.955 20.819  5.856   1.00 39.75  ? 217 LEU B CD2   1 
ATOM   4931 N  N     . ALA B 1 239 ? 18.848 20.896  7.252   1.00 42.64  ? 218 ALA B N     1 
ATOM   4932 C  CA    . ALA B 1 239 ? 19.648 19.768  7.789   1.00 40.56  ? 218 ALA B CA    1 
ATOM   4933 C  C     . ALA B 1 239 ? 20.463 20.257  8.988   1.00 40.10  ? 218 ALA B C     1 
ATOM   4934 O  O     . ALA B 1 239 ? 20.611 19.485  9.967   1.00 37.66  ? 218 ALA B O     1 
ATOM   4935 C  CB    . ALA B 1 239 ? 20.560 19.198  6.727   1.00 41.18  ? 218 ALA B CB    1 
ATOM   4936 N  N     . GLU B 1 240 ? 21.021 21.470  8.898   1.00 39.45  ? 219 GLU B N     1 
ATOM   4937 C  CA    . GLU B 1 240 ? 21.921 22.008  9.950   1.00 43.58  ? 219 GLU B CA    1 
ATOM   4938 C  C     . GLU B 1 240 ? 21.097 22.256  11.226  1.00 44.02  ? 219 GLU B C     1 
ATOM   4939 O  O     . GLU B 1 240 ? 21.665 22.156  12.320  1.00 42.16  ? 219 GLU B O     1 
ATOM   4940 C  CB    . GLU B 1 240 ? 22.652 23.257  9.465   1.00 47.97  ? 219 GLU B CB    1 
ATOM   4941 C  CG    . GLU B 1 240 ? 23.788 22.980  8.500   1.00 50.49  ? 219 GLU B CG    1 
ATOM   4942 C  CD    . GLU B 1 240 ? 24.422 24.224  7.880   1.00 58.53  ? 219 GLU B CD    1 
ATOM   4943 O  OE1   . GLU B 1 240 ? 23.674 25.103  7.412   1.00 59.19  ? 219 GLU B OE1   1 
ATOM   4944 O  OE2   . GLU B 1 240 ? 25.667 24.309  7.852   1.00 64.32  ? 219 GLU B OE2   1 
ATOM   4945 N  N     . ARG B 1 241 ? 19.793 22.511  11.093  1.00 47.87  ? 220 ARG B N     1 
ATOM   4946 C  CA    . ARG B 1 241 ? 18.873 22.732  12.244  1.00 50.79  ? 220 ARG B CA    1 
ATOM   4947 C  C     . ARG B 1 241 ? 18.520 21.387  12.882  1.00 45.59  ? 220 ARG B C     1 
ATOM   4948 O  O     . ARG B 1 241 ? 18.445 21.321  14.117  1.00 50.40  ? 220 ARG B O     1 
ATOM   4949 C  CB    . ARG B 1 241 ? 17.620 23.511  11.820  1.00 49.70  ? 220 ARG B CB    1 
ATOM   4950 C  CG    . ARG B 1 241 ? 17.765 25.023  11.934  1.00 49.87  ? 220 ARG B CG    1 
ATOM   4951 C  CD    . ARG B 1 241 ? 16.515 25.759  11.478  1.00 50.58  ? 220 ARG B CD    1 
ATOM   4952 N  NE    . ARG B 1 241 ? 16.840 27.127  11.088  1.00 55.17  ? 220 ARG B NE    1 
ATOM   4953 C  CZ    . ARG B 1 241 ? 15.974 28.136  10.981  1.00 55.42  ? 220 ARG B CZ    1 
ATOM   4954 N  NH1   . ARG B 1 241 ? 14.691 27.955  11.242  1.00 54.86  ? 220 ARG B NH1   1 
ATOM   4955 N  NH2   . ARG B 1 241 ? 16.406 29.331  10.610  1.00 54.33  ? 220 ARG B NH2   1 
ATOM   4956 N  N     . LEU B 1 242 ? 18.297 20.356  12.074  1.00 49.11  ? 221 LEU B N     1 
ATOM   4957 C  CA    . LEU B 1 242 ? 18.052 18.969  12.556  1.00 50.50  ? 221 LEU B CA    1 
ATOM   4958 C  C     . LEU B 1 242 ? 19.271 18.472  13.365  1.00 51.67  ? 221 LEU B C     1 
ATOM   4959 O  O     . LEU B 1 242 ? 19.067 17.710  14.314  1.00 56.80  ? 221 LEU B O     1 
ATOM   4960 C  CB    . LEU B 1 242 ? 17.753 18.092  11.335  1.00 49.20  ? 221 LEU B CB    1 
ATOM   4961 C  CG    . LEU B 1 242 ? 17.475 16.615  11.609  1.00 52.60  ? 221 LEU B CG    1 
ATOM   4962 C  CD1   . LEU B 1 242 ? 16.515 16.430  12.772  1.00 55.80  ? 221 LEU B CD1   1 
ATOM   4963 C  CD2   . LEU B 1 242 ? 16.923 15.922  10.368  1.00 53.17  ? 221 LEU B CD2   1 
ATOM   4964 N  N     . ALA B 1 243 ? 20.487 18.919  13.021  1.00 56.01  ? 222 ALA B N     1 
ATOM   4965 C  CA    . ALA B 1 243 ? 21.786 18.498  13.611  1.00 57.36  ? 222 ALA B CA    1 
ATOM   4966 C  C     . ALA B 1 243 ? 21.979 19.153  14.986  1.00 57.34  ? 222 ALA B C     1 
ATOM   4967 O  O     . ALA B 1 243 ? 22.521 18.477  15.895  1.00 50.87  ? 222 ALA B O     1 
ATOM   4968 C  CB    . ALA B 1 243 ? 22.928 18.864  12.680  1.00 50.40  ? 222 ALA B CB    1 
ATOM   4969 N  N     . ALA B 1 244 ? 21.568 20.423  15.100  1.00 52.80  ? 223 ALA B N     1 
ATOM   4970 C  CA    . ALA B 1 244 ? 21.562 21.246  16.331  1.00 53.68  ? 223 ALA B CA    1 
ATOM   4971 C  C     . ALA B 1 244 ? 20.757 20.560  17.451  1.00 52.22  ? 223 ALA B C     1 
ATOM   4972 O  O     . ALA B 1 244 ? 21.111 20.773  18.616  1.00 71.07  ? 223 ALA B O     1 
ATOM   4973 C  CB    . ALA B 1 244 ? 21.022 22.624  16.016  1.00 50.88  ? 223 ALA B CB    1 
ATOM   4974 N  N     . ARG B 1 245 ? 19.733 19.767  17.122  1.00 50.83  ? 224 ARG B N     1 
ATOM   4975 C  CA    . ARG B 1 245 ? 18.914 18.958  18.074  1.00 55.84  ? 224 ARG B CA    1 
ATOM   4976 C  C     . ARG B 1 245 ? 19.698 17.764  18.650  1.00 62.36  ? 224 ARG B C     1 
ATOM   4977 O  O     . ARG B 1 245 ? 19.204 17.144  19.613  1.00 62.22  ? 224 ARG B O     1 
ATOM   4978 C  CB    . ARG B 1 245 ? 17.657 18.409  17.382  1.00 54.71  ? 224 ARG B CB    1 
ATOM   4979 C  CG    . ARG B 1 245 ? 16.662 19.473  16.936  1.00 58.46  ? 224 ARG B CG    1 
ATOM   4980 C  CD    . ARG B 1 245 ? 16.616 20.682  17.861  1.00 57.65  ? 224 ARG B CD    1 
ATOM   4981 N  NE    . ARG B 1 245 ? 15.584 21.629  17.474  1.00 61.42  ? 224 ARG B NE    1 
ATOM   4982 C  CZ    . ARG B 1 245 ? 14.279 21.503  17.717  1.00 59.39  ? 224 ARG B CZ    1 
ATOM   4983 N  NH1   . ARG B 1 245 ? 13.804 20.450  18.361  1.00 59.10  ? 224 ARG B NH1   1 
ATOM   4984 N  NH2   . ARG B 1 245 ? 13.448 22.448  17.311  1.00 58.24  ? 224 ARG B NH2   1 
ATOM   4985 N  N     . LEU B 1 246 ? 20.840 17.401  18.062  1.00 62.74  ? 225 LEU B N     1 
ATOM   4986 C  CA    . LEU B 1 246 ? 21.709 16.325  18.600  1.00 58.09  ? 225 LEU B CA    1 
ATOM   4987 C  C     . LEU B 1 246 ? 22.552 16.918  19.719  1.00 49.99  ? 225 LEU B C     1 
ATOM   4988 O  O     . LEU B 1 246 ? 22.937 18.078  19.676  1.00 46.03  ? 225 LEU B O     1 
ATOM   4989 C  CB    . LEU B 1 246 ? 22.588 15.732  17.491  1.00 60.83  ? 225 LEU B CB    1 
ATOM   4990 C  CG    . LEU B 1 246 ? 21.867 14.852  16.469  1.00 62.11  ? 225 LEU B CG    1 
ATOM   4991 C  CD1   . LEU B 1 246 ? 22.870 14.176  15.554  1.00 68.93  ? 225 LEU B CD1   1 
ATOM   4992 C  CD2   . LEU B 1 246 ? 21.000 13.798  17.145  1.00 61.27  ? 225 LEU B CD2   1 
ATOM   4993 N  N     . PRO B 1 247 ? 22.858 16.137  20.766  1.00 45.51  ? 226 PRO B N     1 
ATOM   4994 C  CA    . PRO B 1 247 ? 23.692 16.626  21.856  1.00 47.32  ? 226 PRO B CA    1 
ATOM   4995 C  C     . PRO B 1 247 ? 25.091 17.010  21.368  1.00 51.83  ? 226 PRO B C     1 
ATOM   4996 O  O     . PRO B 1 247 ? 25.493 16.570  20.296  1.00 52.62  ? 226 PRO B O     1 
ATOM   4997 C  CB    . PRO B 1 247 ? 23.765 15.447  22.832  1.00 48.79  ? 226 PRO B CB    1 
ATOM   4998 C  CG    . PRO B 1 247 ? 23.340 14.231  22.026  1.00 48.71  ? 226 PRO B CG    1 
ATOM   4999 C  CD    . PRO B 1 247 ? 22.398 14.762  20.968  1.00 49.08  ? 226 PRO B CD    1 
ATOM   5000 N  N     . ASP B 1 248 ? 25.785 17.831  22.155  1.00 57.42  ? 227 ASP B N     1 
ATOM   5001 C  CA    . ASP B 1 248 ? 27.172 18.275  21.857  1.00 63.89  ? 227 ASP B CA    1 
ATOM   5002 C  C     . ASP B 1 248 ? 28.068 17.025  21.876  1.00 61.48  ? 227 ASP B C     1 
ATOM   5003 O  O     . ASP B 1 248 ? 27.854 16.158  22.749  1.00 59.30  ? 227 ASP B O     1 
ATOM   5004 C  CB    . ASP B 1 248 ? 27.592 19.396  22.812  1.00 65.82  ? 227 ASP B CB    1 
ATOM   5005 C  CG    . ASP B 1 248 ? 26.893 20.721  22.529  1.00 70.05  ? 227 ASP B CG    1 
ATOM   5006 O  OD1   . ASP B 1 248 ? 27.392 21.468  21.663  1.00 79.63  ? 227 ASP B OD1   1 
ATOM   5007 O  OD2   . ASP B 1 248 ? 25.845 20.994  23.160  1.00 67.58  ? 227 ASP B OD2   1 
ATOM   5008 N  N     . GLY B 1 249 ? 28.960 16.896  20.888  1.00 61.00  ? 228 GLY B N     1 
ATOM   5009 C  CA    . GLY B 1 249 ? 29.918 15.780  20.766  1.00 57.18  ? 228 GLY B CA    1 
ATOM   5010 C  C     . GLY B 1 249 ? 29.363 14.571  20.020  1.00 54.47  ? 228 GLY B C     1 
ATOM   5011 O  O     . GLY B 1 249 ? 30.152 13.636  19.807  1.00 56.96  ? 228 GLY B O     1 
ATOM   5012 N  N     . ALA B 1 250 ? 28.081 14.575  19.624  1.00 49.65  ? 229 ALA B N     1 
ATOM   5013 C  CA    . ALA B 1 250 ? 27.416 13.467  18.889  1.00 54.20  ? 229 ALA B CA    1 
ATOM   5014 C  C     . ALA B 1 250 ? 27.867 13.443  17.416  1.00 52.28  ? 229 ALA B C     1 
ATOM   5015 O  O     . ALA B 1 250 ? 28.178 12.355  16.903  1.00 50.56  ? 229 ALA B O     1 
ATOM   5016 C  CB    . ALA B 1 250 ? 25.916 13.591  18.990  1.00 54.93  ? 229 ALA B CB    1 
ATOM   5017 N  N     . LEU B 1 251 ? 27.904 14.611  16.776  1.00 49.81  ? 230 LEU B N     1 
ATOM   5018 C  CA    . LEU B 1 251 ? 28.233 14.805  15.343  1.00 46.04  ? 230 LEU B CA    1 
ATOM   5019 C  C     . LEU B 1 251 ? 29.751 14.964  15.200  1.00 46.99  ? 230 LEU B C     1 
ATOM   5020 O  O     . LEU B 1 251 ? 30.340 15.844  15.850  1.00 42.36  ? 230 LEU B O     1 
ATOM   5021 C  CB    . LEU B 1 251 ? 27.472 16.030  14.824  1.00 45.40  ? 230 LEU B CB    1 
ATOM   5022 C  CG    . LEU B 1 251 ? 27.725 16.438  13.369  1.00 46.06  ? 230 LEU B CG    1 
ATOM   5023 C  CD1   . LEU B 1 251 ? 27.320 15.328  12.402  1.00 46.84  ? 230 LEU B CD1   1 
ATOM   5024 C  CD2   . LEU B 1 251 ? 26.969 17.722  13.052  1.00 46.77  ? 230 LEU B CD2   1 
ATOM   5025 N  N     . ARG B 1 252 ? 30.359 14.094  14.390  1.00 52.93  ? 231 ARG B N     1 
ATOM   5026 C  CA    . ARG B 1 252 ? 31.804 14.095  14.063  1.00 51.59  ? 231 ARG B CA    1 
ATOM   5027 C  C     . ARG B 1 252 ? 31.956 14.284  12.554  1.00 47.11  ? 231 ARG B C     1 
ATOM   5028 O  O     . ARG B 1 252 ? 31.793 13.296  11.825  1.00 50.81  ? 231 ARG B O     1 
ATOM   5029 C  CB    . ARG B 1 252 ? 32.421 12.783  14.542  1.00 55.03  ? 231 ARG B CB    1 
ATOM   5030 C  CG    . ARG B 1 252 ? 32.324 12.574  16.045  1.00 61.82  ? 231 ARG B CG    1 
ATOM   5031 C  CD    . ARG B 1 252 ? 33.534 13.112  16.778  1.00 67.82  ? 231 ARG B CD    1 
ATOM   5032 N  NE    . ARG B 1 252 ? 33.658 12.428  18.051  1.00 73.23  ? 231 ARG B NE    1 
ATOM   5033 C  CZ    . ARG B 1 252 ? 34.054 11.166  18.198  1.00 78.45  ? 231 ARG B CZ    1 
ATOM   5034 N  NH1   . ARG B 1 252 ? 34.378 10.429  17.141  1.00 79.18  ? 231 ARG B NH1   1 
ATOM   5035 N  NH2   . ARG B 1 252 ? 34.114 10.644  19.412  1.00 76.34  ? 231 ARG B NH2   1 
ATOM   5036 N  N     . LEU B 1 253 ? 32.225 15.514  12.123  1.00 40.09  ? 232 LEU B N     1 
ATOM   5037 C  CA    . LEU B 1 253 ? 32.494 15.870  10.712  1.00 42.34  ? 232 LEU B CA    1 
ATOM   5038 C  C     . LEU B 1 253 ? 33.904 15.391  10.344  1.00 45.49  ? 232 LEU B C     1 
ATOM   5039 O  O     . LEU B 1 253 ? 34.615 14.899  11.240  1.00 43.07  ? 232 LEU B O     1 
ATOM   5040 C  CB    . LEU B 1 253 ? 32.349 17.392  10.547  1.00 43.81  ? 232 LEU B CB    1 
ATOM   5041 C  CG    . LEU B 1 253 ? 30.952 17.955  10.817  1.00 40.95  ? 232 LEU B CG    1 
ATOM   5042 C  CD1   . LEU B 1 253 ? 30.860 19.443  10.462  1.00 41.08  ? 232 LEU B CD1   1 
ATOM   5043 C  CD2   . LEU B 1 253 ? 29.917 17.172  10.036  1.00 37.80  ? 232 LEU B CD2   1 
ATOM   5044 N  N     . SER B 1 254 ? 34.273 15.515  9.067   1.00 43.27  ? 233 SER B N     1 
ATOM   5045 C  CA    . SER B 1 254 ? 35.603 15.187  8.494   1.00 43.87  ? 233 SER B CA    1 
ATOM   5046 C  C     . SER B 1 254 ? 36.134 13.846  9.022   1.00 41.84  ? 233 SER B C     1 
ATOM   5047 O  O     . SER B 1 254 ? 37.341 13.733  9.200   1.00 42.22  ? 233 SER B O     1 
ATOM   5048 C  CB    . SER B 1 254 ? 36.539 16.326  8.748   1.00 47.38  ? 233 SER B CB    1 
ATOM   5049 O  OG    . SER B 1 254 ? 35.988 17.504  8.166   1.00 53.79  ? 233 SER B OG    1 
ATOM   5050 N  N     . THR B 1 255 ? 35.255 12.856  9.180   1.00 41.48  ? 234 THR B N     1 
ATOM   5051 C  CA    . THR B 1 255 ? 35.512 11.547  9.829   1.00 45.16  ? 234 THR B CA    1 
ATOM   5052 C  C     . THR B 1 255 ? 34.945 10.431  8.955   1.00 41.17  ? 234 THR B C     1 
ATOM   5053 O  O     . THR B 1 255 ? 33.918 9.835   9.270   1.00 41.72  ? 234 THR B O     1 
ATOM   5054 C  CB    . THR B 1 255 ? 34.906 11.558  11.236  1.00 48.12  ? 234 THR B CB    1 
ATOM   5055 O  OG1   . THR B 1 255 ? 35.431 12.742  11.828  1.00 52.45  ? 234 THR B OG1   1 
ATOM   5056 C  CG2   . THR B 1 255 ? 35.270 10.357  12.079  1.00 51.99  ? 234 THR B CG2   1 
ATOM   5057 N  N     . PRO B 1 256 ? 35.573 10.139  7.798   1.00 38.42  ? 235 PRO B N     1 
ATOM   5058 C  CA    . PRO B 1 256 ? 35.155 8.999   6.983   1.00 37.93  ? 235 PRO B CA    1 
ATOM   5059 C  C     . PRO B 1 256 ? 35.215 7.684   7.783   1.00 38.32  ? 235 PRO B C     1 
ATOM   5060 O  O     . PRO B 1 256 ? 36.165 7.500   8.535   1.00 39.46  ? 235 PRO B O     1 
ATOM   5061 C  CB    . PRO B 1 256 ? 36.178 8.978   5.825   1.00 38.58  ? 235 PRO B CB    1 
ATOM   5062 C  CG    . PRO B 1 256 ? 36.789 10.391  5.806   1.00 37.72  ? 235 PRO B CG    1 
ATOM   5063 C  CD    . PRO B 1 256 ? 36.729 10.867  7.241   1.00 37.25  ? 235 PRO B CD    1 
ATOM   5064 N  N     . VAL B 1 257 ? 34.221 6.807   7.611   1.00 34.78  ? 236 VAL B N     1 
ATOM   5065 C  CA    . VAL B 1 257 ? 34.272 5.406   8.132   1.00 37.38  ? 236 VAL B CA    1 
ATOM   5066 C  C     . VAL B 1 257 ? 34.925 4.517   7.067   1.00 36.35  ? 236 VAL B C     1 
ATOM   5067 O  O     . VAL B 1 257 ? 34.418 4.457   5.951   1.00 37.20  ? 236 VAL B O     1 
ATOM   5068 C  CB    . VAL B 1 257 ? 32.884 4.879   8.538   1.00 34.11  ? 236 VAL B CB    1 
ATOM   5069 C  CG1   . VAL B 1 257 ? 32.867 3.366   8.719   1.00 35.68  ? 236 VAL B CG1   1 
ATOM   5070 C  CG2   . VAL B 1 257 ? 32.388 5.569   9.794   1.00 34.78  ? 236 VAL B CG2   1 
ATOM   5071 N  N     . ARG B 1 258 ? 35.995 3.818   7.419   1.00 39.01  ? 237 ARG B N     1 
ATOM   5072 C  CA    . ARG B 1 258 ? 36.736 2.945   6.471   1.00 45.13  ? 237 ARG B CA    1 
ATOM   5073 C  C     . ARG B 1 258 ? 36.414 1.477   6.737   1.00 39.73  ? 237 ARG B C     1 
ATOM   5074 O  O     . ARG B 1 258 ? 36.481 0.668   5.800   1.00 37.32  ? 237 ARG B O     1 
ATOM   5075 C  CB    . ARG B 1 258 ? 38.227 3.263   6.562   1.00 50.36  ? 237 ARG B CB    1 
ATOM   5076 C  CG    . ARG B 1 258 ? 38.593 4.422   5.647   1.00 57.55  ? 237 ARG B CG    1 
ATOM   5077 C  CD    . ARG B 1 258 ? 39.846 5.152   6.076   1.00 70.61  ? 237 ARG B CD    1 
ATOM   5078 N  NE    . ARG B 1 258 ? 39.709 6.575   5.789   1.00 78.62  ? 237 ARG B NE    1 
ATOM   5079 C  CZ    . ARG B 1 258 ? 40.714 7.436   5.700   1.00 77.19  ? 237 ARG B CZ    1 
ATOM   5080 N  NH1   . ARG B 1 258 ? 41.963 7.011   5.835   1.00 69.75  ? 237 ARG B NH1   1 
ATOM   5081 N  NH2   . ARG B 1 258 ? 40.455 8.714   5.460   1.00 72.96  ? 237 ARG B NH2   1 
ATOM   5082 N  N     . GLY B 1 259 ? 36.033 1.164   7.966   1.00 39.45  ? 238 GLY B N     1 
ATOM   5083 C  CA    . GLY B 1 259 ? 35.986 -0.218  8.461   1.00 35.84  ? 238 GLY B CA    1 
ATOM   5084 C  C     . GLY B 1 259 ? 34.829 -0.392  9.398   1.00 34.16  ? 238 GLY B C     1 
ATOM   5085 O  O     . GLY B 1 259 ? 34.504 0.563   10.110  1.00 32.99  ? 238 GLY B O     1 
ATOM   5086 N  N     . LEU B 1 260 ? 34.209 -1.562  9.349   1.00 34.64  ? 239 LEU B N     1 
ATOM   5087 C  CA    . LEU B 1 260 ? 33.046 -1.905  10.185  1.00 35.58  ? 239 LEU B CA    1 
ATOM   5088 C  C     . LEU B 1 260 ? 33.153 -3.398  10.495  1.00 35.99  ? 239 LEU B C     1 
ATOM   5089 O  O     . LEU B 1 260 ? 32.881 -4.227  9.609   1.00 33.42  ? 239 LEU B O     1 
ATOM   5090 C  CB    . LEU B 1 260 ? 31.772 -1.493  9.436   1.00 34.73  ? 239 LEU B CB    1 
ATOM   5091 C  CG    . LEU B 1 260 ? 30.492 -1.440  10.261  1.00 40.53  ? 239 LEU B CG    1 
ATOM   5092 C  CD1   . LEU B 1 260 ? 30.683 -0.634  11.539  1.00 39.83  ? 239 LEU B CD1   1 
ATOM   5093 C  CD2   . LEU B 1 260 ? 29.356 -0.846  9.439   1.00 40.37  ? 239 LEU B CD2   1 
ATOM   5094 N  N     . ALA B 1 261 ? 33.624 -3.705  11.705  1.00 39.65  ? 240 ALA B N     1 
ATOM   5095 C  CA    . ALA B 1 261 ? 33.770 -5.071  12.258  1.00 40.55  ? 240 ALA B CA    1 
ATOM   5096 C  C     . ALA B 1 261 ? 32.618 -5.315  13.230  1.00 43.74  ? 240 ALA B C     1 
ATOM   5097 O  O     . ALA B 1 261 ? 32.049 -4.336  13.758  1.00 49.61  ? 240 ALA B O     1 
ATOM   5098 C  CB    . ALA B 1 261 ? 35.114 -5.211  12.937  1.00 37.12  ? 240 ALA B CB    1 
ATOM   5099 N  N     . GLN B 1 262 ? 32.277 -6.570  13.458  1.00 40.96  ? 241 GLN B N     1 
ATOM   5100 C  CA    . GLN B 1 262 ? 31.229 -6.914  14.439  1.00 42.67  ? 241 GLN B CA    1 
ATOM   5101 C  C     . GLN B 1 262 ? 31.504 -8.327  14.968  1.00 44.98  ? 241 GLN B C     1 
ATOM   5102 O  O     . GLN B 1 262 ? 32.186 -9.093  14.282  1.00 47.42  ? 241 GLN B O     1 
ATOM   5103 C  CB    . GLN B 1 262 ? 29.854 -6.717  13.797  1.00 38.61  ? 241 GLN B CB    1 
ATOM   5104 C  CG    . GLN B 1 262 ? 29.475 -7.822  12.825  1.00 37.52  ? 241 GLN B CG    1 
ATOM   5105 C  CD    . GLN B 1 262 ? 28.064 -7.734  12.306  1.00 36.29  ? 241 GLN B CD    1 
ATOM   5106 O  OE1   . GLN B 1 262 ? 27.818 -7.592  11.105  1.00 38.22  ? 241 GLN B OE1   1 
ATOM   5107 N  NE2   . GLN B 1 262 ? 27.117 -7.881  13.209  1.00 37.18  ? 241 GLN B NE2   1 
ATOM   5108 N  N     . ASP B 1 263 ? 31.046 -8.600  16.189  1.00 51.62  ? 242 ASP B N     1 
ATOM   5109 C  CA    . ASP B 1 263 ? 31.147 -9.900  16.908  1.00 57.30  ? 242 ASP B CA    1 
ATOM   5110 C  C     . ASP B 1 263 ? 29.841 -10.084 17.707  1.00 58.39  ? 242 ASP B C     1 
ATOM   5111 O  O     . ASP B 1 263 ? 28.862 -9.357  17.407  1.00 58.29  ? 242 ASP B O     1 
ATOM   5112 C  CB    . ASP B 1 263 ? 32.458 -9.967  17.707  1.00 62.40  ? 242 ASP B CB    1 
ATOM   5113 C  CG    . ASP B 1 263 ? 32.655 -8.916  18.800  1.00 61.92  ? 242 ASP B CG    1 
ATOM   5114 O  OD1   . ASP B 1 263 ? 31.677 -8.214  19.144  1.00 54.80  ? 242 ASP B OD1   1 
ATOM   5115 O  OD2   . ASP B 1 263 ? 33.792 -8.824  19.322  1.00 56.79  ? 242 ASP B OD2   1 
ATOM   5116 N  N     . GLY B 1 264 ? 29.790 -10.993 18.686  1.00 55.00  ? 243 GLY B N     1 
ATOM   5117 C  CA    . GLY B 1 264 ? 28.543 -11.288 19.425  1.00 55.65  ? 243 GLY B CA    1 
ATOM   5118 C  C     . GLY B 1 264 ? 28.205 -10.239 20.481  1.00 53.65  ? 243 GLY B C     1 
ATOM   5119 O  O     . GLY B 1 264 ? 27.185 -10.424 21.157  1.00 62.26  ? 243 GLY B O     1 
ATOM   5120 N  N     . ASP B 1 265 ? 29.022 -9.189  20.614  1.00 49.99  ? 244 ASP B N     1 
ATOM   5121 C  CA    . ASP B 1 265 ? 29.004 -8.191  21.716  1.00 53.35  ? 244 ASP B CA    1 
ATOM   5122 C  C     . ASP B 1 265 ? 28.838 -6.744  21.215  1.00 54.70  ? 244 ASP B C     1 
ATOM   5123 O  O     . ASP B 1 265 ? 28.633 -5.857  22.062  1.00 52.50  ? 244 ASP B O     1 
ATOM   5124 C  CB    . ASP B 1 265 ? 30.345 -8.200  22.457  1.00 55.21  ? 244 ASP B CB    1 
ATOM   5125 C  CG    . ASP B 1 265 ? 30.639 -9.481  23.210  1.00 60.47  ? 244 ASP B CG    1 
ATOM   5126 O  OD1   . ASP B 1 265 ? 29.702 -10.291 23.367  1.00 63.49  ? 244 ASP B OD1   1 
ATOM   5127 O  OD2   . ASP B 1 265 ? 31.798 -9.639  23.661  1.00 64.79  ? 244 ASP B OD2   1 
ATOM   5128 N  N     . GLY B 1 266 ? 29.038 -6.479  19.922  1.00 49.32  ? 245 GLY B N     1 
ATOM   5129 C  CA    . GLY B 1 266 ? 29.044 -5.105  19.388  1.00 50.15  ? 245 GLY B CA    1 
ATOM   5130 C  C     . GLY B 1 266 ? 29.743 -4.959  18.040  1.00 47.37  ? 245 GLY B C     1 
ATOM   5131 O  O     . GLY B 1 266 ? 29.898 -5.962  17.293  1.00 42.00  ? 245 GLY B O     1 
ATOM   5132 N  N     . VAL B 1 267 ? 30.098 -3.722  17.714  1.00 37.90  ? 246 VAL B N     1 
ATOM   5133 C  CA    . VAL B 1 267 ? 30.693 -3.358  16.408  1.00 40.17  ? 246 VAL B CA    1 
ATOM   5134 C  C     . VAL B 1 267 ? 31.803 -2.373  16.727  1.00 39.62  ? 246 VAL B C     1 
ATOM   5135 O  O     . VAL B 1 267 ? 31.670 -1.657  17.713  1.00 39.25  ? 246 VAL B O     1 
ATOM   5136 C  CB    . VAL B 1 267 ? 29.661 -2.785  15.410  1.00 42.58  ? 246 VAL B CB    1 
ATOM   5137 C  CG1   . VAL B 1 267 ? 28.353 -3.552  15.420  1.00 42.56  ? 246 VAL B CG1   1 
ATOM   5138 C  CG2   . VAL B 1 267 ? 29.391 -1.308  15.623  1.00 42.91  ? 246 VAL B CG2   1 
ATOM   5139 N  N     . THR B 1 268 ? 32.884 -2.431  15.972  1.00 39.23  ? 247 THR B N     1 
ATOM   5140 C  CA    . THR B 1 268 ? 34.018 -1.493  16.052  1.00 41.84  ? 247 THR B CA    1 
ATOM   5141 C  C     . THR B 1 268 ? 34.049 -0.767  14.721  1.00 43.87  ? 247 THR B C     1 
ATOM   5142 O  O     . THR B 1 268 ? 33.959 -1.437  13.695  1.00 42.85  ? 247 THR B O     1 
ATOM   5143 C  CB    . THR B 1 268 ? 35.351 -2.203  16.304  1.00 44.17  ? 247 THR B CB    1 
ATOM   5144 O  OG1   . THR B 1 268 ? 35.226 -3.097  17.408  1.00 47.23  ? 247 THR B OG1   1 
ATOM   5145 C  CG2   . THR B 1 268 ? 36.461 -1.227  16.609  1.00 47.26  ? 247 THR B CG2   1 
ATOM   5146 N  N     . VAL B 1 269 ? 34.092 0.549   14.745  1.00 44.77  ? 248 VAL B N     1 
ATOM   5147 C  CA    . VAL B 1 269 ? 34.165 1.343   13.496  1.00 47.52  ? 248 VAL B CA    1 
ATOM   5148 C  C     . VAL B 1 269 ? 35.588 1.863   13.420  1.00 46.92  ? 248 VAL B C     1 
ATOM   5149 O  O     . VAL B 1 269 ? 36.033 2.430   14.424  1.00 51.61  ? 248 VAL B O     1 
ATOM   5150 C  CB    . VAL B 1 269 ? 33.115 2.465   13.475  1.00 49.29  ? 248 VAL B CB    1 
ATOM   5151 C  CG1   . VAL B 1 269 ? 33.036 3.126   12.115  1.00 51.83  ? 248 VAL B CG1   1 
ATOM   5152 C  CG2   . VAL B 1 269 ? 31.755 1.930   13.871  1.00 50.90  ? 248 VAL B CG2   1 
ATOM   5153 N  N     . ARG B 1 270 ? 36.275 1.617   12.304  1.00 43.39  ? 249 ARG B N     1 
ATOM   5154 C  CA    . ARG B 1 270 ? 37.649 2.109   12.060  1.00 45.91  ? 249 ARG B CA    1 
ATOM   5155 C  C     . ARG B 1 270 ? 37.524 3.379   11.218  1.00 44.17  ? 249 ARG B C     1 
ATOM   5156 O  O     . ARG B 1 270 ? 36.799 3.341   10.223  1.00 48.49  ? 249 ARG B O     1 
ATOM   5157 C  CB    . ARG B 1 270 ? 38.513 1.021   11.412  1.00 43.66  ? 249 ARG B CB    1 
ATOM   5158 C  CG    . ARG B 1 270 ? 39.935 1.461   11.092  1.00 46.80  ? 249 ARG B CG    1 
ATOM   5159 C  CD    . ARG B 1 270 ? 40.849 0.349   10.592  1.00 46.80  ? 249 ARG B CD    1 
ATOM   5160 N  NE    . ARG B 1 270 ? 40.211 -0.517  9.604   1.00 50.50  ? 249 ARG B NE    1 
ATOM   5161 C  CZ    . ARG B 1 270 ? 40.112 -0.275  8.292   1.00 53.38  ? 249 ARG B CZ    1 
ATOM   5162 N  NH1   . ARG B 1 270 ? 40.598 0.835   7.757   1.00 50.93  ? 249 ARG B NH1   1 
ATOM   5163 N  NH2   . ARG B 1 270 ? 39.512 -1.160  7.510   1.00 52.16  ? 249 ARG B NH2   1 
ATOM   5164 N  N     . THR B 1 271 ? 38.176 4.459   11.648  1.00 43.25  ? 250 THR B N     1 
ATOM   5165 C  CA    . THR B 1 271 ? 38.321 5.743   10.915  1.00 47.78  ? 250 THR B CA    1 
ATOM   5166 C  C     . THR B 1 271 ? 39.814 5.934   10.630  1.00 50.57  ? 250 THR B C     1 
ATOM   5167 O  O     . THR B 1 271 ? 40.557 4.969   10.874  1.00 55.30  ? 250 THR B O     1 
ATOM   5168 C  CB    . THR B 1 271 ? 37.677 6.879   11.723  1.00 45.81  ? 250 THR B CB    1 
ATOM   5169 O  OG1   . THR B 1 271 ? 38.429 6.997   12.927  1.00 48.85  ? 250 THR B OG1   1 
ATOM   5170 C  CG2   . THR B 1 271 ? 36.226 6.618   12.058  1.00 43.82  ? 250 THR B CG2   1 
ATOM   5171 N  N     . ALA B 1 272 ? 40.236 7.129   10.201  1.00 53.10  ? 251 ALA B N     1 
ATOM   5172 C  CA    . ALA B 1 272 ? 41.604 7.445   9.716   1.00 58.33  ? 251 ALA B CA    1 
ATOM   5173 C  C     . ALA B 1 272 ? 42.660 7.065   10.756  1.00 66.93  ? 251 ALA B C     1 
ATOM   5174 O  O     . ALA B 1 272 ? 43.772 6.687   10.360  1.00 81.42  ? 251 ALA B O     1 
ATOM   5175 C  CB    . ALA B 1 272 ? 41.721 8.907   9.364   1.00 60.38  ? 251 ALA B CB    1 
ATOM   5176 N  N     . GLY B 1 273 ? 42.348 7.197   12.041  1.00 74.22  ? 252 GLY B N     1 
ATOM   5177 C  CA    . GLY B 1 273 ? 43.267 6.784   13.118  1.00 74.43  ? 252 GLY B CA    1 
ATOM   5178 C  C     . GLY B 1 273 ? 42.572 6.723   14.461  1.00 71.26  ? 252 GLY B C     1 
ATOM   5179 O  O     . GLY B 1 273 ? 43.186 7.143   15.454  1.00 80.40  ? 252 GLY B O     1 
ATOM   5180 N  N     . GLY B 1 274 ? 41.342 6.207   14.481  1.00 68.50  ? 253 GLY B N     1 
ATOM   5181 C  CA    . GLY B 1 274 ? 40.576 5.909   15.702  1.00 63.51  ? 253 GLY B CA    1 
ATOM   5182 C  C     . GLY B 1 274 ? 39.724 4.674   15.508  1.00 64.74  ? 253 GLY B C     1 
ATOM   5183 O  O     . GLY B 1 274 ? 39.560 4.240   14.352  1.00 61.41  ? 253 GLY B O     1 
ATOM   5184 N  N     . GLU B 1 275 ? 39.246 4.105   16.613  1.00 64.40  ? 254 GLU B N     1 
ATOM   5185 C  CA    . GLU B 1 275 ? 38.131 3.128   16.660  1.00 61.70  ? 254 GLU B CA    1 
ATOM   5186 C  C     . GLU B 1 275 ? 37.028 3.721   17.543  1.00 55.42  ? 254 GLU B C     1 
ATOM   5187 O  O     . GLU B 1 275 ? 37.350 4.384   18.521  1.00 59.25  ? 254 GLU B O     1 
ATOM   5188 C  CB    . GLU B 1 275 ? 38.588 1.775   17.212  1.00 68.11  ? 254 GLU B CB    1 
ATOM   5189 C  CG    . GLU B 1 275 ? 39.389 0.930   16.233  1.00 76.52  ? 254 GLU B CG    1 
ATOM   5190 C  CD    . GLU B 1 275 ? 39.737 -0.470  16.733  1.00 81.21  ? 254 GLU B CD    1 
ATOM   5191 O  OE1   . GLU B 1 275 ? 39.318 -0.831  17.862  1.00 71.40  ? 254 GLU B OE1   1 
ATOM   5192 O  OE2   . GLU B 1 275 ? 40.431 -1.206  15.997  1.00 86.75  ? 254 GLU B OE2   1 
ATOM   5193 N  N     . VAL B 1 276 ? 35.775 3.518   17.166  1.00 50.30  ? 255 VAL B N     1 
ATOM   5194 C  CA    . VAL B 1 276 ? 34.573 3.774   18.000  1.00 44.65  ? 255 VAL B CA    1 
ATOM   5195 C  C     . VAL B 1 276 ? 33.959 2.411   18.254  1.00 43.61  ? 255 VAL B C     1 
ATOM   5196 O  O     . VAL B 1 276 ? 33.926 1.606   17.314  1.00 47.60  ? 255 VAL B O     1 
ATOM   5197 C  CB    . VAL B 1 276 ? 33.562 4.686   17.288  1.00 42.98  ? 255 VAL B CB    1 
ATOM   5198 C  CG1   . VAL B 1 276 ? 32.298 4.834   18.104  1.00 42.06  ? 255 VAL B CG1   1 
ATOM   5199 C  CG2   . VAL B 1 276 ? 34.152 6.044   16.938  1.00 39.59  ? 255 VAL B CG2   1 
ATOM   5200 N  N     . ARG B 1 277 ? 33.508 2.152   19.476  1.00 45.48  ? 256 ARG B N     1 
ATOM   5201 C  CA    . ARG B 1 277 ? 32.845 0.872   19.811  1.00 45.17  ? 256 ARG B CA    1 
ATOM   5202 C  C     . ARG B 1 277 ? 31.376 1.207   20.029  1.00 39.88  ? 256 ARG B C     1 
ATOM   5203 O  O     . ARG B 1 277 ? 31.109 2.260   20.589  1.00 47.92  ? 256 ARG B O     1 
ATOM   5204 C  CB    . ARG B 1 277 ? 33.551 0.202   20.992  1.00 49.48  ? 256 ARG B CB    1 
ATOM   5205 C  CG    . ARG B 1 277 ? 32.951 -1.139  21.396  1.00 62.38  ? 256 ARG B CG    1 
ATOM   5206 C  CD    . ARG B 1 277 ? 33.397 -2.308  20.530  1.00 69.22  ? 256 ARG B CD    1 
ATOM   5207 N  NE    . ARG B 1 277 ? 32.655 -3.545  20.779  1.00 68.56  ? 256 ARG B NE    1 
ATOM   5208 C  CZ    . ARG B 1 277 ? 32.822 -4.689  20.105  1.00 76.95  ? 256 ARG B CZ    1 
ATOM   5209 N  NH1   . ARG B 1 277 ? 33.700 -4.780  19.120  1.00 82.58  ? 256 ARG B NH1   1 
ATOM   5210 N  NH2   . ARG B 1 277 ? 32.101 -5.750  20.413  1.00 78.69  ? 256 ARG B NH2   1 
ATOM   5211 N  N     . ALA B 1 278 ? 30.468 0.390   19.510  1.00 40.06  ? 257 ALA B N     1 
ATOM   5212 C  CA    . ALA B 1 278 ? 29.009 0.544   19.699  1.00 39.12  ? 257 ALA B CA    1 
ATOM   5213 C  C     . ALA B 1 278 ? 28.353 -0.827  19.830  1.00 39.23  ? 257 ALA B C     1 
ATOM   5214 O  O     . ALA B 1 278 ? 28.995 -1.828  19.463  1.00 42.73  ? 257 ALA B O     1 
ATOM   5215 C  CB    . ALA B 1 278 ? 28.416 1.306   18.552  1.00 39.27  ? 257 ALA B CB    1 
ATOM   5216 N  N     . ARG B 1 279 ? 27.113 -0.857  20.318  1.00 39.59  ? 258 ARG B N     1 
ATOM   5217 C  CA    . ARG B 1 279 ? 26.315 -2.107  20.431  1.00 43.48  ? 258 ARG B CA    1 
ATOM   5218 C  C     . ARG B 1 279 ? 25.740 -2.447  19.050  1.00 44.11  ? 258 ARG B C     1 
ATOM   5219 O  O     . ARG B 1 279 ? 25.670 -3.664  18.744  1.00 42.85  ? 258 ARG B O     1 
ATOM   5220 C  CB    . ARG B 1 279 ? 25.262 -1.969  21.542  1.00 44.00  ? 258 ARG B CB    1 
ATOM   5221 C  CG    . ARG B 1 279 ? 25.879 -1.782  22.925  1.00 45.51  ? 258 ARG B CG    1 
ATOM   5222 C  CD    . ARG B 1 279 ? 24.952 -1.270  24.007  1.00 48.11  ? 258 ARG B CD    1 
ATOM   5223 N  NE    . ARG B 1 279 ? 23.916 -2.238  24.346  1.00 53.72  ? 258 ARG B NE    1 
ATOM   5224 C  CZ    . ARG B 1 279 ? 22.780 -1.954  24.992  1.00 58.82  ? 258 ARG B CZ    1 
ATOM   5225 N  NH1   . ARG B 1 279 ? 22.502 -0.717  25.381  1.00 54.77  ? 258 ARG B NH1   1 
ATOM   5226 N  NH2   . ARG B 1 279 ? 21.903 -2.916  25.222  1.00 60.98  ? 258 ARG B NH2   1 
ATOM   5227 N  N     . ARG B 1 280 ? 25.360 -1.419  18.268  1.00 39.52  ? 259 ARG B N     1 
ATOM   5228 C  CA    . ARG B 1 280 ? 24.715 -1.538  16.930  1.00 37.65  ? 259 ARG B CA    1 
ATOM   5229 C  C     . ARG B 1 280 ? 25.041 -0.340  16.044  1.00 39.59  ? 259 ARG B C     1 
ATOM   5230 O  O     . ARG B 1 280 ? 25.511 0.706   16.541  1.00 36.73  ? 259 ARG B O     1 
ATOM   5231 C  CB    . ARG B 1 280 ? 23.197 -1.692  17.039  1.00 40.14  ? 259 ARG B CB    1 
ATOM   5232 C  CG    . ARG B 1 280 ? 22.797 -2.967  17.766  1.00 42.86  ? 259 ARG B CG    1 
ATOM   5233 C  CD    . ARG B 1 280 ? 21.417 -3.501  17.488  1.00 46.66  ? 259 ARG B CD    1 
ATOM   5234 N  NE    . ARG B 1 280 ? 21.466 -4.878  17.951  1.00 52.48  ? 259 ARG B NE    1 
ATOM   5235 C  CZ    . ARG B 1 280 ? 21.326 -5.958  17.193  1.00 53.88  ? 259 ARG B CZ    1 
ATOM   5236 N  NH1   . ARG B 1 280 ? 21.033 -5.874  15.901  1.00 54.97  ? 259 ARG B NH1   1 
ATOM   5237 N  NH2   . ARG B 1 280 ? 21.452 -7.144  17.754  1.00 57.14  ? 259 ARG B NH2   1 
ATOM   5238 N  N     . ALA B 1 281 ? 24.795 -0.496  14.749  1.00 40.70  ? 260 ALA B N     1 
ATOM   5239 C  CA    . ALA B 1 281 ? 25.221 0.490   13.744  1.00 41.93  ? 260 ALA B CA    1 
ATOM   5240 C  C     . ALA B 1 281 ? 24.104 0.717   12.726  1.00 38.82  ? 260 ALA B C     1 
ATOM   5241 O  O     . ALA B 1 281 ? 23.348 -0.247  12.415  1.00 36.88  ? 260 ALA B O     1 
ATOM   5242 C  CB    . ALA B 1 281 ? 26.484 0.001   13.092  1.00 47.95  ? 260 ALA B CB    1 
ATOM   5243 N  N     . ILE B 1 282 ? 23.992 1.962   12.270  1.00 34.91  ? 261 ILE B N     1 
ATOM   5244 C  CA    . ILE B 1 282 ? 23.124 2.332   11.124  1.00 38.44  ? 261 ILE B CA    1 
ATOM   5245 C  C     . ILE B 1 282 ? 24.001 2.933   10.031  1.00 37.32  ? 261 ILE B C     1 
ATOM   5246 O  O     . ILE B 1 282 ? 24.586 4.022   10.248  1.00 33.29  ? 261 ILE B O     1 
ATOM   5247 C  CB    . ILE B 1 282 ? 22.011 3.303   11.527  1.00 43.24  ? 261 ILE B CB    1 
ATOM   5248 C  CG1   . ILE B 1 282 ? 21.060 2.676   12.557  1.00 43.10  ? 261 ILE B CG1   1 
ATOM   5249 C  CG2   . ILE B 1 282 ? 21.297 3.765   10.265  1.00 42.62  ? 261 ILE B CG2   1 
ATOM   5250 C  CD1   . ILE B 1 282 ? 20.058 3.638   13.167  1.00 43.46  ? 261 ILE B CD1   1 
ATOM   5251 N  N     . VAL B 1 283 ? 24.087 2.231   8.900   1.00 37.58  ? 262 VAL B N     1 
ATOM   5252 C  CA    . VAL B 1 283 ? 24.797 2.706   7.682   1.00 33.38  ? 262 VAL B CA    1 
ATOM   5253 C  C     . VAL B 1 283 ? 23.756 3.428   6.830   1.00 31.14  ? 262 VAL B C     1 
ATOM   5254 O  O     . VAL B 1 283 ? 22.764 2.792   6.472   1.00 27.82  ? 262 VAL B O     1 
ATOM   5255 C  CB    . VAL B 1 283 ? 25.467 1.533   6.939   1.00 35.29  ? 262 VAL B CB    1 
ATOM   5256 C  CG1   . VAL B 1 283 ? 26.159 2.007   5.672   1.00 34.41  ? 262 VAL B CG1   1 
ATOM   5257 C  CG2   . VAL B 1 283 ? 26.433 0.777   7.852   1.00 35.81  ? 262 VAL B CG2   1 
ATOM   5258 N  N     . ALA B 1 284 ? 23.945 4.733   6.604   1.00 32.72  ? 263 ALA B N     1 
ATOM   5259 C  CA    . ALA B 1 284 ? 22.986 5.607   5.880   1.00 35.49  ? 263 ALA B CA    1 
ATOM   5260 C  C     . ALA B 1 284 ? 23.717 6.328   4.739   1.00 34.30  ? 263 ALA B C     1 
ATOM   5261 O  O     . ALA B 1 284 ? 23.605 7.546   4.629   1.00 30.13  ? 263 ALA B O     1 
ATOM   5262 C  CB    . ALA B 1 284 ? 22.357 6.597   6.837   1.00 35.96  ? 263 ALA B CB    1 
ATOM   5263 N  N     . VAL B 1 285 ? 24.468 5.588   3.926   1.00 36.78  ? 264 VAL B N     1 
ATOM   5264 C  CA    . VAL B 1 285 ? 25.228 6.157   2.777   1.00 34.44  ? 264 VAL B CA    1 
ATOM   5265 C  C     . VAL B 1 285 ? 24.571 5.662   1.487   1.00 34.57  ? 264 VAL B C     1 
ATOM   5266 O  O     . VAL B 1 285 ? 23.775 4.729   1.520   1.00 35.23  ? 264 VAL B O     1 
ATOM   5267 C  CB    . VAL B 1 285 ? 26.714 5.801   2.912   1.00 33.47  ? 264 VAL B CB    1 
ATOM   5268 C  CG1   . VAL B 1 285 ? 27.264 6.210   4.268   1.00 33.93  ? 264 VAL B CG1   1 
ATOM   5269 C  CG2   . VAL B 1 285 ? 26.983 4.334   2.656   1.00 33.17  ? 264 VAL B CG2   1 
ATOM   5270 N  N     . PRO B 1 286 ? 24.856 6.270   0.309   1.00 35.26  ? 265 PRO B N     1 
ATOM   5271 C  CA    . PRO B 1 286 ? 24.403 5.716   -0.972  1.00 34.37  ? 265 PRO B CA    1 
ATOM   5272 C  C     . PRO B 1 286 ? 24.932 4.296   -1.177  1.00 34.77  ? 265 PRO B C     1 
ATOM   5273 O  O     . PRO B 1 286 ? 25.997 3.937   -0.675  1.00 36.43  ? 265 PRO B O     1 
ATOM   5274 C  CB    . PRO B 1 286 ? 25.000 6.670   -2.008  1.00 34.44  ? 265 PRO B CB    1 
ATOM   5275 C  CG    . PRO B 1 286 ? 25.277 7.957   -1.244  1.00 33.96  ? 265 PRO B CG    1 
ATOM   5276 C  CD    . PRO B 1 286 ? 25.645 7.498   0.148   1.00 35.60  ? 265 PRO B CD    1 
ATOM   5277 N  N     . PRO B 1 287 ? 24.162 3.402   -1.808  1.00 35.79  ? 266 PRO B N     1 
ATOM   5278 C  CA    . PRO B 1 287 ? 24.572 1.998   -1.958  1.00 39.60  ? 266 PRO B CA    1 
ATOM   5279 C  C     . PRO B 1 287 ? 26.012 1.720   -2.436  1.00 39.00  ? 266 PRO B C     1 
ATOM   5280 O  O     . PRO B 1 287 ? 26.719 0.905   -1.802  1.00 36.01  ? 266 PRO B O     1 
ATOM   5281 C  CB    . PRO B 1 287 ? 23.593 1.519   -3.042  1.00 39.24  ? 266 PRO B CB    1 
ATOM   5282 C  CG    . PRO B 1 287 ? 22.334 2.273   -2.715  1.00 37.43  ? 266 PRO B CG    1 
ATOM   5283 C  CD    . PRO B 1 287 ? 22.813 3.659   -2.333  1.00 35.28  ? 266 PRO B CD    1 
ATOM   5284 N  N     . THR B 1 288 ? 26.440 2.396   -3.506  1.00 36.45  ? 267 THR B N     1 
ATOM   5285 C  CA    . THR B 1 288 ? 27.815 2.254   -4.073  1.00 38.93  ? 267 THR B CA    1 
ATOM   5286 C  C     . THR B 1 288 ? 28.870 2.501   -2.979  1.00 36.59  ? 267 THR B C     1 
ATOM   5287 O  O     . THR B 1 288 ? 29.931 1.808   -3.002  1.00 33.22  ? 267 THR B O     1 
ATOM   5288 C  CB    . THR B 1 288 ? 28.039 3.146   -5.310  1.00 41.64  ? 267 THR B CB    1 
ATOM   5289 O  OG1   . THR B 1 288 ? 29.276 2.740   -5.906  1.00 43.37  ? 267 THR B OG1   1 
ATOM   5290 C  CG2   . THR B 1 288 ? 28.114 4.634   -5.021  1.00 42.13  ? 267 THR B CG2   1 
ATOM   5291 N  N     . LEU B 1 289 ? 28.615 3.442   -2.059  1.00 33.58  ? 268 LEU B N     1 
ATOM   5292 C  CA    . LEU B 1 289 ? 29.589 3.806   -0.992  1.00 34.30  ? 268 LEU B CA    1 
ATOM   5293 C  C     . LEU B 1 289 ? 29.513 2.809   0.174   1.00 31.41  ? 268 LEU B C     1 
ATOM   5294 O  O     . LEU B 1 289 ? 30.514 2.672   0.902   1.00 31.81  ? 268 LEU B O     1 
ATOM   5295 C  CB    . LEU B 1 289 ? 29.351 5.252   -0.544  1.00 31.70  ? 268 LEU B CB    1 
ATOM   5296 C  CG    . LEU B 1 289 ? 29.748 6.285   -1.594  1.00 33.64  ? 268 LEU B CG    1 
ATOM   5297 C  CD1   . LEU B 1 289 ? 29.393 7.685   -1.162  1.00 28.32  ? 268 LEU B CD1   1 
ATOM   5298 C  CD2   . LEU B 1 289 ? 31.238 6.190   -1.912  1.00 34.05  ? 268 LEU B CD2   1 
ATOM   5299 N  N     . ALA B 1 290 ? 28.365 2.179   0.379   1.00 30.53  ? 269 ALA B N     1 
ATOM   5300 C  CA    . ALA B 1 290 ? 28.135 1.248   1.495   1.00 30.70  ? 269 ALA B CA    1 
ATOM   5301 C  C     . ALA B 1 290 ? 28.978 -0.017  1.253   1.00 34.03  ? 269 ALA B C     1 
ATOM   5302 O  O     . ALA B 1 290 ? 29.516 -0.567  2.235   1.00 32.88  ? 269 ALA B O     1 
ATOM   5303 C  CB    . ALA B 1 290 ? 26.655 0.962   1.629   1.00 31.70  ? 269 ALA B CB    1 
ATOM   5304 N  N     . GLY B 1 291 ? 29.094 -0.428  -0.015  1.00 37.53  ? 270 GLY B N     1 
ATOM   5305 C  CA    . GLY B 1 291 ? 29.907 -1.569  -0.488  1.00 41.53  ? 270 GLY B CA    1 
ATOM   5306 C  C     . GLY B 1 291 ? 31.410 -1.297  -0.436  1.00 42.75  ? 270 GLY B C     1 
ATOM   5307 O  O     . GLY B 1 291 ? 32.155 -2.273  -0.464  1.00 37.03  ? 270 GLY B O     1 
ATOM   5308 N  N     . ARG B 1 292 ? 31.841 -0.031  -0.341  1.00 37.65  ? 271 ARG B N     1 
ATOM   5309 C  CA    . ARG B 1 292 ? 33.277 0.354   -0.325  1.00 39.94  ? 271 ARG B CA    1 
ATOM   5310 C  C     . ARG B 1 292 ? 33.873 0.272   1.077   1.00 39.38  ? 271 ARG B C     1 
ATOM   5311 O  O     . ARG B 1 292 ? 35.086 0.433   1.201   1.00 40.51  ? 271 ARG B O     1 
ATOM   5312 C  CB    . ARG B 1 292 ? 33.463 1.778   -0.841  1.00 38.74  ? 271 ARG B CB    1 
ATOM   5313 C  CG    . ARG B 1 292 ? 33.250 1.850   -2.340  1.00 41.35  ? 271 ARG B CG    1 
ATOM   5314 C  CD    . ARG B 1 292 ? 33.530 3.207   -2.936  1.00 43.28  ? 271 ARG B CD    1 
ATOM   5315 N  NE    . ARG B 1 292 ? 32.629 3.362   -4.064  1.00 44.87  ? 271 ARG B NE    1 
ATOM   5316 C  CZ    . ARG B 1 292 ? 32.841 4.123   -5.120  1.00 44.09  ? 271 ARG B CZ    1 
ATOM   5317 N  NH1   . ARG B 1 292 ? 33.942 4.846   -5.220  1.00 47.93  ? 271 ARG B NH1   1 
ATOM   5318 N  NH2   . ARG B 1 292 ? 31.917 4.187   -6.062  1.00 46.82  ? 271 ARG B NH2   1 
ATOM   5319 N  N     . ILE B 1 293 ? 33.049 0.041   2.091   1.00 37.89  ? 272 ILE B N     1 
ATOM   5320 C  CA    . ILE B 1 293 ? 33.485 -0.048  3.510   1.00 34.87  ? 272 ILE B CA    1 
ATOM   5321 C  C     . ILE B 1 293 ? 34.050 -1.456  3.747   1.00 35.96  ? 272 ILE B C     1 
ATOM   5322 O  O     . ILE B 1 293 ? 33.477 -2.423  3.223   1.00 34.35  ? 272 ILE B O     1 
ATOM   5323 C  CB    . ILE B 1 293 ? 32.297 0.305   4.414   1.00 33.88  ? 272 ILE B CB    1 
ATOM   5324 C  CG1   . ILE B 1 293 ? 31.978 1.796   4.339   1.00 37.07  ? 272 ILE B CG1   1 
ATOM   5325 C  CG2   . ILE B 1 293 ? 32.555 -0.116  5.843   1.00 34.65  ? 272 ILE B CG2   1 
ATOM   5326 C  CD1   . ILE B 1 293 ? 30.636 2.133   4.973   1.00 40.87  ? 272 ILE B CD1   1 
ATOM   5327 N  N     . ASP B 1 294 ? 35.126 -1.575  4.525   1.00 38.54  ? 273 ASP B N     1 
ATOM   5328 C  CA    . ASP B 1 294 ? 35.737 -2.891  4.875   1.00 43.32  ? 273 ASP B CA    1 
ATOM   5329 C  C     . ASP B 1 294 ? 34.824 -3.551  5.928   1.00 39.35  ? 273 ASP B C     1 
ATOM   5330 O  O     . ASP B 1 294 ? 34.908 -3.156  7.075   1.00 42.80  ? 273 ASP B O     1 
ATOM   5331 C  CB    . ASP B 1 294 ? 37.224 -2.689  5.231   1.00 46.59  ? 273 ASP B CB    1 
ATOM   5332 C  CG    . ASP B 1 294 ? 37.941 -3.831  5.945   1.00 57.02  ? 273 ASP B CG    1 
ATOM   5333 O  OD1   . ASP B 1 294 ? 37.463 -4.985  5.873   1.00 65.47  ? 273 ASP B OD1   1 
ATOM   5334 O  OD2   . ASP B 1 294 ? 38.988 -3.558  6.593   1.00 58.25  ? 273 ASP B OD2   1 
ATOM   5335 N  N     . HIS B 1 295 ? 33.932 -4.470  5.539   1.00 38.96  ? 274 HIS B N     1 
ATOM   5336 C  CA    . HIS B 1 295 ? 33.044 -5.228  6.473   1.00 40.81  ? 274 HIS B CA    1 
ATOM   5337 C  C     . HIS B 1 295 ? 33.785 -6.458  7.014   1.00 42.68  ? 274 HIS B C     1 
ATOM   5338 O  O     . HIS B 1 295 ? 34.455 -7.121  6.242   1.00 39.81  ? 274 HIS B O     1 
ATOM   5339 C  CB    . HIS B 1 295 ? 31.706 -5.617  5.822   1.00 41.70  ? 274 HIS B CB    1 
ATOM   5340 C  CG    . HIS B 1 295 ? 30.870 -4.429  5.498   1.00 45.50  ? 274 HIS B CG    1 
ATOM   5341 N  ND1   . HIS B 1 295 ? 30.044 -3.834  6.444   1.00 47.40  ? 274 HIS B ND1   1 
ATOM   5342 C  CD2   . HIS B 1 295 ? 30.789 -3.672  4.372   1.00 47.01  ? 274 HIS B CD2   1 
ATOM   5343 C  CE1   . HIS B 1 295 ? 29.466 -2.772  5.899   1.00 46.93  ? 274 HIS B CE1   1 
ATOM   5344 N  NE2   . HIS B 1 295 ? 29.903 -2.652  4.621   1.00 45.77  ? 274 HIS B NE2   1 
ATOM   5345 N  N     . ASP B 1 296 ? 33.675 -6.723  8.314   1.00 44.71  ? 275 ASP B N     1 
ATOM   5346 C  CA    . ASP B 1 296 ? 34.216 -7.927  8.993   1.00 46.62  ? 275 ASP B CA    1 
ATOM   5347 C  C     . ASP B 1 296 ? 33.152 -8.459  9.957   1.00 44.16  ? 275 ASP B C     1 
ATOM   5348 O  O     . ASP B 1 296 ? 32.728 -7.797  10.899  1.00 42.13  ? 275 ASP B O     1 
ATOM   5349 C  CB    . ASP B 1 296 ? 35.541 -7.617  9.691   1.00 48.86  ? 275 ASP B CB    1 
ATOM   5350 C  CG    . ASP B 1 296 ? 36.329 -8.864  10.073  1.00 57.49  ? 275 ASP B CG    1 
ATOM   5351 O  OD1   . ASP B 1 296 ? 35.830 -10.013 9.836   1.00 51.60  ? 275 ASP B OD1   1 
ATOM   5352 O  OD2   . ASP B 1 296 ? 37.452 -8.679  10.585  1.00 64.95  ? 275 ASP B OD2   1 
ATOM   5353 N  N     . PRO B 1 297 ? 32.626 -9.671  9.733   1.00 44.74  ? 276 PRO B N     1 
ATOM   5354 C  CA    . PRO B 1 297 ? 32.933 -10.451 8.531   1.00 43.00  ? 276 PRO B CA    1 
ATOM   5355 C  C     . PRO B 1 297 ? 32.475 -9.788  7.234   1.00 41.03  ? 276 PRO B C     1 
ATOM   5356 O  O     . PRO B 1 297 ? 31.713 -8.829  7.266   1.00 40.83  ? 276 PRO B O     1 
ATOM   5357 C  CB    . PRO B 1 297 ? 32.142 -11.758 8.714   1.00 42.09  ? 276 PRO B CB    1 
ATOM   5358 C  CG    . PRO B 1 297 ? 31.626 -11.744 10.145  1.00 41.30  ? 276 PRO B CG    1 
ATOM   5359 C  CD    . PRO B 1 297 ? 31.700 -10.326 10.653  1.00 39.36  ? 276 PRO B CD    1 
ATOM   5360 N  N     . PRO B 1 298 ? 32.862 -10.321 6.044   1.00 44.25  ? 277 PRO B N     1 
ATOM   5361 C  CA    . PRO B 1 298 ? 32.330 -9.820  4.773   1.00 38.47  ? 277 PRO B CA    1 
ATOM   5362 C  C     . PRO B 1 298 ? 30.795 -9.893  4.733   1.00 34.41  ? 277 PRO B C     1 
ATOM   5363 O  O     . PRO B 1 298 ? 30.240 -10.732 5.365   1.00 30.01  ? 277 PRO B O     1 
ATOM   5364 C  CB    . PRO B 1 298 ? 32.947 -10.740 3.698   1.00 39.79  ? 277 PRO B CB    1 
ATOM   5365 C  CG    . PRO B 1 298 ? 34.147 -11.391 4.388   1.00 41.49  ? 277 PRO B CG    1 
ATOM   5366 C  CD    . PRO B 1 298 ? 33.792 -11.454 5.857   1.00 38.57  ? 277 PRO B CD    1 
ATOM   5367 N  N     . LEU B 1 299 ? 30.166 -8.976  3.999   1.00 35.91  ? 278 LEU B N     1 
ATOM   5368 C  CA    . LEU B 1 299 ? 28.707 -8.965  3.693   1.00 34.98  ? 278 LEU B CA    1 
ATOM   5369 C  C     . LEU B 1 299 ? 28.334 -10.270 2.994   1.00 35.55  ? 278 LEU B C     1 
ATOM   5370 O  O     . LEU B 1 299 ? 29.083 -10.771 2.149   1.00 32.05  ? 278 LEU B O     1 
ATOM   5371 C  CB    . LEU B 1 299 ? 28.378 -7.775  2.784   1.00 35.36  ? 278 LEU B CB    1 
ATOM   5372 C  CG    . LEU B 1 299 ? 28.581 -6.362  3.370   1.00 37.91  ? 278 LEU B CG    1 
ATOM   5373 C  CD1   . LEU B 1 299 ? 27.990 -5.336  2.437   1.00 34.35  ? 278 LEU B CD1   1 
ATOM   5374 C  CD2   . LEU B 1 299 ? 27.960 -6.201  4.763   1.00 38.75  ? 278 LEU B CD2   1 
ATOM   5375 N  N     . PRO B 1 300 ? 27.170 -10.876 3.318   1.00 35.28  ? 279 PRO B N     1 
ATOM   5376 C  CA    . PRO B 1 300 ? 26.753 -12.087 2.614   1.00 35.52  ? 279 PRO B CA    1 
ATOM   5377 C  C     . PRO B 1 300 ? 26.722 -11.799 1.114   1.00 33.38  ? 279 PRO B C     1 
ATOM   5378 O  O     . PRO B 1 300 ? 26.599 -10.650 0.688   1.00 31.08  ? 279 PRO B O     1 
ATOM   5379 C  CB    . PRO B 1 300 ? 25.375 -12.455 3.209   1.00 36.77  ? 279 PRO B CB    1 
ATOM   5380 C  CG    . PRO B 1 300 ? 24.934 -11.199 3.986   1.00 37.94  ? 279 PRO B CG    1 
ATOM   5381 C  CD    . PRO B 1 300 ? 26.207 -10.452 4.356   1.00 34.29  ? 279 PRO B CD    1 
ATOM   5382 N  N     . PRO B 1 301 ? 26.876 -12.841 0.272   1.00 33.98  ? 280 PRO B N     1 
ATOM   5383 C  CA    . PRO B 1 301 ? 26.977 -12.663 -1.174  1.00 35.19  ? 280 PRO B CA    1 
ATOM   5384 C  C     . PRO B 1 301 ? 25.844 -11.860 -1.840  1.00 32.14  ? 280 PRO B C     1 
ATOM   5385 O  O     . PRO B 1 301 ? 26.137 -11.107 -2.751  1.00 29.16  ? 280 PRO B O     1 
ATOM   5386 C  CB    . PRO B 1 301 ? 27.002 -14.113 -1.704  1.00 33.97  ? 280 PRO B CB    1 
ATOM   5387 C  CG    . PRO B 1 301 ? 26.456 -14.950 -0.568  1.00 33.90  ? 280 PRO B CG    1 
ATOM   5388 C  CD    . PRO B 1 301 ? 26.999 -14.253 0.661   1.00 35.03  ? 280 PRO B CD    1 
ATOM   5389 N  N     . GLN B 1 302 ? 24.587 -12.081 -1.462  1.00 32.72  ? 281 GLN B N     1 
ATOM   5390 C  CA    . GLN B 1 302 ? 23.426 -11.480 -2.194  1.00 32.36  ? 281 GLN B CA    1 
ATOM   5391 C  C     . GLN B 1 302 ? 23.454 -9.952  -2.000  1.00 30.22  ? 281 GLN B C     1 
ATOM   5392 O  O     . GLN B 1 302 ? 23.184 -9.208  -2.953  1.00 28.54  ? 281 GLN B O     1 
ATOM   5393 C  CB    . GLN B 1 302 ? 22.103 -12.096 -1.728  1.00 33.45  ? 281 GLN B CB    1 
ATOM   5394 C  CG    . GLN B 1 302 ? 20.894 -11.692 -2.569  1.00 35.99  ? 281 GLN B CG    1 
ATOM   5395 C  CD    . GLN B 1 302 ? 19.593 -12.071 -1.899  1.00 37.67  ? 281 GLN B CD    1 
ATOM   5396 O  OE1   . GLN B 1 302 ? 19.534 -12.178 -0.680  1.00 37.12  ? 281 GLN B OE1   1 
ATOM   5397 N  NE2   . GLN B 1 302 ? 18.532 -12.262 -2.676  1.00 34.35  ? 281 GLN B NE2   1 
ATOM   5398 N  N     . ARG B 1 303 ? 23.804 -9.499  -0.814  1.00 28.87  ? 282 ARG B N     1 
ATOM   5399 C  CA    . ARG B 1 303 ? 23.860 -8.057  -0.487  1.00 34.44  ? 282 ARG B CA    1 
ATOM   5400 C  C     . ARG B 1 303 ? 25.069 -7.434  -1.196  1.00 34.67  ? 282 ARG B C     1 
ATOM   5401 O  O     . ARG B 1 303 ? 24.902 -6.325  -1.735  1.00 34.00  ? 282 ARG B O     1 
ATOM   5402 C  CB    . ARG B 1 303 ? 23.873 -7.879  1.034   1.00 38.62  ? 282 ARG B CB    1 
ATOM   5403 C  CG    . ARG B 1 303 ? 24.267 -6.487  1.497   1.00 45.54  ? 282 ARG B CG    1 
ATOM   5404 C  CD    . ARG B 1 303 ? 23.089 -5.686  1.999   1.00 48.47  ? 282 ARG B CD    1 
ATOM   5405 N  NE    . ARG B 1 303 ? 23.461 -4.287  2.127   1.00 57.00  ? 282 ARG B NE    1 
ATOM   5406 C  CZ    . ARG B 1 303 ? 22.604 -3.274  2.104   1.00 52.73  ? 282 ARG B CZ    1 
ATOM   5407 N  NH1   . ARG B 1 303 ? 21.310 -3.495  1.983   1.00 56.22  ? 282 ARG B NH1   1 
ATOM   5408 N  NH2   . ARG B 1 303 ? 23.042 -2.037  2.210   1.00 54.73  ? 282 ARG B NH2   1 
ATOM   5409 N  N     . ASP B 1 304 ? 26.238 -8.094  -1.254  1.00 34.46  ? 283 ASP B N     1 
ATOM   5410 C  CA    . ASP B 1 304 ? 27.387 -7.478  -1.976  1.00 33.88  ? 283 ASP B CA    1 
ATOM   5411 C  C     . ASP B 1 304 ? 26.994 -7.278  -3.446  1.00 34.01  ? 283 ASP B C     1 
ATOM   5412 O  O     . ASP B 1 304 ? 27.162 -6.146  -3.938  1.00 34.58  ? 283 ASP B O     1 
ATOM   5413 C  CB    . ASP B 1 304 ? 28.725 -8.222  -1.887  1.00 35.26  ? 283 ASP B CB    1 
ATOM   5414 C  CG    . ASP B 1 304 ? 29.889 -7.335  -2.370  1.00 39.43  ? 283 ASP B CG    1 
ATOM   5415 O  OD1   . ASP B 1 304 ? 30.432 -6.540  -1.539  1.00 44.04  ? 283 ASP B OD1   1 
ATOM   5416 O  OD2   . ASP B 1 304 ? 30.219 -7.382  -3.586  1.00 34.65  ? 283 ASP B OD2   1 
ATOM   5417 N  N     . GLN B 1 305 ? 26.393 -8.282  -4.090  1.00 29.96  ? 284 GLN B N     1 
ATOM   5418 C  CA    . GLN B 1 305 ? 26.063 -8.216  -5.532  1.00 29.86  ? 284 GLN B CA    1 
ATOM   5419 C  C     . GLN B 1 305 ? 24.944 -7.198  -5.774  1.00 29.96  ? 284 GLN B C     1 
ATOM   5420 O  O     . GLN B 1 305 ? 24.940 -6.582  -6.859  1.00 30.18  ? 284 GLN B O     1 
ATOM   5421 C  CB    . GLN B 1 305 ? 25.722 -9.603  -6.079  1.00 32.60  ? 284 GLN B CB    1 
ATOM   5422 C  CG    . GLN B 1 305 ? 26.903 -10.564 -5.961  1.00 35.62  ? 284 GLN B CG    1 
ATOM   5423 C  CD    . GLN B 1 305 ? 27.034 -11.574 -7.075  1.00 37.38  ? 284 GLN B CD    1 
ATOM   5424 O  OE1   . GLN B 1 305 ? 26.274 -12.542 -7.159  1.00 42.26  ? 284 GLN B OE1   1 
ATOM   5425 N  NE2   . GLN B 1 305 ? 28.065 -11.408 -7.890  1.00 37.22  ? 284 GLN B NE2   1 
ATOM   5426 N  N     . LEU B 1 306 ? 24.022 -7.030  -4.834  1.00 28.74  ? 285 LEU B N     1 
ATOM   5427 C  CA    . LEU B 1 306 ? 22.945 -6.013  -4.958  1.00 28.60  ? 285 LEU B CA    1 
ATOM   5428 C  C     . LEU B 1 306 ? 23.582 -4.631  -5.135  1.00 26.88  ? 285 LEU B C     1 
ATOM   5429 O  O     . LEU B 1 306 ? 23.204 -3.941  -6.087  1.00 32.71  ? 285 LEU B O     1 
ATOM   5430 C  CB    . LEU B 1 306 ? 22.062 -6.034  -3.711  1.00 30.95  ? 285 LEU B CB    1 
ATOM   5431 C  CG    . LEU B 1 306 ? 20.941 -4.978  -3.669  1.00 31.14  ? 285 LEU B CG    1 
ATOM   5432 C  CD1   . LEU B 1 306 ? 20.055 -5.065  -4.912  1.00 30.48  ? 285 LEU B CD1   1 
ATOM   5433 C  CD2   . LEU B 1 306 ? 20.097 -5.140  -2.418  1.00 29.01  ? 285 LEU B CD2   1 
ATOM   5434 N  N     . LEU B 1 307 ? 24.524 -4.277  -4.260  1.00 28.32  ? 286 LEU B N     1 
ATOM   5435 C  CA    . LEU B 1 307 ? 25.239 -2.976  -4.287  1.00 33.05  ? 286 LEU B CA    1 
ATOM   5436 C  C     . LEU B 1 307 ? 25.931 -2.791  -5.649  1.00 35.21  ? 286 LEU B C     1 
ATOM   5437 O  O     . LEU B 1 307 ? 25.861 -1.649  -6.153  1.00 36.83  ? 286 LEU B O     1 
ATOM   5438 C  CB    . LEU B 1 307 ? 26.215 -2.888  -3.112  1.00 35.17  ? 286 LEU B CB    1 
ATOM   5439 C  CG    . LEU B 1 307 ? 25.584 -2.897  -1.710  1.00 39.25  ? 286 LEU B CG    1 
ATOM   5440 C  CD1   . LEU B 1 307 ? 26.658 -2.792  -0.639  1.00 37.46  ? 286 LEU B CD1   1 
ATOM   5441 C  CD2   . LEU B 1 307 ? 24.547 -1.781  -1.527  1.00 39.83  ? 286 LEU B CD2   1 
ATOM   5442 N  N     . GLN B 1 308 ? 26.479 -3.868  -6.244  1.00 32.66  ? 287 GLN B N     1 
ATOM   5443 C  CA    . GLN B 1 308 ? 27.072 -3.897  -7.609  1.00 28.89  ? 287 GLN B CA    1 
ATOM   5444 C  C     . GLN B 1 308 ? 25.975 -3.683  -8.666  1.00 27.27  ? 287 GLN B C     1 
ATOM   5445 O  O     . GLN B 1 308 ? 26.325 -3.246  -9.787  1.00 24.39  ? 287 GLN B O     1 
ATOM   5446 C  CB    . GLN B 1 308 ? 27.787 -5.225  -7.922  1.00 29.73  ? 287 GLN B CB    1 
ATOM   5447 C  CG    . GLN B 1 308 ? 28.980 -5.548  -7.023  1.00 31.36  ? 287 GLN B CG    1 
ATOM   5448 C  CD    . GLN B 1 308 ? 29.662 -6.860  -7.351  1.00 34.76  ? 287 GLN B CD    1 
ATOM   5449 O  OE1   . GLN B 1 308 ? 30.134 -7.589  -6.472  1.00 37.40  ? 287 GLN B OE1   1 
ATOM   5450 N  NE2   . GLN B 1 308 ? 29.749 -7.165  -8.633  1.00 33.57  ? 287 GLN B NE2   1 
ATOM   5451 N  N     . HIS B 1 309 ? 24.708 -3.984  -8.368  1.00 26.59  ? 288 HIS B N     1 
ATOM   5452 C  CA    . HIS B 1 309 ? 23.583 -3.813  -9.329  1.00 29.01  ? 288 HIS B CA    1 
ATOM   5453 C  C     . HIS B 1 309 ? 22.727 -2.574  -9.011  1.00 28.35  ? 288 HIS B C     1 
ATOM   5454 O  O     . HIS B 1 309 ? 21.608 -2.555  -9.479  1.00 30.85  ? 288 HIS B O     1 
ATOM   5455 C  CB    . HIS B 1 309 ? 22.721 -5.078  -9.326  1.00 31.36  ? 288 HIS B CB    1 
ATOM   5456 C  CG    . HIS B 1 309 ? 23.328 -6.205  -10.084 1.00 31.66  ? 288 HIS B CG    1 
ATOM   5457 N  ND1   . HIS B 1 309 ? 24.030 -7.212  -9.467  1.00 32.55  ? 288 HIS B ND1   1 
ATOM   5458 C  CD2   . HIS B 1 309 ? 23.367 -6.470  -11.401 1.00 31.52  ? 288 HIS B CD2   1 
ATOM   5459 C  CE1   . HIS B 1 309 ? 24.451 -8.069  -10.373 1.00 32.39  ? 288 HIS B CE1   1 
ATOM   5460 N  NE2   . HIS B 1 309 ? 24.091 -7.618  -11.566 1.00 31.87  ? 288 HIS B NE2   1 
ATOM   5461 N  N     . MET B 1 310 ? 23.211 -1.623  -8.212  1.00 28.67  ? 289 MET B N     1 
ATOM   5462 C  CA    . MET B 1 310 ? 22.483 -0.381  -7.815  1.00 29.33  ? 289 MET B CA    1 
ATOM   5463 C  C     . MET B 1 310 ? 23.313 0.839   -8.193  1.00 26.68  ? 289 MET B C     1 
ATOM   5464 O  O     . MET B 1 310 ? 23.735 1.570   -7.324  1.00 25.46  ? 289 MET B O     1 
ATOM   5465 C  CB    . MET B 1 310 ? 22.231 -0.367  -6.300  1.00 31.68  ? 289 MET B CB    1 
ATOM   5466 C  CG    . MET B 1 310 ? 21.085 -1.308  -5.884  1.00 35.32  ? 289 MET B CG    1 
ATOM   5467 S  SD    . MET B 1 310 ? 20.739 -1.267  -4.104  1.00 39.72  ? 289 MET B SD    1 
ATOM   5468 C  CE    . MET B 1 310 ? 19.599 0.116   -4.073  1.00 36.65  ? 289 MET B CE    1 
ATOM   5469 N  N     . PRO B 1 311 ? 23.625 1.075   -9.487  1.00 27.18  ? 290 PRO B N     1 
ATOM   5470 C  CA    . PRO B 1 311 ? 24.471 2.199   -9.866  1.00 30.41  ? 290 PRO B CA    1 
ATOM   5471 C  C     . PRO B 1 311 ? 23.727 3.540   -9.717  1.00 32.67  ? 290 PRO B C     1 
ATOM   5472 O  O     . PRO B 1 311 ? 22.540 3.573   -9.935  1.00 33.20  ? 290 PRO B O     1 
ATOM   5473 C  CB    . PRO B 1 311 ? 24.814 1.824   -11.306 1.00 28.48  ? 290 PRO B CB    1 
ATOM   5474 C  CG    . PRO B 1 311 ? 23.605 1.103   -11.814 1.00 27.54  ? 290 PRO B CG    1 
ATOM   5475 C  CD    . PRO B 1 311 ? 23.232 0.249   -10.637 1.00 28.92  ? 290 PRO B CD    1 
ATOM   5476 N  N     . GLN B 1 312 ? 24.407 4.578   -9.228  1.00 35.20  ? 291 GLN B N     1 
ATOM   5477 C  CA    . GLN B 1 312 ? 23.818 5.932   -9.058  1.00 34.29  ? 291 GLN B CA    1 
ATOM   5478 C  C     . GLN B 1 312 ? 23.623 6.541   -10.446 1.00 31.01  ? 291 GLN B C     1 
ATOM   5479 O  O     . GLN B 1 312 ? 24.273 6.106   -11.406 1.00 27.97  ? 291 GLN B O     1 
ATOM   5480 C  CB    . GLN B 1 312 ? 24.680 6.906   -8.246  1.00 39.91  ? 291 GLN B CB    1 
ATOM   5481 C  CG    . GLN B 1 312 ? 25.236 6.389   -6.923  1.00 48.60  ? 291 GLN B CG    1 
ATOM   5482 C  CD    . GLN B 1 312 ? 24.186 5.931   -5.938  1.00 53.06  ? 291 GLN B CD    1 
ATOM   5483 O  OE1   . GLN B 1 312 ? 23.260 6.673   -5.607  1.00 57.72  ? 291 GLN B OE1   1 
ATOM   5484 N  NE2   . GLN B 1 312 ? 24.347 4.708   -5.443  1.00 57.24  ? 291 GLN B NE2   1 
ATOM   5485 N  N     . GLY B 1 313 ? 22.801 7.573   -10.539 1.00 29.09  ? 292 GLY B N     1 
ATOM   5486 C  CA    . GLY B 1 313 ? 22.539 8.227   -11.820 1.00 30.45  ? 292 GLY B CA    1 
ATOM   5487 C  C     . GLY B 1 313 ? 23.647 9.193   -12.183 1.00 28.92  ? 292 GLY B C     1 
ATOM   5488 O  O     . GLY B 1 313 ? 24.608 9.352   -11.406 1.00 30.09  ? 292 GLY B O     1 
ATOM   5489 N  N     . SER B 1 314 ? 23.474 9.856   -13.322 1.00 31.82  ? 293 SER B N     1 
ATOM   5490 C  CA    . SER B 1 314 ? 24.401 10.871  -13.873 1.00 33.08  ? 293 SER B CA    1 
ATOM   5491 C  C     . SER B 1 314 ? 23.638 12.187  -14.004 1.00 30.78  ? 293 SER B C     1 
ATOM   5492 O  O     . SER B 1 314 ? 22.681 12.262  -14.790 1.00 29.36  ? 293 SER B O     1 
ATOM   5493 C  CB    . SER B 1 314 ? 24.968 10.383  -15.179 1.00 34.55  ? 293 SER B CB    1 
ATOM   5494 O  OG    . SER B 1 314 ? 25.505 9.067   -15.016 1.00 36.22  ? 293 SER B OG    1 
ATOM   5495 N  N     . VAL B 1 315 ? 24.015 13.186  -13.227 1.00 29.85  ? 294 VAL B N     1 
ATOM   5496 C  CA    . VAL B 1 315 ? 23.401 14.525  -13.378 1.00 30.61  ? 294 VAL B CA    1 
ATOM   5497 C  C     . VAL B 1 315 ? 24.443 15.590  -13.034 1.00 28.99  ? 294 VAL B C     1 
ATOM   5498 O  O     . VAL B 1 315 ? 25.280 15.356  -12.133 1.00 33.41  ? 294 VAL B O     1 
ATOM   5499 C  CB    . VAL B 1 315 ? 22.117 14.625  -12.536 1.00 31.75  ? 294 VAL B CB    1 
ATOM   5500 C  CG1   . VAL B 1 315 ? 22.398 14.353  -11.078 1.00 31.77  ? 294 VAL B CG1   1 
ATOM   5501 C  CG2   . VAL B 1 315 ? 21.426 15.979  -12.710 1.00 34.40  ? 294 VAL B CG2   1 
ATOM   5502 N  N     . VAL B 1 316 ? 24.406 16.685  -13.784 1.00 29.29  ? 295 VAL B N     1 
ATOM   5503 C  CA    . VAL B 1 316 ? 25.102 17.979  -13.529 1.00 31.20  ? 295 VAL B CA    1 
ATOM   5504 C  C     . VAL B 1 316 ? 24.000 19.037  -13.390 1.00 31.70  ? 295 VAL B C     1 
ATOM   5505 O  O     . VAL B 1 316 ? 23.272 19.291  -14.346 1.00 30.78  ? 295 VAL B O     1 
ATOM   5506 C  CB    . VAL B 1 316 ? 26.082 18.338  -14.672 1.00 35.91  ? 295 VAL B CB    1 
ATOM   5507 C  CG1   . VAL B 1 316 ? 26.844 19.633  -14.388 1.00 34.50  ? 295 VAL B CG1   1 
ATOM   5508 C  CG2   . VAL B 1 316 ? 27.058 17.203  -14.978 1.00 31.62  ? 295 VAL B CG2   1 
ATOM   5509 N  N     . LYS B 1 317 ? 23.820 19.569  -12.196 1.00 34.09  ? 296 LYS B N     1 
ATOM   5510 C  CA    . LYS B 1 317 ? 22.811 20.614  -11.928 1.00 32.72  ? 296 LYS B CA    1 
ATOM   5511 C  C     . LYS B 1 317 ? 23.455 21.980  -12.083 1.00 31.87  ? 296 LYS B C     1 
ATOM   5512 O  O     . LYS B 1 317 ? 24.523 22.202  -11.459 1.00 38.65  ? 296 LYS B O     1 
ATOM   5513 C  CB    . LYS B 1 317 ? 22.292 20.499  -10.494 1.00 33.54  ? 296 LYS B CB    1 
ATOM   5514 C  CG    . LYS B 1 317 ? 21.299 21.577  -10.095 1.00 32.01  ? 296 LYS B CG    1 
ATOM   5515 C  CD    . LYS B 1 317 ? 20.432 21.167  -8.943  1.00 33.81  ? 296 LYS B CD    1 
ATOM   5516 C  CE    . LYS B 1 317 ? 19.440 22.249  -8.574  1.00 33.93  ? 296 LYS B CE    1 
ATOM   5517 N  NZ    . LYS B 1 317 ? 18.679 21.895  -7.361  1.00 35.23  ? 296 LYS B NZ    1 
ATOM   5518 N  N     . PHE B 1 318 ? 22.791 22.896  -12.770 1.00 31.76  ? 297 PHE B N     1 
ATOM   5519 C  CA    . PHE B 1 318 ? 23.345 24.254  -12.960 1.00 34.22  ? 297 PHE B CA    1 
ATOM   5520 C  C     . PHE B 1 318 ? 22.313 25.327  -12.584 1.00 35.34  ? 297 PHE B C     1 
ATOM   5521 O  O     . PHE B 1 318 ? 21.124 25.030  -12.496 1.00 32.06  ? 297 PHE B O     1 
ATOM   5522 C  CB    . PHE B 1 318 ? 23.885 24.366  -14.385 1.00 32.45  ? 297 PHE B CB    1 
ATOM   5523 C  CG    . PHE B 1 318 ? 22.835 24.281  -15.458 1.00 33.50  ? 297 PHE B CG    1 
ATOM   5524 C  CD1   . PHE B 1 318 ? 22.032 25.374  -15.754 1.00 31.54  ? 297 PHE B CD1   1 
ATOM   5525 C  CD2   . PHE B 1 318 ? 22.651 23.112  -16.173 1.00 32.55  ? 297 PHE B CD2   1 
ATOM   5526 C  CE1   . PHE B 1 318 ? 21.070 25.294  -16.744 1.00 30.69  ? 297 PHE B CE1   1 
ATOM   5527 C  CE2   . PHE B 1 318 ? 21.701 23.047  -17.175 1.00 34.17  ? 297 PHE B CE2   1 
ATOM   5528 C  CZ    . PHE B 1 318 ? 20.914 24.138  -17.459 1.00 31.18  ? 297 PHE B CZ    1 
ATOM   5529 N  N     . HIS B 1 319 ? 22.822 26.542  -12.344 1.00 35.25  ? 298 HIS B N     1 
ATOM   5530 C  CA    . HIS B 1 319 ? 22.079 27.810  -12.163 1.00 38.27  ? 298 HIS B CA    1 
ATOM   5531 C  C     . HIS B 1 319 ? 22.789 28.897  -12.972 1.00 38.10  ? 298 HIS B C     1 
ATOM   5532 O  O     . HIS B 1 319 ? 23.983 29.161  -12.711 1.00 42.24  ? 298 HIS B O     1 
ATOM   5533 C  CB    . HIS B 1 319 ? 22.023 28.236  -10.683 1.00 43.48  ? 298 HIS B CB    1 
ATOM   5534 C  CG    . HIS B 1 319 ? 21.420 27.251  -9.736  1.00 40.47  ? 298 HIS B CG    1 
ATOM   5535 N  ND1   . HIS B 1 319 ? 22.140 26.169  -9.238  1.00 43.59  ? 298 HIS B ND1   1 
ATOM   5536 C  CD2   . HIS B 1 319 ? 20.207 27.211  -9.151  1.00 39.23  ? 298 HIS B CD2   1 
ATOM   5537 C  CE1   . HIS B 1 319 ? 21.379 25.492  -8.416  1.00 39.84  ? 298 HIS B CE1   1 
ATOM   5538 N  NE2   . HIS B 1 319 ? 20.186 26.121  -8.330  1.00 41.97  ? 298 HIS B NE2   1 
ATOM   5539 N  N     . VAL B 1 320 ? 22.075 29.523  -13.899 1.00 37.29  ? 299 VAL B N     1 
ATOM   5540 C  CA    . VAL B 1 320 ? 22.583 30.673  -14.696 1.00 37.26  ? 299 VAL B CA    1 
ATOM   5541 C  C     . VAL B 1 320 ? 22.041 31.935  -14.031 1.00 37.31  ? 299 VAL B C     1 
ATOM   5542 O  O     . VAL B 1 320 ? 20.811 32.026  -13.898 1.00 38.54  ? 299 VAL B O     1 
ATOM   5543 C  CB    . VAL B 1 320 ? 22.155 30.566  -16.164 1.00 36.26  ? 299 VAL B CB    1 
ATOM   5544 C  CG1   . VAL B 1 320 ? 23.133 31.316  -17.040 1.00 36.89  ? 299 VAL B CG1   1 
ATOM   5545 C  CG2   . VAL B 1 320 ? 22.041 29.107  -16.607 1.00 37.75  ? 299 VAL B CG2   1 
ATOM   5546 N  N     . ILE B 1 321 ? 22.934 32.814  -13.579 1.00 33.66  ? 300 ILE B N     1 
ATOM   5547 C  CA    . ILE B 1 321 ? 22.597 34.028  -12.790 1.00 37.85  ? 300 ILE B CA    1 
ATOM   5548 C  C     . ILE B 1 321 ? 22.492 35.214  -13.745 1.00 38.47  ? 300 ILE B C     1 
ATOM   5549 O  O     . ILE B 1 321 ? 23.449 35.431  -14.507 1.00 40.38  ? 300 ILE B O     1 
ATOM   5550 C  CB    . ILE B 1 321 ? 23.652 34.289  -11.702 1.00 39.44  ? 300 ILE B CB    1 
ATOM   5551 C  CG1   . ILE B 1 321 ? 23.975 33.033  -10.882 1.00 42.81  ? 300 ILE B CG1   1 
ATOM   5552 C  CG2   . ILE B 1 321 ? 23.217 35.446  -10.827 1.00 39.73  ? 300 ILE B CG2   1 
ATOM   5553 C  CD1   . ILE B 1 321 ? 22.750 32.259  -10.399 1.00 40.10  ? 300 ILE B CD1   1 
ATOM   5554 N  N     . TYR B 1 322 ? 21.379 35.945  -13.675 1.00 38.69  ? 301 TYR B N     1 
ATOM   5555 C  CA    . TYR B 1 322 ? 21.103 37.196  -14.432 1.00 38.82  ? 301 TYR B CA    1 
ATOM   5556 C  C     . TYR B 1 322 ? 20.782 38.336  -13.447 1.00 44.56  ? 301 TYR B C     1 
ATOM   5557 O  O     . TYR B 1 322 ? 20.295 38.074  -12.297 1.00 39.92  ? 301 TYR B O     1 
ATOM   5558 C  CB    . TYR B 1 322 ? 19.943 36.980  -15.408 1.00 38.99  ? 301 TYR B CB    1 
ATOM   5559 C  CG    . TYR B 1 322 ? 20.216 35.992  -16.517 1.00 44.08  ? 301 TYR B CG    1 
ATOM   5560 C  CD1   . TYR B 1 322 ? 20.978 36.331  -17.626 1.00 42.39  ? 301 TYR B CD1   1 
ATOM   5561 C  CD2   . TYR B 1 322 ? 19.711 34.703  -16.466 1.00 44.97  ? 301 TYR B CD2   1 
ATOM   5562 C  CE1   . TYR B 1 322 ? 21.217 35.425  -18.651 1.00 45.19  ? 301 TYR B CE1   1 
ATOM   5563 C  CE2   . TYR B 1 322 ? 19.952 33.784  -17.476 1.00 47.76  ? 301 TYR B CE2   1 
ATOM   5564 C  CZ    . TYR B 1 322 ? 20.710 34.136  -18.581 1.00 47.42  ? 301 TYR B CZ    1 
ATOM   5565 O  OH    . TYR B 1 322 ? 20.924 33.218  -19.584 1.00 40.50  ? 301 TYR B OH    1 
ATOM   5566 N  N     . ASP B 1 323 ? 21.008 39.584  -13.874 1.00 42.28  ? 302 ASP B N     1 
ATOM   5567 C  CA    . ASP B 1 323 ? 20.728 40.777  -13.032 1.00 44.55  ? 302 ASP B CA    1 
ATOM   5568 C  C     . ASP B 1 323 ? 19.243 40.744  -12.656 1.00 40.76  ? 302 ASP B C     1 
ATOM   5569 O  O     . ASP B 1 323 ? 18.922 40.975  -11.481 1.00 45.76  ? 302 ASP B O     1 
ATOM   5570 C  CB    . ASP B 1 323 ? 21.171 42.086  -13.704 1.00 44.42  ? 302 ASP B CB    1 
ATOM   5571 C  CG    . ASP B 1 323 ? 22.686 42.289  -13.756 1.00 50.96  ? 302 ASP B CG    1 
ATOM   5572 O  OD1   . ASP B 1 323 ? 23.394 41.851  -12.826 1.00 53.19  ? 302 ASP B OD1   1 
ATOM   5573 O  OD2   . ASP B 1 323 ? 23.164 42.869  -14.746 1.00 61.78  ? 302 ASP B OD2   1 
ATOM   5574 N  N     . GLU B 1 324 ? 18.371 40.419  -13.604 1.00 48.85  ? 303 GLU B N     1 
ATOM   5575 C  CA    . GLU B 1 324 ? 16.890 40.408  -13.432 1.00 47.53  ? 303 GLU B CA    1 
ATOM   5576 C  C     . GLU B 1 324 ? 16.358 39.118  -14.024 1.00 44.30  ? 303 GLU B C     1 
ATOM   5577 O  O     . GLU B 1 324 ? 16.971 38.595  -14.955 1.00 39.80  ? 303 GLU B O     1 
ATOM   5578 C  CB    . GLU B 1 324 ? 16.191 41.509  -14.237 1.00 54.44  ? 303 GLU B CB    1 
ATOM   5579 C  CG    . GLU B 1 324 ? 16.115 42.866  -13.571 1.00 63.62  ? 303 GLU B CG    1 
ATOM   5580 C  CD    . GLU B 1 324 ? 15.579 43.931  -14.514 1.00 71.15  ? 303 GLU B CD    1 
ATOM   5581 O  OE1   . GLU B 1 324 ? 14.978 43.548  -15.554 1.00 72.41  ? 303 GLU B OE1   1 
ATOM   5582 O  OE2   . GLU B 1 324 ? 15.781 45.136  -14.230 1.00 73.18  ? 303 GLU B OE2   1 
ATOM   5583 N  N     . PRO B 1 325 ? 15.178 38.637  -13.578 1.00 43.63  ? 304 PRO B N     1 
ATOM   5584 C  CA    . PRO B 1 325 ? 14.471 37.567  -14.285 1.00 44.99  ? 304 PRO B CA    1 
ATOM   5585 C  C     . PRO B 1 325 ? 13.776 38.108  -15.544 1.00 47.37  ? 304 PRO B C     1 
ATOM   5586 O  O     . PRO B 1 325 ? 12.562 38.175  -15.555 1.00 46.26  ? 304 PRO B O     1 
ATOM   5587 C  CB    . PRO B 1 325 ? 13.468 37.089  -13.228 1.00 44.97  ? 304 PRO B CB    1 
ATOM   5588 C  CG    . PRO B 1 325 ? 13.132 38.358  -12.469 1.00 45.06  ? 304 PRO B CG    1 
ATOM   5589 C  CD    . PRO B 1 325 ? 14.451 39.105  -12.387 1.00 41.29  ? 304 PRO B CD    1 
ATOM   5590 N  N     . TRP B 1 326 ? 14.565 38.443  -16.574 1.00 47.37  ? 305 TRP B N     1 
ATOM   5591 C  CA    . TRP B 1 326 ? 14.147 39.216  -17.780 1.00 46.30  ? 305 TRP B CA    1 
ATOM   5592 C  C     . TRP B 1 326 ? 13.003 38.520  -18.561 1.00 44.41  ? 305 TRP B C     1 
ATOM   5593 O  O     . TRP B 1 326 ? 12.136 39.235  -19.120 1.00 38.44  ? 305 TRP B O     1 
ATOM   5594 C  CB    . TRP B 1 326 ? 15.382 39.530  -18.664 1.00 45.74  ? 305 TRP B CB    1 
ATOM   5595 C  CG    . TRP B 1 326 ? 16.162 38.339  -19.143 1.00 39.67  ? 305 TRP B CG    1 
ATOM   5596 C  CD1   . TRP B 1 326 ? 17.303 37.813  -18.599 1.00 44.14  ? 305 TRP B CD1   1 
ATOM   5597 C  CD2   . TRP B 1 326 ? 15.860 37.514  -20.283 1.00 38.69  ? 305 TRP B CD2   1 
ATOM   5598 N  NE1   . TRP B 1 326 ? 17.698 36.693  -19.292 1.00 42.65  ? 305 TRP B NE1   1 
ATOM   5599 C  CE2   . TRP B 1 326 ? 16.831 36.491  -20.331 1.00 38.35  ? 305 TRP B CE2   1 
ATOM   5600 C  CE3   . TRP B 1 326 ? 14.853 37.529  -21.247 1.00 40.21  ? 305 TRP B CE3   1 
ATOM   5601 C  CZ2   . TRP B 1 326 ? 16.828 35.518  -21.320 1.00 39.01  ? 305 TRP B CZ2   1 
ATOM   5602 C  CZ3   . TRP B 1 326 ? 14.848 36.563  -22.223 1.00 41.95  ? 305 TRP B CZ3   1 
ATOM   5603 C  CH2   . TRP B 1 326 ? 15.831 35.580  -22.265 1.00 41.18  ? 305 TRP B CH2   1 
ATOM   5604 N  N     . TRP B 1 327 ? 12.967 37.182  -18.596 1.00 43.16  ? 306 TRP B N     1 
ATOM   5605 C  CA    . TRP B 1 327 ? 12.023 36.374  -19.429 1.00 40.83  ? 306 TRP B CA    1 
ATOM   5606 C  C     . TRP B 1 327 ? 10.573 36.598  -18.983 1.00 45.62  ? 306 TRP B C     1 
ATOM   5607 O  O     . TRP B 1 327 ? 9.653  36.450  -19.827 1.00 47.41  ? 306 TRP B O     1 
ATOM   5608 C  CB    . TRP B 1 327 ? 12.388 34.879  -19.395 1.00 37.44  ? 306 TRP B CB    1 
ATOM   5609 C  CG    . TRP B 1 327 ? 12.585 34.347  -18.014 1.00 33.41  ? 306 TRP B CG    1 
ATOM   5610 C  CD1   . TRP B 1 327 ? 11.641 33.796  -17.200 1.00 35.61  ? 306 TRP B CD1   1 
ATOM   5611 C  CD2   . TRP B 1 327 ? 13.793 34.410  -17.245 1.00 33.47  ? 306 TRP B CD2   1 
ATOM   5612 N  NE1   . TRP B 1 327 ? 12.188 33.500  -15.984 1.00 34.89  ? 306 TRP B NE1   1 
ATOM   5613 C  CE2   . TRP B 1 327 ? 13.503 33.872  -15.979 1.00 32.36  ? 306 TRP B CE2   1 
ATOM   5614 C  CE3   . TRP B 1 327 ? 15.092 34.857  -17.509 1.00 36.98  ? 306 TRP B CE3   1 
ATOM   5615 C  CZ2   . TRP B 1 327 ? 14.473 33.749  -14.987 1.00 34.38  ? 306 TRP B CZ2   1 
ATOM   5616 C  CZ3   . TRP B 1 327 ? 16.047 34.734  -16.526 1.00 37.47  ? 306 TRP B CZ3   1 
ATOM   5617 C  CH2   . TRP B 1 327 ? 15.741 34.190  -15.285 1.00 33.62  ? 306 TRP B CH2   1 
ATOM   5618 N  N     . ARG B 1 328 ? 10.365 36.922  -17.706 1.00 51.24  ? 307 ARG B N     1 
ATOM   5619 C  CA    . ARG B 1 328 ? 9.015  37.191  -17.134 1.00 52.68  ? 307 ARG B CA    1 
ATOM   5620 C  C     . ARG B 1 328 ? 8.288  38.278  -17.941 1.00 53.93  ? 307 ARG B C     1 
ATOM   5621 O  O     . ARG B 1 328 ? 7.108  38.051  -18.291 1.00 52.97  ? 307 ARG B O     1 
ATOM   5622 C  CB    . ARG B 1 328 ? 9.156  37.530  -15.649 1.00 51.50  ? 307 ARG B CB    1 
ATOM   5623 C  CG    . ARG B 1 328 ? 9.251  36.288  -14.777 1.00 52.15  ? 307 ARG B CG    1 
ATOM   5624 C  CD    . ARG B 1 328 ? 9.589  36.640  -13.352 1.00 55.42  ? 307 ARG B CD    1 
ATOM   5625 N  NE    . ARG B 1 328 ? 9.789  35.445  -12.550 1.00 57.31  ? 307 ARG B NE    1 
ATOM   5626 C  CZ    . ARG B 1 328 ? 10.023 35.436  -11.246 1.00 58.69  ? 307 ARG B CZ    1 
ATOM   5627 N  NH1   . ARG B 1 328 ? 10.096 36.578  -10.577 1.00 60.00  ? 307 ARG B NH1   1 
ATOM   5628 N  NH2   . ARG B 1 328 ? 10.195 34.285  -10.618 1.00 53.62  ? 307 ARG B NH2   1 
ATOM   5629 N  N     . ALA B 1 329 ? 8.970  39.383  -18.273 1.00 56.97  ? 308 ALA B N     1 
ATOM   5630 C  CA    . ALA B 1 329 ? 8.413  40.521  -19.050 1.00 58.32  ? 308 ALA B CA    1 
ATOM   5631 C  C     . ALA B 1 329 ? 8.029  40.077  -20.471 1.00 63.01  ? 308 ALA B C     1 
ATOM   5632 O  O     . ALA B 1 329 ? 7.099  40.687  -21.044 1.00 65.91  ? 308 ALA B O     1 
ATOM   5633 C  CB    . ALA B 1 329 ? 9.397  41.667  -19.077 1.00 58.02  ? 308 ALA B CB    1 
ATOM   5634 N  N     . GLU B 1 330 ? 8.689  39.050  -21.026 1.00 56.94  ? 309 GLU B N     1 
ATOM   5635 C  CA    . GLU B 1 330 ? 8.395  38.524  -22.389 1.00 53.01  ? 309 GLU B CA    1 
ATOM   5636 C  C     . GLU B 1 330 ? 7.194  37.566  -22.350 1.00 50.44  ? 309 GLU B C     1 
ATOM   5637 O  O     . GLU B 1 330 ? 6.766  37.112  -23.445 1.00 44.05  ? 309 GLU B O     1 
ATOM   5638 C  CB    . GLU B 1 330 ? 9.633  37.820  -22.958 1.00 62.86  ? 309 GLU B CB    1 
ATOM   5639 C  CG    . GLU B 1 330 ? 10.862 38.715  -23.048 1.00 62.85  ? 309 GLU B CG    1 
ATOM   5640 C  CD    . GLU B 1 330 ? 10.564 40.058  -23.700 1.00 68.79  ? 309 GLU B CD    1 
ATOM   5641 O  OE1   . GLU B 1 330 ? 9.959  40.048  -24.806 1.00 60.45  ? 309 GLU B OE1   1 
ATOM   5642 O  OE2   . GLU B 1 330 ? 10.888 41.110  -23.083 1.00 65.84  ? 309 GLU B OE2   1 
ATOM   5643 N  N     . GLY B 1 331 ? 6.661  37.270  -21.154 1.00 46.81  ? 310 GLY B N     1 
ATOM   5644 C  CA    . GLY B 1 331 ? 5.588  36.271  -20.956 1.00 43.14  ? 310 GLY B CA    1 
ATOM   5645 C  C     . GLY B 1 331 ? 6.103  34.825  -21.012 1.00 45.61  ? 310 GLY B C     1 
ATOM   5646 O  O     . GLY B 1 331 ? 5.303  33.935  -21.302 1.00 44.74  ? 310 GLY B O     1 
ATOM   5647 N  N     . LEU B 1 332 ? 7.381  34.579  -20.713 1.00 42.21  ? 311 LEU B N     1 
ATOM   5648 C  CA    . LEU B 1 332 ? 7.961  33.214  -20.641 1.00 44.32  ? 311 LEU B CA    1 
ATOM   5649 C  C     . LEU B 1 332 ? 8.004  32.761  -19.180 1.00 41.52  ? 311 LEU B C     1 
ATOM   5650 O  O     . LEU B 1 332 ? 8.227  33.619  -18.332 1.00 39.38  ? 311 LEU B O     1 
ATOM   5651 C  CB    . LEU B 1 332 ? 9.373  33.243  -21.228 1.00 44.14  ? 311 LEU B CB    1 
ATOM   5652 C  CG    . LEU B 1 332 ? 9.464  33.558  -22.718 1.00 49.27  ? 311 LEU B CG    1 
ATOM   5653 C  CD1   . LEU B 1 332 ? 10.905 33.885  -23.093 1.00 49.46  ? 311 LEU B CD1   1 
ATOM   5654 C  CD2   . LEU B 1 332 ? 8.920  32.408  -23.558 1.00 47.31  ? 311 LEU B CD2   1 
ATOM   5655 N  N     . SER B 1 333 ? 7.879  31.452  -18.924 1.00 39.83  ? 312 SER B N     1 
ATOM   5656 C  CA    . SER B 1 333 ? 8.035  30.825  -17.586 1.00 36.75  ? 312 SER B CA    1 
ATOM   5657 C  C     . SER B 1 333 ? 9.505  30.700  -17.187 1.00 37.09  ? 312 SER B C     1 
ATOM   5658 O  O     . SER B 1 333 ? 9.776  30.600  -15.955 1.00 34.26  ? 312 SER B O     1 
ATOM   5659 C  CB    . SER B 1 333 ? 7.397  29.474  -17.564 1.00 40.49  ? 312 SER B CB    1 
ATOM   5660 O  OG    . SER B 1 333 ? 7.987  28.628  -18.532 1.00 41.90  ? 312 SER B OG    1 
ATOM   5661 N  N     . GLY B 1 334 ? 10.419 30.619  -18.167 1.00 37.81  ? 313 GLY B N     1 
ATOM   5662 C  CA    . GLY B 1 334 ? 11.834 30.242  -17.936 1.00 36.80  ? 313 GLY B CA    1 
ATOM   5663 C  C     . GLY B 1 334 ? 12.064 28.740  -18.107 1.00 39.13  ? 313 GLY B C     1 
ATOM   5664 O  O     . GLY B 1 334 ? 13.251 28.323  -18.094 1.00 38.75  ? 313 GLY B O     1 
ATOM   5665 N  N     . THR B 1 335 ? 10.976 27.964  -18.268 1.00 38.04  ? 314 THR B N     1 
ATOM   5666 C  CA    . THR B 1 335 ? 10.977 26.522  -18.621 1.00 38.60  ? 314 THR B CA    1 
ATOM   5667 C  C     . THR B 1 335 ? 11.126 26.369  -20.141 1.00 38.87  ? 314 THR B C     1 
ATOM   5668 O  O     . THR B 1 335 ? 10.318 26.957  -20.896 1.00 39.26  ? 314 THR B O     1 
ATOM   5669 C  CB    . THR B 1 335 ? 9.714  25.807  -18.123 1.00 39.00  ? 314 THR B CB    1 
ATOM   5670 O  OG1   . THR B 1 335 ? 9.859  25.575  -16.724 1.00 46.51  ? 314 THR B OG1   1 
ATOM   5671 C  CG2   . THR B 1 335 ? 9.460  24.480  -18.795 1.00 39.94  ? 314 THR B CG2   1 
ATOM   5672 N  N     . VAL B 1 336 ? 12.153 25.635  -20.560 1.00 34.12  ? 315 VAL B N     1 
ATOM   5673 C  CA    . VAL B 1 336 ? 12.293 25.117  -21.943 1.00 39.20  ? 315 VAL B CA    1 
ATOM   5674 C  C     . VAL B 1 336 ? 12.367 23.587  -21.837 1.00 39.06  ? 315 VAL B C     1 
ATOM   5675 O  O     . VAL B 1 336 ? 12.859 23.074  -20.818 1.00 42.97  ? 315 VAL B O     1 
ATOM   5676 C  CB    . VAL B 1 336 ? 13.515 25.742  -22.648 1.00 38.57  ? 315 VAL B CB    1 
ATOM   5677 C  CG1   . VAL B 1 336 ? 13.655 27.216  -22.315 1.00 39.56  ? 315 VAL B CG1   1 
ATOM   5678 C  CG2   . VAL B 1 336 ? 14.810 25.018  -22.316 1.00 42.25  ? 315 VAL B CG2   1 
ATOM   5679 N  N     . LEU B 1 337 ? 11.875 22.884  -22.843 1.00 41.26  ? 316 LEU B N     1 
ATOM   5680 C  CA    . LEU B 1 337 ? 11.951 21.407  -22.928 1.00 45.16  ? 316 LEU B CA    1 
ATOM   5681 C  C     . LEU B 1 337 ? 12.510 21.052  -24.310 1.00 41.36  ? 316 LEU B C     1 
ATOM   5682 O  O     . LEU B 1 337 ? 11.949 21.551  -25.286 1.00 44.99  ? 316 LEU B O     1 
ATOM   5683 C  CB    . LEU B 1 337 ? 10.527 20.903  -22.711 1.00 49.33  ? 316 LEU B CB    1 
ATOM   5684 C  CG    . LEU B 1 337 ? 10.399 19.464  -22.245 1.00 56.17  ? 316 LEU B CG    1 
ATOM   5685 C  CD1   . LEU B 1 337 ? 10.763 19.335  -20.775 1.00 57.73  ? 316 LEU B CD1   1 
ATOM   5686 C  CD2   . LEU B 1 337 ? 8.981  18.995  -22.482 1.00 61.13  ? 316 LEU B CD2   1 
ATOM   5687 N  N     . CYS B 1 338 ? 13.601 20.287  -24.388 1.00 42.78  ? 317 CYS B N     1 
ATOM   5688 C  CA    . CYS B 1 338 ? 14.391 20.073  -25.633 1.00 42.16  ? 317 CYS B CA    1 
ATOM   5689 C  C     . CYS B 1 338 ? 14.858 18.625  -25.757 1.00 42.80  ? 317 CYS B C     1 
ATOM   5690 O  O     . CYS B 1 338 ? 15.998 18.309  -25.402 1.00 40.93  ? 317 CYS B O     1 
ATOM   5691 C  CB    . CYS B 1 338 ? 15.622 20.972  -25.646 1.00 48.80  ? 317 CYS B CB    1 
ATOM   5692 S  SG    . CYS B 1 338 ? 15.245 22.738  -25.551 1.00 52.79  ? 317 CYS B SG    1 
ATOM   5693 N  N     . PRO B 1 339 ? 14.010 17.703  -26.275 1.00 43.55  ? 318 PRO B N     1 
ATOM   5694 C  CA    . PRO B 1 339 ? 14.389 16.296  -26.418 1.00 44.98  ? 318 PRO B CA    1 
ATOM   5695 C  C     . PRO B 1 339 ? 15.692 16.021  -27.192 1.00 46.16  ? 318 PRO B C     1 
ATOM   5696 O  O     . PRO B 1 339 ? 16.317 15.030  -26.881 1.00 45.67  ? 318 PRO B O     1 
ATOM   5697 C  CB    . PRO B 1 339 ? 13.215 15.629  -27.160 1.00 44.19  ? 318 PRO B CB    1 
ATOM   5698 C  CG    . PRO B 1 339 ? 12.255 16.746  -27.534 1.00 44.37  ? 318 PRO B CG    1 
ATOM   5699 C  CD    . PRO B 1 339 ? 12.620 17.951  -26.688 1.00 44.60  ? 318 PRO B CD    1 
ATOM   5700 N  N     . ASP B 1 340 ? 16.077 16.891  -28.134 1.00 48.78  ? 319 ASP B N     1 
ATOM   5701 C  CA    . ASP B 1 340 ? 17.200 16.685  -29.090 1.00 53.97  ? 319 ASP B CA    1 
ATOM   5702 C  C     . ASP B 1 340 ? 18.431 17.491  -28.643 1.00 51.84  ? 319 ASP B C     1 
ATOM   5703 O  O     . ASP B 1 340 ? 19.353 17.642  -29.478 1.00 51.43  ? 319 ASP B O     1 
ATOM   5704 C  CB    . ASP B 1 340 ? 16.759 17.072  -30.509 1.00 61.53  ? 319 ASP B CB    1 
ATOM   5705 C  CG    . ASP B 1 340 ? 17.723 16.721  -31.640 1.00 75.25  ? 319 ASP B CG    1 
ATOM   5706 O  OD1   . ASP B 1 340 ? 18.091 15.526  -31.739 1.00 84.90  ? 319 ASP B OD1   1 
ATOM   5707 O  OD2   . ASP B 1 340 ? 18.088 17.650  -32.436 1.00 75.44  ? 319 ASP B OD2   1 
ATOM   5708 N  N     . GLU B 1 341 ? 18.467 17.993  -27.398 1.00 47.47  ? 320 GLU B N     1 
ATOM   5709 C  CA    . GLU B 1 341 ? 19.565 18.874  -26.893 1.00 48.40  ? 320 GLU B CA    1 
ATOM   5710 C  C     . GLU B 1 341 ? 20.256 18.218  -25.695 1.00 44.03  ? 320 GLU B C     1 
ATOM   5711 O  O     . GLU B 1 341 ? 19.718 17.299  -25.103 1.00 45.84  ? 320 GLU B O     1 
ATOM   5712 C  CB    . GLU B 1 341 ? 19.021 20.267  -26.535 1.00 50.44  ? 320 GLU B CB    1 
ATOM   5713 C  CG    . GLU B 1 341 ? 18.433 21.035  -27.716 1.00 48.63  ? 320 GLU B CG    1 
ATOM   5714 C  CD    . GLU B 1 341 ? 19.461 21.414  -28.763 1.00 49.16  ? 320 GLU B CD    1 
ATOM   5715 O  OE1   . GLU B 1 341 ? 20.637 21.546  -28.388 1.00 49.71  ? 320 GLU B OE1   1 
ATOM   5716 O  OE2   . GLU B 1 341 ? 19.089 21.565  -29.944 1.00 48.50  ? 320 GLU B OE2   1 
ATOM   5717 N  N     . PRO B 1 342 ? 21.476 18.651  -25.306 1.00 45.67  ? 321 PRO B N     1 
ATOM   5718 C  CA    . PRO B 1 342 ? 22.133 18.152  -24.097 1.00 49.66  ? 321 PRO B CA    1 
ATOM   5719 C  C     . PRO B 1 342 ? 21.429 18.534  -22.784 1.00 46.02  ? 321 PRO B C     1 
ATOM   5720 O  O     . PRO B 1 342 ? 21.436 17.725  -21.884 1.00 53.64  ? 321 PRO B O     1 
ATOM   5721 C  CB    . PRO B 1 342 ? 23.540 18.772  -24.102 1.00 47.70  ? 321 PRO B CB    1 
ATOM   5722 C  CG    . PRO B 1 342 ? 23.706 19.370  -25.483 1.00 49.19  ? 321 PRO B CG    1 
ATOM   5723 C  CD    . PRO B 1 342 ? 22.314 19.619  -26.028 1.00 47.32  ? 321 PRO B CD    1 
ATOM   5724 N  N     . ILE B 1 343 ? 20.875 19.741  -22.703 1.00 44.84  ? 322 ILE B N     1 
ATOM   5725 C  CA    . ILE B 1 343 ? 20.029 20.225  -21.569 1.00 48.00  ? 322 ILE B CA    1 
ATOM   5726 C  C     . ILE B 1 343 ? 18.622 19.629  -21.741 1.00 49.17  ? 322 ILE B C     1 
ATOM   5727 O  O     . ILE B 1 343 ? 17.957 19.963  -22.743 1.00 53.45  ? 322 ILE B O     1 
ATOM   5728 C  CB    . ILE B 1 343 ? 19.990 21.768  -21.553 1.00 49.35  ? 322 ILE B CB    1 
ATOM   5729 C  CG1   . ILE B 1 343 ? 21.379 22.383  -21.714 1.00 54.58  ? 322 ILE B CG1   1 
ATOM   5730 C  CG2   . ILE B 1 343 ? 19.304 22.302  -20.317 1.00 57.47  ? 322 ILE B CG2   1 
ATOM   5731 C  CD1   . ILE B 1 343 ? 22.421 21.781  -20.828 1.00 53.73  ? 322 ILE B CD1   1 
ATOM   5732 N  N     . GLY B 1 344 ? 18.153 18.834  -20.781 1.00 48.84  ? 323 GLY B N     1 
ATOM   5733 C  CA    . GLY B 1 344 ? 16.775 18.298  -20.763 1.00 56.11  ? 323 GLY B CA    1 
ATOM   5734 C  C     . GLY B 1 344 ? 15.699 19.349  -20.464 1.00 53.43  ? 323 GLY B C     1 
ATOM   5735 O  O     . GLY B 1 344 ? 14.819 19.583  -21.340 1.00 60.84  ? 323 GLY B O     1 
ATOM   5736 N  N     . VAL B 1 345 ? 15.704 19.922  -19.263 1.00 44.45  ? 324 VAL B N     1 
ATOM   5737 C  CA    . VAL B 1 345 ? 14.575 20.760  -18.768 1.00 44.45  ? 324 VAL B CA    1 
ATOM   5738 C  C     . VAL B 1 345 ? 15.111 21.892  -17.881 1.00 41.96  ? 324 VAL B C     1 
ATOM   5739 O  O     . VAL B 1 345 ? 16.189 21.723  -17.279 1.00 41.96  ? 324 VAL B O     1 
ATOM   5740 C  CB    . VAL B 1 345 ? 13.556 19.887  -18.020 1.00 43.45  ? 324 VAL B CB    1 
ATOM   5741 C  CG1   . VAL B 1 345 ? 14.094 19.449  -16.661 1.00 46.29  ? 324 VAL B CG1   1 
ATOM   5742 C  CG2   . VAL B 1 345 ? 12.212 20.596  -17.880 1.00 44.45  ? 324 VAL B CG2   1 
ATOM   5743 N  N     . THR B 1 346 ? 14.397 23.019  -17.812 1.00 37.93  ? 325 THR B N     1 
ATOM   5744 C  CA    . THR B 1 346 ? 14.838 24.203  -17.023 1.00 38.14  ? 325 THR B CA    1 
ATOM   5745 C  C     . THR B 1 346 ? 13.667 24.773  -16.214 1.00 35.81  ? 325 THR B C     1 
ATOM   5746 O  O     . THR B 1 346 ? 12.513 24.544  -16.574 1.00 33.18  ? 325 THR B O     1 
ATOM   5747 C  CB    . THR B 1 346 ? 15.439 25.294  -17.916 1.00 36.32  ? 325 THR B CB    1 
ATOM   5748 O  OG1   . THR B 1 346 ? 14.384 25.765  -18.764 1.00 36.31  ? 325 THR B OG1   1 
ATOM   5749 C  CG2   . THR B 1 346 ? 16.609 24.803  -18.739 1.00 36.22  ? 325 THR B CG2   1 
ATOM   5750 N  N     . PHE B 1 347 ? 13.985 25.495  -15.147 1.00 34.47  ? 326 PHE B N     1 
ATOM   5751 C  CA    . PHE B 1 347 ? 13.006 26.132  -14.245 1.00 34.43  ? 326 PHE B CA    1 
ATOM   5752 C  C     . PHE B 1 347 ? 13.507 27.528  -13.892 1.00 35.46  ? 326 PHE B C     1 
ATOM   5753 O  O     . PHE B 1 347 ? 14.714 27.720  -13.789 1.00 37.24  ? 326 PHE B O     1 
ATOM   5754 C  CB    . PHE B 1 347 ? 12.806 25.290  -12.994 1.00 35.20  ? 326 PHE B CB    1 
ATOM   5755 C  CG    . PHE B 1 347 ? 12.082 23.989  -13.220 1.00 37.65  ? 326 PHE B CG    1 
ATOM   5756 C  CD1   . PHE B 1 347 ? 12.780 22.835  -13.555 1.00 38.71  ? 326 PHE B CD1   1 
ATOM   5757 C  CD2   . PHE B 1 347 ? 10.711 23.905  -13.055 1.00 40.41  ? 326 PHE B CD2   1 
ATOM   5758 C  CE1   . PHE B 1 347 ? 12.117 21.628  -13.730 1.00 37.51  ? 326 PHE B CE1   1 
ATOM   5759 C  CE2   . PHE B 1 347 ? 10.046 22.701  -13.244 1.00 39.81  ? 326 PHE B CE2   1 
ATOM   5760 C  CZ    . PHE B 1 347 ? 10.748 21.569  -13.587 1.00 38.25  ? 326 PHE B CZ    1 
ATOM   5761 N  N     . ASP B 1 348 ? 12.582 28.471  -13.743 1.00 35.41  ? 327 ASP B N     1 
ATOM   5762 C  CA    . ASP B 1 348 ? 12.805 29.743  -13.015 1.00 33.95  ? 327 ASP B CA    1 
ATOM   5763 C  C     . ASP B 1 348 ? 13.245 29.434  -11.571 1.00 34.11  ? 327 ASP B C     1 
ATOM   5764 O  O     . ASP B 1 348 ? 12.418 28.895  -10.824 1.00 38.79  ? 327 ASP B O     1 
ATOM   5765 C  CB    . ASP B 1 348 ? 11.528 30.577  -13.019 1.00 33.26  ? 327 ASP B CB    1 
ATOM   5766 C  CG    . ASP B 1 348 ? 11.787 32.035  -12.723 1.00 33.83  ? 327 ASP B CG    1 
ATOM   5767 O  OD1   . ASP B 1 348 ? 12.758 32.325  -12.006 1.00 33.41  ? 327 ASP B OD1   1 
ATOM   5768 O  OD2   . ASP B 1 348 ? 10.997 32.862  -13.199 1.00 37.65  ? 327 ASP B OD2   1 
ATOM   5769 N  N     . GLY B 1 349 ? 14.480 29.777  -11.198 1.00 31.48  ? 328 GLY B N     1 
ATOM   5770 C  CA    . GLY B 1 349 ? 15.044 29.554  -9.855  1.00 32.10  ? 328 GLY B CA    1 
ATOM   5771 C  C     . GLY B 1 349 ? 15.146 30.836  -9.045  1.00 32.61  ? 328 GLY B C     1 
ATOM   5772 O  O     . GLY B 1 349 ? 15.795 30.817  -8.004  1.00 30.31  ? 328 GLY B O     1 
ATOM   5773 N  N     . THR B 1 350 ? 14.531 31.917  -9.517  1.00 36.08  ? 329 THR B N     1 
ATOM   5774 C  CA    . THR B 1 350 ? 14.559 33.267  -8.897  1.00 37.33  ? 329 THR B CA    1 
ATOM   5775 C  C     . THR B 1 350 ? 13.993 33.183  -7.481  1.00 33.84  ? 329 THR B C     1 
ATOM   5776 O  O     . THR B 1 350 ? 12.914 32.639  -7.299  1.00 30.07  ? 329 THR B O     1 
ATOM   5777 C  CB    . THR B 1 350 ? 13.762 34.243  -9.771  1.00 40.19  ? 329 THR B CB    1 
ATOM   5778 O  OG1   . THR B 1 350 ? 14.395 34.271  -11.057 1.00 39.53  ? 329 THR B OG1   1 
ATOM   5779 C  CG2   . THR B 1 350 ? 13.689 35.637  -9.184  1.00 39.88  ? 329 THR B CG2   1 
ATOM   5780 N  N     . PRO B 1 351 ? 14.689 33.709  -6.447  1.00 31.37  ? 330 PRO B N     1 
ATOM   5781 C  CA    . PRO B 1 351 ? 14.158 33.722  -5.082  1.00 36.36  ? 330 PRO B CA    1 
ATOM   5782 C  C     . PRO B 1 351 ? 13.042 34.753  -4.910  1.00 37.88  ? 330 PRO B C     1 
ATOM   5783 O  O     . PRO B 1 351 ? 12.858 35.614  -5.774  1.00 36.11  ? 330 PRO B O     1 
ATOM   5784 C  CB    . PRO B 1 351 ? 15.376 34.072  -4.208  1.00 38.19  ? 330 PRO B CB    1 
ATOM   5785 C  CG    . PRO B 1 351 ? 16.280 34.881  -5.134  1.00 36.95  ? 330 PRO B CG    1 
ATOM   5786 C  CD    . PRO B 1 351 ? 16.042 34.278  -6.512  1.00 35.22  ? 330 PRO B CD    1 
ATOM   5787 N  N     . PRO B 1 352 ? 12.265 34.676  -3.796  1.00 40.02  ? 331 PRO B N     1 
ATOM   5788 C  CA    . PRO B 1 352 ? 11.085 35.535  -3.595  1.00 41.38  ? 331 PRO B CA    1 
ATOM   5789 C  C     . PRO B 1 352 ? 11.322 37.053  -3.777  1.00 42.37  ? 331 PRO B C     1 
ATOM   5790 O  O     . PRO B 1 352 ? 10.431 37.734  -4.221  1.00 43.63  ? 331 PRO B O     1 
ATOM   5791 C  CB    . PRO B 1 352 ? 10.674 35.223  -2.141  1.00 38.58  ? 331 PRO B CB    1 
ATOM   5792 C  CG    . PRO B 1 352 ? 11.173 33.796  -1.908  1.00 37.00  ? 331 PRO B CG    1 
ATOM   5793 C  CD    . PRO B 1 352 ? 12.478 33.740  -2.673  1.00 36.54  ? 331 PRO B CD    1 
ATOM   5794 N  N     . ALA B 1 353 ? 12.509 37.557  -3.433  1.00 44.43  ? 332 ALA B N     1 
ATOM   5795 C  CA    . ALA B 1 353 ? 12.866 38.991  -3.580  1.00 43.41  ? 332 ALA B CA    1 
ATOM   5796 C  C     . ALA B 1 353 ? 12.725 39.423  -5.048  1.00 41.40  ? 332 ALA B C     1 
ATOM   5797 O  O     . ALA B 1 353 ? 12.589 40.636  -5.263  1.00 39.45  ? 332 ALA B O     1 
ATOM   5798 C  CB    . ALA B 1 353 ? 14.247 39.282  -3.023  1.00 36.28  ? 332 ALA B CB    1 
ATOM   5799 N  N     . GLY B 1 354 ? 12.761 38.487  -6.013  1.00 40.70  ? 333 GLY B N     1 
ATOM   5800 C  CA    . GLY B 1 354 ? 12.571 38.773  -7.454  1.00 37.07  ? 333 GLY B CA    1 
ATOM   5801 C  C     . GLY B 1 354 ? 13.883 39.070  -8.178  1.00 38.12  ? 333 GLY B C     1 
ATOM   5802 O  O     . GLY B 1 354 ? 13.871 39.181  -9.422  1.00 37.38  ? 333 GLY B O     1 
ATOM   5803 N  N     . THR B 1 355 ? 14.989 39.222  -7.448  1.00 40.10  ? 334 THR B N     1 
ATOM   5804 C  CA    . THR B 1 355 ? 16.366 39.299  -8.014  1.00 41.42  ? 334 THR B CA    1 
ATOM   5805 C  C     . THR B 1 355 ? 17.296 38.482  -7.119  1.00 44.21  ? 334 THR B C     1 
ATOM   5806 O  O     . THR B 1 355 ? 16.992 38.253  -5.947  1.00 45.87  ? 334 THR B O     1 
ATOM   5807 C  CB    . THR B 1 355 ? 16.868 40.751  -8.154  1.00 42.70  ? 334 THR B CB    1 
ATOM   5808 O  OG1   . THR B 1 355 ? 17.173 41.281  -6.865  1.00 44.13  ? 334 THR B OG1   1 
ATOM   5809 C  CG2   . THR B 1 355 ? 15.890 41.681  -8.853  1.00 42.21  ? 334 THR B CG2   1 
ATOM   5810 N  N     . PRO B 1 356 ? 18.440 37.979  -7.632  1.00 46.94  ? 335 PRO B N     1 
ATOM   5811 C  CA    . PRO B 1 356 ? 18.765 38.019  -9.063  1.00 43.05  ? 335 PRO B CA    1 
ATOM   5812 C  C     . PRO B 1 356 ? 17.852 37.093  -9.878  1.00 39.33  ? 335 PRO B C     1 
ATOM   5813 O  O     . PRO B 1 356 ? 17.151 36.315  -9.287  1.00 46.77  ? 335 PRO B O     1 
ATOM   5814 C  CB    . PRO B 1 356 ? 20.193 37.469  -9.099  1.00 43.56  ? 335 PRO B CB    1 
ATOM   5815 C  CG    . PRO B 1 356 ? 20.210 36.513  -7.933  1.00 48.76  ? 335 PRO B CG    1 
ATOM   5816 C  CD    . PRO B 1 356 ? 19.456 37.258  -6.847  1.00 47.21  ? 335 PRO B CD    1 
ATOM   5817 N  N     . GLY B 1 357 ? 17.854 37.210  -11.202 1.00 36.19  ? 336 GLY B N     1 
ATOM   5818 C  CA    . GLY B 1 357 ? 17.237 36.199  -12.073 1.00 34.52  ? 336 GLY B CA    1 
ATOM   5819 C  C     . GLY B 1 357 ? 18.082 34.930  -12.057 1.00 34.63  ? 336 GLY B C     1 
ATOM   5820 O  O     . GLY B 1 357 ? 19.315 35.062  -12.150 1.00 33.51  ? 336 GLY B O     1 
ATOM   5821 N  N     . ILE B 1 358 ? 17.456 33.752  -11.930 1.00 33.87  ? 337 ILE B N     1 
ATOM   5822 C  CA    . ILE B 1 358 ? 18.146 32.425  -12.032 1.00 35.94  ? 337 ILE B CA    1 
ATOM   5823 C  C     . ILE B 1 358 ? 17.334 31.521  -12.970 1.00 37.75  ? 337 ILE B C     1 
ATOM   5824 O  O     . ILE B 1 358 ? 16.077 31.462  -12.830 1.00 35.50  ? 337 ILE B O     1 
ATOM   5825 C  CB    . ILE B 1 358 ? 18.370 31.761  -10.657 1.00 35.26  ? 337 ILE B CB    1 
ATOM   5826 C  CG1   . ILE B 1 358 ? 19.071 32.705  -9.677  1.00 40.52  ? 337 ILE B CG1   1 
ATOM   5827 C  CG2   . ILE B 1 358 ? 19.138 30.448  -10.781 1.00 34.08  ? 337 ILE B CG2   1 
ATOM   5828 C  CD1   . ILE B 1 358 ? 19.337 32.102  -8.306  1.00 40.34  ? 337 ILE B CD1   1 
ATOM   5829 N  N     . VAL B 1 359 ? 18.026 30.875  -13.917 1.00 35.38  ? 338 VAL B N     1 
ATOM   5830 C  CA    . VAL B 1 359 ? 17.487 29.729  -14.693 1.00 35.99  ? 338 VAL B CA    1 
ATOM   5831 C  C     . VAL B 1 359 ? 18.194 28.473  -14.177 1.00 34.80  ? 338 VAL B C     1 
ATOM   5832 O  O     . VAL B 1 359 ? 19.397 28.419  -14.237 1.00 33.18  ? 338 VAL B O     1 
ATOM   5833 C  CB    . VAL B 1 359 ? 17.681 29.923  -16.205 1.00 40.01  ? 338 VAL B CB    1 
ATOM   5834 C  CG1   . VAL B 1 359 ? 17.202 28.705  -16.981 1.00 38.20  ? 338 VAL B CG1   1 
ATOM   5835 C  CG2   . VAL B 1 359 ? 17.006 31.201  -16.714 1.00 41.32  ? 338 VAL B CG2   1 
ATOM   5836 N  N     . THR B 1 360 ? 17.438 27.505  -13.688 1.00 36.34  ? 339 THR B N     1 
ATOM   5837 C  CA    . THR B 1 360 ? 17.935 26.243  -13.096 1.00 35.21  ? 339 THR B CA    1 
ATOM   5838 C  C     . THR B 1 360 ? 17.757 25.158  -14.151 1.00 35.23  ? 339 THR B C     1 
ATOM   5839 O  O     . THR B 1 360 ? 16.716 25.191  -14.838 1.00 38.11  ? 339 THR B O     1 
ATOM   5840 C  CB    . THR B 1 360 ? 17.205 25.894  -11.788 1.00 35.88  ? 339 THR B CB    1 
ATOM   5841 O  OG1   . THR B 1 360 ? 17.329 26.985  -10.875 1.00 36.01  ? 339 THR B OG1   1 
ATOM   5842 C  CG2   . THR B 1 360 ? 17.772 24.651  -11.135 1.00 36.91  ? 339 THR B CG2   1 
ATOM   5843 N  N     . GLY B 1 361 ? 18.726 24.250  -14.284 1.00 30.84  ? 340 GLY B N     1 
ATOM   5844 C  CA    . GLY B 1 361 ? 18.626 23.180  -15.284 1.00 31.44  ? 340 GLY B CA    1 
ATOM   5845 C  C     . GLY B 1 361 ? 19.582 22.044  -15.003 1.00 29.08  ? 340 GLY B C     1 
ATOM   5846 O  O     . GLY B 1 361 ? 20.313 22.129  -13.995 1.00 27.11  ? 340 GLY B O     1 
ATOM   5847 N  N     . PHE B 1 362 ? 19.526 21.018  -15.854 1.00 28.05  ? 341 PHE B N     1 
ATOM   5848 C  CA    . PHE B 1 362 ? 20.127 19.686  -15.624 1.00 31.12  ? 341 PHE B CA    1 
ATOM   5849 C  C     . PHE B 1 362 ? 20.681 19.139  -16.941 1.00 33.25  ? 341 PHE B C     1 
ATOM   5850 O  O     . PHE B 1 362 ? 19.978 19.215  -17.988 1.00 32.07  ? 341 PHE B O     1 
ATOM   5851 C  CB    . PHE B 1 362 ? 19.096 18.719  -15.035 1.00 31.91  ? 341 PHE B CB    1 
ATOM   5852 C  CG    . PHE B 1 362 ? 18.354 19.230  -13.823 1.00 35.56  ? 341 PHE B CG    1 
ATOM   5853 C  CD1   . PHE B 1 362 ? 17.204 19.993  -13.959 1.00 33.04  ? 341 PHE B CD1   1 
ATOM   5854 C  CD2   . PHE B 1 362 ? 18.803 18.950  -12.533 1.00 37.13  ? 341 PHE B CD2   1 
ATOM   5855 C  CE1   . PHE B 1 362 ? 16.536 20.467  -12.836 1.00 36.39  ? 341 PHE B CE1   1 
ATOM   5856 C  CE2   . PHE B 1 362 ? 18.135 19.440  -11.414 1.00 35.07  ? 341 PHE B CE2   1 
ATOM   5857 C  CZ    . PHE B 1 362 ? 17.005 20.198  -11.569 1.00 33.04  ? 341 PHE B CZ    1 
ATOM   5858 N  N     . PHE B 1 363 ? 21.906 18.601  -16.887 1.00 31.37  ? 342 PHE B N     1 
ATOM   5859 C  CA    . PHE B 1 363 ? 22.395 17.557  -17.820 1.00 31.03  ? 342 PHE B CA    1 
ATOM   5860 C  C     . PHE B 1 363 ? 22.065 16.201  -17.181 1.00 34.09  ? 342 PHE B C     1 
ATOM   5861 O  O     . PHE B 1 363 ? 22.441 15.963  -16.042 1.00 35.96  ? 342 PHE B O     1 
ATOM   5862 C  CB    . PHE B 1 363 ? 23.895 17.693  -18.080 1.00 31.16  ? 342 PHE B CB    1 
ATOM   5863 C  CG    . PHE B 1 363 ? 24.375 18.971  -18.732 1.00 32.06  ? 342 PHE B CG    1 
ATOM   5864 C  CD1   . PHE B 1 363 ? 24.560 20.134  -17.991 1.00 32.64  ? 342 PHE B CD1   1 
ATOM   5865 C  CD2   . PHE B 1 363 ? 24.764 18.975  -20.068 1.00 34.60  ? 342 PHE B CD2   1 
ATOM   5866 C  CE1   . PHE B 1 363 ? 25.080 21.288  -18.572 1.00 35.12  ? 342 PHE B CE1   1 
ATOM   5867 C  CE2   . PHE B 1 363 ? 25.298 20.121  -20.649 1.00 36.77  ? 342 PHE B CE2   1 
ATOM   5868 C  CZ    . PHE B 1 363 ? 25.453 21.281  -19.897 1.00 37.04  ? 342 PHE B CZ    1 
ATOM   5869 N  N     . GLU B 1 364 ? 21.364 15.330  -17.893 1.00 34.53  ? 343 GLU B N     1 
ATOM   5870 C  CA    . GLU B 1 364 ? 20.922 14.017  -17.382 1.00 34.51  ? 343 GLU B CA    1 
ATOM   5871 C  C     . GLU B 1 364 ? 21.599 12.907  -18.201 1.00 34.09  ? 343 GLU B C     1 
ATOM   5872 O  O     . GLU B 1 364 ? 21.709 13.069  -19.409 1.00 35.78  ? 343 GLU B O     1 
ATOM   5873 C  CB    . GLU B 1 364 ? 19.398 13.910  -17.514 1.00 40.08  ? 343 GLU B CB    1 
ATOM   5874 C  CG    . GLU B 1 364 ? 18.593 15.052  -16.897 1.00 41.23  ? 343 GLU B CG    1 
ATOM   5875 C  CD    . GLU B 1 364 ? 18.585 15.082  -15.383 1.00 40.22  ? 343 GLU B CD    1 
ATOM   5876 O  OE1   . GLU B 1 364 ? 19.374 14.337  -14.789 1.00 44.71  ? 343 GLU B OE1   1 
ATOM   5877 O  OE2   . GLU B 1 364 ? 17.793 15.850  -14.803 1.00 44.56  ? 343 GLU B OE2   1 
ATOM   5878 N  N     . GLY B 1 365 ? 22.006 11.802  -17.571 1.00 35.62  ? 344 GLY B N     1 
ATOM   5879 C  CA    . GLY B 1 365 ? 22.384 10.539  -18.254 1.00 36.37  ? 344 GLY B CA    1 
ATOM   5880 C  C     . GLY B 1 365 ? 23.637 10.702  -19.117 1.00 34.39  ? 344 GLY B C     1 
ATOM   5881 O  O     . GLY B 1 365 ? 24.618 11.266  -18.631 1.00 37.13  ? 344 GLY B O     1 
ATOM   5882 N  N     . PRO B 1 366 ? 23.623 10.279  -20.412 1.00 35.03  ? 345 PRO B N     1 
ATOM   5883 C  CA    . PRO B 1 366 ? 24.757 10.448  -21.323 1.00 34.68  ? 345 PRO B CA    1 
ATOM   5884 C  C     . PRO B 1 366 ? 25.242 11.892  -21.441 1.00 36.19  ? 345 PRO B C     1 
ATOM   5885 O  O     . PRO B 1 366 ? 26.418 12.080  -21.524 1.00 37.87  ? 345 PRO B O     1 
ATOM   5886 C  CB    . PRO B 1 366 ? 24.197 10.018  -22.688 1.00 33.69  ? 345 PRO B CB    1 
ATOM   5887 C  CG    . PRO B 1 366 ? 23.171 8.988   -22.323 1.00 36.45  ? 345 PRO B CG    1 
ATOM   5888 C  CD    . PRO B 1 366 ? 22.513 9.583   -21.092 1.00 38.59  ? 345 PRO B CD    1 
ATOM   5889 N  N     . ALA B 1 367 ? 24.318 12.855  -21.492 1.00 36.64  ? 346 ALA B N     1 
ATOM   5890 C  CA    . ALA B 1 367 ? 24.646 14.294  -21.601 1.00 35.27  ? 346 ALA B CA    1 
ATOM   5891 C  C     . ALA B 1 367 ? 25.434 14.769  -20.358 1.00 33.01  ? 346 ALA B C     1 
ATOM   5892 O  O     . ALA B 1 367 ? 26.299 15.669  -20.492 1.00 34.97  ? 346 ALA B O     1 
ATOM   5893 C  CB    . ALA B 1 367 ? 23.372 15.081  -21.817 1.00 34.32  ? 346 ALA B CB    1 
ATOM   5894 N  N     . ALA B 1 368 ? 25.156 14.213  -19.179 1.00 30.93  ? 347 ALA B N     1 
ATOM   5895 C  CA    . ALA B 1 368 ? 25.860 14.566  -17.921 1.00 31.63  ? 347 ALA B CA    1 
ATOM   5896 C  C     . ALA B 1 368 ? 27.266 13.964  -17.946 1.00 33.07  ? 347 ALA B C     1 
ATOM   5897 O  O     . ALA B 1 368 ? 28.217 14.643  -17.507 1.00 34.59  ? 347 ALA B O     1 
ATOM   5898 C  CB    . ALA B 1 368 ? 25.084 14.116  -16.705 1.00 30.17  ? 347 ALA B CB    1 
ATOM   5899 N  N     . VAL B 1 369 ? 27.409 12.742  -18.464 1.00 34.77  ? 348 VAL B N     1 
ATOM   5900 C  CA    . VAL B 1 369 ? 28.728 12.051  -18.501 1.00 34.40  ? 348 VAL B CA    1 
ATOM   5901 C  C     . VAL B 1 369 ? 29.644 12.823  -19.464 1.00 36.60  ? 348 VAL B C     1 
ATOM   5902 O  O     . VAL B 1 369 ? 30.802 13.109  -19.053 1.00 36.58  ? 348 VAL B O     1 
ATOM   5903 C  CB    . VAL B 1 369 ? 28.590 10.564  -18.875 1.00 34.76  ? 348 VAL B CB    1 
ATOM   5904 C  CG1   . VAL B 1 369 ? 29.958 9.899   -18.926 1.00 35.77  ? 348 VAL B CG1   1 
ATOM   5905 C  CG2   . VAL B 1 369 ? 27.673 9.828   -17.919 1.00 29.89  ? 348 VAL B CG2   1 
ATOM   5906 N  N     . ALA B 1 370 ? 29.129 13.245  -20.629 1.00 32.21  ? 349 ALA B N     1 
ATOM   5907 C  CA    . ALA B 1 370 ? 29.891 14.030  -21.631 1.00 36.01  ? 349 ALA B CA    1 
ATOM   5908 C  C     . ALA B 1 370 ? 30.269 15.404  -21.060 1.00 35.20  ? 349 ALA B C     1 
ATOM   5909 O  O     . ALA B 1 370 ? 31.426 15.792  -21.216 1.00 39.00  ? 349 ALA B O     1 
ATOM   5910 C  CB    . ALA B 1 370 ? 29.116 14.170  -22.918 1.00 36.29  ? 349 ALA B CB    1 
ATOM   5911 N  N     . ALA B 1 371 ? 29.333 16.134  -20.455 1.00 35.38  ? 350 ALA B N     1 
ATOM   5912 C  CA    . ALA B 1 371 ? 29.574 17.501  -19.920 1.00 36.19  ? 350 ALA B CA    1 
ATOM   5913 C  C     . ALA B 1 371 ? 30.446 17.463  -18.646 1.00 35.49  ? 350 ALA B C     1 
ATOM   5914 O  O     . ALA B 1 371 ? 31.196 18.415  -18.398 1.00 35.97  ? 350 ALA B O     1 
ATOM   5915 C  CB    . ALA B 1 371 ? 28.262 18.200  -19.686 1.00 36.64  ? 350 ALA B CB    1 
ATOM   5916 N  N     . GLY B 1 372 ? 30.424 16.376  -17.880 1.00 36.44  ? 351 GLY B N     1 
ATOM   5917 C  CA    . GLY B 1 372 ? 31.312 16.212  -16.711 1.00 34.85  ? 351 GLY B CA    1 
ATOM   5918 C  C     . GLY B 1 372 ? 32.766 16.087  -17.130 1.00 37.09  ? 351 GLY B C     1 
ATOM   5919 O  O     . GLY B 1 372 ? 33.651 16.338  -16.295 1.00 38.29  ? 351 GLY B O     1 
ATOM   5920 N  N     . ALA B 1 373 ? 33.035 15.741  -18.390 1.00 38.27  ? 352 ALA B N     1 
ATOM   5921 C  CA    . ALA B 1 373 ? 34.416 15.568  -18.899 1.00 40.81  ? 352 ALA B CA    1 
ATOM   5922 C  C     . ALA B 1 373 ? 35.007 16.925  -19.293 1.00 40.26  ? 352 ALA B C     1 
ATOM   5923 O  O     . ALA B 1 373 ? 36.212 16.999  -19.364 1.00 46.21  ? 352 ALA B O     1 
ATOM   5924 C  CB    . ALA B 1 373 ? 34.436 14.584  -20.036 1.00 41.68  ? 352 ALA B CB    1 
ATOM   5925 N  N     . ARG B 1 374 ? 34.165 17.943  -19.479 1.00 43.92  ? 353 ARG B N     1 
ATOM   5926 C  CA    . ARG B 1 374 ? 34.465 19.283  -20.044 1.00 43.81  ? 353 ARG B CA    1 
ATOM   5927 C  C     . ARG B 1 374 ? 34.640 20.255  -18.884 1.00 44.04  ? 353 ARG B C     1 
ATOM   5928 O  O     . ARG B 1 374 ? 34.338 19.846  -17.777 1.00 42.36  ? 353 ARG B O     1 
ATOM   5929 C  CB    . ARG B 1 374 ? 33.314 19.696  -20.971 1.00 50.56  ? 353 ARG B CB    1 
ATOM   5930 C  CG    . ARG B 1 374 ? 33.155 18.764  -22.170 1.00 57.00  ? 353 ARG B CG    1 
ATOM   5931 C  CD    . ARG B 1 374 ? 32.001 19.033  -23.128 1.00 64.40  ? 353 ARG B CD    1 
ATOM   5932 N  NE    . ARG B 1 374 ? 31.993 20.301  -23.869 1.00 72.31  ? 353 ARG B NE    1 
ATOM   5933 C  CZ    . ARG B 1 374 ? 32.941 20.738  -24.715 1.00 77.78  ? 353 ARG B CZ    1 
ATOM   5934 N  NH1   . ARG B 1 374 ? 34.051 20.047  -24.930 1.00 85.46  ? 353 ARG B NH1   1 
ATOM   5935 N  NH2   . ARG B 1 374 ? 32.783 21.890  -25.342 1.00 71.25  ? 353 ARG B NH2   1 
ATOM   5936 N  N     . THR B 1 375 ? 35.108 21.487  -19.117 1.00 42.24  ? 354 THR B N     1 
ATOM   5937 C  CA    . THR B 1 375 ? 35.334 22.492  -18.032 1.00 44.57  ? 354 THR B CA    1 
ATOM   5938 C  C     . THR B 1 375 ? 33.990 23.122  -17.641 1.00 40.61  ? 354 THR B C     1 
ATOM   5939 O  O     . THR B 1 375 ? 33.075 23.050  -18.458 1.00 36.59  ? 354 THR B O     1 
ATOM   5940 C  CB    . THR B 1 375 ? 36.362 23.557  -18.449 1.00 45.77  ? 354 THR B CB    1 
ATOM   5941 O  OG1   . THR B 1 375 ? 35.784 24.426  -19.428 1.00 46.16  ? 354 THR B OG1   1 
ATOM   5942 C  CG2   . THR B 1 375 ? 37.643 22.947  -18.983 1.00 42.61  ? 354 THR B CG2   1 
ATOM   5943 N  N     . ARG B 1 376 ? 33.888 23.732  -16.460 1.00 39.10  ? 355 ARG B N     1 
ATOM   5944 C  CA    . ARG B 1 376 ? 32.732 24.592  -16.084 1.00 47.14  ? 355 ARG B CA    1 
ATOM   5945 C  C     . ARG B 1 376 ? 32.421 25.583  -17.224 1.00 46.46  ? 355 ARG B C     1 
ATOM   5946 O  O     . ARG B 1 376 ? 31.231 25.751  -17.545 1.00 49.18  ? 355 ARG B O     1 
ATOM   5947 C  CB    . ARG B 1 376 ? 32.993 25.322  -14.761 1.00 49.52  ? 355 ARG B CB    1 
ATOM   5948 C  CG    . ARG B 1 376 ? 31.768 26.019  -14.181 1.00 51.95  ? 355 ARG B CG    1 
ATOM   5949 C  CD    . ARG B 1 376 ? 32.037 27.010  -13.043 1.00 61.00  ? 355 ARG B CD    1 
ATOM   5950 N  NE    . ARG B 1 376 ? 32.949 28.115  -13.359 1.00 63.84  ? 355 ARG B NE    1 
ATOM   5951 C  CZ    . ARG B 1 376 ? 32.623 29.285  -13.938 1.00 64.34  ? 355 ARG B CZ    1 
ATOM   5952 N  NH1   . ARG B 1 376 ? 31.385 29.570  -14.295 1.00 60.13  ? 355 ARG B NH1   1 
ATOM   5953 N  NH2   . ARG B 1 376 ? 33.563 30.184  -14.171 1.00 69.79  ? 355 ARG B NH2   1 
ATOM   5954 N  N     . GLU B 1 377 ? 33.437 26.198  -17.835 1.00 48.11  ? 356 GLU B N     1 
ATOM   5955 C  CA    . GLU B 1 377 ? 33.288 27.265  -18.872 1.00 51.20  ? 356 GLU B CA    1 
ATOM   5956 C  C     . GLU B 1 377 ? 32.719 26.656  -20.163 1.00 47.81  ? 356 GLU B C     1 
ATOM   5957 O  O     . GLU B 1 377 ? 31.854 27.292  -20.789 1.00 41.71  ? 356 GLU B O     1 
ATOM   5958 C  CB    . GLU B 1 377 ? 34.628 27.950  -19.177 1.00 59.48  ? 356 GLU B CB    1 
ATOM   5959 C  CG    . GLU B 1 377 ? 35.167 28.813  -18.044 1.00 69.03  ? 356 GLU B CG    1 
ATOM   5960 C  CD    . GLU B 1 377 ? 35.521 28.077  -16.753 1.00 78.93  ? 356 GLU B CD    1 
ATOM   5961 O  OE1   . GLU B 1 377 ? 36.195 27.014  -16.820 1.00 74.39  ? 356 GLU B OE1   1 
ATOM   5962 O  OE2   . GLU B 1 377 ? 35.110 28.556  -15.673 1.00 81.48  ? 356 GLU B OE2   1 
ATOM   5963 N  N     . GLU B 1 378 ? 33.182 25.469  -20.562 1.00 42.48  ? 357 GLU B N     1 
ATOM   5964 C  CA    . GLU B 1 378 ? 32.620 24.760  -21.744 1.00 43.55  ? 357 GLU B CA    1 
ATOM   5965 C  C     . GLU B 1 378 ? 31.135 24.447  -21.460 1.00 41.25  ? 357 GLU B C     1 
ATOM   5966 O  O     . GLU B 1 378 ? 30.300 24.725  -22.332 1.00 42.98  ? 357 GLU B O     1 
ATOM   5967 C  CB    . GLU B 1 378 ? 33.463 23.526  -22.088 1.00 43.32  ? 357 GLU B CB    1 
ATOM   5968 C  CG    . GLU B 1 378 ? 34.883 23.856  -22.549 1.00 44.87  ? 357 GLU B CG    1 
ATOM   5969 C  CD    . GLU B 1 378 ? 35.846 22.682  -22.714 1.00 47.75  ? 357 GLU B CD    1 
ATOM   5970 O  OE1   . GLU B 1 378 ? 35.729 21.684  -21.974 1.00 53.70  ? 357 GLU B OE1   1 
ATOM   5971 O  OE2   . GLU B 1 378 ? 36.734 22.769  -23.586 1.00 55.23  ? 357 GLU B OE2   1 
ATOM   5972 N  N     . ARG B 1 379 ? 30.811 23.945  -20.262 1.00 37.27  ? 358 ARG B N     1 
ATOM   5973 C  CA    . ARG B 1 379 ? 29.421 23.635  -19.835 1.00 36.53  ? 358 ARG B CA    1 
ATOM   5974 C  C     . ARG B 1 379 ? 28.588 24.924  -19.821 1.00 30.72  ? 358 ARG B C     1 
ATOM   5975 O  O     . ARG B 1 379 ? 27.505 24.902  -20.336 1.00 27.35  ? 358 ARG B O     1 
ATOM   5976 C  CB    . ARG B 1 379 ? 29.435 22.913  -18.487 1.00 37.93  ? 358 ARG B CB    1 
ATOM   5977 C  CG    . ARG B 1 379 ? 29.820 21.439  -18.586 1.00 39.12  ? 358 ARG B CG    1 
ATOM   5978 C  CD    . ARG B 1 379 ? 29.344 20.721  -17.342 1.00 40.24  ? 358 ARG B CD    1 
ATOM   5979 N  NE    . ARG B 1 379 ? 29.965 21.328  -16.170 1.00 40.58  ? 358 ARG B NE    1 
ATOM   5980 C  CZ    . ARG B 1 379 ? 31.099 20.931  -15.618 1.00 39.81  ? 358 ARG B CZ    1 
ATOM   5981 N  NH1   . ARG B 1 379 ? 31.759 19.896  -16.111 1.00 43.10  ? 358 ARG B NH1   1 
ATOM   5982 N  NH2   . ARG B 1 379 ? 31.553 21.553  -14.546 1.00 40.89  ? 358 ARG B NH2   1 
ATOM   5983 N  N     . ARG B 1 380 ? 29.121 26.043  -19.356 1.00 33.55  ? 359 ARG B N     1 
ATOM   5984 C  CA    . ARG B 1 380 ? 28.399 27.337  -19.448 1.00 38.73  ? 359 ARG B CA    1 
ATOM   5985 C  C     . ARG B 1 380 ? 28.021 27.655  -20.911 1.00 41.18  ? 359 ARG B C     1 
ATOM   5986 O  O     . ARG B 1 380 ? 26.866 28.072  -21.127 1.00 39.52  ? 359 ARG B O     1 
ATOM   5987 C  CB    . ARG B 1 380 ? 29.214 28.479  -18.840 1.00 43.30  ? 359 ARG B CB    1 
ATOM   5988 C  CG    . ARG B 1 380 ? 28.426 29.778  -18.799 1.00 49.12  ? 359 ARG B CG    1 
ATOM   5989 C  CD    . ARG B 1 380 ? 29.196 30.988  -18.320 1.00 58.91  ? 359 ARG B CD    1 
ATOM   5990 N  NE    . ARG B 1 380 ? 30.444 31.199  -19.027 1.00 64.93  ? 359 ARG B NE    1 
ATOM   5991 C  CZ    . ARG B 1 380 ? 30.549 31.521  -20.307 1.00 71.76  ? 359 ARG B CZ    1 
ATOM   5992 N  NH1   . ARG B 1 380 ? 29.471 31.654  -21.068 1.00 73.10  ? 359 ARG B NH1   1 
ATOM   5993 N  NH2   . ARG B 1 380 ? 31.752 31.693  -20.828 1.00 76.66  ? 359 ARG B NH2   1 
ATOM   5994 N  N     . ASP B 1 381 ? 28.938 27.486  -21.878 1.00 42.91  ? 360 ASP B N     1 
ATOM   5995 C  CA    . ASP B 1 381 ? 28.713 27.843  -23.312 1.00 41.67  ? 360 ASP B CA    1 
ATOM   5996 C  C     . ASP B 1 381 ? 27.591 26.949  -23.857 1.00 38.45  ? 360 ASP B C     1 
ATOM   5997 O  O     . ASP B 1 381 ? 26.743 27.433  -24.631 1.00 30.98  ? 360 ASP B O     1 
ATOM   5998 C  CB    . ASP B 1 381 ? 29.989 27.720  -24.164 1.00 44.36  ? 360 ASP B CB    1 
ATOM   5999 C  CG    . ASP B 1 381 ? 31.144 28.668  -23.818 1.00 52.44  ? 360 ASP B CG    1 
ATOM   6000 O  OD1   . ASP B 1 381 ? 30.905 29.731  -23.169 1.00 45.81  ? 360 ASP B OD1   1 
ATOM   6001 O  OD2   . ASP B 1 381 ? 32.301 28.340  -24.204 1.00 55.18  ? 360 ASP B OD2   1 
ATOM   6002 N  N     . VAL B 1 382 ? 27.583 25.668  -23.492 1.00 34.98  ? 361 VAL B N     1 
ATOM   6003 C  CA    . VAL B 1 382 ? 26.545 24.738  -24.022 1.00 35.91  ? 361 VAL B CA    1 
ATOM   6004 C  C     . VAL B 1 382 ? 25.172 25.190  -23.512 1.00 36.18  ? 361 VAL B C     1 
ATOM   6005 O  O     . VAL B 1 382 ? 24.236 25.269  -24.343 1.00 43.06  ? 361 VAL B O     1 
ATOM   6006 C  CB    . VAL B 1 382 ? 26.848 23.274  -23.664 1.00 36.16  ? 361 VAL B CB    1 
ATOM   6007 C  CG1   . VAL B 1 382 ? 25.618 22.408  -23.847 1.00 36.99  ? 361 VAL B CG1   1 
ATOM   6008 C  CG2   . VAL B 1 382 ? 28.016 22.740  -24.478 1.00 35.54  ? 361 VAL B CG2   1 
ATOM   6009 N  N     . VAL B 1 383 ? 25.034 25.452  -22.207 1.00 34.39  ? 362 VAL B N     1 
ATOM   6010 C  CA    . VAL B 1 383 ? 23.740 25.884  -21.597 1.00 37.38  ? 362 VAL B CA    1 
ATOM   6011 C  C     . VAL B 1 383 ? 23.262 27.184  -22.266 1.00 34.75  ? 362 VAL B C     1 
ATOM   6012 O  O     . VAL B 1 383 ? 22.091 27.241  -22.673 1.00 31.09  ? 362 VAL B O     1 
ATOM   6013 C  CB    . VAL B 1 383 ? 23.845 26.054  -20.066 1.00 40.34  ? 362 VAL B CB    1 
ATOM   6014 C  CG1   . VAL B 1 383 ? 22.644 26.797  -19.491 1.00 37.62  ? 362 VAL B CG1   1 
ATOM   6015 C  CG2   . VAL B 1 383 ? 24.029 24.716  -19.353 1.00 38.55  ? 362 VAL B CG2   1 
ATOM   6016 N  N     . VAL B 1 384 ? 24.117 28.208  -22.351 1.00 39.23  ? 363 VAL B N     1 
ATOM   6017 C  CA    . VAL B 1 384 ? 23.725 29.533  -22.911 1.00 41.32  ? 363 VAL B CA    1 
ATOM   6018 C  C     . VAL B 1 384 ? 23.335 29.408  -24.401 1.00 37.61  ? 363 VAL B C     1 
ATOM   6019 O  O     . VAL B 1 384 ? 22.368 30.075  -24.789 1.00 35.16  ? 363 VAL B O     1 
ATOM   6020 C  CB    . VAL B 1 384 ? 24.793 30.619  -22.673 1.00 51.98  ? 363 VAL B CB    1 
ATOM   6021 C  CG1   . VAL B 1 384 ? 26.149 30.249  -23.248 1.00 67.16  ? 363 VAL B CG1   1 
ATOM   6022 C  CG2   . VAL B 1 384 ? 24.350 31.957  -23.248 1.00 54.29  ? 363 VAL B CG2   1 
ATOM   6023 N  N     . ASP B 1 385 ? 24.007 28.583  -25.218 1.00 38.02  ? 364 ASP B N     1 
ATOM   6024 C  CA    . ASP B 1 385 ? 23.589 28.358  -26.632 1.00 43.57  ? 364 ASP B CA    1 
ATOM   6025 C  C     . ASP B 1 385 ? 22.128 27.876  -26.692 1.00 41.51  ? 364 ASP B C     1 
ATOM   6026 O  O     . ASP B 1 385 ? 21.345 28.485  -27.439 1.00 44.38  ? 364 ASP B O     1 
ATOM   6027 C  CB    . ASP B 1 385 ? 24.480 27.380  -27.399 1.00 50.55  ? 364 ASP B CB    1 
ATOM   6028 C  CG    . ASP B 1 385 ? 23.888 26.984  -28.757 1.00 68.22  ? 364 ASP B CG    1 
ATOM   6029 O  OD1   . ASP B 1 385 ? 23.694 27.900  -29.631 1.00 78.39  ? 364 ASP B OD1   1 
ATOM   6030 O  OD2   . ASP B 1 385 ? 23.586 25.769  -28.946 1.00 69.92  ? 364 ASP B OD2   1 
ATOM   6031 N  N     . VAL B 1 386 ? 21.764 26.829  -25.941 1.00 39.93  ? 365 VAL B N     1 
ATOM   6032 C  CA    . VAL B 1 386 ? 20.363 26.299  -25.886 1.00 37.23  ? 365 VAL B CA    1 
ATOM   6033 C  C     . VAL B 1 386 ? 19.401 27.419  -25.455 1.00 33.96  ? 365 VAL B C     1 
ATOM   6034 O  O     . VAL B 1 386 ? 18.358 27.570  -26.103 1.00 31.85  ? 365 VAL B O     1 
ATOM   6035 C  CB    . VAL B 1 386 ? 20.219 25.073  -24.968 1.00 37.94  ? 365 VAL B CB    1 
ATOM   6036 C  CG1   . VAL B 1 386 ? 18.768 24.601  -24.927 1.00 40.43  ? 365 VAL B CG1   1 
ATOM   6037 C  CG2   . VAL B 1 386 ? 21.151 23.940  -25.386 1.00 38.62  ? 365 VAL B CG2   1 
ATOM   6038 N  N     . LEU B 1 387 ? 19.707 28.167  -24.393 1.00 35.68  ? 366 LEU B N     1 
ATOM   6039 C  CA    . LEU B 1 387 ? 18.766 29.187  -23.856 1.00 35.11  ? 366 LEU B CA    1 
ATOM   6040 C  C     . LEU B 1 387 ? 18.583 30.326  -24.863 1.00 37.65  ? 366 LEU B C     1 
ATOM   6041 O  O     . LEU B 1 387 ? 17.461 30.853  -24.929 1.00 40.36  ? 366 LEU B O     1 
ATOM   6042 C  CB    . LEU B 1 387 ? 19.261 29.736  -22.516 1.00 36.09  ? 366 LEU B CB    1 
ATOM   6043 C  CG    . LEU B 1 387 ? 19.315 28.740  -21.356 1.00 36.50  ? 366 LEU B CG    1 
ATOM   6044 C  CD1   . LEU B 1 387 ? 19.845 29.399  -20.099 1.00 35.41  ? 366 LEU B CD1   1 
ATOM   6045 C  CD2   . LEU B 1 387 ? 17.962 28.102  -21.108 1.00 38.48  ? 366 LEU B CD2   1 
ATOM   6046 N  N     . ALA B 1 388 ? 19.624 30.711  -25.604 1.00 37.72  ? 367 ALA B N     1 
ATOM   6047 C  CA    . ALA B 1 388 ? 19.557 31.818  -26.591 1.00 41.26  ? 367 ALA B CA    1 
ATOM   6048 C  C     . ALA B 1 388 ? 18.591 31.429  -27.710 1.00 43.37  ? 367 ALA B C     1 
ATOM   6049 O  O     . ALA B 1 388 ? 17.898 32.325  -28.218 1.00 38.76  ? 367 ALA B O     1 
ATOM   6050 C  CB    . ALA B 1 388 ? 20.930 32.127  -27.145 1.00 41.77  ? 367 ALA B CB    1 
ATOM   6051 N  N     . ARG B 1 389 ? 18.540 30.135  -28.064 1.00 43.31  ? 368 ARG B N     1 
ATOM   6052 C  CA    . ARG B 1 389 ? 17.730 29.636  -29.207 1.00 42.35  ? 368 ARG B CA    1 
ATOM   6053 C  C     . ARG B 1 389 ? 16.267 29.467  -28.804 1.00 43.29  ? 368 ARG B C     1 
ATOM   6054 O  O     . ARG B 1 389 ? 15.458 29.260  -29.724 1.00 49.46  ? 368 ARG B O     1 
ATOM   6055 C  CB    . ARG B 1 389 ? 18.276 28.312  -29.750 1.00 47.57  ? 368 ARG B CB    1 
ATOM   6056 C  CG    . ARG B 1 389 ? 19.256 28.516  -30.895 1.00 52.24  ? 368 ARG B CG    1 
ATOM   6057 C  CD    . ARG B 1 389 ? 19.670 27.258  -31.613 1.00 53.30  ? 368 ARG B CD    1 
ATOM   6058 N  NE    . ARG B 1 389 ? 20.546 26.457  -30.777 1.00 55.58  ? 368 ARG B NE    1 
ATOM   6059 C  CZ    . ARG B 1 389 ? 20.239 25.251  -30.292 1.00 61.65  ? 368 ARG B CZ    1 
ATOM   6060 N  NH1   . ARG B 1 389 ? 19.071 24.693  -30.578 1.00 61.12  ? 368 ARG B NH1   1 
ATOM   6061 N  NH2   . ARG B 1 389 ? 21.112 24.599  -29.536 1.00 54.68  ? 368 ARG B NH2   1 
ATOM   6062 N  N     . THR B 1 390 ? 15.955 29.494  -27.502 1.00 38.95  ? 369 THR B N     1 
ATOM   6063 C  CA    . THR B 1 390 ? 14.635 29.093  -26.940 1.00 38.09  ? 369 THR B CA    1 
ATOM   6064 C  C     . THR B 1 390 ? 14.023 30.265  -26.167 1.00 37.62  ? 369 THR B C     1 
ATOM   6065 O  O     . THR B 1 390 ? 12.853 30.600  -26.421 1.00 40.27  ? 369 THR B O     1 
ATOM   6066 C  CB    . THR B 1 390 ? 14.749 27.838  -26.058 1.00 41.50  ? 369 THR B CB    1 
ATOM   6067 O  OG1   . THR B 1 390 ? 15.853 27.923  -25.141 1.00 36.97  ? 369 THR B OG1   1 
ATOM   6068 C  CG2   . THR B 1 390 ? 14.881 26.570  -26.884 1.00 41.98  ? 369 THR B CG2   1 
ATOM   6069 N  N     . LEU B 1 391 ? 14.752 30.833  -25.204 1.00 42.00  ? 370 LEU B N     1 
ATOM   6070 C  CA    . LEU B 1 391 ? 14.252 31.979  -24.397 1.00 39.42  ? 370 LEU B CA    1 
ATOM   6071 C  C     . LEU B 1 391 ? 14.522 33.280  -25.171 1.00 41.04  ? 370 LEU B C     1 
ATOM   6072 O  O     . LEU B 1 391 ? 13.707 34.178  -25.056 1.00 39.94  ? 370 LEU B O     1 
ATOM   6073 C  CB    . LEU B 1 391 ? 14.906 31.962  -23.016 1.00 38.80  ? 370 LEU B CB    1 
ATOM   6074 C  CG    . LEU B 1 391 ? 14.538 30.780  -22.115 1.00 39.90  ? 370 LEU B CG    1 
ATOM   6075 C  CD1   . LEU B 1 391 ? 15.166 30.944  -20.735 1.00 43.48  ? 370 LEU B CD1   1 
ATOM   6076 C  CD2   . LEU B 1 391 ? 13.038 30.624  -21.984 1.00 40.69  ? 370 LEU B CD2   1 
ATOM   6077 N  N     . GLY B 1 392 ? 15.603 33.337  -25.959 1.00 40.79  ? 371 GLY B N     1 
ATOM   6078 C  CA    . GLY B 1 392 ? 15.938 34.486  -26.824 1.00 47.86  ? 371 GLY B CA    1 
ATOM   6079 C  C     . GLY B 1 392 ? 17.329 35.024  -26.553 1.00 44.38  ? 371 GLY B C     1 
ATOM   6080 O  O     . GLY B 1 392 ? 18.002 34.501  -25.646 1.00 46.73  ? 371 GLY B O     1 
ATOM   6081 N  N     . GLU B 1 393 ? 17.723 36.063  -27.286 1.00 50.15  ? 372 GLU B N     1 
ATOM   6082 C  CA    . GLU B 1 393 ? 19.126 36.557  -27.373 1.00 51.09  ? 372 GLU B CA    1 
ATOM   6083 C  C     . GLU B 1 393 ? 19.600 37.089  -26.003 1.00 43.24  ? 372 GLU B C     1 
ATOM   6084 O  O     . GLU B 1 393 ? 20.808 36.995  -25.731 1.00 40.53  ? 372 GLU B O     1 
ATOM   6085 C  CB    . GLU B 1 393 ? 19.255 37.555  -28.535 1.00 54.15  ? 372 GLU B CB    1 
ATOM   6086 C  CG    . GLU B 1 393 ? 20.700 37.933  -28.893 1.00 65.98  ? 372 GLU B CG    1 
ATOM   6087 C  CD    . GLU B 1 393 ? 21.594 36.936  -29.645 1.00 76.42  ? 372 GLU B CD    1 
ATOM   6088 O  OE1   . GLU B 1 393 ? 21.191 35.765  -29.839 1.00 84.39  ? 372 GLU B OE1   1 
ATOM   6089 O  OE2   . GLU B 1 393 ? 22.721 37.338  -30.045 1.00 73.64  ? 372 GLU B OE2   1 
ATOM   6090 N  N     . ARG B 1 394 ? 18.707 37.545  -25.127 1.00 41.82  ? 373 ARG B N     1 
ATOM   6091 C  CA    . ARG B 1 394 ? 19.091 38.146  -23.821 1.00 42.57  ? 373 ARG B CA    1 
ATOM   6092 C  C     . ARG B 1 394 ? 19.665 37.084  -22.851 1.00 41.72  ? 373 ARG B C     1 
ATOM   6093 O  O     . ARG B 1 394 ? 20.254 37.478  -21.802 1.00 46.31  ? 373 ARG B O     1 
ATOM   6094 C  CB    . ARG B 1 394 ? 17.887 38.915  -23.277 1.00 52.21  ? 373 ARG B CB    1 
ATOM   6095 C  CG    . ARG B 1 394 ? 18.238 39.897  -22.171 1.00 66.06  ? 373 ARG B CG    1 
ATOM   6096 C  CD    . ARG B 1 394 ? 17.315 41.106  -22.123 1.00 68.10  ? 373 ARG B CD    1 
ATOM   6097 N  NE    . ARG B 1 394 ? 17.266 41.651  -20.766 1.00 74.83  ? 373 ARG B NE    1 
ATOM   6098 C  CZ    . ARG B 1 394 ? 16.365 42.533  -20.326 1.00 73.26  ? 373 ARG B CZ    1 
ATOM   6099 N  NH1   . ARG B 1 394 ? 15.436 43.003  -21.144 1.00 70.69  ? 373 ARG B NH1   1 
ATOM   6100 N  NH2   . ARG B 1 394 ? 16.392 42.932  -19.063 1.00 72.05  ? 373 ARG B NH2   1 
ATOM   6101 N  N     . ALA B 1 395 ? 19.600 35.795  -23.198 1.00 38.50  ? 374 ALA B N     1 
ATOM   6102 C  CA    . ALA B 1 395 ? 20.226 34.675  -22.459 1.00 42.29  ? 374 ALA B CA    1 
ATOM   6103 C  C     . ALA B 1 395 ? 21.750 34.820  -22.393 1.00 40.32  ? 374 ALA B C     1 
ATOM   6104 O  O     . ALA B 1 395 ? 22.361 34.110  -21.554 1.00 39.32  ? 374 ALA B O     1 
ATOM   6105 C  CB    . ALA B 1 395 ? 19.860 33.357  -23.100 1.00 44.07  ? 374 ALA B CB    1 
ATOM   6106 N  N     . ARG B 1 396 ? 22.349 35.659  -23.248 1.00 41.59  ? 375 ARG B N     1 
ATOM   6107 C  CA    . ARG B 1 396 ? 23.828 35.816  -23.359 1.00 43.80  ? 375 ARG B CA    1 
ATOM   6108 C  C     . ARG B 1 396 ? 24.339 36.882  -22.378 1.00 44.67  ? 375 ARG B C     1 
ATOM   6109 O  O     . ARG B 1 396 ? 25.539 36.873  -22.057 1.00 42.40  ? 375 ARG B O     1 
ATOM   6110 C  CB    . ARG B 1 396 ? 24.229 36.125  -24.804 1.00 47.57  ? 375 ARG B CB    1 
ATOM   6111 C  CG    . ARG B 1 396 ? 23.863 35.017  -25.786 1.00 48.37  ? 375 ARG B CG    1 
ATOM   6112 C  CD    . ARG B 1 396 ? 24.502 35.138  -27.164 1.00 45.84  ? 375 ARG B CD    1 
ATOM   6113 N  NE    . ARG B 1 396 ? 24.208 33.938  -27.945 1.00 44.38  ? 375 ARG B NE    1 
ATOM   6114 C  CZ    . ARG B 1 396 ? 24.832 32.763  -27.824 1.00 44.47  ? 375 ARG B CZ    1 
ATOM   6115 N  NH1   . ARG B 1 396 ? 25.821 32.599  -26.957 1.00 47.43  ? 375 ARG B NH1   1 
ATOM   6116 N  NH2   . ARG B 1 396 ? 24.474 31.750  -28.595 1.00 45.47  ? 375 ARG B NH2   1 
ATOM   6117 N  N     . ASP B 1 397 ? 23.471 37.751  -21.874 1.00 51.53  ? 376 ASP B N     1 
ATOM   6118 C  CA    . ASP B 1 397 ? 23.846 38.755  -20.845 1.00 52.05  ? 376 ASP B CA    1 
ATOM   6119 C  C     . ASP B 1 397 ? 23.921 38.061  -19.470 1.00 44.98  ? 376 ASP B C     1 
ATOM   6120 O  O     . ASP B 1 397 ? 23.181 38.433  -18.574 1.00 47.56  ? 376 ASP B O     1 
ATOM   6121 C  CB    . ASP B 1 397 ? 22.879 39.943  -20.909 1.00 63.83  ? 376 ASP B CB    1 
ATOM   6122 C  CG    . ASP B 1 397 ? 23.541 41.289  -20.668 1.00 74.39  ? 376 ASP B CG    1 
ATOM   6123 O  OD1   . ASP B 1 397 ? 24.688 41.314  -20.121 1.00 68.25  ? 376 ASP B OD1   1 
ATOM   6124 O  OD2   . ASP B 1 397 ? 22.906 42.306  -21.033 1.00 89.12  ? 376 ASP B OD2   1 
ATOM   6125 N  N     . VAL B 1 398 ? 24.844 37.118  -19.305 1.00 46.06  ? 377 VAL B N     1 
ATOM   6126 C  CA    . VAL B 1 398 ? 24.997 36.251  -18.105 1.00 44.96  ? 377 VAL B CA    1 
ATOM   6127 C  C     . VAL B 1 398 ? 25.873 36.950  -17.071 1.00 46.62  ? 377 VAL B C     1 
ATOM   6128 O  O     . VAL B 1 398 ? 27.008 37.300  -17.425 1.00 47.64  ? 377 VAL B O     1 
ATOM   6129 C  CB    . VAL B 1 398 ? 25.614 34.896  -18.491 1.00 48.28  ? 377 VAL B CB    1 
ATOM   6130 C  CG1   . VAL B 1 398 ? 26.186 34.160  -17.283 1.00 47.09  ? 377 VAL B CG1   1 
ATOM   6131 C  CG2   . VAL B 1 398 ? 24.596 34.036  -19.226 1.00 50.01  ? 377 VAL B CG2   1 
ATOM   6132 N  N     . ARG B 1 399 ? 25.398 37.053  -15.824 1.00 49.04  ? 378 ARG B N     1 
ATOM   6133 C  CA    . ARG B 1 399 ? 26.166 37.643  -14.694 1.00 49.11  ? 378 ARG B CA    1 
ATOM   6134 C  C     . ARG B 1 399 ? 27.080 36.557  -14.110 1.00 47.64  ? 378 ARG B C     1 
ATOM   6135 O  O     . ARG B 1 399 ? 28.243 36.852  -13.827 1.00 45.96  ? 378 ARG B O     1 
ATOM   6136 C  CB    . ARG B 1 399 ? 25.238 38.263  -13.644 1.00 54.29  ? 378 ARG B CB    1 
ATOM   6137 C  CG    . ARG B 1 399 ? 25.980 38.765  -12.412 1.00 68.42  ? 378 ARG B CG    1 
ATOM   6138 C  CD    . ARG B 1 399 ? 25.575 40.152  -11.942 1.00 78.32  ? 378 ARG B CD    1 
ATOM   6139 N  NE    . ARG B 1 399 ? 25.577 40.232  -10.483 1.00 85.16  ? 378 ARG B NE    1 
ATOM   6140 C  CZ    . ARG B 1 399 ? 24.515 40.049  -9.686  1.00 87.29  ? 378 ARG B CZ    1 
ATOM   6141 N  NH1   . ARG B 1 399 ? 23.319 39.786  -10.189 1.00 79.81  ? 378 ARG B NH1   1 
ATOM   6142 N  NH2   . ARG B 1 399 ? 24.658 40.137  -8.373  1.00 88.01  ? 378 ARG B NH2   1 
ATOM   6143 N  N     . ASP B 1 400 ? 26.594 35.325  -13.965 1.00 45.88  ? 379 ASP B N     1 
ATOM   6144 C  CA    . ASP B 1 400 ? 27.439 34.218  -13.450 1.00 43.71  ? 379 ASP B CA    1 
ATOM   6145 C  C     . ASP B 1 400 ? 26.838 32.854  -13.812 1.00 39.54  ? 379 ASP B C     1 
ATOM   6146 O  O     . ASP B 1 400 ? 25.692 32.769  -14.237 1.00 33.43  ? 379 ASP B O     1 
ATOM   6147 C  CB    . ASP B 1 400 ? 27.644 34.366  -11.940 1.00 49.28  ? 379 ASP B CB    1 
ATOM   6148 C  CG    . ASP B 1 400 ? 28.861 33.633  -11.405 1.00 45.69  ? 379 ASP B CG    1 
ATOM   6149 O  OD1   . ASP B 1 400 ? 29.675 33.214  -12.223 1.00 45.25  ? 379 ASP B OD1   1 
ATOM   6150 O  OD2   . ASP B 1 400 ? 28.953 33.459  -10.180 1.00 47.70  ? 379 ASP B OD2   1 
ATOM   6151 N  N     . TYR B 1 401 ? 27.630 31.812  -13.638 1.00 37.91  ? 380 TYR B N     1 
ATOM   6152 C  CA    . TYR B 1 401 ? 27.229 30.420  -13.916 1.00 39.61  ? 380 TYR B CA    1 
ATOM   6153 C  C     . TYR B 1 401 ? 27.800 29.572  -12.782 1.00 37.64  ? 380 TYR B C     1 
ATOM   6154 O  O     . TYR B 1 401 ? 29.017 29.625  -12.596 1.00 37.45  ? 380 TYR B O     1 
ATOM   6155 C  CB    . TYR B 1 401 ? 27.730 29.981  -15.299 1.00 36.01  ? 380 TYR B CB    1 
ATOM   6156 C  CG    . TYR B 1 401 ? 27.428 28.534  -15.590 1.00 35.11  ? 380 TYR B CG    1 
ATOM   6157 C  CD1   . TYR B 1 401 ? 26.184 28.151  -16.062 1.00 32.23  ? 380 TYR B CD1   1 
ATOM   6158 C  CD2   . TYR B 1 401 ? 28.367 27.541  -15.357 1.00 31.97  ? 380 TYR B CD2   1 
ATOM   6159 C  CE1   . TYR B 1 401 ? 25.889 26.823  -16.324 1.00 31.95  ? 380 TYR B CE1   1 
ATOM   6160 C  CE2   . TYR B 1 401 ? 28.089 26.206  -15.620 1.00 32.66  ? 380 TYR B CE2   1 
ATOM   6161 C  CZ    . TYR B 1 401 ? 26.838 25.846  -16.088 1.00 31.33  ? 380 TYR B CZ    1 
ATOM   6162 O  OH    . TYR B 1 401 ? 26.526 24.543  -16.319 1.00 32.05  ? 380 TYR B OH    1 
ATOM   6163 N  N     . ILE B 1 402 ? 26.951 28.851  -12.048 1.00 37.98  ? 381 ILE B N     1 
ATOM   6164 C  CA    . ILE B 1 402 ? 27.368 27.885  -10.988 1.00 41.34  ? 381 ILE B CA    1 
ATOM   6165 C  C     . ILE B 1 402 ? 26.803 26.512  -11.360 1.00 38.85  ? 381 ILE B C     1 
ATOM   6166 O  O     . ILE B 1 402 ? 25.616 26.469  -11.681 1.00 36.73  ? 381 ILE B O     1 
ATOM   6167 C  CB    . ILE B 1 402 ? 26.863 28.381  -9.619  1.00 45.90  ? 381 ILE B CB    1 
ATOM   6168 C  CG1   . ILE B 1 402 ? 27.581 29.668  -9.201  1.00 51.77  ? 381 ILE B CG1   1 
ATOM   6169 C  CG2   . ILE B 1 402 ? 26.991 27.302  -8.562  1.00 45.16  ? 381 ILE B CG2   1 
ATOM   6170 C  CD1   . ILE B 1 402 ? 26.657 30.804  -8.814  1.00 53.32  ? 381 ILE B CD1   1 
ATOM   6171 N  N     . ASP B 1 403 ? 27.605 25.440  -11.336 1.00 39.96  ? 382 ASP B N     1 
ATOM   6172 C  CA    . ASP B 1 403 ? 27.072 24.059  -11.512 1.00 37.44  ? 382 ASP B CA    1 
ATOM   6173 C  C     . ASP B 1 403 ? 27.774 23.066  -10.591 1.00 36.16  ? 382 ASP B C     1 
ATOM   6174 O  O     . ASP B 1 403 ? 28.688 23.474  -9.860  1.00 33.58  ? 382 ASP B O     1 
ATOM   6175 C  CB    . ASP B 1 403 ? 27.053 23.645  -12.986 1.00 41.75  ? 382 ASP B CB    1 
ATOM   6176 C  CG    . ASP B 1 403 ? 28.370 23.277  -13.649 1.00 43.35  ? 382 ASP B CG    1 
ATOM   6177 O  OD1   . ASP B 1 403 ? 29.388 23.199  -12.928 1.00 41.53  ? 382 ASP B OD1   1 
ATOM   6178 O  OD2   . ASP B 1 403 ? 28.346 23.070  -14.914 1.00 37.34  ? 382 ASP B OD2   1 
ATOM   6179 N  N     . ARG B 1 404 ? 27.314 21.809  -10.600 1.00 35.04  ? 383 ARG B N     1 
ATOM   6180 C  CA    . ARG B 1 404 ? 27.850 20.729  -9.743  1.00 32.86  ? 383 ARG B CA    1 
ATOM   6181 C  C     . ARG B 1 404 ? 27.634 19.371  -10.430 1.00 36.07  ? 383 ARG B C     1 
ATOM   6182 O  O     . ARG B 1 404 ? 26.462 19.015  -10.688 1.00 33.98  ? 383 ARG B O     1 
ATOM   6183 C  CB    . ARG B 1 404 ? 27.153 20.785  -8.378  1.00 35.82  ? 383 ARG B CB    1 
ATOM   6184 C  CG    . ARG B 1 404 ? 27.397 19.578  -7.482  1.00 38.67  ? 383 ARG B CG    1 
ATOM   6185 C  CD    . ARG B 1 404 ? 28.798 19.521  -6.939  1.00 43.09  ? 383 ARG B CD    1 
ATOM   6186 N  NE    . ARG B 1 404 ? 29.134 20.623  -6.030  1.00 43.44  ? 383 ARG B NE    1 
ATOM   6187 C  CZ    . ARG B 1 404 ? 28.916 20.621  -4.715  1.00 48.51  ? 383 ARG B CZ    1 
ATOM   6188 N  NH1   . ARG B 1 404 ? 28.302 19.606  -4.117  1.00 51.88  ? 383 ARG B NH1   1 
ATOM   6189 N  NH2   . ARG B 1 404 ? 29.296 21.657  -4.001  1.00 44.29  ? 383 ARG B NH2   1 
ATOM   6190 N  N     . ASP B 1 405 ? 28.717 18.636  -10.691 1.00 33.64  ? 384 ASP B N     1 
ATOM   6191 C  CA    . ASP B 1 405 ? 28.662 17.245  -11.193 1.00 39.60  ? 384 ASP B CA    1 
ATOM   6192 C  C     . ASP B 1 405 ? 28.649 16.329  -9.962  1.00 37.18  ? 384 ASP B C     1 
ATOM   6193 O  O     . ASP B 1 405 ? 29.682 16.242  -9.296  1.00 41.52  ? 384 ASP B O     1 
ATOM   6194 C  CB    . ASP B 1 405 ? 29.811 16.935  -12.170 1.00 38.46  ? 384 ASP B CB    1 
ATOM   6195 C  CG    . ASP B 1 405 ? 29.775 15.509  -12.724 1.00 42.45  ? 384 ASP B CG    1 
ATOM   6196 O  OD1   . ASP B 1 405 ? 28.891 14.688  -12.280 1.00 42.85  ? 384 ASP B OD1   1 
ATOM   6197 O  OD2   . ASP B 1 405 ? 30.604 15.219  -13.613 1.00 42.50  ? 384 ASP B OD2   1 
ATOM   6198 N  N     . TRP B 1 406 ? 27.519 15.695  -9.655  1.00 33.75  ? 385 TRP B N     1 
ATOM   6199 C  CA    . TRP B 1 406 ? 27.392 14.847  -8.436  1.00 34.96  ? 385 TRP B CA    1 
ATOM   6200 C  C     . TRP B 1 406 ? 28.105 13.502  -8.638  1.00 33.13  ? 385 TRP B C     1 
ATOM   6201 O  O     . TRP B 1 406 ? 28.448 12.861  -7.631  1.00 32.84  ? 385 TRP B O     1 
ATOM   6202 C  CB    . TRP B 1 406 ? 25.924 14.689  -8.039  1.00 35.43  ? 385 TRP B CB    1 
ATOM   6203 C  CG    . TRP B 1 406 ? 25.438 15.942  -7.379  1.00 36.87  ? 385 TRP B CG    1 
ATOM   6204 C  CD1   . TRP B 1 406 ? 24.879 17.038  -7.977  1.00 33.58  ? 385 TRP B CD1   1 
ATOM   6205 C  CD2   . TRP B 1 406 ? 25.582 16.266  -5.987  1.00 34.70  ? 385 TRP B CD2   1 
ATOM   6206 N  NE1   . TRP B 1 406 ? 24.625 18.004  -7.046  1.00 33.30  ? 385 TRP B NE1   1 
ATOM   6207 C  CE2   . TRP B 1 406 ? 25.044 17.559  -5.813  1.00 35.61  ? 385 TRP B CE2   1 
ATOM   6208 C  CE3   . TRP B 1 406 ? 26.087 15.578  -4.877  1.00 35.30  ? 385 TRP B CE3   1 
ATOM   6209 C  CZ2   . TRP B 1 406 ? 25.015 18.179  -4.561  1.00 34.63  ? 385 TRP B CZ2   1 
ATOM   6210 C  CZ3   . TRP B 1 406 ? 26.061 16.193  -3.646  1.00 34.10  ? 385 TRP B CZ3   1 
ATOM   6211 C  CH2   . TRP B 1 406 ? 25.523 17.474  -3.491  1.00 34.73  ? 385 TRP B CH2   1 
ATOM   6212 N  N     . SER B 1 407 ? 28.367 13.115  -9.883  1.00 31.25  ? 386 SER B N     1 
ATOM   6213 C  CA    . SER B 1 407 ? 29.206 11.935  -10.209 1.00 31.85  ? 386 SER B CA    1 
ATOM   6214 C  C     . SER B 1 407 ? 30.643 12.178  -9.745  1.00 30.46  ? 386 SER B C     1 
ATOM   6215 O  O     . SER B 1 407 ? 31.261 11.213  -9.311  1.00 30.28  ? 386 SER B O     1 
ATOM   6216 C  CB    . SER B 1 407 ? 29.145 11.616  -11.670 1.00 33.85  ? 386 SER B CB    1 
ATOM   6217 O  OG    . SER B 1 407 ? 27.864 11.126  -12.027 1.00 32.41  ? 386 SER B OG    1 
ATOM   6218 N  N     . ALA B 1 408 ? 31.128 13.431  -9.777  1.00 30.52  ? 387 ALA B N     1 
ATOM   6219 C  CA    . ALA B 1 408 ? 32.503 13.825  -9.365  1.00 29.53  ? 387 ALA B CA    1 
ATOM   6220 C  C     . ALA B 1 408 ? 32.650 13.956  -7.839  1.00 30.10  ? 387 ALA B C     1 
ATOM   6221 O  O     . ALA B 1 408 ? 33.791 13.980  -7.409  1.00 32.91  ? 387 ALA B O     1 
ATOM   6222 C  CB    . ALA B 1 408 ? 32.915 15.107  -10.052 1.00 30.15  ? 387 ALA B CB    1 
ATOM   6223 N  N     . GLU B 1 409 ? 31.555 14.046  -7.056  1.00 32.46  ? 388 GLU B N     1 
ATOM   6224 C  CA    . GLU B 1 409 ? 31.556 14.067  -5.557  1.00 30.63  ? 388 GLU B CA    1 
ATOM   6225 C  C     . GLU B 1 409 ? 31.914 12.681  -5.014  1.00 34.24  ? 388 GLU B C     1 
ATOM   6226 O  O     . GLU B 1 409 ? 31.141 11.730  -5.164  1.00 30.49  ? 388 GLU B O     1 
ATOM   6227 C  CB    . GLU B 1 409 ? 30.185 14.467  -5.022  1.00 33.08  ? 388 GLU B CB    1 
ATOM   6228 C  CG    . GLU B 1 409 ? 29.819 15.917  -5.309  1.00 35.29  ? 388 GLU B CG    1 
ATOM   6229 C  CD    . GLU B 1 409 ? 30.607 16.906  -4.461  1.00 41.16  ? 388 GLU B CD    1 
ATOM   6230 O  OE1   . GLU B 1 409 ? 30.702 16.661  -3.231  1.00 43.99  ? 388 GLU B OE1   1 
ATOM   6231 O  OE2   . GLU B 1 409 ? 31.153 17.889  -5.024  1.00 44.22  ? 388 GLU B OE2   1 
ATOM   6232 N  N     . PRO B 1 410 ? 33.094 12.522  -4.367  1.00 34.18  ? 389 PRO B N     1 
ATOM   6233 C  CA    . PRO B 1 410 ? 33.547 11.215  -3.892  1.00 32.31  ? 389 PRO B CA    1 
ATOM   6234 C  C     . PRO B 1 410 ? 32.633 10.617  -2.819  1.00 33.52  ? 389 PRO B C     1 
ATOM   6235 O  O     . PRO B 1 410 ? 32.611 9.364   -2.680  1.00 29.88  ? 389 PRO B O     1 
ATOM   6236 C  CB    . PRO B 1 410 ? 34.957 11.437  -3.330  1.00 34.35  ? 389 PRO B CB    1 
ATOM   6237 C  CG    . PRO B 1 410 ? 35.155 12.946  -3.281  1.00 34.80  ? 389 PRO B CG    1 
ATOM   6238 C  CD    . PRO B 1 410 ? 34.078 13.585  -4.131  1.00 33.14  ? 389 PRO B CD    1 
ATOM   6239 N  N     . TRP B 1 411 ? 31.870 11.475  -2.125  1.00 31.67  ? 390 TRP B N     1 
ATOM   6240 C  CA    . TRP B 1 411 ? 31.004 11.018  -1.003  1.00 32.37  ? 390 TRP B CA    1 
ATOM   6241 C  C     . TRP B 1 411 ? 29.554 10.878  -1.460  1.00 30.41  ? 390 TRP B C     1 
ATOM   6242 O  O     . TRP B 1 411 ? 28.692 10.638  -0.604  1.00 29.56  ? 390 TRP B O     1 
ATOM   6243 C  CB    . TRP B 1 411 ? 31.215 11.872  0.258   1.00 31.59  ? 390 TRP B CB    1 
ATOM   6244 C  CG    . TRP B 1 411 ? 32.624 11.756  0.761   1.00 31.96  ? 390 TRP B CG    1 
ATOM   6245 C  CD1   . TRP B 1 411 ? 33.574 12.736  0.841   1.00 34.28  ? 390 TRP B CD1   1 
ATOM   6246 C  CD2   . TRP B 1 411 ? 33.274 10.541  1.184   1.00 31.25  ? 390 TRP B CD2   1 
ATOM   6247 N  NE1   . TRP B 1 411 ? 34.757 12.218  1.307   1.00 34.63  ? 390 TRP B NE1   1 
ATOM   6248 C  CE2   . TRP B 1 411 ? 34.607 10.870  1.500   1.00 34.16  ? 390 TRP B CE2   1 
ATOM   6249 C  CE3   . TRP B 1 411 ? 32.860 9.213   1.301   1.00 32.62  ? 390 TRP B CE3   1 
ATOM   6250 C  CZ2   . TRP B 1 411 ? 35.522 9.909   1.931   1.00 36.23  ? 390 TRP B CZ2   1 
ATOM   6251 C  CZ3   . TRP B 1 411 ? 33.761 8.263   1.730   1.00 32.50  ? 390 TRP B CZ3   1 
ATOM   6252 C  CH2   . TRP B 1 411 ? 35.068 8.613   2.051   1.00 33.41  ? 390 TRP B CH2   1 
ATOM   6253 N  N     . THR B 1 412 ? 29.317 10.879  -2.773  1.00 32.15  ? 391 THR B N     1 
ATOM   6254 C  CA    . THR B 1 412 ? 27.990 10.569  -3.371  1.00 30.77  ? 391 THR B CA    1 
ATOM   6255 C  C     . THR B 1 412 ? 28.130 9.624   -4.556  1.00 30.17  ? 391 THR B C     1 
ATOM   6256 O  O     . THR B 1 412 ? 27.404 8.614   -4.575  1.00 33.04  ? 391 THR B O     1 
ATOM   6257 C  CB    . THR B 1 412 ? 27.257 11.811  -3.876  1.00 30.46  ? 391 THR B CB    1 
ATOM   6258 O  OG1   . THR B 1 412 ? 27.259 12.779  -2.833  1.00 30.50  ? 391 THR B OG1   1 
ATOM   6259 C  CG2   . THR B 1 412 ? 25.841 11.479  -4.276  1.00 30.35  ? 391 THR B CG2   1 
ATOM   6260 N  N     . ARG B 1 413 ? 28.966 10.001  -5.529  1.00 31.02  ? 392 ARG B N     1 
ATOM   6261 C  CA    . ARG B 1 413 ? 29.233 9.266   -6.799  1.00 31.61  ? 392 ARG B CA    1 
ATOM   6262 C  C     . ARG B 1 413 ? 27.946 9.107   -7.617  1.00 30.46  ? 392 ARG B C     1 
ATOM   6263 O  O     . ARG B 1 413 ? 27.782 8.067   -8.264  1.00 31.67  ? 392 ARG B O     1 
ATOM   6264 C  CB    . ARG B 1 413 ? 29.947 7.940   -6.518  1.00 32.18  ? 392 ARG B CB    1 
ATOM   6265 C  CG    . ARG B 1 413 ? 31.374 8.101   -6.015  1.00 34.53  ? 392 ARG B CG    1 
ATOM   6266 C  CD    . ARG B 1 413 ? 32.177 9.013   -6.932  1.00 38.24  ? 392 ARG B CD    1 
ATOM   6267 N  NE    . ARG B 1 413 ? 33.632 8.867   -6.884  1.00 40.94  ? 392 ARG B NE    1 
ATOM   6268 C  CZ    . ARG B 1 413 ? 34.493 9.387   -7.768  1.00 43.69  ? 392 ARG B CZ    1 
ATOM   6269 N  NH1   . ARG B 1 413 ? 34.068 10.111  -8.790  1.00 45.79  ? 392 ARG B NH1   1 
ATOM   6270 N  NH2   . ARG B 1 413 ? 35.791 9.191   -7.623  1.00 49.90  ? 392 ARG B NH2   1 
ATOM   6271 N  N     . GLY B 1 414 ? 27.136 10.164  -7.701  1.00 31.75  ? 393 GLY B N     1 
ATOM   6272 C  CA    . GLY B 1 414 ? 25.974 10.219  -8.610  1.00 35.70  ? 393 GLY B CA    1 
ATOM   6273 C  C     . GLY B 1 414 ? 24.650 10.552  -7.923  1.00 36.55  ? 393 GLY B C     1 
ATOM   6274 O  O     . GLY B 1 414 ? 24.350 10.030  -6.833  1.00 39.99  ? 393 GLY B O     1 
ATOM   6275 N  N     . CYS B 1 415 ? 23.867 11.401  -8.577  1.00 38.68  ? 394 CYS B N     1 
ATOM   6276 C  CA    . CYS B 1 415 ? 22.509 11.822  -8.165  1.00 38.54  ? 394 CYS B CA    1 
ATOM   6277 C  C     . CYS B 1 415 ? 21.563 11.363  -9.266  1.00 35.73  ? 394 CYS B C     1 
ATOM   6278 O  O     . CYS B 1 415 ? 22.038 10.989  -10.335 1.00 34.44  ? 394 CYS B O     1 
ATOM   6279 C  CB    . CYS B 1 415 ? 22.464 13.328  -7.920  1.00 36.94  ? 394 CYS B CB    1 
ATOM   6280 S  SG    . CYS B 1 415 ? 22.585 13.736  -6.160  1.00 36.51  ? 394 CYS B SG    1 
ATOM   6281 N  N     . TYR B 1 416 ? 20.256 11.318  -8.990  1.00 37.10  ? 395 TYR B N     1 
ATOM   6282 C  CA    . TYR B 1 416 ? 19.673 11.611  -7.692  1.00 36.90  ? 395 TYR B CA    1 
ATOM   6283 C  C     . TYR B 1 416 ? 19.873 10.445  -6.714  1.00 38.69  ? 395 TYR B C     1 
ATOM   6284 O  O     . TYR B 1 416 ? 19.873 10.658  -5.501  1.00 41.85  ? 395 TYR B O     1 
ATOM   6285 C  CB    . TYR B 1 416 ? 18.185 11.866  -7.893  1.00 36.39  ? 395 TYR B CB    1 
ATOM   6286 C  CG    . TYR B 1 416 ? 17.917 12.782  -9.057  1.00 33.88  ? 395 TYR B CG    1 
ATOM   6287 C  CD1   . TYR B 1 416 ? 18.523 14.023  -9.146  1.00 32.13  ? 395 TYR B CD1   1 
ATOM   6288 C  CD2   . TYR B 1 416 ? 17.088 12.391  -10.077 1.00 30.73  ? 395 TYR B CD2   1 
ATOM   6289 C  CE1   . TYR B 1 416 ? 18.286 14.862  -10.220 1.00 31.52  ? 395 TYR B CE1   1 
ATOM   6290 C  CE2   . TYR B 1 416 ? 16.827 13.223  -11.147 1.00 34.39  ? 395 TYR B CE2   1 
ATOM   6291 C  CZ    . TYR B 1 416 ? 17.440 14.453  -11.229 1.00 31.17  ? 395 TYR B CZ    1 
ATOM   6292 O  OH    . TYR B 1 416 ? 17.169 15.245  -12.302 1.00 34.85  ? 395 TYR B OH    1 
ATOM   6293 N  N     . GLY B 1 417 ? 19.992 9.231   -7.234  1.00 38.06  ? 396 GLY B N     1 
ATOM   6294 C  CA    . GLY B 1 417 ? 20.078 8.009   -6.419  1.00 40.57  ? 396 GLY B CA    1 
ATOM   6295 C  C     . GLY B 1 417 ? 20.177 6.808   -7.319  1.00 37.12  ? 396 GLY B C     1 
ATOM   6296 O  O     . GLY B 1 417 ? 20.292 6.990   -8.515  1.00 40.02  ? 396 GLY B O     1 
ATOM   6297 N  N     . ALA B 1 418 ? 20.139 5.605   -6.779  1.00 38.42  ? 397 ALA B N     1 
ATOM   6298 C  CA    . ALA B 1 418 ? 20.392 4.392   -7.587  1.00 36.68  ? 397 ALA B CA    1 
ATOM   6299 C  C     . ALA B 1 418 ? 19.168 4.101   -8.457  1.00 34.31  ? 397 ALA B C     1 
ATOM   6300 O  O     . ALA B 1 418 ? 18.039 4.373   -8.053  1.00 35.85  ? 397 ALA B O     1 
ATOM   6301 C  CB    . ALA B 1 418 ? 20.776 3.220   -6.701  1.00 39.19  ? 397 ALA B CB    1 
ATOM   6302 N  N     . HIS B 1 419 ? 19.414 3.527   -9.623  1.00 36.11  ? 398 HIS B N     1 
ATOM   6303 C  CA    . HIS B 1 419 ? 18.420 2.789   -10.435 1.00 33.26  ? 398 HIS B CA    1 
ATOM   6304 C  C     . HIS B 1 419 ? 18.892 1.341   -10.492 1.00 34.46  ? 398 HIS B C     1 
ATOM   6305 O  O     . HIS B 1 419 ? 20.068 1.095   -10.137 1.00 38.28  ? 398 HIS B O     1 
ATOM   6306 C  CB    . HIS B 1 419 ? 18.293 3.446   -11.806 1.00 34.99  ? 398 HIS B CB    1 
ATOM   6307 C  CG    . HIS B 1 419 ? 19.572 3.542   -12.571 1.00 36.02  ? 398 HIS B CG    1 
ATOM   6308 N  ND1   . HIS B 1 419 ? 19.991 2.547   -13.414 1.00 35.95  ? 398 HIS B ND1   1 
ATOM   6309 C  CD2   . HIS B 1 419 ? 20.518 4.507   -12.628 1.00 37.60  ? 398 HIS B CD2   1 
ATOM   6310 C  CE1   . HIS B 1 419 ? 21.125 2.895   -13.977 1.00 38.53  ? 398 HIS B CE1   1 
ATOM   6311 N  NE2   . HIS B 1 419 ? 21.480 4.095   -13.502 1.00 39.40  ? 398 HIS B NE2   1 
ATOM   6312 N  N     . LEU B 1 420 ? 18.016 0.419   -10.888 1.00 34.93  ? 399 LEU B N     1 
ATOM   6313 C  CA    . LEU B 1 420 ? 18.323 -1.035  -10.990 1.00 33.18  ? 399 LEU B CA    1 
ATOM   6314 C  C     . LEU B 1 420 ? 18.075 -1.475  -12.425 1.00 31.06  ? 399 LEU B C     1 
ATOM   6315 O  O     . LEU B 1 420 ? 17.023 -1.228  -12.988 1.00 34.40  ? 399 LEU B O     1 
ATOM   6316 C  CB    . LEU B 1 420 ? 17.484 -1.822  -9.979  1.00 33.39  ? 399 LEU B CB    1 
ATOM   6317 C  CG    . LEU B 1 420 ? 18.032 -1.824  -8.546  1.00 35.44  ? 399 LEU B CG    1 
ATOM   6318 C  CD1   . LEU B 1 420 ? 17.665 -0.545  -7.807  1.00 38.75  ? 399 LEU B CD1   1 
ATOM   6319 C  CD2   . LEU B 1 420 ? 17.550 -3.043  -7.775  1.00 37.86  ? 399 LEU B CD2   1 
ATOM   6320 N  N     . PRO B 1 421 ? 19.080 -2.061  -13.101 1.00 34.79  ? 400 PRO B N     1 
ATOM   6321 C  CA    . PRO B 1 421 ? 18.917 -2.503  -14.483 1.00 33.34  ? 400 PRO B CA    1 
ATOM   6322 C  C     . PRO B 1 421 ? 18.141 -3.812  -14.420 1.00 31.01  ? 400 PRO B C     1 
ATOM   6323 O  O     . PRO B 1 421 ? 17.841 -4.278  -13.328 1.00 31.18  ? 400 PRO B O     1 
ATOM   6324 C  CB    . PRO B 1 421 ? 20.354 -2.674  -14.988 1.00 31.84  ? 400 PRO B CB    1 
ATOM   6325 C  CG    . PRO B 1 421 ? 21.161 -2.980  -13.746 1.00 36.07  ? 400 PRO B CG    1 
ATOM   6326 C  CD    . PRO B 1 421 ? 20.416 -2.380  -12.566 1.00 34.80  ? 400 PRO B CD    1 
ATOM   6327 N  N     . PRO B 1 422 ? 17.776 -4.393  -15.577 1.00 33.05  ? 401 PRO B N     1 
ATOM   6328 C  CA    . PRO B 1 422 ? 17.114 -5.694  -15.645 1.00 33.69  ? 401 PRO B CA    1 
ATOM   6329 C  C     . PRO B 1 422 ? 17.768 -6.862  -14.895 1.00 36.48  ? 401 PRO B C     1 
ATOM   6330 O  O     . PRO B 1 422 ? 19.007 -7.011  -14.937 1.00 35.63  ? 401 PRO B O     1 
ATOM   6331 C  CB    . PRO B 1 422 ? 17.198 -5.997  -17.141 1.00 34.47  ? 401 PRO B CB    1 
ATOM   6332 C  CG    . PRO B 1 422 ? 17.062 -4.657  -17.776 1.00 34.13  ? 401 PRO B CG    1 
ATOM   6333 C  CD    . PRO B 1 422 ? 17.919 -3.775  -16.901 1.00 35.72  ? 401 PRO B CD    1 
ATOM   6334 N  N     . GLY B 1 423 ? 16.924 -7.669  -14.243 1.00 38.64  ? 402 GLY B N     1 
ATOM   6335 C  CA    . GLY B 1 423 ? 17.298 -8.907  -13.527 1.00 36.21  ? 402 GLY B CA    1 
ATOM   6336 C  C     . GLY B 1 423 ? 17.711 -8.621  -12.099 1.00 38.06  ? 402 GLY B C     1 
ATOM   6337 O  O     . GLY B 1 423 ? 17.995 -9.575  -11.376 1.00 45.89  ? 402 GLY B O     1 
ATOM   6338 N  N     . ALA B 1 424 ? 17.739 -7.354  -11.685 1.00 32.61  ? 403 ALA B N     1 
ATOM   6339 C  CA    . ALA B 1 424 ? 18.369 -6.938  -10.413 1.00 34.76  ? 403 ALA B CA    1 
ATOM   6340 C  C     . ALA B 1 424 ? 17.380 -7.013  -9.237  1.00 32.77  ? 403 ALA B C     1 
ATOM   6341 O  O     . ALA B 1 424 ? 17.776 -7.498  -8.127  1.00 30.12  ? 403 ALA B O     1 
ATOM   6342 C  CB    . ALA B 1 424 ? 18.956 -5.544  -10.561 1.00 36.27  ? 403 ALA B CB    1 
ATOM   6343 N  N     . TRP B 1 425 ? 16.172 -6.479  -9.411  1.00 32.93  ? 404 TRP B N     1 
ATOM   6344 C  CA    . TRP B 1 425 ? 15.162 -6.448  -8.327  1.00 33.55  ? 404 TRP B CA    1 
ATOM   6345 C  C     . TRP B 1 425 ? 14.827 -7.871  -7.877  1.00 32.04  ? 404 TRP B C     1 
ATOM   6346 O  O     . TRP B 1 425 ? 14.758 -8.083  -6.655  1.00 35.00  ? 404 TRP B O     1 
ATOM   6347 C  CB    . TRP B 1 425 ? 13.908 -5.678  -8.733  1.00 34.27  ? 404 TRP B CB    1 
ATOM   6348 C  CG    . TRP B 1 425 ? 13.946 -4.247  -8.320  1.00 36.08  ? 404 TRP B CG    1 
ATOM   6349 C  CD1   . TRP B 1 425 ? 13.788 -3.158  -9.119  1.00 36.42  ? 404 TRP B CD1   1 
ATOM   6350 C  CD2   . TRP B 1 425 ? 14.121 -3.750  -6.985  1.00 38.71  ? 404 TRP B CD2   1 
ATOM   6351 N  NE1   . TRP B 1 425 ? 13.853 -2.012  -8.372  1.00 39.82  ? 404 TRP B NE1   1 
ATOM   6352 C  CE2   . TRP B 1 425 ? 14.062 -2.341  -7.061  1.00 39.66  ? 404 TRP B CE2   1 
ATOM   6353 C  CE3   . TRP B 1 425 ? 14.312 -4.352  -5.735  1.00 40.67  ? 404 TRP B CE3   1 
ATOM   6354 C  CZ2   . TRP B 1 425 ? 14.199 -1.528  -5.936  1.00 42.25  ? 404 TRP B CZ2   1 
ATOM   6355 C  CZ3   . TRP B 1 425 ? 14.472 -3.547  -4.624  1.00 44.85  ? 404 TRP B CZ3   1 
ATOM   6356 C  CH2   . TRP B 1 425 ? 14.407 -2.153  -4.722  1.00 44.71  ? 404 TRP B CH2   1 
ATOM   6357 N  N     . THR B 1 426 ? 14.587 -8.803  -8.794  1.00 32.47  ? 405 THR B N     1 
ATOM   6358 C  CA    . THR B 1 426 ? 13.986 -10.123 -8.426  1.00 38.16  ? 405 THR B CA    1 
ATOM   6359 C  C     . THR B 1 426 ? 15.036 -11.037 -7.802  1.00 41.95  ? 405 THR B C     1 
ATOM   6360 O  O     . THR B 1 426 ? 14.639 -11.882 -6.993  1.00 52.18  ? 405 THR B O     1 
ATOM   6361 C  CB    . THR B 1 426 ? 13.317 -10.824 -9.610  1.00 33.90  ? 405 THR B CB    1 
ATOM   6362 O  OG1   . THR B 1 426 ? 14.226 -10.808 -10.706 1.00 37.32  ? 405 THR B OG1   1 
ATOM   6363 C  CG2   . THR B 1 426 ? 12.041 -10.124 -10.029 1.00 36.19  ? 405 THR B CG2   1 
ATOM   6364 N  N     . VAL B 1 427 ? 16.317 -10.851 -8.144  1.00 44.75  ? 406 VAL B N     1 
ATOM   6365 C  CA    . VAL B 1 427 ? 17.411 -11.824 -7.832  1.00 35.18  ? 406 VAL B CA    1 
ATOM   6366 C  C     . VAL B 1 427 ? 18.180 -11.351 -6.604  1.00 32.34  ? 406 VAL B C     1 
ATOM   6367 O  O     . VAL B 1 427 ? 18.417 -12.195 -5.717  1.00 32.45  ? 406 VAL B O     1 
ATOM   6368 C  CB    . VAL B 1 427 ? 18.363 -12.005 -9.026  1.00 35.48  ? 406 VAL B CB    1 
ATOM   6369 C  CG1   . VAL B 1 427 ? 19.486 -12.961 -8.660  1.00 36.60  ? 406 VAL B CG1   1 
ATOM   6370 C  CG2   . VAL B 1 427 ? 17.626 -12.457 -10.285 1.00 32.60  ? 406 VAL B CG2   1 
ATOM   6371 N  N     . TYR B 1 428 ? 18.582 -10.075 -6.579  1.00 31.35  ? 407 TYR B N     1 
ATOM   6372 C  CA    . TYR B 1 428 ? 19.423 -9.464  -5.513  1.00 33.32  ? 407 TYR B CA    1 
ATOM   6373 C  C     . TYR B 1 428 ? 18.584 -8.555  -4.597  1.00 33.38  ? 407 TYR B C     1 
ATOM   6374 O  O     . TYR B 1 428 ? 18.976 -8.386  -3.427  1.00 33.81  ? 407 TYR B O     1 
ATOM   6375 C  CB    . TYR B 1 428 ? 20.597 -8.677  -6.117  1.00 34.47  ? 407 TYR B CB    1 
ATOM   6376 C  CG    . TYR B 1 428 ? 21.358 -9.439  -7.175  1.00 36.57  ? 407 TYR B CG    1 
ATOM   6377 C  CD1   . TYR B 1 428 ? 22.305 -10.392 -6.827  1.00 35.15  ? 407 TYR B CD1   1 
ATOM   6378 C  CD2   . TYR B 1 428 ? 21.103 -9.250  -8.523  1.00 36.74  ? 407 TYR B CD2   1 
ATOM   6379 C  CE1   . TYR B 1 428 ? 22.997 -11.107 -7.786  1.00 33.45  ? 407 TYR B CE1   1 
ATOM   6380 C  CE2   . TYR B 1 428 ? 21.788 -9.964  -9.493  1.00 35.94  ? 407 TYR B CE2   1 
ATOM   6381 C  CZ    . TYR B 1 428 ? 22.740 -10.889 -9.119  1.00 33.33  ? 407 TYR B CZ    1 
ATOM   6382 O  OH    . TYR B 1 428 ? 23.412 -11.602 -10.058 1.00 40.84  ? 407 TYR B OH    1 
ATOM   6383 N  N     . GLY B 1 429 ? 17.491 -7.986  -5.113  1.00 33.53  ? 408 GLY B N     1 
ATOM   6384 C  CA    . GLY B 1 429 ? 16.635 -6.999  -4.423  1.00 35.47  ? 408 GLY B CA    1 
ATOM   6385 C  C     . GLY B 1 429 ? 16.210 -7.376  -2.999  1.00 31.78  ? 408 GLY B C     1 
ATOM   6386 O  O     . GLY B 1 429 ? 16.222 -6.525  -2.119  1.00 36.75  ? 408 GLY B O     1 
ATOM   6387 N  N     . PRO B 1 430 ? 15.783 -8.616  -2.693  1.00 31.20  ? 409 PRO B N     1 
ATOM   6388 C  CA    . PRO B 1 430 ? 15.399 -8.968  -1.325  1.00 32.45  ? 409 PRO B CA    1 
ATOM   6389 C  C     . PRO B 1 430 ? 16.386 -8.655  -0.187  1.00 34.65  ? 409 PRO B C     1 
ATOM   6390 O  O     . PRO B 1 430 ? 15.963 -8.697  0.944   1.00 39.89  ? 409 PRO B O     1 
ATOM   6391 C  CB    . PRO B 1 430 ? 15.199 -10.483 -1.453  1.00 36.10  ? 409 PRO B CB    1 
ATOM   6392 C  CG    . PRO B 1 430 ? 14.681 -10.676 -2.863  1.00 31.25  ? 409 PRO B CG    1 
ATOM   6393 C  CD    . PRO B 1 430 ? 15.521 -9.701  -3.648  1.00 33.24  ? 409 PRO B CD    1 
ATOM   6394 N  N     . ALA B 1 431 ? 17.659 -8.326  -0.460  1.00 36.52  ? 410 ALA B N     1 
ATOM   6395 C  CA    . ALA B 1 431 ? 18.663 -8.042  0.599   1.00 32.53  ? 410 ALA B CA    1 
ATOM   6396 C  C     . ALA B 1 431 ? 18.737 -6.526  0.881   1.00 34.38  ? 410 ALA B C     1 
ATOM   6397 O  O     . ALA B 1 431 ? 19.665 -6.059  1.604   1.00 36.27  ? 410 ALA B O     1 
ATOM   6398 C  CB    . ALA B 1 431 ? 20.004 -8.611  0.212   1.00 30.58  ? 410 ALA B CB    1 
ATOM   6399 N  N     . LEU B 1 432 ? 17.798 -5.755  0.350   1.00 36.70  ? 411 LEU B N     1 
ATOM   6400 C  CA    . LEU B 1 432 ? 17.874 -4.271  0.391   1.00 36.93  ? 411 LEU B CA    1 
ATOM   6401 C  C     . LEU B 1 432 ? 17.890 -3.772  1.848   1.00 36.88  ? 411 LEU B C     1 
ATOM   6402 O  O     . LEU B 1 432 ? 18.758 -2.961  2.163   1.00 42.48  ? 411 LEU B O     1 
ATOM   6403 C  CB    . LEU B 1 432 ? 16.697 -3.695  -0.397  1.00 34.87  ? 411 LEU B CB    1 
ATOM   6404 C  CG    . LEU B 1 432 ? 16.677 -2.172  -0.481  1.00 34.83  ? 411 LEU B CG    1 
ATOM   6405 C  CD1   . LEU B 1 432 ? 17.805 -1.668  -1.375  1.00 35.96  ? 411 LEU B CD1   1 
ATOM   6406 C  CD2   . LEU B 1 432 ? 15.317 -1.664  -0.950  1.00 36.53  ? 411 LEU B CD2   1 
ATOM   6407 N  N     . ARG B 1 433 ? 16.969 -4.232  2.696   1.00 36.40  ? 412 ARG B N     1 
ATOM   6408 C  CA    . ARG B 1 433 ? 16.709 -3.676  4.059   1.00 40.93  ? 412 ARG B CA    1 
ATOM   6409 C  C     . ARG B 1 433 ? 17.062 -4.670  5.175   1.00 41.28  ? 412 ARG B C     1 
ATOM   6410 O  O     . ARG B 1 433 ? 17.202 -4.218  6.319   1.00 42.00  ? 412 ARG B O     1 
ATOM   6411 C  CB    . ARG B 1 433 ? 15.218 -3.347  4.211   1.00 41.73  ? 412 ARG B CB    1 
ATOM   6412 C  CG    . ARG B 1 433 ? 14.840 -1.954  3.748   1.00 43.00  ? 412 ARG B CG    1 
ATOM   6413 C  CD    . ARG B 1 433 ? 13.352 -1.733  3.897   1.00 45.15  ? 412 ARG B CD    1 
ATOM   6414 N  NE    . ARG B 1 433 ? 12.665 -2.475  2.857   1.00 46.27  ? 412 ARG B NE    1 
ATOM   6415 C  CZ    . ARG B 1 433 ? 12.208 -1.958  1.735   1.00 43.34  ? 412 ARG B CZ    1 
ATOM   6416 N  NH1   . ARG B 1 433 ? 12.310 -0.665  1.479   1.00 44.73  ? 412 ARG B NH1   1 
ATOM   6417 N  NH2   . ARG B 1 433 ? 11.633 -2.745  0.859   1.00 45.04  ? 412 ARG B NH2   1 
ATOM   6418 N  N     . VAL B 1 434 ? 17.131 -5.972  4.885   1.00 42.61  ? 413 VAL B N     1 
ATOM   6419 C  CA    . VAL B 1 434 ? 17.435 -7.015  5.904   1.00 45.53  ? 413 VAL B CA    1 
ATOM   6420 C  C     . VAL B 1 434 ? 18.702 -6.589  6.637   1.00 42.68  ? 413 VAL B C     1 
ATOM   6421 O  O     . VAL B 1 434 ? 19.726 -6.381  5.998   1.00 44.88  ? 413 VAL B O     1 
ATOM   6422 C  CB    . VAL B 1 434 ? 17.607 -8.400  5.250   1.00 49.43  ? 413 VAL B CB    1 
ATOM   6423 C  CG1   . VAL B 1 434 ? 17.957 -9.466  6.276   1.00 51.65  ? 413 VAL B CG1   1 
ATOM   6424 C  CG2   . VAL B 1 434 ? 16.368 -8.816  4.480   1.00 51.59  ? 413 VAL B CG2   1 
ATOM   6425 N  N     . PRO B 1 435 ? 18.700 -6.438  7.982   1.00 44.92  ? 414 PRO B N     1 
ATOM   6426 C  CA    . PRO B 1 435 ? 19.950 -6.203  8.716   1.00 44.00  ? 414 PRO B CA    1 
ATOM   6427 C  C     . PRO B 1 435 ? 20.897 -7.420  8.633   1.00 40.73  ? 414 PRO B C     1 
ATOM   6428 O  O     . PRO B 1 435 ? 20.479 -8.544  8.526   1.00 41.46  ? 414 PRO B O     1 
ATOM   6429 C  CB    . PRO B 1 435 ? 19.528 -5.926  10.173  1.00 41.73  ? 414 PRO B CB    1 
ATOM   6430 C  CG    . PRO B 1 435 ? 18.004 -5.821  10.139  1.00 42.93  ? 414 PRO B CG    1 
ATOM   6431 C  CD    . PRO B 1 435 ? 17.528 -6.504  8.872   1.00 42.94  ? 414 PRO B CD    1 
ATOM   6432 N  N     . VAL B 1 436 ? 22.184 -7.156  8.645   1.00 36.50  ? 415 VAL B N     1 
ATOM   6433 C  CA    . VAL B 1 436 ? 23.242 -8.197  8.731   1.00 39.14  ? 415 VAL B CA    1 
ATOM   6434 C  C     . VAL B 1 436 ? 23.810 -8.146  10.160  1.00 36.95  ? 415 VAL B C     1 
ATOM   6435 O  O     . VAL B 1 436 ? 24.591 -7.215  10.470  1.00 38.65  ? 415 VAL B O     1 
ATOM   6436 C  CB    . VAL B 1 436 ? 24.310 -7.928  7.651   1.00 36.78  ? 415 VAL B CB    1 
ATOM   6437 C  CG1   . VAL B 1 436 ? 25.475 -8.908  7.735   1.00 34.17  ? 415 VAL B CG1   1 
ATOM   6438 C  CG2   . VAL B 1 436 ? 23.681 -7.902  6.265   1.00 36.97  ? 415 VAL B CG2   1 
ATOM   6439 N  N     . GLY B 1 437 ? 23.373 -9.062  11.020  1.00 38.37  ? 416 GLY B N     1 
ATOM   6440 C  CA    . GLY B 1 437 ? 23.724 -9.056  12.451  1.00 37.46  ? 416 GLY B CA    1 
ATOM   6441 C  C     . GLY B 1 437 ? 23.369 -7.730  13.103  1.00 36.14  ? 416 GLY B C     1 
ATOM   6442 O  O     . GLY B 1 437 ? 22.194 -7.446  13.198  1.00 43.91  ? 416 GLY B O     1 
ATOM   6443 N  N     . ARG B 1 438 ? 24.363 -6.952  13.523  1.00 39.57  ? 417 ARG B N     1 
ATOM   6444 C  CA    . ARG B 1 438 ? 24.198 -5.720  14.345  1.00 41.73  ? 417 ARG B CA    1 
ATOM   6445 C  C     . ARG B 1 438 ? 24.203 -4.478  13.443  1.00 40.56  ? 417 ARG B C     1 
ATOM   6446 O  O     . ARG B 1 438 ? 24.170 -3.352  13.981  1.00 40.64  ? 417 ARG B O     1 
ATOM   6447 C  CB    . ARG B 1 438 ? 25.330 -5.633  15.374  1.00 42.66  ? 417 ARG B CB    1 
ATOM   6448 C  CG    . ARG B 1 438 ? 25.296 -6.743  16.418  1.00 42.05  ? 417 ARG B CG    1 
ATOM   6449 C  CD    . ARG B 1 438 ? 26.255 -6.524  17.579  1.00 43.95  ? 417 ARG B CD    1 
ATOM   6450 N  NE    . ARG B 1 438 ? 26.030 -7.457  18.687  1.00 49.65  ? 417 ARG B NE    1 
ATOM   6451 C  CZ    . ARG B 1 438 ? 25.187 -7.291  19.717  1.00 51.12  ? 417 ARG B CZ    1 
ATOM   6452 N  NH1   . ARG B 1 438 ? 24.437 -6.205  19.849  1.00 51.92  ? 417 ARG B NH1   1 
ATOM   6453 N  NH2   . ARG B 1 438 ? 25.097 -8.245  20.621  1.00 50.40  ? 417 ARG B NH2   1 
ATOM   6454 N  N     . VAL B 1 439 ? 24.253 -4.674  12.122  1.00 37.79  ? 418 VAL B N     1 
ATOM   6455 C  CA    . VAL B 1 439 ? 24.396 -3.570  11.136  1.00 37.88  ? 418 VAL B CA    1 
ATOM   6456 C  C     . VAL B 1 439 ? 23.065 -3.460  10.390  1.00 37.52  ? 418 VAL B C     1 
ATOM   6457 O  O     . VAL B 1 439 ? 22.590 -4.455  9.807   1.00 37.76  ? 418 VAL B O     1 
ATOM   6458 C  CB    . VAL B 1 439 ? 25.592 -3.760  10.178  1.00 39.80  ? 418 VAL B CB    1 
ATOM   6459 C  CG1   . VAL B 1 439 ? 25.738 -2.566  9.244   1.00 42.06  ? 418 VAL B CG1   1 
ATOM   6460 C  CG2   . VAL B 1 439 ? 26.912 -4.021  10.907  1.00 38.83  ? 418 VAL B CG2   1 
ATOM   6461 N  N     . HIS B 1 440 ? 22.497 -2.264  10.452  1.00 37.68  ? 419 HIS B N     1 
ATOM   6462 C  CA    . HIS B 1 440 ? 21.201 -1.878  9.864   1.00 38.13  ? 419 HIS B CA    1 
ATOM   6463 C  C     . HIS B 1 440 ? 21.450 -0.877  8.745   1.00 34.28  ? 419 HIS B C     1 
ATOM   6464 O  O     . HIS B 1 440 ? 22.478 -0.128  8.818   1.00 38.31  ? 419 HIS B O     1 
ATOM   6465 C  CB    . HIS B 1 440 ? 20.324 -1.264  10.963  1.00 41.43  ? 419 HIS B CB    1 
ATOM   6466 C  CG    . HIS B 1 440 ? 19.791 -2.262  11.934  1.00 43.68  ? 419 HIS B CG    1 
ATOM   6467 N  ND1   . HIS B 1 440 ? 20.490 -2.640  13.068  1.00 48.64  ? 419 HIS B ND1   1 
ATOM   6468 C  CD2   . HIS B 1 440 ? 18.629 -2.947  11.952  1.00 44.51  ? 419 HIS B CD2   1 
ATOM   6469 C  CE1   . HIS B 1 440 ? 19.774 -3.518  13.744  1.00 46.13  ? 419 HIS B CE1   1 
ATOM   6470 N  NE2   . HIS B 1 440 ? 18.628 -3.721  13.075  1.00 48.50  ? 419 HIS B NE2   1 
ATOM   6471 N  N     . TRP B 1 441 ? 20.502 -0.807  7.810   1.00 33.70  ? 420 TRP B N     1 
ATOM   6472 C  CA    . TRP B 1 441 ? 20.599 -0.004  6.563   1.00 35.68  ? 420 TRP B CA    1 
ATOM   6473 C  C     . TRP B 1 441 ? 19.507 1.081   6.535   1.00 33.55  ? 420 TRP B C     1 
ATOM   6474 O  O     . TRP B 1 441 ? 18.323 0.757   6.783   1.00 34.14  ? 420 TRP B O     1 
ATOM   6475 C  CB    . TRP B 1 441 ? 20.493 -0.937  5.355   1.00 36.80  ? 420 TRP B CB    1 
ATOM   6476 C  CG    . TRP B 1 441 ? 21.343 -2.157  5.470   1.00 36.86  ? 420 TRP B CG    1 
ATOM   6477 C  CD1   . TRP B 1 441 ? 20.922 -3.432  5.693   1.00 37.76  ? 420 TRP B CD1   1 
ATOM   6478 C  CD2   . TRP B 1 441 ? 22.775 -2.207  5.407   1.00 37.83  ? 420 TRP B CD2   1 
ATOM   6479 N  NE1   . TRP B 1 441 ? 21.996 -4.279  5.759   1.00 38.55  ? 420 TRP B NE1   1 
ATOM   6480 C  CE2   . TRP B 1 441 ? 23.145 -3.558  5.578   1.00 39.68  ? 420 TRP B CE2   1 
ATOM   6481 C  CE3   . TRP B 1 441 ? 23.770 -1.258  5.151   1.00 37.93  ? 420 TRP B CE3   1 
ATOM   6482 C  CZ2   . TRP B 1 441 ? 24.473 -3.977  5.517   1.00 40.53  ? 420 TRP B CZ2   1 
ATOM   6483 C  CZ3   . TRP B 1 441 ? 25.085 -1.665  5.112   1.00 40.57  ? 420 TRP B CZ3   1 
ATOM   6484 C  CH2   . TRP B 1 441 ? 25.430 -3.009  5.289   1.00 42.38  ? 420 TRP B CH2   1 
ATOM   6485 N  N     . ALA B 1 442 ? 19.903 2.304   6.198   1.00 32.07  ? 421 ALA B N     1 
ATOM   6486 C  CA    . ALA B 1 442 ? 19.007 3.443   5.881   1.00 33.42  ? 421 ALA B CA    1 
ATOM   6487 C  C     . ALA B 1 442 ? 19.551 4.176   4.646   1.00 33.01  ? 421 ALA B C     1 
ATOM   6488 O  O     . ALA B 1 442 ? 20.587 3.751   4.110   1.00 34.56  ? 421 ALA B O     1 
ATOM   6489 C  CB    . ALA B 1 442 ? 18.912 4.363   7.078   1.00 32.21  ? 421 ALA B CB    1 
ATOM   6490 N  N     . GLY B 1 443 ? 18.907 5.280   4.268   1.00 30.49  ? 422 GLY B N     1 
ATOM   6491 C  CA    . GLY B 1 443 ? 19.172 6.065   3.055   1.00 29.52  ? 422 GLY B CA    1 
ATOM   6492 C  C     . GLY B 1 443 ? 17.959 5.971   2.176   1.00 29.56  ? 422 GLY B C     1 
ATOM   6493 O  O     . GLY B 1 443 ? 17.274 4.949   2.292   1.00 30.36  ? 422 GLY B O     1 
ATOM   6494 N  N     . THR B 1 444 ? 17.691 6.981   1.334   1.00 33.26  ? 423 THR B N     1 
ATOM   6495 C  CA    . THR B 1 444 ? 16.429 7.106   0.543   1.00 32.47  ? 423 THR B CA    1 
ATOM   6496 C  C     . THR B 1 444 ? 16.170 5.834   -0.297  1.00 34.26  ? 423 THR B C     1 
ATOM   6497 O  O     . THR B 1 444 ? 14.984 5.488   -0.475  1.00 36.44  ? 423 THR B O     1 
ATOM   6498 C  CB    . THR B 1 444 ? 16.441 8.405   -0.266  1.00 32.71  ? 423 THR B CB    1 
ATOM   6499 O  OG1   . THR B 1 444 ? 15.151 8.556   -0.848  1.00 36.31  ? 423 THR B OG1   1 
ATOM   6500 C  CG2   . THR B 1 444 ? 17.476 8.431   -1.370  1.00 34.82  ? 423 THR B CG2   1 
ATOM   6501 N  N     . GLU B 1 445 ? 17.213 5.128   -0.755  1.00 34.88  ? 424 GLU B N     1 
ATOM   6502 C  CA    . GLU B 1 445 ? 17.110 3.917   -1.627  1.00 36.27  ? 424 GLU B CA    1 
ATOM   6503 C  C     . GLU B 1 445 ? 16.432 2.750   -0.883  1.00 37.41  ? 424 GLU B C     1 
ATOM   6504 O  O     . GLU B 1 445 ? 16.055 1.756   -1.551  1.00 34.20  ? 424 GLU B O     1 
ATOM   6505 C  CB    . GLU B 1 445 ? 18.501 3.510   -2.139  1.00 36.01  ? 424 GLU B CB    1 
ATOM   6506 C  CG    . GLU B 1 445 ? 19.102 4.482   -3.158  1.00 39.38  ? 424 GLU B CG    1 
ATOM   6507 C  CD    . GLU B 1 445 ? 19.860 5.745   -2.698  1.00 43.41  ? 424 GLU B CD    1 
ATOM   6508 O  OE1   . GLU B 1 445 ? 20.060 6.004   -1.449  1.00 45.07  ? 424 GLU B OE1   1 
ATOM   6509 O  OE2   . GLU B 1 445 ? 20.246 6.508   -3.604  1.00 43.51  ? 424 GLU B OE2   1 
ATOM   6510 N  N     . THR B 1 446 ? 16.326 2.815   0.451   1.00 38.32  ? 425 THR B N     1 
ATOM   6511 C  CA    . THR B 1 446 ? 15.655 1.767   1.268   1.00 37.93  ? 425 THR B CA    1 
ATOM   6512 C  C     . THR B 1 446 ? 14.220 2.188   1.608   1.00 36.76  ? 425 THR B C     1 
ATOM   6513 O  O     . THR B 1 446 ? 13.554 1.398   2.241   1.00 37.63  ? 425 THR B O     1 
ATOM   6514 C  CB    . THR B 1 446 ? 16.434 1.434   2.551   1.00 34.88  ? 425 THR B CB    1 
ATOM   6515 O  OG1   . THR B 1 446 ? 16.470 2.592   3.385   1.00 32.64  ? 425 THR B OG1   1 
ATOM   6516 C  CG2   . THR B 1 446 ? 17.849 0.971   2.279   1.00 38.33  ? 425 THR B CG2   1 
ATOM   6517 N  N     . ALA B 1 447 ? 13.770 3.387   1.231   1.00 39.54  ? 426 ALA B N     1 
ATOM   6518 C  CA    . ALA B 1 447 ? 12.436 3.918   1.613   1.00 39.60  ? 426 ALA B CA    1 
ATOM   6519 C  C     . ALA B 1 447 ? 11.357 3.205   0.790   1.00 39.90  ? 426 ALA B C     1 
ATOM   6520 O  O     . ALA B 1 447 ? 11.652 2.824   -0.372  1.00 39.21  ? 426 ALA B O     1 
ATOM   6521 C  CB    . ALA B 1 447 ? 12.378 5.417   1.435   1.00 35.02  ? 426 ALA B CB    1 
ATOM   6522 N  N     . GLU B 1 448 ? 10.158 3.037   1.363   1.00 42.90  ? 427 GLU B N     1 
ATOM   6523 C  CA    . GLU B 1 448 ? 8.957  2.466   0.674   1.00 48.64  ? 427 GLU B CA    1 
ATOM   6524 C  C     . GLU B 1 448 ? 8.261  3.540   -0.186  1.00 45.74  ? 427 GLU B C     1 
ATOM   6525 O  O     . GLU B 1 448 ? 7.870  3.227   -1.332  1.00 46.50  ? 427 GLU B O     1 
ATOM   6526 C  CB    . GLU B 1 448 ? 7.946  1.925   1.691   1.00 52.79  ? 427 GLU B CB    1 
ATOM   6527 C  CG    . GLU B 1 448 ? 8.334  0.588   2.297   1.00 61.93  ? 427 GLU B CG    1 
ATOM   6528 C  CD    . GLU B 1 448 ? 7.265  -0.109  3.138   1.00 66.58  ? 427 GLU B CD    1 
ATOM   6529 O  OE1   . GLU B 1 448 ? 6.067  0.286   3.073   1.00 64.15  ? 427 GLU B OE1   1 
ATOM   6530 O  OE2   . GLU B 1 448 ? 7.636  -1.062  3.858   1.00 70.36  ? 427 GLU B OE2   1 
ATOM   6531 N  N     . ARG B 1 449 ? 8.094  4.747   0.363   1.00 41.74  ? 428 ARG B N     1 
ATOM   6532 C  CA    . ARG B 1 449 ? 7.319  5.869   -0.231  1.00 47.01  ? 428 ARG B CA    1 
ATOM   6533 C  C     . ARG B 1 449 ? 8.288  7.016   -0.513  1.00 37.90  ? 428 ARG B C     1 
ATOM   6534 O  O     . ARG B 1 449 ? 9.091  7.326   0.386   1.00 34.16  ? 428 ARG B O     1 
ATOM   6535 C  CB    . ARG B 1 449 ? 6.185  6.326   0.708   1.00 56.11  ? 428 ARG B CB    1 
ATOM   6536 C  CG    . ARG B 1 449 ? 4.846  5.632   0.474   1.00 60.65  ? 428 ARG B CG    1 
ATOM   6537 C  CD    . ARG B 1 449 ? 3.629  6.340   1.055   1.00 69.58  ? 428 ARG B CD    1 
ATOM   6538 N  NE    . ARG B 1 449 ? 3.129  7.520   0.333   1.00 74.48  ? 428 ARG B NE    1 
ATOM   6539 C  CZ    . ARG B 1 449 ? 3.089  8.777   0.812   1.00 70.66  ? 428 ARG B CZ    1 
ATOM   6540 N  NH1   . ARG B 1 449 ? 3.553  9.065   2.021   1.00 71.58  ? 428 ARG B NH1   1 
ATOM   6541 N  NH2   . ARG B 1 449 ? 2.589  9.755   0.070   1.00 61.42  ? 428 ARG B NH2   1 
ATOM   6542 N  N     . TRP B 1 450 ? 8.183  7.626   -1.697  1.00 35.07  ? 429 TRP B N     1 
ATOM   6543 C  CA    . TRP B 1 450 ? 9.054  8.736   -2.161  1.00 35.30  ? 429 TRP B CA    1 
ATOM   6544 C  C     . TRP B 1 450 ? 10.533 8.309   -2.121  1.00 33.18  ? 429 TRP B C     1 
ATOM   6545 O  O     . TRP B 1 450 ? 11.397 9.137   -1.716  1.00 27.29  ? 429 TRP B O     1 
ATOM   6546 C  CB    . TRP B 1 450 ? 8.781  9.995   -1.321  1.00 37.35  ? 429 TRP B CB    1 
ATOM   6547 C  CG    . TRP B 1 450 ? 7.498  10.668  -1.698  1.00 41.70  ? 429 TRP B CG    1 
ATOM   6548 C  CD1   . TRP B 1 450 ? 6.357  10.777  -0.954  1.00 41.21  ? 429 TRP B CD1   1 
ATOM   6549 C  CD2   . TRP B 1 450 ? 7.228  11.322  -2.946  1.00 39.74  ? 429 TRP B CD2   1 
ATOM   6550 N  NE1   . TRP B 1 450 ? 5.400  11.449  -1.659  1.00 40.24  ? 429 TRP B NE1   1 
ATOM   6551 C  CE2   . TRP B 1 450 ? 5.903  11.800  -2.881  1.00 39.07  ? 429 TRP B CE2   1 
ATOM   6552 C  CE3   . TRP B 1 450 ? 7.971  11.531  -4.111  1.00 36.62  ? 429 TRP B CE3   1 
ATOM   6553 C  CZ2   . TRP B 1 450 ? 5.311  12.494  -3.933  1.00 39.15  ? 429 TRP B CZ2   1 
ATOM   6554 C  CZ3   . TRP B 1 450 ? 7.379  12.208  -5.157  1.00 41.39  ? 429 TRP B CZ3   1 
ATOM   6555 C  CH2   . TRP B 1 450 ? 6.069  12.688  -5.064  1.00 39.76  ? 429 TRP B CH2   1 
ATOM   6556 N  N     . THR B 1 451 ? 10.818 7.057   -2.512  1.00 33.63  ? 430 THR B N     1 
ATOM   6557 C  CA    . THR B 1 451 ? 12.205 6.556   -2.711  1.00 32.86  ? 430 THR B CA    1 
ATOM   6558 C  C     . THR B 1 451 ? 12.911 7.488   -3.713  1.00 31.80  ? 430 THR B C     1 
ATOM   6559 O  O     . THR B 1 451 ? 12.268 7.889   -4.704  1.00 28.30  ? 430 THR B O     1 
ATOM   6560 C  CB    . THR B 1 451 ? 12.204 5.070   -3.092  1.00 29.93  ? 430 THR B CB    1 
ATOM   6561 O  OG1   . THR B 1 451 ? 13.544 4.635   -2.936  1.00 28.88  ? 430 THR B OG1   1 
ATOM   6562 C  CG2   . THR B 1 451 ? 11.732 4.775   -4.494  1.00 31.19  ? 430 THR B CG2   1 
ATOM   6563 N  N     . GLY B 1 452 ? 14.152 7.885   -3.421  1.00 31.87  ? 431 GLY B N     1 
ATOM   6564 C  CA    . GLY B 1 452 ? 14.938 8.816   -4.266  1.00 34.28  ? 431 GLY B CA    1 
ATOM   6565 C  C     . GLY B 1 452 ? 14.767 10.295  -3.887  1.00 37.90  ? 431 GLY B C     1 
ATOM   6566 O  O     . GLY B 1 452 ? 15.508 11.124  -4.477  1.00 40.39  ? 431 GLY B O     1 
ATOM   6567 N  N     . TYR B 1 453 ? 13.897 10.622  -2.907  1.00 34.45  ? 432 TYR B N     1 
ATOM   6568 C  CA    . TYR B 1 453 ? 13.545 12.010  -2.479  1.00 32.98  ? 432 TYR B CA    1 
ATOM   6569 C  C     . TYR B 1 453 ? 14.000 12.227  -1.033  1.00 33.21  ? 432 TYR B C     1 
ATOM   6570 O  O     . TYR B 1 453 ? 14.311 11.234  -0.334  1.00 31.84  ? 432 TYR B O     1 
ATOM   6571 C  CB    . TYR B 1 453 ? 12.044 12.252  -2.691  1.00 32.26  ? 432 TYR B CB    1 
ATOM   6572 C  CG    . TYR B 1 453 ? 11.637 12.260  -4.151  1.00 30.08  ? 432 TYR B CG    1 
ATOM   6573 C  CD1   . TYR B 1 453 ? 11.503 11.090  -4.867  1.00 27.24  ? 432 TYR B CD1   1 
ATOM   6574 C  CD2   . TYR B 1 453 ? 11.473 13.450  -4.839  1.00 33.37  ? 432 TYR B CD2   1 
ATOM   6575 C  CE1   . TYR B 1 453 ? 11.223 11.091  -6.214  1.00 29.06  ? 432 TYR B CE1   1 
ATOM   6576 C  CE2   . TYR B 1 453 ? 11.156 13.472  -6.187  1.00 34.71  ? 432 TYR B CE2   1 
ATOM   6577 C  CZ    . TYR B 1 453 ? 11.038 12.285  -6.888  1.00 34.80  ? 432 TYR B CZ    1 
ATOM   6578 O  OH    . TYR B 1 453 ? 10.685 12.306  -8.218  1.00 36.14  ? 432 TYR B OH    1 
ATOM   6579 N  N     . ILE B 1 454 ? 14.081 13.488  -0.607  1.00 28.66  ? 433 ILE B N     1 
ATOM   6580 C  CA    . ILE B 1 454 ? 14.407 13.875  0.799   1.00 32.04  ? 433 ILE B CA    1 
ATOM   6581 C  C     . ILE B 1 454 ? 13.415 13.206  1.769   1.00 33.71  ? 433 ILE B C     1 
ATOM   6582 O  O     . ILE B 1 454 ? 13.840 12.736  2.858   1.00 29.80  ? 433 ILE B O     1 
ATOM   6583 C  CB    . ILE B 1 454 ? 14.422 15.409  0.978   1.00 31.83  ? 433 ILE B CB    1 
ATOM   6584 C  CG1   . ILE B 1 454 ? 15.479 16.077  0.105   1.00 32.80  ? 433 ILE B CG1   1 
ATOM   6585 C  CG2   . ILE B 1 454 ? 14.609 15.792  2.435   1.00 32.44  ? 433 ILE B CG2   1 
ATOM   6586 C  CD1   . ILE B 1 454 ? 15.209 17.562  -0.127  1.00 36.58  ? 433 ILE B CD1   1 
ATOM   6587 N  N     . ASP B 1 455 ? 12.132 13.182  1.398   1.00 39.62  ? 434 ASP B N     1 
ATOM   6588 C  CA    . ASP B 1 455 ? 11.045 12.498  2.143   1.00 38.56  ? 434 ASP B CA    1 
ATOM   6589 C  C     . ASP B 1 455 ? 11.405 11.025  2.417   1.00 37.52  ? 434 ASP B C     1 
ATOM   6590 O  O     . ASP B 1 455 ? 11.163 10.565  3.557   1.00 38.42  ? 434 ASP B O     1 
ATOM   6591 C  CB    . ASP B 1 455 ? 9.723  12.604  1.378   1.00 41.47  ? 434 ASP B CB    1 
ATOM   6592 C  CG    . ASP B 1 455 ? 8.508  12.365  2.264   1.00 41.77  ? 434 ASP B CG    1 
ATOM   6593 O  OD1   . ASP B 1 455 ? 8.204  13.260  3.088   1.00 39.54  ? 434 ASP B OD1   1 
ATOM   6594 O  OD2   . ASP B 1 455 ? 7.895  11.284  2.135   1.00 36.46  ? 434 ASP B OD2   1 
ATOM   6595 N  N     . GLY B 1 456 ? 11.898 10.299  1.413   1.00 35.61  ? 435 GLY B N     1 
ATOM   6596 C  CA    . GLY B 1 456 ? 12.210 8.859   1.521   1.00 35.79  ? 435 GLY B CA    1 
ATOM   6597 C  C     . GLY B 1 456 ? 13.364 8.636   2.473   1.00 33.02  ? 435 GLY B C     1 
ATOM   6598 O  O     . GLY B 1 456 ? 13.362 7.648   3.204   1.00 38.93  ? 435 GLY B O     1 
ATOM   6599 N  N     . ALA B 1 457 ? 14.329 9.546   2.475   1.00 32.92  ? 436 ALA B N     1 
ATOM   6600 C  CA    . ALA B 1 457 ? 15.520 9.491   3.357   1.00 32.49  ? 436 ALA B CA    1 
ATOM   6601 C  C     . ALA B 1 457 ? 15.068 9.500   4.822   1.00 34.25  ? 436 ALA B C     1 
ATOM   6602 O  O     . ALA B 1 457 ? 15.633 8.714   5.632   1.00 32.52  ? 436 ALA B O     1 
ATOM   6603 C  CB    . ALA B 1 457 ? 16.451 10.640  3.061   1.00 29.43  ? 436 ALA B CB    1 
ATOM   6604 N  N     . ILE B 1 458 ? 14.140 10.409  5.150   1.00 34.18  ? 437 ILE B N     1 
ATOM   6605 C  CA    . ILE B 1 458 ? 13.553 10.578  6.510   1.00 34.31  ? 437 ILE B CA    1 
ATOM   6606 C  C     . ILE B 1 458 ? 12.793 9.304   6.910   1.00 31.77  ? 437 ILE B C     1 
ATOM   6607 O  O     . ILE B 1 458 ? 13.070 8.783   7.994   1.00 35.75  ? 437 ILE B O     1 
ATOM   6608 C  CB    . ILE B 1 458 ? 12.675 11.835  6.602   1.00 31.99  ? 437 ILE B CB    1 
ATOM   6609 C  CG1   . ILE B 1 458 ? 13.498 13.100  6.344   1.00 32.05  ? 437 ILE B CG1   1 
ATOM   6610 C  CG2   . ILE B 1 458 ? 11.983 11.869  7.965   1.00 31.94  ? 437 ILE B CG2   1 
ATOM   6611 C  CD1   . ILE B 1 458 ? 12.674 14.393  6.279   1.00 33.45  ? 437 ILE B CD1   1 
ATOM   6612 N  N     . GLU B 1 459 ? 11.895 8.793   6.082   1.00 30.84  ? 438 GLU B N     1 
ATOM   6613 C  CA    . GLU B 1 459 ? 11.219 7.515   6.380   1.00 34.93  ? 438 GLU B CA    1 
ATOM   6614 C  C     . GLU B 1 459 ? 12.291 6.482   6.754   1.00 38.17  ? 438 GLU B C     1 
ATOM   6615 O  O     . GLU B 1 459 ? 12.081 5.749   7.708   1.00 37.32  ? 438 GLU B O     1 
ATOM   6616 C  CB    . GLU B 1 459 ? 10.396 7.007   5.196   1.00 39.10  ? 438 GLU B CB    1 
ATOM   6617 C  CG    . GLU B 1 459 ? 9.748  5.656   5.486   1.00 40.75  ? 438 GLU B CG    1 
ATOM   6618 C  CD    . GLU B 1 459 ? 9.191  4.904   4.293   1.00 48.78  ? 438 GLU B CD    1 
ATOM   6619 O  OE1   . GLU B 1 459 ? 8.661  5.547   3.375   1.00 52.37  ? 438 GLU B OE1   1 
ATOM   6620 O  OE2   . GLU B 1 459 ? 9.309  3.658   4.282   1.00 64.82  ? 438 GLU B OE2   1 
ATOM   6621 N  N     . SER B 1 460 ? 13.383 6.417   5.995   1.00 37.91  ? 439 SER B N     1 
ATOM   6622 C  CA    . SER B 1 460 ? 14.412 5.352   6.116   1.00 40.94  ? 439 SER B CA    1 
ATOM   6623 C  C     . SER B 1 460 ? 15.088 5.490   7.484   1.00 37.88  ? 439 SER B C     1 
ATOM   6624 O  O     . SER B 1 460 ? 15.215 4.479   8.172   1.00 37.99  ? 439 SER B O     1 
ATOM   6625 C  CB    . SER B 1 460 ? 15.398 5.369   4.947   1.00 35.75  ? 439 SER B CB    1 
ATOM   6626 O  OG    . SER B 1 460 ? 16.497 6.236   5.204   1.00 34.31  ? 439 SER B OG    1 
ATOM   6627 N  N     . GLY B 1 461 ? 15.445 6.713   7.876   1.00 40.76  ? 440 GLY B N     1 
ATOM   6628 C  CA    . GLY B 1 461 ? 15.972 7.035   9.221   1.00 42.88  ? 440 GLY B CA    1 
ATOM   6629 C  C     . GLY B 1 461 ? 15.045 6.596   10.359  1.00 42.12  ? 440 GLY B C     1 
ATOM   6630 O  O     . GLY B 1 461 ? 15.586 6.158   11.393  1.00 38.93  ? 440 GLY B O     1 
ATOM   6631 N  N     . GLN B 1 462 ? 13.716 6.736   10.193  1.00 41.66  ? 441 GLN B N     1 
ATOM   6632 C  CA    . GLN B 1 462 ? 12.681 6.414   11.221  1.00 43.57  ? 441 GLN B CA    1 
ATOM   6633 C  C     . GLN B 1 462 ? 12.577 4.889   11.346  1.00 42.32  ? 441 GLN B C     1 
ATOM   6634 O  O     . GLN B 1 462 ? 12.446 4.389   12.475  1.00 41.52  ? 441 GLN B O     1 
ATOM   6635 C  CB    . GLN B 1 462 ? 11.288 6.973   10.875  1.00 43.50  ? 441 GLN B CB    1 
ATOM   6636 C  CG    . GLN B 1 462 ? 11.131 8.491   11.021  1.00 47.91  ? 441 GLN B CG    1 
ATOM   6637 C  CD    . GLN B 1 462 ? 9.867  9.030   10.376  1.00 55.22  ? 441 GLN B CD    1 
ATOM   6638 O  OE1   . GLN B 1 462 ? 8.987  8.263   9.976   1.00 57.26  ? 441 GLN B OE1   1 
ATOM   6639 N  NE2   . GLN B 1 462 ? 9.750  10.356  10.258  1.00 50.89  ? 441 GLN B NE2   1 
ATOM   6640 N  N     . ARG B 1 463 ? 12.594 4.173   10.221  1.00 45.26  ? 442 ARG B N     1 
ATOM   6641 C  CA    . ARG B 1 463 ? 12.504 2.686   10.196  1.00 48.70  ? 442 ARG B CA    1 
ATOM   6642 C  C     . ARG B 1 463 ? 13.737 2.112   10.918  1.00 46.85  ? 442 ARG B C     1 
ATOM   6643 O  O     . ARG B 1 463 ? 13.567 1.286   11.825  1.00 52.30  ? 442 ARG B O     1 
ATOM   6644 C  CB    . ARG B 1 463 ? 12.379 2.154   8.764   1.00 47.59  ? 442 ARG B CB    1 
ATOM   6645 C  CG    . ARG B 1 463 ? 11.757 0.769   8.672   1.00 46.88  ? 442 ARG B CG    1 
ATOM   6646 C  CD    . ARG B 1 463 ? 12.562 -0.205  7.848   1.00 47.18  ? 442 ARG B CD    1 
ATOM   6647 N  NE    . ARG B 1 463 ? 13.392 0.455   6.837   1.00 49.56  ? 442 ARG B NE    1 
ATOM   6648 C  CZ    . ARG B 1 463 ? 14.725 0.437   6.780   1.00 48.53  ? 442 ARG B CZ    1 
ATOM   6649 N  NH1   . ARG B 1 463 ? 15.454 -0.214  7.673   1.00 56.25  ? 442 ARG B NH1   1 
ATOM   6650 N  NH2   . ARG B 1 463 ? 15.344 1.083   5.814   1.00 49.43  ? 442 ARG B NH2   1 
ATOM   6651 N  N     . ALA B 1 464 ? 14.934 2.570   10.558  1.00 45.16  ? 443 ALA B N     1 
ATOM   6652 C  CA    . ALA B 1 464 ? 16.202 1.969   11.024  1.00 49.27  ? 443 ALA B CA    1 
ATOM   6653 C  C     . ALA B 1 464 ? 16.338 2.213   12.530  1.00 46.93  ? 443 ALA B C     1 
ATOM   6654 O  O     . ALA B 1 464 ? 16.760 1.283   13.215  1.00 40.63  ? 443 ALA B O     1 
ATOM   6655 C  CB    . ALA B 1 464 ? 17.381 2.517   10.250  1.00 48.07  ? 443 ALA B CB    1 
ATOM   6656 N  N     . ALA B 1 465 ? 16.020 3.424   13.004  1.00 42.86  ? 444 ALA B N     1 
ATOM   6657 C  CA    . ALA B 1 465 ? 16.012 3.796   14.436  1.00 47.08  ? 444 ALA B CA    1 
ATOM   6658 C  C     . ALA B 1 465 ? 15.106 2.831   15.230  1.00 48.55  ? 444 ALA B C     1 
ATOM   6659 O  O     . ALA B 1 465 ? 15.559 2.334   16.274  1.00 51.65  ? 444 ALA B O     1 
ATOM   6660 C  CB    . ALA B 1 465 ? 15.619 5.247   14.597  1.00 47.59  ? 444 ALA B CB    1 
ATOM   6661 N  N     . ALA B 1 466 ? 13.908 2.520   14.726  1.00 45.46  ? 445 ALA B N     1 
ATOM   6662 C  CA    . ALA B 1 466 ? 12.951 1.570   15.335  1.00 44.40  ? 445 ALA B CA    1 
ATOM   6663 C  C     . ALA B 1 466 ? 13.563 0.163   15.446  1.00 46.08  ? 445 ALA B C     1 
ATOM   6664 O  O     . ALA B 1 466 ? 13.486 -0.456  16.530  1.00 48.09  ? 445 ALA B O     1 
ATOM   6665 C  CB    . ALA B 1 466 ? 11.678 1.562   14.525  1.00 44.65  ? 445 ALA B CB    1 
ATOM   6666 N  N     . GLU B 1 467 ? 14.102 -0.384  14.362  1.00 44.90  ? 446 GLU B N     1 
ATOM   6667 C  CA    . GLU B 1 467 ? 14.652 -1.767  14.381  1.00 44.73  ? 446 GLU B CA    1 
ATOM   6668 C  C     . GLU B 1 467 ? 15.703 -1.893  15.490  1.00 43.85  ? 446 GLU B C     1 
ATOM   6669 O  O     . GLU B 1 467 ? 15.634 -2.887  16.219  1.00 49.14  ? 446 GLU B O     1 
ATOM   6670 C  CB    . GLU B 1 467 ? 15.299 -2.125  13.053  1.00 42.68  ? 446 GLU B CB    1 
ATOM   6671 C  CG    . GLU B 1 467 ? 14.317 -2.405  11.941  1.00 44.13  ? 446 GLU B CG    1 
ATOM   6672 C  CD    . GLU B 1 467 ? 14.994 -2.463  10.579  1.00 45.68  ? 446 GLU B CD    1 
ATOM   6673 O  OE1   . GLU B 1 467 ? 16.249 -2.478  10.529  1.00 41.70  ? 446 GLU B OE1   1 
ATOM   6674 O  OE2   . GLU B 1 467 ? 14.273 -2.466  9.575   1.00 51.45  ? 446 GLU B OE2   1 
ATOM   6675 N  N     . VAL B 1 468 ? 16.600 -0.901  15.590  1.00 41.74  ? 447 VAL B N     1 
ATOM   6676 C  CA    . VAL B 1 468 ? 17.785 -0.790  16.496  1.00 44.17  ? 447 VAL B CA    1 
ATOM   6677 C  C     . VAL B 1 468 ? 17.327 -0.626  17.956  1.00 50.61  ? 447 VAL B C     1 
ATOM   6678 O  O     . VAL B 1 468 ? 17.892 -1.344  18.832  1.00 51.35  ? 447 VAL B O     1 
ATOM   6679 C  CB    . VAL B 1 468 ? 18.706 0.375   16.050  1.00 46.45  ? 447 VAL B CB    1 
ATOM   6680 C  CG1   . VAL B 1 468 ? 19.702 0.812   17.106  1.00 47.50  ? 447 VAL B CG1   1 
ATOM   6681 C  CG2   . VAL B 1 468 ? 19.466 0.058   14.764  1.00 49.44  ? 447 VAL B CG2   1 
ATOM   6682 N  N     . LEU B 1 469 ? 16.409 0.318   18.225  1.00 51.89  ? 448 LEU B N     1 
ATOM   6683 C  CA    . LEU B 1 469 ? 15.813 0.574   19.571  1.00 49.68  ? 448 LEU B CA    1 
ATOM   6684 C  C     . LEU B 1 469 ? 15.184 -0.719  20.104  1.00 49.43  ? 448 LEU B C     1 
ATOM   6685 O  O     . LEU B 1 469 ? 15.433 -1.046  21.284  1.00 52.07  ? 448 LEU B O     1 
ATOM   6686 C  CB    . LEU B 1 469 ? 14.761 1.690   19.499  1.00 46.97  ? 448 LEU B CB    1 
ATOM   6687 C  CG    . LEU B 1 469 ? 15.285 3.114   19.285  1.00 49.91  ? 448 LEU B CG    1 
ATOM   6688 C  CD1   . LEU B 1 469 ? 14.160 4.129   19.453  1.00 50.84  ? 448 LEU B CD1   1 
ATOM   6689 C  CD2   . LEU B 1 469 ? 16.450 3.456   20.211  1.00 49.51  ? 448 LEU B CD2   1 
ATOM   6690 N  N     . ALA B 1 470 ? 14.414 -1.425  19.271  1.00 44.60  ? 449 ALA B N     1 
ATOM   6691 C  CA    . ALA B 1 470 ? 13.793 -2.726  19.606  1.00 44.05  ? 449 ALA B CA    1 
ATOM   6692 C  C     . ALA B 1 470 ? 14.872 -3.732  20.039  1.00 52.09  ? 449 ALA B C     1 
ATOM   6693 O  O     . ALA B 1 470 ? 14.697 -4.375  21.115  1.00 55.26  ? 449 ALA B O     1 
ATOM   6694 C  CB    . ALA B 1 470 ? 12.992 -3.238  18.431  1.00 40.73  ? 449 ALA B CB    1 
ATOM   6695 N  N     . ALA B 1 471 ? 15.954 -3.852  19.257  1.00 53.64  ? 450 ALA B N     1 
ATOM   6696 C  CA    . ALA B 1 471 ? 16.973 -4.922  19.387  1.00 54.69  ? 450 ALA B CA    1 
ATOM   6697 C  C     . ALA B 1 471 ? 17.849 -4.667  20.622  1.00 51.08  ? 450 ALA B C     1 
ATOM   6698 O  O     . ALA B 1 471 ? 18.145 -5.622  21.351  1.00 52.34  ? 450 ALA B O     1 
ATOM   6699 C  CB    . ALA B 1 471 ? 17.788 -5.019  18.124  1.00 55.55  ? 450 ALA B CB    1 
ATOM   6700 N  N     . LEU B 1 472 ? 18.229 -3.421  20.878  1.00 52.12  ? 451 LEU B N     1 
ATOM   6701 C  CA    . LEU B 1 472 ? 18.967 -3.085  22.118  1.00 62.84  ? 451 LEU B CA    1 
ATOM   6702 C  C     . LEU B 1 472 ? 18.230 -3.767  23.293  1.00 78.96  ? 451 LEU B C     1 
ATOM   6703 O  O     . LEU B 1 472 ? 18.899 -4.538  24.022  1.00 93.50  ? 451 LEU B O     1 
ATOM   6704 C  CB    . LEU B 1 472 ? 19.072 -1.562  22.275  1.00 58.62  ? 451 LEU B CB    1 
ATOM   6705 C  CG    . LEU B 1 472 ? 19.992 -0.823  21.295  1.00 57.44  ? 451 LEU B CG    1 
ATOM   6706 C  CD1   . LEU B 1 472 ? 19.928 0.683   21.513  1.00 55.58  ? 451 LEU B CD1   1 
ATOM   6707 C  CD2   . LEU B 1 472 ? 21.436 -1.274  21.407  1.00 54.65  ? 451 LEU B CD2   1 
ATOM   6708 N  N     . GLY B 1 473 ? 16.900 -3.575  23.402  1.00 81.38  ? 452 GLY B N     1 
ATOM   6709 C  CA    . GLY B 1 473 ? 15.991 -4.216  24.384  1.00 79.49  ? 452 GLY B CA    1 
ATOM   6710 C  C     . GLY B 1 473 ? 16.112 -5.736  24.400  1.00 78.66  ? 452 GLY B C     1 
ATOM   6711 O  O     . GLY B 1 473 ? 15.239 -6.495  23.977  1.00 70.50  ? 452 GLY B O     1 
HETATM 6712 P  PA    . FAD C 2 .   ? 41.920 -12.325 -10.601 1.00 25.75  ? 501 FAD A PA    1 
HETATM 6713 O  O1A   . FAD C 2 .   ? 40.604 -12.032 -9.987  1.00 24.84  ? 501 FAD A O1A   1 
HETATM 6714 O  O2A   . FAD C 2 .   ? 42.349 -13.773 -10.558 1.00 25.82  ? 501 FAD A O2A   1 
HETATM 6715 O  O5B   . FAD C 2 .   ? 43.097 -11.581 -9.774  1.00 26.13  ? 501 FAD A O5B   1 
HETATM 6716 C  C5B   . FAD C 2 .   ? 42.822 -10.459 -8.937  1.00 28.13  ? 501 FAD A C5B   1 
HETATM 6717 C  C4B   . FAD C 2 .   ? 43.654 -10.502 -7.661  1.00 26.97  ? 501 FAD A C4B   1 
HETATM 6718 O  O4B   . FAD C 2 .   ? 43.598 -9.211  -6.954  1.00 29.70  ? 501 FAD A O4B   1 
HETATM 6719 C  C3B   . FAD C 2 .   ? 43.202 -11.574 -6.706  1.00 25.70  ? 501 FAD A C3B   1 
HETATM 6720 O  O3B   . FAD C 2 .   ? 44.343 -12.432 -6.348  1.00 25.92  ? 501 FAD A O3B   1 
HETATM 6721 C  C2B   . FAD C 2 .   ? 42.665 -10.795 -5.525  1.00 26.09  ? 501 FAD A C2B   1 
HETATM 6722 O  O2B   . FAD C 2 .   ? 42.940 -11.400 -4.262  1.00 27.44  ? 501 FAD A O2B   1 
HETATM 6723 C  C1B   . FAD C 2 .   ? 43.423 -9.492  -5.543  1.00 27.80  ? 501 FAD A C1B   1 
HETATM 6724 N  N9A   . FAD C 2 .   ? 42.798 -8.273  -4.936  1.00 28.33  ? 501 FAD A N9A   1 
HETATM 6725 C  C8A   . FAD C 2 .   ? 41.537 -7.825  -5.025  1.00 28.73  ? 501 FAD A C8A   1 
HETATM 6726 N  N7A   . FAD C 2 .   ? 41.430 -6.631  -4.370  1.00 29.47  ? 501 FAD A N7A   1 
HETATM 6727 C  C5A   . FAD C 2 .   ? 42.664 -6.306  -3.908  1.00 28.14  ? 501 FAD A C5A   1 
HETATM 6728 C  C6A   . FAD C 2 .   ? 43.174 -5.247  -3.167  1.00 30.21  ? 501 FAD A C6A   1 
HETATM 6729 N  N6A   . FAD C 2 .   ? 42.380 -4.212  -2.771  1.00 30.75  ? 501 FAD A N6A   1 
HETATM 6730 N  N1A   . FAD C 2 .   ? 44.496 -5.238  -2.824  1.00 27.08  ? 501 FAD A N1A   1 
HETATM 6731 C  C2A   . FAD C 2 .   ? 45.274 -6.279  -3.214  1.00 28.48  ? 501 FAD A C2A   1 
HETATM 6732 N  N3A   . FAD C 2 .   ? 44.816 -7.309  -3.938  1.00 24.95  ? 501 FAD A N3A   1 
HETATM 6733 C  C4A   . FAD C 2 .   ? 43.510 -7.346  -4.268  1.00 27.60  ? 501 FAD A C4A   1 
HETATM 6734 N  N1    . FAD C 2 .   ? 38.871 -19.019 -17.119 1.00 28.75  ? 501 FAD A N1    1 
HETATM 6735 C  C2    . FAD C 2 .   ? 39.455 -19.912 -17.965 1.00 30.26  ? 501 FAD A C2    1 
HETATM 6736 O  O2    . FAD C 2 .   ? 40.361 -19.497 -18.736 1.00 28.29  ? 501 FAD A O2    1 
HETATM 6737 N  N3    . FAD C 2 .   ? 39.042 -21.229 -17.975 1.00 27.25  ? 501 FAD A N3    1 
HETATM 6738 C  C4    . FAD C 2 .   ? 38.057 -21.658 -17.141 1.00 27.44  ? 501 FAD A C4    1 
HETATM 6739 O  O4    . FAD C 2 .   ? 37.658 -22.849 -17.144 1.00 29.52  ? 501 FAD A O4    1 
HETATM 6740 C  C4X   . FAD C 2 .   ? 37.431 -20.774 -16.288 1.00 27.58  ? 501 FAD A C4X   1 
HETATM 6741 N  N5    . FAD C 2 .   ? 36.444 -21.224 -15.459 1.00 24.80  ? 501 FAD A N5    1 
HETATM 6742 C  C5X   . FAD C 2 .   ? 36.099 -20.359 -14.447 1.00 28.53  ? 501 FAD A C5X   1 
HETATM 6743 C  C6    . FAD C 2 .   ? 35.328 -20.829 -13.375 1.00 26.62  ? 501 FAD A C6    1 
HETATM 6744 C  C7    . FAD C 2 .   ? 35.149 -20.121 -12.176 1.00 26.03  ? 501 FAD A C7    1 
HETATM 6745 C  C7M   . FAD C 2 .   ? 34.284 -20.744 -11.089 1.00 24.00  ? 501 FAD A C7M   1 
HETATM 6746 C  C8    . FAD C 2 .   ? 35.813 -18.903 -12.054 1.00 28.13  ? 501 FAD A C8    1 
HETATM 6747 C  C8M   . FAD C 2 .   ? 35.803 -18.041 -10.813 1.00 30.12  ? 501 FAD A C8M   1 
HETATM 6748 C  C9    . FAD C 2 .   ? 36.588 -18.410 -13.124 1.00 28.97  ? 501 FAD A C9    1 
HETATM 6749 C  C9A   . FAD C 2 .   ? 36.752 -19.094 -14.317 1.00 26.74  ? 501 FAD A C9A   1 
HETATM 6750 N  N10   . FAD C 2 .   ? 37.367 -18.539 -15.379 1.00 27.32  ? 501 FAD A N10   1 
HETATM 6751 C  C10   . FAD C 2 .   ? 37.887 -19.427 -16.259 1.00 29.00  ? 501 FAD A C10   1 
HETATM 6752 C  "C1'" . FAD C 2 .   ? 37.818 -17.101 -15.447 1.00 27.30  ? 501 FAD A "C1'" 1 
HETATM 6753 C  "C2'" . FAD C 2 .   ? 39.303 -16.884 -15.133 1.00 25.99  ? 501 FAD A "C2'" 1 
HETATM 6754 O  "O2'" . FAD C 2 .   ? 39.570 -17.601 -13.948 1.00 26.26  ? 501 FAD A "O2'" 1 
HETATM 6755 C  "C3'" . FAD C 2 .   ? 39.589 -15.426 -14.860 1.00 25.85  ? 501 FAD A "C3'" 1 
HETATM 6756 O  "O3'" . FAD C 2 .   ? 39.185 -14.655 -15.993 1.00 29.80  ? 501 FAD A "O3'" 1 
HETATM 6757 C  "C4'" . FAD C 2 .   ? 41.037 -15.061 -14.608 1.00 24.54  ? 501 FAD A "C4'" 1 
HETATM 6758 O  "O4'" . FAD C 2 .   ? 41.564 -15.795 -13.547 1.00 21.40  ? 501 FAD A "O4'" 1 
HETATM 6759 C  "C5'" . FAD C 2 .   ? 41.162 -13.601 -14.220 1.00 23.10  ? 501 FAD A "C5'" 1 
HETATM 6760 O  "O5'" . FAD C 2 .   ? 42.483 -13.302 -13.804 1.00 25.05  ? 501 FAD A "O5'" 1 
HETATM 6761 P  P     . FAD C 2 .   ? 42.825 -11.787 -13.338 1.00 27.14  ? 501 FAD A P     1 
HETATM 6762 O  O1P   . FAD C 2 .   ? 44.265 -11.742 -12.912 1.00 27.92  ? 501 FAD A O1P   1 
HETATM 6763 O  O2P   . FAD C 2 .   ? 42.278 -10.853 -14.312 1.00 25.41  ? 501 FAD A O2P   1 
HETATM 6764 O  O3P   . FAD C 2 .   ? 41.861 -11.615 -12.031 1.00 24.58  ? 501 FAD A O3P   1 
HETATM 6765 MG MG    . MG  D 3 .   ? 30.301 -36.100 -25.938 1.00 56.65  ? 502 MG  A MG    1 
HETATM 6766 P  PA    . FAD E 2 .   ? 22.874 11.357  1.554   1.00 30.38  ? 501 FAD B PA    1 
HETATM 6767 O  O1A   . FAD E 2 .   ? 23.683 10.853  0.356   1.00 35.59  ? 501 FAD B O1A   1 
HETATM 6768 O  O2A   . FAD E 2 .   ? 22.399 12.804  1.587   1.00 35.08  ? 501 FAD B O2A   1 
HETATM 6769 O  O5B   . FAD E 2 .   ? 23.813 11.197  2.850   1.00 34.35  ? 501 FAD B O5B   1 
HETATM 6770 C  C5B   . FAD E 2 .   ? 24.828 10.211  2.958   1.00 35.14  ? 501 FAD B C5B   1 
HETATM 6771 C  C4B   . FAD E 2 .   ? 25.907 10.795  3.821   1.00 33.87  ? 501 FAD B C4B   1 
HETATM 6772 O  O4B   . FAD E 2 .   ? 26.949 9.826   4.054   1.00 31.37  ? 501 FAD B O4B   1 
HETATM 6773 C  C3B   . FAD E 2 .   ? 26.537 11.980  3.127   1.00 34.24  ? 501 FAD B C3B   1 
HETATM 6774 O  O3B   . FAD E 2 .   ? 26.638 13.038  4.069   1.00 31.58  ? 501 FAD B O3B   1 
HETATM 6775 C  C2B   . FAD E 2 .   ? 27.930 11.501  2.747   1.00 32.83  ? 501 FAD B C2B   1 
HETATM 6776 O  O2B   . FAD E 2 .   ? 28.811 12.603  2.839   1.00 34.14  ? 501 FAD B O2B   1 
HETATM 6777 C  C1B   . FAD E 2 .   ? 28.236 10.442  3.795   1.00 34.92  ? 501 FAD B C1B   1 
HETATM 6778 N  N9A   . FAD E 2 .   ? 29.147 9.292   3.530   1.00 37.17  ? 501 FAD B N9A   1 
HETATM 6779 C  C8A   . FAD E 2 .   ? 29.229 8.488   2.450   1.00 37.30  ? 501 FAD B C8A   1 
HETATM 6780 N  N7A   . FAD E 2 .   ? 30.136 7.505   2.680   1.00 36.36  ? 501 FAD B N7A   1 
HETATM 6781 C  C5A   . FAD E 2 .   ? 30.600 7.702   3.943   1.00 37.40  ? 501 FAD B C5A   1 
HETATM 6782 C  C6A   . FAD E 2 .   ? 31.532 7.058   4.722   1.00 38.38  ? 501 FAD B C6A   1 
HETATM 6783 N  N6A   . FAD E 2 .   ? 32.183 5.961   4.239   1.00 39.08  ? 501 FAD B N6A   1 
HETATM 6784 N  N1A   . FAD E 2 .   ? 31.772 7.507   5.989   1.00 38.90  ? 501 FAD B N1A   1 
HETATM 6785 C  C2A   . FAD E 2 .   ? 31.143 8.575   6.478   1.00 38.81  ? 501 FAD B C2A   1 
HETATM 6786 N  N3A   . FAD E 2 .   ? 30.235 9.248   5.757   1.00 38.80  ? 501 FAD B N3A   1 
HETATM 6787 C  C4A   . FAD E 2 .   ? 29.958 8.811   4.477   1.00 40.92  ? 501 FAD B C4A   1 
HETATM 6788 N  N1    . FAD E 2 .   ? 15.239 15.247  -3.654  1.00 32.52  ? 501 FAD B N1    1 
HETATM 6789 C  C2    . FAD E 2 .   ? 14.136 15.962  -3.395  1.00 35.93  ? 501 FAD B C2    1 
HETATM 6790 O  O2    . FAD E 2 .   ? 13.361 15.585  -2.475  1.00 36.68  ? 501 FAD B O2    1 
HETATM 6791 N  N3    . FAD E 2 .   ? 13.872 17.061  -4.142  1.00 35.69  ? 501 FAD B N3    1 
HETATM 6792 C  C4    . FAD E 2 .   ? 14.716 17.466  -5.098  1.00 35.07  ? 501 FAD B C4    1 
HETATM 6793 O  O4    . FAD E 2 .   ? 14.420 18.502  -5.704  1.00 36.76  ? 501 FAD B O4    1 
HETATM 6794 C  C4X   . FAD E 2 .   ? 15.853 16.707  -5.386  1.00 35.87  ? 501 FAD B C4X   1 
HETATM 6795 N  N5    . FAD E 2 .   ? 16.761 17.022  -6.383  1.00 36.11  ? 501 FAD B N5    1 
HETATM 6796 C  C5X   . FAD E 2 .   ? 17.937 16.343  -6.493  1.00 30.86  ? 501 FAD B C5X   1 
HETATM 6797 C  C6    . FAD E 2 .   ? 18.943 16.959  -7.221  1.00 32.86  ? 501 FAD B C6    1 
HETATM 6798 C  C7    . FAD E 2 .   ? 20.293 16.662  -7.049  1.00 31.25  ? 501 FAD B C7    1 
HETATM 6799 C  C7M   . FAD E 2 .   ? 21.259 17.397  -7.943  1.00 34.11  ? 501 FAD B C7M   1 
HETATM 6800 C  C8    . FAD E 2 .   ? 20.680 15.720  -6.113  1.00 29.87  ? 501 FAD B C8    1 
HETATM 6801 C  C8M   . FAD E 2 .   ? 22.125 15.325  -5.891  1.00 33.10  ? 501 FAD B C8M   1 
HETATM 6802 C  C9    . FAD E 2 .   ? 19.659 15.075  -5.391  1.00 32.60  ? 501 FAD B C9    1 
HETATM 6803 C  C9A   . FAD E 2 .   ? 18.281 15.380  -5.558  1.00 31.53  ? 501 FAD B C9A   1 
HETATM 6804 N  N10   . FAD E 2 .   ? 17.259 14.853  -4.793  1.00 35.61  ? 501 FAD B N10   1 
HETATM 6805 C  C10   . FAD E 2 .   ? 16.120 15.595  -4.597  1.00 33.62  ? 501 FAD B C10   1 
HETATM 6806 C  "C1'" . FAD E 2 .   ? 17.425 13.660  -3.927  1.00 31.43  ? 501 FAD B "C1'" 1 
HETATM 6807 C  "C2'" . FAD E 2 .   ? 17.879 13.950  -2.481  1.00 31.31  ? 501 FAD B "C2'" 1 
HETATM 6808 O  "O2'" . FAD E 2 .   ? 18.979 14.904  -2.424  1.00 27.28  ? 501 FAD B "O2'" 1 
HETATM 6809 C  "C3'" . FAD E 2 .   ? 18.250 12.603  -1.796  1.00 31.46  ? 501 FAD B "C3'" 1 
HETATM 6810 O  "O3'" . FAD E 2 .   ? 17.277 11.543  -2.020  1.00 31.03  ? 501 FAD B "O3'" 1 
HETATM 6811 C  "C4'" . FAD E 2 .   ? 18.489 12.718  -0.284  1.00 32.48  ? 501 FAD B "C4'" 1 
HETATM 6812 O  "O4'" . FAD E 2 .   ? 19.244 13.922  0.034   1.00 28.50  ? 501 FAD B "O4'" 1 
HETATM 6813 C  "C5'" . FAD E 2 .   ? 19.174 11.422  0.219   1.00 29.72  ? 501 FAD B "C5'" 1 
HETATM 6814 O  "O5'" . FAD E 2 .   ? 19.540 11.478  1.606   1.00 31.12  ? 501 FAD B "O5'" 1 
HETATM 6815 P  P     . FAD E 2 .   ? 20.283 10.236  2.333   1.00 30.29  ? 501 FAD B P     1 
HETATM 6816 O  O1P   . FAD E 2 .   ? 20.487 10.642  3.778   1.00 29.92  ? 501 FAD B O1P   1 
HETATM 6817 O  O2P   . FAD E 2 .   ? 19.437 9.015   1.926   1.00 27.69  ? 501 FAD B O2P   1 
HETATM 6818 O  O3P   . FAD E 2 .   ? 21.704 10.236  1.582   1.00 28.44  ? 501 FAD B O3P   1 
HETATM 6819 N  N     . ABN F 4 .   ? 14.281 15.440  -7.722  1.00 43.52  ? 502 ABN B N     1 
HETATM 6820 C  C     . ABN F 4 .   ? 13.754 14.865  -9.003  1.00 48.42  ? 502 ABN B C     1 
HETATM 6821 C  C1    . ABN F 4 .   ? 13.782 15.858  -10.161 1.00 51.68  ? 502 ABN B C1    1 
HETATM 6822 C  C2    . ABN F 4 .   ? 12.669 16.067  -10.992 1.00 53.30  ? 502 ABN B C2    1 
HETATM 6823 C  C3    . ABN F 4 .   ? 12.706 16.980  -12.067 1.00 58.52  ? 502 ABN B C3    1 
HETATM 6824 C  C4    . ABN F 4 .   ? 13.859 17.728  -12.322 1.00 55.61  ? 502 ABN B C4    1 
HETATM 6825 C  C5    . ABN F 4 .   ? 14.974 17.533  -11.484 1.00 56.37  ? 502 ABN B C5    1 
HETATM 6826 C  C6    . ABN F 4 .   ? 14.935 16.614  -10.424 1.00 51.50  ? 502 ABN B C6    1 
HETATM 6827 MG MG    . MG  G 3 .   ? 3.511  26.726  -15.915 1.00 48.29  ? 503 MG  B MG    1 
HETATM 6828 O  O     . HOH H 5 .   ? 33.510 -20.877 -22.567 1.00 28.01  ? 601 HOH A O     1 
HETATM 6829 O  O     . HOH H 5 .   ? 50.742 -25.514 -23.561 1.00 37.01  ? 602 HOH A O     1 
HETATM 6830 O  O     . HOH H 5 .   ? 31.531 -36.285 -27.679 1.00 50.97  ? 603 HOH A O     1 
HETATM 6831 O  O     . HOH H 5 .   ? 43.482 -39.545 -8.439  1.00 37.01  ? 604 HOH A O     1 
HETATM 6832 O  O     . HOH H 5 .   ? 43.838 -15.073 -12.087 1.00 32.42  ? 605 HOH A O     1 
HETATM 6833 O  O     . HOH H 5 .   ? 32.023 -27.856 -23.508 1.00 35.33  ? 606 HOH A O     1 
HETATM 6834 O  O     . HOH H 5 .   ? 52.670 4.121   -22.288 1.00 34.71  ? 607 HOH A O     1 
HETATM 6835 O  O     . HOH H 5 .   ? 30.225 9.254   -22.419 1.00 37.31  ? 608 HOH A O     1 
HETATM 6836 O  O     . HOH H 5 .   ? 49.420 -27.946 -12.568 1.00 29.59  ? 609 HOH A O     1 
HETATM 6837 O  O     . HOH H 5 .   ? 22.457 -22.883 -13.233 1.00 30.27  ? 610 HOH A O     1 
HETATM 6838 O  O     . HOH H 5 .   ? 41.780 -3.649  -12.109 1.00 34.52  ? 611 HOH A O     1 
HETATM 6839 O  O     . HOH H 5 .   ? 22.167 -38.732 -1.042  1.00 34.49  ? 612 HOH A O     1 
HETATM 6840 O  O     . HOH H 5 .   ? 30.046 -35.974 -23.973 1.00 55.26  ? 613 HOH A O     1 
HETATM 6841 O  O     . HOH H 5 .   ? 56.533 -28.054 -21.313 1.00 34.34  ? 614 HOH A O     1 
HETATM 6842 O  O     . HOH H 5 .   ? 45.187 -32.695 -23.349 1.00 48.14  ? 615 HOH A O     1 
HETATM 6843 O  O     . HOH H 5 .   ? 18.791 -34.937 -2.874  1.00 27.14  ? 616 HOH A O     1 
HETATM 6844 O  O     . HOH H 5 .   ? 64.434 0.775   -8.618  1.00 46.96  ? 617 HOH A O     1 
HETATM 6845 O  O     . HOH H 5 .   ? 27.401 -18.337 -0.294  1.00 31.30  ? 618 HOH A O     1 
HETATM 6846 O  O     . HOH H 5 .   ? 26.746 -0.535  -8.997  1.00 33.88  ? 619 HOH A O     1 
HETATM 6847 O  O     . HOH H 5 .   ? 32.177 -13.710 -18.300 1.00 30.74  ? 620 HOH A O     1 
HETATM 6848 O  O     . HOH H 5 .   ? 66.027 -2.073  -11.803 1.00 36.94  ? 621 HOH A O     1 
HETATM 6849 O  O     . HOH H 5 .   ? 31.795 -34.224 -25.606 1.00 52.59  ? 622 HOH A O     1 
HETATM 6850 O  O     . HOH H 5 .   ? 41.436 -37.478 -20.335 1.00 44.94  ? 623 HOH A O     1 
HETATM 6851 O  O     . HOH H 5 .   ? 55.869 -19.654 -6.272  1.00 33.17  ? 624 HOH A O     1 
HETATM 6852 O  O     . HOH H 5 .   ? 15.196 -29.779 -17.715 1.00 36.84  ? 625 HOH A O     1 
HETATM 6853 O  O     . HOH H 5 .   ? 44.720 6.455   -7.360  1.00 33.59  ? 626 HOH A O     1 
HETATM 6854 O  O     . HOH H 5 .   ? 58.705 -12.696 -4.290  1.00 41.58  ? 627 HOH A O     1 
HETATM 6855 O  O     . HOH H 5 .   ? 38.809 -21.880 -21.639 1.00 31.42  ? 628 HOH A O     1 
HETATM 6856 O  O     . HOH H 5 .   ? 41.375 -34.029 -10.376 1.00 30.83  ? 629 HOH A O     1 
HETATM 6857 O  O     . HOH H 5 .   ? 62.604 -6.670  -10.684 1.00 41.90  ? 630 HOH A O     1 
HETATM 6858 O  O     . HOH H 5 .   ? 42.819 -27.774 -14.914 1.00 36.42  ? 631 HOH A O     1 
HETATM 6859 O  O     . HOH H 5 .   ? 50.377 -14.499 3.967   1.00 33.91  ? 632 HOH A O     1 
HETATM 6860 O  O     . HOH H 5 .   ? 65.301 0.533   -11.482 1.00 48.84  ? 633 HOH A O     1 
HETATM 6861 O  O     . HOH H 5 .   ? 39.714 -18.034 -30.594 1.00 43.31  ? 634 HOH A O     1 
HETATM 6862 O  O     . HOH H 5 .   ? 39.068 5.423   -24.911 1.00 47.28  ? 635 HOH A O     1 
HETATM 6863 O  O     . HOH H 5 .   ? 28.917 -34.954 -26.837 1.00 68.55  ? 636 HOH A O     1 
HETATM 6864 O  O     . HOH H 5 .   ? 55.516 9.485   -19.451 1.00 46.10  ? 637 HOH A O     1 
HETATM 6865 O  O     . HOH H 5 .   ? 18.569 -42.234 -15.481 1.00 42.42  ? 638 HOH A O     1 
HETATM 6866 O  O     . HOH H 5 .   ? 59.082 -20.938 -12.455 1.00 39.54  ? 639 HOH A O     1 
HETATM 6867 O  O     . HOH H 5 .   ? 41.142 -23.005 -10.422 1.00 35.93  ? 640 HOH A O     1 
HETATM 6868 O  O     . HOH H 5 .   ? 44.913 -37.643 -9.558  1.00 37.29  ? 641 HOH A O     1 
HETATM 6869 O  O     . HOH H 5 .   ? 41.321 -8.949  -12.635 1.00 38.90  ? 642 HOH A O     1 
HETATM 6870 O  O     . HOH H 5 .   ? 45.166 -15.083 -5.059  1.00 22.25  ? 643 HOH A O     1 
HETATM 6871 O  O     . HOH H 5 .   ? 39.914 -12.432 -7.388  1.00 30.89  ? 644 HOH A O     1 
HETATM 6872 O  O     . HOH H 5 .   ? 54.736 -6.746  -22.042 1.00 41.41  ? 645 HOH A O     1 
HETATM 6873 O  O     . HOH H 5 .   ? 8.004  -21.908 -29.891 1.00 46.22  ? 646 HOH A O     1 
HETATM 6874 O  O     . HOH H 5 .   ? 40.761 -1.420  -1.306  1.00 38.41  ? 647 HOH A O     1 
HETATM 6875 O  O     . HOH H 5 .   ? 44.010 -11.781 3.901   1.00 46.49  ? 648 HOH A O     1 
HETATM 6876 O  O     . HOH H 5 .   ? 37.557 -32.299 -11.602 1.00 31.63  ? 649 HOH A O     1 
HETATM 6877 O  O     . HOH H 5 .   ? 38.638 -32.854 -24.989 1.00 39.59  ? 650 HOH A O     1 
HETATM 6878 O  O     . HOH H 5 .   ? 35.685 -23.787 -14.828 1.00 28.61  ? 651 HOH A O     1 
HETATM 6879 O  O     . HOH H 5 .   ? 29.172 -11.823 -15.956 1.00 34.54  ? 652 HOH A O     1 
HETATM 6880 O  O     . HOH H 5 .   ? 30.041 -16.179 -8.251  1.00 35.74  ? 653 HOH A O     1 
HETATM 6881 O  O     . HOH H 5 .   ? 45.874 -10.008 -11.311 1.00 19.53  ? 654 HOH A O     1 
HETATM 6882 O  O     . HOH H 5 .   ? 51.821 -6.269  4.681   1.00 46.63  ? 655 HOH A O     1 
HETATM 6883 O  O     . HOH H 5 .   ? 40.610 -34.294 -12.865 1.00 36.91  ? 656 HOH A O     1 
HETATM 6884 O  O     . HOH H 5 .   ? 28.873 4.068   -33.347 1.00 39.82  ? 657 HOH A O     1 
HETATM 6885 O  O     . HOH H 5 .   ? 17.356 -16.182 -7.729  1.00 48.31  ? 658 HOH A O     1 
HETATM 6886 O  O     . HOH H 5 .   ? 47.197 -36.862 -7.826  1.00 29.73  ? 659 HOH A O     1 
HETATM 6887 O  O     . HOH H 5 .   ? 55.021 -11.869 -18.367 1.00 35.62  ? 660 HOH A O     1 
HETATM 6888 O  O     . HOH H 5 .   ? 30.973 -14.003 -16.041 1.00 31.05  ? 661 HOH A O     1 
HETATM 6889 O  O     . HOH H 5 .   ? 31.274 -35.378 -19.489 1.00 40.83  ? 662 HOH A O     1 
HETATM 6890 O  O     . HOH H 5 .   ? 15.542 -26.981 -3.372  1.00 47.59  ? 663 HOH A O     1 
HETATM 6891 O  O     . HOH H 5 .   ? 53.004 12.719  -13.073 1.00 42.72  ? 664 HOH A O     1 
HETATM 6892 O  O     . HOH H 5 .   ? 36.325 -22.434 -19.975 1.00 31.03  ? 665 HOH A O     1 
HETATM 6893 O  O     . HOH H 5 .   ? 38.254 -13.994 -1.221  1.00 29.81  ? 666 HOH A O     1 
HETATM 6894 O  O     . HOH H 5 .   ? 31.822 -20.705 -0.979  1.00 32.27  ? 667 HOH A O     1 
HETATM 6895 O  O     . HOH H 5 .   ? 38.156 -34.741 -16.544 1.00 39.56  ? 668 HOH A O     1 
HETATM 6896 O  O     . HOH H 5 .   ? 48.519 -29.728 -7.283  1.00 36.81  ? 669 HOH A O     1 
HETATM 6897 O  O     . HOH H 5 .   ? 59.246 9.925   -10.898 1.00 41.20  ? 670 HOH A O     1 
HETATM 6898 O  O     . HOH H 5 .   ? 59.055 -13.061 -1.786  1.00 44.42  ? 671 HOH A O     1 
HETATM 6899 O  O     . HOH H 5 .   ? 64.164 -18.380 -17.342 1.00 56.15  ? 672 HOH A O     1 
HETATM 6900 O  O     . HOH H 5 .   ? 39.623 -3.543  -2.960  1.00 32.69  ? 673 HOH A O     1 
HETATM 6901 O  O     . HOH H 5 .   ? 34.051 -7.480  -0.318  1.00 27.79  ? 674 HOH A O     1 
HETATM 6902 O  O     . HOH H 5 .   ? 35.537 -24.082 -1.180  1.00 43.61  ? 675 HOH A O     1 
HETATM 6903 O  O     . HOH H 5 .   ? 19.598 -37.899 -1.977  1.00 22.31  ? 676 HOH A O     1 
HETATM 6904 O  O     . HOH H 5 .   ? 53.112 -14.207 -20.806 1.00 43.38  ? 677 HOH A O     1 
HETATM 6905 O  O     . HOH H 5 .   ? 65.607 -13.196 -5.245  1.00 45.00  ? 678 HOH A O     1 
HETATM 6906 O  O     . HOH H 5 .   ? 38.561 -12.514 -32.870 1.00 39.33  ? 679 HOH A O     1 
HETATM 6907 O  O     . HOH H 5 .   ? 42.286 -19.338 -20.913 1.00 27.74  ? 680 HOH A O     1 
HETATM 6908 O  O     . HOH H 5 .   ? 19.621 -19.518 -13.273 1.00 42.18  ? 681 HOH A O     1 
HETATM 6909 O  O     . HOH H 5 .   ? 42.254 10.088  -10.109 1.00 49.02  ? 682 HOH A O     1 
HETATM 6910 O  O     . HOH H 5 .   ? 44.805 7.245   -1.021  1.00 43.71  ? 683 HOH A O     1 
HETATM 6911 O  O     . HOH H 5 .   ? 39.511 -30.578 -10.451 1.00 31.12  ? 684 HOH A O     1 
HETATM 6912 O  O     . HOH H 5 .   ? 21.458 -13.359 -12.023 1.00 35.30  ? 685 HOH A O     1 
HETATM 6913 O  O     . HOH H 5 .   ? 35.516 -31.115 -14.938 1.00 31.60  ? 686 HOH A O     1 
HETATM 6914 O  O     . HOH H 5 .   ? 40.177 -35.857 1.067   1.00 39.24  ? 687 HOH A O     1 
HETATM 6915 O  O     . HOH H 5 .   ? 43.370 -4.542  4.906   1.00 31.87  ? 688 HOH A O     1 
HETATM 6916 O  O     . HOH H 5 .   ? 24.638 -12.609 -12.817 1.00 37.67  ? 689 HOH A O     1 
HETATM 6917 O  O     . HOH H 5 .   ? 50.353 -19.117 -3.541  1.00 37.97  ? 690 HOH A O     1 
HETATM 6918 O  O     . HOH H 5 .   ? 19.410 -23.045 -7.231  1.00 43.39  ? 691 HOH A O     1 
HETATM 6919 O  O     . HOH H 5 .   ? 35.295 -17.824 -18.192 1.00 28.64  ? 692 HOH A O     1 
HETATM 6920 O  O     . HOH H 5 .   ? 43.410 -40.584 -5.603  1.00 43.27  ? 693 HOH A O     1 
HETATM 6921 O  O     . HOH H 5 .   ? 10.848 -22.731 -41.078 1.00 44.20  ? 694 HOH A O     1 
HETATM 6922 O  O     . HOH H 5 .   ? 48.841 -11.281 -26.305 1.00 46.04  ? 695 HOH A O     1 
HETATM 6923 O  O     . HOH H 5 .   ? 31.117 -29.780 -27.585 1.00 48.62  ? 696 HOH A O     1 
HETATM 6924 O  O     . HOH H 5 .   ? 32.251 -22.957 -35.783 1.00 55.78  ? 697 HOH A O     1 
HETATM 6925 O  O     . HOH H 5 .   ? 32.017 -6.926  2.410   1.00 29.07  ? 698 HOH A O     1 
HETATM 6926 O  O     . HOH H 5 .   ? 34.058 9.181   -23.628 1.00 36.37  ? 699 HOH A O     1 
HETATM 6927 O  O     . HOH H 5 .   ? 8.282  -15.702 -34.999 1.00 45.56  ? 700 HOH A O     1 
HETATM 6928 O  O     . HOH H 5 .   ? 39.829 -2.378  -13.134 1.00 38.75  ? 701 HOH A O     1 
HETATM 6929 O  O     . HOH H 5 .   ? 45.264 2.237   6.569   1.00 40.01  ? 702 HOH A O     1 
HETATM 6930 O  O     . HOH H 5 .   ? 31.141 -43.516 -3.964  1.00 27.08  ? 703 HOH A O     1 
HETATM 6931 O  O     . HOH H 5 .   ? 39.885 -40.331 -16.794 1.00 46.09  ? 704 HOH A O     1 
HETATM 6932 O  O     . HOH H 5 .   ? 18.192 -29.315 -0.276  1.00 42.51  ? 705 HOH A O     1 
HETATM 6933 O  O     . HOH H 5 .   ? 36.552 -39.755 -23.650 1.00 42.93  ? 706 HOH A O     1 
HETATM 6934 O  O     . HOH H 5 .   ? 43.532 -15.672 2.077   1.00 23.88  ? 707 HOH A O     1 
HETATM 6935 O  O     . HOH H 5 .   ? 13.827 -34.416 -36.497 1.00 44.30  ? 708 HOH A O     1 
HETATM 6936 O  O     . HOH H 5 .   ? 27.797 -44.704 -5.853  1.00 40.62  ? 709 HOH A O     1 
HETATM 6937 O  O     . HOH H 5 .   ? 61.378 -14.674 -16.156 1.00 34.80  ? 710 HOH A O     1 
HETATM 6938 O  O     . HOH H 5 .   ? 52.080 -31.020 -14.748 1.00 48.82  ? 711 HOH A O     1 
HETATM 6939 O  O     . HOH H 5 .   ? 29.280 -3.925  -3.118  1.00 42.20  ? 712 HOH A O     1 
HETATM 6940 O  O     . HOH H 5 .   ? 19.133 -24.013 -4.639  1.00 36.47  ? 713 HOH A O     1 
HETATM 6941 O  O     . HOH H 5 .   ? 47.361 5.862   -0.456  1.00 42.74  ? 714 HOH A O     1 
HETATM 6942 O  O     . HOH H 5 .   ? 24.171 -22.709 -17.254 1.00 45.22  ? 715 HOH A O     1 
HETATM 6943 O  O     . HOH H 5 .   ? 22.188 -46.053 -11.221 1.00 39.93  ? 716 HOH A O     1 
HETATM 6944 O  O     . HOH H 5 .   ? 45.863 -38.520 -12.229 1.00 20.53  ? 717 HOH A O     1 
HETATM 6945 O  O     . HOH H 5 .   ? 35.264 11.949  -16.601 1.00 16.59  ? 718 HOH A O     1 
HETATM 6946 O  O     . HOH H 5 .   ? 39.535 1.133   1.490   1.00 37.37  ? 719 HOH A O     1 
HETATM 6947 O  O     . HOH H 5 .   ? 15.749 -23.376 -14.794 1.00 48.47  ? 720 HOH A O     1 
HETATM 6948 O  O     . HOH H 5 .   ? 43.356 -41.588 -19.214 1.00 43.51  ? 721 HOH A O     1 
HETATM 6949 O  O     . HOH H 5 .   ? 24.411 -16.221 2.225   1.00 46.03  ? 722 HOH A O     1 
HETATM 6950 O  O     . HOH H 5 .   ? 36.863 -43.683 -25.771 1.00 49.17  ? 723 HOH A O     1 
HETATM 6951 O  O     . HOH H 5 .   ? 64.412 -13.989 -9.718  1.00 47.82  ? 724 HOH A O     1 
HETATM 6952 O  O     . HOH H 5 .   ? 38.577 1.155   -33.327 1.00 43.98  ? 725 HOH A O     1 
HETATM 6953 O  O     . HOH H 5 .   ? 52.852 -33.895 -15.781 1.00 48.43  ? 726 HOH A O     1 
HETATM 6954 O  O     . HOH H 5 .   ? 58.903 -23.680 -13.504 1.00 41.81  ? 727 HOH A O     1 
HETATM 6955 O  O     . HOH H 5 .   ? 12.340 -38.699 -13.493 1.00 40.94  ? 728 HOH A O     1 
HETATM 6956 O  O     . HOH H 5 .   ? 34.652 -20.279 -18.336 1.00 32.92  ? 729 HOH A O     1 
HETATM 6957 O  O     . HOH H 5 .   ? 41.264 2.132   -25.075 1.00 35.80  ? 730 HOH A O     1 
HETATM 6958 O  O     . HOH H 5 .   ? 30.596 -44.956 -25.854 1.00 43.65  ? 731 HOH A O     1 
HETATM 6959 O  O     . HOH H 5 .   ? 56.887 -5.355  -22.033 1.00 36.56  ? 732 HOH A O     1 
HETATM 6960 O  O     . HOH H 5 .   ? 45.971 -25.905 -25.105 1.00 45.70  ? 733 HOH A O     1 
HETATM 6961 O  O     . HOH H 5 .   ? 19.904 -43.787 -18.455 1.00 48.53  ? 734 HOH A O     1 
HETATM 6962 O  O     . HOH H 5 .   ? 36.878 -6.885  1.840   1.00 46.68  ? 735 HOH A O     1 
HETATM 6963 O  O     . HOH H 5 .   ? 29.485 -19.650 0.806   1.00 42.20  ? 736 HOH A O     1 
HETATM 6964 O  O     . HOH H 5 .   ? 43.892 -38.668 -19.750 1.00 39.44  ? 737 HOH A O     1 
HETATM 6965 O  O     . HOH H 5 .   ? 37.131 0.559   -35.492 1.00 48.19  ? 738 HOH A O     1 
HETATM 6966 O  O     . HOH I 5 .   ? -1.337 0.287   -4.981  1.00 48.27  ? 601 HOH B O     1 
HETATM 6967 O  O     . HOH I 5 .   ? -0.032 15.626  -8.967  1.00 46.66  ? 602 HOH B O     1 
HETATM 6968 O  O     . HOH I 5 .   ? 14.071 -9.779  2.147   1.00 47.93  ? 603 HOH B O     1 
HETATM 6969 O  O     . HOH I 5 .   ? 6.166  22.440  6.240   1.00 41.54  ? 604 HOH B O     1 
HETATM 6970 O  O     . HOH I 5 .   ? 34.772 7.787   -4.854  1.00 40.09  ? 605 HOH B O     1 
HETATM 6971 O  O     . HOH I 5 .   ? 1.810  26.558  -15.127 1.00 28.59  ? 606 HOH B O     1 
HETATM 6972 O  O     . HOH I 5 .   ? 10.102 14.667  -9.571  1.00 37.48  ? 607 HOH B O     1 
HETATM 6973 O  O     . HOH I 5 .   ? 32.907 15.316  -23.273 1.00 44.35  ? 608 HOH B O     1 
HETATM 6974 O  O     . HOH I 5 .   ? 15.196 19.276  -29.054 1.00 42.79  ? 609 HOH B O     1 
HETATM 6975 O  O     . HOH I 5 .   ? 25.072 -13.224 -4.959  1.00 36.02  ? 610 HOH B O     1 
HETATM 6976 O  O     . HOH I 5 .   ? 20.105 16.215  -20.239 1.00 36.07  ? 611 HOH B O     1 
HETATM 6977 O  O     . HOH I 5 .   ? 33.906 17.918  3.087   1.00 42.03  ? 612 HOH B O     1 
HETATM 6978 O  O     . HOH I 5 .   ? 16.448 27.136  4.939   1.00 37.04  ? 613 HOH B O     1 
HETATM 6979 O  O     . HOH I 5 .   ? 9.991  -6.691  2.210   1.00 41.09  ? 614 HOH B O     1 
HETATM 6980 O  O     . HOH I 5 .   ? 14.901 24.886  -1.752  1.00 34.52  ? 615 HOH B O     1 
HETATM 6981 O  O     . HOH I 5 .   ? 18.125 -14.744 -5.129  1.00 42.35  ? 616 HOH B O     1 
HETATM 6982 O  O     . HOH I 5 .   ? 29.547 23.548  -0.473  1.00 42.63  ? 617 HOH B O     1 
HETATM 6983 O  O     . HOH I 5 .   ? 3.005  27.711  -17.495 1.00 49.50  ? 618 HOH B O     1 
HETATM 6984 O  O     . HOH I 5 .   ? 22.765 20.403  20.935  1.00 51.08  ? 619 HOH B O     1 
HETATM 6985 O  O     . HOH I 5 .   ? -0.054 22.088  -30.822 1.00 53.18  ? 620 HOH B O     1 
HETATM 6986 O  O     . HOH I 5 .   ? 17.980 31.718  -4.517  1.00 38.68  ? 621 HOH B O     1 
HETATM 6987 O  O     . HOH I 5 .   ? 27.428 24.339  1.403   1.00 44.73  ? 622 HOH B O     1 
HETATM 6988 O  O     . HOH I 5 .   ? 6.571  -12.285 -7.520  1.00 44.04  ? 623 HOH B O     1 
HETATM 6989 O  O     . HOH I 5 .   ? 11.256 15.327  -0.813  1.00 27.00  ? 624 HOH B O     1 
HETATM 6990 O  O     . HOH I 5 .   ? 8.423  8.634   2.651   1.00 44.02  ? 625 HOH B O     1 
HETATM 6991 O  O     . HOH I 5 .   ? 14.081 11.719  13.963  1.00 33.72  ? 626 HOH B O     1 
HETATM 6992 O  O     . HOH I 5 .   ? 11.232 7.145   -24.228 1.00 34.26  ? 627 HOH B O     1 
HETATM 6993 O  O     . HOH I 5 .   ? 22.342 9.962   5.635   1.00 29.33  ? 628 HOH B O     1 
HETATM 6994 O  O     . HOH I 5 .   ? 9.961  27.830  -15.220 1.00 31.34  ? 629 HOH B O     1 
HETATM 6995 O  O     . HOH I 5 .   ? 19.518 6.579   -11.383 1.00 32.58  ? 630 HOH B O     1 
HETATM 6996 O  O     . HOH I 5 .   ? 23.476 2.761   3.367   1.00 30.90  ? 631 HOH B O     1 
HETATM 6997 O  O     . HOH I 5 .   ? 11.858 -0.431  -1.189  1.00 51.35  ? 632 HOH B O     1 
HETATM 6998 O  O     . HOH I 5 .   ? 30.916 -5.058  0.689   1.00 37.49  ? 633 HOH B O     1 
HETATM 6999 O  O     . HOH I 5 .   ? 14.910 12.957  -6.792  1.00 35.76  ? 634 HOH B O     1 
HETATM 7000 O  O     . HOH I 5 .   ? 26.018 36.141  -1.380  1.00 49.39  ? 635 HOH B O     1 
HETATM 7001 O  O     . HOH I 5 .   ? 5.631  26.997  -16.214 1.00 32.53  ? 636 HOH B O     1 
HETATM 7002 O  O     . HOH I 5 .   ? 7.619  20.002  -12.818 1.00 35.23  ? 637 HOH B O     1 
HETATM 7003 O  O     . HOH I 5 .   ? 31.930 17.590  -7.635  1.00 43.84  ? 638 HOH B O     1 
HETATM 7004 O  O     . HOH I 5 .   ? 34.248 -5.854  3.183   1.00 34.75  ? 639 HOH B O     1 
HETATM 7005 O  O     . HOH I 5 .   ? 25.619 12.830  -11.012 1.00 45.24  ? 640 HOH B O     1 
HETATM 7006 O  O     . HOH I 5 .   ? 32.431 4.469   1.749   1.00 29.65  ? 641 HOH B O     1 
HETATM 7007 O  O     . HOH I 5 .   ? -3.159 14.120  -13.574 1.00 45.34  ? 642 HOH B O     1 
HETATM 7008 O  O     . HOH I 5 .   ? 9.840  29.878  -21.006 1.00 30.00  ? 643 HOH B O     1 
HETATM 7009 O  O     . HOH I 5 .   ? 27.261 15.740  4.157   1.00 34.55  ? 644 HOH B O     1 
HETATM 7010 O  O     . HOH I 5 .   ? 22.142 39.951  -16.494 1.00 47.00  ? 645 HOH B O     1 
HETATM 7011 O  O     . HOH I 5 .   ? 1.747  34.271  -24.284 1.00 44.09  ? 646 HOH B O     1 
HETATM 7012 O  O     . HOH I 5 .   ? 30.322 -13.245 1.790   1.00 43.17  ? 647 HOH B O     1 
HETATM 7013 O  O     . HOH I 5 .   ? 13.625 11.635  -8.685  1.00 33.67  ? 648 HOH B O     1 
HETATM 7014 O  O     . HOH I 5 .   ? 32.381 12.461  -16.807 1.00 43.08  ? 649 HOH B O     1 
HETATM 7015 O  O     . HOH I 5 .   ? 18.492 38.165  -3.548  1.00 44.18  ? 650 HOH B O     1 
HETATM 7016 O  O     . HOH I 5 .   ? -0.657 13.300  2.205   1.00 48.10  ? 651 HOH B O     1 
HETATM 7017 O  O     . HOH I 5 .   ? 31.281 19.473  -9.827  1.00 39.46  ? 652 HOH B O     1 
HETATM 7018 O  O     . HOH I 5 .   ? 21.096 -7.514  3.787   1.00 39.46  ? 653 HOH B O     1 
HETATM 7019 O  O     . HOH I 5 .   ? 12.283 29.941  -7.917  1.00 39.04  ? 654 HOH B O     1 
HETATM 7020 O  O     . HOH I 5 .   ? 12.952 2.451   4.852   1.00 43.27  ? 655 HOH B O     1 
HETATM 7021 O  O     . HOH I 5 .   ? 24.517 41.621  -16.927 1.00 50.80  ? 656 HOH B O     1 
HETATM 7022 O  O     . HOH I 5 .   ? 2.681  11.062  -2.731  1.00 39.46  ? 657 HOH B O     1 
HETATM 7023 O  O     . HOH I 5 .   ? 4.207  25.975  -7.605  1.00 39.22  ? 658 HOH B O     1 
HETATM 7024 O  O     . HOH I 5 .   ? 18.122 -2.369  8.322   1.00 37.12  ? 659 HOH B O     1 
HETATM 7025 O  O     . HOH I 5 .   ? 29.868 -2.370  22.665  1.00 44.31  ? 660 HOH B O     1 
HETATM 7026 O  O     . HOH I 5 .   ? 5.217  -2.808  4.798   1.00 50.25  ? 661 HOH B O     1 
HETATM 7027 O  O     . HOH I 5 .   ? 16.859 19.676  -7.703  1.00 29.16  ? 662 HOH B O     1 
HETATM 7028 O  O     . HOH I 5 .   ? 32.154 14.612  -1.775  1.00 42.46  ? 663 HOH B O     1 
HETATM 7029 O  O     . HOH I 5 .   ? 29.754 -7.392  8.883   1.00 35.50  ? 664 HOH B O     1 
HETATM 7030 O  O     . HOH I 5 .   ? 38.594 7.609   3.292   1.00 36.02  ? 665 HOH B O     1 
HETATM 7031 O  O     . HOH I 5 .   ? 4.234  25.688  -14.114 1.00 53.06  ? 666 HOH B O     1 
HETATM 7032 O  O     . HOH I 5 .   ? 3.573  25.364  -16.896 1.00 40.96  ? 667 HOH B O     1 
HETATM 7033 O  O     . HOH I 5 .   ? 37.822 7.355   -6.522  1.00 32.85  ? 668 HOH B O     1 
HETATM 7034 O  O     . HOH I 5 .   ? 27.907 10.120  -23.155 1.00 38.79  ? 669 HOH B O     1 
HETATM 7035 O  O     . HOH I 5 .   ? 34.614 3.431   3.182   1.00 41.58  ? 670 HOH B O     1 
HETATM 7036 O  O     . HOH I 5 .   ? 23.559 7.478   -18.828 1.00 39.99  ? 671 HOH B O     1 
HETATM 7037 O  O     . HOH I 5 .   ? 41.378 2.185   5.218   1.00 28.60  ? 672 HOH B O     1 
HETATM 7038 O  O     . HOH I 5 .   ? 16.174 -13.833 -1.727  1.00 38.11  ? 673 HOH B O     1 
HETATM 7039 O  O     . HOH I 5 .   ? 21.002 -9.360  15.782  1.00 49.35  ? 674 HOH B O     1 
HETATM 7040 O  O     . HOH I 5 .   ? 42.130 3.053   9.081   1.00 48.16  ? 675 HOH B O     1 
HETATM 7041 O  O     . HOH I 5 .   ? 21.797 7.000   1.514   1.00 33.85  ? 676 HOH B O     1 
HETATM 7042 O  O     . HOH I 5 .   ? 6.608  -13.325 -12.174 1.00 46.12  ? 677 HOH B O     1 
HETATM 7043 O  O     . HOH I 5 .   ? -0.182 10.963  -9.776  1.00 44.06  ? 678 HOH B O     1 
HETATM 7044 O  O     . HOH I 5 .   ? 27.191 21.502  8.289   1.00 40.12  ? 679 HOH B O     1 
HETATM 7045 O  O     . HOH I 5 .   ? 3.022  20.840  -14.159 1.00 36.39  ? 680 HOH B O     1 
HETATM 7046 O  O     . HOH I 5 .   ? 22.843 15.892  -26.092 1.00 47.28  ? 681 HOH B O     1 
HETATM 7047 O  O     . HOH I 5 .   ? 4.734  16.168  -20.159 1.00 43.81  ? 682 HOH B O     1 
HETATM 7048 O  O     . HOH I 5 .   ? 23.293 -14.363 0.482   1.00 20.24  ? 683 HOH B O     1 
HETATM 7049 O  O     . HOH I 5 .   ? 14.421 36.166  -1.115  1.00 28.52  ? 684 HOH B O     1 
HETATM 7050 O  O     . HOH I 5 .   ? 6.803  23.563  -15.340 1.00 47.19  ? 685 HOH B O     1 
HETATM 7051 O  O     . HOH I 5 .   ? 30.112 32.831  -16.084 1.00 39.69  ? 686 HOH B O     1 
HETATM 7052 O  O     . HOH I 5 .   ? 11.366 15.555  -30.728 1.00 46.34  ? 687 HOH B O     1 
HETATM 7053 O  O     . HOH I 5 .   ? 12.393 -5.935  2.913   1.00 40.21  ? 688 HOH B O     1 
HETATM 7054 O  O     . HOH I 5 .   ? 37.930 13.548  2.210   1.00 48.51  ? 689 HOH B O     1 
HETATM 7055 O  O     . HOH I 5 .   ? 19.306 40.533  -17.122 1.00 33.23  ? 690 HOH B O     1 
HETATM 7056 O  O     . HOH I 5 .   ? 30.298 -1.577  -4.423  1.00 47.77  ? 691 HOH B O     1 
HETATM 7057 O  O     . HOH I 5 .   ? 37.064 14.267  -15.696 1.00 38.06  ? 692 HOH B O     1 
HETATM 7058 O  O     . HOH I 5 .   ? 5.847  21.700  -17.076 1.00 41.40  ? 693 HOH B O     1 
HETATM 7059 O  O     . HOH I 5 .   ? 9.973  16.095  -14.622 1.00 47.44  ? 694 HOH B O     1 
HETATM 7060 O  O     . HOH I 5 .   ? 18.113 29.610  6.382   1.00 41.13  ? 695 HOH B O     1 
HETATM 7061 O  O     . HOH I 5 .   ? 25.129 29.157  3.542   1.00 42.51  ? 696 HOH B O     1 
HETATM 7062 O  O     . HOH I 5 .   ? 26.386 20.947  10.917  1.00 41.12  ? 697 HOH B O     1 
HETATM 7063 O  O     . HOH I 5 .   ? -2.489 17.161  -20.048 1.00 43.94  ? 698 HOH B O     1 
HETATM 7064 O  O     . HOH I 5 .   ? 27.021 19.445  -26.382 1.00 44.37  ? 699 HOH B O     1 
# 
