data_9H5P
# 
_entry.id   9H5P 
# 
_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   9H5P         pdb_00009h5p 10.2210/pdb9h5p/pdb 
WWPDB D_1292142542 ?            ?                   
# 
_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                        9H5P 
_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 
# 
_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    1   ? ? ? ? 
4 non-polymer syn 1,4-DIAMINOBUTANE             88.151    3   ? ? ? ? 
5 water       nat water                         18.015    151 ? ? ? ? 
# 
_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 1,4-DIAMINOBUTANE             PUT 
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 
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 
PUT non-polymer         . 1,4-DIAMINOBUTANE             PUTRESCINE 'C4 H12 N2'         88.151  
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   ?   ?   ?   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 PUT ? ? PUT ? ? '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 4 PUT 1  503 604 PUT PUT A . 
F 4 PUT 1  504 605 PUT PUT A . 
G 2 FAD 1  600 600 FAD FAD B . 
H 4 PUT 1  601 601 PUT PUT B . 
I 5 HOH 1  601 111 HOH HOH A . 
I 5 HOH 2  602 129 HOH HOH A . 
I 5 HOH 3  603 144 HOH HOH A . 
I 5 HOH 4  604 115 HOH HOH A . 
I 5 HOH 5  605 8   HOH HOH A . 
I 5 HOH 6  606 35  HOH HOH A . 
I 5 HOH 7  607 114 HOH HOH A . 
I 5 HOH 8  608 141 HOH HOH A . 
I 5 HOH 9  609 67  HOH HOH A . 
I 5 HOH 10 610 3   HOH HOH A . 
I 5 HOH 11 611 133 HOH HOH A . 
I 5 HOH 12 612 139 HOH HOH A . 
I 5 HOH 13 613 45  HOH HOH A . 
I 5 HOH 14 614 61  HOH HOH A . 
I 5 HOH 15 615 147 HOH HOH A . 
I 5 HOH 16 616 36  HOH HOH A . 
I 5 HOH 17 617 10  HOH HOH A . 
I 5 HOH 18 618 52  HOH HOH A . 
I 5 HOH 19 619 96  HOH HOH A . 
I 5 HOH 20 620 107 HOH HOH A . 
I 5 HOH 21 621 48  HOH HOH A . 
I 5 HOH 22 622 146 HOH HOH A . 
I 5 HOH 23 623 73  HOH HOH A . 
I 5 HOH 24 624 32  HOH HOH A . 
I 5 HOH 25 625 4   HOH HOH A . 
I 5 HOH 26 626 53  HOH HOH A . 
I 5 HOH 27 627 15  HOH HOH A . 
I 5 HOH 28 628 29  HOH HOH A . 
I 5 HOH 29 629 25  HOH HOH A . 
I 5 HOH 30 630 150 HOH HOH A . 
I 5 HOH 31 631 56  HOH HOH A . 
I 5 HOH 32 632 64  HOH HOH A . 
I 5 HOH 33 633 1   HOH HOH A . 
I 5 HOH 34 634 34  HOH HOH A . 
I 5 HOH 35 635 26  HOH HOH A . 
I 5 HOH 36 636 145 HOH HOH A . 
I 5 HOH 37 637 47  HOH HOH A . 
I 5 HOH 38 638 74  HOH HOH A . 
I 5 HOH 39 639 63  HOH HOH A . 
I 5 HOH 40 640 38  HOH HOH A . 
I 5 HOH 41 641 108 HOH HOH A . 
I 5 HOH 42 642 98  HOH HOH A . 
I 5 HOH 43 643 142 HOH HOH A . 
I 5 HOH 44 644 28  HOH HOH A . 
I 5 HOH 45 645 2   HOH HOH A . 
I 5 HOH 46 646 16  HOH HOH A . 
I 5 HOH 47 647 62  HOH HOH A . 
I 5 HOH 48 648 128 HOH HOH A . 
I 5 HOH 49 649 86  HOH HOH A . 
I 5 HOH 50 650 85  HOH HOH A . 
I 5 HOH 51 651 87  HOH HOH A . 
I 5 HOH 52 652 24  HOH HOH A . 
I 5 HOH 53 653 6   HOH HOH A . 
I 5 HOH 54 654 95  HOH HOH A . 
I 5 HOH 55 655 119 HOH HOH A . 
I 5 HOH 56 656 77  HOH HOH A . 
I 5 HOH 57 657 148 HOH HOH A . 
I 5 HOH 58 658 109 HOH HOH A . 
I 5 HOH 59 659 138 HOH HOH A . 
I 5 HOH 60 660 49  HOH HOH A . 
I 5 HOH 61 661 13  HOH HOH A . 
I 5 HOH 62 662 102 HOH HOH A . 
I 5 HOH 63 663 66  HOH HOH A . 
I 5 HOH 64 664 42  HOH HOH A . 
I 5 HOH 65 665 12  HOH HOH A . 
I 5 HOH 66 666 100 HOH HOH A . 
I 5 HOH 67 667 93  HOH HOH A . 
I 5 HOH 68 668 132 HOH HOH A . 
I 5 HOH 69 669 137 HOH HOH A . 
I 5 HOH 70 670 80  HOH HOH A . 
I 5 HOH 71 671 19  HOH HOH A . 
I 5 HOH 72 672 122 HOH HOH A . 
I 5 HOH 73 673 9   HOH HOH A . 
I 5 HOH 74 674 151 HOH HOH A . 
I 5 HOH 75 675 11  HOH HOH A . 
I 5 HOH 76 676 130 HOH HOH A . 
I 5 HOH 77 677 135 HOH HOH A . 
I 5 HOH 78 678 51  HOH HOH A . 
I 5 HOH 79 679 105 HOH HOH A . 
I 5 HOH 80 680 136 HOH HOH A . 
I 5 HOH 81 681 143 HOH HOH A . 
I 5 HOH 82 682 120 HOH HOH A . 
I 5 HOH 83 683 121 HOH HOH A . 
J 5 HOH 1  701 17  HOH HOH B . 
J 5 HOH 2  702 78  HOH HOH B . 
J 5 HOH 3  703 20  HOH HOH B . 
J 5 HOH 4  704 23  HOH HOH B . 
J 5 HOH 5  705 69  HOH HOH B . 
J 5 HOH 6  706 76  HOH HOH B . 
J 5 HOH 7  707 44  HOH HOH B . 
J 5 HOH 8  708 90  HOH HOH B . 
J 5 HOH 9  709 101 HOH HOH B . 
J 5 HOH 10 710 110 HOH HOH B . 
J 5 HOH 11 711 117 HOH HOH B . 
J 5 HOH 12 712 31  HOH HOH B . 
J 5 HOH 13 713 50  HOH HOH B . 
J 5 HOH 14 714 116 HOH HOH B . 
J 5 HOH 15 715 104 HOH HOH B . 
J 5 HOH 16 716 92  HOH HOH B . 
J 5 HOH 17 717 83  HOH HOH B . 
J 5 HOH 18 718 30  HOH HOH B . 
J 5 HOH 19 719 59  HOH HOH B . 
J 5 HOH 20 720 39  HOH HOH B . 
J 5 HOH 21 721 5   HOH HOH B . 
J 5 HOH 22 722 82  HOH HOH B . 
J 5 HOH 23 723 7   HOH HOH B . 
J 5 HOH 24 724 41  HOH HOH B . 
J 5 HOH 25 725 33  HOH HOH B . 
J 5 HOH 26 726 40  HOH HOH B . 
J 5 HOH 27 727 81  HOH HOH B . 
J 5 HOH 28 728 14  HOH HOH B . 
J 5 HOH 29 729 94  HOH HOH B . 
J 5 HOH 30 730 70  HOH HOH B . 
J 5 HOH 31 731 72  HOH HOH B . 
J 5 HOH 32 732 18  HOH HOH B . 
J 5 HOH 33 733 46  HOH HOH B . 
J 5 HOH 34 734 112 HOH HOH B . 
J 5 HOH 35 735 57  HOH HOH B . 
J 5 HOH 36 736 60  HOH HOH B . 
J 5 HOH 37 737 75  HOH HOH B . 
J 5 HOH 38 738 84  HOH HOH B . 
J 5 HOH 39 739 37  HOH HOH B . 
J 5 HOH 40 740 71  HOH HOH B . 
J 5 HOH 41 741 131 HOH HOH B . 
J 5 HOH 42 742 22  HOH HOH B . 
J 5 HOH 43 743 106 HOH HOH B . 
J 5 HOH 44 744 54  HOH HOH B . 
J 5 HOH 45 745 27  HOH HOH B . 
J 5 HOH 46 746 43  HOH HOH B . 
J 5 HOH 47 747 21  HOH HOH B . 
J 5 HOH 48 748 79  HOH HOH B . 
J 5 HOH 49 749 58  HOH HOH B . 
J 5 HOH 50 750 97  HOH HOH B . 
J 5 HOH 51 751 55  HOH HOH B . 
J 5 HOH 52 752 91  HOH HOH B . 
J 5 HOH 53 753 103 HOH HOH B . 
J 5 HOH 54 754 125 HOH HOH B . 
J 5 HOH 55 755 118 HOH HOH B . 
J 5 HOH 56 756 140 HOH HOH B . 
J 5 HOH 57 757 65  HOH HOH B . 
J 5 HOH 58 758 88  HOH HOH B . 
J 5 HOH 59 759 134 HOH HOH B . 
J 5 HOH 60 760 68  HOH HOH B . 
J 5 HOH 61 761 99  HOH HOH B . 
J 5 HOH 62 762 123 HOH HOH B . 
J 5 HOH 63 763 113 HOH HOH B . 
J 5 HOH 64 764 149 HOH HOH B . 
J 5 HOH 65 765 124 HOH HOH B . 
J 5 HOH 66 766 127 HOH HOH B . 
J 5 HOH 67 767 89  HOH HOH B . 
J 5 HOH 68 768 126 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                     9H5P 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     68.816 
_cell.length_a_esd                 ? 
_cell.length_b                     100.338 
_cell.length_b_esd                 ? 
_cell.length_c                     120.845 
_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                         9H5P 
_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                   9H5P 
_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             2.08 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.93 
_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         2023-02-16 
_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   0.9677 
_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 ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9677 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H5P 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.14 
_reflns.d_resolution_low                               60.4 
_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                                     37362 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.6 
_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                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.19 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.14 
_reflns_shell.d_res_low                                     2.3 
_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                             3256 
_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                                  0.704 
_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                                  0.99 
_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]                            1.17 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            1.25 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -2.42 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.759 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.931 
_refine.correlation_coeff_Fo_to_Fc_free          0.874 
_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                                 9H5P 
_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                            2.30 
_refine.ls_d_res_low                             60.4 
_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                     35546 
_refine.ls_number_reflns_R_free                  1763 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.44 
_refine.ls_percent_reflns_R_free                 4.7 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20591 
_refine.ls_R_factor_R_free                       0.27542 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20259 
_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                       0.453 
_refine.pdbx_overall_ESU_R_Free                  0.287 
_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                             8.946 
_refine.overall_SU_ML                            0.216 
_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                       2.30 
_refine_hist.d_res_low                        60.4 
_refine_hist.number_atoms_solvent             151 
_refine_hist.number_atoms_total               6967 
_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        6691 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         125 
_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  6992  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  6468  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.679  1.668  9586  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.780  1.587  14814 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.404  5.000  893   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 29.548 20.347 375   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.514 15.000 948   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.792 15.000 70    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.067  0.200  883   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  8041  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1597  ? 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' ? 2.438  3.074  3578  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.435  3.073  3576  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.510  4.604  4469  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.511  4.604  4469  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.508  3.260  3414  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.508  3.260  3415  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.781  4.794  5118  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.276  35.826 7618  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.270  35.819 7609  ? 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                       2.300 
_refine_ls_shell.d_res_low                        2.360 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             118 
_refine_ls_shell.number_reflns_R_work             2323 
_refine_ls_shell.percent_reflns_obs               88.93 
_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                  0.245 
_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                  0.336 
# 
_struct.entry_id                     9H5P 
_struct.title                        
'Crystal structure of Thermoanaerobacterales bacterium monoamine oxidase in complex with putrescine' 
_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        9H5P 
_struct_keywords.text            'monoamine oxidase, Thermoanaerobacterales bacterium, enzyme, putrescine, FLAVOPROTEIN' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 2 ? 
H N N 4 ? 
I N N 5 ? 
J 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 9H5P A 22 ? 474 ? A0AAJ6N6J2 1 ? 453 ? 1 453 
2 1 9H5P 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 9H5P MET A 1  ? UNP A0AAJ6N6J2 ? ? 'initiating methionine' -20 1  
1 9H5P GLY A 2  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -19 2  
1 9H5P SER A 3  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -18 3  
1 9H5P SER A 4  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -17 4  
1 9H5P HIS A 5  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -16 5  
1 9H5P HIS A 6  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -15 6  
1 9H5P HIS A 7  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -14 7  
1 9H5P HIS A 8  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -13 8  
1 9H5P HIS A 9  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -12 9  
1 9H5P HIS A 10 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -11 10 
1 9H5P GLY A 11 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -10 11 
1 9H5P SER A 12 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -9  12 
1 9H5P GLY A 13 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -8  13 
1 9H5P LEU A 14 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -7  14 
1 9H5P VAL A 15 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -6  15 
1 9H5P PRO A 16 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -5  16 
1 9H5P ARG A 17 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -4  17 
1 9H5P GLY A 18 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -3  18 
1 9H5P SER A 19 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -2  19 
1 9H5P ALA A 20 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -1  20 
1 9H5P GLY A 21 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        0   21 
2 9H5P MET B 1  ? UNP A0AAJ6N6J2 ? ? 'initiating methionine' -20 22 
2 9H5P GLY B 2  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -19 23 
2 9H5P SER B 3  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -18 24 
2 9H5P SER B 4  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -17 25 
2 9H5P HIS B 5  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -16 26 
2 9H5P HIS B 6  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -15 27 
2 9H5P HIS B 7  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -14 28 
2 9H5P HIS B 8  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -13 29 
2 9H5P HIS B 9  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -12 30 
2 9H5P HIS B 10 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -11 31 
2 9H5P GLY B 11 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -10 32 
2 9H5P SER B 12 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -9  33 
2 9H5P GLY B 13 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -8  34 
2 9H5P LEU B 14 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -7  35 
2 9H5P VAL B 15 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -6  36 
2 9H5P PRO B 16 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -5  37 
2 9H5P ARG B 17 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -4  38 
2 9H5P GLY B 18 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -3  39 
2 9H5P SER B 19 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -2  40 
2 9H5P ALA B 20 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -1  41 
2 9H5P 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)' 7280  ? 
1 MORE         -25   ? 
1 'SSA (A^2)'  29970 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_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  ? GLY A 49  ? GLY A 14  GLY A 28  1 ? 15 
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 ? LYS A 149 ? SER A 108 LYS A 128 1 ? 21 
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 ? ALA A 166 ? GLU A 139 ALA A 145 1 ? 7  
HELX_P HELX_P7  AA7 THR A 168 ? THR A 176 ? THR A 147 THR A 155 1 ? 9  
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 ? ARG A 389 ? THR A 354 ARG A 368 1 ? 15 
HELX_P HELX_P17 AB8 GLY A 392 ? ASP A 397 ? GLY A 371 ASP A 376 5 ? 6  
HELX_P HELX_P18 AB9 GLY A 423 ? TYR A 428 ? GLY A 402 TYR A 407 1 ? 6  
HELX_P HELX_P19 AC1 GLY A 429 ? LEU A 432 ? GLY A 408 LEU A 411 5 ? 4  
HELX_P HELX_P20 AC2 GLY A 443 ? ALA A 447 ? GLY A 422 ALA A 426 5 ? 5  
HELX_P HELX_P21 AC3 TYR A 453 ? GLY A 473 ? TYR A 432 GLY A 452 1 ? 21 
HELX_P HELX_P22 AC4 GLY B 35  ? GLU B 47  ? GLY B 14  GLU B 26  1 ? 13 
HELX_P HELX_P23 AC5 GLN B 86  ? GLY B 97  ? GLN B 65  GLY B 76  1 ? 12 
HELX_P HELX_P24 AC6 ASP B 123 ? PHE B 128 ? ASP B 102 PHE B 107 5 ? 6  
HELX_P HELX_P25 AC7 SER B 129 ? LYS B 149 ? SER B 108 LYS B 128 1 ? 21 
HELX_P HELX_P26 AC8 ALA B 154 ? ALA B 158 ? ALA B 133 ALA B 137 5 ? 5  
HELX_P HELX_P27 AC9 GLU B 160 ? ALA B 166 ? GLU B 139 ALA B 145 1 ? 7  
HELX_P HELX_P28 AD1 THR B 168 ? GLY B 177 ? THR B 147 GLY B 156 1 ? 10 
HELX_P HELX_P29 AD2 PRO B 179 ? ALA B 195 ? PRO B 158 ALA B 174 1 ? 17 
HELX_P HELX_P30 AD3 SER B 202 ? GLY B 214 ? SER B 181 GLY B 193 1 ? 13 
HELX_P HELX_P31 AD4 GLY B 215 ? ASP B 221 ? GLY B 194 ASP B 200 1 ? 7  
HELX_P HELX_P32 AD5 GLY B 234 ? ALA B 244 ? GLY B 213 ALA B 223 1 ? 11 
HELX_P HELX_P33 AD6 PRO B 286 ? ARG B 292 ? PRO B 265 ARG B 271 1 ? 7  
HELX_P HELX_P34 AD7 PRO B 300 ? HIS B 309 ? PRO B 279 HIS B 288 1 ? 10 
HELX_P HELX_P35 AD8 PRO B 325 ? ALA B 329 ? PRO B 304 ALA B 308 5 ? 5  
HELX_P HELX_P36 AD9 GLY B 365 ? ALA B 373 ? GLY B 344 ALA B 352 1 ? 9  
HELX_P HELX_P37 AE1 THR B 375 ? ARG B 389 ? THR B 354 ARG B 368 1 ? 15 
HELX_P HELX_P38 AE2 GLY B 392 ? ASP B 397 ? GLY B 371 ASP B 376 5 ? 6  
HELX_P HELX_P39 AE3 GLY B 423 ? TYR B 428 ? GLY B 402 TYR B 407 1 ? 6  
HELX_P HELX_P40 AE4 GLY B 429 ? LEU B 432 ? GLY B 408 LEU B 411 5 ? 4  
HELX_P HELX_P41 AE5 GLY B 443 ? ALA B 447 ? GLY B 422 ALA B 426 5 ? 5  
HELX_P HELX_P42 AE6 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 ? ? ? ? ? ? ? 1.635 ? ? 
covale2 covale none ? B CYS 415 SG ? ? ? 1_555 G FAD . C8M ? ? B CYS 394 B FAD 600 1_555 ? ? ? ? ? ? ? 1.654 ? ? 
metalc1 metalc ?    ? A THR 105 O  ? ? ? 1_555 D MG  . MG  ? ? A THR 84  A MG  502 1_555 ? ? ? ? ? ? ? 2.691 ? ? 
metalc2 metalc ?    ? D MG  .   MG ? ? ? 1_555 I HOH . O   ? ? A MG  502 A HOH 603 1_555 ? ? ? ? ? ? ? 2.506 ? ? 
metalc3 metalc ?    ? D MG  .   MG ? ? ? 1_555 I HOH . O   ? ? A MG  502 A HOH 622 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
metalc4 metalc ?    ? D MG  .   MG ? ? ? 1_555 I HOH . O   ? ? A MG  502 A HOH 636 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
# 
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 ? I HOH . ? A HOH 603 ? 1_555 54.8  ? 
2 O ? A THR 105 ? A THR 84  ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? I HOH . ? A HOH 622 ? 1_555 67.0  ? 
3 O ? I HOH .   ? A HOH 603 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? I HOH . ? A HOH 622 ? 1_555 69.3  ? 
4 O ? A THR 105 ? A THR 84  ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? I HOH . ? A HOH 636 ? 1_555 115.0 ? 
5 O ? I HOH .   ? A HOH 603 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? I HOH . ? A HOH 636 ? 1_555 61.7  ? 
6 O ? I HOH .   ? A HOH 622 ? 1_555 MG ? D MG . ? A MG 502 ? 1_555 O ? I HOH . ? A HOH 636 ? 1_555 80.2  ? 
# 
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 G . ? CYS B 415 ? FAD B 600 ? 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 1.71  
2 THR 355 A . ? THR 334 A PRO 356 A ? PRO 335 A 1 -6.47 
3 CYS 415 A . ? CYS 394 A TYR 416 A ? TYR 395 A 1 2.90  
4 ASP 296 B . ? ASP 275 B PRO 297 B ? PRO 276 B 1 -4.27 
5 THR 355 B . ? THR 334 B PRO 356 B ? PRO 335 B 1 -5.94 
6 CYS 415 B . ? CYS 394 B TYR 416 B ? TYR 395 B 1 -6.51 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 3 ? 
AA5 ? 4 ? 
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 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? 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 29  ? VAL A 32  ? VAL A 8   VAL A 11  
AA1 4 ARG A 280 ? VAL A 283 ? ARG A 259 VAL A 262 
AA1 5 VAL A 439 ? TRP A 441 ? VAL A 418 TRP A 420 
AA2 1 THR A 67  ? HIS A 70  ? THR A 46  HIS A 49  
AA2 2 THR A 73  ? ASP A 76  ? THR A 52  ASP A 55  
AA3 1 TRP A 81  ? ILE A 82  ? TRP A 60  ILE A 61  
AA3 2 ASP A 229 ? LEU A 231 ? ASP A 208 LEU A 210 
AA3 3 THR A 100 ? PRO A 102 ? THR A 79  PRO A 81  
AA4 1 GLN A 119 ? ALA A 121 ? GLN A 98  ALA A 100 
AA4 2 ASP A 108 ? VAL A 111 ? ASP A 87  VAL A 90  
AA4 3 LEU A 332 ? LEU A 337 ? LEU A 311 LEU A 316 
AA5 1 GLU A 275 ? ALA A 278 ? GLU A 254 ALA A 257 
AA5 2 GLY A 266 ? THR A 271 ? GLY A 245 THR A 250 
AA5 3 VAL A 257 ? ASP A 263 ? VAL A 236 ASP A 242 
AA5 4 ASP A 294 ? ASP A 296 ? ASP A 273 ASP A 275 
AA6 1 THR A 346 ? ASP A 348 ? THR A 325 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 GLY B 274 ? VAL B 283 ? GLY B 253 VAL B 262 
AA7 5 GLY B 266 ? THR B 271 ? GLY B 245 THR B 250 
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 GLY B 274 ? VAL B 283 ? GLY B 253 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 THR B 346 ? ASP B 348 ? THR B 325 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 N ALA A 281 ? N ALA A 260 O HIS A 440 ? O HIS A 419 
AA2 1 2 N HIS A 70  ? N HIS A 49  O THR A 73  ? O THR A 52  
AA3 1 2 N ILE A 82  ? N ILE A 61  O ASP A 229 ? O ASP A 208 
AA3 2 3 O ARG A 230 ? O ARG A 209 N TYR A 101 ? N TYR A 80  
AA4 1 2 O GLN A 119 ? O GLN A 98  N VAL A 111 ? N VAL A 90  
AA4 2 3 N VAL A 110 ? N VAL A 89  O LEU A 337 ? O LEU A 316 
AA5 1 2 O VAL A 276 ? O VAL A 255 N VAL A 269 ? N VAL A 248 
AA5 2 3 O THR A 268 ? O THR A 247 N ALA A 261 ? N ALA A 240 
AA5 3 4 N LEU A 260 ? N LEU A 239 O ASP A 294 ? O ASP A 273 
AA6 1 2 N PHE A 347 ? N PHE A 326 O THR A 360 ? O THR A 339 
AA6 2 3 O VAL A 359 ? O VAL A 338 N VAL A 320 ? N VAL A 299 
AA6 3 4 N ILE A 321 ? N ILE A 300 O ASP A 400 ? O ASP A 379 
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 ALA B 278 ? O ALA B 257 N VAL B 267 ? N VAL B 246 
AA7 5 6 O THR B 268 ? O THR B 247 N ALA B 261 ? N ALA B 240 
AA7 6 7 N GLN B 262 ? N GLN B 241 O ASP B 296 ? O ASP B 275 
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 ALA B 121 ? O ALA B 100 N ASP B 109 ? N ASP B 88  
AB2 2 3 N VAL B 110 ? N VAL B 89  O LEU B 337 ? O LEU B 316 
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                   9H5P 
_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_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 ALA A 13  ? ? -106.57 46.82  
2  1 ASP A 94  ? ? -89.31  30.20  
3  1 VAL A 103 ? ? -27.86  -53.15 
4  1 THR A 113 ? ? -29.80  -67.95 
5  1 ALA A 133 ? ? -164.50 66.88  
6  1 THR A 201 ? ? -79.50  -79.58 
7  1 THR A 369 ? ? -128.04 -69.48 
8  1 THR A 391 ? ? -133.80 -59.03 
9  1 TRP A 429 ? ? 39.08   48.65  
10 1 ALA B 13  ? ? -106.08 43.48  
11 1 ARG B 43  ? ? -66.78  4.12   
12 1 CYS B 45  ? ? -169.49 118.17 
13 1 ASP B 55  ? ? -64.99  96.91  
14 1 GLN B 59  ? ? -145.48 -33.14 
15 1 ALA B 133 ? ? -165.26 72.28  
16 1 ALA B 175 ? ? 177.07  154.20 
17 1 GLU B 202 ? ? 162.62  115.52 
18 1 PRO B 226 ? ? -47.92  150.16 
19 1 MET B 289 ? ? -116.85 65.56  
20 1 THR B 369 ? ? -123.27 -60.31 
21 1 THR B 391 ? ? -137.23 -58.88 
22 1 PRO B 409 ? ? -49.10  -18.54 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A 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 GLN 5   ? A GLN 26  
27 1 Y 1 A SER 453 ? A SER 474 
28 1 Y 1 B MET -20 ? B MET 1   
29 1 Y 1 B GLY -19 ? B GLY 2   
30 1 Y 1 B SER -18 ? B SER 3   
31 1 Y 1 B SER -17 ? B SER 4   
32 1 Y 1 B HIS -16 ? B HIS 5   
33 1 Y 1 B HIS -15 ? B HIS 6   
34 1 Y 1 B HIS -14 ? B HIS 7   
35 1 Y 1 B HIS -13 ? B HIS 8   
36 1 Y 1 B HIS -12 ? B HIS 9   
37 1 Y 1 B HIS -11 ? B HIS 10  
38 1 Y 1 B GLY -10 ? B GLY 11  
39 1 Y 1 B SER -9  ? B SER 12  
40 1 Y 1 B GLY -8  ? B GLY 13  
41 1 Y 1 B LEU -7  ? B LEU 14  
42 1 Y 1 B VAL -6  ? B VAL 15  
43 1 Y 1 B PRO -5  ? B PRO 16  
44 1 Y 1 B ARG -4  ? B ARG 17  
45 1 Y 1 B GLY -3  ? B GLY 18  
46 1 Y 1 B SER -2  ? B SER 19  
47 1 Y 1 B ALA -1  ? B ALA 20  
48 1 Y 1 B GLY 0   ? B GLY 21  
49 1 Y 1 B MET 1   ? B MET 22  
50 1 Y 1 B PRO 2   ? B PRO 23  
51 1 Y 1 B SER 3   ? B SER 24  
52 1 Y 1 B GLU 4   ? B GLU 25  
53 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 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASP N      N  N N 41  
ASP CA     C  N S 42  
ASP C      C  N N 43  
ASP O      O  N N 44  
ASP CB     C  N N 45  
ASP CG     C  N N 46  
ASP OD1    O  N N 47  
ASP OD2    O  N N 48  
ASP OXT    O  N N 49  
ASP H      H  N N 50  
ASP H2     H  N N 51  
ASP HA     H  N N 52  
ASP HB2    H  N N 53  
ASP HB3    H  N N 54  
ASP HD2    H  N N 55  
ASP HXT    H  N N 56  
CYS N      N  N N 57  
CYS CA     C  N R 58  
CYS C      C  N N 59  
CYS O      O  N N 60  
CYS CB     C  N N 61  
CYS SG     S  N N 62  
CYS OXT    O  N N 63  
CYS H      H  N N 64  
CYS H2     H  N N 65  
CYS HA     H  N N 66  
CYS HB2    H  N N 67  
CYS HB3    H  N N 68  
CYS HG     H  N N 69  
CYS HXT    H  N N 70  
FAD PA     P  N R 71  
FAD O1A    O  N N 72  
FAD O2A    O  N N 73  
FAD O5B    O  N N 74  
FAD C5B    C  N N 75  
FAD C4B    C  N R 76  
FAD O4B    O  N N 77  
FAD C3B    C  N S 78  
FAD O3B    O  N N 79  
FAD C2B    C  N R 80  
FAD O2B    O  N N 81  
FAD C1B    C  N R 82  
FAD N9A    N  Y N 83  
FAD C8A    C  Y N 84  
FAD N7A    N  Y N 85  
FAD C5A    C  Y N 86  
FAD C6A    C  Y N 87  
FAD N6A    N  N N 88  
FAD N1A    N  Y N 89  
FAD C2A    C  Y N 90  
FAD N3A    N  Y N 91  
FAD C4A    C  Y N 92  
FAD N1     N  N N 93  
FAD C2     C  N N 94  
FAD O2     O  N N 95  
FAD N3     N  N N 96  
FAD C4     C  N N 97  
FAD O4     O  N N 98  
FAD C4X    C  N N 99  
FAD N5     N  N N 100 
FAD C5X    C  Y N 101 
FAD C6     C  Y N 102 
FAD C7     C  Y N 103 
FAD C7M    C  N N 104 
FAD C8     C  Y N 105 
FAD C8M    C  N N 106 
FAD C9     C  Y N 107 
FAD C9A    C  Y N 108 
FAD N10    N  N N 109 
FAD C10    C  N N 110 
FAD "C1'"  C  N N 111 
FAD "C2'"  C  N S 112 
FAD "O2'"  O  N N 113 
FAD "C3'"  C  N S 114 
FAD "O3'"  O  N N 115 
FAD "C4'"  C  N R 116 
FAD "O4'"  O  N N 117 
FAD "C5'"  C  N N 118 
FAD "O5'"  O  N N 119 
FAD P      P  N R 120 
FAD O1P    O  N N 121 
FAD O2P    O  N N 122 
FAD O3P    O  N N 123 
FAD HOA2   H  N N 124 
FAD H51A   H  N N 125 
FAD H52A   H  N N 126 
FAD H4B    H  N N 127 
FAD H3B    H  N N 128 
FAD HO3A   H  N N 129 
FAD H2B    H  N N 130 
FAD HO2A   H  N N 131 
FAD H1B    H  N N 132 
FAD H8A    H  N N 133 
FAD H61A   H  N N 134 
FAD H62A   H  N N 135 
FAD H2A    H  N N 136 
FAD HN3    H  N N 137 
FAD H6     H  N N 138 
FAD HM71   H  N N 139 
FAD HM72   H  N N 140 
FAD HM73   H  N N 141 
FAD HM81   H  N N 142 
FAD HM82   H  N N 143 
FAD HM83   H  N N 144 
FAD H9     H  N N 145 
FAD "H1'1" H  N N 146 
FAD "H1'2" H  N N 147 
FAD "H2'"  H  N N 148 
FAD "HO2'" H  N N 149 
FAD "H3'"  H  N N 150 
FAD "HO3'" H  N N 151 
FAD "H4'"  H  N N 152 
FAD "HO4'" H  N N 153 
FAD "H5'1" H  N N 154 
FAD "H5'2" H  N N 155 
FAD HOP2   H  N N 156 
GLN N      N  N N 157 
GLN CA     C  N S 158 
GLN C      C  N N 159 
GLN O      O  N N 160 
GLN CB     C  N N 161 
GLN CG     C  N N 162 
GLN CD     C  N N 163 
GLN OE1    O  N N 164 
GLN NE2    N  N N 165 
GLN OXT    O  N N 166 
GLN H      H  N N 167 
GLN H2     H  N N 168 
GLN HA     H  N N 169 
GLN HB2    H  N N 170 
GLN HB3    H  N N 171 
GLN HG2    H  N N 172 
GLN HG3    H  N N 173 
GLN HE21   H  N N 174 
GLN HE22   H  N N 175 
GLN HXT    H  N N 176 
GLU N      N  N N 177 
GLU CA     C  N S 178 
GLU C      C  N N 179 
GLU O      O  N N 180 
GLU CB     C  N N 181 
GLU CG     C  N N 182 
GLU CD     C  N N 183 
GLU OE1    O  N N 184 
GLU OE2    O  N N 185 
GLU OXT    O  N N 186 
GLU H      H  N N 187 
GLU H2     H  N N 188 
GLU HA     H  N N 189 
GLU HB2    H  N N 190 
GLU HB3    H  N N 191 
GLU HG2    H  N N 192 
GLU HG3    H  N N 193 
GLU HE2    H  N N 194 
GLU HXT    H  N N 195 
GLY N      N  N N 196 
GLY CA     C  N N 197 
GLY C      C  N N 198 
GLY O      O  N N 199 
GLY OXT    O  N N 200 
GLY H      H  N N 201 
GLY H2     H  N N 202 
GLY HA2    H  N N 203 
GLY HA3    H  N N 204 
GLY HXT    H  N N 205 
HIS N      N  N N 206 
HIS CA     C  N S 207 
HIS C      C  N N 208 
HIS O      O  N N 209 
HIS CB     C  N N 210 
HIS CG     C  Y N 211 
HIS ND1    N  Y N 212 
HIS CD2    C  Y N 213 
HIS CE1    C  Y N 214 
HIS NE2    N  Y N 215 
HIS OXT    O  N N 216 
HIS H      H  N N 217 
HIS H2     H  N N 218 
HIS HA     H  N N 219 
HIS HB2    H  N N 220 
HIS HB3    H  N N 221 
HIS HD1    H  N N 222 
HIS HD2    H  N N 223 
HIS HE1    H  N N 224 
HIS HE2    H  N N 225 
HIS HXT    H  N N 226 
HOH O      O  N N 227 
HOH H1     H  N N 228 
HOH H2     H  N N 229 
ILE N      N  N N 230 
ILE CA     C  N S 231 
ILE C      C  N N 232 
ILE O      O  N N 233 
ILE CB     C  N S 234 
ILE CG1    C  N N 235 
ILE CG2    C  N N 236 
ILE CD1    C  N N 237 
ILE OXT    O  N N 238 
ILE H      H  N N 239 
ILE H2     H  N N 240 
ILE HA     H  N N 241 
ILE HB     H  N N 242 
ILE HG12   H  N N 243 
ILE HG13   H  N N 244 
ILE HG21   H  N N 245 
ILE HG22   H  N N 246 
ILE HG23   H  N N 247 
ILE HD11   H  N N 248 
ILE HD12   H  N N 249 
ILE HD13   H  N N 250 
ILE HXT    H  N N 251 
LEU N      N  N N 252 
LEU CA     C  N S 253 
LEU C      C  N N 254 
LEU O      O  N N 255 
LEU CB     C  N N 256 
LEU CG     C  N N 257 
LEU CD1    C  N N 258 
LEU CD2    C  N N 259 
LEU OXT    O  N N 260 
LEU H      H  N N 261 
LEU H2     H  N N 262 
LEU HA     H  N N 263 
LEU HB2    H  N N 264 
LEU HB3    H  N N 265 
LEU HG     H  N N 266 
LEU HD11   H  N N 267 
LEU HD12   H  N N 268 
LEU HD13   H  N N 269 
LEU HD21   H  N N 270 
LEU HD22   H  N N 271 
LEU HD23   H  N N 272 
LEU HXT    H  N N 273 
LYS N      N  N N 274 
LYS CA     C  N S 275 
LYS C      C  N N 276 
LYS O      O  N N 277 
LYS CB     C  N N 278 
LYS CG     C  N N 279 
LYS CD     C  N N 280 
LYS CE     C  N N 281 
LYS NZ     N  N N 282 
LYS OXT    O  N N 283 
LYS H      H  N N 284 
LYS H2     H  N N 285 
LYS HA     H  N N 286 
LYS HB2    H  N N 287 
LYS HB3    H  N N 288 
LYS HG2    H  N N 289 
LYS HG3    H  N N 290 
LYS HD2    H  N N 291 
LYS HD3    H  N N 292 
LYS HE2    H  N N 293 
LYS HE3    H  N N 294 
LYS HZ1    H  N N 295 
LYS HZ2    H  N N 296 
LYS HZ3    H  N N 297 
LYS HXT    H  N N 298 
MET N      N  N N 299 
MET CA     C  N S 300 
MET C      C  N N 301 
MET O      O  N N 302 
MET CB     C  N N 303 
MET CG     C  N N 304 
MET SD     S  N N 305 
MET CE     C  N N 306 
MET OXT    O  N N 307 
MET H      H  N N 308 
MET H2     H  N N 309 
MET HA     H  N N 310 
MET HB2    H  N N 311 
MET HB3    H  N N 312 
MET HG2    H  N N 313 
MET HG3    H  N N 314 
MET HE1    H  N N 315 
MET HE2    H  N N 316 
MET HE3    H  N N 317 
MET HXT    H  N N 318 
MG  MG     MG N N 319 
PHE N      N  N N 320 
PHE CA     C  N S 321 
PHE C      C  N N 322 
PHE O      O  N N 323 
PHE CB     C  N N 324 
PHE CG     C  Y N 325 
PHE CD1    C  Y N 326 
PHE CD2    C  Y N 327 
PHE CE1    C  Y N 328 
PHE CE2    C  Y N 329 
PHE CZ     C  Y N 330 
PHE OXT    O  N N 331 
PHE H      H  N N 332 
PHE H2     H  N N 333 
PHE HA     H  N N 334 
PHE HB2    H  N N 335 
PHE HB3    H  N N 336 
PHE HD1    H  N N 337 
PHE HD2    H  N N 338 
PHE HE1    H  N N 339 
PHE HE2    H  N N 340 
PHE HZ     H  N N 341 
PHE HXT    H  N N 342 
PRO N      N  N N 343 
PRO CA     C  N S 344 
PRO C      C  N N 345 
PRO O      O  N N 346 
PRO CB     C  N N 347 
PRO CG     C  N N 348 
PRO CD     C  N N 349 
PRO OXT    O  N N 350 
PRO H      H  N N 351 
PRO HA     H  N N 352 
PRO HB2    H  N N 353 
PRO HB3    H  N N 354 
PRO HG2    H  N N 355 
PRO HG3    H  N N 356 
PRO HD2    H  N N 357 
PRO HD3    H  N N 358 
PRO HXT    H  N N 359 
PUT N2     N  N N 360 
PUT C4     C  N N 361 
PUT C3     C  N N 362 
PUT C2     C  N N 363 
PUT C1     C  N N 364 
PUT N1     N  N N 365 
PUT HN21   H  N N 366 
PUT HN22   H  N N 367 
PUT H41    H  N N 368 
PUT H42    H  N N 369 
PUT H31    H  N N 370 
PUT H32    H  N N 371 
PUT H21    H  N N 372 
PUT H22    H  N N 373 
PUT H11    H  N N 374 
PUT H12    H  N N 375 
PUT HN11   H  N N 376 
PUT HN12   H  N N 377 
SER N      N  N N 378 
SER CA     C  N S 379 
SER C      C  N N 380 
SER O      O  N N 381 
SER CB     C  N N 382 
SER OG     O  N N 383 
SER OXT    O  N N 384 
SER H      H  N N 385 
SER H2     H  N N 386 
SER HA     H  N N 387 
SER HB2    H  N N 388 
SER HB3    H  N N 389 
SER HG     H  N N 390 
SER HXT    H  N N 391 
THR N      N  N N 392 
THR CA     C  N S 393 
THR C      C  N N 394 
THR O      O  N N 395 
THR CB     C  N R 396 
THR OG1    O  N N 397 
THR CG2    C  N N 398 
THR OXT    O  N N 399 
THR H      H  N N 400 
THR H2     H  N N 401 
THR HA     H  N N 402 
THR HB     H  N N 403 
THR HG1    H  N N 404 
THR HG21   H  N N 405 
THR HG22   H  N N 406 
THR HG23   H  N N 407 
THR HXT    H  N N 408 
TRP N      N  N N 409 
TRP CA     C  N S 410 
TRP C      C  N N 411 
TRP O      O  N N 412 
TRP CB     C  N N 413 
TRP CG     C  Y N 414 
TRP CD1    C  Y N 415 
TRP CD2    C  Y N 416 
TRP NE1    N  Y N 417 
TRP CE2    C  Y N 418 
TRP CE3    C  Y N 419 
TRP CZ2    C  Y N 420 
TRP CZ3    C  Y N 421 
TRP CH2    C  Y N 422 
TRP OXT    O  N N 423 
TRP H      H  N N 424 
TRP H2     H  N N 425 
TRP HA     H  N N 426 
TRP HB2    H  N N 427 
TRP HB3    H  N N 428 
TRP HD1    H  N N 429 
TRP HE1    H  N N 430 
TRP HE3    H  N N 431 
TRP HZ2    H  N N 432 
TRP HZ3    H  N N 433 
TRP HH2    H  N N 434 
TRP HXT    H  N N 435 
TYR N      N  N N 436 
TYR CA     C  N S 437 
TYR C      C  N N 438 
TYR O      O  N N 439 
TYR CB     C  N N 440 
TYR CG     C  Y N 441 
TYR CD1    C  Y N 442 
TYR CD2    C  Y N 443 
TYR CE1    C  Y N 444 
TYR CE2    C  Y N 445 
TYR CZ     C  Y N 446 
TYR OH     O  N N 447 
TYR OXT    O  N N 448 
TYR H      H  N N 449 
TYR H2     H  N N 450 
TYR HA     H  N N 451 
TYR HB2    H  N N 452 
TYR HB3    H  N N 453 
TYR HD1    H  N N 454 
TYR HD2    H  N N 455 
TYR HE1    H  N N 456 
TYR HE2    H  N N 457 
TYR HH     H  N N 458 
TYR HXT    H  N N 459 
VAL N      N  N N 460 
VAL CA     C  N S 461 
VAL C      C  N N 462 
VAL O      O  N N 463 
VAL CB     C  N N 464 
VAL CG1    C  N N 465 
VAL CG2    C  N N 466 
VAL OXT    O  N N 467 
VAL H      H  N N 468 
VAL H2     H  N N 469 
VAL HA     H  N N 470 
VAL HB     H  N N 471 
VAL HG11   H  N N 472 
VAL HG12   H  N N 473 
VAL HG13   H  N N 474 
VAL HG21   H  N N 475 
VAL HG22   H  N N 476 
VAL HG23   H  N N 477 
VAL HXT    H  N N 478 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASP N     CA     sing N N 39  
ASP N     H      sing N N 40  
ASP N     H2     sing N N 41  
ASP CA    C      sing N N 42  
ASP CA    CB     sing N N 43  
ASP CA    HA     sing N N 44  
ASP C     O      doub N N 45  
ASP C     OXT    sing N N 46  
ASP CB    CG     sing N N 47  
ASP CB    HB2    sing N N 48  
ASP CB    HB3    sing N N 49  
ASP CG    OD1    doub N N 50  
ASP CG    OD2    sing N N 51  
ASP OD2   HD2    sing N N 52  
ASP OXT   HXT    sing N N 53  
CYS N     CA     sing N N 54  
CYS N     H      sing N N 55  
CYS N     H2     sing N N 56  
CYS CA    C      sing N N 57  
CYS CA    CB     sing N N 58  
CYS CA    HA     sing N N 59  
CYS C     O      doub N N 60  
CYS C     OXT    sing N N 61  
CYS CB    SG     sing N N 62  
CYS CB    HB2    sing N N 63  
CYS CB    HB3    sing N N 64  
CYS SG    HG     sing N N 65  
CYS OXT   HXT    sing N N 66  
FAD PA    O1A    doub N N 67  
FAD PA    O2A    sing N N 68  
FAD PA    O5B    sing N N 69  
FAD PA    O3P    sing N N 70  
FAD O2A   HOA2   sing N N 71  
FAD O5B   C5B    sing N N 72  
FAD C5B   C4B    sing N N 73  
FAD C5B   H51A   sing N N 74  
FAD C5B   H52A   sing N N 75  
FAD C4B   O4B    sing N N 76  
FAD C4B   C3B    sing N N 77  
FAD C4B   H4B    sing N N 78  
FAD O4B   C1B    sing N N 79  
FAD C3B   O3B    sing N N 80  
FAD C3B   C2B    sing N N 81  
FAD C3B   H3B    sing N N 82  
FAD O3B   HO3A   sing N N 83  
FAD C2B   O2B    sing N N 84  
FAD C2B   C1B    sing N N 85  
FAD C2B   H2B    sing N N 86  
FAD O2B   HO2A   sing N N 87  
FAD C1B   N9A    sing N N 88  
FAD C1B   H1B    sing N N 89  
FAD N9A   C8A    sing Y N 90  
FAD N9A   C4A    sing Y N 91  
FAD C8A   N7A    doub Y N 92  
FAD C8A   H8A    sing N N 93  
FAD N7A   C5A    sing Y N 94  
FAD C5A   C6A    sing Y N 95  
FAD C5A   C4A    doub Y N 96  
FAD C6A   N6A    sing N N 97  
FAD C6A   N1A    doub Y N 98  
FAD N6A   H61A   sing N N 99  
FAD N6A   H62A   sing N N 100 
FAD N1A   C2A    sing Y N 101 
FAD C2A   N3A    doub Y N 102 
FAD C2A   H2A    sing N N 103 
FAD N3A   C4A    sing Y N 104 
FAD N1    C2     sing N N 105 
FAD N1    C10    doub N N 106 
FAD C2    O2     doub N N 107 
FAD C2    N3     sing N N 108 
FAD N3    C4     sing N N 109 
FAD N3    HN3    sing N N 110 
FAD C4    O4     doub N N 111 
FAD C4    C4X    sing N N 112 
FAD C4X   N5     doub N N 113 
FAD C4X   C10    sing N N 114 
FAD N5    C5X    sing N N 115 
FAD C5X   C6     doub Y N 116 
FAD C5X   C9A    sing Y N 117 
FAD C6    C7     sing Y N 118 
FAD C6    H6     sing N N 119 
FAD C7    C7M    sing N N 120 
FAD C7    C8     doub Y N 121 
FAD C7M   HM71   sing N N 122 
FAD C7M   HM72   sing N N 123 
FAD C7M   HM73   sing N N 124 
FAD C8    C8M    sing N N 125 
FAD C8    C9     sing Y N 126 
FAD C8M   HM81   sing N N 127 
FAD C8M   HM82   sing N N 128 
FAD C8M   HM83   sing N N 129 
FAD C9    C9A    doub Y N 130 
FAD C9    H9     sing N N 131 
FAD C9A   N10    sing N N 132 
FAD N10   C10    sing N N 133 
FAD N10   "C1'"  sing N N 134 
FAD "C1'" "C2'"  sing N N 135 
FAD "C1'" "H1'1" sing N N 136 
FAD "C1'" "H1'2" sing N N 137 
FAD "C2'" "O2'"  sing N N 138 
FAD "C2'" "C3'"  sing N N 139 
FAD "C2'" "H2'"  sing N N 140 
FAD "O2'" "HO2'" sing N N 141 
FAD "C3'" "O3'"  sing N N 142 
FAD "C3'" "C4'"  sing N N 143 
FAD "C3'" "H3'"  sing N N 144 
FAD "O3'" "HO3'" sing N N 145 
FAD "C4'" "O4'"  sing N N 146 
FAD "C4'" "C5'"  sing N N 147 
FAD "C4'" "H4'"  sing N N 148 
FAD "O4'" "HO4'" sing N N 149 
FAD "C5'" "O5'"  sing N N 150 
FAD "C5'" "H5'1" sing N N 151 
FAD "C5'" "H5'2" sing N N 152 
FAD "O5'" P      sing N N 153 
FAD P     O1P    doub N N 154 
FAD P     O2P    sing N N 155 
FAD P     O3P    sing N N 156 
FAD O2P   HOP2   sing N N 157 
GLN N     CA     sing N N 158 
GLN N     H      sing N N 159 
GLN N     H2     sing N N 160 
GLN CA    C      sing N N 161 
GLN CA    CB     sing N N 162 
GLN CA    HA     sing N N 163 
GLN C     O      doub N N 164 
GLN C     OXT    sing N N 165 
GLN CB    CG     sing N N 166 
GLN CB    HB2    sing N N 167 
GLN CB    HB3    sing N N 168 
GLN CG    CD     sing N N 169 
GLN CG    HG2    sing N N 170 
GLN CG    HG3    sing N N 171 
GLN CD    OE1    doub N N 172 
GLN CD    NE2    sing N N 173 
GLN NE2   HE21   sing N N 174 
GLN NE2   HE22   sing N N 175 
GLN OXT   HXT    sing N N 176 
GLU N     CA     sing N N 177 
GLU N     H      sing N N 178 
GLU N     H2     sing N N 179 
GLU CA    C      sing N N 180 
GLU CA    CB     sing N N 181 
GLU CA    HA     sing N N 182 
GLU C     O      doub N N 183 
GLU C     OXT    sing N N 184 
GLU CB    CG     sing N N 185 
GLU CB    HB2    sing N N 186 
GLU CB    HB3    sing N N 187 
GLU CG    CD     sing N N 188 
GLU CG    HG2    sing N N 189 
GLU CG    HG3    sing N N 190 
GLU CD    OE1    doub N N 191 
GLU CD    OE2    sing N N 192 
GLU OE2   HE2    sing N N 193 
GLU OXT   HXT    sing N N 194 
GLY N     CA     sing N N 195 
GLY N     H      sing N N 196 
GLY N     H2     sing N N 197 
GLY CA    C      sing N N 198 
GLY CA    HA2    sing N N 199 
GLY CA    HA3    sing N N 200 
GLY C     O      doub N N 201 
GLY C     OXT    sing N N 202 
GLY OXT   HXT    sing N N 203 
HIS N     CA     sing N N 204 
HIS N     H      sing N N 205 
HIS N     H2     sing N N 206 
HIS CA    C      sing N N 207 
HIS CA    CB     sing N N 208 
HIS CA    HA     sing N N 209 
HIS C     O      doub N N 210 
HIS C     OXT    sing N N 211 
HIS CB    CG     sing N N 212 
HIS CB    HB2    sing N N 213 
HIS CB    HB3    sing N N 214 
HIS CG    ND1    sing Y N 215 
HIS CG    CD2    doub Y N 216 
HIS ND1   CE1    doub Y N 217 
HIS ND1   HD1    sing N N 218 
HIS CD2   NE2    sing Y N 219 
HIS CD2   HD2    sing N N 220 
HIS CE1   NE2    sing Y N 221 
HIS CE1   HE1    sing N N 222 
HIS NE2   HE2    sing N N 223 
HIS OXT   HXT    sing N N 224 
HOH O     H1     sing N N 225 
HOH O     H2     sing N N 226 
ILE N     CA     sing N N 227 
ILE N     H      sing N N 228 
ILE N     H2     sing N N 229 
ILE CA    C      sing N N 230 
ILE CA    CB     sing N N 231 
ILE CA    HA     sing N N 232 
ILE C     O      doub N N 233 
ILE C     OXT    sing N N 234 
ILE CB    CG1    sing N N 235 
ILE CB    CG2    sing N N 236 
ILE CB    HB     sing N N 237 
ILE CG1   CD1    sing N N 238 
ILE CG1   HG12   sing N N 239 
ILE CG1   HG13   sing N N 240 
ILE CG2   HG21   sing N N 241 
ILE CG2   HG22   sing N N 242 
ILE CG2   HG23   sing N N 243 
ILE CD1   HD11   sing N N 244 
ILE CD1   HD12   sing N N 245 
ILE CD1   HD13   sing N N 246 
ILE OXT   HXT    sing N N 247 
LEU N     CA     sing N N 248 
LEU N     H      sing N N 249 
LEU N     H2     sing N N 250 
LEU CA    C      sing N N 251 
LEU CA    CB     sing N N 252 
LEU CA    HA     sing N N 253 
LEU C     O      doub N N 254 
LEU C     OXT    sing N N 255 
LEU CB    CG     sing N N 256 
LEU CB    HB2    sing N N 257 
LEU CB    HB3    sing N N 258 
LEU CG    CD1    sing N N 259 
LEU CG    CD2    sing N N 260 
LEU CG    HG     sing N N 261 
LEU CD1   HD11   sing N N 262 
LEU CD1   HD12   sing N N 263 
LEU CD1   HD13   sing N N 264 
LEU CD2   HD21   sing N N 265 
LEU CD2   HD22   sing N N 266 
LEU CD2   HD23   sing N N 267 
LEU OXT   HXT    sing N N 268 
LYS N     CA     sing N N 269 
LYS N     H      sing N N 270 
LYS N     H2     sing N N 271 
LYS CA    C      sing N N 272 
LYS CA    CB     sing N N 273 
LYS CA    HA     sing N N 274 
LYS C     O      doub N N 275 
LYS C     OXT    sing N N 276 
LYS CB    CG     sing N N 277 
LYS CB    HB2    sing N N 278 
LYS CB    HB3    sing N N 279 
LYS CG    CD     sing N N 280 
LYS CG    HG2    sing N N 281 
LYS CG    HG3    sing N N 282 
LYS CD    CE     sing N N 283 
LYS CD    HD2    sing N N 284 
LYS CD    HD3    sing N N 285 
LYS CE    NZ     sing N N 286 
LYS CE    HE2    sing N N 287 
LYS CE    HE3    sing N N 288 
LYS NZ    HZ1    sing N N 289 
LYS NZ    HZ2    sing N N 290 
LYS NZ    HZ3    sing N N 291 
LYS OXT   HXT    sing N N 292 
MET N     CA     sing N N 293 
MET N     H      sing N N 294 
MET N     H2     sing N N 295 
MET CA    C      sing N N 296 
MET CA    CB     sing N N 297 
MET CA    HA     sing N N 298 
MET C     O      doub N N 299 
MET C     OXT    sing N N 300 
MET CB    CG     sing N N 301 
MET CB    HB2    sing N N 302 
MET CB    HB3    sing N N 303 
MET CG    SD     sing N N 304 
MET CG    HG2    sing N N 305 
MET CG    HG3    sing N N 306 
MET SD    CE     sing N N 307 
MET CE    HE1    sing N N 308 
MET CE    HE2    sing N N 309 
MET CE    HE3    sing N N 310 
MET OXT   HXT    sing N N 311 
PHE N     CA     sing N N 312 
PHE N     H      sing N N 313 
PHE N     H2     sing N N 314 
PHE CA    C      sing N N 315 
PHE CA    CB     sing N N 316 
PHE CA    HA     sing N N 317 
PHE C     O      doub N N 318 
PHE C     OXT    sing N N 319 
PHE CB    CG     sing N N 320 
PHE CB    HB2    sing N N 321 
PHE CB    HB3    sing N N 322 
PHE CG    CD1    doub Y N 323 
PHE CG    CD2    sing Y N 324 
PHE CD1   CE1    sing Y N 325 
PHE CD1   HD1    sing N N 326 
PHE CD2   CE2    doub Y N 327 
PHE CD2   HD2    sing N N 328 
PHE CE1   CZ     doub Y N 329 
PHE CE1   HE1    sing N N 330 
PHE CE2   CZ     sing Y N 331 
PHE CE2   HE2    sing N N 332 
PHE CZ    HZ     sing N N 333 
PHE OXT   HXT    sing N N 334 
PRO N     CA     sing N N 335 
PRO N     CD     sing N N 336 
PRO N     H      sing N N 337 
PRO CA    C      sing N N 338 
PRO CA    CB     sing N N 339 
PRO CA    HA     sing N N 340 
PRO C     O      doub N N 341 
PRO C     OXT    sing N N 342 
PRO CB    CG     sing N N 343 
PRO CB    HB2    sing N N 344 
PRO CB    HB3    sing N N 345 
PRO CG    CD     sing N N 346 
PRO CG    HG2    sing N N 347 
PRO CG    HG3    sing N N 348 
PRO CD    HD2    sing N N 349 
PRO CD    HD3    sing N N 350 
PRO OXT   HXT    sing N N 351 
PUT N2    C4     sing N N 352 
PUT N2    HN21   sing N N 353 
PUT N2    HN22   sing N N 354 
PUT C4    C3     sing N N 355 
PUT C4    H41    sing N N 356 
PUT C4    H42    sing N N 357 
PUT C3    C2     sing N N 358 
PUT C3    H31    sing N N 359 
PUT C3    H32    sing N N 360 
PUT C2    C1     sing N N 361 
PUT C2    H21    sing N N 362 
PUT C2    H22    sing N N 363 
PUT C1    N1     sing N N 364 
PUT C1    H11    sing N N 365 
PUT C1    H12    sing N N 366 
PUT N1    HN11   sing N N 367 
PUT N1    HN12   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                    9H5P 
_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]   0.014532 
_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]   0.009966 
_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]   0.008275 
_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     . VAL A 1 27  ? 24.770  2.133   -4.659  1.00 25.60 ? 6   VAL A N     1 
ATOM   2    C  CA    . VAL A 1 27  ? 24.815  1.212   -5.860  1.00 27.19 ? 6   VAL A CA    1 
ATOM   3    C  C     . VAL A 1 27  ? 24.375  1.948   -7.130  1.00 26.56 ? 6   VAL A C     1 
ATOM   4    O  O     . VAL A 1 27  ? 23.678  2.958   -7.006  1.00 29.32 ? 6   VAL A O     1 
ATOM   5    C  CB    . VAL A 1 27  ? 23.967  -0.061  -5.657  1.00 27.03 ? 6   VAL A CB    1 
ATOM   6    C  CG1   . VAL A 1 27  ? 24.594  -0.987  -4.632  1.00 28.60 ? 6   VAL A CG1   1 
ATOM   7    C  CG2   . VAL A 1 27  ? 22.504  0.228   -5.322  1.00 26.99 ? 6   VAL A CG2   1 
ATOM   8    N  N     . ASP A 1 28  ? 24.745  1.432   -8.306  1.00 28.57 ? 7   ASP A N     1 
ATOM   9    C  CA    . ASP A 1 28  ? 24.296  1.956   -9.633  1.00 29.91 ? 7   ASP A CA    1 
ATOM   10   C  C     . ASP A 1 28  ? 22.777  1.718   -9.750  1.00 30.23 ? 7   ASP A C     1 
ATOM   11   O  O     . ASP A 1 28  ? 22.061  2.699   -9.920  1.00 30.16 ? 7   ASP A O     1 
ATOM   12   C  CB    . ASP A 1 28  ? 25.065  1.320   -10.810 1.00 30.73 ? 7   ASP A CB    1 
ATOM   13   C  CG    . ASP A 1 28  ? 26.575  1.611   -10.855 1.00 32.23 ? 7   ASP A CG    1 
ATOM   14   O  OD1   . ASP A 1 28  ? 26.982  2.675   -10.380 1.00 29.49 ? 7   ASP A OD1   1 
ATOM   15   O  OD2   . ASP A 1 28  ? 27.348  0.763   -11.372 1.00 34.02 ? 7   ASP A OD2   1 
ATOM   16   N  N     . VAL A 1 29  ? 22.321  0.458   -9.624  1.00 29.77 ? 8   VAL A N     1 
ATOM   17   C  CA    . VAL A 1 29  ? 20.905  0.019   -9.860  1.00 29.77 ? 8   VAL A CA    1 
ATOM   18   C  C     . VAL A 1 29  ? 20.365  -0.779  -8.651  1.00 29.66 ? 8   VAL A C     1 
ATOM   19   O  O     . VAL A 1 29  ? 21.051  -1.733  -8.186  1.00 27.82 ? 8   VAL A O     1 
ATOM   20   C  CB    . VAL A 1 29  ? 20.813  -0.829  -11.138 1.00 30.40 ? 8   VAL A CB    1 
ATOM   21   C  CG1   . VAL A 1 29  ? 19.370  -1.101  -11.559 1.00 29.79 ? 8   VAL A CG1   1 
ATOM   22   C  CG2   . VAL A 1 29  ? 21.596  -0.195  -12.270 1.00 28.59 ? 8   VAL A CG2   1 
ATOM   23   N  N     . VAL A 1 30  ? 19.186  -0.403  -8.148  1.00 25.48 ? 9   VAL A N     1 
ATOM   24   C  CA    . VAL A 1 30  ? 18.363  -1.276  -7.269  1.00 26.33 ? 9   VAL A CA    1 
ATOM   25   C  C     . VAL A 1 30  ? 17.219  -1.845  -8.127  1.00 27.32 ? 9   VAL A C     1 
ATOM   26   O  O     . VAL A 1 30  ? 16.492  -1.055  -8.789  1.00 26.39 ? 9   VAL A O     1 
ATOM   27   C  CB    . VAL A 1 30  ? 17.874  -0.564  -5.992  1.00 26.29 ? 9   VAL A CB    1 
ATOM   28   C  CG1   . VAL A 1 30  ? 17.019  0.647   -6.287  1.00 29.79 ? 9   VAL A CG1   1 
ATOM   29   C  CG2   . VAL A 1 30  ? 17.093  -1.491  -5.077  1.00 27.60 ? 9   VAL A CG2   1 
ATOM   30   N  N     . VAL A 1 31  ? 17.119  -3.176  -8.152  1.00 26.65 ? 10  VAL A N     1 
ATOM   31   C  CA    . VAL A 1 31  ? 15.993  -3.968  -8.734  1.00 26.19 ? 10  VAL A CA    1 
ATOM   32   C  C     . VAL A 1 31  ? 15.000  -4.317  -7.599  1.00 28.33 ? 10  VAL A C     1 
ATOM   33   O  O     . VAL A 1 31  ? 15.435  -4.858  -6.567  1.00 23.86 ? 10  VAL A O     1 
ATOM   34   C  CB    . VAL A 1 31  ? 16.563  -5.226  -9.423  1.00 24.32 ? 10  VAL A CB    1 
ATOM   35   C  CG1   . VAL A 1 31  ? 15.481  -6.168  -9.909  1.00 25.31 ? 10  VAL A CG1   1 
ATOM   36   C  CG2   . VAL A 1 31  ? 17.493  -4.856  -10.560 1.00 24.17 ? 10  VAL A CG2   1 
ATOM   37   N  N     . VAL A 1 32  ? 13.700  -4.030  -7.773  1.00 28.08 ? 11  VAL A N     1 
ATOM   38   C  CA    . VAL A 1 32  ? 12.643  -4.455  -6.813  1.00 25.09 ? 11  VAL A CA    1 
ATOM   39   C  C     . VAL A 1 32  ? 11.972  -5.718  -7.384  1.00 25.93 ? 11  VAL A C     1 
ATOM   40   O  O     . VAL A 1 32  ? 11.322  -5.598  -8.473  1.00 23.59 ? 11  VAL A O     1 
ATOM   41   C  CB    . VAL A 1 32  ? 11.652  -3.306  -6.563  1.00 26.13 ? 11  VAL A CB    1 
ATOM   42   C  CG1   . VAL A 1 32  ? 10.718  -3.602  -5.403  1.00 24.80 ? 11  VAL A CG1   1 
ATOM   43   C  CG2   . VAL A 1 32  ? 12.358  -1.965  -6.359  1.00 24.74 ? 11  VAL A CG2   1 
ATOM   44   N  N     . GLY A 1 33  ? 12.175  -6.876  -6.724  1.00 22.70 ? 12  GLY A N     1 
ATOM   45   C  CA    . GLY A 1 33  ? 11.595  -8.193  -7.081  1.00 22.75 ? 12  GLY A CA    1 
ATOM   46   C  C     . GLY A 1 33  ? 12.623  -9.152  -7.689  1.00 23.72 ? 12  GLY A C     1 
ATOM   47   O  O     . GLY A 1 33  ? 13.284  -8.777  -8.666  1.00 25.84 ? 12  GLY A O     1 
ATOM   48   N  N     . ALA A 1 34  ? 12.753  -10.362 -7.134  1.00 23.12 ? 13  ALA A N     1 
ATOM   49   C  CA    . ALA A 1 34  ? 13.605  -11.463 -7.642  1.00 23.43 ? 13  ALA A CA    1 
ATOM   50   C  C     . ALA A 1 34  ? 12.734  -12.570 -8.281  1.00 23.77 ? 13  ALA A C     1 
ATOM   51   O  O     . ALA A 1 34  ? 12.975  -13.785 -8.035  1.00 22.07 ? 13  ALA A O     1 
ATOM   52   C  CB    . ALA A 1 34  ? 14.503  -11.981 -6.530  1.00 23.31 ? 13  ALA A CB    1 
ATOM   53   N  N     . GLY A 1 35  ? 11.777  -12.168 -9.130  1.00 22.51 ? 14  GLY A N     1 
ATOM   54   C  CA    . GLY A 1 35  ? 11.137  -13.044 -10.123 1.00 21.13 ? 14  GLY A CA    1 
ATOM   55   C  C     . GLY A 1 35  ? 12.085  -13.167 -11.292 1.00 21.39 ? 14  GLY A C     1 
ATOM   56   O  O     . GLY A 1 35  ? 13.214  -12.703 -11.132 1.00 20.36 ? 14  GLY A O     1 
ATOM   57   N  N     . PHE A 1 36  ? 11.690  -13.807 -12.386 1.00 19.15 ? 15  PHE A N     1 
ATOM   58   C  CA    . PHE A 1 36  ? 12.553  -13.954 -13.583 1.00 20.30 ? 15  PHE A CA    1 
ATOM   59   C  C     . PHE A 1 36  ? 12.860  -12.580 -14.198 1.00 22.21 ? 15  PHE A C     1 
ATOM   60   O  O     . PHE A 1 36  ? 13.953  -12.460 -14.761 1.00 20.81 ? 15  PHE A O     1 
ATOM   61   C  CB    . PHE A 1 36  ? 11.941  -14.910 -14.609 1.00 17.96 ? 15  PHE A CB    1 
ATOM   62   C  CG    . PHE A 1 36  ? 12.283  -16.338 -14.306 1.00 17.61 ? 15  PHE A CG    1 
ATOM   63   C  CD1   . PHE A 1 36  ? 13.457  -16.895 -14.765 1.00 18.38 ? 15  PHE A CD1   1 
ATOM   64   C  CD2   . PHE A 1 36  ? 11.459  -17.105 -13.510 1.00 17.85 ? 15  PHE A CD2   1 
ATOM   65   C  CE1   . PHE A 1 36  ? 13.778  -18.213 -14.472 1.00 18.47 ? 15  PHE A CE1   1 
ATOM   66   C  CE2   . PHE A 1 36  ? 11.790  -18.407 -13.192 1.00 17.84 ? 15  PHE A CE2   1 
ATOM   67   C  CZ    . PHE A 1 36  ? 12.945  -18.963 -13.686 1.00 18.37 ? 15  PHE A CZ    1 
ATOM   68   N  N     . ALA A 1 37  ? 11.927  -11.614 -14.117 1.00 23.68 ? 16  ALA A N     1 
ATOM   69   C  CA    . ALA A 1 37  ? 12.104  -10.234 -14.632 1.00 23.94 ? 16  ALA A CA    1 
ATOM   70   C  C     . ALA A 1 37  ? 13.187  -9.529  -13.809 1.00 24.21 ? 16  ALA A C     1 
ATOM   71   O  O     . ALA A 1 37  ? 14.210  -9.097  -14.374 1.00 23.41 ? 16  ALA A O     1 
ATOM   72   C  CB    . ALA A 1 37  ? 10.798  -9.497  -14.531 1.00 25.41 ? 16  ALA A CB    1 
ATOM   73   N  N     . GLY A 1 38  ? 12.976  -9.445  -12.498 1.00 22.99 ? 17  GLY A N     1 
ATOM   74   C  CA    . GLY A 1 38  ? 13.973  -8.872  -11.573 1.00 25.31 ? 17  GLY A CA    1 
ATOM   75   C  C     . GLY A 1 38  ? 15.359  -9.478  -11.755 1.00 23.30 ? 17  GLY A C     1 
ATOM   76   O  O     . GLY A 1 38  ? 16.319  -8.733  -11.920 1.00 22.20 ? 17  GLY A O     1 
ATOM   77   N  N     . LEU A 1 39  ? 15.464  -10.796 -11.668 1.00 23.73 ? 18  LEU A N     1 
ATOM   78   C  CA    . LEU A 1 39  ? 16.758  -11.513 -11.638 1.00 24.02 ? 18  LEU A CA    1 
ATOM   79   C  C     . LEU A 1 39  ? 17.487  -11.360 -12.965 1.00 23.82 ? 18  LEU A C     1 
ATOM   80   O  O     . LEU A 1 39  ? 18.710  -11.254 -12.934 1.00 24.11 ? 18  LEU A O     1 
ATOM   81   C  CB    . LEU A 1 39  ? 16.526  -12.991 -11.336 1.00 23.86 ? 18  LEU A CB    1 
ATOM   82   C  CG    . LEU A 1 39  ? 16.254  -13.309 -9.867  1.00 24.38 ? 18  LEU A CG    1 
ATOM   83   C  CD1   . LEU A 1 39  ? 16.065  -14.801 -9.675  1.00 25.43 ? 18  LEU A CD1   1 
ATOM   84   C  CD2   . LEU A 1 39  ? 17.391  -12.832 -8.993  1.00 26.03 ? 18  LEU A CD2   1 
ATOM   85   N  N     . THR A 1 40  ? 16.761  -11.417 -14.076 1.00 24.33 ? 19  THR A N     1 
ATOM   86   C  CA    . THR A 1 40  ? 17.311  -11.254 -15.451 1.00 23.28 ? 19  THR A CA    1 
ATOM   87   C  C     . THR A 1 40  ? 17.836  -9.817  -15.634 1.00 23.71 ? 19  THR A C     1 
ATOM   88   O  O     . THR A 1 40  ? 18.871  -9.662  -16.303 1.00 24.50 ? 19  THR A O     1 
ATOM   89   C  CB    . THR A 1 40  ? 16.266  -11.612 -16.513 1.00 21.48 ? 19  THR A CB    1 
ATOM   90   O  OG1   . THR A 1 40  ? 15.948  -12.996 -16.371 1.00 19.19 ? 19  THR A OG1   1 
ATOM   91   C  CG2   . THR A 1 40  ? 16.742  -11.334 -17.927 1.00 22.45 ? 19  THR A CG2   1 
ATOM   92   N  N     . ALA A 1 41  ? 17.131  -8.809  -15.120 1.00 21.27 ? 20  ALA A N     1 
ATOM   93   C  CA    . ALA A 1 41  ? 17.596  -7.400  -15.145 1.00 24.47 ? 20  ALA A CA    1 
ATOM   94   C  C     . ALA A 1 41  ? 18.860  -7.263  -14.286 1.00 23.43 ? 20  ALA A C     1 
ATOM   95   O  O     . ALA A 1 41  ? 19.795  -6.583  -14.750 1.00 21.54 ? 20  ALA A O     1 
ATOM   96   C  CB    . ALA A 1 41  ? 16.524  -6.434  -14.682 1.00 24.59 ? 20  ALA A CB    1 
ATOM   97   N  N     . ALA A 1 42  ? 18.897  -7.892  -13.102 1.00 24.42 ? 21  ALA A N     1 
ATOM   98   C  CA    . ALA A 1 42  ? 19.977  -7.710  -12.100 1.00 27.28 ? 21  ALA A CA    1 
ATOM   99   C  C     . ALA A 1 42  ? 21.267  -8.260  -12.685 1.00 28.45 ? 21  ALA A C     1 
ATOM   100  O  O     . ALA A 1 42  ? 22.347  -7.607  -12.512 1.00 26.78 ? 21  ALA A O     1 
ATOM   101  C  CB    . ALA A 1 42  ? 19.668  -8.383  -10.795 1.00 27.28 ? 21  ALA A CB    1 
ATOM   102  N  N     . ARG A 1 43  ? 21.135  -9.399  -13.360 1.00 25.53 ? 22  ARG A N     1 
ATOM   103  C  CA    . ARG A 1 43  ? 22.272  -10.126 -13.973 1.00 26.57 ? 22  ARG A CA    1 
ATOM   104  C  C     . ARG A 1 43  ? 22.860  -9.323  -15.150 1.00 28.60 ? 22  ARG A C     1 
ATOM   105  O  O     . ARG A 1 43  ? 24.085  -9.064  -15.133 1.00 24.97 ? 22  ARG A O     1 
ATOM   106  C  CB    . ARG A 1 43  ? 21.783  -11.496 -14.420 1.00 25.81 ? 22  ARG A CB    1 
ATOM   107  C  CG    . ARG A 1 43  ? 22.908  -12.438 -14.785 1.00 29.86 ? 22  ARG A CG    1 
ATOM   108  C  CD    . ARG A 1 43  ? 22.668  -13.123 -16.109 1.00 30.66 ? 22  ARG A CD    1 
ATOM   109  N  NE    . ARG A 1 43  ? 23.703  -14.121 -16.247 1.00 32.70 ? 22  ARG A NE    1 
ATOM   110  C  CZ    . ARG A 1 43  ? 23.571  -15.286 -16.870 1.00 35.34 ? 22  ARG A CZ    1 
ATOM   111  N  NH1   . ARG A 1 43  ? 22.428  -15.618 -17.452 1.00 33.54 ? 22  ARG A NH1   1 
ATOM   112  N  NH2   . ARG A 1 43  ? 24.602  -16.118 -16.889 1.00 34.70 ? 22  ARG A NH2   1 
ATOM   113  N  N     . ALA A 1 44  ? 22.046  -8.973  -16.165 1.00 27.05 ? 23  ALA A N     1 
ATOM   114  C  CA    . ALA A 1 44  ? 22.513  -8.228  -17.361 1.00 26.25 ? 23  ALA A CA    1 
ATOM   115  C  C     . ALA A 1 44  ? 23.216  -6.946  -16.901 1.00 24.03 ? 23  ALA A C     1 
ATOM   116  O  O     . ALA A 1 44  ? 24.253  -6.592  -17.467 1.00 28.89 ? 23  ALA A O     1 
ATOM   117  C  CB    . ALA A 1 44  ? 21.376  -7.947  -18.317 1.00 26.84 ? 23  ALA A CB    1 
ATOM   118  N  N     . VAL A 1 45  ? 22.714  -6.308  -15.855 1.00 23.84 ? 24  VAL A N     1 
ATOM   119  C  CA    . VAL A 1 45  ? 23.329  -5.093  -15.242 1.00 26.81 ? 24  VAL A CA    1 
ATOM   120  C  C     . VAL A 1 45  ? 24.690  -5.442  -14.600 1.00 29.68 ? 24  VAL A C     1 
ATOM   121  O  O     . VAL A 1 45  ? 25.642  -4.648  -14.768 1.00 30.13 ? 24  VAL A O     1 
ATOM   122  C  CB    . VAL A 1 45  ? 22.328  -4.474  -14.251 1.00 28.22 ? 24  VAL A CB    1 
ATOM   123  C  CG1   . VAL A 1 45  ? 22.945  -3.393  -13.388 1.00 30.83 ? 24  VAL A CG1   1 
ATOM   124  C  CG2   . VAL A 1 45  ? 21.108  -3.924  -14.973 1.00 27.80 ? 24  VAL A CG2   1 
ATOM   125  N  N     . HIS A 1 46  ? 24.806  -6.611  -13.951 1.00 31.50 ? 25  HIS A N     1 
ATOM   126  C  CA    . HIS A 1 46  ? 26.015  -7.120  -13.241 1.00 32.02 ? 25  HIS A CA    1 
ATOM   127  C  C     . HIS A 1 46  ? 27.147  -7.440  -14.218 1.00 34.27 ? 25  HIS A C     1 
ATOM   128  O  O     . HIS A 1 46  ? 28.311  -7.055  -13.927 1.00 32.37 ? 25  HIS A O     1 
ATOM   129  C  CB    . HIS A 1 46  ? 25.672  -8.378  -12.421 1.00 32.81 ? 25  HIS A CB    1 
ATOM   130  C  CG    . HIS A 1 46  ? 26.840  -9.221  -12.023 1.00 31.62 ? 25  HIS A CG    1 
ATOM   131  N  ND1   . HIS A 1 46  ? 27.825  -8.764  -11.140 1.00 29.70 ? 25  HIS A ND1   1 
ATOM   132  C  CD2   . HIS A 1 46  ? 27.164  -10.497 -12.348 1.00 31.49 ? 25  HIS A CD2   1 
ATOM   133  C  CE1   . HIS A 1 46  ? 28.729  -9.717  -10.984 1.00 31.98 ? 25  HIS A CE1   1 
ATOM   134  N  NE2   . HIS A 1 46  ? 28.347  -10.795 -11.721 1.00 32.30 ? 25  HIS A NE2   1 
ATOM   135  N  N     . GLU A 1 47  ? 26.833  -8.193  -15.271 1.00 36.48 ? 26  GLU A N     1 
ATOM   136  C  CA    . GLU A 1 47  ? 27.797  -8.623  -16.312 1.00 38.38 ? 26  GLU A CA    1 
ATOM   137  C  C     . GLU A 1 47  ? 28.177  -7.432  -17.205 1.00 40.04 ? 26  GLU A C     1 
ATOM   138  O  O     . GLU A 1 47  ? 29.243  -7.498  -17.826 1.00 46.12 ? 26  GLU A O     1 
ATOM   139  C  CB    . GLU A 1 47  ? 27.203  -9.744  -17.152 1.00 41.02 ? 26  GLU A CB    1 
ATOM   140  C  CG    . GLU A 1 47  ? 27.051  -11.031 -16.382 1.00 44.64 ? 26  GLU A CG    1 
ATOM   141  C  CD    . GLU A 1 47  ? 26.650  -12.226 -17.232 1.00 52.74 ? 26  GLU A CD    1 
ATOM   142  O  OE1   . GLU A 1 47  ? 26.717  -13.371 -16.688 1.00 58.26 ? 26  GLU A OE1   1 
ATOM   143  O  OE2   . GLU A 1 47  ? 26.256  -12.017 -18.430 1.00 52.35 ? 26  GLU A OE2   1 
ATOM   144  N  N     . ALA A 1 48  ? 27.359  -6.384  -17.278 1.00 38.50 ? 27  ALA A N     1 
ATOM   145  C  CA    . ALA A 1 48  ? 27.696  -5.158  -18.040 1.00 42.33 ? 27  ALA A CA    1 
ATOM   146  C  C     . ALA A 1 48  ? 28.870  -4.435  -17.366 1.00 47.16 ? 27  ALA A C     1 
ATOM   147  O  O     . ALA A 1 48  ? 29.602  -3.739  -18.104 1.00 55.92 ? 27  ALA A O     1 
ATOM   148  C  CB    . ALA A 1 48  ? 26.502  -4.249  -18.160 1.00 41.14 ? 27  ALA A CB    1 
ATOM   149  N  N     . GLY A 1 49  ? 29.025  -4.597  -16.038 1.00 47.18 ? 28  GLY A N     1 
ATOM   150  C  CA    . GLY A 1 49  ? 30.088  -3.999  -15.197 1.00 40.92 ? 28  GLY A CA    1 
ATOM   151  C  C     . GLY A 1 49  ? 29.563  -2.992  -14.174 1.00 41.91 ? 28  GLY A C     1 
ATOM   152  O  O     . GLY A 1 49  ? 30.329  -2.107  -13.763 1.00 45.51 ? 28  GLY A O     1 
ATOM   153  N  N     . ARG A 1 50  ? 28.309  -3.124  -13.742 1.00 40.08 ? 29  ARG A N     1 
ATOM   154  C  CA    . ARG A 1 50  ? 27.606  -2.146  -12.876 1.00 38.55 ? 29  ARG A CA    1 
ATOM   155  C  C     . ARG A 1 50  ? 27.234  -2.839  -11.567 1.00 35.26 ? 29  ARG A C     1 
ATOM   156  O  O     . ARG A 1 50  ? 27.119  -4.087  -11.597 1.00 34.52 ? 29  ARG A O     1 
ATOM   157  C  CB    . ARG A 1 50  ? 26.335  -1.651  -13.572 1.00 43.06 ? 29  ARG A CB    1 
ATOM   158  C  CG    . ARG A 1 50  ? 26.582  -1.014  -14.934 1.00 44.24 ? 29  ARG A CG    1 
ATOM   159  C  CD    . ARG A 1 50  ? 27.499  0.188   -14.807 1.00 47.85 ? 29  ARG A CD    1 
ATOM   160  N  NE    . ARG A 1 50  ? 27.025  1.340   -15.548 1.00 51.23 ? 29  ARG A NE    1 
ATOM   161  C  CZ    . ARG A 1 50  ? 27.520  2.562   -15.427 1.00 56.54 ? 29  ARG A CZ    1 
ATOM   162  N  NH1   . ARG A 1 50  ? 28.523  2.781   -14.589 1.00 60.90 ? 29  ARG A NH1   1 
ATOM   163  N  NH2   . ARG A 1 50  ? 27.022  3.552   -16.156 1.00 52.70 ? 29  ARG A NH2   1 
ATOM   164  N  N     . SER A 1 51  ? 27.067  -2.062  -10.485 1.00 30.66 ? 30  SER A N     1 
ATOM   165  C  CA    . SER A 1 51  ? 26.704  -2.548  -9.129  1.00 29.95 ? 30  SER A CA    1 
ATOM   166  C  C     . SER A 1 51  ? 25.168  -2.611  -8.996  1.00 31.66 ? 30  SER A C     1 
ATOM   167  O  O     . SER A 1 51  ? 24.441  -1.679  -9.477  1.00 32.23 ? 30  SER A O     1 
ATOM   168  C  CB    . SER A 1 51  ? 27.361  -1.713  -8.050  1.00 29.68 ? 30  SER A CB    1 
ATOM   169  O  OG    . SER A 1 51  ? 26.971  -0.350  -8.126  1.00 28.55 ? 30  SER A OG    1 
ATOM   170  N  N     . VAL A 1 52  ? 24.660  -3.671  -8.375  1.00 29.04 ? 31  VAL A N     1 
ATOM   171  C  CA    . VAL A 1 52  ? 23.197  -3.893  -8.299  1.00 28.16 ? 31  VAL A CA    1 
ATOM   172  C  C     . VAL A 1 52  ? 22.851  -4.598  -6.991  1.00 29.07 ? 31  VAL A C     1 
ATOM   173  O  O     . VAL A 1 52  ? 23.602  -5.498  -6.569  1.00 27.53 ? 31  VAL A O     1 
ATOM   174  C  CB    . VAL A 1 52  ? 22.739  -4.665  -9.557  1.00 28.25 ? 31  VAL A CB    1 
ATOM   175  C  CG1   . VAL A 1 52  ? 23.398  -6.024  -9.680  1.00 26.09 ? 31  VAL A CG1   1 
ATOM   176  C  CG2   . VAL A 1 52  ? 21.228  -4.763  -9.636  1.00 27.19 ? 31  VAL A CG2   1 
ATOM   177  N  N     . LEU A 1 53  ? 21.736  -4.193  -6.380  1.00 31.37 ? 32  LEU A N     1 
ATOM   178  C  CA    . LEU A 1 53  ? 21.008  -4.999  -5.359  1.00 29.25 ? 32  LEU A CA    1 
ATOM   179  C  C     . LEU A 1 53  ? 19.630  -5.403  -5.897  1.00 27.22 ? 32  LEU A C     1 
ATOM   180  O  O     . LEU A 1 53  ? 18.974  -4.569  -6.599  1.00 24.82 ? 32  LEU A O     1 
ATOM   181  C  CB    . LEU A 1 53  ? 20.830  -4.191  -4.073  1.00 30.89 ? 32  LEU A CB    1 
ATOM   182  C  CG    . LEU A 1 53  ? 22.105  -3.694  -3.419  1.00 29.98 ? 32  LEU A CG    1 
ATOM   183  C  CD1   . LEU A 1 53  ? 21.768  -2.836  -2.215  1.00 29.43 ? 32  LEU A CD1   1 
ATOM   184  C  CD2   . LEU A 1 53  ? 23.003  -4.853  -3.041  1.00 29.79 ? 32  LEU A CD2   1 
ATOM   185  N  N     . VAL A 1 54  ? 19.211  -6.619  -5.546  1.00 24.63 ? 33  VAL A N     1 
ATOM   186  C  CA    . VAL A 1 54  ? 17.822  -7.117  -5.733  1.00 25.32 ? 33  VAL A CA    1 
ATOM   187  C  C     . VAL A 1 54  ? 17.161  -7.197  -4.360  1.00 23.74 ? 33  VAL A C     1 
ATOM   188  O  O     . VAL A 1 54  ? 17.627  -8.016  -3.555  1.00 21.65 ? 33  VAL A O     1 
ATOM   189  C  CB    . VAL A 1 54  ? 17.775  -8.491  -6.425  1.00 24.99 ? 33  VAL A CB    1 
ATOM   190  C  CG1   . VAL A 1 54  ? 16.342  -8.833  -6.804  1.00 25.46 ? 33  VAL A CG1   1 
ATOM   191  C  CG2   . VAL A 1 54  ? 18.679  -8.553  -7.642  1.00 24.41 ? 33  VAL A CG2   1 
ATOM   192  N  N     . LEU A 1 55  ? 16.128  -6.382  -4.111  1.00 22.24 ? 34  LEU A N     1 
ATOM   193  C  CA    . LEU A 1 55  ? 15.371  -6.423  -2.842  1.00 20.42 ? 34  LEU A CA    1 
ATOM   194  C  C     . LEU A 1 55  ? 14.056  -7.164  -3.116  1.00 23.00 ? 34  LEU A C     1 
ATOM   195  O  O     . LEU A 1 55  ? 13.216  -6.667  -3.944  1.00 19.66 ? 34  LEU A O     1 
ATOM   196  C  CB    . LEU A 1 55  ? 15.140  -5.016  -2.284  1.00 20.12 ? 34  LEU A CB    1 
ATOM   197  C  CG    . LEU A 1 55  ? 16.325  -4.069  -2.309  1.00 19.68 ? 34  LEU A CG    1 
ATOM   198  C  CD1   . LEU A 1 55  ? 15.939  -2.708  -1.760  1.00 20.73 ? 34  LEU A CD1   1 
ATOM   199  C  CD2   . LEU A 1 55  ? 17.486  -4.642  -1.526  1.00 20.42 ? 34  LEU A CD2   1 
ATOM   200  N  N     . GLU A 1 56  ? 13.888  -8.296  -2.412  1.00 22.39 ? 35  GLU A N     1 
ATOM   201  C  CA    . GLU A 1 56  ? 12.800  -9.275  -2.604  1.00 21.85 ? 35  GLU A CA    1 
ATOM   202  C  C     . GLU A 1 56  ? 12.053  -9.421  -1.291  1.00 21.60 ? 35  GLU A C     1 
ATOM   203  O  O     . GLU A 1 56  ? 12.709  -9.701  -0.290  1.00 23.89 ? 35  GLU A O     1 
ATOM   204  C  CB    . GLU A 1 56  ? 13.378  -10.617 -3.047  1.00 23.98 ? 35  GLU A CB    1 
ATOM   205  C  CG    . GLU A 1 56  ? 12.387  -11.765 -2.980  1.00 25.84 ? 35  GLU A CG    1 
ATOM   206  C  CD    . GLU A 1 56  ? 11.062  -11.541 -3.695  1.00 23.20 ? 35  GLU A CD    1 
ATOM   207  O  OE1   . GLU A 1 56  ? 10.007  -11.767 -3.047  1.00 22.88 ? 35  GLU A OE1   1 
ATOM   208  O  OE2   . GLU A 1 56  ? 11.090  -11.156 -4.888  1.00 19.91 ? 35  GLU A OE2   1 
ATOM   209  N  N     . ALA A 1 57  ? 10.728  -9.301  -1.345  1.00 20.83 ? 36  ALA A N     1 
ATOM   210  C  CA    . ALA A 1 57  ? 9.796   -9.327  -0.198  1.00 20.70 ? 36  ALA A CA    1 
ATOM   211  C  C     . ALA A 1 57  ? 9.762   -10.714 0.480   1.00 20.07 ? 36  ALA A C     1 
ATOM   212  O  O     . ALA A 1 57  ? 9.774   -10.740 1.699   1.00 20.22 ? 36  ALA A O     1 
ATOM   213  C  CB    . ALA A 1 57  ? 8.417   -8.905  -0.669  1.00 21.98 ? 36  ALA A CB    1 
ATOM   214  N  N     . ARG A 1 58  ? 9.667   -11.808 -0.283  1.00 20.37 ? 37  ARG A N     1 
ATOM   215  C  CA    . ARG A 1 58  ? 9.620   -13.209 0.209   1.00 18.67 ? 37  ARG A CA    1 
ATOM   216  C  C     . ARG A 1 58  ? 11.007  -13.646 0.673   1.00 19.17 ? 37  ARG A C     1 
ATOM   217  O  O     . ARG A 1 58  ? 11.986  -13.004 0.288   1.00 17.81 ? 37  ARG A O     1 
ATOM   218  C  CB    . ARG A 1 58  ? 9.191   -14.179 -0.898  1.00 18.06 ? 37  ARG A CB    1 
ATOM   219  C  CG    . ARG A 1 58  ? 7.728   -14.060 -1.312  1.00 19.69 ? 37  ARG A CG    1 
ATOM   220  C  CD    . ARG A 1 58  ? 7.444   -15.011 -2.462  1.00 20.06 ? 37  ARG A CD    1 
ATOM   221  N  NE    . ARG A 1 58  ? 6.013   -15.169 -2.668  1.00 20.60 ? 37  ARG A NE    1 
ATOM   222  C  CZ    . ARG A 1 58  ? 5.312   -14.699 -3.680  1.00 21.34 ? 37  ARG A CZ    1 
ATOM   223  N  NH1   . ARG A 1 58  ? 5.908   -14.009 -4.646  1.00 22.99 ? 37  ARG A NH1   1 
ATOM   224  N  NH2   . ARG A 1 58  ? 4.016   -14.952 -3.741  1.00 20.71 ? 37  ARG A NH2   1 
ATOM   225  N  N     . ASP A 1 59  ? 11.074  -14.793 1.351   1.00 19.63 ? 38  ASP A N     1 
ATOM   226  C  CA    . ASP A 1 59  ? 12.339  -15.434 1.791   1.00 20.55 ? 38  ASP A CA    1 
ATOM   227  C  C     . ASP A 1 59  ? 12.917  -16.293 0.655   1.00 19.94 ? 38  ASP A C     1 
ATOM   228  O  O     . ASP A 1 59  ? 13.796  -17.122 0.947   1.00 20.45 ? 38  ASP A O     1 
ATOM   229  C  CB    . ASP A 1 59  ? 12.120  -16.293 3.039   1.00 20.97 ? 38  ASP A CB    1 
ATOM   230  C  CG    . ASP A 1 59  ? 11.207  -17.492 2.788   1.00 23.90 ? 38  ASP A CG    1 
ATOM   231  O  OD1   . ASP A 1 59  ? 10.790  -17.676 1.629   1.00 26.22 ? 38  ASP A OD1   1 
ATOM   232  O  OD2   . ASP A 1 59  ? 10.918  -18.235 3.750   1.00 24.61 ? 38  ASP A OD2   1 
ATOM   233  N  N     . ARG A 1 60  ? 12.443  -16.144 -0.578  1.00 18.30 ? 39  ARG A N     1 
ATOM   234  C  CA    . ARG A 1 60  ? 12.917  -17.001 -1.682  1.00 17.77 ? 39  ARG A CA    1 
ATOM   235  C  C     . ARG A 1 60  ? 12.839  -16.190 -2.955  1.00 18.32 ? 39  ARG A C     1 
ATOM   236  O  O     . ARG A 1 60  ? 12.186  -15.102 -2.924  1.00 19.01 ? 39  ARG A O     1 
ATOM   237  C  CB    . ARG A 1 60  ? 12.081  -18.274 -1.816  1.00 19.33 ? 39  ARG A CB    1 
ATOM   238  C  CG    . ARG A 1 60  ? 10.646  -18.014 -2.276  1.00 20.05 ? 39  ARG A CG    1 
ATOM   239  C  CD    . ARG A 1 60  ? 9.770   -19.224 -2.534  1.00 20.30 ? 39  ARG A CD    1 
ATOM   240  N  NE    . ARG A 1 60  ? 8.401   -18.789 -2.830  1.00 20.85 ? 39  ARG A NE    1 
ATOM   241  C  CZ    . ARG A 1 60  ? 8.015   -18.377 -4.025  1.00 21.33 ? 39  ARG A CZ    1 
ATOM   242  N  NH1   . ARG A 1 60  ? 8.888   -18.377 -5.031  1.00 22.42 ? 39  ARG A NH1   1 
ATOM   243  N  NH2   . ARG A 1 60  ? 6.773   -17.970 -4.222  1.00 19.25 ? 39  ARG A NH2   1 
ATOM   244  N  N     . VAL A 1 61  ? 13.434  -16.738 -4.018  1.00 18.26 ? 40  VAL A N     1 
ATOM   245  C  CA    . VAL A 1 61  ? 13.357  -16.202 -5.404  1.00 18.13 ? 40  VAL A CA    1 
ATOM   246  C  C     . VAL A 1 61  ? 12.342  -17.033 -6.218  1.00 19.56 ? 40  VAL A C     1 
ATOM   247  O  O     . VAL A 1 61  ? 11.935  -18.159 -5.784  1.00 22.13 ? 40  VAL A O     1 
ATOM   248  C  CB    . VAL A 1 61  ? 14.742  -16.163 -6.069  1.00 17.35 ? 40  VAL A CB    1 
ATOM   249  C  CG1   . VAL A 1 61  ? 15.772  -15.466 -5.198  1.00 17.78 ? 40  VAL A CG1   1 
ATOM   250  C  CG2   . VAL A 1 61  ? 15.220  -17.535 -6.485  1.00 16.19 ? 40  VAL A CG2   1 
ATOM   251  N  N     . GLY A 1 62  ? 11.942  -16.507 -7.366  1.00 19.38 ? 41  GLY A N     1 
ATOM   252  C  CA    . GLY A 1 62  ? 11.054  -17.200 -8.316  1.00 21.27 ? 41  GLY A CA    1 
ATOM   253  C  C     . GLY A 1 62  ? 9.705   -16.535 -8.453  1.00 19.45 ? 41  GLY A C     1 
ATOM   254  O  O     . GLY A 1 62  ? 9.085   -16.772 -9.473  1.00 23.40 ? 41  GLY A O     1 
ATOM   255  N  N     . GLY A 1 63  ? 9.233   -15.809 -7.438  1.00 19.52 ? 42  GLY A N     1 
ATOM   256  C  CA    . GLY A 1 63  ? 7.933   -15.102 -7.459  1.00 19.86 ? 42  GLY A CA    1 
ATOM   257  C  C     . GLY A 1 63  ? 6.742   -16.005 -7.803  1.00 19.03 ? 42  GLY A C     1 
ATOM   258  O  O     . GLY A 1 63  ? 6.344   -16.806 -6.979  1.00 19.66 ? 42  GLY A O     1 
ATOM   259  N  N     . ARG A 1 64  ? 6.178   -15.852 -8.995  1.00 19.91 ? 43  ARG A N     1 
ATOM   260  C  CA    . ARG A 1 64  ? 4.968   -16.566 -9.498  1.00 18.14 ? 43  ARG A CA    1 
ATOM   261  C  C     . ARG A 1 64  ? 5.385   -17.955 -9.986  1.00 18.12 ? 43  ARG A C     1 
ATOM   262  O  O     . ARG A 1 64  ? 4.509   -18.686 -10.427 1.00 18.31 ? 43  ARG A O     1 
ATOM   263  C  CB    . ARG A 1 64  ? 4.283   -15.790 -10.631 1.00 16.61 ? 43  ARG A CB    1 
ATOM   264  C  CG    . ARG A 1 64  ? 3.283   -14.725 -10.203 1.00 16.58 ? 43  ARG A CG    1 
ATOM   265  C  CD    . ARG A 1 64  ? 2.766   -13.893 -11.364 1.00 15.85 ? 43  ARG A CD    1 
ATOM   266  N  NE    . ARG A 1 64  ? 3.467   -12.656 -11.633 1.00 15.58 ? 43  ARG A NE    1 
ATOM   267  C  CZ    . ARG A 1 64  ? 3.120   -11.774 -12.588 1.00 16.02 ? 43  ARG A CZ    1 
ATOM   268  N  NH1   . ARG A 1 64  ? 2.081   -11.986 -13.376 1.00 14.38 ? 43  ARG A NH1   1 
ATOM   269  N  NH2   . ARG A 1 64  ? 3.825   -10.669 -12.752 1.00 17.45 ? 43  ARG A NH2   1 
ATOM   270  N  N     . THR A 1 65  ? 6.678   -18.299 -9.915  1.00 18.84 ? 44  THR A N     1 
ATOM   271  C  CA    . THR A 1 65  ? 7.154   -19.707 -10.004 1.00 20.45 ? 44  THR A CA    1 
ATOM   272  C  C     . THR A 1 65  ? 7.553   -20.098 -8.588  1.00 20.91 ? 44  THR A C     1 
ATOM   273  O  O     . THR A 1 65  ? 8.032   -19.220 -7.878  1.00 19.56 ? 44  THR A O     1 
ATOM   274  C  CB    . THR A 1 65  ? 8.258   -19.921 -11.058 1.00 22.16 ? 44  THR A CB    1 
ATOM   275  O  OG1   . THR A 1 65  ? 9.507   -19.438 -10.541 1.00 22.53 ? 44  THR A OG1   1 
ATOM   276  C  CG2   . THR A 1 65  ? 7.916   -19.279 -12.399 1.00 20.54 ? 44  THR A CG2   1 
ATOM   277  N  N     . CYS A 1 66  ? 7.294   -21.340 -8.182  1.00 20.97 ? 45  CYS A N     1 
ATOM   278  C  CA    . CYS A 1 66  ? 7.440   -21.779 -6.771  1.00 22.33 ? 45  CYS A CA    1 
ATOM   279  C  C     . CYS A 1 66  ? 7.410   -23.294 -6.750  1.00 21.93 ? 45  CYS A C     1 
ATOM   280  O  O     . CYS A 1 66  ? 6.435   -23.835 -7.260  1.00 22.51 ? 45  CYS A O     1 
ATOM   281  C  CB    . CYS A 1 66  ? 6.348   -21.208 -5.864  1.00 23.00 ? 45  CYS A CB    1 
ATOM   282  S  SG    . CYS A 1 66  ? 6.339   -21.904 -4.189  1.00 24.96 ? 45  CYS A SG    1 
ATOM   283  N  N     . THR A 1 67  ? 8.484   -23.920 -6.254  1.00 22.51 ? 46  THR A N     1 
ATOM   284  C  CA    . THR A 1 67  ? 8.634   -25.391 -6.243  1.00 22.84 ? 46  THR A CA    1 
ATOM   285  C  C     . THR A 1 67  ? 8.885   -25.859 -4.815  1.00 22.11 ? 46  THR A C     1 
ATOM   286  O  O     . THR A 1 67  ? 9.690   -25.254 -4.133  1.00 24.09 ? 46  THR A O     1 
ATOM   287  C  CB    . THR A 1 67  ? 9.694   -25.881 -7.229  1.00 21.17 ? 46  THR A CB    1 
ATOM   288  O  OG1   . THR A 1 67  ? 9.486   -25.258 -8.492  1.00 22.00 ? 46  THR A OG1   1 
ATOM   289  C  CG2   . THR A 1 67  ? 9.611   -27.374 -7.432  1.00 22.12 ? 46  THR A CG2   1 
ATOM   290  N  N     . GLU A 1 68  ? 8.150   -26.887 -4.414  1.00 23.80 ? 47  GLU A N     1 
ATOM   291  C  CA    . GLU A 1 68  ? 8.234   -27.579 -3.111  1.00 26.83 ? 47  GLU A CA    1 
ATOM   292  C  C     . GLU A 1 68  ? 8.455   -29.069 -3.374  1.00 28.26 ? 47  GLU A C     1 
ATOM   293  O  O     . GLU A 1 68  ? 7.824   -29.576 -4.318  1.00 27.27 ? 47  GLU A O     1 
ATOM   294  C  CB    . GLU A 1 68  ? 6.954   -27.304 -2.326  1.00 26.30 ? 47  GLU A CB    1 
ATOM   295  C  CG    . GLU A 1 68  ? 7.006   -25.966 -1.597  1.00 26.49 ? 47  GLU A CG    1 
ATOM   296  C  CD    . GLU A 1 68  ? 5.685   -25.471 -1.011  1.00 31.19 ? 47  GLU A CD    1 
ATOM   297  O  OE1   . GLU A 1 68  ? 5.657   -24.277 -0.587  1.00 38.40 ? 47  GLU A OE1   1 
ATOM   298  O  OE2   . GLU A 1 68  ? 4.688   -26.261 -0.958  1.00 26.05 ? 47  GLU A OE2   1 
ATOM   299  N  N     . GLU A 1 69  ? 9.274   -29.735 -2.552  1.00 28.13 ? 48  GLU A N     1 
ATOM   300  C  CA    . GLU A 1 69  ? 9.446   -31.216 -2.562  1.00 32.88 ? 48  GLU A CA    1 
ATOM   301  C  C     . GLU A 1 69  ? 8.288   -31.879 -1.795  1.00 30.06 ? 48  GLU A C     1 
ATOM   302  O  O     . GLU A 1 69  ? 8.103   -31.535 -0.649  1.00 29.22 ? 48  GLU A O     1 
ATOM   303  C  CB    . GLU A 1 69  ? 10.790  -31.594 -1.929  1.00 40.33 ? 48  GLU A CB    1 
ATOM   304  C  CG    . GLU A 1 69  ? 11.198  -33.059 -2.137  1.00 49.51 ? 48  GLU A CG    1 
ATOM   305  C  CD    . GLU A 1 69  ? 12.160  -33.347 -3.292  1.00 57.74 ? 48  GLU A CD    1 
ATOM   306  O  OE1   . GLU A 1 69  ? 12.641  -34.516 -3.366  1.00 57.06 ? 48  GLU A OE1   1 
ATOM   307  O  OE2   . GLU A 1 69  ? 12.421  -32.418 -4.135  1.00 56.26 ? 48  GLU A OE2   1 
ATOM   308  N  N     . HIS A 1 70  ? 7.551   -32.804 -2.419  1.00 28.48 ? 49  HIS A N     1 
ATOM   309  C  CA    . HIS A 1 70  ? 6.466   -33.610 -1.787  1.00 26.04 ? 49  HIS A CA    1 
ATOM   310  C  C     . HIS A 1 70  ? 6.401   -34.988 -2.436  1.00 25.34 ? 49  HIS A C     1 
ATOM   311  O  O     . HIS A 1 70  ? 6.354   -35.034 -3.662  1.00 26.86 ? 49  HIS A O     1 
ATOM   312  C  CB    . HIS A 1 70  ? 5.098   -32.931 -1.939  1.00 25.18 ? 49  HIS A CB    1 
ATOM   313  C  CG    . HIS A 1 70  ? 4.950   -31.632 -1.230  1.00 24.76 ? 49  HIS A CG    1 
ATOM   314  N  ND1   . HIS A 1 70  ? 4.468   -31.553 0.055   1.00 27.04 ? 49  HIS A ND1   1 
ATOM   315  C  CD2   . HIS A 1 70  ? 5.106   -30.358 -1.657  1.00 26.16 ? 49  HIS A CD2   1 
ATOM   316  C  CE1   . HIS A 1 70  ? 4.355   -30.285 0.411   1.00 27.03 ? 49  HIS A CE1   1 
ATOM   317  N  NE2   . HIS A 1 70  ? 4.734   -29.524 -0.633  1.00 26.46 ? 49  HIS A NE2   1 
ATOM   318  N  N     . HIS A 1 71  ? 6.402   -36.063 -1.639  1.00 25.20 ? 50  HIS A N     1 
ATOM   319  C  CA    . HIS A 1 71  ? 6.214   -37.466 -2.099  1.00 23.61 ? 50  HIS A CA    1 
ATOM   320  C  C     . HIS A 1 71  ? 7.351   -37.895 -3.026  1.00 23.63 ? 50  HIS A C     1 
ATOM   321  O  O     . HIS A 1 71  ? 7.099   -38.715 -3.929  1.00 25.04 ? 50  HIS A O     1 
ATOM   322  C  CB    . HIS A 1 71  ? 4.824   -37.645 -2.741  1.00 24.69 ? 50  HIS A CB    1 
ATOM   323  C  CG    . HIS A 1 71  ? 3.687   -37.345 -1.813  1.00 25.29 ? 50  HIS A CG    1 
ATOM   324  N  ND1   . HIS A 1 71  ? 3.254   -38.264 -0.869  1.00 24.32 ? 50  HIS A ND1   1 
ATOM   325  C  CD2   . HIS A 1 71  ? 2.949   -36.217 -1.634  1.00 25.21 ? 50  HIS A CD2   1 
ATOM   326  C  CE1   . HIS A 1 71  ? 2.288   -37.732 -0.148  1.00 25.48 ? 50  HIS A CE1   1 
ATOM   327  N  NE2   . HIS A 1 71  ? 2.070   -36.465 -0.606  1.00 27.66 ? 50  HIS A NE2   1 
ATOM   328  N  N     . GLY A 1 72  ? 8.574   -37.421 -2.769  1.00 25.23 ? 51  GLY A N     1 
ATOM   329  C  CA    . GLY A 1 72  ? 9.780   -37.848 -3.504  1.00 22.31 ? 51  GLY A CA    1 
ATOM   330  C  C     . GLY A 1 72  ? 9.941   -37.109 -4.832  1.00 25.59 ? 51  GLY A C     1 
ATOM   331  O  O     . GLY A 1 72  ? 10.806  -37.519 -5.625  1.00 25.15 ? 51  GLY A O     1 
ATOM   332  N  N     . THR A 1 73  ? 9.182   -36.026 -5.077  1.00 25.09 ? 52  THR A N     1 
ATOM   333  C  CA    . THR A 1 73  ? 9.213   -35.321 -6.387  1.00 25.26 ? 52  THR A CA    1 
ATOM   334  C  C     . THR A 1 73  ? 8.960   -33.823 -6.218  1.00 22.39 ? 52  THR A C     1 
ATOM   335  O  O     . THR A 1 73  ? 8.769   -33.361 -5.120  1.00 23.67 ? 52  THR A O     1 
ATOM   336  C  CB    . THR A 1 73  ? 8.232   -35.993 -7.357  1.00 26.80 ? 52  THR A CB    1 
ATOM   337  O  OG1   . THR A 1 73  ? 8.627   -35.705 -8.697  1.00 28.69 ? 52  THR A OG1   1 
ATOM   338  C  CG2   . THR A 1 73  ? 6.799   -35.547 -7.159  1.00 28.96 ? 52  THR A CG2   1 
ATOM   339  N  N     . TRP A 1 74  ? 9.004   -33.084 -7.319  1.00 24.65 ? 53  TRP A N     1 
ATOM   340  C  CA    . TRP A 1 74  ? 8.875   -31.602 -7.358  1.00 21.41 ? 53  TRP A CA    1 
ATOM   341  C  C     . TRP A 1 74  ? 7.416   -31.261 -7.648  1.00 19.60 ? 53  TRP A C     1 
ATOM   342  O  O     . TRP A 1 74  ? 6.782   -31.974 -8.468  1.00 16.94 ? 53  TRP A O     1 
ATOM   343  C  CB    . TRP A 1 74  ? 9.844   -30.997 -8.384  1.00 22.73 ? 53  TRP A CB    1 
ATOM   344  C  CG    . TRP A 1 74  ? 9.720   -31.607 -9.745  1.00 24.95 ? 53  TRP A CG    1 
ATOM   345  C  CD1   . TRP A 1 74  ? 8.892   -31.201 -10.754 1.00 23.17 ? 53  TRP A CD1   1 
ATOM   346  C  CD2   . TRP A 1 74  ? 10.375  -32.794 -10.217 1.00 25.55 ? 53  TRP A CD2   1 
ATOM   347  N  NE1   . TRP A 1 74  ? 9.010   -32.036 -11.823 1.00 24.22 ? 53  TRP A NE1   1 
ATOM   348  C  CE2   . TRP A 1 74  ? 9.909   -33.024 -11.525 1.00 25.09 ? 53  TRP A CE2   1 
ATOM   349  C  CE3   . TRP A 1 74  ? 11.300  -33.693 -9.660  1.00 25.86 ? 53  TRP A CE3   1 
ATOM   350  C  CZ2   . TRP A 1 74  ? 10.338  -34.120 -12.279 1.00 27.82 ? 53  TRP A CZ2   1 
ATOM   351  C  CZ3   . TRP A 1 74  ? 11.741  -34.756 -10.412 1.00 22.85 ? 53  TRP A CZ3   1 
ATOM   352  C  CH2   . TRP A 1 74  ? 11.261  -34.971 -11.703 1.00 25.72 ? 53  TRP A CH2   1 
ATOM   353  N  N     . ILE A 1 75  ? 6.893   -30.283 -6.917  1.00 19.15 ? 54  ILE A N     1 
ATOM   354  C  CA    . ILE A 1 75  ? 5.504   -29.766 -7.016  1.00 19.47 ? 54  ILE A CA    1 
ATOM   355  C  C     . ILE A 1 75  ? 5.601   -28.287 -7.389  1.00 20.53 ? 54  ILE A C     1 
ATOM   356  O  O     . ILE A 1 75  ? 5.983   -27.453 -6.529  1.00 20.23 ? 54  ILE A O     1 
ATOM   357  C  CB    . ILE A 1 75  ? 4.736   -29.987 -5.702  1.00 19.94 ? 54  ILE A CB    1 
ATOM   358  C  CG1   . ILE A 1 75  ? 4.737   -31.453 -5.260  1.00 20.09 ? 54  ILE A CG1   1 
ATOM   359  C  CG2   . ILE A 1 75  ? 3.323   -29.458 -5.832  1.00 21.48 ? 54  ILE A CG2   1 
ATOM   360  C  CD1   . ILE A 1 75  ? 4.156   -32.452 -6.297  1.00 20.75 ? 54  ILE A CD1   1 
ATOM   361  N  N     . ASP A 1 76  ? 5.328   -27.987 -8.664  1.00 22.51 ? 55  ASP A N     1 
ATOM   362  C  CA    . ASP A 1 76  ? 5.228   -26.612 -9.207  1.00 20.69 ? 55  ASP A CA    1 
ATOM   363  C  C     . ASP A 1 76  ? 3.863   -26.035 -8.820  1.00 21.68 ? 55  ASP A C     1 
ATOM   364  O  O     . ASP A 1 76  ? 2.862   -26.334 -9.540  1.00 22.36 ? 55  ASP A O     1 
ATOM   365  C  CB    . ASP A 1 76  ? 5.480   -26.620 -10.716 1.00 20.05 ? 55  ASP A CB    1 
ATOM   366  C  CG    . ASP A 1 76  ? 6.959   -26.579 -11.079 1.00 19.66 ? 55  ASP A CG    1 
ATOM   367  O  OD1   . ASP A 1 76  ? 7.692   -25.798 -10.452 1.00 19.16 ? 55  ASP A OD1   1 
ATOM   368  O  OD2   . ASP A 1 76  ? 7.358   -27.326 -11.974 1.00 18.10 ? 55  ASP A OD2   1 
ATOM   369  N  N     . LEU A 1 77  ? 3.825   -25.210 -7.765  1.00 20.17 ? 56  LEU A N     1 
ATOM   370  C  CA    . LEU A 1 77  ? 2.599   -24.498 -7.302  1.00 20.64 ? 56  LEU A CA    1 
ATOM   371  C  C     . LEU A 1 77  ? 2.339   -23.325 -8.240  1.00 19.90 ? 56  LEU A C     1 
ATOM   372  O  O     . LEU A 1 77  ? 1.182   -22.899 -8.335  1.00 19.18 ? 56  LEU A O     1 
ATOM   373  C  CB    . LEU A 1 77  ? 2.781   -24.013 -5.854  1.00 22.60 ? 56  LEU A CB    1 
ATOM   374  C  CG    . LEU A 1 77  ? 3.110   -25.127 -4.853  1.00 23.60 ? 56  LEU A CG    1 
ATOM   375  C  CD1   . LEU A 1 77  ? 3.980   -24.612 -3.731  1.00 27.20 ? 56  LEU A CD1   1 
ATOM   376  C  CD2   . LEU A 1 77  ? 1.856   -25.765 -4.305  1.00 25.45 ? 56  LEU A CD2   1 
ATOM   377  N  N     . GLY A 1 78  ? 3.379   -22.820 -8.905  1.00 19.39 ? 57  GLY A N     1 
ATOM   378  C  CA    . GLY A 1 78  ? 3.241   -21.739 -9.905  1.00 20.30 ? 57  GLY A CA    1 
ATOM   379  C  C     . GLY A 1 78  ? 3.515   -22.245 -11.312 1.00 20.18 ? 57  GLY A C     1 
ATOM   380  O  O     . GLY A 1 78  ? 3.324   -23.453 -11.543 1.00 17.93 ? 57  GLY A O     1 
ATOM   381  N  N     . GLY A 1 79  ? 3.985   -21.359 -12.207 1.00 19.24 ? 58  GLY A N     1 
ATOM   382  C  CA    . GLY A 1 79  ? 4.270   -21.697 -13.608 1.00 18.55 ? 58  GLY A CA    1 
ATOM   383  C  C     . GLY A 1 79  ? 5.135   -22.931 -13.749 1.00 17.73 ? 58  GLY A C     1 
ATOM   384  O  O     . GLY A 1 79  ? 6.075   -23.051 -12.986 1.00 17.20 ? 58  GLY A O     1 
ATOM   385  N  N     . GLN A 1 80  ? 4.827   -23.837 -14.680 1.00 17.82 ? 59  GLN A N     1 
ATOM   386  C  CA    . GLN A 1 80  ? 5.580   -25.103 -14.789 1.00 19.17 ? 59  GLN A CA    1 
ATOM   387  C  C     . GLN A 1 80  ? 6.022   -25.387 -16.224 1.00 20.37 ? 59  GLN A C     1 
ATOM   388  O  O     . GLN A 1 80  ? 7.020   -26.089 -16.364 1.00 17.72 ? 59  GLN A O     1 
ATOM   389  C  CB    . GLN A 1 80  ? 4.779   -26.278 -14.232 1.00 20.44 ? 59  GLN A CB    1 
ATOM   390  C  CG    . GLN A 1 80  ? 3.480   -26.605 -14.969 1.00 20.76 ? 59  GLN A CG    1 
ATOM   391  C  CD    . GLN A 1 80  ? 2.766   -27.757 -14.288 1.00 21.80 ? 59  GLN A CD    1 
ATOM   392  O  OE1   . GLN A 1 80  ? 2.701   -27.821 -13.064 1.00 21.58 ? 59  GLN A OE1   1 
ATOM   393  N  NE2   . GLN A 1 80  ? 2.269   -28.713 -15.064 1.00 23.36 ? 59  GLN A NE2   1 
ATOM   394  N  N     . TRP A 1 81  ? 5.261   -24.904 -17.211 1.00 22.90 ? 60  TRP A N     1 
ATOM   395  C  CA    . TRP A 1 81  ? 5.307   -25.312 -18.641 1.00 23.56 ? 60  TRP A CA    1 
ATOM   396  C  C     . TRP A 1 81  ? 6.190   -24.357 -19.453 1.00 23.58 ? 60  TRP A C     1 
ATOM   397  O  O     . TRP A 1 81  ? 6.116   -23.133 -19.229 1.00 23.91 ? 60  TRP A O     1 
ATOM   398  C  CB    . TRP A 1 81  ? 3.895   -25.320 -19.217 1.00 26.05 ? 60  TRP A CB    1 
ATOM   399  C  CG    . TRP A 1 81  ? 3.077   -26.532 -18.900 1.00 26.93 ? 60  TRP A CG    1 
ATOM   400  C  CD1   . TRP A 1 81  ? 3.386   -27.829 -19.180 1.00 27.39 ? 60  TRP A CD1   1 
ATOM   401  C  CD2   . TRP A 1 81  ? 1.788   -26.556 -18.268 1.00 26.89 ? 60  TRP A CD2   1 
ATOM   402  N  NE1   . TRP A 1 81  ? 2.372   -28.657 -18.770 1.00 27.71 ? 60  TRP A NE1   1 
ATOM   403  C  CE2   . TRP A 1 81  ? 1.369   -27.904 -18.228 1.00 28.60 ? 60  TRP A CE2   1 
ATOM   404  C  CE3   . TRP A 1 81  ? 0.936   -25.575 -17.759 1.00 28.05 ? 60  TRP A CE3   1 
ATOM   405  C  CZ2   . TRP A 1 81  ? 0.147   -28.295 -17.685 1.00 28.46 ? 60  TRP A CZ2   1 
ATOM   406  C  CZ3   . TRP A 1 81  ? -0.267  -25.962 -17.208 1.00 27.75 ? 60  TRP A CZ3   1 
ATOM   407  C  CH2   . TRP A 1 81  ? -0.656  -27.304 -17.180 1.00 29.42 ? 60  TRP A CH2   1 
ATOM   408  N  N     . ILE A 1 82  ? 7.020   -24.895 -20.348 1.00 23.62 ? 61  ILE A N     1 
ATOM   409  C  CA    . ILE A 1 82  ? 7.611   -24.123 -21.472 1.00 21.90 ? 61  ILE A CA    1 
ATOM   410  C  C     . ILE A 1 82  ? 7.278   -24.886 -22.754 1.00 22.67 ? 61  ILE A C     1 
ATOM   411  O  O     . ILE A 1 82  ? 7.049   -26.090 -22.669 1.00 20.37 ? 61  ILE A O     1 
ATOM   412  C  CB    . ILE A 1 82  ? 9.122   -23.863 -21.303 1.00 22.00 ? 61  ILE A CB    1 
ATOM   413  C  CG1   . ILE A 1 82  ? 9.966   -25.136 -21.404 1.00 22.58 ? 61  ILE A CG1   1 
ATOM   414  C  CG2   . ILE A 1 82  ? 9.426   -23.089 -20.024 1.00 21.11 ? 61  ILE A CG2   1 
ATOM   415  C  CD1   . ILE A 1 82  ? 11.403  -24.875 -21.785 1.00 24.15 ? 61  ILE A CD1   1 
ATOM   416  N  N     . GLY A 1 83  ? 7.233   -24.170 -23.879 1.00 23.71 ? 62  GLY A N     1 
ATOM   417  C  CA    . GLY A 1 83  ? 6.934   -24.715 -25.205 1.00 25.24 ? 62  GLY A CA    1 
ATOM   418  C  C     . GLY A 1 83  ? 7.670   -23.967 -26.311 1.00 26.70 ? 62  GLY A C     1 
ATOM   419  O  O     . GLY A 1 83  ? 8.401   -23.004 -26.068 1.00 23.59 ? 62  GLY A O     1 
ATOM   420  N  N     . PRO A 1 84  ? 7.509   -24.415 -27.573 1.00 28.96 ? 63  PRO A N     1 
ATOM   421  C  CA    . PRO A 1 84  ? 8.271   -23.849 -28.692 1.00 29.62 ? 63  PRO A CA    1 
ATOM   422  C  C     . PRO A 1 84  ? 7.801   -22.412 -28.949 1.00 27.66 ? 63  PRO A C     1 
ATOM   423  O  O     . PRO A 1 84  ? 6.638   -22.107 -28.655 1.00 31.07 ? 63  PRO A O     1 
ATOM   424  C  CB    . PRO A 1 84  ? 7.975   -24.831 -29.832 1.00 31.60 ? 63  PRO A CB    1 
ATOM   425  C  CG    . PRO A 1 84  ? 6.586   -25.356 -29.502 1.00 31.32 ? 63  PRO A CG    1 
ATOM   426  C  CD    . PRO A 1 84  ? 6.627   -25.514 -27.986 1.00 32.16 ? 63  PRO A CD    1 
ATOM   427  N  N     . GLY A 1 85  ? 8.728   -21.560 -29.387 1.00 24.02 ? 64  GLY A N     1 
ATOM   428  C  CA    . GLY A 1 85  ? 8.517   -20.111 -29.575 1.00 22.46 ? 64  GLY A CA    1 
ATOM   429  C  C     . GLY A 1 85  ? 8.990   -19.302 -28.381 1.00 20.32 ? 64  GLY A C     1 
ATOM   430  O  O     . GLY A 1 85  ? 9.096   -18.068 -28.504 1.00 17.08 ? 64  GLY A O     1 
ATOM   431  N  N     . GLN A 1 86  ? 9.239   -19.971 -27.252 1.00 20.90 ? 65  GLN A N     1 
ATOM   432  C  CA    . GLN A 1 86  ? 9.703   -19.328 -26.000 1.00 22.81 ? 65  GLN A CA    1 
ATOM   433  C  C     . GLN A 1 86  ? 11.232  -19.432 -25.943 1.00 23.86 ? 65  GLN A C     1 
ATOM   434  O  O     . GLN A 1 86  ? 11.735  -20.229 -25.123 1.00 25.46 ? 65  GLN A O     1 
ATOM   435  C  CB    . GLN A 1 86  ? 9.010   -19.972 -24.787 1.00 23.66 ? 65  GLN A CB    1 
ATOM   436  C  CG    . GLN A 1 86  ? 7.497   -19.787 -24.714 1.00 19.96 ? 65  GLN A CG    1 
ATOM   437  C  CD    . GLN A 1 86  ? 6.921   -20.509 -23.513 1.00 21.12 ? 65  GLN A CD    1 
ATOM   438  O  OE1   . GLN A 1 86  ? 7.576   -21.322 -22.875 1.00 20.37 ? 65  GLN A OE1   1 
ATOM   439  N  NE2   . GLN A 1 86  ? 5.678   -20.208 -23.164 1.00 22.65 ? 65  GLN A NE2   1 
ATOM   440  N  N     . ASP A 1 87  ? 11.929  -18.588 -26.717 1.00 27.18 ? 66  ASP A N     1 
ATOM   441  C  CA    . ASP A 1 87  ? 13.394  -18.648 -27.044 1.00 28.23 ? 66  ASP A CA    1 
ATOM   442  C  C     . ASP A 1 87  ? 14.235  -18.375 -25.796 1.00 26.29 ? 66  ASP A C     1 
ATOM   443  O  O     . ASP A 1 87  ? 15.342  -18.958 -25.633 1.00 25.76 ? 66  ASP A O     1 
ATOM   444  C  CB    . ASP A 1 87  ? 13.766  -17.592 -28.105 1.00 29.44 ? 66  ASP A CB    1 
ATOM   445  C  CG    . ASP A 1 87  ? 13.144  -17.853 -29.463 1.00 32.19 ? 66  ASP A CG    1 
ATOM   446  O  OD1   . ASP A 1 87  ? 12.986  -19.036 -29.798 1.00 36.98 ? 66  ASP A OD1   1 
ATOM   447  O  OD2   . ASP A 1 87  ? 12.795  -16.882 -30.167 1.00 35.32 ? 66  ASP A OD2   1 
ATOM   448  N  N     . ARG A 1 88  ? 13.762  -17.468 -24.949 1.00 26.87 ? 67  ARG A N     1 
ATOM   449  C  CA    . ARG A 1 88  ? 14.614  -16.882 -23.880 1.00 25.37 ? 67  ARG A CA    1 
ATOM   450  C  C     . ARG A 1 88  ? 14.672  -17.832 -22.683 1.00 23.61 ? 67  ARG A C     1 
ATOM   451  O  O     . ARG A 1 88  ? 15.781  -18.027 -22.158 1.00 28.09 ? 67  ARG A O     1 
ATOM   452  C  CB    . ARG A 1 88  ? 14.134  -15.468 -23.582 1.00 26.94 ? 67  ARG A CB    1 
ATOM   453  C  CG    . ARG A 1 88  ? 14.155  -14.575 -24.811 1.00 27.35 ? 67  ARG A CG    1 
ATOM   454  C  CD    . ARG A 1 88  ? 13.746  -13.174 -24.463 1.00 32.17 ? 67  ARG A CD    1 
ATOM   455  N  NE    . ARG A 1 88  ? 12.502  -12.796 -25.128 1.00 41.37 ? 67  ARG A NE    1 
ATOM   456  C  CZ    . ARG A 1 88  ? 12.394  -11.910 -26.126 1.00 44.77 ? 67  ARG A CZ    1 
ATOM   457  N  NH1   . ARG A 1 88  ? 13.480  -11.297 -26.596 1.00 45.08 ? 67  ARG A NH1   1 
ATOM   458  N  NH2   . ARG A 1 88  ? 11.195  -11.639 -26.633 1.00 38.81 ? 67  ARG A NH2   1 
ATOM   459  N  N     . VAL A 1 89  ? 13.564  -18.463 -22.302 1.00 22.22 ? 68  VAL A N     1 
ATOM   460  C  CA    . VAL A 1 89  ? 13.552  -19.404 -21.146 1.00 20.70 ? 68  VAL A CA    1 
ATOM   461  C  C     . VAL A 1 89  ? 14.256  -20.685 -21.599 1.00 20.34 ? 68  VAL A C     1 
ATOM   462  O  O     . VAL A 1 89  ? 14.910  -21.328 -20.749 1.00 19.06 ? 68  VAL A O     1 
ATOM   463  C  CB    . VAL A 1 89  ? 12.122  -19.661 -20.599 1.00 21.41 ? 68  VAL A CB    1 
ATOM   464  C  CG1   . VAL A 1 89  ? 11.199  -20.272 -21.627 1.00 21.34 ? 68  VAL A CG1   1 
ATOM   465  C  CG2   . VAL A 1 89  ? 12.103  -20.526 -19.333 1.00 20.62 ? 68  VAL A CG2   1 
ATOM   466  N  N     . ALA A 1 90  ? 14.110  -21.069 -22.869 1.00 19.14 ? 69  ALA A N     1 
ATOM   467  C  CA    . ALA A 1 90  ? 14.764  -22.290 -23.385 1.00 21.93 ? 69  ALA A CA    1 
ATOM   468  C  C     . ALA A 1 90  ? 16.278  -22.046 -23.393 1.00 22.34 ? 69  ALA A C     1 
ATOM   469  O  O     . ALA A 1 90  ? 16.990  -22.921 -22.904 1.00 29.59 ? 69  ALA A O     1 
ATOM   470  C  CB    . ALA A 1 90  ? 14.211  -22.685 -24.718 1.00 21.02 ? 69  ALA A CB    1 
ATOM   471  N  N     . ALA A 1 91  ? 16.740  -20.872 -23.807 1.00 20.63 ? 70  ALA A N     1 
ATOM   472  C  CA    . ALA A 1 91  ? 18.143  -20.404 -23.624 1.00 23.17 ? 70  ALA A CA    1 
ATOM   473  C  C     . ALA A 1 91  ? 18.580  -20.409 -22.146 1.00 22.85 ? 70  ALA A C     1 
ATOM   474  O  O     . ALA A 1 91  ? 19.717  -20.740 -21.895 1.00 21.37 ? 70  ALA A O     1 
ATOM   475  C  CB    . ALA A 1 91  ? 18.304  -18.990 -24.174 1.00 23.72 ? 70  ALA A CB    1 
ATOM   476  N  N     . LEU A 1 92  ? 17.742  -19.958 -21.203 1.00 22.03 ? 71  LEU A N     1 
ATOM   477  C  CA    . LEU A 1 92  ? 18.123  -19.868 -19.770 1.00 22.06 ? 71  LEU A CA    1 
ATOM   478  C  C     . LEU A 1 92  ? 18.295  -21.293 -19.227 1.00 23.77 ? 71  LEU A C     1 
ATOM   479  O  O     . LEU A 1 92  ? 19.330  -21.560 -18.525 1.00 19.38 ? 71  LEU A O     1 
ATOM   480  C  CB    . LEU A 1 92  ? 17.059  -19.110 -18.961 1.00 21.90 ? 71  LEU A CB    1 
ATOM   481  C  CG    . LEU A 1 92  ? 17.466  -18.646 -17.567 1.00 22.29 ? 71  LEU A CG    1 
ATOM   482  C  CD1   . LEU A 1 92  ? 18.705  -17.773 -17.615 1.00 22.16 ? 71  LEU A CD1   1 
ATOM   483  C  CD2   . LEU A 1 92  ? 16.334  -17.870 -16.912 1.00 23.71 ? 71  LEU A CD2   1 
ATOM   484  N  N     . ALA A 1 93  ? 17.337  -22.178 -19.514 1.00 23.68 ? 72  ALA A N     1 
ATOM   485  C  CA    . ALA A 1 93  ? 17.345  -23.547 -18.946 1.00 26.14 ? 72  ALA A CA    1 
ATOM   486  C  C     . ALA A 1 93  ? 18.622  -24.229 -19.424 1.00 27.11 ? 72  ALA A C     1 
ATOM   487  O  O     . ALA A 1 93  ? 19.311  -24.901 -18.619 1.00 27.20 ? 72  ALA A O     1 
ATOM   488  C  CB    . ALA A 1 93  ? 16.109  -24.330 -19.330 1.00 25.81 ? 72  ALA A CB    1 
ATOM   489  N  N     . ALA A 1 94  ? 18.950  -24.011 -20.687 1.00 29.94 ? 73  ALA A N     1 
ATOM   490  C  CA    . ALA A 1 94  ? 20.079  -24.693 -21.346 1.00 30.62 ? 73  ALA A CA    1 
ATOM   491  C  C     . ALA A 1 94  ? 21.376  -24.101 -20.796 1.00 30.77 ? 73  ALA A C     1 
ATOM   492  O  O     . ALA A 1 94  ? 22.255  -24.875 -20.392 1.00 32.86 ? 73  ALA A O     1 
ATOM   493  C  CB    . ALA A 1 94  ? 19.954  -24.546 -22.833 1.00 28.47 ? 73  ALA A CB    1 
ATOM   494  N  N     . GLU A 1 95  ? 21.470  -22.776 -20.737 1.00 30.74 ? 74  GLU A N     1 
ATOM   495  C  CA    . GLU A 1 95  ? 22.648  -22.100 -20.143 1.00 31.69 ? 74  GLU A CA    1 
ATOM   496  C  C     . GLU A 1 95  ? 22.960  -22.689 -18.757 1.00 30.17 ? 74  GLU A C     1 
ATOM   497  O  O     . GLU A 1 95  ? 24.140  -22.920 -18.471 1.00 27.03 ? 74  GLU A O     1 
ATOM   498  C  CB    . GLU A 1 95  ? 22.424  -20.597 -20.049 1.00 31.79 ? 74  GLU A CB    1 
ATOM   499  C  CG    . GLU A 1 95  ? 23.663  -19.872 -19.544 1.00 34.50 ? 74  GLU A CG    1 
ATOM   500  C  CD    . GLU A 1 95  ? 23.440  -18.451 -19.062 1.00 35.66 ? 74  GLU A CD    1 
ATOM   501  O  OE1   . GLU A 1 95  ? 24.391  -17.863 -18.512 1.00 41.70 ? 74  GLU A OE1   1 
ATOM   502  O  OE2   . GLU A 1 95  ? 22.331  -17.930 -19.234 1.00 39.16 ? 74  GLU A OE2   1 
ATOM   503  N  N     . LEU A 1 96  ? 21.934  -22.917 -17.931 1.00 27.60 ? 75  LEU A N     1 
ATOM   504  C  CA    . LEU A 1 96  ? 22.080  -23.166 -16.475 1.00 27.84 ? 75  LEU A CA    1 
ATOM   505  C  C     . LEU A 1 96  ? 21.917  -24.663 -16.142 1.00 26.26 ? 75  LEU A C     1 
ATOM   506  O  O     . LEU A 1 96  ? 21.780  -24.972 -14.948 1.00 23.20 ? 75  LEU A O     1 
ATOM   507  C  CB    . LEU A 1 96  ? 21.036  -22.306 -15.760 1.00 28.58 ? 75  LEU A CB    1 
ATOM   508  C  CG    . LEU A 1 96  ? 21.163  -20.792 -15.946 1.00 28.81 ? 75  LEU A CG    1 
ATOM   509  C  CD1   . LEU A 1 96  ? 20.159  -20.080 -15.048 1.00 28.43 ? 75  LEU A CD1   1 
ATOM   510  C  CD2   . LEU A 1 96  ? 22.581  -20.310 -15.625 1.00 31.09 ? 75  LEU A CD2   1 
ATOM   511  N  N     . GLY A 1 97  ? 21.942  -25.546 -17.149 1.00 24.57 ? 76  GLY A N     1 
ATOM   512  C  CA    . GLY A 1 97  ? 22.039  -27.010 -16.987 1.00 25.54 ? 76  GLY A CA    1 
ATOM   513  C  C     . GLY A 1 97  ? 20.773  -27.637 -16.413 1.00 26.25 ? 76  GLY A C     1 
ATOM   514  O  O     . GLY A 1 97  ? 20.894  -28.579 -15.595 1.00 20.71 ? 76  GLY A O     1 
ATOM   515  N  N     . VAL A 1 98  ? 19.590  -27.168 -16.848 1.00 31.15 ? 77  VAL A N     1 
ATOM   516  C  CA    . VAL A 1 98  ? 18.263  -27.722 -16.410 1.00 29.57 ? 77  VAL A CA    1 
ATOM   517  C  C     . VAL A 1 98  ? 17.630  -28.490 -17.560 1.00 27.20 ? 77  VAL A C     1 
ATOM   518  O  O     . VAL A 1 98  ? 17.442  -27.931 -18.623 1.00 29.28 ? 77  VAL A O     1 
ATOM   519  C  CB    . VAL A 1 98  ? 17.281  -26.665 -15.893 1.00 28.95 ? 77  VAL A CB    1 
ATOM   520  C  CG1   . VAL A 1 98  ? 15.945  -27.307 -15.516 1.00 26.52 ? 77  VAL A CG1   1 
ATOM   521  C  CG2   . VAL A 1 98  ? 17.873  -25.903 -14.708 1.00 31.00 ? 77  VAL A CG2   1 
ATOM   522  N  N     . GLU A 1 99  ? 17.290  -29.731 -17.290 1.00 27.64 ? 78  GLU A N     1 
ATOM   523  C  CA    . GLU A 1 99  ? 16.740  -30.685 -18.271 1.00 31.04 ? 78  GLU A CA    1 
ATOM   524  C  C     . GLU A 1 99  ? 15.235  -30.456 -18.316 1.00 27.25 ? 78  GLU A C     1 
ATOM   525  O  O     . GLU A 1 99  ? 14.696  -29.926 -17.354 1.00 27.69 ? 78  GLU A O     1 
ATOM   526  C  CB    . GLU A 1 99  ? 17.015  -32.128 -17.857 1.00 33.92 ? 78  GLU A CB    1 
ATOM   527  C  CG    . GLU A 1 99  ? 18.399  -32.347 -17.281 1.00 40.78 ? 78  GLU A CG    1 
ATOM   528  C  CD    . GLU A 1 99  ? 19.402  -32.937 -18.245 1.00 45.81 ? 78  GLU A CD    1 
ATOM   529  O  OE1   . GLU A 1 99  ? 19.404  -32.512 -19.430 1.00 51.75 ? 78  GLU A OE1   1 
ATOM   530  O  OE2   . GLU A 1 99  ? 20.167  -33.822 -17.807 1.00 49.14 ? 78  GLU A OE2   1 
ATOM   531  N  N     . THR A 1 100 ? 14.622  -30.837 -19.419 1.00 25.49 ? 79  THR A N     1 
ATOM   532  C  CA    . THR A 1 100 ? 13.181  -30.711 -19.723 1.00 23.22 ? 79  THR A CA    1 
ATOM   533  C  C     . THR A 1 100 ? 12.650  -32.138 -19.851 1.00 23.12 ? 79  THR A C     1 
ATOM   534  O  O     . THR A 1 100 ? 13.484  -33.042 -20.043 1.00 23.21 ? 79  THR A O     1 
ATOM   535  C  CB    . THR A 1 100 ? 13.002  -29.910 -21.019 1.00 23.77 ? 79  THR A CB    1 
ATOM   536  O  OG1   . THR A 1 100 ? 13.451  -30.731 -22.107 1.00 22.06 ? 79  THR A OG1   1 
ATOM   537  C  CG2   . THR A 1 100 ? 13.775  -28.608 -21.000 1.00 23.50 ? 79  THR A CG2   1 
ATOM   538  N  N     . TYR A 1 101 ? 11.340  -32.334 -19.696 1.00 22.94 ? 80  TYR A N     1 
ATOM   539  C  CA    . TYR A 1 101 ? 10.629  -33.591 -20.039 1.00 21.69 ? 80  TYR A CA    1 
ATOM   540  C  C     . TYR A 1 101 ? 9.333   -33.145 -20.681 1.00 19.57 ? 80  TYR A C     1 
ATOM   541  O  O     . TYR A 1 101 ? 8.927   -32.027 -20.439 1.00 18.60 ? 80  TYR A O     1 
ATOM   542  C  CB    . TYR A 1 101 ? 10.423  -34.537 -18.846 1.00 22.10 ? 80  TYR A CB    1 
ATOM   543  C  CG    . TYR A 1 101 ? 9.626   -34.003 -17.681 1.00 23.90 ? 80  TYR A CG    1 
ATOM   544  C  CD1   . TYR A 1 101 ? 10.224  -33.162 -16.762 1.00 22.70 ? 80  TYR A CD1   1 
ATOM   545  C  CD2   . TYR A 1 101 ? 8.297   -34.353 -17.456 1.00 24.31 ? 80  TYR A CD2   1 
ATOM   546  C  CE1   . TYR A 1 101 ? 9.531   -32.638 -15.692 1.00 21.11 ? 80  TYR A CE1   1 
ATOM   547  C  CE2   . TYR A 1 101 ? 7.598   -33.847 -16.363 1.00 23.92 ? 80  TYR A CE2   1 
ATOM   548  C  CZ    . TYR A 1 101 ? 8.225   -32.987 -15.477 1.00 22.55 ? 80  TYR A CZ    1 
ATOM   549  O  OH    . TYR A 1 101 ? 7.625   -32.468 -14.358 1.00 22.93 ? 80  TYR A OH    1 
ATOM   550  N  N     . PRO A 1 102 ? 8.760   -33.933 -21.610 1.00 19.48 ? 81  PRO A N     1 
ATOM   551  C  CA    . PRO A 1 102 ? 7.491   -33.587 -22.233 1.00 21.48 ? 81  PRO A CA    1 
ATOM   552  C  C     . PRO A 1 102 ? 6.289   -33.755 -21.304 1.00 21.10 ? 81  PRO A C     1 
ATOM   553  O  O     . PRO A 1 102 ? 6.273   -34.695 -20.539 1.00 22.18 ? 81  PRO A O     1 
ATOM   554  C  CB    . PRO A 1 102 ? 7.329   -34.607 -23.388 1.00 21.79 ? 81  PRO A CB    1 
ATOM   555  C  CG    . PRO A 1 102 ? 8.188   -35.802 -22.947 1.00 22.72 ? 81  PRO A CG    1 
ATOM   556  C  CD    . PRO A 1 102 ? 9.346   -35.165 -22.181 1.00 22.18 ? 81  PRO A CD    1 
ATOM   557  N  N     . GLN A 1 103 ? 5.288   -32.893 -21.475 1.00 22.14 ? 82  GLN A N     1 
ATOM   558  C  CA    . GLN A 1 103 ? 3.919   -33.137 -20.969 1.00 24.07 ? 82  GLN A CA    1 
ATOM   559  C  C     . GLN A 1 103 ? 3.381   -34.384 -21.676 1.00 26.52 ? 82  GLN A C     1 
ATOM   560  O  O     . GLN A 1 103 ? 3.329   -34.407 -22.907 1.00 24.22 ? 82  GLN A O     1 
ATOM   561  C  CB    . GLN A 1 103 ? 3.028   -31.911 -21.189 1.00 23.81 ? 82  GLN A CB    1 
ATOM   562  C  CG    . GLN A 1 103 ? 1.586   -32.130 -20.759 1.00 23.97 ? 82  GLN A CG    1 
ATOM   563  C  CD    . GLN A 1 103 ? 1.487   -32.374 -19.279 1.00 23.67 ? 82  GLN A CD    1 
ATOM   564  O  OE1   . GLN A 1 103 ? 1.980   -31.590 -18.495 1.00 28.12 ? 82  GLN A OE1   1 
ATOM   565  N  NE2   . GLN A 1 103 ? 0.858   -33.458 -18.871 1.00 23.36 ? 82  GLN A NE2   1 
ATOM   566  N  N     . PRO A 1 104 ? 2.954   -35.440 -20.923 1.00 26.91 ? 83  PRO A N     1 
ATOM   567  C  CA    . PRO A 1 104 ? 2.366   -36.631 -21.526 1.00 25.73 ? 83  PRO A CA    1 
ATOM   568  C  C     . PRO A 1 104 ? 1.137   -36.290 -22.390 1.00 29.74 ? 83  PRO A C     1 
ATOM   569  O  O     . PRO A 1 104 ? 0.375   -35.406 -22.059 1.00 32.13 ? 83  PRO A O     1 
ATOM   570  C  CB    . PRO A 1 104 ? 2.014   -37.552 -20.339 1.00 25.06 ? 83  PRO A CB    1 
ATOM   571  C  CG    . PRO A 1 104 ? 2.836   -37.049 -19.190 1.00 25.05 ? 83  PRO A CG    1 
ATOM   572  C  CD    . PRO A 1 104 ? 3.051   -35.563 -19.457 1.00 25.49 ? 83  PRO A CD    1 
ATOM   573  N  N     . THR A 1 105 ? 0.985   -37.033 -23.484 1.00 33.67 ? 84  THR A N     1 
ATOM   574  C  CA    . THR A 1 105 ? 0.107   -36.730 -24.643 1.00 38.31 ? 84  THR A CA    1 
ATOM   575  C  C     . THR A 1 105 ? -0.859  -37.898 -24.885 1.00 36.21 ? 84  THR A C     1 
ATOM   576  O  O     . THR A 1 105 ? -1.990  -37.620 -25.278 1.00 40.97 ? 84  THR A O     1 
ATOM   577  C  CB    . THR A 1 105 ? 1.000   -36.400 -25.849 1.00 36.50 ? 84  THR A CB    1 
ATOM   578  O  OG1   . THR A 1 105 ? 2.238   -37.083 -25.627 1.00 38.12 ? 84  THR A OG1   1 
ATOM   579  C  CG2   . THR A 1 105 ? 1.253   -34.917 -26.002 1.00 34.71 ? 84  THR A CG2   1 
ATOM   580  N  N     . GLU A 1 106 ? -0.414  -39.130 -24.611 1.00 36.94 ? 85  GLU A N     1 
ATOM   581  C  CA    . GLU A 1 106 ? -1.092  -40.415 -24.911 1.00 35.96 ? 85  GLU A CA    1 
ATOM   582  C  C     . GLU A 1 106 ? -2.236  -40.665 -23.929 1.00 35.90 ? 85  GLU A C     1 
ATOM   583  O  O     . GLU A 1 106 ? -2.192  -40.069 -22.826 1.00 35.18 ? 85  GLU A O     1 
ATOM   584  C  CB    . GLU A 1 106 ? -0.089  -41.567 -24.837 1.00 40.61 ? 85  GLU A CB    1 
ATOM   585  C  CG    . GLU A 1 106 ? 0.625   -41.830 -26.159 1.00 47.56 ? 85  GLU A CG    1 
ATOM   586  C  CD    . GLU A 1 106 ? -0.330  -42.147 -27.302 1.00 53.77 ? 85  GLU A CD    1 
ATOM   587  O  OE1   . GLU A 1 106 ? -1.331  -42.898 -27.047 1.00 51.28 ? 85  GLU A OE1   1 
ATOM   588  O  OE2   . GLU A 1 106 ? -0.109  -41.612 -28.428 1.00 50.50 ? 85  GLU A OE2   1 
ATOM   589  N  N     . GLY A 1 107 ? -3.216  -41.496 -24.346 1.00 30.78 ? 86  GLY A N     1 
ATOM   590  C  CA    . GLY A 1 107 ? -4.416  -41.884 -23.578 1.00 29.20 ? 86  GLY A CA    1 
ATOM   591  C  C     . GLY A 1 107 ? -5.701  -41.256 -24.121 1.00 28.40 ? 86  GLY A C     1 
ATOM   592  O  O     . GLY A 1 107 ? -5.651  -40.194 -24.805 1.00 28.77 ? 86  GLY A O     1 
ATOM   593  N  N     . ASP A 1 108 ? -6.846  -41.858 -23.820 1.00 27.83 ? 87  ASP A N     1 
ATOM   594  C  CA    . ASP A 1 108 ? -8.162  -41.249 -24.161 1.00 32.44 ? 87  ASP A CA    1 
ATOM   595  C  C     . ASP A 1 108 ? -8.439  -40.067 -23.204 1.00 34.70 ? 87  ASP A C     1 
ATOM   596  O  O     . ASP A 1 108 ? -8.288  -40.231 -21.969 1.00 32.58 ? 87  ASP A O     1 
ATOM   597  C  CB    . ASP A 1 108 ? -9.285  -42.285 -24.182 1.00 31.87 ? 87  ASP A CB    1 
ATOM   598  C  CG    . ASP A 1 108 ? -9.220  -43.285 -25.332 1.00 33.15 ? 87  ASP A CG    1 
ATOM   599  O  OD1   . ASP A 1 108 ? -8.508  -43.014 -26.300 1.00 35.40 ? 87  ASP A OD1   1 
ATOM   600  O  OD2   . ASP A 1 108 ? -9.908  -44.328 -25.254 1.00 31.32 ? 87  ASP A OD2   1 
ATOM   601  N  N     . ASP A 1 109 ? -8.740  -38.897 -23.776 1.00 33.85 ? 88  ASP A N     1 
ATOM   602  C  CA    . ASP A 1 109 ? -9.287  -37.723 -23.054 1.00 35.18 ? 88  ASP A CA    1 
ATOM   603  C  C     . ASP A 1 109 ? -10.767 -38.028 -22.764 1.00 37.69 ? 88  ASP A C     1 
ATOM   604  O  O     . ASP A 1 109 ? -11.347 -38.920 -23.443 1.00 38.44 ? 88  ASP A O     1 
ATOM   605  C  CB    . ASP A 1 109 ? -9.094  -36.425 -23.848 1.00 37.99 ? 88  ASP A CB    1 
ATOM   606  C  CG    . ASP A 1 109 ? -7.654  -36.054 -24.217 1.00 42.40 ? 88  ASP A CG    1 
ATOM   607  O  OD1   . ASP A 1 109 ? -6.703  -36.646 -23.647 1.00 39.69 ? 88  ASP A OD1   1 
ATOM   608  O  OD2   . ASP A 1 109 ? -7.483  -35.149 -25.071 1.00 42.13 ? 88  ASP A OD2   1 
ATOM   609  N  N     . VAL A 1 110 ? -11.341 -37.342 -21.773 1.00 35.80 ? 89  VAL A N     1 
ATOM   610  C  CA    . VAL A 1 110 ? -12.774 -37.419 -21.377 1.00 34.32 ? 89  VAL A CA    1 
ATOM   611  C  C     . VAL A 1 110 ? -13.337 -36.008 -21.485 1.00 32.96 ? 89  VAL A C     1 
ATOM   612  O  O     . VAL A 1 110 ? -12.699 -35.091 -20.932 1.00 31.00 ? 89  VAL A O     1 
ATOM   613  C  CB    . VAL A 1 110 ? -12.945 -37.977 -19.949 1.00 38.44 ? 89  VAL A CB    1 
ATOM   614  C  CG1   . VAL A 1 110 ? -14.419 -38.093 -19.535 1.00 43.82 ? 89  VAL A CG1   1 
ATOM   615  C  CG2   . VAL A 1 110 ? -12.245 -39.311 -19.776 1.00 38.94 ? 89  VAL A CG2   1 
ATOM   616  N  N     . VAL A 1 111 ? -14.483 -35.843 -22.158 1.00 34.26 ? 90  VAL A N     1 
ATOM   617  C  CA    . VAL A 1 111 ? -15.241 -34.553 -22.215 1.00 33.08 ? 90  VAL A CA    1 
ATOM   618  C  C     . VAL A 1 111 ? -16.598 -34.812 -21.572 1.00 30.96 ? 90  VAL A C     1 
ATOM   619  O  O     . VAL A 1 111 ? -17.117 -35.879 -21.811 1.00 27.96 ? 90  VAL A O     1 
ATOM   620  C  CB    . VAL A 1 111 ? -15.388 -34.035 -23.658 1.00 36.97 ? 90  VAL A CB    1 
ATOM   621  C  CG1   . VAL A 1 111 ? -15.946 -32.617 -23.738 1.00 34.21 ? 90  VAL A CG1   1 
ATOM   622  C  CG2   . VAL A 1 111 ? -14.070 -34.134 -24.393 1.00 37.87 ? 90  VAL A CG2   1 
ATOM   623  N  N     . LEU A 1 112 ? -17.088 -33.857 -20.770 1.00 35.76 ? 91  LEU A N     1 
ATOM   624  C  CA    . LEU A 1 112 ? -18.376 -33.885 -20.023 1.00 37.18 ? 91  LEU A CA    1 
ATOM   625  C  C     . LEU A 1 112 ? -19.097 -32.526 -20.144 1.00 43.23 ? 91  LEU A C     1 
ATOM   626  O  O     . LEU A 1 112 ? -18.548 -31.497 -19.635 1.00 35.67 ? 91  LEU A O     1 
ATOM   627  C  CB    . LEU A 1 112 ? -18.096 -34.211 -18.553 1.00 35.71 ? 91  LEU A CB    1 
ATOM   628  C  CG    . LEU A 1 112 ? -19.335 -34.425 -17.678 1.00 37.55 ? 91  LEU A CG    1 
ATOM   629  C  CD1   . LEU A 1 112 ? -20.124 -35.659 -18.114 1.00 36.70 ? 91  LEU A CD1   1 
ATOM   630  C  CD2   . LEU A 1 112 ? -18.956 -34.556 -16.210 1.00 39.06 ? 91  LEU A CD2   1 
ATOM   631  N  N     . PHE A 1 113 ? -20.301 -32.539 -20.751 1.00 47.40 ? 92  PHE A N     1 
ATOM   632  C  CA    . PHE A 1 113 ? -21.259 -31.401 -20.857 1.00 49.96 ? 92  PHE A CA    1 
ATOM   633  C  C     . PHE A 1 113 ? -22.504 -31.653 -19.991 1.00 49.88 ? 92  PHE A C     1 
ATOM   634  O  O     . PHE A 1 113 ? -23.092 -32.750 -20.096 1.00 53.13 ? 92  PHE A O     1 
ATOM   635  C  CB    . PHE A 1 113 ? -21.705 -31.205 -22.309 1.00 49.32 ? 92  PHE A CB    1 
ATOM   636  C  CG    . PHE A 1 113 ? -20.595 -30.925 -23.287 1.00 50.98 ? 92  PHE A CG    1 
ATOM   637  C  CD1   . PHE A 1 113 ? -20.019 -29.667 -23.359 1.00 50.49 ? 92  PHE A CD1   1 
ATOM   638  C  CD2   . PHE A 1 113 ? -20.137 -31.915 -24.150 1.00 55.81 ? 92  PHE A CD2   1 
ATOM   639  C  CE1   . PHE A 1 113 ? -19.000 -29.414 -24.264 1.00 50.79 ? 92  PHE A CE1   1 
ATOM   640  C  CE2   . PHE A 1 113 ? -19.134 -31.651 -25.071 1.00 49.13 ? 92  PHE A CE2   1 
ATOM   641  C  CZ    . PHE A 1 113 ? -18.569 -30.403 -25.119 1.00 47.23 ? 92  PHE A CZ    1 
ATOM   642  N  N     . GLY A 1 114 ? -22.887 -30.663 -19.174 1.00 50.76 ? 93  GLY A N     1 
ATOM   643  C  CA    . GLY A 1 114 ? -24.158 -30.613 -18.420 1.00 48.27 ? 93  GLY A CA    1 
ATOM   644  C  C     . GLY A 1 114 ? -24.370 -31.848 -17.565 1.00 51.46 ? 93  GLY A C     1 
ATOM   645  O  O     . GLY A 1 114 ? -23.380 -32.414 -17.055 1.00 51.12 ? 93  GLY A O     1 
ATOM   646  N  N     . ASP A 1 115 ? -25.625 -32.275 -17.430 1.00 55.97 ? 94  ASP A N     1 
ATOM   647  C  CA    . ASP A 1 115 ? -26.005 -33.528 -16.728 1.00 57.90 ? 94  ASP A CA    1 
ATOM   648  C  C     . ASP A 1 115 ? -25.994 -34.668 -17.750 1.00 60.03 ? 94  ASP A C     1 
ATOM   649  O  O     . ASP A 1 115 ? -26.799 -35.608 -17.583 1.00 58.76 ? 94  ASP A O     1 
ATOM   650  C  CB    . ASP A 1 115 ? -27.360 -33.378 -16.032 1.00 61.46 ? 94  ASP A CB    1 
ATOM   651  C  CG    . ASP A 1 115 ? -27.432 -32.153 -15.131 1.00 65.89 ? 94  ASP A CG    1 
ATOM   652  O  OD1   . ASP A 1 115 ? -26.850 -32.212 -14.031 1.00 61.22 ? 94  ASP A OD1   1 
ATOM   653  O  OD2   . ASP A 1 115 ? -28.037 -31.131 -15.559 1.00 63.48 ? 94  ASP A OD2   1 
ATOM   654  N  N     . GLY A 1 116 ? -25.129 -34.563 -18.774 1.00 57.37 ? 95  GLY A N     1 
ATOM   655  C  CA    . GLY A 1 116 ? -24.765 -35.653 -19.698 1.00 59.46 ? 95  GLY A CA    1 
ATOM   656  C  C     . GLY A 1 116 ? -23.788 -36.631 -19.057 1.00 62.23 ? 95  GLY A C     1 
ATOM   657  O  O     . GLY A 1 116 ? -23.378 -36.409 -17.896 1.00 62.19 ? 95  GLY A O     1 
ATOM   658  N  N     . GLU A 1 117 ? -23.430 -37.693 -19.780 1.00 65.00 ? 96  GLU A N     1 
ATOM   659  C  CA    . GLU A 1 117 ? -22.463 -38.727 -19.324 1.00 60.42 ? 96  GLU A CA    1 
ATOM   660  C  C     . GLU A 1 117 ? -21.087 -38.328 -19.843 1.00 56.23 ? 96  GLU A C     1 
ATOM   661  O  O     . GLU A 1 117 ? -20.993 -37.540 -20.785 1.00 54.76 ? 96  GLU A O     1 
ATOM   662  C  CB    . GLU A 1 117 ? -22.863 -40.112 -19.843 1.00 62.69 ? 96  GLU A CB    1 
ATOM   663  C  CG    . GLU A 1 117 ? -24.284 -40.514 -19.494 1.00 64.60 ? 96  GLU A CG    1 
ATOM   664  C  CD    . GLU A 1 117 ? -24.546 -40.617 -18.005 1.00 67.06 ? 96  GLU A CD    1 
ATOM   665  O  OE1   . GLU A 1 117 ? -23.981 -41.535 -17.374 1.00 68.72 ? 96  GLU A OE1   1 
ATOM   666  O  OE2   . GLU A 1 117 ? -25.290 -39.762 -17.476 1.00 71.80 ? 96  GLU A OE2   1 
ATOM   667  N  N     . PRO A 1 118 ? -19.990 -38.880 -19.282 1.00 48.93 ? 97  PRO A N     1 
ATOM   668  C  CA    . PRO A 1 118 ? -18.652 -38.609 -19.809 1.00 51.00 ? 97  PRO A CA    1 
ATOM   669  C  C     . PRO A 1 118 ? -18.394 -39.371 -21.126 1.00 52.93 ? 97  PRO A C     1 
ATOM   670  O  O     . PRO A 1 118 ? -18.872 -40.513 -21.245 1.00 47.83 ? 97  PRO A O     1 
ATOM   671  C  CB    . PRO A 1 118 ? -17.738 -39.062 -18.664 1.00 50.87 ? 97  PRO A CB    1 
ATOM   672  C  CG    . PRO A 1 118 ? -18.525 -40.180 -17.987 1.00 53.28 ? 97  PRO A CG    1 
ATOM   673  C  CD    . PRO A 1 118 ? -19.986 -39.800 -18.137 1.00 50.31 ? 97  PRO A CD    1 
ATOM   674  N  N     . GLN A 1 119 ? -17.700 -38.718 -22.081 1.00 47.81 ? 98  GLN A N     1 
ATOM   675  C  CA    . GLN A 1 119 ? -17.380 -39.233 -23.439 1.00 44.95 ? 98  GLN A CA    1 
ATOM   676  C  C     . GLN A 1 119 ? -15.864 -39.417 -23.563 1.00 44.89 ? 98  GLN A C     1 
ATOM   677  O  O     . GLN A 1 119 ? -15.129 -38.412 -23.433 1.00 34.42 ? 98  GLN A O     1 
ATOM   678  C  CB    . GLN A 1 119 ? -17.848 -38.270 -24.534 1.00 46.62 ? 98  GLN A CB    1 
ATOM   679  C  CG    . GLN A 1 119 ? -19.287 -37.818 -24.382 1.00 52.37 ? 98  GLN A CG    1 
ATOM   680  C  CD    . GLN A 1 119 ? -20.216 -38.992 -24.187 1.00 57.77 ? 98  GLN A CD    1 
ATOM   681  O  OE1   . GLN A 1 119 ? -20.344 -39.845 -25.063 1.00 60.34 ? 98  GLN A OE1   1 
ATOM   682  N  NE2   . GLN A 1 119 ? -20.861 -39.057 -23.027 1.00 54.95 ? 98  GLN A NE2   1 
ATOM   683  N  N     . ARG A 1 120 ? -15.431 -40.648 -23.846 1.00 42.76 ? 99  ARG A N     1 
ATOM   684  C  CA    . ARG A 1 120 ? -14.020 -40.999 -24.124 1.00 44.51 ? 99  ARG A CA    1 
ATOM   685  C  C     . ARG A 1 120 ? -13.716 -40.840 -25.611 1.00 44.38 ? 99  ARG A C     1 
ATOM   686  O  O     . ARG A 1 120 ? -14.332 -41.543 -26.424 1.00 49.40 ? 99  ARG A O     1 
ATOM   687  C  CB    . ARG A 1 120 ? -13.732 -42.447 -23.737 1.00 46.06 ? 99  ARG A CB    1 
ATOM   688  C  CG    . ARG A 1 120 ? -13.996 -42.747 -22.273 1.00 46.69 ? 99  ARG A CG    1 
ATOM   689  C  CD    . ARG A 1 120 ? -13.511 -44.125 -21.883 1.00 47.81 ? 99  ARG A CD    1 
ATOM   690  N  NE    . ARG A 1 120 ? -12.176 -44.384 -22.392 1.00 43.72 ? 99  ARG A NE    1 
ATOM   691  C  CZ    . ARG A 1 120 ? -11.316 -45.228 -21.861 1.00 44.01 ? 99  ARG A CZ    1 
ATOM   692  N  NH1   . ARG A 1 120 ? -11.620 -45.898 -20.763 1.00 43.02 ? 99  ARG A NH1   1 
ATOM   693  N  NH2   . ARG A 1 120 ? -10.129 -45.377 -22.421 1.00 46.63 ? 99  ARG A NH2   1 
ATOM   694  N  N     . ALA A 1 121 ? -12.752 -39.993 -25.934 1.00 44.44 ? 100 ALA A N     1 
ATOM   695  C  CA    . ALA A 1 121 ? -12.191 -39.845 -27.287 1.00 51.37 ? 100 ALA A CA    1 
ATOM   696  C  C     . ALA A 1 121 ? -10.670 -39.872 -27.178 1.00 55.59 ? 100 ALA A C     1 
ATOM   697  O  O     . ALA A 1 121 ? -10.128 -39.642 -26.094 1.00 52.66 ? 100 ALA A O     1 
ATOM   698  C  CB    . ALA A 1 121 ? -12.693 -38.560 -27.904 1.00 53.23 ? 100 ALA A CB    1 
ATOM   699  N  N     . PRO A 1 122 ? -9.944  -40.140 -28.291 1.00 55.70 ? 101 PRO A N     1 
ATOM   700  C  CA    . PRO A 1 122 ? -8.483  -40.171 -28.273 1.00 56.17 ? 101 PRO A CA    1 
ATOM   701  C  C     . PRO A 1 122 ? -7.931  -38.736 -28.211 1.00 53.44 ? 101 PRO A C     1 
ATOM   702  O  O     . PRO A 1 122 ? -6.772  -38.557 -27.894 1.00 51.74 ? 101 PRO A O     1 
ATOM   703  C  CB    . PRO A 1 122 ? -8.083  -40.912 -29.568 1.00 57.92 ? 101 PRO A CB    1 
ATOM   704  C  CG    . PRO A 1 122 ? -9.386  -41.243 -30.300 1.00 58.03 ? 101 PRO A CG    1 
ATOM   705  C  CD    . PRO A 1 122 ? -10.476 -40.425 -29.631 1.00 56.37 ? 101 PRO A CD    1 
ATOM   706  N  N     . ASP A 1 123 ? -8.775  -37.753 -28.534 1.00 56.07 ? 102 ASP A N     1 
ATOM   707  C  CA    . ASP A 1 123 ? -8.523  -36.310 -28.292 1.00 51.80 ? 102 ASP A CA    1 
ATOM   708  C  C     . ASP A 1 123 ? -9.857  -35.598 -28.070 1.00 49.63 ? 102 ASP A C     1 
ATOM   709  O  O     . ASP A 1 123 ? -10.792 -35.879 -28.807 1.00 45.83 ? 102 ASP A O     1 
ATOM   710  C  CB    . ASP A 1 123 ? -7.791  -35.629 -29.443 1.00 49.81 ? 102 ASP A CB    1 
ATOM   711  C  CG    . ASP A 1 123 ? -7.497  -34.175 -29.118 1.00 57.68 ? 102 ASP A CG    1 
ATOM   712  O  OD1   . ASP A 1 123 ? -6.587  -33.924 -28.273 1.00 59.31 ? 102 ASP A OD1   1 
ATOM   713  O  OD2   . ASP A 1 123 ? -8.189  -33.299 -29.679 1.00 51.62 ? 102 ASP A OD2   1 
ATOM   714  N  N     . VAL A 1 124 ? -9.904  -34.703 -27.083 1.00 48.81 ? 103 VAL A N     1 
ATOM   715  C  CA    . VAL A 1 124 ? -11.009 -33.736 -26.806 1.00 47.71 ? 103 VAL A CA    1 
ATOM   716  C  C     . VAL A 1 124 ? -11.765 -33.375 -28.092 1.00 43.66 ? 103 VAL A C     1 
ATOM   717  O  O     . VAL A 1 124 ? -12.993 -33.485 -28.089 1.00 42.28 ? 103 VAL A O     1 
ATOM   718  C  CB    . VAL A 1 124 ? -10.442 -32.485 -26.107 1.00 47.65 ? 103 VAL A CB    1 
ATOM   719  C  CG1   . VAL A 1 124 ? -11.145 -31.198 -26.521 1.00 51.61 ? 103 VAL A CG1   1 
ATOM   720  C  CG2   . VAL A 1 124 ? -10.478 -32.658 -24.597 1.00 46.30 ? 103 VAL A CG2   1 
ATOM   721  N  N     . ALA A 1 125 ? -11.060 -32.936 -29.131 1.00 42.36 ? 104 ALA A N     1 
ATOM   722  C  CA    . ALA A 1 125 ? -11.623 -32.439 -30.414 1.00 44.45 ? 104 ALA A CA    1 
ATOM   723  C  C     . ALA A 1 125 ? -12.722 -33.378 -30.931 1.00 43.76 ? 104 ALA A C     1 
ATOM   724  O  O     . ALA A 1 125 ? -13.763 -32.871 -31.439 1.00 36.03 ? 104 ALA A O     1 
ATOM   725  C  CB    . ALA A 1 125 ? -10.530 -32.275 -31.445 1.00 41.78 ? 104 ALA A CB    1 
ATOM   726  N  N     . LEU A 1 126 ? -12.501 -34.689 -30.779 1.00 47.96 ? 105 LEU A N     1 
ATOM   727  C  CA    . LEU A 1 126 ? -13.328 -35.760 -31.387 1.00 48.12 ? 105 LEU A CA    1 
ATOM   728  C  C     . LEU A 1 126 ? -14.567 -36.041 -30.540 1.00 45.36 ? 105 LEU A C     1 
ATOM   729  O  O     . LEU A 1 126 ? -15.174 -37.098 -30.789 1.00 48.45 ? 105 LEU A O     1 
ATOM   730  C  CB    . LEU A 1 126 ? -12.509 -37.049 -31.540 1.00 53.16 ? 105 LEU A CB    1 
ATOM   731  C  CG    . LEU A 1 126 ? -11.371 -37.073 -32.568 1.00 53.19 ? 105 LEU A CG    1 
ATOM   732  C  CD1   . LEU A 1 126 ? -11.260 -38.463 -33.183 1.00 54.01 ? 105 LEU A CD1   1 
ATOM   733  C  CD2   . LEU A 1 126 ? -11.535 -36.025 -33.659 1.00 55.42 ? 105 LEU A CD2   1 
ATOM   734  N  N     . ALA A 1 127 ? -14.945 -35.169 -29.594 1.00 46.14 ? 106 ALA A N     1 
ATOM   735  C  CA    . ALA A 1 127 ? -16.239 -35.273 -28.860 1.00 48.18 ? 106 ALA A CA    1 
ATOM   736  C  C     . ALA A 1 127 ? -17.226 -34.245 -29.410 1.00 43.70 ? 106 ALA A C     1 
ATOM   737  O  O     . ALA A 1 127 ? -18.322 -34.113 -28.861 1.00 47.11 ? 106 ALA A O     1 
ATOM   738  C  CB    . ALA A 1 127 ? -16.052 -35.093 -27.376 1.00 50.13 ? 106 ALA A CB    1 
ATOM   739  N  N     . PHE A 1 128 ? -16.813 -33.522 -30.446 1.00 43.65 ? 107 PHE A N     1 
ATOM   740  C  CA    . PHE A 1 128 ? -17.618 -32.481 -31.121 1.00 38.87 ? 107 PHE A CA    1 
ATOM   741  C  C     . PHE A 1 128 ? -17.887 -32.962 -32.549 1.00 38.76 ? 107 PHE A C     1 
ATOM   742  O  O     . PHE A 1 128 ? -17.049 -33.730 -33.106 1.00 34.43 ? 107 PHE A O     1 
ATOM   743  C  CB    . PHE A 1 128 ? -16.890 -31.142 -31.037 1.00 39.33 ? 107 PHE A CB    1 
ATOM   744  C  CG    . PHE A 1 128 ? -16.546 -30.722 -29.631 1.00 42.70 ? 107 PHE A CG    1 
ATOM   745  C  CD1   . PHE A 1 128 ? -15.619 -31.435 -28.880 1.00 44.16 ? 107 PHE A CD1   1 
ATOM   746  C  CD2   . PHE A 1 128 ? -17.138 -29.609 -29.057 1.00 43.70 ? 107 PHE A CD2   1 
ATOM   747  C  CE1   . PHE A 1 128 ? -15.312 -31.061 -27.581 1.00 47.79 ? 107 PHE A CE1   1 
ATOM   748  C  CE2   . PHE A 1 128 ? -16.811 -29.222 -27.766 1.00 48.03 ? 107 PHE A CE2   1 
ATOM   749  C  CZ    . PHE A 1 128 ? -15.896 -29.945 -27.029 1.00 47.94 ? 107 PHE A CZ    1 
ATOM   750  N  N     . SER A 1 129 ? -19.027 -32.539 -33.093 1.00 35.76 ? 108 SER A N     1 
ATOM   751  C  CA    . SER A 1 129 ? -19.421 -32.736 -34.507 1.00 39.44 ? 108 SER A CA    1 
ATOM   752  C  C     . SER A 1 129 ? -18.392 -32.080 -35.439 1.00 43.18 ? 108 SER A C     1 
ATOM   753  O  O     . SER A 1 129 ? -17.548 -31.249 -34.960 1.00 37.86 ? 108 SER A O     1 
ATOM   754  C  CB    . SER A 1 129 ? -20.822 -32.207 -34.765 1.00 38.89 ? 108 SER A CB    1 
ATOM   755  O  OG    . SER A 1 129 ? -20.882 -30.793 -34.628 1.00 41.27 ? 108 SER A OG    1 
ATOM   756  N  N     . ASP A 1 130 ? -18.441 -32.496 -36.710 1.00 47.28 ? 109 ASP A N     1 
ATOM   757  C  CA    . ASP A 1 130 ? -17.857 -31.809 -37.898 1.00 48.76 ? 109 ASP A CA    1 
ATOM   758  C  C     . ASP A 1 130 ? -18.191 -30.314 -37.844 1.00 43.97 ? 109 ASP A C     1 
ATOM   759  O  O     . ASP A 1 130 ? -17.251 -29.526 -37.899 1.00 43.11 ? 109 ASP A O     1 
ATOM   760  C  CB    . ASP A 1 130 ? -18.384 -32.417 -39.207 1.00 50.19 ? 109 ASP A CB    1 
ATOM   761  C  CG    . ASP A 1 130 ? -17.648 -33.671 -39.653 1.00 53.14 ? 109 ASP A CG    1 
ATOM   762  O  OD1   . ASP A 1 130 ? -16.495 -33.869 -39.198 1.00 49.15 ? 109 ASP A OD1   1 
ATOM   763  O  OD2   . ASP A 1 130 ? -18.234 -34.444 -40.460 1.00 53.16 ? 109 ASP A OD2   1 
ATOM   764  N  N     . GLU A 1 131 ? -19.479 -29.957 -37.763 1.00 42.97 ? 110 GLU A N     1 
ATOM   765  C  CA    . GLU A 1 131 ? -19.939 -28.548 -37.659 1.00 46.13 ? 110 GLU A CA    1 
ATOM   766  C  C     . GLU A 1 131 ? -19.137 -27.883 -36.533 1.00 40.57 ? 110 GLU A C     1 
ATOM   767  O  O     . GLU A 1 131 ? -18.426 -26.910 -36.808 1.00 39.40 ? 110 GLU A O     1 
ATOM   768  C  CB    . GLU A 1 131 ? -21.458 -28.449 -37.427 1.00 55.75 ? 110 GLU A CB    1 
ATOM   769  C  CG    . GLU A 1 131 ? -22.081 -27.115 -37.872 1.00 60.62 ? 110 GLU A CG    1 
ATOM   770  C  CD    . GLU A 1 131 ? -23.492 -26.762 -37.388 1.00 68.28 ? 110 GLU A CD    1 
ATOM   771  O  OE1   . GLU A 1 131 ? -23.689 -26.585 -36.143 1.00 62.51 ? 110 GLU A OE1   1 
ATOM   772  O  OE2   . GLU A 1 131 ? -24.403 -26.629 -38.257 1.00 70.51 ? 110 GLU A OE2   1 
ATOM   773  N  N     . GLU A 1 132 ? -19.204 -28.440 -35.327 1.00 38.38 ? 111 GLU A N     1 
ATOM   774  C  CA    . GLU A 1 132 ? -18.740 -27.773 -34.082 1.00 39.99 ? 111 GLU A CA    1 
ATOM   775  C  C     . GLU A 1 132 ? -17.253 -27.454 -34.199 1.00 38.29 ? 111 GLU A C     1 
ATOM   776  O  O     . GLU A 1 132 ? -16.860 -26.381 -33.725 1.00 43.81 ? 111 GLU A O     1 
ATOM   777  C  CB    . GLU A 1 132 ? -19.055 -28.631 -32.860 1.00 40.49 ? 111 GLU A CB    1 
ATOM   778  C  CG    . GLU A 1 132 ? -20.492 -28.473 -32.416 1.00 37.64 ? 111 GLU A CG    1 
ATOM   779  C  CD    . GLU A 1 132 ? -20.981 -29.487 -31.396 1.00 41.20 ? 111 GLU A CD    1 
ATOM   780  O  OE1   . GLU A 1 132 ? -22.125 -29.298 -30.908 1.00 41.02 ? 111 GLU A OE1   1 
ATOM   781  O  OE2   . GLU A 1 132 ? -20.242 -30.478 -31.117 1.00 35.61 ? 111 GLU A OE2   1 
ATOM   782  N  N     . LEU A 1 133 ? -16.483 -28.323 -34.851 1.00 37.70 ? 112 LEU A N     1 
ATOM   783  C  CA    . LEU A 1 133 ? -15.003 -28.221 -34.930 1.00 40.78 ? 112 LEU A CA    1 
ATOM   784  C  C     . LEU A 1 133 ? -14.625 -27.105 -35.914 1.00 38.13 ? 112 LEU A C     1 
ATOM   785  O  O     . LEU A 1 133 ? -13.938 -26.153 -35.504 1.00 36.66 ? 112 LEU A O     1 
ATOM   786  C  CB    . LEU A 1 133 ? -14.421 -29.574 -35.359 1.00 44.12 ? 112 LEU A CB    1 
ATOM   787  C  CG    . LEU A 1 133 ? -12.903 -29.679 -35.251 1.00 44.01 ? 112 LEU A CG    1 
ATOM   788  C  CD1   . LEU A 1 133 ? -12.466 -29.430 -33.819 1.00 49.75 ? 112 LEU A CD1   1 
ATOM   789  C  CD2   . LEU A 1 133 ? -12.409 -31.029 -35.733 1.00 45.49 ? 112 LEU A CD2   1 
ATOM   790  N  N     . THR A 1 134 ? -15.081 -27.221 -37.162 1.00 35.81 ? 113 THR A N     1 
ATOM   791  C  CA    . THR A 1 134 ? -15.124 -26.126 -38.165 1.00 34.81 ? 113 THR A CA    1 
ATOM   792  C  C     . THR A 1 134 ? -15.298 -24.765 -37.471 1.00 32.48 ? 113 THR A C     1 
ATOM   793  O  O     . THR A 1 134 ? -14.348 -23.955 -37.515 1.00 38.70 ? 113 THR A O     1 
ATOM   794  C  CB    . THR A 1 134 ? -16.244 -26.379 -39.175 1.00 36.26 ? 113 THR A CB    1 
ATOM   795  O  OG1   . THR A 1 134 ? -16.088 -27.710 -39.674 1.00 34.31 ? 113 THR A OG1   1 
ATOM   796  C  CG2   . THR A 1 134 ? -16.225 -25.377 -40.307 1.00 39.65 ? 113 THR A CG2   1 
ATOM   797  N  N     . ALA A 1 135 ? -16.453 -24.511 -36.862 1.00 31.42 ? 114 ALA A N     1 
ATOM   798  C  CA    . ALA A 1 135 ? -16.808 -23.204 -36.266 1.00 30.10 ? 114 ALA A CA    1 
ATOM   799  C  C     . ALA A 1 135 ? -15.770 -22.806 -35.209 1.00 28.74 ? 114 ALA A C     1 
ATOM   800  O  O     . ALA A 1 135 ? -15.435 -21.617 -35.132 1.00 28.70 ? 114 ALA A O     1 
ATOM   801  C  CB    . ALA A 1 135 ? -18.186 -23.279 -35.693 1.00 28.69 ? 114 ALA A CB    1 
ATOM   802  N  N     . TYR A 1 136 ? -15.264 -23.771 -34.437 1.00 29.07 ? 115 TYR A N     1 
ATOM   803  C  CA    . TYR A 1 136 ? -14.240 -23.545 -33.387 1.00 32.07 ? 115 TYR A CA    1 
ATOM   804  C  C     . TYR A 1 136 ? -12.939 -22.999 -33.996 1.00 32.17 ? 115 TYR A C     1 
ATOM   805  O  O     . TYR A 1 136 ? -12.454 -21.959 -33.513 1.00 32.30 ? 115 TYR A O     1 
ATOM   806  C  CB    . TYR A 1 136 ? -13.902 -24.816 -32.614 1.00 33.20 ? 115 TYR A CB    1 
ATOM   807  C  CG    . TYR A 1 136 ? -12.836 -24.561 -31.583 1.00 33.72 ? 115 TYR A CG    1 
ATOM   808  C  CD1   . TYR A 1 136 ? -11.511 -24.917 -31.815 1.00 34.25 ? 115 TYR A CD1   1 
ATOM   809  C  CD2   . TYR A 1 136 ? -13.144 -23.874 -30.415 1.00 33.74 ? 115 TYR A CD2   1 
ATOM   810  C  CE1   . TYR A 1 136 ? -10.525 -24.634 -30.886 1.00 33.34 ? 115 TYR A CE1   1 
ATOM   811  C  CE2   . TYR A 1 136 ? -12.176 -23.600 -29.467 1.00 33.80 ? 115 TYR A CE2   1 
ATOM   812  C  CZ    . TYR A 1 136 ? -10.865 -23.970 -29.712 1.00 36.31 ? 115 TYR A CZ    1 
ATOM   813  O  OH    . TYR A 1 136 ? -9.934  -23.691 -28.757 1.00 36.36 ? 115 TYR A OH    1 
ATOM   814  N  N     . LEU A 1 137 ? -12.384 -23.714 -34.979 1.00 33.52 ? 116 LEU A N     1 
ATOM   815  C  CA    . LEU A 1 137 ? -11.127 -23.381 -35.701 1.00 35.97 ? 116 LEU A CA    1 
ATOM   816  C  C     . LEU A 1 137 ? -11.314 -22.085 -36.512 1.00 39.08 ? 116 LEU A C     1 
ATOM   817  O  O     . LEU A 1 137 ? -10.297 -21.357 -36.667 1.00 39.29 ? 116 LEU A O     1 
ATOM   818  C  CB    . LEU A 1 137 ? -10.715 -24.545 -36.615 1.00 36.88 ? 116 LEU A CB    1 
ATOM   819  C  CG    . LEU A 1 137 ? -10.455 -25.881 -35.919 1.00 40.44 ? 116 LEU A CG    1 
ATOM   820  C  CD1   . LEU A 1 137 ? -10.296 -27.017 -36.928 1.00 39.48 ? 116 LEU A CD1   1 
ATOM   821  C  CD2   . LEU A 1 137 ? -9.226  -25.792 -35.021 1.00 40.04 ? 116 LEU A CD2   1 
ATOM   822  N  N     . GLU A 1 138 ? -12.536 -21.807 -37.005 1.00 35.73 ? 117 GLU A N     1 
ATOM   823  C  CA    . GLU A 1 138 ? -12.870 -20.549 -37.720 1.00 37.85 ? 117 GLU A CA    1 
ATOM   824  C  C     . GLU A 1 138 ? -13.013 -19.396 -36.710 1.00 36.79 ? 117 GLU A C     1 
ATOM   825  O  O     . GLU A 1 138 ? -12.702 -18.253 -37.070 1.00 35.15 ? 117 GLU A O     1 
ATOM   826  C  CB    . GLU A 1 138 ? -14.128 -20.734 -38.578 1.00 42.69 ? 117 GLU A CB    1 
ATOM   827  C  CG    . GLU A 1 138 ? -13.853 -21.421 -39.911 1.00 46.49 ? 117 GLU A CG    1 
ATOM   828  C  CD    . GLU A 1 138 ? -15.066 -21.892 -40.704 1.00 47.18 ? 117 GLU A CD    1 
ATOM   829  O  OE1   . GLU A 1 138 ? -14.943 -22.882 -41.457 1.00 45.01 ? 117 GLU A OE1   1 
ATOM   830  O  OE2   . GLU A 1 138 ? -16.122 -21.255 -40.594 1.00 49.57 ? 117 GLU A OE2   1 
ATOM   831  N  N     . LEU A 1 139 ? -13.450 -19.667 -35.479 1.00 33.39 ? 118 LEU A N     1 
ATOM   832  C  CA    . LEU A 1 139 ? -13.543 -18.619 -34.425 1.00 34.22 ? 118 LEU A CA    1 
ATOM   833  C  C     . LEU A 1 139 ? -12.118 -18.251 -33.968 1.00 31.70 ? 118 LEU A C     1 
ATOM   834  O  O     . LEU A 1 139 ? -11.843 -17.047 -33.797 1.00 33.03 ? 118 LEU A O     1 
ATOM   835  C  CB    . LEU A 1 139 ? -14.424 -19.165 -33.293 1.00 34.48 ? 118 LEU A CB    1 
ATOM   836  C  CG    . LEU A 1 139 ? -14.607 -18.280 -32.067 1.00 33.69 ? 118 LEU A CG    1 
ATOM   837  C  CD1   . LEU A 1 139 ? -15.048 -16.895 -32.457 1.00 33.97 ? 118 LEU A CD1   1 
ATOM   838  C  CD2   . LEU A 1 139 ? -15.625 -18.889 -31.120 1.00 35.02 ? 118 LEU A CD2   1 
ATOM   839  N  N     . ALA A 1 140 ? -11.226 -19.239 -33.834 1.00 29.67 ? 119 ALA A N     1 
ATOM   840  C  CA    . ALA A 1 140 ? -9.794  -19.048 -33.475 1.00 32.96 ? 119 ALA A CA    1 
ATOM   841  C  C     . ALA A 1 140 ? -9.079  -18.294 -34.605 1.00 34.32 ? 119 ALA A C     1 
ATOM   842  O  O     . ALA A 1 140 ? -8.434  -17.252 -34.322 1.00 36.64 ? 119 ALA A O     1 
ATOM   843  C  CB    . ALA A 1 140 ? -9.114  -20.373 -33.200 1.00 31.71 ? 119 ALA A CB    1 
ATOM   844  N  N     . GLY A 1 141 ? -9.226  -18.785 -35.840 1.00 33.91 ? 120 GLY A N     1 
ATOM   845  C  CA    . GLY A 1 141 ? -8.716  -18.144 -37.067 1.00 32.81 ? 120 GLY A CA    1 
ATOM   846  C  C     . GLY A 1 141 ? -9.140  -16.686 -37.172 1.00 31.14 ? 120 GLY A C     1 
ATOM   847  O  O     . GLY A 1 141 ? -8.361  -15.889 -37.717 1.00 29.36 ? 120 GLY A O     1 
ATOM   848  N  N     . ALA A 1 142 ? -10.342 -16.361 -36.690 1.00 29.00 ? 121 ALA A N     1 
ATOM   849  C  CA    . ALA A 1 142 ? -10.925 -15.000 -36.697 1.00 31.07 ? 121 ALA A CA    1 
ATOM   850  C  C     . ALA A 1 142 ? -10.232 -14.094 -35.668 1.00 27.83 ? 121 ALA A C     1 
ATOM   851  O  O     . ALA A 1 142 ? -10.003 -12.919 -35.969 1.00 28.25 ? 121 ALA A O     1 
ATOM   852  C  CB    . ALA A 1 142 ? -12.407 -15.070 -36.416 1.00 32.29 ? 121 ALA A CB    1 
ATOM   853  N  N     . LEU A 1 143 ? -9.984  -14.595 -34.469 1.00 27.45 ? 122 LEU A N     1 
ATOM   854  C  CA    . LEU A 1 143 ? -9.356  -13.794 -33.387 1.00 26.78 ? 122 LEU A CA    1 
ATOM   855  C  C     . LEU A 1 143 ? -7.894  -13.535 -33.773 1.00 25.98 ? 122 LEU A C     1 
ATOM   856  O  O     . LEU A 1 143 ? -7.381  -12.469 -33.402 1.00 24.23 ? 122 LEU A O     1 
ATOM   857  C  CB    . LEU A 1 143 ? -9.483  -14.551 -32.060 1.00 28.48 ? 122 LEU A CB    1 
ATOM   858  C  CG    . LEU A 1 143 ? -8.839  -13.883 -30.847 1.00 30.42 ? 122 LEU A CG    1 
ATOM   859  C  CD1   . LEU A 1 143 ? -9.559  -12.588 -30.480 1.00 30.69 ? 122 LEU A CD1   1 
ATOM   860  C  CD2   . LEU A 1 143 ? -8.813  -14.835 -29.663 1.00 31.47 ? 122 LEU A CD2   1 
ATOM   861  N  N     . GLU A 1 144 ? -7.268  -14.474 -34.497 1.00 24.60 ? 123 GLU A N     1 
ATOM   862  C  CA    . GLU A 1 144 ? -5.865  -14.376 -34.956 1.00 26.91 ? 123 GLU A CA    1 
ATOM   863  C  C     . GLU A 1 144 ? -5.821  -13.236 -35.961 1.00 27.68 ? 123 GLU A C     1 
ATOM   864  O  O     . GLU A 1 144 ? -4.827  -12.519 -35.978 1.00 26.82 ? 123 GLU A O     1 
ATOM   865  C  CB    . GLU A 1 144 ? -5.339  -15.701 -35.551 1.00 28.53 ? 123 GLU A CB    1 
ATOM   866  C  CG    . GLU A 1 144 ? -4.942  -16.718 -34.495 1.00 29.14 ? 123 GLU A CG    1 
ATOM   867  C  CD    . GLU A 1 144 ? -4.600  -18.120 -34.968 1.00 31.04 ? 123 GLU A CD    1 
ATOM   868  O  OE1   . GLU A 1 144 ? -4.488  -19.008 -34.106 1.00 30.80 ? 123 GLU A OE1   1 
ATOM   869  O  OE2   . GLU A 1 144 ? -4.469  -18.339 -36.189 1.00 38.72 ? 123 GLU A OE2   1 
ATOM   870  N  N     . ALA A 1 145 ? -6.877  -13.081 -36.762 1.00 29.16 ? 124 ALA A N     1 
ATOM   871  C  CA    . ALA A 1 145 ? -6.935  -12.061 -37.831 1.00 29.43 ? 124 ALA A CA    1 
ATOM   872  C  C     . ALA A 1 145 ? -6.786  -10.708 -37.151 1.00 26.97 ? 124 ALA A C     1 
ATOM   873  O  O     . ALA A 1 145 ? -5.888  -9.945  -37.536 1.00 25.42 ? 124 ALA A O     1 
ATOM   874  C  CB    . ALA A 1 145 ? -8.215  -12.155 -38.634 1.00 30.06 ? 124 ALA A CB    1 
ATOM   875  N  N     . ILE A 1 146 ? -7.604  -10.484 -36.131 1.00 26.06 ? 125 ILE A N     1 
ATOM   876  C  CA    . ILE A 1 146 ? -7.567  -9.239  -35.304 1.00 27.61 ? 125 ILE A CA    1 
ATOM   877  C  C     . ILE A 1 146 ? -6.176  -9.097  -34.670 1.00 25.39 ? 125 ILE A C     1 
ATOM   878  O  O     . ILE A 1 146 ? -5.571  -8.024  -34.817 1.00 24.81 ? 125 ILE A O     1 
ATOM   879  C  CB    . ILE A 1 146 ? -8.733  -9.260  -34.282 1.00 29.58 ? 125 ILE A CB    1 
ATOM   880  C  CG1   . ILE A 1 146 ? -10.084 -9.203  -35.002 1.00 31.70 ? 125 ILE A CG1   1 
ATOM   881  C  CG2   . ILE A 1 146 ? -8.604  -8.153  -33.237 1.00 28.34 ? 125 ILE A CG2   1 
ATOM   882  C  CD1   . ILE A 1 146 ? -11.227 -9.897  -34.294 1.00 32.22 ? 125 ILE A CD1   1 
ATOM   883  N  N     . ALA A 1 147 ? -5.656  -10.160 -34.031 1.00 27.25 ? 126 ALA A N     1 
ATOM   884  C  CA    . ALA A 1 147 ? -4.347  -10.182 -33.313 1.00 26.53 ? 126 ALA A CA    1 
ATOM   885  C  C     . ALA A 1 147 ? -3.221  -9.672  -34.231 1.00 26.96 ? 126 ALA A C     1 
ATOM   886  O  O     . ALA A 1 147 ? -2.511  -8.730  -33.815 1.00 26.40 ? 126 ALA A O     1 
ATOM   887  C  CB    . ALA A 1 147 ? -4.040  -11.568 -32.804 1.00 23.78 ? 126 ALA A CB    1 
ATOM   888  N  N     . GLU A 1 148 ? -3.084  -10.243 -35.434 1.00 27.88 ? 127 GLU A N     1 
ATOM   889  C  CA    . GLU A 1 148 ? -1.996  -9.906  -36.402 1.00 32.95 ? 127 GLU A CA    1 
ATOM   890  C  C     . GLU A 1 148 ? -1.939  -8.389  -36.667 1.00 27.17 ? 127 GLU A C     1 
ATOM   891  O  O     . GLU A 1 148 ? -0.844  -7.896  -36.949 1.00 28.24 ? 127 GLU A O     1 
ATOM   892  C  CB    . GLU A 1 148 ? -2.094  -10.689 -37.721 1.00 37.73 ? 127 GLU A CB    1 
ATOM   893  C  CG    . GLU A 1 148 ? -0.767  -10.712 -38.512 1.00 43.36 ? 127 GLU A CG    1 
ATOM   894  C  CD    . GLU A 1 148 ? 0.534   -11.020 -37.742 1.00 48.14 ? 127 GLU A CD    1 
ATOM   895  O  OE1   . GLU A 1 148 ? 1.336   -10.045 -37.428 1.00 45.54 ? 127 GLU A OE1   1 
ATOM   896  O  OE2   . GLU A 1 148 ? 0.780   -12.232 -37.459 1.00 41.35 ? 127 GLU A OE2   1 
ATOM   897  N  N     . LYS A 1 149 ? -3.017  -7.648  -36.461 1.00 25.23 ? 128 LYS A N     1 
ATOM   898  C  CA    . LYS A 1 149 ? -3.040  -6.186  -36.730 1.00 26.80 ? 128 LYS A CA    1 
ATOM   899  C  C     . LYS A 1 149 ? -2.725  -5.369  -35.476 1.00 24.70 ? 128 LYS A C     1 
ATOM   900  O  O     . LYS A 1 149 ? -2.791  -4.148  -35.591 1.00 24.74 ? 128 LYS A O     1 
ATOM   901  C  CB    . LYS A 1 149 ? -4.402  -5.762  -37.293 1.00 29.35 ? 128 LYS A CB    1 
ATOM   902  C  CG    . LYS A 1 149 ? -4.827  -6.561  -38.520 1.00 31.59 ? 128 LYS A CG    1 
ATOM   903  C  CD    . LYS A 1 149 ? -5.877  -5.894  -39.358 1.00 36.20 ? 128 LYS A CD    1 
ATOM   904  C  CE    . LYS A 1 149 ? -6.383  -6.797  -40.473 1.00 42.23 ? 128 LYS A CE    1 
ATOM   905  N  NZ    . LYS A 1 149 ? -7.869  -6.777  -40.567 1.00 42.71 ? 128 LYS A NZ    1 
ATOM   906  N  N     . VAL A 1 150 ? -2.410  -6.000  -34.338 1.00 26.22 ? 129 VAL A N     1 
ATOM   907  C  CA    . VAL A 1 150 ? -2.212  -5.304  -33.028 1.00 24.48 ? 129 VAL A CA    1 
ATOM   908  C  C     . VAL A 1 150 ? -0.716  -5.210  -32.772 1.00 24.04 ? 129 VAL A C     1 
ATOM   909  O  O     . VAL A 1 150 ? -0.059  -6.235  -32.594 1.00 27.76 ? 129 VAL A O     1 
ATOM   910  C  CB    . VAL A 1 150 ? -2.930  -6.018  -31.865 1.00 24.56 ? 129 VAL A CB    1 
ATOM   911  C  CG1   . VAL A 1 150 ? -2.570  -5.386  -30.523 1.00 25.63 ? 129 VAL A CG1   1 
ATOM   912  C  CG2   . VAL A 1 150 ? -4.433  -6.025  -32.068 1.00 23.04 ? 129 VAL A CG2   1 
ATOM   913  N  N     . PRO A 1 151 ? -0.124  -4.004  -32.744 1.00 22.53 ? 130 PRO A N     1 
ATOM   914  C  CA    . PRO A 1 151 ? 1.315   -3.868  -32.514 1.00 22.11 ? 130 PRO A CA    1 
ATOM   915  C  C     . PRO A 1 151 ? 1.693   -4.344  -31.106 1.00 22.26 ? 130 PRO A C     1 
ATOM   916  O  O     . PRO A 1 151 ? 1.097   -3.908  -30.167 1.00 22.75 ? 130 PRO A O     1 
ATOM   917  C  CB    . PRO A 1 151 ? 1.573   -2.373  -32.703 1.00 23.43 ? 130 PRO A CB    1 
ATOM   918  C  CG    . PRO A 1 151 ? 0.375   -1.899  -33.507 1.00 24.80 ? 130 PRO A CG    1 
ATOM   919  C  CD    . PRO A 1 151 ? -0.785  -2.713  -32.965 1.00 24.08 ? 130 PRO A CD    1 
ATOM   920  N  N     . LEU A 1 152 ? 2.664   -5.252  -30.993 1.00 23.82 ? 131 LEU A N     1 
ATOM   921  C  CA    . LEU A 1 152 ? 3.049   -5.875  -29.692 1.00 26.39 ? 131 LEU A CA    1 
ATOM   922  C  C     . LEU A 1 152 ? 3.566   -4.812  -28.716 1.00 25.91 ? 131 LEU A C     1 
ATOM   923  O  O     . LEU A 1 152 ? 3.361   -4.988  -27.505 1.00 27.62 ? 131 LEU A O     1 
ATOM   924  C  CB    . LEU A 1 152 ? 4.089   -6.969  -29.940 1.00 27.20 ? 131 LEU A CB    1 
ATOM   925  C  CG    . LEU A 1 152 ? 3.565   -8.188  -30.696 1.00 27.78 ? 131 LEU A CG    1 
ATOM   926  C  CD1   . LEU A 1 152 ? 4.662   -9.239  -30.846 1.00 30.29 ? 131 LEU A CD1   1 
ATOM   927  C  CD2   . LEU A 1 152 ? 2.355   -8.769  -29.996 1.00 25.15 ? 131 LEU A CD2   1 
ATOM   928  N  N     . ASP A 1 153 ? 4.159   -3.729  -29.220 1.00 25.38 ? 132 ASP A N     1 
ATOM   929  C  CA    . ASP A 1 153 ? 4.787   -2.691  -28.369 1.00 27.64 ? 132 ASP A CA    1 
ATOM   930  C  C     . ASP A 1 153 ? 3.783   -1.581  -28.047 1.00 27.02 ? 132 ASP A C     1 
ATOM   931  O  O     . ASP A 1 153 ? 4.128   -0.753  -27.205 1.00 29.34 ? 132 ASP A O     1 
ATOM   932  C  CB    . ASP A 1 153 ? 6.077   -2.155  -28.995 1.00 29.68 ? 132 ASP A CB    1 
ATOM   933  C  CG    . ASP A 1 153 ? 5.901   -1.401  -30.297 1.00 31.59 ? 132 ASP A CG    1 
ATOM   934  O  OD1   . ASP A 1 153 ? 4.774   -1.379  -30.827 1.00 34.18 ? 132 ASP A OD1   1 
ATOM   935  O  OD2   . ASP A 1 153 ? 6.894   -0.819  -30.752 1.00 36.98 ? 132 ASP A OD2   1 
ATOM   936  N  N     . ALA A 1 154 ? 2.611   -1.557  -28.678 1.00 24.57 ? 133 ALA A N     1 
ATOM   937  C  CA    . ALA A 1 154 ? 1.693   -0.402  -28.649 1.00 23.08 ? 133 ALA A CA    1 
ATOM   938  C  C     . ALA A 1 154 ? 0.321   -0.835  -29.130 1.00 25.11 ? 133 ALA A C     1 
ATOM   939  O  O     . ALA A 1 154 ? -0.128  -0.427  -30.198 1.00 29.85 ? 133 ALA A O     1 
ATOM   940  C  CB    . ALA A 1 154 ? 2.229   0.689   -29.522 1.00 25.29 ? 133 ALA A CB    1 
ATOM   941  N  N     . PRO A 1 155 ? -0.374  -1.699  -28.367 1.00 25.10 ? 134 PRO A N     1 
ATOM   942  C  CA    . PRO A 1 155 ? -1.744  -2.105  -28.690 1.00 24.98 ? 134 PRO A CA    1 
ATOM   943  C  C     . PRO A 1 155 ? -2.702  -0.957  -29.035 1.00 23.87 ? 134 PRO A C     1 
ATOM   944  O  O     . PRO A 1 155 ? -3.572  -1.143  -29.846 1.00 24.56 ? 134 PRO A O     1 
ATOM   945  C  CB    . PRO A 1 155 ? -2.225  -2.709  -27.366 1.00 24.61 ? 134 PRO A CB    1 
ATOM   946  C  CG    . PRO A 1 155 ? -0.980  -3.255  -26.728 1.00 25.78 ? 134 PRO A CG    1 
ATOM   947  C  CD    . PRO A 1 155 ? 0.142   -2.342  -27.149 1.00 25.05 ? 134 PRO A CD    1 
ATOM   948  N  N     . TRP A 1 156 ? -2.531  0.171   -28.354 1.00 23.03 ? 135 TRP A N     1 
ATOM   949  C  CA    . TRP A 1 156 ? -3.298  1.417   -28.538 1.00 24.02 ? 135 TRP A CA    1 
ATOM   950  C  C     . TRP A 1 156 ? -3.186  1.921   -29.988 1.00 24.95 ? 135 TRP A C     1 
ATOM   951  O  O     . TRP A 1 156 ? -4.038  2.729   -30.380 1.00 24.92 ? 135 TRP A O     1 
ATOM   952  C  CB    . TRP A 1 156 ? -2.849  2.463   -27.491 1.00 24.96 ? 135 TRP A CB    1 
ATOM   953  C  CG    . TRP A 1 156 ? -1.401  2.864   -27.463 1.00 26.37 ? 135 TRP A CG    1 
ATOM   954  C  CD1   . TRP A 1 156 ? -0.825  3.916   -28.125 1.00 26.63 ? 135 TRP A CD1   1 
ATOM   955  C  CD2   . TRP A 1 156 ? -0.356  2.294   -26.644 1.00 25.60 ? 135 TRP A CD2   1 
ATOM   956  N  NE1   . TRP A 1 156 ? 0.509   4.001   -27.817 1.00 24.75 ? 135 TRP A NE1   1 
ATOM   957  C  CE2   . TRP A 1 156 ? 0.821   3.017   -26.912 1.00 24.42 ? 135 TRP A CE2   1 
ATOM   958  C  CE3   . TRP A 1 156 ? -0.290  1.228   -25.733 1.00 26.90 ? 135 TRP A CE3   1 
ATOM   959  C  CZ2   . TRP A 1 156 ? 2.038   2.692   -26.307 1.00 25.56 ? 135 TRP A CZ2   1 
ATOM   960  C  CZ3   . TRP A 1 156 ? 0.917   0.914   -25.139 1.00 26.73 ? 135 TRP A CZ3   1 
ATOM   961  C  CH2   . TRP A 1 156 ? 2.064   1.644   -25.416 1.00 23.75 ? 135 TRP A CH2   1 
ATOM   962  N  N     . LEU A 1 157 ? -2.189  1.475   -30.757 1.00 28.46 ? 136 LEU A N     1 
ATOM   963  C  CA    . LEU A 1 157 ? -1.896  2.006   -32.121 1.00 31.10 ? 136 LEU A CA    1 
ATOM   964  C  C     . LEU A 1 157 ? -2.431  1.056   -33.199 1.00 30.46 ? 136 LEU A C     1 
ATOM   965  O  O     . LEU A 1 157 ? -2.244  1.348   -34.364 1.00 31.44 ? 136 LEU A O     1 
ATOM   966  C  CB    . LEU A 1 157 ? -0.386  2.238   -32.292 1.00 32.13 ? 136 LEU A CB    1 
ATOM   967  C  CG    . LEU A 1 157 ? 0.237   3.342   -31.432 1.00 36.81 ? 136 LEU A CG    1 
ATOM   968  C  CD1   . LEU A 1 157 ? 1.666   3.634   -31.885 1.00 37.92 ? 136 LEU A CD1   1 
ATOM   969  C  CD2   . LEU A 1 157 ? -0.587  4.631   -31.442 1.00 35.17 ? 136 LEU A CD2   1 
ATOM   970  N  N     . ALA A 1 158 ? -3.133  -0.020  -32.861 1.00 34.24 ? 137 ALA A N     1 
ATOM   971  C  CA    . ALA A 1 158 ? -3.852  -0.803  -33.893 1.00 32.91 ? 137 ALA A CA    1 
ATOM   972  C  C     . ALA A 1 158 ? -4.774  0.183   -34.610 1.00 32.02 ? 137 ALA A C     1 
ATOM   973  O  O     . ALA A 1 158 ? -5.193  1.163   -34.015 1.00 35.81 ? 137 ALA A O     1 
ATOM   974  C  CB    . ALA A 1 158 ? -4.582  -1.976  -33.264 1.00 31.81 ? 137 ALA A CB    1 
ATOM   975  N  N     . PRO A 1 159 ? -5.047  0.045   -35.921 1.00 34.01 ? 138 PRO A N     1 
ATOM   976  C  CA    . PRO A 1 159 ? -5.990  0.936   -36.602 1.00 32.88 ? 138 PRO A CA    1 
ATOM   977  C  C     . PRO A 1 159 ? -7.427  0.903   -36.056 1.00 31.18 ? 138 PRO A C     1 
ATOM   978  O  O     . PRO A 1 159 ? -8.069  1.930   -36.036 1.00 25.80 ? 138 PRO A O     1 
ATOM   979  C  CB    . PRO A 1 159 ? -5.995  0.420   -38.047 1.00 34.01 ? 138 PRO A CB    1 
ATOM   980  C  CG    . PRO A 1 159 ? -4.641  -0.241  -38.198 1.00 37.12 ? 138 PRO A CG    1 
ATOM   981  C  CD    . PRO A 1 159 ? -4.372  -0.879  -36.846 1.00 37.48 ? 138 PRO A CD    1 
ATOM   982  N  N     . GLU A 1 160 ? -7.876  -0.262  -35.591 1.00 30.76 ? 139 GLU A N     1 
ATOM   983  C  CA    . GLU A 1 160 ? -9.238  -0.481  -35.047 1.00 31.30 ? 139 GLU A CA    1 
ATOM   984  C  C     . GLU A 1 160 ? -9.258  -0.376  -33.504 1.00 31.93 ? 139 GLU A C     1 
ATOM   985  O  O     . GLU A 1 160 ? -10.218 -0.926  -32.863 1.00 30.02 ? 139 GLU A O     1 
ATOM   986  C  CB    . GLU A 1 160 ? -9.748  -1.833  -35.553 1.00 36.04 ? 139 GLU A CB    1 
ATOM   987  C  CG    . GLU A 1 160 ? -10.573 -1.742  -36.831 1.00 38.48 ? 139 GLU A CG    1 
ATOM   988  C  CD    . GLU A 1 160 ? -11.934 -1.087  -36.667 1.00 40.64 ? 139 GLU A CD    1 
ATOM   989  O  OE1   . GLU A 1 160 ? -12.831 -1.731  -36.063 1.00 42.67 ? 139 GLU A OE1   1 
ATOM   990  O  OE2   . GLU A 1 160 ? -12.103 0.067   -37.157 1.00 49.39 ? 139 GLU A OE2   1 
ATOM   991  N  N     . ALA A 1 161 ? -8.299  0.345   -32.908 1.00 28.35 ? 140 ALA A N     1 
ATOM   992  C  CA    . ALA A 1 161 ? -8.018  0.337   -31.454 1.00 26.66 ? 140 ALA A CA    1 
ATOM   993  C  C     . ALA A 1 161 ? -9.242  0.874   -30.682 1.00 26.10 ? 140 ALA A C     1 
ATOM   994  O  O     . ALA A 1 161 ? -9.657  0.262   -29.695 1.00 24.96 ? 140 ALA A O     1 
ATOM   995  C  CB    . ALA A 1 161 ? -6.762  1.148   -31.182 1.00 26.23 ? 140 ALA A CB    1 
ATOM   996  N  N     . ALA A 1 162 ? -9.810  1.979   -31.133 1.00 25.22 ? 141 ALA A N     1 
ATOM   997  C  CA    . ALA A 1 162 ? -11.072 2.543   -30.618 1.00 29.01 ? 141 ALA A CA    1 
ATOM   998  C  C     . ALA A 1 162 ? -12.126 1.438   -30.472 1.00 28.05 ? 141 ALA A C     1 
ATOM   999  O  O     . ALA A 1 162 ? -12.677 1.240   -29.371 1.00 31.17 ? 141 ALA A O     1 
ATOM   1000 C  CB    . ALA A 1 162 ? -11.544 3.630   -31.562 1.00 33.55 ? 141 ALA A CB    1 
ATOM   1001 N  N     . ALA A 1 163 ? -12.430 0.740   -31.548 1.00 28.68 ? 142 ALA A N     1 
ATOM   1002 C  CA    . ALA A 1 163 ? -13.544 -0.229  -31.563 1.00 31.71 ? 142 ALA A CA    1 
ATOM   1003 C  C     . ALA A 1 163 ? -13.162 -1.387  -30.658 1.00 28.97 ? 142 ALA A C     1 
ATOM   1004 O  O     . ALA A 1 163 ? -14.002 -1.857  -29.893 1.00 32.71 ? 142 ALA A O     1 
ATOM   1005 C  CB    . ALA A 1 163 ? -13.837 -0.705  -32.964 1.00 32.84 ? 142 ALA A CB    1 
ATOM   1006 N  N     . TRP A 1 164 ? -11.921 -1.830  -30.756 1.00 28.53 ? 143 TRP A N     1 
ATOM   1007 C  CA    . TRP A 1 164 ? -11.500 -3.101  -30.113 1.00 28.65 ? 143 TRP A CA    1 
ATOM   1008 C  C     . TRP A 1 164 ? -11.405 -2.934  -28.577 1.00 24.72 ? 143 TRP A C     1 
ATOM   1009 O  O     . TRP A 1 164 ? -11.714 -3.899  -27.866 1.00 24.45 ? 143 TRP A O     1 
ATOM   1010 C  CB    . TRP A 1 164 ? -10.227 -3.608  -30.790 1.00 28.00 ? 143 TRP A CB    1 
ATOM   1011 C  CG    . TRP A 1 164 ? -10.466 -4.130  -32.174 1.00 31.71 ? 143 TRP A CG    1 
ATOM   1012 C  CD1   . TRP A 1 164 ? -11.664 -4.474  -32.746 1.00 30.89 ? 143 TRP A CD1   1 
ATOM   1013 C  CD2   . TRP A 1 164 ? -9.457  -4.427  -33.159 1.00 35.52 ? 143 TRP A CD2   1 
ATOM   1014 N  NE1   . TRP A 1 164 ? -11.472 -4.931  -34.022 1.00 30.25 ? 143 TRP A NE1   1 
ATOM   1015 C  CE2   . TRP A 1 164 ? -10.129 -4.924  -34.300 1.00 34.33 ? 143 TRP A CE2   1 
ATOM   1016 C  CE3   . TRP A 1 164 ? -8.055  -4.351  -33.174 1.00 35.61 ? 143 TRP A CE3   1 
ATOM   1017 C  CZ2   . TRP A 1 164 ? -9.438  -5.342  -35.436 1.00 34.92 ? 143 TRP A CZ2   1 
ATOM   1018 C  CZ3   . TRP A 1 164 ? -7.377  -4.725  -34.310 1.00 36.23 ? 143 TRP A CZ3   1 
ATOM   1019 C  CH2   . TRP A 1 164 ? -8.064  -5.218  -35.423 1.00 39.11 ? 143 TRP A CH2   1 
ATOM   1020 N  N     . ASP A 1 165 ? -11.086 -1.736  -28.089 1.00 23.87 ? 144 ASP A N     1 
ATOM   1021 C  CA    . ASP A 1 165 ? -10.887 -1.438  -26.643 1.00 24.81 ? 144 ASP A CA    1 
ATOM   1022 C  C     . ASP A 1 165 ? -12.216 -1.096  -25.972 1.00 26.05 ? 144 ASP A C     1 
ATOM   1023 O  O     . ASP A 1 165 ? -12.257 -1.075  -24.748 1.00 32.36 ? 144 ASP A O     1 
ATOM   1024 C  CB    . ASP A 1 165 ? -9.951  -0.255  -26.429 1.00 25.81 ? 144 ASP A CB    1 
ATOM   1025 C  CG    . ASP A 1 165 ? -9.270  -0.231  -25.075 1.00 25.10 ? 144 ASP A CG    1 
ATOM   1026 O  OD1   . ASP A 1 165 ? -9.028  -1.332  -24.519 1.00 27.93 ? 144 ASP A OD1   1 
ATOM   1027 O  OD2   . ASP A 1 165 ? -8.944  0.886   -24.623 1.00 21.62 ? 144 ASP A OD2   1 
ATOM   1028 N  N     . ALA A 1 166 ? -13.260 -0.833  -26.743 1.00 25.17 ? 145 ALA A N     1 
ATOM   1029 C  CA    . ALA A 1 166 ? -14.613 -0.557  -26.224 1.00 25.19 ? 145 ALA A CA    1 
ATOM   1030 C  C     . ALA A 1 166 ? -15.428 -1.849  -26.187 1.00 25.99 ? 145 ALA A C     1 
ATOM   1031 O  O     . ALA A 1 166 ? -16.596 -1.780  -25.773 1.00 30.36 ? 145 ALA A O     1 
ATOM   1032 C  CB    . ALA A 1 166 ? -15.269 0.490   -27.104 1.00 24.79 ? 145 ALA A CB    1 
ATOM   1033 N  N     . THR A 1 167 ? -14.869 -2.961  -26.669 1.00 24.72 ? 146 THR A N     1 
ATOM   1034 C  CA    . THR A 1 167 ? -15.589 -4.247  -26.866 1.00 23.72 ? 146 THR A CA    1 
ATOM   1035 C  C     . THR A 1 167 ? -14.936 -5.313  -25.966 1.00 26.07 ? 146 THR A C     1 
ATOM   1036 O  O     . THR A 1 167 ? -13.680 -5.428  -25.993 1.00 25.08 ? 146 THR A O     1 
ATOM   1037 C  CB    . THR A 1 167 ? -15.603 -4.645  -28.351 1.00 23.98 ? 146 THR A CB    1 
ATOM   1038 O  OG1   . THR A 1 167 ? -16.218 -3.619  -29.153 1.00 24.14 ? 146 THR A OG1   1 
ATOM   1039 C  CG2   . THR A 1 167 ? -16.284 -5.973  -28.597 1.00 23.25 ? 146 THR A CG2   1 
ATOM   1040 N  N     . THR A 1 168 ? -15.763 -6.089  -25.242 1.00 26.30 ? 147 THR A N     1 
ATOM   1041 C  CA    . THR A 1 168 ? -15.349 -7.259  -24.419 1.00 27.18 ? 147 THR A CA    1 
ATOM   1042 C  C     . THR A 1 168 ? -15.107 -8.421  -25.369 1.00 27.99 ? 147 THR A C     1 
ATOM   1043 O  O     . THR A 1 168 ? -15.679 -8.396  -26.492 1.00 26.05 ? 147 THR A O     1 
ATOM   1044 C  CB    . THR A 1 168 ? -16.412 -7.739  -23.411 1.00 25.67 ? 147 THR A CB    1 
ATOM   1045 O  OG1   . THR A 1 168 ? -17.503 -8.262  -24.168 1.00 25.51 ? 147 THR A OG1   1 
ATOM   1046 C  CG2   . THR A 1 168 ? -16.894 -6.668  -22.461 1.00 24.05 ? 147 THR A CG2   1 
ATOM   1047 N  N     . LEU A 1 169 ? -14.340 -9.417  -24.936 1.00 26.70 ? 148 LEU A N     1 
ATOM   1048 C  CA    . LEU A 1 169 ? -14.171 -10.630 -25.770 1.00 28.81 ? 148 LEU A CA    1 
ATOM   1049 C  C     . LEU A 1 169 ? -15.562 -11.272 -25.872 1.00 27.06 ? 148 LEU A C     1 
ATOM   1050 O  O     . LEU A 1 169 ? -15.866 -11.787 -26.952 1.00 25.19 ? 148 LEU A O     1 
ATOM   1051 C  CB    . LEU A 1 169 ? -13.092 -11.569 -25.192 1.00 28.13 ? 148 LEU A CB    1 
ATOM   1052 C  CG    . LEU A 1 169 ? -12.897 -12.890 -25.943 1.00 29.10 ? 148 LEU A CG    1 
ATOM   1053 C  CD1   . LEU A 1 169 ? -12.345 -12.655 -27.344 1.00 27.06 ? 148 LEU A CD1   1 
ATOM   1054 C  CD2   . LEU A 1 169 ? -11.995 -13.855 -25.181 1.00 27.70 ? 148 LEU A CD2   1 
ATOM   1055 N  N     . ARG A 1 170 ? -16.389 -11.203 -24.814 1.00 29.81 ? 149 ARG A N     1 
ATOM   1056 C  CA    . ARG A 1 170 ? -17.688 -11.935 -24.782 1.00 29.67 ? 149 ARG A CA    1 
ATOM   1057 C  C     . ARG A 1 170 ? -18.576 -11.387 -25.906 1.00 27.76 ? 149 ARG A C     1 
ATOM   1058 O  O     . ARG A 1 170 ? -19.059 -12.187 -26.748 1.00 22.47 ? 149 ARG A O     1 
ATOM   1059 C  CB    . ARG A 1 170 ? -18.410 -11.856 -23.436 1.00 31.83 ? 149 ARG A CB    1 
ATOM   1060 C  CG    . ARG A 1 170 ? -19.810 -12.465 -23.501 1.00 32.84 ? 149 ARG A CG    1 
ATOM   1061 C  CD    . ARG A 1 170 ? -20.282 -13.147 -22.243 1.00 34.58 ? 149 ARG A CD    1 
ATOM   1062 N  NE    . ARG A 1 170 ? -19.287 -14.068 -21.695 1.00 37.68 ? 149 ARG A NE    1 
ATOM   1063 C  CZ    . ARG A 1 170 ? -19.358 -14.639 -20.490 1.00 35.95 ? 149 ARG A CZ    1 
ATOM   1064 N  NH1   . ARG A 1 170 ? -20.402 -14.418 -19.708 1.00 36.08 ? 149 ARG A NH1   1 
ATOM   1065 N  NH2   . ARG A 1 170 ? -18.390 -15.437 -20.076 1.00 35.45 ? 149 ARG A NH2   1 
ATOM   1066 N  N     . GLU A 1 171 ? -18.758 -10.067 -25.924 1.00 29.95 ? 150 GLU A N     1 
ATOM   1067 C  CA    . GLU A 1 171 ? -19.484 -9.334  -27.000 1.00 33.84 ? 150 GLU A CA    1 
ATOM   1068 C  C     . GLU A 1 171 ? -19.061 -9.878  -28.385 1.00 35.46 ? 150 GLU A C     1 
ATOM   1069 O  O     . GLU A 1 171 ? -19.975 -10.208 -29.223 1.00 33.15 ? 150 GLU A O     1 
ATOM   1070 C  CB    . GLU A 1 171 ? -19.197 -7.846  -26.821 1.00 36.86 ? 150 GLU A CB    1 
ATOM   1071 C  CG    . GLU A 1 171 ? -19.960 -6.914  -27.749 1.00 39.24 ? 150 GLU A CG    1 
ATOM   1072 C  CD    . GLU A 1 171 ? -19.859 -5.467  -27.277 1.00 42.41 ? 150 GLU A CD    1 
ATOM   1073 O  OE1   . GLU A 1 171 ? -19.242 -5.251  -26.188 1.00 42.59 ? 150 GLU A OE1   1 
ATOM   1074 O  OE2   . GLU A 1 171 ? -20.401 -4.556  -27.969 1.00 42.47 ? 150 GLU A OE2   1 
ATOM   1075 N  N     . TRP A 1 172 ? -17.742 -10.007 -28.630 1.00 29.12 ? 151 TRP A N     1 
ATOM   1076 C  CA    . TRP A 1 172 ? -17.197 -10.387 -29.958 1.00 27.74 ? 151 TRP A CA    1 
ATOM   1077 C  C     . TRP A 1 172 ? -17.611 -11.828 -30.299 1.00 29.21 ? 151 TRP A C     1 
ATOM   1078 O  O     . TRP A 1 172 ? -18.194 -12.044 -31.393 1.00 27.32 ? 151 TRP A O     1 
ATOM   1079 C  CB    . TRP A 1 172 ? -15.677 -10.183 -29.968 1.00 29.06 ? 151 TRP A CB    1 
ATOM   1080 C  CG    . TRP A 1 172 ? -15.014 -10.631 -31.228 1.00 29.43 ? 151 TRP A CG    1 
ATOM   1081 C  CD1   . TRP A 1 172 ? -14.835 -9.904  -32.374 1.00 29.64 ? 151 TRP A CD1   1 
ATOM   1082 C  CD2   . TRP A 1 172 ? -14.432 -11.926 -31.468 1.00 27.20 ? 151 TRP A CD2   1 
ATOM   1083 N  NE1   . TRP A 1 172 ? -14.157 -10.656 -33.295 1.00 30.19 ? 151 TRP A NE1   1 
ATOM   1084 C  CE2   . TRP A 1 172 ? -13.917 -11.905 -32.778 1.00 28.71 ? 151 TRP A CE2   1 
ATOM   1085 C  CE3   . TRP A 1 172 ? -14.272 -13.081 -30.700 1.00 26.09 ? 151 TRP A CE3   1 
ATOM   1086 C  CZ2   . TRP A 1 172 ? -13.291 -13.021 -33.343 1.00 29.82 ? 151 TRP A CZ2   1 
ATOM   1087 C  CZ3   . TRP A 1 172 ? -13.665 -14.185 -31.258 1.00 26.26 ? 151 TRP A CZ3   1 
ATOM   1088 C  CH2   . TRP A 1 172 ? -13.181 -14.155 -32.564 1.00 26.52 ? 151 TRP A CH2   1 
ATOM   1089 N  N     . VAL A 1 173 ? -17.335 -12.776 -29.390 1.00 28.07 ? 152 VAL A N     1 
ATOM   1090 C  CA    . VAL A 1 173 ? -17.749 -14.208 -29.500 1.00 27.50 ? 152 VAL A CA    1 
ATOM   1091 C  C     . VAL A 1 173 ? -19.235 -14.279 -29.891 1.00 28.96 ? 152 VAL A C     1 
ATOM   1092 O  O     . VAL A 1 173 ? -19.556 -15.073 -30.829 1.00 27.16 ? 152 VAL A O     1 
ATOM   1093 C  CB    . VAL A 1 173 ? -17.482 -15.004 -28.205 1.00 25.20 ? 152 VAL A CB    1 
ATOM   1094 C  CG1   . VAL A 1 173 ? -18.175 -16.348 -28.237 1.00 24.21 ? 152 VAL A CG1   1 
ATOM   1095 C  CG2   . VAL A 1 173 ? -16.002 -15.196 -27.964 1.00 23.96 ? 152 VAL A CG2   1 
ATOM   1096 N  N     . ALA A 1 174 ? -20.092 -13.504 -29.213 1.00 26.38 ? 153 ALA A N     1 
ATOM   1097 C  CA    . ALA A 1 174 ? -21.564 -13.490 -29.394 1.00 29.35 ? 153 ALA A CA    1 
ATOM   1098 C  C     . ALA A 1 174 ? -21.905 -13.047 -30.812 1.00 33.04 ? 153 ALA A C     1 
ATOM   1099 O  O     . ALA A 1 174 ? -22.917 -13.532 -31.330 1.00 38.43 ? 153 ALA A O     1 
ATOM   1100 C  CB    . ALA A 1 174 ? -22.221 -12.588 -28.383 1.00 31.23 ? 153 ALA A CB    1 
ATOM   1101 N  N     . GLY A 1 175 ? -21.071 -12.176 -31.403 1.00 34.93 ? 154 GLY A N     1 
ATOM   1102 C  CA    . GLY A 1 175 ? -21.156 -11.722 -32.798 1.00 31.60 ? 154 GLY A CA    1 
ATOM   1103 C  C     . GLY A 1 175 ? -20.969 -12.869 -33.778 1.00 33.77 ? 154 GLY A C     1 
ATOM   1104 O  O     . GLY A 1 175 ? -21.738 -12.936 -34.742 1.00 42.95 ? 154 GLY A O     1 
ATOM   1105 N  N     . THR A 1 176 ? -20.014 -13.763 -33.523 1.00 32.59 ? 155 THR A N     1 
ATOM   1106 C  CA    . THR A 1 176 ? -19.614 -14.873 -34.430 1.00 32.26 ? 155 THR A CA    1 
ATOM   1107 C  C     . THR A 1 176 ? -20.803 -15.787 -34.717 1.00 32.84 ? 155 THR A C     1 
ATOM   1108 O  O     . THR A 1 176 ? -20.675 -16.581 -35.662 1.00 36.20 ? 155 THR A O     1 
ATOM   1109 C  CB    . THR A 1 176 ? -18.392 -15.642 -33.899 1.00 32.57 ? 155 THR A CB    1 
ATOM   1110 O  OG1   . THR A 1 176 ? -18.688 -16.478 -32.766 1.00 28.57 ? 155 THR A OG1   1 
ATOM   1111 C  CG2   . THR A 1 176 ? -17.285 -14.666 -33.568 1.00 34.40 ? 155 THR A CG2   1 
ATOM   1112 N  N     . GLY A 1 177 ? -21.905 -15.663 -33.958 1.00 37.64 ? 156 GLY A N     1 
ATOM   1113 C  CA    . GLY A 1 177 ? -23.106 -16.520 -34.072 1.00 38.28 ? 156 GLY A CA    1 
ATOM   1114 C  C     . GLY A 1 177 ? -22.737 -17.998 -33.999 1.00 46.82 ? 156 GLY A C     1 
ATOM   1115 O  O     . GLY A 1 177 ? -23.302 -18.816 -34.798 1.00 45.42 ? 156 GLY A O     1 
ATOM   1116 N  N     . VAL A 1 178 ? -21.805 -18.342 -33.097 1.00 45.39 ? 157 VAL A N     1 
ATOM   1117 C  CA    . VAL A 1 178 ? -21.311 -19.737 -32.888 1.00 46.42 ? 157 VAL A CA    1 
ATOM   1118 C  C     . VAL A 1 178 ? -22.291 -20.454 -31.956 1.00 41.22 ? 157 VAL A C     1 
ATOM   1119 O  O     . VAL A 1 178 ? -22.971 -19.816 -31.156 1.00 41.92 ? 157 VAL A O     1 
ATOM   1120 C  CB    . VAL A 1 178 ? -19.848 -19.711 -32.389 1.00 47.78 ? 157 VAL A CB    1 
ATOM   1121 C  CG1   . VAL A 1 178 ? -19.669 -20.339 -31.029 1.00 46.40 ? 157 VAL A CG1   1 
ATOM   1122 C  CG2   . VAL A 1 178 ? -18.889 -20.329 -33.401 1.00 48.90 ? 157 VAL A CG2   1 
ATOM   1123 N  N     . PRO A 1 179 ? -22.486 -21.785 -32.085 1.00 44.04 ? 158 PRO A N     1 
ATOM   1124 C  CA    . PRO A 1 179 ? -23.392 -22.518 -31.193 1.00 43.49 ? 158 PRO A CA    1 
ATOM   1125 C  C     . PRO A 1 179 ? -22.906 -22.497 -29.733 1.00 43.91 ? 158 PRO A C     1 
ATOM   1126 O  O     . PRO A 1 179 ? -21.728 -22.211 -29.496 1.00 38.68 ? 158 PRO A O     1 
ATOM   1127 C  CB    . PRO A 1 179 ? -23.381 -23.964 -31.721 1.00 44.00 ? 158 PRO A CB    1 
ATOM   1128 C  CG    . PRO A 1 179 ? -22.796 -23.856 -33.122 1.00 43.70 ? 158 PRO A CG    1 
ATOM   1129 C  CD    . PRO A 1 179 ? -21.850 -22.670 -33.076 1.00 43.26 ? 158 PRO A CD    1 
ATOM   1130 N  N     . ASP A 1 180 ? -23.812 -22.781 -28.793 1.00 42.84 ? 159 ASP A N     1 
ATOM   1131 C  CA    . ASP A 1 180 ? -23.554 -22.676 -27.330 1.00 45.49 ? 159 ASP A CA    1 
ATOM   1132 C  C     . ASP A 1 180 ? -22.388 -23.584 -26.938 1.00 42.63 ? 159 ASP A C     1 
ATOM   1133 O  O     . ASP A 1 180 ? -21.588 -23.134 -26.118 1.00 41.84 ? 159 ASP A O     1 
ATOM   1134 C  CB    . ASP A 1 180 ? -24.797 -22.994 -26.498 1.00 46.39 ? 159 ASP A CB    1 
ATOM   1135 C  CG    . ASP A 1 180 ? -25.875 -21.937 -26.652 1.00 46.75 ? 159 ASP A CG    1 
ATOM   1136 O  OD1   . ASP A 1 180 ? -27.057 -22.309 -26.585 1.00 50.13 ? 159 ASP A OD1   1 
ATOM   1137 O  OD2   . ASP A 1 180 ? -25.516 -20.745 -26.845 1.00 46.68 ? 159 ASP A OD2   1 
ATOM   1138 N  N     . ARG A 1 181 ? -22.279 -24.772 -27.542 1.00 41.50 ? 160 ARG A N     1 
ATOM   1139 C  CA    . ARG A 1 181 ? -21.291 -25.821 -27.175 1.00 42.18 ? 160 ARG A CA    1 
ATOM   1140 C  C     . ARG A 1 181 ? -19.896 -25.387 -27.656 1.00 44.47 ? 160 ARG A C     1 
ATOM   1141 O  O     . ARG A 1 181 ? -18.887 -25.764 -27.014 1.00 43.98 ? 160 ARG A O     1 
ATOM   1142 C  CB    . ARG A 1 181 ? -21.745 -27.165 -27.757 1.00 45.09 ? 160 ARG A CB    1 
ATOM   1143 C  CG    . ARG A 1 181 ? -21.203 -28.370 -27.008 1.00 52.58 ? 160 ARG A CG    1 
ATOM   1144 C  CD    . ARG A 1 181 ? -22.214 -29.470 -26.717 1.00 57.06 ? 160 ARG A CD    1 
ATOM   1145 N  NE    . ARG A 1 181 ? -22.849 -30.022 -27.915 1.00 66.27 ? 160 ARG A NE    1 
ATOM   1146 C  CZ    . ARG A 1 181 ? -22.359 -30.985 -28.699 1.00 68.48 ? 160 ARG A CZ    1 
ATOM   1147 N  NH1   . ARG A 1 181 ? -21.180 -31.541 -28.457 1.00 70.11 ? 160 ARG A NH1   1 
ATOM   1148 N  NH2   . ARG A 1 181 ? -23.060 -31.377 -29.751 1.00 71.50 ? 160 ARG A NH2   1 
ATOM   1149 N  N     . VAL A 1 182 ? -19.828 -24.613 -28.741 1.00 40.97 ? 161 VAL A N     1 
ATOM   1150 C  CA    . VAL A 1 182 ? -18.553 -24.076 -29.298 1.00 37.71 ? 161 VAL A CA    1 
ATOM   1151 C  C     . VAL A 1 182 ? -18.206 -22.800 -28.534 1.00 33.83 ? 161 VAL A C     1 
ATOM   1152 O  O     . VAL A 1 182 ? -16.997 -22.523 -28.383 1.00 38.92 ? 161 VAL A O     1 
ATOM   1153 C  CB    . VAL A 1 182 ? -18.628 -23.835 -30.821 1.00 41.61 ? 161 VAL A CB    1 
ATOM   1154 C  CG1   . VAL A 1 182 ? -17.383 -23.146 -31.368 1.00 40.14 ? 161 VAL A CG1   1 
ATOM   1155 C  CG2   . VAL A 1 182 ? -18.888 -25.131 -31.588 1.00 44.09 ? 161 VAL A CG2   1 
ATOM   1156 N  N     . ALA A 1 183 ? -19.199 -22.048 -28.068 1.00 29.35 ? 162 ALA A N     1 
ATOM   1157 C  CA    . ALA A 1 183 ? -18.969 -20.861 -27.213 1.00 28.86 ? 162 ALA A CA    1 
ATOM   1158 C  C     . ALA A 1 183 ? -18.520 -21.336 -25.828 1.00 30.41 ? 162 ALA A C     1 
ATOM   1159 O  O     . ALA A 1 183 ? -17.703 -20.651 -25.241 1.00 32.98 ? 162 ALA A O     1 
ATOM   1160 C  CB    . ALA A 1 183 ? -20.175 -19.964 -27.158 1.00 27.50 ? 162 ALA A CB    1 
ATOM   1161 N  N     . GLY A 1 184 ? -18.993 -22.501 -25.367 1.00 30.90 ? 163 GLY A N     1 
ATOM   1162 C  CA    . GLY A 1 184 ? -18.634 -23.113 -24.074 1.00 28.02 ? 163 GLY A CA    1 
ATOM   1163 C  C     . GLY A 1 184 ? -17.197 -23.614 -24.088 1.00 30.01 ? 163 GLY A C     1 
ATOM   1164 O  O     . GLY A 1 184 ? -16.449 -23.406 -23.088 1.00 27.07 ? 163 GLY A O     1 
ATOM   1165 N  N     . LEU A 1 185 ? -16.812 -24.261 -25.182 1.00 26.65 ? 164 LEU A N     1 
ATOM   1166 C  CA    . LEU A 1 185 ? -15.464 -24.829 -25.385 1.00 29.13 ? 164 LEU A CA    1 
ATOM   1167 C  C     . LEU A 1 185 ? -14.462 -23.668 -25.415 1.00 28.96 ? 164 LEU A C     1 
ATOM   1168 O  O     . LEU A 1 185 ? -13.452 -23.718 -24.657 1.00 26.74 ? 164 LEU A O     1 
ATOM   1169 C  CB    . LEU A 1 185 ? -15.498 -25.627 -26.692 1.00 33.59 ? 164 LEU A CB    1 
ATOM   1170 C  CG    . LEU A 1 185 ? -14.158 -26.097 -27.252 1.00 35.16 ? 164 LEU A CG    1 
ATOM   1171 C  CD1   . LEU A 1 185 ? -13.417 -26.979 -26.259 1.00 39.06 ? 164 LEU A CD1   1 
ATOM   1172 C  CD2   . LEU A 1 185 ? -14.385 -26.857 -28.551 1.00 38.52 ? 164 LEU A CD2   1 
ATOM   1173 N  N     . PHE A 1 186 ? -14.760 -22.637 -26.219 1.00 26.57 ? 165 PHE A N     1 
ATOM   1174 C  CA    . PHE A 1 186 ? -13.909 -21.433 -26.365 1.00 26.58 ? 165 PHE A CA    1 
ATOM   1175 C  C     . PHE A 1 186 ? -13.774 -20.738 -25.003 1.00 26.54 ? 165 PHE A C     1 
ATOM   1176 O  O     . PHE A 1 186 ? -12.654 -20.262 -24.724 1.00 23.68 ? 165 PHE A O     1 
ATOM   1177 C  CB    . PHE A 1 186 ? -14.454 -20.497 -27.441 1.00 28.38 ? 165 PHE A CB    1 
ATOM   1178 C  CG    . PHE A 1 186 ? -13.545 -19.339 -27.746 1.00 28.05 ? 165 PHE A CG    1 
ATOM   1179 C  CD1   . PHE A 1 186 ? -13.839 -18.069 -27.293 1.00 25.09 ? 165 PHE A CD1   1 
ATOM   1180 C  CD2   . PHE A 1 186 ? -12.377 -19.529 -28.475 1.00 31.55 ? 165 PHE A CD2   1 
ATOM   1181 C  CE1   . PHE A 1 186 ? -13.014 -17.006 -27.603 1.00 25.33 ? 165 PHE A CE1   1 
ATOM   1182 C  CE2   . PHE A 1 186 ? -11.527 -18.465 -28.739 1.00 29.92 ? 165 PHE A CE2   1 
ATOM   1183 C  CZ    . PHE A 1 186 ? -11.855 -17.206 -28.306 1.00 26.82 ? 165 PHE A CZ    1 
ATOM   1184 N  N     . GLU A 1 187 ? -14.845 -20.726 -24.193 1.00 24.74 ? 166 GLU A N     1 
ATOM   1185 C  CA    . GLU A 1 187 ? -14.842 -20.134 -22.829 1.00 26.06 ? 166 GLU A CA    1 
ATOM   1186 C  C     . GLU A 1 187 ? -13.904 -20.912 -21.887 1.00 27.24 ? 166 GLU A C     1 
ATOM   1187 O  O     . GLU A 1 187 ? -13.297 -20.243 -21.021 1.00 25.81 ? 166 GLU A O     1 
ATOM   1188 C  CB    . GLU A 1 187 ? -16.227 -20.071 -22.187 1.00 24.35 ? 166 GLU A CB    1 
ATOM   1189 C  CG    . GLU A 1 187 ? -16.251 -19.191 -20.930 1.00 23.78 ? 166 GLU A CG    1 
ATOM   1190 C  CD    . GLU A 1 187 ? -16.017 -17.704 -21.159 1.00 28.03 ? 166 GLU A CD    1 
ATOM   1191 O  OE1   . GLU A 1 187 ? -15.534 -16.985 -20.218 1.00 27.78 ? 166 GLU A OE1   1 
ATOM   1192 O  OE2   . GLU A 1 187 ? -16.300 -17.238 -22.293 1.00 32.49 ? 166 GLU A OE2   1 
ATOM   1193 N  N     . VAL A 1 188 ? -13.818 -22.242 -21.979 1.00 25.20 ? 167 VAL A N     1 
ATOM   1194 C  CA    . VAL A 1 188 ? -12.886 -23.046 -21.133 1.00 27.58 ? 167 VAL A CA    1 
ATOM   1195 C  C     . VAL A 1 188 ? -11.428 -22.684 -21.510 1.00 26.41 ? 167 VAL A C     1 
ATOM   1196 O  O     . VAL A 1 188 ? -10.606 -22.500 -20.585 1.00 28.38 ? 167 VAL A O     1 
ATOM   1197 C  CB    . VAL A 1 188 ? -13.167 -24.559 -21.231 1.00 31.27 ? 167 VAL A CB    1 
ATOM   1198 C  CG1   . VAL A 1 188 ? -12.000 -25.411 -20.730 1.00 33.15 ? 167 VAL A CG1   1 
ATOM   1199 C  CG2   . VAL A 1 188 ? -14.439 -24.918 -20.486 1.00 34.43 ? 167 VAL A CG2   1 
ATOM   1200 N  N     . ALA A 1 189 ? -11.134 -22.491 -22.794 1.00 25.72 ? 168 ALA A N     1 
ATOM   1201 C  CA    . ALA A 1 189 ? -9.790  -22.112 -23.312 1.00 26.35 ? 168 ALA A CA    1 
ATOM   1202 C  C     . ALA A 1 189 ? -9.469  -20.676 -22.894 1.00 25.71 ? 168 ALA A C     1 
ATOM   1203 O  O     . ALA A 1 189 ? -8.353  -20.427 -22.378 1.00 31.50 ? 168 ALA A O     1 
ATOM   1204 C  CB    . ALA A 1 189 ? -9.715  -22.272 -24.804 1.00 25.02 ? 168 ALA A CB    1 
ATOM   1205 N  N     . VAL A 1 190 ? -10.430 -19.769 -22.994 1.00 23.11 ? 169 VAL A N     1 
ATOM   1206 C  CA    . VAL A 1 190 ? -10.222 -18.381 -22.510 1.00 22.91 ? 169 VAL A CA    1 
ATOM   1207 C  C     . VAL A 1 190 ? -9.849  -18.411 -21.021 1.00 22.20 ? 169 VAL A C     1 
ATOM   1208 O  O     . VAL A 1 190 ? -8.909  -17.732 -20.656 1.00 22.59 ? 169 VAL A O     1 
ATOM   1209 C  CB    . VAL A 1 190 ? -11.440 -17.489 -22.801 1.00 23.24 ? 169 VAL A CB    1 
ATOM   1210 C  CG1   . VAL A 1 190 ? -11.382 -16.169 -22.027 1.00 24.59 ? 169 VAL A CG1   1 
ATOM   1211 C  CG2   . VAL A 1 190 ? -11.568 -17.212 -24.297 1.00 21.56 ? 169 VAL A CG2   1 
ATOM   1212 N  N     . GLN A 1 191 ? -10.559 -19.161 -20.180 1.00 23.52 ? 170 GLN A N     1 
ATOM   1213 C  CA    . GLN A 1 191 ? -10.397 -19.071 -18.698 1.00 24.28 ? 170 GLN A CA    1 
ATOM   1214 C  C     . GLN A 1 191 ? -9.090  -19.775 -18.297 1.00 22.84 ? 170 GLN A C     1 
ATOM   1215 O  O     . GLN A 1 191 ? -8.434  -19.273 -17.380 1.00 23.67 ? 170 GLN A O     1 
ATOM   1216 C  CB    . GLN A 1 191 ? -11.644 -19.550 -17.954 1.00 24.09 ? 170 GLN A CB    1 
ATOM   1217 C  CG    . GLN A 1 191 ? -12.843 -18.614 -18.144 1.00 25.21 ? 170 GLN A CG    1 
ATOM   1218 C  CD    . GLN A 1 191 ? -14.050 -19.017 -17.324 1.00 27.79 ? 170 GLN A CD    1 
ATOM   1219 O  OE1   . GLN A 1 191 ? -13.943 -19.832 -16.405 1.00 30.62 ? 170 GLN A OE1   1 
ATOM   1220 N  NE2   . GLN A 1 191 ? -15.219 -18.481 -17.674 1.00 26.25 ? 170 GLN A NE2   1 
ATOM   1221 N  N     . ALA A 1 192 ? -8.687  -20.801 -19.041 1.00 20.27 ? 171 ALA A N     1 
ATOM   1222 C  CA    . ALA A 1 192 ? -7.418  -21.538 -18.888 1.00 21.58 ? 171 ALA A CA    1 
ATOM   1223 C  C     . ALA A 1 192 ? -6.210  -20.700 -19.337 1.00 22.62 ? 171 ALA A C     1 
ATOM   1224 O  O     . ALA A 1 192 ? -5.116  -20.955 -18.837 1.00 20.73 ? 171 ALA A O     1 
ATOM   1225 C  CB    . ALA A 1 192 ? -7.515  -22.808 -19.695 1.00 23.00 ? 171 ALA A CB    1 
ATOM   1226 N  N     . VAL A 1 193 ? -6.388  -19.760 -20.273 1.00 24.29 ? 172 VAL A N     1 
ATOM   1227 C  CA    . VAL A 1 193 ? -5.286  -18.852 -20.715 1.00 23.49 ? 172 VAL A CA    1 
ATOM   1228 C  C     . VAL A 1 193 ? -5.233  -17.567 -19.870 1.00 22.76 ? 172 VAL A C     1 
ATOM   1229 O  O     . VAL A 1 193 ? -4.112  -17.160 -19.561 1.00 19.50 ? 172 VAL A O     1 
ATOM   1230 C  CB    . VAL A 1 193 ? -5.377  -18.539 -22.212 1.00 23.38 ? 172 VAL A CB    1 
ATOM   1231 C  CG1   . VAL A 1 193 ? -4.352  -17.489 -22.599 1.00 23.41 ? 172 VAL A CG1   1 
ATOM   1232 C  CG2   . VAL A 1 193 ? -5.200  -19.808 -23.046 1.00 22.39 ? 172 VAL A CG2   1 
ATOM   1233 N  N     . PHE A 1 194 ? -6.350  -16.932 -19.492 1.00 22.43 ? 173 PHE A N     1 
ATOM   1234 C  CA    . PHE A 1 194 ? -6.286  -15.579 -18.860 1.00 23.71 ? 173 PHE A CA    1 
ATOM   1235 C  C     . PHE A 1 194 ? -6.647  -15.577 -17.373 1.00 21.90 ? 173 PHE A C     1 
ATOM   1236 O  O     . PHE A 1 194 ? -6.462  -14.544 -16.730 1.00 24.59 ? 173 PHE A O     1 
ATOM   1237 C  CB    . PHE A 1 194 ? -7.203  -14.597 -19.580 1.00 25.36 ? 173 PHE A CB    1 
ATOM   1238 C  CG    . PHE A 1 194 ? -6.817  -14.289 -20.998 1.00 24.76 ? 173 PHE A CG    1 
ATOM   1239 C  CD1   . PHE A 1 194 ? -5.927  -13.271 -21.276 1.00 26.28 ? 173 PHE A CD1   1 
ATOM   1240 C  CD2   . PHE A 1 194 ? -7.386  -14.981 -22.055 1.00 26.13 ? 173 PHE A CD2   1 
ATOM   1241 C  CE1   . PHE A 1 194 ? -5.608  -12.959 -22.588 1.00 26.57 ? 173 PHE A CE1   1 
ATOM   1242 C  CE2   . PHE A 1 194 ? -7.060  -14.670 -23.366 1.00 26.97 ? 173 PHE A CE2   1 
ATOM   1243 C  CZ    . PHE A 1 194 ? -6.149  -13.673 -23.627 1.00 26.17 ? 173 PHE A CZ    1 
ATOM   1244 N  N     . ALA A 1 195 ? -7.181  -16.671 -16.845 1.00 22.85 ? 174 ALA A N     1 
ATOM   1245 C  CA    . ALA A 1 195 ? -7.653  -16.785 -15.443 1.00 22.78 ? 174 ALA A CA    1 
ATOM   1246 C  C     . ALA A 1 195 ? -8.702  -15.697 -15.164 1.00 20.65 ? 174 ALA A C     1 
ATOM   1247 O  O     . ALA A 1 195 ? -8.727  -15.161 -14.054 1.00 18.21 ? 174 ALA A O     1 
ATOM   1248 C  CB    . ALA A 1 195 ? -6.464  -16.738 -14.490 1.00 22.53 ? 174 ALA A CB    1 
ATOM   1249 N  N     . ALA A 1 196 ? -9.532  -15.427 -16.174 1.00 21.05 ? 175 ALA A N     1 
ATOM   1250 C  CA    . ALA A 1 196 ? -10.621 -14.426 -16.228 1.00 21.42 ? 175 ALA A CA    1 
ATOM   1251 C  C     . ALA A 1 196 ? -11.575 -14.844 -17.355 1.00 24.67 ? 175 ALA A C     1 
ATOM   1252 O  O     . ALA A 1 196 ? -11.059 -15.532 -18.288 1.00 27.80 ? 175 ALA A O     1 
ATOM   1253 C  CB    . ALA A 1 196 ? -9.999  -13.083 -16.474 1.00 21.28 ? 175 ALA A CB    1 
ATOM   1254 N  N     . THR A 1 197 ? -12.885 -14.514 -17.283 1.00 24.63 ? 176 THR A N     1 
ATOM   1255 C  CA    . THR A 1 197 ? -13.922 -14.872 -18.302 1.00 22.39 ? 176 THR A CA    1 
ATOM   1256 C  C     . THR A 1 197 ? -13.791 -13.944 -19.519 1.00 22.08 ? 176 THR A C     1 
ATOM   1257 O  O     . THR A 1 197 ? -13.139 -12.880 -19.377 1.00 21.66 ? 176 THR A O     1 
ATOM   1258 C  CB    . THR A 1 197 ? -15.395 -14.693 -17.869 1.00 21.81 ? 176 THR A CB    1 
ATOM   1259 O  OG1   . THR A 1 197 ? -15.683 -13.296 -17.725 1.00 22.11 ? 176 THR A OG1   1 
ATOM   1260 C  CG2   . THR A 1 197 ? -15.770 -15.417 -16.595 1.00 21.59 ? 176 THR A CG2   1 
ATOM   1261 N  N     . SER A 1 198 ? -14.480 -14.272 -20.621 1.00 20.14 ? 177 SER A N     1 
ATOM   1262 C  CA    . SER A 1 198 ? -14.486 -13.468 -21.866 1.00 19.66 ? 177 SER A CA    1 
ATOM   1263 C  C     . SER A 1 198 ? -15.065 -12.084 -21.601 1.00 19.57 ? 177 SER A C     1 
ATOM   1264 O  O     . SER A 1 198 ? -14.719 -11.150 -22.351 1.00 19.75 ? 177 SER A O     1 
ATOM   1265 C  CB    . SER A 1 198 ? -15.167 -14.155 -23.006 1.00 19.70 ? 177 SER A CB    1 
ATOM   1266 O  OG    . SER A 1 198 ? -16.353 -14.804 -22.610 1.00 18.80 ? 177 SER A OG    1 
ATOM   1267 N  N     . ALA A 1 199 ? -15.833 -11.933 -20.528 1.00 22.22 ? 178 ALA A N     1 
ATOM   1268 C  CA    . ALA A 1 199 ? -16.573 -10.696 -20.197 1.00 22.10 ? 178 ALA A CA    1 
ATOM   1269 C  C     . ALA A 1 199 ? -15.656 -9.685  -19.539 1.00 22.05 ? 178 ALA A C     1 
ATOM   1270 O  O     . ALA A 1 199 ? -15.907 -8.472  -19.672 1.00 26.78 ? 178 ALA A O     1 
ATOM   1271 C  CB    . ALA A 1 199 ? -17.736 -11.016 -19.306 1.00 24.04 ? 178 ALA A CB    1 
ATOM   1272 N  N     . GLN A 1 200 ? -14.620 -10.144 -18.866 1.00 22.20 ? 179 GLN A N     1 
ATOM   1273 C  CA    . GLN A 1 200 ? -13.718 -9.262  -18.074 1.00 22.23 ? 179 GLN A CA    1 
ATOM   1274 C  C     . GLN A 1 200 ? -12.678 -8.582  -18.973 1.00 23.60 ? 179 GLN A C     1 
ATOM   1275 O  O     . GLN A 1 200 ? -12.078 -7.582  -18.509 1.00 24.67 ? 179 GLN A O     1 
ATOM   1276 C  CB    . GLN A 1 200 ? -13.005 -10.083 -17.001 1.00 22.53 ? 179 GLN A CB    1 
ATOM   1277 C  CG    . GLN A 1 200 ? -13.947 -10.842 -16.071 1.00 22.90 ? 179 GLN A CG    1 
ATOM   1278 C  CD    . GLN A 1 200 ? -13.186 -11.651 -15.044 1.00 23.38 ? 179 GLN A CD    1 
ATOM   1279 O  OE1   . GLN A 1 200 ? -13.298 -12.866 -14.988 1.00 26.80 ? 179 GLN A OE1   1 
ATOM   1280 N  NE2   . GLN A 1 200 ? -12.407 -10.979 -14.215 1.00 22.64 ? 179 GLN A NE2   1 
ATOM   1281 N  N     . LEU A 1 201 ? -12.417 -9.141  -20.167 1.00 25.33 ? 180 LEU A N     1 
ATOM   1282 C  CA    . LEU A 1 201 ? -11.288 -8.764  -21.067 1.00 26.36 ? 180 LEU A CA    1 
ATOM   1283 C  C     . LEU A 1 201 ? -11.827 -7.871  -22.189 1.00 24.05 ? 180 LEU A C     1 
ATOM   1284 O  O     . LEU A 1 201 ? -12.879 -8.213  -22.759 1.00 27.57 ? 180 LEU A O     1 
ATOM   1285 C  CB    . LEU A 1 201 ? -10.677 -10.025 -21.702 1.00 28.45 ? 180 LEU A CB    1 
ATOM   1286 C  CG    . LEU A 1 201 ? -9.875  -10.992 -20.821 1.00 30.59 ? 180 LEU A CG    1 
ATOM   1287 C  CD1   . LEU A 1 201 ? -9.343  -10.327 -19.567 1.00 30.83 ? 180 LEU A CD1   1 
ATOM   1288 C  CD2   . LEU A 1 201 ? -10.675 -12.206 -20.445 1.00 31.99 ? 180 LEU A CD2   1 
ATOM   1289 N  N     . SER A 1 202 ? -11.126 -6.795  -22.531 1.00 23.44 ? 181 SER A N     1 
ATOM   1290 C  CA    . SER A 1 202 ? -11.346 -6.055  -23.801 1.00 23.06 ? 181 SER A CA    1 
ATOM   1291 C  C     . SER A 1 202 ? -10.965 -6.987  -24.947 1.00 24.45 ? 181 SER A C     1 
ATOM   1292 O  O     . SER A 1 202 ? -10.029 -7.776  -24.757 1.00 24.74 ? 181 SER A O     1 
ATOM   1293 C  CB    . SER A 1 202 ? -10.496 -4.842  -23.887 1.00 25.21 ? 181 SER A CB    1 
ATOM   1294 O  OG    . SER A 1 202 ? -9.146  -5.240  -24.087 1.00 24.70 ? 181 SER A OG    1 
ATOM   1295 N  N     . LEU A 1 203 ? -11.587 -6.848  -26.113 1.00 22.67 ? 182 LEU A N     1 
ATOM   1296 C  CA    . LEU A 1 203 ? -11.167 -7.613  -27.309 1.00 23.60 ? 182 LEU A CA    1 
ATOM   1297 C  C     . LEU A 1 203 ? -9.708  -7.260  -27.647 1.00 22.92 ? 182 LEU A C     1 
ATOM   1298 O  O     . LEU A 1 203 ? -8.972  -8.150  -28.163 1.00 19.27 ? 182 LEU A O     1 
ATOM   1299 C  CB    . LEU A 1 203 ? -12.133 -7.288  -28.449 1.00 23.54 ? 182 LEU A CB    1 
ATOM   1300 C  CG    . LEU A 1 203 ? -11.819 -7.865  -29.819 1.00 23.98 ? 182 LEU A CG    1 
ATOM   1301 C  CD1   . LEU A 1 203 ? -11.776 -9.392  -29.826 1.00 22.74 ? 182 LEU A CD1   1 
ATOM   1302 C  CD2   . LEU A 1 203 ? -12.859 -7.347  -30.805 1.00 25.96 ? 182 LEU A CD2   1 
ATOM   1303 N  N     . LEU A 1 204 ? -9.304  -6.015  -27.387 1.00 24.00 ? 183 LEU A N     1 
ATOM   1304 C  CA    . LEU A 1 204 ? -7.957  -5.527  -27.779 1.00 26.13 ? 183 LEU A CA    1 
ATOM   1305 C  C     . LEU A 1 204 ? -6.911  -6.212  -26.897 1.00 24.29 ? 183 LEU A C     1 
ATOM   1306 O  O     . LEU A 1 204 ? -5.848  -6.528  -27.417 1.00 28.57 ? 183 LEU A O     1 
ATOM   1307 C  CB    . LEU A 1 204 ? -7.879  -3.997  -27.683 1.00 26.74 ? 183 LEU A CB    1 
ATOM   1308 C  CG    . LEU A 1 204 ? -6.548  -3.393  -28.129 1.00 30.20 ? 183 LEU A CG    1 
ATOM   1309 C  CD1   . LEU A 1 204 ? -6.230  -3.737  -29.581 1.00 29.88 ? 183 LEU A CD1   1 
ATOM   1310 C  CD2   . LEU A 1 204 ? -6.537  -1.890  -27.946 1.00 32.23 ? 183 LEU A CD2   1 
ATOM   1311 N  N     . HIS A 1 205 ? -7.180  -6.395  -25.604 1.00 22.56 ? 184 HIS A N     1 
ATOM   1312 C  CA    . HIS A 1 205 ? -6.258  -7.111  -24.686 1.00 20.90 ? 184 HIS A CA    1 
ATOM   1313 C  C     . HIS A 1 205 ? -6.118  -8.549  -25.153 1.00 19.87 ? 184 HIS A C     1 
ATOM   1314 O  O     . HIS A 1 205 ? -4.980  -9.062  -25.134 1.00 20.84 ? 184 HIS A O     1 
ATOM   1315 C  CB    . HIS A 1 205 ? -6.709  -7.074  -23.212 1.00 19.38 ? 184 HIS A CB    1 
ATOM   1316 C  CG    . HIS A 1 205 ? -5.777  -7.799  -22.308 1.00 17.73 ? 184 HIS A CG    1 
ATOM   1317 N  ND1   . HIS A 1 205 ? -4.597  -7.229  -21.842 1.00 17.44 ? 184 HIS A ND1   1 
ATOM   1318 C  CD2   . HIS A 1 205 ? -5.809  -9.055  -21.806 1.00 17.63 ? 184 HIS A CD2   1 
ATOM   1319 C  CE1   . HIS A 1 205 ? -3.962  -8.117  -21.090 1.00 15.98 ? 184 HIS A CE1   1 
ATOM   1320 N  NE2   . HIS A 1 205 ? -4.669  -9.237  -21.072 1.00 15.04 ? 184 HIS A NE2   1 
ATOM   1321 N  N     . ALA A 1 206 ? -7.222  -9.197  -25.521 1.00 18.75 ? 185 ALA A N     1 
ATOM   1322 C  CA    . ALA A 1 206 ? -7.179  -10.640 -25.837 1.00 20.04 ? 185 ALA A CA    1 
ATOM   1323 C  C     . ALA A 1 206 ? -6.335  -10.801 -27.106 1.00 19.44 ? 185 ALA A C     1 
ATOM   1324 O  O     . ALA A 1 206 ? -5.429  -11.673 -27.117 1.00 19.03 ? 185 ALA A O     1 
ATOM   1325 C  CB    . ALA A 1 206 ? -8.560  -11.215 -25.944 1.00 19.48 ? 185 ALA A CB    1 
ATOM   1326 N  N     . ALA A 1 207 ? -6.560  -9.901  -28.069 1.00 20.80 ? 186 ALA A N     1 
ATOM   1327 C  CA    . ALA A 1 207 ? -5.951  -9.876  -29.423 1.00 21.84 ? 186 ALA A CA    1 
ATOM   1328 C  C     . ALA A 1 207 ? -4.462  -9.601  -29.289 1.00 21.47 ? 186 ALA A C     1 
ATOM   1329 O  O     . ALA A 1 207 ? -3.649  -10.291 -29.943 1.00 20.34 ? 186 ALA A O     1 
ATOM   1330 C  CB    . ALA A 1 207 ? -6.576  -8.817  -30.295 1.00 21.90 ? 186 ALA A CB    1 
ATOM   1331 N  N     . HIS A 1 208 ? -4.107  -8.621  -28.474 1.00 20.87 ? 187 HIS A N     1 
ATOM   1332 C  CA    . HIS A 1 208 ? -2.673  -8.381  -28.162 1.00 20.95 ? 187 HIS A CA    1 
ATOM   1333 C  C     . HIS A 1 208 ? -2.029  -9.671  -27.601 1.00 22.42 ? 187 HIS A C     1 
ATOM   1334 O  O     . HIS A 1 208 ? -0.895  -10.023 -28.046 1.00 23.25 ? 187 HIS A O     1 
ATOM   1335 C  CB    . HIS A 1 208 ? -2.536  -7.192  -27.229 1.00 20.54 ? 187 HIS A CB    1 
ATOM   1336 C  CG    . HIS A 1 208 ? -1.168  -7.089  -26.678 1.00 21.30 ? 187 HIS A CG    1 
ATOM   1337 N  ND1   . HIS A 1 208 ? -0.153  -6.415  -27.354 1.00 23.17 ? 187 HIS A ND1   1 
ATOM   1338 C  CD2   . HIS A 1 208 ? -0.632  -7.638  -25.572 1.00 19.83 ? 187 HIS A CD2   1 
ATOM   1339 C  CE1   . HIS A 1 208 ? 0.960   -6.550  -26.667 1.00 22.57 ? 187 HIS A CE1   1 
ATOM   1340 N  NE2   . HIS A 1 208 ? 0.675   -7.291  -25.562 1.00 22.50 ? 187 HIS A NE2   1 
ATOM   1341 N  N     . TYR A 1 209 ? -2.698  -10.367 -26.670 1.00 19.58 ? 188 TYR A N     1 
ATOM   1342 C  CA    . TYR A 1 209 ? -2.101  -11.522 -25.939 1.00 20.18 ? 188 TYR A CA    1 
ATOM   1343 C  C     . TYR A 1 209 ? -1.859  -12.688 -26.918 1.00 20.88 ? 188 TYR A C     1 
ATOM   1344 O  O     . TYR A 1 209 ? -0.897  -13.438 -26.673 1.00 21.35 ? 188 TYR A O     1 
ATOM   1345 C  CB    . TYR A 1 209 ? -2.995  -11.930 -24.762 1.00 18.64 ? 188 TYR A CB    1 
ATOM   1346 C  CG    . TYR A 1 209 ? -2.370  -12.709 -23.627 1.00 19.28 ? 188 TYR A CG    1 
ATOM   1347 C  CD1   . TYR A 1 209 ? -2.370  -14.086 -23.630 1.00 17.68 ? 188 TYR A CD1   1 
ATOM   1348 C  CD2   . TYR A 1 209 ? -1.830  -12.064 -22.508 1.00 21.40 ? 188 TYR A CD2   1 
ATOM   1349 C  CE1   . TYR A 1 209 ? -1.840  -14.802 -22.572 1.00 19.17 ? 188 TYR A CE1   1 
ATOM   1350 C  CE2   . TYR A 1 209 ? -1.274  -12.765 -21.448 1.00 19.87 ? 188 TYR A CE2   1 
ATOM   1351 C  CZ    . TYR A 1 209 ? -1.289  -14.147 -21.484 1.00 19.91 ? 188 TYR A CZ    1 
ATOM   1352 O  OH    . TYR A 1 209 ? -0.775  -14.887 -20.459 1.00 23.31 ? 188 TYR A OH    1 
ATOM   1353 N  N     . VAL A 1 210 ? -2.690  -12.837 -27.956 1.00 20.76 ? 189 VAL A N     1 
ATOM   1354 C  CA    . VAL A 1 210 ? -2.646  -13.959 -28.953 1.00 22.53 ? 189 VAL A CA    1 
ATOM   1355 C  C     . VAL A 1 210 ? -1.542  -13.658 -29.969 1.00 22.20 ? 189 VAL A C     1 
ATOM   1356 O  O     . VAL A 1 210 ? -0.802  -14.578 -30.384 1.00 21.66 ? 189 VAL A O     1 
ATOM   1357 C  CB    . VAL A 1 210 ? -4.013  -14.154 -29.650 1.00 24.21 ? 189 VAL A CB    1 
ATOM   1358 C  CG1   . VAL A 1 210 ? -3.898  -14.995 -30.906 1.00 27.39 ? 189 VAL A CG1   1 
ATOM   1359 C  CG2   . VAL A 1 210 ? -5.059  -14.767 -28.718 1.00 22.99 ? 189 VAL A CG2   1 
ATOM   1360 N  N     . HIS A 1 211 ? -1.451  -12.400 -30.368 1.00 21.29 ? 190 HIS A N     1 
ATOM   1361 C  CA    . HIS A 1 211 ? -0.346  -11.899 -31.209 1.00 22.56 ? 190 HIS A CA    1 
ATOM   1362 C  C     . HIS A 1 211 ? 0.968   -12.176 -30.480 1.00 21.46 ? 190 HIS A C     1 
ATOM   1363 O  O     . HIS A 1 211 ? 1.835   -12.812 -31.085 1.00 21.11 ? 190 HIS A O     1 
ATOM   1364 C  CB    . HIS A 1 211 ? -0.504  -10.410 -31.531 1.00 21.46 ? 190 HIS A CB    1 
ATOM   1365 C  CG    . HIS A 1 211 ? 0.327   -10.024 -32.690 1.00 23.62 ? 190 HIS A CG    1 
ATOM   1366 N  ND1   . HIS A 1 211 ? 0.594   -8.706  -32.994 1.00 24.52 ? 190 HIS A ND1   1 
ATOM   1367 C  CD2   . HIS A 1 211 ? 0.959   -10.787 -33.622 1.00 24.10 ? 190 HIS A CD2   1 
ATOM   1368 C  CE1   . HIS A 1 211 ? 1.358   -8.675  -34.085 1.00 26.11 ? 190 HIS A CE1   1 
ATOM   1369 N  NE2   . HIS A 1 211 ? 1.579   -9.938  -34.497 1.00 23.81 ? 190 HIS A NE2   1 
ATOM   1370 N  N     . SER A 1 212 ? 1.051   -11.766 -29.213 1.00 19.76 ? 191 SER A N     1 
ATOM   1371 C  CA    . SER A 1 212 ? 2.256   -11.875 -28.355 1.00 20.50 ? 191 SER A CA    1 
ATOM   1372 C  C     . SER A 1 212 ? 2.753   -13.322 -28.284 1.00 20.59 ? 191 SER A C     1 
ATOM   1373 O  O     . SER A 1 212 ? 4.002   -13.541 -28.175 1.00 19.51 ? 191 SER A O     1 
ATOM   1374 C  CB    . SER A 1 212 ? 1.968   -11.347 -26.975 1.00 20.17 ? 191 SER A CB    1 
ATOM   1375 O  OG    . SER A 1 212 ? 3.124   -11.315 -26.168 1.00 17.78 ? 191 SER A OG    1 
ATOM   1376 N  N     . ALA A 1 213 ? 1.827   -14.274 -28.289 1.00 20.10 ? 192 ALA A N     1 
ATOM   1377 C  CA    . ALA A 1 213 ? 2.159   -15.695 -28.081 1.00 20.99 ? 192 ALA A CA    1 
ATOM   1378 C  C     . ALA A 1 213 ? 2.426   -16.369 -29.432 1.00 20.72 ? 192 ALA A C     1 
ATOM   1379 O  O     . ALA A 1 213 ? 2.971   -17.509 -29.430 1.00 18.97 ? 192 ALA A O     1 
ATOM   1380 C  CB    . ALA A 1 213 ? 1.042   -16.356 -27.310 1.00 20.61 ? 192 ALA A CB    1 
ATOM   1381 N  N     . GLY A 1 214 ? 2.048   -15.721 -30.536 1.00 20.92 ? 193 GLY A N     1 
ATOM   1382 C  CA    . GLY A 1 214 ? 2.097   -16.341 -31.886 1.00 23.04 ? 193 GLY A CA    1 
ATOM   1383 C  C     . GLY A 1 214 ? 0.857   -17.184 -32.229 1.00 23.12 ? 193 GLY A C     1 
ATOM   1384 O  O     . GLY A 1 214 ? 1.016   -18.169 -32.990 1.00 25.59 ? 193 GLY A O     1 
ATOM   1385 N  N     . GLY A 1 215 ? -0.326  -16.850 -31.703 1.00 23.04 ? 194 GLY A N     1 
ATOM   1386 C  CA    . GLY A 1 215 ? -1.615  -17.436 -32.128 1.00 24.35 ? 194 GLY A CA    1 
ATOM   1387 C  C     . GLY A 1 215 ? -2.250  -18.370 -31.100 1.00 27.91 ? 194 GLY A C     1 
ATOM   1388 O  O     . GLY A 1 215 ? -1.587  -18.756 -30.085 1.00 24.83 ? 194 GLY A O     1 
ATOM   1389 N  N     . TRP A 1 216 ? -3.503  -18.752 -31.368 1.00 28.47 ? 195 TRP A N     1 
ATOM   1390 C  CA    . TRP A 1 216 ? -4.423  -19.419 -30.411 1.00 30.60 ? 195 TRP A CA    1 
ATOM   1391 C  C     . TRP A 1 216 ? -3.910  -20.813 -30.025 1.00 30.40 ? 195 TRP A C     1 
ATOM   1392 O  O     . TRP A 1 216 ? -3.922  -21.141 -28.813 1.00 27.69 ? 195 TRP A O     1 
ATOM   1393 C  CB    . TRP A 1 216 ? -5.834  -19.499 -31.001 1.00 32.18 ? 195 TRP A CB    1 
ATOM   1394 C  CG    . TRP A 1 216 ? -6.804  -19.973 -29.972 1.00 29.17 ? 195 TRP A CG    1 
ATOM   1395 C  CD1   . TRP A 1 216 ? -7.441  -21.180 -29.909 1.00 27.00 ? 195 TRP A CD1   1 
ATOM   1396 C  CD2   . TRP A 1 216 ? -7.186  -19.238 -28.798 1.00 25.88 ? 195 TRP A CD2   1 
ATOM   1397 N  NE1   . TRP A 1 216 ? -8.194  -21.239 -28.769 1.00 26.58 ? 195 TRP A NE1   1 
ATOM   1398 C  CE2   . TRP A 1 216 ? -8.057  -20.063 -28.069 1.00 27.17 ? 195 TRP A CE2   1 
ATOM   1399 C  CE3   . TRP A 1 216 ? -6.862  -17.982 -28.293 1.00 26.12 ? 195 TRP A CE3   1 
ATOM   1400 C  CZ2   . TRP A 1 216 ? -8.641  -19.639 -26.877 1.00 29.41 ? 195 TRP A CZ2   1 
ATOM   1401 C  CZ3   . TRP A 1 216 ? -7.432  -17.568 -27.114 1.00 27.30 ? 195 TRP A CZ3   1 
ATOM   1402 C  CH2   . TRP A 1 216 ? -8.325  -18.380 -26.420 1.00 27.03 ? 195 TRP A CH2   1 
ATOM   1403 N  N     . SER A 1 217 ? -3.458  -21.584 -31.015 1.00 29.31 ? 196 SER A N     1 
ATOM   1404 C  CA    . SER A 1 217 ? -2.902  -22.954 -30.856 1.00 31.98 ? 196 SER A CA    1 
ATOM   1405 C  C     . SER A 1 217 ? -1.590  -22.909 -30.042 1.00 30.04 ? 196 SER A C     1 
ATOM   1406 O  O     . SER A 1 217 ? -1.283  -23.861 -29.316 1.00 24.86 ? 196 SER A O     1 
ATOM   1407 C  CB    . SER A 1 217 ? -2.717  -23.591 -32.218 1.00 34.47 ? 196 SER A CB    1 
ATOM   1408 O  OG    . SER A 1 217 ? -2.141  -22.653 -33.123 1.00 42.36 ? 196 SER A OG    1 
ATOM   1409 N  N     . LYS A 1 218 ? -0.826  -21.828 -30.179 1.00 28.83 ? 197 LYS A N     1 
ATOM   1410 C  CA    . LYS A 1 218 ? 0.375   -21.588 -29.354 1.00 28.07 ? 197 LYS A CA    1 
ATOM   1411 C  C     . LYS A 1 218 ? -0.037  -21.488 -27.871 1.00 27.85 ? 197 LYS A C     1 
ATOM   1412 O  O     . LYS A 1 218 ? 0.656   -22.106 -27.000 1.00 23.79 ? 197 LYS A O     1 
ATOM   1413 C  CB    . LYS A 1 218 ? 1.146   -20.402 -29.942 1.00 28.47 ? 197 LYS A CB    1 
ATOM   1414 C  CG    . LYS A 1 218 ? 2.233   -20.800 -30.941 1.00 29.81 ? 197 LYS A CG    1 
ATOM   1415 C  CD    . LYS A 1 218 ? 3.458   -21.418 -30.224 1.00 34.89 ? 197 LYS A CD    1 
ATOM   1416 C  CE    . LYS A 1 218 ? 4.412   -22.208 -31.099 1.00 36.50 ? 197 LYS A CE    1 
ATOM   1417 N  NZ    . LYS A 1 218 ? 5.252   -21.331 -31.943 1.00 34.93 ? 197 LYS A NZ    1 
ATOM   1418 N  N     . LEU A 1 219 ? -1.146  -20.817 -27.560 1.00 23.38 ? 198 LEU A N     1 
ATOM   1419 C  CA    . LEU A 1 219 ? -1.570  -20.697 -26.148 1.00 23.36 ? 198 LEU A CA    1 
ATOM   1420 C  C     . LEU A 1 219 ? -2.204  -22.004 -25.627 1.00 24.41 ? 198 LEU A C     1 
ATOM   1421 O  O     . LEU A 1 219 ? -1.959  -22.339 -24.473 1.00 24.63 ? 198 LEU A O     1 
ATOM   1422 C  CB    . LEU A 1 219 ? -2.555  -19.543 -26.039 1.00 22.61 ? 198 LEU A CB    1 
ATOM   1423 C  CG    . LEU A 1 219 ? -2.037  -18.166 -26.401 1.00 21.23 ? 198 LEU A CG    1 
ATOM   1424 C  CD1   . LEU A 1 219 ? -3.213  -17.215 -26.529 1.00 22.29 ? 198 LEU A CD1   1 
ATOM   1425 C  CD2   . LEU A 1 219 ? -1.056  -17.644 -25.374 1.00 22.03 ? 198 LEU A CD2   1 
ATOM   1426 N  N     . THR A 1 220 ? -2.951  -22.748 -26.458 1.00 25.33 ? 199 THR A N     1 
ATOM   1427 C  CA    . THR A 1 220 ? -3.884  -23.824 -26.027 1.00 23.35 ? 199 THR A CA    1 
ATOM   1428 C  C     . THR A 1 220 ? -3.268  -25.225 -26.161 1.00 25.54 ? 199 THR A C     1 
ATOM   1429 O  O     . THR A 1 220 ? -3.733  -26.133 -25.409 1.00 23.71 ? 199 THR A O     1 
ATOM   1430 C  CB    . THR A 1 220 ? -5.198  -23.803 -26.821 1.00 22.44 ? 199 THR A CB    1 
ATOM   1431 O  OG1   . THR A 1 220 ? -4.967  -24.047 -28.207 1.00 24.19 ? 199 THR A OG1   1 
ATOM   1432 C  CG2   . THR A 1 220 ? -5.953  -22.506 -26.663 1.00 21.93 ? 199 THR A CG2   1 
ATOM   1433 N  N     . ASP A 1 221 ? -2.316  -25.438 -27.074 1.00 24.59 ? 200 ASP A N     1 
ATOM   1434 C  CA    . ASP A 1 221 ? -1.913  -26.821 -27.434 1.00 28.59 ? 200 ASP A CA    1 
ATOM   1435 C  C     . ASP A 1 221 ? -0.831  -27.256 -26.465 1.00 28.69 ? 200 ASP A C     1 
ATOM   1436 O  O     . ASP A 1 221 ? -0.071  -26.395 -26.043 1.00 28.53 ? 200 ASP A O     1 
ATOM   1437 C  CB    . ASP A 1 221 ? -1.350  -26.976 -28.852 1.00 32.44 ? 200 ASP A CB    1 
ATOM   1438 C  CG    . ASP A 1 221 ? -2.315  -26.691 -29.997 1.00 34.75 ? 200 ASP A CG    1 
ATOM   1439 O  OD1   . ASP A 1 221 ? -3.539  -26.616 -29.729 1.00 37.73 ? 200 ASP A OD1   1 
ATOM   1440 O  OD2   . ASP A 1 221 ? -1.821  -26.518 -31.156 1.00 34.20 ? 200 ASP A OD2   1 
ATOM   1441 N  N     . THR A 1 222 ? -0.737  -28.561 -26.240 1.00 27.68 ? 201 THR A N     1 
ATOM   1442 C  CA    . THR A 1 222 ? 0.382   -29.260 -25.567 1.00 27.35 ? 201 THR A CA    1 
ATOM   1443 C  C     . THR A 1 222 ? 1.530   -29.427 -26.584 1.00 27.56 ? 201 THR A C     1 
ATOM   1444 O  O     . THR A 1 222 ? 2.490   -28.627 -26.552 1.00 24.97 ? 201 THR A O     1 
ATOM   1445 C  CB    . THR A 1 222 ? -0.168  -30.561 -24.957 1.00 27.39 ? 201 THR A CB    1 
ATOM   1446 O  OG1   . THR A 1 222 ? -1.312  -30.166 -24.193 1.00 26.68 ? 201 THR A OG1   1 
ATOM   1447 C  CG2   . THR A 1 222 ? 0.841   -31.326 -24.118 1.00 25.87 ? 201 THR A CG2   1 
ATOM   1448 N  N     . GLU A 1 223 ? 1.435   -30.417 -27.471 1.00 30.24 ? 202 GLU A N     1 
ATOM   1449 C  CA    . GLU A 1 223 ? 2.450   -30.686 -28.503 1.00 33.56 ? 202 GLU A CA    1 
ATOM   1450 C  C     . GLU A 1 223 ? 2.387   -29.496 -29.465 1.00 31.93 ? 202 GLU A C     1 
ATOM   1451 O  O     . GLU A 1 223 ? 1.289   -29.201 -29.958 1.00 33.76 ? 202 GLU A O     1 
ATOM   1452 C  CB    . GLU A 1 223 ? 2.229   -32.059 -29.159 1.00 41.32 ? 202 GLU A CB    1 
ATOM   1453 C  CG    . GLU A 1 223 ? 3.345   -32.444 -30.144 1.00 49.92 ? 202 GLU A CG    1 
ATOM   1454 C  CD    . GLU A 1 223 ? 3.781   -33.911 -30.225 1.00 58.64 ? 202 GLU A CD    1 
ATOM   1455 O  OE1   . GLU A 1 223 ? 4.952   -34.201 -29.856 1.00 59.51 ? 202 GLU A OE1   1 
ATOM   1456 O  OE2   . GLU A 1 223 ? 2.973   -34.770 -30.695 1.00 56.06 ? 202 GLU A OE2   1 
ATOM   1457 N  N     . GLY A 1 224 ? 3.510   -28.798 -29.652 1.00 30.73 ? 203 GLY A N     1 
ATOM   1458 C  CA    . GLY A 1 224 ? 3.616   -27.560 -30.448 1.00 28.97 ? 203 GLY A CA    1 
ATOM   1459 C  C     . GLY A 1 224 ? 3.095   -26.334 -29.716 1.00 28.14 ? 203 GLY A C     1 
ATOM   1460 O  O     . GLY A 1 224 ? 3.041   -25.270 -30.357 1.00 30.89 ? 203 GLY A O     1 
ATOM   1461 N  N     . GLY A 1 225 ? 2.759   -26.443 -28.421 1.00 28.68 ? 204 GLY A N     1 
ATOM   1462 C  CA    . GLY A 1 225 ? 2.129   -25.347 -27.649 1.00 27.31 ? 204 GLY A CA    1 
ATOM   1463 C  C     . GLY A 1 225 ? 2.822   -25.014 -26.321 1.00 23.90 ? 204 GLY A C     1 
ATOM   1464 O  O     . GLY A 1 225 ? 3.851   -25.640 -25.982 1.00 21.90 ? 204 GLY A O     1 
ATOM   1465 N  N     . ALA A 1 226 ? 2.234   -24.064 -25.577 1.00 20.27 ? 205 ALA A N     1 
ATOM   1466 C  CA    . ALA A 1 226 ? 2.748   -23.514 -24.306 1.00 18.80 ? 205 ALA A CA    1 
ATOM   1467 C  C     . ALA A 1 226 ? 2.835   -24.625 -23.234 1.00 18.87 ? 205 ALA A C     1 
ATOM   1468 O  O     . ALA A 1 226 ? 3.654   -24.474 -22.311 1.00 16.51 ? 205 ALA A O     1 
ATOM   1469 C  CB    . ALA A 1 226 ? 1.884   -22.366 -23.866 1.00 18.19 ? 205 ALA A CB    1 
ATOM   1470 N  N     . GLN A 1 227 ? 2.100   -25.733 -23.378 1.00 18.21 ? 206 GLN A N     1 
ATOM   1471 C  CA    . GLN A 1 227 ? 2.092   -26.804 -22.355 1.00 19.38 ? 206 GLN A CA    1 
ATOM   1472 C  C     . GLN A 1 227 ? 2.926   -27.994 -22.815 1.00 19.97 ? 206 GLN A C     1 
ATOM   1473 O  O     . GLN A 1 227 ? 2.759   -29.105 -22.221 1.00 21.05 ? 206 GLN A O     1 
ATOM   1474 C  CB    . GLN A 1 227 ? 0.656   -27.185 -21.989 1.00 18.11 ? 206 GLN A CB    1 
ATOM   1475 C  CG    . GLN A 1 227 ? -0.003  -26.167 -21.083 1.00 18.82 ? 206 GLN A CG    1 
ATOM   1476 C  CD    . GLN A 1 227 ? -0.484  -24.948 -21.831 1.00 20.47 ? 206 GLN A CD    1 
ATOM   1477 O  OE1   . GLN A 1 227 ? -1.228  -25.054 -22.811 1.00 22.40 ? 206 GLN A OE1   1 
ATOM   1478 N  NE2   . GLN A 1 227 ? -0.109  -23.778 -21.337 1.00 18.91 ? 206 GLN A NE2   1 
ATOM   1479 N  N     . GLN A 1 228 ? 3.858   -27.787 -23.748 1.00 21.95 ? 207 GLN A N     1 
ATOM   1480 C  CA    . GLN A 1 228 ? 4.654   -28.908 -24.318 1.00 22.42 ? 207 GLN A CA    1 
ATOM   1481 C  C     . GLN A 1 228 ? 5.600   -29.533 -23.274 1.00 23.27 ? 207 GLN A C     1 
ATOM   1482 O  O     . GLN A 1 228 ? 5.653   -30.789 -23.183 1.00 23.35 ? 207 GLN A O     1 
ATOM   1483 C  CB    . GLN A 1 228 ? 5.511   -28.463 -25.496 1.00 22.88 ? 207 GLN A CB    1 
ATOM   1484 C  CG    . GLN A 1 228 ? 6.015   -29.665 -26.282 1.00 22.47 ? 207 GLN A CG    1 
ATOM   1485 C  CD    . GLN A 1 228 ? 6.769   -29.250 -27.525 1.00 23.75 ? 207 GLN A CD    1 
ATOM   1486 O  OE1   . GLN A 1 228 ? 6.184   -28.880 -28.534 1.00 23.39 ? 207 GLN A OE1   1 
ATOM   1487 N  NE2   . GLN A 1 228 ? 8.092   -29.286 -27.447 1.00 22.40 ? 207 GLN A NE2   1 
ATOM   1488 N  N     . ASP A 1 229 ? 6.392   -28.727 -22.562 1.00 21.00 ? 208 ASP A N     1 
ATOM   1489 C  CA    . ASP A 1 229 ? 7.507   -29.287 -21.753 1.00 21.79 ? 208 ASP A CA    1 
ATOM   1490 C  C     . ASP A 1 229 ? 7.504   -28.727 -20.335 1.00 22.00 ? 208 ASP A C     1 
ATOM   1491 O  O     . ASP A 1 229 ? 6.894   -27.664 -20.117 1.00 22.98 ? 208 ASP A O     1 
ATOM   1492 C  CB    . ASP A 1 229 ? 8.869   -29.089 -22.425 1.00 21.78 ? 208 ASP A CB    1 
ATOM   1493 C  CG    . ASP A 1 229 ? 9.014   -29.913 -23.693 1.00 21.53 ? 208 ASP A CG    1 
ATOM   1494 O  OD1   . ASP A 1 229 ? 8.827   -31.138 -23.629 1.00 21.66 ? 208 ASP A OD1   1 
ATOM   1495 O  OD2   . ASP A 1 229 ? 9.227   -29.303 -24.743 1.00 21.60 ? 208 ASP A OD2   1 
ATOM   1496 N  N     . ARG A 1 230 ? 8.119   -29.495 -19.428 1.00 20.69 ? 209 ARG A N     1 
ATOM   1497 C  CA    . ARG A 1 230 ? 8.312   -29.191 -17.993 1.00 19.36 ? 209 ARG A CA    1 
ATOM   1498 C  C     . ARG A 1 230 ? 9.816   -29.237 -17.740 1.00 19.92 ? 209 ARG A C     1 
ATOM   1499 O  O     . ARG A 1 230 ? 10.548  -29.733 -18.624 1.00 16.15 ? 209 ARG A O     1 
ATOM   1500 C  CB    . ARG A 1 230 ? 7.628   -30.252 -17.127 1.00 19.64 ? 209 ARG A CB    1 
ATOM   1501 C  CG    . ARG A 1 230 ? 6.117   -30.382 -17.287 1.00 19.59 ? 209 ARG A CG    1 
ATOM   1502 C  CD    . ARG A 1 230 ? 5.265   -29.644 -16.261 1.00 20.31 ? 209 ARG A CD    1 
ATOM   1503 N  NE    . ARG A 1 230 ? 5.837   -29.552 -14.919 1.00 19.19 ? 209 ARG A NE    1 
ATOM   1504 C  CZ    . ARG A 1 230 ? 5.404   -30.181 -13.811 1.00 18.81 ? 209 ARG A CZ    1 
ATOM   1505 N  NH1   . ARG A 1 230 ? 4.351   -30.973 -13.860 1.00 19.01 ? 209 ARG A NH1   1 
ATOM   1506 N  NH2   . ARG A 1 230 ? 6.015   -29.983 -12.646 1.00 16.40 ? 209 ARG A NH2   1 
ATOM   1507 N  N     . LEU A 1 231 ? 10.262  -28.747 -16.579 1.00 21.48 ? 210 LEU A N     1 
ATOM   1508 C  CA    . LEU A 1 231 ? 11.691  -28.797 -16.155 1.00 21.98 ? 210 LEU A CA    1 
ATOM   1509 C  C     . LEU A 1 231 ? 11.850  -29.891 -15.087 1.00 22.75 ? 210 LEU A C     1 
ATOM   1510 O  O     . LEU A 1 231 ? 11.078  -29.881 -14.085 1.00 25.93 ? 210 LEU A O     1 
ATOM   1511 C  CB    . LEU A 1 231 ? 12.081  -27.407 -15.628 1.00 21.82 ? 210 LEU A CB    1 
ATOM   1512 C  CG    . LEU A 1 231 ? 11.732  -26.216 -16.533 1.00 21.03 ? 210 LEU A CG    1 
ATOM   1513 C  CD1   . LEU A 1 231 ? 12.290  -24.934 -15.963 1.00 20.52 ? 210 LEU A CD1   1 
ATOM   1514 C  CD2   . LEU A 1 231 ? 12.260  -26.373 -17.956 1.00 21.62 ? 210 LEU A CD2   1 
ATOM   1515 N  N     . VAL A 1 232 ? 12.772  -30.839 -15.282 1.00 23.89 ? 211 VAL A N     1 
ATOM   1516 C  CA    . VAL A 1 232 ? 13.171  -31.852 -14.240 1.00 20.84 ? 211 VAL A CA    1 
ATOM   1517 C  C     . VAL A 1 232 ? 13.582  -31.086 -12.983 1.00 19.09 ? 211 VAL A C     1 
ATOM   1518 O  O     . VAL A 1 232 ? 14.424  -30.176 -13.093 1.00 20.00 ? 211 VAL A O     1 
ATOM   1519 C  CB    . VAL A 1 232 ? 14.280  -32.819 -14.697 1.00 20.49 ? 211 VAL A CB    1 
ATOM   1520 C  CG1   . VAL A 1 232 ? 14.554  -33.864 -13.644 1.00 20.92 ? 211 VAL A CG1   1 
ATOM   1521 C  CG2   . VAL A 1 232 ? 13.966  -33.527 -16.007 1.00 21.33 ? 211 VAL A CG2   1 
ATOM   1522 N  N     . GLY A 1 233 ? 12.947  -31.397 -11.849 1.00 20.50 ? 212 GLY A N     1 
ATOM   1523 C  CA    . GLY A 1 233 ? 13.123  -30.724 -10.532 1.00 20.63 ? 212 GLY A CA    1 
ATOM   1524 C  C     . GLY A 1 233 ? 12.363  -29.409 -10.393 1.00 20.21 ? 212 GLY A C     1 
ATOM   1525 O  O     . GLY A 1 233 ? 12.556  -28.759 -9.361  1.00 23.83 ? 212 GLY A O     1 
ATOM   1526 N  N     . GLY A 1 234 ? 11.605  -28.969 -11.411 1.00 21.11 ? 213 GLY A N     1 
ATOM   1527 C  CA    . GLY A 1 234 ? 10.627  -27.857 -11.353 1.00 21.20 ? 213 GLY A CA    1 
ATOM   1528 C  C     . GLY A 1 234 ? 11.207  -26.501 -11.731 1.00 22.07 ? 213 GLY A C     1 
ATOM   1529 O  O     . GLY A 1 234 ? 12.415  -26.397 -11.983 1.00 22.66 ? 213 GLY A O     1 
ATOM   1530 N  N     . VAL A 1 235 ? 10.391  -25.446 -11.741 1.00 23.02 ? 214 VAL A N     1 
ATOM   1531 C  CA    . VAL A 1 235 ? 10.849  -24.120 -12.256 1.00 21.65 ? 214 VAL A CA    1 
ATOM   1532 C  C     . VAL A 1 235 ? 11.634  -23.350 -11.183 1.00 21.89 ? 214 VAL A C     1 
ATOM   1533 O  O     . VAL A 1 235 ? 12.550  -22.632 -11.595 1.00 23.16 ? 214 VAL A O     1 
ATOM   1534 C  CB    . VAL A 1 235 ? 9.690   -23.299 -12.849 1.00 21.12 ? 214 VAL A CB    1 
ATOM   1535 C  CG1   . VAL A 1 235 ? 10.151  -21.968 -13.411 1.00 21.03 ? 214 VAL A CG1   1 
ATOM   1536 C  CG2   . VAL A 1 235 ? 8.980   -24.086 -13.943 1.00 20.92 ? 214 VAL A CG2   1 
ATOM   1537 N  N     . GLN A 1 236 ? 11.305  -23.430 -9.884  1.00 21.37 ? 215 GLN A N     1 
ATOM   1538 C  CA    . GLN A 1 236 ? 11.909  -22.526 -8.863  1.00 21.60 ? 215 GLN A CA    1 
ATOM   1539 C  C     . GLN A 1 236 ? 13.435  -22.677 -8.845  1.00 22.44 ? 215 GLN A C     1 
ATOM   1540 O  O     . GLN A 1 236 ? 14.125  -21.695 -8.620  1.00 18.22 ? 215 GLN A O     1 
ATOM   1541 C  CB    . GLN A 1 236 ? 11.346  -22.738 -7.455  1.00 23.11 ? 215 GLN A CB    1 
ATOM   1542 C  CG    . GLN A 1 236 ? 11.972  -21.821 -6.410  1.00 23.24 ? 215 GLN A CG    1 
ATOM   1543 C  CD    . GLN A 1 236 ? 11.198  -21.716 -5.113  1.00 27.07 ? 215 GLN A CD    1 
ATOM   1544 O  OE1   . GLN A 1 236 ? 9.997   -21.985 -5.028  1.00 22.46 ? 215 GLN A OE1   1 
ATOM   1545 N  NE2   . GLN A 1 236 ? 11.900  -21.281 -4.073  1.00 29.85 ? 215 GLN A NE2   1 
ATOM   1546 N  N     . PRO A 1 237 ? 14.010  -23.899 -8.995  1.00 22.82 ? 216 PRO A N     1 
ATOM   1547 C  CA    . PRO A 1 237 ? 15.470  -24.059 -9.084  1.00 24.57 ? 216 PRO A CA    1 
ATOM   1548 C  C     . PRO A 1 237 ? 16.190  -23.285 -10.214 1.00 26.15 ? 216 PRO A C     1 
ATOM   1549 O  O     . PRO A 1 237 ? 17.331  -22.799 -10.003 1.00 22.35 ? 216 PRO A O     1 
ATOM   1550 C  CB    . PRO A 1 237 ? 15.645  -25.579 -9.233  1.00 24.19 ? 216 PRO A CB    1 
ATOM   1551 C  CG    . PRO A 1 237 ? 14.428  -26.142 -8.470  1.00 23.36 ? 216 PRO A CG    1 
ATOM   1552 C  CD    . PRO A 1 237 ? 13.306  -25.186 -8.859  1.00 22.48 ? 216 PRO A CD    1 
ATOM   1553 N  N     . LEU A 1 238 ? 15.539  -23.148 -11.368 1.00 24.80 ? 217 LEU A N     1 
ATOM   1554 C  CA    . LEU A 1 238 ? 16.090  -22.373 -12.509 1.00 24.49 ? 217 LEU A CA    1 
ATOM   1555 C  C     . LEU A 1 238 ? 16.270  -20.919 -12.066 1.00 25.01 ? 217 LEU A C     1 
ATOM   1556 O  O     . LEU A 1 238 ? 17.303  -20.341 -12.348 1.00 27.74 ? 217 LEU A O     1 
ATOM   1557 C  CB    . LEU A 1 238 ? 15.149  -22.472 -13.709 1.00 23.76 ? 217 LEU A CB    1 
ATOM   1558 C  CG    . LEU A 1 238 ? 15.676  -21.819 -14.989 1.00 23.89 ? 217 LEU A CG    1 
ATOM   1559 C  CD1   . LEU A 1 238 ? 17.050  -22.350 -15.343 1.00 24.67 ? 217 LEU A CD1   1 
ATOM   1560 C  CD2   . LEU A 1 238 ? 14.743  -22.033 -16.164 1.00 22.85 ? 217 LEU A CD2   1 
ATOM   1561 N  N     . ALA A 1 239 ? 15.305  -20.364 -11.346 1.00 24.31 ? 218 ALA A N     1 
ATOM   1562 C  CA    . ALA A 1 239 ? 15.378  -19.000 -10.781 1.00 23.38 ? 218 ALA A CA    1 
ATOM   1563 C  C     . ALA A 1 239 ? 16.530  -18.913 -9.770  1.00 21.71 ? 218 ALA A C     1 
ATOM   1564 O  O     . ALA A 1 239 ? 17.175  -17.866 -9.719  1.00 20.64 ? 218 ALA A O     1 
ATOM   1565 C  CB    . ALA A 1 239 ? 14.057  -18.622 -10.170 1.00 24.03 ? 218 ALA A CB    1 
ATOM   1566 N  N     . GLU A 1 240 ? 16.797  -19.978 -9.024  1.00 22.13 ? 219 GLU A N     1 
ATOM   1567 C  CA    . GLU A 1 240 ? 17.858  -20.004 -7.978  1.00 23.43 ? 219 GLU A CA    1 
ATOM   1568 C  C     . GLU A 1 240 ? 19.227  -19.993 -8.655  1.00 23.71 ? 219 GLU A C     1 
ATOM   1569 O  O     . GLU A 1 240 ? 20.135  -19.296 -8.182  1.00 25.86 ? 219 GLU A O     1 
ATOM   1570 C  CB    . GLU A 1 240 ? 17.664  -21.207 -7.046  1.00 24.88 ? 219 GLU A CB    1 
ATOM   1571 C  CG    . GLU A 1 240 ? 16.750  -20.872 -5.869  1.00 28.55 ? 219 GLU A CG    1 
ATOM   1572 C  CD    . GLU A 1 240 ? 15.956  -21.995 -5.225  1.00 28.83 ? 219 GLU A CD    1 
ATOM   1573 O  OE1   . GLU A 1 240 ? 15.057  -21.683 -4.415  1.00 29.46 ? 219 GLU A OE1   1 
ATOM   1574 O  OE2   . GLU A 1 240 ? 16.215  -23.172 -5.545  1.00 34.37 ? 219 GLU A OE2   1 
ATOM   1575 N  N     . ARG A 1 241 ? 19.372  -20.784 -9.706  1.00 25.21 ? 220 ARG A N     1 
ATOM   1576 C  CA    . ARG A 1 241 ? 20.593  -20.837 -10.540 1.00 24.38 ? 220 ARG A CA    1 
ATOM   1577 C  C     . ARG A 1 241 ? 20.849  -19.468 -11.165 1.00 23.83 ? 220 ARG A C     1 
ATOM   1578 O  O     . ARG A 1 241 ? 22.018  -19.055 -11.204 1.00 25.52 ? 220 ARG A O     1 
ATOM   1579 C  CB    . ARG A 1 241 ? 20.448  -21.913 -11.613 1.00 24.08 ? 220 ARG A CB    1 
ATOM   1580 C  CG    . ARG A 1 241 ? 20.446  -23.311 -11.033 1.00 26.95 ? 220 ARG A CG    1 
ATOM   1581 C  CD    . ARG A 1 241 ? 20.668  -24.369 -12.077 1.00 28.98 ? 220 ARG A CD    1 
ATOM   1582 N  NE    . ARG A 1 241 ? 20.499  -25.649 -11.436 1.00 31.79 ? 220 ARG A NE    1 
ATOM   1583 C  CZ    . ARG A 1 241 ? 20.699  -26.832 -12.008 1.00 34.02 ? 220 ARG A CZ    1 
ATOM   1584 N  NH1   . ARG A 1 241 ? 21.121  -26.915 -13.261 1.00 32.30 ? 220 ARG A NH1   1 
ATOM   1585 N  NH2   . ARG A 1 241 ? 20.509  -27.926 -11.285 1.00 32.68 ? 220 ARG A NH2   1 
ATOM   1586 N  N     . LEU A 1 242 ? 19.818  -18.814 -11.682 1.00 22.35 ? 221 LEU A N     1 
ATOM   1587 C  CA    . LEU A 1 242 ? 19.991  -17.438 -12.216 1.00 21.87 ? 221 LEU A CA    1 
ATOM   1588 C  C     . LEU A 1 242 ? 20.458  -16.539 -11.053 1.00 22.11 ? 221 LEU A C     1 
ATOM   1589 O  O     . LEU A 1 242 ? 21.361  -15.710 -11.266 1.00 22.76 ? 221 LEU A O     1 
ATOM   1590 C  CB    . LEU A 1 242 ? 18.690  -16.981 -12.891 1.00 19.19 ? 221 LEU A CB    1 
ATOM   1591 C  CG    . LEU A 1 242 ? 18.709  -15.569 -13.486 1.00 18.40 ? 221 LEU A CG    1 
ATOM   1592 C  CD1   . LEU A 1 242 ? 19.761  -15.423 -14.561 1.00 17.69 ? 221 LEU A CD1   1 
ATOM   1593 C  CD2   . LEU A 1 242 ? 17.362  -15.170 -14.050 1.00 17.76 ? 221 LEU A CD2   1 
ATOM   1594 N  N     . ALA A 1 243 ? 19.965  -16.742 -9.829  1.00 24.00 ? 222 ALA A N     1 
ATOM   1595 C  CA    . ALA A 1 243 ? 20.274  -15.837 -8.679  1.00 26.61 ? 222 ALA A CA    1 
ATOM   1596 C  C     . ALA A 1 243 ? 21.745  -16.009 -8.251  1.00 25.68 ? 222 ALA A C     1 
ATOM   1597 O  O     . ALA A 1 243 ? 22.341  -15.013 -7.762  1.00 23.80 ? 222 ALA A O     1 
ATOM   1598 C  CB    . ALA A 1 243 ? 19.328  -16.054 -7.500  1.00 27.04 ? 222 ALA A CB    1 
ATOM   1599 N  N     . ALA A 1 244 ? 22.310  -17.206 -8.448  1.00 23.09 ? 223 ALA A N     1 
ATOM   1600 C  CA    . ALA A 1 244 ? 23.703  -17.547 -8.070  1.00 24.24 ? 223 ALA A CA    1 
ATOM   1601 C  C     . ALA A 1 244 ? 24.701  -16.927 -9.068  1.00 23.87 ? 223 ALA A C     1 
ATOM   1602 O  O     . ALA A 1 244 ? 25.877  -16.994 -8.806  1.00 24.46 ? 223 ALA A O     1 
ATOM   1603 C  CB    . ALA A 1 244 ? 23.854  -19.053 -7.961  1.00 23.75 ? 223 ALA A CB    1 
ATOM   1604 N  N     . ARG A 1 245 ? 24.240  -16.324 -10.166 1.00 25.38 ? 224 ARG A N     1 
ATOM   1605 C  CA    . ARG A 1 245 ? 25.108  -15.568 -11.102 1.00 27.03 ? 224 ARG A CA    1 
ATOM   1606 C  C     . ARG A 1 245 ? 25.373  -14.173 -10.519 1.00 29.18 ? 224 ARG A C     1 
ATOM   1607 O  O     . ARG A 1 245 ? 26.152  -13.408 -11.109 1.00 30.27 ? 224 ARG A O     1 
ATOM   1608 C  CB    . ARG A 1 245 ? 24.450  -15.517 -12.481 1.00 30.36 ? 224 ARG A CB    1 
ATOM   1609 C  CG    . ARG A 1 245 ? 24.255  -16.885 -13.135 1.00 31.90 ? 224 ARG A CG    1 
ATOM   1610 C  CD    . ARG A 1 245 ? 25.549  -17.363 -13.729 1.00 33.07 ? 224 ARG A CD    1 
ATOM   1611 N  NE    . ARG A 1 245 ? 25.556  -18.757 -14.133 1.00 36.40 ? 224 ARG A NE    1 
ATOM   1612 C  CZ    . ARG A 1 245 ? 26.262  -19.219 -15.176 1.00 38.73 ? 224 ARG A CZ    1 
ATOM   1613 N  NH1   . ARG A 1 245 ? 26.941  -18.376 -15.929 1.00 41.56 ? 224 ARG A NH1   1 
ATOM   1614 N  NH2   . ARG A 1 245 ? 26.266  -20.502 -15.498 1.00 39.33 ? 224 ARG A NH2   1 
ATOM   1615 N  N     . LEU A 1 246 ? 24.709  -13.833 -9.417  1.00 28.89 ? 225 LEU A N     1 
ATOM   1616 C  CA    . LEU A 1 246 ? 24.891  -12.541 -8.724  1.00 28.16 ? 225 LEU A CA    1 
ATOM   1617 C  C     . LEU A 1 246 ? 25.971  -12.706 -7.663  1.00 27.53 ? 225 LEU A C     1 
ATOM   1618 O  O     . LEU A 1 246 ? 26.058  -13.756 -7.022  1.00 27.72 ? 225 LEU A O     1 
ATOM   1619 C  CB    . LEU A 1 246 ? 23.555  -12.091 -8.125  1.00 27.93 ? 225 LEU A CB    1 
ATOM   1620 C  CG    . LEU A 1 246 ? 22.460  -11.799 -9.151  1.00 28.81 ? 225 LEU A CG    1 
ATOM   1621 C  CD1   . LEU A 1 246 ? 21.117  -11.632 -8.478  1.00 27.57 ? 225 LEU A CD1   1 
ATOM   1622 C  CD2   . LEU A 1 246 ? 22.811  -10.565 -9.991  1.00 30.27 ? 225 LEU A CD2   1 
ATOM   1623 N  N     . PRO A 1 247 ? 26.831  -11.678 -7.455  1.00 26.69 ? 226 PRO A N     1 
ATOM   1624 C  CA    . PRO A 1 247 ? 27.846  -11.742 -6.409  1.00 27.27 ? 226 PRO A CA    1 
ATOM   1625 C  C     . PRO A 1 247 ? 27.120  -11.866 -5.059  1.00 27.31 ? 226 PRO A C     1 
ATOM   1626 O  O     . PRO A 1 247 ? 25.968  -11.425 -4.990  1.00 24.50 ? 226 PRO A O     1 
ATOM   1627 C  CB    . PRO A 1 247 ? 28.619  -10.423 -6.566  1.00 26.73 ? 226 PRO A CB    1 
ATOM   1628 C  CG    . PRO A 1 247 ? 27.621  -9.491  -7.211  1.00 25.73 ? 226 PRO A CG    1 
ATOM   1629 C  CD    . PRO A 1 247 ? 26.828  -10.377 -8.147  1.00 25.34 ? 226 PRO A CD    1 
ATOM   1630 N  N     . ASP A 1 248 ? 27.774  -12.479 -4.062  1.00 25.66 ? 227 ASP A N     1 
ATOM   1631 C  CA    . ASP A 1 248 ? 27.255  -12.580 -2.679  1.00 26.66 ? 227 ASP A CA    1 
ATOM   1632 C  C     . ASP A 1 248 ? 26.934  -11.159 -2.227  1.00 25.31 ? 227 ASP A C     1 
ATOM   1633 O  O     . ASP A 1 248 ? 27.714  -10.235 -2.609  1.00 26.35 ? 227 ASP A O     1 
ATOM   1634 C  CB    . ASP A 1 248 ? 28.271  -13.222 -1.734  1.00 28.54 ? 227 ASP A CB    1 
ATOM   1635 C  CG    . ASP A 1 248 ? 28.508  -14.699 -1.938  1.00 30.10 ? 227 ASP A CG    1 
ATOM   1636 O  OD1   . ASP A 1 248 ? 27.630  -15.387 -2.508  1.00 32.01 ? 227 ASP A OD1   1 
ATOM   1637 O  OD2   . ASP A 1 248 ? 29.582  -15.152 -1.537  1.00 40.35 ? 227 ASP A OD2   1 
ATOM   1638 N  N     . GLY A 1 249 ? 25.833  -10.982 -1.490  1.00 23.25 ? 228 GLY A N     1 
ATOM   1639 C  CA    . GLY A 1 249 ? 25.422  -9.683  -0.938  1.00 23.90 ? 228 GLY A CA    1 
ATOM   1640 C  C     . GLY A 1 249 ? 24.547  -8.886  -1.893  1.00 24.82 ? 228 GLY A C     1 
ATOM   1641 O  O     . GLY A 1 249 ? 23.980  -7.899  -1.437  1.00 25.27 ? 228 GLY A O     1 
ATOM   1642 N  N     . ALA A 1 250 ? 24.459  -9.246  -3.178  1.00 26.37 ? 229 ALA A N     1 
ATOM   1643 C  CA    . ALA A 1 250 ? 23.609  -8.549  -4.192  1.00 26.38 ? 229 ALA A CA    1 
ATOM   1644 C  C     . ALA A 1 250 ? 22.103  -8.796  -3.941  1.00 25.40 ? 229 ALA A C     1 
ATOM   1645 O  O     . ALA A 1 250 ? 21.301  -7.854  -4.045  1.00 25.38 ? 229 ALA A O     1 
ATOM   1646 C  CB    . ALA A 1 250 ? 24.006  -8.987  -5.581  1.00 25.48 ? 229 ALA A CB    1 
ATOM   1647 N  N     . LEU A 1 251 ? 21.726  -10.027 -3.599  1.00 26.31 ? 230 LEU A N     1 
ATOM   1648 C  CA    . LEU A 1 251 ? 20.321  -10.444 -3.336  1.00 24.75 ? 230 LEU A CA    1 
ATOM   1649 C  C     . LEU A 1 251 ? 19.979  -10.213 -1.863  1.00 24.97 ? 230 LEU A C     1 
ATOM   1650 O  O     . LEU A 1 251 ? 20.650  -10.852 -1.021  1.00 24.29 ? 230 LEU A O     1 
ATOM   1651 C  CB    . LEU A 1 251 ? 20.192  -11.927 -3.675  1.00 22.63 ? 230 LEU A CB    1 
ATOM   1652 C  CG    . LEU A 1 251 ? 18.841  -12.522 -3.332  1.00 24.73 ? 230 LEU A CG    1 
ATOM   1653 C  CD1   . LEU A 1 251 ? 17.745  -11.774 -4.086  1.00 26.20 ? 230 LEU A CD1   1 
ATOM   1654 C  CD2   . LEU A 1 251 ? 18.812  -14.015 -3.627  1.00 24.64 ? 230 LEU A CD2   1 
ATOM   1655 N  N     . ARG A 1 252 ? 18.962  -9.398  -1.564  1.00 24.24 ? 231 ARG A N     1 
ATOM   1656 C  CA    . ARG A 1 252 ? 18.421  -9.230  -0.178  1.00 24.84 ? 231 ARG A CA    1 
ATOM   1657 C  C     . ARG A 1 252 ? 17.026  -9.858  -0.095  1.00 24.16 ? 231 ARG A C     1 
ATOM   1658 O  O     . ARG A 1 252 ? 16.087  -9.288  -0.693  1.00 23.50 ? 231 ARG A O     1 
ATOM   1659 C  CB    . ARG A 1 252 ? 18.386  -7.764  0.279   1.00 25.14 ? 231 ARG A CB    1 
ATOM   1660 C  CG    . ARG A 1 252 ? 19.674  -6.977  0.033   1.00 25.86 ? 231 ARG A CG    1 
ATOM   1661 C  CD    . ARG A 1 252 ? 20.882  -7.526  0.781   1.00 25.57 ? 231 ARG A CD    1 
ATOM   1662 N  NE    . ARG A 1 252 ? 22.185  -6.988  0.367   1.00 25.68 ? 231 ARG A NE    1 
ATOM   1663 C  CZ    . ARG A 1 252 ? 22.653  -5.770  0.669   1.00 24.46 ? 231 ARG A CZ    1 
ATOM   1664 N  NH1   . ARG A 1 252 ? 21.911  -4.908  1.350   1.00 21.92 ? 231 ARG A NH1   1 
ATOM   1665 N  NH2   . ARG A 1 252 ? 23.858  -5.417  0.263   1.00 22.76 ? 231 ARG A NH2   1 
ATOM   1666 N  N     . LEU A 1 253 ? 16.889  -10.943 0.692   1.00 23.61 ? 232 LEU A N     1 
ATOM   1667 C  CA    . LEU A 1 253 ? 15.614  -11.689 0.889   1.00 21.36 ? 232 LEU A CA    1 
ATOM   1668 C  C     . LEU A 1 253 ? 14.837  -11.132 2.098   1.00 21.53 ? 232 LEU A C     1 
ATOM   1669 O  O     . LEU A 1 253 ? 15.417  -10.412 2.944   1.00 21.04 ? 232 LEU A O     1 
ATOM   1670 C  CB    . LEU A 1 253 ? 15.942  -13.181 1.018   1.00 20.65 ? 232 LEU A CB    1 
ATOM   1671 C  CG    . LEU A 1 253 ? 16.437  -13.812 -0.284  1.00 22.44 ? 232 LEU A CG    1 
ATOM   1672 C  CD1   . LEU A 1 253 ? 16.931  -15.226 -0.083  1.00 21.33 ? 232 LEU A CD1   1 
ATOM   1673 C  CD2   . LEU A 1 253 ? 15.363  -13.771 -1.376  1.00 22.66 ? 232 LEU A CD2   1 
ATOM   1674 N  N     . SER A 1 254 ? 13.544  -11.440 2.168   1.00 20.18 ? 233 SER A N     1 
ATOM   1675 C  CA    . SER A 1 254 ? 12.657  -11.010 3.260   1.00 20.33 ? 233 SER A CA    1 
ATOM   1676 C  C     . SER A 1 254 ? 12.830  -9.500  3.424   1.00 21.42 ? 233 SER A C     1 
ATOM   1677 O  O     . SER A 1 254 ? 12.846  -9.044  4.534   1.00 23.97 ? 233 SER A O     1 
ATOM   1678 C  CB    . SER A 1 254 ? 12.982  -11.750 4.539   1.00 21.77 ? 233 SER A CB    1 
ATOM   1679 O  OG    . SER A 1 254 ? 12.813  -13.148 4.396   1.00 21.15 ? 233 SER A OG    1 
ATOM   1680 N  N     . THR A 1 255 ? 12.945  -8.748  2.331   1.00 22.75 ? 234 THR A N     1 
ATOM   1681 C  CA    . THR A 1 255 ? 13.264  -7.298  2.344   1.00 22.13 ? 234 THR A CA    1 
ATOM   1682 C  C     . THR A 1 255 ? 12.278  -6.562  1.456   1.00 21.45 ? 234 THR A C     1 
ATOM   1683 O  O     . THR A 1 255 ? 12.656  -6.163  0.371   1.00 21.10 ? 234 THR A O     1 
ATOM   1684 C  CB    . THR A 1 255 ? 14.705  -7.044  1.891   1.00 21.46 ? 234 THR A CB    1 
ATOM   1685 O  OG1   . THR A 1 255 ? 15.557  -7.895  2.647   1.00 22.59 ? 234 THR A OG1   1 
ATOM   1686 C  CG2   . THR A 1 255 ? 15.146  -5.624  2.127   1.00 21.89 ? 234 THR A CG2   1 
ATOM   1687 N  N     . PRO A 1 256 ? 11.000  -6.401  1.888   1.00 22.72 ? 235 PRO A N     1 
ATOM   1688 C  CA    . PRO A 1 256 ? 9.969   -5.765  1.071   1.00 22.61 ? 235 PRO A CA    1 
ATOM   1689 C  C     . PRO A 1 256 ? 10.275  -4.287  0.834   1.00 23.45 ? 235 PRO A C     1 
ATOM   1690 O  O     . PRO A 1 256 ? 10.713  -3.619  1.774   1.00 23.60 ? 235 PRO A O     1 
ATOM   1691 C  CB    . PRO A 1 256 ? 8.650   -5.895  1.865   1.00 23.19 ? 235 PRO A CB    1 
ATOM   1692 C  CG    . PRO A 1 256 ? 8.943   -6.944  2.950   1.00 23.18 ? 235 PRO A CG    1 
ATOM   1693 C  CD    . PRO A 1 256 ? 10.446  -6.886  3.171   1.00 23.22 ? 235 PRO A CD    1 
ATOM   1694 N  N     . VAL A 1 257 ? 10.028  -3.795  -0.386  1.00 23.15 ? 236 VAL A N     1 
ATOM   1695 C  CA    . VAL A 1 257 ? 10.215  -2.349  -0.663  1.00 23.76 ? 236 VAL A CA    1 
ATOM   1696 C  C     . VAL A 1 257 ? 8.903   -1.641  -0.358  1.00 25.61 ? 236 VAL A C     1 
ATOM   1697 O  O     . VAL A 1 257 ? 7.893   -1.924  -1.043  1.00 26.28 ? 236 VAL A O     1 
ATOM   1698 C  CB    . VAL A 1 257 ? 10.764  -2.082  -2.069  1.00 23.67 ? 236 VAL A CB    1 
ATOM   1699 C  CG1   . VAL A 1 257 ? 10.785  -0.590  -2.388  1.00 23.92 ? 236 VAL A CG1   1 
ATOM   1700 C  CG2   . VAL A 1 257 ? 12.154  -2.674  -2.181  1.00 23.35 ? 236 VAL A CG2   1 
ATOM   1701 N  N     . ARG A 1 258 ? 8.931   -0.790  0.677   1.00 27.34 ? 237 ARG A N     1 
ATOM   1702 C  CA    . ARG A 1 258 ? 7.751   -0.031  1.154   1.00 30.25 ? 237 ARG A CA    1 
ATOM   1703 C  C     . ARG A 1 258 ? 7.676   1.301   0.414   1.00 26.94 ? 237 ARG A C     1 
ATOM   1704 O  O     . ARG A 1 258 ? 6.574   1.785   0.207   1.00 28.51 ? 237 ARG A O     1 
ATOM   1705 C  CB    . ARG A 1 258 ? 7.830   0.195   2.662   1.00 34.09 ? 237 ARG A CB    1 
ATOM   1706 C  CG    . ARG A 1 258 ? 7.533   -1.044  3.504   1.00 38.96 ? 237 ARG A CG    1 
ATOM   1707 C  CD    . ARG A 1 258 ? 7.153   -0.567  4.898   1.00 44.97 ? 237 ARG A CD    1 
ATOM   1708 N  NE    . ARG A 1 258 ? 7.414   -1.506  5.978   1.00 42.82 ? 237 ARG A NE    1 
ATOM   1709 C  CZ    . ARG A 1 258 ? 7.733   -1.166  7.221   1.00 43.71 ? 237 ARG A CZ    1 
ATOM   1710 N  NH1   . ARG A 1 258 ? 7.876   0.106   7.568   1.00 43.46 ? 237 ARG A NH1   1 
ATOM   1711 N  NH2   . ARG A 1 258 ? 7.944   -2.123  8.109   1.00 43.66 ? 237 ARG A NH2   1 
ATOM   1712 N  N     . GLY A 1 259 ? 8.814   1.881   0.068   1.00 26.52 ? 238 GLY A N     1 
ATOM   1713 C  CA    . GLY A 1 259 ? 8.866   3.269   -0.437  1.00 26.92 ? 238 GLY A CA    1 
ATOM   1714 C  C     . GLY A 1 259 ? 9.978   3.484   -1.435  1.00 23.28 ? 238 GLY A C     1 
ATOM   1715 O  O     . GLY A 1 259 ? 11.032  2.831   -1.290  1.00 20.81 ? 238 GLY A O     1 
ATOM   1716 N  N     . LEU A 1 260 ? 9.746   4.386   -2.394  1.00 25.79 ? 239 LEU A N     1 
ATOM   1717 C  CA    . LEU A 1 260 ? 10.681  4.682   -3.512  1.00 30.71 ? 239 LEU A CA    1 
ATOM   1718 C  C     . LEU A 1 260 ? 10.659  6.194   -3.808  1.00 33.15 ? 239 LEU A C     1 
ATOM   1719 O  O     . LEU A 1 260 ? 9.648   6.698   -4.417  1.00 34.25 ? 239 LEU A O     1 
ATOM   1720 C  CB    . LEU A 1 260 ? 10.279  3.806   -4.718  1.00 35.63 ? 239 LEU A CB    1 
ATOM   1721 C  CG    . LEU A 1 260 ? 11.272  3.691   -5.888  1.00 36.94 ? 239 LEU A CG    1 
ATOM   1722 C  CD1   . LEU A 1 260 ? 12.721  3.603   -5.428  1.00 39.03 ? 239 LEU A CD1   1 
ATOM   1723 C  CD2   . LEU A 1 260 ? 10.941  2.483   -6.750  1.00 37.03 ? 239 LEU A CD2   1 
ATOM   1724 N  N     . ALA A 1 261 ? 11.728  6.897   -3.386  1.00 30.88 ? 240 ALA A N     1 
ATOM   1725 C  CA    . ALA A 1 261 ? 11.906  8.362   -3.524  1.00 30.55 ? 240 ALA A CA    1 
ATOM   1726 C  C     . ALA A 1 261 ? 12.928  8.628   -4.619  1.00 32.36 ? 240 ALA A C     1 
ATOM   1727 O  O     . ALA A 1 261 ? 13.773  7.762   -4.865  1.00 37.30 ? 240 ALA A O     1 
ATOM   1728 C  CB    . ALA A 1 261 ? 12.331  9.003   -2.216  1.00 33.35 ? 240 ALA A CB    1 
ATOM   1729 N  N     . GLN A 1 262 ? 12.843  9.791   -5.256  1.00 31.48 ? 241 GLN A N     1 
ATOM   1730 C  CA    . GLN A 1 262 ? 13.715  10.130  -6.389  1.00 30.70 ? 241 GLN A CA    1 
ATOM   1731 C  C     . GLN A 1 262 ? 13.863  11.647  -6.502  1.00 32.98 ? 241 GLN A C     1 
ATOM   1732 O  O     . GLN A 1 262 ? 12.919  12.377  -6.240  1.00 32.27 ? 241 GLN A O     1 
ATOM   1733 C  CB    . GLN A 1 262 ? 13.171  9.463   -7.651  1.00 31.75 ? 241 GLN A CB    1 
ATOM   1734 C  CG    . GLN A 1 262 ? 12.139  10.266  -8.427  1.00 29.53 ? 241 GLN A CG    1 
ATOM   1735 C  CD    . GLN A 1 262 ? 12.002  9.723   -9.829  1.00 28.16 ? 241 GLN A CD    1 
ATOM   1736 O  OE1   . GLN A 1 262 ? 12.973  9.680   -10.581 1.00 28.37 ? 241 GLN A OE1   1 
ATOM   1737 N  NE2   . GLN A 1 262 ? 10.793  9.328   -10.211 1.00 25.92 ? 241 GLN A NE2   1 
ATOM   1738 N  N     . ASP A 1 263 ? 15.039  12.086  -6.930  1.00 38.48 ? 242 ASP A N     1 
ATOM   1739 C  CA    . ASP A 1 263 ? 15.333  13.493  -7.312  1.00 42.59 ? 242 ASP A CA    1 
ATOM   1740 C  C     . ASP A 1 263 ? 16.206  13.435  -8.571  1.00 45.54 ? 242 ASP A C     1 
ATOM   1741 O  O     . ASP A 1 263 ? 16.565  12.318  -8.985  1.00 46.36 ? 242 ASP A O     1 
ATOM   1742 C  CB    . ASP A 1 263 ? 16.021  14.232  -6.157  1.00 41.95 ? 242 ASP A CB    1 
ATOM   1743 C  CG    . ASP A 1 263 ? 17.267  13.516  -5.657  1.00 40.90 ? 242 ASP A CG    1 
ATOM   1744 O  OD1   . ASP A 1 263 ? 18.096  13.073  -6.502  1.00 38.84 ? 242 ASP A OD1   1 
ATOM   1745 O  OD2   . ASP A 1 263 ? 17.397  13.400  -4.431  1.00 47.37 ? 242 ASP A OD2   1 
ATOM   1746 N  N     . GLY A 1 264 ? 16.598  14.586  -9.113  1.00 45.93 ? 243 GLY A N     1 
ATOM   1747 C  CA    . GLY A 1 264 ? 17.479  14.667  -10.295 1.00 44.71 ? 243 GLY A CA    1 
ATOM   1748 C  C     . GLY A 1 264 ? 18.822  13.973  -10.109 1.00 41.02 ? 243 GLY A C     1 
ATOM   1749 O  O     . GLY A 1 264 ? 19.498  13.856  -11.109 1.00 39.64 ? 243 GLY A O     1 
ATOM   1750 N  N     . ASP A 1 265 ? 19.188  13.532  -8.894  1.00 41.86 ? 244 ASP A N     1 
ATOM   1751 C  CA    . ASP A 1 265 ? 20.508  12.912  -8.580  1.00 43.27 ? 244 ASP A CA    1 
ATOM   1752 C  C     . ASP A 1 265 ? 20.373  11.387  -8.451  1.00 40.03 ? 244 ASP A C     1 
ATOM   1753 O  O     . ASP A 1 265 ? 21.368  10.685  -8.703  1.00 37.26 ? 244 ASP A O     1 
ATOM   1754 C  CB    . ASP A 1 265 ? 21.122  13.471  -7.284  1.00 50.24 ? 244 ASP A CB    1 
ATOM   1755 C  CG    . ASP A 1 265 ? 21.810  14.831  -7.415  1.00 57.96 ? 244 ASP A CG    1 
ATOM   1756 O  OD1   . ASP A 1 265 ? 22.734  14.943  -8.245  1.00 58.72 ? 244 ASP A OD1   1 
ATOM   1757 O  OD2   . ASP A 1 265 ? 21.428  15.772  -6.668  1.00 58.85 ? 244 ASP A OD2   1 
ATOM   1758 N  N     . GLY A 1 266 ? 19.243  10.859  -7.982  1.00 34.40 ? 245 GLY A N     1 
ATOM   1759 C  CA    . GLY A 1 266 ? 19.151  9.397   -7.778  1.00 32.33 ? 245 GLY A CA    1 
ATOM   1760 C  C     . GLY A 1 266 ? 17.890  8.992   -7.057  1.00 30.71 ? 245 GLY A C     1 
ATOM   1761 O  O     . GLY A 1 266 ? 16.983  9.827   -6.993  1.00 27.54 ? 245 GLY A O     1 
ATOM   1762 N  N     . VAL A 1 267 ? 17.865  7.778   -6.495  1.00 29.74 ? 246 VAL A N     1 
ATOM   1763 C  CA    . VAL A 1 267 ? 16.634  7.183   -5.916  1.00 35.87 ? 246 VAL A CA    1 
ATOM   1764 C  C     . VAL A 1 267 ? 16.957  6.602   -4.540  1.00 36.24 ? 246 VAL A C     1 
ATOM   1765 O  O     . VAL A 1 267 ? 17.945  5.881   -4.422  1.00 44.53 ? 246 VAL A O     1 
ATOM   1766 C  CB    . VAL A 1 267 ? 16.034  6.094   -6.832  1.00 39.10 ? 246 VAL A CB    1 
ATOM   1767 C  CG1   . VAL A 1 267 ? 15.727  6.600   -8.232  1.00 36.93 ? 246 VAL A CG1   1 
ATOM   1768 C  CG2   . VAL A 1 267 ? 16.936  4.876   -6.897  1.00 46.27 ? 246 VAL A CG2   1 
ATOM   1769 N  N     . THR A 1 268 ? 16.094  6.875   -3.566  1.00 37.99 ? 247 THR A N     1 
ATOM   1770 C  CA    . THR A 1 268 ? 16.167  6.394   -2.166  1.00 39.91 ? 247 THR A CA    1 
ATOM   1771 C  C     . THR A 1 268 ? 15.094  5.315   -1.988  1.00 35.51 ? 247 THR A C     1 
ATOM   1772 O  O     . THR A 1 268 ? 13.905  5.616   -2.173  1.00 34.32 ? 247 THR A O     1 
ATOM   1773 C  CB    . THR A 1 268 ? 16.032  7.572   -1.183  1.00 40.31 ? 247 THR A CB    1 
ATOM   1774 O  OG1   . THR A 1 268 ? 17.186  8.400   -1.347  1.00 40.11 ? 247 THR A OG1   1 
ATOM   1775 C  CG2   . THR A 1 268 ? 15.921  7.145   0.266   1.00 38.05 ? 247 THR A CG2   1 
ATOM   1776 N  N     . VAL A 1 269 ? 15.514  4.094   -1.682  1.00 33.10 ? 248 VAL A N     1 
ATOM   1777 C  CA    . VAL A 1 269 ? 14.598  2.939   -1.479  1.00 33.33 ? 248 VAL A CA    1 
ATOM   1778 C  C     . VAL A 1 269 ? 14.505  2.691   0.021   1.00 31.12 ? 248 VAL A C     1 
ATOM   1779 O  O     . VAL A 1 269 ? 15.514  2.305   0.621   1.00 30.12 ? 248 VAL A O     1 
ATOM   1780 C  CB    . VAL A 1 269 ? 15.079  1.702   -2.257  1.00 32.54 ? 248 VAL A CB    1 
ATOM   1781 C  CG1   . VAL A 1 269 ? 14.005  0.634   -2.375  1.00 35.16 ? 248 VAL A CG1   1 
ATOM   1782 C  CG2   . VAL A 1 269 ? 15.562  2.094   -3.628  1.00 32.79 ? 248 VAL A CG2   1 
ATOM   1783 N  N     . ARG A 1 270 ? 13.341  2.979   0.591   1.00 33.56 ? 249 ARG A N     1 
ATOM   1784 C  CA    . ARG A 1 270 ? 13.016  2.720   2.017   1.00 34.02 ? 249 ARG A CA    1 
ATOM   1785 C  C     . ARG A 1 270 ? 12.435  1.308   2.131   1.00 35.83 ? 249 ARG A C     1 
ATOM   1786 O  O     . ARG A 1 270 ? 11.395  1.033   1.483   1.00 35.88 ? 249 ARG A O     1 
ATOM   1787 C  CB    . ARG A 1 270 ? 12.002  3.724   2.562   1.00 34.68 ? 249 ARG A CB    1 
ATOM   1788 C  CG    . ARG A 1 270 ? 11.587  3.431   3.996   1.00 38.82 ? 249 ARG A CG    1 
ATOM   1789 C  CD    . ARG A 1 270 ? 10.709  4.504   4.613   1.00 39.69 ? 249 ARG A CD    1 
ATOM   1790 N  NE    . ARG A 1 270 ? 9.531   4.766   3.813   1.00 41.24 ? 249 ARG A NE    1 
ATOM   1791 C  CZ    . ARG A 1 270 ? 8.388   4.091   3.877   1.00 44.37 ? 249 ARG A CZ    1 
ATOM   1792 N  NH1   . ARG A 1 270 ? 8.251   3.065   4.708   1.00 43.56 ? 249 ARG A NH1   1 
ATOM   1793 N  NH2   . ARG A 1 270 ? 7.385   4.449   3.083   1.00 43.34 ? 249 ARG A NH2   1 
ATOM   1794 N  N     . THR A 1 271 ? 13.125  0.444   2.879   1.00 35.38 ? 250 THR A N     1 
ATOM   1795 C  CA    . THR A 1 271 ? 12.612  -0.858  3.359   1.00 34.62 ? 250 THR A CA    1 
ATOM   1796 C  C     . THR A 1 271 ? 12.285  -0.692  4.840   1.00 35.26 ? 250 THR A C     1 
ATOM   1797 O  O     . THR A 1 271 ? 12.540  0.398   5.383   1.00 36.68 ? 250 THR A O     1 
ATOM   1798 C  CB    . THR A 1 271 ? 13.672  -1.943  3.178   1.00 29.78 ? 250 THR A CB    1 
ATOM   1799 O  OG1   . THR A 1 271 ? 14.615  -1.542  4.157   1.00 27.59 ? 250 THR A OG1   1 
ATOM   1800 C  CG2   . THR A 1 271 ? 14.323  -2.005  1.816   1.00 27.89 ? 250 THR A CG2   1 
ATOM   1801 N  N     . ALA A 1 272 ? 11.784  -1.739  5.480   1.00 37.99 ? 251 ALA A N     1 
ATOM   1802 C  CA    . ALA A 1 272 ? 11.712  -1.829  6.954   1.00 40.60 ? 251 ALA A CA    1 
ATOM   1803 C  C     . ALA A 1 272 ? 13.093  -2.285  7.440   1.00 42.50 ? 251 ALA A C     1 
ATOM   1804 O  O     . ALA A 1 272 ? 13.625  -3.303  6.902   1.00 37.54 ? 251 ALA A O     1 
ATOM   1805 C  CB    . ALA A 1 272 ? 10.621  -2.779  7.374   1.00 41.97 ? 251 ALA A CB    1 
ATOM   1806 N  N     . GLY A 1 273 ? 13.664  -1.534  8.382   1.00 41.75 ? 252 GLY A N     1 
ATOM   1807 C  CA    . GLY A 1 273 ? 15.028  -1.760  8.886   1.00 45.33 ? 252 GLY A CA    1 
ATOM   1808 C  C     . GLY A 1 273 ? 16.061  -1.659  7.776   1.00 46.88 ? 252 GLY A C     1 
ATOM   1809 O  O     . GLY A 1 273 ? 16.677  -2.701  7.456   1.00 41.48 ? 252 GLY A O     1 
ATOM   1810 N  N     . GLY A 1 274 ? 16.256  -0.448  7.226   1.00 50.11 ? 253 GLY A N     1 
ATOM   1811 C  CA    . GLY A 1 274 ? 17.281  -0.144  6.201   1.00 50.05 ? 253 GLY A CA    1 
ATOM   1812 C  C     . GLY A 1 274 ? 16.863  0.988   5.271   1.00 48.30 ? 253 GLY A C     1 
ATOM   1813 O  O     . GLY A 1 274 ? 15.692  1.392   5.281   1.00 55.83 ? 253 GLY A O     1 
ATOM   1814 N  N     . GLU A 1 275 ? 17.799  1.493   4.480   1.00 46.16 ? 254 GLU A N     1 
ATOM   1815 C  CA    . GLU A 1 275 ? 17.522  2.459   3.392   1.00 43.38 ? 254 GLU A CA    1 
ATOM   1816 C  C     . GLU A 1 275 ? 18.626  2.304   2.345   1.00 38.75 ? 254 GLU A C     1 
ATOM   1817 O  O     . GLU A 1 275 ? 19.788  2.387   2.720   1.00 38.33 ? 254 GLU A O     1 
ATOM   1818 C  CB    . GLU A 1 275 ? 17.453  3.881   3.952   1.00 47.42 ? 254 GLU A CB    1 
ATOM   1819 C  CG    . GLU A 1 275 ? 17.270  4.938   2.878   1.00 48.30 ? 254 GLU A CG    1 
ATOM   1820 C  CD    . GLU A 1 275 ? 16.832  6.300   3.393   1.00 49.32 ? 254 GLU A CD    1 
ATOM   1821 O  OE1   . GLU A 1 275 ? 15.608  6.592   3.345   1.00 58.28 ? 254 GLU A OE1   1 
ATOM   1822 O  OE2   . GLU A 1 275 ? 17.694  7.059   3.823   1.00 38.21 ? 254 GLU A OE2   1 
ATOM   1823 N  N     . VAL A 1 276 ? 18.259  2.063   1.088   1.00 37.88 ? 255 VAL A N     1 
ATOM   1824 C  CA    . VAL A 1 276 ? 19.209  1.817   -0.033  1.00 35.03 ? 255 VAL A CA    1 
ATOM   1825 C  C     . VAL A 1 276 ? 19.164  3.033   -0.963  1.00 35.46 ? 255 VAL A C     1 
ATOM   1826 O  O     . VAL A 1 276 ? 18.097  3.683   -1.071  1.00 34.74 ? 255 VAL A O     1 
ATOM   1827 C  CB    . VAL A 1 276 ? 18.859  0.512   -0.765  1.00 35.34 ? 255 VAL A CB    1 
ATOM   1828 C  CG1   . VAL A 1 276 ? 19.745  0.289   -1.974  1.00 37.59 ? 255 VAL A CG1   1 
ATOM   1829 C  CG2   . VAL A 1 276 ? 18.904  -0.689  0.170   1.00 35.44 ? 255 VAL A CG2   1 
ATOM   1830 N  N     . ARG A 1 277 ? 20.292  3.345   -1.587  1.00 33.10 ? 256 ARG A N     1 
ATOM   1831 C  CA    . ARG A 1 277 ? 20.470  4.601   -2.351  1.00 38.72 ? 256 ARG A CA    1 
ATOM   1832 C  C     . ARG A 1 277 ? 21.176  4.195   -3.646  1.00 38.52 ? 256 ARG A C     1 
ATOM   1833 O  O     . ARG A 1 277 ? 22.231  3.542   -3.512  1.00 37.44 ? 256 ARG A O     1 
ATOM   1834 C  CB    . ARG A 1 277 ? 21.209  5.621   -1.471  1.00 37.55 ? 256 ARG A CB    1 
ATOM   1835 C  CG    . ARG A 1 277 ? 21.568  6.929   -2.158  1.00 41.37 ? 256 ARG A CG    1 
ATOM   1836 C  CD    . ARG A 1 277 ? 20.358  7.639   -2.753  1.00 46.41 ? 256 ARG A CD    1 
ATOM   1837 N  NE    . ARG A 1 277 ? 20.677  8.927   -3.362  1.00 46.52 ? 256 ARG A NE    1 
ATOM   1838 C  CZ    . ARG A 1 277 ? 19.784  9.827   -3.782  1.00 50.55 ? 256 ARG A CZ    1 
ATOM   1839 N  NH1   . ARG A 1 277 ? 18.482  9.601   -3.679  1.00 51.43 ? 256 ARG A NH1   1 
ATOM   1840 N  NH2   . ARG A 1 277 ? 20.198  10.973  -4.295  1.00 51.38 ? 256 ARG A NH2   1 
ATOM   1841 N  N     . ALA A 1 278 ? 20.577  4.469   -4.822  1.00 33.31 ? 257 ALA A N     1 
ATOM   1842 C  CA    . ALA A 1 278 ? 21.140  4.099   -6.145  1.00 31.82 ? 257 ALA A CA    1 
ATOM   1843 C  C     . ALA A 1 278 ? 20.999  5.263   -7.122  1.00 31.59 ? 257 ALA A C     1 
ATOM   1844 O  O     . ALA A 1 278 ? 20.501  6.302   -6.709  1.00 34.21 ? 257 ALA A O     1 
ATOM   1845 C  CB    . ALA A 1 278 ? 20.469  2.872   -6.677  1.00 30.66 ? 257 ALA A CB    1 
ATOM   1846 N  N     . ARG A 1 279 ? 21.488  5.106   -8.350  1.00 35.86 ? 258 ARG A N     1 
ATOM   1847 C  CA    . ARG A 1 279 ? 21.233  6.085   -9.447  1.00 42.36 ? 258 ARG A CA    1 
ATOM   1848 C  C     . ARG A 1 279 ? 19.825  5.817   -10.002 1.00 40.29 ? 258 ARG A C     1 
ATOM   1849 O  O     . ARG A 1 279 ? 19.015  6.733   -9.886  1.00 41.85 ? 258 ARG A O     1 
ATOM   1850 C  CB    . ARG A 1 279 ? 22.301  6.045   -10.548 1.00 43.16 ? 258 ARG A CB    1 
ATOM   1851 C  CG    . ARG A 1 279 ? 23.620  6.696   -10.144 1.00 50.00 ? 258 ARG A CG    1 
ATOM   1852 C  CD    . ARG A 1 279 ? 24.842  5.964   -10.674 1.00 51.02 ? 258 ARG A CD    1 
ATOM   1853 N  NE    . ARG A 1 279 ? 25.354  6.446   -11.951 1.00 54.37 ? 258 ARG A NE    1 
ATOM   1854 C  CZ    . ARG A 1 279 ? 26.278  5.813   -12.682 1.00 57.59 ? 258 ARG A CZ    1 
ATOM   1855 N  NH1   . ARG A 1 279 ? 26.779  4.647   -12.294 1.00 54.15 ? 258 ARG A NH1   1 
ATOM   1856 N  NH2   . ARG A 1 279 ? 26.685  6.344   -13.822 1.00 60.52 ? 258 ARG A NH2   1 
ATOM   1857 N  N     . ARG A 1 280 ? 19.538  4.606   -10.519 1.00 34.07 ? 259 ARG A N     1 
ATOM   1858 C  CA    . ARG A 1 280 ? 18.212  4.260   -11.106 1.00 28.61 ? 259 ARG A CA    1 
ATOM   1859 C  C     . ARG A 1 280 ? 17.635  2.964   -10.511 1.00 29.40 ? 259 ARG A C     1 
ATOM   1860 O  O     . ARG A 1 280 ? 18.407  2.142   -9.937  1.00 24.83 ? 259 ARG A O     1 
ATOM   1861 C  CB    . ARG A 1 280 ? 18.355  4.139   -12.616 1.00 30.70 ? 259 ARG A CB    1 
ATOM   1862 C  CG    . ARG A 1 280 ? 18.322  5.491   -13.307 1.00 32.59 ? 259 ARG A CG    1 
ATOM   1863 C  CD    . ARG A 1 280 ? 18.811  5.429   -14.723 1.00 32.22 ? 259 ARG A CD    1 
ATOM   1864 N  NE    . ARG A 1 280 ? 19.100  6.800   -15.068 1.00 31.57 ? 259 ARG A NE    1 
ATOM   1865 C  CZ    . ARG A 1 280 ? 18.193  7.682   -15.430 1.00 33.03 ? 259 ARG A CZ    1 
ATOM   1866 N  NH1   . ARG A 1 280 ? 16.919  7.340   -15.545 1.00 36.72 ? 259 ARG A NH1   1 
ATOM   1867 N  NH2   . ARG A 1 280 ? 18.557  8.919   -15.686 1.00 34.28 ? 259 ARG A NH2   1 
ATOM   1868 N  N     . ALA A 1 281 ? 16.305  2.804   -10.626 1.00 24.89 ? 260 ALA A N     1 
ATOM   1869 C  CA    . ALA A 1 281 ? 15.551  1.653   -10.088 1.00 24.96 ? 260 ALA A CA    1 
ATOM   1870 C  C     . ALA A 1 281 ? 14.883  0.893   -11.222 1.00 23.59 ? 260 ALA A C     1 
ATOM   1871 O  O     . ALA A 1 281 ? 14.396  1.525   -12.167 1.00 26.65 ? 260 ALA A O     1 
ATOM   1872 C  CB    . ALA A 1 281 ? 14.539  2.069   -9.051  1.00 24.60 ? 260 ALA A CB    1 
ATOM   1873 N  N     . ILE A 1 282 ? 14.890  -0.429  -11.109 1.00 20.25 ? 261 ILE A N     1 
ATOM   1874 C  CA    . ILE A 1 282 ? 13.990  -1.306  -11.886 1.00 19.80 ? 261 ILE A CA    1 
ATOM   1875 C  C     . ILE A 1 282 ? 12.986  -1.943  -10.910 1.00 19.83 ? 261 ILE A C     1 
ATOM   1876 O  O     . ILE A 1 282 ? 13.381  -2.756  -10.053 1.00 21.37 ? 261 ILE A O     1 
ATOM   1877 C  CB    . ILE A 1 282 ? 14.809  -2.334  -12.688 1.00 19.61 ? 261 ILE A CB    1 
ATOM   1878 C  CG1   . ILE A 1 282 ? 15.829  -1.650  -13.622 1.00 20.72 ? 261 ILE A CG1   1 
ATOM   1879 C  CG2   . ILE A 1 282 ? 13.845  -3.248  -13.428 1.00 19.22 ? 261 ILE A CG2   1 
ATOM   1880 C  CD1   . ILE A 1 282 ? 16.669  -2.597  -14.505 1.00 19.12 ? 261 ILE A CD1   1 
ATOM   1881 N  N     . VAL A 1 283 ? 11.719  -1.581  -11.045 1.00 20.46 ? 262 VAL A N     1 
ATOM   1882 C  CA    . VAL A 1 283 ? 10.554  -2.195  -10.327 1.00 20.05 ? 262 VAL A CA    1 
ATOM   1883 C  C     . VAL A 1 283 ? 10.031  -3.334  -11.219 1.00 19.84 ? 262 VAL A C     1 
ATOM   1884 O  O     . VAL A 1 283 ? 9.514   -3.043  -12.283 1.00 20.88 ? 262 VAL A O     1 
ATOM   1885 C  CB    . VAL A 1 283 ? 9.487   -1.121  -10.019 1.00 19.69 ? 262 VAL A CB    1 
ATOM   1886 C  CG1   . VAL A 1 283 ? 8.244   -1.663  -9.310  1.00 18.45 ? 262 VAL A CG1   1 
ATOM   1887 C  CG2   . VAL A 1 283 ? 10.091  0.032   -9.220  1.00 20.03 ? 262 VAL A CG2   1 
ATOM   1888 N  N     . ALA A 1 284 ? 10.208  -4.584  -10.797 1.00 21.67 ? 263 ALA A N     1 
ATOM   1889 C  CA    . ALA A 1 284 ? 9.838   -5.821  -11.519 1.00 21.24 ? 263 ALA A CA    1 
ATOM   1890 C  C     . ALA A 1 284 ? 8.771   -6.624  -10.750 1.00 21.70 ? 263 ALA A C     1 
ATOM   1891 O  O     . ALA A 1 284 ? 8.860   -7.845  -10.717 1.00 21.21 ? 263 ALA A O     1 
ATOM   1892 C  CB    . ALA A 1 284 ? 11.101  -6.614  -11.726 1.00 22.05 ? 263 ALA A CB    1 
ATOM   1893 N  N     . VAL A 1 285 ? 7.766   -5.955  -10.178 1.00 25.00 ? 264 VAL A N     1 
ATOM   1894 C  CA    . VAL A 1 285 ? 6.634   -6.583  -9.429  1.00 23.59 ? 264 VAL A CA    1 
ATOM   1895 C  C     . VAL A 1 285 ? 5.368   -6.561  -10.297 1.00 23.26 ? 264 VAL A C     1 
ATOM   1896 O  O     . VAL A 1 285 ? 5.267   -5.826  -11.285 1.00 22.19 ? 264 VAL A O     1 
ATOM   1897 C  CB    . VAL A 1 285 ? 6.414   -5.875  -8.077  1.00 25.47 ? 264 VAL A CB    1 
ATOM   1898 C  CG1   . VAL A 1 285 ? 7.691   -5.809  -7.244  1.00 25.73 ? 264 VAL A CG1   1 
ATOM   1899 C  CG2   . VAL A 1 285 ? 5.838   -4.482  -8.251  1.00 26.43 ? 264 VAL A CG2   1 
ATOM   1900 N  N     . PRO A 1 286 ? 4.366   -7.398  -9.963  1.00 21.48 ? 265 PRO A N     1 
ATOM   1901 C  CA    . PRO A 1 286 ? 3.033   -7.284  -10.564 1.00 24.05 ? 265 PRO A CA    1 
ATOM   1902 C  C     . PRO A 1 286 ? 2.401   -5.882  -10.445 1.00 27.07 ? 265 PRO A C     1 
ATOM   1903 O  O     . PRO A 1 286 ? 2.543   -5.189  -9.416  1.00 27.04 ? 265 PRO A O     1 
ATOM   1904 C  CB    . PRO A 1 286 ? 2.216   -8.331  -9.791  1.00 24.58 ? 265 PRO A CB    1 
ATOM   1905 C  CG    . PRO A 1 286 ? 3.247   -9.318  -9.255  1.00 23.91 ? 265 PRO A CG    1 
ATOM   1906 C  CD    . PRO A 1 286 ? 4.489   -8.500  -9.001  1.00 21.44 ? 265 PRO A CD    1 
ATOM   1907 N  N     . PRO A 1 287 ? 1.764   -5.375  -11.531 1.00 28.14 ? 266 PRO A N     1 
ATOM   1908 C  CA    . PRO A 1 287 ? 1.325   -3.975  -11.593 1.00 27.50 ? 266 PRO A CA    1 
ATOM   1909 C  C     . PRO A 1 287 ? 0.642   -3.475  -10.311 1.00 26.29 ? 266 PRO A C     1 
ATOM   1910 O  O     . PRO A 1 287 ? 1.032   -2.429  -9.756  1.00 25.48 ? 266 PRO A O     1 
ATOM   1911 C  CB    . PRO A 1 287 ? 0.338   -4.014  -12.776 1.00 29.38 ? 266 PRO A CB    1 
ATOM   1912 C  CG    . PRO A 1 287 ? 0.879   -5.080  -13.712 1.00 26.43 ? 266 PRO A CG    1 
ATOM   1913 C  CD    . PRO A 1 287 ? 1.530   -6.091  -12.801 1.00 26.98 ? 266 PRO A CD    1 
ATOM   1914 N  N     . THR A 1 288 ? -0.339  -4.235  -9.825  1.00 26.04 ? 267 THR A N     1 
ATOM   1915 C  CA    . THR A 1 288 ? -1.137  -3.858  -8.632  1.00 26.28 ? 267 THR A CA    1 
ATOM   1916 C  C     . THR A 1 288 ? -0.210  -3.709  -7.420  1.00 25.53 ? 267 THR A C     1 
ATOM   1917 O  O     . THR A 1 288 ? -0.546  -2.854  -6.592  1.00 26.26 ? 267 THR A O     1 
ATOM   1918 C  CB    . THR A 1 288 ? -2.295  -4.814  -8.306  1.00 27.14 ? 267 THR A CB    1 
ATOM   1919 O  OG1   . THR A 1 288 ? -2.950  -4.145  -7.227  1.00 27.00 ? 267 THR A OG1   1 
ATOM   1920 C  CG2   . THR A 1 288 ? -1.883  -6.213  -7.889  1.00 26.32 ? 267 THR A CG2   1 
ATOM   1921 N  N     . LEU A 1 289 ? 0.865   -4.500  -7.310  1.00 24.17 ? 268 LEU A N     1 
ATOM   1922 C  CA    . LEU A 1 289 ? 1.869   -4.367  -6.217  1.00 26.36 ? 268 LEU A CA    1 
ATOM   1923 C  C     . LEU A 1 289 ? 2.788   -3.189  -6.525  1.00 24.88 ? 268 LEU A C     1 
ATOM   1924 O  O     . LEU A 1 289 ? 3.301   -2.576  -5.574  1.00 30.13 ? 268 LEU A O     1 
ATOM   1925 C  CB    . LEU A 1 289 ? 2.674   -5.658  -6.048  1.00 25.15 ? 268 LEU A CB    1 
ATOM   1926 C  CG    . LEU A 1 289 ? 1.855   -6.907  -5.717  1.00 28.93 ? 268 LEU A CG    1 
ATOM   1927 C  CD1   . LEU A 1 289 ? 2.718   -8.155  -5.727  1.00 30.29 ? 268 LEU A CD1   1 
ATOM   1928 C  CD2   . LEU A 1 289 ? 1.169   -6.788  -4.354  1.00 30.82 ? 268 LEU A CD2   1 
ATOM   1929 N  N     . ALA A 1 290 ? 2.991   -2.858  -7.789  1.00 21.48 ? 269 ALA A N     1 
ATOM   1930 C  CA    . ALA A 1 290 ? 3.876   -1.717  -8.138  1.00 24.56 ? 269 ALA A CA    1 
ATOM   1931 C  C     . ALA A 1 290 ? 3.290   -0.398  -7.600  1.00 23.81 ? 269 ALA A C     1 
ATOM   1932 O  O     . ALA A 1 290 ? 4.043   0.422   -7.124  1.00 25.51 ? 269 ALA A O     1 
ATOM   1933 C  CB    . ALA A 1 290 ? 4.129   -1.678  -9.630  1.00 24.07 ? 269 ALA A CB    1 
ATOM   1934 N  N     . GLY A 1 291 ? 1.977   -0.197  -7.689  1.00 26.92 ? 270 GLY A N     1 
ATOM   1935 C  CA    . GLY A 1 291 ? 1.296   1.044   -7.270  1.00 26.96 ? 270 GLY A CA    1 
ATOM   1936 C  C     . GLY A 1 291 ? 1.099   1.138   -5.769  1.00 29.17 ? 270 GLY A C     1 
ATOM   1937 O  O     . GLY A 1 291 ? 0.708   2.208   -5.326  1.00 30.36 ? 270 GLY A O     1 
ATOM   1938 N  N     . ARG A 1 292 ? 1.318   0.044   -5.026  1.00 27.09 ? 271 ARG A N     1 
ATOM   1939 C  CA    . ARG A 1 292 ? 1.234   -0.007  -3.557  1.00 26.41 ? 271 ARG A CA    1 
ATOM   1940 C  C     . ARG A 1 292 ? 2.480   0.650   -2.940  1.00 28.21 ? 271 ARG A C     1 
ATOM   1941 O  O     . ARG A 1 292 ? 2.400   1.063   -1.759  1.00 31.57 ? 271 ARG A O     1 
ATOM   1942 C  CB    . ARG A 1 292 ? 1.008   -1.459  -3.117  1.00 26.56 ? 271 ARG A CB    1 
ATOM   1943 C  CG    . ARG A 1 292 ? -0.418  -1.907  -3.378  1.00 29.02 ? 271 ARG A CG    1 
ATOM   1944 C  CD    . ARG A 1 292 ? -0.790  -3.284  -2.907  1.00 28.94 ? 271 ARG A CD    1 
ATOM   1945 N  NE    . ARG A 1 292 ? -1.706  -3.892  -3.870  1.00 29.83 ? 271 ARG A NE    1 
ATOM   1946 C  CZ    . ARG A 1 292 ? -2.618  -4.828  -3.603  1.00 29.36 ? 271 ARG A CZ    1 
ATOM   1947 N  NH1   . ARG A 1 292 ? -2.807  -5.225  -2.359  1.00 25.44 ? 271 ARG A NH1   1 
ATOM   1948 N  NH2   . ARG A 1 292 ? -3.354  -5.336  -4.590  1.00 28.46 ? 271 ARG A NH2   1 
ATOM   1949 N  N     . ILE A 1 293 ? 3.595   0.713   -3.673  1.00 27.43 ? 272 ILE A N     1 
ATOM   1950 C  CA    . ILE A 1 293 ? 4.859   1.351   -3.189  1.00 27.79 ? 272 ILE A CA    1 
ATOM   1951 C  C     . ILE A 1 293 ? 4.612   2.852   -2.942  1.00 30.51 ? 272 ILE A C     1 
ATOM   1952 O  O     . ILE A 1 293 ? 3.948   3.499   -3.788  1.00 27.01 ? 272 ILE A O     1 
ATOM   1953 C  CB    . ILE A 1 293 ? 6.003   1.131   -4.189  1.00 26.11 ? 272 ILE A CB    1 
ATOM   1954 C  CG1   . ILE A 1 293 ? 6.272   -0.353  -4.450  1.00 25.34 ? 272 ILE A CG1   1 
ATOM   1955 C  CG2   . ILE A 1 293 ? 7.258   1.861   -3.738  1.00 25.03 ? 272 ILE A CG2   1 
ATOM   1956 C  CD1   . ILE A 1 293 ? 7.138   -0.586  -5.673  1.00 23.90 ? 272 ILE A CD1   1 
ATOM   1957 N  N     . ASP A 1 294 ? 5.129   3.385   -1.828  1.00 30.04 ? 273 ASP A N     1 
ATOM   1958 C  CA    . ASP A 1 294 ? 5.123   4.840   -1.546  1.00 32.16 ? 273 ASP A CA    1 
ATOM   1959 C  C     . ASP A 1 294 ? 6.155   5.486   -2.481  1.00 32.85 ? 273 ASP A C     1 
ATOM   1960 O  O     . ASP A 1 294 ? 7.374   5.435   -2.209  1.00 32.42 ? 273 ASP A O     1 
ATOM   1961 C  CB    . ASP A 1 294 ? 5.373   5.136   -0.063  1.00 36.35 ? 273 ASP A CB    1 
ATOM   1962 C  CG    . ASP A 1 294 ? 5.197   6.605   0.302   1.00 37.26 ? 273 ASP A CG    1 
ATOM   1963 O  OD1   . ASP A 1 294 ? 4.294   7.259   -0.295  1.00 36.79 ? 273 ASP A OD1   1 
ATOM   1964 O  OD2   . ASP A 1 294 ? 5.948   7.087   1.179   1.00 37.02 ? 273 ASP A OD2   1 
ATOM   1965 N  N     . HIS A 1 295 ? 5.667   6.013   -3.594  1.00 34.54 ? 274 HIS A N     1 
ATOM   1966 C  CA    . HIS A 1 295 ? 6.454   6.738   -4.623  1.00 33.26 ? 274 HIS A CA    1 
ATOM   1967 C  C     . HIS A 1 295 ? 6.525   8.200   -4.214  1.00 30.77 ? 274 HIS A C     1 
ATOM   1968 O  O     . HIS A 1 295 ? 5.452   8.750   -3.915  1.00 28.64 ? 274 HIS A O     1 
ATOM   1969 C  CB    . HIS A 1 295 ? 5.802   6.554   -5.992  1.00 30.49 ? 274 HIS A CB    1 
ATOM   1970 C  CG    . HIS A 1 295 ? 5.934   5.167   -6.530  1.00 31.22 ? 274 HIS A CG    1 
ATOM   1971 N  ND1   . HIS A 1 295 ? 7.069   4.731   -7.184  1.00 30.52 ? 274 HIS A ND1   1 
ATOM   1972 C  CD2   . HIS A 1 295 ? 5.079   4.132   -6.540  1.00 30.56 ? 274 HIS A CD2   1 
ATOM   1973 C  CE1   . HIS A 1 295 ? 6.914   3.471   -7.524  1.00 30.19 ? 274 HIS A CE1   1 
ATOM   1974 N  NE2   . HIS A 1 295 ? 5.707   3.091   -7.155  1.00 29.59 ? 274 HIS A NE2   1 
ATOM   1975 N  N     . ASP A 1 296 ? 7.725   8.781   -4.212  1.00 32.69 ? 275 ASP A N     1 
ATOM   1976 C  CA    . ASP A 1 296 ? 7.932   10.239  -4.005  1.00 34.23 ? 275 ASP A CA    1 
ATOM   1977 C  C     . ASP A 1 296 ? 8.916   10.750  -5.050  1.00 33.85 ? 275 ASP A C     1 
ATOM   1978 O  O     . ASP A 1 296 ? 10.059  10.294  -5.062  1.00 35.16 ? 275 ASP A O     1 
ATOM   1979 C  CB    . ASP A 1 296 ? 8.434   10.556  -2.601  1.00 37.22 ? 275 ASP A CB    1 
ATOM   1980 C  CG    . ASP A 1 296 ? 8.351   12.030  -2.291  1.00 38.41 ? 275 ASP A CG    1 
ATOM   1981 O  OD1   . ASP A 1 296 ? 7.421   12.404  -1.570  1.00 50.28 ? 275 ASP A OD1   1 
ATOM   1982 O  OD2   . ASP A 1 296 ? 9.192   12.790  -2.797  1.00 42.47 ? 275 ASP A OD2   1 
ATOM   1983 N  N     . PRO A 1 297 ? 8.527   11.675  -5.968  1.00 30.72 ? 276 PRO A N     1 
ATOM   1984 C  CA    . PRO A 1 297 ? 7.192   12.263  -6.005  1.00 28.45 ? 276 PRO A CA    1 
ATOM   1985 C  C     . PRO A 1 297 ? 6.165   11.202  -6.361  1.00 27.44 ? 276 PRO A C     1 
ATOM   1986 O  O     . PRO A 1 297 ? 6.544   10.133  -6.831  1.00 23.10 ? 276 PRO A O     1 
ATOM   1987 C  CB    . PRO A 1 297 ? 7.201   13.284  -7.150  1.00 31.38 ? 276 PRO A CB    1 
ATOM   1988 C  CG    . PRO A 1 297 ? 8.672   13.395  -7.573  1.00 31.57 ? 276 PRO A CG    1 
ATOM   1989 C  CD    . PRO A 1 297 ? 9.358   12.137  -7.086  1.00 28.17 ? 276 PRO A CD    1 
ATOM   1990 N  N     . PRO A 1 298 ? 4.851   11.460  -6.130  1.00 30.75 ? 277 PRO A N     1 
ATOM   1991 C  CA    . PRO A 1 298 ? 3.797   10.522  -6.545  1.00 28.57 ? 277 PRO A CA    1 
ATOM   1992 C  C     . PRO A 1 298 ? 3.873   10.229  -8.051  1.00 28.91 ? 277 PRO A C     1 
ATOM   1993 O  O     . PRO A 1 298 ? 4.285   11.114  -8.797  1.00 28.22 ? 277 PRO A O     1 
ATOM   1994 C  CB    . PRO A 1 298 ? 2.498   11.250  -6.176  1.00 31.37 ? 277 PRO A CB    1 
ATOM   1995 C  CG    . PRO A 1 298 ? 2.904   12.264  -5.110  1.00 32.26 ? 277 PRO A CG    1 
ATOM   1996 C  CD    . PRO A 1 298 ? 4.328   12.653  -5.435  1.00 28.79 ? 277 PRO A CD    1 
ATOM   1997 N  N     . LEU A 1 299 ? 3.535   9.006   -8.475  1.00 28.53 ? 278 LEU A N     1 
ATOM   1998 C  CA    . LEU A 1 299 ? 3.550   8.619   -9.911  1.00 27.23 ? 278 LEU A CA    1 
ATOM   1999 C  C     . LEU A 1 299 ? 2.670   9.595   -10.677 1.00 28.60 ? 278 LEU A C     1 
ATOM   2000 O  O     . LEU A 1 299 ? 1.743   10.161  -10.088 1.00 30.48 ? 278 LEU A O     1 
ATOM   2001 C  CB    . LEU A 1 299 ? 3.006   7.203   -10.093 1.00 28.12 ? 278 LEU A CB    1 
ATOM   2002 C  CG    . LEU A 1 299 ? 3.824   6.067   -9.488  1.00 29.09 ? 278 LEU A CG    1 
ATOM   2003 C  CD1   . LEU A 1 299 ? 3.263   4.735   -9.948  1.00 29.40 ? 278 LEU A CD1   1 
ATOM   2004 C  CD2   . LEU A 1 299 ? 5.295   6.172   -9.857  1.00 30.32 ? 278 LEU A CD2   1 
ATOM   2005 N  N     . PRO A 1 300 ? 2.918   9.829   -11.990 1.00 28.24 ? 279 PRO A N     1 
ATOM   2006 C  CA    . PRO A 1 300 ? 1.986   10.599  -12.816 1.00 30.68 ? 279 PRO A CA    1 
ATOM   2007 C  C     . PRO A 1 300 ? 0.639   9.891   -12.777 1.00 29.08 ? 279 PRO A C     1 
ATOM   2008 O  O     . PRO A 1 300 ? 0.635   8.669   -12.653 1.00 30.82 ? 279 PRO A O     1 
ATOM   2009 C  CB    . PRO A 1 300 ? 2.632   10.616  -14.216 1.00 29.07 ? 279 PRO A CB    1 
ATOM   2010 C  CG    . PRO A 1 300 ? 4.095   10.372  -13.930 1.00 28.04 ? 279 PRO A CG    1 
ATOM   2011 C  CD    . PRO A 1 300 ? 4.107   9.419   -12.750 1.00 28.30 ? 279 PRO A CD    1 
ATOM   2012 N  N     . PRO A 1 301 ? -0.505  10.625  -12.824 1.00 28.88 ? 280 PRO A N     1 
ATOM   2013 C  CA    . PRO A 1 301 ? -1.851  10.047  -12.717 1.00 30.63 ? 280 PRO A CA    1 
ATOM   2014 C  C     . PRO A 1 301 ? -2.243  8.984   -13.760 1.00 29.84 ? 280 PRO A C     1 
ATOM   2015 O  O     . PRO A 1 301 ? -3.050  8.123   -13.436 1.00 29.99 ? 280 PRO A O     1 
ATOM   2016 C  CB    . PRO A 1 301 ? -2.800  11.252  -12.908 1.00 30.90 ? 280 PRO A CB    1 
ATOM   2017 C  CG    . PRO A 1 301 ? -1.946  12.332  -13.519 1.00 29.52 ? 280 PRO A CG    1 
ATOM   2018 C  CD    . PRO A 1 301 ? -0.575  12.085  -12.930 1.00 31.03 ? 280 PRO A CD    1 
ATOM   2019 N  N     . GLN A 1 302 ? -1.706  9.084   -14.980 1.00 30.29 ? 281 GLN A N     1 
ATOM   2020 C  CA    . GLN A 1 302 ? -2.036  8.152   -16.095 1.00 28.45 ? 281 GLN A CA    1 
ATOM   2021 C  C     . GLN A 1 302 ? -1.508  6.788   -15.682 1.00 27.89 ? 281 GLN A C     1 
ATOM   2022 O  O     . GLN A 1 302 ? -2.219  5.784   -15.933 1.00 27.58 ? 281 GLN A O     1 
ATOM   2023 C  CB    . GLN A 1 302 ? -1.450  8.623   -17.427 1.00 26.95 ? 281 GLN A CB    1 
ATOM   2024 C  CG    . GLN A 1 302 ? -1.683  7.632   -18.562 1.00 26.58 ? 281 GLN A CG    1 
ATOM   2025 C  CD    . GLN A 1 302 ? -1.069  8.061   -19.876 1.00 24.91 ? 281 GLN A CD    1 
ATOM   2026 O  OE1   . GLN A 1 302 ? 0.101   8.438   -19.951 1.00 25.17 ? 281 GLN A OE1   1 
ATOM   2027 N  NE2   . GLN A 1 302 ? -1.836  7.954   -20.952 1.00 24.84 ? 281 GLN A NE2   1 
ATOM   2028 N  N     . ARG A 1 303 ? -0.321  6.773   -15.053 1.00 27.82 ? 282 ARG A N     1 
ATOM   2029 C  CA    . ARG A 1 303 ? 0.358   5.512   -14.648 1.00 29.46 ? 282 ARG A CA    1 
ATOM   2030 C  C     . ARG A 1 303 ? -0.300  4.932   -13.395 1.00 25.98 ? 282 ARG A C     1 
ATOM   2031 O  O     . ARG A 1 303 ? -0.454  3.706   -13.361 1.00 26.10 ? 282 ARG A O     1 
ATOM   2032 C  CB    . ARG A 1 303 ? 1.861   5.632   -14.369 1.00 29.18 ? 282 ARG A CB    1 
ATOM   2033 C  CG    . ARG A 1 303 ? 2.466   4.263   -14.102 1.00 29.33 ? 282 ARG A CG    1 
ATOM   2034 C  CD    . ARG A 1 303 ? 3.963   4.159   -14.278 1.00 32.81 ? 282 ARG A CD    1 
ATOM   2035 N  NE    . ARG A 1 303 ? 4.197   2.963   -15.063 1.00 33.83 ? 282 ARG A NE    1 
ATOM   2036 C  CZ    . ARG A 1 303 ? 4.184   1.737   -14.578 1.00 32.30 ? 282 ARG A CZ    1 
ATOM   2037 N  NH1   . ARG A 1 303 ? 4.388   0.707   -15.373 1.00 34.39 ? 282 ARG A NH1   1 
ATOM   2038 N  NH2   . ARG A 1 303 ? 4.004   1.540   -13.298 1.00 34.99 ? 282 ARG A NH2   1 
ATOM   2039 N  N     . ASP A 1 304 ? -0.621  5.768   -12.400 1.00 26.39 ? 283 ASP A N     1 
ATOM   2040 C  CA    . ASP A 1 304 ? -1.308  5.313   -11.167 1.00 25.49 ? 283 ASP A CA    1 
ATOM   2041 C  C     . ASP A 1 304 ? -2.637  4.712   -11.600 1.00 24.38 ? 283 ASP A C     1 
ATOM   2042 O  O     . ASP A 1 304 ? -2.952  3.605   -11.111 1.00 25.53 ? 283 ASP A O     1 
ATOM   2043 C  CB    . ASP A 1 304 ? -1.505  6.416   -10.125 1.00 27.17 ? 283 ASP A CB    1 
ATOM   2044 C  CG    . ASP A 1 304 ? -2.129  5.885   -8.838  1.00 26.83 ? 283 ASP A CG    1 
ATOM   2045 O  OD1   . ASP A 1 304 ? -1.374  5.529   -7.924  1.00 29.01 ? 283 ASP A OD1   1 
ATOM   2046 O  OD2   . ASP A 1 304 ? -3.361  5.814   -8.772  1.00 24.19 ? 283 ASP A OD2   1 
ATOM   2047 N  N     . GLN A 1 305 ? -3.360  5.405   -12.477 1.00 20.71 ? 284 GLN A N     1 
ATOM   2048 C  CA    . GLN A 1 305 ? -4.685  4.935   -12.932 1.00 22.95 ? 284 GLN A CA    1 
ATOM   2049 C  C     . GLN A 1 305 ? -4.500  3.733   -13.873 1.00 23.59 ? 284 GLN A C     1 
ATOM   2050 O  O     . GLN A 1 305 ? -5.335  2.819   -13.789 1.00 26.78 ? 284 GLN A O     1 
ATOM   2051 C  CB    . GLN A 1 305 ? -5.501  6.112   -13.484 1.00 23.93 ? 284 GLN A CB    1 
ATOM   2052 C  CG    . GLN A 1 305 ? -5.846  7.167   -12.428 1.00 23.19 ? 284 GLN A CG    1 
ATOM   2053 C  CD    . GLN A 1 305 ? -7.133  7.932   -12.666 1.00 25.07 ? 284 GLN A CD    1 
ATOM   2054 O  OE1   . GLN A 1 305 ? -7.932  8.097   -11.745 1.00 30.24 ? 284 GLN A OE1   1 
ATOM   2055 N  NE2   . GLN A 1 305 ? -7.355  8.436   -13.878 1.00 22.39 ? 284 GLN A NE2   1 
ATOM   2056 N  N     . LEU A 1 306 ? -3.434  3.647   -14.688 1.00 21.80 ? 285 LEU A N     1 
ATOM   2057 C  CA    . LEU A 1 306 ? -3.212  2.402   -15.474 1.00 20.55 ? 285 LEU A CA    1 
ATOM   2058 C  C     . LEU A 1 306 ? -3.233  1.218   -14.495 1.00 21.98 ? 285 LEU A C     1 
ATOM   2059 O  O     . LEU A 1 306 ? -3.909  0.232   -14.817 1.00 23.42 ? 285 LEU A O     1 
ATOM   2060 C  CB    . LEU A 1 306 ? -1.920  2.441   -16.304 1.00 20.65 ? 285 LEU A CB    1 
ATOM   2061 C  CG    . LEU A 1 306 ? -1.541  1.134   -17.002 1.00 19.84 ? 285 LEU A CG    1 
ATOM   2062 C  CD1   . LEU A 1 306 ? -2.607  0.710   -17.981 1.00 20.88 ? 285 LEU A CD1   1 
ATOM   2063 C  CD2   . LEU A 1 306 ? -0.191  1.196   -17.717 1.00 19.85 ? 285 LEU A CD2   1 
ATOM   2064 N  N     . LEU A 1 307 ? -2.557  1.307   -13.343 1.00 21.49 ? 286 LEU A N     1 
ATOM   2065 C  CA    . LEU A 1 307 ? -2.347  0.145   -12.443 1.00 21.51 ? 286 LEU A CA    1 
ATOM   2066 C  C     . LEU A 1 307 ? -3.683  -0.233  -11.777 1.00 22.48 ? 286 LEU A C     1 
ATOM   2067 O  O     . LEU A 1 307 ? -3.971  -1.431  -11.716 1.00 22.57 ? 286 LEU A O     1 
ATOM   2068 C  CB    . LEU A 1 307 ? -1.228  0.471   -11.450 1.00 23.52 ? 286 LEU A CB    1 
ATOM   2069 C  CG    . LEU A 1 307 ? 0.094   0.921   -12.090 1.00 24.93 ? 286 LEU A CG    1 
ATOM   2070 C  CD1   . LEU A 1 307 ? 1.004   1.566   -11.079 1.00 25.63 ? 286 LEU A CD1   1 
ATOM   2071 C  CD2   . LEU A 1 307 ? 0.805   -0.232  -12.771 1.00 26.11 ? 286 LEU A CD2   1 
ATOM   2072 N  N     . GLN A 1 308 ? -4.539  0.746   -11.443 1.00 22.46 ? 287 GLN A N     1 
ATOM   2073 C  CA    . GLN A 1 308 ? -5.936  0.549   -10.947 1.00 20.73 ? 287 GLN A CA    1 
ATOM   2074 C  C     . GLN A 1 308 ? -6.783  -0.180  -12.006 1.00 23.56 ? 287 GLN A C     1 
ATOM   2075 O  O     . GLN A 1 308 ? -7.857  -0.696  -11.664 1.00 26.13 ? 287 GLN A O     1 
ATOM   2076 C  CB    . GLN A 1 308 ? -6.612  1.895   -10.664 1.00 20.53 ? 287 GLN A CB    1 
ATOM   2077 C  CG    . GLN A 1 308 ? -5.925  2.789   -9.634  1.00 19.95 ? 287 GLN A CG    1 
ATOM   2078 C  CD    . GLN A 1 308 ? -6.772  4.018   -9.352  1.00 21.40 ? 287 GLN A CD    1 
ATOM   2079 O  OE1   . GLN A 1 308 ? -8.021  3.975   -9.297  1.00 20.85 ? 287 GLN A OE1   1 
ATOM   2080 N  NE2   . GLN A 1 308 ? -6.099  5.139   -9.147  1.00 19.15 ? 287 GLN A NE2   1 
ATOM   2081 N  N     . HIS A 1 309 ? -6.344  -0.153  -13.269 1.00 24.70 ? 288 HIS A N     1 
ATOM   2082 C  CA    . HIS A 1 309 ? -7.021  -0.750  -14.444 1.00 22.46 ? 288 HIS A CA    1 
ATOM   2083 C  C     . HIS A 1 309 ? -6.277  -2.004  -14.920 1.00 20.50 ? 288 HIS A C     1 
ATOM   2084 O  O     . HIS A 1 309 ? -6.684  -2.490  -15.977 1.00 20.76 ? 288 HIS A O     1 
ATOM   2085 C  CB    . HIS A 1 309 ? -7.151  0.295   -15.575 1.00 27.08 ? 288 HIS A CB    1 
ATOM   2086 C  CG    . HIS A 1 309 ? -8.152  1.379   -15.315 1.00 27.46 ? 288 HIS A CG    1 
ATOM   2087 N  ND1   . HIS A 1 309 ? -9.505  1.220   -15.579 1.00 27.01 ? 288 HIS A ND1   1 
ATOM   2088 C  CD2   . HIS A 1 309 ? -8.002  2.624   -14.824 1.00 26.22 ? 288 HIS A CD2   1 
ATOM   2089 C  CE1   . HIS A 1 309 ? -10.144 2.328   -15.253 1.00 28.59 ? 288 HIS A CE1   1 
ATOM   2090 N  NE2   . HIS A 1 309 ? -9.231  3.204   -14.793 1.00 28.48 ? 288 HIS A NE2   1 
ATOM   2091 N  N     . MET A 1 310 ? -5.311  -2.557  -14.155 1.00 18.24 ? 289 MET A N     1 
ATOM   2092 C  CA    . MET A 1 310 ? -4.561  -3.793  -14.532 1.00 17.95 ? 289 MET A CA    1 
ATOM   2093 C  C     . MET A 1 310 ? -4.745  -4.864  -13.463 1.00 19.29 ? 289 MET A C     1 
ATOM   2094 O  O     . MET A 1 310 ? -3.778  -5.351  -12.878 1.00 17.72 ? 289 MET A O     1 
ATOM   2095 C  CB    . MET A 1 310 ? -3.062  -3.516  -14.754 1.00 18.92 ? 289 MET A CB    1 
ATOM   2096 C  CG    . MET A 1 310 ? -2.763  -2.683  -16.024 1.00 18.29 ? 289 MET A CG    1 
ATOM   2097 S  SD    . MET A 1 310 ? -0.990  -2.435  -16.414 1.00 18.10 ? 289 MET A SD    1 
ATOM   2098 C  CE    . MET A 1 310 ? -0.612  -4.091  -16.994 1.00 18.84 ? 289 MET A CE    1 
ATOM   2099 N  N     . PRO A 1 311 ? -6.004  -5.263  -13.176 1.00 20.73 ? 290 PRO A N     1 
ATOM   2100 C  CA    . PRO A 1 311 ? -6.263  -6.308  -12.203 1.00 22.40 ? 290 PRO A CA    1 
ATOM   2101 C  C     . PRO A 1 311 ? -5.557  -7.629  -12.552 1.00 26.57 ? 290 PRO A C     1 
ATOM   2102 O  O     . PRO A 1 311 ? -5.521  -8.009  -13.731 1.00 25.92 ? 290 PRO A O     1 
ATOM   2103 C  CB    . PRO A 1 311 ? -7.785  -6.517  -12.246 1.00 23.98 ? 290 PRO A CB    1 
ATOM   2104 C  CG    . PRO A 1 311 ? -8.246  -5.838  -13.516 1.00 23.05 ? 290 PRO A CG    1 
ATOM   2105 C  CD    . PRO A 1 311 ? -7.242  -4.727  -13.763 1.00 21.75 ? 290 PRO A CD    1 
ATOM   2106 N  N     . GLN A 1 312 ? -5.025  -8.303  -11.526 1.00 25.14 ? 291 GLN A N     1 
ATOM   2107 C  CA    . GLN A 1 312 ? -4.500  -9.691  -11.659 1.00 24.88 ? 291 GLN A CA    1 
ATOM   2108 C  C     . GLN A 1 312 ? -5.685  -10.649 -11.865 1.00 22.68 ? 291 GLN A C     1 
ATOM   2109 O  O     . GLN A 1 312 ? -6.784  -10.384 -11.376 1.00 23.16 ? 291 GLN A O     1 
ATOM   2110 C  CB    . GLN A 1 312 ? -3.649  -10.089 -10.447 1.00 24.28 ? 291 GLN A CB    1 
ATOM   2111 C  CG    . GLN A 1 312 ? -2.442  -9.184  -10.187 1.00 24.70 ? 291 GLN A CG    1 
ATOM   2112 C  CD    . GLN A 1 312 ? -1.326  -9.413  -11.174 1.00 26.04 ? 291 GLN A CD    1 
ATOM   2113 O  OE1   . GLN A 1 312 ? -1.033  -8.570  -12.006 1.00 31.45 ? 291 GLN A OE1   1 
ATOM   2114 N  NE2   . GLN A 1 312 ? -0.676  -10.560 -11.088 1.00 25.76 ? 291 GLN A NE2   1 
ATOM   2115 N  N     . GLY A 1 313 ? -5.462  -11.746 -12.564 1.00 21.00 ? 292 GLY A N     1 
ATOM   2116 C  CA    . GLY A 1 313 ? -6.453  -12.823 -12.719 1.00 20.49 ? 292 GLY A CA    1 
ATOM   2117 C  C     . GLY A 1 313 ? -6.640  -13.613 -11.441 1.00 18.87 ? 292 GLY A C     1 
ATOM   2118 O  O     . GLY A 1 313 ? -6.024  -13.302 -10.442 1.00 18.73 ? 292 GLY A O     1 
ATOM   2119 N  N     . SER A 1 314 ? -7.453  -14.650 -11.520 1.00 19.94 ? 293 SER A N     1 
ATOM   2120 C  CA    . SER A 1 314 ? -7.924  -15.472 -10.376 1.00 20.22 ? 293 SER A CA    1 
ATOM   2121 C  C     . SER A 1 314 ? -7.731  -16.961 -10.663 1.00 19.47 ? 293 SER A C     1 
ATOM   2122 O  O     . SER A 1 314 ? -8.454  -17.503 -11.558 1.00 21.82 ? 293 SER A O     1 
ATOM   2123 C  CB    . SER A 1 314 ? -9.353  -15.137 -10.122 1.00 21.09 ? 293 SER A CB    1 
ATOM   2124 O  OG    . SER A 1 314 ? -9.433  -13.776 -9.714  1.00 21.81 ? 293 SER A OG    1 
ATOM   2125 N  N     . VAL A 1 315 ? -6.806  -17.606 -9.951  1.00 18.56 ? 294 VAL A N     1 
ATOM   2126 C  CA    . VAL A 1 315 ? -6.466  -19.029 -10.204 1.00 19.21 ? 294 VAL A CA    1 
ATOM   2127 C  C     . VAL A 1 315 ? -6.089  -19.682 -8.874  1.00 18.97 ? 294 VAL A C     1 
ATOM   2128 O  O     . VAL A 1 315 ? -5.438  -19.078 -8.030  1.00 19.42 ? 294 VAL A O     1 
ATOM   2129 C  CB    . VAL A 1 315 ? -5.372  -19.157 -11.289 1.00 21.97 ? 294 VAL A CB    1 
ATOM   2130 C  CG1   . VAL A 1 315 ? -4.179  -18.277 -10.958 1.00 22.36 ? 294 VAL A CG1   1 
ATOM   2131 C  CG2   . VAL A 1 315 ? -4.916  -20.589 -11.548 1.00 22.24 ? 294 VAL A CG2   1 
ATOM   2132 N  N     . VAL A 1 316 ? -6.602  -20.878 -8.676  1.00 18.59 ? 295 VAL A N     1 
ATOM   2133 C  CA    . VAL A 1 316 ? -6.160  -21.840 -7.642  1.00 16.74 ? 295 VAL A CA    1 
ATOM   2134 C  C     . VAL A 1 316 ? -5.649  -22.984 -8.487  1.00 17.09 ? 295 VAL A C     1 
ATOM   2135 O  O     . VAL A 1 316 ? -6.489  -23.521 -9.312  1.00 17.16 ? 295 VAL A O     1 
ATOM   2136 C  CB    . VAL A 1 316 ? -7.331  -22.301 -6.749  1.00 17.87 ? 295 VAL A CB    1 
ATOM   2137 C  CG1   . VAL A 1 316 ? -6.860  -23.213 -5.634  1.00 17.57 ? 295 VAL A CG1   1 
ATOM   2138 C  CG2   . VAL A 1 316 ? -8.127  -21.126 -6.201  1.00 18.44 ? 295 VAL A CG2   1 
ATOM   2139 N  N     . LYS A 1 317 ? -4.351  -23.262 -8.368  1.00 16.39 ? 296 LYS A N     1 
ATOM   2140 C  CA    . LYS A 1 317 ? -3.666  -24.378 -9.050  1.00 15.67 ? 296 LYS A CA    1 
ATOM   2141 C  C     . LYS A 1 317 ? -3.533  -25.529 -8.045  1.00 15.32 ? 296 LYS A C     1 
ATOM   2142 O  O     . LYS A 1 317 ? -3.149  -25.254 -6.904  1.00 14.20 ? 296 LYS A O     1 
ATOM   2143 C  CB    . LYS A 1 317 ? -2.282  -23.967 -9.558  1.00 15.59 ? 296 LYS A CB    1 
ATOM   2144 C  CG    . LYS A 1 317 ? -1.581  -25.077 -10.347 1.00 16.07 ? 296 LYS A CG    1 
ATOM   2145 C  CD    . LYS A 1 317 ? -0.213  -24.689 -10.864 1.00 17.04 ? 296 LYS A CD    1 
ATOM   2146 C  CE    . LYS A 1 317 ? 0.489   -25.825 -11.584 1.00 17.53 ? 296 LYS A CE    1 
ATOM   2147 N  NZ    . LYS A 1 317 ? 1.772   -25.356 -12.158 1.00 16.81 ? 296 LYS A NZ    1 
ATOM   2148 N  N     . PHE A 1 318 ? -3.783  -26.760 -8.504  1.00 15.17 ? 297 PHE A N     1 
ATOM   2149 C  CA    . PHE A 1 318 ? -3.844  -27.970 -7.665  1.00 16.52 ? 297 PHE A CA    1 
ATOM   2150 C  C     . PHE A 1 318 ? -3.139  -29.134 -8.370  1.00 16.62 ? 297 PHE A C     1 
ATOM   2151 O  O     . PHE A 1 318 ? -3.027  -29.193 -9.587  1.00 17.21 ? 297 PHE A O     1 
ATOM   2152 C  CB    . PHE A 1 318 ? -5.294  -28.294 -7.267  1.00 15.91 ? 297 PHE A CB    1 
ATOM   2153 C  CG    . PHE A 1 318 ? -6.185  -28.728 -8.403  1.00 14.85 ? 297 PHE A CG    1 
ATOM   2154 C  CD1   . PHE A 1 318 ? -7.172  -27.882 -8.878  1.00 15.78 ? 297 PHE A CD1   1 
ATOM   2155 C  CD2   . PHE A 1 318 ? -6.052  -29.974 -8.986  1.00 15.57 ? 297 PHE A CD2   1 
ATOM   2156 C  CE1   . PHE A 1 318 ? -8.015  -28.267 -9.902  1.00 14.93 ? 297 PHE A CE1   1 
ATOM   2157 C  CE2   . PHE A 1 318 ? -6.887  -30.353 -10.032 1.00 17.09 ? 297 PHE A CE2   1 
ATOM   2158 C  CZ    . PHE A 1 318 ? -7.871  -29.502 -10.482 1.00 15.73 ? 297 PHE A CZ    1 
ATOM   2159 N  N     . HIS A 1 319 ? -2.740  -30.066 -7.526  1.00 18.74 ? 298 HIS A N     1 
ATOM   2160 C  CA    . HIS A 1 319 ? -2.091  -31.362 -7.809  1.00 21.97 ? 298 HIS A CA    1 
ATOM   2161 C  C     . HIS A 1 319 ? -2.767  -32.401 -6.913  1.00 23.91 ? 298 HIS A C     1 
ATOM   2162 O  O     . HIS A 1 319 ? -2.545  -32.366 -5.657  1.00 22.68 ? 298 HIS A O     1 
ATOM   2163 C  CB    . HIS A 1 319 ? -0.600  -31.277 -7.464  1.00 20.87 ? 298 HIS A CB    1 
ATOM   2164 C  CG    . HIS A 1 319 ? 0.103   -30.240 -8.267  1.00 21.94 ? 298 HIS A CG    1 
ATOM   2165 N  ND1   . HIS A 1 319 ? 0.640   -30.511 -9.499  1.00 22.63 ? 298 HIS A ND1   1 
ATOM   2166 C  CD2   . HIS A 1 319 ? 0.324   -28.929 -8.028  1.00 21.79 ? 298 HIS A CD2   1 
ATOM   2167 C  CE1   . HIS A 1 319 ? 1.183   -29.411 -9.996  1.00 22.72 ? 298 HIS A CE1   1 
ATOM   2168 N  NE2   . HIS A 1 319 ? 1.018   -28.430 -9.093  1.00 21.97 ? 298 HIS A NE2   1 
ATOM   2169 N  N     . VAL A 1 320 ? -3.566  -33.272 -7.516  1.00 22.05 ? 299 VAL A N     1 
ATOM   2170 C  CA    . VAL A 1 320 ? -4.167  -34.421 -6.789  1.00 20.44 ? 299 VAL A CA    1 
ATOM   2171 C  C     . VAL A 1 320 ? -3.145  -35.554 -6.834  1.00 21.12 ? 299 VAL A C     1 
ATOM   2172 O  O     . VAL A 1 320 ? -2.629  -35.818 -7.935  1.00 20.32 ? 299 VAL A O     1 
ATOM   2173 C  CB    . VAL A 1 320 ? -5.517  -34.841 -7.374  1.00 20.00 ? 299 VAL A CB    1 
ATOM   2174 C  CG1   . VAL A 1 320 ? -6.213  -35.807 -6.418  1.00 20.23 ? 299 VAL A CG1   1 
ATOM   2175 C  CG2   . VAL A 1 320 ? -6.395  -33.635 -7.679  1.00 18.67 ? 299 VAL A CG2   1 
ATOM   2176 N  N     . ILE A 1 321 ? -2.845  -36.155 -5.675  1.00 20.31 ? 300 ILE A N     1 
ATOM   2177 C  CA    . ILE A 1 321 ? -1.731  -37.121 -5.525  1.00 20.59 ? 300 ILE A CA    1 
ATOM   2178 C  C     . ILE A 1 321 ? -2.349  -38.492 -5.296  1.00 19.92 ? 300 ILE A C     1 
ATOM   2179 O  O     . ILE A 1 321 ? -3.084  -38.641 -4.327  1.00 19.82 ? 300 ILE A O     1 
ATOM   2180 C  CB    . ILE A 1 321 ? -0.780  -36.732 -4.377  1.00 22.33 ? 300 ILE A CB    1 
ATOM   2181 C  CG1   . ILE A 1 321 ? -0.503  -35.227 -4.281  1.00 23.11 ? 300 ILE A CG1   1 
ATOM   2182 C  CG2   . ILE A 1 321 ? 0.492   -37.549 -4.497  1.00 23.17 ? 300 ILE A CG2   1 
ATOM   2183 C  CD1   . ILE A 1 321 ? 0.156   -34.626 -5.515  1.00 24.93 ? 300 ILE A CD1   1 
ATOM   2184 N  N     . TYR A 1 322 ? -2.070  -39.426 -6.196  1.00 22.69 ? 301 TYR A N     1 
ATOM   2185 C  CA    . TYR A 1 322 ? -2.382  -40.870 -6.067  1.00 22.51 ? 301 TYR A CA    1 
ATOM   2186 C  C     . TYR A 1 322 ? -1.076  -41.660 -5.943  1.00 23.40 ? 301 TYR A C     1 
ATOM   2187 O  O     . TYR A 1 322 ? -0.020  -41.197 -6.427  1.00 24.69 ? 301 TYR A O     1 
ATOM   2188 C  CB    . TYR A 1 322 ? -3.220  -41.311 -7.259  1.00 21.68 ? 301 TYR A CB    1 
ATOM   2189 C  CG    . TYR A 1 322 ? -4.521  -40.559 -7.368  1.00 21.78 ? 301 TYR A CG    1 
ATOM   2190 C  CD1   . TYR A 1 322 ? -5.646  -40.974 -6.670  1.00 18.92 ? 301 TYR A CD1   1 
ATOM   2191 C  CD2   . TYR A 1 322 ? -4.597  -39.392 -8.114  1.00 20.40 ? 301 TYR A CD2   1 
ATOM   2192 C  CE1   . TYR A 1 322 ? -6.825  -40.265 -6.751  1.00 20.09 ? 301 TYR A CE1   1 
ATOM   2193 C  CE2   . TYR A 1 322 ? -5.776  -38.681 -8.210  1.00 20.63 ? 301 TYR A CE2   1 
ATOM   2194 C  CZ    . TYR A 1 322 ? -6.897  -39.127 -7.533  1.00 19.67 ? 301 TYR A CZ    1 
ATOM   2195 O  OH    . TYR A 1 322 ? -8.047  -38.409 -7.631  1.00 19.18 ? 301 TYR A OH    1 
ATOM   2196 N  N     . ASP A 1 323 ? -1.143  -42.829 -5.319  1.00 27.62 ? 302 ASP A N     1 
ATOM   2197 C  CA    . ASP A 1 323 ? 0.022   -43.754 -5.247  1.00 31.94 ? 302 ASP A CA    1 
ATOM   2198 C  C     . ASP A 1 323 ? 0.481   -44.050 -6.668  1.00 34.56 ? 302 ASP A C     1 
ATOM   2199 O  O     . ASP A 1 323 ? 1.707   -44.198 -6.849  1.00 35.48 ? 302 ASP A O     1 
ATOM   2200 C  CB    . ASP A 1 323 ? -0.275  -45.053 -4.504  1.00 31.76 ? 302 ASP A CB    1 
ATOM   2201 C  CG    . ASP A 1 323 ? -0.570  -44.849 -3.034  1.00 39.22 ? 302 ASP A CG    1 
ATOM   2202 O  OD1   . ASP A 1 323 ? -0.032  -43.867 -2.451  1.00 41.16 ? 302 ASP A OD1   1 
ATOM   2203 O  OD2   . ASP A 1 323 ? -1.354  -45.662 -2.479  1.00 46.06 ? 302 ASP A OD2   1 
ATOM   2204 N  N     . GLU A 1 324 ? -0.449  -44.127 -7.634  1.00 35.02 ? 303 GLU A N     1 
ATOM   2205 C  CA    . GLU A 1 324 ? -0.066  -44.445 -9.033  1.00 38.22 ? 303 GLU A CA    1 
ATOM   2206 C  C     . GLU A 1 324 ? -0.971  -43.741 -10.038 1.00 33.16 ? 303 GLU A C     1 
ATOM   2207 O  O     . GLU A 1 324 ? -2.051  -43.289 -9.695  1.00 29.48 ? 303 GLU A O     1 
ATOM   2208 C  CB    . GLU A 1 324 ? -0.013  -45.963 -9.205  1.00 42.48 ? 303 GLU A CB    1 
ATOM   2209 C  CG    . GLU A 1 324 ? 1.198   -46.562 -8.496  1.00 48.92 ? 303 GLU A CG    1 
ATOM   2210 C  CD    . GLU A 1 324 ? 1.783   -47.824 -9.097  1.00 56.07 ? 303 GLU A CD    1 
ATOM   2211 O  OE1   . GLU A 1 324 ? 2.426   -47.734 -10.182 1.00 56.40 ? 303 GLU A OE1   1 
ATOM   2212 O  OE2   . GLU A 1 324 ? 1.581   -48.896 -8.481  1.00 64.51 ? 303 GLU A OE2   1 
ATOM   2213 N  N     . PRO A 1 325 ? -0.474  -43.550 -11.285 1.00 31.48 ? 304 PRO A N     1 
ATOM   2214 C  CA    . PRO A 1 325 ? -1.281  -43.027 -12.389 1.00 29.08 ? 304 PRO A CA    1 
ATOM   2215 C  C     . PRO A 1 325 ? -2.211  -44.115 -12.952 1.00 29.12 ? 304 PRO A C     1 
ATOM   2216 O  O     . PRO A 1 325 ? -2.035  -44.574 -14.054 1.00 23.90 ? 304 PRO A O     1 
ATOM   2217 C  CB    . PRO A 1 325 ? -0.207  -42.564 -13.373 1.00 29.44 ? 304 PRO A CB    1 
ATOM   2218 C  CG    . PRO A 1 325 ? 0.944   -43.549 -13.174 1.00 28.21 ? 304 PRO A CG    1 
ATOM   2219 C  CD    . PRO A 1 325 ? 0.931   -43.793 -11.676 1.00 29.90 ? 304 PRO A CD    1 
ATOM   2220 N  N     . TRP A 1 326 ? -3.214  -44.461 -12.148 1.00 29.14 ? 305 TRP A N     1 
ATOM   2221 C  CA    . TRP A 1 326 ? -4.122  -45.619 -12.333 1.00 27.75 ? 305 TRP A CA    1 
ATOM   2222 C  C     . TRP A 1 326 ? -4.979  -45.426 -13.580 1.00 27.32 ? 305 TRP A C     1 
ATOM   2223 O  O     . TRP A 1 326 ? -5.547  -46.421 -14.039 1.00 32.09 ? 305 TRP A O     1 
ATOM   2224 C  CB    . TRP A 1 326 ? -4.997  -45.797 -11.087 1.00 25.09 ? 305 TRP A CB    1 
ATOM   2225 C  CG    . TRP A 1 326 ? -5.728  -44.540 -10.716 1.00 23.05 ? 305 TRP A CG    1 
ATOM   2226 C  CD1   . TRP A 1 326 ? -5.361  -43.617 -9.774  1.00 21.29 ? 305 TRP A CD1   1 
ATOM   2227 C  CD2   . TRP A 1 326 ? -6.942  -44.051 -11.305 1.00 21.91 ? 305 TRP A CD2   1 
ATOM   2228 N  NE1   . TRP A 1 326 ? -6.269  -42.593 -9.725  1.00 21.63 ? 305 TRP A NE1   1 
ATOM   2229 C  CE2   . TRP A 1 326 ? -7.251  -42.829 -10.651 1.00 22.83 ? 305 TRP A CE2   1 
ATOM   2230 C  CE3   . TRP A 1 326 ? -7.813  -44.533 -12.284 1.00 22.43 ? 305 TRP A CE3   1 
ATOM   2231 C  CZ2   . TRP A 1 326 ? -8.394  -42.098 -10.950 1.00 21.41 ? 305 TRP A CZ2   1 
ATOM   2232 C  CZ3   . TRP A 1 326 ? -8.935  -43.794 -12.600 1.00 22.49 ? 305 TRP A CZ3   1 
ATOM   2233 C  CH2   . TRP A 1 326 ? -9.214  -42.598 -11.934 1.00 22.57 ? 305 TRP A CH2   1 
ATOM   2234 N  N     . TRP A 1 327 ? -5.117  -44.192 -14.056 1.00 27.63 ? 306 TRP A N     1 
ATOM   2235 C  CA    . TRP A 1 327 ? -5.924  -43.830 -15.251 1.00 25.81 ? 306 TRP A CA    1 
ATOM   2236 C  C     . TRP A 1 327 ? -5.252  -44.373 -16.517 1.00 29.28 ? 306 TRP A C     1 
ATOM   2237 O  O     . TRP A 1 327 ? -6.000  -44.831 -17.424 1.00 29.25 ? 306 TRP A O     1 
ATOM   2238 C  CB    . TRP A 1 327 ? -6.163  -42.321 -15.326 1.00 24.90 ? 306 TRP A CB    1 
ATOM   2239 C  CG    . TRP A 1 327 ? -4.926  -41.487 -15.228 1.00 24.80 ? 306 TRP A CG    1 
ATOM   2240 C  CD1   . TRP A 1 327 ? -4.122  -41.061 -16.248 1.00 24.41 ? 306 TRP A CD1   1 
ATOM   2241 C  CD2   . TRP A 1 327 ? -4.388  -40.908 -14.025 1.00 24.46 ? 306 TRP A CD2   1 
ATOM   2242 N  NE1   . TRP A 1 327 ? -3.100  -40.289 -15.756 1.00 22.77 ? 306 TRP A NE1   1 
ATOM   2243 C  CE2   . TRP A 1 327 ? -3.229  -40.184 -14.398 1.00 23.27 ? 306 TRP A CE2   1 
ATOM   2244 C  CE3   . TRP A 1 327 ? -4.770  -40.931 -12.679 1.00 22.80 ? 306 TRP A CE3   1 
ATOM   2245 C  CZ2   . TRP A 1 327 ? -2.440  -39.510 -13.466 1.00 23.27 ? 306 TRP A CZ2   1 
ATOM   2246 C  CZ3   . TRP A 1 327 ? -3.984  -40.267 -11.758 1.00 23.10 ? 306 TRP A CZ3   1 
ATOM   2247 C  CH2   . TRP A 1 327 ? -2.836  -39.575 -12.152 1.00 23.48 ? 306 TRP A CH2   1 
ATOM   2248 N  N     . ARG A 1 328 ? -3.914  -44.352 -16.572 1.00 28.07 ? 307 ARG A N     1 
ATOM   2249 C  CA    . ARG A 1 328 ? -3.119  -44.847 -17.726 1.00 28.24 ? 307 ARG A CA    1 
ATOM   2250 C  C     . ARG A 1 328 ? -3.482  -46.308 -17.966 1.00 28.94 ? 307 ARG A C     1 
ATOM   2251 O  O     . ARG A 1 328 ? -3.790  -46.626 -19.103 1.00 27.00 ? 307 ARG A O     1 
ATOM   2252 C  CB    . ARG A 1 328 ? -1.611  -44.712 -17.478 1.00 29.38 ? 307 ARG A CB    1 
ATOM   2253 C  CG    . ARG A 1 328 ? -1.098  -43.273 -17.466 1.00 29.81 ? 307 ARG A CG    1 
ATOM   2254 C  CD    . ARG A 1 328 ? 0.380   -43.193 -17.078 1.00 30.68 ? 307 ARG A CD    1 
ATOM   2255 N  NE    . ARG A 1 328 ? 0.864   -41.813 -17.012 1.00 30.79 ? 307 ARG A NE    1 
ATOM   2256 C  CZ    . ARG A 1 328 ? 2.134   -41.448 -17.016 1.00 28.06 ? 307 ARG A CZ    1 
ATOM   2257 N  NH1   . ARG A 1 328 ? 3.088   -42.361 -17.057 1.00 31.03 ? 307 ARG A NH1   1 
ATOM   2258 N  NH2   . ARG A 1 328 ? 2.451   -40.174 -17.003 1.00 24.63 ? 307 ARG A NH2   1 
ATOM   2259 N  N     . ALA A 1 329 ? -3.500  -47.143 -16.916 1.00 32.73 ? 308 ALA A N     1 
ATOM   2260 C  CA    . ALA A 1 329 ? -3.878  -48.576 -16.991 1.00 34.34 ? 308 ALA A CA    1 
ATOM   2261 C  C     . ALA A 1 329 ? -5.286  -48.730 -17.598 1.00 37.24 ? 308 ALA A C     1 
ATOM   2262 O  O     . ALA A 1 329 ? -5.576  -49.788 -18.160 1.00 42.40 ? 308 ALA A O     1 
ATOM   2263 C  CB    . ALA A 1 329 ? -3.785  -49.216 -15.627 1.00 34.98 ? 308 ALA A CB    1 
ATOM   2264 N  N     . GLU A 1 330 ? -6.147  -47.714 -17.535 1.00 38.97 ? 309 GLU A N     1 
ATOM   2265 C  CA    . GLU A 1 330 ? -7.485  -47.765 -18.189 1.00 42.79 ? 309 GLU A CA    1 
ATOM   2266 C  C     . GLU A 1 330 ? -7.363  -47.215 -19.611 1.00 38.95 ? 309 GLU A C     1 
ATOM   2267 O  O     . GLU A 1 330 ? -8.419  -47.037 -20.272 1.00 43.09 ? 309 GLU A O     1 
ATOM   2268 C  CB    . GLU A 1 330 ? -8.548  -46.958 -17.430 1.00 44.54 ? 309 GLU A CB    1 
ATOM   2269 C  CG    . GLU A 1 330 ? -8.656  -47.286 -15.956 1.00 49.90 ? 309 GLU A CG    1 
ATOM   2270 C  CD    . GLU A 1 330 ? -9.432  -48.556 -15.675 1.00 54.72 ? 309 GLU A CD    1 
ATOM   2271 O  OE1   . GLU A 1 330 ? -10.382 -48.508 -14.862 1.00 57.31 ? 309 GLU A OE1   1 
ATOM   2272 O  OE2   . GLU A 1 330 ? -9.081  -49.581 -16.272 1.00 55.55 ? 309 GLU A OE2   1 
ATOM   2273 N  N     . GLY A 1 331 ? -6.148  -46.906 -20.047 1.00 31.77 ? 310 GLY A N     1 
ATOM   2274 C  CA    . GLY A 1 331 ? -5.909  -46.281 -21.357 1.00 33.81 ? 310 GLY A CA    1 
ATOM   2275 C  C     . GLY A 1 331 ? -6.289  -44.811 -21.375 1.00 31.78 ? 310 GLY A C     1 
ATOM   2276 O  O     . GLY A 1 331 ? -6.522  -44.285 -22.468 1.00 31.87 ? 310 GLY A O     1 
ATOM   2277 N  N     . LEU A 1 332 ? -6.317  -44.159 -20.218 1.00 29.53 ? 311 LEU A N     1 
ATOM   2278 C  CA    . LEU A 1 332 ? -6.772  -42.749 -20.082 1.00 31.51 ? 311 LEU A CA    1 
ATOM   2279 C  C     . LEU A 1 332 ? -5.555  -41.838 -19.915 1.00 29.13 ? 311 LEU A C     1 
ATOM   2280 O  O     . LEU A 1 332 ? -4.629  -42.229 -19.167 1.00 30.80 ? 311 LEU A O     1 
ATOM   2281 C  CB    . LEU A 1 332 ? -7.729  -42.600 -18.889 1.00 31.42 ? 311 LEU A CB    1 
ATOM   2282 C  CG    . LEU A 1 332 ? -9.096  -43.269 -19.026 1.00 31.22 ? 311 LEU A CG    1 
ATOM   2283 C  CD1   . LEU A 1 332 ? -9.903  -43.018 -17.771 1.00 34.75 ? 311 LEU A CD1   1 
ATOM   2284 C  CD2   . LEU A 1 332 ? -9.848  -42.761 -20.247 1.00 32.83 ? 311 LEU A CD2   1 
ATOM   2285 N  N     . SER A 1 333 ? -5.593  -40.679 -20.583 1.00 27.15 ? 312 SER A N     1 
ATOM   2286 C  CA    . SER A 1 333 ? -4.550  -39.619 -20.581 1.00 27.53 ? 312 SER A CA    1 
ATOM   2287 C  C     . SER A 1 333 ? -4.470  -38.950 -19.211 1.00 29.59 ? 312 SER A C     1 
ATOM   2288 O  O     . SER A 1 333 ? -3.367  -38.475 -18.854 1.00 28.92 ? 312 SER A O     1 
ATOM   2289 C  CB    . SER A 1 333 ? -4.850  -38.571 -21.615 1.00 26.45 ? 312 SER A CB    1 
ATOM   2290 O  OG    . SER A 1 333 ? -6.051  -37.906 -21.297 1.00 22.78 ? 312 SER A OG    1 
ATOM   2291 N  N     . GLY A 1 334 ? -5.618  -38.866 -18.527 1.00 26.70 ? 313 GLY A N     1 
ATOM   2292 C  CA    . GLY A 1 334 ? -5.786  -38.061 -17.312 1.00 28.56 ? 313 GLY A CA    1 
ATOM   2293 C  C     . GLY A 1 334 ? -6.292  -36.660 -17.598 1.00 31.39 ? 313 GLY A C     1 
ATOM   2294 O  O     . GLY A 1 334 ? -6.398  -35.872 -16.624 1.00 35.35 ? 313 GLY A O     1 
ATOM   2295 N  N     . THR A 1 335 ? -6.537  -36.315 -18.870 1.00 31.98 ? 314 THR A N     1 
ATOM   2296 C  CA    . THR A 1 335 ? -7.092  -35.004 -19.305 1.00 30.66 ? 314 THR A CA    1 
ATOM   2297 C  C     . THR A 1 335 ? -8.622  -35.141 -19.394 1.00 32.78 ? 314 THR A C     1 
ATOM   2298 O  O     . THR A 1 335 ? -9.108  -35.981 -20.218 1.00 26.66 ? 314 THR A O     1 
ATOM   2299 C  CB    . THR A 1 335 ? -6.484  -34.522 -20.631 1.00 31.73 ? 314 THR A CB    1 
ATOM   2300 O  OG1   . THR A 1 335 ? -5.132  -34.115 -20.456 1.00 29.74 ? 314 THR A OG1   1 
ATOM   2301 C  CG2   . THR A 1 335 ? -7.239  -33.360 -21.242 1.00 34.89 ? 314 THR A CG2   1 
ATOM   2302 N  N     . VAL A 1 336 ? -9.332  -34.374 -18.554 1.00 31.69 ? 315 VAL A N     1 
ATOM   2303 C  CA    . VAL A 1 336 ? -10.803 -34.157 -18.640 1.00 31.85 ? 315 VAL A CA    1 
ATOM   2304 C  C     . VAL A 1 336 ? -11.052 -32.705 -19.029 1.00 32.03 ? 315 VAL A C     1 
ATOM   2305 O  O     . VAL A 1 336 ? -10.279 -31.837 -18.611 1.00 31.35 ? 315 VAL A O     1 
ATOM   2306 C  CB    . VAL A 1 336 ? -11.544 -34.490 -17.330 1.00 32.90 ? 315 VAL A CB    1 
ATOM   2307 C  CG1   . VAL A 1 336 ? -11.183 -35.872 -16.837 1.00 34.82 ? 315 VAL A CG1   1 
ATOM   2308 C  CG2   . VAL A 1 336 ? -11.302 -33.438 -16.249 1.00 33.82 ? 315 VAL A CG2   1 
ATOM   2309 N  N     . LEU A 1 337 ? -12.125 -32.472 -19.786 1.00 32.59 ? 316 LEU A N     1 
ATOM   2310 C  CA    . LEU A 1 337 ? -12.569 -31.123 -20.198 1.00 34.39 ? 316 LEU A CA    1 
ATOM   2311 C  C     . LEU A 1 337 ? -14.065 -31.036 -19.945 1.00 31.52 ? 316 LEU A C     1 
ATOM   2312 O  O     . LEU A 1 337 ? -14.802 -31.758 -20.595 1.00 32.57 ? 316 LEU A O     1 
ATOM   2313 C  CB    . LEU A 1 337 ? -12.279 -30.880 -21.677 1.00 34.62 ? 316 LEU A CB    1 
ATOM   2314 C  CG    . LEU A 1 337 ? -12.684 -29.486 -22.160 1.00 37.51 ? 316 LEU A CG    1 
ATOM   2315 C  CD1   . LEU A 1 337 ? -11.464 -28.595 -22.301 1.00 37.83 ? 316 LEU A CD1   1 
ATOM   2316 C  CD2   . LEU A 1 337 ? -13.441 -29.559 -23.481 1.00 40.24 ? 316 LEU A CD2   1 
ATOM   2317 N  N     . CYS A 1 338 ? -14.460 -30.164 -19.030 1.00 31.83 ? 317 CYS A N     1 
ATOM   2318 C  CA    . CYS A 1 338 ? -15.832 -30.045 -18.491 1.00 30.24 ? 317 CYS A CA    1 
ATOM   2319 C  C     . CYS A 1 338 ? -16.175 -28.567 -18.478 1.00 29.61 ? 317 CYS A C     1 
ATOM   2320 O  O     . CYS A 1 338 ? -15.754 -27.861 -17.570 1.00 33.52 ? 317 CYS A O     1 
ATOM   2321 C  CB    . CYS A 1 338 ? -15.890 -30.617 -17.082 1.00 31.71 ? 317 CYS A CB    1 
ATOM   2322 S  SG    . CYS A 1 338 ? -15.126 -32.253 -16.922 1.00 34.57 ? 317 CYS A SG    1 
ATOM   2323 N  N     . PRO A 1 339 ? -16.876 -28.027 -19.497 1.00 30.48 ? 318 PRO A N     1 
ATOM   2324 C  CA    . PRO A 1 339 ? -17.053 -26.581 -19.599 1.00 30.75 ? 318 PRO A CA    1 
ATOM   2325 C  C     . PRO A 1 339 ? -18.069 -26.064 -18.568 1.00 30.23 ? 318 PRO A C     1 
ATOM   2326 O  O     . PRO A 1 339 ? -17.966 -24.904 -18.174 1.00 29.65 ? 318 PRO A O     1 
ATOM   2327 C  CB    . PRO A 1 339 ? -17.518 -26.349 -21.045 1.00 33.30 ? 318 PRO A CB    1 
ATOM   2328 C  CG    . PRO A 1 339 ? -17.864 -27.709 -21.609 1.00 33.01 ? 318 PRO A CG    1 
ATOM   2329 C  CD    . PRO A 1 339 ? -17.594 -28.755 -20.547 1.00 32.20 ? 318 PRO A CD    1 
ATOM   2330 N  N     . ASP A 1 340 ? -18.962 -26.926 -18.077 1.00 27.48 ? 319 ASP A N     1 
ATOM   2331 C  CA    . ASP A 1 340 ? -19.963 -26.479 -17.073 1.00 31.06 ? 319 ASP A CA    1 
ATOM   2332 C  C     . ASP A 1 340 ? -19.480 -26.786 -15.655 1.00 29.42 ? 319 ASP A C     1 
ATOM   2333 O  O     . ASP A 1 340 ? -20.238 -26.471 -14.751 1.00 31.07 ? 319 ASP A O     1 
ATOM   2334 C  CB    . ASP A 1 340 ? -21.340 -27.063 -17.381 1.00 33.72 ? 319 ASP A CB    1 
ATOM   2335 C  CG    . ASP A 1 340 ? -21.671 -26.900 -18.855 1.00 38.09 ? 319 ASP A CG    1 
ATOM   2336 O  OD1   . ASP A 1 340 ? -21.639 -25.739 -19.333 1.00 36.36 ? 319 ASP A OD1   1 
ATOM   2337 O  OD2   . ASP A 1 340 ? -21.867 -27.950 -19.533 1.00 42.49 ? 319 ASP A OD2   1 
ATOM   2338 N  N     . GLU A 1 341 ? -18.288 -27.367 -15.446 1.00 27.00 ? 320 GLU A N     1 
ATOM   2339 C  CA    . GLU A 1 341 ? -17.847 -27.758 -14.082 1.00 25.84 ? 320 GLU A CA    1 
ATOM   2340 C  C     . GLU A 1 341 ? -16.973 -26.636 -13.582 1.00 25.16 ? 320 GLU A C     1 
ATOM   2341 O  O     . GLU A 1 341 ? -16.503 -25.880 -14.395 1.00 30.05 ? 320 GLU A O     1 
ATOM   2342 C  CB    . GLU A 1 341 ? -17.121 -29.090 -14.059 1.00 25.64 ? 320 GLU A CB    1 
ATOM   2343 C  CG    . GLU A 1 341 ? -17.983 -30.244 -14.524 1.00 27.25 ? 320 GLU A CG    1 
ATOM   2344 C  CD    . GLU A 1 341 ? -19.033 -30.719 -13.542 1.00 25.46 ? 320 GLU A CD    1 
ATOM   2345 O  OE1   . GLU A 1 341 ? -19.820 -31.602 -13.899 1.00 23.91 ? 320 GLU A OE1   1 
ATOM   2346 O  OE2   . GLU A 1 341 ? -19.025 -30.245 -12.422 1.00 27.17 ? 320 GLU A OE2   1 
ATOM   2347 N  N     . PRO A 1 342 ? -16.786 -26.468 -12.262 1.00 25.83 ? 321 PRO A N     1 
ATOM   2348 C  CA    . PRO A 1 342 ? -15.888 -25.448 -11.717 1.00 28.32 ? 321 PRO A CA    1 
ATOM   2349 C  C     . PRO A 1 342 ? -14.388 -25.630 -12.063 1.00 29.90 ? 321 PRO A C     1 
ATOM   2350 O  O     . PRO A 1 342 ? -13.625 -24.749 -11.793 1.00 25.36 ? 321 PRO A O     1 
ATOM   2351 C  CB    . PRO A 1 342 ? -16.008 -25.582 -10.183 1.00 27.38 ? 321 PRO A CB    1 
ATOM   2352 C  CG    . PRO A 1 342 ? -17.195 -26.510 -9.918  1.00 27.60 ? 321 PRO A CG    1 
ATOM   2353 C  CD    . PRO A 1 342 ? -17.439 -27.269 -11.212 1.00 28.25 ? 321 PRO A CD    1 
ATOM   2354 N  N     . ILE A 1 343 ? -13.980 -26.791 -12.585 1.00 33.40 ? 322 ILE A N     1 
ATOM   2355 C  CA    . ILE A 1 343 ? -12.596 -26.988 -13.098 1.00 37.76 ? 322 ILE A CA    1 
ATOM   2356 C  C     . ILE A 1 343 ? -12.687 -27.177 -14.609 1.00 34.29 ? 322 ILE A C     1 
ATOM   2357 O  O     . ILE A 1 343 ? -13.573 -27.895 -15.056 1.00 32.16 ? 322 ILE A O     1 
ATOM   2358 C  CB    . ILE A 1 343 ? -11.827 -28.108 -12.356 1.00 42.27 ? 322 ILE A CB    1 
ATOM   2359 C  CG1   . ILE A 1 343 ? -12.303 -29.518 -12.715 1.00 43.77 ? 322 ILE A CG1   1 
ATOM   2360 C  CG2   . ILE A 1 343 ? -11.826 -27.856 -10.843 1.00 38.47 ? 322 ILE A CG2   1 
ATOM   2361 C  CD1   . ILE A 1 343 ? -11.312 -30.604 -12.306 1.00 45.55 ? 322 ILE A CD1   1 
ATOM   2362 N  N     . GLY A 1 344 ? -11.819 -26.490 -15.352 1.00 37.94 ? 323 GLY A N     1 
ATOM   2363 C  CA    . GLY A 1 344 ? -11.880 -26.459 -16.818 1.00 39.31 ? 323 GLY A CA    1 
ATOM   2364 C  C     . GLY A 1 344 ? -11.220 -27.690 -17.400 1.00 38.93 ? 323 GLY A C     1 
ATOM   2365 O  O     . GLY A 1 344 ? -11.949 -28.599 -17.904 1.00 39.93 ? 323 GLY A O     1 
ATOM   2366 N  N     . VAL A 1 345 ? -9.886  -27.698 -17.352 1.00 38.26 ? 324 VAL A N     1 
ATOM   2367 C  CA    . VAL A 1 345 ? -8.992  -28.705 -18.007 1.00 35.45 ? 324 VAL A CA    1 
ATOM   2368 C  C     . VAL A 1 345 ? -8.127  -29.349 -16.923 1.00 29.80 ? 324 VAL A C     1 
ATOM   2369 O  O     . VAL A 1 345 ? -7.716  -28.601 -16.002 1.00 29.70 ? 324 VAL A O     1 
ATOM   2370 C  CB    . VAL A 1 345 ? -8.105  -28.055 -19.086 1.00 38.26 ? 324 VAL A CB    1 
ATOM   2371 C  CG1   . VAL A 1 345 ? -7.133  -29.050 -19.688 1.00 37.70 ? 324 VAL A CG1   1 
ATOM   2372 C  CG2   . VAL A 1 345 ? -8.934  -27.442 -20.204 1.00 46.73 ? 324 VAL A CG2   1 
ATOM   2373 N  N     . THR A 1 346 ? -7.860  -30.652 -17.033 1.00 22.47 ? 325 THR A N     1 
ATOM   2374 C  CA    . THR A 1 346 ? -6.839  -31.353 -16.200 1.00 23.30 ? 325 THR A CA    1 
ATOM   2375 C  C     . THR A 1 346 ? -5.714  -31.900 -17.098 1.00 22.78 ? 325 THR A C     1 
ATOM   2376 O  O     . THR A 1 346 ? -5.912  -31.972 -18.339 1.00 19.50 ? 325 THR A O     1 
ATOM   2377 C  CB    . THR A 1 346 ? -7.452  -32.450 -15.308 1.00 20.34 ? 325 THR A CB    1 
ATOM   2378 O  OG1   . THR A 1 346 ? -7.863  -33.512 -16.156 1.00 19.57 ? 325 THR A OG1   1 
ATOM   2379 C  CG2   . THR A 1 346 ? -8.618  -31.989 -14.455 1.00 19.63 ? 325 THR A CG2   1 
ATOM   2380 N  N     . PHE A 1 347 ? -4.612  -32.311 -16.461 1.00 22.30 ? 326 PHE A N     1 
ATOM   2381 C  CA    . PHE A 1 347 ? -3.342  -32.750 -17.087 1.00 23.87 ? 326 PHE A CA    1 
ATOM   2382 C  C     . PHE A 1 347 ? -2.660  -33.791 -16.199 1.00 24.75 ? 326 PHE A C     1 
ATOM   2383 O  O     . PHE A 1 347 ? -2.506  -33.556 -14.975 1.00 26.89 ? 326 PHE A O     1 
ATOM   2384 C  CB    . PHE A 1 347 ? -2.355  -31.587 -17.218 1.00 25.08 ? 326 PHE A CB    1 
ATOM   2385 C  CG    . PHE A 1 347 ? -2.701  -30.513 -18.223 1.00 27.12 ? 326 PHE A CG    1 
ATOM   2386 C  CD1   . PHE A 1 347 ? -2.163  -30.536 -19.504 1.00 25.70 ? 326 PHE A CD1   1 
ATOM   2387 C  CD2   . PHE A 1 347 ? -3.518  -29.443 -17.873 1.00 27.71 ? 326 PHE A CD2   1 
ATOM   2388 C  CE1   . PHE A 1 347 ? -2.470  -29.540 -20.417 1.00 24.49 ? 326 PHE A CE1   1 
ATOM   2389 C  CE2   . PHE A 1 347 ? -3.812  -28.438 -18.783 1.00 25.22 ? 326 PHE A CE2   1 
ATOM   2390 C  CZ    . PHE A 1 347 ? -3.278  -28.489 -20.049 1.00 26.31 ? 326 PHE A CZ    1 
ATOM   2391 N  N     . ASP A 1 348 ? -2.199  -34.886 -16.803 1.00 25.25 ? 327 ASP A N     1 
ATOM   2392 C  CA    . ASP A 1 348 ? -1.329  -35.882 -16.130 1.00 24.32 ? 327 ASP A CA    1 
ATOM   2393 C  C     . ASP A 1 348 ? -0.004  -35.209 -15.723 1.00 22.78 ? 327 ASP A C     1 
ATOM   2394 O  O     . ASP A 1 348 ? 0.801   -34.866 -16.594 1.00 26.32 ? 327 ASP A O     1 
ATOM   2395 C  CB    . ASP A 1 348 ? -1.085  -37.088 -17.024 1.00 25.33 ? 327 ASP A CB    1 
ATOM   2396 C  CG    . ASP A 1 348 ? -0.328  -38.160 -16.271 1.00 26.29 ? 327 ASP A CG    1 
ATOM   2397 O  OD1   . ASP A 1 348 ? 0.246   -37.824 -15.249 1.00 29.54 ? 327 ASP A OD1   1 
ATOM   2398 O  OD2   . ASP A 1 348 ? -0.404  -39.319 -16.660 1.00 30.02 ? 327 ASP A OD2   1 
ATOM   2399 N  N     . GLY A 1 349 ? 0.205   -34.998 -14.438 1.00 20.16 ? 328 GLY A N     1 
ATOM   2400 C  CA    . GLY A 1 349 ? 1.399   -34.304 -13.924 1.00 19.63 ? 328 GLY A CA    1 
ATOM   2401 C  C     . GLY A 1 349 ? 2.395   -35.275 -13.330 1.00 17.70 ? 328 GLY A C     1 
ATOM   2402 O  O     . GLY A 1 349 ? 3.215   -34.840 -12.584 1.00 15.53 ? 328 GLY A O     1 
ATOM   2403 N  N     . THR A 1 350 ? 2.269   -36.568 -13.630 1.00 18.62 ? 329 THR A N     1 
ATOM   2404 C  CA    . THR A 1 350 ? 3.177   -37.627 -13.129 1.00 20.05 ? 329 THR A CA    1 
ATOM   2405 C  C     . THR A 1 350 ? 4.602   -37.334 -13.633 1.00 20.75 ? 329 THR A C     1 
ATOM   2406 O  O     . THR A 1 350 ? 4.814   -37.094 -14.817 1.00 19.11 ? 329 THR A O     1 
ATOM   2407 C  CB    . THR A 1 350 ? 2.594   -38.994 -13.515 1.00 21.74 ? 329 THR A CB    1 
ATOM   2408 O  OG1   . THR A 1 350 ? 1.222   -39.074 -13.103 1.00 20.83 ? 329 THR A OG1   1 
ATOM   2409 C  CG2   . THR A 1 350 ? 3.371   -40.154 -12.930 1.00 22.09 ? 329 THR A CG2   1 
ATOM   2410 N  N     . PRO A 1 351 ? 5.652   -37.339 -12.771 1.00 22.07 ? 330 PRO A N     1 
ATOM   2411 C  CA    . PRO A 1 351 ? 7.032   -37.176 -13.241 1.00 21.86 ? 330 PRO A CA    1 
ATOM   2412 C  C     . PRO A 1 351 ? 7.543   -38.352 -14.072 1.00 24.21 ? 330 PRO A C     1 
ATOM   2413 O  O     . PRO A 1 351 ? 6.859   -39.383 -14.204 1.00 23.03 ? 330 PRO A O     1 
ATOM   2414 C  CB    . PRO A 1 351 ? 7.819   -37.039 -11.936 1.00 21.64 ? 330 PRO A CB    1 
ATOM   2415 C  CG    . PRO A 1 351 ? 7.043   -37.860 -10.946 1.00 21.37 ? 330 PRO A CG    1 
ATOM   2416 C  CD    . PRO A 1 351 ? 5.599   -37.541 -11.307 1.00 23.62 ? 330 PRO A CD    1 
ATOM   2417 N  N     . PRO A 1 352 ? 8.750   -38.224 -14.682 1.00 24.83 ? 331 PRO A N     1 
ATOM   2418 C  CA    . PRO A 1 352 ? 9.261   -39.257 -15.583 1.00 26.86 ? 331 PRO A CA    1 
ATOM   2419 C  C     . PRO A 1 352 ? 9.438   -40.629 -14.913 1.00 26.47 ? 331 PRO A C     1 
ATOM   2420 O  O     . PRO A 1 352 ? 9.424   -41.596 -15.626 1.00 29.90 ? 331 PRO A O     1 
ATOM   2421 C  CB    . PRO A 1 352 ? 10.602  -38.695 -16.093 1.00 26.37 ? 331 PRO A CB    1 
ATOM   2422 C  CG    . PRO A 1 352 ? 10.465  -37.190 -15.895 1.00 25.47 ? 331 PRO A CG    1 
ATOM   2423 C  CD    . PRO A 1 352 ? 9.620   -37.037 -14.651 1.00 25.17 ? 331 PRO A CD    1 
ATOM   2424 N  N     . ALA A 1 353 ? 9.579   -40.699 -13.591 1.00 26.50 ? 332 ALA A N     1 
ATOM   2425 C  CA    . ALA A 1 353 ? 9.794   -41.970 -12.852 1.00 27.22 ? 332 ALA A CA    1 
ATOM   2426 C  C     . ALA A 1 353 ? 8.463   -42.733 -12.699 1.00 27.63 ? 332 ALA A C     1 
ATOM   2427 O  O     . ALA A 1 353 ? 8.504   -43.913 -12.418 1.00 25.47 ? 332 ALA A O     1 
ATOM   2428 C  CB    . ALA A 1 353 ? 10.438  -41.689 -11.510 1.00 29.88 ? 332 ALA A CB    1 
ATOM   2429 N  N     . GLY A 1 354 ? 7.311   -42.096 -12.915 1.00 27.91 ? 333 GLY A N     1 
ATOM   2430 C  CA    . GLY A 1 354 ? 6.045   -42.833 -13.092 1.00 28.87 ? 333 GLY A CA    1 
ATOM   2431 C  C     . GLY A 1 354 ? 5.209   -42.892 -11.819 1.00 33.04 ? 333 GLY A C     1 
ATOM   2432 O  O     . GLY A 1 354 ? 4.011   -43.306 -11.912 1.00 37.09 ? 333 GLY A O     1 
ATOM   2433 N  N     . THR A 1 355 ? 5.794   -42.525 -10.669 1.00 30.77 ? 334 THR A N     1 
ATOM   2434 C  CA    . THR A 1 355 ? 5.072   -42.279 -9.400  1.00 30.95 ? 334 THR A CA    1 
ATOM   2435 C  C     . THR A 1 355 ? 5.714   -41.064 -8.732  1.00 29.94 ? 334 THR A C     1 
ATOM   2436 O  O     . THR A 1 355 ? 6.865   -40.695 -9.012  1.00 27.59 ? 334 THR A O     1 
ATOM   2437 C  CB    . THR A 1 355 ? 5.026   -43.522 -8.479  1.00 32.48 ? 334 THR A CB    1 
ATOM   2438 O  OG1   . THR A 1 355 ? 6.314   -43.701 -7.881  1.00 29.45 ? 334 THR A OG1   1 
ATOM   2439 C  CG2   . THR A 1 355 ? 4.595   -44.795 -9.187  1.00 30.65 ? 334 THR A CG2   1 
ATOM   2440 N  N     . PRO A 1 356 ? 4.949   -40.380 -7.848  1.00 27.65 ? 335 PRO A N     1 
ATOM   2441 C  CA    . PRO A 1 356 ? 3.527   -40.685 -7.636  1.00 26.09 ? 335 PRO A CA    1 
ATOM   2442 C  C     . PRO A 1 356 ? 2.708   -40.266 -8.857  1.00 24.15 ? 335 PRO A C     1 
ATOM   2443 O  O     . PRO A 1 356 ? 3.180   -39.462 -9.626  1.00 25.18 ? 335 PRO A O     1 
ATOM   2444 C  CB    . PRO A 1 356 ? 3.131   -39.819 -6.428  1.00 25.65 ? 335 PRO A CB    1 
ATOM   2445 C  CG    . PRO A 1 356 ? 4.077   -38.644 -6.545  1.00 27.79 ? 335 PRO A CG    1 
ATOM   2446 C  CD    . PRO A 1 356 ? 5.392   -39.238 -7.042  1.00 27.60 ? 335 PRO A CD    1 
ATOM   2447 N  N     . GLY A 1 357 ? 1.506   -40.805 -9.007  1.00 24.29 ? 336 GLY A N     1 
ATOM   2448 C  CA    . GLY A 1 357 ? 0.550   -40.316 -10.018 1.00 22.57 ? 336 GLY A CA    1 
ATOM   2449 C  C     . GLY A 1 357 ? 0.029   -38.953 -9.602  1.00 20.63 ? 336 GLY A C     1 
ATOM   2450 O  O     . GLY A 1 357 ? -0.265  -38.772 -8.397  1.00 21.34 ? 336 GLY A O     1 
ATOM   2451 N  N     . ILE A 1 358 ? -0.038  -38.006 -10.532 1.00 20.64 ? 337 ILE A N     1 
ATOM   2452 C  CA    . ILE A 1 358 ? -0.548  -36.631 -10.244 1.00 21.64 ? 337 ILE A CA    1 
ATOM   2453 C  C     . ILE A 1 358 ? -1.567  -36.238 -11.317 1.00 21.02 ? 337 ILE A C     1 
ATOM   2454 O  O     . ILE A 1 358 ? -1.273  -36.403 -12.526 1.00 17.50 ? 337 ILE A O     1 
ATOM   2455 C  CB    . ILE A 1 358 ? 0.584   -35.591 -10.148 1.00 20.27 ? 337 ILE A CB    1 
ATOM   2456 C  CG1   . ILE A 1 358 ? 1.682   -36.052 -9.176  1.00 22.68 ? 337 ILE A CG1   1 
ATOM   2457 C  CG2   . ILE A 1 358 ? -0.007  -34.242 -9.797  1.00 18.55 ? 337 ILE A CG2   1 
ATOM   2458 C  CD1   . ILE A 1 358 ? 2.755   -35.024 -8.880  1.00 21.61 ? 337 ILE A CD1   1 
ATOM   2459 N  N     . VAL A 1 359 ? -2.707  -35.691 -10.873 1.00 22.16 ? 338 VAL A N     1 
ATOM   2460 C  CA    . VAL A 1 359 ? -3.651  -34.963 -11.763 1.00 21.60 ? 338 VAL A CA    1 
ATOM   2461 C  C     . VAL A 1 359 ? -3.566  -33.490 -11.406 1.00 20.01 ? 338 VAL A C     1 
ATOM   2462 O  O     . VAL A 1 359 ? -3.985  -33.189 -10.338 1.00 19.57 ? 338 VAL A O     1 
ATOM   2463 C  CB    . VAL A 1 359 ? -5.094  -35.471 -11.678 1.00 21.88 ? 338 VAL A CB    1 
ATOM   2464 C  CG1   . VAL A 1 359 ? -6.026  -34.624 -12.553 1.00 22.19 ? 338 VAL A CG1   1 
ATOM   2465 C  CG2   . VAL A 1 359 ? -5.147  -36.939 -12.042 1.00 23.04 ? 338 VAL A CG2   1 
ATOM   2466 N  N     . THR A 1 360 ? -3.090  -32.663 -12.345 1.00 21.20 ? 339 THR A N     1 
ATOM   2467 C  CA    . THR A 1 360 ? -2.880  -31.204 -12.222 1.00 22.76 ? 339 THR A CA    1 
ATOM   2468 C  C     . THR A 1 360 ? -4.038  -30.451 -12.884 1.00 21.61 ? 339 THR A C     1 
ATOM   2469 O  O     . THR A 1 360 ? -4.495  -30.896 -13.937 1.00 19.94 ? 339 THR A O     1 
ATOM   2470 C  CB    . THR A 1 360 ? -1.526  -30.845 -12.848 1.00 23.18 ? 339 THR A CB    1 
ATOM   2471 O  OG1   . THR A 1 360 ? -0.558  -31.615 -12.127 1.00 21.68 ? 339 THR A OG1   1 
ATOM   2472 C  CG2   . THR A 1 360 ? -1.223  -29.370 -12.797 1.00 23.34 ? 339 THR A CG2   1 
ATOM   2473 N  N     . GLY A 1 361 ? -4.468  -29.341 -12.268 1.00 20.91 ? 340 GLY A N     1 
ATOM   2474 C  CA    . GLY A 1 361 ? -5.547  -28.490 -12.785 1.00 19.78 ? 340 GLY A CA    1 
ATOM   2475 C  C     . GLY A 1 361 ? -5.708  -27.189 -12.027 1.00 19.27 ? 340 GLY A C     1 
ATOM   2476 O  O     . GLY A 1 361 ? -4.842  -26.806 -11.265 1.00 18.53 ? 340 GLY A O     1 
ATOM   2477 N  N     . PHE A 1 362 ? -6.820  -26.521 -12.297 1.00 19.86 ? 341 PHE A N     1 
ATOM   2478 C  CA    . PHE A 1 362 ? -7.045  -25.087 -12.015 1.00 20.39 ? 341 PHE A CA    1 
ATOM   2479 C  C     . PHE A 1 362 ? -8.543  -24.845 -11.823 1.00 21.09 ? 341 PHE A C     1 
ATOM   2480 O  O     . PHE A 1 362 ? -9.370  -25.434 -12.536 1.00 20.84 ? 341 PHE A O     1 
ATOM   2481 C  CB    . PHE A 1 362 ? -6.537  -24.215 -13.170 1.00 18.97 ? 341 PHE A CB    1 
ATOM   2482 C  CG    . PHE A 1 362 ? -5.149  -24.549 -13.667 1.00 20.40 ? 341 PHE A CG    1 
ATOM   2483 C  CD1   . PHE A 1 362 ? -4.037  -23.945 -13.104 1.00 20.16 ? 341 PHE A CD1   1 
ATOM   2484 C  CD2   . PHE A 1 362 ? -4.956  -25.439 -14.704 1.00 20.76 ? 341 PHE A CD2   1 
ATOM   2485 C  CE1   . PHE A 1 362 ? -2.774  -24.219 -13.562 1.00 20.46 ? 341 PHE A CE1   1 
ATOM   2486 C  CE2   . PHE A 1 362 ? -3.682  -25.717 -15.168 1.00 23.88 ? 341 PHE A CE2   1 
ATOM   2487 C  CZ    . PHE A 1 362 ? -2.590  -25.120 -14.573 1.00 22.11 ? 341 PHE A CZ    1 
ATOM   2488 N  N     . PHE A 1 363 ? -8.868  -24.002 -10.852 1.00 21.50 ? 342 PHE A N     1 
ATOM   2489 C  CA    . PHE A 1 363 ? -10.142 -23.259 -10.786 1.00 20.62 ? 342 PHE A CA    1 
ATOM   2490 C  C     . PHE A 1 363 ? -9.761  -21.895 -11.339 1.00 21.21 ? 342 PHE A C     1 
ATOM   2491 O  O     . PHE A 1 363 ? -8.711  -21.430 -10.913 1.00 24.17 ? 342 PHE A O     1 
ATOM   2492 C  CB    . PHE A 1 363 ? -10.676 -23.144 -9.359  1.00 19.79 ? 342 PHE A CB    1 
ATOM   2493 C  CG    . PHE A 1 363 ? -10.904 -24.411 -8.579  1.00 17.67 ? 342 PHE A CG    1 
ATOM   2494 C  CD1   . PHE A 1 363 ? -12.186 -24.898 -8.398  1.00 17.89 ? 342 PHE A CD1   1 
ATOM   2495 C  CD2   . PHE A 1 363 ? -9.881  -24.995 -7.865  1.00 16.82 ? 342 PHE A CD2   1 
ATOM   2496 C  CE1   . PHE A 1 363 ? -12.411 -26.012 -7.608  1.00 18.53 ? 342 PHE A CE1   1 
ATOM   2497 C  CE2   . PHE A 1 363 ? -10.106 -26.116 -7.083  1.00 17.36 ? 342 PHE A CE2   1 
ATOM   2498 C  CZ    . PHE A 1 363 ? -11.371 -26.614 -6.938  1.00 16.98 ? 342 PHE A CZ    1 
ATOM   2499 N  N     . GLU A 1 364 ? -10.499 -21.376 -12.313 1.00 22.92 ? 343 GLU A N     1 
ATOM   2500 C  CA    . GLU A 1 364 ? -10.140 -20.177 -13.106 1.00 22.57 ? 343 GLU A CA    1 
ATOM   2501 C  C     . GLU A 1 364 ? -11.237 -19.147 -12.899 1.00 22.24 ? 343 GLU A C     1 
ATOM   2502 O  O     . GLU A 1 364 ? -12.392 -19.557 -12.774 1.00 21.50 ? 343 GLU A O     1 
ATOM   2503 C  CB    . GLU A 1 364 ? -10.065 -20.521 -14.588 1.00 24.19 ? 343 GLU A CB    1 
ATOM   2504 C  CG    . GLU A 1 364 ? -9.075  -21.642 -14.950 1.00 27.22 ? 343 GLU A CG    1 
ATOM   2505 C  CD    . GLU A 1 364 ? -7.606  -21.261 -14.818 1.00 27.95 ? 343 GLU A CD    1 
ATOM   2506 O  OE1   . GLU A 1 364 ? -6.727  -21.924 -15.465 1.00 29.17 ? 343 GLU A OE1   1 
ATOM   2507 O  OE2   . GLU A 1 364 ? -7.329  -20.293 -14.082 1.00 30.41 ? 343 GLU A OE2   1 
ATOM   2508 N  N     . GLY A 1 365 ? -10.894 -17.866 -12.910 1.00 22.47 ? 344 GLY A N     1 
ATOM   2509 C  CA    . GLY A 1 365 ? -11.897 -16.786 -12.903 1.00 21.71 ? 344 GLY A CA    1 
ATOM   2510 C  C     . GLY A 1 365 ? -12.860 -16.940 -11.723 1.00 21.05 ? 344 GLY A C     1 
ATOM   2511 O  O     . GLY A 1 365 ? -12.408 -17.163 -10.597 1.00 20.11 ? 344 GLY A O     1 
ATOM   2512 N  N     . PRO A 1 366 ? -14.191 -16.834 -11.950 1.00 18.78 ? 345 PRO A N     1 
ATOM   2513 C  CA    . PRO A 1 366 ? -15.190 -16.854 -10.874 1.00 19.41 ? 345 PRO A CA    1 
ATOM   2514 C  C     . PRO A 1 366 ? -15.133 -18.117 -10.010 1.00 17.59 ? 345 PRO A C     1 
ATOM   2515 O  O     . PRO A 1 366 ? -15.359 -17.995 -8.861  1.00 14.56 ? 345 PRO A O     1 
ATOM   2516 C  CB    . PRO A 1 366 ? -16.554 -16.827 -11.605 1.00 19.26 ? 345 PRO A CB    1 
ATOM   2517 C  CG    . PRO A 1 366 ? -16.218 -16.154 -12.934 1.00 19.39 ? 345 PRO A CG    1 
ATOM   2518 C  CD    . PRO A 1 366 ? -14.833 -16.676 -13.262 1.00 19.67 ? 345 PRO A CD    1 
ATOM   2519 N  N     . ALA A 1 367 ? -14.838 -19.278 -10.609 1.00 16.92 ? 346 ALA A N     1 
ATOM   2520 C  CA    . ALA A 1 367 ? -14.809 -20.563 -9.890  1.00 16.81 ? 346 ALA A CA    1 
ATOM   2521 C  C     . ALA A 1 367 ? -13.595 -20.567 -8.956  1.00 17.04 ? 346 ALA A C     1 
ATOM   2522 O  O     . ALA A 1 367 ? -13.666 -21.263 -7.924  1.00 19.82 ? 346 ALA A O     1 
ATOM   2523 C  CB    . ALA A 1 367 ? -14.830 -21.734 -10.850 1.00 16.59 ? 346 ALA A CB    1 
ATOM   2524 N  N     . ALA A 1 368 ? -12.572 -19.767 -9.256  1.00 17.24 ? 347 ALA A N     1 
ATOM   2525 C  CA    . ALA A 1 368 ? -11.351 -19.658 -8.442  1.00 19.27 ? 347 ALA A CA    1 
ATOM   2526 C  C     . ALA A 1 368 ? -11.624 -18.774 -7.227  1.00 19.78 ? 347 ALA A C     1 
ATOM   2527 O  O     . ALA A 1 368 ? -11.135 -19.128 -6.127  1.00 21.03 ? 347 ALA A O     1 
ATOM   2528 C  CB    . ALA A 1 368 ? -10.173 -19.140 -9.236  1.00 19.37 ? 347 ALA A CB    1 
ATOM   2529 N  N     . VAL A 1 369 ? -12.360 -17.683 -7.406  1.00 21.08 ? 348 VAL A N     1 
ATOM   2530 C  CA    . VAL A 1 369 ? -12.757 -16.756 -6.295  1.00 22.60 ? 348 VAL A CA    1 
ATOM   2531 C  C     . VAL A 1 369 ? -13.640 -17.525 -5.294  1.00 22.36 ? 348 VAL A C     1 
ATOM   2532 O  O     . VAL A 1 369 ? -13.401 -17.390 -4.096  1.00 21.88 ? 348 VAL A O     1 
ATOM   2533 C  CB    . VAL A 1 369 ? -13.501 -15.515 -6.851  1.00 26.19 ? 348 VAL A CB    1 
ATOM   2534 C  CG1   . VAL A 1 369 ? -13.981 -14.584 -5.734  1.00 27.03 ? 348 VAL A CG1   1 
ATOM   2535 C  CG2   . VAL A 1 369 ? -12.657 -14.748 -7.875  1.00 25.05 ? 348 VAL A CG2   1 
ATOM   2536 N  N     . ALA A 1 370 ? -14.639 -18.279 -5.784  1.00 21.34 ? 349 ALA A N     1 
ATOM   2537 C  CA    . ALA A 1 370 ? -15.574 -19.118 -4.986  1.00 23.16 ? 349 ALA A CA    1 
ATOM   2538 C  C     . ALA A 1 370 ? -14.822 -20.205 -4.215  1.00 21.93 ? 349 ALA A C     1 
ATOM   2539 O  O     . ALA A 1 370 ? -15.117 -20.366 -3.050  1.00 22.49 ? 349 ALA A O     1 
ATOM   2540 C  CB    . ALA A 1 370 ? -16.664 -19.725 -5.862  1.00 22.48 ? 349 ALA A CB    1 
ATOM   2541 N  N     . ALA A 1 371 ? -13.870 -20.888 -4.858  1.00 25.69 ? 350 ALA A N     1 
ATOM   2542 C  CA    . ALA A 1 371 ? -13.007 -21.951 -4.266  1.00 24.38 ? 350 ALA A CA    1 
ATOM   2543 C  C     . ALA A 1 371 ? -12.068 -21.376 -3.199  1.00 23.24 ? 350 ALA A C     1 
ATOM   2544 O  O     . ALA A 1 371 ? -11.808 -22.086 -2.186  1.00 20.67 ? 350 ALA A O     1 
ATOM   2545 C  CB    . ALA A 1 371 ? -12.190 -22.640 -5.334  1.00 25.29 ? 350 ALA A CB    1 
ATOM   2546 N  N     . GLY A 1 372 ? -11.592 -20.148 -3.422  1.00 22.63 ? 351 GLY A N     1 
ATOM   2547 C  CA    . GLY A 1 372 ? -10.600 -19.475 -2.564  1.00 23.36 ? 351 GLY A CA    1 
ATOM   2548 C  C     . GLY A 1 372 ? -11.203 -19.104 -1.225  1.00 23.98 ? 351 GLY A C     1 
ATOM   2549 O  O     . GLY A 1 372 ? -10.466 -18.971 -0.256  1.00 20.00 ? 351 GLY A O     1 
ATOM   2550 N  N     . ALA A 1 373 ? -12.531 -18.980 -1.190  1.00 25.83 ? 352 ALA A N     1 
ATOM   2551 C  CA    . ALA A 1 373 ? -13.291 -18.513 -0.019  1.00 28.98 ? 352 ALA A CA    1 
ATOM   2552 C  C     . ALA A 1 373 ? -13.527 -19.723 0.890   1.00 27.18 ? 352 ALA A C     1 
ATOM   2553 O  O     . ALA A 1 373 ? -14.000 -19.527 2.017   1.00 27.20 ? 352 ALA A O     1 
ATOM   2554 C  CB    . ALA A 1 373 ? -14.571 -17.845 -0.490  1.00 28.27 ? 352 ALA A CB    1 
ATOM   2555 N  N     . ARG A 1 374 ? -13.188 -20.914 0.398   1.00 24.68 ? 353 ARG A N     1 
ATOM   2556 C  CA    . ARG A 1 374 ? -13.504 -22.222 1.032   1.00 26.11 ? 353 ARG A CA    1 
ATOM   2557 C  C     . ARG A 1 374 ? -12.174 -22.781 1.540   1.00 26.76 ? 353 ARG A C     1 
ATOM   2558 O  O     . ARG A 1 374 ? -11.137 -22.157 1.267   1.00 27.90 ? 353 ARG A O     1 
ATOM   2559 C  CB    . ARG A 1 374 ? -14.257 -23.116 0.022   1.00 28.38 ? 353 ARG A CB    1 
ATOM   2560 C  CG    . ARG A 1 374 ? -15.617 -22.577 -0.441  1.00 27.21 ? 353 ARG A CG    1 
ATOM   2561 C  CD    . ARG A 1 374 ? -16.334 -23.386 -1.523  1.00 29.66 ? 353 ARG A CD    1 
ATOM   2562 N  NE    . ARG A 1 374 ? -16.726 -24.722 -1.057  1.00 33.18 ? 353 ARG A NE    1 
ATOM   2563 C  CZ    . ARG A 1 374 ? -17.421 -25.643 -1.745  1.00 35.82 ? 353 ARG A CZ    1 
ATOM   2564 N  NH1   . ARG A 1 374 ? -17.857 -25.409 -2.973  1.00 40.09 ? 353 ARG A NH1   1 
ATOM   2565 N  NH2   . ARG A 1 374 ? -17.705 -26.808 -1.196  1.00 34.59 ? 353 ARG A NH2   1 
ATOM   2566 N  N     . THR A 1 375 ? -12.180 -23.889 2.281   1.00 26.12 ? 354 THR A N     1 
ATOM   2567 C  CA    . THR A 1 375 ? -10.940 -24.545 2.786   1.00 23.50 ? 354 THR A CA    1 
ATOM   2568 C  C     . THR A 1 375 ? -10.353 -25.477 1.722   1.00 23.38 ? 354 THR A C     1 
ATOM   2569 O  O     . THR A 1 375 ? -11.071 -25.859 0.735   1.00 20.82 ? 354 THR A O     1 
ATOM   2570 C  CB    . THR A 1 375 ? -11.173 -25.345 4.077   1.00 21.69 ? 354 THR A CB    1 
ATOM   2571 O  OG1   . THR A 1 375 ? -11.788 -26.547 3.663   1.00 18.37 ? 354 THR A OG1   1 
ATOM   2572 C  CG2   . THR A 1 375 ? -12.037 -24.642 5.101   1.00 21.59 ? 354 THR A CG2   1 
ATOM   2573 N  N     . ARG A 1 376 ? -9.098  -25.860 1.959   1.00 24.15 ? 355 ARG A N     1 
ATOM   2574 C  CA    . ARG A 1 376 ? -8.355  -26.900 1.211   1.00 24.62 ? 355 ARG A CA    1 
ATOM   2575 C  C     . ARG A 1 376 ? -9.260  -28.128 1.004   1.00 25.00 ? 355 ARG A C     1 
ATOM   2576 O  O     . ARG A 1 376 ? -9.347  -28.658 -0.128  1.00 24.13 ? 355 ARG A O     1 
ATOM   2577 C  CB    . ARG A 1 376 ? -7.074  -27.241 1.990   1.00 24.81 ? 355 ARG A CB    1 
ATOM   2578 C  CG    . ARG A 1 376 ? -6.042  -28.018 1.186   1.00 27.15 ? 355 ARG A CG    1 
ATOM   2579 C  CD    . ARG A 1 376 ? -5.129  -28.886 2.027   1.00 28.68 ? 355 ARG A CD    1 
ATOM   2580 N  NE    . ARG A 1 376 ? -5.870  -30.006 2.634   1.00 30.95 ? 355 ARG A NE    1 
ATOM   2581 C  CZ    . ARG A 1 376 ? -5.785  -31.285 2.276   1.00 27.68 ? 355 ARG A CZ    1 
ATOM   2582 N  NH1   . ARG A 1 376 ? -4.974  -31.679 1.313   1.00 29.15 ? 355 ARG A NH1   1 
ATOM   2583 N  NH2   . ARG A 1 376 ? -6.529  -32.179 2.889   1.00 28.80 ? 355 ARG A NH2   1 
ATOM   2584 N  N     . GLU A 1 377 ? -9.911  -28.585 2.072   1.00 26.82 ? 356 GLU A N     1 
ATOM   2585 C  CA    . GLU A 1 377 ? -10.675 -29.863 2.088   1.00 28.82 ? 356 GLU A CA    1 
ATOM   2586 C  C     . GLU A 1 377 ? -11.912 -29.736 1.206   1.00 26.70 ? 356 GLU A C     1 
ATOM   2587 O  O     . GLU A 1 377 ? -12.216 -30.703 0.509   1.00 26.82 ? 356 GLU A O     1 
ATOM   2588 C  CB    . GLU A 1 377 ? -11.064 -30.274 3.513   1.00 30.04 ? 356 GLU A CB    1 
ATOM   2589 C  CG    . GLU A 1 377 ? -9.898  -30.850 4.272   1.00 28.74 ? 356 GLU A CG    1 
ATOM   2590 C  CD    . GLU A 1 377 ? -8.920  -29.810 4.765   1.00 31.61 ? 356 GLU A CD    1 
ATOM   2591 O  OE1   . GLU A 1 377 ? -7.708  -30.077 4.687   1.00 32.52 ? 356 GLU A OE1   1 
ATOM   2592 O  OE2   . GLU A 1 377 ? -9.379  -28.726 5.211   1.00 32.59 ? 356 GLU A OE2   1 
ATOM   2593 N  N     . GLU A 1 378 ? -12.558 -28.571 1.188   1.00 26.71 ? 357 GLU A N     1 
ATOM   2594 C  CA    . GLU A 1 378 ? -13.743 -28.346 0.317   1.00 26.13 ? 357 GLU A CA    1 
ATOM   2595 C  C     . GLU A 1 378 ? -13.330 -28.325 -1.165  1.00 28.46 ? 357 GLU A C     1 
ATOM   2596 O  O     . GLU A 1 378 ? -14.134 -28.799 -1.999  1.00 27.24 ? 357 GLU A O     1 
ATOM   2597 C  CB    . GLU A 1 378 ? -14.430 -27.038 0.682   1.00 26.36 ? 357 GLU A CB    1 
ATOM   2598 C  CG    . GLU A 1 378 ? -15.135 -27.103 2.011   1.00 25.34 ? 357 GLU A CG    1 
ATOM   2599 C  CD    . GLU A 1 378 ? -15.705 -25.766 2.442   1.00 26.27 ? 357 GLU A CD    1 
ATOM   2600 O  OE1   . GLU A 1 378 ? -16.948 -25.600 2.409   1.00 27.49 ? 357 GLU A OE1   1 
ATOM   2601 O  OE2   . GLU A 1 378 ? -14.905 -24.905 2.813   1.00 24.53 ? 357 GLU A OE2   1 
ATOM   2602 N  N     . ARG A 1 379 ? -12.145 -27.779 -1.496  1.00 26.42 ? 358 ARG A N     1 
ATOM   2603 C  CA    . ARG A 1 379 ? -11.676 -27.695 -2.898  1.00 24.11 ? 358 ARG A CA    1 
ATOM   2604 C  C     . ARG A 1 379 ? -11.330 -29.110 -3.357  1.00 25.32 ? 358 ARG A C     1 
ATOM   2605 O  O     . ARG A 1 379 ? -11.771 -29.492 -4.446  1.00 25.82 ? 358 ARG A O     1 
ATOM   2606 C  CB    . ARG A 1 379 ? -10.485 -26.746 -3.016  1.00 24.68 ? 358 ARG A CB    1 
ATOM   2607 C  CG    . ARG A 1 379 ? -10.866 -25.285 -2.841  1.00 24.93 ? 358 ARG A CG    1 
ATOM   2608 C  CD    . ARG A 1 379 ? -9.751  -24.339 -3.235  1.00 26.55 ? 358 ARG A CD    1 
ATOM   2609 N  NE    . ARG A 1 379 ? -8.543  -24.495 -2.432  1.00 25.50 ? 358 ARG A NE    1 
ATOM   2610 C  CZ    . ARG A 1 379 ? -8.199  -23.731 -1.395  1.00 27.19 ? 358 ARG A CZ    1 
ATOM   2611 N  NH1   . ARG A 1 379 ? -8.990  -22.756 -0.987  1.00 26.99 ? 358 ARG A NH1   1 
ATOM   2612 N  NH2   . ARG A 1 379 ? -7.056  -23.948 -0.758  1.00 24.86 ? 358 ARG A NH2   1 
ATOM   2613 N  N     . ARG A 1 380 ? -10.595 -29.859 -2.531  1.00 23.56 ? 359 ARG A N     1 
ATOM   2614 C  CA    . ARG A 1 380 ? -10.268 -31.288 -2.761  1.00 22.25 ? 359 ARG A CA    1 
ATOM   2615 C  C     . ARG A 1 380 ? -11.559 -32.058 -3.152  1.00 21.72 ? 359 ARG A C     1 
ATOM   2616 O  O     . ARG A 1 380 ? -11.563 -32.796 -4.164  1.00 19.08 ? 359 ARG A O     1 
ATOM   2617 C  CB    . ARG A 1 380 ? -9.590  -31.838 -1.494  1.00 20.21 ? 359 ARG A CB    1 
ATOM   2618 C  CG    . ARG A 1 380 ? -9.329  -33.341 -1.541  1.00 22.76 ? 359 ARG A CG    1 
ATOM   2619 C  CD    . ARG A 1 380 ? -9.050  -33.966 -0.185  1.00 21.13 ? 359 ARG A CD    1 
ATOM   2620 N  NE    . ARG A 1 380 ? -10.302 -34.013 0.531   1.00 22.49 ? 359 ARG A NE    1 
ATOM   2621 C  CZ    . ARG A 1 380 ? -10.438 -34.062 1.843   1.00 23.47 ? 359 ARG A CZ    1 
ATOM   2622 N  NH1   . ARG A 1 380 ? -9.373  -34.030 2.638   1.00 24.79 ? 359 ARG A NH1   1 
ATOM   2623 N  NH2   . ARG A 1 380 ? -11.656 -34.128 2.350   1.00 21.34 ? 359 ARG A NH2   1 
ATOM   2624 N  N     . ASP A 1 381 ? -12.618 -31.916 -2.359  1.00 23.06 ? 360 ASP A N     1 
ATOM   2625 C  CA    . ASP A 1 381 ? -13.904 -32.655 -2.521  1.00 23.11 ? 360 ASP A CA    1 
ATOM   2626 C  C     . ASP A 1 381 ? -14.526 -32.251 -3.861  1.00 20.44 ? 360 ASP A C     1 
ATOM   2627 O  O     . ASP A 1 381 ? -14.935 -33.143 -4.586  1.00 18.54 ? 360 ASP A O     1 
ATOM   2628 C  CB    . ASP A 1 381 ? -14.807 -32.441 -1.299  1.00 23.31 ? 360 ASP A CB    1 
ATOM   2629 C  CG    . ASP A 1 381 ? -14.225 -32.951 0.021   1.00 23.43 ? 360 ASP A CG    1 
ATOM   2630 O  OD1   . ASP A 1 381 ? -13.282 -33.724 -0.015  1.00 24.20 ? 360 ASP A OD1   1 
ATOM   2631 O  OD2   . ASP A 1 381 ? -14.706 -32.524 1.084   1.00 26.84 ? 360 ASP A OD2   1 
ATOM   2632 N  N     . VAL A 1 382 ? -14.494 -30.972 -4.241  1.00 20.35 ? 361 VAL A N     1 
ATOM   2633 C  CA    . VAL A 1 382 ? -15.024 -30.542 -5.576  1.00 19.80 ? 361 VAL A CA    1 
ATOM   2634 C  C     . VAL A 1 382 ? -14.195 -31.188 -6.708  1.00 18.74 ? 361 VAL A C     1 
ATOM   2635 O  O     . VAL A 1 382 ? -14.831 -31.729 -7.667  1.00 20.22 ? 361 VAL A O     1 
ATOM   2636 C  CB    . VAL A 1 382 ? -15.112 -29.010 -5.715  1.00 21.54 ? 361 VAL A CB    1 
ATOM   2637 C  CG1   . VAL A 1 382 ? -15.651 -28.587 -7.087  1.00 21.27 ? 361 VAL A CG1   1 
ATOM   2638 C  CG2   . VAL A 1 382 ? -15.962 -28.402 -4.611  1.00 22.43 ? 361 VAL A CG2   1 
ATOM   2639 N  N     . VAL A 1 383 ? -12.852 -31.126 -6.650  1.00 16.58 ? 362 VAL A N     1 
ATOM   2640 C  CA    . VAL A 1 383 ? -11.944 -31.681 -7.703  1.00 16.47 ? 362 VAL A CA    1 
ATOM   2641 C  C     . VAL A 1 383 ? -12.208 -33.189 -7.840  1.00 18.21 ? 362 VAL A C     1 
ATOM   2642 O  O     . VAL A 1 383 ? -12.589 -33.674 -8.950  1.00 18.25 ? 362 VAL A O     1 
ATOM   2643 C  CB    . VAL A 1 383 ? -10.481 -31.386 -7.355  1.00 17.61 ? 362 VAL A CB    1 
ATOM   2644 C  CG1   . VAL A 1 383 ? -9.520  -32.144 -8.260  1.00 17.06 ? 362 VAL A CG1   1 
ATOM   2645 C  CG2   . VAL A 1 383 ? -10.200 -29.890 -7.384  1.00 17.63 ? 362 VAL A CG2   1 
ATOM   2646 N  N     . VAL A 1 384 ? -12.054 -33.912 -6.727  1.00 18.22 ? 363 VAL A N     1 
ATOM   2647 C  CA    . VAL A 1 384 ? -12.285 -35.374 -6.615  1.00 19.94 ? 363 VAL A CA    1 
ATOM   2648 C  C     . VAL A 1 384 ? -13.706 -35.725 -7.120  1.00 20.64 ? 363 VAL A C     1 
ATOM   2649 O  O     . VAL A 1 384 ? -13.840 -36.702 -7.877  1.00 19.21 ? 363 VAL A O     1 
ATOM   2650 C  CB    . VAL A 1 384 ? -11.982 -35.776 -5.157  1.00 23.32 ? 363 VAL A CB    1 
ATOM   2651 C  CG1   . VAL A 1 384 ? -12.710 -37.024 -4.696  1.00 25.21 ? 363 VAL A CG1   1 
ATOM   2652 C  CG2   . VAL A 1 384 ? -10.493 -35.890 -4.926  1.00 20.89 ? 363 VAL A CG2   1 
ATOM   2653 N  N     . ASP A 1 385 ? -14.736 -34.909 -6.865  1.00 20.91 ? 364 ASP A N     1 
ATOM   2654 C  CA    . ASP A 1 385 ? -16.100 -35.211 -7.380  1.00 19.92 ? 364 ASP A CA    1 
ATOM   2655 C  C     . ASP A 1 385 ? -16.087 -35.161 -8.905  1.00 21.12 ? 364 ASP A C     1 
ATOM   2656 O  O     . ASP A 1 385 ? -16.442 -36.173 -9.555  1.00 21.00 ? 364 ASP A O     1 
ATOM   2657 C  CB    . ASP A 1 385 ? -17.195 -34.276 -6.856  1.00 23.02 ? 364 ASP A CB    1 
ATOM   2658 C  CG    . ASP A 1 385 ? -18.579 -34.689 -7.351  1.00 23.74 ? 364 ASP A CG    1 
ATOM   2659 O  OD1   . ASP A 1 385 ? -19.010 -35.812 -6.958  1.00 21.67 ? 364 ASP A OD1   1 
ATOM   2660 O  OD2   . ASP A 1 385 ? -19.191 -33.920 -8.198  1.00 24.42 ? 364 ASP A OD2   1 
ATOM   2661 N  N     . VAL A 1 386 ? -15.631 -34.059 -9.483  1.00 21.10 ? 365 VAL A N     1 
ATOM   2662 C  CA    . VAL A 1 386 ? -15.504 -33.966 -10.967 1.00 21.32 ? 365 VAL A CA    1 
ATOM   2663 C  C     . VAL A 1 386 ? -14.684 -35.143 -11.527 1.00 21.59 ? 365 VAL A C     1 
ATOM   2664 O  O     . VAL A 1 386 ? -15.135 -35.748 -12.531 1.00 21.46 ? 365 VAL A O     1 
ATOM   2665 C  CB    . VAL A 1 386 ? -14.918 -32.606 -11.395 1.00 23.63 ? 365 VAL A CB    1 
ATOM   2666 C  CG1   . VAL A 1 386 ? -14.702 -32.544 -12.900 1.00 23.08 ? 365 VAL A CG1   1 
ATOM   2667 C  CG2   . VAL A 1 386 ? -15.784 -31.428 -10.896 1.00 21.81 ? 365 VAL A CG2   1 
ATOM   2668 N  N     . LEU A 1 387 ? -13.489 -35.426 -10.996 1.00 21.98 ? 366 LEU A N     1 
ATOM   2669 C  CA    . LEU A 1 387 ? -12.645 -36.528 -11.524 1.00 22.36 ? 366 LEU A CA    1 
ATOM   2670 C  C     . LEU A 1 387 ? -13.416 -37.853 -11.421 1.00 23.37 ? 366 LEU A C     1 
ATOM   2671 O  O     . LEU A 1 387 ? -13.318 -38.682 -12.376 1.00 25.45 ? 366 LEU A O     1 
ATOM   2672 C  CB    . LEU A 1 387 ? -11.297 -36.599 -10.786 1.00 24.22 ? 366 LEU A CB    1 
ATOM   2673 C  CG    . LEU A 1 387 ? -10.369 -35.394 -10.972 1.00 24.39 ? 366 LEU A CG    1 
ATOM   2674 C  CD1   . LEU A 1 387 ? -9.078  -35.553 -10.181 1.00 24.32 ? 366 LEU A CD1   1 
ATOM   2675 C  CD2   . LEU A 1 387 ? -10.057 -35.159 -12.443 1.00 25.17 ? 366 LEU A CD2   1 
ATOM   2676 N  N     . ALA A 1 388 ? -14.183 -38.072 -10.344 1.00 23.41 ? 367 ALA A N     1 
ATOM   2677 C  CA    . ALA A 1 388 ? -14.843 -39.372 -10.103 1.00 24.36 ? 367 ALA A CA    1 
ATOM   2678 C  C     . ALA A 1 388 ? -15.879 -39.597 -11.205 1.00 22.81 ? 367 ALA A C     1 
ATOM   2679 O  O     . ALA A 1 388 ? -16.007 -40.752 -11.697 1.00 23.63 ? 367 ALA A O     1 
ATOM   2680 C  CB    . ALA A 1 388 ? -15.440 -39.453 -8.728  1.00 26.51 ? 367 ALA A CB    1 
ATOM   2681 N  N     . ARG A 1 389 ? -16.520 -38.528 -11.647 1.00 22.57 ? 368 ARG A N     1 
ATOM   2682 C  CA    . ARG A 1 389 ? -17.586 -38.608 -12.680 1.00 26.74 ? 368 ARG A CA    1 
ATOM   2683 C  C     . ARG A 1 389 ? -16.987 -38.607 -14.084 1.00 24.79 ? 368 ARG A C     1 
ATOM   2684 O  O     . ARG A 1 389 ? -17.785 -38.608 -15.021 1.00 25.72 ? 368 ARG A O     1 
ATOM   2685 C  CB    . ARG A 1 389 ? -18.587 -37.453 -12.555 1.00 25.47 ? 368 ARG A CB    1 
ATOM   2686 C  CG    . ARG A 1 389 ? -19.468 -37.554 -11.327 1.00 24.06 ? 368 ARG A CG    1 
ATOM   2687 C  CD    . ARG A 1 389 ? -20.404 -36.366 -11.224 1.00 21.84 ? 368 ARG A CD    1 
ATOM   2688 N  NE    . ARG A 1 389 ? -19.764 -35.149 -10.757 1.00 21.09 ? 368 ARG A NE    1 
ATOM   2689 C  CZ    . ARG A 1 389 ? -19.757 -33.958 -11.379 1.00 19.94 ? 368 ARG A CZ    1 
ATOM   2690 N  NH1   . ARG A 1 389 ? -20.332 -33.810 -12.556 1.00 18.15 ? 368 ARG A NH1   1 
ATOM   2691 N  NH2   . ARG A 1 389 ? -19.171 -32.911 -10.804 1.00 18.78 ? 368 ARG A NH2   1 
ATOM   2692 N  N     . THR A 1 390 ? -15.660 -38.580 -14.224 1.00 26.95 ? 369 THR A N     1 
ATOM   2693 C  CA    . THR A 1 390 ? -14.974 -38.476 -15.537 1.00 26.71 ? 369 THR A CA    1 
ATOM   2694 C  C     . THR A 1 390 ? -13.931 -39.597 -15.662 1.00 29.15 ? 369 THR A C     1 
ATOM   2695 O  O     . THR A 1 390 ? -14.155 -40.487 -16.490 1.00 28.98 ? 369 THR A O     1 
ATOM   2696 C  CB    . THR A 1 390 ? -14.400 -37.066 -15.706 1.00 28.14 ? 369 THR A CB    1 
ATOM   2697 O  OG1   . THR A 1 390 ? -13.744 -36.783 -14.481 1.00 28.68 ? 369 THR A OG1   1 
ATOM   2698 C  CG2   . THR A 1 390 ? -15.440 -35.995 -15.959 1.00 29.36 ? 369 THR A CG2   1 
ATOM   2699 N  N     . LEU A 1 391 ? -12.835 -39.542 -14.886 1.00 31.60 ? 370 LEU A N     1 
ATOM   2700 C  CA    . LEU A 1 391 ? -11.739 -40.550 -14.915 1.00 28.08 ? 370 LEU A CA    1 
ATOM   2701 C  C     . LEU A 1 391 ? -12.256 -41.842 -14.289 1.00 27.98 ? 370 LEU A C     1 
ATOM   2702 O  O     . LEU A 1 391 ? -11.885 -42.898 -14.765 1.00 34.51 ? 370 LEU A O     1 
ATOM   2703 C  CB    . LEU A 1 391 ? -10.479 -40.045 -14.196 1.00 27.44 ? 370 LEU A CB    1 
ATOM   2704 C  CG    . LEU A 1 391 ? -9.698  -38.866 -14.821 1.00 27.12 ? 370 LEU A CG    1 
ATOM   2705 C  CD1   . LEU A 1 391 ? -8.528  -38.451 -13.933 1.00 26.51 ? 370 LEU A CD1   1 
ATOM   2706 C  CD2   . LEU A 1 391 ? -9.168  -39.160 -16.214 1.00 25.66 ? 370 LEU A CD2   1 
ATOM   2707 N  N     . GLY A 1 392 ? -13.099 -41.785 -13.264 1.00 31.79 ? 371 GLY A N     1 
ATOM   2708 C  CA    . GLY A 1 392 ? -13.547 -43.022 -12.583 1.00 31.20 ? 371 GLY A CA    1 
ATOM   2709 C  C     . GLY A 1 392 ? -13.550 -42.914 -11.063 1.00 30.84 ? 371 GLY A C     1 
ATOM   2710 O  O     . GLY A 1 392 ? -12.856 -42.032 -10.493 1.00 25.37 ? 371 GLY A O     1 
ATOM   2711 N  N     . GLU A 1 393 ? -14.294 -43.815 -10.421 1.00 31.92 ? 372 GLU A N     1 
ATOM   2712 C  CA    . GLU A 1 393 ? -14.719 -43.655 -9.011  1.00 35.11 ? 372 GLU A CA    1 
ATOM   2713 C  C     . GLU A 1 393 ? -13.488 -43.807 -8.134  1.00 30.22 ? 372 GLU A C     1 
ATOM   2714 O  O     . GLU A 1 393 ? -13.500 -43.249 -7.024  1.00 30.08 ? 372 GLU A O     1 
ATOM   2715 C  CB    . GLU A 1 393 ? -15.825 -44.639 -8.633  1.00 39.52 ? 372 GLU A CB    1 
ATOM   2716 C  CG    . GLU A 1 393 ? -16.761 -44.103 -7.559  1.00 45.41 ? 372 GLU A CG    1 
ATOM   2717 C  CD    . GLU A 1 393 ? -17.489 -42.797 -7.854  1.00 46.15 ? 372 GLU A CD    1 
ATOM   2718 O  OE1   . GLU A 1 393 ? -18.033 -42.625 -8.968  1.00 49.17 ? 372 GLU A OE1   1 
ATOM   2719 O  OE2   . GLU A 1 393 ? -17.516 -41.958 -6.963  1.00 43.38 ? 372 GLU A OE2   1 
ATOM   2720 N  N     . ARG A 1 394 ? -12.453 -44.468 -8.660  1.00 30.36 ? 373 ARG A N     1 
ATOM   2721 C  CA    . ARG A 1 394 ? -11.162 -44.684 -7.951  1.00 30.36 ? 373 ARG A CA    1 
ATOM   2722 C  C     . ARG A 1 394 ? -10.503 -43.323 -7.664  1.00 25.71 ? 373 ARG A C     1 
ATOM   2723 O  O     . ARG A 1 394 ? -9.652  -43.274 -6.809  1.00 24.44 ? 373 ARG A O     1 
ATOM   2724 C  CB    . ARG A 1 394 ? -10.283 -45.626 -8.777  1.00 37.55 ? 373 ARG A CB    1 
ATOM   2725 C  CG    . ARG A 1 394 ? -8.810  -45.611 -8.386  1.00 44.71 ? 373 ARG A CG    1 
ATOM   2726 C  CD    . ARG A 1 394 ? -8.033  -46.726 -9.044  1.00 46.52 ? 373 ARG A CD    1 
ATOM   2727 N  NE    . ARG A 1 394 ? -6.795  -47.031 -8.335  1.00 48.81 ? 373 ARG A NE    1 
ATOM   2728 C  CZ    . ARG A 1 394 ? -6.105  -48.166 -8.501  1.00 49.29 ? 373 ARG A CZ    1 
ATOM   2729 N  NH1   . ARG A 1 394 ? -6.545  -49.098 -9.329  1.00 48.51 ? 373 ARG A NH1   1 
ATOM   2730 N  NH2   . ARG A 1 394 ? -4.987  -48.373 -7.834  1.00 47.58 ? 373 ARG A NH2   1 
ATOM   2731 N  N     . ALA A 1 395 ? -10.900 -42.245 -8.343  1.00 24.23 ? 374 ALA A N     1 
ATOM   2732 C  CA    . ALA A 1 395 ? -10.373 -40.882 -8.120  1.00 24.89 ? 374 ALA A CA    1 
ATOM   2733 C  C     . ALA A 1 395 ? -10.669 -40.392 -6.682  1.00 25.88 ? 374 ALA A C     1 
ATOM   2734 O  O     . ALA A 1 395 ? -9.950  -39.442 -6.250  1.00 22.63 ? 374 ALA A O     1 
ATOM   2735 C  CB    . ALA A 1 395 ? -10.922 -39.941 -9.168  1.00 26.00 ? 374 ALA A CB    1 
ATOM   2736 N  N     . ARG A 1 396 ? -11.638 -40.989 -5.947  1.00 23.90 ? 375 ARG A N     1 
ATOM   2737 C  CA    . ARG A 1 396 ? -11.975 -40.570 -4.548  1.00 23.88 ? 375 ARG A CA    1 
ATOM   2738 C  C     . ARG A 1 396 ? -10.936 -41.158 -3.576  1.00 24.99 ? 375 ARG A C     1 
ATOM   2739 O  O     . ARG A 1 396 ? -10.911 -40.716 -2.393  1.00 23.88 ? 375 ARG A O     1 
ATOM   2740 C  CB    . ARG A 1 396 ? -13.385 -40.984 -4.090  1.00 22.00 ? 375 ARG A CB    1 
ATOM   2741 C  CG    . ARG A 1 396 ? -14.517 -40.559 -5.025  1.00 22.35 ? 375 ARG A CG    1 
ATOM   2742 C  CD    . ARG A 1 396 ? -15.944 -40.700 -4.502  1.00 21.42 ? 375 ARG A CD    1 
ATOM   2743 N  NE    . ARG A 1 396 ? -16.952 -40.160 -5.420  1.00 19.66 ? 375 ARG A NE    1 
ATOM   2744 C  CZ    . ARG A 1 396 ? -17.286 -38.879 -5.543  1.00 20.54 ? 375 ARG A CZ    1 
ATOM   2745 N  NH1   . ARG A 1 396 ? -16.729 -37.938 -4.789  1.00 19.68 ? 375 ARG A NH1   1 
ATOM   2746 N  NH2   . ARG A 1 396 ? -18.223 -38.538 -6.411  1.00 22.29 ? 375 ARG A NH2   1 
ATOM   2747 N  N     . ASP A 1 397 ? -10.142 -42.136 -4.026  1.00 23.76 ? 376 ASP A N     1 
ATOM   2748 C  CA    . ASP A 1 397 ? -9.057  -42.762 -3.223  1.00 26.27 ? 376 ASP A CA    1 
ATOM   2749 C  C     . ASP A 1 397 ? -7.793  -41.919 -3.378  1.00 23.89 ? 376 ASP A C     1 
ATOM   2750 O  O     . ASP A 1 397 ? -6.839  -42.381 -4.015  1.00 24.56 ? 376 ASP A O     1 
ATOM   2751 C  CB    . ASP A 1 397 ? -8.817  -44.214 -3.649  1.00 29.16 ? 376 ASP A CB    1 
ATOM   2752 C  CG    . ASP A 1 397 ? -7.929  -45.010 -2.699  1.00 28.65 ? 376 ASP A CG    1 
ATOM   2753 O  OD1   . ASP A 1 397 ? -7.596  -44.494 -1.623  1.00 25.22 ? 376 ASP A OD1   1 
ATOM   2754 O  OD2   . ASP A 1 397 ? -7.619  -46.165 -3.050  1.00 32.79 ? 376 ASP A OD2   1 
ATOM   2755 N  N     . VAL A 1 398 ? -7.811  -40.718 -2.811  1.00 25.17 ? 377 VAL A N     1 
ATOM   2756 C  CA    . VAL A 1 398 ? -6.732  -39.695 -2.933  1.00 25.98 ? 377 VAL A CA    1 
ATOM   2757 C  C     . VAL A 1 398 ? -5.684  -39.978 -1.855  1.00 26.38 ? 377 VAL A C     1 
ATOM   2758 O  O     . VAL A 1 398 ? -6.061  -40.285 -0.722  1.00 29.56 ? 377 VAL A O     1 
ATOM   2759 C  CB    . VAL A 1 398 ? -7.308  -38.268 -2.864  1.00 26.55 ? 377 VAL A CB    1 
ATOM   2760 C  CG1   . VAL A 1 398 ? -7.584  -37.815 -1.446  1.00 27.05 ? 377 VAL A CG1   1 
ATOM   2761 C  CG2   . VAL A 1 398 ? -6.431  -37.258 -3.547  1.00 28.36 ? 377 VAL A CG2   1 
ATOM   2762 N  N     . ARG A 1 399 ? -4.408  -39.917 -2.213  1.00 26.78 ? 378 ARG A N     1 
ATOM   2763 C  CA    . ARG A 1 399 ? -3.276  -40.066 -1.274  1.00 26.77 ? 378 ARG A CA    1 
ATOM   2764 C  C     . ARG A 1 399 ? -3.004  -38.707 -0.638  1.00 27.78 ? 378 ARG A C     1 
ATOM   2765 O  O     . ARG A 1 399 ? -2.743  -38.665 0.573   1.00 28.92 ? 378 ARG A O     1 
ATOM   2766 C  CB    . ARG A 1 399 ? -2.037  -40.550 -2.017  1.00 29.84 ? 378 ARG A CB    1 
ATOM   2767 C  CG    . ARG A 1 399 ? -0.747  -40.426 -1.227  1.00 29.48 ? 378 ARG A CG    1 
ATOM   2768 C  CD    . ARG A 1 399 ? -0.753  -41.414 -0.089  1.00 32.63 ? 378 ARG A CD    1 
ATOM   2769 N  NE    . ARG A 1 399 ? 0.614   -41.734 0.239   1.00 37.59 ? 378 ARG A NE    1 
ATOM   2770 C  CZ    . ARG A 1 399 ? 1.006   -42.275 1.374   1.00 43.91 ? 378 ARG A CZ    1 
ATOM   2771 N  NH1   . ARG A 1 399 ? 0.112   -42.598 2.300   1.00 51.93 ? 378 ARG A NH1   1 
ATOM   2772 N  NH2   . ARG A 1 399 ? 2.296   -42.491 1.573   1.00 41.12 ? 378 ARG A NH2   1 
ATOM   2773 N  N     . ASP A 1 400 ? -3.070  -37.633 -1.428  1.00 27.89 ? 379 ASP A N     1 
ATOM   2774 C  CA    . ASP A 1 400 ? -2.833  -36.253 -0.941  1.00 25.59 ? 379 ASP A CA    1 
ATOM   2775 C  C     . ASP A 1 400 ? -3.372  -35.274 -1.997  1.00 28.98 ? 379 ASP A C     1 
ATOM   2776 O  O     . ASP A 1 400 ? -3.508  -35.666 -3.179  1.00 29.74 ? 379 ASP A O     1 
ATOM   2777 C  CB    . ASP A 1 400 ? -1.354  -36.111 -0.574  1.00 25.42 ? 379 ASP A CB    1 
ATOM   2778 C  CG    . ASP A 1 400 ? -0.985  -34.901 0.272   1.00 26.74 ? 379 ASP A CG    1 
ATOM   2779 O  OD1   . ASP A 1 400 ? -1.863  -34.095 0.556   1.00 24.91 ? 379 ASP A OD1   1 
ATOM   2780 O  OD2   . ASP A 1 400 ? 0.216   -34.742 0.597   1.00 31.08 ? 379 ASP A OD2   1 
ATOM   2781 N  N     . TYR A 1 401 ? -3.708  -34.054 -1.572  1.00 30.18 ? 380 TYR A N     1 
ATOM   2782 C  CA    . TYR A 1 401 ? -4.169  -32.921 -2.421  1.00 29.42 ? 380 TYR A CA    1 
ATOM   2783 C  C     . TYR A 1 401 ? -3.317  -31.696 -2.045  1.00 27.83 ? 380 TYR A C     1 
ATOM   2784 O  O     . TYR A 1 401 ? -3.195  -31.438 -0.853  1.00 28.19 ? 380 TYR A O     1 
ATOM   2785 C  CB    . TYR A 1 401 ? -5.688  -32.729 -2.248  1.00 26.87 ? 380 TYR A CB    1 
ATOM   2786 C  CG    . TYR A 1 401 ? -6.259  -31.516 -2.947  1.00 24.73 ? 380 TYR A CG    1 
ATOM   2787 C  CD1   . TYR A 1 401 ? -6.401  -30.312 -2.285  1.00 22.38 ? 380 TYR A CD1   1 
ATOM   2788 C  CD2   . TYR A 1 401 ? -6.655  -31.575 -4.265  1.00 22.84 ? 380 TYR A CD2   1 
ATOM   2789 C  CE1   . TYR A 1 401 ? -6.901  -29.199 -2.914  1.00 22.01 ? 380 TYR A CE1   1 
ATOM   2790 C  CE2   . TYR A 1 401 ? -7.157  -30.468 -4.918  1.00 22.24 ? 380 TYR A CE2   1 
ATOM   2791 C  CZ    . TYR A 1 401 ? -7.280  -29.271 -4.240  1.00 23.18 ? 380 TYR A CZ    1 
ATOM   2792 O  OH    . TYR A 1 401 ? -7.754  -28.167 -4.896  1.00 22.69 ? 380 TYR A OH    1 
ATOM   2793 N  N     . ILE A 1 402 ? -2.694  -31.016 -3.014  1.00 26.85 ? 381 ILE A N     1 
ATOM   2794 C  CA    . ILE A 1 402 ? -1.796  -29.846 -2.751  1.00 24.82 ? 381 ILE A CA    1 
ATOM   2795 C  C     . ILE A 1 402 ? -2.214  -28.738 -3.702  1.00 23.23 ? 381 ILE A C     1 
ATOM   2796 O  O     . ILE A 1 402 ? -2.296  -29.024 -4.887  1.00 21.26 ? 381 ILE A O     1 
ATOM   2797 C  CB    . ILE A 1 402 ? -0.309  -30.205 -2.938  1.00 26.12 ? 381 ILE A CB    1 
ATOM   2798 C  CG1   . ILE A 1 402 ? 0.020   -31.519 -2.230  1.00 25.44 ? 381 ILE A CG1   1 
ATOM   2799 C  CG2   . ILE A 1 402 ? 0.574   -29.055 -2.448  1.00 26.49 ? 381 ILE A CG2   1 
ATOM   2800 C  CD1   . ILE A 1 402 ? 1.437   -31.959 -2.382  1.00 26.37 ? 381 ILE A CD1   1 
ATOM   2801 N  N     . ASP A 1 403 ? -2.492  -27.530 -3.196  1.00 22.34 ? 382 ASP A N     1 
ATOM   2802 C  CA    . ASP A 1 403 ? -2.991  -26.419 -4.051  1.00 21.39 ? 382 ASP A CA    1 
ATOM   2803 C  C     . ASP A 1 403 ? -2.502  -25.082 -3.499  1.00 21.48 ? 382 ASP A C     1 
ATOM   2804 O  O     . ASP A 1 403 ? -1.976  -25.059 -2.383  1.00 19.15 ? 382 ASP A O     1 
ATOM   2805 C  CB    . ASP A 1 403 ? -4.512  -26.512 -4.270  1.00 21.33 ? 382 ASP A CB    1 
ATOM   2806 C  CG    . ASP A 1 403 ? -5.404  -25.936 -3.190  1.00 20.53 ? 382 ASP A CG    1 
ATOM   2807 O  OD1   . ASP A 1 403 ? -4.874  -25.291 -2.249  1.00 17.98 ? 382 ASP A OD1   1 
ATOM   2808 O  OD2   . ASP A 1 403 ? -6.645  -26.124 -3.321  1.00 21.22 ? 382 ASP A OD2   1 
ATOM   2809 N  N     . ARG A 1 404 ? -2.589  -24.043 -4.329  1.00 22.45 ? 383 ARG A N     1 
ATOM   2810 C  CA    . ARG A 1 404 ? -2.218  -22.648 -3.996  1.00 23.61 ? 383 ARG A CA    1 
ATOM   2811 C  C     . ARG A 1 404 ? -3.200  -21.696 -4.698  1.00 25.35 ? 383 ARG A C     1 
ATOM   2812 O  O     . ARG A 1 404 ? -3.311  -21.781 -5.948  1.00 23.79 ? 383 ARG A O     1 
ATOM   2813 C  CB    . ARG A 1 404 ? -0.801  -22.297 -4.461  1.00 24.61 ? 383 ARG A CB    1 
ATOM   2814 C  CG    . ARG A 1 404 ? -0.346  -20.924 -3.979  1.00 25.42 ? 383 ARG A CG    1 
ATOM   2815 C  CD    . ARG A 1 404 ? 1.100   -20.933 -3.497  1.00 27.72 ? 383 ARG A CD    1 
ATOM   2816 N  NE    . ARG A 1 404 ? 1.224   -21.842 -2.378  1.00 32.27 ? 383 ARG A NE    1 
ATOM   2817 C  CZ    . ARG A 1 404 ? 2.354   -22.099 -1.724  1.00 37.23 ? 383 ARG A CZ    1 
ATOM   2818 N  NH1   . ARG A 1 404 ? 3.477   -21.507 -2.092  1.00 34.62 ? 383 ARG A NH1   1 
ATOM   2819 N  NH2   . ARG A 1 404 ? 2.354   -22.953 -0.702  1.00 41.13 ? 383 ARG A NH2   1 
ATOM   2820 N  N     . ASP A 1 405 ? -3.874  -20.847 -3.907  1.00 23.82 ? 384 ASP A N     1 
ATOM   2821 C  CA    . ASP A 1 405 ? -4.647  -19.656 -4.347  1.00 23.78 ? 384 ASP A CA    1 
ATOM   2822 C  C     . ASP A 1 405 ? -3.665  -18.478 -4.462  1.00 21.84 ? 384 ASP A C     1 
ATOM   2823 O  O     . ASP A 1 405 ? -3.310  -17.917 -3.437  1.00 22.76 ? 384 ASP A O     1 
ATOM   2824 C  CB    . ASP A 1 405 ? -5.790  -19.307 -3.385  1.00 22.02 ? 384 ASP A CB    1 
ATOM   2825 C  CG    . ASP A 1 405 ? -6.729  -18.235 -3.934  1.00 23.65 ? 384 ASP A CG    1 
ATOM   2826 O  OD1   . ASP A 1 405 ? -6.511  -17.799 -5.075  1.00 26.65 ? 384 ASP A OD1   1 
ATOM   2827 O  OD2   . ASP A 1 405 ? -7.686  -17.838 -3.222  1.00 21.72 ? 384 ASP A OD2   1 
ATOM   2828 N  N     . TRP A 1 406 ? -3.240  -18.134 -5.674  1.00 21.70 ? 385 TRP A N     1 
ATOM   2829 C  CA    . TRP A 1 406 ? -2.288  -17.020 -5.911  1.00 21.46 ? 385 TRP A CA    1 
ATOM   2830 C  C     . TRP A 1 406 ? -2.948  -15.669 -5.640  1.00 20.47 ? 385 TRP A C     1 
ATOM   2831 O  O     . TRP A 1 406 ? -2.225  -14.705 -5.619  1.00 23.74 ? 385 TRP A O     1 
ATOM   2832 C  CB    . TRP A 1 406 ? -1.735  -17.105 -7.316  1.00 21.63 ? 385 TRP A CB    1 
ATOM   2833 C  CG    . TRP A 1 406 ? -0.776  -18.241 -7.429  1.00 20.74 ? 385 TRP A CG    1 
ATOM   2834 C  CD1   . TRP A 1 406 ? -1.023  -19.510 -7.868  1.00 19.65 ? 385 TRP A CD1   1 
ATOM   2835 C  CD2   . TRP A 1 406 ? 0.603   -18.192 -7.041  1.00 20.46 ? 385 TRP A CD2   1 
ATOM   2836 N  NE1   . TRP A 1 406 ? 0.112   -20.265 -7.756  1.00 19.97 ? 385 TRP A NE1   1 
ATOM   2837 C  CE2   . TRP A 1 406 ? 1.138   -19.475 -7.293  1.00 20.35 ? 385 TRP A CE2   1 
ATOM   2838 C  CE3   . TRP A 1 406 ? 1.442   -17.179 -6.575  1.00 19.87 ? 385 TRP A CE3   1 
ATOM   2839 C  CZ2   . TRP A 1 406 ? 2.482   -19.765 -7.071  1.00 20.00 ? 385 TRP A CZ2   1 
ATOM   2840 C  CZ3   . TRP A 1 406 ? 2.773   -17.474 -6.349  1.00 20.53 ? 385 TRP A CZ3   1 
ATOM   2841 C  CH2   . TRP A 1 406 ? 3.278   -18.747 -6.591  1.00 20.10 ? 385 TRP A CH2   1 
ATOM   2842 N  N     . SER A 1 407 ? -4.268  -15.615 -5.458  1.00 18.91 ? 386 SER A N     1 
ATOM   2843 C  CA    . SER A 1 407 ? -4.997  -14.372 -5.128  1.00 17.84 ? 386 SER A CA    1 
ATOM   2844 C  C     . SER A 1 407 ? -4.744  -14.042 -3.652  1.00 17.92 ? 386 SER A C     1 
ATOM   2845 O  O     . SER A 1 407 ? -4.712  -12.890 -3.323  1.00 15.63 ? 386 SER A O     1 
ATOM   2846 C  CB    . SER A 1 407 ? -6.463  -14.481 -5.457  1.00 17.80 ? 386 SER A CB    1 
ATOM   2847 O  OG    . SER A 1 407 ? -6.672  -14.829 -6.817  1.00 17.89 ? 386 SER A OG    1 
ATOM   2848 N  N     . ALA A 1 408 ? -4.479  -15.064 -2.829  1.00 21.51 ? 387 ALA A N     1 
ATOM   2849 C  CA    . ALA A 1 408 ? -4.296  -14.989 -1.372  1.00 22.27 ? 387 ALA A CA    1 
ATOM   2850 C  C     . ALA A 1 408 ? -2.845  -14.605 -1.061  1.00 22.22 ? 387 ALA A C     1 
ATOM   2851 O  O     . ALA A 1 408 ? -2.593  -13.985 -0.007  1.00 26.51 ? 387 ALA A O     1 
ATOM   2852 C  CB    . ALA A 1 408 ? -4.723  -16.302 -0.741  1.00 23.08 ? 387 ALA A CB    1 
ATOM   2853 N  N     . GLU A 1 409 ? -1.924  -14.945 -1.949  1.00 24.98 ? 388 GLU A N     1 
ATOM   2854 C  CA    . GLU A 1 409 ? -0.461  -14.628 -1.873  1.00 22.48 ? 388 GLU A CA    1 
ATOM   2855 C  C     . GLU A 1 409 ? -0.259  -13.122 -1.814  1.00 21.45 ? 388 GLU A C     1 
ATOM   2856 O  O     . GLU A 1 409 ? -0.531  -12.463 -2.808  1.00 25.16 ? 388 GLU A O     1 
ATOM   2857 C  CB    . GLU A 1 409 ? 0.220   -15.175 -3.133  1.00 22.01 ? 388 GLU A CB    1 
ATOM   2858 C  CG    . GLU A 1 409 ? 0.485   -16.673 -3.082  1.00 22.04 ? 388 GLU A CG    1 
ATOM   2859 C  CD    . GLU A 1 409 ? 1.545   -17.136 -2.060  1.00 22.17 ? 388 GLU A CD    1 
ATOM   2860 O  OE1   . GLU A 1 409 ? 1.265   -18.153 -1.402  1.00 22.89 ? 388 GLU A OE1   1 
ATOM   2861 O  OE2   . GLU A 1 409 ? 2.644   -16.474 -1.902  1.00 17.73 ? 388 GLU A OE2   1 
ATOM   2862 N  N     . PRO A 1 410 ? 0.182   -12.499 -0.694  1.00 20.30 ? 389 PRO A N     1 
ATOM   2863 C  CA    . PRO A 1 410 ? 0.215   -11.044 -0.620  1.00 19.55 ? 389 PRO A CA    1 
ATOM   2864 C  C     . PRO A 1 410 ? 1.200   -10.437 -1.623  1.00 21.55 ? 389 PRO A C     1 
ATOM   2865 O  O     . PRO A 1 410 ? 0.918   -9.314  -2.050  1.00 22.15 ? 389 PRO A O     1 
ATOM   2866 C  CB    . PRO A 1 410 ? 0.660   -10.736 0.809   1.00 21.10 ? 389 PRO A CB    1 
ATOM   2867 C  CG    . PRO A 1 410 ? 1.383   -12.003 1.231   1.00 20.72 ? 389 PRO A CG    1 
ATOM   2868 C  CD    . PRO A 1 410 ? 0.605   -13.119 0.567   1.00 21.20 ? 389 PRO A CD    1 
ATOM   2869 N  N     . TRP A 1 411 ? 2.283   -11.163 -1.989  1.00 21.32 ? 390 TRP A N     1 
ATOM   2870 C  CA    . TRP A 1 411 ? 3.348   -10.671 -2.916  1.00 21.42 ? 390 TRP A CA    1 
ATOM   2871 C  C     . TRP A 1 411 ? 3.106   -11.139 -4.359  1.00 20.83 ? 390 TRP A C     1 
ATOM   2872 O  O     . TRP A 1 411 ? 4.047   -11.055 -5.144  1.00 21.69 ? 390 TRP A O     1 
ATOM   2873 C  CB    . TRP A 1 411 ? 4.754   -11.058 -2.433  1.00 19.96 ? 390 TRP A CB    1 
ATOM   2874 C  CG    . TRP A 1 411 ? 4.963   -10.649 -1.020  1.00 19.78 ? 390 TRP A CG    1 
ATOM   2875 C  CD1   . TRP A 1 411 ? 5.102   -11.475 0.060   1.00 19.03 ? 390 TRP A CD1   1 
ATOM   2876 C  CD2   . TRP A 1 411 ? 4.987   -9.297  -0.519  1.00 19.16 ? 390 TRP A CD2   1 
ATOM   2877 N  NE1   . TRP A 1 411 ? 5.195   -10.722 1.202   1.00 19.16 ? 390 TRP A NE1   1 
ATOM   2878 C  CE2   . TRP A 1 411 ? 5.123   -9.382  0.877   1.00 19.69 ? 390 TRP A CE2   1 
ATOM   2879 C  CE3   . TRP A 1 411 ? 4.909   -8.032  -1.105  1.00 20.41 ? 390 TRP A CE3   1 
ATOM   2880 C  CZ2   . TRP A 1 411 ? 5.206   -8.243  1.682   1.00 18.91 ? 390 TRP A CZ2   1 
ATOM   2881 C  CZ3   . TRP A 1 411 ? 4.947   -6.909  -0.309  1.00 19.04 ? 390 TRP A CZ3   1 
ATOM   2882 C  CH2   . TRP A 1 411 ? 5.097   -7.017  1.067   1.00 19.25 ? 390 TRP A CH2   1 
ATOM   2883 N  N     . THR A 1 412 ? 1.889   -11.547 -4.705  1.00 20.72 ? 391 THR A N     1 
ATOM   2884 C  CA    . THR A 1 412 ? 1.441   -11.700 -6.115  1.00 22.13 ? 391 THR A CA    1 
ATOM   2885 C  C     . THR A 1 412 ? 0.062   -11.062 -6.267  1.00 21.21 ? 391 THR A C     1 
ATOM   2886 O  O     . THR A 1 412 ? -0.079  -10.181 -7.096  1.00 20.09 ? 391 THR A O     1 
ATOM   2887 C  CB    . THR A 1 412 ? 1.398   -13.174 -6.563  1.00 22.33 ? 391 THR A CB    1 
ATOM   2888 O  OG1   . THR A 1 412 ? 2.705   -13.717 -6.342  1.00 22.62 ? 391 THR A OG1   1 
ATOM   2889 C  CG2   . THR A 1 412 ? 0.961   -13.332 -8.007  1.00 21.04 ? 391 THR A CG2   1 
ATOM   2890 N  N     . ARG A 1 413 ? -0.917  -11.537 -5.507  1.00 21.26 ? 392 ARG A N     1 
ATOM   2891 C  CA    . ARG A 1 413 ? -2.302  -11.010 -5.544  1.00 21.75 ? 392 ARG A CA    1 
ATOM   2892 C  C     . ARG A 1 413 ? -2.944  -11.350 -6.898  1.00 21.25 ? 392 ARG A C     1 
ATOM   2893 O  O     . ARG A 1 413 ? -3.777  -10.576 -7.345  1.00 25.36 ? 392 ARG A O     1 
ATOM   2894 C  CB    . ARG A 1 413 ? -2.313  -9.512  -5.197  1.00 22.87 ? 392 ARG A CB    1 
ATOM   2895 C  CG    . ARG A 1 413 ? -2.020  -9.222  -3.727  1.00 23.75 ? 392 ARG A CG    1 
ATOM   2896 C  CD    . ARG A 1 413 ? -2.947  -10.098 -2.883  1.00 26.40 ? 392 ARG A CD    1 
ATOM   2897 N  NE    . ARG A 1 413 ? -3.168  -9.674  -1.505  1.00 26.93 ? 392 ARG A NE    1 
ATOM   2898 C  CZ    . ARG A 1 413 ? -4.035  -10.224 -0.658  1.00 25.48 ? 392 ARG A CZ    1 
ATOM   2899 N  NH1   . ARG A 1 413 ? -4.800  -11.247 -1.024  1.00 25.38 ? 392 ARG A NH1   1 
ATOM   2900 N  NH2   . ARG A 1 413 ? -4.135  -9.718  0.558   1.00 23.80 ? 392 ARG A NH2   1 
ATOM   2901 N  N     . GLY A 1 414 ? -2.659  -12.529 -7.442  1.00 18.41 ? 393 GLY A N     1 
ATOM   2902 C  CA    . GLY A 1 414 ? -3.412  -13.166 -8.539  1.00 18.12 ? 393 GLY A CA    1 
ATOM   2903 C  C     . GLY A 1 414 ? -2.484  -13.648 -9.632  1.00 17.37 ? 393 GLY A C     1 
ATOM   2904 O  O     . GLY A 1 414 ? -1.513  -12.940 -9.906  1.00 15.03 ? 393 GLY A O     1 
ATOM   2905 N  N     . CYS A 1 415 ? -2.742  -14.823 -10.201 1.00 19.27 ? 394 CYS A N     1 
ATOM   2906 C  CA    . CYS A 1 415 ? -2.060  -15.350 -11.431 1.00 20.41 ? 394 CYS A CA    1 
ATOM   2907 C  C     . CYS A 1 415 ? -3.083  -15.437 -12.562 1.00 21.82 ? 394 CYS A C     1 
ATOM   2908 O  O     . CYS A 1 415 ? -4.297  -15.414 -12.302 1.00 20.62 ? 394 CYS A O     1 
ATOM   2909 C  CB    . CYS A 1 415 ? -1.388  -16.697 -11.148 1.00 21.14 ? 394 CYS A CB    1 
ATOM   2910 S  SG    . CYS A 1 415 ? 0.332   -16.540 -10.568 1.00 23.65 ? 394 CYS A SG    1 
ATOM   2911 N  N     . TYR A 1 416 ? -2.619  -15.580 -13.822 1.00 21.90 ? 395 TYR A N     1 
ATOM   2912 C  CA    . TYR A 1 416 ? -1.224  -15.719 -14.199 1.00 23.47 ? 395 TYR A CA    1 
ATOM   2913 C  C     . TYR A 1 416 ? -0.603  -14.321 -14.293 1.00 23.62 ? 395 TYR A C     1 
ATOM   2914 O  O     . TYR A 1 416 ? 0.626   -14.191 -14.117 1.00 28.77 ? 395 TYR A O     1 
ATOM   2915 C  CB    . TYR A 1 416 ? -1.101  -16.576 -15.476 1.00 26.10 ? 395 TYR A CB    1 
ATOM   2916 C  CG    . TYR A 1 416 ? -1.968  -17.822 -15.466 1.00 28.30 ? 395 TYR A CG    1 
ATOM   2917 C  CD1   . TYR A 1 416 ? -1.814  -18.791 -14.492 1.00 29.76 ? 395 TYR A CD1   1 
ATOM   2918 C  CD2   . TYR A 1 416 ? -3.017  -17.996 -16.358 1.00 32.30 ? 395 TYR A CD2   1 
ATOM   2919 C  CE1   . TYR A 1 416 ? -2.628  -19.912 -14.428 1.00 29.39 ? 395 TYR A CE1   1 
ATOM   2920 C  CE2   . TYR A 1 416 ? -3.843  -19.117 -16.314 1.00 31.38 ? 395 TYR A CE2   1 
ATOM   2921 C  CZ    . TYR A 1 416 ? -3.650  -20.080 -15.341 1.00 29.90 ? 395 TYR A CZ    1 
ATOM   2922 O  OH    . TYR A 1 416 ? -4.448  -21.187 -15.284 1.00 30.35 ? 395 TYR A OH    1 
ATOM   2923 N  N     . GLY A 1 417 ? -1.417  -13.295 -14.517 1.00 20.91 ? 396 GLY A N     1 
ATOM   2924 C  CA    . GLY A 1 417 ? -0.948  -11.902 -14.512 1.00 21.93 ? 396 GLY A CA    1 
ATOM   2925 C  C     . GLY A 1 417 ? -2.100  -10.956 -14.767 1.00 22.33 ? 396 GLY A C     1 
ATOM   2926 O  O     . GLY A 1 417 ? -3.262  -11.376 -14.609 1.00 21.61 ? 396 GLY A O     1 
ATOM   2927 N  N     . ALA A 1 418 ? -1.798  -9.720  -15.136 1.00 23.20 ? 397 ALA A N     1 
ATOM   2928 C  CA    . ALA A 1 418 ? -2.817  -8.662  -15.303 1.00 23.80 ? 397 ALA A CA    1 
ATOM   2929 C  C     . ALA A 1 418 ? -3.589  -8.907  -16.607 1.00 22.82 ? 397 ALA A C     1 
ATOM   2930 O  O     . ALA A 1 418 ? -3.025  -9.487  -17.520 1.00 22.37 ? 397 ALA A O     1 
ATOM   2931 C  CB    . ALA A 1 418 ? -2.173  -7.308  -15.257 1.00 23.11 ? 397 ALA A CB    1 
ATOM   2932 N  N     . HIS A 1 419 ? -4.869  -8.534  -16.631 1.00 24.91 ? 398 HIS A N     1 
ATOM   2933 C  CA    . HIS A 1 419 ? -5.696  -8.285  -17.831 1.00 22.13 ? 398 HIS A CA    1 
ATOM   2934 C  C     . HIS A 1 419 ? -6.189  -6.834  -17.779 1.00 24.29 ? 398 HIS A C     1 
ATOM   2935 O  O     . HIS A 1 419 ? -6.015  -6.163  -16.761 1.00 23.52 ? 398 HIS A O     1 
ATOM   2936 C  CB    . HIS A 1 419 ? -6.794  -9.319  -17.922 1.00 23.77 ? 398 HIS A CB    1 
ATOM   2937 C  CG    . HIS A 1 419 ? -7.732  -9.332  -16.767 1.00 25.18 ? 398 HIS A CG    1 
ATOM   2938 N  ND1   . HIS A 1 419 ? -7.552  -10.175 -15.680 1.00 25.09 ? 398 HIS A ND1   1 
ATOM   2939 C  CD2   . HIS A 1 419 ? -8.875  -8.637  -16.539 1.00 26.79 ? 398 HIS A CD2   1 
ATOM   2940 C  CE1   . HIS A 1 419 ? -8.537  -9.979  -14.817 1.00 25.37 ? 398 HIS A CE1   1 
ATOM   2941 N  NE2   . HIS A 1 419 ? -9.355  -9.025  -15.316 1.00 26.89 ? 398 HIS A NE2   1 
ATOM   2942 N  N     . LEU A 1 420 ? -6.642  -6.306  -18.903 1.00 26.23 ? 399 LEU A N     1 
ATOM   2943 C  CA    . LEU A 1 420 ? -7.154  -4.920  -19.013 1.00 24.72 ? 399 LEU A CA    1 
ATOM   2944 C  C     . LEU A 1 420 ? -8.613  -5.011  -19.472 1.00 24.60 ? 399 LEU A C     1 
ATOM   2945 O  O     . LEU A 1 420 ? -8.961  -5.750  -20.414 1.00 23.92 ? 399 LEU A O     1 
ATOM   2946 C  CB    . LEU A 1 420 ? -6.234  -4.122  -19.943 1.00 23.15 ? 399 LEU A CB    1 
ATOM   2947 C  CG    . LEU A 1 420 ? -4.993  -3.503  -19.271 1.00 24.89 ? 399 LEU A CG    1 
ATOM   2948 C  CD1   . LEU A 1 420 ? -3.855  -4.495  -19.166 1.00 25.14 ? 399 LEU A CD1   1 
ATOM   2949 C  CD2   . LEU A 1 420 ? -4.489  -2.261  -19.990 1.00 23.83 ? 399 LEU A CD2   1 
ATOM   2950 N  N     . PRO A 1 421 ? -9.538  -4.377  -18.725 1.00 25.89 ? 400 PRO A N     1 
ATOM   2951 C  CA    . PRO A 1 421 ? -10.949 -4.348  -19.112 1.00 25.84 ? 400 PRO A CA    1 
ATOM   2952 C  C     . PRO A 1 421 ? -11.171 -3.284  -20.184 1.00 26.86 ? 400 PRO A C     1 
ATOM   2953 O  O     . PRO A 1 421 ? -10.281 -2.496  -20.472 1.00 29.59 ? 400 PRO A O     1 
ATOM   2954 C  CB    . PRO A 1 421 ? -11.663 -3.977  -17.811 1.00 27.69 ? 400 PRO A CB    1 
ATOM   2955 C  CG    . PRO A 1 421 ? -10.650 -3.105  -17.085 1.00 30.09 ? 400 PRO A CG    1 
ATOM   2956 C  CD    . PRO A 1 421 ? -9.282  -3.681  -17.447 1.00 27.23 ? 400 PRO A CD    1 
ATOM   2957 N  N     . PRO A 1 422 ? -12.353 -3.216  -20.822 1.00 26.80 ? 401 PRO A N     1 
ATOM   2958 C  CA    . PRO A 1 422 ? -12.593 -2.208  -21.839 1.00 27.72 ? 401 PRO A CA    1 
ATOM   2959 C  C     . PRO A 1 422 ? -12.238 -0.798  -21.338 1.00 24.36 ? 401 PRO A C     1 
ATOM   2960 O  O     . PRO A 1 422 ? -12.549 -0.459  -20.224 1.00 22.20 ? 401 PRO A O     1 
ATOM   2961 C  CB    . PRO A 1 422 ? -14.073 -2.380  -22.239 1.00 26.56 ? 401 PRO A CB    1 
ATOM   2962 C  CG    . PRO A 1 422 ? -14.651 -3.404  -21.274 1.00 26.75 ? 401 PRO A CG    1 
ATOM   2963 C  CD    . PRO A 1 422 ? -13.472 -4.160  -20.703 1.00 28.86 ? 401 PRO A CD    1 
ATOM   2964 N  N     . GLY A 1 423 ? -11.543 -0.052  -22.202 1.00 26.75 ? 402 GLY A N     1 
ATOM   2965 C  CA    . GLY A 1 423 ? -11.210 1.380   -22.060 1.00 25.19 ? 402 GLY A CA    1 
ATOM   2966 C  C     . GLY A 1 423 ? -9.819  1.589   -21.498 1.00 26.07 ? 402 GLY A C     1 
ATOM   2967 O  O     . GLY A 1 423 ? -9.340  2.737   -21.586 1.00 30.32 ? 402 GLY A O     1 
ATOM   2968 N  N     . ALA A 1 424 ? -9.177  0.546   -20.949 1.00 25.52 ? 403 ALA A N     1 
ATOM   2969 C  CA    . ALA A 1 424 ? -7.863  0.654   -20.254 1.00 26.61 ? 403 ALA A CA    1 
ATOM   2970 C  C     . ALA A 1 424 ? -6.711  0.894   -21.252 1.00 24.29 ? 403 ALA A C     1 
ATOM   2971 O  O     . ALA A 1 424 ? -5.879  1.799   -20.980 1.00 26.56 ? 403 ALA A O     1 
ATOM   2972 C  CB    . ALA A 1 424 ? -7.605  -0.580  -19.404 1.00 26.59 ? 403 ALA A CB    1 
ATOM   2973 N  N     . TRP A 1 425 ? -6.636  0.125   -22.349 1.00 23.49 ? 404 TRP A N     1 
ATOM   2974 C  CA    . TRP A 1 425 ? -5.421  0.051   -23.213 1.00 23.47 ? 404 TRP A CA    1 
ATOM   2975 C  C     . TRP A 1 425 ? -5.214  1.360   -24.005 1.00 22.30 ? 404 TRP A C     1 
ATOM   2976 O  O     . TRP A 1 425 ? -4.063  1.838   -24.119 1.00 23.10 ? 404 TRP A O     1 
ATOM   2977 C  CB    . TRP A 1 425 ? -5.474  -1.172  -24.149 1.00 24.36 ? 404 TRP A CB    1 
ATOM   2978 C  CG    . TRP A 1 425 ? -4.697  -2.383  -23.720 1.00 22.44 ? 404 TRP A CG    1 
ATOM   2979 C  CD1   . TRP A 1 425 ? -5.194  -3.637  -23.534 1.00 22.97 ? 404 TRP A CD1   1 
ATOM   2980 C  CD2   . TRP A 1 425 ? -3.283  -2.489  -23.497 1.00 20.93 ? 404 TRP A CD2   1 
ATOM   2981 N  NE1   . TRP A 1 425 ? -4.196  -4.505  -23.185 1.00 23.32 ? 404 TRP A NE1   1 
ATOM   2982 C  CE2   . TRP A 1 425 ? -3.018  -3.820  -23.129 1.00 22.52 ? 404 TRP A CE2   1 
ATOM   2983 C  CE3   . TRP A 1 425 ? -2.226  -1.579  -23.513 1.00 21.71 ? 404 TRP A CE3   1 
ATOM   2984 C  CZ2   . TRP A 1 425 ? -1.738  -4.279  -22.829 1.00 22.60 ? 404 TRP A CZ2   1 
ATOM   2985 C  CZ3   . TRP A 1 425 ? -0.968  -2.018  -23.171 1.00 22.64 ? 404 TRP A CZ3   1 
ATOM   2986 C  CH2   . TRP A 1 425 ? -0.728  -3.353  -22.855 1.00 22.82 ? 404 TRP A CH2   1 
ATOM   2987 N  N     . THR A 1 426 ? -6.269  1.953   -24.535 1.00 23.82 ? 405 THR A N     1 
ATOM   2988 C  CA    . THR A 1 426 ? -6.170  3.140   -25.436 1.00 24.87 ? 405 THR A CA    1 
ATOM   2989 C  C     . THR A 1 426 ? -5.990  4.396   -24.590 1.00 23.62 ? 405 THR A C     1 
ATOM   2990 O  O     . THR A 1 426 ? -5.428  5.381   -25.123 1.00 29.05 ? 405 THR A O     1 
ATOM   2991 C  CB    . THR A 1 426 ? -7.386  3.254   -26.369 1.00 24.41 ? 405 THR A CB    1 
ATOM   2992 O  OG1   . THR A 1 426 ? -8.598  3.188   -25.616 1.00 26.52 ? 405 THR A OG1   1 
ATOM   2993 C  CG2   . THR A 1 426 ? -7.444  2.114   -27.359 1.00 25.70 ? 405 THR A CG2   1 
ATOM   2994 N  N     . VAL A 1 427 ? -6.423  4.373   -23.325 1.00 22.26 ? 406 VAL A N     1 
ATOM   2995 C  CA    . VAL A 1 427 ? -6.482  5.600   -22.457 1.00 21.35 ? 406 VAL A CA    1 
ATOM   2996 C  C     . VAL A 1 427 ? -5.337  5.631   -21.459 1.00 20.09 ? 406 VAL A C     1 
ATOM   2997 O  O     . VAL A 1 427 ? -4.783  6.703   -21.339 1.00 22.71 ? 406 VAL A O     1 
ATOM   2998 C  CB    . VAL A 1 427 ? -7.812  5.696   -21.703 1.00 22.16 ? 406 VAL A CB    1 
ATOM   2999 C  CG1   . VAL A 1 427 ? -7.825  6.871   -20.733 1.00 22.83 ? 406 VAL A CG1   1 
ATOM   3000 C  CG2   . VAL A 1 427 ? -8.991  5.712   -22.675 1.00 22.42 ? 406 VAL A CG2   1 
ATOM   3001 N  N     . TYR A 1 428 ? -5.080  4.550   -20.701 1.00 20.11 ? 407 TYR A N     1 
ATOM   3002 C  CA    . TYR A 1 428 ? -4.028  4.523   -19.652 1.00 21.33 ? 407 TYR A CA    1 
ATOM   3003 C  C     . TYR A 1 428 ? -2.802  3.726   -20.110 1.00 21.85 ? 407 TYR A C     1 
ATOM   3004 O  O     . TYR A 1 428 ? -1.756  3.970   -19.566 1.00 20.12 ? 407 TYR A O     1 
ATOM   3005 C  CB    . TYR A 1 428 ? -4.572  3.947   -18.351 1.00 22.90 ? 407 TYR A CB    1 
ATOM   3006 C  CG    . TYR A 1 428 ? -5.863  4.576   -17.905 1.00 25.51 ? 407 TYR A CG    1 
ATOM   3007 C  CD1   . TYR A 1 428 ? -5.866  5.731   -17.140 1.00 24.86 ? 407 TYR A CD1   1 
ATOM   3008 C  CD2   . TYR A 1 428 ? -7.072  4.037   -18.290 1.00 24.76 ? 407 TYR A CD2   1 
ATOM   3009 C  CE1   . TYR A 1 428 ? -7.043  6.320   -16.735 1.00 25.91 ? 407 TYR A CE1   1 
ATOM   3010 C  CE2   . TYR A 1 428 ? -8.262  4.628   -17.910 1.00 26.91 ? 407 TYR A CE2   1 
ATOM   3011 C  CZ    . TYR A 1 428 ? -8.244  5.756   -17.116 1.00 26.90 ? 407 TYR A CZ    1 
ATOM   3012 O  OH    . TYR A 1 428 ? -9.421  6.353   -16.786 1.00 29.86 ? 407 TYR A OH    1 
ATOM   3013 N  N     . GLY A 1 429 ? -2.965  2.802   -21.073 1.00 25.49 ? 408 GLY A N     1 
ATOM   3014 C  CA    . GLY A 1 429 ? -1.961  1.828   -21.575 1.00 20.79 ? 408 GLY A CA    1 
ATOM   3015 C  C     . GLY A 1 429 ? -0.653  2.448   -22.035 1.00 19.59 ? 408 GLY A C     1 
ATOM   3016 O  O     . GLY A 1 429 ? 0.393   1.863   -21.783 1.00 18.61 ? 408 GLY A O     1 
ATOM   3017 N  N     . PRO A 1 430 ? -0.633  3.613   -22.731 1.00 19.16 ? 409 PRO A N     1 
ATOM   3018 C  CA    . PRO A 1 430 ? 0.632   4.234   -23.126 1.00 20.54 ? 409 PRO A CA    1 
ATOM   3019 C  C     . PRO A 1 430 ? 1.620   4.442   -21.959 1.00 21.85 ? 409 PRO A C     1 
ATOM   3020 O  O     . PRO A 1 430 ? 2.811   4.533   -22.216 1.00 20.48 ? 409 PRO A O     1 
ATOM   3021 C  CB    . PRO A 1 430 ? 0.200   5.574   -23.742 1.00 19.71 ? 409 PRO A CB    1 
ATOM   3022 C  CG    . PRO A 1 430 ? -1.235  5.331   -24.219 1.00 19.23 ? 409 PRO A CG    1 
ATOM   3023 C  CD    . PRO A 1 430 ? -1.794  4.382   -23.197 1.00 20.71 ? 409 PRO A CD    1 
ATOM   3024 N  N     . ALA A 1 431 ? 1.145   4.498   -20.704 1.00 22.79 ? 410 ALA A N     1 
ATOM   3025 C  CA    . ALA A 1 431 ? 2.059   4.633   -19.540 1.00 26.69 ? 410 ALA A CA    1 
ATOM   3026 C  C     . ALA A 1 431 ? 2.764   3.301   -19.184 1.00 24.40 ? 410 ALA A C     1 
ATOM   3027 O  O     . ALA A 1 431 ? 3.656   3.361   -18.364 1.00 26.48 ? 410 ALA A O     1 
ATOM   3028 C  CB    . ALA A 1 431 ? 1.329   5.230   -18.367 1.00 25.47 ? 410 ALA A CB    1 
ATOM   3029 N  N     . LEU A 1 432 ? 2.433   2.178   -19.832 1.00 23.48 ? 411 LEU A N     1 
ATOM   3030 C  CA    . LEU A 1 432 ? 2.858   0.800   -19.449 1.00 24.34 ? 411 LEU A CA    1 
ATOM   3031 C  C     . LEU A 1 432 ? 4.348   0.783   -19.120 1.00 24.17 ? 411 LEU A C     1 
ATOM   3032 O  O     . LEU A 1 432 ? 4.646   0.478   -17.977 1.00 25.08 ? 411 LEU A O     1 
ATOM   3033 C  CB    . LEU A 1 432 ? 2.527   -0.193  -20.579 1.00 23.98 ? 411 LEU A CB    1 
ATOM   3034 C  CG    . LEU A 1 432 ? 2.767   -1.676  -20.272 1.00 25.51 ? 411 LEU A CG    1 
ATOM   3035 C  CD1   . LEU A 1 432 ? 1.889   -2.149  -19.116 1.00 26.93 ? 411 LEU A CD1   1 
ATOM   3036 C  CD2   . LEU A 1 432 ? 2.527   -2.554  -21.496 1.00 24.68 ? 411 LEU A CD2   1 
ATOM   3037 N  N     . ARG A 1 433 ? 5.215   1.125   -20.089 1.00 27.40 ? 412 ARG A N     1 
ATOM   3038 C  CA    . ARG A 1 433 ? 6.699   0.980   -20.049 1.00 29.03 ? 412 ARG A CA    1 
ATOM   3039 C  C     . ARG A 1 433 ? 7.441   2.304   -19.781 1.00 30.74 ? 412 ARG A C     1 
ATOM   3040 O  O     . ARG A 1 433 ? 8.671   2.258   -19.596 1.00 30.23 ? 412 ARG A O     1 
ATOM   3041 C  CB    . ARG A 1 433 ? 7.235   0.511   -21.400 1.00 29.56 ? 412 ARG A CB    1 
ATOM   3042 C  CG    . ARG A 1 433 ? 6.680   -0.814  -21.878 1.00 32.71 ? 412 ARG A CG    1 
ATOM   3043 C  CD    . ARG A 1 433 ? 7.460   -1.397  -23.043 1.00 28.95 ? 412 ARG A CD    1 
ATOM   3044 N  NE    . ARG A 1 433 ? 6.720   -2.533  -23.563 1.00 31.04 ? 412 ARG A NE    1 
ATOM   3045 C  CZ    . ARG A 1 433 ? 5.633   -2.442  -24.347 1.00 35.38 ? 412 ARG A CZ    1 
ATOM   3046 N  NH1   . ARG A 1 433 ? 5.171   -1.262  -24.726 1.00 35.06 ? 412 ARG A NH1   1 
ATOM   3047 N  NH2   . ARG A 1 433 ? 5.003   -3.527  -24.766 1.00 36.32 ? 412 ARG A NH2   1 
ATOM   3048 N  N     . VAL A 1 434 ? 6.790   3.459   -19.888 1.00 29.66 ? 413 VAL A N     1 
ATOM   3049 C  CA    . VAL A 1 434 ? 7.531   4.756   -19.893 1.00 30.69 ? 413 VAL A CA    1 
ATOM   3050 C  C     . VAL A 1 434 ? 8.188   4.912   -18.530 1.00 30.61 ? 413 VAL A C     1 
ATOM   3051 O  O     . VAL A 1 434 ? 7.502   4.877   -17.519 1.00 29.99 ? 413 VAL A O     1 
ATOM   3052 C  CB    . VAL A 1 434 ? 6.621   5.961   -20.204 1.00 32.52 ? 413 VAL A CB    1 
ATOM   3053 C  CG1   . VAL A 1 434 ? 7.272   7.286   -19.813 1.00 32.76 ? 413 VAL A CG1   1 
ATOM   3054 C  CG2   . VAL A 1 434 ? 6.203   5.986   -21.661 1.00 34.47 ? 413 VAL A CG2   1 
ATOM   3055 N  N     . PRO A 1 435 ? 9.517   5.116   -18.445 1.00 31.00 ? 414 PRO A N     1 
ATOM   3056 C  CA    . PRO A 1 435 ? 10.133  5.411   -17.168 1.00 31.13 ? 414 PRO A CA    1 
ATOM   3057 C  C     . PRO A 1 435 ? 9.491   6.683   -16.602 1.00 28.96 ? 414 PRO A C     1 
ATOM   3058 O  O     . PRO A 1 435 ? 9.121   7.545   -17.358 1.00 26.02 ? 414 PRO A O     1 
ATOM   3059 C  CB    . PRO A 1 435 ? 11.629  5.603   -17.506 1.00 34.09 ? 414 PRO A CB    1 
ATOM   3060 C  CG    . PRO A 1 435 ? 11.818  4.919   -18.840 1.00 33.26 ? 414 PRO A CG    1 
ATOM   3061 C  CD    . PRO A 1 435 ? 10.498  5.110   -19.545 1.00 33.44 ? 414 PRO A CD    1 
ATOM   3062 N  N     . VAL A 1 436 ? 9.353   6.738   -15.282 1.00 27.79 ? 415 VAL A N     1 
ATOM   3063 C  CA    . VAL A 1 436 ? 9.176   8.006   -14.533 1.00 30.11 ? 415 VAL A CA    1 
ATOM   3064 C  C     . VAL A 1 436 ? 10.533  8.356   -13.919 1.00 30.91 ? 415 VAL A C     1 
ATOM   3065 O  O     . VAL A 1 436 ? 10.976  7.651   -12.973 1.00 32.09 ? 415 VAL A O     1 
ATOM   3066 C  CB    . VAL A 1 436 ? 8.048   7.866   -13.508 1.00 29.61 ? 415 VAL A CB    1 
ATOM   3067 C  CG1   . VAL A 1 436 ? 7.761   9.180   -12.805 1.00 33.28 ? 415 VAL A CG1   1 
ATOM   3068 C  CG2   . VAL A 1 436 ? 6.792   7.344   -14.194 1.00 31.44 ? 415 VAL A CG2   1 
ATOM   3069 N  N     . GLY A 1 437 ? 11.196  9.350   -14.502 1.00 27.79 ? 416 GLY A N     1 
ATOM   3070 C  CA    . GLY A 1 437 ? 12.521  9.825   -14.081 1.00 30.62 ? 416 GLY A CA    1 
ATOM   3071 C  C     . GLY A 1 437 ? 13.517  8.682   -14.036 1.00 32.23 ? 416 GLY A C     1 
ATOM   3072 O  O     . GLY A 1 437 ? 13.868  8.150   -15.106 1.00 34.82 ? 416 GLY A O     1 
ATOM   3073 N  N     . ARG A 1 438 ? 13.923  8.293   -12.832 1.00 31.81 ? 417 ARG A N     1 
ATOM   3074 C  CA    . ARG A 1 438 ? 14.988  7.287   -12.582 1.00 31.37 ? 417 ARG A CA    1 
ATOM   3075 C  C     . ARG A 1 438 ? 14.339  5.928   -12.303 1.00 28.61 ? 417 ARG A C     1 
ATOM   3076 O  O     . ARG A 1 438 ? 15.067  4.964   -12.082 1.00 25.62 ? 417 ARG A O     1 
ATOM   3077 C  CB    . ARG A 1 438 ? 15.837  7.755   -11.394 1.00 33.76 ? 417 ARG A CB    1 
ATOM   3078 C  CG    . ARG A 1 438 ? 16.118  9.252   -11.399 1.00 34.53 ? 417 ARG A CG    1 
ATOM   3079 C  CD    . ARG A 1 438 ? 17.260  9.668   -10.483 1.00 35.80 ? 417 ARG A CD    1 
ATOM   3080 N  NE    . ARG A 1 438 ? 18.049  10.703  -11.129 1.00 34.78 ? 417 ARG A NE    1 
ATOM   3081 C  CZ    . ARG A 1 438 ? 19.215  10.515  -11.734 1.00 35.83 ? 417 ARG A CZ    1 
ATOM   3082 N  NH1   . ARG A 1 438 ? 19.798  9.327   -11.767 1.00 35.84 ? 417 ARG A NH1   1 
ATOM   3083 N  NH2   . ARG A 1 438 ? 19.806  11.543  -12.310 1.00 40.98 ? 417 ARG A NH2   1 
ATOM   3084 N  N     . VAL A 1 439 ? 13.003  5.865   -12.309 1.00 27.94 ? 418 VAL A N     1 
ATOM   3085 C  CA    . VAL A 1 439 ? 12.251  4.617   -12.014 1.00 26.87 ? 418 VAL A CA    1 
ATOM   3086 C  C     . VAL A 1 439 ? 11.893  3.917   -13.328 1.00 25.95 ? 418 VAL A C     1 
ATOM   3087 O  O     . VAL A 1 439 ? 11.049  4.432   -14.078 1.00 29.05 ? 418 VAL A O     1 
ATOM   3088 C  CB    . VAL A 1 439 ? 11.025  4.943   -11.148 1.00 26.20 ? 418 VAL A CB    1 
ATOM   3089 C  CG1   . VAL A 1 439 ? 10.159  3.718   -10.885 1.00 24.14 ? 418 VAL A CG1   1 
ATOM   3090 C  CG2   . VAL A 1 439 ? 11.469  5.580   -9.840  1.00 26.08 ? 418 VAL A CG2   1 
ATOM   3091 N  N     . HIS A 1 440 ? 12.502  2.770   -13.592 1.00 26.74 ? 419 HIS A N     1 
ATOM   3092 C  CA    . HIS A 1 440 ? 12.227  1.926   -14.789 1.00 28.06 ? 419 HIS A CA    1 
ATOM   3093 C  C     . HIS A 1 440 ? 11.330  0.738   -14.394 1.00 27.46 ? 419 HIS A C     1 
ATOM   3094 O  O     . HIS A 1 440 ? 11.216  0.458   -13.180 1.00 23.02 ? 419 HIS A O     1 
ATOM   3095 C  CB    . HIS A 1 440 ? 13.560  1.519   -15.434 1.00 28.76 ? 419 HIS A CB    1 
ATOM   3096 C  CG    . HIS A 1 440 ? 14.298  2.662   -16.054 1.00 27.96 ? 419 HIS A CG    1 
ATOM   3097 N  ND1   . HIS A 1 440 ? 14.602  2.700   -17.400 1.00 29.73 ? 419 HIS A ND1   1 
ATOM   3098 C  CD2   . HIS A 1 440 ? 14.768  3.819   -15.528 1.00 28.73 ? 419 HIS A CD2   1 
ATOM   3099 C  CE1   . HIS A 1 440 ? 15.229  3.831   -17.676 1.00 28.59 ? 419 HIS A CE1   1 
ATOM   3100 N  NE2   . HIS A 1 440 ? 15.349  4.539   -16.542 1.00 27.45 ? 419 HIS A NE2   1 
ATOM   3101 N  N     . TRP A 1 441 ? 10.716  0.083   -15.395 1.00 28.39 ? 420 TRP A N     1 
ATOM   3102 C  CA    . TRP A 1 441 ? 9.614   -0.912  -15.238 1.00 28.15 ? 420 TRP A CA    1 
ATOM   3103 C  C     . TRP A 1 441 ? 9.963   -2.204  -15.968 1.00 25.82 ? 420 TRP A C     1 
ATOM   3104 O  O     . TRP A 1 441 ? 10.291  -2.126  -17.125 1.00 23.78 ? 420 TRP A O     1 
ATOM   3105 C  CB    . TRP A 1 441 ? 8.265   -0.396  -15.746 1.00 27.82 ? 420 TRP A CB    1 
ATOM   3106 C  CG    . TRP A 1 441 ? 7.905   0.939   -15.194 1.00 28.96 ? 420 TRP A CG    1 
ATOM   3107 C  CD1   . TRP A 1 441 ? 7.838   2.119   -15.879 1.00 28.37 ? 420 TRP A CD1   1 
ATOM   3108 C  CD2   . TRP A 1 441 ? 7.587   1.234   -13.824 1.00 31.45 ? 420 TRP A CD2   1 
ATOM   3109 N  NE1   . TRP A 1 441 ? 7.527   3.135   -15.021 1.00 29.08 ? 420 TRP A NE1   1 
ATOM   3110 C  CE2   . TRP A 1 441 ? 7.367   2.626   -13.756 1.00 31.98 ? 420 TRP A CE2   1 
ATOM   3111 C  CE3   . TRP A 1 441 ? 7.480   0.470   -12.653 1.00 30.40 ? 420 TRP A CE3   1 
ATOM   3112 C  CZ2   . TRP A 1 441 ? 7.020   3.255   -12.557 1.00 35.55 ? 420 TRP A CZ2   1 
ATOM   3113 C  CZ3   . TRP A 1 441 ? 7.174   1.097   -11.465 1.00 29.00 ? 420 TRP A CZ3   1 
ATOM   3114 C  CH2   . TRP A 1 441 ? 6.939   2.474   -11.421 1.00 32.56 ? 420 TRP A CH2   1 
ATOM   3115 N  N     . ALA A 1 442 ? 9.813   -3.338  -15.281 1.00 24.82 ? 421 ALA A N     1 
ATOM   3116 C  CA    . ALA A 1 442 ? 9.958   -4.715  -15.792 1.00 24.35 ? 421 ALA A CA    1 
ATOM   3117 C  C     . ALA A 1 442 ? 8.842   -5.568  -15.181 1.00 24.30 ? 421 ALA A C     1 
ATOM   3118 O  O     . ALA A 1 442 ? 8.080   -5.068  -14.286 1.00 23.86 ? 421 ALA A O     1 
ATOM   3119 C  CB    . ALA A 1 442 ? 11.327  -5.261  -15.427 1.00 25.88 ? 421 ALA A CB    1 
ATOM   3120 N  N     . GLY A 1 443 ? 8.779   -6.829  -15.601 1.00 23.51 ? 422 GLY A N     1 
ATOM   3121 C  CA    . GLY A 1 443 ? 7.644   -7.725  -15.331 1.00 20.48 ? 422 GLY A CA    1 
ATOM   3122 C  C     . GLY A 1 443 ? 7.102   -8.276  -16.640 1.00 19.20 ? 422 GLY A C     1 
ATOM   3123 O  O     . GLY A 1 443 ? 7.174   -7.575  -17.666 1.00 17.85 ? 422 GLY A O     1 
ATOM   3124 N  N     . THR A 1 444 ? 6.569   -9.497  -16.612 1.00 18.24 ? 423 THR A N     1 
ATOM   3125 C  CA    . THR A 1 444 ? 6.022   -10.180 -17.805 1.00 20.63 ? 423 THR A CA    1 
ATOM   3126 C  C     . THR A 1 444 ? 4.960   -9.274  -18.480 1.00 20.82 ? 423 THR A C     1 
ATOM   3127 O  O     . THR A 1 444 ? 4.860   -9.325  -19.740 1.00 19.53 ? 423 THR A O     1 
ATOM   3128 C  CB    . THR A 1 444 ? 5.542   -11.566 -17.377 1.00 20.12 ? 423 THR A CB    1 
ATOM   3129 O  OG1   . THR A 1 444 ? 5.423   -12.368 -18.543 1.00 17.29 ? 423 THR A OG1   1 
ATOM   3130 C  CG2   . THR A 1 444 ? 4.247   -11.495 -16.589 1.00 20.88 ? 423 THR A CG2   1 
ATOM   3131 N  N     . GLU A 1 445 ? 4.225   -8.472  -17.691 1.00 18.81 ? 424 GLU A N     1 
ATOM   3132 C  CA    . GLU A 1 445 ? 3.128   -7.597  -18.176 1.00 21.19 ? 424 GLU A CA    1 
ATOM   3133 C  C     . GLU A 1 445 ? 3.725   -6.486  -19.065 1.00 22.28 ? 424 GLU A C     1 
ATOM   3134 O  O     . GLU A 1 445 ? 2.938   -5.795  -19.743 1.00 20.30 ? 424 GLU A O     1 
ATOM   3135 C  CB    . GLU A 1 445 ? 2.306   -6.992  -17.022 1.00 20.62 ? 424 GLU A CB    1 
ATOM   3136 C  CG    . GLU A 1 445 ? 1.393   -7.963  -16.310 1.00 20.63 ? 424 GLU A CG    1 
ATOM   3137 C  CD    . GLU A 1 445 ? 2.073   -8.865  -15.282 1.00 20.49 ? 424 GLU A CD    1 
ATOM   3138 O  OE1   . GLU A 1 445 ? 1.441   -9.836  -14.849 1.00 21.15 ? 424 GLU A OE1   1 
ATOM   3139 O  OE2   . GLU A 1 445 ? 3.244   -8.615  -14.941 1.00 20.19 ? 424 GLU A OE2   1 
ATOM   3140 N  N     . THR A 1 446 ? 5.048   -6.288  -19.073 1.00 23.24 ? 425 THR A N     1 
ATOM   3141 C  CA    . THR A 1 446 ? 5.681   -5.251  -19.937 1.00 24.41 ? 425 THR A CA    1 
ATOM   3142 C  C     . THR A 1 446 ? 6.334   -5.889  -21.173 1.00 22.98 ? 425 THR A C     1 
ATOM   3143 O  O     . THR A 1 446 ? 6.870   -5.112  -21.973 1.00 24.16 ? 425 THR A O     1 
ATOM   3144 C  CB    . THR A 1 446 ? 6.658   -4.357  -19.159 1.00 23.89 ? 425 THR A CB    1 
ATOM   3145 O  OG1   . THR A 1 446 ? 7.683   -5.194  -18.647 1.00 24.64 ? 425 THR A OG1   1 
ATOM   3146 C  CG2   . THR A 1 446 ? 6.011   -3.624  -18.008 1.00 24.58 ? 425 THR A CG2   1 
ATOM   3147 N  N     . ALA A 1 447 ? 6.304   -7.215  -21.322 1.00 21.85 ? 426 ALA A N     1 
ATOM   3148 C  CA    . ALA A 1 447 ? 6.883   -7.959  -22.476 1.00 22.20 ? 426 ALA A CA    1 
ATOM   3149 C  C     . ALA A 1 447 ? 6.082   -7.697  -23.760 1.00 22.55 ? 426 ALA A C     1 
ATOM   3150 O  O     . ALA A 1 447 ? 4.843   -7.602  -23.667 1.00 23.67 ? 426 ALA A O     1 
ATOM   3151 C  CB    . ALA A 1 447 ? 6.900   -9.445  -22.194 1.00 20.81 ? 426 ALA A CB    1 
ATOM   3152 N  N     . GLU A 1 448 ? 6.771   -7.650  -24.905 1.00 23.36 ? 427 GLU A N     1 
ATOM   3153 C  CA    . GLU A 1 448 ? 6.184   -7.695  -26.274 1.00 25.10 ? 427 GLU A CA    1 
ATOM   3154 C  C     . GLU A 1 448 ? 5.772   -9.134  -26.613 1.00 23.43 ? 427 GLU A C     1 
ATOM   3155 O  O     . GLU A 1 448 ? 4.662   -9.297  -27.102 1.00 25.59 ? 427 GLU A O     1 
ATOM   3156 C  CB    . GLU A 1 448 ? 7.156   -7.181  -27.356 1.00 25.79 ? 427 GLU A CB    1 
ATOM   3157 C  CG    . GLU A 1 448 ? 7.433   -5.671  -27.306 1.00 28.54 ? 427 GLU A CG    1 
ATOM   3158 C  CD    . GLU A 1 448 ? 8.285   -5.085  -28.441 1.00 29.97 ? 427 GLU A CD    1 
ATOM   3159 O  OE1   . GLU A 1 448 ? 8.910   -4.024  -28.228 1.00 28.77 ? 427 GLU A OE1   1 
ATOM   3160 O  OE2   . GLU A 1 448 ? 8.263   -5.649  -29.570 1.00 31.94 ? 427 GLU A OE2   1 
ATOM   3161 N  N     . ARG A 1 449 ? 6.667   -10.114 -26.457 1.00 21.94 ? 428 ARG A N     1 
ATOM   3162 C  CA    . ARG A 1 449 ? 6.434   -11.537 -26.865 1.00 23.96 ? 428 ARG A CA    1 
ATOM   3163 C  C     . ARG A 1 449 ? 6.224   -12.432 -25.615 1.00 19.88 ? 428 ARG A C     1 
ATOM   3164 O  O     . ARG A 1 449 ? 6.890   -12.227 -24.577 1.00 18.14 ? 428 ARG A O     1 
ATOM   3165 C  CB    . ARG A 1 449 ? 7.577   -12.028 -27.777 1.00 25.05 ? 428 ARG A CB    1 
ATOM   3166 C  CG    . ARG A 1 449 ? 7.495   -11.534 -29.219 1.00 30.13 ? 428 ARG A CG    1 
ATOM   3167 C  CD    . ARG A 1 449 ? 8.331   -12.296 -30.257 1.00 33.87 ? 428 ARG A CD    1 
ATOM   3168 N  NE    . ARG A 1 449 ? 8.314   -13.762 -30.103 1.00 38.61 ? 428 ARG A NE    1 
ATOM   3169 C  CZ    . ARG A 1 449 ? 9.322   -14.521 -29.610 1.00 41.11 ? 428 ARG A CZ    1 
ATOM   3170 N  NH1   . ARG A 1 449 ? 9.159   -15.835 -29.527 1.00 38.72 ? 428 ARG A NH1   1 
ATOM   3171 N  NH2   . ARG A 1 449 ? 10.483  -13.986 -29.225 1.00 37.46 ? 428 ARG A NH2   1 
ATOM   3172 N  N     . TRP A 1 450 ? 5.332   -13.411 -25.720 1.00 18.15 ? 429 TRP A N     1 
ATOM   3173 C  CA    . TRP A 1 450 ? 4.841   -14.218 -24.572 1.00 18.85 ? 429 TRP A CA    1 
ATOM   3174 C  C     . TRP A 1 450 ? 4.635   -13.370 -23.312 1.00 16.85 ? 429 TRP A C     1 
ATOM   3175 O  O     . TRP A 1 450 ? 5.025   -13.791 -22.217 1.00 16.25 ? 429 TRP A O     1 
ATOM   3176 C  CB    . TRP A 1 450 ? 5.807   -15.382 -24.343 1.00 19.69 ? 429 TRP A CB    1 
ATOM   3177 C  CG    . TRP A 1 450 ? 5.719   -16.379 -25.450 1.00 20.52 ? 429 TRP A CG    1 
ATOM   3178 C  CD1   . TRP A 1 450 ? 6.596   -16.536 -26.485 1.00 20.30 ? 429 TRP A CD1   1 
ATOM   3179 C  CD2   . TRP A 1 450 ? 4.663   -17.334 -25.658 1.00 21.52 ? 429 TRP A CD2   1 
ATOM   3180 N  NE1   . TRP A 1 450 ? 6.169   -17.546 -27.306 1.00 21.10 ? 429 TRP A NE1   1 
ATOM   3181 C  CE2   . TRP A 1 450 ? 4.995   -18.065 -26.816 1.00 21.95 ? 429 TRP A CE2   1 
ATOM   3182 C  CE3   . TRP A 1 450 ? 3.495   -17.677 -24.966 1.00 23.65 ? 429 TRP A CE3   1 
ATOM   3183 C  CZ2   . TRP A 1 450 ? 4.190   -19.100 -27.295 1.00 21.70 ? 429 TRP A CZ2   1 
ATOM   3184 C  CZ3   . TRP A 1 450 ? 2.697   -18.703 -25.439 1.00 21.99 ? 429 TRP A CZ3   1 
ATOM   3185 C  CH2   . TRP A 1 450 ? 3.042   -19.397 -26.593 1.00 22.98 ? 429 TRP A CH2   1 
ATOM   3186 N  N     . THR A 1 451 ? 3.958   -12.238 -23.417 1.00 18.53 ? 430 THR A N     1 
ATOM   3187 C  CA    . THR A 1 451 ? 3.467   -11.511 -22.210 1.00 19.10 ? 430 THR A CA    1 
ATOM   3188 C  C     . THR A 1 451 ? 2.597   -12.482 -21.393 1.00 19.06 ? 430 THR A C     1 
ATOM   3189 O  O     . THR A 1 451 ? 1.829   -13.234 -21.977 1.00 18.68 ? 430 THR A O     1 
ATOM   3190 C  CB    . THR A 1 451 ? 2.764   -10.195 -22.558 1.00 19.63 ? 430 THR A CB    1 
ATOM   3191 O  OG1   . THR A 1 451 ? 2.687   -9.443  -21.341 1.00 20.64 ? 430 THR A OG1   1 
ATOM   3192 C  CG2   . THR A 1 451 ? 1.388   -10.361 -23.185 1.00 19.27 ? 430 THR A CG2   1 
ATOM   3193 N  N     . GLY A 1 452 ? 2.774   -12.511 -20.083 1.00 19.47 ? 431 GLY A N     1 
ATOM   3194 C  CA    . GLY A 1 452 ? 2.025   -13.401 -19.191 1.00 20.99 ? 431 GLY A CA    1 
ATOM   3195 C  C     . GLY A 1 452 ? 2.823   -14.638 -18.829 1.00 20.66 ? 431 GLY A C     1 
ATOM   3196 O  O     . GLY A 1 452 ? 2.365   -15.378 -17.941 1.00 24.75 ? 431 GLY A O     1 
ATOM   3197 N  N     . TYR A 1 453 ? 3.944   -14.884 -19.493 1.00 19.21 ? 432 TYR A N     1 
ATOM   3198 C  CA    . TYR A 1 453 ? 4.724   -16.145 -19.340 1.00 20.30 ? 432 TYR A CA    1 
ATOM   3199 C  C     . TYR A 1 453 ? 6.117   -15.791 -18.791 1.00 19.93 ? 432 TYR A C     1 
ATOM   3200 O  O     . TYR A 1 453 ? 6.436   -14.584 -18.776 1.00 20.51 ? 432 TYR A O     1 
ATOM   3201 C  CB    . TYR A 1 453 ? 4.751   -16.935 -20.650 1.00 20.35 ? 432 TYR A CB    1 
ATOM   3202 C  CG    . TYR A 1 453 ? 3.412   -17.461 -21.099 1.00 20.08 ? 432 TYR A CG    1 
ATOM   3203 C  CD1   . TYR A 1 453 ? 3.069   -18.787 -20.908 1.00 20.49 ? 432 TYR A CD1   1 
ATOM   3204 C  CD2   . TYR A 1 453 ? 2.446   -16.631 -21.644 1.00 21.23 ? 432 TYR A CD2   1 
ATOM   3205 C  CE1   . TYR A 1 453 ? 1.838   -19.280 -21.285 1.00 20.06 ? 432 TYR A CE1   1 
ATOM   3206 C  CE2   . TYR A 1 453 ? 1.214   -17.121 -22.046 1.00 20.79 ? 432 TYR A CE2   1 
ATOM   3207 C  CZ    . TYR A 1 453 ? 0.908   -18.455 -21.872 1.00 20.68 ? 432 TYR A CZ    1 
ATOM   3208 O  OH    . TYR A 1 453 ? -0.327  -18.962 -22.201 1.00 21.85 ? 432 TYR A OH    1 
ATOM   3209 N  N     . ILE A 1 454 ? 6.836   -16.791 -18.251 1.00 18.68 ? 433 ILE A N     1 
ATOM   3210 C  CA    . ILE A 1 454 ? 8.260   -16.709 -17.796 1.00 19.04 ? 433 ILE A CA    1 
ATOM   3211 C  C     . ILE A 1 454 ? 9.108   -16.064 -18.899 1.00 19.60 ? 433 ILE A C     1 
ATOM   3212 O  O     . ILE A 1 454 ? 9.907   -15.169 -18.583 1.00 19.98 ? 433 ILE A O     1 
ATOM   3213 C  CB    . ILE A 1 454 ? 8.819   -18.097 -17.427 1.00 19.18 ? 433 ILE A CB    1 
ATOM   3214 C  CG1   . ILE A 1 454 ? 8.059   -18.740 -16.263 1.00 18.40 ? 433 ILE A CG1   1 
ATOM   3215 C  CG2   . ILE A 1 454 ? 10.313  -17.999 -17.135 1.00 18.98 ? 433 ILE A CG2   1 
ATOM   3216 C  CD1   . ILE A 1 454 ? 8.110   -20.235 -16.273 1.00 19.76 ? 433 ILE A CD1   1 
ATOM   3217 N  N     . ASP A 1 455 ? 8.926   -16.527 -20.133 1.00 18.74 ? 434 ASP A N     1 
ATOM   3218 C  CA    . ASP A 1 455 ? 9.659   -16.078 -21.334 1.00 20.24 ? 434 ASP A CA    1 
ATOM   3219 C  C     . ASP A 1 455 ? 9.519   -14.562 -21.460 1.00 21.07 ? 434 ASP A C     1 
ATOM   3220 O  O     . ASP A 1 455 ? 10.556  -13.900 -21.628 1.00 22.18 ? 434 ASP A O     1 
ATOM   3221 C  CB    . ASP A 1 455 ? 9.159   -16.803 -22.588 1.00 21.86 ? 434 ASP A CB    1 
ATOM   3222 C  CG    . ASP A 1 455 ? 10.119  -16.672 -23.752 1.00 21.68 ? 434 ASP A CG    1 
ATOM   3223 O  OD1   . ASP A 1 455 ? 9.877   -15.807 -24.586 1.00 19.91 ? 434 ASP A OD1   1 
ATOM   3224 O  OD2   . ASP A 1 455 ? 11.131  -17.414 -23.759 1.00 25.38 ? 434 ASP A OD2   1 
ATOM   3225 N  N     . GLY A 1 456 ? 8.292   -14.050 -21.366 1.00 19.67 ? 435 GLY A N     1 
ATOM   3226 C  CA    . GLY A 1 456 ? 7.975   -12.611 -21.277 1.00 19.21 ? 435 GLY A CA    1 
ATOM   3227 C  C     . GLY A 1 456 ? 8.676   -11.909 -20.121 1.00 18.59 ? 435 GLY A C     1 
ATOM   3228 O  O     . GLY A 1 456 ? 9.199   -10.776 -20.310 1.00 18.43 ? 435 GLY A O     1 
ATOM   3229 N  N     . ALA A 1 457 ? 8.622   -12.468 -18.919 1.00 19.53 ? 436 ALA A N     1 
ATOM   3230 C  CA    . ALA A 1 457 ? 9.374   -11.921 -17.755 1.00 20.16 ? 436 ALA A CA    1 
ATOM   3231 C  C     . ALA A 1 457 ? 10.834  -11.675 -18.190 1.00 19.74 ? 436 ALA A C     1 
ATOM   3232 O  O     . ALA A 1 457 ? 11.346  -10.576 -17.971 1.00 19.58 ? 436 ALA A O     1 
ATOM   3233 C  CB    . ALA A 1 457 ? 9.302   -12.863 -16.573 1.00 19.37 ? 436 ALA A CB    1 
ATOM   3234 N  N     . ILE A 1 458 ? 11.442  -12.685 -18.810 1.00 20.18 ? 437 ILE A N     1 
ATOM   3235 C  CA    . ILE A 1 458 ? 12.881  -12.700 -19.199 1.00 21.43 ? 437 ILE A CA    1 
ATOM   3236 C  C     . ILE A 1 458 ? 13.110  -11.540 -20.159 1.00 21.58 ? 437 ILE A C     1 
ATOM   3237 O  O     . ILE A 1 458 ? 13.962  -10.689 -19.826 1.00 24.65 ? 437 ILE A O     1 
ATOM   3238 C  CB    . ILE A 1 458 ? 13.310  -14.069 -19.745 1.00 20.35 ? 437 ILE A CB    1 
ATOM   3239 C  CG1   . ILE A 1 458 ? 13.272  -15.096 -18.603 1.00 20.81 ? 437 ILE A CG1   1 
ATOM   3240 C  CG2   . ILE A 1 458 ? 14.694  -13.989 -20.409 1.00 21.33 ? 437 ILE A CG2   1 
ATOM   3241 C  CD1   . ILE A 1 458 ? 13.563  -16.547 -19.009 1.00 21.07 ? 437 ILE A CD1   1 
ATOM   3242 N  N     . GLU A 1 459 ? 12.285  -11.439 -21.202 1.00 20.25 ? 438 GLU A N     1 
ATOM   3243 C  CA    . GLU A 1 459 ? 12.318  -10.319 -22.174 1.00 19.92 ? 438 GLU A CA    1 
ATOM   3244 C  C     . GLU A 1 459 ? 12.333  -8.999  -21.404 1.00 19.67 ? 438 GLU A C     1 
ATOM   3245 O  O     . GLU A 1 459 ? 13.314  -8.283  -21.582 1.00 19.14 ? 438 GLU A O     1 
ATOM   3246 C  CB    . GLU A 1 459 ? 11.127  -10.359 -23.127 1.00 20.46 ? 438 GLU A CB    1 
ATOM   3247 C  CG    . GLU A 1 459 ? 11.233  -9.290  -24.214 1.00 20.33 ? 438 GLU A CG    1 
ATOM   3248 C  CD    . GLU A 1 459 ? 9.928   -9.042  -24.925 1.00 21.07 ? 438 GLU A CD    1 
ATOM   3249 O  OE1   . GLU A 1 459 ? 9.453   -7.890  -24.874 1.00 22.32 ? 438 GLU A OE1   1 
ATOM   3250 O  OE2   . GLU A 1 459 ? 9.400   -10.010 -25.533 1.00 20.74 ? 438 GLU A OE2   1 
ATOM   3251 N  N     . SER A 1 460 ? 11.289  -8.710  -20.595 1.00 20.18 ? 439 SER A N     1 
ATOM   3252 C  CA    . SER A 1 460 ? 11.150  -7.465  -19.780 1.00 20.15 ? 439 SER A CA    1 
ATOM   3253 C  C     . SER A 1 460 ? 12.454  -7.179  -19.030 1.00 19.80 ? 439 SER A C     1 
ATOM   3254 O  O     . SER A 1 460 ? 12.883  -6.021  -19.046 1.00 19.35 ? 439 SER A O     1 
ATOM   3255 C  CB    . SER A 1 460 ? 9.928   -7.449  -18.848 1.00 20.25 ? 439 SER A CB    1 
ATOM   3256 O  OG    . SER A 1 460 ? 10.071  -8.307  -17.709 1.00 21.23 ? 439 SER A OG    1 
ATOM   3257 N  N     . GLY A 1 461 ? 13.060  -8.176  -18.378 1.00 21.09 ? 440 GLY A N     1 
ATOM   3258 C  CA    . GLY A 1 461 ? 14.343  -7.984  -17.666 1.00 20.87 ? 440 GLY A CA    1 
ATOM   3259 C  C     . GLY A 1 461 ? 15.446  -7.491  -18.582 1.00 22.85 ? 440 GLY A C     1 
ATOM   3260 O  O     . GLY A 1 461 ? 16.112  -6.499  -18.232 1.00 28.35 ? 440 GLY A O     1 
ATOM   3261 N  N     . GLN A 1 462 ? 15.662  -8.161  -19.715 1.00 23.56 ? 441 GLN A N     1 
ATOM   3262 C  CA    . GLN A 1 462 ? 16.706  -7.790  -20.707 1.00 24.28 ? 441 GLN A CA    1 
ATOM   3263 C  C     . GLN A 1 462 ? 16.479  -6.328  -21.145 1.00 25.46 ? 441 GLN A C     1 
ATOM   3264 O  O     . GLN A 1 462 ? 17.460  -5.551  -21.100 1.00 30.79 ? 441 GLN A O     1 
ATOM   3265 C  CB    . GLN A 1 462 ? 16.705  -8.759  -21.898 1.00 24.02 ? 441 GLN A CB    1 
ATOM   3266 C  CG    . GLN A 1 462 ? 17.149  -10.192 -21.585 1.00 23.47 ? 441 GLN A CG    1 
ATOM   3267 C  CD    . GLN A 1 462 ? 16.849  -11.155 -22.722 1.00 24.41 ? 441 GLN A CD    1 
ATOM   3268 O  OE1   . GLN A 1 462 ? 16.329  -10.776 -23.768 1.00 24.92 ? 441 GLN A OE1   1 
ATOM   3269 N  NE2   . GLN A 1 462 ? 17.135  -12.430 -22.531 1.00 22.10 ? 441 GLN A NE2   1 
ATOM   3270 N  N     . ARG A 1 463 ? 15.241  -5.953  -21.507 1.00 23.87 ? 442 ARG A N     1 
ATOM   3271 C  CA    . ARG A 1 463 ? 14.851  -4.619  -22.037 1.00 23.71 ? 442 ARG A CA    1 
ATOM   3272 C  C     . ARG A 1 463 ? 15.009  -3.530  -20.955 1.00 27.15 ? 442 ARG A C     1 
ATOM   3273 O  O     . ARG A 1 463 ? 15.571  -2.488  -21.283 1.00 32.32 ? 442 ARG A O     1 
ATOM   3274 C  CB    . ARG A 1 463 ? 13.416  -4.660  -22.560 1.00 24.64 ? 442 ARG A CB    1 
ATOM   3275 C  CG    . ARG A 1 463 ? 12.952  -3.400  -23.283 1.00 23.43 ? 442 ARG A CG    1 
ATOM   3276 C  CD    . ARG A 1 463 ? 12.267  -2.406  -22.390 1.00 24.87 ? 442 ARG A CD    1 
ATOM   3277 N  NE    . ARG A 1 463 ? 11.204  -3.024  -21.576 1.00 28.25 ? 442 ARG A NE    1 
ATOM   3278 C  CZ    . ARG A 1 463 ? 10.698  -2.515  -20.453 1.00 26.18 ? 442 ARG A CZ    1 
ATOM   3279 N  NH1   . ARG A 1 463 ? 11.157  -1.367  -19.983 1.00 26.03 ? 442 ARG A NH1   1 
ATOM   3280 N  NH2   . ARG A 1 463 ? 9.755   -3.167  -19.783 1.00 29.02 ? 442 ARG A NH2   1 
ATOM   3281 N  N     . ALA A 1 464 ? 14.557  -3.749  -19.720 1.00 25.09 ? 443 ALA A N     1 
ATOM   3282 C  CA    . ALA A 1 464 ? 14.698  -2.798  -18.589 1.00 26.23 ? 443 ALA A CA    1 
ATOM   3283 C  C     . ALA A 1 464 ? 16.169  -2.572  -18.236 1.00 25.64 ? 443 ALA A C     1 
ATOM   3284 O  O     . ALA A 1 464 ? 16.497  -1.492  -17.758 1.00 22.86 ? 443 ALA A O     1 
ATOM   3285 C  CB    . ALA A 1 464 ? 13.970  -3.327  -17.375 1.00 27.25 ? 443 ALA A CB    1 
ATOM   3286 N  N     . ALA A 1 465 ? 17.012  -3.589  -18.360 1.00 26.56 ? 444 ALA A N     1 
ATOM   3287 C  CA    . ALA A 1 465 ? 18.452  -3.444  -18.034 1.00 28.42 ? 444 ALA A CA    1 
ATOM   3288 C  C     . ALA A 1 465 ? 19.133  -2.620  -19.139 1.00 26.36 ? 444 ALA A C     1 
ATOM   3289 O  O     . ALA A 1 465 ? 19.740  -1.608  -18.785 1.00 26.66 ? 444 ALA A O     1 
ATOM   3290 C  CB    . ALA A 1 465 ? 19.104  -4.785  -17.813 1.00 26.86 ? 444 ALA A CB    1 
ATOM   3291 N  N     . ALA A 1 466 ? 18.957  -2.979  -20.414 1.00 27.57 ? 445 ALA A N     1 
ATOM   3292 C  CA    . ALA A 1 466 ? 19.464  -2.226  -21.590 1.00 27.70 ? 445 ALA A CA    1 
ATOM   3293 C  C     . ALA A 1 466 ? 19.132  -0.742  -21.444 1.00 27.62 ? 445 ALA A C     1 
ATOM   3294 O  O     . ALA A 1 466 ? 19.997  0.096   -21.708 1.00 28.96 ? 445 ALA A O     1 
ATOM   3295 C  CB    . ALA A 1 466 ? 18.847  -2.751  -22.848 1.00 27.98 ? 445 ALA A CB    1 
ATOM   3296 N  N     . GLU A 1 467 ? 17.901  -0.448  -21.046 1.00 28.44 ? 446 GLU A N     1 
ATOM   3297 C  CA    . GLU A 1 467 ? 17.397  0.928   -20.831 1.00 28.97 ? 446 GLU A CA    1 
ATOM   3298 C  C     . GLU A 1 467 ? 18.280  1.644   -19.799 1.00 29.33 ? 446 GLU A C     1 
ATOM   3299 O  O     . GLU A 1 467 ? 18.560  2.852   -19.989 1.00 33.52 ? 446 GLU A O     1 
ATOM   3300 C  CB    . GLU A 1 467 ? 15.951  0.869   -20.349 1.00 28.26 ? 446 GLU A CB    1 
ATOM   3301 C  CG    . GLU A 1 467 ? 14.928  0.990   -21.441 1.00 28.17 ? 446 GLU A CG    1 
ATOM   3302 C  CD    . GLU A 1 467 ? 13.497  0.999   -20.942 1.00 26.02 ? 446 GLU A CD    1 
ATOM   3303 O  OE1   . GLU A 1 467 ? 12.668  0.486   -21.703 1.00 27.23 ? 446 GLU A OE1   1 
ATOM   3304 O  OE2   . GLU A 1 467 ? 13.203  1.587   -19.826 1.00 22.76 ? 446 GLU A OE2   1 
ATOM   3305 N  N     . VAL A 1 468 ? 18.639  0.971   -18.706 1.00 30.94 ? 447 VAL A N     1 
ATOM   3306 C  CA    . VAL A 1 468 ? 19.271  1.633   -17.527 1.00 31.67 ? 447 VAL A CA    1 
ATOM   3307 C  C     . VAL A 1 468 ? 20.777  1.744   -17.811 1.00 32.87 ? 447 VAL A C     1 
ATOM   3308 O  O     . VAL A 1 468 ? 21.352  2.751   -17.467 1.00 36.18 ? 447 VAL A O     1 
ATOM   3309 C  CB    . VAL A 1 468 ? 18.924  0.907   -16.208 1.00 34.62 ? 447 VAL A CB    1 
ATOM   3310 C  CG1   . VAL A 1 468 ? 19.722  1.433   -15.026 1.00 38.33 ? 447 VAL A CG1   1 
ATOM   3311 C  CG2   . VAL A 1 468 ? 17.443  0.988   -15.874 1.00 31.70 ? 447 VAL A CG2   1 
ATOM   3312 N  N     . LEU A 1 469 ? 21.383  0.780   -18.491 1.00 32.94 ? 448 LEU A N     1 
ATOM   3313 C  CA    . LEU A 1 469 ? 22.786  0.888   -18.960 1.00 37.12 ? 448 LEU A CA    1 
ATOM   3314 C  C     . LEU A 1 469 ? 22.911  2.103   -19.887 1.00 42.17 ? 448 LEU A C     1 
ATOM   3315 O  O     . LEU A 1 469 ? 23.652  3.031   -19.524 1.00 43.44 ? 448 LEU A O     1 
ATOM   3316 C  CB    . LEU A 1 469 ? 23.197  -0.416  -19.634 1.00 35.28 ? 448 LEU A CB    1 
ATOM   3317 C  CG    . LEU A 1 469 ? 23.157  -1.615  -18.693 1.00 33.56 ? 448 LEU A CG    1 
ATOM   3318 C  CD1   . LEU A 1 469 ? 23.635  -2.884  -19.393 1.00 30.99 ? 448 LEU A CD1   1 
ATOM   3319 C  CD2   . LEU A 1 469 ? 23.967  -1.321  -17.433 1.00 32.66 ? 448 LEU A CD2   1 
ATOM   3320 N  N     . ALA A 1 470 ? 22.121  2.151   -20.960 1.00 42.69 ? 449 ALA A N     1 
ATOM   3321 C  CA    . ALA A 1 470 ? 22.025  3.300   -21.887 1.00 40.15 ? 449 ALA A CA    1 
ATOM   3322 C  C     . ALA A 1 470 ? 21.910  4.607   -21.093 1.00 43.44 ? 449 ALA A C     1 
ATOM   3323 O  O     . ALA A 1 470 ? 22.801  5.461   -21.224 1.00 45.47 ? 449 ALA A O     1 
ATOM   3324 C  CB    . ALA A 1 470 ? 20.838  3.110   -22.789 1.00 40.81 ? 449 ALA A CB    1 
ATOM   3325 N  N     . ALA A 1 471 ? 20.854  4.747   -20.289 1.00 43.85 ? 450 ALA A N     1 
ATOM   3326 C  CA    . ALA A 1 471 ? 20.436  6.009   -19.634 1.00 42.86 ? 450 ALA A CA    1 
ATOM   3327 C  C     . ALA A 1 471 ? 21.427  6.443   -18.544 1.00 46.52 ? 450 ALA A C     1 
ATOM   3328 O  O     . ALA A 1 471 ? 21.301  7.591   -18.092 1.00 45.81 ? 450 ALA A O     1 
ATOM   3329 C  CB    . ALA A 1 471 ? 19.051  5.845   -19.053 1.00 46.53 ? 450 ALA A CB    1 
ATOM   3330 N  N     . LEU A 1 472 ? 22.349  5.572   -18.117 1.00 51.00 ? 451 LEU A N     1 
ATOM   3331 C  CA    . LEU A 1 472 ? 23.258  5.802   -16.956 1.00 52.05 ? 451 LEU A CA    1 
ATOM   3332 C  C     . LEU A 1 472 ? 24.510  6.563   -17.405 1.00 53.09 ? 451 LEU A C     1 
ATOM   3333 O  O     . LEU A 1 472 ? 24.845  7.584   -16.745 1.00 42.72 ? 451 LEU A O     1 
ATOM   3334 C  CB    . LEU A 1 472 ? 23.667  4.461   -16.328 1.00 53.34 ? 451 LEU A CB    1 
ATOM   3335 C  CG    . LEU A 1 472 ? 22.858  3.985   -15.114 1.00 48.98 ? 451 LEU A CG    1 
ATOM   3336 C  CD1   . LEU A 1 472 ? 23.154  2.513   -14.811 1.00 46.86 ? 451 LEU A CD1   1 
ATOM   3337 C  CD2   . LEU A 1 472 ? 23.150  4.842   -13.894 1.00 48.65 ? 451 LEU A CD2   1 
ATOM   3338 N  N     . GLY A 1 473 ? 25.179  6.053   -18.451 1.00 58.85 ? 452 GLY A N     1 
ATOM   3339 C  CA    . GLY A 1 473 ? 26.494  6.523   -18.935 1.00 64.96 ? 452 GLY A CA    1 
ATOM   3340 C  C     . GLY A 1 473 ? 26.383  7.353   -20.203 1.00 64.53 ? 452 GLY A C     1 
ATOM   3341 O  O     . GLY A 1 473 ? 27.396  7.535   -20.868 1.00 59.94 ? 452 GLY A O     1 
ATOM   3342 N  N     . GLN B 1 26  ? -4.056  3.859   22.990  1.00 50.56 ? 5   GLN B N     1 
ATOM   3343 C  CA    . GLN B 1 26  ? -5.183  2.887   22.973  1.00 52.21 ? 5   GLN B CA    1 
ATOM   3344 C  C     . GLN B 1 26  ? -6.488  3.682   23.004  1.00 47.30 ? 5   GLN B C     1 
ATOM   3345 O  O     . GLN B 1 26  ? -6.572  4.610   23.784  1.00 45.32 ? 5   GLN B O     1 
ATOM   3346 C  CB    . GLN B 1 26  ? -5.077  1.874   24.125  1.00 48.80 ? 5   GLN B CB    1 
ATOM   3347 C  CG    . GLN B 1 26  ? -6.301  0.968   24.293  1.00 52.99 ? 5   GLN B CG    1 
ATOM   3348 C  CD    . GLN B 1 26  ? -6.487  -0.111  23.242  1.00 59.65 ? 5   GLN B CD    1 
ATOM   3349 O  OE1   . GLN B 1 26  ? -5.554  -0.526  22.560  1.00 65.07 ? 5   GLN B OE1   1 
ATOM   3350 N  NE2   . GLN B 1 26  ? -7.707  -0.612  23.107  1.00 62.21 ? 5   GLN B NE2   1 
ATOM   3351 N  N     . VAL B 1 27  ? -7.437  3.317   22.150  1.00 44.26 ? 6   VAL B N     1 
ATOM   3352 C  CA    . VAL B 1 27  ? -8.834  3.836   22.120  1.00 46.45 ? 6   VAL B CA    1 
ATOM   3353 C  C     . VAL B 1 27  ? -9.735  2.696   21.617  1.00 46.80 ? 6   VAL B C     1 
ATOM   3354 O  O     . VAL B 1 27  ? -9.197  1.643   21.138  1.00 39.16 ? 6   VAL B O     1 
ATOM   3355 C  CB    . VAL B 1 27  ? -8.983  5.084   21.214  1.00 55.05 ? 6   VAL B CB    1 
ATOM   3356 C  CG1   . VAL B 1 27  ? -8.327  6.323   21.812  1.00 60.33 ? 6   VAL B CG1   1 
ATOM   3357 C  CG2   . VAL B 1 27  ? -8.463  4.838   19.797  1.00 53.89 ? 6   VAL B CG2   1 
ATOM   3358 N  N     . ASP B 1 28  ? -11.050 2.917   21.654  1.00 38.23 ? 7   ASP B N     1 
ATOM   3359 C  CA    . ASP B 1 28  ? -12.052 1.895   21.268  1.00 38.67 ? 7   ASP B CA    1 
ATOM   3360 C  C     . ASP B 1 28  ? -12.017 1.724   19.726  1.00 35.50 ? 7   ASP B C     1 
ATOM   3361 O  O     . ASP B 1 28  ? -12.019 0.552   19.234  1.00 26.57 ? 7   ASP B O     1 
ATOM   3362 C  CB    . ASP B 1 28  ? -13.420 2.218   21.911  1.00 40.66 ? 7   ASP B CB    1 
ATOM   3363 C  CG    . ASP B 1 28  ? -13.439 2.393   23.441  1.00 40.01 ? 7   ASP B CG    1 
ATOM   3364 O  OD1   . ASP B 1 28  ? -12.407 2.100   24.110  1.00 34.52 ? 7   ASP B OD1   1 
ATOM   3365 O  OD2   . ASP B 1 28  ? -14.482 2.866   23.966  1.00 38.36 ? 7   ASP B OD2   1 
ATOM   3366 N  N     . VAL B 1 29  ? -11.966 2.827   18.975  1.00 32.57 ? 8   VAL B N     1 
ATOM   3367 C  CA    . VAL B 1 29  ? -12.118 2.812   17.489  1.00 33.86 ? 8   VAL B CA    1 
ATOM   3368 C  C     . VAL B 1 29  ? -11.137 3.807   16.858  1.00 34.11 ? 8   VAL B C     1 
ATOM   3369 O  O     . VAL B 1 29  ? -10.978 4.922   17.394  1.00 40.47 ? 8   VAL B O     1 
ATOM   3370 C  CB    . VAL B 1 29  ? -13.564 3.107   17.058  1.00 34.00 ? 8   VAL B CB    1 
ATOM   3371 C  CG1   . VAL B 1 29  ? -13.691 3.239   15.538  1.00 33.89 ? 8   VAL B CG1   1 
ATOM   3372 C  CG2   . VAL B 1 29  ? -14.534 2.053   17.582  1.00 33.63 ? 8   VAL B CG2   1 
ATOM   3373 N  N     . VAL B 1 30  ? -10.495 3.402   15.764  1.00 32.98 ? 9   VAL B N     1 
ATOM   3374 C  CA    . VAL B 1 30  ? -9.592  4.258   14.940  1.00 33.09 ? 9   VAL B CA    1 
ATOM   3375 C  C     . VAL B 1 30  ? -10.223 4.380   13.551  1.00 33.90 ? 9   VAL B C     1 
ATOM   3376 O  O     . VAL B 1 30  ? -10.534 3.335   12.927  1.00 30.93 ? 9   VAL B O     1 
ATOM   3377 C  CB    . VAL B 1 30  ? -8.168  3.688   14.893  1.00 31.06 ? 9   VAL B CB    1 
ATOM   3378 C  CG1   . VAL B 1 30  ? -8.152  2.314   14.240  1.00 34.27 ? 9   VAL B CG1   1 
ATOM   3379 C  CG2   . VAL B 1 30  ? -7.210  4.646   14.208  1.00 31.04 ? 9   VAL B CG2   1 
ATOM   3380 N  N     . VAL B 1 31  ? -10.496 5.608   13.118  1.00 33.52 ? 10  VAL B N     1 
ATOM   3381 C  CA    . VAL B 1 31  ? -11.123 5.857   11.789  1.00 31.46 ? 10  VAL B CA    1 
ATOM   3382 C  C     . VAL B 1 31  ? -9.990  6.309   10.863  1.00 30.10 ? 10  VAL B C     1 
ATOM   3383 O  O     . VAL B 1 31  ? -9.230  7.188   11.266  1.00 30.04 ? 10  VAL B O     1 
ATOM   3384 C  CB    . VAL B 1 31  ? -12.307 6.842   11.898  1.00 33.74 ? 10  VAL B CB    1 
ATOM   3385 C  CG1   . VAL B 1 31  ? -13.032 7.056   10.572  1.00 31.44 ? 10  VAL B CG1   1 
ATOM   3386 C  CG2   . VAL B 1 31  ? -13.317 6.390   12.963  1.00 33.22 ? 10  VAL B CG2   1 
ATOM   3387 N  N     . VAL B 1 32  ? -9.829  5.652   9.711   1.00 30.24 ? 11  VAL B N     1 
ATOM   3388 C  CA    . VAL B 1 32  ? -8.858  6.048   8.640   1.00 29.92 ? 11  VAL B CA    1 
ATOM   3389 C  C     . VAL B 1 32  ? -9.615  6.854   7.587   1.00 28.81 ? 11  VAL B C     1 
ATOM   3390 O  O     . VAL B 1 32  ? -10.474 6.271   6.908   1.00 30.13 ? 11  VAL B O     1 
ATOM   3391 C  CB    . VAL B 1 32  ? -8.144  4.836   8.023   1.00 29.61 ? 11  VAL B CB    1 
ATOM   3392 C  CG1   . VAL B 1 32  ? -6.978  5.271   7.162   1.00 31.59 ? 11  VAL B CG1   1 
ATOM   3393 C  CG2   . VAL B 1 32  ? -7.672  3.860   9.080   1.00 27.75 ? 11  VAL B CG2   1 
ATOM   3394 N  N     . GLY B 1 33  ? -9.355  8.168   7.538   1.00 31.24 ? 12  GLY B N     1 
ATOM   3395 C  CA    . GLY B 1 33  ? -9.960  9.128   6.594   1.00 30.78 ? 12  GLY B CA    1 
ATOM   3396 C  C     . GLY B 1 33  ? -10.892 10.146  7.267   1.00 30.46 ? 12  GLY B C     1 
ATOM   3397 O  O     . GLY B 1 33  ? -11.891 9.741   7.906   1.00 28.55 ? 12  GLY B O     1 
ATOM   3398 N  N     . ALA B 1 34  ? -10.619 11.438  7.072   1.00 29.82 ? 13  ALA B N     1 
ATOM   3399 C  CA    . ALA B 1 34  ? -11.426 12.550  7.618   1.00 28.83 ? 13  ALA B CA    1 
ATOM   3400 C  C     . ALA B 1 34  ? -12.233 13.179  6.485   1.00 30.11 ? 13  ALA B C     1 
ATOM   3401 O  O     . ALA B 1 34  ? -12.268 14.416  6.407   1.00 29.35 ? 13  ALA B O     1 
ATOM   3402 C  CB    . ALA B 1 34  ? -10.533 13.539  8.312   1.00 29.44 ? 13  ALA B CB    1 
ATOM   3403 N  N     . GLY B 1 35  ? -12.830 12.343  5.623   1.00 29.22 ? 14  GLY B N     1 
ATOM   3404 C  CA    . GLY B 1 35  ? -13.903 12.749  4.697   1.00 28.84 ? 14  GLY B CA    1 
ATOM   3405 C  C     . GLY B 1 35  ? -15.218 12.716  5.455   1.00 28.94 ? 14  GLY B C     1 
ATOM   3406 O  O     . GLY B 1 35  ? -15.165 12.418  6.658   1.00 29.14 ? 14  GLY B O     1 
ATOM   3407 N  N     . PHE B 1 36  ? -16.347 12.942  4.784   1.00 27.77 ? 15  PHE B N     1 
ATOM   3408 C  CA    . PHE B 1 36  ? -17.694 12.966  5.413   1.00 31.28 ? 15  PHE B CA    1 
ATOM   3409 C  C     . PHE B 1 36  ? -18.106 11.587  5.938   1.00 32.39 ? 15  PHE B C     1 
ATOM   3410 O  O     . PHE B 1 36  ? -18.858 11.586  6.901   1.00 29.40 ? 15  PHE B O     1 
ATOM   3411 C  CB    . PHE B 1 36  ? -18.771 13.443  4.444   1.00 29.61 ? 15  PHE B CB    1 
ATOM   3412 C  CG    . PHE B 1 36  ? -18.887 14.942  4.357   1.00 30.09 ? 15  PHE B CG    1 
ATOM   3413 C  CD1   . PHE B 1 36  ? -19.702 15.639  5.232   1.00 27.83 ? 15  PHE B CD1   1 
ATOM   3414 C  CD2   . PHE B 1 36  ? -18.224 15.641  3.366   1.00 27.67 ? 15  PHE B CD2   1 
ATOM   3415 C  CE1   . PHE B 1 36  ? -19.835 17.010  5.128   1.00 26.20 ? 15  PHE B CE1   1 
ATOM   3416 C  CE2   . PHE B 1 36  ? -18.338 17.011  3.285   1.00 28.54 ? 15  PHE B CE2   1 
ATOM   3417 C  CZ    . PHE B 1 36  ? -19.138 17.695  4.168   1.00 27.14 ? 15  PHE B CZ    1 
ATOM   3418 N  N     . ALA B 1 37  ? -17.678 10.483  5.302   1.00 38.72 ? 16  ALA B N     1 
ATOM   3419 C  CA    . ALA B 1 37  ? -17.926 9.088   5.761   1.00 38.03 ? 16  ALA B CA    1 
ATOM   3420 C  C     . ALA B 1 37  ? -17.120 8.838   7.049   1.00 40.96 ? 16  ALA B C     1 
ATOM   3421 O  O     . ALA B 1 37  ? -17.744 8.426   8.072   1.00 38.99 ? 16  ALA B O     1 
ATOM   3422 C  CB    . ALA B 1 37  ? -17.571 8.086   4.681   1.00 34.93 ? 16  ALA B CB    1 
ATOM   3423 N  N     . GLY B 1 38  ? -15.801 9.112   7.024   1.00 39.94 ? 17  GLY B N     1 
ATOM   3424 C  CA    . GLY B 1 38  ? -14.902 8.943   8.189   1.00 38.29 ? 17  GLY B CA    1 
ATOM   3425 C  C     . GLY B 1 38  ? -15.333 9.792   9.384   1.00 39.48 ? 17  GLY B C     1 
ATOM   3426 O  O     . GLY B 1 38  ? -15.269 9.320   10.546  1.00 33.75 ? 17  GLY B O     1 
ATOM   3427 N  N     . LEU B 1 39  ? -15.761 11.030  9.138   1.00 38.59 ? 18  LEU B N     1 
ATOM   3428 C  CA    . LEU B 1 39  ? -16.089 11.961  10.243  1.00 39.25 ? 18  LEU B CA    1 
ATOM   3429 C  C     . LEU B 1 39  ? -17.486 11.597  10.759  1.00 36.07 ? 18  LEU B C     1 
ATOM   3430 O  O     . LEU B 1 39  ? -17.684 11.610  11.979  1.00 30.53 ? 18  LEU B O     1 
ATOM   3431 C  CB    . LEU B 1 39  ? -15.983 13.411  9.755   1.00 41.46 ? 18  LEU B CB    1 
ATOM   3432 C  CG    . LEU B 1 39  ? -14.567 13.925  9.465   1.00 40.89 ? 18  LEU B CG    1 
ATOM   3433 C  CD1   . LEU B 1 39  ? -14.631 15.245  8.702   1.00 44.23 ? 18  LEU B CD1   1 
ATOM   3434 C  CD2   . LEU B 1 39  ? -13.730 14.075  10.727  1.00 38.59 ? 18  LEU B CD2   1 
ATOM   3435 N  N     . THR B 1 40  ? -18.396 11.211  9.865   1.00 34.14 ? 19  THR B N     1 
ATOM   3436 C  CA    . THR B 1 40  ? -19.800 10.905  10.231  1.00 34.87 ? 19  THR B CA    1 
ATOM   3437 C  C     . THR B 1 40  ? -19.781 9.713   11.191  1.00 33.76 ? 19  THR B C     1 
ATOM   3438 O  O     . THR B 1 40  ? -20.584 9.713   12.156  1.00 36.21 ? 19  THR B O     1 
ATOM   3439 C  CB    . THR B 1 40  ? -20.705 10.640  9.016   1.00 31.79 ? 19  THR B CB    1 
ATOM   3440 O  OG1   . THR B 1 40  ? -20.768 11.798  8.180   1.00 30.28 ? 19  THR B OG1   1 
ATOM   3441 C  CG2   . THR B 1 40  ? -22.118 10.274  9.416   1.00 31.10 ? 19  THR B CG2   1 
ATOM   3442 N  N     . ALA B 1 41  ? -18.909 8.745   10.924  1.00 32.94 ? 20  ALA B N     1 
ATOM   3443 C  CA    . ALA B 1 41  ? -18.766 7.514   11.729  1.00 32.00 ? 20  ALA B CA    1 
ATOM   3444 C  C     . ALA B 1 41  ? -18.072 7.896   13.043  1.00 32.49 ? 20  ALA B C     1 
ATOM   3445 O  O     . ALA B 1 41  ? -18.544 7.456   14.102  1.00 32.58 ? 20  ALA B O     1 
ATOM   3446 C  CB    . ALA B 1 41  ? -17.997 6.463   10.969  1.00 29.53 ? 20  ALA B CB    1 
ATOM   3447 N  N     . ALA B 1 42  ? -16.996 8.685   12.975  1.00 33.07 ? 21  ALA B N     1 
ATOM   3448 C  CA    . ALA B 1 42  ? -16.231 9.145   14.158  1.00 34.49 ? 21  ALA B CA    1 
ATOM   3449 C  C     . ALA B 1 42  ? -17.197 9.874   15.105  1.00 37.87 ? 21  ALA B C     1 
ATOM   3450 O  O     . ALA B 1 42  ? -17.150 9.636   16.354  1.00 32.89 ? 21  ALA B O     1 
ATOM   3451 C  CB    . ALA B 1 42  ? -15.076 10.020  13.720  1.00 34.26 ? 21  ALA B CB    1 
ATOM   3452 N  N     . ARG B 1 43  ? -18.097 10.680  14.524  1.00 35.57 ? 22  ARG B N     1 
ATOM   3453 C  CA    . ARG B 1 43  ? -19.138 11.383  15.313  1.00 37.77 ? 22  ARG B CA    1 
ATOM   3454 C  C     . ARG B 1 43  ? -20.021 10.366  16.040  1.00 36.20 ? 22  ARG B C     1 
ATOM   3455 O  O     . ARG B 1 43  ? -20.225 10.565  17.243  1.00 36.74 ? 22  ARG B O     1 
ATOM   3456 C  CB    . ARG B 1 43  ? -20.056 12.284  14.490  1.00 37.39 ? 22  ARG B CB    1 
ATOM   3457 C  CG    . ARG B 1 43  ? -20.763 13.315  15.351  1.00 40.50 ? 22  ARG B CG    1 
ATOM   3458 C  CD    . ARG B 1 43  ? -22.083 13.788  14.783  1.00 46.70 ? 22  ARG B CD    1 
ATOM   3459 N  NE    . ARG B 1 43  ? -22.356 15.134  15.282  1.00 51.03 ? 22  ARG B NE    1 
ATOM   3460 C  CZ    . ARG B 1 43  ? -23.241 15.998  14.776  1.00 53.30 ? 22  ARG B CZ    1 
ATOM   3461 N  NH1   . ARG B 1 43  ? -24.000 15.676  13.735  1.00 52.47 ? 22  ARG B NH1   1 
ATOM   3462 N  NH2   . ARG B 1 43  ? -23.358 17.191  15.334  1.00 56.38 ? 22  ARG B NH2   1 
ATOM   3463 N  N     . ALA B 1 44  ? -20.607 9.394   15.335  1.00 33.21 ? 23  ALA B N     1 
ATOM   3464 C  CA    . ALA B 1 44  ? -21.660 8.519   15.910  1.00 36.04 ? 23  ALA B CA    1 
ATOM   3465 C  C     . ALA B 1 44  ? -21.024 7.545   16.918  1.00 32.51 ? 23  ALA B C     1 
ATOM   3466 O  O     . ALA B 1 44  ? -21.773 7.062   17.788  1.00 33.82 ? 23  ALA B O     1 
ATOM   3467 C  CB    . ALA B 1 44  ? -22.442 7.812   14.818  1.00 36.17 ? 23  ALA B CB    1 
ATOM   3468 N  N     . VAL B 1 45  ? -19.695 7.339   16.851  1.00 35.15 ? 24  VAL B N     1 
ATOM   3469 C  CA    . VAL B 1 45  ? -18.883 6.555   17.848  1.00 36.25 ? 24  VAL B CA    1 
ATOM   3470 C  C     . VAL B 1 45  ? -18.684 7.369   19.134  1.00 37.88 ? 24  VAL B C     1 
ATOM   3471 O  O     . VAL B 1 45  ? -18.922 6.798   20.231  1.00 35.59 ? 24  VAL B O     1 
ATOM   3472 C  CB    . VAL B 1 45  ? -17.531 6.092   17.277  1.00 37.51 ? 24  VAL B CB    1 
ATOM   3473 C  CG1   . VAL B 1 45  ? -16.503 5.789   18.376  1.00 37.03 ? 24  VAL B CG1   1 
ATOM   3474 C  CG2   . VAL B 1 45  ? -17.723 4.906   16.333  1.00 36.31 ? 24  VAL B CG2   1 
ATOM   3475 N  N     . HIS B 1 46  ? -18.256 8.626   19.028  1.00 37.42 ? 25  HIS B N     1 
ATOM   3476 C  CA    . HIS B 1 46  ? -18.119 9.540   20.198  1.00 42.92 ? 25  HIS B CA    1 
ATOM   3477 C  C     . HIS B 1 46  ? -19.483 9.741   20.900  1.00 38.71 ? 25  HIS B C     1 
ATOM   3478 O  O     . HIS B 1 46  ? -19.584 9.490   22.117  1.00 37.63 ? 25  HIS B O     1 
ATOM   3479 C  CB    . HIS B 1 46  ? -17.468 10.858  19.766  1.00 46.06 ? 25  HIS B CB    1 
ATOM   3480 C  CG    . HIS B 1 46  ? -17.555 11.874  20.849  1.00 51.61 ? 25  HIS B CG    1 
ATOM   3481 N  ND1   . HIS B 1 46  ? -17.023 11.642  22.103  1.00 57.77 ? 25  HIS B ND1   1 
ATOM   3482 C  CD2   . HIS B 1 46  ? -18.176 13.070  20.905  1.00 52.69 ? 25  HIS B CD2   1 
ATOM   3483 C  CE1   . HIS B 1 46  ? -17.286 12.675  22.878  1.00 60.57 ? 25  HIS B CE1   1 
ATOM   3484 N  NE2   . HIS B 1 46  ? -17.986 13.569  22.163  1.00 55.29 ? 25  HIS B NE2   1 
ATOM   3485 N  N     . GLU B 1 47  ? -20.524 10.121  20.155  1.00 42.52 ? 26  GLU B N     1 
ATOM   3486 C  CA    . GLU B 1 47  ? -21.923 10.294  20.658  1.00 42.32 ? 26  GLU B CA    1 
ATOM   3487 C  C     . GLU B 1 47  ? -22.449 9.066   21.433  1.00 41.77 ? 26  GLU B C     1 
ATOM   3488 O  O     . GLU B 1 47  ? -23.385 9.269   22.244  1.00 36.83 ? 26  GLU B O     1 
ATOM   3489 C  CB    . GLU B 1 47  ? -22.880 10.596  19.506  1.00 39.57 ? 26  GLU B CB    1 
ATOM   3490 C  CG    . GLU B 1 47  ? -23.009 12.080  19.225  1.00 42.18 ? 26  GLU B CG    1 
ATOM   3491 C  CD    . GLU B 1 47  ? -24.096 12.428  18.229  1.00 42.67 ? 26  GLU B CD    1 
ATOM   3492 O  OE1   . GLU B 1 47  ? -24.986 11.571  17.996  1.00 47.38 ? 26  GLU B OE1   1 
ATOM   3493 O  OE2   . GLU B 1 47  ? -24.049 13.548  17.680  1.00 41.00 ? 26  GLU B OE2   1 
ATOM   3494 N  N     . ALA B 1 48  ? -21.929 7.855   21.156  1.00 40.89 ? 27  ALA B N     1 
ATOM   3495 C  CA    . ALA B 1 48  ? -22.300 6.565   21.794  1.00 41.48 ? 27  ALA B CA    1 
ATOM   3496 C  C     . ALA B 1 48  ? -21.430 6.344   23.038  1.00 42.18 ? 27  ALA B C     1 
ATOM   3497 O  O     . ALA B 1 48  ? -21.630 5.319   23.755  1.00 47.08 ? 27  ALA B O     1 
ATOM   3498 C  CB    . ALA B 1 48  ? -22.133 5.421   20.818  1.00 42.02 ? 27  ALA B CB    1 
ATOM   3499 N  N     . GLY B 1 49  ? -20.479 7.248   23.271  1.00 35.57 ? 28  GLY B N     1 
ATOM   3500 C  CA    . GLY B 1 49  ? -19.683 7.284   24.505  1.00 36.21 ? 28  GLY B CA    1 
ATOM   3501 C  C     . GLY B 1 49  ? -18.426 6.457   24.396  1.00 35.56 ? 28  GLY B C     1 
ATOM   3502 O  O     . GLY B 1 49  ? -17.833 6.212   25.434  1.00 33.23 ? 28  GLY B O     1 
ATOM   3503 N  N     . ARG B 1 50  ? -18.027 6.061   23.179  1.00 38.09 ? 29  ARG B N     1 
ATOM   3504 C  CA    . ARG B 1 50  ? -16.732 5.366   22.913  1.00 39.25 ? 29  ARG B CA    1 
ATOM   3505 C  C     . ARG B 1 50  ? -15.672 6.362   22.412  1.00 35.13 ? 29  ARG B C     1 
ATOM   3506 O  O     . ARG B 1 50  ? -16.022 7.246   21.608  1.00 31.55 ? 29  ARG B O     1 
ATOM   3507 C  CB    . ARG B 1 50  ? -16.904 4.239   21.887  1.00 39.88 ? 29  ARG B CB    1 
ATOM   3508 C  CG    . ARG B 1 50  ? -17.887 3.160   22.309  1.00 42.12 ? 29  ARG B CG    1 
ATOM   3509 C  CD    . ARG B 1 50  ? -17.354 2.204   23.365  1.00 41.78 ? 29  ARG B CD    1 
ATOM   3510 N  NE    . ARG B 1 50  ? -18.213 1.037   23.497  1.00 41.78 ? 29  ARG B NE    1 
ATOM   3511 C  CZ    . ARG B 1 50  ? -18.013 0.032   24.334  1.00 40.17 ? 29  ARG B CZ    1 
ATOM   3512 N  NH1   . ARG B 1 50  ? -16.973 0.041   25.148  1.00 41.90 ? 29  ARG B NH1   1 
ATOM   3513 N  NH2   . ARG B 1 50  ? -18.865 -0.979  24.358  1.00 41.35 ? 29  ARG B NH2   1 
ATOM   3514 N  N     . SER B 1 51  ? -14.418 6.154   22.837  1.00 32.66 ? 30  SER B N     1 
ATOM   3515 C  CA    . SER B 1 51  ? -13.210 6.887   22.390  1.00 32.85 ? 30  SER B CA    1 
ATOM   3516 C  C     . SER B 1 51  ? -12.884 6.552   20.913  1.00 33.83 ? 30  SER B C     1 
ATOM   3517 O  O     . SER B 1 51  ? -13.070 5.384   20.487  1.00 33.31 ? 30  SER B O     1 
ATOM   3518 C  CB    . SER B 1 51  ? -12.044 6.622   23.322  1.00 31.12 ? 30  SER B CB    1 
ATOM   3519 O  OG    . SER B 1 51  ? -11.883 5.232   23.586  1.00 33.49 ? 30  SER B OG    1 
ATOM   3520 N  N     . VAL B 1 52  ? -12.418 7.558   20.160  1.00 33.45 ? 31  VAL B N     1 
ATOM   3521 C  CA    . VAL B 1 52  ? -12.133 7.510   18.695  1.00 37.24 ? 31  VAL B CA    1 
ATOM   3522 C  C     . VAL B 1 52  ? -10.900 8.369   18.386  1.00 37.53 ? 31  VAL B C     1 
ATOM   3523 O  O     . VAL B 1 52  ? -10.725 9.426   19.030  1.00 40.53 ? 31  VAL B O     1 
ATOM   3524 C  CB    . VAL B 1 52  ? -13.360 7.970   17.878  1.00 38.62 ? 31  VAL B CB    1 
ATOM   3525 C  CG1   . VAL B 1 52  ? -13.636 9.463   18.056  1.00 37.62 ? 31  VAL B CG1   1 
ATOM   3526 C  CG2   . VAL B 1 52  ? -13.228 7.614   16.403  1.00 35.43 ? 31  VAL B CG2   1 
ATOM   3527 N  N     . LEU B 1 53  ? -10.064 7.917   17.455  1.00 39.41 ? 32  LEU B N     1 
ATOM   3528 C  CA    . LEU B 1 53  ? -9.003  8.738   16.804  1.00 44.27 ? 32  LEU B CA    1 
ATOM   3529 C  C     . LEU B 1 53  ? -9.192  8.628   15.283  1.00 41.61 ? 32  LEU B C     1 
ATOM   3530 O  O     . LEU B 1 53  ? -9.267  7.481   14.764  1.00 39.82 ? 32  LEU B O     1 
ATOM   3531 C  CB    . LEU B 1 53  ? -7.592  8.268   17.188  1.00 46.72 ? 32  LEU B CB    1 
ATOM   3532 C  CG    . LEU B 1 53  ? -7.197  8.338   18.661  1.00 51.29 ? 32  LEU B CG    1 
ATOM   3533 C  CD1   . LEU B 1 53  ? -5.684  8.209   18.782  1.00 54.74 ? 32  LEU B CD1   1 
ATOM   3534 C  CD2   . LEU B 1 53  ? -7.658  9.629   19.339  1.00 55.37 ? 32  LEU B CD2   1 
ATOM   3535 N  N     . VAL B 1 54  ? -9.299  9.774   14.610  1.00 39.33 ? 33  VAL B N     1 
ATOM   3536 C  CA    . VAL B 1 54  ? -9.453  9.877   13.135  1.00 36.57 ? 33  VAL B CA    1 
ATOM   3537 C  C     . VAL B 1 54  ? -8.059  10.212  12.635  1.00 38.27 ? 33  VAL B C     1 
ATOM   3538 O  O     . VAL B 1 54  ? -7.471  11.163  13.214  1.00 36.49 ? 33  VAL B O     1 
ATOM   3539 C  CB    . VAL B 1 54  ? -10.502 10.930  12.743  1.00 37.53 ? 33  VAL B CB    1 
ATOM   3540 C  CG1   . VAL B 1 54  ? -10.666 11.079  11.228  1.00 36.30 ? 33  VAL B CG1   1 
ATOM   3541 C  CG2   . VAL B 1 54  ? -11.842 10.646  13.415  1.00 37.79 ? 33  VAL B CG2   1 
ATOM   3542 N  N     . LEU B 1 55  ? -7.519  9.377   11.729  1.00 35.90 ? 34  LEU B N     1 
ATOM   3543 C  CA    . LEU B 1 55  ? -6.184  9.582   11.091  1.00 35.37 ? 34  LEU B CA    1 
ATOM   3544 C  C     . LEU B 1 55  ? -6.378  9.964   9.615   1.00 32.76 ? 34  LEU B C     1 
ATOM   3545 O  O     . LEU B 1 55  ? -7.001  9.182   8.856   1.00 32.77 ? 34  LEU B O     1 
ATOM   3546 C  CB    . LEU B 1 55  ? -5.307  8.334   11.254  1.00 33.27 ? 34  LEU B CB    1 
ATOM   3547 C  CG    . LEU B 1 55  ? -5.097  7.837   12.686  1.00 34.96 ? 34  LEU B CG    1 
ATOM   3548 C  CD1   . LEU B 1 55  ? -4.027  6.759   12.715  1.00 35.14 ? 34  LEU B CD1   1 
ATOM   3549 C  CD2   . LEU B 1 55  ? -4.719  8.968   13.649  1.00 36.92 ? 34  LEU B CD2   1 
ATOM   3550 N  N     . GLU B 1 56  ? -5.830  11.122  9.237   1.00 30.79 ? 35  GLU B N     1 
ATOM   3551 C  CA    . GLU B 1 56  ? -6.035  11.785  7.926   1.00 30.80 ? 35  GLU B CA    1 
ATOM   3552 C  C     . GLU B 1 56  ? -4.666  12.189  7.389   1.00 31.93 ? 35  GLU B C     1 
ATOM   3553 O  O     . GLU B 1 56  ? -3.973  12.926  8.076   1.00 30.35 ? 35  GLU B O     1 
ATOM   3554 C  CB    . GLU B 1 56  ? -7.030  12.941  8.080   1.00 30.33 ? 35  GLU B CB    1 
ATOM   3555 C  CG    . GLU B 1 56  ? -7.125  13.850  6.872   1.00 29.99 ? 35  GLU B CG    1 
ATOM   3556 C  CD    . GLU B 1 56  ? -7.589  13.225  5.567   1.00 27.75 ? 35  GLU B CD    1 
ATOM   3557 O  OE1   . GLU B 1 56  ? -6.835  13.292  4.586   1.00 23.92 ? 35  GLU B OE1   1 
ATOM   3558 O  OE2   . GLU B 1 56  ? -8.724  12.675  5.538   1.00 31.57 ? 35  GLU B OE2   1 
ATOM   3559 N  N     . ALA B 1 57  ? -4.327  11.686  6.194   1.00 33.39 ? 36  ALA B N     1 
ATOM   3560 C  CA    . ALA B 1 57  ? -3.032  11.831  5.492   1.00 33.10 ? 36  ALA B CA    1 
ATOM   3561 C  C     . ALA B 1 57  ? -2.758  13.287  5.097   1.00 30.77 ? 36  ALA B C     1 
ATOM   3562 O  O     . ALA B 1 57  ? -1.579  13.641  5.023   1.00 33.25 ? 36  ALA B O     1 
ATOM   3563 C  CB    . ALA B 1 57  ? -3.053  10.953  4.258   1.00 35.33 ? 36  ALA B CB    1 
ATOM   3564 N  N     . ARG B 1 58  ? -3.802  14.044  4.751   1.00 31.03 ? 37  ARG B N     1 
ATOM   3565 C  CA    . ARG B 1 58  ? -3.748  15.476  4.345   1.00 31.15 ? 37  ARG B CA    1 
ATOM   3566 C  C     . ARG B 1 58  ? -3.686  16.355  5.613   1.00 36.37 ? 37  ARG B C     1 
ATOM   3567 O  O     . ARG B 1 58  ? -4.018  15.833  6.735   1.00 37.80 ? 37  ARG B O     1 
ATOM   3568 C  CB    . ARG B 1 58  ? -5.002  15.876  3.556   1.00 30.60 ? 37  ARG B CB    1 
ATOM   3569 C  CG    . ARG B 1 58  ? -5.141  15.297  2.145   1.00 30.87 ? 37  ARG B CG    1 
ATOM   3570 C  CD    . ARG B 1 58  ? -6.323  15.952  1.442   1.00 29.00 ? 37  ARG B CD    1 
ATOM   3571 N  NE    . ARG B 1 58  ? -6.440  15.656  0.016   1.00 30.25 ? 37  ARG B NE    1 
ATOM   3572 C  CZ    . ARG B 1 58  ? -7.061  14.599  -0.507  1.00 29.44 ? 37  ARG B CZ    1 
ATOM   3573 N  NH1   . ARG B 1 58  ? -7.638  13.702  0.283   1.00 29.52 ? 37  ARG B NH1   1 
ATOM   3574 N  NH2   . ARG B 1 58  ? -7.107  14.451  -1.822  1.00 29.12 ? 37  ARG B NH2   1 
ATOM   3575 N  N     . ASP B 1 59  ? -3.320  17.636  5.444   1.00 30.92 ? 38  ASP B N     1 
ATOM   3576 C  CA    . ASP B 1 59  ? -3.275  18.675  6.512   1.00 31.54 ? 38  ASP B CA    1 
ATOM   3577 C  C     . ASP B 1 59  ? -4.661  19.321  6.644   1.00 28.63 ? 38  ASP B C     1 
ATOM   3578 O  O     . ASP B 1 59  ? -4.746  20.425  7.127   1.00 28.72 ? 38  ASP B O     1 
ATOM   3579 C  CB    . ASP B 1 59  ? -2.143  19.676  6.267   1.00 31.09 ? 38  ASP B CB    1 
ATOM   3580 C  CG    . ASP B 1 59  ? -2.016  20.229  4.847   1.00 36.80 ? 38  ASP B CG    1 
ATOM   3581 O  OD1   . ASP B 1 59  ? -3.042  20.699  4.268   1.00 33.82 ? 38  ASP B OD1   1 
ATOM   3582 O  OD2   . ASP B 1 59  ? -0.873  20.206  4.317   1.00 48.83 ? 38  ASP B OD2   1 
ATOM   3583 N  N     . ARG B 1 60  ? -5.727  18.604  6.294   1.00 29.73 ? 39  ARG B N     1 
ATOM   3584 C  CA    . ARG B 1 60  ? -7.110  19.144  6.254   1.00 29.06 ? 39  ARG B CA    1 
ATOM   3585 C  C     . ARG B 1 60  ? -8.112  17.994  6.208   1.00 28.62 ? 39  ARG B C     1 
ATOM   3586 O  O     . ARG B 1 60  ? -7.727  16.851  5.943   1.00 32.72 ? 39  ARG B O     1 
ATOM   3587 C  CB    . ARG B 1 60  ? -7.305  20.021  5.003   1.00 30.79 ? 39  ARG B CB    1 
ATOM   3588 C  CG    . ARG B 1 60  ? -7.110  19.279  3.684   1.00 31.26 ? 39  ARG B CG    1 
ATOM   3589 C  CD    . ARG B 1 60  ? -7.583  20.035  2.466   1.00 32.35 ? 39  ARG B CD    1 
ATOM   3590 N  NE    . ARG B 1 60  ? -7.700  19.157  1.321   1.00 34.96 ? 39  ARG B NE    1 
ATOM   3591 C  CZ    . ARG B 1 60  ? -8.826  18.579  0.883   1.00 42.25 ? 39  ARG B CZ    1 
ATOM   3592 N  NH1   . ARG B 1 60  ? -9.989  18.770  1.499   1.00 41.35 ? 39  ARG B NH1   1 
ATOM   3593 N  NH2   . ARG B 1 60  ? -8.776  17.791  -0.187  1.00 41.77 ? 39  ARG B NH2   1 
ATOM   3594 N  N     . VAL B 1 61  ? -9.377  18.345  6.294   1.00 28.66 ? 40  VAL B N     1 
ATOM   3595 C  CA    . VAL B 1 61  ? -10.536 17.425  6.255   1.00 28.96 ? 40  VAL B CA    1 
ATOM   3596 C  C     . VAL B 1 61  ? -11.325 17.777  5.001   1.00 29.71 ? 40  VAL B C     1 
ATOM   3597 O  O     . VAL B 1 61  ? -10.977 18.779  4.357   1.00 34.35 ? 40  VAL B O     1 
ATOM   3598 C  CB    . VAL B 1 61  ? -11.326 17.591  7.567   1.00 30.08 ? 40  VAL B CB    1 
ATOM   3599 C  CG1   . VAL B 1 61  ? -10.374 17.523  8.757   1.00 28.25 ? 40  VAL B CG1   1 
ATOM   3600 C  CG2   . VAL B 1 61  ? -12.151 18.874  7.586   1.00 29.14 ? 40  VAL B CG2   1 
ATOM   3601 N  N     . GLY B 1 62  ? -12.336 16.980  4.665   1.00 31.77 ? 41  GLY B N     1 
ATOM   3602 C  CA    . GLY B 1 62  ? -13.214 17.161  3.489   1.00 28.81 ? 41  GLY B CA    1 
ATOM   3603 C  C     . GLY B 1 62  ? -12.996 16.069  2.453   1.00 26.91 ? 41  GLY B C     1 
ATOM   3604 O  O     . GLY B 1 62  ? -13.987 15.600  1.878   1.00 31.20 ? 41  GLY B O     1 
ATOM   3605 N  N     . GLY B 1 63  ? -11.751 15.676  2.231   1.00 26.68 ? 42  GLY B N     1 
ATOM   3606 C  CA    . GLY B 1 63  ? -11.391 14.621  1.255   1.00 28.99 ? 42  GLY B CA    1 
ATOM   3607 C  C     . GLY B 1 63  ? -11.671 15.039  -0.180  1.00 27.58 ? 42  GLY B C     1 
ATOM   3608 O  O     . GLY B 1 63  ? -11.112 16.046  -0.635  1.00 30.45 ? 42  GLY B O     1 
ATOM   3609 N  N     . ARG B 1 64  ? -12.543 14.311  -0.874  1.00 27.34 ? 43  ARG B N     1 
ATOM   3610 C  CA    . ARG B 1 64  ? -13.020 14.688  -2.228  1.00 27.81 ? 43  ARG B CA    1 
ATOM   3611 C  C     . ARG B 1 64  ? -13.874 15.975  -2.189  1.00 28.89 ? 43  ARG B C     1 
ATOM   3612 O  O     . ARG B 1 64  ? -14.435 16.348  -3.259  1.00 33.87 ? 43  ARG B O     1 
ATOM   3613 C  CB    . ARG B 1 64  ? -13.749 13.492  -2.845  1.00 26.75 ? 43  ARG B CB    1 
ATOM   3614 C  CG    . ARG B 1 64  ? -12.789 12.375  -3.210  1.00 25.64 ? 43  ARG B CG    1 
ATOM   3615 C  CD    . ARG B 1 64  ? -13.472 11.158  -3.785  1.00 25.11 ? 43  ARG B CD    1 
ATOM   3616 N  NE    . ARG B 1 64  ? -13.506 10.098  -2.789  1.00 25.02 ? 43  ARG B NE    1 
ATOM   3617 C  CZ    . ARG B 1 64  ? -14.166 8.955   -2.921  1.00 24.78 ? 43  ARG B CZ    1 
ATOM   3618 N  NH1   . ARG B 1 64  ? -14.820 8.694   -4.037  1.00 25.49 ? 43  ARG B NH1   1 
ATOM   3619 N  NH2   . ARG B 1 64  ? -14.160 8.070   -1.943  1.00 25.35 ? 43  ARG B NH2   1 
ATOM   3620 N  N     . THR B 1 65  ? -14.011 16.623  -1.023  1.00 29.49 ? 44  THR B N     1 
ATOM   3621 C  CA    . THR B 1 65  ? -14.572 17.994  -0.857  1.00 27.23 ? 44  THR B CA    1 
ATOM   3622 C  C     . THR B 1 65  ? -13.489 18.882  -0.266  1.00 25.27 ? 44  THR B C     1 
ATOM   3623 O  O     . THR B 1 65  ? -12.851 18.472  0.666   1.00 22.78 ? 44  THR B O     1 
ATOM   3624 C  CB    . THR B 1 65  ? -15.827 18.066  0.015   1.00 26.63 ? 44  THR B CB    1 
ATOM   3625 O  OG1   . THR B 1 65  ? -15.385 17.812  1.346   1.00 25.96 ? 44  THR B OG1   1 
ATOM   3626 C  CG2   . THR B 1 65  ? -16.918 17.109  -0.431  1.00 27.43 ? 44  THR B CG2   1 
ATOM   3627 N  N     . CYS B 1 66  ? -13.333 20.062  -0.856  1.00 29.41 ? 45  CYS B N     1 
ATOM   3628 C  CA    . CYS B 1 66  ? -12.141 20.935  -0.767  1.00 31.68 ? 45  CYS B CA    1 
ATOM   3629 C  C     . CYS B 1 66  ? -12.496 22.293  -1.376  1.00 37.07 ? 45  CYS B C     1 
ATOM   3630 O  O     . CYS B 1 66  ? -12.896 22.345  -2.577  1.00 37.03 ? 45  CYS B O     1 
ATOM   3631 C  CB    . CYS B 1 66  ? -10.964 20.294  -1.481  1.00 33.72 ? 45  CYS B CB    1 
ATOM   3632 S  SG    . CYS B 1 66  ? -9.544  21.393  -1.676  1.00 29.22 ? 45  CYS B SG    1 
ATOM   3633 N  N     . THR B 1 67  ? -12.425 23.332  -0.539  1.00 39.16 ? 46  THR B N     1 
ATOM   3634 C  CA    . THR B 1 67  ? -12.824 24.721  -0.851  1.00 40.39 ? 46  THR B CA    1 
ATOM   3635 C  C     . THR B 1 67  ? -11.637 25.629  -0.540  1.00 39.79 ? 46  THR B C     1 
ATOM   3636 O  O     . THR B 1 67  ? -11.036 25.443  0.538   1.00 51.12 ? 46  THR B O     1 
ATOM   3637 C  CB    . THR B 1 67  ? -14.053 25.120  -0.023  1.00 40.65 ? 46  THR B CB    1 
ATOM   3638 O  OG1   . THR B 1 67  ? -15.015 24.059  -0.073  1.00 34.53 ? 46  THR B OG1   1 
ATOM   3639 C  CG2   . THR B 1 67  ? -14.656 26.434  -0.488  1.00 38.11 ? 46  THR B CG2   1 
ATOM   3640 N  N     . GLU B 1 68  ? -11.296 26.546  -1.429  1.00 36.62 ? 47  GLU B N     1 
ATOM   3641 C  CA    . GLU B 1 68  ? -10.228 27.545  -1.166  1.00 38.95 ? 47  GLU B CA    1 
ATOM   3642 C  C     . GLU B 1 68  ? -10.769 28.960  -1.385  1.00 38.43 ? 47  GLU B C     1 
ATOM   3643 O  O     . GLU B 1 68  ? -11.741 29.106  -2.170  1.00 41.64 ? 47  GLU B O     1 
ATOM   3644 C  CB    . GLU B 1 68  ? -9.055  27.287  -2.095  1.00 38.19 ? 47  GLU B CB    1 
ATOM   3645 C  CG    . GLU B 1 68  ? -8.412  25.941  -1.894  1.00 39.39 ? 47  GLU B CG    1 
ATOM   3646 C  CD    . GLU B 1 68  ? -7.275  25.688  -2.876  1.00 39.13 ? 47  GLU B CD    1 
ATOM   3647 O  OE1   . GLU B 1 68  ? -6.510  24.741  -2.640  1.00 37.95 ? 47  GLU B OE1   1 
ATOM   3648 O  OE2   . GLU B 1 68  ? -7.151  26.458  -3.862  1.00 32.75 ? 47  GLU B OE2   1 
ATOM   3649 N  N     . GLU B 1 69  ? -10.162 29.950  -0.731  1.00 38.43 ? 48  GLU B N     1 
ATOM   3650 C  CA    . GLU B 1 69  ? -10.525 31.390  -0.863  1.00 41.77 ? 48  GLU B CA    1 
ATOM   3651 C  C     . GLU B 1 69  ? -9.667  31.974  -1.992  1.00 39.74 ? 48  GLU B C     1 
ATOM   3652 O  O     . GLU B 1 69  ? -8.427  31.883  -1.885  1.00 39.22 ? 48  GLU B O     1 
ATOM   3653 C  CB    . GLU B 1 69  ? -10.331 32.142  0.465   1.00 46.81 ? 48  GLU B CB    1 
ATOM   3654 C  CG    . GLU B 1 69  ? -10.710 33.622  0.423   1.00 50.31 ? 48  GLU B CG    1 
ATOM   3655 C  CD    . GLU B 1 69  ? -12.189 33.962  0.575   1.00 61.53 ? 48  GLU B CD    1 
ATOM   3656 O  OE1   . GLU B 1 69  ? -12.622 34.983  -0.025  1.00 60.09 ? 48  GLU B OE1   1 
ATOM   3657 O  OE2   . GLU B 1 69  ? -12.909 33.225  1.311   1.00 68.74 ? 48  GLU B OE2   1 
ATOM   3658 N  N     . HIS B 1 70  ? -10.335 32.509  -3.028  1.00 40.58 ? 49  HIS B N     1 
ATOM   3659 C  CA    . HIS B 1 70  ? -9.794  33.257  -4.201  1.00 39.81 ? 49  HIS B CA    1 
ATOM   3660 C  C     . HIS B 1 70  ? -10.773 34.385  -4.542  1.00 38.91 ? 49  HIS B C     1 
ATOM   3661 O  O     . HIS B 1 70  ? -12.009 34.165  -4.431  1.00 40.36 ? 49  HIS B O     1 
ATOM   3662 C  CB    . HIS B 1 70  ? -9.636  32.337  -5.435  1.00 40.61 ? 49  HIS B CB    1 
ATOM   3663 C  CG    . HIS B 1 70  ? -8.719  31.172  -5.227  1.00 42.47 ? 49  HIS B CG    1 
ATOM   3664 N  ND1   . HIS B 1 70  ? -7.358  31.235  -5.497  1.00 42.85 ? 49  HIS B ND1   1 
ATOM   3665 C  CD2   . HIS B 1 70  ? -8.952  29.923  -4.762  1.00 43.07 ? 49  HIS B CD2   1 
ATOM   3666 C  CE1   . HIS B 1 70  ? -6.789  30.083  -5.203  1.00 43.18 ? 49  HIS B CE1   1 
ATOM   3667 N  NE2   . HIS B 1 70  ? -7.747  29.253  -4.756  1.00 49.28 ? 49  HIS B NE2   1 
ATOM   3668 N  N     . HIS B 1 71  ? -10.266 35.542  -4.960  1.00 34.93 ? 50  HIS B N     1 
ATOM   3669 C  CA    . HIS B 1 71  ? -11.101 36.657  -5.482  1.00 33.57 ? 50  HIS B CA    1 
ATOM   3670 C  C     . HIS B 1 71  ? -12.297 36.925  -4.543  1.00 31.50 ? 50  HIS B C     1 
ATOM   3671 O  O     . HIS B 1 71  ? -13.420 37.202  -5.052  1.00 26.57 ? 50  HIS B O     1 
ATOM   3672 C  CB    . HIS B 1 71  ? -11.509 36.344  -6.930  1.00 34.78 ? 50  HIS B CB    1 
ATOM   3673 C  CG    . HIS B 1 71  ? -10.390 35.877  -7.804  1.00 35.09 ? 50  HIS B CG    1 
ATOM   3674 N  ND1   . HIS B 1 71  ? -9.340  36.700  -8.161  1.00 35.96 ? 50  HIS B ND1   1 
ATOM   3675 C  CD2   . HIS B 1 71  ? -10.136 34.674  -8.369  1.00 33.40 ? 50  HIS B CD2   1 
ATOM   3676 C  CE1   . HIS B 1 71  ? -8.486  36.028  -8.910  1.00 37.21 ? 50  HIS B CE1   1 
ATOM   3677 N  NE2   . HIS B 1 71  ? -8.952  34.784  -9.056  1.00 37.88 ? 50  HIS B NE2   1 
ATOM   3678 N  N     . GLY B 1 72  ? -12.071 36.832  -3.223  1.00 34.82 ? 51  GLY B N     1 
ATOM   3679 C  CA    . GLY B 1 72  ? -13.050 37.168  -2.158  1.00 41.14 ? 51  GLY B CA    1 
ATOM   3680 C  C     . GLY B 1 72  ? -14.332 36.323  -2.181  1.00 39.72 ? 51  GLY B C     1 
ATOM   3681 O  O     . GLY B 1 72  ? -15.396 36.819  -1.775  1.00 37.87 ? 51  GLY B O     1 
ATOM   3682 N  N     . THR B 1 73  ? -14.252 35.074  -2.639  1.00 42.04 ? 52  THR B N     1 
ATOM   3683 C  CA    . THR B 1 73  ? -15.378 34.105  -2.632  1.00 37.29 ? 52  THR B CA    1 
ATOM   3684 C  C     . THR B 1 73  ? -14.765 32.738  -2.340  1.00 35.86 ? 52  THR B C     1 
ATOM   3685 O  O     . THR B 1 73  ? -13.504 32.679  -2.171  1.00 36.09 ? 52  THR B O     1 
ATOM   3686 C  CB    . THR B 1 73  ? -16.183 34.227  -3.935  1.00 36.17 ? 52  THR B CB    1 
ATOM   3687 O  OG1   . THR B 1 73  ? -17.457 33.586  -3.838  1.00 28.92 ? 52  THR B OG1   1 
ATOM   3688 C  CG2   . THR B 1 73  ? -15.407 33.691  -5.119  1.00 38.11 ? 52  THR B CG2   1 
ATOM   3689 N  N     . TRP B 1 74  ? -15.612 31.705  -2.305  1.00 31.37 ? 53  TRP B N     1 
ATOM   3690 C  CA    . TRP B 1 74  ? -15.244 30.298  -1.983  1.00 30.85 ? 53  TRP B CA    1 
ATOM   3691 C  C     . TRP B 1 74  ? -15.045 29.460  -3.279  1.00 31.65 ? 53  TRP B C     1 
ATOM   3692 O  O     . TRP B 1 74  ? -15.944 29.450  -4.154  1.00 30.52 ? 53  TRP B O     1 
ATOM   3693 C  CB    . TRP B 1 74  ? -16.324 29.747  -1.028  1.00 28.84 ? 53  TRP B CB    1 
ATOM   3694 C  CG    . TRP B 1 74  ? -17.742 29.772  -1.529  1.00 25.04 ? 53  TRP B CG    1 
ATOM   3695 C  CD1   . TRP B 1 74  ? -18.351 28.836  -2.319  1.00 25.49 ? 53  TRP B CD1   1 
ATOM   3696 C  CD2   . TRP B 1 74  ? -18.765 30.742  -1.220  1.00 25.69 ? 53  TRP B CD2   1 
ATOM   3697 N  NE1   . TRP B 1 74  ? -19.665 29.168  -2.549  1.00 23.79 ? 53  TRP B NE1   1 
ATOM   3698 C  CE2   . TRP B 1 74  ? -19.949 30.336  -1.893  1.00 25.39 ? 53  TRP B CE2   1 
ATOM   3699 C  CE3   . TRP B 1 74  ? -18.792 31.933  -0.474  1.00 23.95 ? 53  TRP B CE3   1 
ATOM   3700 C  CZ2   . TRP B 1 74  ? -21.143 31.077  -1.824  1.00 26.88 ? 53  TRP B CZ2   1 
ATOM   3701 C  CZ3   . TRP B 1 74  ? -19.961 32.665  -0.410  1.00 23.66 ? 53  TRP B CZ3   1 
ATOM   3702 C  CH2   . TRP B 1 74  ? -21.124 32.245  -1.082  1.00 25.47 ? 53  TRP B CH2   1 
ATOM   3703 N  N     . ILE B 1 75  ? -13.895 28.803  -3.463  1.00 30.64 ? 54  ILE B N     1 
ATOM   3704 C  CA    . ILE B 1 75  ? -13.668 27.940  -4.671  1.00 31.26 ? 54  ILE B CA    1 
ATOM   3705 C  C     . ILE B 1 75  ? -13.688 26.449  -4.263  1.00 28.76 ? 54  ILE B C     1 
ATOM   3706 O  O     . ILE B 1 75  ? -12.630 25.900  -3.901  1.00 27.20 ? 54  ILE B O     1 
ATOM   3707 C  CB    . ILE B 1 75  ? -12.394 28.328  -5.466  1.00 27.91 ? 54  ILE B CB    1 
ATOM   3708 C  CG1   . ILE B 1 75  ? -12.356 29.801  -5.891  1.00 28.58 ? 54  ILE B CG1   1 
ATOM   3709 C  CG2   . ILE B 1 75  ? -12.241 27.446  -6.679  1.00 29.57 ? 54  ILE B CG2   1 
ATOM   3710 C  CD1   . ILE B 1 75  ? -13.353 30.172  -6.959  1.00 31.51 ? 54  ILE B CD1   1 
ATOM   3711 N  N     . ASP B 1 76  ? -14.855 25.813  -4.428  1.00 28.83 ? 55  ASP B N     1 
ATOM   3712 C  CA    . ASP B 1 76  ? -15.073 24.346  -4.318  1.00 29.89 ? 55  ASP B CA    1 
ATOM   3713 C  C     . ASP B 1 76  ? -14.309 23.605  -5.426  1.00 31.32 ? 55  ASP B C     1 
ATOM   3714 O  O     . ASP B 1 76  ? -14.861 23.441  -6.530  1.00 33.96 ? 55  ASP B O     1 
ATOM   3715 C  CB    . ASP B 1 76  ? -16.555 23.979  -4.425  1.00 31.29 ? 55  ASP B CB    1 
ATOM   3716 C  CG    . ASP B 1 76  ? -17.382 24.156  -3.155  1.00 32.05 ? 55  ASP B CG    1 
ATOM   3717 O  OD1   . ASP B 1 76  ? -16.853 23.878  -2.059  1.00 30.07 ? 55  ASP B OD1   1 
ATOM   3718 O  OD2   . ASP B 1 76  ? -18.569 24.530  -3.284  1.00 31.95 ? 55  ASP B OD2   1 
ATOM   3719 N  N     . LEU B 1 77  ? -13.120 23.103  -5.107  1.00 30.78 ? 56  LEU B N     1 
ATOM   3720 C  CA    . LEU B 1 77  ? -12.348 22.206  -5.987  1.00 30.57 ? 56  LEU B CA    1 
ATOM   3721 C  C     . LEU B 1 77  ? -12.965 20.811  -5.970  1.00 30.71 ? 56  LEU B C     1 
ATOM   3722 O  O     . LEU B 1 77  ? -12.797 20.101  -6.966  1.00 31.63 ? 56  LEU B O     1 
ATOM   3723 C  CB    . LEU B 1 77  ? -10.893 22.191  -5.525  1.00 30.93 ? 56  LEU B CB    1 
ATOM   3724 C  CG    . LEU B 1 77  ? -10.200 23.549  -5.571  1.00 34.70 ? 56  LEU B CG    1 
ATOM   3725 C  CD1   . LEU B 1 77  ? -8.761  23.433  -5.108  1.00 39.61 ? 56  LEU B CD1   1 
ATOM   3726 C  CD2   . LEU B 1 77  ? -10.265 24.133  -6.976  1.00 37.10 ? 56  LEU B CD2   1 
ATOM   3727 N  N     . GLY B 1 78  ? -13.614 20.433  -4.870  1.00 32.50 ? 57  GLY B N     1 
ATOM   3728 C  CA    . GLY B 1 78  ? -14.190 19.091  -4.659  1.00 30.37 ? 57  GLY B CA    1 
ATOM   3729 C  C     . GLY B 1 78  ? -15.681 19.106  -4.952  1.00 31.06 ? 57  GLY B C     1 
ATOM   3730 O  O     . GLY B 1 78  ? -16.134 20.055  -5.665  1.00 25.52 ? 57  GLY B O     1 
ATOM   3731 N  N     . GLY B 1 79  ? -16.420 18.123  -4.416  1.00 26.43 ? 58  GLY B N     1 
ATOM   3732 C  CA    . GLY B 1 79  ? -17.901 18.128  -4.430  1.00 26.29 ? 58  GLY B CA    1 
ATOM   3733 C  C     . GLY B 1 79  ? -18.472 19.456  -3.956  1.00 24.35 ? 58  GLY B C     1 
ATOM   3734 O  O     . GLY B 1 79  ? -17.781 20.138  -3.149  1.00 22.55 ? 58  GLY B O     1 
ATOM   3735 N  N     . GLN B 1 80  ? -19.654 19.832  -4.483  1.00 26.73 ? 59  GLN B N     1 
ATOM   3736 C  CA    . GLN B 1 80  ? -20.277 21.185  -4.304  1.00 30.08 ? 59  GLN B CA    1 
ATOM   3737 C  C     . GLN B 1 80  ? -21.834 21.148  -4.222  1.00 29.29 ? 59  GLN B C     1 
ATOM   3738 O  O     . GLN B 1 80  ? -22.381 22.032  -3.520  1.00 29.98 ? 59  GLN B O     1 
ATOM   3739 C  CB    . GLN B 1 80  ? -19.722 22.150  -5.382  1.00 28.66 ? 59  GLN B CB    1 
ATOM   3740 C  CG    . GLN B 1 80  ? -20.358 22.058  -6.770  1.00 27.90 ? 59  GLN B CG    1 
ATOM   3741 C  CD    . GLN B 1 80  ? -19.938 23.199  -7.687  1.00 29.11 ? 59  GLN B CD    1 
ATOM   3742 O  OE1   . GLN B 1 80  ? -18.843 23.755  -7.596  1.00 31.46 ? 59  GLN B OE1   1 
ATOM   3743 N  NE2   . GLN B 1 80  ? -20.816 23.578  -8.593  1.00 25.18 ? 59  GLN B NE2   1 
ATOM   3744 N  N     . TRP B 1 81  ? -22.528 20.235  -4.919  1.00 28.29 ? 60  TRP B N     1 
ATOM   3745 C  CA    . TRP B 1 81  ? -24.007 20.242  -5.149  1.00 30.21 ? 60  TRP B CA    1 
ATOM   3746 C  C     . TRP B 1 81  ? -24.756 19.260  -4.219  1.00 32.43 ? 60  TRP B C     1 
ATOM   3747 O  O     . TRP B 1 81  ? -24.257 18.097  -3.976  1.00 29.34 ? 60  TRP B O     1 
ATOM   3748 C  CB    . TRP B 1 81  ? -24.360 19.899  -6.604  1.00 31.41 ? 60  TRP B CB    1 
ATOM   3749 C  CG    . TRP B 1 81  ? -24.194 21.010  -7.590  1.00 34.75 ? 60  TRP B CG    1 
ATOM   3750 C  CD1   . TRP B 1 81  ? -24.725 22.267  -7.528  1.00 36.71 ? 60  TRP B CD1   1 
ATOM   3751 C  CD2   . TRP B 1 81  ? -23.487 20.934  -8.836  1.00 36.42 ? 60  TRP B CD2   1 
ATOM   3752 N  NE1   . TRP B 1 81  ? -24.389 22.982  -8.643  1.00 38.70 ? 60  TRP B NE1   1 
ATOM   3753 C  CE2   . TRP B 1 81  ? -23.625 22.192  -9.467  1.00 38.88 ? 60  TRP B CE2   1 
ATOM   3754 C  CE3   . TRP B 1 81  ? -22.778 19.924  -9.494  1.00 37.64 ? 60  TRP B CE3   1 
ATOM   3755 C  CZ2   . TRP B 1 81  ? -23.046 22.464  -10.711 1.00 36.90 ? 60  TRP B CZ2   1 
ATOM   3756 C  CZ3   . TRP B 1 81  ? -22.202 20.198  -10.716 1.00 36.02 ? 60  TRP B CZ3   1 
ATOM   3757 C  CH2   . TRP B 1 81  ? -22.335 21.450  -11.313 1.00 38.11 ? 60  TRP B CH2   1 
ATOM   3758 N  N     . ILE B 1 82  ? -25.950 19.680  -3.787  1.00 28.01 ? 61  ILE B N     1 
ATOM   3759 C  CA    . ILE B 1 82  ? -26.957 18.804  -3.120  1.00 31.91 ? 61  ILE B CA    1 
ATOM   3760 C  C     . ILE B 1 82  ? -28.343 19.069  -3.737  1.00 33.60 ? 61  ILE B C     1 
ATOM   3761 O  O     . ILE B 1 82  ? -28.578 20.095  -4.436  1.00 30.61 ? 61  ILE B O     1 
ATOM   3762 C  CB    . ILE B 1 82  ? -26.957 18.982  -1.592  1.00 30.68 ? 61  ILE B CB    1 
ATOM   3763 C  CG1   . ILE B 1 82  ? -27.323 20.413  -1.189  1.00 32.18 ? 61  ILE B CG1   1 
ATOM   3764 C  CG2   . ILE B 1 82  ? -25.631 18.553  -0.988  1.00 31.48 ? 61  ILE B CG2   1 
ATOM   3765 C  CD1   . ILE B 1 82  ? -27.894 20.541  0.215   1.00 33.12 ? 61  ILE B CD1   1 
ATOM   3766 N  N     . GLY B 1 83  ? -29.250 18.129  -3.537  1.00 37.81 ? 62  GLY B N     1 
ATOM   3767 C  CA    . GLY B 1 83  ? -30.561 18.189  -4.197  1.00 35.15 ? 62  GLY B CA    1 
ATOM   3768 C  C     . GLY B 1 83  ? -31.543 17.246  -3.536  1.00 32.54 ? 62  GLY B C     1 
ATOM   3769 O  O     . GLY B 1 83  ? -31.177 16.485  -2.633  1.00 24.26 ? 62  GLY B O     1 
ATOM   3770 N  N     . PRO B 1 84  ? -32.789 17.277  -4.056  1.00 34.50 ? 63  PRO B N     1 
ATOM   3771 C  CA    . PRO B 1 84  ? -33.901 16.500  -3.519  1.00 35.26 ? 63  PRO B CA    1 
ATOM   3772 C  C     . PRO B 1 84  ? -33.616 14.991  -3.436  1.00 38.11 ? 63  PRO B C     1 
ATOM   3773 O  O     . PRO B 1 84  ? -33.065 14.426  -4.411  1.00 37.40 ? 63  PRO B O     1 
ATOM   3774 C  CB    . PRO B 1 84  ? -35.062 16.727  -4.507  1.00 38.31 ? 63  PRO B CB    1 
ATOM   3775 C  CG    . PRO B 1 84  ? -34.670 17.936  -5.337  1.00 38.00 ? 63  PRO B CG    1 
ATOM   3776 C  CD    . PRO B 1 84  ? -33.163 18.062  -5.241  1.00 36.69 ? 63  PRO B CD    1 
ATOM   3777 N  N     . GLY B 1 85  ? -34.047 14.376  -2.321  1.00 35.11 ? 64  GLY B N     1 
ATOM   3778 C  CA    . GLY B 1 85  ? -33.797 12.964  -1.980  1.00 35.49 ? 64  GLY B CA    1 
ATOM   3779 C  C     . GLY B 1 85  ? -32.568 12.804  -1.097  1.00 36.02 ? 64  GLY B C     1 
ATOM   3780 O  O     . GLY B 1 85  ? -32.510 11.780  -0.401  1.00 38.53 ? 64  GLY B O     1 
ATOM   3781 N  N     . GLN B 1 86  ? -31.619 13.754  -1.145  1.00 33.52 ? 65  GLN B N     1 
ATOM   3782 C  CA    . GLN B 1 86  ? -30.342 13.707  -0.394  1.00 32.61 ? 65  GLN B CA    1 
ATOM   3783 C  C     . GLN B 1 86  ? -30.623 14.172  1.039   1.00 33.59 ? 65  GLN B C     1 
ATOM   3784 O  O     . GLN B 1 86  ? -30.193 15.283  1.433   1.00 32.02 ? 65  GLN B O     1 
ATOM   3785 C  CB    . GLN B 1 86  ? -29.279 14.572  -1.081  1.00 35.31 ? 65  GLN B CB    1 
ATOM   3786 C  CG    . GLN B 1 86  ? -28.574 13.872  -2.242  1.00 36.41 ? 65  GLN B CG    1 
ATOM   3787 C  CD    . GLN B 1 86  ? -27.570 14.735  -2.979  1.00 35.98 ? 65  GLN B CD    1 
ATOM   3788 O  OE1   . GLN B 1 86  ? -26.969 15.656  -2.430  1.00 35.38 ? 65  GLN B OE1   1 
ATOM   3789 N  NE2   . GLN B 1 86  ? -27.377 14.435  -4.259  1.00 35.08 ? 65  GLN B NE2   1 
ATOM   3790 N  N     . ASP B 1 87  ? -31.316 13.336  1.799   1.00 36.61 ? 66  ASP B N     1 
ATOM   3791 C  CA    . ASP B 1 87  ? -31.908 13.670  3.128   1.00 41.46 ? 66  ASP B CA    1 
ATOM   3792 C  C     . ASP B 1 87  ? -30.810 13.734  4.217   1.00 39.32 ? 66  ASP B C     1 
ATOM   3793 O  O     . ASP B 1 87  ? -30.962 14.525  5.164   1.00 34.73 ? 66  ASP B O     1 
ATOM   3794 C  CB    . ASP B 1 87  ? -33.069 12.707  3.436   1.00 40.84 ? 66  ASP B CB    1 
ATOM   3795 C  CG    . ASP B 1 87  ? -34.379 13.064  2.744   1.00 44.36 ? 66  ASP B CG    1 
ATOM   3796 O  OD1   . ASP B 1 87  ? -34.676 14.298  2.646   1.00 44.70 ? 66  ASP B OD1   1 
ATOM   3797 O  OD2   . ASP B 1 87  ? -35.098 12.120  2.302   1.00 42.96 ? 66  ASP B OD2   1 
ATOM   3798 N  N     . ARG B 1 88  ? -29.699 13.016  4.055   1.00 37.50 ? 67  ARG B N     1 
ATOM   3799 C  CA    . ARG B 1 88  ? -28.605 13.023  5.063   1.00 38.47 ? 67  ARG B CA    1 
ATOM   3800 C  C     . ARG B 1 88  ? -27.917 14.387  5.049   1.00 37.18 ? 67  ARG B C     1 
ATOM   3801 O  O     . ARG B 1 88  ? -28.016 15.085  6.060   1.00 37.37 ? 67  ARG B O     1 
ATOM   3802 C  CB    . ARG B 1 88  ? -27.605 11.884  4.828   1.00 39.96 ? 67  ARG B CB    1 
ATOM   3803 C  CG    . ARG B 1 88  ? -28.243 10.583  4.351   1.00 43.97 ? 67  ARG B CG    1 
ATOM   3804 C  CD    . ARG B 1 88  ? -27.942 9.378   5.230   1.00 45.47 ? 67  ARG B CD    1 
ATOM   3805 N  NE    . ARG B 1 88  ? -28.712 8.236   4.767   1.00 45.24 ? 67  ARG B NE    1 
ATOM   3806 C  CZ    . ARG B 1 88  ? -29.070 7.213   5.520   1.00 44.65 ? 67  ARG B CZ    1 
ATOM   3807 N  NH1   . ARG B 1 88  ? -28.736 7.175   6.800   1.00 43.72 ? 67  ARG B NH1   1 
ATOM   3808 N  NH2   . ARG B 1 88  ? -29.756 6.227   4.974   1.00 45.73 ? 67  ARG B NH2   1 
ATOM   3809 N  N     . VAL B 1 89  ? -27.260 14.748  3.936   1.00 37.82 ? 68  VAL B N     1 
ATOM   3810 C  CA    . VAL B 1 89  ? -26.444 15.998  3.798   1.00 36.45 ? 68  VAL B CA    1 
ATOM   3811 C  C     . VAL B 1 89  ? -27.353 17.213  4.070   1.00 33.07 ? 68  VAL B C     1 
ATOM   3812 O  O     . VAL B 1 89  ? -26.919 18.144  4.786   1.00 26.91 ? 68  VAL B O     1 
ATOM   3813 C  CB    . VAL B 1 89  ? -25.777 16.076  2.404   1.00 35.31 ? 68  VAL B CB    1 
ATOM   3814 C  CG1   . VAL B 1 89  ? -26.785 16.361  1.287   1.00 32.99 ? 68  VAL B CG1   1 
ATOM   3815 C  CG2   . VAL B 1 89  ? -24.619 17.073  2.363   1.00 33.55 ? 68  VAL B CG2   1 
ATOM   3816 N  N     . ALA B 1 90  ? -28.587 17.165  3.549   1.00 33.72 ? 69  ALA B N     1 
ATOM   3817 C  CA    . ALA B 1 90  ? -29.613 18.226  3.703   1.00 35.11 ? 69  ALA B CA    1 
ATOM   3818 C  C     . ALA B 1 90  ? -29.778 18.567  5.192   1.00 39.47 ? 69  ALA B C     1 
ATOM   3819 O  O     . ALA B 1 90  ? -29.644 19.774  5.528   1.00 41.16 ? 69  ALA B O     1 
ATOM   3820 C  CB    . ALA B 1 90  ? -30.902 17.807  3.053   1.00 29.84 ? 69  ALA B CB    1 
ATOM   3821 N  N     . ALA B 1 91  ? -29.930 17.532  6.043   1.00 45.00 ? 70  ALA B N     1 
ATOM   3822 C  CA    . ALA B 1 91  ? -30.149 17.616  7.512   1.00 42.77 ? 70  ALA B CA    1 
ATOM   3823 C  C     . ALA B 1 91  ? -28.835 17.893  8.255   1.00 40.96 ? 70  ALA B C     1 
ATOM   3824 O  O     . ALA B 1 91  ? -28.911 18.551  9.311   1.00 43.67 ? 70  ALA B O     1 
ATOM   3825 C  CB    . ALA B 1 91  ? -30.816 16.362  8.041   1.00 38.61 ? 70  ALA B CB    1 
ATOM   3826 N  N     . LEU B 1 92  ? -27.691 17.397  7.779   1.00 39.11 ? 71  LEU B N     1 
ATOM   3827 C  CA    . LEU B 1 92  ? -26.372 17.718  8.404   1.00 38.51 ? 71  LEU B CA    1 
ATOM   3828 C  C     . LEU B 1 92  ? -26.084 19.204  8.198   1.00 35.77 ? 71  LEU B C     1 
ATOM   3829 O  O     . LEU B 1 92  ? -25.490 19.813  9.116   1.00 34.16 ? 71  LEU B O     1 
ATOM   3830 C  CB    . LEU B 1 92  ? -25.234 16.894  7.788   1.00 39.45 ? 71  LEU B CB    1 
ATOM   3831 C  CG    . LEU B 1 92  ? -23.828 17.351  8.201   1.00 41.69 ? 71  LEU B CG    1 
ATOM   3832 C  CD1   . LEU B 1 92  ? -23.562 17.043  9.675   1.00 41.76 ? 71  LEU B CD1   1 
ATOM   3833 C  CD2   . LEU B 1 92  ? -22.754 16.728  7.329   1.00 38.92 ? 71  LEU B CD2   1 
ATOM   3834 N  N     . ALA B 1 93  ? -26.447 19.733  7.019   1.00 36.09 ? 72  ALA B N     1 
ATOM   3835 C  CA    . ALA B 1 93  ? -26.283 21.164  6.654   1.00 40.38 ? 72  ALA B CA    1 
ATOM   3836 C  C     . ALA B 1 93  ? -27.039 22.065  7.653   1.00 42.29 ? 72  ALA B C     1 
ATOM   3837 O  O     . ALA B 1 93  ? -26.352 22.860  8.353   1.00 46.53 ? 72  ALA B O     1 
ATOM   3838 C  CB    . ALA B 1 93  ? -26.734 21.394  5.235   1.00 42.72 ? 72  ALA B CB    1 
ATOM   3839 N  N     . ALA B 1 94  ? -28.375 21.909  7.727   1.00 37.18 ? 73  ALA B N     1 
ATOM   3840 C  CA    . ALA B 1 94  ? -29.352 22.634  8.579   1.00 35.28 ? 73  ALA B CA    1 
ATOM   3841 C  C     . ALA B 1 94  ? -28.984 22.565  10.064  1.00 36.03 ? 73  ALA B C     1 
ATOM   3842 O  O     . ALA B 1 94  ? -29.059 23.644  10.714  1.00 35.36 ? 73  ALA B O     1 
ATOM   3843 C  CB    . ALA B 1 94  ? -30.740 22.090  8.364   1.00 35.31 ? 73  ALA B CB    1 
ATOM   3844 N  N     . GLU B 1 95  ? -28.619 21.374  10.573  1.00 37.76 ? 74  GLU B N     1 
ATOM   3845 C  CA    . GLU B 1 95  ? -28.042 21.163  11.938  1.00 43.02 ? 74  GLU B CA    1 
ATOM   3846 C  C     . GLU B 1 95  ? -26.850 22.103  12.172  1.00 43.79 ? 74  GLU B C     1 
ATOM   3847 O  O     . GLU B 1 95  ? -26.879 22.907  13.114  1.00 43.95 ? 74  GLU B O     1 
ATOM   3848 C  CB    . GLU B 1 95  ? -27.569 19.720  12.181  1.00 44.50 ? 74  GLU B CB    1 
ATOM   3849 C  CG    . GLU B 1 95  ? -26.650 19.577  13.402  1.00 46.67 ? 74  GLU B CG    1 
ATOM   3850 C  CD    . GLU B 1 95  ? -26.176 18.176  13.794  1.00 49.57 ? 74  GLU B CD    1 
ATOM   3851 O  OE1   . GLU B 1 95  ? -25.909 17.971  15.014  1.00 40.43 ? 74  GLU B OE1   1 
ATOM   3852 O  OE2   . GLU B 1 95  ? -26.012 17.298  12.884  1.00 44.70 ? 74  GLU B OE2   1 
ATOM   3853 N  N     . LEU B 1 96  ? -25.794 21.977  11.383  1.00 48.07 ? 75  LEU B N     1 
ATOM   3854 C  CA    . LEU B 1 96  ? -24.532 22.696  11.681  1.00 50.70 ? 75  LEU B CA    1 
ATOM   3855 C  C     . LEU B 1 96  ? -24.641 24.128  11.133  1.00 49.90 ? 75  LEU B C     1 
ATOM   3856 O  O     . LEU B 1 96  ? -23.681 24.912  11.292  1.00 46.14 ? 75  LEU B O     1 
ATOM   3857 C  CB    . LEU B 1 96  ? -23.358 21.890  11.112  1.00 52.99 ? 75  LEU B CB    1 
ATOM   3858 C  CG    . LEU B 1 96  ? -23.111 20.536  11.787  1.00 57.81 ? 75  LEU B CG    1 
ATOM   3859 C  CD1   . LEU B 1 96  ? -21.908 19.822  11.175  1.00 58.66 ? 75  LEU B CD1   1 
ATOM   3860 C  CD2   . LEU B 1 96  ? -22.916 20.686  13.292  1.00 55.39 ? 75  LEU B CD2   1 
ATOM   3861 N  N     . GLY B 1 97  ? -25.797 24.467  10.550  1.00 53.87 ? 76  GLY B N     1 
ATOM   3862 C  CA    . GLY B 1 97  ? -26.151 25.836  10.119  1.00 54.32 ? 76  GLY B CA    1 
ATOM   3863 C  C     . GLY B 1 97  ? -25.300 26.335  8.955   1.00 50.45 ? 76  GLY B C     1 
ATOM   3864 O  O     . GLY B 1 97  ? -24.750 27.437  9.067   1.00 42.95 ? 76  GLY B O     1 
ATOM   3865 N  N     . VAL B 1 98  ? -25.179 25.558  7.875   1.00 43.85 ? 77  VAL B N     1 
ATOM   3866 C  CA    . VAL B 1 98  ? -24.690 26.090  6.571   1.00 41.18 ? 77  VAL B CA    1 
ATOM   3867 C  C     . VAL B 1 98  ? -25.918 26.301  5.680   1.00 40.62 ? 77  VAL B C     1 
ATOM   3868 O  O     . VAL B 1 98  ? -26.656 25.327  5.484   1.00 39.34 ? 77  VAL B O     1 
ATOM   3869 C  CB    . VAL B 1 98  ? -23.653 25.161  5.928   1.00 37.78 ? 77  VAL B CB    1 
ATOM   3870 C  CG1   . VAL B 1 98  ? -23.263 25.637  4.537   1.00 36.69 ? 77  VAL B CG1   1 
ATOM   3871 C  CG2   . VAL B 1 98  ? -22.420 24.994  6.818   1.00 37.55 ? 77  VAL B CG2   1 
ATOM   3872 N  N     . GLU B 1 99  ? -26.148 27.538  5.211   1.00 40.16 ? 78  GLU B N     1 
ATOM   3873 C  CA    . GLU B 1 99  ? -27.321 27.878  4.371   1.00 40.44 ? 78  GLU B CA    1 
ATOM   3874 C  C     . GLU B 1 99  ? -26.963 27.443  2.957   1.00 39.93 ? 78  GLU B C     1 
ATOM   3875 O  O     . GLU B 1 99  ? -25.759 27.329  2.661   1.00 39.92 ? 78  GLU B O     1 
ATOM   3876 C  CB    . GLU B 1 99  ? -27.723 29.356  4.472   1.00 45.18 ? 78  GLU B CB    1 
ATOM   3877 C  CG    . GLU B 1 99  ? -28.459 29.730  5.765   1.00 51.92 ? 78  GLU B CG    1 
ATOM   3878 C  CD    . GLU B 1 99  ? -29.960 29.413  5.859   1.00 59.47 ? 78  GLU B CD    1 
ATOM   3879 O  OE1   . GLU B 1 99  ? -30.403 28.387  5.285   1.00 57.87 ? 78  GLU B OE1   1 
ATOM   3880 O  OE2   . GLU B 1 99  ? -30.707 30.203  6.512   1.00 56.08 ? 78  GLU B OE2   1 
ATOM   3881 N  N     . THR B 1 100 ? -27.984 27.151  2.157   1.00 36.59 ? 79  THR B N     1 
ATOM   3882 C  CA    . THR B 1 100 ? -27.881 26.727  0.747   1.00 37.68 ? 79  THR B CA    1 
ATOM   3883 C  C     . THR B 1 100 ? -28.348 27.871  -0.169  1.00 36.95 ? 79  THR B C     1 
ATOM   3884 O  O     . THR B 1 100 ? -29.067 28.776  0.322   1.00 34.34 ? 79  THR B O     1 
ATOM   3885 C  CB    . THR B 1 100 ? -28.660 25.422  0.571   1.00 38.48 ? 79  THR B CB    1 
ATOM   3886 O  OG1   . THR B 1 100 ? -30.041 25.752  0.434   1.00 36.26 ? 79  THR B OG1   1 
ATOM   3887 C  CG2   . THR B 1 100 ? -28.436 24.467  1.729   1.00 38.19 ? 79  THR B CG2   1 
ATOM   3888 N  N     . TYR B 1 101 ? -27.937 27.833  -1.438  1.00 34.84 ? 80  TYR B N     1 
ATOM   3889 C  CA    . TYR B 1 101 ? -28.339 28.784  -2.512  1.00 34.04 ? 80  TYR B CA    1 
ATOM   3890 C  C     . TYR B 1 101 ? -28.631 27.991  -3.785  1.00 31.54 ? 80  TYR B C     1 
ATOM   3891 O  O     . TYR B 1 101 ? -28.077 26.920  -3.985  1.00 26.19 ? 80  TYR B O     1 
ATOM   3892 C  CB    . TYR B 1 101 ? -27.312 29.912  -2.661  1.00 32.50 ? 80  TYR B CB    1 
ATOM   3893 C  CG    . TYR B 1 101 ? -25.917 29.548  -3.106  1.00 37.49 ? 80  TYR B CG    1 
ATOM   3894 C  CD1   . TYR B 1 101 ? -24.992 29.029  -2.212  1.00 37.06 ? 80  TYR B CD1   1 
ATOM   3895 C  CD2   . TYR B 1 101 ? -25.484 29.810  -4.401  1.00 37.27 ? 80  TYR B CD2   1 
ATOM   3896 C  CE1   . TYR B 1 101 ? -23.697 28.727  -2.588  1.00 34.12 ? 80  TYR B CE1   1 
ATOM   3897 C  CE2   . TYR B 1 101 ? -24.187 29.511  -4.791  1.00 36.64 ? 80  TYR B CE2   1 
ATOM   3898 C  CZ    . TYR B 1 101 ? -23.292 28.968  -3.881  1.00 37.85 ? 80  TYR B CZ    1 
ATOM   3899 O  OH    . TYR B 1 101 ? -22.017 28.636  -4.241  1.00 39.58 ? 80  TYR B OH    1 
ATOM   3900 N  N     . PRO B 1 102 ? -29.606 28.411  -4.624  1.00 34.58 ? 81  PRO B N     1 
ATOM   3901 C  CA    . PRO B 1 102 ? -29.966 27.631  -5.811  1.00 36.58 ? 81  PRO B CA    1 
ATOM   3902 C  C     . PRO B 1 102 ? -28.898 27.746  -6.916  1.00 32.07 ? 81  PRO B C     1 
ATOM   3903 O  O     . PRO B 1 102 ? -28.423 28.800  -7.137  1.00 31.22 ? 81  PRO B O     1 
ATOM   3904 C  CB    . PRO B 1 102 ? -31.345 28.166  -6.270  1.00 36.47 ? 81  PRO B CB    1 
ATOM   3905 C  CG    . PRO B 1 102 ? -31.719 29.270  -5.265  1.00 37.63 ? 81  PRO B CG    1 
ATOM   3906 C  CD    . PRO B 1 102 ? -30.468 29.594  -4.459  1.00 37.21 ? 81  PRO B CD    1 
ATOM   3907 N  N     . GLN B 1 103 ? -28.526 26.630  -7.542  1.00 31.54 ? 82  GLN B N     1 
ATOM   3908 C  CA    . GLN B 1 103 ? -27.837 26.640  -8.853  1.00 34.23 ? 82  GLN B CA    1 
ATOM   3909 C  C     . GLN B 1 103 ? -28.719 27.431  -9.815  1.00 31.41 ? 82  GLN B C     1 
ATOM   3910 O  O     . GLN B 1 103 ? -29.905 27.146  -9.942  1.00 33.69 ? 82  GLN B O     1 
ATOM   3911 C  CB    . GLN B 1 103 ? -27.651 25.208  -9.377  1.00 35.66 ? 82  GLN B CB    1 
ATOM   3912 C  CG    . GLN B 1 103 ? -26.876 25.124  -10.685 1.00 36.92 ? 82  GLN B CG    1 
ATOM   3913 C  CD    . GLN B 1 103 ? -25.517 25.782  -10.631 1.00 34.48 ? 82  GLN B CD    1 
ATOM   3914 O  OE1   . GLN B 1 103 ? -24.688 25.505  -9.769  1.00 36.83 ? 82  GLN B OE1   1 
ATOM   3915 N  NE2   . GLN B 1 103 ? -25.286 26.700  -11.550 1.00 36.15 ? 82  GLN B NE2   1 
ATOM   3916 N  N     . PRO B 1 104 ? -28.205 28.466  -10.498 1.00 29.22 ? 83  PRO B N     1 
ATOM   3917 C  CA    . PRO B 1 104 ? -29.000 29.137  -11.517 1.00 30.00 ? 83  PRO B CA    1 
ATOM   3918 C  C     . PRO B 1 104 ? -29.392 28.158  -12.629 1.00 33.33 ? 83  PRO B C     1 
ATOM   3919 O  O     . PRO B 1 104 ? -28.552 27.308  -12.988 1.00 28.03 ? 83  PRO B O     1 
ATOM   3920 C  CB    . PRO B 1 104 ? -28.084 30.265  -11.989 1.00 28.68 ? 83  PRO B CB    1 
ATOM   3921 C  CG    . PRO B 1 104 ? -27.224 30.521  -10.760 1.00 30.83 ? 83  PRO B CG    1 
ATOM   3922 C  CD    . PRO B 1 104 ? -26.925 29.135  -10.229 1.00 29.18 ? 83  PRO B CD    1 
ATOM   3923 N  N     . THR B 1 105 ? -30.655 28.270  -13.070 1.00 36.12 ? 84  THR B N     1 
ATOM   3924 C  CA    . THR B 1 105 ? -31.310 27.466  -14.128 1.00 40.40 ? 84  THR B CA    1 
ATOM   3925 C  C     . THR B 1 105 ? -31.573 28.292  -15.392 1.00 45.44 ? 84  THR B C     1 
ATOM   3926 O  O     . THR B 1 105 ? -31.665 27.654  -16.474 1.00 47.78 ? 84  THR B O     1 
ATOM   3927 C  CB    . THR B 1 105 ? -32.672 26.935  -13.657 1.00 46.31 ? 84  THR B CB    1 
ATOM   3928 O  OG1   . THR B 1 105 ? -33.332 27.981  -12.936 1.00 40.61 ? 84  THR B OG1   1 
ATOM   3929 C  CG2   . THR B 1 105 ? -32.558 25.682  -12.809 1.00 46.39 ? 84  THR B CG2   1 
ATOM   3930 N  N     . GLU B 1 106 ? -31.721 29.626  -15.267 1.00 47.02 ? 85  GLU B N     1 
ATOM   3931 C  CA    . GLU B 1 106 ? -32.364 30.510  -16.289 1.00 45.78 ? 85  GLU B CA    1 
ATOM   3932 C  C     . GLU B 1 106 ? -31.353 31.005  -17.334 1.00 39.92 ? 85  GLU B C     1 
ATOM   3933 O  O     . GLU B 1 106 ? -30.165 31.143  -17.003 1.00 38.84 ? 85  GLU B O     1 
ATOM   3934 C  CB    . GLU B 1 106 ? -33.046 31.714  -15.622 1.00 49.25 ? 85  GLU B CB    1 
ATOM   3935 C  CG    . GLU B 1 106 ? -34.001 31.345  -14.485 1.00 51.59 ? 85  GLU B CG    1 
ATOM   3936 C  CD    . GLU B 1 106 ? -35.047 30.273  -14.795 1.00 52.70 ? 85  GLU B CD    1 
ATOM   3937 O  OE1   . GLU B 1 106 ? -35.052 29.220  -14.104 1.00 52.50 ? 85  GLU B OE1   1 
ATOM   3938 O  OE2   . GLU B 1 106 ? -35.863 30.484  -15.719 1.00 48.62 ? 85  GLU B OE2   1 
ATOM   3939 N  N     . GLY B 1 107 ? -31.867 31.334  -18.523 1.00 39.74 ? 86  GLY B N     1 
ATOM   3940 C  CA    . GLY B 1 107 ? -31.121 31.718  -19.736 1.00 42.37 ? 86  GLY B CA    1 
ATOM   3941 C  C     . GLY B 1 107 ? -31.027 30.550  -20.696 1.00 43.74 ? 86  GLY B C     1 
ATOM   3942 O  O     . GLY B 1 107 ? -31.310 29.432  -20.261 1.00 40.71 ? 86  GLY B O     1 
ATOM   3943 N  N     . ASP B 1 108 ? -30.651 30.788  -21.960 1.00 48.19 ? 87  ASP B N     1 
ATOM   3944 C  CA    . ASP B 1 108 ? -30.458 29.716  -22.983 1.00 43.21 ? 87  ASP B CA    1 
ATOM   3945 C  C     . ASP B 1 108 ? -29.265 28.814  -22.617 1.00 38.49 ? 87  ASP B C     1 
ATOM   3946 O  O     . ASP B 1 108 ? -28.210 29.327  -22.190 1.00 34.26 ? 87  ASP B O     1 
ATOM   3947 C  CB    . ASP B 1 108 ? -30.244 30.302  -24.374 1.00 43.40 ? 87  ASP B CB    1 
ATOM   3948 C  CG    . ASP B 1 108 ? -31.438 31.091  -24.860 1.00 47.68 ? 87  ASP B CG    1 
ATOM   3949 O  OD1   . ASP B 1 108 ? -32.535 30.891  -24.312 1.00 50.88 ? 87  ASP B OD1   1 
ATOM   3950 O  OD2   . ASP B 1 108 ? -31.246 31.911  -25.766 1.00 50.06 ? 87  ASP B OD2   1 
ATOM   3951 N  N     . ASP B 1 109 ? -29.435 27.500  -22.765 1.00 36.70 ? 88  ASP B N     1 
ATOM   3952 C  CA    . ASP B 1 109 ? -28.289 26.562  -22.809 1.00 37.74 ? 88  ASP B CA    1 
ATOM   3953 C  C     . ASP B 1 109 ? -27.754 26.580  -24.230 1.00 37.06 ? 88  ASP B C     1 
ATOM   3954 O  O     . ASP B 1 109 ? -28.542 26.931  -25.133 1.00 36.84 ? 88  ASP B O     1 
ATOM   3955 C  CB    . ASP B 1 109 ? -28.686 25.156  -22.391 1.00 39.30 ? 88  ASP B CB    1 
ATOM   3956 C  CG    . ASP B 1 109 ? -29.276 25.098  -21.002 1.00 37.09 ? 88  ASP B CG    1 
ATOM   3957 O  OD1   . ASP B 1 109 ? -28.808 25.862  -20.131 1.00 34.07 ? 88  ASP B OD1   1 
ATOM   3958 O  OD2   . ASP B 1 109 ? -30.221 24.320  -20.826 1.00 38.68 ? 88  ASP B OD2   1 
ATOM   3959 N  N     . VAL B 1 110 ? -26.470 26.240  -24.397 1.00 36.97 ? 89  VAL B N     1 
ATOM   3960 C  CA    . VAL B 1 110 ? -25.783 26.103  -25.717 1.00 32.60 ? 89  VAL B CA    1 
ATOM   3961 C  C     . VAL B 1 110 ? -25.394 24.634  -25.924 1.00 33.22 ? 89  VAL B C     1 
ATOM   3962 O  O     . VAL B 1 110 ? -24.493 24.139  -25.191 1.00 32.61 ? 89  VAL B O     1 
ATOM   3963 C  CB    . VAL B 1 110 ? -24.547 27.016  -25.809 1.00 30.90 ? 89  VAL B CB    1 
ATOM   3964 C  CG1   . VAL B 1 110 ? -23.875 26.904  -27.167 1.00 32.88 ? 89  VAL B CG1   1 
ATOM   3965 C  CG2   . VAL B 1 110 ? -24.884 28.457  -25.507 1.00 30.05 ? 89  VAL B CG2   1 
ATOM   3966 N  N     . VAL B 1 111 ? -26.008 23.970  -26.900 1.00 30.28 ? 90  VAL B N     1 
ATOM   3967 C  CA    . VAL B 1 111 ? -25.627 22.576  -27.283 1.00 34.21 ? 90  VAL B CA    1 
ATOM   3968 C  C     . VAL B 1 111 ? -24.825 22.590  -28.594 1.00 33.36 ? 90  VAL B C     1 
ATOM   3969 O  O     . VAL B 1 111 ? -25.170 23.386  -29.485 1.00 36.93 ? 90  VAL B O     1 
ATOM   3970 C  CB    . VAL B 1 111 ? -26.890 21.712  -27.389 1.00 32.02 ? 90  VAL B CB    1 
ATOM   3971 C  CG1   . VAL B 1 111 ? -26.589 20.313  -27.908 1.00 32.58 ? 90  VAL B CG1   1 
ATOM   3972 C  CG2   . VAL B 1 111 ? -27.601 21.668  -26.048 1.00 33.36 ? 90  VAL B CG2   1 
ATOM   3973 N  N     . LEU B 1 112 ? -23.837 21.705  -28.731 1.00 36.66 ? 91  LEU B N     1 
ATOM   3974 C  CA    . LEU B 1 112 ? -22.887 21.687  -29.886 1.00 38.19 ? 91  LEU B CA    1 
ATOM   3975 C  C     . LEU B 1 112 ? -22.415 20.268  -30.219 1.00 34.78 ? 91  LEU B C     1 
ATOM   3976 O  O     . LEU B 1 112 ? -21.638 19.719  -29.436 1.00 34.74 ? 91  LEU B O     1 
ATOM   3977 C  CB    . LEU B 1 112 ? -21.691 22.571  -29.534 1.00 37.26 ? 91  LEU B CB    1 
ATOM   3978 C  CG    . LEU B 1 112 ? -20.541 22.546  -30.537 1.00 41.20 ? 91  LEU B CG    1 
ATOM   3979 C  CD1   . LEU B 1 112 ? -21.005 22.951  -31.929 1.00 38.83 ? 91  LEU B CD1   1 
ATOM   3980 C  CD2   . LEU B 1 112 ? -19.419 23.461  -30.062 1.00 47.08 ? 91  LEU B CD2   1 
ATOM   3981 N  N     . PHE B 1 113 ? -22.838 19.722  -31.365 1.00 38.79 ? 92  PHE B N     1 
ATOM   3982 C  CA    . PHE B 1 113 ? -22.406 18.393  -31.879 1.00 40.41 ? 92  PHE B CA    1 
ATOM   3983 C  C     . PHE B 1 113 ? -21.378 18.606  -32.994 1.00 40.48 ? 92  PHE B C     1 
ATOM   3984 O  O     . PHE B 1 113 ? -21.692 19.295  -33.983 1.00 38.05 ? 92  PHE B O     1 
ATOM   3985 C  CB    . PHE B 1 113 ? -23.569 17.562  -32.429 1.00 45.99 ? 92  PHE B CB    1 
ATOM   3986 C  CG    . PHE B 1 113 ? -24.872 17.583  -31.667 1.00 53.53 ? 92  PHE B CG    1 
ATOM   3987 C  CD1   . PHE B 1 113 ? -25.915 18.417  -32.068 1.00 57.62 ? 92  PHE B CD1   1 
ATOM   3988 C  CD2   . PHE B 1 113 ? -25.092 16.719  -30.596 1.00 55.76 ? 92  PHE B CD2   1 
ATOM   3989 C  CE1   . PHE B 1 113 ? -27.134 18.406  -31.399 1.00 54.28 ? 92  PHE B CE1   1 
ATOM   3990 C  CE2   . PHE B 1 113 ? -26.304 16.720  -29.916 1.00 53.00 ? 92  PHE B CE2   1 
ATOM   3991 C  CZ    . PHE B 1 113 ? -27.321 17.562  -30.322 1.00 55.10 ? 92  PHE B CZ    1 
ATOM   3992 N  N     . GLY B 1 114 ? -20.165 18.086  -32.794 1.00 44.07 ? 93  GLY B N     1 
ATOM   3993 C  CA    . GLY B 1 114 ? -19.110 17.896  -33.820 1.00 46.27 ? 93  GLY B CA    1 
ATOM   3994 C  C     . GLY B 1 114 ? -18.737 19.161  -34.586 1.00 44.84 ? 93  GLY B C     1 
ATOM   3995 O  O     . GLY B 1 114 ? -18.151 20.086  -33.984 1.00 47.28 ? 93  GLY B O     1 
ATOM   3996 N  N     . ASP B 1 115 ? -19.078 19.178  -35.875 1.00 45.44 ? 94  ASP B N     1 
ATOM   3997 C  CA    . ASP B 1 115 ? -18.719 20.214  -36.883 1.00 44.26 ? 94  ASP B CA    1 
ATOM   3998 C  C     . ASP B 1 115 ? -19.835 21.264  -37.023 1.00 37.79 ? 94  ASP B C     1 
ATOM   3999 O  O     . ASP B 1 115 ? -19.675 22.159  -37.855 1.00 34.02 ? 94  ASP B O     1 
ATOM   4000 C  CB    . ASP B 1 115 ? -18.499 19.547  -38.250 1.00 46.53 ? 94  ASP B CB    1 
ATOM   4001 C  CG    . ASP B 1 115 ? -17.359 18.537  -38.280 1.00 46.63 ? 94  ASP B CG    1 
ATOM   4002 O  OD1   . ASP B 1 115 ? -16.194 18.974  -38.132 1.00 43.09 ? 94  ASP B OD1   1 
ATOM   4003 O  OD2   . ASP B 1 115 ? -17.648 17.319  -38.431 1.00 48.08 ? 94  ASP B OD2   1 
ATOM   4004 N  N     . GLY B 1 116 ? -20.931 21.138  -36.268 1.00 35.13 ? 95  GLY B N     1 
ATOM   4005 C  CA    . GLY B 1 116 ? -22.212 21.834  -36.519 1.00 32.06 ? 95  GLY B CA    1 
ATOM   4006 C  C     . GLY B 1 116 ? -22.282 23.183  -35.821 1.00 31.42 ? 95  GLY B C     1 
ATOM   4007 O  O     . GLY B 1 116 ? -21.268 23.599  -35.183 1.00 37.02 ? 95  GLY B O     1 
ATOM   4008 N  N     . GLU B 1 117 ? -23.408 23.874  -35.976 1.00 31.97 ? 96  GLU B N     1 
ATOM   4009 C  CA    . GLU B 1 117 ? -23.596 25.262  -35.492 1.00 35.03 ? 96  GLU B CA    1 
ATOM   4010 C  C     . GLU B 1 117 ? -24.086 25.123  -34.065 1.00 34.08 ? 96  GLU B C     1 
ATOM   4011 O  O     . GLU B 1 117 ? -24.940 24.275  -33.832 1.00 32.38 ? 96  GLU B O     1 
ATOM   4012 C  CB    . GLU B 1 117 ? -24.590 25.995  -36.393 1.00 39.48 ? 96  GLU B CB    1 
ATOM   4013 C  CG    . GLU B 1 117 ? -24.573 27.516  -36.284 1.00 41.88 ? 96  GLU B CG    1 
ATOM   4014 C  CD    . GLU B 1 117 ? -25.422 28.225  -37.346 1.00 43.44 ? 96  GLU B CD    1 
ATOM   4015 O  OE1   . GLU B 1 117 ? -26.177 27.542  -38.072 1.00 44.77 ? 96  GLU B OE1   1 
ATOM   4016 O  OE2   . GLU B 1 117 ? -25.362 29.457  -37.425 1.00 43.58 ? 96  GLU B OE2   1 
ATOM   4017 N  N     . PRO B 1 118 ? -23.508 25.859  -33.084 1.00 35.47 ? 97  PRO B N     1 
ATOM   4018 C  CA    . PRO B 1 118 ? -24.037 25.901  -31.721 1.00 34.37 ? 97  PRO B CA    1 
ATOM   4019 C  C     . PRO B 1 118 ? -25.515 26.298  -31.668 1.00 35.66 ? 97  PRO B C     1 
ATOM   4020 O  O     . PRO B 1 118 ? -25.815 27.317  -32.198 1.00 39.95 ? 97  PRO B O     1 
ATOM   4021 C  CB    . PRO B 1 118 ? -23.220 26.999  -31.038 1.00 34.78 ? 97  PRO B CB    1 
ATOM   4022 C  CG    . PRO B 1 118 ? -21.925 27.042  -31.820 1.00 34.96 ? 97  PRO B CG    1 
ATOM   4023 C  CD    . PRO B 1 118 ? -22.303 26.692  -33.240 1.00 36.24 ? 97  PRO B CD    1 
ATOM   4024 N  N     . GLN B 1 119 ? -26.359 25.505  -30.997 1.00 40.39 ? 98  GLN B N     1 
ATOM   4025 C  CA    . GLN B 1 119 ? -27.811 25.771  -30.785 1.00 42.42 ? 98  GLN B CA    1 
ATOM   4026 C  C     . GLN B 1 119 ? -28.055 26.341  -29.383 1.00 38.34 ? 98  GLN B C     1 
ATOM   4027 O  O     . GLN B 1 119 ? -27.698 25.658  -28.412 1.00 34.58 ? 98  GLN B O     1 
ATOM   4028 C  CB    . GLN B 1 119 ? -28.625 24.482  -30.953 1.00 49.19 ? 98  GLN B CB    1 
ATOM   4029 C  CG    . GLN B 1 119 ? -29.035 24.172  -32.393 1.00 52.74 ? 98  GLN B CG    1 
ATOM   4030 C  CD    . GLN B 1 119 ? -29.852 25.283  -33.007 1.00 62.26 ? 98  GLN B CD    1 
ATOM   4031 O  OE1   . GLN B 1 119 ? -30.391 26.149  -32.313 1.00 71.97 ? 98  GLN B OE1   1 
ATOM   4032 N  NE2   . GLN B 1 119 ? -29.926 25.288  -34.328 1.00 62.17 ? 98  GLN B NE2   1 
ATOM   4033 N  N     . ARG B 1 120 ? -28.647 27.541  -29.306 1.00 39.93 ? 99  ARG B N     1 
ATOM   4034 C  CA    . ARG B 1 120 ? -29.289 28.121  -28.088 1.00 42.55 ? 99  ARG B CA    1 
ATOM   4035 C  C     . ARG B 1 120 ? -30.695 27.540  -27.915 1.00 42.53 ? 99  ARG B C     1 
ATOM   4036 O  O     . ARG B 1 120 ? -31.440 27.502  -28.907 1.00 36.51 ? 99  ARG B O     1 
ATOM   4037 C  CB    . ARG B 1 120 ? -29.501 29.632  -28.187 1.00 41.09 ? 99  ARG B CB    1 
ATOM   4038 C  CG    . ARG B 1 120 ? -28.231 30.451  -28.064 1.00 45.28 ? 99  ARG B CG    1 
ATOM   4039 C  CD    . ARG B 1 120 ? -28.486 31.901  -28.401 1.00 44.15 ? 99  ARG B CD    1 
ATOM   4040 N  NE    . ARG B 1 120 ? -29.292 32.536  -27.370 1.00 42.69 ? 99  ARG B NE    1 
ATOM   4041 C  CZ    . ARG B 1 120 ? -28.963 33.643  -26.704 1.00 42.94 ? 99  ARG B CZ    1 
ATOM   4042 N  NH1   . ARG B 1 120 ? -27.836 34.290  -26.952 1.00 40.05 ? 99  ARG B NH1   1 
ATOM   4043 N  NH2   . ARG B 1 120 ? -29.793 34.116  -25.792 1.00 41.32 ? 99  ARG B NH2   1 
ATOM   4044 N  N     . ALA B 1 121 ? -31.043 27.135  -26.694 1.00 46.02 ? 100 ALA B N     1 
ATOM   4045 C  CA    . ALA B 1 121 ? -32.403 26.688  -26.310 1.00 50.36 ? 100 ALA B CA    1 
ATOM   4046 C  C     . ALA B 1 121 ? -32.588 26.999  -24.836 1.00 46.08 ? 100 ALA B C     1 
ATOM   4047 O  O     . ALA B 1 121 ? -31.609 26.999  -24.107 1.00 45.25 ? 100 ALA B O     1 
ATOM   4048 C  CB    . ALA B 1 121 ? -32.605 25.217  -26.598 1.00 52.02 ? 100 ALA B CB    1 
ATOM   4049 N  N     . PRO B 1 122 ? -33.809 27.376  -24.386 1.00 52.98 ? 101 PRO B N     1 
ATOM   4050 C  CA    . PRO B 1 122 ? -34.087 27.572  -22.956 1.00 51.52 ? 101 PRO B CA    1 
ATOM   4051 C  C     . PRO B 1 122 ? -33.770 26.370  -22.048 1.00 48.64 ? 101 PRO B C     1 
ATOM   4052 O  O     . PRO B 1 122 ? -33.510 26.583  -20.876 1.00 50.52 ? 101 PRO B O     1 
ATOM   4053 C  CB    . PRO B 1 122 ? -35.595 27.882  -22.929 1.00 53.40 ? 101 PRO B CB    1 
ATOM   4054 C  CG    . PRO B 1 122 ? -35.875 28.487  -24.297 1.00 55.57 ? 101 PRO B CG    1 
ATOM   4055 C  CD    . PRO B 1 122 ? -34.951 27.745  -25.243 1.00 51.55 ? 101 PRO B CD    1 
ATOM   4056 N  N     . ASP B 1 123 ? -33.828 25.147  -22.584 1.00 47.34 ? 102 ASP B N     1 
ATOM   4057 C  CA    . ASP B 1 123 ? -33.232 23.939  -21.951 1.00 51.25 ? 102 ASP B CA    1 
ATOM   4058 C  C     . ASP B 1 123 ? -32.658 23.012  -23.037 1.00 46.71 ? 102 ASP B C     1 
ATOM   4059 O  O     . ASP B 1 123 ? -33.182 22.987  -24.184 1.00 40.84 ? 102 ASP B O     1 
ATOM   4060 C  CB    . ASP B 1 123 ? -34.228 23.239  -21.019 1.00 56.60 ? 102 ASP B CB    1 
ATOM   4061 C  CG    . ASP B 1 123 ? -33.939 21.755  -20.813 1.00 64.68 ? 102 ASP B CG    1 
ATOM   4062 O  OD1   . ASP B 1 123 ? -33.033 21.423  -19.995 1.00 62.42 ? 102 ASP B OD1   1 
ATOM   4063 O  OD2   . ASP B 1 123 ? -34.596 20.932  -21.504 1.00 61.54 ? 102 ASP B OD2   1 
ATOM   4064 N  N     . VAL B 1 124 ? -31.613 22.266  -22.666 1.00 47.93 ? 103 VAL B N     1 
ATOM   4065 C  CA    . VAL B 1 124 ? -30.853 21.329  -23.549 1.00 46.87 ? 103 VAL B CA    1 
ATOM   4066 C  C     . VAL B 1 124 ? -31.849 20.535  -24.416 1.00 51.14 ? 103 VAL B C     1 
ATOM   4067 O  O     . VAL B 1 124 ? -31.668 20.487  -25.655 1.00 52.68 ? 103 VAL B O     1 
ATOM   4068 C  CB    . VAL B 1 124 ? -29.925 20.438  -22.693 1.00 43.49 ? 103 VAL B CB    1 
ATOM   4069 C  CG1   . VAL B 1 124 ? -29.371 19.226  -23.440 1.00 43.95 ? 103 VAL B CG1   1 
ATOM   4070 C  CG2   . VAL B 1 124 ? -28.777 21.245  -22.123 1.00 39.45 ? 103 VAL B CG2   1 
ATOM   4071 N  N     . ALA B 1 125 ? -32.895 19.980  -23.804 1.00 46.49 ? 104 ALA B N     1 
ATOM   4072 C  CA    . ALA B 1 125 ? -33.892 19.113  -24.470 1.00 46.59 ? 104 ALA B CA    1 
ATOM   4073 C  C     . ALA B 1 125 ? -34.424 19.787  -25.730 1.00 47.40 ? 104 ALA B C     1 
ATOM   4074 O  O     . ALA B 1 125 ? -34.631 19.071  -26.744 1.00 47.31 ? 104 ALA B O     1 
ATOM   4075 C  CB    . ALA B 1 125 ? -35.033 18.802  -23.533 1.00 47.71 ? 104 ALA B CB    1 
ATOM   4076 N  N     . LEU B 1 126 ? -34.686 21.095  -25.665 1.00 49.16 ? 105 LEU B N     1 
ATOM   4077 C  CA    . LEU B 1 126 ? -35.491 21.791  -26.706 1.00 53.09 ? 105 LEU B CA    1 
ATOM   4078 C  C     . LEU B 1 126 ? -34.627 21.979  -27.957 1.00 55.62 ? 105 LEU B C     1 
ATOM   4079 O  O     . LEU B 1 126 ? -35.180 22.343  -28.997 1.00 61.07 ? 105 LEU B O     1 
ATOM   4080 C  CB    . LEU B 1 126 ? -36.044 23.110  -26.147 1.00 58.62 ? 105 LEU B CB    1 
ATOM   4081 C  CG    . LEU B 1 126 ? -36.857 22.999  -24.847 1.00 59.50 ? 105 LEU B CG    1 
ATOM   4082 C  CD1   . LEU B 1 126 ? -37.430 24.347  -24.421 1.00 56.51 ? 105 LEU B CD1   1 
ATOM   4083 C  CD2   . LEU B 1 126 ? -37.975 21.970  -24.965 1.00 59.88 ? 105 LEU B CD2   1 
ATOM   4084 N  N     . ALA B 1 127 ? -33.327 21.671  -27.859 1.00 63.45 ? 106 ALA B N     1 
ATOM   4085 C  CA    . ALA B 1 127 ? -32.362 21.625  -28.984 1.00 57.58 ? 106 ALA B CA    1 
ATOM   4086 C  C     . ALA B 1 127 ? -32.417 20.278  -29.725 1.00 53.73 ? 106 ALA B C     1 
ATOM   4087 O  O     . ALA B 1 127 ? -31.637 20.109  -30.683 1.00 51.48 ? 106 ALA B O     1 
ATOM   4088 C  CB    . ALA B 1 127 ? -30.976 21.906  -28.455 1.00 59.32 ? 106 ALA B CB    1 
ATOM   4089 N  N     . PHE B 1 128 ? -33.284 19.346  -29.321 1.00 47.02 ? 107 PHE B N     1 
ATOM   4090 C  CA    . PHE B 1 128 ? -33.458 18.037  -30.001 1.00 50.32 ? 107 PHE B CA    1 
ATOM   4091 C  C     . PHE B 1 128 ? -34.820 17.990  -30.685 1.00 49.68 ? 107 PHE B C     1 
ATOM   4092 O  O     . PHE B 1 128 ? -35.736 18.671  -30.172 1.00 47.96 ? 107 PHE B O     1 
ATOM   4093 C  CB    . PHE B 1 128 ? -33.314 16.890  -28.999 1.00 56.22 ? 107 PHE B CB    1 
ATOM   4094 C  CG    . PHE B 1 128 ? -31.883 16.656  -28.596 1.00 58.20 ? 107 PHE B CG    1 
ATOM   4095 C  CD1   . PHE B 1 128 ? -31.172 15.589  -29.119 1.00 59.11 ? 107 PHE B CD1   1 
ATOM   4096 C  CD2   . PHE B 1 128 ? -31.230 17.541  -27.748 1.00 56.36 ? 107 PHE B CD2   1 
ATOM   4097 C  CE1   . PHE B 1 128 ? -29.848 15.388  -28.766 1.00 62.70 ? 107 PHE B CE1   1 
ATOM   4098 C  CE2   . PHE B 1 128 ? -29.904 17.340  -27.399 1.00 59.64 ? 107 PHE B CE2   1 
ATOM   4099 C  CZ    . PHE B 1 128 ? -29.214 16.266  -27.914 1.00 61.28 ? 107 PHE B CZ    1 
ATOM   4100 N  N     . SER B 1 129 ? -34.936 17.210  -31.771 1.00 47.28 ? 108 SER B N     1 
ATOM   4101 C  CA    . SER B 1 129 ? -36.211 16.942  -32.504 1.00 52.29 ? 108 SER B CA    1 
ATOM   4102 C  C     . SER B 1 129 ? -37.215 16.227  -31.583 1.00 57.35 ? 108 SER B C     1 
ATOM   4103 O  O     . SER B 1 129 ? -36.782 15.706  -30.520 1.00 63.15 ? 108 SER B O     1 
ATOM   4104 C  CB    . SER B 1 129 ? -35.982 16.158  -33.800 1.00 52.51 ? 108 SER B CB    1 
ATOM   4105 O  OG    . SER B 1 129 ? -35.132 15.028  -33.619 1.00 45.98 ? 108 SER B OG    1 
ATOM   4106 N  N     . ASP B 1 130 ? -38.505 16.226  -31.956 1.00 63.52 ? 109 ASP B N     1 
ATOM   4107 C  CA    . ASP B 1 130 ? -39.579 15.419  -31.308 1.00 59.63 ? 109 ASP B CA    1 
ATOM   4108 C  C     . ASP B 1 130 ? -39.081 13.970  -31.236 1.00 56.46 ? 109 ASP B C     1 
ATOM   4109 O  O     . ASP B 1 130 ? -39.089 13.397  -30.135 1.00 58.14 ? 109 ASP B O     1 
ATOM   4110 C  CB    . ASP B 1 130 ? -40.912 15.471  -32.073 1.00 62.70 ? 109 ASP B CB    1 
ATOM   4111 C  CG    . ASP B 1 130 ? -41.628 16.823  -32.105 1.00 70.90 ? 109 ASP B CG    1 
ATOM   4112 O  OD1   . ASP B 1 130 ? -41.259 17.720  -31.302 1.00 75.59 ? 109 ASP B OD1   1 
ATOM   4113 O  OD2   . ASP B 1 130 ? -42.565 16.981  -32.941 1.00 69.58 ? 109 ASP B OD2   1 
ATOM   4114 N  N     . GLU B 1 131 ? -38.614 13.444  -32.374 1.00 52.38 ? 110 GLU B N     1 
ATOM   4115 C  CA    . GLU B 1 131 ? -38.178 12.037  -32.577 1.00 52.36 ? 110 GLU B CA    1 
ATOM   4116 C  C     . GLU B 1 131 ? -36.988 11.703  -31.670 1.00 50.47 ? 110 GLU B C     1 
ATOM   4117 O  O     . GLU B 1 131 ? -36.990 10.594  -31.099 1.00 46.78 ? 110 GLU B O     1 
ATOM   4118 C  CB    . GLU B 1 131 ? -37.787 11.798  -34.033 1.00 54.47 ? 110 GLU B CB    1 
ATOM   4119 C  CG    . GLU B 1 131 ? -37.652 10.327  -34.385 1.00 63.26 ? 110 GLU B CG    1 
ATOM   4120 C  CD    . GLU B 1 131 ? -36.574 10.040  -35.416 1.00 66.78 ? 110 GLU B CD    1 
ATOM   4121 O  OE1   . GLU B 1 131 ? -36.503 10.798  -36.410 1.00 67.86 ? 110 GLU B OE1   1 
ATOM   4122 O  OE2   . GLU B 1 131 ? -35.796 9.079   -35.212 1.00 62.28 ? 110 GLU B OE2   1 
ATOM   4123 N  N     . GLU B 1 132 ? -36.011 12.611  -31.566 1.00 47.86 ? 111 GLU B N     1 
ATOM   4124 C  CA    . GLU B 1 132 ? -34.756 12.416  -30.783 1.00 47.11 ? 111 GLU B CA    1 
ATOM   4125 C  C     . GLU B 1 132 ? -35.081 12.316  -29.293 1.00 41.86 ? 111 GLU B C     1 
ATOM   4126 O  O     . GLU B 1 132 ? -34.562 11.378  -28.671 1.00 38.60 ? 111 GLU B O     1 
ATOM   4127 C  CB    . GLU B 1 132 ? -33.740 13.530  -31.050 1.00 47.47 ? 111 GLU B CB    1 
ATOM   4128 C  CG    . GLU B 1 132 ? -32.808 13.214  -32.212 1.00 46.78 ? 111 GLU B CG    1 
ATOM   4129 C  CD    . GLU B 1 132 ? -32.071 14.391  -32.825 1.00 49.43 ? 111 GLU B CD    1 
ATOM   4130 O  OE1   . GLU B 1 132 ? -31.168 14.127  -33.657 1.00 55.62 ? 111 GLU B OE1   1 
ATOM   4131 O  OE2   . GLU B 1 132 ? -32.391 15.560  -32.477 1.00 44.45 ? 111 GLU B OE2   1 
ATOM   4132 N  N     . LEU B 1 133 ? -35.914 13.225  -28.766 1.00 41.45 ? 112 LEU B N     1 
ATOM   4133 C  CA    . LEU B 1 133 ? -36.216 13.354  -27.311 1.00 42.66 ? 112 LEU B CA    1 
ATOM   4134 C  C     . LEU B 1 133 ? -37.011 12.129  -26.833 1.00 44.08 ? 112 LEU B C     1 
ATOM   4135 O  O     . LEU B 1 133 ? -36.756 11.657  -25.701 1.00 38.81 ? 112 LEU B O     1 
ATOM   4136 C  CB    . LEU B 1 133 ? -36.987 14.652  -27.050 1.00 47.32 ? 112 LEU B CB    1 
ATOM   4137 C  CG    . LEU B 1 133 ? -36.967 15.129  -25.593 1.00 50.07 ? 112 LEU B CG    1 
ATOM   4138 C  CD1   . LEU B 1 133 ? -35.625 15.787  -25.267 1.00 48.26 ? 112 LEU B CD1   1 
ATOM   4139 C  CD2   . LEU B 1 133 ? -38.119 16.084  -25.300 1.00 49.01 ? 112 LEU B CD2   1 
ATOM   4140 N  N     . THR B 1 134 ? -37.918 11.613  -27.673 1.00 48.26 ? 113 THR B N     1 
ATOM   4141 C  CA    . THR B 1 134 ? -38.628 10.311  -27.466 1.00 51.62 ? 113 THR B CA    1 
ATOM   4142 C  C     . THR B 1 134 ? -37.585 9.207   -27.215 1.00 48.77 ? 113 THR B C     1 
ATOM   4143 O  O     . THR B 1 134 ? -37.561 8.679   -26.075 1.00 48.13 ? 113 THR B O     1 
ATOM   4144 C  CB    . THR B 1 134 ? -39.568 9.978   -28.638 1.00 49.71 ? 113 THR B CB    1 
ATOM   4145 O  OG1   . THR B 1 134 ? -40.488 11.063  -28.757 1.00 49.69 ? 113 THR B OG1   1 
ATOM   4146 C  CG2   . THR B 1 134 ? -40.352 8.696   -28.457 1.00 48.05 ? 113 THR B CG2   1 
ATOM   4147 N  N     . ALA B 1 135 ? -36.753 8.914   -28.228 1.00 45.05 ? 114 ALA B N     1 
ATOM   4148 C  CA    . ALA B 1 135 ? -35.645 7.928   -28.211 1.00 43.17 ? 114 ALA B CA    1 
ATOM   4149 C  C     . ALA B 1 135 ? -34.789 8.132   -26.953 1.00 42.64 ? 114 ALA B C     1 
ATOM   4150 O  O     . ALA B 1 135 ? -34.482 7.117   -26.269 1.00 43.39 ? 114 ALA B O     1 
ATOM   4151 C  CB    . ALA B 1 135 ? -34.819 8.048   -29.473 1.00 42.07 ? 114 ALA B CB    1 
ATOM   4152 N  N     . TYR B 1 136 ? -34.440 9.381   -26.621 1.00 36.92 ? 115 TYR B N     1 
ATOM   4153 C  CA    . TYR B 1 136 ? -33.634 9.667   -25.414 1.00 35.43 ? 115 TYR B CA    1 
ATOM   4154 C  C     . TYR B 1 136 ? -34.413 9.211   -24.186 1.00 39.21 ? 115 TYR B C     1 
ATOM   4155 O  O     . TYR B 1 136 ? -33.833 8.546   -23.333 1.00 44.58 ? 115 TYR B O     1 
ATOM   4156 C  CB    . TYR B 1 136 ? -33.275 11.141  -25.243 1.00 37.38 ? 115 TYR B CB    1 
ATOM   4157 C  CG    . TYR B 1 136 ? -32.542 11.443  -23.948 1.00 39.46 ? 115 TYR B CG    1 
ATOM   4158 C  CD1   . TYR B 1 136 ? -33.232 11.771  -22.785 1.00 40.53 ? 115 TYR B CD1   1 
ATOM   4159 C  CD2   . TYR B 1 136 ? -31.158 11.388  -23.879 1.00 38.60 ? 115 TYR B CD2   1 
ATOM   4160 C  CE1   . TYR B 1 136 ? -32.572 12.052  -21.602 1.00 38.94 ? 115 TYR B CE1   1 
ATOM   4161 C  CE2   . TYR B 1 136 ? -30.482 11.659  -22.704 1.00 40.00 ? 115 TYR B CE2   1 
ATOM   4162 C  CZ    . TYR B 1 136 ? -31.191 11.995  -21.564 1.00 40.87 ? 115 TYR B CZ    1 
ATOM   4163 O  OH    . TYR B 1 136 ? -30.518 12.256  -20.405 1.00 42.78 ? 115 TYR B OH    1 
ATOM   4164 N  N     . LEU B 1 137 ? -35.687 9.572   -24.087 1.00 39.76 ? 116 LEU B N     1 
ATOM   4165 C  CA    . LEU B 1 137 ? -36.471 9.344   -22.846 1.00 37.49 ? 116 LEU B CA    1 
ATOM   4166 C  C     . LEU B 1 137 ? -36.734 7.848   -22.698 1.00 34.55 ? 116 LEU B C     1 
ATOM   4167 O  O     . LEU B 1 137 ? -36.626 7.323   -21.565 1.00 32.81 ? 116 LEU B O     1 
ATOM   4168 C  CB    . LEU B 1 137 ? -37.770 10.150  -22.931 1.00 41.19 ? 116 LEU B CB    1 
ATOM   4169 C  CG    . LEU B 1 137 ? -37.609 11.658  -22.750 1.00 39.94 ? 116 LEU B CG    1 
ATOM   4170 C  CD1   . LEU B 1 137 ? -38.842 12.388  -23.254 1.00 42.85 ? 116 LEU B CD1   1 
ATOM   4171 C  CD2   . LEU B 1 137 ? -37.318 12.002  -21.298 1.00 40.88 ? 116 LEU B CD2   1 
ATOM   4172 N  N     . GLU B 1 138 ? -37.046 7.182   -23.809 1.00 34.21 ? 117 GLU B N     1 
ATOM   4173 C  CA    . GLU B 1 138 ? -37.249 5.715   -23.839 1.00 35.86 ? 117 GLU B CA    1 
ATOM   4174 C  C     . GLU B 1 138 ? -35.915 5.040   -23.487 1.00 36.15 ? 117 GLU B C     1 
ATOM   4175 O  O     . GLU B 1 138 ? -35.972 4.008   -22.805 1.00 41.31 ? 117 GLU B O     1 
ATOM   4176 C  CB    . GLU B 1 138 ? -37.840 5.277   -25.183 1.00 39.03 ? 117 GLU B CB    1 
ATOM   4177 C  CG    . GLU B 1 138 ? -39.265 5.756   -25.406 1.00 41.90 ? 117 GLU B CG    1 
ATOM   4178 C  CD    . GLU B 1 138 ? -39.892 5.249   -26.696 1.00 51.71 ? 117 GLU B CD    1 
ATOM   4179 O  OE1   . GLU B 1 138 ? -41.163 5.245   -26.795 1.00 50.75 ? 117 GLU B OE1   1 
ATOM   4180 O  OE2   . GLU B 1 138 ? -39.107 4.873   -27.618 1.00 51.27 ? 117 GLU B OE2   1 
ATOM   4181 N  N     . LEU B 1 139 ? -34.764 5.620   -23.862 1.00 34.23 ? 118 LEU B N     1 
ATOM   4182 C  CA    . LEU B 1 139 ? -33.426 5.068   -23.489 1.00 33.49 ? 118 LEU B CA    1 
ATOM   4183 C  C     . LEU B 1 139 ? -33.239 5.089   -21.965 1.00 31.09 ? 118 LEU B C     1 
ATOM   4184 O  O     . LEU B 1 139 ? -32.877 4.033   -21.419 1.00 28.00 ? 118 LEU B O     1 
ATOM   4185 C  CB    . LEU B 1 139 ? -32.312 5.847   -24.193 1.00 36.77 ? 118 LEU B CB    1 
ATOM   4186 C  CG    . LEU B 1 139 ? -30.875 5.450   -23.827 1.00 36.53 ? 118 LEU B CG    1 
ATOM   4187 C  CD1   . LEU B 1 139 ? -30.638 3.958   -23.988 1.00 39.39 ? 118 LEU B CD1   1 
ATOM   4188 C  CD2   . LEU B 1 139 ? -29.892 6.204   -24.695 1.00 35.78 ? 118 LEU B CD2   1 
ATOM   4189 N  N     . ALA B 1 140 ? -33.526 6.221   -21.309 1.00 30.62 ? 119 ALA B N     1 
ATOM   4190 C  CA    . ALA B 1 140 ? -33.438 6.429   -19.837 1.00 30.32 ? 119 ALA B CA    1 
ATOM   4191 C  C     . ALA B 1 140 ? -34.498 5.574   -19.102 1.00 32.46 ? 119 ALA B C     1 
ATOM   4192 O  O     . ALA B 1 140 ? -34.182 4.953   -18.044 1.00 33.29 ? 119 ALA B O     1 
ATOM   4193 C  CB    . ALA B 1 140 ? -33.595 7.900   -19.524 1.00 28.12 ? 119 ALA B CB    1 
ATOM   4194 N  N     . GLY B 1 141 ? -35.718 5.518   -19.635 1.00 30.29 ? 120 GLY B N     1 
ATOM   4195 C  CA    . GLY B 1 141 ? -36.762 4.620   -19.127 1.00 29.12 ? 120 GLY B CA    1 
ATOM   4196 C  C     . GLY B 1 141 ? -36.276 3.184   -19.143 1.00 30.77 ? 120 GLY B C     1 
ATOM   4197 O  O     . GLY B 1 141 ? -36.344 2.514   -18.116 1.00 33.04 ? 120 GLY B O     1 
ATOM   4198 N  N     . ALA B 1 142 ? -35.752 2.725   -20.272 1.00 32.71 ? 121 ALA B N     1 
ATOM   4199 C  CA    . ALA B 1 142 ? -35.363 1.312   -20.476 1.00 31.35 ? 121 ALA B CA    1 
ATOM   4200 C  C     . ALA B 1 142 ? -34.207 0.945   -19.541 1.00 30.14 ? 121 ALA B C     1 
ATOM   4201 O  O     . ALA B 1 142 ? -34.173 -0.231  -19.122 1.00 36.00 ? 121 ALA B O     1 
ATOM   4202 C  CB    . ALA B 1 142 ? -35.049 1.059   -21.933 1.00 32.02 ? 121 ALA B CB    1 
ATOM   4203 N  N     . LEU B 1 143 ? -33.333 1.904   -19.204 1.00 29.49 ? 122 LEU B N     1 
ATOM   4204 C  CA    . LEU B 1 143 ? -32.238 1.734   -18.205 1.00 29.55 ? 122 LEU B CA    1 
ATOM   4205 C  C     . LEU B 1 143 ? -32.824 1.716   -16.798 1.00 30.88 ? 122 LEU B C     1 
ATOM   4206 O  O     . LEU B 1 143 ? -32.350 0.871   -16.001 1.00 33.59 ? 122 LEU B O     1 
ATOM   4207 C  CB    . LEU B 1 143 ? -31.179 2.843   -18.277 1.00 27.58 ? 122 LEU B CB    1 
ATOM   4208 C  CG    . LEU B 1 143 ? -30.050 2.699   -17.252 1.00 25.08 ? 122 LEU B CG    1 
ATOM   4209 C  CD1   . LEU B 1 143 ? -29.374 1.346   -17.407 1.00 22.69 ? 122 LEU B CD1   1 
ATOM   4210 C  CD2   . LEU B 1 143 ? -29.022 3.823   -17.361 1.00 23.20 ? 122 LEU B CD2   1 
ATOM   4211 N  N     . GLU B 1 144 ? -33.755 2.630   -16.504 1.00 34.02 ? 123 GLU B N     1 
ATOM   4212 C  CA    . GLU B 1 144 ? -34.420 2.761   -15.166 1.00 35.66 ? 123 GLU B CA    1 
ATOM   4213 C  C     . GLU B 1 144 ? -35.181 1.470   -14.822 1.00 35.15 ? 123 GLU B C     1 
ATOM   4214 O  O     . GLU B 1 144 ? -35.160 1.086   -13.661 1.00 32.20 ? 123 GLU B O     1 
ATOM   4215 C  CB    . GLU B 1 144 ? -35.365 3.964   -15.142 1.00 39.01 ? 123 GLU B CB    1 
ATOM   4216 C  CG    . GLU B 1 144 ? -34.696 5.287   -14.762 1.00 40.40 ? 123 GLU B CG    1 
ATOM   4217 C  CD    . GLU B 1 144 ? -35.591 6.518   -14.890 1.00 41.28 ? 123 GLU B CD    1 
ATOM   4218 O  OE1   . GLU B 1 144 ? -35.245 7.588   -14.301 1.00 40.83 ? 123 GLU B OE1   1 
ATOM   4219 O  OE2   . GLU B 1 144 ? -36.647 6.410   -15.569 1.00 38.83 ? 123 GLU B OE2   1 
ATOM   4220 N  N     . ALA B 1 145 ? -35.800 0.813   -15.815 1.00 35.96 ? 124 ALA B N     1 
ATOM   4221 C  CA    . ALA B 1 145 ? -36.518 -0.480  -15.674 1.00 37.20 ? 124 ALA B CA    1 
ATOM   4222 C  C     . ALA B 1 145 ? -35.529 -1.630  -15.407 1.00 37.42 ? 124 ALA B C     1 
ATOM   4223 O  O     . ALA B 1 145 ? -35.923 -2.613  -14.759 1.00 37.14 ? 124 ALA B O     1 
ATOM   4224 C  CB    . ALA B 1 145 ? -37.338 -0.749  -16.912 1.00 40.50 ? 124 ALA B CB    1 
ATOM   4225 N  N     . ILE B 1 146 ? -34.284 -1.534  -15.884 1.00 37.60 ? 125 ILE B N     1 
ATOM   4226 C  CA    . ILE B 1 146 ? -33.195 -2.459  -15.442 1.00 35.69 ? 125 ILE B CA    1 
ATOM   4227 C  C     . ILE B 1 146 ? -32.850 -2.141  -13.988 1.00 33.49 ? 125 ILE B C     1 
ATOM   4228 O  O     . ILE B 1 146 ? -32.868 -3.075  -13.172 1.00 33.38 ? 125 ILE B O     1 
ATOM   4229 C  CB    . ILE B 1 146 ? -31.963 -2.400  -16.360 1.00 38.03 ? 125 ILE B CB    1 
ATOM   4230 C  CG1   . ILE B 1 146 ? -32.270 -3.055  -17.709 1.00 42.38 ? 125 ILE B CG1   1 
ATOM   4231 C  CG2   . ILE B 1 146 ? -30.763 -3.048  -15.682 1.00 37.75 ? 125 ILE B CG2   1 
ATOM   4232 C  CD1   . ILE B 1 146 ? -31.639 -2.354  -18.889 1.00 47.98 ? 125 ILE B CD1   1 
ATOM   4233 N  N     . ALA B 1 147 ? -32.550 -0.870  -13.715 1.00 32.32 ? 126 ALA B N     1 
ATOM   4234 C  CA    . ALA B 1 147 ? -32.230 -0.299  -12.388 1.00 31.15 ? 126 ALA B CA    1 
ATOM   4235 C  C     . ALA B 1 147 ? -33.233 -0.777  -11.334 1.00 32.80 ? 126 ALA B C     1 
ATOM   4236 O  O     . ALA B 1 147 ? -32.769 -1.098  -10.227 1.00 34.81 ? 126 ALA B O     1 
ATOM   4237 C  CB    . ALA B 1 147 ? -32.215 1.211   -12.465 1.00 30.89 ? 126 ALA B CB    1 
ATOM   4238 N  N     . GLU B 1 148 ? -34.537 -0.841  -11.653 1.00 31.27 ? 127 GLU B N     1 
ATOM   4239 C  CA    . GLU B 1 148 ? -35.603 -1.116  -10.637 1.00 34.93 ? 127 GLU B CA    1 
ATOM   4240 C  C     . GLU B 1 148 ? -35.478 -2.556  -10.085 1.00 32.27 ? 127 GLU B C     1 
ATOM   4241 O  O     . GLU B 1 148 ? -35.793 -2.728  -8.908  1.00 34.77 ? 127 GLU B O     1 
ATOM   4242 C  CB    . GLU B 1 148 ? -36.999 -0.787  -11.192 1.00 37.12 ? 127 GLU B CB    1 
ATOM   4243 C  CG    . GLU B 1 148 ? -38.109 -0.703  -10.137 1.00 42.82 ? 127 GLU B CG    1 
ATOM   4244 C  CD    . GLU B 1 148 ? -37.748 -0.057  -8.799  1.00 49.45 ? 127 GLU B CD    1 
ATOM   4245 O  OE1   . GLU B 1 148 ? -38.014 -0.688  -7.739  1.00 51.16 ? 127 GLU B OE1   1 
ATOM   4246 O  OE2   . GLU B 1 148 ? -37.171 1.067   -8.806  1.00 51.55 ? 127 GLU B OE2   1 
ATOM   4247 N  N     . LYS B 1 149 ? -34.996 -3.538  -10.866 1.00 31.29 ? 128 LYS B N     1 
ATOM   4248 C  CA    . LYS B 1 149 ? -34.834 -4.959  -10.437 1.00 30.57 ? 128 LYS B CA    1 
ATOM   4249 C  C     . LYS B 1 149 ? -33.418 -5.209  -9.886  1.00 31.55 ? 128 LYS B C     1 
ATOM   4250 O  O     . LYS B 1 149 ? -33.061 -6.397  -9.713  1.00 32.95 ? 128 LYS B O     1 
ATOM   4251 C  CB    . LYS B 1 149 ? -35.150 -5.900  -11.600 1.00 31.98 ? 128 LYS B CB    1 
ATOM   4252 C  CG    . LYS B 1 149 ? -36.502 -5.669  -12.261 1.00 35.82 ? 128 LYS B CG    1 
ATOM   4253 C  CD    . LYS B 1 149 ? -36.751 -6.547  -13.481 1.00 40.45 ? 128 LYS B CD    1 
ATOM   4254 C  CE    . LYS B 1 149 ? -37.034 -7.999  -13.154 1.00 42.30 ? 128 LYS B CE    1 
ATOM   4255 N  NZ    . LYS B 1 149 ? -38.193 -8.499  -13.930 1.00 43.39 ? 128 LYS B NZ    1 
ATOM   4256 N  N     . VAL B 1 150 ? -32.647 -4.154  -9.570  1.00 27.75 ? 129 VAL B N     1 
ATOM   4257 C  CA    . VAL B 1 150 ? -31.231 -4.282  -9.115  1.00 27.59 ? 129 VAL B CA    1 
ATOM   4258 C  C     . VAL B 1 150 ? -31.207 -3.924  -7.639  1.00 25.79 ? 129 VAL B C     1 
ATOM   4259 O  O     . VAL B 1 150 ? -31.310 -2.760  -7.293  1.00 25.91 ? 129 VAL B O     1 
ATOM   4260 C  CB    . VAL B 1 150 ? -30.265 -3.411  -9.943  1.00 26.38 ? 129 VAL B CB    1 
ATOM   4261 C  CG1   . VAL B 1 150 ? -28.836 -3.443  -9.416  1.00 25.85 ? 129 VAL B CG1   1 
ATOM   4262 C  CG2   . VAL B 1 150 ? -30.308 -3.799  -11.404 1.00 25.48 ? 129 VAL B CG2   1 
ATOM   4263 N  N     . PRO B 1 151 ? -31.078 -4.915  -6.736  1.00 25.33 ? 130 PRO B N     1 
ATOM   4264 C  CA    . PRO B 1 151 ? -31.108 -4.642  -5.301  1.00 26.32 ? 130 PRO B CA    1 
ATOM   4265 C  C     . PRO B 1 151 ? -30.024 -3.644  -4.869  1.00 27.61 ? 130 PRO B C     1 
ATOM   4266 O  O     . PRO B 1 151 ? -28.869 -3.891  -5.156  1.00 29.52 ? 130 PRO B O     1 
ATOM   4267 C  CB    . PRO B 1 151 ? -30.856 -6.026  -4.683  1.00 26.75 ? 130 PRO B CB    1 
ATOM   4268 C  CG    . PRO B 1 151 ? -31.333 -7.004  -5.743  1.00 25.42 ? 130 PRO B CG    1 
ATOM   4269 C  CD    . PRO B 1 151 ? -30.905 -6.347  -7.037  1.00 25.59 ? 130 PRO B CD    1 
ATOM   4270 N  N     . LEU B 1 152 ? -30.410 -2.565  -4.180  1.00 27.51 ? 131 LEU B N     1 
ATOM   4271 C  CA    . LEU B 1 152 ? -29.479 -1.522  -3.687  1.00 29.96 ? 131 LEU B CA    1 
ATOM   4272 C  C     . LEU B 1 152 ? -28.455 -2.145  -2.740  1.00 29.59 ? 131 LEU B C     1 
ATOM   4273 O  O     . LEU B 1 152 ? -27.350 -1.610  -2.681  1.00 31.33 ? 131 LEU B O     1 
ATOM   4274 C  CB    . LEU B 1 152 ? -30.241 -0.366  -3.020  1.00 29.77 ? 131 LEU B CB    1 
ATOM   4275 C  CG    . LEU B 1 152 ? -31.193 0.442   -3.920  1.00 29.97 ? 131 LEU B CG    1 
ATOM   4276 C  CD1   . LEU B 1 152 ? -31.780 1.628   -3.155  1.00 28.25 ? 131 LEU B CD1   1 
ATOM   4277 C  CD2   . LEU B 1 152 ? -30.511 0.923   -5.211  1.00 28.64 ? 131 LEU B CD2   1 
ATOM   4278 N  N     . ASP B 1 153 ? -28.805 -3.214  -2.019  1.00 31.51 ? 132 ASP B N     1 
ATOM   4279 C  CA    . ASP B 1 153 ? -27.945 -3.792  -0.939  1.00 33.32 ? 132 ASP B CA    1 
ATOM   4280 C  C     . ASP B 1 153 ? -27.091 -4.946  -1.468  1.00 33.13 ? 132 ASP B C     1 
ATOM   4281 O  O     . ASP B 1 153 ? -26.195 -5.394  -0.736  1.00 37.08 ? 132 ASP B O     1 
ATOM   4282 C  CB    . ASP B 1 153 ? -28.752 -4.228  0.305   1.00 33.16 ? 132 ASP B CB    1 
ATOM   4283 C  CG    . ASP B 1 153 ? -29.914 -5.197  0.089   1.00 35.05 ? 132 ASP B CG    1 
ATOM   4284 O  OD1   . ASP B 1 153 ? -30.150 -5.634  -1.093  1.00 29.74 ? 132 ASP B OD1   1 
ATOM   4285 O  OD2   . ASP B 1 153 ? -30.591 -5.504  1.107   1.00 32.58 ? 132 ASP B OD2   1 
ATOM   4286 N  N     . ALA B 1 154 ? -27.382 -5.456  -2.663  1.00 33.09 ? 133 ALA B N     1 
ATOM   4287 C  CA    . ALA B 1 154 ? -26.787 -6.713  -3.162  1.00 35.95 ? 133 ALA B CA    1 
ATOM   4288 C  C     . ALA B 1 154 ? -27.045 -6.793  -4.650  1.00 34.53 ? 133 ALA B C     1 
ATOM   4289 O  O     . ALA B 1 154 ? -27.866 -7.597  -5.079  1.00 33.29 ? 133 ALA B O     1 
ATOM   4290 C  CB    . ALA B 1 154 ? -27.350 -7.922  -2.425  1.00 37.83 ? 133 ALA B CB    1 
ATOM   4291 N  N     . PRO B 1 155 ? -26.342 -5.960  -5.455  1.00 36.84 ? 134 PRO B N     1 
ATOM   4292 C  CA    . PRO B 1 155 ? -26.610 -5.857  -6.893  1.00 33.82 ? 134 PRO B CA    1 
ATOM   4293 C  C     . PRO B 1 155 ? -26.502 -7.228  -7.570  1.00 35.70 ? 134 PRO B C     1 
ATOM   4294 O  O     . PRO B 1 155 ? -27.197 -7.492  -8.572  1.00 38.45 ? 134 PRO B O     1 
ATOM   4295 C  CB    . PRO B 1 155 ? -25.523 -4.895  -7.398  1.00 34.72 ? 134 PRO B CB    1 
ATOM   4296 C  CG    . PRO B 1 155 ? -25.122 -4.098  -6.152  1.00 35.16 ? 134 PRO B CG    1 
ATOM   4297 C  CD    . PRO B 1 155 ? -25.248 -5.072  -5.010  1.00 34.68 ? 134 PRO B CD    1 
ATOM   4298 N  N     . TRP B 1 156 ? -25.667 -8.085  -6.984  1.00 34.88 ? 135 TRP B N     1 
ATOM   4299 C  CA    . TRP B 1 156 ? -25.384 -9.464  -7.463  1.00 35.78 ? 135 TRP B CA    1 
ATOM   4300 C  C     . TRP B 1 156 ? -26.586 -10.394 -7.268  1.00 36.17 ? 135 TRP B C     1 
ATOM   4301 O  O     . TRP B 1 156 ? -26.509 -11.542 -7.807  1.00 30.93 ? 135 TRP B O     1 
ATOM   4302 C  CB    . TRP B 1 156 ? -24.156 -10.008 -6.747  1.00 34.52 ? 135 TRP B CB    1 
ATOM   4303 C  CG    . TRP B 1 156 ? -24.292 -9.951  -5.261  1.00 37.12 ? 135 TRP B CG    1 
ATOM   4304 C  CD1   . TRP B 1 156 ? -24.917 -10.876 -4.476  1.00 32.10 ? 135 TRP B CD1   1 
ATOM   4305 C  CD2   . TRP B 1 156 ? -23.775 -8.939  -4.376  1.00 36.77 ? 135 TRP B CD2   1 
ATOM   4306 N  NE1   . TRP B 1 156 ? -24.839 -10.498 -3.169  1.00 36.29 ? 135 TRP B NE1   1 
ATOM   4307 C  CE2   . TRP B 1 156 ? -24.133 -9.328  -3.066  1.00 35.92 ? 135 TRP B CE2   1 
ATOM   4308 C  CE3   . TRP B 1 156 ? -23.049 -7.754  -4.544  1.00 36.19 ? 135 TRP B CE3   1 
ATOM   4309 C  CZ2   . TRP B 1 156 ? -23.780 -8.578  -1.941  1.00 37.49 ? 135 TRP B CZ2   1 
ATOM   4310 C  CZ3   . TRP B 1 156 ? -22.702 -7.010  -3.428  1.00 36.01 ? 135 TRP B CZ3   1 
ATOM   4311 C  CH2   . TRP B 1 156 ? -23.055 -7.419  -2.146  1.00 36.15 ? 135 TRP B CH2   1 
ATOM   4312 N  N     . LEU B 1 157 ? -27.641 -9.929  -6.573  1.00 33.09 ? 136 LEU B N     1 
ATOM   4313 C  CA    . LEU B 1 157 ? -28.902 -10.698 -6.359  1.00 38.32 ? 136 LEU B CA    1 
ATOM   4314 C  C     . LEU B 1 157 ? -30.021 -10.296 -7.346  1.00 38.12 ? 136 LEU B C     1 
ATOM   4315 O  O     . LEU B 1 157 ? -31.140 -10.836 -7.227  1.00 34.83 ? 136 LEU B O     1 
ATOM   4316 C  CB    . LEU B 1 157 ? -29.341 -10.550 -4.895  1.00 39.17 ? 136 LEU B CB    1 
ATOM   4317 C  CG    . LEU B 1 157 ? -28.572 -11.414 -3.888  1.00 39.19 ? 136 LEU B CG    1 
ATOM   4318 C  CD1   . LEU B 1 157 ? -29.113 -11.235 -2.467  1.00 34.35 ? 136 LEU B CD1   1 
ATOM   4319 C  CD2   . LEU B 1 157 ? -28.599 -12.890 -4.297  1.00 40.26 ? 136 LEU B CD2   1 
ATOM   4320 N  N     . ALA B 1 158 ? -29.757 -9.450  -8.338  1.00 37.37 ? 137 ALA B N     1 
ATOM   4321 C  CA    . ALA B 1 158 ? -30.730 -9.194  -9.429  1.00 39.15 ? 137 ALA B CA    1 
ATOM   4322 C  C     . ALA B 1 158 ? -30.977 -10.494 -10.197 1.00 43.83 ? 137 ALA B C     1 
ATOM   4323 O  O     . ALA B 1 158 ? -30.045 -11.238 -10.501 1.00 41.83 ? 137 ALA B O     1 
ATOM   4324 C  CB    . ALA B 1 158 ? -30.232 -8.112  -10.357 1.00 38.15 ? 137 ALA B CB    1 
ATOM   4325 N  N     . PRO B 1 159 ? -32.230 -10.810 -10.591 1.00 47.84 ? 138 PRO B N     1 
ATOM   4326 C  CA    . PRO B 1 159 ? -32.526 -12.110 -11.201 1.00 49.10 ? 138 PRO B CA    1 
ATOM   4327 C  C     . PRO B 1 159 ? -31.567 -12.400 -12.372 1.00 48.93 ? 138 PRO B C     1 
ATOM   4328 O  O     . PRO B 1 159 ? -31.077 -13.529 -12.484 1.00 44.19 ? 138 PRO B O     1 
ATOM   4329 C  CB    . PRO B 1 159 ? -33.994 -11.982 -11.665 1.00 48.09 ? 138 PRO B CB    1 
ATOM   4330 C  CG    . PRO B 1 159 ? -34.246 -10.489 -11.706 1.00 51.63 ? 138 PRO B CG    1 
ATOM   4331 C  CD    . PRO B 1 159 ? -33.395 -9.914  -10.585 1.00 50.98 ? 138 PRO B CD    1 
ATOM   4332 N  N     . GLU B 1 160 ? -31.290 -11.363 -13.176 1.00 42.69 ? 139 GLU B N     1 
ATOM   4333 C  CA    . GLU B 1 160 ? -30.436 -11.436 -14.382 1.00 43.47 ? 139 GLU B CA    1 
ATOM   4334 C  C     . GLU B 1 160 ? -29.065 -10.798 -14.099 1.00 36.65 ? 139 GLU B C     1 
ATOM   4335 O  O     . GLU B 1 160 ? -28.486 -10.245 -15.026 1.00 32.12 ? 139 GLU B O     1 
ATOM   4336 C  CB    . GLU B 1 160 ? -31.187 -10.770 -15.541 1.00 50.54 ? 139 GLU B CB    1 
ATOM   4337 C  CG    . GLU B 1 160 ? -32.372 -11.587 -16.060 1.00 54.83 ? 139 GLU B CG    1 
ATOM   4338 C  CD    . GLU B 1 160 ? -32.022 -12.896 -16.759 1.00 55.45 ? 139 GLU B CD    1 
ATOM   4339 O  OE1   . GLU B 1 160 ? -32.940 -13.699 -17.014 1.00 55.50 ? 139 GLU B OE1   1 
ATOM   4340 O  OE2   . GLU B 1 160 ? -30.827 -13.113 -17.050 1.00 65.31 ? 139 GLU B OE2   1 
ATOM   4341 N  N     . ALA B 1 161 ? -28.557 -10.877 -12.868 1.00 34.16 ? 140 ALA B N     1 
ATOM   4342 C  CA    . ALA B 1 161 ? -27.289 -10.228 -12.459 1.00 33.77 ? 140 ALA B CA    1 
ATOM   4343 C  C     . ALA B 1 161 ? -26.119 -10.724 -13.330 1.00 32.03 ? 140 ALA B C     1 
ATOM   4344 O  O     . ALA B 1 161 ? -25.282 -9.885  -13.701 1.00 30.30 ? 140 ALA B O     1 
ATOM   4345 C  CB    . ALA B 1 161 ? -27.022 -10.445 -10.997 1.00 31.59 ? 140 ALA B CB    1 
ATOM   4346 N  N     . ALA B 1 162 ? -26.070 -12.023 -13.656 1.00 30.90 ? 141 ALA B N     1 
ATOM   4347 C  CA    . ALA B 1 162 ? -24.968 -12.686 -14.406 1.00 31.57 ? 141 ALA B CA    1 
ATOM   4348 C  C     . ALA B 1 162 ? -24.799 -12.042 -15.795 1.00 32.54 ? 141 ALA B C     1 
ATOM   4349 O  O     . ALA B 1 162 ? -23.665 -11.616 -16.122 1.00 30.55 ? 141 ALA B O     1 
ATOM   4350 C  CB    . ALA B 1 162 ? -25.234 -14.173 -14.535 1.00 32.39 ? 141 ALA B CB    1 
ATOM   4351 N  N     . ALA B 1 163 ? -25.890 -11.995 -16.570 1.00 28.23 ? 142 ALA B N     1 
ATOM   4352 C  CA    . ALA B 1 163 ? -26.004 -11.393 -17.918 1.00 30.37 ? 142 ALA B CA    1 
ATOM   4353 C  C     . ALA B 1 163 ? -25.678 -9.888  -17.892 1.00 31.24 ? 142 ALA B C     1 
ATOM   4354 O  O     . ALA B 1 163 ? -24.975 -9.441  -18.810 1.00 28.95 ? 142 ALA B O     1 
ATOM   4355 C  CB    . ALA B 1 163 ? -27.403 -11.631 -18.445 1.00 30.69 ? 142 ALA B CB    1 
ATOM   4356 N  N     . TRP B 1 164 ? -26.208 -9.138  -16.912 1.00 31.72 ? 143 TRP B N     1 
ATOM   4357 C  CA    . TRP B 1 164 ? -26.052 -7.662  -16.754 1.00 32.94 ? 143 TRP B CA    1 
ATOM   4358 C  C     . TRP B 1 164 ? -24.617 -7.293  -16.364 1.00 35.69 ? 143 TRP B C     1 
ATOM   4359 O  O     . TRP B 1 164 ? -24.117 -6.241  -16.882 1.00 33.92 ? 143 TRP B O     1 
ATOM   4360 C  CB    . TRP B 1 164 ? -27.054 -7.078  -15.746 1.00 31.81 ? 143 TRP B CB    1 
ATOM   4361 C  CG    . TRP B 1 164 ? -28.464 -7.100  -16.254 1.00 33.44 ? 143 TRP B CG    1 
ATOM   4362 C  CD1   . TRP B 1 164 ? -28.879 -7.318  -17.540 1.00 34.65 ? 143 TRP B CD1   1 
ATOM   4363 C  CD2   . TRP B 1 164 ? -29.657 -6.879  -15.481 1.00 35.46 ? 143 TRP B CD2   1 
ATOM   4364 N  NE1   . TRP B 1 164 ? -30.244 -7.253  -17.624 1.00 37.57 ? 143 TRP B NE1   1 
ATOM   4365 C  CE2   . TRP B 1 164 ? -30.749 -6.980  -16.375 1.00 39.16 ? 143 TRP B CE2   1 
ATOM   4366 C  CE3   . TRP B 1 164 ? -29.905 -6.583  -14.135 1.00 35.80 ? 143 TRP B CE3   1 
ATOM   4367 C  CZ2   . TRP B 1 164 ? -32.066 -6.833  -15.944 1.00 37.02 ? 143 TRP B CZ2   1 
ATOM   4368 C  CZ3   . TRP B 1 164 ? -31.204 -6.427  -13.716 1.00 37.02 ? 143 TRP B CZ3   1 
ATOM   4369 C  CH2   . TRP B 1 164 ? -32.266 -6.573  -14.606 1.00 36.07 ? 143 TRP B CH2   1 
ATOM   4370 N  N     . ASP B 1 165 ? -23.998 -8.094  -15.491 1.00 30.16 ? 144 ASP B N     1 
ATOM   4371 C  CA    . ASP B 1 165 ? -22.552 -7.997  -15.166 1.00 28.69 ? 144 ASP B CA    1 
ATOM   4372 C  C     . ASP B 1 165 ? -21.693 -8.329  -16.404 1.00 26.69 ? 144 ASP B C     1 
ATOM   4373 O  O     . ASP B 1 165 ? -20.605 -7.751  -16.515 1.00 27.74 ? 144 ASP B O     1 
ATOM   4374 C  CB    . ASP B 1 165 ? -22.195 -8.857  -13.950 1.00 27.82 ? 144 ASP B CB    1 
ATOM   4375 C  CG    . ASP B 1 165 ? -21.133 -8.234  -13.052 1.00 30.25 ? 144 ASP B CG    1 
ATOM   4376 O  OD1   . ASP B 1 165 ? -20.982 -6.966  -13.074 1.00 30.08 ? 144 ASP B OD1   1 
ATOM   4377 O  OD2   . ASP B 1 165 ? -20.467 -9.020  -12.325 1.00 30.62 ? 144 ASP B OD2   1 
ATOM   4378 N  N     . ALA B 1 166 ? -22.120 -9.230  -17.288 1.00 21.72 ? 145 ALA B N     1 
ATOM   4379 C  CA    . ALA B 1 166 ? -21.319 -9.630  -18.468 1.00 22.94 ? 145 ALA B CA    1 
ATOM   4380 C  C     . ALA B 1 166 ? -21.400 -8.577  -19.593 1.00 24.90 ? 145 ALA B C     1 
ATOM   4381 O  O     . ALA B 1 166 ? -20.763 -8.784  -20.626 1.00 28.66 ? 145 ALA B O     1 
ATOM   4382 C  CB    . ALA B 1 166 ? -21.774 -10.980 -18.955 1.00 22.50 ? 145 ALA B CB    1 
ATOM   4383 N  N     . THR B 1 167 ? -22.160 -7.492  -19.425 1.00 25.53 ? 146 THR B N     1 
ATOM   4384 C  CA    . THR B 1 167 ? -22.414 -6.466  -20.475 1.00 25.76 ? 146 THR B CA    1 
ATOM   4385 C  C     . THR B 1 167 ? -21.822 -5.135  -20.007 1.00 23.47 ? 146 THR B C     1 
ATOM   4386 O  O     . THR B 1 167 ? -21.840 -4.875  -18.793 1.00 20.68 ? 146 THR B O     1 
ATOM   4387 C  CB    . THR B 1 167 ? -23.912 -6.371  -20.825 1.00 27.52 ? 146 THR B CB    1 
ATOM   4388 O  OG1   . THR B 1 167 ? -24.450 -7.664  -21.130 1.00 28.23 ? 146 THR B OG1   1 
ATOM   4389 C  CG2   . THR B 1 167 ? -24.187 -5.502  -22.030 1.00 30.57 ? 146 THR B CG2   1 
ATOM   4390 N  N     . THR B 1 168 ? -21.304 -4.327  -20.939 1.00 21.54 ? 147 THR B N     1 
ATOM   4391 C  CA    . THR B 1 168 ? -20.934 -2.916  -20.664 1.00 22.27 ? 147 THR B CA    1 
ATOM   4392 C  C     . THR B 1 168 ? -22.195 -2.073  -20.762 1.00 23.22 ? 147 THR B C     1 
ATOM   4393 O  O     . THR B 1 168 ? -23.130 -2.533  -21.426 1.00 23.39 ? 147 THR B O     1 
ATOM   4394 C  CB    . THR B 1 168 ? -19.889 -2.394  -21.642 1.00 20.71 ? 147 THR B CB    1 
ATOM   4395 O  OG1   . THR B 1 168 ? -20.467 -2.501  -22.938 1.00 20.97 ? 147 THR B OG1   1 
ATOM   4396 C  CG2   . THR B 1 168 ? -18.601 -3.174  -21.573 1.00 22.77 ? 147 THR B CG2   1 
ATOM   4397 N  N     . LEU B 1 169 ? -22.193 -0.856  -20.220 1.00 25.19 ? 148 LEU B N     1 
ATOM   4398 C  CA    . LEU B 1 169 ? -23.255 0.140   -20.554 1.00 28.32 ? 148 LEU B CA    1 
ATOM   4399 C  C     . LEU B 1 169 ? -23.301 0.379   -22.077 1.00 31.04 ? 148 LEU B C     1 
ATOM   4400 O  O     . LEU B 1 169 ? -24.442 0.414   -22.650 1.00 29.49 ? 148 LEU B O     1 
ATOM   4401 C  CB    . LEU B 1 169 ? -22.997 1.445   -19.794 1.00 27.93 ? 148 LEU B CB    1 
ATOM   4402 C  CG    . LEU B 1 169 ? -24.094 2.504   -19.885 1.00 29.30 ? 148 LEU B CG    1 
ATOM   4403 C  CD1   . LEU B 1 169 ? -25.491 1.899   -19.765 1.00 30.05 ? 148 LEU B CD1   1 
ATOM   4404 C  CD2   . LEU B 1 169 ? -23.893 3.554   -18.802 1.00 30.47 ? 148 LEU B CD2   1 
ATOM   4405 N  N     . ARG B 1 170 ? -22.118 0.519   -22.706 1.00 34.31 ? 149 ARG B N     1 
ATOM   4406 C  CA    . ARG B 1 170 ? -21.923 0.909   -24.135 1.00 34.28 ? 149 ARG B CA    1 
ATOM   4407 C  C     . ARG B 1 170 ? -22.635 -0.078  -25.060 1.00 35.52 ? 149 ARG B C     1 
ATOM   4408 O  O     . ARG B 1 170 ? -23.285 0.361   -26.015 1.00 34.23 ? 149 ARG B O     1 
ATOM   4409 C  CB    . ARG B 1 170 ? -20.426 0.924   -24.454 1.00 34.35 ? 149 ARG B CB    1 
ATOM   4410 C  CG    . ARG B 1 170 ? -20.074 1.115   -25.926 1.00 37.47 ? 149 ARG B CG    1 
ATOM   4411 C  CD    . ARG B 1 170 ? -20.157 2.554   -26.409 1.00 36.82 ? 149 ARG B CD    1 
ATOM   4412 N  NE    . ARG B 1 170 ? -19.383 3.475   -25.582 1.00 36.47 ? 149 ARG B NE    1 
ATOM   4413 C  CZ    . ARG B 1 170 ? -18.239 4.040   -25.927 1.00 37.48 ? 149 ARG B CZ    1 
ATOM   4414 N  NH1   . ARG B 1 170 ? -17.691 3.796   -27.101 1.00 38.35 ? 149 ARG B NH1   1 
ATOM   4415 N  NH2   . ARG B 1 170 ? -17.638 4.857   -25.086 1.00 39.97 ? 149 ARG B NH2   1 
ATOM   4416 N  N     . GLU B 1 171 ? -22.440 -1.371  -24.790 1.00 37.82 ? 150 GLU B N     1 
ATOM   4417 C  CA    . GLU B 1 171 ? -22.989 -2.538  -25.536 1.00 36.64 ? 150 GLU B CA    1 
ATOM   4418 C  C     . GLU B 1 171 ? -24.520 -2.484  -25.536 1.00 36.71 ? 150 GLU B C     1 
ATOM   4419 O  O     . GLU B 1 171 ? -25.142 -2.704  -26.616 1.00 33.89 ? 150 GLU B O     1 
ATOM   4420 C  CB    . GLU B 1 171 ? -22.423 -3.770  -24.834 1.00 38.12 ? 150 GLU B CB    1 
ATOM   4421 C  CG    . GLU B 1 171 ? -22.979 -5.108  -25.252 1.00 40.71 ? 150 GLU B CG    1 
ATOM   4422 C  CD    . GLU B 1 171 ? -22.259 -6.217  -24.500 1.00 43.81 ? 150 GLU B CD    1 
ATOM   4423 O  OE1   . GLU B 1 171 ? -21.334 -5.873  -23.663 1.00 34.44 ? 150 GLU B OE1   1 
ATOM   4424 O  OE2   . GLU B 1 171 ? -22.617 -7.415  -24.728 1.00 45.97 ? 150 GLU B OE2   1 
ATOM   4425 N  N     . TRP B 1 172 ? -25.103 -2.183  -24.375 1.00 35.50 ? 151 TRP B N     1 
ATOM   4426 C  CA    . TRP B 1 172 ? -26.574 -2.120  -24.152 1.00 38.56 ? 151 TRP B CA    1 
ATOM   4427 C  C     . TRP B 1 172 ? -27.210 -0.942  -24.927 1.00 39.54 ? 151 TRP B C     1 
ATOM   4428 O  O     . TRP B 1 172 ? -28.233 -1.186  -25.652 1.00 37.49 ? 151 TRP B O     1 
ATOM   4429 C  CB    . TRP B 1 172 ? -26.852 -2.062  -22.646 1.00 41.24 ? 151 TRP B CB    1 
ATOM   4430 C  CG    . TRP B 1 172 ? -28.294 -1.866  -22.317 1.00 43.45 ? 151 TRP B CG    1 
ATOM   4431 C  CD1   . TRP B 1 172 ? -29.252 -2.828  -22.208 1.00 45.37 ? 151 TRP B CD1   1 
ATOM   4432 C  CD2   . TRP B 1 172 ? -28.945 -0.609  -22.076 1.00 44.26 ? 151 TRP B CD2   1 
ATOM   4433 N  NE1   . TRP B 1 172 ? -30.458 -2.254  -21.915 1.00 45.93 ? 151 TRP B NE1   1 
ATOM   4434 C  CE2   . TRP B 1 172 ? -30.299 -0.897  -21.819 1.00 45.19 ? 151 TRP B CE2   1 
ATOM   4435 C  CE3   . TRP B 1 172 ? -28.518 0.725   -22.068 1.00 43.70 ? 151 TRP B CE3   1 
ATOM   4436 C  CZ2   . TRP B 1 172 ? -31.230 0.106   -21.553 1.00 44.18 ? 151 TRP B CZ2   1 
ATOM   4437 C  CZ3   . TRP B 1 172 ? -29.435 1.713   -21.792 1.00 44.91 ? 151 TRP B CZ3   1 
ATOM   4438 C  CH2   . TRP B 1 172 ? -30.777 1.405   -21.551 1.00 44.40 ? 151 TRP B CH2   1 
ATOM   4439 N  N     . VAL B 1 173 ? -26.651 0.275   -24.801 1.00 35.39 ? 152 VAL B N     1 
ATOM   4440 C  CA    . VAL B 1 173 ? -27.039 1.495   -25.585 1.00 32.93 ? 152 VAL B CA    1 
ATOM   4441 C  C     . VAL B 1 173 ? -27.129 1.118   -27.065 1.00 34.42 ? 152 VAL B C     1 
ATOM   4442 O  O     . VAL B 1 173 ? -28.183 1.388   -27.697 1.00 30.85 ? 152 VAL B O     1 
ATOM   4443 C  CB    . VAL B 1 173 ? -26.030 2.639   -25.366 1.00 33.07 ? 152 VAL B CB    1 
ATOM   4444 C  CG1   . VAL B 1 173 ? -26.264 3.828   -26.286 1.00 32.50 ? 152 VAL B CG1   1 
ATOM   4445 C  CG2   . VAL B 1 173 ? -26.001 3.075   -23.909 1.00 34.47 ? 152 VAL B CG2   1 
ATOM   4446 N  N     . ALA B 1 174 ? -26.053 0.510   -27.586 1.00 39.94 ? 153 ALA B N     1 
ATOM   4447 C  CA    . ALA B 1 174 ? -25.902 0.089   -29.001 1.00 42.56 ? 153 ALA B CA    1 
ATOM   4448 C  C     . ALA B 1 174 ? -27.099 -0.790  -29.395 1.00 48.77 ? 153 ALA B C     1 
ATOM   4449 O  O     . ALA B 1 174 ? -27.601 -0.614  -30.536 1.00 49.97 ? 153 ALA B O     1 
ATOM   4450 C  CB    . ALA B 1 174 ? -24.574 -0.603  -29.219 1.00 41.59 ? 153 ALA B CB    1 
ATOM   4451 N  N     . GLY B 1 175 ? -27.579 -1.620  -28.452 1.00 49.72 ? 154 GLY B N     1 
ATOM   4452 C  CA    . GLY B 1 175 ? -28.685 -2.586  -28.615 1.00 47.90 ? 154 GLY B CA    1 
ATOM   4453 C  C     . GLY B 1 175 ? -30.050 -1.924  -28.649 1.00 48.65 ? 154 GLY B C     1 
ATOM   4454 O  O     . GLY B 1 175 ? -30.975 -2.554  -29.177 1.00 52.81 ? 154 GLY B O     1 
ATOM   4455 N  N     . THR B 1 176 ? -30.194 -0.719  -28.088 1.00 49.96 ? 155 THR B N     1 
ATOM   4456 C  CA    . THR B 1 176 ? -31.470 0.051   -28.076 1.00 46.87 ? 155 THR B CA    1 
ATOM   4457 C  C     . THR B 1 176 ? -31.646 0.693   -29.454 1.00 51.81 ? 155 THR B C     1 
ATOM   4458 O  O     . THR B 1 176 ? -32.815 0.897   -29.845 1.00 50.68 ? 155 THR B O     1 
ATOM   4459 C  CB    . THR B 1 176 ? -31.524 1.147   -27.003 1.00 43.75 ? 155 THR B CB    1 
ATOM   4460 O  OG1   . THR B 1 176 ? -30.833 2.271   -27.551 1.00 40.17 ? 155 THR B OG1   1 
ATOM   4461 C  CG2   . THR B 1 176 ? -30.951 0.729   -25.662 1.00 40.56 ? 155 THR B CG2   1 
ATOM   4462 N  N     . GLY B 1 177 ? -30.516 1.013   -30.116 1.00 54.21 ? 156 GLY B N     1 
ATOM   4463 C  CA    . GLY B 1 177 ? -30.405 1.430   -31.529 1.00 48.97 ? 156 GLY B CA    1 
ATOM   4464 C  C     . GLY B 1 177 ? -30.813 2.877   -31.743 1.00 49.57 ? 156 GLY B C     1 
ATOM   4465 O  O     . GLY B 1 177 ? -31.417 3.165   -32.803 1.00 49.54 ? 156 GLY B O     1 
ATOM   4466 N  N     . VAL B 1 178 ? -30.505 3.768   -30.793 1.00 41.57 ? 157 VAL B N     1 
ATOM   4467 C  CA    . VAL B 1 178 ? -30.931 5.200   -30.862 1.00 42.69 ? 157 VAL B CA    1 
ATOM   4468 C  C     . VAL B 1 178 ? -30.152 5.902   -31.975 1.00 45.39 ? 157 VAL B C     1 
ATOM   4469 O  O     . VAL B 1 178 ? -29.217 5.341   -32.540 1.00 47.27 ? 157 VAL B O     1 
ATOM   4470 C  CB    . VAL B 1 178 ? -30.773 5.927   -29.512 1.00 39.37 ? 157 VAL B CB    1 
ATOM   4471 C  CG1   . VAL B 1 178 ? -31.770 5.419   -28.482 1.00 35.93 ? 157 VAL B CG1   1 
ATOM   4472 C  CG2   . VAL B 1 178 ? -29.352 5.863   -28.986 1.00 39.55 ? 157 VAL B CG2   1 
ATOM   4473 N  N     . PRO B 1 179 ? -30.532 7.138   -32.365 1.00 48.38 ? 158 PRO B N     1 
ATOM   4474 C  CA    . PRO B 1 179 ? -29.670 7.974   -33.204 1.00 48.72 ? 158 PRO B CA    1 
ATOM   4475 C  C     . PRO B 1 179 ? -28.367 8.352   -32.470 1.00 49.28 ? 158 PRO B C     1 
ATOM   4476 O  O     . PRO B 1 179 ? -28.231 8.065   -31.275 1.00 45.34 ? 158 PRO B O     1 
ATOM   4477 C  CB    . PRO B 1 179 ? -30.525 9.215   -33.527 1.00 48.91 ? 158 PRO B CB    1 
ATOM   4478 C  CG    . PRO B 1 179 ? -31.957 8.800   -33.193 1.00 50.93 ? 158 PRO B CG    1 
ATOM   4479 C  CD    . PRO B 1 179 ? -31.829 7.773   -32.084 1.00 50.00 ? 158 PRO B CD    1 
ATOM   4480 N  N     . ASP B 1 180 ? -27.418 8.957   -33.196 1.00 44.33 ? 159 ASP B N     1 
ATOM   4481 C  CA    . ASP B 1 180 ? -26.055 9.263   -32.686 1.00 45.84 ? 159 ASP B CA    1 
ATOM   4482 C  C     . ASP B 1 180 ? -26.151 10.439  -31.710 1.00 42.32 ? 159 ASP B C     1 
ATOM   4483 O  O     . ASP B 1 180 ? -25.825 10.252  -30.551 1.00 47.69 ? 159 ASP B O     1 
ATOM   4484 C  CB    . ASP B 1 180 ? -25.083 9.441   -33.853 1.00 49.11 ? 159 ASP B CB    1 
ATOM   4485 C  CG    . ASP B 1 180 ? -24.992 8.165   -34.675 1.00 54.15 ? 159 ASP B CG    1 
ATOM   4486 O  OD1   . ASP B 1 180 ? -25.999 7.421   -34.699 1.00 54.68 ? 159 ASP B OD1   1 
ATOM   4487 O  OD2   . ASP B 1 180 ? -23.916 7.904   -35.251 1.00 58.54 ? 159 ASP B OD2   1 
ATOM   4488 N  N     . ARG B 1 181 ? -26.679 11.579  -32.141 1.00 41.81 ? 160 ARG B N     1 
ATOM   4489 C  CA    . ARG B 1 181 ? -26.917 12.754  -31.260 1.00 41.29 ? 160 ARG B CA    1 
ATOM   4490 C  C     . ARG B 1 181 ? -27.453 12.283  -29.903 1.00 38.59 ? 160 ARG B C     1 
ATOM   4491 O  O     . ARG B 1 181 ? -26.998 12.837  -28.876 1.00 39.56 ? 160 ARG B O     1 
ATOM   4492 C  CB    . ARG B 1 181 ? -27.889 13.733  -31.926 1.00 45.35 ? 160 ARG B CB    1 
ATOM   4493 C  CG    . ARG B 1 181 ? -27.273 14.551  -33.054 1.00 48.97 ? 160 ARG B CG    1 
ATOM   4494 C  CD    . ARG B 1 181 ? -28.303 15.340  -33.833 1.00 52.13 ? 160 ARG B CD    1 
ATOM   4495 N  NE    . ARG B 1 181 ? -27.853 16.698  -34.107 1.00 59.01 ? 160 ARG B NE    1 
ATOM   4496 C  CZ    . ARG B 1 181 ? -28.563 17.625  -34.755 1.00 65.21 ? 160 ARG B CZ    1 
ATOM   4497 N  NH1   . ARG B 1 181 ? -29.777 17.357  -35.214 1.00 68.71 ? 160 ARG B NH1   1 
ATOM   4498 N  NH2   . ARG B 1 181 ? -28.048 18.825  -34.948 1.00 63.54 ? 160 ARG B NH2   1 
ATOM   4499 N  N     . VAL B 1 182 ? -28.390 11.323  -29.921 1.00 37.53 ? 161 VAL B N     1 
ATOM   4500 C  CA    . VAL B 1 182 ? -29.078 10.735  -28.733 1.00 37.14 ? 161 VAL B CA    1 
ATOM   4501 C  C     . VAL B 1 182 ? -28.052 9.968   -27.908 1.00 36.07 ? 161 VAL B C     1 
ATOM   4502 O  O     . VAL B 1 182 ? -27.985 10.214  -26.713 1.00 35.36 ? 161 VAL B O     1 
ATOM   4503 C  CB    . VAL B 1 182 ? -30.250 9.820   -29.138 1.00 39.62 ? 161 VAL B CB    1 
ATOM   4504 C  CG1   . VAL B 1 182 ? -30.875 9.103   -27.935 1.00 39.79 ? 161 VAL B CG1   1 
ATOM   4505 C  CG2   . VAL B 1 182 ? -31.314 10.601  -29.903 1.00 39.60 ? 161 VAL B CG2   1 
ATOM   4506 N  N     . ALA B 1 183 ? -27.281 9.087   -28.549 1.00 38.26 ? 162 ALA B N     1 
ATOM   4507 C  CA    . ALA B 1 183 ? -26.256 8.235   -27.897 1.00 39.05 ? 162 ALA B CA    1 
ATOM   4508 C  C     . ALA B 1 183 ? -25.107 9.090   -27.334 1.00 37.18 ? 162 ALA B C     1 
ATOM   4509 O  O     . ALA B 1 183 ? -24.479 8.663   -26.358 1.00 34.21 ? 162 ALA B O     1 
ATOM   4510 C  CB    . ALA B 1 183 ? -25.751 7.206   -28.878 1.00 40.96 ? 162 ALA B CB    1 
ATOM   4511 N  N     . GLY B 1 184 ? -24.834 10.239  -27.951 1.00 37.14 ? 163 GLY B N     1 
ATOM   4512 C  CA    . GLY B 1 184 ? -23.732 11.142  -27.582 1.00 36.70 ? 163 GLY B CA    1 
ATOM   4513 C  C     . GLY B 1 184 ? -24.155 12.097  -26.486 1.00 34.09 ? 163 GLY B C     1 
ATOM   4514 O  O     . GLY B 1 184 ? -23.377 12.310  -25.573 1.00 36.42 ? 163 GLY B O     1 
ATOM   4515 N  N     . LEU B 1 185 ? -25.362 12.639  -26.582 1.00 38.64 ? 164 LEU B N     1 
ATOM   4516 C  CA    . LEU B 1 185 ? -26.037 13.379  -25.483 1.00 41.70 ? 164 LEU B CA    1 
ATOM   4517 C  C     . LEU B 1 185 ? -26.076 12.500  -24.224 1.00 37.85 ? 164 LEU B C     1 
ATOM   4518 O  O     . LEU B 1 185 ? -25.715 13.016  -23.140 1.00 42.51 ? 164 LEU B O     1 
ATOM   4519 C  CB    . LEU B 1 185 ? -27.443 13.795  -25.934 1.00 45.67 ? 164 LEU B CB    1 
ATOM   4520 C  CG    . LEU B 1 185 ? -28.227 14.653  -24.935 1.00 48.77 ? 164 LEU B CG    1 
ATOM   4521 C  CD1   . LEU B 1 185 ? -27.678 16.074  -24.888 1.00 48.62 ? 164 LEU B CD1   1 
ATOM   4522 C  CD2   . LEU B 1 185 ? -29.714 14.643  -25.259 1.00 50.82 ? 164 LEU B CD2   1 
ATOM   4523 N  N     . PHE B 1 186 ? -26.512 11.241  -24.356 1.00 35.39 ? 165 PHE B N     1 
ATOM   4524 C  CA    . PHE B 1 186 ? -26.492 10.207  -23.282 1.00 32.93 ? 165 PHE B CA    1 
ATOM   4525 C  C     . PHE B 1 186 ? -25.053 10.049  -22.789 1.00 32.16 ? 165 PHE B C     1 
ATOM   4526 O  O     . PHE B 1 186 ? -24.825 10.177  -21.581 1.00 30.70 ? 165 PHE B O     1 
ATOM   4527 C  CB    . PHE B 1 186 ? -27.019 8.858   -23.780 1.00 32.78 ? 165 PHE B CB    1 
ATOM   4528 C  CG    . PHE B 1 186 ? -27.268 7.842   -22.695 1.00 34.97 ? 165 PHE B CG    1 
ATOM   4529 C  CD1   . PHE B 1 186 ? -26.524 6.677   -22.626 1.00 35.75 ? 165 PHE B CD1   1 
ATOM   4530 C  CD2   . PHE B 1 186 ? -28.233 8.059   -21.715 1.00 37.21 ? 165 PHE B CD2   1 
ATOM   4531 C  CE1   . PHE B 1 186 ? -26.748 5.747   -21.618 1.00 35.33 ? 165 PHE B CE1   1 
ATOM   4532 C  CE2   . PHE B 1 186 ? -28.440 7.139   -20.695 1.00 36.93 ? 165 PHE B CE2   1 
ATOM   4533 C  CZ    . PHE B 1 186 ? -27.695 5.984   -20.646 1.00 33.28 ? 165 PHE B CZ    1 
ATOM   4534 N  N     . GLU B 1 187 ? -24.103 9.815   -23.707 1.00 29.74 ? 166 GLU B N     1 
ATOM   4535 C  CA    . GLU B 1 187 ? -22.668 9.666   -23.352 1.00 28.65 ? 166 GLU B CA    1 
ATOM   4536 C  C     . GLU B 1 187 ? -22.223 10.908  -22.560 1.00 26.28 ? 166 GLU B C     1 
ATOM   4537 O  O     . GLU B 1 187 ? -21.514 10.739  -21.580 1.00 25.94 ? 166 GLU B O     1 
ATOM   4538 C  CB    . GLU B 1 187 ? -21.785 9.459   -24.592 1.00 29.10 ? 166 GLU B CB    1 
ATOM   4539 C  CG    . GLU B 1 187 ? -20.405 8.897   -24.255 1.00 28.99 ? 166 GLU B CG    1 
ATOM   4540 C  CD    . GLU B 1 187 ? -20.399 7.529   -23.574 1.00 26.28 ? 166 GLU B CD    1 
ATOM   4541 O  OE1   . GLU B 1 187 ? -19.420 7.185   -22.864 1.00 23.98 ? 166 GLU B OE1   1 
ATOM   4542 O  OE2   . GLU B 1 187 ? -21.354 6.809   -23.774 1.00 24.70 ? 166 GLU B OE2   1 
ATOM   4543 N  N     . VAL B 1 188 ? -22.609 12.120  -22.967 1.00 27.01 ? 167 VAL B N     1 
ATOM   4544 C  CA    . VAL B 1 188 ? -22.164 13.341  -22.234 1.00 28.38 ? 167 VAL B CA    1 
ATOM   4545 C  C     . VAL B 1 188 ? -22.583 13.170  -20.779 1.00 25.81 ? 167 VAL B C     1 
ATOM   4546 O  O     . VAL B 1 188 ? -21.738 13.385  -19.908 1.00 26.35 ? 167 VAL B O     1 
ATOM   4547 C  CB    . VAL B 1 188 ? -22.716 14.666  -22.780 1.00 30.50 ? 167 VAL B CB    1 
ATOM   4548 C  CG1   . VAL B 1 188 ? -22.319 15.800  -21.841 1.00 32.12 ? 167 VAL B CG1   1 
ATOM   4549 C  CG2   . VAL B 1 188 ? -22.220 14.956  -24.177 1.00 35.25 ? 167 VAL B CG2   1 
ATOM   4550 N  N     . ALA B 1 189 ? -23.833 12.745  -20.576 1.00 25.69 ? 168 ALA B N     1 
ATOM   4551 C  CA    . ALA B 1 189 ? -24.483 12.620  -19.248 1.00 27.80 ? 168 ALA B CA    1 
ATOM   4552 C  C     . ALA B 1 189 ? -23.813 11.516  -18.417 1.00 25.49 ? 168 ALA B C     1 
ATOM   4553 O  O     . ALA B 1 189 ? -23.535 11.769  -17.261 1.00 28.93 ? 168 ALA B O     1 
ATOM   4554 C  CB    . ALA B 1 189 ? -25.960 12.381  -19.418 1.00 26.39 ? 168 ALA B CB    1 
ATOM   4555 N  N     . VAL B 1 190 ? -23.593 10.344  -19.007 1.00 24.21 ? 169 VAL B N     1 
ATOM   4556 C  CA    . VAL B 1 190 ? -22.897 9.180   -18.393 1.00 23.66 ? 169 VAL B CA    1 
ATOM   4557 C  C     . VAL B 1 190 ? -21.571 9.657   -17.791 1.00 24.66 ? 169 VAL B C     1 
ATOM   4558 O  O     . VAL B 1 190 ? -21.183 9.114   -16.768 1.00 21.84 ? 169 VAL B O     1 
ATOM   4559 C  CB    . VAL B 1 190 ? -22.657 8.063   -19.436 1.00 22.86 ? 169 VAL B CB    1 
ATOM   4560 C  CG1   . VAL B 1 190 ? -21.654 7.002   -18.950 1.00 22.39 ? 169 VAL B CG1   1 
ATOM   4561 C  CG2   . VAL B 1 190 ? -23.964 7.413   -19.874 1.00 21.59 ? 169 VAL B CG2   1 
ATOM   4562 N  N     . GLN B 1 191 ? -20.866 10.577  -18.462 1.00 27.66 ? 170 GLN B N     1 
ATOM   4563 C  CA    . GLN B 1 191 ? -19.449 10.911  -18.136 1.00 29.32 ? 170 GLN B CA    1 
ATOM   4564 C  C     . GLN B 1 191 ? -19.454 12.074  -17.137 1.00 27.59 ? 170 GLN B C     1 
ATOM   4565 O  O     . GLN B 1 191 ? -18.515 12.207  -16.356 1.00 25.55 ? 170 GLN B O     1 
ATOM   4566 C  CB    . GLN B 1 191 ? -18.659 11.236  -19.413 1.00 31.18 ? 170 GLN B CB    1 
ATOM   4567 C  CG    . GLN B 1 191 ? -17.922 10.049  -20.017 1.00 33.96 ? 170 GLN B CG    1 
ATOM   4568 C  CD    . GLN B 1 191 ? -17.171 10.399  -21.281 1.00 36.21 ? 170 GLN B CD    1 
ATOM   4569 O  OE1   . GLN B 1 191 ? -16.587 11.468  -21.382 1.00 34.66 ? 170 GLN B OE1   1 
ATOM   4570 N  NE2   . GLN B 1 191 ? -17.182 9.498   -22.260 1.00 36.28 ? 170 GLN B NE2   1 
ATOM   4571 N  N     . ALA B 1 192 ? -20.515 12.872  -17.164 1.00 29.74 ? 171 ALA B N     1 
ATOM   4572 C  CA    . ALA B 1 192 ? -20.837 13.903  -16.151 1.00 30.72 ? 171 ALA B CA    1 
ATOM   4573 C  C     . ALA B 1 192 ? -21.227 13.250  -14.817 1.00 30.12 ? 171 ALA B C     1 
ATOM   4574 O  O     . ALA B 1 192 ? -20.968 13.893  -13.772 1.00 35.65 ? 171 ALA B O     1 
ATOM   4575 C  CB    . ALA B 1 192 ? -21.928 14.817  -16.663 1.00 31.62 ? 171 ALA B CB    1 
ATOM   4576 N  N     . VAL B 1 193 ? -21.762 12.025  -14.831 1.00 28.68 ? 172 VAL B N     1 
ATOM   4577 C  CA    . VAL B 1 193 ? -22.141 11.239  -13.595 1.00 30.57 ? 172 VAL B CA    1 
ATOM   4578 C  C     . VAL B 1 193 ? -20.984 10.333  -13.131 1.00 26.77 ? 172 VAL B C     1 
ATOM   4579 O  O     . VAL B 1 193 ? -20.694 10.284  -11.927 1.00 26.06 ? 172 VAL B O     1 
ATOM   4580 C  CB    . VAL B 1 193 ? -23.437 10.425  -13.833 1.00 26.96 ? 172 VAL B CB    1 
ATOM   4581 C  CG1   . VAL B 1 193 ? -23.742 9.435   -12.720 1.00 26.99 ? 172 VAL B CG1   1 
ATOM   4582 C  CG2   . VAL B 1 193 ? -24.611 11.361  -14.040 1.00 28.18 ? 172 VAL B CG2   1 
ATOM   4583 N  N     . PHE B 1 194 ? -20.353 9.607   -14.048 1.00 27.68 ? 173 PHE B N     1 
ATOM   4584 C  CA    . PHE B 1 194 ? -19.519 8.423   -13.707 1.00 27.40 ? 173 PHE B CA    1 
ATOM   4585 C  C     . PHE B 1 194 ? -18.035 8.782   -13.803 1.00 25.55 ? 173 PHE B C     1 
ATOM   4586 O  O     . PHE B 1 194 ? -17.225 8.079   -13.182 1.00 29.97 ? 173 PHE B O     1 
ATOM   4587 C  CB    . PHE B 1 194 ? -19.900 7.238   -14.609 1.00 27.57 ? 173 PHE B CB    1 
ATOM   4588 C  CG    . PHE B 1 194 ? -21.244 6.606   -14.313 1.00 27.10 ? 173 PHE B CG    1 
ATOM   4589 C  CD1   . PHE B 1 194 ? -21.378 5.681   -13.281 1.00 25.24 ? 173 PHE B CD1   1 
ATOM   4590 C  CD2   . PHE B 1 194 ? -22.383 6.941   -15.050 1.00 25.47 ? 173 PHE B CD2   1 
ATOM   4591 C  CE1   . PHE B 1 194 ? -22.606 5.098   -13.012 1.00 22.84 ? 173 PHE B CE1   1 
ATOM   4592 C  CE2   . PHE B 1 194 ? -23.605 6.339   -14.787 1.00 24.46 ? 173 PHE B CE2   1 
ATOM   4593 C  CZ    . PHE B 1 194 ? -23.701 5.393   -13.784 1.00 23.97 ? 173 PHE B CZ    1 
ATOM   4594 N  N     . ALA B 1 195 ? -17.698 9.829   -14.554 1.00 25.48 ? 174 ALA B N     1 
ATOM   4595 C  CA    . ALA B 1 195 ? -16.310 10.245  -14.853 1.00 24.22 ? 174 ALA B CA    1 
ATOM   4596 C  C     . ALA B 1 195 ? -15.570 9.074   -15.524 1.00 22.42 ? 174 ALA B C     1 
ATOM   4597 O  O     . ALA B 1 195 ? -14.452 8.693   -15.079 1.00 20.85 ? 174 ALA B O     1 
ATOM   4598 C  CB    . ALA B 1 195 ? -15.637 10.725  -13.597 1.00 25.19 ? 174 ALA B CB    1 
ATOM   4599 N  N     . ALA B 1 196 ? -16.197 8.525   -16.568 1.00 21.08 ? 175 ALA B N     1 
ATOM   4600 C  CA    . ALA B 1 196 ? -15.758 7.306   -17.284 1.00 21.57 ? 175 ALA B CA    1 
ATOM   4601 C  C     . ALA B 1 196 ? -16.788 6.984   -18.357 1.00 22.89 ? 175 ALA B C     1 
ATOM   4602 O  O     . ALA B 1 196 ? -17.951 7.420   -18.200 1.00 21.45 ? 175 ALA B O     1 
ATOM   4603 C  CB    . ALA B 1 196 ? -15.570 6.144   -16.340 1.00 23.24 ? 175 ALA B CB    1 
ATOM   4604 N  N     . THR B 1 197 ? -16.351 6.292   -19.417 1.00 23.45 ? 176 THR B N     1 
ATOM   4605 C  CA    . THR B 1 197 ? -17.151 6.071   -20.633 1.00 22.48 ? 176 THR B CA    1 
ATOM   4606 C  C     . THR B 1 197 ? -18.106 4.918   -20.354 1.00 23.69 ? 176 THR B C     1 
ATOM   4607 O  O     . THR B 1 197 ? -17.816 4.123   -19.441 1.00 24.57 ? 176 THR B O     1 
ATOM   4608 C  CB    . THR B 1 197 ? -16.269 5.823   -21.858 1.00 21.48 ? 176 THR B CB    1 
ATOM   4609 O  OG1   . THR B 1 197 ? -15.866 4.458   -21.810 1.00 21.43 ? 176 THR B OG1   1 
ATOM   4610 C  CG2   . THR B 1 197 ? -15.079 6.753   -21.930 1.00 21.69 ? 176 THR B CG2   1 
ATOM   4611 N  N     . SER B 1 198 ? -19.181 4.839   -21.138 1.00 25.64 ? 177 SER B N     1 
ATOM   4612 C  CA    . SER B 1 198 ? -20.185 3.750   -21.122 1.00 29.04 ? 177 SER B CA    1 
ATOM   4613 C  C     . SER B 1 198 ? -19.509 2.402   -21.430 1.00 30.55 ? 177 SER B C     1 
ATOM   4614 O  O     . SER B 1 198 ? -20.111 1.348   -21.100 1.00 26.64 ? 177 SER B O     1 
ATOM   4615 C  CB    . SER B 1 198 ? -21.283 4.056   -22.089 1.00 31.46 ? 177 SER B CB    1 
ATOM   4616 O  OG    . SER B 1 198 ? -20.747 4.383   -23.359 1.00 34.04 ? 177 SER B OG    1 
ATOM   4617 N  N     . ALA B 1 199 ? -18.302 2.414   -22.029 1.00 31.57 ? 178 ALA B N     1 
ATOM   4618 C  CA    . ALA B 1 199 ? -17.495 1.197   -22.318 1.00 32.70 ? 178 ALA B CA    1 
ATOM   4619 C  C     . ALA B 1 199 ? -16.785 0.677   -21.056 1.00 30.91 ? 178 ALA B C     1 
ATOM   4620 O  O     . ALA B 1 199 ? -16.574 -0.569  -20.951 1.00 29.70 ? 178 ALA B O     1 
ATOM   4621 C  CB    . ALA B 1 199 ? -16.494 1.478   -23.418 1.00 35.74 ? 178 ALA B CB    1 
ATOM   4622 N  N     . GLN B 1 200 ? -16.419 1.569   -20.130 1.00 28.44 ? 179 GLN B N     1 
ATOM   4623 C  CA    . GLN B 1 200 ? -15.688 1.178   -18.905 1.00 27.19 ? 179 GLN B CA    1 
ATOM   4624 C  C     . GLN B 1 200 ? -16.655 0.496   -17.913 1.00 28.29 ? 179 GLN B C     1 
ATOM   4625 O  O     . GLN B 1 200 ? -16.180 -0.270  -17.047 1.00 23.52 ? 179 GLN B O     1 
ATOM   4626 C  CB    . GLN B 1 200 ? -15.021 2.405   -18.291 1.00 26.93 ? 179 GLN B CB    1 
ATOM   4627 C  CG    . GLN B 1 200 ? -13.976 3.070   -19.186 1.00 25.55 ? 179 GLN B CG    1 
ATOM   4628 C  CD    . GLN B 1 200 ? -13.232 4.157   -18.450 1.00 23.02 ? 179 GLN B CD    1 
ATOM   4629 O  OE1   . GLN B 1 200 ? -13.453 5.333   -18.670 1.00 21.94 ? 179 GLN B OE1   1 
ATOM   4630 N  NE2   . GLN B 1 200 ? -12.384 3.770   -17.514 1.00 24.26 ? 179 GLN B NE2   1 
ATOM   4631 N  N     . LEU B 1 201 ? -17.959 0.777   -18.015 1.00 29.34 ? 180 LEU B N     1 
ATOM   4632 C  CA    . LEU B 1 201 ? -18.963 0.457   -16.967 1.00 27.99 ? 180 LEU B CA    1 
ATOM   4633 C  C     . LEU B 1 201 ? -19.753 -0.794  -17.352 1.00 29.10 ? 180 LEU B C     1 
ATOM   4634 O  O     . LEU B 1 201 ? -20.385 -0.820  -18.446 1.00 28.29 ? 180 LEU B O     1 
ATOM   4635 C  CB    . LEU B 1 201 ? -19.930 1.632   -16.819 1.00 31.24 ? 180 LEU B CB    1 
ATOM   4636 C  CG    . LEU B 1 201 ? -19.320 3.016   -16.571 1.00 31.34 ? 180 LEU B CG    1 
ATOM   4637 C  CD1   . LEU B 1 201 ? -20.434 4.031   -16.364 1.00 31.91 ? 180 LEU B CD1   1 
ATOM   4638 C  CD2   . LEU B 1 201 ? -18.355 3.027   -15.396 1.00 29.88 ? 180 LEU B CD2   1 
ATOM   4639 N  N     . SER B 1 202 ? -19.795 -1.774  -16.450 1.00 29.22 ? 181 SER B N     1 
ATOM   4640 C  CA    . SER B 1 202 ? -20.806 -2.860  -16.504 1.00 27.20 ? 181 SER B CA    1 
ATOM   4641 C  C     . SER B 1 202 ? -22.188 -2.200  -16.451 1.00 26.27 ? 181 SER B C     1 
ATOM   4642 O  O     . SER B 1 202 ? -22.354 -1.179  -15.702 1.00 22.77 ? 181 SER B O     1 
ATOM   4643 C  CB    . SER B 1 202 ? -20.611 -3.907  -15.400 1.00 25.63 ? 181 SER B CB    1 
ATOM   4644 O  OG    . SER B 1 202 ? -21.128 -3.467  -14.159 1.00 26.25 ? 181 SER B OG    1 
ATOM   4645 N  N     . LEU B 1 203 ? -23.129 -2.727  -17.234 1.00 26.00 ? 182 LEU B N     1 
ATOM   4646 C  CA    . LEU B 1 203 ? -24.525 -2.235  -17.235 1.00 26.18 ? 182 LEU B CA    1 
ATOM   4647 C  C     . LEU B 1 203 ? -25.043 -2.377  -15.805 1.00 27.84 ? 182 LEU B C     1 
ATOM   4648 O  O     . LEU B 1 203 ? -25.648 -1.370  -15.295 1.00 29.42 ? 182 LEU B O     1 
ATOM   4649 C  CB    . LEU B 1 203 ? -25.344 -3.024  -18.267 1.00 29.96 ? 182 LEU B CB    1 
ATOM   4650 C  CG    . LEU B 1 203 ? -26.872 -3.010  -18.106 1.00 30.66 ? 182 LEU B CG    1 
ATOM   4651 C  CD1   . LEU B 1 203 ? -27.490 -1.746  -18.702 1.00 29.90 ? 182 LEU B CD1   1 
ATOM   4652 C  CD2   . LEU B 1 203 ? -27.480 -4.252  -18.746 1.00 29.68 ? 182 LEU B CD2   1 
ATOM   4653 N  N     . LEU B 1 204 ? -24.727 -3.512  -15.151 1.00 24.95 ? 183 LEU B N     1 
ATOM   4654 C  CA    . LEU B 1 204 ? -25.222 -3.857  -13.793 1.00 24.16 ? 183 LEU B CA    1 
ATOM   4655 C  C     . LEU B 1 204 ? -24.793 -2.749  -12.825 1.00 25.05 ? 183 LEU B C     1 
ATOM   4656 O  O     . LEU B 1 204 ? -25.673 -2.327  -11.961 1.00 21.51 ? 183 LEU B O     1 
ATOM   4657 C  CB    . LEU B 1 204 ? -24.732 -5.241  -13.341 1.00 24.99 ? 183 LEU B CB    1 
ATOM   4658 C  CG    . LEU B 1 204 ? -25.079 -5.628  -11.898 1.00 30.46 ? 183 LEU B CG    1 
ATOM   4659 C  CD1   . LEU B 1 204 ? -26.587 -5.611  -11.663 1.00 30.83 ? 183 LEU B CD1   1 
ATOM   4660 C  CD2   . LEU B 1 204 ? -24.514 -7.007  -11.518 1.00 33.76 ? 183 LEU B CD2   1 
ATOM   4661 N  N     . HIS B 1 205 ? -23.515 -2.329  -12.909 1.00 22.49 ? 184 HIS B N     1 
ATOM   4662 C  CA    . HIS B 1 205 ? -22.960 -1.245  -12.064 1.00 24.07 ? 184 HIS B CA    1 
ATOM   4663 C  C     . HIS B 1 205 ? -23.714 0.062   -12.315 1.00 26.35 ? 184 HIS B C     1 
ATOM   4664 O  O     . HIS B 1 205 ? -23.980 0.762   -11.336 1.00 23.67 ? 184 HIS B O     1 
ATOM   4665 C  CB    . HIS B 1 205 ? -21.477 -1.025  -12.326 1.00 25.05 ? 184 HIS B CB    1 
ATOM   4666 C  CG    . HIS B 1 205 ? -20.993 0.232   -11.711 1.00 24.19 ? 184 HIS B CG    1 
ATOM   4667 N  ND1   . HIS B 1 205 ? -20.788 0.348   -10.366 1.00 23.93 ? 184 HIS B ND1   1 
ATOM   4668 C  CD2   . HIS B 1 205 ? -20.687 1.429   -12.257 1.00 25.33 ? 184 HIS B CD2   1 
ATOM   4669 C  CE1   . HIS B 1 205 ? -20.368 1.570   -10.100 1.00 24.53 ? 184 HIS B CE1   1 
ATOM   4670 N  NE2   . HIS B 1 205 ? -20.320 2.257   -11.240 1.00 23.51 ? 184 HIS B NE2   1 
ATOM   4671 N  N     . ALA B 1 206 ? -24.005 0.394   -13.587 1.00 29.16 ? 185 ALA B N     1 
ATOM   4672 C  CA    . ALA B 1 206 ? -24.702 1.645   -13.980 1.00 29.95 ? 185 ALA B CA    1 
ATOM   4673 C  C     . ALA B 1 206 ? -26.163 1.593   -13.495 1.00 33.69 ? 185 ALA B C     1 
ATOM   4674 O  O     . ALA B 1 206 ? -26.686 2.626   -12.995 1.00 36.19 ? 185 ALA B O     1 
ATOM   4675 C  CB    . ALA B 1 206 ? -24.626 1.846   -15.473 1.00 31.18 ? 185 ALA B CB    1 
ATOM   4676 N  N     . ALA B 1 207 ? -26.811 0.429   -13.633 1.00 30.77 ? 186 ALA B N     1 
ATOM   4677 C  CA    . ALA B 1 207 ? -28.214 0.219   -13.212 1.00 28.36 ? 186 ALA B CA    1 
ATOM   4678 C  C     . ALA B 1 207 ? -28.307 0.405   -11.693 1.00 27.83 ? 186 ALA B C     1 
ATOM   4679 O  O     . ALA B 1 207 ? -29.261 1.053   -11.263 1.00 24.77 ? 186 ALA B O     1 
ATOM   4680 C  CB    . ALA B 1 207 ? -28.711 -1.137  -13.645 1.00 28.01 ? 186 ALA B CB    1 
ATOM   4681 N  N     . HIS B 1 208 ? -27.353 -0.145  -10.925 1.00 26.44 ? 187 HIS B N     1 
ATOM   4682 C  CA    . HIS B 1 208 ? -27.329 -0.033  -9.444  1.00 27.47 ? 187 HIS B CA    1 
ATOM   4683 C  C     . HIS B 1 208 ? -27.185 1.444   -9.076  1.00 28.69 ? 187 HIS B C     1 
ATOM   4684 O  O     . HIS B 1 208 ? -27.886 1.912   -8.115  1.00 28.36 ? 187 HIS B O     1 
ATOM   4685 C  CB    . HIS B 1 208 ? -26.216 -0.860  -8.807  1.00 28.41 ? 187 HIS B CB    1 
ATOM   4686 C  CG    . HIS B 1 208 ? -25.821 -0.442  -7.412  1.00 30.48 ? 187 HIS B CG    1 
ATOM   4687 N  ND1   . HIS B 1 208 ? -26.224 -1.142  -6.267  1.00 27.83 ? 187 HIS B ND1   1 
ATOM   4688 C  CD2   . HIS B 1 208 ? -25.025 0.551   -6.974  1.00 28.79 ? 187 HIS B CD2   1 
ATOM   4689 C  CE1   . HIS B 1 208 ? -25.691 -0.602  -5.204  1.00 27.55 ? 187 HIS B CE1   1 
ATOM   4690 N  NE2   . HIS B 1 208 ? -24.950 0.440   -5.604  1.00 33.85 ? 187 HIS B NE2   1 
ATOM   4691 N  N     . TYR B 1 209 ? -26.296 2.137   -9.789  1.00 25.43 ? 188 TYR B N     1 
ATOM   4692 C  CA    . TYR B 1 209 ? -25.934 3.537   -9.479  1.00 26.37 ? 188 TYR B CA    1 
ATOM   4693 C  C     . TYR B 1 209 ? -27.172 4.410   -9.643  1.00 25.55 ? 188 TYR B C     1 
ATOM   4694 O  O     . TYR B 1 209 ? -27.415 5.246   -8.787  1.00 21.16 ? 188 TYR B O     1 
ATOM   4695 C  CB    . TYR B 1 209 ? -24.839 4.034   -10.416 1.00 27.02 ? 188 TYR B CB    1 
ATOM   4696 C  CG    . TYR B 1 209 ? -24.056 5.187   -9.853  1.00 24.70 ? 188 TYR B CG    1 
ATOM   4697 C  CD1   . TYR B 1 209 ? -24.408 6.497   -10.131 1.00 22.90 ? 188 TYR B CD1   1 
ATOM   4698 C  CD2   . TYR B 1 209 ? -22.945 4.954   -9.052  1.00 25.94 ? 188 TYR B CD2   1 
ATOM   4699 C  CE1   . TYR B 1 209 ? -23.667 7.558   -9.632  1.00 23.06 ? 188 TYR B CE1   1 
ATOM   4700 C  CE2   . TYR B 1 209 ? -22.168 6.001   -8.574  1.00 25.29 ? 188 TYR B CE2   1 
ATOM   4701 C  CZ    . TYR B 1 209 ? -22.546 7.304   -8.862  1.00 24.82 ? 188 TYR B CZ    1 
ATOM   4702 O  OH    . TYR B 1 209 ? -21.816 8.334   -8.364  1.00 26.37 ? 188 TYR B OH    1 
ATOM   4703 N  N     . VAL B 1 210 ? -27.909 4.157   -10.735 1.00 28.28 ? 189 VAL B N     1 
ATOM   4704 C  CA    . VAL B 1 210 ? -29.197 4.811   -11.102 1.00 30.45 ? 189 VAL B CA    1 
ATOM   4705 C  C     . VAL B 1 210 ? -30.281 4.451   -10.064 1.00 31.44 ? 189 VAL B C     1 
ATOM   4706 O  O     . VAL B 1 210 ? -30.886 5.396   -9.537  1.00 35.49 ? 189 VAL B O     1 
ATOM   4707 C  CB    . VAL B 1 210 ? -29.601 4.493   -12.558 1.00 29.13 ? 189 VAL B CB    1 
ATOM   4708 C  CG1   . VAL B 1 210 ? -31.017 4.981   -12.868 1.00 30.79 ? 189 VAL B CG1   1 
ATOM   4709 C  CG2   . VAL B 1 210 ? -28.612 5.110   -13.548 1.00 27.92 ? 189 VAL B CG2   1 
ATOM   4710 N  N     . HIS B 1 211 ? -30.531 3.177   -9.734  1.00 32.13 ? 190 HIS B N     1 
ATOM   4711 C  CA    . HIS B 1 211 ? -31.507 2.808   -8.662  1.00 30.01 ? 190 HIS B CA    1 
ATOM   4712 C  C     . HIS B 1 211 ? -31.153 3.585   -7.377  1.00 30.53 ? 190 HIS B C     1 
ATOM   4713 O  O     . HIS B 1 211 ? -32.044 4.267   -6.854  1.00 31.66 ? 190 HIS B O     1 
ATOM   4714 C  CB    . HIS B 1 211 ? -31.605 1.279   -8.474  1.00 32.34 ? 190 HIS B CB    1 
ATOM   4715 C  CG    . HIS B 1 211 ? -32.791 0.821   -7.671  1.00 36.15 ? 190 HIS B CG    1 
ATOM   4716 N  ND1   . HIS B 1 211 ? -32.920 -0.483  -7.212  1.00 32.19 ? 190 HIS B ND1   1 
ATOM   4717 C  CD2   . HIS B 1 211 ? -33.881 1.493   -7.209  1.00 35.50 ? 190 HIS B CD2   1 
ATOM   4718 C  CE1   . HIS B 1 211 ? -34.036 -0.595  -6.515  1.00 35.01 ? 190 HIS B CE1   1 
ATOM   4719 N  NE2   . HIS B 1 211 ? -34.642 0.609   -6.486  1.00 35.97 ? 190 HIS B NE2   1 
ATOM   4720 N  N     . SER B 1 212 ? -29.886 3.579   -6.940  1.00 27.30 ? 191 SER B N     1 
ATOM   4721 C  CA    . SER B 1 212 ? -29.376 4.215   -5.689  1.00 25.44 ? 191 SER B CA    1 
ATOM   4722 C  C     . SER B 1 212 ? -29.716 5.715   -5.550  1.00 26.47 ? 191 SER B C     1 
ATOM   4723 O  O     . SER B 1 212 ? -29.744 6.206   -4.415  1.00 27.03 ? 191 SER B O     1 
ATOM   4724 C  CB    . SER B 1 212 ? -27.891 4.061   -5.657  1.00 23.57 ? 191 SER B CB    1 
ATOM   4725 O  OG    . SER B 1 212 ? -27.360 4.666   -4.499  1.00 20.59 ? 191 SER B OG    1 
ATOM   4726 N  N     . ALA B 1 213 ? -29.777 6.431   -6.674  1.00 27.40 ? 192 ALA B N     1 
ATOM   4727 C  CA    . ALA B 1 213 ? -30.102 7.869   -6.824  1.00 27.70 ? 192 ALA B CA    1 
ATOM   4728 C  C     . ALA B 1 213 ? -31.620 8.109   -6.903  1.00 30.16 ? 192 ALA B C     1 
ATOM   4729 O  O     . ALA B 1 213 ? -32.049 9.246   -6.622  1.00 29.30 ? 192 ALA B O     1 
ATOM   4730 C  CB    . ALA B 1 213 ? -29.446 8.357   -8.095  1.00 25.71 ? 192 ALA B CB    1 
ATOM   4731 N  N     . GLY B 1 214 ? -32.381 7.124   -7.405  1.00 28.74 ? 193 GLY B N     1 
ATOM   4732 C  CA    . GLY B 1 214 ? -33.817 7.263   -7.702  1.00 29.98 ? 193 GLY B CA    1 
ATOM   4733 C  C     . GLY B 1 214 ? -34.058 7.695   -9.143  1.00 30.01 ? 193 GLY B C     1 
ATOM   4734 O  O     . GLY B 1 214 ? -35.113 8.278   -9.415  1.00 26.59 ? 193 GLY B O     1 
ATOM   4735 N  N     . GLY B 1 215 ? -33.096 7.475   -10.038 1.00 29.96 ? 194 GLY B N     1 
ATOM   4736 C  CA    . GLY B 1 215 ? -33.345 7.553   -11.493 1.00 32.75 ? 194 GLY B CA    1 
ATOM   4737 C  C     . GLY B 1 215 ? -32.424 8.526   -12.214 1.00 31.03 ? 194 GLY B C     1 
ATOM   4738 O  O     . GLY B 1 215 ? -31.652 9.245   -11.561 1.00 27.84 ? 194 GLY B O     1 
ATOM   4739 N  N     . TRP B 1 216 ? -32.508 8.498   -13.538 1.00 31.08 ? 195 TRP B N     1 
ATOM   4740 C  CA    . TRP B 1 216 ? -31.688 9.292   -14.483 1.00 32.26 ? 195 TRP B CA    1 
ATOM   4741 C  C     . TRP B 1 216 ? -31.964 10.791  -14.291 1.00 33.99 ? 195 TRP B C     1 
ATOM   4742 O  O     . TRP B 1 216 ? -30.981 11.552  -14.392 1.00 34.39 ? 195 TRP B O     1 
ATOM   4743 C  CB    . TRP B 1 216 ? -31.967 8.811   -15.915 1.00 33.09 ? 195 TRP B CB    1 
ATOM   4744 C  CG    . TRP B 1 216 ? -30.888 9.162   -16.895 1.00 35.00 ? 195 TRP B CG    1 
ATOM   4745 C  CD1   . TRP B 1 216 ? -31.015 9.899   -18.035 1.00 34.14 ? 195 TRP B CD1   1 
ATOM   4746 C  CD2   . TRP B 1 216 ? -29.500 8.811   -16.798 1.00 36.64 ? 195 TRP B CD2   1 
ATOM   4747 N  NE1   . TRP B 1 216 ? -29.802 10.037  -18.647 1.00 36.20 ? 195 TRP B NE1   1 
ATOM   4748 C  CE2   . TRP B 1 216 ? -28.853 9.384   -17.912 1.00 35.40 ? 195 TRP B CE2   1 
ATOM   4749 C  CE3   . TRP B 1 216 ? -28.734 8.094   -15.865 1.00 40.23 ? 195 TRP B CE3   1 
ATOM   4750 C  CZ2   . TRP B 1 216 ? -27.486 9.237   -18.137 1.00 34.42 ? 195 TRP B CZ2   1 
ATOM   4751 C  CZ3   . TRP B 1 216 ? -27.379 7.950   -16.091 1.00 38.15 ? 195 TRP B CZ3   1 
ATOM   4752 C  CH2   . TRP B 1 216 ? -26.768 8.519   -17.208 1.00 37.55 ? 195 TRP B CH2   1 
ATOM   4753 N  N     . SER B 1 217 ? -33.226 11.195  -14.014 1.00 33.69 ? 196 SER B N     1 
ATOM   4754 C  CA    . SER B 1 217 ? -33.642 12.606  -13.728 1.00 34.09 ? 196 SER B CA    1 
ATOM   4755 C  C     . SER B 1 217 ? -32.970 13.104  -12.446 1.00 31.46 ? 196 SER B C     1 
ATOM   4756 O  O     . SER B 1 217 ? -32.580 14.292  -12.388 1.00 30.00 ? 196 SER B O     1 
ATOM   4757 C  CB    . SER B 1 217 ? -35.150 12.789  -13.626 1.00 34.47 ? 196 SER B CB    1 
ATOM   4758 O  OG    . SER B 1 217 ? -35.743 12.835  -14.916 1.00 34.56 ? 196 SER B OG    1 
ATOM   4759 N  N     . LYS B 1 218 ? -32.849 12.231  -11.453 1.00 31.35 ? 197 LYS B N     1 
ATOM   4760 C  CA    . LYS B 1 218 ? -32.268 12.575  -10.135 1.00 34.11 ? 197 LYS B CA    1 
ATOM   4761 C  C     . LYS B 1 218 ? -30.795 12.906  -10.361 1.00 29.86 ? 197 LYS B C     1 
ATOM   4762 O  O     . LYS B 1 218 ? -30.307 13.841  -9.737  1.00 28.98 ? 197 LYS B O     1 
ATOM   4763 C  CB    . LYS B 1 218 ? -32.470 11.422  -9.141  1.00 38.71 ? 197 LYS B CB    1 
ATOM   4764 C  CG    . LYS B 1 218 ? -33.723 11.531  -8.274  1.00 42.20 ? 197 LYS B CG    1 
ATOM   4765 C  CD    . LYS B 1 218 ? -33.615 12.597  -7.185  1.00 42.76 ? 197 LYS B CD    1 
ATOM   4766 C  CE    . LYS B 1 218 ? -34.899 13.358  -6.914  1.00 45.18 ? 197 LYS B CE    1 
ATOM   4767 N  NZ    . LYS B 1 218 ? -35.802 12.606  -6.007  1.00 46.18 ? 197 LYS B NZ    1 
ATOM   4768 N  N     . LEU B 1 219 ? -30.148 12.147  -11.243 1.00 29.77 ? 198 LEU B N     1 
ATOM   4769 C  CA    . LEU B 1 219 ? -28.694 12.240  -11.543 1.00 32.86 ? 198 LEU B CA    1 
ATOM   4770 C  C     . LEU B 1 219 ? -28.394 13.439  -12.447 1.00 31.08 ? 198 LEU B C     1 
ATOM   4771 O  O     . LEU B 1 219 ? -27.393 14.126  -12.183 1.00 29.11 ? 198 LEU B O     1 
ATOM   4772 C  CB    . LEU B 1 219 ? -28.262 10.944  -12.229 1.00 33.72 ? 198 LEU B CB    1 
ATOM   4773 C  CG    . LEU B 1 219 ? -28.180 9.738   -11.300 1.00 34.29 ? 198 LEU B CG    1 
ATOM   4774 C  CD1   . LEU B 1 219 ? -27.928 8.458   -12.083 1.00 32.99 ? 198 LEU B CD1   1 
ATOM   4775 C  CD2   . LEU B 1 219 ? -27.126 9.959   -10.229 1.00 31.32 ? 198 LEU B CD2   1 
ATOM   4776 N  N     . THR B 1 220 ? -29.222 13.664  -13.471 1.00 31.26 ? 199 THR B N     1 
ATOM   4777 C  CA    . THR B 1 220 ? -28.949 14.630  -14.568 1.00 33.81 ? 199 THR B CA    1 
ATOM   4778 C  C     . THR B 1 220 ? -29.680 15.971  -14.382 1.00 33.10 ? 199 THR B C     1 
ATOM   4779 O  O     . THR B 1 220 ? -29.199 16.923  -14.953 1.00 34.11 ? 199 THR B O     1 
ATOM   4780 C  CB    . THR B 1 220 ? -29.284 13.987  -15.919 1.00 33.06 ? 199 THR B CB    1 
ATOM   4781 O  OG1   . THR B 1 220 ? -30.650 13.564  -15.897 1.00 33.55 ? 199 THR B OG1   1 
ATOM   4782 C  CG2   . THR B 1 220 ? -28.362 12.825  -16.216 1.00 29.34 ? 199 THR B CG2   1 
ATOM   4783 N  N     . ASP B 1 221 ? -30.810 16.058  -13.671 1.00 37.40 ? 200 ASP B N     1 
ATOM   4784 C  CA    . ASP B 1 221 ? -31.573 17.339  -13.514 1.00 38.93 ? 200 ASP B CA    1 
ATOM   4785 C  C     . ASP B 1 221 ? -30.760 18.276  -12.616 1.00 34.68 ? 200 ASP B C     1 
ATOM   4786 O  O     . ASP B 1 221 ? -29.959 17.762  -11.831 1.00 35.91 ? 200 ASP B O     1 
ATOM   4787 C  CB    . ASP B 1 221 ? -32.993 17.173  -12.936 1.00 39.97 ? 200 ASP B CB    1 
ATOM   4788 C  CG    . ASP B 1 221 ? -34.041 16.581  -13.879 1.00 42.30 ? 200 ASP B CG    1 
ATOM   4789 O  OD1   . ASP B 1 221 ? -33.703 16.291  -15.043 1.00 45.45 ? 200 ASP B OD1   1 
ATOM   4790 O  OD2   . ASP B 1 221 ? -35.193 16.407  -13.444 1.00 41.14 ? 200 ASP B OD2   1 
ATOM   4791 N  N     . THR B 1 222 ? -30.948 19.587  -12.778 1.00 37.08 ? 201 THR B N     1 
ATOM   4792 C  CA    . THR B 1 222 ? -30.227 20.687  -12.070 1.00 46.94 ? 201 THR B CA    1 
ATOM   4793 C  C     . THR B 1 222 ? -31.192 21.446  -11.139 1.00 52.43 ? 201 THR B C     1 
ATOM   4794 O  O     . THR B 1 222 ? -30.929 22.655  -10.863 1.00 58.06 ? 201 THR B O     1 
ATOM   4795 C  CB    . THR B 1 222 ? -29.557 21.609  -13.101 1.00 46.94 ? 201 THR B CB    1 
ATOM   4796 O  OG1   . THR B 1 222 ? -28.467 20.849  -13.627 1.00 50.21 ? 201 THR B OG1   1 
ATOM   4797 C  CG2   . THR B 1 222 ? -29.054 22.927  -12.548 1.00 49.06 ? 201 THR B CG2   1 
ATOM   4798 N  N     . GLU B 1 223 ? -32.233 20.763  -10.643 1.00 44.40 ? 202 GLU B N     1 
ATOM   4799 C  CA    . GLU B 1 223 ? -33.477 21.362  -10.080 1.00 45.92 ? 202 GLU B CA    1 
ATOM   4800 C  C     . GLU B 1 223 ? -34.528 20.253  -10.052 1.00 41.88 ? 202 GLU B C     1 
ATOM   4801 O  O     . GLU B 1 223 ? -34.900 19.732  -11.138 1.00 37.16 ? 202 GLU B O     1 
ATOM   4802 C  CB    . GLU B 1 223 ? -33.959 22.609  -10.840 1.00 45.07 ? 202 GLU B CB    1 
ATOM   4803 C  CG    . GLU B 1 223 ? -34.977 22.371  -11.946 1.00 48.16 ? 202 GLU B CG    1 
ATOM   4804 C  CD    . GLU B 1 223 ? -36.442 22.407  -11.528 1.00 55.93 ? 202 GLU B CD    1 
ATOM   4805 O  OE1   . GLU B 1 223 ? -36.824 23.278  -10.699 1.00 60.97 ? 202 GLU B OE1   1 
ATOM   4806 O  OE2   . GLU B 1 223 ? -37.206 21.577  -12.040 1.00 51.70 ? 202 GLU B OE2   1 
ATOM   4807 N  N     . GLY B 1 224 ? -34.947 19.891  -8.841  1.00 42.53 ? 203 GLY B N     1 
ATOM   4808 C  CA    . GLY B 1 224 ? -35.553 18.581  -8.547  1.00 45.02 ? 203 GLY B CA    1 
ATOM   4809 C  C     . GLY B 1 224 ? -34.531 17.453  -8.667  1.00 40.17 ? 203 GLY B C     1 
ATOM   4810 O  O     . GLY B 1 224 ? -34.966 16.287  -8.746  1.00 38.06 ? 203 GLY B O     1 
ATOM   4811 N  N     . GLY B 1 225 ? -33.230 17.782  -8.672  1.00 36.19 ? 204 GLY B N     1 
ATOM   4812 C  CA    . GLY B 1 225 ? -32.140 16.827  -8.986  1.00 37.96 ? 204 GLY B CA    1 
ATOM   4813 C  C     . GLY B 1 225 ? -30.835 17.148  -8.280  1.00 32.91 ? 204 GLY B C     1 
ATOM   4814 O  O     . GLY B 1 225 ? -30.789 18.138  -7.518  1.00 32.35 ? 204 GLY B O     1 
ATOM   4815 N  N     . ALA B 1 226 ? -29.803 16.339  -8.518  1.00 31.87 ? 205 ALA B N     1 
ATOM   4816 C  CA    . ALA B 1 226 ? -28.511 16.360  -7.781  1.00 33.57 ? 205 ALA B CA    1 
ATOM   4817 C  C     . ALA B 1 226 ? -27.775 17.708  -7.957  1.00 33.24 ? 205 ALA B C     1 
ATOM   4818 O  O     . ALA B 1 226 ? -26.901 18.011  -7.117  1.00 32.40 ? 205 ALA B O     1 
ATOM   4819 C  CB    . ALA B 1 226 ? -27.650 15.186  -8.227  1.00 33.85 ? 205 ALA B CB    1 
ATOM   4820 N  N     . GLN B 1 227 ? -28.106 18.509  -8.983  1.00 33.47 ? 206 GLN B N     1 
ATOM   4821 C  CA    . GLN B 1 227 ? -27.449 19.825  -9.240  1.00 31.61 ? 206 GLN B CA    1 
ATOM   4822 C  C     . GLN B 1 227 ? -28.377 21.013  -8.897  1.00 33.25 ? 206 GLN B C     1 
ATOM   4823 O  O     . GLN B 1 227 ? -28.200 22.095  -9.486  1.00 35.44 ? 206 GLN B O     1 
ATOM   4824 C  CB    . GLN B 1 227 ? -26.965 19.847  -10.691 1.00 29.14 ? 206 GLN B CB    1 
ATOM   4825 C  CG    . GLN B 1 227 ? -25.684 19.030  -10.926 1.00 29.72 ? 206 GLN B CG    1 
ATOM   4826 C  CD    . GLN B 1 227 ? -25.938 17.555  -11.165 1.00 27.87 ? 206 GLN B CD    1 
ATOM   4827 O  OE1   . GLN B 1 227 ? -26.679 17.171  -12.090 1.00 25.32 ? 206 GLN B OE1   1 
ATOM   4828 N  NE2   . GLN B 1 227 ? -25.389 16.728  -10.281 1.00 26.02 ? 206 GLN B NE2   1 
ATOM   4829 N  N     . GLN B 1 228 ? -29.343 20.861  -7.985  1.00 33.00 ? 207 GLN B N     1 
ATOM   4830 C  CA    . GLN B 1 228 ? -30.294 21.959  -7.656  1.00 29.68 ? 207 GLN B CA    1 
ATOM   4831 C  C     . GLN B 1 228 ? -29.605 23.040  -6.803  1.00 29.24 ? 207 GLN B C     1 
ATOM   4832 O  O     . GLN B 1 228 ? -29.766 24.253  -7.120  1.00 28.07 ? 207 GLN B O     1 
ATOM   4833 C  CB    . GLN B 1 228 ? -31.531 21.405  -6.947  1.00 34.44 ? 207 GLN B CB    1 
ATOM   4834 C  CG    . GLN B 1 228 ? -32.613 22.461  -6.687  1.00 36.60 ? 207 GLN B CG    1 
ATOM   4835 C  CD    . GLN B 1 228 ? -33.868 21.905  -6.065  1.00 34.38 ? 207 GLN B CD    1 
ATOM   4836 O  OE1   . GLN B 1 228 ? -34.743 21.370  -6.751  1.00 33.45 ? 207 GLN B OE1   1 
ATOM   4837 N  NE2   . GLN B 1 228 ? -33.975 22.069  -4.758  1.00 32.94 ? 207 GLN B NE2   1 
ATOM   4838 N  N     . ASP B 1 229 ? -28.853 22.647  -5.766  1.00 30.97 ? 208 ASP B N     1 
ATOM   4839 C  CA    . ASP B 1 229 ? -28.486 23.559  -4.647  1.00 31.81 ? 208 ASP B CA    1 
ATOM   4840 C  C     . ASP B 1 229 ? -26.987 23.513  -4.363  1.00 30.26 ? 208 ASP B C     1 
ATOM   4841 O  O     . ASP B 1 229 ? -26.367 22.453  -4.504  1.00 32.35 ? 208 ASP B O     1 
ATOM   4842 C  CB    . ASP B 1 229 ? -29.347 23.252  -3.407  1.00 32.57 ? 208 ASP B CB    1 
ATOM   4843 C  CG    . ASP B 1 229 ? -30.826 23.632  -3.574  1.00 33.32 ? 208 ASP B CG    1 
ATOM   4844 O  OD1   . ASP B 1 229 ? -31.138 24.840  -3.493  1.00 28.20 ? 208 ASP B OD1   1 
ATOM   4845 O  OD2   . ASP B 1 229 ? -31.670 22.703  -3.767  1.00 35.01 ? 208 ASP B OD2   1 
ATOM   4846 N  N     . ARG B 1 230 ? -26.444 24.652  -3.946  1.00 32.58 ? 209 ARG B N     1 
ATOM   4847 C  CA    . ARG B 1 230 ? -25.033 24.839  -3.516  1.00 33.33 ? 209 ARG B CA    1 
ATOM   4848 C  C     . ARG B 1 230 ? -24.989 25.127  -2.005  1.00 33.51 ? 209 ARG B C     1 
ATOM   4849 O  O     . ARG B 1 230 ? -26.053 25.431  -1.410  1.00 26.76 ? 209 ARG B O     1 
ATOM   4850 C  CB    . ARG B 1 230 ? -24.416 26.043  -4.238  1.00 36.15 ? 209 ARG B CB    1 
ATOM   4851 C  CG    . ARG B 1 230 ? -24.113 25.864  -5.725  1.00 36.06 ? 209 ARG B CG    1 
ATOM   4852 C  CD    . ARG B 1 230 ? -22.831 25.084  -6.032  1.00 35.43 ? 209 ARG B CD    1 
ATOM   4853 N  NE    . ARG B 1 230 ? -21.569 25.382  -5.316  1.00 34.47 ? 209 ARG B NE    1 
ATOM   4854 C  CZ    . ARG B 1 230 ? -20.503 26.056  -5.815  1.00 32.37 ? 209 ARG B CZ    1 
ATOM   4855 N  NH1   . ARG B 1 230 ? -20.529 26.637  -7.010  1.00 28.08 ? 209 ARG B NH1   1 
ATOM   4856 N  NH2   . ARG B 1 230 ? -19.416 26.186  -5.074  1.00 31.64 ? 209 ARG B NH2   1 
ATOM   4857 N  N     . LEU B 1 231 ? -23.796 25.148  -1.416  1.00 34.38 ? 210 LEU B N     1 
ATOM   4858 C  CA    . LEU B 1 231 ? -23.651 25.452  0.028   1.00 39.78 ? 210 LEU B CA    1 
ATOM   4859 C  C     . LEU B 1 231 ? -22.968 26.811  0.163   1.00 38.16 ? 210 LEU B C     1 
ATOM   4860 O  O     . LEU B 1 231 ? -21.894 26.990  -0.455  1.00 36.56 ? 210 LEU B O     1 
ATOM   4861 C  CB    . LEU B 1 231 ? -22.865 24.341  0.747   1.00 43.31 ? 210 LEU B CB    1 
ATOM   4862 C  CG    . LEU B 1 231 ? -23.555 22.975  0.915   1.00 42.63 ? 210 LEU B CG    1 
ATOM   4863 C  CD1   . LEU B 1 231 ? -24.966 23.105  1.449   1.00 42.78 ? 210 LEU B CD1   1 
ATOM   4864 C  CD2   . LEU B 1 231 ? -23.566 22.185  -0.395  1.00 46.13 ? 210 LEU B CD2   1 
ATOM   4865 N  N     . VAL B 1 232 ? -23.585 27.712  0.948   1.00 38.45 ? 211 VAL B N     1 
ATOM   4866 C  CA    . VAL B 1 232 ? -23.080 29.085  1.245   1.00 37.36 ? 211 VAL B CA    1 
ATOM   4867 C  C     . VAL B 1 232 ? -21.765 28.936  2.013   1.00 34.65 ? 211 VAL B C     1 
ATOM   4868 O  O     . VAL B 1 232 ? -21.801 28.269  3.026   1.00 43.87 ? 211 VAL B O     1 
ATOM   4869 C  CB    . VAL B 1 232 ? -24.102 29.926  2.032   1.00 36.62 ? 211 VAL B CB    1 
ATOM   4870 C  CG1   . VAL B 1 232 ? -23.524 31.292  2.421   1.00 35.92 ? 211 VAL B CG1   1 
ATOM   4871 C  CG2   . VAL B 1 232 ? -25.397 30.085  1.251   1.00 38.19 ? 211 VAL B CG2   1 
ATOM   4872 N  N     . GLY B 1 233 ? -20.658 29.489  1.510   1.00 31.95 ? 212 GLY B N     1 
ATOM   4873 C  CA    . GLY B 1 233 ? -19.321 29.331  2.102   1.00 33.63 ? 212 GLY B CA    1 
ATOM   4874 C  C     . GLY B 1 233 ? -18.609 28.092  1.591   1.00 34.47 ? 212 GLY B C     1 
ATOM   4875 O  O     . GLY B 1 233 ? -17.401 27.926  1.921   1.00 33.70 ? 212 GLY B O     1 
ATOM   4876 N  N     . GLY B 1 234 ? -19.308 27.269  0.799   1.00 36.81 ? 213 GLY B N     1 
ATOM   4877 C  CA    . GLY B 1 234 ? -18.759 26.037  0.207   1.00 43.22 ? 213 GLY B CA    1 
ATOM   4878 C  C     . GLY B 1 234 ? -18.735 24.860  1.187   1.00 44.17 ? 213 GLY B C     1 
ATOM   4879 O  O     . GLY B 1 234 ? -19.173 25.019  2.345   1.00 46.54 ? 213 GLY B O     1 
ATOM   4880 N  N     . VAL B 1 235 ? -18.223 23.717  0.718   1.00 39.77 ? 214 VAL B N     1 
ATOM   4881 C  CA    . VAL B 1 235 ? -18.460 22.357  1.274   1.00 35.56 ? 214 VAL B CA    1 
ATOM   4882 C  C     . VAL B 1 235 ? -17.377 22.017  2.302   1.00 32.64 ? 214 VAL B C     1 
ATOM   4883 O  O     . VAL B 1 235 ? -17.736 21.331  3.268   1.00 33.94 ? 214 VAL B O     1 
ATOM   4884 C  CB    . VAL B 1 235 ? -18.515 21.306  0.139   1.00 36.87 ? 214 VAL B CB    1 
ATOM   4885 C  CG1   . VAL B 1 235 ? -18.681 19.884  0.653   1.00 37.00 ? 214 VAL B CG1   1 
ATOM   4886 C  CG2   . VAL B 1 235 ? -19.613 21.616  -0.860  1.00 40.61 ? 214 VAL B CG2   1 
ATOM   4887 N  N     . GLN B 1 236 ? -16.114 22.408  2.107   1.00 29.79 ? 215 GLN B N     1 
ATOM   4888 C  CA    . GLN B 1 236 ? -15.025 21.992  3.040   1.00 34.85 ? 215 GLN B CA    1 
ATOM   4889 C  C     . GLN B 1 236 ? -15.374 22.482  4.456   1.00 38.53 ? 215 GLN B C     1 
ATOM   4890 O  O     . GLN B 1 236 ? -15.339 21.701  5.424   1.00 33.11 ? 215 GLN B O     1 
ATOM   4891 C  CB    . GLN B 1 236 ? -13.629 22.419  2.551   1.00 32.86 ? 215 GLN B CB    1 
ATOM   4892 C  CG    . GLN B 1 236 ? -12.546 22.263  3.613   1.00 33.88 ? 215 GLN B CG    1 
ATOM   4893 C  CD    . GLN B 1 236 ? -11.091 22.259  3.172   1.00 33.47 ? 215 GLN B CD    1 
ATOM   4894 O  OE1   . GLN B 1 236 ? -10.723 22.012  2.029   1.00 33.60 ? 215 GLN B OE1   1 
ATOM   4895 N  NE2   . GLN B 1 236 ? -10.213 22.473  4.129   1.00 33.96 ? 215 GLN B NE2   1 
ATOM   4896 N  N     . PRO B 1 237 ? -15.735 23.784  4.617   1.00 42.35 ? 216 PRO B N     1 
ATOM   4897 C  CA    . PRO B 1 237 ? -16.299 24.302  5.872   1.00 39.18 ? 216 PRO B CA    1 
ATOM   4898 C  C     . PRO B 1 237 ? -17.273 23.376  6.626   1.00 37.43 ? 216 PRO B C     1 
ATOM   4899 O  O     . PRO B 1 237 ? -17.045 23.164  7.785   1.00 38.08 ? 216 PRO B O     1 
ATOM   4900 C  CB    . PRO B 1 237 ? -17.015 25.570  5.370   1.00 40.33 ? 216 PRO B CB    1 
ATOM   4901 C  CG    . PRO B 1 237 ? -16.027 26.104  4.342   1.00 45.68 ? 216 PRO B CG    1 
ATOM   4902 C  CD    . PRO B 1 237 ? -15.549 24.857  3.613   1.00 43.88 ? 216 PRO B CD    1 
ATOM   4903 N  N     . LEU B 1 238 ? -18.310 22.850  5.964   1.00 37.32 ? 217 LEU B N     1 
ATOM   4904 C  CA    . LEU B 1 238 ? -19.369 21.985  6.573   1.00 37.58 ? 217 LEU B CA    1 
ATOM   4905 C  C     . LEU B 1 238 ? -18.751 20.722  7.193   1.00 36.00 ? 217 LEU B C     1 
ATOM   4906 O  O     . LEU B 1 238 ? -19.196 20.331  8.269   1.00 36.58 ? 217 LEU B O     1 
ATOM   4907 C  CB    . LEU B 1 238 ? -20.409 21.599  5.517   1.00 34.75 ? 217 LEU B CB    1 
ATOM   4908 C  CG    . LEU B 1 238 ? -21.437 20.566  5.971   1.00 37.40 ? 217 LEU B CG    1 
ATOM   4909 C  CD1   . LEU B 1 238 ? -22.143 21.005  7.252   1.00 37.94 ? 217 LEU B CD1   1 
ATOM   4910 C  CD2   . LEU B 1 238 ? -22.457 20.277  4.877   1.00 37.65 ? 217 LEU B CD2   1 
ATOM   4911 N  N     . ALA B 1 239 ? -17.789 20.098  6.513   1.00 40.19 ? 218 ALA B N     1 
ATOM   4912 C  CA    . ALA B 1 239 ? -16.909 19.017  7.033   1.00 38.24 ? 218 ALA B CA    1 
ATOM   4913 C  C     . ALA B 1 239 ? -15.997 19.558  8.148   1.00 37.45 ? 218 ALA B C     1 
ATOM   4914 O  O     . ALA B 1 239 ? -15.604 18.752  9.038   1.00 33.11 ? 218 ALA B O     1 
ATOM   4915 C  CB    . ALA B 1 239 ? -16.094 18.421  5.909   1.00 38.91 ? 218 ALA B CB    1 
ATOM   4916 N  N     . GLU B 1 240 ? -15.675 20.854  8.135   1.00 36.82 ? 219 GLU B N     1 
ATOM   4917 C  CA    . GLU B 1 240 ? -14.871 21.460  9.237   1.00 43.49 ? 219 GLU B CA    1 
ATOM   4918 C  C     . GLU B 1 240 ? -15.778 21.623  10.463  1.00 40.50 ? 219 GLU B C     1 
ATOM   4919 O  O     . GLU B 1 240 ? -15.284 21.457  11.602  1.00 41.28 ? 219 GLU B O     1 
ATOM   4920 C  CB    . GLU B 1 240 ? -14.166 22.747  8.782   1.00 43.48 ? 219 GLU B CB    1 
ATOM   4921 C  CG    . GLU B 1 240 ? -12.732 22.509  8.273   1.00 43.17 ? 219 GLU B CG    1 
ATOM   4922 C  CD    . GLU B 1 240 ? -12.137 23.562  7.333   1.00 44.92 ? 219 GLU B CD    1 
ATOM   4923 O  OE1   . GLU B 1 240 ? -10.890 23.560  7.175   1.00 39.62 ? 219 GLU B OE1   1 
ATOM   4924 O  OE2   . GLU B 1 240 ? -12.915 24.389  6.757   1.00 39.87 ? 219 GLU B OE2   1 
ATOM   4925 N  N     . ARG B 1 241 ? -17.070 21.860  10.238  1.00 42.54 ? 220 ARG B N     1 
ATOM   4926 C  CA    . ARG B 1 241 ? -18.083 21.977  11.331  1.00 49.53 ? 220 ARG B CA    1 
ATOM   4927 C  C     . ARG B 1 241 ? -18.434 20.594  11.913  1.00 45.80 ? 220 ARG B C     1 
ATOM   4928 O  O     . ARG B 1 241 ? -18.832 20.558  13.088  1.00 39.70 ? 220 ARG B O     1 
ATOM   4929 C  CB    . ARG B 1 241 ? -19.351 22.694  10.852  1.00 52.56 ? 220 ARG B CB    1 
ATOM   4930 C  CG    . ARG B 1 241 ? -19.204 24.206  10.772  1.00 55.40 ? 220 ARG B CG    1 
ATOM   4931 C  CD    . ARG B 1 241 ? -20.524 24.924  10.566  1.00 58.92 ? 220 ARG B CD    1 
ATOM   4932 N  NE    . ARG B 1 241 ? -20.274 26.304  10.180  1.00 61.90 ? 220 ARG B NE    1 
ATOM   4933 C  CZ    . ARG B 1 241 ? -21.212 27.223  9.973   1.00 65.54 ? 220 ARG B CZ    1 
ATOM   4934 N  NH1   . ARG B 1 241 ? -22.491 26.927  10.118  1.00 59.61 ? 220 ARG B NH1   1 
ATOM   4935 N  NH2   . ARG B 1 241 ? -20.861 28.446  9.609   1.00 69.96 ? 220 ARG B NH2   1 
ATOM   4936 N  N     . LEU B 1 242 ? -18.327 19.521  11.109  1.00 46.17 ? 221 LEU B N     1 
ATOM   4937 C  CA    . LEU B 1 242 ? -18.485 18.101  11.541  1.00 44.00 ? 221 LEU B CA    1 
ATOM   4938 C  C     . LEU B 1 242 ? -17.238 17.683  12.329  1.00 36.71 ? 221 LEU B C     1 
ATOM   4939 O  O     . LEU B 1 242 ? -17.383 16.963  13.298  1.00 38.79 ? 221 LEU B O     1 
ATOM   4940 C  CB    . LEU B 1 242 ? -18.700 17.196  10.314  1.00 42.77 ? 221 LEU B CB    1 
ATOM   4941 C  CG    . LEU B 1 242 ? -18.973 15.719  10.623  1.00 41.93 ? 221 LEU B CG    1 
ATOM   4942 C  CD1   . LEU B 1 242 ? -20.223 15.564  11.478  1.00 43.35 ? 221 LEU B CD1   1 
ATOM   4943 C  CD2   . LEU B 1 242 ? -19.137 14.903  9.352   1.00 43.60 ? 221 LEU B CD2   1 
ATOM   4944 N  N     . ALA B 1 243 ? -16.058 18.098  11.895  1.00 37.46 ? 222 ALA B N     1 
ATOM   4945 C  CA    . ALA B 1 243 ? -14.770 17.824  12.573  1.00 41.18 ? 222 ALA B CA    1 
ATOM   4946 C  C     . ALA B 1 243 ? -14.793 18.470  13.959  1.00 38.94 ? 222 ALA B C     1 
ATOM   4947 O  O     . ALA B 1 243 ? -14.447 17.784  14.927  1.00 33.66 ? 222 ALA B O     1 
ATOM   4948 C  CB    . ALA B 1 243 ? -13.609 18.336  11.747  1.00 41.91 ? 222 ALA B CB    1 
ATOM   4949 N  N     . ALA B 1 244 ? -15.245 19.723  14.048  1.00 40.63 ? 223 ALA B N     1 
ATOM   4950 C  CA    . ALA B 1 244 ? -15.215 20.534  15.294  1.00 41.91 ? 223 ALA B CA    1 
ATOM   4951 C  C     . ALA B 1 244 ? -16.098 19.919  16.400  1.00 39.80 ? 223 ALA B C     1 
ATOM   4952 O  O     . ALA B 1 244 ? -15.966 20.346  17.555  1.00 39.11 ? 223 ALA B O     1 
ATOM   4953 C  CB    . ALA B 1 244 ? -15.631 21.952  14.985  1.00 40.78 ? 223 ALA B CB    1 
ATOM   4954 N  N     . ARG B 1 245 ? -16.991 18.983  16.068  1.00 39.38 ? 224 ARG B N     1 
ATOM   4955 C  CA    . ARG B 1 245 ? -17.908 18.313  17.035  1.00 41.66 ? 224 ARG B CA    1 
ATOM   4956 C  C     . ARG B 1 245 ? -17.277 17.016  17.560  1.00 40.76 ? 224 ARG B C     1 
ATOM   4957 O  O     . ARG B 1 245 ? -17.988 16.233  18.188  1.00 43.41 ? 224 ARG B O     1 
ATOM   4958 C  CB    . ARG B 1 245 ? -19.257 18.000  16.379  1.00 43.48 ? 224 ARG B CB    1 
ATOM   4959 C  CG    . ARG B 1 245 ? -20.098 19.233  16.083  1.00 49.52 ? 224 ARG B CG    1 
ATOM   4960 C  CD    . ARG B 1 245 ? -20.510 20.063  17.300  1.00 48.39 ? 224 ARG B CD    1 
ATOM   4961 N  NE    . ARG B 1 245 ? -21.565 20.972  16.866  1.00 50.48 ? 224 ARG B NE    1 
ATOM   4962 C  CZ    . ARG B 1 245 ? -22.879 20.733  16.920  1.00 47.48 ? 224 ARG B CZ    1 
ATOM   4963 N  NH1   . ARG B 1 245 ? -23.350 19.622  17.467  1.00 49.73 ? 224 ARG B NH1   1 
ATOM   4964 N  NH2   . ARG B 1 245 ? -23.724 21.624  16.429  1.00 44.00 ? 224 ARG B NH2   1 
ATOM   4965 N  N     . LEU B 1 246 ? -15.998 16.787  17.274  1.00 44.56 ? 225 LEU B N     1 
ATOM   4966 C  CA    . LEU B 1 246 ? -15.193 15.707  17.895  1.00 48.68 ? 225 LEU B CA    1 
ATOM   4967 C  C     . LEU B 1 246 ? -14.491 16.312  19.100  1.00 47.05 ? 225 LEU B C     1 
ATOM   4968 O  O     . LEU B 1 246 ? -14.248 17.520  19.131  1.00 42.51 ? 225 LEU B O     1 
ATOM   4969 C  CB    . LEU B 1 246 ? -14.179 15.122  16.895  1.00 50.29 ? 225 LEU B CB    1 
ATOM   4970 C  CG    . LEU B 1 246 ? -14.749 14.344  15.697  1.00 49.22 ? 225 LEU B CG    1 
ATOM   4971 C  CD1   . LEU B 1 246 ? -13.651 13.507  15.059  1.00 46.78 ? 225 LEU B CD1   1 
ATOM   4972 C  CD2   . LEU B 1 246 ? -15.949 13.470  16.090  1.00 49.36 ? 225 LEU B CD2   1 
ATOM   4973 N  N     . PRO B 1 247 ? -14.198 15.485  20.129  1.00 47.32 ? 226 PRO B N     1 
ATOM   4974 C  CA    . PRO B 1 247 ? -13.287 15.883  21.198  1.00 47.93 ? 226 PRO B CA    1 
ATOM   4975 C  C     . PRO B 1 247 ? -11.987 16.495  20.642  1.00 50.72 ? 226 PRO B C     1 
ATOM   4976 O  O     . PRO B 1 247 ? -11.621 16.173  19.521  1.00 41.93 ? 226 PRO B O     1 
ATOM   4977 C  CB    . PRO B 1 247 ? -13.033 14.559  21.940  1.00 47.83 ? 226 PRO B CB    1 
ATOM   4978 C  CG    . PRO B 1 247 ? -14.311 13.759  21.730  1.00 46.61 ? 226 PRO B CG    1 
ATOM   4979 C  CD    . PRO B 1 247 ? -14.741 14.124  20.322  1.00 46.80 ? 226 PRO B CD    1 
ATOM   4980 N  N     . ASP B 1 248 ? -11.395 17.413  21.418  1.00 52.47 ? 227 ASP B N     1 
ATOM   4981 C  CA    . ASP B 1 248 ? -9.975  17.851  21.352  1.00 55.38 ? 227 ASP B CA    1 
ATOM   4982 C  C     . ASP B 1 248 ? -9.091  16.598  21.340  1.00 52.34 ? 227 ASP B C     1 
ATOM   4983 O  O     . ASP B 1 248 ? -9.276  15.752  22.240  1.00 52.04 ? 227 ASP B O     1 
ATOM   4984 C  CB    . ASP B 1 248 ? -9.620  18.756  22.546  1.00 58.87 ? 227 ASP B CB    1 
ATOM   4985 C  CG    . ASP B 1 248 ? -8.262  19.441  22.444  1.00 64.64 ? 227 ASP B CG    1 
ATOM   4986 O  OD1   . ASP B 1 248 ? -7.248  18.814  22.827  1.00 67.96 ? 227 ASP B OD1   1 
ATOM   4987 O  OD2   . ASP B 1 248 ? -8.223  20.597  21.975  1.00 64.14 ? 227 ASP B OD2   1 
ATOM   4988 N  N     . GLY B 1 249 ? -8.211  16.475  20.341  1.00 44.51 ? 228 GLY B N     1 
ATOM   4989 C  CA    . GLY B 1 249 ? -7.177  15.421  20.255  1.00 46.32 ? 228 GLY B CA    1 
ATOM   4990 C  C     . GLY B 1 249 ? -7.648  14.210  19.451  1.00 47.79 ? 228 GLY B C     1 
ATOM   4991 O  O     . GLY B 1 249 ? -6.841  13.251  19.295  1.00 43.11 ? 228 GLY B O     1 
ATOM   4992 N  N     . ALA B 1 250 ? -8.899  14.241  18.963  1.00 41.42 ? 229 ALA B N     1 
ATOM   4993 C  CA    . ALA B 1 250 ? -9.551  13.146  18.197  1.00 41.70 ? 229 ALA B CA    1 
ATOM   4994 C  C     . ALA B 1 250 ? -8.906  13.018  16.804  1.00 37.95 ? 229 ALA B C     1 
ATOM   4995 O  O     . ALA B 1 250 ? -8.647  11.901  16.356  1.00 39.34 ? 229 ALA B O     1 
ATOM   4996 C  CB    . ALA B 1 250 ? -11.043 13.403  18.112  1.00 37.30 ? 229 ALA B CB    1 
ATOM   4997 N  N     . LEU B 1 251 ? -8.607  14.152  16.171  1.00 40.14 ? 230 LEU B N     1 
ATOM   4998 C  CA    . LEU B 1 251 ? -8.127  14.270  14.767  1.00 37.61 ? 230 LEU B CA    1 
ATOM   4999 C  C     . LEU B 1 251 ? -6.608  14.517  14.752  1.00 35.74 ? 230 LEU B C     1 
ATOM   5000 O  O     . LEU B 1 251 ? -6.176  15.505  15.367  1.00 35.05 ? 230 LEU B O     1 
ATOM   5001 C  CB    . LEU B 1 251 ? -8.922  15.431  14.154  1.00 37.32 ? 230 LEU B CB    1 
ATOM   5002 C  CG    . LEU B 1 251 ? -8.702  15.743  12.673  1.00 38.58 ? 230 LEU B CG    1 
ATOM   5003 C  CD1   . LEU B 1 251 ? -9.470  14.771  11.790  1.00 37.44 ? 230 LEU B CD1   1 
ATOM   5004 C  CD2   . LEU B 1 251 ? -9.124  17.170  12.354  1.00 36.75 ? 230 LEU B CD2   1 
ATOM   5005 N  N     . ARG B 1 252 ? -5.826  13.659  14.082  1.00 35.50 ? 231 ARG B N     1 
ATOM   5006 C  CA    . ARG B 1 252 ? -4.417  13.961  13.687  1.00 37.74 ? 231 ARG B CA    1 
ATOM   5007 C  C     . ARG B 1 252 ? -4.371  14.116  12.164  1.00 38.55 ? 231 ARG B C     1 
ATOM   5008 O  O     . ARG B 1 252 ? -4.504  13.070  11.481  1.00 39.86 ? 231 ARG B O     1 
ATOM   5009 C  CB    . ARG B 1 252 ? -3.442  12.846  14.090  1.00 42.03 ? 231 ARG B CB    1 
ATOM   5010 C  CG    . ARG B 1 252 ? -3.604  12.314  15.504  1.00 46.07 ? 231 ARG B CG    1 
ATOM   5011 C  CD    . ARG B 1 252 ? -2.791  13.070  16.541  1.00 50.72 ? 231 ARG B CD    1 
ATOM   5012 N  NE    . ARG B 1 252 ? -3.566  13.285  17.769  1.00 55.59 ? 231 ARG B NE    1 
ATOM   5013 C  CZ    . ARG B 1 252 ? -3.846  12.354  18.688  1.00 53.26 ? 231 ARG B CZ    1 
ATOM   5014 N  NH1   . ARG B 1 252 ? -3.393  11.113  18.556  1.00 47.46 ? 231 ARG B NH1   1 
ATOM   5015 N  NH2   . ARG B 1 252 ? -4.572  12.681  19.749  1.00 54.32 ? 231 ARG B NH2   1 
ATOM   5016 N  N     . LEU B 1 253 ? -4.210  15.345  11.639  1.00 37.57 ? 232 LEU B N     1 
ATOM   5017 C  CA    . LEU B 1 253 ? -3.950  15.590  10.192  1.00 34.00 ? 232 LEU B CA    1 
ATOM   5018 C  C     . LEU B 1 253 ? -2.489  15.234  9.909   1.00 35.62 ? 232 LEU B C     1 
ATOM   5019 O  O     . LEU B 1 253 ? -1.777  14.911  10.886  1.00 35.12 ? 232 LEU B O     1 
ATOM   5020 C  CB    . LEU B 1 253 ? -4.228  17.054  9.844   1.00 33.68 ? 232 LEU B CB    1 
ATOM   5021 C  CG    . LEU B 1 253 ? -5.601  17.553  10.246  1.00 32.44 ? 232 LEU B CG    1 
ATOM   5022 C  CD1   . LEU B 1 253 ? -5.625  19.075  10.294  1.00 32.00 ? 232 LEU B CD1   1 
ATOM   5023 C  CD2   . LEU B 1 253 ? -6.676  16.980  9.312   1.00 30.77 ? 232 LEU B CD2   1 
ATOM   5024 N  N     . SER B 1 254 ? -2.065  15.263  8.634   1.00 37.52 ? 233 SER B N     1 
ATOM   5025 C  CA    . SER B 1 254 ? -0.682  14.922  8.177   1.00 36.03 ? 233 SER B CA    1 
ATOM   5026 C  C     . SER B 1 254 ? -0.217  13.598  8.809   1.00 34.24 ? 233 SER B C     1 
ATOM   5027 O  O     . SER B 1 254 ? 0.997   13.408  9.036   1.00 32.22 ? 233 SER B O     1 
ATOM   5028 C  CB    . SER B 1 254 ? 0.254   16.061  8.446   1.00 36.14 ? 233 SER B CB    1 
ATOM   5029 O  OG    . SER B 1 254 ? -0.321  17.271  7.938   1.00 40.76 ? 233 SER B OG    1 
ATOM   5030 N  N     . THR B 1 255 ? -1.173  12.688  9.011   1.00 35.11 ? 234 THR B N     1 
ATOM   5031 C  CA    . THR B 1 255 ? -0.998  11.370  9.668   1.00 33.42 ? 234 THR B CA    1 
ATOM   5032 C  C     . THR B 1 255 ? -1.550  10.288  8.735   1.00 35.01 ? 234 THR B C     1 
ATOM   5033 O  O     . THR B 1 255 ? -2.626  9.748   8.958   1.00 36.92 ? 234 THR B O     1 
ATOM   5034 C  CB    . THR B 1 255 ? -1.639  11.393  11.057  1.00 34.01 ? 234 THR B CB    1 
ATOM   5035 O  OG1   . THR B 1 255 ? -1.375  12.648  11.705  1.00 29.36 ? 234 THR B OG1   1 
ATOM   5036 C  CG2   . THR B 1 255 ? -1.127  10.243  11.899  1.00 36.64 ? 234 THR B CG2   1 
ATOM   5037 N  N     . PRO B 1 256 ? -0.839  9.938   7.640   1.00 36.12 ? 235 PRO B N     1 
ATOM   5038 C  CA    . PRO B 1 256 ? -1.273  8.859   6.757   1.00 37.43 ? 235 PRO B CA    1 
ATOM   5039 C  C     . PRO B 1 256 ? -1.086  7.480   7.406   1.00 36.03 ? 235 PRO B C     1 
ATOM   5040 O  O     . PRO B 1 256 ? -0.051  7.254   8.044   1.00 30.84 ? 235 PRO B O     1 
ATOM   5041 C  CB    . PRO B 1 256 ? -0.337  8.989   5.553   1.00 37.44 ? 235 PRO B CB    1 
ATOM   5042 C  CG    . PRO B 1 256 ? 0.924   9.558   6.148   1.00 40.22 ? 235 PRO B CG    1 
ATOM   5043 C  CD    . PRO B 1 256 ? 0.433   10.534  7.201   1.00 38.32 ? 235 PRO B CD    1 
ATOM   5044 N  N     . VAL B 1 257 ? -2.068  6.586   7.237   1.00 35.10 ? 236 VAL B N     1 
ATOM   5045 C  CA    . VAL B 1 257 ? -1.959  5.201   7.786   1.00 34.96 ? 236 VAL B CA    1 
ATOM   5046 C  C     . VAL B 1 257 ? -1.246  4.307   6.748   1.00 33.58 ? 236 VAL B C     1 
ATOM   5047 O  O     . VAL B 1 257 ? -1.751  4.160   5.614   1.00 35.42 ? 236 VAL B O     1 
ATOM   5048 C  CB    . VAL B 1 257 ? -3.321  4.673   8.263   1.00 33.36 ? 236 VAL B CB    1 
ATOM   5049 C  CG1   . VAL B 1 257 ? -3.252  3.206   8.646   1.00 34.44 ? 236 VAL B CG1   1 
ATOM   5050 C  CG2   . VAL B 1 257 ? -3.858  5.494   9.420   1.00 32.08 ? 236 VAL B CG2   1 
ATOM   5051 N  N     . ARG B 1 258 ? -0.087  3.766   7.143   1.00 34.37 ? 237 ARG B N     1 
ATOM   5052 C  CA    . ARG B 1 258 ? 0.822   2.920   6.325   1.00 36.47 ? 237 ARG B CA    1 
ATOM   5053 C  C     . ARG B 1 258 ? 0.532   1.423   6.521   1.00 35.32 ? 237 ARG B C     1 
ATOM   5054 O  O     . ARG B 1 258 ? 0.838   0.646   5.591   1.00 36.04 ? 237 ARG B O     1 
ATOM   5055 C  CB    . ARG B 1 258 ? 2.273   3.185   6.725   1.00 36.17 ? 237 ARG B CB    1 
ATOM   5056 C  CG    . ARG B 1 258 ? 2.738   4.604   6.450   1.00 41.34 ? 237 ARG B CG    1 
ATOM   5057 C  CD    . ARG B 1 258 ? 4.247   4.657   6.610   1.00 44.52 ? 237 ARG B CD    1 
ATOM   5058 N  NE    . ARG B 1 258 ? 4.880   5.882   6.133   1.00 44.10 ? 237 ARG B NE    1 
ATOM   5059 C  CZ    . ARG B 1 258 ? 6.161   6.202   6.351   1.00 43.76 ? 237 ARG B CZ    1 
ATOM   5060 N  NH1   . ARG B 1 258 ? 6.957   5.391   7.037   1.00 37.59 ? 237 ARG B NH1   1 
ATOM   5061 N  NH2   . ARG B 1 258 ? 6.637   7.338   5.873   1.00 45.41 ? 237 ARG B NH2   1 
ATOM   5062 N  N     . GLY B 1 259 ? 0.028   1.028   7.695   1.00 34.56 ? 238 GLY B N     1 
ATOM   5063 C  CA    . GLY B 1 259 ? -0.011  -0.385  8.127   1.00 36.08 ? 238 GLY B CA    1 
ATOM   5064 C  C     . GLY B 1 259 ? -1.096  -0.645  9.156   1.00 36.04 ? 238 GLY B C     1 
ATOM   5065 O  O     . GLY B 1 259 ? -1.281  0.200   10.048  1.00 35.45 ? 238 GLY B O     1 
ATOM   5066 N  N     . LEU B 1 260 ? -1.770  -1.793  9.058   1.00 35.40 ? 239 LEU B N     1 
ATOM   5067 C  CA    . LEU B 1 260 ? -2.881  -2.193  9.952   1.00 35.13 ? 239 LEU B CA    1 
ATOM   5068 C  C     . LEU B 1 260 ? -2.742  -3.680  10.278  1.00 37.82 ? 239 LEU B C     1 
ATOM   5069 O  O     . LEU B 1 260 ? -2.898  -4.495  9.347   1.00 45.64 ? 239 LEU B O     1 
ATOM   5070 C  CB    . LEU B 1 260 ? -4.188  -1.891  9.224   1.00 35.58 ? 239 LEU B CB    1 
ATOM   5071 C  CG    . LEU B 1 260 ? -5.326  -1.437  10.126  1.00 36.19 ? 239 LEU B CG    1 
ATOM   5072 C  CD1   . LEU B 1 260 ? -5.172  0.041   10.423  1.00 38.59 ? 239 LEU B CD1   1 
ATOM   5073 C  CD2   . LEU B 1 260 ? -6.664  -1.717  9.482   1.00 38.15 ? 239 LEU B CD2   1 
ATOM   5074 N  N     . ALA B 1 261 ? -2.453  -4.009  11.540  1.00 37.80 ? 240 ALA B N     1 
ATOM   5075 C  CA    . ALA B 1 261 ? -2.174  -5.377  12.047  1.00 35.51 ? 240 ALA B CA    1 
ATOM   5076 C  C     . ALA B 1 261 ? -3.239  -5.747  13.075  1.00 38.53 ? 240 ALA B C     1 
ATOM   5077 O  O     . ALA B 1 261 ? -3.396  -5.004  14.035  1.00 44.60 ? 240 ALA B O     1 
ATOM   5078 C  CB    . ALA B 1 261 ? -0.804  -5.444  12.658  1.00 32.35 ? 240 ALA B CB    1 
ATOM   5079 N  N     . GLN B 1 262 ? -3.969  -6.834  12.872  1.00 36.87 ? 241 GLN B N     1 
ATOM   5080 C  CA    . GLN B 1 262 ? -4.998  -7.260  13.845  1.00 37.75 ? 241 GLN B CA    1 
ATOM   5081 C  C     . GLN B 1 262 ? -4.550  -8.593  14.453  1.00 40.09 ? 241 GLN B C     1 
ATOM   5082 O  O     . GLN B 1 262 ? -3.793  -9.310  13.806  1.00 35.79 ? 241 GLN B O     1 
ATOM   5083 C  CB    . GLN B 1 262 ? -6.394  -7.203  13.210  1.00 33.67 ? 241 GLN B CB    1 
ATOM   5084 C  CG    . GLN B 1 262 ? -6.801  -8.387  12.349  1.00 31.77 ? 241 GLN B CG    1 
ATOM   5085 C  CD    . GLN B 1 262 ? -8.219  -8.156  11.876  1.00 35.13 ? 241 GLN B CD    1 
ATOM   5086 O  OE1   . GLN B 1 262 ? -9.198  -8.290  12.622  1.00 37.15 ? 241 GLN B OE1   1 
ATOM   5087 N  NE2   . GLN B 1 262 ? -8.355  -7.717  10.637  1.00 34.84 ? 241 GLN B NE2   1 
ATOM   5088 N  N     . ASP B 1 263 ? -4.916  -8.828  15.713  1.00 47.64 ? 242 ASP B N     1 
ATOM   5089 C  CA    . ASP B 1 263 ? -4.672  -10.094 16.460  1.00 50.63 ? 242 ASP B CA    1 
ATOM   5090 C  C     . ASP B 1 263 ? -5.935  -10.318 17.290  1.00 49.41 ? 242 ASP B C     1 
ATOM   5091 O  O     . ASP B 1 263 ? -6.926  -9.637  16.977  1.00 53.54 ? 242 ASP B O     1 
ATOM   5092 C  CB    . ASP B 1 263 ? -3.361  -10.045 17.258  1.00 49.86 ? 242 ASP B CB    1 
ATOM   5093 C  CG    . ASP B 1 263 ? -3.301  -8.961  18.324  1.00 55.60 ? 242 ASP B CG    1 
ATOM   5094 O  OD1   . ASP B 1 263 ? -4.372  -8.419  18.663  1.00 51.31 ? 242 ASP B OD1   1 
ATOM   5095 O  OD2   . ASP B 1 263 ? -2.171  -8.659  18.818  1.00 57.81 ? 242 ASP B OD2   1 
ATOM   5096 N  N     . GLY B 1 264 ? -5.916  -11.208 18.286  1.00 44.98 ? 243 GLY B N     1 
ATOM   5097 C  CA    . GLY B 1 264 ? -7.114  -11.529 19.084  1.00 43.78 ? 243 GLY B CA    1 
ATOM   5098 C  C     . GLY B 1 264 ? -7.692  -10.328 19.835  1.00 44.43 ? 243 GLY B C     1 
ATOM   5099 O  O     . GLY B 1 264 ? -8.922  -10.331 20.038  1.00 38.68 ? 243 GLY B O     1 
ATOM   5100 N  N     . ASP B 1 265 ? -6.857  -9.348  20.224  1.00 43.16 ? 244 ASP B N     1 
ATOM   5101 C  CA    . ASP B 1 265 ? -7.158  -8.297  21.236  1.00 45.77 ? 244 ASP B CA    1 
ATOM   5102 C  C     . ASP B 1 265 ? -7.386  -6.934  20.572  1.00 50.80 ? 244 ASP B C     1 
ATOM   5103 O  O     . ASP B 1 265 ? -7.519  -5.930  21.311  1.00 54.46 ? 244 ASP B O     1 
ATOM   5104 C  CB    . ASP B 1 265 ? -6.006  -8.098  22.227  1.00 47.72 ? 244 ASP B CB    1 
ATOM   5105 C  CG    . ASP B 1 265 ? -5.647  -9.328  23.042  1.00 49.69 ? 244 ASP B CG    1 
ATOM   5106 O  OD1   . ASP B 1 265 ? -6.590  -10.048 23.438  1.00 50.14 ? 244 ASP B OD1   1 
ATOM   5107 O  OD2   . ASP B 1 265 ? -4.419  -9.561  23.264  1.00 48.97 ? 244 ASP B OD2   1 
ATOM   5108 N  N     . GLY B 1 266 ? -7.397  -6.858  19.241  1.00 47.00 ? 245 GLY B N     1 
ATOM   5109 C  CA    . GLY B 1 266 ? -7.553  -5.559  18.565  1.00 44.80 ? 245 GLY B CA    1 
ATOM   5110 C  C     . GLY B 1 266 ? -6.644  -5.380  17.368  1.00 41.87 ? 245 GLY B C     1 
ATOM   5111 O  O     . GLY B 1 266 ? -6.082  -6.376  16.884  1.00 36.80 ? 245 GLY B O     1 
ATOM   5112 N  N     . VAL B 1 267 ? -6.523  -4.122  16.924  1.00 42.23 ? 246 VAL B N     1 
ATOM   5113 C  CA    . VAL B 1 267 ? -5.778  -3.688  15.710  1.00 39.18 ? 246 VAL B CA    1 
ATOM   5114 C  C     . VAL B 1 267 ? -4.660  -2.725  16.127  1.00 33.05 ? 246 VAL B C     1 
ATOM   5115 O  O     . VAL B 1 267 ? -4.868  -1.963  17.051  1.00 36.97 ? 246 VAL B O     1 
ATOM   5116 C  CB    . VAL B 1 267 ? -6.724  -3.040  14.686  1.00 41.26 ? 246 VAL B CB    1 
ATOM   5117 C  CG1   . VAL B 1 267 ? -8.099  -3.703  14.697  1.00 43.68 ? 246 VAL B CG1   1 
ATOM   5118 C  CG2   . VAL B 1 267 ? -6.828  -1.529  14.878  1.00 41.29 ? 246 VAL B CG2   1 
ATOM   5119 N  N     . THR B 1 268 ? -3.535  -2.774  15.425  1.00 29.45 ? 247 THR B N     1 
ATOM   5120 C  CA    . THR B 1 268 ? -2.346  -1.911  15.579  1.00 28.24 ? 247 THR B CA    1 
ATOM   5121 C  C     . THR B 1 268 ? -2.150  -1.148  14.273  1.00 28.55 ? 247 THR B C     1 
ATOM   5122 O  O     . THR B 1 268 ? -1.909  -1.803  13.235  1.00 27.98 ? 247 THR B O     1 
ATOM   5123 C  CB    . THR B 1 268 ? -1.119  -2.734  15.958  1.00 27.72 ? 247 THR B CB    1 
ATOM   5124 O  OG1   . THR B 1 268 ? -1.407  -3.208  17.263  1.00 29.66 ? 247 THR B OG1   1 
ATOM   5125 C  CG2   . THR B 1 268 ? 0.175   -1.959  15.987  1.00 28.61 ? 247 THR B CG2   1 
ATOM   5126 N  N     . VAL B 1 269 ? -2.309  0.177   14.346  1.00 30.39 ? 248 VAL B N     1 
ATOM   5127 C  CA    . VAL B 1 269 ? -2.282  1.133   13.207  1.00 31.68 ? 248 VAL B CA    1 
ATOM   5128 C  C     . VAL B 1 269 ? -0.905  1.780   13.180  1.00 35.09 ? 248 VAL B C     1 
ATOM   5129 O  O     . VAL B 1 269 ? -0.638  2.600   14.080  1.00 36.37 ? 248 VAL B O     1 
ATOM   5130 C  CB    . VAL B 1 269 ? -3.388  2.196   13.311  1.00 32.78 ? 248 VAL B CB    1 
ATOM   5131 C  CG1   . VAL B 1 269 ? -3.497  3.000   12.024  1.00 32.92 ? 248 VAL B CG1   1 
ATOM   5132 C  CG2   . VAL B 1 269 ? -4.730  1.574   13.661  1.00 32.76 ? 248 VAL B CG2   1 
ATOM   5133 N  N     . ARG B 1 270 ? -0.077  1.382   12.209  1.00 35.90 ? 249 ARG B N     1 
ATOM   5134 C  CA    . ARG B 1 270 ? 1.282   1.912   11.985  1.00 38.75 ? 249 ARG B CA    1 
ATOM   5135 C  C     . ARG B 1 270 ? 1.164   3.146   11.097  1.00 40.54 ? 249 ARG B C     1 
ATOM   5136 O  O     . ARG B 1 270 ? 0.611   3.045   9.978   1.00 36.93 ? 249 ARG B O     1 
ATOM   5137 C  CB    . ARG B 1 270 ? 2.172   0.867   11.314  1.00 40.70 ? 249 ARG B CB    1 
ATOM   5138 C  CG    . ARG B 1 270 ? 3.630   1.285   11.179  1.00 42.23 ? 249 ARG B CG    1 
ATOM   5139 C  CD    . ARG B 1 270 ? 4.551   0.139   10.752  1.00 46.08 ? 249 ARG B CD    1 
ATOM   5140 N  NE    . ARG B 1 270 ? 4.055   -0.568  9.569   1.00 47.24 ? 249 ARG B NE    1 
ATOM   5141 C  CZ    . ARG B 1 270 ? 4.223   -0.158  8.319   1.00 50.70 ? 249 ARG B CZ    1 
ATOM   5142 N  NH1   . ARG B 1 270 ? 4.911   0.944   8.061   1.00 53.21 ? 249 ARG B NH1   1 
ATOM   5143 N  NH2   . ARG B 1 270 ? 3.694   -0.851  7.324   1.00 54.68 ? 249 ARG B NH2   1 
ATOM   5144 N  N     . THR B 1 271 ? 1.631   4.271   11.616  1.00 42.39 ? 250 THR B N     1 
ATOM   5145 C  CA    . THR B 1 271 ? 1.935   5.494   10.841  1.00 46.75 ? 250 THR B CA    1 
ATOM   5146 C  C     . THR B 1 271 ? 3.455   5.561   10.714  1.00 45.06 ? 250 THR B C     1 
ATOM   5147 O  O     . THR B 1 271 ? 4.108   4.624   11.189  1.00 40.60 ? 250 THR B O     1 
ATOM   5148 C  CB    . THR B 1 271 ? 1.324   6.710   11.544  1.00 47.01 ? 250 THR B CB    1 
ATOM   5149 O  OG1   . THR B 1 271 ? 2.156   6.979   12.669  1.00 47.56 ? 250 THR B OG1   1 
ATOM   5150 C  CG2   . THR B 1 271 ? -0.107  6.481   11.987  1.00 45.27 ? 250 THR B CG2   1 
ATOM   5151 N  N     . ALA B 1 272 ? 3.989   6.623   10.112  1.00 50.31 ? 251 ALA B N     1 
ATOM   5152 C  CA    . ALA B 1 272 ? 5.442   6.929   10.085  1.00 53.77 ? 251 ALA B CA    1 
ATOM   5153 C  C     . ALA B 1 272 ? 5.988   7.115   11.508  1.00 60.99 ? 251 ALA B C     1 
ATOM   5154 O  O     . ALA B 1 272 ? 7.126   6.661   11.756  1.00 70.56 ? 251 ALA B O     1 
ATOM   5155 C  CB    . ALA B 1 272 ? 5.693   8.163   9.257   1.00 57.18 ? 251 ALA B CB    1 
ATOM   5156 N  N     . GLY B 1 273 ? 5.215   7.746   12.405  1.00 60.78 ? 252 GLY B N     1 
ATOM   5157 C  CA    . GLY B 1 273 ? 5.684   8.197   13.733  1.00 63.06 ? 252 GLY B CA    1 
ATOM   5158 C  C     . GLY B 1 273 ? 5.279   7.286   14.887  1.00 62.88 ? 252 GLY B C     1 
ATOM   5159 O  O     . GLY B 1 273 ? 5.045   7.826   15.992  1.00 58.38 ? 252 GLY B O     1 
ATOM   5160 N  N     . GLY B 1 274 ? 5.224   5.963   14.671  1.00 62.73 ? 253 GLY B N     1 
ATOM   5161 C  CA    . GLY B 1 274 ? 4.900   4.969   15.718  1.00 59.77 ? 253 GLY B CA    1 
ATOM   5162 C  C     . GLY B 1 274 ? 3.554   4.288   15.502  1.00 60.28 ? 253 GLY B C     1 
ATOM   5163 O  O     . GLY B 1 274 ? 3.144   4.113   14.328  1.00 59.78 ? 253 GLY B O     1 
ATOM   5164 N  N     . GLU B 1 275 ? 2.889   3.896   16.597  1.00 61.65 ? 254 GLU B N     1 
ATOM   5165 C  CA    . GLU B 1 275 ? 1.725   2.967   16.576  1.00 57.21 ? 254 GLU B CA    1 
ATOM   5166 C  C     . GLU B 1 275 ? 0.583   3.510   17.439  1.00 47.83 ? 254 GLU B C     1 
ATOM   5167 O  O     . GLU B 1 275 ? 0.837   4.384   18.243  1.00 48.29 ? 254 GLU B O     1 
ATOM   5168 C  CB    . GLU B 1 275 ? 2.185   1.576   17.011  1.00 57.28 ? 254 GLU B CB    1 
ATOM   5169 C  CG    . GLU B 1 275 ? 3.110   0.926   15.999  1.00 58.09 ? 254 GLU B CG    1 
ATOM   5170 C  CD    . GLU B 1 275 ? 3.788   -0.339  16.483  1.00 65.96 ? 254 GLU B CD    1 
ATOM   5171 O  OE1   . GLU B 1 275 ? 4.329   -1.081  15.633  1.00 65.49 ? 254 GLU B OE1   1 
ATOM   5172 O  OE2   . GLU B 1 275 ? 3.793   -0.568  17.712  1.00 69.50 ? 254 GLU B OE2   1 
ATOM   5173 N  N     . VAL B 1 276 ? -0.622  2.965   17.244  1.00 52.73 ? 255 VAL B N     1 
ATOM   5174 C  CA    . VAL B 1 276 ? -1.930  3.382   17.844  1.00 49.35 ? 255 VAL B CA    1 
ATOM   5175 C  C     . VAL B 1 276 ? -2.819  2.136   17.985  1.00 48.68 ? 255 VAL B C     1 
ATOM   5176 O  O     . VAL B 1 276 ? -3.395  1.706   16.954  1.00 49.29 ? 255 VAL B O     1 
ATOM   5177 C  CB    . VAL B 1 276 ? -2.620  4.442   16.960  1.00 53.92 ? 255 VAL B CB    1 
ATOM   5178 C  CG1   . VAL B 1 276 ? -4.069  4.704   17.371  1.00 54.13 ? 255 VAL B CG1   1 
ATOM   5179 C  CG2   . VAL B 1 276 ? -1.825  5.738   16.932  1.00 52.66 ? 255 VAL B CG2   1 
ATOM   5180 N  N     . ARG B 1 277 ? -2.917  1.568   19.196  1.00 45.28 ? 256 ARG B N     1 
ATOM   5181 C  CA    . ARG B 1 277 ? -3.641  0.297   19.484  1.00 43.02 ? 256 ARG B CA    1 
ATOM   5182 C  C     . ARG B 1 277 ? -5.127  0.649   19.660  1.00 39.19 ? 256 ARG B C     1 
ATOM   5183 O  O     . ARG B 1 277 ? -5.424  1.644   20.331  1.00 37.08 ? 256 ARG B O     1 
ATOM   5184 C  CB    . ARG B 1 277 ? -3.003  -0.408  20.698  1.00 47.88 ? 256 ARG B CB    1 
ATOM   5185 C  CG    . ARG B 1 277 ? -2.691  -1.898  20.541  1.00 51.25 ? 256 ARG B CG    1 
ATOM   5186 C  CD    . ARG B 1 277 ? -3.876  -2.838  20.293  1.00 54.35 ? 256 ARG B CD    1 
ATOM   5187 N  NE    . ARG B 1 277 ? -3.613  -4.239  20.660  1.00 56.30 ? 256 ARG B NE    1 
ATOM   5188 C  CZ    . ARG B 1 277 ? -3.497  -5.283  19.826  1.00 55.60 ? 256 ARG B CZ    1 
ATOM   5189 N  NH1   . ARG B 1 277 ? -3.611  -5.137  18.514  1.00 59.77 ? 256 ARG B NH1   1 
ATOM   5190 N  NH2   . ARG B 1 277 ? -3.247  -6.484  20.317  1.00 49.75 ? 256 ARG B NH2   1 
ATOM   5191 N  N     . ALA B 1 278 ? -6.028  -0.114  19.039  1.00 38.00 ? 257 ALA B N     1 
ATOM   5192 C  CA    . ALA B 1 278 ? -7.496  0.084   19.091  1.00 36.20 ? 257 ALA B CA    1 
ATOM   5193 C  C     . ALA B 1 278 ? -8.194  -1.272  19.235  1.00 35.14 ? 257 ALA B C     1 
ATOM   5194 O  O     . ALA B 1 278 ? -7.534  -2.310  19.113  1.00 42.17 ? 257 ALA B O     1 
ATOM   5195 C  CB    . ALA B 1 278 ? -7.964  0.826   17.859  1.00 37.34 ? 257 ALA B CB    1 
ATOM   5196 N  N     . ARG B 1 279 ? -9.484  -1.277  19.527  1.00 35.77 ? 258 ARG B N     1 
ATOM   5197 C  CA    . ARG B 1 279 ? -10.262 -2.539  19.582  1.00 39.79 ? 258 ARG B CA    1 
ATOM   5198 C  C     . ARG B 1 279 ? -10.725 -2.832  18.150  1.00 36.33 ? 258 ARG B C     1 
ATOM   5199 O  O     . ARG B 1 279 ? -10.644 -3.993  17.711  1.00 32.16 ? 258 ARG B O     1 
ATOM   5200 C  CB    . ARG B 1 279 ? -11.404 -2.447  20.602  1.00 42.81 ? 258 ARG B CB    1 
ATOM   5201 C  CG    . ARG B 1 279 ? -10.986 -2.732  22.039  1.00 49.56 ? 258 ARG B CG    1 
ATOM   5202 C  CD    . ARG B 1 279 ? -11.877 -2.061  23.079  1.00 60.32 ? 258 ARG B CD    1 
ATOM   5203 N  NE    . ARG B 1 279 ? -13.172 -2.708  23.339  1.00 65.04 ? 258 ARG B NE    1 
ATOM   5204 C  CZ    . ARG B 1 279 ? -14.106 -2.258  24.202  1.00 66.67 ? 258 ARG B CZ    1 
ATOM   5205 N  NH1   . ARG B 1 279 ? -13.914 -1.145  24.911  1.00 60.71 ? 258 ARG B NH1   1 
ATOM   5206 N  NH2   . ARG B 1 279 ? -15.237 -2.933  24.341  1.00 61.31 ? 258 ARG B NH2   1 
ATOM   5207 N  N     . ARG B 1 280 ? -11.152 -1.800  17.434  1.00 32.91 ? 259 ARG B N     1 
ATOM   5208 C  CA    . ARG B 1 280 ? -11.677 -1.937  16.060  1.00 37.31 ? 259 ARG B CA    1 
ATOM   5209 C  C     . ARG B 1 280 ? -11.324 -0.692  15.253  1.00 37.77 ? 259 ARG B C     1 
ATOM   5210 O  O     . ARG B 1 280 ? -11.277 0.397   15.850  1.00 34.91 ? 259 ARG B O     1 
ATOM   5211 C  CB    . ARG B 1 280 ? -13.189 -2.138  16.082  1.00 38.90 ? 259 ARG B CB    1 
ATOM   5212 C  CG    . ARG B 1 280 ? -13.616 -3.281  16.989  1.00 41.76 ? 259 ARG B CG    1 
ATOM   5213 C  CD    . ARG B 1 280 ? -14.763 -4.059  16.412  1.00 40.27 ? 259 ARG B CD    1 
ATOM   5214 N  NE    . ARG B 1 280 ? -14.684 -5.409  16.915  1.00 38.55 ? 259 ARG B NE    1 
ATOM   5215 C  CZ    . ARG B 1 280 ? -15.000 -6.498  16.220  1.00 39.49 ? 259 ARG B CZ    1 
ATOM   5216 N  NH1   . ARG B 1 280 ? -15.401 -6.411  14.953  1.00 36.74 ? 259 ARG B NH1   1 
ATOM   5217 N  NH2   . ARG B 1 280 ? -14.889 -7.674  16.809  1.00 36.63 ? 259 ARG B NH2   1 
ATOM   5218 N  N     . ALA B 1 281 ? -11.093 -0.877  13.951  1.00 36.58 ? 260 ALA B N     1 
ATOM   5219 C  CA    . ALA B 1 281 ? -10.752 0.189   12.988  1.00 36.83 ? 260 ALA B CA    1 
ATOM   5220 C  C     . ALA B 1 281 ? -11.907 0.325   12.011  1.00 34.52 ? 260 ALA B C     1 
ATOM   5221 O  O     . ALA B 1 281 ? -12.506 -0.717  11.665  1.00 34.76 ? 260 ALA B O     1 
ATOM   5222 C  CB    . ALA B 1 281 ? -9.461  -0.142  12.279  1.00 41.50 ? 260 ALA B CB    1 
ATOM   5223 N  N     . ILE B 1 282 ? -12.236 1.559   11.633  1.00 31.76 ? 261 ILE B N     1 
ATOM   5224 C  CA    . ILE B 1 282 ? -13.021 1.828   10.399  1.00 29.65 ? 261 ILE B CA    1 
ATOM   5225 C  C     . ILE B 1 282 ? -12.075 2.462   9.381   1.00 28.70 ? 261 ILE B C     1 
ATOM   5226 O  O     . ILE B 1 282 ? -11.549 3.553   9.649   1.00 26.40 ? 261 ILE B O     1 
ATOM   5227 C  CB    . ILE B 1 282 ? -14.265 2.694   10.680  1.00 33.11 ? 261 ILE B CB    1 
ATOM   5228 C  CG1   . ILE B 1 282 ? -15.284 1.963   11.569  1.00 30.26 ? 261 ILE B CG1   1 
ATOM   5229 C  CG2   . ILE B 1 282 ? -14.890 3.152   9.364   1.00 33.47 ? 261 ILE B CG2   1 
ATOM   5230 C  CD1   . ILE B 1 282 ? -16.278 2.875   12.253  1.00 28.56 ? 261 ILE B CD1   1 
ATOM   5231 N  N     . VAL B 1 283 ? -11.852 1.778   8.256   1.00 29.02 ? 262 VAL B N     1 
ATOM   5232 C  CA    . VAL B 1 283 ? -11.104 2.338   7.098   1.00 28.57 ? 262 VAL B CA    1 
ATOM   5233 C  C     . VAL B 1 283 ? -12.138 2.956   6.158   1.00 25.68 ? 262 VAL B C     1 
ATOM   5234 O  O     . VAL B 1 283 ? -13.029 2.213   5.733   1.00 26.63 ? 262 VAL B O     1 
ATOM   5235 C  CB    . VAL B 1 283 ? -10.237 1.271   6.402   1.00 28.78 ? 262 VAL B CB    1 
ATOM   5236 C  CG1   . VAL B 1 283 ? -9.585  1.845   5.153   1.00 29.35 ? 262 VAL B CG1   1 
ATOM   5237 C  CG2   . VAL B 1 283 ? -9.179  0.698   7.331   1.00 28.29 ? 262 VAL B CG2   1 
ATOM   5238 N  N     . ALA B 1 284 ? -12.041 4.265   5.902   1.00 22.92 ? 263 ALA B N     1 
ATOM   5239 C  CA    . ALA B 1 284 ? -13.063 5.065   5.187   1.00 22.88 ? 263 ALA B CA    1 
ATOM   5240 C  C     . ALA B 1 284 ? -12.395 5.874   4.062   1.00 23.43 ? 263 ALA B C     1 
ATOM   5241 O  O     . ALA B 1 284 ? -12.721 7.071   3.870   1.00 23.69 ? 263 ALA B O     1 
ATOM   5242 C  CB    . ALA B 1 284 ? -13.762 5.974   6.175   1.00 22.83 ? 263 ALA B CB    1 
ATOM   5243 N  N     . VAL B 1 285 ? -11.470 5.242   3.360   1.00 24.07 ? 264 VAL B N     1 
ATOM   5244 C  CA    . VAL B 1 285 ? -10.659 5.859   2.278   1.00 23.91 ? 264 VAL B CA    1 
ATOM   5245 C  C     . VAL B 1 285 ? -11.180 5.283   0.976   1.00 25.08 ? 264 VAL B C     1 
ATOM   5246 O  O     . VAL B 1 285 ? -11.895 4.277   0.971   1.00 25.77 ? 264 VAL B O     1 
ATOM   5247 C  CB    . VAL B 1 285 ? -9.162  5.565   2.464   1.00 24.19 ? 264 VAL B CB    1 
ATOM   5248 C  CG1   . VAL B 1 285 ? -8.636  6.146   3.770   1.00 23.01 ? 264 VAL B CG1   1 
ATOM   5249 C  CG2   . VAL B 1 285 ? -8.862  4.063   2.377   1.00 24.20 ? 264 VAL B CG2   1 
ATOM   5250 N  N     . PRO B 1 286 ? -10.896 5.928   -0.166  1.00 23.93 ? 265 PRO B N     1 
ATOM   5251 C  CA    . PRO B 1 286 ? -11.219 5.335   -1.457  1.00 23.51 ? 265 PRO B CA    1 
ATOM   5252 C  C     . PRO B 1 286 ? -10.679 3.913   -1.599  1.00 21.94 ? 265 PRO B C     1 
ATOM   5253 O  O     . PRO B 1 286 ? -9.561  3.610   -1.193  1.00 18.69 ? 265 PRO B O     1 
ATOM   5254 C  CB    . PRO B 1 286 ? -10.563 6.296   -2.468  1.00 25.17 ? 265 PRO B CB    1 
ATOM   5255 C  CG    . PRO B 1 286 ? -10.528 7.636   -1.741  1.00 25.64 ? 265 PRO B CG    1 
ATOM   5256 C  CD    . PRO B 1 286 ? -10.361 7.294   -0.268  1.00 26.81 ? 265 PRO B CD    1 
ATOM   5257 N  N     . PRO B 1 287 ? -11.459 3.003   -2.213  1.00 23.51 ? 266 PRO B N     1 
ATOM   5258 C  CA    . PRO B 1 287 ? -11.118 1.579   -2.266  1.00 26.28 ? 266 PRO B CA    1 
ATOM   5259 C  C     . PRO B 1 287 ? -9.719  1.229   -2.812  1.00 24.66 ? 266 PRO B C     1 
ATOM   5260 O  O     . PRO B 1 287 ? -9.129  0.272   -2.359  1.00 24.41 ? 266 PRO B O     1 
ATOM   5261 C  CB    . PRO B 1 287 ? -12.172 0.983   -3.215  1.00 26.05 ? 266 PRO B CB    1 
ATOM   5262 C  CG    . PRO B 1 287 ? -12.721 2.165   -3.968  1.00 26.89 ? 266 PRO B CG    1 
ATOM   5263 C  CD    . PRO B 1 287 ? -12.653 3.322   -3.000  1.00 23.40 ? 266 PRO B CD    1 
ATOM   5264 N  N     . THR B 1 288 ? -9.206  2.029   -3.744  1.00 28.18 ? 267 THR B N     1 
ATOM   5265 C  CA    . THR B 1 288 ? -7.833  1.909   -4.316  1.00 28.08 ? 267 THR B CA    1 
ATOM   5266 C  C     . THR B 1 288 ? -6.772  2.267   -3.266  1.00 26.18 ? 267 THR B C     1 
ATOM   5267 O  O     . THR B 1 288 ? -5.683  1.613   -3.264  1.00 28.73 ? 267 THR B O     1 
ATOM   5268 C  CB    . THR B 1 288 ? -7.699  2.780   -5.575  1.00 30.21 ? 267 THR B CB    1 
ATOM   5269 O  OG1   . THR B 1 288 ? -6.442  2.440   -6.151  1.00 37.21 ? 267 THR B OG1   1 
ATOM   5270 C  CG2   . THR B 1 288 ? -7.740  4.271   -5.321  1.00 29.80 ? 267 THR B CG2   1 
ATOM   5271 N  N     . LEU B 1 289 ? -7.006  3.312   -2.469  1.00 21.99 ? 268 LEU B N     1 
ATOM   5272 C  CA    . LEU B 1 289 ? -6.101  3.702   -1.359  1.00 22.31 ? 268 LEU B CA    1 
ATOM   5273 C  C     . LEU B 1 289 ? -6.157  2.631   -0.255  1.00 22.78 ? 268 LEU B C     1 
ATOM   5274 O  O     . LEU B 1 289 ? -5.109  2.338   0.339   1.00 22.59 ? 268 LEU B O     1 
ATOM   5275 C  CB    . LEU B 1 289 ? -6.502  5.086   -0.849  1.00 21.79 ? 268 LEU B CB    1 
ATOM   5276 C  CG    . LEU B 1 289 ? -6.545  6.187   -1.911  1.00 22.10 ? 268 LEU B CG    1 
ATOM   5277 C  CD1   . LEU B 1 289 ? -6.358  7.557   -1.294  1.00 20.73 ? 268 LEU B CD1   1 
ATOM   5278 C  CD2   . LEU B 1 289 ? -5.485  5.970   -2.978  1.00 24.05 ? 268 LEU B CD2   1 
ATOM   5279 N  N     . ALA B 1 290 ? -7.334  2.070   -0.002  1.00 25.54 ? 269 ALA B N     1 
ATOM   5280 C  CA    . ALA B 1 290 ? -7.586  1.041   1.045   1.00 30.11 ? 269 ALA B CA    1 
ATOM   5281 C  C     . ALA B 1 290 ? -6.693  -0.184  0.802   1.00 30.23 ? 269 ALA B C     1 
ATOM   5282 O  O     . ALA B 1 290 ? -6.103  -0.697  1.763   1.00 32.06 ? 269 ALA B O     1 
ATOM   5283 C  CB    . ALA B 1 290 ? -9.057  0.668   1.070   1.00 27.22 ? 269 ALA B CB    1 
ATOM   5284 N  N     . GLY B 1 291 ? -6.610  -0.636  -0.449  1.00 35.21 ? 270 GLY B N     1 
ATOM   5285 C  CA    . GLY B 1 291 ? -5.817  -1.824  -0.842  1.00 37.01 ? 270 GLY B CA    1 
ATOM   5286 C  C     . GLY B 1 291 ? -4.308  -1.633  -0.683  1.00 33.58 ? 270 GLY B C     1 
ATOM   5287 O  O     . GLY B 1 291 ? -3.613  -2.647  -0.476  1.00 34.86 ? 270 GLY B O     1 
ATOM   5288 N  N     . ARG B 1 292 ? -3.807  -0.397  -0.769  1.00 31.36 ? 271 ARG B N     1 
ATOM   5289 C  CA    . ARG B 1 292 ? -2.351  -0.076  -0.709  1.00 33.34 ? 271 ARG B CA    1 
ATOM   5290 C  C     . ARG B 1 292 ? -1.843  -0.157  0.734   1.00 34.57 ? 271 ARG B C     1 
ATOM   5291 O  O     . ARG B 1 292 ? -0.615  -0.185  0.935   1.00 29.93 ? 271 ARG B O     1 
ATOM   5292 C  CB    . ARG B 1 292 ? -2.074  1.329   -1.255  1.00 34.51 ? 271 ARG B CB    1 
ATOM   5293 C  CG    . ARG B 1 292 ? -2.908  1.688   -2.475  1.00 35.14 ? 271 ARG B CG    1 
ATOM   5294 C  CD    . ARG B 1 292 ? -2.271  2.669   -3.440  1.00 35.47 ? 271 ARG B CD    1 
ATOM   5295 N  NE    . ARG B 1 292 ? -3.187  2.881   -4.552  1.00 36.43 ? 271 ARG B NE    1 
ATOM   5296 C  CZ    . ARG B 1 292 ? -2.968  3.699   -5.574  1.00 38.00 ? 271 ARG B CZ    1 
ATOM   5297 N  NH1   . ARG B 1 292 ? -1.870  4.428   -5.606  1.00 36.71 ? 271 ARG B NH1   1 
ATOM   5298 N  NH2   . ARG B 1 292 ? -3.868  3.822   -6.538  1.00 38.29 ? 271 ARG B NH2   1 
ATOM   5299 N  N     . ILE B 1 293 ? -2.744  -0.157  1.722   1.00 36.02 ? 272 ILE B N     1 
ATOM   5300 C  CA    . ILE B 1 293 ? -2.332  -0.232  3.156   1.00 35.34 ? 272 ILE B CA    1 
ATOM   5301 C  C     . ILE B 1 293 ? -1.740  -1.632  3.392   1.00 33.79 ? 272 ILE B C     1 
ATOM   5302 O  O     . ILE B 1 293 ? -2.202  -2.606  2.788   1.00 31.05 ? 272 ILE B O     1 
ATOM   5303 C  CB    . ILE B 1 293 ? -3.491  0.112   4.120   1.00 36.67 ? 272 ILE B CB    1 
ATOM   5304 C  CG1   . ILE B 1 293 ? -4.203  1.411   3.719   1.00 34.46 ? 272 ILE B CG1   1 
ATOM   5305 C  CG2   . ILE B 1 293 ? -2.994  0.147   5.571   1.00 33.46 ? 272 ILE B CG2   1 
ATOM   5306 C  CD1   . ILE B 1 293 ? -5.431  1.735   4.544   1.00 36.36 ? 272 ILE B CD1   1 
ATOM   5307 N  N     . ASP B 1 294 ? -0.710  -1.717  4.217   1.00 32.12 ? 273 ASP B N     1 
ATOM   5308 C  CA    . ASP B 1 294 ? -0.076  -3.008  4.577   1.00 32.40 ? 273 ASP B CA    1 
ATOM   5309 C  C     . ASP B 1 294 ? -1.036  -3.699  5.577   1.00 30.56 ? 273 ASP B C     1 
ATOM   5310 O  O     . ASP B 1 294 ? -1.135  -3.267  6.697   1.00 25.56 ? 273 ASP B O     1 
ATOM   5311 C  CB    . ASP B 1 294 ? 1.354   -2.686  5.008   1.00 33.99 ? 273 ASP B CB    1 
ATOM   5312 C  CG    . ASP B 1 294 ? 2.151   -3.854  5.526   1.00 40.71 ? 273 ASP B CG    1 
ATOM   5313 O  OD1   . ASP B 1 294 ? 1.796   -5.005  5.179   1.00 44.23 ? 273 ASP B OD1   1 
ATOM   5314 O  OD2   . ASP B 1 294 ? 3.124   -3.596  6.275   1.00 41.77 ? 273 ASP B OD2   1 
ATOM   5315 N  N     . HIS B 1 295 ? -1.805  -4.704  5.170   1.00 30.96 ? 274 HIS B N     1 
ATOM   5316 C  CA    . HIS B 1 295 ? -2.769  -5.391  6.073   1.00 33.31 ? 274 HIS B CA    1 
ATOM   5317 C  C     . HIS B 1 295 ? -2.069  -6.600  6.687   1.00 32.49 ? 274 HIS B C     1 
ATOM   5318 O  O     . HIS B 1 295 ? -1.277  -7.219  5.975   1.00 35.15 ? 274 HIS B O     1 
ATOM   5319 C  CB    . HIS B 1 295 ? -4.076  -5.750  5.352   1.00 31.05 ? 274 HIS B CB    1 
ATOM   5320 C  CG    . HIS B 1 295 ? -4.942  -4.570  5.060   1.00 32.30 ? 274 HIS B CG    1 
ATOM   5321 N  ND1   . HIS B 1 295 ? -5.749  -3.991  6.028   1.00 33.61 ? 274 HIS B ND1   1 
ATOM   5322 C  CD2   . HIS B 1 295 ? -5.136  -3.864  3.918   1.00 32.62 ? 274 HIS B CD2   1 
ATOM   5323 C  CE1   . HIS B 1 295 ? -6.408  -2.975  5.500   1.00 33.98 ? 274 HIS B CE1   1 
ATOM   5324 N  NE2   . HIS B 1 295 ? -6.038  -2.867  4.196   1.00 37.30 ? 274 HIS B NE2   1 
ATOM   5325 N  N     . ASP B 1 296 ? -2.343  -6.911  7.958   1.00 32.59 ? 275 ASP B N     1 
ATOM   5326 C  CA    . ASP B 1 296 ? -1.711  -8.073  8.640   1.00 34.03 ? 275 ASP B CA    1 
ATOM   5327 C  C     . ASP B 1 296 ? -2.657  -8.662  9.684   1.00 34.19 ? 275 ASP B C     1 
ATOM   5328 O  O     . ASP B 1 296 ? -2.983  -7.992  10.664  1.00 30.48 ? 275 ASP B O     1 
ATOM   5329 C  CB    . ASP B 1 296 ? -0.389  -7.649  9.250   1.00 33.28 ? 275 ASP B CB    1 
ATOM   5330 C  CG    . ASP B 1 296 ? 0.445   -8.810  9.707   1.00 35.11 ? 275 ASP B CG    1 
ATOM   5331 O  OD1   . ASP B 1 296 ? 0.172   -9.941  9.303   1.00 36.36 ? 275 ASP B OD1   1 
ATOM   5332 O  OD2   . ASP B 1 296 ? 1.373   -8.555  10.458  1.00 43.33 ? 275 ASP B OD2   1 
ATOM   5333 N  N     . PRO B 1 297 ? -3.166  -9.905  9.490   1.00 32.44 ? 276 PRO B N     1 
ATOM   5334 C  CA    . PRO B 1 297 ? -2.925  -10.690 8.272   1.00 31.07 ? 276 PRO B CA    1 
ATOM   5335 C  C     . PRO B 1 297 ? -3.282  -10.018 6.941   1.00 30.03 ? 276 PRO B C     1 
ATOM   5336 O  O     . PRO B 1 297 ? -4.011  -9.027  6.907   1.00 26.33 ? 276 PRO B O     1 
ATOM   5337 C  CB    . PRO B 1 297 ? -3.878  -11.903 8.418   1.00 33.61 ? 276 PRO B CB    1 
ATOM   5338 C  CG    . PRO B 1 297 ? -4.175  -12.015 9.898   1.00 36.15 ? 276 PRO B CG    1 
ATOM   5339 C  CD    . PRO B 1 297 ? -4.047  -10.602 10.443  1.00 33.92 ? 276 PRO B CD    1 
ATOM   5340 N  N     . PRO B 1 298 ? -2.819  -10.565 5.788   1.00 30.03 ? 277 PRO B N     1 
ATOM   5341 C  CA    . PRO B 1 298 ? -3.151  -10.017 4.475   1.00 27.14 ? 277 PRO B CA    1 
ATOM   5342 C  C     . PRO B 1 298 ? -4.665  -10.163 4.339   1.00 25.64 ? 277 PRO B C     1 
ATOM   5343 O  O     . PRO B 1 298 ? -5.165  -11.095 4.879   1.00 26.36 ? 277 PRO B O     1 
ATOM   5344 C  CB    . PRO B 1 298 ? -2.433  -10.896 3.437   1.00 28.42 ? 277 PRO B CB    1 
ATOM   5345 C  CG    . PRO B 1 298 ? -1.480  -11.769 4.249   1.00 30.91 ? 277 PRO B CG    1 
ATOM   5346 C  CD    . PRO B 1 298 ? -1.979  -11.769 5.684   1.00 31.05 ? 277 PRO B CD    1 
ATOM   5347 N  N     . LEU B 1 299 ? -5.336  -9.215  3.695   1.00 26.43 ? 278 LEU B N     1 
ATOM   5348 C  CA    . LEU B 1 299 ? -6.795  -9.248  3.472   1.00 28.08 ? 278 LEU B CA    1 
ATOM   5349 C  C     . LEU B 1 299 ? -7.163  -10.541 2.744   1.00 29.37 ? 278 LEU B C     1 
ATOM   5350 O  O     . LEU B 1 299 ? -6.344  -11.152 2.058   1.00 25.20 ? 278 LEU B O     1 
ATOM   5351 C  CB    . LEU B 1 299 ? -7.192  -8.020  2.656   1.00 31.57 ? 278 LEU B CB    1 
ATOM   5352 C  CG    . LEU B 1 299 ? -7.027  -6.662  3.348   1.00 34.78 ? 278 LEU B CG    1 
ATOM   5353 C  CD1   . LEU B 1 299 ? -7.775  -5.597  2.571   1.00 37.55 ? 278 LEU B CD1   1 
ATOM   5354 C  CD2   . LEU B 1 299 ? -7.518  -6.683  4.803   1.00 33.97 ? 278 LEU B CD2   1 
ATOM   5355 N  N     . PRO B 1 300 ? -8.414  -11.014 2.904   1.00 28.42 ? 279 PRO B N     1 
ATOM   5356 C  CA    . PRO B 1 300 ? -8.894  -12.158 2.139   1.00 27.69 ? 279 PRO B CA    1 
ATOM   5357 C  C     . PRO B 1 300 ? -8.862  -11.893 0.641   1.00 25.26 ? 279 PRO B C     1 
ATOM   5358 O  O     . PRO B 1 300 ? -9.103  -10.779 0.177   1.00 22.86 ? 279 PRO B O     1 
ATOM   5359 C  CB    . PRO B 1 300 ? -10.352 -12.374 2.584   1.00 28.17 ? 279 PRO B CB    1 
ATOM   5360 C  CG    . PRO B 1 300 ? -10.496 -11.550 3.863   1.00 27.65 ? 279 PRO B CG    1 
ATOM   5361 C  CD    . PRO B 1 300 ? -9.427  -10.474 3.823   1.00 27.11 ? 279 PRO B CD    1 
ATOM   5362 N  N     . PRO B 1 301 ? -8.606  -12.948 -0.155  1.00 25.74 ? 280 PRO B N     1 
ATOM   5363 C  CA    . PRO B 1 301 ? -8.432  -12.789 -1.590  1.00 23.30 ? 280 PRO B CA    1 
ATOM   5364 C  C     . PRO B 1 301 ? -9.561  -11.993 -2.263  1.00 24.01 ? 280 PRO B C     1 
ATOM   5365 O  O     . PRO B 1 301 ? -9.262  -11.082 -3.038  1.00 21.06 ? 280 PRO B O     1 
ATOM   5366 C  CB    . PRO B 1 301 ? -8.384  -14.233 -2.105  1.00 24.68 ? 280 PRO B CB    1 
ATOM   5367 C  CG    . PRO B 1 301 ? -8.817  -15.124 -0.924  1.00 23.89 ? 280 PRO B CG    1 
ATOM   5368 C  CD    . PRO B 1 301 ? -8.431  -14.341 0.304   1.00 24.64 ? 280 PRO B CD    1 
ATOM   5369 N  N     . GLN B 1 302 ? -10.815 -12.377 -2.030  1.00 22.97 ? 281 GLN B N     1 
ATOM   5370 C  CA    . GLN B 1 302 ? -11.973 -11.777 -2.753  1.00 26.34 ? 281 GLN B CA    1 
ATOM   5371 C  C     . GLN B 1 302 ? -11.973 -10.261 -2.529  1.00 26.74 ? 281 GLN B C     1 
ATOM   5372 O  O     . GLN B 1 302 ? -12.318 -9.509  -3.478  1.00 26.67 ? 281 GLN B O     1 
ATOM   5373 C  CB    . GLN B 1 302 ? -13.305 -12.352 -2.267  1.00 26.02 ? 281 GLN B CB    1 
ATOM   5374 C  CG    . GLN B 1 302 ? -14.507 -11.987 -3.133  1.00 26.05 ? 281 GLN B CG    1 
ATOM   5375 C  CD    . GLN B 1 302 ? -15.768 -12.571 -2.527  1.00 26.03 ? 281 GLN B CD    1 
ATOM   5376 O  OE1   . GLN B 1 302 ? -15.776 -12.985 -1.375  1.00 30.44 ? 281 GLN B OE1   1 
ATOM   5377 N  NE2   . GLN B 1 302 ? -16.819 -12.684 -3.316  1.00 24.13 ? 281 GLN B NE2   1 
ATOM   5378 N  N     . ARG B 1 303 ? -11.584 -9.834  -1.318  1.00 28.03 ? 282 ARG B N     1 
ATOM   5379 C  CA    . ARG B 1 303 ? -11.600 -8.407  -0.942  1.00 27.29 ? 282 ARG B CA    1 
ATOM   5380 C  C     . ARG B 1 303 ? -10.454 -7.733  -1.678  1.00 23.69 ? 282 ARG B C     1 
ATOM   5381 O  O     . ARG B 1 303 ? -10.750 -6.857  -2.479  1.00 26.39 ? 282 ARG B O     1 
ATOM   5382 C  CB    . ARG B 1 303 ? -11.545 -8.185  0.573   1.00 33.59 ? 282 ARG B CB    1 
ATOM   5383 C  CG    . ARG B 1 303 ? -11.225 -6.745  0.957   1.00 35.71 ? 282 ARG B CG    1 
ATOM   5384 C  CD    . ARG B 1 303 ? -12.050 -6.150  2.077   1.00 42.43 ? 282 ARG B CD    1 
ATOM   5385 N  NE    . ARG B 1 303 ? -11.908 -4.698  2.023   1.00 44.82 ? 282 ARG B NE    1 
ATOM   5386 C  CZ    . ARG B 1 303 ? -12.821 -3.850  1.573   1.00 44.06 ? 282 ARG B CZ    1 
ATOM   5387 N  NH1   . ARG B 1 303 ? -14.017 -4.276  1.187   1.00 47.23 ? 282 ARG B NH1   1 
ATOM   5388 N  NH2   . ARG B 1 303 ? -12.536 -2.563  1.551   1.00 44.55 ? 282 ARG B NH2   1 
ATOM   5389 N  N     . ASP B 1 304 ? -9.204  -8.121  -1.431  1.00 25.62 ? 283 ASP B N     1 
ATOM   5390 C  CA    . ASP B 1 304 ? -8.038  -7.545  -2.157  1.00 24.02 ? 283 ASP B CA    1 
ATOM   5391 C  C     . ASP B 1 304 ? -8.344  -7.412  -3.651  1.00 24.44 ? 283 ASP B C     1 
ATOM   5392 O  O     . ASP B 1 304 ? -8.183  -6.317  -4.193  1.00 24.47 ? 283 ASP B O     1 
ATOM   5393 C  CB    . ASP B 1 304 ? -6.785  -8.385  -2.031  1.00 24.19 ? 283 ASP B CB    1 
ATOM   5394 C  CG    . ASP B 1 304 ? -5.577  -7.595  -2.489  1.00 24.86 ? 283 ASP B CG    1 
ATOM   5395 O  OD1   . ASP B 1 304 ? -5.188  -6.684  -1.750  1.00 26.97 ? 283 ASP B OD1   1 
ATOM   5396 O  OD2   . ASP B 1 304 ? -5.081  -7.853  -3.601  1.00 24.41 ? 283 ASP B OD2   1 
ATOM   5397 N  N     . GLN B 1 305 ? -8.787  -8.491  -4.293  1.00 22.59 ? 284 GLN B N     1 
ATOM   5398 C  CA    . GLN B 1 305 ? -9.086  -8.478  -5.744  1.00 24.66 ? 284 GLN B CA    1 
ATOM   5399 C  C     . GLN B 1 305 ? -10.323 -7.598  -6.066  1.00 28.87 ? 284 GLN B C     1 
ATOM   5400 O  O     . GLN B 1 305 ? -10.334 -7.006  -7.187  1.00 26.60 ? 284 GLN B O     1 
ATOM   5401 C  CB    . GLN B 1 305 ? -9.201  -9.918  -6.255  1.00 24.29 ? 284 GLN B CB    1 
ATOM   5402 C  CG    . GLN B 1 305 ? -7.855  -10.647 -6.263  1.00 21.86 ? 284 GLN B CG    1 
ATOM   5403 C  CD    . GLN B 1 305 ? -7.746  -11.625 -7.404  1.00 23.48 ? 284 GLN B CD    1 
ATOM   5404 O  OE1   . GLN B 1 305 ? -6.711  -11.711 -8.092  1.00 25.16 ? 284 GLN B OE1   1 
ATOM   5405 N  NE2   . GLN B 1 305 ? -8.824  -12.371 -7.620  1.00 23.24 ? 284 GLN B NE2   1 
ATOM   5406 N  N     . LEU B 1 306 ? -11.311 -7.470  -5.160  1.00 27.21 ? 285 LEU B N     1 
ATOM   5407 C  CA    . LEU B 1 306 ? -12.398 -6.457  -5.312  1.00 28.52 ? 285 LEU B CA    1 
ATOM   5408 C  C     . LEU B 1 306 ? -11.802 -5.064  -5.514  1.00 23.94 ? 285 LEU B C     1 
ATOM   5409 O  O     . LEU B 1 306 ? -12.234 -4.380  -6.449  1.00 22.50 ? 285 LEU B O     1 
ATOM   5410 C  CB    . LEU B 1 306 ? -13.320 -6.410  -4.089  1.00 29.55 ? 285 LEU B CB    1 
ATOM   5411 C  CG    . LEU B 1 306 ? -14.347 -5.275  -4.128  1.00 29.03 ? 285 LEU B CG    1 
ATOM   5412 C  CD1   . LEU B 1 306 ? -15.290 -5.455  -5.301  1.00 29.08 ? 285 LEU B CD1   1 
ATOM   5413 C  CD2   . LEU B 1 306 ? -15.132 -5.191  -2.844  1.00 29.18 ? 285 LEU B CD2   1 
ATOM   5414 N  N     . LEU B 1 307 ? -10.929 -4.635  -4.612  1.00 23.01 ? 286 LEU B N     1 
ATOM   5415 C  CA    . LEU B 1 307 ? -10.232 -3.312  -4.698  1.00 25.58 ? 286 LEU B CA    1 
ATOM   5416 C  C     . LEU B 1 307 ? -9.520  -3.192  -6.058  1.00 24.97 ? 286 LEU B C     1 
ATOM   5417 O  O     . LEU B 1 307 ? -9.603  -2.101  -6.680  1.00 30.34 ? 286 LEU B O     1 
ATOM   5418 C  CB    . LEU B 1 307 ? -9.228  -3.142  -3.543  1.00 25.72 ? 286 LEU B CB    1 
ATOM   5419 C  CG    . LEU B 1 307 ? -9.802  -3.348  -2.135  1.00 28.51 ? 286 LEU B CG    1 
ATOM   5420 C  CD1   . LEU B 1 307 ? -8.811  -2.958  -1.066  1.00 30.01 ? 286 LEU B CD1   1 
ATOM   5421 C  CD2   . LEU B 1 307 ? -11.108 -2.592  -1.928  1.00 33.54 ? 286 LEU B CD2   1 
ATOM   5422 N  N     . GLN B 1 308 ? -8.862  -4.257  -6.520  1.00 21.52 ? 287 GLN B N     1 
ATOM   5423 C  CA    . GLN B 1 308 ? -8.183  -4.280  -7.848  1.00 23.61 ? 287 GLN B CA    1 
ATOM   5424 C  C     . GLN B 1 308 ? -9.178  -3.949  -8.976  1.00 24.25 ? 287 GLN B C     1 
ATOM   5425 O  O     . GLN B 1 308 ? -8.761  -3.457  -10.043 1.00 22.11 ? 287 GLN B O     1 
ATOM   5426 C  CB    . GLN B 1 308 ? -7.524  -5.641  -8.077  1.00 21.75 ? 287 GLN B CB    1 
ATOM   5427 C  CG    . GLN B 1 308 ? -6.156  -5.745  -7.412  1.00 21.50 ? 287 GLN B CG    1 
ATOM   5428 C  CD    . GLN B 1 308 ? -5.553  -7.087  -7.728  1.00 20.91 ? 287 GLN B CD    1 
ATOM   5429 O  OE1   . GLN B 1 308 ? -5.525  -7.521  -8.875  1.00 21.95 ? 287 GLN B OE1   1 
ATOM   5430 N  NE2   . GLN B 1 308 ? -5.089  -7.773  -6.699  1.00 22.01 ? 287 GLN B NE2   1 
ATOM   5431 N  N     . HIS B 1 309 ? -10.456 -4.247  -8.749  1.00 25.09 ? 288 HIS B N     1 
ATOM   5432 C  CA    . HIS B 1 309 ? -11.547 -4.068  -9.723  1.00 24.66 ? 288 HIS B CA    1 
ATOM   5433 C  C     . HIS B 1 309 ? -12.421 -2.841  -9.377  1.00 24.86 ? 288 HIS B C     1 
ATOM   5434 O  O     . HIS B 1 309 ? -13.529 -2.745  -9.990  1.00 28.44 ? 288 HIS B O     1 
ATOM   5435 C  CB    . HIS B 1 309 ? -12.335 -5.374  -9.746  1.00 25.00 ? 288 HIS B CB    1 
ATOM   5436 C  CG    . HIS B 1 309 ? -11.673 -6.503  -10.464 1.00 23.98 ? 288 HIS B CG    1 
ATOM   5437 N  ND1   . HIS B 1 309 ? -12.066 -6.884  -11.741 1.00 23.93 ? 288 HIS B ND1   1 
ATOM   5438 C  CD2   . HIS B 1 309 ? -10.751 -7.405  -10.067 1.00 23.43 ? 288 HIS B CD2   1 
ATOM   5439 C  CE1   . HIS B 1 309 ? -11.345 -7.916  -12.126 1.00 24.93 ? 288 HIS B CE1   1 
ATOM   5440 N  NE2   . HIS B 1 309 ? -10.531 -8.256  -11.118 1.00 26.15 ? 288 HIS B NE2   1 
ATOM   5441 N  N     . MET B 1 310 ? -12.012 -1.946  -8.452  1.00 24.92 ? 289 MET B N     1 
ATOM   5442 C  CA    . MET B 1 310 ? -12.732 -0.645  -8.159  1.00 26.33 ? 289 MET B CA    1 
ATOM   5443 C  C     . MET B 1 310 ? -11.827 0.560   -8.494  1.00 26.77 ? 289 MET B C     1 
ATOM   5444 O  O     . MET B 1 310 ? -11.384 1.321   -7.629  1.00 24.64 ? 289 MET B O     1 
ATOM   5445 C  CB    . MET B 1 310 ? -13.216 -0.582  -6.702  1.00 25.75 ? 289 MET B CB    1 
ATOM   5446 C  CG    . MET B 1 310 ? -14.143 -1.740  -6.349  1.00 25.71 ? 289 MET B CG    1 
ATOM   5447 S  SD    . MET B 1 310 ? -14.850 -1.757  -4.683  1.00 26.25 ? 289 MET B SD    1 
ATOM   5448 C  CE    . MET B 1 310 ? -16.023 -0.396  -4.753  1.00 26.13 ? 289 MET B CE    1 
ATOM   5449 N  N     . PRO B 1 311 ? -11.483 0.765   -9.787  1.00 27.44 ? 290 PRO B N     1 
ATOM   5450 C  CA    . PRO B 1 311 ? -10.683 1.924   -10.196 1.00 27.43 ? 290 PRO B CA    1 
ATOM   5451 C  C     . PRO B 1 311 ? -11.461 3.217   -9.975  1.00 25.97 ? 290 PRO B C     1 
ATOM   5452 O  O     . PRO B 1 311 ? -12.666 3.183   -10.131 1.00 28.92 ? 290 PRO B O     1 
ATOM   5453 C  CB    . PRO B 1 311 ? -10.460 1.693   -11.696 1.00 27.00 ? 290 PRO B CB    1 
ATOM   5454 C  CG    . PRO B 1 311 ? -11.580 0.795   -12.132 1.00 25.20 ? 290 PRO B CG    1 
ATOM   5455 C  CD    . PRO B 1 311 ? -11.821 -0.100  -10.934 1.00 24.94 ? 290 PRO B CD    1 
ATOM   5456 N  N     . GLN B 1 312 ? -10.781 4.306   -9.642  1.00 27.91 ? 291 GLN B N     1 
ATOM   5457 C  CA    . GLN B 1 312 ? -11.445 5.635   -9.517  1.00 31.13 ? 291 GLN B CA    1 
ATOM   5458 C  C     . GLN B 1 312 ? -11.668 6.219   -10.917 1.00 27.43 ? 291 GLN B C     1 
ATOM   5459 O  O     . GLN B 1 312 ? -10.859 5.914   -11.808 1.00 29.74 ? 291 GLN B O     1 
ATOM   5460 C  CB    . GLN B 1 312 ? -10.636 6.627   -8.670  1.00 31.86 ? 291 GLN B CB    1 
ATOM   5461 C  CG    . GLN B 1 312 ? -10.338 6.161   -7.240  1.00 36.15 ? 291 GLN B CG    1 
ATOM   5462 C  CD    . GLN B 1 312 ? -11.547 6.118   -6.335  1.00 36.76 ? 291 GLN B CD    1 
ATOM   5463 O  OE1   . GLN B 1 312 ? -12.221 7.129   -6.106  1.00 39.65 ? 291 GLN B OE1   1 
ATOM   5464 N  NE2   . GLN B 1 312 ? -11.826 4.936   -5.809  1.00 36.68 ? 291 GLN B NE2   1 
ATOM   5465 N  N     . GLY B 1 313 ? -12.701 7.057   -11.075 1.00 24.44 ? 292 GLY B N     1 
ATOM   5466 C  CA    . GLY B 1 313 ? -12.954 7.854   -12.288 1.00 23.67 ? 292 GLY B CA    1 
ATOM   5467 C  C     . GLY B 1 313 ? -11.797 8.797   -12.558 1.00 21.91 ? 292 GLY B C     1 
ATOM   5468 O  O     . GLY B 1 313 ? -10.885 8.860   -11.737 1.00 21.76 ? 292 GLY B O     1 
ATOM   5469 N  N     . SER B 1 314 ? -11.817 9.496   -13.682 1.00 23.02 ? 293 SER B N     1 
ATOM   5470 C  CA    . SER B 1 314 ? -10.769 10.479  -14.068 1.00 24.99 ? 293 SER B CA    1 
ATOM   5471 C  C     . SER B 1 314 ? -11.432 11.840  -14.264 1.00 24.43 ? 293 SER B C     1 
ATOM   5472 O  O     . SER B 1 314 ? -12.329 11.984  -15.092 1.00 25.73 ? 293 SER B O     1 
ATOM   5473 C  CB    . SER B 1 314 ? -10.017 10.029  -15.290 1.00 27.37 ? 293 SER B CB    1 
ATOM   5474 O  OG    . SER B 1 314 ? -9.552  8.677   -15.158 1.00 27.85 ? 293 SER B OG    1 
ATOM   5475 N  N     . VAL B 1 315 ? -11.061 12.812  -13.467 1.00 25.78 ? 294 VAL B N     1 
ATOM   5476 C  CA    . VAL B 1 315 ? -11.779 14.103  -13.536 1.00 26.38 ? 294 VAL B CA    1 
ATOM   5477 C  C     . VAL B 1 315 ? -10.790 15.211  -13.207 1.00 24.67 ? 294 VAL B C     1 
ATOM   5478 O  O     . VAL B 1 315 ? -9.999  15.021  -12.255 1.00 24.44 ? 294 VAL B O     1 
ATOM   5479 C  CB    . VAL B 1 315 ? -13.012 14.080  -12.609 1.00 30.98 ? 294 VAL B CB    1 
ATOM   5480 C  CG1   . VAL B 1 315 ? -12.627 14.309  -11.159 1.00 30.46 ? 294 VAL B CG1   1 
ATOM   5481 C  CG2   . VAL B 1 315 ? -14.063 15.078  -13.055 1.00 30.82 ? 294 VAL B CG2   1 
ATOM   5482 N  N     . VAL B 1 316 ? -10.788 16.251  -14.055 1.00 23.52 ? 295 VAL B N     1 
ATOM   5483 C  CA    . VAL B 1 316 ? -10.206 17.591  -13.793 1.00 22.15 ? 295 VAL B CA    1 
ATOM   5484 C  C     . VAL B 1 316 ? -11.381 18.551  -13.698 1.00 23.39 ? 295 VAL B C     1 
ATOM   5485 O  O     . VAL B 1 316 ? -12.181 18.583  -14.695 1.00 27.05 ? 295 VAL B O     1 
ATOM   5486 C  CB    . VAL B 1 316 ? -9.265  17.992  -14.935 1.00 23.30 ? 295 VAL B CB    1 
ATOM   5487 C  CG1   . VAL B 1 316 ? -8.806  19.436  -14.818 1.00 23.44 ? 295 VAL B CG1   1 
ATOM   5488 C  CG2   . VAL B 1 316 ? -8.093  17.030  -15.026 1.00 23.61 ? 295 VAL B CG2   1 
ATOM   5489 N  N     . LYS B 1 317 ? -11.508 19.271  -12.579 1.00 23.47 ? 296 LYS B N     1 
ATOM   5490 C  CA    . LYS B 1 317 ? -12.608 20.256  -12.356 1.00 27.66 ? 296 LYS B CA    1 
ATOM   5491 C  C     . LYS B 1 317 ? -12.037 21.679  -12.416 1.00 27.01 ? 296 LYS B C     1 
ATOM   5492 O  O     . LYS B 1 317 ? -11.018 21.950  -11.704 1.00 23.75 ? 296 LYS B O     1 
ATOM   5493 C  CB    . LYS B 1 317 ? -13.310 20.057  -11.008 1.00 28.03 ? 296 LYS B CB    1 
ATOM   5494 C  CG    . LYS B 1 317 ? -14.472 21.010  -10.749 1.00 30.97 ? 296 LYS B CG    1 
ATOM   5495 C  CD    . LYS B 1 317 ? -15.054 20.950  -9.320  1.00 33.18 ? 296 LYS B CD    1 
ATOM   5496 C  CE    . LYS B 1 317 ? -16.218 21.901  -9.125  1.00 33.37 ? 296 LYS B CE    1 
ATOM   5497 N  NZ    . LYS B 1 317 ? -17.080 21.487  -7.998  1.00 36.15 ? 296 LYS B NZ    1 
ATOM   5498 N  N     . PHE B 1 318 ? -12.680 22.564  -13.187 1.00 25.78 ? 297 PHE B N     1 
ATOM   5499 C  CA    . PHE B 1 318 ? -12.170 23.952  -13.381 1.00 26.68 ? 297 PHE B CA    1 
ATOM   5500 C  C     . PHE B 1 318 ? -13.225 24.984  -12.995 1.00 26.03 ? 297 PHE B C     1 
ATOM   5501 O  O     . PHE B 1 318 ? -14.450 24.698  -13.113 1.00 27.61 ? 297 PHE B O     1 
ATOM   5502 C  CB    . PHE B 1 318 ? -11.679 24.180  -14.813 1.00 23.62 ? 297 PHE B CB    1 
ATOM   5503 C  CG    . PHE B 1 318 ? -12.690 23.913  -15.900 1.00 25.62 ? 297 PHE B CG    1 
ATOM   5504 C  CD1   . PHE B 1 318 ? -12.752 22.671  -16.514 1.00 27.73 ? 297 PHE B CD1   1 
ATOM   5505 C  CD2   . PHE B 1 318 ? -13.528 24.911  -16.362 1.00 25.38 ? 297 PHE B CD2   1 
ATOM   5506 C  CE1   . PHE B 1 318 ? -13.643 22.425  -17.546 1.00 29.66 ? 297 PHE B CE1   1 
ATOM   5507 C  CE2   . PHE B 1 318 ? -14.426 24.660  -17.387 1.00 29.68 ? 297 PHE B CE2   1 
ATOM   5508 C  CZ    . PHE B 1 318 ? -14.473 23.423  -17.996 1.00 30.59 ? 297 PHE B CZ    1 
ATOM   5509 N  N     . HIS B 1 319 ? -12.735 26.169  -12.623 1.00 28.49 ? 298 HIS B N     1 
ATOM   5510 C  CA    . HIS B 1 319 ? -13.513 27.440  -12.472 1.00 31.85 ? 298 HIS B CA    1 
ATOM   5511 C  C     . HIS B 1 319 ? -12.858 28.560  -13.300 1.00 31.22 ? 298 HIS B C     1 
ATOM   5512 O  O     . HIS B 1 319 ? -11.653 28.807  -13.125 1.00 28.55 ? 298 HIS B O     1 
ATOM   5513 C  CB    . HIS B 1 319 ? -13.641 27.834  -10.988 1.00 28.06 ? 298 HIS B CB    1 
ATOM   5514 C  CG    . HIS B 1 319 ? -14.317 26.812  -10.140 1.00 26.60 ? 298 HIS B CG    1 
ATOM   5515 N  ND1   . HIS B 1 319 ? -15.680 26.610  -10.177 1.00 29.12 ? 298 HIS B ND1   1 
ATOM   5516 C  CD2   . HIS B 1 319 ? -13.828 25.933  -9.239  1.00 26.92 ? 298 HIS B CD2   1 
ATOM   5517 C  CE1   . HIS B 1 319 ? -16.010 25.664  -9.311  1.00 28.09 ? 298 HIS B CE1   1 
ATOM   5518 N  NE2   . HIS B 1 319 ? -14.890 25.222  -8.733  1.00 26.46 ? 298 HIS B NE2   1 
ATOM   5519 N  N     . VAL B 1 320 ? -13.613 29.209  -14.189 1.00 32.41 ? 299 VAL B N     1 
ATOM   5520 C  CA    . VAL B 1 320 ? -13.068 30.337  -15.000 1.00 34.46 ? 299 VAL B CA    1 
ATOM   5521 C  C     . VAL B 1 320 ? -13.570 31.643  -14.378 1.00 32.78 ? 299 VAL B C     1 
ATOM   5522 O  O     . VAL B 1 320 ? -14.785 31.859  -14.410 1.00 26.67 ? 299 VAL B O     1 
ATOM   5523 C  CB    . VAL B 1 320 ? -13.452 30.235  -16.490 1.00 35.55 ? 299 VAL B CB    1 
ATOM   5524 C  CG1   . VAL B 1 320 ? -12.727 31.293  -17.314 1.00 36.35 ? 299 VAL B CG1   1 
ATOM   5525 C  CG2   . VAL B 1 320 ? -13.192 28.849  -17.068 1.00 36.25 ? 299 VAL B CG2   1 
ATOM   5526 N  N     . ILE B 1 321 ? -12.659 32.453  -13.831 1.00 32.54 ? 300 ILE B N     1 
ATOM   5527 C  CA    . ILE B 1 321 ? -12.973 33.717  -13.097 1.00 36.26 ? 300 ILE B CA    1 
ATOM   5528 C  C     . ILE B 1 321 ? -13.126 34.859  -14.124 1.00 40.06 ? 300 ILE B C     1 
ATOM   5529 O  O     . ILE B 1 321 ? -12.157 35.101  -14.908 1.00 32.32 ? 300 ILE B O     1 
ATOM   5530 C  CB    . ILE B 1 321 ? -11.880 34.034  -12.046 1.00 40.10 ? 300 ILE B CB    1 
ATOM   5531 C  CG1   . ILE B 1 321 ? -11.423 32.808  -11.236 1.00 37.89 ? 300 ILE B CG1   1 
ATOM   5532 C  CG2   . ILE B 1 321 ? -12.349 35.161  -11.141 1.00 39.52 ? 300 ILE B CG2   1 
ATOM   5533 C  CD1   . ILE B 1 321 ? -12.531 32.108  -10.476 1.00 37.67 ? 300 ILE B CD1   1 
ATOM   5534 N  N     . TYR B 1 322 ? -14.313 35.486  -14.170 1.00 39.16 ? 301 TYR B N     1 
ATOM   5535 C  CA    . TYR B 1 322 ? -14.577 36.777  -14.854 1.00 38.71 ? 301 TYR B CA    1 
ATOM   5536 C  C     . TYR B 1 322 ? -15.052 37.799  -13.814 1.00 46.20 ? 301 TYR B C     1 
ATOM   5537 O  O     . TYR B 1 322 ? -15.695 37.398  -12.791 1.00 47.09 ? 301 TYR B O     1 
ATOM   5538 C  CB    . TYR B 1 322 ? -15.618 36.642  -15.965 1.00 38.84 ? 301 TYR B CB    1 
ATOM   5539 C  CG    . TYR B 1 322 ? -15.299 35.596  -17.005 1.00 37.48 ? 301 TYR B CG    1 
ATOM   5540 C  CD1   . TYR B 1 322 ? -14.582 35.913  -18.141 1.00 34.91 ? 301 TYR B CD1   1 
ATOM   5541 C  CD2   . TYR B 1 322 ? -15.709 34.278  -16.849 1.00 32.75 ? 301 TYR B CD2   1 
ATOM   5542 C  CE1   . TYR B 1 322 ? -14.271 34.951  -19.092 1.00 34.39 ? 301 TYR B CE1   1 
ATOM   5543 C  CE2   . TYR B 1 322 ? -15.437 33.315  -17.802 1.00 31.20 ? 301 TYR B CE2   1 
ATOM   5544 C  CZ    . TYR B 1 322 ? -14.696 33.641  -18.926 1.00 32.45 ? 301 TYR B CZ    1 
ATOM   5545 O  OH    . TYR B 1 322 ? -14.381 32.675  -19.851 1.00 28.31 ? 301 TYR B OH    1 
ATOM   5546 N  N     . ASP B 1 323 ? -14.726 39.077  -14.048 1.00 45.27 ? 302 ASP B N     1 
ATOM   5547 C  CA    . ASP B 1 323 ? -15.146 40.221  -13.193 1.00 44.86 ? 302 ASP B CA    1 
ATOM   5548 C  C     . ASP B 1 323 ? -16.669 40.187  -12.996 1.00 41.02 ? 302 ASP B C     1 
ATOM   5549 O  O     . ASP B 1 323 ? -17.089 40.514  -11.882 1.00 40.99 ? 302 ASP B O     1 
ATOM   5550 C  CB    . ASP B 1 323 ? -14.748 41.579  -13.783 1.00 44.62 ? 302 ASP B CB    1 
ATOM   5551 C  CG    . ASP B 1 323 ? -13.252 41.829  -13.850 1.00 49.05 ? 302 ASP B CG    1 
ATOM   5552 O  OD1   . ASP B 1 323 ? -12.491 41.171  -13.079 1.00 49.52 ? 302 ASP B OD1   1 
ATOM   5553 O  OD2   . ASP B 1 323 ? -12.851 42.657  -14.703 1.00 51.46 ? 302 ASP B OD2   1 
ATOM   5554 N  N     . GLU B 1 324 ? -17.445 39.832  -14.029 1.00 37.20 ? 303 GLU B N     1 
ATOM   5555 C  CA    . GLU B 1 324 ? -18.933 39.789  -13.989 1.00 39.80 ? 303 GLU B CA    1 
ATOM   5556 C  C     . GLU B 1 324 ? -19.441 38.550  -14.703 1.00 36.69 ? 303 GLU B C     1 
ATOM   5557 O  O     . GLU B 1 324 ? -18.783 38.065  -15.614 1.00 40.23 ? 303 GLU B O     1 
ATOM   5558 C  CB    . GLU B 1 324 ? -19.556 40.999  -14.690 1.00 43.45 ? 303 GLU B CB    1 
ATOM   5559 C  CG    . GLU B 1 324 ? -19.290 42.309  -13.979 1.00 48.66 ? 303 GLU B CG    1 
ATOM   5560 C  CD    . GLU B 1 324 ? -20.266 43.432  -14.282 1.00 51.80 ? 303 GLU B CD    1 
ATOM   5561 O  OE1   . GLU B 1 324 ? -20.648 44.150  -13.334 1.00 57.30 ? 303 GLU B OE1   1 
ATOM   5562 O  OE2   . GLU B 1 324 ? -20.644 43.585  -15.453 1.00 56.70 ? 303 GLU B OE2   1 
ATOM   5563 N  N     . PRO B 1 325 ? -20.655 38.051  -14.368 1.00 38.63 ? 304 PRO B N     1 
ATOM   5564 C  CA    . PRO B 1 325 ? -21.347 37.051  -15.191 1.00 39.38 ? 304 PRO B CA    1 
ATOM   5565 C  C     . PRO B 1 325 ? -21.936 37.687  -16.464 1.00 39.81 ? 304 PRO B C     1 
ATOM   5566 O  O     . PRO B 1 325 ? -23.162 37.673  -16.644 1.00 37.18 ? 304 PRO B O     1 
ATOM   5567 C  CB    . PRO B 1 325 ? -22.428 36.485  -14.253 1.00 37.29 ? 304 PRO B CB    1 
ATOM   5568 C  CG    . PRO B 1 325 ? -22.744 37.655  -13.331 1.00 37.82 ? 304 PRO B CG    1 
ATOM   5569 C  CD    . PRO B 1 325 ? -21.437 38.414  -13.178 1.00 38.85 ? 304 PRO B CD    1 
ATOM   5570 N  N     . TRP B 1 326 ? -21.043 38.182  -17.335 1.00 38.21 ? 305 TRP B N     1 
ATOM   5571 C  CA    . TRP B 1 326 ? -21.379 38.906  -18.585 1.00 36.66 ? 305 TRP B CA    1 
ATOM   5572 C  C     . TRP B 1 326 ? -22.423 38.108  -19.366 1.00 36.87 ? 305 TRP B C     1 
ATOM   5573 O  O     . TRP B 1 326 ? -23.296 38.740  -19.991 1.00 39.07 ? 305 TRP B O     1 
ATOM   5574 C  CB    . TRP B 1 326 ? -20.119 39.154  -19.422 1.00 35.85 ? 305 TRP B CB    1 
ATOM   5575 C  CG    . TRP B 1 326 ? -19.420 37.896  -19.835 1.00 34.67 ? 305 TRP B CG    1 
ATOM   5576 C  CD1   . TRP B 1 326 ? -18.429 37.256  -19.153 1.00 31.06 ? 305 TRP B CD1   1 
ATOM   5577 C  CD2   . TRP B 1 326 ? -19.666 37.127  -21.024 1.00 30.57 ? 305 TRP B CD2   1 
ATOM   5578 N  NE1   . TRP B 1 326 ? -18.038 36.144  -19.840 1.00 32.23 ? 305 TRP B NE1   1 
ATOM   5579 C  CE2   . TRP B 1 326 ? -18.790 36.021  -20.978 1.00 33.18 ? 305 TRP B CE2   1 
ATOM   5580 C  CE3   . TRP B 1 326 ? -20.551 37.249  -22.110 1.00 32.45 ? 305 TRP B CE3   1 
ATOM   5581 C  CZ2   . TRP B 1 326 ? -18.755 35.051  -21.992 1.00 32.75 ? 305 TRP B CZ2   1 
ATOM   5582 C  CZ3   . TRP B 1 326 ? -20.535 36.284  -23.098 1.00 32.14 ? 305 TRP B CZ3   1 
ATOM   5583 C  CH2   . TRP B 1 326 ? -19.648 35.199  -23.038 1.00 32.65 ? 305 TRP B CH2   1 
ATOM   5584 N  N     . TRP B 1 327 ? -22.346 36.774  -19.314 1.00 33.81 ? 306 TRP B N     1 
ATOM   5585 C  CA    . TRP B 1 327 ? -23.248 35.860  -20.071 1.00 32.52 ? 306 TRP B CA    1 
ATOM   5586 C  C     . TRP B 1 327 ? -24.735 36.064  -19.729 1.00 32.99 ? 306 TRP B C     1 
ATOM   5587 O  O     . TRP B 1 327 ? -25.571 35.823  -20.625 1.00 33.75 ? 306 TRP B O     1 
ATOM   5588 C  CB    . TRP B 1 327 ? -22.824 34.391  -19.912 1.00 32.59 ? 306 TRP B CB    1 
ATOM   5589 C  CG    . TRP B 1 327 ? -22.634 33.890  -18.512 1.00 28.36 ? 306 TRP B CG    1 
ATOM   5590 C  CD1   . TRP B 1 327 ? -23.579 33.319  -17.709 1.00 27.98 ? 306 TRP B CD1   1 
ATOM   5591 C  CD2   . TRP B 1 327 ? -21.414 33.914  -17.748 1.00 26.09 ? 306 TRP B CD2   1 
ATOM   5592 N  NE1   . TRP B 1 327 ? -23.030 32.979  -16.508 1.00 28.72 ? 306 TRP B NE1   1 
ATOM   5593 C  CE2   . TRP B 1 327 ? -21.704 33.330  -16.501 1.00 27.09 ? 306 TRP B CE2   1 
ATOM   5594 C  CE3   . TRP B 1 327 ? -20.109 34.346  -18.004 1.00 24.52 ? 306 TRP B CE3   1 
ATOM   5595 C  CZ2   . TRP B 1 327 ? -20.733 33.173  -15.520 1.00 25.46 ? 306 TRP B CZ2   1 
ATOM   5596 C  CZ3   . TRP B 1 327 ? -19.146 34.189  -17.039 1.00 24.64 ? 306 TRP B CZ3   1 
ATOM   5597 C  CH2   . TRP B 1 327 ? -19.458 33.611  -15.810 1.00 25.83 ? 306 TRP B CH2   1 
ATOM   5598 N  N     . ARG B 1 328 ? -25.085 36.502  -18.518 1.00 33.87 ? 307 ARG B N     1 
ATOM   5599 C  CA    . ARG B 1 328 ? -26.503 36.767  -18.155 1.00 36.87 ? 307 ARG B CA    1 
ATOM   5600 C  C     . ARG B 1 328 ? -27.038 37.916  -19.026 1.00 47.53 ? 307 ARG B C     1 
ATOM   5601 O  O     . ARG B 1 328 ? -28.246 37.861  -19.388 1.00 48.80 ? 307 ARG B O     1 
ATOM   5602 C  CB    . ARG B 1 328 ? -26.625 37.047  -16.658 1.00 40.78 ? 307 ARG B CB    1 
ATOM   5603 C  CG    . ARG B 1 328 ? -26.284 35.842  -15.791 1.00 37.66 ? 307 ARG B CG    1 
ATOM   5604 C  CD    . ARG B 1 328 ? -26.752 35.985  -14.363 1.00 39.12 ? 307 ARG B CD    1 
ATOM   5605 N  NE    . ARG B 1 328 ? -26.061 35.017  -13.513 1.00 39.77 ? 307 ARG B NE    1 
ATOM   5606 C  CZ    . ARG B 1 328 ? -25.996 35.046  -12.185 1.00 39.70 ? 307 ARG B CZ    1 
ATOM   5607 N  NH1   . ARG B 1 328 ? -26.588 36.010  -11.493 1.00 39.80 ? 307 ARG B NH1   1 
ATOM   5608 N  NH2   . ARG B 1 328 ? -25.312 34.105  -11.551 1.00 38.93 ? 307 ARG B NH2   1 
ATOM   5609 N  N     . ALA B 1 329 ? -26.163 38.865  -19.416 1.00 49.86 ? 308 ALA B N     1 
ATOM   5610 C  CA    . ALA B 1 329 ? -26.470 40.008  -20.315 1.00 47.21 ? 308 ALA B CA    1 
ATOM   5611 C  C     . ALA B 1 329 ? -27.007 39.488  -21.652 1.00 46.75 ? 308 ALA B C     1 
ATOM   5612 O  O     . ALA B 1 329 ? -27.960 40.085  -22.144 1.00 41.27 ? 308 ALA B O     1 
ATOM   5613 C  CB    . ALA B 1 329 ? -25.252 40.887  -20.526 1.00 41.12 ? 308 ALA B CB    1 
ATOM   5614 N  N     . GLU B 1 330 ? -26.401 38.422  -22.188 1.00 45.61 ? 309 GLU B N     1 
ATOM   5615 C  CA    . GLU B 1 330 ? -26.695 37.839  -23.525 1.00 48.75 ? 309 GLU B CA    1 
ATOM   5616 C  C     . GLU B 1 330 ? -27.910 36.904  -23.461 1.00 44.96 ? 309 GLU B C     1 
ATOM   5617 O  O     . GLU B 1 330 ? -28.233 36.300  -24.508 1.00 44.30 ? 309 GLU B O     1 
ATOM   5618 C  CB    . GLU B 1 330 ? -25.506 37.015  -24.053 1.00 51.61 ? 309 GLU B CB    1 
ATOM   5619 C  CG    . GLU B 1 330 ? -24.173 37.743  -24.080 1.00 52.77 ? 309 GLU B CG    1 
ATOM   5620 C  CD    . GLU B 1 330 ? -24.229 39.179  -24.561 1.00 57.06 ? 309 GLU B CD    1 
ATOM   5621 O  OE1   . GLU B 1 330 ? -23.592 40.038  -23.907 1.00 56.57 ? 309 GLU B OE1   1 
ATOM   5622 O  OE2   . GLU B 1 330 ? -24.925 39.439  -25.581 1.00 59.12 ? 309 GLU B OE2   1 
ATOM   5623 N  N     . GLY B 1 331 ? -28.535 36.743  -22.291 1.00 44.68 ? 310 GLY B N     1 
ATOM   5624 C  CA    . GLY B 1 331 ? -29.709 35.861  -22.106 1.00 45.46 ? 310 GLY B CA    1 
ATOM   5625 C  C     . GLY B 1 331 ? -29.303 34.404  -22.108 1.00 41.39 ? 310 GLY B C     1 
ATOM   5626 O  O     . GLY B 1 331 ? -30.100 33.582  -22.562 1.00 41.50 ? 310 GLY B O     1 
ATOM   5627 N  N     . LEU B 1 332 ? -28.089 34.115  -21.627 1.00 44.40 ? 311 LEU B N     1 
ATOM   5628 C  CA    . LEU B 1 332 ? -27.460 32.762  -21.598 1.00 44.14 ? 311 LEU B CA    1 
ATOM   5629 C  C     . LEU B 1 332 ? -27.363 32.255  -20.155 1.00 40.53 ? 311 LEU B C     1 
ATOM   5630 O  O     . LEU B 1 332 ? -26.926 33.054  -19.289 1.00 41.21 ? 311 LEU B O     1 
ATOM   5631 C  CB    . LEU B 1 332 ? -26.046 32.841  -22.190 1.00 45.76 ? 311 LEU B CB    1 
ATOM   5632 C  CG    . LEU B 1 332 ? -25.921 33.313  -23.635 1.00 46.39 ? 311 LEU B CG    1 
ATOM   5633 C  CD1   . LEU B 1 332 ? -24.466 33.647  -23.943 1.00 46.51 ? 311 LEU B CD1   1 
ATOM   5634 C  CD2   . LEU B 1 332 ? -26.454 32.262  -24.599 1.00 45.67 ? 311 LEU B CD2   1 
ATOM   5635 N  N     . SER B 1 333 ? -27.665 30.966  -19.930 1.00 38.46 ? 312 SER B N     1 
ATOM   5636 C  CA    . SER B 1 333 ? -27.492 30.251  -18.631 1.00 36.53 ? 312 SER B CA    1 
ATOM   5637 C  C     . SER B 1 333 ? -26.031 30.252  -18.177 1.00 33.56 ? 312 SER B C     1 
ATOM   5638 O  O     . SER B 1 333 ? -25.788 30.432  -16.992 1.00 36.90 ? 312 SER B O     1 
ATOM   5639 C  CB    . SER B 1 333 ? -28.010 28.834  -18.702 1.00 38.94 ? 312 SER B CB    1 
ATOM   5640 O  OG    . SER B 1 333 ? -27.330 28.081  -19.696 1.00 41.18 ? 312 SER B OG    1 
ATOM   5641 N  N     . GLY B 1 334 ? -25.083 30.052  -19.090 1.00 35.34 ? 313 GLY B N     1 
ATOM   5642 C  CA    . GLY B 1 334 ? -23.686 29.743  -18.736 1.00 31.57 ? 313 GLY B CA    1 
ATOM   5643 C  C     . GLY B 1 334 ? -23.403 28.255  -18.832 1.00 31.38 ? 313 GLY B C     1 
ATOM   5644 O  O     . GLY B 1 334 ? -22.263 27.870  -18.524 1.00 36.13 ? 313 GLY B O     1 
ATOM   5645 N  N     . THR B 1 335 ? -24.387 27.449  -19.255 1.00 30.28 ? 314 THR B N     1 
ATOM   5646 C  CA    . THR B 1 335 ? -24.238 25.990  -19.509 1.00 31.02 ? 314 THR B CA    1 
ATOM   5647 C  C     . THR B 1 335 ? -24.016 25.767  -21.001 1.00 31.81 ? 314 THR B C     1 
ATOM   5648 O  O     . THR B 1 335 ? -24.909 26.227  -21.780 1.00 27.49 ? 314 THR B O     1 
ATOM   5649 C  CB    . THR B 1 335 ? -25.479 25.186  -19.104 1.00 30.59 ? 314 THR B CB    1 
ATOM   5650 O  OG1   . THR B 1 335 ? -25.454 25.047  -17.681 1.00 32.34 ? 314 THR B OG1   1 
ATOM   5651 C  CG2   . THR B 1 335 ? -25.537 23.824  -19.767 1.00 28.62 ? 314 THR B CG2   1 
ATOM   5652 N  N     . VAL B 1 336 ? -22.893 25.105  -21.357 1.00 33.68 ? 315 VAL B N     1 
ATOM   5653 C  CA    . VAL B 1 336 ? -22.607 24.552  -22.731 1.00 34.09 ? 315 VAL B CA    1 
ATOM   5654 C  C     . VAL B 1 336 ? -22.527 23.025  -22.645 1.00 31.51 ? 315 VAL B C     1 
ATOM   5655 O  O     . VAL B 1 336 ? -21.955 22.516  -21.660 1.00 27.94 ? 315 VAL B O     1 
ATOM   5656 C  CB    . VAL B 1 336 ? -21.325 25.132  -23.364 1.00 32.71 ? 315 VAL B CB    1 
ATOM   5657 C  CG1   . VAL B 1 336 ? -21.179 26.611  -23.056 1.00 32.49 ? 315 VAL B CG1   1 
ATOM   5658 C  CG2   . VAL B 1 336 ? -20.069 24.382  -22.943 1.00 34.04 ? 315 VAL B CG2   1 
ATOM   5659 N  N     . LEU B 1 337 ? -23.099 22.331  -23.634 1.00 32.15 ? 316 LEU B N     1 
ATOM   5660 C  CA    . LEU B 1 337 ? -23.124 20.851  -23.707 1.00 33.00 ? 316 LEU B CA    1 
ATOM   5661 C  C     . LEU B 1 337 ? -22.487 20.387  -25.022 1.00 33.31 ? 316 LEU B C     1 
ATOM   5662 O  O     . LEU B 1 337 ? -23.083 20.632  -26.117 1.00 33.73 ? 316 LEU B O     1 
ATOM   5663 C  CB    . LEU B 1 337 ? -24.578 20.370  -23.591 1.00 39.51 ? 316 LEU B CB    1 
ATOM   5664 C  CG    . LEU B 1 337 ? -24.754 18.888  -23.238 1.00 41.05 ? 316 LEU B CG    1 
ATOM   5665 C  CD1   . LEU B 1 337 ? -24.156 18.598  -21.878 1.00 42.61 ? 316 LEU B CD1   1 
ATOM   5666 C  CD2   . LEU B 1 337 ? -26.222 18.477  -23.250 1.00 45.88 ? 316 LEU B CD2   1 
ATOM   5667 N  N     . CYS B 1 338 ? -21.341 19.702  -24.929 1.00 33.74 ? 317 CYS B N     1 
ATOM   5668 C  CA    . CYS B 1 338 ? -20.461 19.415  -26.095 1.00 34.55 ? 317 CYS B CA    1 
ATOM   5669 C  C     . CYS B 1 338 ? -20.015 17.960  -26.081 1.00 34.57 ? 317 CYS B C     1 
ATOM   5670 O  O     . CYS B 1 338 ? -19.006 17.644  -25.448 1.00 34.28 ? 317 CYS B O     1 
ATOM   5671 C  CB    . CYS B 1 338 ? -19.264 20.353  -26.095 1.00 37.19 ? 317 CYS B CB    1 
ATOM   5672 S  SG    . CYS B 1 338 ? -19.702 22.097  -26.347 1.00 43.72 ? 317 CYS B SG    1 
ATOM   5673 N  N     . PRO B 1 339 ? -20.771 17.056  -26.763 1.00 34.62 ? 318 PRO B N     1 
ATOM   5674 C  CA    . PRO B 1 339 ? -20.399 15.645  -26.905 1.00 33.46 ? 318 PRO B CA    1 
ATOM   5675 C  C     . PRO B 1 339 ? -19.001 15.385  -27.486 1.00 33.78 ? 318 PRO B C     1 
ATOM   5676 O  O     . PRO B 1 339 ? -18.384 14.433  -27.038 1.00 28.57 ? 318 PRO B O     1 
ATOM   5677 C  CB    . PRO B 1 339 ? -21.429 15.097  -27.899 1.00 34.83 ? 318 PRO B CB    1 
ATOM   5678 C  CG    . PRO B 1 339 ? -22.634 15.997  -27.706 1.00 35.38 ? 318 PRO B CG    1 
ATOM   5679 C  CD    . PRO B 1 339 ? -22.039 17.358  -27.450 1.00 34.60 ? 318 PRO B CD    1 
ATOM   5680 N  N     . ASP B 1 340 ? -18.537 16.248  -28.407 1.00 31.94 ? 319 ASP B N     1 
ATOM   5681 C  CA    . ASP B 1 340 ? -17.312 16.035  -29.218 1.00 32.48 ? 319 ASP B CA    1 
ATOM   5682 C  C     . ASP B 1 340 ? -16.207 17.044  -28.833 1.00 32.90 ? 319 ASP B C     1 
ATOM   5683 O  O     . ASP B 1 340 ? -15.178 17.059  -29.520 1.00 33.93 ? 319 ASP B O     1 
ATOM   5684 C  CB    . ASP B 1 340 ? -17.692 16.041  -30.698 1.00 34.44 ? 319 ASP B CB    1 
ATOM   5685 C  CG    . ASP B 1 340 ? -18.774 15.018  -31.050 1.00 35.79 ? 319 ASP B CG    1 
ATOM   5686 O  OD1   . ASP B 1 340 ? -18.561 13.825  -30.756 1.00 37.29 ? 319 ASP B OD1   1 
ATOM   5687 O  OD2   . ASP B 1 340 ? -19.826 15.412  -31.614 1.00 33.02 ? 319 ASP B OD2   1 
ATOM   5688 N  N     . GLU B 1 341 ? -16.346 17.813  -27.742 1.00 31.63 ? 320 GLU B N     1 
ATOM   5689 C  CA    . GLU B 1 341 ? -15.269 18.715  -27.236 1.00 29.22 ? 320 GLU B CA    1 
ATOM   5690 C  C     . GLU B 1 341 ? -14.610 18.065  -26.022 1.00 30.40 ? 320 GLU B C     1 
ATOM   5691 O  O     . GLU B 1 341 ? -15.169 17.162  -25.424 1.00 26.55 ? 320 GLU B O     1 
ATOM   5692 C  CB    . GLU B 1 341 ? -15.827 20.086  -26.866 1.00 30.25 ? 320 GLU B CB    1 
ATOM   5693 C  CG    . GLU B 1 341 ? -16.484 20.831  -28.019 1.00 29.57 ? 320 GLU B CG    1 
ATOM   5694 C  CD    . GLU B 1 341 ? -15.566 21.096  -29.196 1.00 26.93 ? 320 GLU B CD    1 
ATOM   5695 O  OE1   . GLU B 1 341 ? -16.069 21.273  -30.319 1.00 25.79 ? 320 GLU B OE1   1 
ATOM   5696 O  OE2   . GLU B 1 341 ? -14.365 21.123  -28.970 1.00 24.52 ? 320 GLU B OE2   1 
ATOM   5697 N  N     . PRO B 1 342 ? -13.393 18.475  -25.608 1.00 31.69 ? 321 PRO B N     1 
ATOM   5698 C  CA    . PRO B 1 342 ? -12.764 17.897  -24.418 1.00 32.93 ? 321 PRO B CA    1 
ATOM   5699 C  C     . PRO B 1 342 ? -13.522 18.251  -23.132 1.00 32.27 ? 321 PRO B C     1 
ATOM   5700 O  O     . PRO B 1 342 ? -13.337 17.576  -22.163 1.00 33.07 ? 321 PRO B O     1 
ATOM   5701 C  CB    . PRO B 1 342 ? -11.374 18.543  -24.359 1.00 29.66 ? 321 PRO B CB    1 
ATOM   5702 C  CG    . PRO B 1 342 ? -11.181 19.119  -25.729 1.00 30.03 ? 321 PRO B CG    1 
ATOM   5703 C  CD    . PRO B 1 342 ? -12.554 19.495  -26.240 1.00 29.88 ? 321 PRO B CD    1 
ATOM   5704 N  N     . ILE B 1 343 ? -14.320 19.314  -23.175 1.00 31.84 ? 322 ILE B N     1 
ATOM   5705 C  CA    . ILE B 1 343 ? -15.148 19.850  -22.050 1.00 34.53 ? 322 ILE B CA    1 
ATOM   5706 C  C     . ILE B 1 343 ? -16.587 19.321  -22.185 1.00 35.61 ? 322 ILE B C     1 
ATOM   5707 O  O     . ILE B 1 343 ? -17.239 19.608  -23.215 1.00 37.31 ? 322 ILE B O     1 
ATOM   5708 C  CB    . ILE B 1 343 ? -15.076 21.398  -22.085 1.00 37.91 ? 322 ILE B CB    1 
ATOM   5709 C  CG1   . ILE B 1 343 ? -13.670 21.891  -21.741 1.00 37.58 ? 322 ILE B CG1   1 
ATOM   5710 C  CG2   . ILE B 1 343 ? -16.133 22.072  -21.216 1.00 40.47 ? 322 ILE B CG2   1 
ATOM   5711 C  CD1   . ILE B 1 343 ? -12.964 21.027  -20.743 1.00 41.15 ? 322 ILE B CD1   1 
ATOM   5712 N  N     . GLY B 1 344 ? -17.092 18.632  -21.162 1.00 36.52 ? 323 GLY B N     1 
ATOM   5713 C  CA    . GLY B 1 344 ? -18.425 17.996  -21.184 1.00 40.32 ? 323 GLY B CA    1 
ATOM   5714 C  C     . GLY B 1 344 ? -19.565 18.983  -20.965 1.00 41.06 ? 323 GLY B C     1 
ATOM   5715 O  O     . GLY B 1 344 ? -20.205 19.408  -21.981 1.00 39.46 ? 323 GLY B O     1 
ATOM   5716 N  N     . VAL B 1 345 ? -19.832 19.300  -19.691 1.00 36.55 ? 324 VAL B N     1 
ATOM   5717 C  CA    . VAL B 1 345 ? -20.952 20.178  -19.258 1.00 36.22 ? 324 VAL B CA    1 
ATOM   5718 C  C     . VAL B 1 345 ? -20.409 21.320  -18.398 1.00 34.97 ? 324 VAL B C     1 
ATOM   5719 O  O     . VAL B 1 345 ? -19.490 21.090  -17.583 1.00 38.07 ? 324 VAL B O     1 
ATOM   5720 C  CB    . VAL B 1 345 ? -22.028 19.360  -18.528 1.00 41.36 ? 324 VAL B CB    1 
ATOM   5721 C  CG1   . VAL B 1 345 ? -21.575 18.927  -17.133 1.00 46.64 ? 324 VAL B CG1   1 
ATOM   5722 C  CG2   . VAL B 1 345 ? -23.358 20.101  -18.494 1.00 40.74 ? 324 VAL B CG2   1 
ATOM   5723 N  N     . THR B 1 346 ? -20.896 22.536  -18.632 1.00 30.77 ? 325 THR B N     1 
ATOM   5724 C  CA    . THR B 1 346 ? -20.518 23.719  -17.821 1.00 31.36 ? 325 THR B CA    1 
ATOM   5725 C  C     . THR B 1 346 ? -21.746 24.190  -17.033 1.00 28.13 ? 325 THR B C     1 
ATOM   5726 O  O     . THR B 1 346 ? -22.894 23.857  -17.447 1.00 30.18 ? 325 THR B O     1 
ATOM   5727 C  CB    . THR B 1 346 ? -19.859 24.825  -18.663 1.00 29.23 ? 325 THR B CB    1 
ATOM   5728 O  OG1   . THR B 1 346 ? -20.736 25.283  -19.695 1.00 24.69 ? 325 THR B OG1   1 
ATOM   5729 C  CG2   . THR B 1 346 ? -18.550 24.352  -19.247 1.00 31.25 ? 325 THR B CG2   1 
ATOM   5730 N  N     . PHE B 1 347 ? -21.486 24.955  -15.977 1.00 28.32 ? 326 PHE B N     1 
ATOM   5731 C  CA    . PHE B 1 347 ? -22.479 25.490  -15.019 1.00 32.62 ? 326 PHE B CA    1 
ATOM   5732 C  C     . PHE B 1 347 ? -22.031 26.879  -14.567 1.00 34.03 ? 326 PHE B C     1 
ATOM   5733 O  O     . PHE B 1 347 ? -20.830 27.058  -14.222 1.00 33.55 ? 326 PHE B O     1 
ATOM   5734 C  CB    . PHE B 1 347 ? -22.587 24.555  -13.807 1.00 36.02 ? 326 PHE B CB    1 
ATOM   5735 C  CG    . PHE B 1 347 ? -23.284 23.247  -14.087 1.00 32.56 ? 326 PHE B CG    1 
ATOM   5736 C  CD1   . PHE B 1 347 ? -24.666 23.163  -14.062 1.00 33.61 ? 326 PHE B CD1   1 
ATOM   5737 C  CD2   . PHE B 1 347 ? -22.563 22.102  -14.383 1.00 33.74 ? 326 PHE B CD2   1 
ATOM   5738 C  CE1   . PHE B 1 347 ? -25.319 21.958  -14.309 1.00 33.91 ? 326 PHE B CE1   1 
ATOM   5739 C  CE2   . PHE B 1 347 ? -23.212 20.896  -14.620 1.00 34.79 ? 326 PHE B CE2   1 
ATOM   5740 C  CZ    . PHE B 1 347 ? -24.594 20.822  -14.578 1.00 33.67 ? 326 PHE B CZ    1 
ATOM   5741 N  N     . ASP B 1 348 ? -22.974 27.826  -14.568 1.00 33.90 ? 327 ASP B N     1 
ATOM   5742 C  CA    . ASP B 1 348 ? -22.828 29.159  -13.927 1.00 30.76 ? 327 ASP B CA    1 
ATOM   5743 C  C     . ASP B 1 348 ? -22.523 28.951  -12.439 1.00 29.16 ? 327 ASP B C     1 
ATOM   5744 O  O     . ASP B 1 348 ? -23.466 28.517  -11.740 1.00 32.80 ? 327 ASP B O     1 
ATOM   5745 C  CB    . ASP B 1 348 ? -24.099 29.996  -14.112 1.00 31.16 ? 327 ASP B CB    1 
ATOM   5746 C  CG    . ASP B 1 348 ? -23.966 31.430  -13.623 1.00 30.87 ? 327 ASP B CG    1 
ATOM   5747 O  OD1   . ASP B 1 348 ? -23.093 31.710  -12.761 1.00 33.73 ? 327 ASP B OD1   1 
ATOM   5748 O  OD2   . ASP B 1 348 ? -24.733 32.252  -14.097 1.00 31.65 ? 327 ASP B OD2   1 
ATOM   5749 N  N     . GLY B 1 349 ? -21.297 29.286  -11.998 1.00 26.70 ? 328 GLY B N     1 
ATOM   5750 C  CA    . GLY B 1 349 ? -20.736 29.105  -10.639 1.00 24.84 ? 328 GLY B CA    1 
ATOM   5751 C  C     . GLY B 1 349 ? -20.629 30.402  -9.834  1.00 24.79 ? 328 GLY B C     1 
ATOM   5752 O  O     . GLY B 1 349 ? -20.003 30.399  -8.766  1.00 22.66 ? 328 GLY B O     1 
ATOM   5753 N  N     . THR B 1 350 ? -21.267 31.473  -10.304 1.00 29.61 ? 329 THR B N     1 
ATOM   5754 C  CA    . THR B 1 350 ? -21.268 32.832  -9.695  1.00 29.94 ? 329 THR B CA    1 
ATOM   5755 C  C     . THR B 1 350 ? -21.924 32.766  -8.311  1.00 30.39 ? 329 THR B C     1 
ATOM   5756 O  O     . THR B 1 350 ? -23.067 32.340  -8.223  1.00 31.90 ? 329 THR B O     1 
ATOM   5757 C  CB    . THR B 1 350 ? -22.034 33.801  -10.617 1.00 30.54 ? 329 THR B CB    1 
ATOM   5758 O  OG1   . THR B 1 350 ? -21.537 33.644  -11.950 1.00 28.03 ? 329 THR B OG1   1 
ATOM   5759 C  CG2   . THR B 1 350 ? -21.940 35.246  -10.162 1.00 28.35 ? 329 THR B CG2   1 
ATOM   5760 N  N     . PRO B 1 351 ? -21.264 33.164  -7.198  1.00 29.62 ? 330 PRO B N     1 
ATOM   5761 C  CA    . PRO B 1 351 ? -21.937 33.258  -5.894  1.00 31.62 ? 330 PRO B CA    1 
ATOM   5762 C  C     . PRO B 1 351 ? -23.137 34.201  -5.895  1.00 32.68 ? 330 PRO B C     1 
ATOM   5763 O  O     . PRO B 1 351 ? -23.338 34.955  -6.840  1.00 30.22 ? 330 PRO B O     1 
ATOM   5764 C  CB    . PRO B 1 351 ? -20.863 33.827  -4.952  1.00 33.24 ? 330 PRO B CB    1 
ATOM   5765 C  CG    . PRO B 1 351 ? -19.874 34.487  -5.897  1.00 32.48 ? 330 PRO B CG    1 
ATOM   5766 C  CD    . PRO B 1 351 ? -19.868 33.610  -7.137  1.00 30.46 ? 330 PRO B CD    1 
ATOM   5767 N  N     . PRO B 1 352 ? -24.015 34.180  -4.869  1.00 38.68 ? 331 PRO B N     1 
ATOM   5768 C  CA    . PRO B 1 352 ? -25.210 35.031  -4.879  1.00 38.13 ? 331 PRO B CA    1 
ATOM   5769 C  C     . PRO B 1 352 ? -24.881 36.536  -4.844  1.00 40.16 ? 331 PRO B C     1 
ATOM   5770 O  O     . PRO B 1 352 ? -25.695 37.315  -5.339  1.00 40.91 ? 331 PRO B O     1 
ATOM   5771 C  CB    . PRO B 1 352 ? -25.978 34.581  -3.626  1.00 39.12 ? 331 PRO B CB    1 
ATOM   5772 C  CG    . PRO B 1 352 ? -25.433 33.191  -3.369  1.00 40.77 ? 331 PRO B CG    1 
ATOM   5773 C  CD    . PRO B 1 352 ? -23.956 33.322  -3.680  1.00 39.94 ? 331 PRO B CD    1 
ATOM   5774 N  N     . ALA B 1 353 ? -23.713 36.927  -4.308  1.00 37.73 ? 332 ALA B N     1 
ATOM   5775 C  CA    . ALA B 1 353 ? -23.234 38.333  -4.325  1.00 39.56 ? 332 ALA B CA    1 
ATOM   5776 C  C     . ALA B 1 353 ? -23.279 38.868  -5.774  1.00 43.30 ? 332 ALA B C     1 
ATOM   5777 O  O     . ALA B 1 353 ? -23.395 40.090  -5.966  1.00 49.68 ? 332 ALA B O     1 
ATOM   5778 C  CB    . ALA B 1 353 ? -21.852 38.415  -3.712  1.00 38.15 ? 332 ALA B CB    1 
ATOM   5779 N  N     . GLY B 1 354 ? -23.177 37.975  -6.767  1.00 41.56 ? 333 GLY B N     1 
ATOM   5780 C  CA    . GLY B 1 354 ? -23.339 38.271  -8.205  1.00 38.87 ? 333 GLY B CA    1 
ATOM   5781 C  C     . GLY B 1 354 ? -22.027 38.556  -8.937  1.00 35.97 ? 333 GLY B C     1 
ATOM   5782 O  O     . GLY B 1 354 ? -22.123 38.866  -10.137 1.00 35.55 ? 333 GLY B O     1 
ATOM   5783 N  N     . THR B 1 355 ? -20.880 38.538  -8.237  1.00 33.10 ? 334 THR B N     1 
ATOM   5784 C  CA    . THR B 1 355 ? -19.497 38.691  -8.764  1.00 33.14 ? 334 THR B CA    1 
ATOM   5785 C  C     . THR B 1 355 ? -18.531 37.982  -7.820  1.00 34.67 ? 334 THR B C     1 
ATOM   5786 O  O     . THR B 1 355 ? -18.816 37.843  -6.631  1.00 39.62 ? 334 THR B O     1 
ATOM   5787 C  CB    . THR B 1 355 ? -19.034 40.154  -8.907  1.00 34.16 ? 334 THR B CB    1 
ATOM   5788 O  OG1   . THR B 1 355 ? -18.823 40.721  -7.615  1.00 35.06 ? 334 THR B OG1   1 
ATOM   5789 C  CG2   . THR B 1 355 ? -19.998 41.025  -9.677  1.00 33.52 ? 334 THR B CG2   1 
ATOM   5790 N  N     . PRO B 1 356 ? -17.371 37.481  -8.311  1.00 34.40 ? 335 PRO B N     1 
ATOM   5791 C  CA    . PRO B 1 356 ? -17.056 37.478  -9.743  1.00 33.42 ? 335 PRO B CA    1 
ATOM   5792 C  C     . PRO B 1 356 ? -17.985 36.548  -10.533 1.00 32.52 ? 335 PRO B C     1 
ATOM   5793 O  O     . PRO B 1 356 ? -18.555 35.670  -9.924  1.00 35.28 ? 335 PRO B O     1 
ATOM   5794 C  CB    . PRO B 1 356 ? -15.639 36.891  -9.779  1.00 31.72 ? 335 PRO B CB    1 
ATOM   5795 C  CG    . PRO B 1 356 ? -15.587 36.019  -8.558  1.00 30.92 ? 335 PRO B CG    1 
ATOM   5796 C  CD    . PRO B 1 356 ? -16.352 36.794  -7.510  1.00 30.95 ? 335 PRO B CD    1 
ATOM   5797 N  N     . GLY B 1 357 ? -18.080 36.712  -11.852 1.00 33.17 ? 336 GLY B N     1 
ATOM   5798 C  CA    . GLY B 1 357 ? -18.599 35.649  -12.737 1.00 30.92 ? 336 GLY B CA    1 
ATOM   5799 C  C     . GLY B 1 357 ? -17.714 34.404  -12.662 1.00 29.82 ? 336 GLY B C     1 
ATOM   5800 O  O     . GLY B 1 357 ? -16.460 34.529  -12.781 1.00 30.09 ? 336 GLY B O     1 
ATOM   5801 N  N     . ILE B 1 358 ? -18.304 33.229  -12.481 1.00 27.27 ? 337 ILE B N     1 
ATOM   5802 C  CA    . ILE B 1 358 ? -17.551 31.938  -12.561 1.00 27.06 ? 337 ILE B CA    1 
ATOM   5803 C  C     . ILE B 1 358 ? -18.284 31.007  -13.533 1.00 26.20 ? 337 ILE B C     1 
ATOM   5804 O  O     . ILE B 1 358 ? -19.515 30.871  -13.418 1.00 25.49 ? 337 ILE B O     1 
ATOM   5805 C  CB    . ILE B 1 358 ? -17.361 31.329  -11.152 1.00 28.07 ? 337 ILE B CB    1 
ATOM   5806 C  CG1   . ILE B 1 358 ? -16.688 32.337  -10.213 1.00 28.82 ? 337 ILE B CG1   1 
ATOM   5807 C  CG2   . ILE B 1 358 ? -16.602 30.000  -11.213 1.00 27.96 ? 337 ILE B CG2   1 
ATOM   5808 C  CD1   . ILE B 1 358 ? -16.455 31.830  -8.806  1.00 32.22 ? 337 ILE B CD1   1 
ATOM   5809 N  N     . VAL B 1 359 ? -17.563 30.439  -14.500 1.00 27.02 ? 338 VAL B N     1 
ATOM   5810 C  CA    . VAL B 1 359 ? -18.025 29.267  -15.298 1.00 27.77 ? 338 VAL B CA    1 
ATOM   5811 C  C     . VAL B 1 359 ? -17.326 28.028  -14.742 1.00 28.31 ? 338 VAL B C     1 
ATOM   5812 O  O     . VAL B 1 359 ? -16.092 27.948  -14.839 1.00 29.94 ? 338 VAL B O     1 
ATOM   5813 C  CB    . VAL B 1 359 ? -17.759 29.397  -16.806 1.00 30.49 ? 338 VAL B CB    1 
ATOM   5814 C  CG1   . VAL B 1 359 ? -18.139 28.099  -17.531 1.00 29.85 ? 338 VAL B CG1   1 
ATOM   5815 C  CG2   . VAL B 1 359 ? -18.451 30.614  -17.424 1.00 29.05 ? 338 VAL B CG2   1 
ATOM   5816 N  N     . THR B 1 360 ? -18.111 27.114  -14.172 1.00 27.69 ? 339 THR B N     1 
ATOM   5817 C  CA    . THR B 1 360 ? -17.627 25.853  -13.581 1.00 26.79 ? 339 THR B CA    1 
ATOM   5818 C  C     . THR B 1 360 ? -17.865 24.724  -14.580 1.00 27.10 ? 339 THR B C     1 
ATOM   5819 O  O     . THR B 1 360 ? -18.915 24.714  -15.285 1.00 23.20 ? 339 THR B O     1 
ATOM   5820 C  CB    . THR B 1 360 ? -18.290 25.606  -12.232 1.00 27.98 ? 339 THR B CB    1 
ATOM   5821 O  OG1   . THR B 1 360 ? -17.900 26.713  -11.423 1.00 28.39 ? 339 THR B OG1   1 
ATOM   5822 C  CG2   . THR B 1 360 ? -17.873 24.294  -11.610 1.00 28.45 ? 339 THR B CG2   1 
ATOM   5823 N  N     . GLY B 1 361 ? -16.874 23.845  -14.683 1.00 26.81 ? 340 GLY B N     1 
ATOM   5824 C  CA    . GLY B 1 361 ? -16.894 22.766  -15.677 1.00 27.39 ? 340 GLY B CA    1 
ATOM   5825 C  C     . GLY B 1 361 ? -15.864 21.721  -15.348 1.00 27.04 ? 340 GLY B C     1 
ATOM   5826 O  O     . GLY B 1 361 ? -15.097 21.941  -14.375 1.00 25.82 ? 340 GLY B O     1 
ATOM   5827 N  N     . PHE B 1 362 ? -15.862 20.648  -16.147 1.00 26.63 ? 341 PHE B N     1 
ATOM   5828 C  CA    . PHE B 1 362 ? -15.014 19.451  -15.959 1.00 29.84 ? 341 PHE B CA    1 
ATOM   5829 C  C     . PHE B 1 362 ? -14.519 18.896  -17.312 1.00 29.89 ? 341 PHE B C     1 
ATOM   5830 O  O     . PHE B 1 362 ? -15.231 18.910  -18.355 1.00 30.24 ? 341 PHE B O     1 
ATOM   5831 C  CB    . PHE B 1 362 ? -15.784 18.360  -15.192 1.00 35.75 ? 341 PHE B CB    1 
ATOM   5832 C  CG    . PHE B 1 362 ? -16.727 18.811  -14.100 1.00 34.13 ? 341 PHE B CG    1 
ATOM   5833 C  CD1   . PHE B 1 362 ? -16.397 18.650  -12.764 1.00 35.22 ? 341 PHE B CD1   1 
ATOM   5834 C  CD2   . PHE B 1 362 ? -17.962 19.364  -14.417 1.00 32.27 ? 341 PHE B CD2   1 
ATOM   5835 C  CE1   . PHE B 1 362 ? -17.274 19.051  -11.765 1.00 37.01 ? 341 PHE B CE1   1 
ATOM   5836 C  CE2   . PHE B 1 362 ? -18.829 19.776  -13.419 1.00 33.66 ? 341 PHE B CE2   1 
ATOM   5837 C  CZ    . PHE B 1 362 ? -18.489 19.612  -12.095 1.00 34.01 ? 341 PHE B CZ    1 
ATOM   5838 N  N     . PHE B 1 363 ? -13.302 18.357  -17.283 1.00 27.84 ? 342 PHE B N     1 
ATOM   5839 C  CA    . PHE B 1 363 ? -12.837 17.312  -18.218 1.00 26.90 ? 342 PHE B CA    1 
ATOM   5840 C  C     . PHE B 1 363 ? -13.207 15.993  -17.533 1.00 27.97 ? 342 PHE B C     1 
ATOM   5841 O  O     . PHE B 1 363 ? -12.887 15.877  -16.348 1.00 23.83 ? 342 PHE B O     1 
ATOM   5842 C  CB    . PHE B 1 363 ? -11.324 17.396  -18.473 1.00 25.99 ? 342 PHE B CB    1 
ATOM   5843 C  CG    . PHE B 1 363 ? -10.792 18.674  -19.077 1.00 27.85 ? 342 PHE B CG    1 
ATOM   5844 C  CD1   . PHE B 1 363 ? -10.326 18.703  -20.394 1.00 27.47 ? 342 PHE B CD1   1 
ATOM   5845 C  CD2   . PHE B 1 363 ? -10.656 19.833  -18.309 1.00 28.03 ? 342 PHE B CD2   1 
ATOM   5846 C  CE1   . PHE B 1 363 ? -9.751  19.855  -20.926 1.00 29.00 ? 342 PHE B CE1   1 
ATOM   5847 C  CE2   . PHE B 1 363 ? -10.123 20.994  -18.858 1.00 29.42 ? 342 PHE B CE2   1 
ATOM   5848 C  CZ    . PHE B 1 363 ? -9.659  21.004  -20.164 1.00 28.02 ? 342 PHE B CZ    1 
ATOM   5849 N  N     . GLU B 1 364 ? -13.841 15.061  -18.258 1.00 31.28 ? 343 GLU B N     1 
ATOM   5850 C  CA    . GLU B 1 364 ? -14.302 13.742  -17.741 1.00 33.54 ? 343 GLU B CA    1 
ATOM   5851 C  C     . GLU B 1 364 ? -13.644 12.633  -18.554 1.00 32.15 ? 343 GLU B C     1 
ATOM   5852 O  O     . GLU B 1 364 ? -13.513 12.814  -19.754 1.00 33.87 ? 343 GLU B O     1 
ATOM   5853 C  CB    . GLU B 1 364 ? -15.815 13.580  -17.916 1.00 37.78 ? 343 GLU B CB    1 
ATOM   5854 C  CG    . GLU B 1 364 ? -16.656 14.773  -17.485 1.00 37.96 ? 343 GLU B CG    1 
ATOM   5855 C  CD    . GLU B 1 364 ? -16.942 14.757  -16.004 1.00 41.85 ? 343 GLU B CD    1 
ATOM   5856 O  OE1   . GLU B 1 364 ? -16.098 14.207  -15.274 1.00 51.71 ? 343 GLU B OE1   1 
ATOM   5857 O  OE2   . GLU B 1 364 ? -17.989 15.277  -15.587 1.00 39.34 ? 343 GLU B OE2   1 
ATOM   5858 N  N     . GLY B 1 365 ? -13.255 11.532  -17.912 1.00 33.40 ? 344 GLY B N     1 
ATOM   5859 C  CA    . GLY B 1 365 ? -12.824 10.289  -18.577 1.00 32.23 ? 344 GLY B CA    1 
ATOM   5860 C  C     . GLY B 1 365 ? -11.511 10.459  -19.345 1.00 31.32 ? 344 GLY B C     1 
ATOM   5861 O  O     . GLY B 1 365 ? -10.562 11.048  -18.843 1.00 31.17 ? 344 GLY B O     1 
ATOM   5862 N  N     . PRO B 1 366 ? -11.426 9.938   -20.585 1.00 28.29 ? 345 PRO B N     1 
ATOM   5863 C  CA    . PRO B 1 366 ? -10.249 10.107  -21.436 1.00 28.16 ? 345 PRO B CA    1 
ATOM   5864 C  C     . PRO B 1 366 ? -9.772  11.548  -21.637 1.00 28.94 ? 345 PRO B C     1 
ATOM   5865 O  O     . PRO B 1 366 ? -8.548  11.777  -21.789 1.00 27.00 ? 345 PRO B O     1 
ATOM   5866 C  CB    . PRO B 1 366 ? -10.745 9.591   -22.794 1.00 30.73 ? 345 PRO B CB    1 
ATOM   5867 C  CG    . PRO B 1 366 ? -11.741 8.522   -22.401 1.00 32.42 ? 345 PRO B CG    1 
ATOM   5868 C  CD    . PRO B 1 366 ? -12.484 9.155   -21.237 1.00 30.57 ? 345 PRO B CD    1 
ATOM   5869 N  N     . ALA B 1 367 ? -10.727 12.482  -21.681 1.00 28.13 ? 346 ALA B N     1 
ATOM   5870 C  CA    . ALA B 1 367 ? -10.436 13.934  -21.761 1.00 29.17 ? 346 ALA B CA    1 
ATOM   5871 C  C     . ALA B 1 367 ? -9.740  14.387  -20.469 1.00 25.73 ? 346 ALA B C     1 
ATOM   5872 O  O     . ALA B 1 367 ? -8.906  15.267  -20.563 1.00 22.02 ? 346 ALA B O     1 
ATOM   5873 C  CB    . ALA B 1 367 ? -11.686 14.732  -22.036 1.00 29.25 ? 346 ALA B CB    1 
ATOM   5874 N  N     . ALA B 1 368 ? -10.087 13.814  -19.309 1.00 25.70 ? 347 ALA B N     1 
ATOM   5875 C  CA    . ALA B 1 368 ? -9.443  14.161  -18.022 1.00 25.01 ? 347 ALA B CA    1 
ATOM   5876 C  C     . ALA B 1 368 ? -7.995  13.675  -18.049 1.00 24.20 ? 347 ALA B C     1 
ATOM   5877 O  O     . ALA B 1 368 ? -7.114  14.439  -17.599 1.00 21.62 ? 347 ALA B O     1 
ATOM   5878 C  CB    . ALA B 1 368 ? -10.181 13.592  -16.843 1.00 24.36 ? 347 ALA B CB    1 
ATOM   5879 N  N     . VAL B 1 369 ? -7.774  12.450  -18.543 1.00 23.89 ? 348 VAL B N     1 
ATOM   5880 C  CA    . VAL B 1 369 ? -6.426  11.795  -18.587 1.00 24.39 ? 348 VAL B CA    1 
ATOM   5881 C  C     . VAL B 1 369 ? -5.516  12.571  -19.558 1.00 24.50 ? 348 VAL B C     1 
ATOM   5882 O  O     . VAL B 1 369 ? -4.357  12.793  -19.194 1.00 25.48 ? 348 VAL B O     1 
ATOM   5883 C  CB    . VAL B 1 369 ? -6.513  10.294  -18.939 1.00 24.40 ? 348 VAL B CB    1 
ATOM   5884 C  CG1   . VAL B 1 369 ? -5.135  9.656   -19.003 1.00 23.44 ? 348 VAL B CG1   1 
ATOM   5885 C  CG2   . VAL B 1 369 ? -7.399  9.513   -17.976 1.00 24.86 ? 348 VAL B CG2   1 
ATOM   5886 N  N     . ALA B 1 370 ? -6.006  12.970  -20.745 1.00 27.60 ? 349 ALA B N     1 
ATOM   5887 C  CA    . ALA B 1 370 ? -5.262  13.808  -21.717 1.00 28.49 ? 349 ALA B CA    1 
ATOM   5888 C  C     . ALA B 1 370 ? -4.899  15.129  -21.043 1.00 29.81 ? 349 ALA B C     1 
ATOM   5889 O  O     . ALA B 1 370 ? -3.708  15.400  -20.944 1.00 33.66 ? 349 ALA B O     1 
ATOM   5890 C  CB    . ALA B 1 370 ? -6.041  14.045  -22.986 1.00 29.38 ? 349 ALA B CB    1 
ATOM   5891 N  N     . ALA B 1 371 ? -5.889  15.899  -20.586 1.00 29.23 ? 350 ALA B N     1 
ATOM   5892 C  CA    . ALA B 1 371 ? -5.724  17.206  -19.900 1.00 27.68 ? 350 ALA B CA    1 
ATOM   5893 C  C     . ALA B 1 371 ? -4.767  17.075  -18.708 1.00 31.20 ? 350 ALA B C     1 
ATOM   5894 O  O     . ALA B 1 371 ? -3.969  18.007  -18.457 1.00 25.52 ? 350 ALA B O     1 
ATOM   5895 C  CB    . ALA B 1 371 ? -7.067  17.686  -19.440 1.00 28.67 ? 350 ALA B CB    1 
ATOM   5896 N  N     . GLY B 1 372 ? -4.857  15.941  -17.994 1.00 30.38 ? 351 GLY B N     1 
ATOM   5897 C  CA    . GLY B 1 372 ? -4.070  15.672  -16.784 1.00 30.07 ? 351 GLY B CA    1 
ATOM   5898 C  C     . GLY B 1 372 ? -2.576  15.747  -17.049 1.00 30.76 ? 351 GLY B C     1 
ATOM   5899 O  O     . GLY B 1 372 ? -1.868  16.204  -16.167 1.00 31.50 ? 351 GLY B O     1 
ATOM   5900 N  N     . ALA B 1 373 ? -2.131  15.335  -18.236 1.00 32.78 ? 352 ALA B N     1 
ATOM   5901 C  CA    . ALA B 1 373 ? -0.713  15.237  -18.637 1.00 34.20 ? 352 ALA B CA    1 
ATOM   5902 C  C     . ALA B 1 373 ? -0.203  16.595  -19.134 1.00 35.44 ? 352 ALA B C     1 
ATOM   5903 O  O     . ALA B 1 373 ? 0.995   16.703  -19.309 1.00 35.41 ? 352 ALA B O     1 
ATOM   5904 C  CB    . ALA B 1 373 ? -0.575  14.180  -19.705 1.00 33.17 ? 352 ALA B CB    1 
ATOM   5905 N  N     . ARG B 1 374 ? -1.083  17.582  -19.327 1.00 36.46 ? 353 ARG B N     1 
ATOM   5906 C  CA    . ARG B 1 374 ? -0.740  18.959  -19.793 1.00 38.29 ? 353 ARG B CA    1 
ATOM   5907 C  C     . ARG B 1 374 ? -0.623  19.892  -18.579 1.00 37.50 ? 353 ARG B C     1 
ATOM   5908 O  O     . ARG B 1 374 ? -0.925  19.455  -17.458 1.00 40.58 ? 353 ARG B O     1 
ATOM   5909 C  CB    . ARG B 1 374 ? -1.784  19.424  -20.821 1.00 40.45 ? 353 ARG B CB    1 
ATOM   5910 C  CG    . ARG B 1 374 ? -1.908  18.491  -22.028 1.00 40.85 ? 353 ARG B CG    1 
ATOM   5911 C  CD    . ARG B 1 374 ? -2.812  19.009  -23.138 1.00 46.59 ? 353 ARG B CD    1 
ATOM   5912 N  NE    . ARG B 1 374 ? -2.086  19.818  -24.124 1.00 51.75 ? 353 ARG B NE    1 
ATOM   5913 C  CZ    . ARG B 1 374 ? -2.569  20.902  -24.746 1.00 57.99 ? 353 ARG B CZ    1 
ATOM   5914 N  NH1   . ARG B 1 374 ? -3.801  21.337  -24.505 1.00 61.48 ? 353 ARG B NH1   1 
ATOM   5915 N  NH2   . ARG B 1 374 ? -1.808  21.557  -25.611 1.00 55.41 ? 353 ARG B NH2   1 
ATOM   5916 N  N     . THR B 1 375 ? -0.155  21.124  -18.769 1.00 35.25 ? 354 THR B N     1 
ATOM   5917 C  CA    . THR B 1 375 ? 0.016   22.116  -17.670 1.00 32.55 ? 354 THR B CA    1 
ATOM   5918 C  C     . THR B 1 375 ? -1.326  22.784  -17.385 1.00 33.48 ? 354 THR B C     1 
ATOM   5919 O  O     . THR B 1 375 ? -2.276  22.595  -18.196 1.00 32.86 ? 354 THR B O     1 
ATOM   5920 C  CB    . THR B 1 375 ? 1.044   23.214  -17.998 1.00 31.12 ? 354 THR B CB    1 
ATOM   5921 O  OG1   . THR B 1 375 ? 0.488   24.125  -18.945 1.00 26.03 ? 354 THR B OG1   1 
ATOM   5922 C  CG2   . THR B 1 375 ? 2.366   22.668  -18.504 1.00 29.42 ? 354 THR B CG2   1 
ATOM   5923 N  N     . ARG B 1 376 ? -1.384  23.597  -16.332 1.00 35.39 ? 355 ARG B N     1 
ATOM   5924 C  CA    . ARG B 1 376 ? -2.602  24.384  -16.000 1.00 42.17 ? 355 ARG B CA    1 
ATOM   5925 C  C     . ARG B 1 376 ? -2.884  25.370  -17.156 1.00 39.90 ? 355 ARG B C     1 
ATOM   5926 O  O     . ARG B 1 376 ? -4.048  25.443  -17.611 1.00 42.13 ? 355 ARG B O     1 
ATOM   5927 C  CB    . ARG B 1 376 ? -2.476  25.029  -14.609 1.00 49.85 ? 355 ARG B CB    1 
ATOM   5928 C  CG    . ARG B 1 376 ? -3.752  24.922  -13.777 1.00 53.59 ? 355 ARG B CG    1 
ATOM   5929 C  CD    . ARG B 1 376 ? -3.623  24.946  -12.258 1.00 57.98 ? 355 ARG B CD    1 
ATOM   5930 N  NE    . ARG B 1 376 ? -3.805  26.321  -11.795 1.00 71.32 ? 355 ARG B NE    1 
ATOM   5931 C  CZ    . ARG B 1 376 ? -4.524  26.735  -10.736 1.00 69.32 ? 355 ARG B CZ    1 
ATOM   5932 N  NH1   . ARG B 1 376 ? -5.187  25.886  -9.960  1.00 60.19 ? 355 ARG B NH1   1 
ATOM   5933 N  NH2   . ARG B 1 376 ? -4.584  28.034  -10.475 1.00 67.05 ? 355 ARG B NH2   1 
ATOM   5934 N  N     . GLU B 1 377 ? -1.852  26.047  -17.665 1.00 39.56 ? 356 GLU B N     1 
ATOM   5935 C  CA    . GLU B 1 377 ? -1.963  27.116  -18.695 1.00 41.75 ? 356 GLU B CA    1 
ATOM   5936 C  C     . GLU B 1 377 ? -2.598  26.530  -19.956 1.00 41.20 ? 356 GLU B C     1 
ATOM   5937 O  O     . GLU B 1 377 ? -3.575  27.138  -20.449 1.00 40.95 ? 356 GLU B O     1 
ATOM   5938 C  CB    . GLU B 1 377 ? -0.597  27.714  -19.033 1.00 46.81 ? 356 GLU B CB    1 
ATOM   5939 C  CG    . GLU B 1 377 ? 0.066   28.428  -17.863 1.00 52.82 ? 356 GLU B CG    1 
ATOM   5940 C  CD    . GLU B 1 377 ? 0.410   27.551  -16.659 1.00 57.37 ? 356 GLU B CD    1 
ATOM   5941 O  OE1   . GLU B 1 377 ? 0.133   27.993  -15.505 1.00 55.80 ? 356 GLU B OE1   1 
ATOM   5942 O  OE2   . GLU B 1 377 ? 0.931   26.414  -16.866 1.00 55.07 ? 356 GLU B OE2   1 
ATOM   5943 N  N     . GLU B 1 378 ? -2.088  25.374  -20.409 1.00 36.77 ? 357 GLU B N     1 
ATOM   5944 C  CA    . GLU B 1 378 ? -2.580  24.597  -21.587 1.00 35.58 ? 357 GLU B CA    1 
ATOM   5945 C  C     . GLU B 1 378 ? -4.054  24.178  -21.416 1.00 32.13 ? 357 GLU B C     1 
ATOM   5946 O  O     . GLU B 1 378 ? -4.830  24.328  -22.393 1.00 30.71 ? 357 GLU B O     1 
ATOM   5947 C  CB    . GLU B 1 378 ? -1.654  23.399  -21.828 1.00 38.09 ? 357 GLU B CB    1 
ATOM   5948 C  CG    . GLU B 1 378 ? -0.299  23.810  -22.399 1.00 41.33 ? 357 GLU B CG    1 
ATOM   5949 C  CD    . GLU B 1 378 ? 0.790   22.746  -22.495 1.00 46.87 ? 357 GLU B CD    1 
ATOM   5950 O  OE1   . GLU B 1 378 ? 1.845   23.063  -23.066 1.00 49.46 ? 357 GLU B OE1   1 
ATOM   5951 O  OE2   . GLU B 1 378 ? 0.600   21.613  -21.980 1.00 51.37 ? 357 GLU B OE2   1 
ATOM   5952 N  N     . ARG B 1 379 ? -4.447  23.672  -20.241 1.00 29.42 ? 358 ARG B N     1 
ATOM   5953 C  CA    . ARG B 1 379 ? -5.849  23.281  -19.934 1.00 27.30 ? 358 ARG B CA    1 
ATOM   5954 C  C     . ARG B 1 379 ? -6.725  24.533  -19.977 1.00 27.28 ? 358 ARG B C     1 
ATOM   5955 O  O     . ARG B 1 379 ? -7.841  24.458  -20.504 1.00 26.15 ? 358 ARG B O     1 
ATOM   5956 C  CB    . ARG B 1 379 ? -5.953  22.614  -18.557 1.00 29.36 ? 358 ARG B CB    1 
ATOM   5957 C  CG    . ARG B 1 379 ? -5.441  21.178  -18.500 1.00 28.19 ? 358 ARG B CG    1 
ATOM   5958 C  CD    . ARG B 1 379 ? -5.913  20.467  -17.242 1.00 26.23 ? 358 ARG B CD    1 
ATOM   5959 N  NE    . ARG B 1 379 ? -5.328  21.050  -16.056 1.00 25.80 ? 358 ARG B NE    1 
ATOM   5960 C  CZ    . ARG B 1 379 ? -4.230  20.606  -15.428 1.00 26.58 ? 358 ARG B CZ    1 
ATOM   5961 N  NH1   . ARG B 1 379 ? -3.576  19.549  -15.873 1.00 26.27 ? 358 ARG B NH1   1 
ATOM   5962 N  NH2   . ARG B 1 379 ? -3.776  21.237  -14.354 1.00 24.92 ? 358 ARG B NH2   1 
ATOM   5963 N  N     . ARG B 1 380 ? -6.243  25.643  -19.420 1.00 28.78 ? 359 ARG B N     1 
ATOM   5964 C  CA    . ARG B 1 380 ? -6.937  26.950  -19.528 1.00 33.17 ? 359 ARG B CA    1 
ATOM   5965 C  C     . ARG B 1 380 ? -7.200  27.309  -21.008 1.00 33.87 ? 359 ARG B C     1 
ATOM   5966 O  O     . ARG B 1 380 ? -8.382  27.630  -21.362 1.00 31.70 ? 359 ARG B O     1 
ATOM   5967 C  CB    . ARG B 1 380 ? -6.147  28.060  -18.833 1.00 38.25 ? 359 ARG B CB    1 
ATOM   5968 C  CG    . ARG B 1 380 ? -6.928  29.367  -18.761 1.00 41.93 ? 359 ARG B CG    1 
ATOM   5969 C  CD    . ARG B 1 380 ? -6.027  30.574  -18.644 1.00 45.30 ? 359 ARG B CD    1 
ATOM   5970 N  NE    . ARG B 1 380 ? -5.123  30.631  -19.783 1.00 52.32 ? 359 ARG B NE    1 
ATOM   5971 C  CZ    . ARG B 1 380 ? -3.944  31.255  -19.790 1.00 56.31 ? 359 ARG B CZ    1 
ATOM   5972 N  NH1   . ARG B 1 380 ? -3.514  31.905  -18.718 1.00 55.00 ? 359 ARG B NH1   1 
ATOM   5973 N  NH2   . ARG B 1 380 ? -3.191  31.218  -20.878 1.00 58.69 ? 359 ARG B NH2   1 
ATOM   5974 N  N     . ASP B 1 381 ? -6.180  27.281  -21.867 1.00 31.52 ? 360 ASP B N     1 
ATOM   5975 C  CA    . ASP B 1 381 ? -6.380  27.641  -23.297 1.00 32.19 ? 360 ASP B CA    1 
ATOM   5976 C  C     . ASP B 1 381 ? -7.539  26.787  -23.836 1.00 31.56 ? 360 ASP B C     1 
ATOM   5977 O  O     . ASP B 1 381 ? -8.404  27.325  -24.558 1.00 26.71 ? 360 ASP B O     1 
ATOM   5978 C  CB    . ASP B 1 381 ? -5.099  27.466  -24.120 1.00 34.15 ? 360 ASP B CB    1 
ATOM   5979 C  CG    . ASP B 1 381 ? -3.954  28.384  -23.711 1.00 39.01 ? 360 ASP B CG    1 
ATOM   5980 O  OD1   . ASP B 1 381 ? -4.230  29.523  -23.294 1.00 39.84 ? 360 ASP B OD1   1 
ATOM   5981 O  OD2   . ASP B 1 381 ? -2.788  27.948  -23.787 1.00 44.65 ? 360 ASP B OD2   1 
ATOM   5982 N  N     . VAL B 1 382 ? -7.549  25.494  -23.505 1.00 30.32 ? 361 VAL B N     1 
ATOM   5983 C  CA    . VAL B 1 382 ? -8.459  24.492  -24.139 1.00 33.94 ? 361 VAL B CA    1 
ATOM   5984 C  C     . VAL B 1 382 ? -9.910  24.858  -23.789 1.00 32.40 ? 361 VAL B C     1 
ATOM   5985 O  O     . VAL B 1 382 ? -10.772 24.797  -24.698 1.00 31.04 ? 361 VAL B O     1 
ATOM   5986 C  CB    . VAL B 1 382 ? -8.109  23.045  -23.728 1.00 35.07 ? 361 VAL B CB    1 
ATOM   5987 C  CG1   . VAL B 1 382 ? -9.294  22.103  -23.905 1.00 34.58 ? 361 VAL B CG1   1 
ATOM   5988 C  CG2   . VAL B 1 382 ? -6.895  22.534  -24.499 1.00 35.49 ? 361 VAL B CG2   1 
ATOM   5989 N  N     . VAL B 1 383 ? -10.143 25.275  -22.545 1.00 28.93 ? 362 VAL B N     1 
ATOM   5990 C  CA    . VAL B 1 383 ? -11.504 25.581  -22.025 1.00 27.43 ? 362 VAL B CA    1 
ATOM   5991 C  C     . VAL B 1 383 ? -11.951 26.909  -22.628 1.00 26.35 ? 362 VAL B C     1 
ATOM   5992 O  O     . VAL B 1 383 ? -13.113 26.980  -23.133 1.00 26.53 ? 362 VAL B O     1 
ATOM   5993 C  CB    . VAL B 1 383 ? -11.522 25.598  -20.492 1.00 27.02 ? 362 VAL B CB    1 
ATOM   5994 C  CG1   . VAL B 1 383 ? -12.832 26.096  -19.927 1.00 26.37 ? 362 VAL B CG1   1 
ATOM   5995 C  CG2   . VAL B 1 383 ? -11.208 24.227  -19.942 1.00 28.96 ? 362 VAL B CG2   1 
ATOM   5996 N  N     . VAL B 1 384 ? -11.080 27.913  -22.621 1.00 24.06 ? 363 VAL B N     1 
ATOM   5997 C  CA    . VAL B 1 384 ? -11.411 29.221  -23.256 1.00 26.15 ? 363 VAL B CA    1 
ATOM   5998 C  C     . VAL B 1 384 ? -11.791 29.011  -24.736 1.00 25.70 ? 363 VAL B C     1 
ATOM   5999 O  O     . VAL B 1 384 ? -12.808 29.548  -25.151 1.00 26.16 ? 363 VAL B O     1 
ATOM   6000 C  CB    . VAL B 1 384 ? -10.292 30.251  -23.055 1.00 26.58 ? 363 VAL B CB    1 
ATOM   6001 C  CG1   . VAL B 1 384 ? -10.568 31.511  -23.858 1.00 27.23 ? 363 VAL B CG1   1 
ATOM   6002 C  CG2   . VAL B 1 384 ? -10.130 30.610  -21.581 1.00 27.92 ? 363 VAL B CG2   1 
ATOM   6003 N  N     . ASP B 1 385 ? -11.056 28.184  -25.484 1.00 26.95 ? 364 ASP B N     1 
ATOM   6004 C  CA    . ASP B 1 385 ? -11.303 27.941  -26.925 1.00 27.37 ? 364 ASP B CA    1 
ATOM   6005 C  C     . ASP B 1 385 ? -12.705 27.358  -27.099 1.00 27.13 ? 364 ASP B C     1 
ATOM   6006 O  O     . ASP B 1 385 ? -13.431 27.830  -28.006 1.00 24.06 ? 364 ASP B O     1 
ATOM   6007 C  CB    . ASP B 1 385 ? -10.204 27.089  -27.556 1.00 29.45 ? 364 ASP B CB    1 
ATOM   6008 C  CG    . ASP B 1 385 ? -8.918  27.871  -27.839 1.00 35.52 ? 364 ASP B CG    1 
ATOM   6009 O  OD1   . ASP B 1 385 ? -8.911  29.131  -27.672 1.00 39.05 ? 364 ASP B OD1   1 
ATOM   6010 O  OD2   . ASP B 1 385 ? -7.919  27.226  -28.207 1.00 34.94 ? 364 ASP B OD2   1 
ATOM   6011 N  N     . VAL B 1 386 ? -13.104 26.416  -26.239 1.00 26.47 ? 365 VAL B N     1 
ATOM   6012 C  CA    . VAL B 1 386 ? -14.503 25.867  -26.233 1.00 24.95 ? 365 VAL B CA    1 
ATOM   6013 C  C     . VAL B 1 386 ? -15.479 27.008  -25.912 1.00 23.28 ? 365 VAL B C     1 
ATOM   6014 O  O     . VAL B 1 386 ? -16.397 27.211  -26.709 1.00 21.52 ? 365 VAL B O     1 
ATOM   6015 C  CB    . VAL B 1 386 ? -14.684 24.696  -25.248 1.00 24.71 ? 365 VAL B CB    1 
ATOM   6016 C  CG1   . VAL B 1 386 ? -16.079 24.135  -25.334 1.00 24.77 ? 365 VAL B CG1   1 
ATOM   6017 C  CG2   . VAL B 1 386 ? -13.643 23.601  -25.459 1.00 26.88 ? 365 VAL B CG2   1 
ATOM   6018 N  N     . LEU B 1 387 ? -15.268 27.739  -24.812 1.00 23.82 ? 366 LEU B N     1 
ATOM   6019 C  CA    . LEU B 1 387 ? -16.256 28.725  -24.289 1.00 26.01 ? 366 LEU B CA    1 
ATOM   6020 C  C     . LEU B 1 387 ? -16.510 29.806  -25.350 1.00 29.03 ? 366 LEU B C     1 
ATOM   6021 O  O     . LEU B 1 387 ? -17.698 30.141  -25.577 1.00 26.72 ? 366 LEU B O     1 
ATOM   6022 C  CB    . LEU B 1 387 ? -15.779 29.342  -22.962 1.00 26.78 ? 366 LEU B CB    1 
ATOM   6023 C  CG    . LEU B 1 387 ? -15.799 28.430  -21.721 1.00 27.99 ? 366 LEU B CG    1 
ATOM   6024 C  CD1   . LEU B 1 387 ? -15.977 29.238  -20.458 1.00 28.44 ? 366 LEU B CD1   1 
ATOM   6025 C  CD2   . LEU B 1 387 ? -16.893 27.369  -21.805 1.00 30.39 ? 366 LEU B CD2   1 
ATOM   6026 N  N     . ALA B 1 388 ? -15.451 30.335  -25.976 1.00 27.70 ? 367 ALA B N     1 
ATOM   6027 C  CA    . ALA B 1 388 ? -15.546 31.436  -26.957 1.00 30.62 ? 367 ALA B CA    1 
ATOM   6028 C  C     . ALA B 1 388 ? -16.480 31.047  -28.116 1.00 33.23 ? 367 ALA B C     1 
ATOM   6029 O  O     . ALA B 1 388 ? -17.311 31.895  -28.502 1.00 36.82 ? 367 ALA B O     1 
ATOM   6030 C  CB    . ALA B 1 388 ? -14.157 31.796  -27.436 1.00 33.67 ? 367 ALA B CB    1 
ATOM   6031 N  N     . ARG B 1 389 ? -16.393 29.807  -28.626 1.00 33.65 ? 368 ARG B N     1 
ATOM   6032 C  CA    . ARG B 1 389 ? -17.212 29.313  -29.766 1.00 31.12 ? 368 ARG B CA    1 
ATOM   6033 C  C     . ARG B 1 389 ? -18.628 28.917  -29.319 1.00 32.43 ? 368 ARG B C     1 
ATOM   6034 O  O     . ARG B 1 389 ? -19.409 28.478  -30.196 1.00 34.15 ? 368 ARG B O     1 
ATOM   6035 C  CB    . ARG B 1 389 ? -16.538 28.105  -30.423 1.00 33.87 ? 368 ARG B CB    1 
ATOM   6036 C  CG    . ARG B 1 389 ? -15.311 28.457  -31.252 1.00 35.53 ? 368 ARG B CG    1 
ATOM   6037 C  CD    . ARG B 1 389 ? -14.798 27.279  -32.050 1.00 33.04 ? 368 ARG B CD    1 
ATOM   6038 N  NE    . ARG B 1 389 ? -14.274 26.245  -31.168 1.00 32.65 ? 368 ARG B NE    1 
ATOM   6039 C  CZ    . ARG B 1 389 ? -14.768 25.012  -31.036 1.00 36.91 ? 368 ARG B CZ    1 
ATOM   6040 N  NH1   . ARG B 1 389 ? -15.826 24.610  -31.737 1.00 39.63 ? 368 ARG B NH1   1 
ATOM   6041 N  NH2   . ARG B 1 389 ? -14.189 24.170  -30.197 1.00 35.39 ? 368 ARG B NH2   1 
ATOM   6042 N  N     . THR B 1 390 ? -18.952 29.012  -28.024 1.00 31.38 ? 369 THR B N     1 
ATOM   6043 C  CA    . THR B 1 390 ? -20.241 28.529  -27.445 1.00 33.89 ? 369 THR B CA    1 
ATOM   6044 C  C     . THR B 1 390 ? -20.941 29.697  -26.733 1.00 32.74 ? 369 THR B C     1 
ATOM   6045 O  O     . THR B 1 390 ? -22.042 30.037  -27.158 1.00 32.69 ? 369 THR B O     1 
ATOM   6046 C  CB    . THR B 1 390 ? -20.033 27.266  -26.576 1.00 34.38 ? 369 THR B CB    1 
ATOM   6047 O  OG1   . THR B 1 390 ? -18.999 27.429  -25.591 1.00 30.12 ? 369 THR B OG1   1 
ATOM   6048 C  CG2   . THR B 1 390 ? -19.717 26.045  -27.420 1.00 33.36 ? 369 THR B CG2   1 
ATOM   6049 N  N     . LEU B 1 391 ? -20.307 30.292  -25.713 1.00 36.22 ? 370 LEU B N     1 
ATOM   6050 C  CA    . LEU B 1 391 ? -20.779 31.508  -24.986 1.00 36.08 ? 370 LEU B CA    1 
ATOM   6051 C  C     . LEU B 1 391 ? -20.443 32.783  -25.778 1.00 39.02 ? 370 LEU B C     1 
ATOM   6052 O  O     . LEU B 1 391 ? -21.250 33.709  -25.667 1.00 41.48 ? 370 LEU B O     1 
ATOM   6053 C  CB    . LEU B 1 391 ? -20.156 31.564  -23.585 1.00 33.58 ? 370 LEU B CB    1 
ATOM   6054 C  CG    . LEU B 1 391 ? -20.396 30.337  -22.700 1.00 36.29 ? 370 LEU B CG    1 
ATOM   6055 C  CD1   . LEU B 1 391 ? -19.886 30.555  -21.284 1.00 35.43 ? 370 LEU B CD1   1 
ATOM   6056 C  CD2   . LEU B 1 391 ? -21.867 29.975  -22.649 1.00 36.78 ? 370 LEU B CD2   1 
ATOM   6057 N  N     . GLY B 1 392 ? -19.302 32.864  -26.493 1.00 41.06 ? 371 GLY B N     1 
ATOM   6058 C  CA    . GLY B 1 392 ? -18.928 34.030  -27.336 1.00 42.53 ? 371 GLY B CA    1 
ATOM   6059 C  C     . GLY B 1 392 ? -17.576 34.649  -26.983 1.00 43.94 ? 371 GLY B C     1 
ATOM   6060 O  O     . GLY B 1 392 ? -16.996 34.260  -25.954 1.00 43.03 ? 371 GLY B O     1 
ATOM   6061 N  N     . GLU B 1 393 ? -17.111 35.615  -27.799 1.00 46.18 ? 372 GLU B N     1 
ATOM   6062 C  CA    . GLU B 1 393 ? -15.743 36.234  -27.771 1.00 46.48 ? 372 GLU B CA    1 
ATOM   6063 C  C     . GLU B 1 393 ? -15.416 36.768  -26.360 1.00 47.51 ? 372 GLU B C     1 
ATOM   6064 O  O     . GLU B 1 393 ? -14.192 36.796  -25.986 1.00 42.91 ? 372 GLU B O     1 
ATOM   6065 C  CB    . GLU B 1 393 ? -15.649 37.310  -28.870 1.00 50.09 ? 372 GLU B CB    1 
ATOM   6066 C  CG    . GLU B 1 393 ? -14.378 38.175  -28.871 1.00 59.24 ? 372 GLU B CG    1 
ATOM   6067 C  CD    . GLU B 1 393 ? -13.183 37.726  -29.716 1.00 66.56 ? 372 GLU B CD    1 
ATOM   6068 O  OE1   . GLU B 1 393 ? -12.274 38.556  -29.939 1.00 57.33 ? 372 GLU B OE1   1 
ATOM   6069 O  OE2   . GLU B 1 393 ? -13.149 36.547  -30.160 1.00 84.27 ? 372 GLU B OE2   1 
ATOM   6070 N  N     . ARG B 1 394 ? -16.451 37.173  -25.605 1.00 44.88 ? 373 ARG B N     1 
ATOM   6071 C  CA    . ARG B 1 394 ? -16.348 37.784  -24.246 1.00 48.41 ? 373 ARG B CA    1 
ATOM   6072 C  C     . ARG B 1 394 ? -15.681 36.796  -23.273 1.00 40.69 ? 373 ARG B C     1 
ATOM   6073 O  O     . ARG B 1 394 ? -15.170 37.243  -22.233 1.00 38.87 ? 373 ARG B O     1 
ATOM   6074 C  CB    . ARG B 1 394 ? -17.747 38.215  -23.770 1.00 50.80 ? 373 ARG B CB    1 
ATOM   6075 C  CG    . ARG B 1 394 ? -18.009 39.718  -23.776 1.00 58.91 ? 373 ARG B CG    1 
ATOM   6076 C  CD    . ARG B 1 394 ? -17.910 40.370  -22.394 1.00 66.87 ? 373 ARG B CD    1 
ATOM   6077 N  NE    . ARG B 1 394 ? -17.287 41.698  -22.394 1.00 73.68 ? 373 ARG B NE    1 
ATOM   6078 C  CZ    . ARG B 1 394 ? -16.884 42.379  -21.308 1.00 76.70 ? 373 ARG B CZ    1 
ATOM   6079 N  NH1   . ARG B 1 394 ? -17.038 41.875  -20.091 1.00 74.39 ? 373 ARG B NH1   1 
ATOM   6080 N  NH2   . ARG B 1 394 ? -16.328 43.576  -21.450 1.00 68.70 ? 373 ARG B NH2   1 
ATOM   6081 N  N     . ALA B 1 395 ? -15.732 35.502  -23.604 1.00 39.22 ? 374 ALA B N     1 
ATOM   6082 C  CA    . ALA B 1 395 ? -15.209 34.357  -22.821 1.00 37.34 ? 374 ALA B CA    1 
ATOM   6083 C  C     . ALA B 1 395 ? -13.685 34.430  -22.731 1.00 36.17 ? 374 ALA B C     1 
ATOM   6084 O  O     . ALA B 1 395 ? -13.125 33.754  -21.842 1.00 36.19 ? 374 ALA B O     1 
ATOM   6085 C  CB    . ALA B 1 395 ? -15.664 33.071  -23.470 1.00 37.32 ? 374 ALA B CB    1 
ATOM   6086 N  N     . ARG B 1 396 ? -13.028 35.193  -23.623 1.00 34.76 ? 375 ARG B N     1 
ATOM   6087 C  CA    . ARG B 1 396 ? -11.544 35.333  -23.618 1.00 35.49 ? 375 ARG B CA    1 
ATOM   6088 C  C     . ARG B 1 396 ? -11.117 36.349  -22.550 1.00 36.20 ? 375 ARG B C     1 
ATOM   6089 O  O     . ARG B 1 396 ? -10.013 36.177  -22.017 1.00 37.24 ? 375 ARG B O     1 
ATOM   6090 C  CB    . ARG B 1 396 ? -11.003 35.718  -24.999 1.00 34.30 ? 375 ARG B CB    1 
ATOM   6091 C  CG    . ARG B 1 396 ? -11.318 34.681  -26.060 1.00 32.39 ? 375 ARG B CG    1 
ATOM   6092 C  CD    . ARG B 1 396 ? -10.558 34.857  -27.346 1.00 32.12 ? 375 ARG B CD    1 
ATOM   6093 N  NE    . ARG B 1 396 ? -10.817 33.683  -28.158 1.00 33.41 ? 375 ARG B NE    1 
ATOM   6094 C  CZ    . ARG B 1 396 ? -10.287 32.494  -27.928 1.00 31.59 ? 375 ARG B CZ    1 
ATOM   6095 N  NH1   . ARG B 1 396 ? -9.454  32.330  -26.917 1.00 35.07 ? 375 ARG B NH1   1 
ATOM   6096 N  NH2   . ARG B 1 396 ? -10.591 31.473  -28.703 1.00 31.40 ? 375 ARG B NH2   1 
ATOM   6097 N  N     . ASP B 1 397 ? -11.960 37.335  -22.225 1.00 36.71 ? 376 ASP B N     1 
ATOM   6098 C  CA    . ASP B 1 397 ? -11.586 38.461  -21.323 1.00 42.57 ? 376 ASP B CA    1 
ATOM   6099 C  C     . ASP B 1 397 ? -11.571 37.903  -19.898 1.00 41.24 ? 376 ASP B C     1 
ATOM   6100 O  O     . ASP B 1 397 ? -12.414 38.314  -19.077 1.00 42.71 ? 376 ASP B O     1 
ATOM   6101 C  CB    . ASP B 1 397 ? -12.487 39.683  -21.572 1.00 46.82 ? 376 ASP B CB    1 
ATOM   6102 C  CG    . ASP B 1 397 ? -12.346 40.303  -22.968 1.00 48.70 ? 376 ASP B CG    1 
ATOM   6103 O  OD1   . ASP B 1 397 ? -13.127 41.220  -23.283 1.00 50.12 ? 376 ASP B OD1   1 
ATOM   6104 O  OD2   . ASP B 1 397 ? -11.439 39.883  -23.742 1.00 51.00 ? 376 ASP B OD2   1 
ATOM   6105 N  N     . VAL B 1 398 ? -10.662 36.957  -19.657 1.00 38.30 ? 377 VAL B N     1 
ATOM   6106 C  CA    . VAL B 1 398 ? -10.653 36.043  -18.479 1.00 39.39 ? 377 VAL B CA    1 
ATOM   6107 C  C     . VAL B 1 398 ? -9.817  36.709  -17.387 1.00 42.83 ? 377 VAL B C     1 
ATOM   6108 O  O     . VAL B 1 398 ? -8.752  37.264  -17.736 1.00 48.78 ? 377 VAL B O     1 
ATOM   6109 C  CB    . VAL B 1 398 ? -10.110 34.650  -18.867 1.00 38.86 ? 377 VAL B CB    1 
ATOM   6110 C  CG1   . VAL B 1 398 ? -9.843  33.755  -17.666 1.00 40.19 ? 377 VAL B CG1   1 
ATOM   6111 C  CG2   . VAL B 1 398 ? -11.049 33.942  -19.833 1.00 40.40 ? 377 VAL B CG2   1 
ATOM   6112 N  N     . ARG B 1 399 ? -10.280 36.652  -16.132 1.00 41.11 ? 378 ARG B N     1 
ATOM   6113 C  CA    . ARG B 1 399 ? -9.599  37.245  -14.953 1.00 41.09 ? 378 ARG B CA    1 
ATOM   6114 C  C     . ARG B 1 399 ? -8.609  36.211  -14.405 1.00 39.40 ? 378 ARG B C     1 
ATOM   6115 O  O     . ARG B 1 399 ? -7.505  36.603  -13.972 1.00 41.93 ? 378 ARG B O     1 
ATOM   6116 C  CB    . ARG B 1 399 ? -10.631 37.734  -13.927 1.00 47.82 ? 378 ARG B CB    1 
ATOM   6117 C  CG    . ARG B 1 399 ? -10.081 38.055  -12.542 1.00 54.54 ? 378 ARG B CG    1 
ATOM   6118 C  CD    . ARG B 1 399 ? -9.118  39.231  -12.484 1.00 63.98 ? 378 ARG B CD    1 
ATOM   6119 N  NE    . ARG B 1 399 ? -9.759  40.536  -12.697 1.00 73.68 ? 378 ARG B NE    1 
ATOM   6120 C  CZ    . ARG B 1 399 ? -9.409  41.451  -13.617 1.00 69.73 ? 378 ARG B CZ    1 
ATOM   6121 N  NH1   . ARG B 1 399 ? -8.401  41.247  -14.452 1.00 69.45 ? 378 ARG B NH1   1 
ATOM   6122 N  NH2   . ARG B 1 399 ? -10.071 42.593  -13.687 1.00 64.86 ? 378 ARG B NH2   1 
ATOM   6123 N  N     . ASP B 1 400 ? -8.959  34.929  -14.436 1.00 35.87 ? 379 ASP B N     1 
ATOM   6124 C  CA    . ASP B 1 400 ? -8.151  33.867  -13.774 1.00 33.17 ? 379 ASP B CA    1 
ATOM   6125 C  C     . ASP B 1 400 ? -8.739  32.478  -14.060 1.00 30.10 ? 379 ASP B C     1 
ATOM   6126 O  O     . ASP B 1 400 ? -9.947  32.376  -14.392 1.00 28.35 ? 379 ASP B O     1 
ATOM   6127 C  CB    . ASP B 1 400 ? -8.091  34.090  -12.260 1.00 33.78 ? 379 ASP B CB    1 
ATOM   6128 C  CG    . ASP B 1 400 ? -7.032  33.277  -11.547 1.00 32.34 ? 379 ASP B CG    1 
ATOM   6129 O  OD1   . ASP B 1 400 ? -6.271  32.584  -12.220 1.00 31.46 ? 379 ASP B OD1   1 
ATOM   6130 O  OD2   . ASP B 1 400 ? -6.962  33.392  -10.328 1.00 37.25 ? 379 ASP B OD2   1 
ATOM   6131 N  N     . TYR B 1 401 ? -7.903  31.449  -13.922 1.00 30.70 ? 380 TYR B N     1 
ATOM   6132 C  CA    . TYR B 1 401 ? -8.289  30.019  -14.076 1.00 30.19 ? 380 TYR B CA    1 
ATOM   6133 C  C     . TYR B 1 401 ? -7.632  29.232  -12.961 1.00 26.48 ? 380 TYR B C     1 
ATOM   6134 O  O     . TYR B 1 401 ? -6.447  29.385  -12.768 1.00 26.21 ? 380 TYR B O     1 
ATOM   6135 C  CB    . TYR B 1 401 ? -7.862  29.468  -15.435 1.00 27.71 ? 380 TYR B CB    1 
ATOM   6136 C  CG    . TYR B 1 401 ? -8.152  28.015  -15.728 1.00 26.69 ? 380 TYR B CG    1 
ATOM   6137 C  CD1   . TYR B 1 401 ? -7.217  27.028  -15.460 1.00 26.22 ? 380 TYR B CD1   1 
ATOM   6138 C  CD2   . TYR B 1 401 ? -9.323  27.633  -16.360 1.00 28.01 ? 380 TYR B CD2   1 
ATOM   6139 C  CE1   . TYR B 1 401 ? -7.442  25.704  -15.800 1.00 24.06 ? 380 TYR B CE1   1 
ATOM   6140 C  CE2   . TYR B 1 401 ? -9.570  26.310  -16.698 1.00 26.12 ? 380 TYR B CE2   1 
ATOM   6141 C  CZ    . TYR B 1 401 ? -8.617  25.351  -16.427 1.00 22.68 ? 380 TYR B CZ    1 
ATOM   6142 O  OH    . TYR B 1 401 ? -8.849  24.057  -16.733 1.00 22.61 ? 380 TYR B OH    1 
ATOM   6143 N  N     . ILE B 1 402 ? -8.456  28.451  -12.283 1.00 28.21 ? 381 ILE B N     1 
ATOM   6144 C  CA    . ILE B 1 402 ? -8.143  27.558  -11.133 1.00 31.66 ? 381 ILE B CA    1 
ATOM   6145 C  C     . ILE B 1 402 ? -8.699  26.169  -11.483 1.00 33.41 ? 381 ILE B C     1 
ATOM   6146 O  O     . ILE B 1 402 ? -9.924  26.080  -11.804 1.00 38.41 ? 381 ILE B O     1 
ATOM   6147 C  CB    . ILE B 1 402 ? -8.797  28.145  -9.865  1.00 33.04 ? 381 ILE B CB    1 
ATOM   6148 C  CG1   . ILE B 1 402 ? -8.160  29.494  -9.516  1.00 35.01 ? 381 ILE B CG1   1 
ATOM   6149 C  CG2   . ILE B 1 402 ? -8.765  27.161  -8.690  1.00 33.85 ? 381 ILE B CG2   1 
ATOM   6150 C  CD1   . ILE B 1 402 ? -8.943  30.314  -8.502  1.00 35.96 ? 381 ILE B CD1   1 
ATOM   6151 N  N     . ASP B 1 403 ? -7.873  25.125  -11.485 1.00 30.30 ? 382 ASP B N     1 
ATOM   6152 C  CA    . ASP B 1 403 ? -8.424  23.759  -11.677 1.00 30.52 ? 382 ASP B CA    1 
ATOM   6153 C  C     . ASP B 1 403 ? -7.700  22.773  -10.759 1.00 30.46 ? 382 ASP B C     1 
ATOM   6154 O  O     . ASP B 1 403 ? -6.682  23.169  -10.137 1.00 26.31 ? 382 ASP B O     1 
ATOM   6155 C  CB    . ASP B 1 403 ? -8.450  23.405  -13.165 1.00 31.87 ? 382 ASP B CB    1 
ATOM   6156 C  CG    . ASP B 1 403 ? -7.121  22.991  -13.769 1.00 27.93 ? 382 ASP B CG    1 
ATOM   6157 O  OD1   . ASP B 1 403 ? -6.097  23.023  -13.049 1.00 27.81 ? 382 ASP B OD1   1 
ATOM   6158 O  OD2   . ASP B 1 403 ? -7.149  22.611  -14.936 1.00 24.62 ? 382 ASP B OD2   1 
ATOM   6159 N  N     . ARG B 1 404 ? -8.294  21.583  -10.600 1.00 32.85 ? 383 ARG B N     1 
ATOM   6160 C  CA    . ARG B 1 404 ? -7.722  20.461  -9.806  1.00 32.79 ? 383 ARG B CA    1 
ATOM   6161 C  C     . ARG B 1 404 ? -7.889  19.137  -10.564 1.00 28.29 ? 383 ARG B C     1 
ATOM   6162 O  O     . ARG B 1 404 ? -9.014  18.769  -10.891 1.00 22.96 ? 383 ARG B O     1 
ATOM   6163 C  CB    . ARG B 1 404 ? -8.375  20.366  -8.424  1.00 39.24 ? 383 ARG B CB    1 
ATOM   6164 C  CG    . ARG B 1 404 ? -7.796  19.246  -7.569  1.00 41.49 ? 383 ARG B CG    1 
ATOM   6165 C  CD    . ARG B 1 404 ? -7.589  19.665  -6.139  1.00 46.83 ? 383 ARG B CD    1 
ATOM   6166 N  NE    . ARG B 1 404 ? -6.591  20.713  -6.059  1.00 53.87 ? 383 ARG B NE    1 
ATOM   6167 C  CZ    . ARG B 1 404 ? -6.148  21.243  -4.924  1.00 57.58 ? 383 ARG B CZ    1 
ATOM   6168 N  NH1   . ARG B 1 404 ? -6.617  20.803  -3.770  1.00 52.31 ? 383 ARG B NH1   1 
ATOM   6169 N  NH2   . ARG B 1 404 ? -5.240  22.210  -4.950  1.00 59.43 ? 383 ARG B NH2   1 
ATOM   6170 N  N     . ASP B 1 405 ? -6.769  18.452  -10.807 1.00 28.65 ? 384 ASP B N     1 
ATOM   6171 C  CA    . ASP B 1 405 ? -6.732  17.058  -11.293 1.00 27.30 ? 384 ASP B CA    1 
ATOM   6172 C  C     . ASP B 1 405 ? -6.835  16.122  -10.080 1.00 26.56 ? 384 ASP B C     1 
ATOM   6173 O  O     . ASP B 1 405 ? -5.800  15.885  -9.405  1.00 25.67 ? 384 ASP B O     1 
ATOM   6174 C  CB    . ASP B 1 405 ? -5.497  16.798  -12.173 1.00 29.24 ? 384 ASP B CB    1 
ATOM   6175 C  CG    . ASP B 1 405 ? -5.505  15.404  -12.788 1.00 27.40 ? 384 ASP B CG    1 
ATOM   6176 O  OD1   . ASP B 1 405 ? -6.545  14.722  -12.624 1.00 26.61 ? 384 ASP B OD1   1 
ATOM   6177 O  OD2   . ASP B 1 405 ? -4.483  15.008  -13.409 1.00 27.82 ? 384 ASP B OD2   1 
ATOM   6178 N  N     . TRP B 1 406 ? -8.025  15.547  -9.851  1.00 25.65 ? 385 TRP B N     1 
ATOM   6179 C  CA    . TRP B 1 406 ? -8.242  14.597  -8.730  1.00 26.47 ? 385 TRP B CA    1 
ATOM   6180 C  C     . TRP B 1 406 ? -7.519  13.260  -8.964  1.00 28.87 ? 385 TRP B C     1 
ATOM   6181 O  O     . TRP B 1 406 ? -7.181  12.614  -7.952  1.00 35.67 ? 385 TRP B O     1 
ATOM   6182 C  CB    . TRP B 1 406 ? -9.735  14.434  -8.452  1.00 28.22 ? 385 TRP B CB    1 
ATOM   6183 C  CG    . TRP B 1 406 ? -10.286 15.648  -7.776  1.00 30.03 ? 385 TRP B CG    1 
ATOM   6184 C  CD1   . TRP B 1 406 ? -10.901 16.711  -8.368  1.00 31.55 ? 385 TRP B CD1   1 
ATOM   6185 C  CD2   . TRP B 1 406 ? -10.234 15.944  -6.372  1.00 31.81 ? 385 TRP B CD2   1 
ATOM   6186 N  NE1   . TRP B 1 406 ? -11.251 17.637  -7.424  1.00 33.24 ? 385 TRP B NE1   1 
ATOM   6187 C  CE2   . TRP B 1 406 ? -10.855 17.196  -6.192  1.00 33.09 ? 385 TRP B CE2   1 
ATOM   6188 C  CE3   . TRP B 1 406 ? -9.756  15.267  -5.248  1.00 34.85 ? 385 TRP B CE3   1 
ATOM   6189 C  CZ2   . TRP B 1 406 ? -11.007 17.777  -4.937  1.00 33.02 ? 385 TRP B CZ2   1 
ATOM   6190 C  CZ3   . TRP B 1 406 ? -9.899  15.849  -4.005  1.00 33.47 ? 385 TRP B CZ3   1 
ATOM   6191 C  CH2   . TRP B 1 406 ? -10.519 17.083  -3.855  1.00 33.72 ? 385 TRP B CH2   1 
ATOM   6192 N  N     . SER B 1 407 ? -7.270  12.846  -10.215 1.00 26.23 ? 386 SER B N     1 
ATOM   6193 C  CA    . SER B 1 407 ? -6.397  11.690  -10.527 1.00 26.70 ? 386 SER B CA    1 
ATOM   6194 C  C     . SER B 1 407 ? -4.972  11.938  -9.988  1.00 26.74 ? 386 SER B C     1 
ATOM   6195 O  O     . SER B 1 407 ? -4.278  10.972  -9.659  1.00 23.57 ? 386 SER B O     1 
ATOM   6196 C  CB    . SER B 1 407 ? -6.389  11.418  -12.013 1.00 26.84 ? 386 SER B CB    1 
ATOM   6197 O  OG    . SER B 1 407 ? -7.707  11.184  -12.478 1.00 28.65 ? 386 SER B OG    1 
ATOM   6198 N  N     . ALA B 1 408 ? -4.542  13.197  -9.913  1.00 29.42 ? 387 ALA B N     1 
ATOM   6199 C  CA    . ALA B 1 408 ? -3.152  13.598  -9.586  1.00 28.92 ? 387 ALA B CA    1 
ATOM   6200 C  C     . ALA B 1 408 ? -2.945  13.703  -8.062  1.00 30.71 ? 387 ALA B C     1 
ATOM   6201 O  O     . ALA B 1 408 ? -1.772  13.710  -7.650  1.00 32.54 ? 387 ALA B O     1 
ATOM   6202 C  CB    . ALA B 1 408 ? -2.844  14.895  -10.304 1.00 28.56 ? 387 ALA B CB    1 
ATOM   6203 N  N     . GLU B 1 409 ? -4.037  13.804  -7.271  1.00 33.19 ? 388 GLU B N     1 
ATOM   6204 C  CA    . GLU B 1 409 ? -4.086  13.780  -5.774  1.00 28.86 ? 388 GLU B CA    1 
ATOM   6205 C  C     . GLU B 1 409 ? -3.729  12.403  -5.225  1.00 28.64 ? 388 GLU B C     1 
ATOM   6206 O  O     . GLU B 1 409 ? -4.500  11.454  -5.397  1.00 25.46 ? 388 GLU B O     1 
ATOM   6207 C  CB    . GLU B 1 409 ? -5.499  14.036  -5.261  1.00 31.09 ? 388 GLU B CB    1 
ATOM   6208 C  CG    . GLU B 1 409 ? -5.979  15.457  -5.435  1.00 34.38 ? 388 GLU B CG    1 
ATOM   6209 C  CD    . GLU B 1 409 ? -5.333  16.449  -4.488  1.00 33.81 ? 388 GLU B CD    1 
ATOM   6210 O  OE1   . GLU B 1 409 ? -5.026  17.540  -4.948  1.00 36.77 ? 388 GLU B OE1   1 
ATOM   6211 O  OE2   . GLU B 1 409 ? -5.131  16.116  -3.304  1.00 31.24 ? 388 GLU B OE2   1 
ATOM   6212 N  N     . PRO B 1 410 ? -2.571  12.245  -4.533  1.00 28.84 ? 389 PRO B N     1 
ATOM   6213 C  CA    . PRO B 1 410 ? -2.164  10.939  -4.004  1.00 27.69 ? 389 PRO B CA    1 
ATOM   6214 C  C     . PRO B 1 410 ? -3.045  10.347  -2.886  1.00 29.44 ? 389 PRO B C     1 
ATOM   6215 O  O     . PRO B 1 410 ? -2.853  9.168   -2.559  1.00 31.47 ? 389 PRO B O     1 
ATOM   6216 C  CB    . PRO B 1 410 ? -0.747  11.149  -3.455  1.00 26.73 ? 389 PRO B CB    1 
ATOM   6217 C  CG    . PRO B 1 410 ? -0.587  12.653  -3.317  1.00 29.71 ? 389 PRO B CG    1 
ATOM   6218 C  CD    . PRO B 1 410 ? -1.570  13.296  -4.278  1.00 28.95 ? 389 PRO B CD    1 
ATOM   6219 N  N     . TRP B 1 411 ? -3.969  11.131  -2.321  1.00 29.12 ? 390 TRP B N     1 
ATOM   6220 C  CA    . TRP B 1 411 ? -4.902  10.681  -1.250  1.00 28.63 ? 390 TRP B CA    1 
ATOM   6221 C  C     . TRP B 1 411 ? -6.346  10.645  -1.758  1.00 27.85 ? 390 TRP B C     1 
ATOM   6222 O  O     . TRP B 1 411 ? -7.258  10.547  -0.944  1.00 33.09 ? 390 TRP B O     1 
ATOM   6223 C  CB    . TRP B 1 411 ? -4.704  11.556  -0.010  1.00 30.16 ? 390 TRP B CB    1 
ATOM   6224 C  CG    . TRP B 1 411 ? -3.292  11.493  0.478   1.00 28.30 ? 390 TRP B CG    1 
ATOM   6225 C  CD1   . TRP B 1 411 ? -2.353  12.484  0.413   1.00 32.01 ? 390 TRP B CD1   1 
ATOM   6226 C  CD2   . TRP B 1 411 ? -2.614  10.340  1.007   1.00 30.76 ? 390 TRP B CD2   1 
ATOM   6227 N  NE1   . TRP B 1 411 ? -1.154  12.043  0.903   1.00 28.83 ? 390 TRP B NE1   1 
ATOM   6228 C  CE2   . TRP B 1 411 ? -1.274  10.723  1.248   1.00 27.53 ? 390 TRP B CE2   1 
ATOM   6229 C  CE3   . TRP B 1 411 ? -2.998  9.017   1.285   1.00 31.59 ? 390 TRP B CE3   1 
ATOM   6230 C  CZ2   . TRP B 1 411 ? -0.344  9.853   1.806   1.00 27.26 ? 390 TRP B CZ2   1 
ATOM   6231 C  CZ3   . TRP B 1 411 ? -2.065  8.155   1.822   1.00 30.23 ? 390 TRP B CZ3   1 
ATOM   6232 C  CH2   . TRP B 1 411 ? -0.760  8.573   2.086   1.00 28.45 ? 390 TRP B CH2   1 
ATOM   6233 N  N     . THR B 1 412 ? -6.531  10.625  -3.079  1.00 30.28 ? 391 THR B N     1 
ATOM   6234 C  CA    . THR B 1 412 ? -7.814  10.372  -3.784  1.00 24.89 ? 391 THR B CA    1 
ATOM   6235 C  C     . THR B 1 412 ? -7.566  9.435   -4.975  1.00 25.85 ? 391 THR B C     1 
ATOM   6236 O  O     . THR B 1 412 ? -8.263  8.399   -5.054  1.00 26.07 ? 391 THR B O     1 
ATOM   6237 C  CB    . THR B 1 412 ? -8.417  11.691  -4.276  1.00 25.75 ? 391 THR B CB    1 
ATOM   6238 O  OG1   . THR B 1 412 ? -8.643  12.559  -3.172  1.00 24.80 ? 391 THR B OG1   1 
ATOM   6239 C  CG2   . THR B 1 412 ? -9.715  11.508  -5.033  1.00 27.73 ? 391 THR B CG2   1 
ATOM   6240 N  N     . ARG B 1 413 ? -6.694  9.844   -5.917  1.00 23.79 ? 392 ARG B N     1 
ATOM   6241 C  CA    . ARG B 1 413 ? -6.373  9.109   -7.162  1.00 24.02 ? 392 ARG B CA    1 
ATOM   6242 C  C     . ARG B 1 413 ? -7.644  8.886   -7.990  1.00 25.70 ? 392 ARG B C     1 
ATOM   6243 O  O     . ARG B 1 413 ? -7.739  7.822   -8.608  1.00 27.72 ? 392 ARG B O     1 
ATOM   6244 C  CB    . ARG B 1 413 ? -5.695  7.773   -6.838  1.00 22.83 ? 392 ARG B CB    1 
ATOM   6245 C  CG    . ARG B 1 413 ? -4.285  7.927   -6.285  1.00 22.54 ? 392 ARG B CG    1 
ATOM   6246 C  CD    . ARG B 1 413 ? -3.427  8.764   -7.208  1.00 22.78 ? 392 ARG B CD    1 
ATOM   6247 N  NE    . ARG B 1 413 ? -2.011  8.569   -7.048  1.00 23.69 ? 392 ARG B NE    1 
ATOM   6248 C  CZ    . ARG B 1 413 ? -1.085  9.153   -7.803  1.00 29.48 ? 392 ARG B CZ    1 
ATOM   6249 N  NH1   . ARG B 1 413 ? -1.424  9.976   -8.788  1.00 30.46 ? 392 ARG B NH1   1 
ATOM   6250 N  NH2   . ARG B 1 413 ? 0.196   8.960   -7.542  1.00 30.43 ? 392 ARG B NH2   1 
ATOM   6251 N  N     . GLY B 1 414 ? -8.544  9.868   -8.034  1.00 26.40 ? 393 GLY B N     1 
ATOM   6252 C  CA    . GLY B 1 414 ? -9.599  10.000  -9.059  1.00 25.59 ? 393 GLY B CA    1 
ATOM   6253 C  C     . GLY B 1 414 ? -10.948 10.281  -8.422  1.00 25.56 ? 393 GLY B C     1 
ATOM   6254 O  O     . GLY B 1 414 ? -11.242 9.686   -7.386  1.00 24.30 ? 393 GLY B O     1 
ATOM   6255 N  N     . CYS B 1 415 ? -11.716 11.189  -9.011  1.00 25.30 ? 394 CYS B N     1 
ATOM   6256 C  CA    . CYS B 1 415 ? -13.116 11.484  -8.658  1.00 26.34 ? 394 CYS B CA    1 
ATOM   6257 C  C     . CYS B 1 415 ? -13.979 10.992  -9.813  1.00 27.46 ? 394 CYS B C     1 
ATOM   6258 O  O     . CYS B 1 415 ? -13.432 10.587  -10.832 1.00 31.40 ? 394 CYS B O     1 
ATOM   6259 C  CB    . CYS B 1 415 ? -13.285 12.968  -8.392  1.00 26.39 ? 394 CYS B CB    1 
ATOM   6260 S  SG    . CYS B 1 415 ? -13.010 13.431  -6.670  1.00 29.63 ? 394 CYS B SG    1 
ATOM   6261 N  N     . TYR B 1 416 ? -15.302 10.968  -9.651  1.00 27.04 ? 395 TYR B N     1 
ATOM   6262 C  CA    . TYR B 1 416 ? -15.962 11.255  -8.390  1.00 31.25 ? 395 TYR B CA    1 
ATOM   6263 C  C     . TYR B 1 416 ? -15.772 10.076  -7.407  1.00 29.92 ? 395 TYR B C     1 
ATOM   6264 O  O     . TYR B 1 416 ? -15.646 10.296  -6.183  1.00 31.47 ? 395 TYR B O     1 
ATOM   6265 C  CB    . TYR B 1 416 ? -17.422 11.605  -8.679  1.00 31.36 ? 395 TYR B CB    1 
ATOM   6266 C  CG    . TYR B 1 416 ? -17.587 12.557  -9.831  1.00 32.19 ? 395 TYR B CG    1 
ATOM   6267 C  CD1   . TYR B 1 416 ? -16.910 13.764  -9.851  1.00 31.63 ? 395 TYR B CD1   1 
ATOM   6268 C  CD2   . TYR B 1 416 ? -18.399 12.246  -10.910 1.00 34.69 ? 395 TYR B CD2   1 
ATOM   6269 C  CE1   . TYR B 1 416 ? -17.040 14.651  -10.902 1.00 30.94 ? 395 TYR B CE1   1 
ATOM   6270 C  CE2   . TYR B 1 416 ? -18.526 13.116  -11.979 1.00 34.49 ? 395 TYR B CE2   1 
ATOM   6271 C  CZ    . TYR B 1 416 ? -17.844 14.323  -11.972 1.00 33.32 ? 395 TYR B CZ    1 
ATOM   6272 O  OH    . TYR B 1 416 ? -17.943 15.201  -13.012 1.00 40.18 ? 395 TYR B OH    1 
ATOM   6273 N  N     . GLY B 1 417 ? -15.756 8.850   -7.918  1.00 29.63 ? 396 GLY B N     1 
ATOM   6274 C  CA    . GLY B 1 417 ? -15.543 7.644   -7.098  1.00 30.61 ? 396 GLY B CA    1 
ATOM   6275 C  C     . GLY B 1 417 ? -15.165 6.490   -7.989  1.00 30.01 ? 396 GLY B C     1 
ATOM   6276 O  O     . GLY B 1 417 ? -14.759 6.741   -9.149  1.00 30.55 ? 396 GLY B O     1 
ATOM   6277 N  N     . ALA B 1 418 ? -15.364 5.279   -7.493  1.00 26.11 ? 397 ALA B N     1 
ATOM   6278 C  CA    . ALA B 1 418 ? -15.001 4.031   -8.185  1.00 25.35 ? 397 ALA B CA    1 
ATOM   6279 C  C     . ALA B 1 418 ? -16.143 3.620   -9.120  1.00 25.76 ? 397 ALA B C     1 
ATOM   6280 O  O     . ALA B 1 418 ? -17.348 3.880   -8.841  1.00 33.04 ? 397 ALA B O     1 
ATOM   6281 C  CB    . ALA B 1 418 ? -14.652 2.940   -7.186  1.00 23.25 ? 397 ALA B CB    1 
ATOM   6282 N  N     . HIS B 1 419 ? -15.770 2.950   -10.199 1.00 25.79 ? 398 HIS B N     1 
ATOM   6283 C  CA    . HIS B 1 419 ? -16.682 2.186   -11.082 1.00 24.67 ? 398 HIS B CA    1 
ATOM   6284 C  C     . HIS B 1 419 ? -16.203 0.735   -11.045 1.00 25.09 ? 398 HIS B C     1 
ATOM   6285 O  O     . HIS B 1 419 ? -15.113 0.467   -10.504 1.00 23.69 ? 398 HIS B O     1 
ATOM   6286 C  CB    . HIS B 1 419 ? -16.722 2.798   -12.493 1.00 23.65 ? 398 HIS B CB    1 
ATOM   6287 C  CG    . HIS B 1 419 ? -15.392 2.874   -13.159 1.00 25.52 ? 398 HIS B CG    1 
ATOM   6288 N  ND1   . HIS B 1 419 ? -14.550 3.974   -13.010 1.00 26.99 ? 398 HIS B ND1   1 
ATOM   6289 C  CD2   . HIS B 1 419 ? -14.737 1.995   -13.947 1.00 23.38 ? 398 HIS B CD2   1 
ATOM   6290 C  CE1   . HIS B 1 419 ? -13.453 3.769   -13.703 1.00 23.80 ? 398 HIS B CE1   1 
ATOM   6291 N  NE2   . HIS B 1 419 ? -13.547 2.569   -14.275 1.00 25.15 ? 398 HIS B NE2   1 
ATOM   6292 N  N     . LEU B 1 420 ? -17.016 -0.166  -11.572 1.00 25.84 ? 399 LEU B N     1 
ATOM   6293 C  CA    . LEU B 1 420 ? -16.697 -1.604  -11.643 1.00 27.86 ? 399 LEU B CA    1 
ATOM   6294 C  C     . LEU B 1 420 ? -16.892 -2.100  -13.081 1.00 26.83 ? 399 LEU B C     1 
ATOM   6295 O  O     . LEU B 1 420 ? -17.970 -2.045  -13.676 1.00 23.26 ? 399 LEU B O     1 
ATOM   6296 C  CB    . LEU B 1 420 ? -17.574 -2.322  -10.604 1.00 27.05 ? 399 LEU B CB    1 
ATOM   6297 C  CG    . LEU B 1 420 ? -17.062 -2.288  -9.164  1.00 27.91 ? 399 LEU B CG    1 
ATOM   6298 C  CD1   . LEU B 1 420 ? -17.449 -0.994  -8.465  1.00 30.07 ? 399 LEU B CD1   1 
ATOM   6299 C  CD2   . LEU B 1 420 ? -17.568 -3.478  -8.359  1.00 27.85 ? 399 LEU B CD2   1 
ATOM   6300 N  N     . PRO B 1 421 ? -15.841 -2.661  -13.705 1.00 31.88 ? 400 PRO B N     1 
ATOM   6301 C  CA    . PRO B 1 421 ? -15.956 -3.170  -15.073 1.00 30.50 ? 400 PRO B CA    1 
ATOM   6302 C  C     . PRO B 1 421 ? -16.764 -4.461  -15.078 1.00 31.02 ? 400 PRO B C     1 
ATOM   6303 O  O     . PRO B 1 421 ? -17.125 -4.982  -14.013 1.00 25.76 ? 400 PRO B O     1 
ATOM   6304 C  CB    . PRO B 1 421 ? -14.503 -3.443  -15.421 1.00 30.22 ? 400 PRO B CB    1 
ATOM   6305 C  CG    . PRO B 1 421 ? -13.957 -3.928  -14.119 1.00 30.88 ? 400 PRO B CG    1 
ATOM   6306 C  CD    . PRO B 1 421 ? -14.536 -2.954  -13.112 1.00 30.64 ? 400 PRO B CD    1 
ATOM   6307 N  N     . PRO B 1 422 ? -17.084 -4.999  -16.278 1.00 30.26 ? 401 PRO B N     1 
ATOM   6308 C  CA    . PRO B 1 422 ? -17.809 -6.264  -16.378 1.00 28.62 ? 401 PRO B CA    1 
ATOM   6309 C  C     . PRO B 1 422 ? -17.185 -7.333  -15.471 1.00 26.50 ? 401 PRO B C     1 
ATOM   6310 O  O     . PRO B 1 422 ? -15.965 -7.417  -15.406 1.00 27.66 ? 401 PRO B O     1 
ATOM   6311 C  CB    . PRO B 1 422 ? -17.694 -6.633  -17.871 1.00 30.75 ? 401 PRO B CB    1 
ATOM   6312 C  CG    . PRO B 1 422 ? -17.579 -5.286  -18.568 1.00 33.09 ? 401 PRO B CG    1 
ATOM   6313 C  CD    . PRO B 1 422 ? -16.782 -4.418  -17.599 1.00 31.59 ? 401 PRO B CD    1 
ATOM   6314 N  N     . GLY B 1 423 ? -18.032 -8.079  -14.756 1.00 25.86 ? 402 GLY B N     1 
ATOM   6315 C  CA    . GLY B 1 423 ? -17.645 -9.296  -14.016 1.00 24.96 ? 402 GLY B CA    1 
ATOM   6316 C  C     . GLY B 1 423 ? -17.263 -8.971  -12.601 1.00 24.63 ? 402 GLY B C     1 
ATOM   6317 O  O     . GLY B 1 423 ? -17.089 -9.915  -11.803 1.00 27.83 ? 402 GLY B O     1 
ATOM   6318 N  N     . ALA B 1 424 ? -17.130 -7.690  -12.284 1.00 22.50 ? 403 ALA B N     1 
ATOM   6319 C  CA    . ALA B 1 424 ? -16.632 -7.259  -10.964 1.00 22.29 ? 403 ALA B CA    1 
ATOM   6320 C  C     . ALA B 1 424 ? -17.701 -7.560  -9.920  1.00 23.18 ? 403 ALA B C     1 
ATOM   6321 O  O     . ALA B 1 424 ? -17.389 -8.210  -8.935  1.00 20.99 ? 403 ALA B O     1 
ATOM   6322 C  CB    . ALA B 1 424 ? -16.293 -5.802  -10.985 1.00 21.98 ? 403 ALA B CB    1 
ATOM   6323 N  N     . TRP B 1 425 ? -18.921 -7.072  -10.149 1.00 26.85 ? 404 TRP B N     1 
ATOM   6324 C  CA    . TRP B 1 425 ? -19.981 -6.982  -9.113  1.00 30.09 ? 404 TRP B CA    1 
ATOM   6325 C  C     . TRP B 1 425 ? -20.407 -8.384  -8.666  1.00 30.24 ? 404 TRP B C     1 
ATOM   6326 O  O     . TRP B 1 425 ? -20.566 -8.584  -7.477  1.00 29.31 ? 404 TRP B O     1 
ATOM   6327 C  CB    . TRP B 1 425 ? -21.182 -6.175  -9.613  1.00 31.60 ? 404 TRP B CB    1 
ATOM   6328 C  CG    . TRP B 1 425 ? -21.195 -4.736  -9.212  1.00 30.54 ? 404 TRP B CG    1 
ATOM   6329 C  CD1   . TRP B 1 425 ? -21.275 -3.667  -10.052 1.00 31.57 ? 404 TRP B CD1   1 
ATOM   6330 C  CD2   . TRP B 1 425 ? -21.177 -4.204  -7.874  1.00 30.86 ? 404 TRP B CD2   1 
ATOM   6331 N  NE1   . TRP B 1 425 ? -21.301 -2.504  -9.325  1.00 33.24 ? 404 TRP B NE1   1 
ATOM   6332 C  CE2   . TRP B 1 425 ? -21.251 -2.801  -7.989  1.00 32.51 ? 404 TRP B CE2   1 
ATOM   6333 C  CE3   . TRP B 1 425 ? -21.103 -4.769  -6.596  1.00 34.09 ? 404 TRP B CE3   1 
ATOM   6334 C  CZ2   . TRP B 1 425 ? -21.239 -1.956  -6.875  1.00 34.51 ? 404 TRP B CZ2   1 
ATOM   6335 C  CZ3   . TRP B 1 425 ? -21.109 -3.942  -5.490  1.00 34.89 ? 404 TRP B CZ3   1 
ATOM   6336 C  CH2   . TRP B 1 425 ? -21.179 -2.553  -5.630  1.00 35.77 ? 404 TRP B CH2   1 
ATOM   6337 N  N     . THR B 1 426 ? -20.556 -9.321  -9.591  1.00 31.67 ? 405 THR B N     1 
ATOM   6338 C  CA    . THR B 1 426 ? -21.176 -10.638 -9.297  1.00 33.68 ? 405 THR B CA    1 
ATOM   6339 C  C     . THR B 1 426 ? -20.170 -11.545 -8.605  1.00 31.96 ? 405 THR B C     1 
ATOM   6340 O  O     . THR B 1 426 ? -20.613 -12.437 -7.881  1.00 35.63 ? 405 THR B O     1 
ATOM   6341 C  CB    . THR B 1 426 ? -21.692 -11.319 -10.561 1.00 32.70 ? 405 THR B CB    1 
ATOM   6342 O  OG1   . THR B 1 426 ? -20.626 -11.174 -11.499 1.00 31.81 ? 405 THR B OG1   1 
ATOM   6343 C  CG2   . THR B 1 426 ? -22.986 -10.698 -11.040 1.00 33.07 ? 405 THR B CG2   1 
ATOM   6344 N  N     . VAL B 1 427 ? -18.879 -11.321 -8.831  1.00 30.79 ? 406 VAL B N     1 
ATOM   6345 C  CA    . VAL B 1 427 ? -17.793 -12.263 -8.419  1.00 28.28 ? 406 VAL B CA    1 
ATOM   6346 C  C     . VAL B 1 427 ? -17.065 -11.712 -7.200  1.00 23.41 ? 406 VAL B C     1 
ATOM   6347 O  O     . VAL B 1 427 ? -16.845 -12.515 -6.292  1.00 24.11 ? 406 VAL B O     1 
ATOM   6348 C  CB    . VAL B 1 427 ? -16.810 -12.562 -9.567  1.00 26.79 ? 406 VAL B CB    1 
ATOM   6349 C  CG1   . VAL B 1 427 ? -15.579 -13.328 -9.075  1.00 25.62 ? 406 VAL B CG1   1 
ATOM   6350 C  CG2   . VAL B 1 427 ? -17.500 -13.305 -10.701 1.00 27.20 ? 406 VAL B CG2   1 
ATOM   6351 N  N     . TYR B 1 428 ? -16.686 -10.435 -7.219  1.00 21.55 ? 407 TYR B N     1 
ATOM   6352 C  CA    . TYR B 1 428 ? -15.921 -9.762  -6.125  1.00 23.35 ? 407 TYR B CA    1 
ATOM   6353 C  C     . TYR B 1 428 ? -16.814 -8.862  -5.273  1.00 22.62 ? 407 TYR B C     1 
ATOM   6354 O  O     . TYR B 1 428 ? -16.456 -8.673  -4.107  1.00 25.44 ? 407 TYR B O     1 
ATOM   6355 C  CB    . TYR B 1 428 ? -14.765 -8.929  -6.691  1.00 23.78 ? 407 TYR B CB    1 
ATOM   6356 C  CG    . TYR B 1 428 ? -13.886 -9.703  -7.642  1.00 26.65 ? 407 TYR B CG    1 
ATOM   6357 C  CD1   . TYR B 1 428 ? -12.789 -10.429 -7.198  1.00 29.08 ? 407 TYR B CD1   1 
ATOM   6358 C  CD2   . TYR B 1 428 ? -14.221 -9.795  -8.977  1.00 26.75 ? 407 TYR B CD2   1 
ATOM   6359 C  CE1   . TYR B 1 428 ? -12.001 -11.162 -8.074  1.00 27.84 ? 407 TYR B CE1   1 
ATOM   6360 C  CE2   . TYR B 1 428 ? -13.469 -10.542 -9.858  1.00 29.72 ? 407 TYR B CE2   1 
ATOM   6361 C  CZ    . TYR B 1 428 ? -12.350 -11.220 -9.409  1.00 28.47 ? 407 TYR B CZ    1 
ATOM   6362 O  OH    . TYR B 1 428 ? -11.652 -11.944 -10.322 1.00 24.74 ? 407 TYR B OH    1 
ATOM   6363 N  N     . GLY B 1 429 ? -17.858 -8.266  -5.860  1.00 23.89 ? 408 GLY B N     1 
ATOM   6364 C  CA    . GLY B 1 429 ? -18.862 -7.413  -5.187  1.00 27.64 ? 408 GLY B CA    1 
ATOM   6365 C  C     . GLY B 1 429 ? -19.208 -7.889  -3.773  1.00 26.69 ? 408 GLY B C     1 
ATOM   6366 O  O     . GLY B 1 429 ? -19.032 -7.160  -2.816  1.00 26.31 ? 408 GLY B O     1 
ATOM   6367 N  N     . PRO B 1 430 ? -19.623 -9.153  -3.558  1.00 28.17 ? 409 PRO B N     1 
ATOM   6368 C  CA    . PRO B 1 430 ? -20.080 -9.576  -2.234  1.00 27.82 ? 409 PRO B CA    1 
ATOM   6369 C  C     . PRO B 1 430 ? -19.143 -9.206  -1.076  1.00 24.66 ? 409 PRO B C     1 
ATOM   6370 O  O     . PRO B 1 430 ? -19.650 -9.166  -0.013  1.00 25.55 ? 409 PRO B O     1 
ATOM   6371 C  CB    . PRO B 1 430 ? -20.225 -11.100 -2.390  1.00 26.46 ? 409 PRO B CB    1 
ATOM   6372 C  CG    . PRO B 1 430 ? -20.568 -11.269 -3.848  1.00 27.17 ? 409 PRO B CG    1 
ATOM   6373 C  CD    . PRO B 1 430 ? -19.671 -10.253 -4.533  1.00 28.02 ? 409 PRO B CD    1 
ATOM   6374 N  N     . ALA B 1 431 ? -17.858 -8.887  -1.303  1.00 26.89 ? 410 ALA B N     1 
ATOM   6375 C  CA    . ALA B 1 431 ? -16.852 -8.587  -0.239  1.00 25.65 ? 410 ALA B CA    1 
ATOM   6376 C  C     . ALA B 1 431 ? -16.892 -7.116  0.178   1.00 25.41 ? 410 ALA B C     1 
ATOM   6377 O  O     . ALA B 1 431 ? -16.094 -6.729  1.057   1.00 23.60 ? 410 ALA B O     1 
ATOM   6378 C  CB    . ALA B 1 431 ? -15.454 -8.915  -0.702  1.00 25.40 ? 410 ALA B CB    1 
ATOM   6379 N  N     . LEU B 1 432 ? -17.746 -6.325  -0.467  1.00 24.61 ? 411 LEU B N     1 
ATOM   6380 C  CA    . LEU B 1 432 ? -17.684 -4.846  -0.448  1.00 27.61 ? 411 LEU B CA    1 
ATOM   6381 C  C     . LEU B 1 432 ? -17.874 -4.267  0.963   1.00 28.61 ? 411 LEU B C     1 
ATOM   6382 O  O     . LEU B 1 432 ? -17.296 -3.226  1.240   1.00 29.45 ? 411 LEU B O     1 
ATOM   6383 C  CB    . LEU B 1 432 ? -18.777 -4.348  -1.387  1.00 30.36 ? 411 LEU B CB    1 
ATOM   6384 C  CG    . LEU B 1 432 ? -18.946 -2.831  -1.412  1.00 34.09 ? 411 LEU B CG    1 
ATOM   6385 C  CD1   . LEU B 1 432 ? -17.665 -2.173  -1.916  1.00 33.49 ? 411 LEU B CD1   1 
ATOM   6386 C  CD2   . LEU B 1 432 ? -20.148 -2.452  -2.259  1.00 32.68 ? 411 LEU B CD2   1 
ATOM   6387 N  N     . ARG B 1 433 ? -18.745 -4.852  1.788   1.00 29.96 ? 412 ARG B N     1 
ATOM   6388 C  CA    . ARG B 1 433 ? -19.094 -4.321  3.139   1.00 31.35 ? 412 ARG B CA    1 
ATOM   6389 C  C     . ARG B 1 433 ? -18.625 -5.335  4.181   1.00 30.33 ? 412 ARG B C     1 
ATOM   6390 O  O     . ARG B 1 433 ? -18.537 -4.917  5.337   1.00 30.10 ? 412 ARG B O     1 
ATOM   6391 C  CB    . ARG B 1 433 ? -20.601 -4.051  3.336   1.00 32.02 ? 412 ARG B CB    1 
ATOM   6392 C  CG    . ARG B 1 433 ? -21.153 -2.838  2.595   1.00 32.77 ? 412 ARG B CG    1 
ATOM   6393 C  CD    . ARG B 1 433 ? -22.665 -2.825  2.427   1.00 30.93 ? 412 ARG B CD    1 
ATOM   6394 N  NE    . ARG B 1 433 ? -23.048 -2.301  1.112   1.00 33.62 ? 412 ARG B NE    1 
ATOM   6395 C  CZ    . ARG B 1 433 ? -23.752 -2.945  0.154   1.00 32.15 ? 412 ARG B CZ    1 
ATOM   6396 N  NH1   . ARG B 1 433 ? -24.164 -4.196  0.311   1.00 30.58 ? 412 ARG B NH1   1 
ATOM   6397 N  NH2   . ARG B 1 433 ? -24.040 -2.316  -0.973  1.00 30.83 ? 412 ARG B NH2   1 
ATOM   6398 N  N     . VAL B 1 434 ? -18.299 -6.580  3.782   1.00 27.94 ? 413 VAL B N     1 
ATOM   6399 C  CA    . VAL B 1 434 ? -17.952 -7.699  4.718   1.00 29.32 ? 413 VAL B CA    1 
ATOM   6400 C  C     . VAL B 1 434 ? -16.826 -7.215  5.634   1.00 30.52 ? 413 VAL B C     1 
ATOM   6401 O  O     . VAL B 1 434 ? -15.751 -6.852  5.181   1.00 26.83 ? 413 VAL B O     1 
ATOM   6402 C  CB    . VAL B 1 434 ? -17.546 -8.992  3.979   1.00 31.92 ? 413 VAL B CB    1 
ATOM   6403 C  CG1   . VAL B 1 434 ? -17.426 -10.196 4.904   1.00 32.75 ? 413 VAL B CG1   1 
ATOM   6404 C  CG2   . VAL B 1 434 ? -18.492 -9.323  2.847   1.00 36.57 ? 413 VAL B CG2   1 
ATOM   6405 N  N     . PRO B 1 435 ? -17.046 -7.085  6.957   1.00 32.87 ? 414 PRO B N     1 
ATOM   6406 C  CA    . PRO B 1 435 ? -15.933 -6.785  7.856   1.00 31.88 ? 414 PRO B CA    1 
ATOM   6407 C  C     . PRO B 1 435 ? -14.872 -7.887  7.735   1.00 31.20 ? 414 PRO B C     1 
ATOM   6408 O  O     . PRO B 1 435 ? -15.218 -8.992  7.307   1.00 33.09 ? 414 PRO B O     1 
ATOM   6409 C  CB    . PRO B 1 435 ? -16.587 -6.701  9.243   1.00 29.66 ? 414 PRO B CB    1 
ATOM   6410 C  CG    . PRO B 1 435 ? -18.038 -6.385  8.941   1.00 31.63 ? 414 PRO B CG    1 
ATOM   6411 C  CD    . PRO B 1 435 ? -18.351 -7.093  7.634   1.00 30.25 ? 414 PRO B CD    1 
ATOM   6412 N  N     . VAL B 1 436 ? -13.620 -7.539  8.042   1.00 28.39 ? 415 VAL B N     1 
ATOM   6413 C  CA    . VAL B 1 436 ? -12.445 -8.455  8.031   1.00 28.55 ? 415 VAL B CA    1 
ATOM   6414 C  C     . VAL B 1 436 ? -11.847 -8.450  9.437   1.00 28.72 ? 415 VAL B C     1 
ATOM   6415 O  O     . VAL B 1 436 ? -11.088 -7.495  9.787   1.00 22.26 ? 415 VAL B O     1 
ATOM   6416 C  CB    . VAL B 1 436 ? -11.401 -8.065  6.971   1.00 34.14 ? 415 VAL B CB    1 
ATOM   6417 C  CG1   . VAL B 1 436 ? -10.097 -8.858  7.130   1.00 31.30 ? 415 VAL B CG1   1 
ATOM   6418 C  CG2   . VAL B 1 436 ? -11.976 -8.217  5.566   1.00 34.98 ? 415 VAL B CG2   1 
ATOM   6419 N  N     . GLY B 1 437 ? -12.240 -9.459  10.221  1.00 28.39 ? 416 GLY B N     1 
ATOM   6420 C  CA    . GLY B 1 437 ? -11.940 -9.528  11.655  1.00 30.56 ? 416 GLY B CA    1 
ATOM   6421 C  C     . GLY B 1 437 ? -12.456 -8.285  12.359  1.00 32.96 ? 416 GLY B C     1 
ATOM   6422 O  O     . GLY B 1 437 ? -13.692 -8.107  12.392  1.00 35.63 ? 416 GLY B O     1 
ATOM   6423 N  N     . ARG B 1 438 ? -11.560 -7.451  12.893  1.00 31.94 ? 417 ARG B N     1 
ATOM   6424 C  CA    . ARG B 1 438 ? -11.925 -6.256  13.695  1.00 31.65 ? 417 ARG B CA    1 
ATOM   6425 C  C     . ARG B 1 438 ? -11.820 -4.989  12.829  1.00 31.20 ? 417 ARG B C     1 
ATOM   6426 O  O     . ARG B 1 438 ? -11.931 -3.913  13.423  1.00 32.31 ? 417 ARG B O     1 
ATOM   6427 C  CB    . ARG B 1 438 ? -10.988 -6.149  14.906  1.00 33.11 ? 417 ARG B CB    1 
ATOM   6428 C  CG    . ARG B 1 438 ? -11.030 -7.350  15.833  1.00 32.83 ? 417 ARG B CG    1 
ATOM   6429 C  CD    . ARG B 1 438 ? -9.961  -7.302  16.919  1.00 34.43 ? 417 ARG B CD    1 
ATOM   6430 N  NE    . ARG B 1 438 ? -10.465 -7.930  18.139  1.00 38.27 ? 417 ARG B NE    1 
ATOM   6431 C  CZ    . ARG B 1 438 ? -11.238 -7.356  19.084  1.00 38.09 ? 417 ARG B CZ    1 
ATOM   6432 N  NH1   . ARG B 1 438 ? -11.592 -6.079  19.040  1.00 35.04 ? 417 ARG B NH1   1 
ATOM   6433 N  NH2   . ARG B 1 438 ? -11.652 -8.091  20.100  1.00 41.46 ? 417 ARG B NH2   1 
ATOM   6434 N  N     . VAL B 1 439 ? -11.575 -5.099  11.506  1.00 29.47 ? 418 VAL B N     1 
ATOM   6435 C  CA    . VAL B 1 439 ? -11.523 -3.937  10.564  1.00 27.08 ? 418 VAL B CA    1 
ATOM   6436 C  C     . VAL B 1 439 ? -12.817 -3.868  9.748   1.00 27.73 ? 418 VAL B C     1 
ATOM   6437 O  O     . VAL B 1 439 ? -13.170 -4.894  9.109   1.00 23.96 ? 418 VAL B O     1 
ATOM   6438 C  CB    . VAL B 1 439 ? -10.313 -4.012  9.621   1.00 27.12 ? 418 VAL B CB    1 
ATOM   6439 C  CG1   . VAL B 1 439 ? -10.355 -2.892  8.586   1.00 27.38 ? 418 VAL B CG1   1 
ATOM   6440 C  CG2   . VAL B 1 439 ? -9.000  -3.987  10.391  1.00 26.75 ? 418 VAL B CG2   1 
ATOM   6441 N  N     . HIS B 1 440 ? -13.445 -2.681  9.735   1.00 26.36 ? 419 HIS B N     1 
ATOM   6442 C  CA    . HIS B 1 440 ? -14.740 -2.375  9.063   1.00 26.76 ? 419 HIS B CA    1 
ATOM   6443 C  C     . HIS B 1 440 ? -14.542 -1.331  7.951   1.00 26.49 ? 419 HIS B C     1 
ATOM   6444 O  O     . HIS B 1 440 ? -13.500 -0.641  7.922   1.00 24.22 ? 419 HIS B O     1 
ATOM   6445 C  CB    . HIS B 1 440 ? -15.817 -1.915  10.065  1.00 27.07 ? 419 HIS B CB    1 
ATOM   6446 C  CG    . HIS B 1 440 ? -16.166 -2.928  11.106  1.00 26.95 ? 419 HIS B CG    1 
ATOM   6447 N  ND1   . HIS B 1 440 ? -17.456 -3.385  11.275  1.00 25.52 ? 419 HIS B ND1   1 
ATOM   6448 C  CD2   . HIS B 1 440 ? -15.400 -3.584  12.004  1.00 27.62 ? 419 HIS B CD2   1 
ATOM   6449 C  CE1   . HIS B 1 440 ? -17.474 -4.288  12.238  1.00 25.44 ? 419 HIS B CE1   1 
ATOM   6450 N  NE2   . HIS B 1 440 ? -16.220 -4.428  12.693  1.00 29.68 ? 419 HIS B NE2   1 
ATOM   6451 N  N     . TRP B 1 441 ? -15.546 -1.231  7.086   1.00 26.73 ? 420 TRP B N     1 
ATOM   6452 C  CA    . TRP B 1 441 ? -15.483 -0.523  5.788   1.00 27.85 ? 420 TRP B CA    1 
ATOM   6453 C  C     . TRP B 1 441 ? -16.542 0.599   5.772   1.00 28.82 ? 420 TRP B C     1 
ATOM   6454 O  O     . TRP B 1 441 ? -17.700 0.360   6.179   1.00 26.98 ? 420 TRP B O     1 
ATOM   6455 C  CB    . TRP B 1 441 ? -15.606 -1.555  4.639   1.00 26.69 ? 420 TRP B CB    1 
ATOM   6456 C  CG    . TRP B 1 441 ? -14.650 -2.704  4.811   1.00 26.83 ? 420 TRP B CG    1 
ATOM   6457 C  CD1   . TRP B 1 441 ? -14.963 -3.983  5.176   1.00 26.32 ? 420 TRP B CD1   1 
ATOM   6458 C  CD2   . TRP B 1 441 ? -13.202 -2.638  4.788   1.00 26.65 ? 420 TRP B CD2   1 
ATOM   6459 N  NE1   . TRP B 1 441 ? -13.816 -4.716  5.352   1.00 25.95 ? 420 TRP B NE1   1 
ATOM   6460 C  CE2   . TRP B 1 441 ? -12.722 -3.921  5.122   1.00 25.28 ? 420 TRP B CE2   1 
ATOM   6461 C  CE3   . TRP B 1 441 ? -12.267 -1.631  4.493   1.00 25.98 ? 420 TRP B CE3   1 
ATOM   6462 C  CZ2   . TRP B 1 441 ? -11.358 -4.230  5.140   1.00 25.29 ? 420 TRP B CZ2   1 
ATOM   6463 C  CZ3   . TRP B 1 441 ? -10.919 -1.935  4.520   1.00 24.34 ? 420 TRP B CZ3   1 
ATOM   6464 C  CH2   . TRP B 1 441 ? -10.475 -3.220  4.828   1.00 25.17 ? 420 TRP B CH2   1 
ATOM   6465 N  N     . ALA B 1 442 ? -16.140 1.790   5.331   1.00 28.45 ? 421 ALA B N     1 
ATOM   6466 C  CA    . ALA B 1 442 ? -17.040 2.915   4.973   1.00 28.64 ? 421 ALA B CA    1 
ATOM   6467 C  C     . ALA B 1 442 ? -16.512 3.654   3.723   1.00 26.50 ? 421 ALA B C     1 
ATOM   6468 O  O     . ALA B 1 442 ? -15.443 3.262   3.186   1.00 25.37 ? 421 ALA B O     1 
ATOM   6469 C  CB    . ALA B 1 442 ? -17.172 3.828   6.177   1.00 25.85 ? 421 ALA B CB    1 
ATOM   6470 N  N     . GLY B 1 443 ? -17.230 4.706   3.306   1.00 26.01 ? 422 GLY B N     1 
ATOM   6471 C  CA    . GLY B 1 443 ? -16.951 5.573   2.146   1.00 22.96 ? 422 GLY B CA    1 
ATOM   6472 C  C     . GLY B 1 443 ? -18.100 5.449   1.167   1.00 23.81 ? 422 GLY B C     1 
ATOM   6473 O  O     . GLY B 1 443 ? -18.756 4.391   1.221   1.00 25.67 ? 422 GLY B O     1 
ATOM   6474 N  N     . THR B 1 444 ? -18.364 6.459   0.318   1.00 23.07 ? 423 THR B N     1 
ATOM   6475 C  CA    . THR B 1 444 ? -19.591 6.541   -0.536  1.00 23.00 ? 423 THR B CA    1 
ATOM   6476 C  C     . THR B 1 444 ? -19.719 5.259   -1.390  1.00 26.67 ? 423 THR B C     1 
ATOM   6477 O  O     . THR B 1 444 ? -20.858 4.914   -1.816  1.00 25.42 ? 423 THR B O     1 
ATOM   6478 C  CB    . THR B 1 444 ? -19.571 7.802   -1.430  1.00 22.68 ? 423 THR B CB    1 
ATOM   6479 O  OG1   . THR B 1 444 ? -20.840 8.007   -2.064  1.00 21.52 ? 423 THR B OG1   1 
ATOM   6480 C  CG2   . THR B 1 444 ? -18.540 7.738   -2.547  1.00 21.56 ? 423 THR B CG2   1 
ATOM   6481 N  N     . GLU B 1 445 ? -18.584 4.609   -1.692  1.00 28.83 ? 424 GLU B N     1 
ATOM   6482 C  CA    . GLU B 1 445 ? -18.515 3.369   -2.526  1.00 31.02 ? 424 GLU B CA    1 
ATOM   6483 C  C     . GLU B 1 445 ? -19.320 2.251   -1.863  1.00 30.27 ? 424 GLU B C     1 
ATOM   6484 O  O     . GLU B 1 445 ? -19.747 1.358   -2.595  1.00 37.05 ? 424 GLU B O     1 
ATOM   6485 C  CB    . GLU B 1 445 ? -17.067 2.914   -2.761  1.00 30.30 ? 424 GLU B CB    1 
ATOM   6486 C  CG    . GLU B 1 445 ? -16.349 3.725   -3.828  1.00 31.24 ? 424 GLU B CG    1 
ATOM   6487 C  CD    . GLU B 1 445 ? -15.825 5.118   -3.470  1.00 30.75 ? 424 GLU B CD    1 
ATOM   6488 O  OE1   . GLU B 1 445 ? -15.488 5.844   -4.423  1.00 29.10 ? 424 GLU B OE1   1 
ATOM   6489 O  OE2   . GLU B 1 445 ? -15.755 5.480   -2.259  1.00 27.96 ? 424 GLU B OE2   1 
ATOM   6490 N  N     . THR B 1 446 ? -19.520 2.301   -0.542  1.00 31.45 ? 425 THR B N     1 
ATOM   6491 C  CA    . THR B 1 446 ? -20.252 1.253   0.239   1.00 29.51 ? 425 THR B CA    1 
ATOM   6492 C  C     . THR B 1 446 ? -21.717 1.634   0.542   1.00 27.06 ? 425 THR B C     1 
ATOM   6493 O  O     . THR B 1 446 ? -22.386 0.787   1.174   1.00 27.06 ? 425 THR B O     1 
ATOM   6494 C  CB    . THR B 1 446 ? -19.559 0.946   1.577   1.00 25.93 ? 425 THR B CB    1 
ATOM   6495 O  OG1   . THR B 1 446 ? -19.639 2.064   2.457   1.00 25.71 ? 425 THR B OG1   1 
ATOM   6496 C  CG2   . THR B 1 446 ? -18.106 0.575   1.435   1.00 25.12 ? 425 THR B CG2   1 
ATOM   6497 N  N     . ALA B 1 447 ? -22.212 2.827   0.178   1.00 25.46 ? 426 ALA B N     1 
ATOM   6498 C  CA    . ALA B 1 447 ? -23.606 3.248   0.496   1.00 28.89 ? 426 ALA B CA    1 
ATOM   6499 C  C     . ALA B 1 447 ? -24.622 2.507   -0.395  1.00 31.19 ? 426 ALA B C     1 
ATOM   6500 O  O     . ALA B 1 447 ? -24.266 2.111   -1.520  1.00 36.84 ? 426 ALA B O     1 
ATOM   6501 C  CB    . ALA B 1 447 ? -23.772 4.730   0.315   1.00 28.52 ? 426 ALA B CB    1 
ATOM   6502 N  N     . GLU B 1 448 ? -25.861 2.349   0.060   1.00 32.94 ? 427 GLU B N     1 
ATOM   6503 C  CA    . GLU B 1 448 ? -26.965 1.775   -0.770  1.00 32.03 ? 427 GLU B CA    1 
ATOM   6504 C  C     . GLU B 1 448 ? -27.711 2.922   -1.468  1.00 30.79 ? 427 GLU B C     1 
ATOM   6505 O  O     . GLU B 1 448 ? -28.339 2.669   -2.531  1.00 28.26 ? 427 GLU B O     1 
ATOM   6506 C  CB    . GLU B 1 448 ? -27.916 0.928   0.080   1.00 28.89 ? 427 GLU B CB    1 
ATOM   6507 C  CG    . GLU B 1 448 ? -27.221 -0.039  1.050   1.00 32.14 ? 427 GLU B CG    1 
ATOM   6508 C  CD    . GLU B 1 448 ? -28.158 -1.023  1.749   1.00 29.26 ? 427 GLU B CD    1 
ATOM   6509 O  OE1   . GLU B 1 448 ? -27.735 -1.753  2.626   1.00 34.53 ? 427 GLU B OE1   1 
ATOM   6510 O  OE2   . GLU B 1 448 ? -29.306 -1.059  1.402   1.00 32.13 ? 427 GLU B OE2   1 
ATOM   6511 N  N     . ARG B 1 449 ? -27.698 4.113   -0.854  1.00 33.36 ? 428 ARG B N     1 
ATOM   6512 C  CA    . ARG B 1 449 ? -28.481 5.296   -1.310  1.00 42.06 ? 428 ARG B CA    1 
ATOM   6513 C  C     . ARG B 1 449 ? -27.478 6.400   -1.675  1.00 33.92 ? 428 ARG B C     1 
ATOM   6514 O  O     . ARG B 1 449 ? -26.590 6.698   -0.872  1.00 28.40 ? 428 ARG B O     1 
ATOM   6515 C  CB    . ARG B 1 449 ? -29.567 5.730   -0.296  1.00 46.24 ? 428 ARG B CB    1 
ATOM   6516 C  CG    . ARG B 1 449 ? -30.938 6.016   -0.916  1.00 53.30 ? 428 ARG B CG    1 
ATOM   6517 C  CD    . ARG B 1 449 ? -31.932 6.806   -0.057  1.00 61.99 ? 428 ARG B CD    1 
ATOM   6518 N  NE    . ARG B 1 449 ? -31.597 8.233   0.077   1.00 67.32 ? 428 ARG B NE    1 
ATOM   6519 C  CZ    . ARG B 1 449 ? -31.110 8.840   1.172   1.00 66.93 ? 428 ARG B CZ    1 
ATOM   6520 N  NH1   . ARG B 1 449 ? -30.892 8.166   2.290   1.00 69.25 ? 428 ARG B NH1   1 
ATOM   6521 N  NH2   . ARG B 1 449 ? -30.834 10.137  1.144   1.00 60.58 ? 428 ARG B NH2   1 
ATOM   6522 N  N     . TRP B 1 450 ? -27.632 6.954   -2.878  1.00 32.91 ? 429 TRP B N     1 
ATOM   6523 C  CA    . TRP B 1 450 ? -26.801 8.081   -3.347  1.00 30.50 ? 429 TRP B CA    1 
ATOM   6524 C  C     . TRP B 1 450 ? -25.335 7.671   -3.151  1.00 31.19 ? 429 TRP B C     1 
ATOM   6525 O  O     . TRP B 1 450 ? -24.536 8.457   -2.503  1.00 29.57 ? 429 TRP B O     1 
ATOM   6526 C  CB    . TRP B 1 450 ? -27.185 9.355   -2.577  1.00 29.35 ? 429 TRP B CB    1 
ATOM   6527 C  CG    . TRP B 1 450 ? -28.425 10.035  -3.067  1.00 29.07 ? 429 TRP B CG    1 
ATOM   6528 C  CD1   . TRP B 1 450 ? -29.629 10.131  -2.422  1.00 31.09 ? 429 TRP B CD1   1 
ATOM   6529 C  CD2   . TRP B 1 450 ? -28.577 10.751  -4.305  1.00 30.04 ? 429 TRP B CD2   1 
ATOM   6530 N  NE1   . TRP B 1 450 ? -30.514 10.862  -3.168  1.00 29.50 ? 429 TRP B NE1   1 
ATOM   6531 C  CE2   . TRP B 1 450 ? -29.897 11.252  -4.330  1.00 28.38 ? 429 TRP B CE2   1 
ATOM   6532 C  CE3   . TRP B 1 450 ? -27.732 10.999  -5.395  1.00 28.98 ? 429 TRP B CE3   1 
ATOM   6533 C  CZ2   . TRP B 1 450 ? -30.386 11.993  -5.401  1.00 28.90 ? 429 TRP B CZ2   1 
ATOM   6534 C  CZ3   . TRP B 1 450 ? -28.214 11.740  -6.452  1.00 30.71 ? 429 TRP B CZ3   1 
ATOM   6535 C  CH2   . TRP B 1 450 ? -29.529 12.215  -6.459  1.00 32.08 ? 429 TRP B CH2   1 
ATOM   6536 N  N     . THR B 1 451 ? -25.010 6.439   -3.591  1.00 28.77 ? 430 THR B N     1 
ATOM   6537 C  CA    . THR B 1 451 ? -23.609 5.951   -3.726  1.00 27.50 ? 430 THR B CA    1 
ATOM   6538 C  C     . THR B 1 451 ? -22.867 6.938   -4.647  1.00 25.81 ? 430 THR B C     1 
ATOM   6539 O  O     . THR B 1 451 ? -23.471 7.381   -5.646  1.00 24.28 ? 430 THR B O     1 
ATOM   6540 C  CB    . THR B 1 451 ? -23.538 4.479   -4.164  1.00 26.23 ? 430 THR B CB    1 
ATOM   6541 O  OG1   . THR B 1 451 ? -22.180 4.090   -3.976  1.00 23.05 ? 430 THR B OG1   1 
ATOM   6542 C  CG2   . THR B 1 451 ? -23.955 4.212   -5.597  1.00 27.96 ? 430 THR B CG2   1 
ATOM   6543 N  N     . GLY B 1 452 ? -21.653 7.333   -4.269  1.00 24.83 ? 431 GLY B N     1 
ATOM   6544 C  CA    . GLY B 1 452 ? -20.820 8.208   -5.107  1.00 27.93 ? 431 GLY B CA    1 
ATOM   6545 C  C     . GLY B 1 452 ? -20.991 9.683   -4.760  1.00 29.15 ? 431 GLY B C     1 
ATOM   6546 O  O     . GLY B 1 452 ? -20.195 10.502  -5.278  1.00 30.02 ? 431 GLY B O     1 
ATOM   6547 N  N     . TYR B 1 453 ? -21.956 10.024  -3.896  1.00 27.10 ? 432 TYR B N     1 
ATOM   6548 C  CA    . TYR B 1 453 ? -22.256 11.420  -3.472  1.00 24.48 ? 432 TYR B CA    1 
ATOM   6549 C  C     . TYR B 1 453 ? -21.835 11.632  -2.019  1.00 23.35 ? 432 TYR B C     1 
ATOM   6550 O  O     . TYR B 1 453 ? -21.506 10.682  -1.317  1.00 29.27 ? 432 TYR B O     1 
ATOM   6551 C  CB    . TYR B 1 453 ? -23.738 11.685  -3.733  1.00 24.77 ? 432 TYR B CB    1 
ATOM   6552 C  CG    . TYR B 1 453 ? -24.046 11.736  -5.203  1.00 23.90 ? 432 TYR B CG    1 
ATOM   6553 C  CD1   . TYR B 1 453 ? -24.297 12.944  -5.837  1.00 23.37 ? 432 TYR B CD1   1 
ATOM   6554 C  CD2   . TYR B 1 453 ? -24.008 10.581  -5.975  1.00 24.43 ? 432 TYR B CD2   1 
ATOM   6555 C  CE1   . TYR B 1 453 ? -24.515 13.009  -7.199  1.00 22.36 ? 432 TYR B CE1   1 
ATOM   6556 C  CE2   . TYR B 1 453 ? -24.235 10.619  -7.334  1.00 23.07 ? 432 TYR B CE2   1 
ATOM   6557 C  CZ    . TYR B 1 453 ? -24.489 11.844  -7.947  1.00 24.67 ? 432 TYR B CZ    1 
ATOM   6558 O  OH    . TYR B 1 453 ? -24.714 11.920  -9.288  1.00 22.35 ? 432 TYR B OH    1 
ATOM   6559 N  N     . ILE B 1 454 ? -21.836 12.867  -1.559  1.00 25.14 ? 433 ILE B N     1 
ATOM   6560 C  CA    . ILE B 1 454 ? -21.604 13.228  -0.121  1.00 29.69 ? 433 ILE B CA    1 
ATOM   6561 C  C     . ILE B 1 454 ? -22.634 12.527  0.807   1.00 32.38 ? 433 ILE B C     1 
ATOM   6562 O  O     . ILE B 1 454 ? -22.229 11.983  1.852   1.00 29.76 ? 433 ILE B O     1 
ATOM   6563 C  CB    . ILE B 1 454 ? -21.655 14.757  0.010   1.00 31.24 ? 433 ILE B CB    1 
ATOM   6564 C  CG1   . ILE B 1 454 ? -20.532 15.414  -0.789  1.00 34.41 ? 433 ILE B CG1   1 
ATOM   6565 C  CG2   . ILE B 1 454 ? -21.618 15.176  1.465   1.00 33.54 ? 433 ILE B CG2   1 
ATOM   6566 C  CD1   . ILE B 1 454 ? -20.897 16.768  -1.315  1.00 39.07 ? 433 ILE B CD1   1 
ATOM   6567 N  N     . ASP B 1 455 ? -23.920 12.537  0.411   1.00 34.21 ? 434 ASP B N     1 
ATOM   6568 C  CA    . ASP B 1 455 ? -25.104 11.940  1.083   1.00 33.38 ? 434 ASP B CA    1 
ATOM   6569 C  C     . ASP B 1 455 ? -24.916 10.438  1.342   1.00 34.19 ? 434 ASP B C     1 
ATOM   6570 O  O     . ASP B 1 455 ? -25.281 9.980   2.441   1.00 33.74 ? 434 ASP B O     1 
ATOM   6571 C  CB    . ASP B 1 455 ? -26.333 12.169  0.202   1.00 37.64 ? 434 ASP B CB    1 
ATOM   6572 C  CG    . ASP B 1 455 ? -27.642 11.929  0.923   1.00 37.68 ? 434 ASP B CG    1 
ATOM   6573 O  OD1   . ASP B 1 455 ? -28.318 10.974  0.549   1.00 38.82 ? 434 ASP B OD1   1 
ATOM   6574 O  OD2   . ASP B 1 455 ? -27.984 12.732  1.832   1.00 40.75 ? 434 ASP B OD2   1 
ATOM   6575 N  N     . GLY B 1 456 ? -24.420 9.689   0.344   1.00 36.85 ? 435 GLY B N     1 
ATOM   6576 C  CA    . GLY B 1 456 ? -23.956 8.283   0.458   1.00 31.17 ? 435 GLY B CA    1 
ATOM   6577 C  C     . GLY B 1 456 ? -22.683 8.100   1.302   1.00 26.23 ? 435 GLY B C     1 
ATOM   6578 O  O     . GLY B 1 456 ? -22.494 7.024   1.879   1.00 21.99 ? 435 GLY B O     1 
ATOM   6579 N  N     . ALA B 1 457 ? -21.788 9.068   1.394   1.00 25.82 ? 436 ALA B N     1 
ATOM   6580 C  CA    . ALA B 1 457 ? -20.662 8.933   2.349   1.00 26.93 ? 436 ALA B CA    1 
ATOM   6581 C  C     . ALA B 1 457 ? -21.262 8.936   3.747   1.00 28.73 ? 436 ALA B C     1 
ATOM   6582 O  O     . ALA B 1 457 ? -20.870 8.064   4.595   1.00 28.18 ? 436 ALA B O     1 
ATOM   6583 C  CB    . ALA B 1 457 ? -19.668 10.054  2.215   1.00 28.60 ? 436 ALA B CB    1 
ATOM   6584 N  N     . ILE B 1 458 ? -22.162 9.900   3.982   1.00 29.29 ? 437 ILE B N     1 
ATOM   6585 C  CA    . ILE B 1 458 ? -22.815 10.085  5.315   1.00 29.94 ? 437 ILE B CA    1 
ATOM   6586 C  C     . ILE B 1 458 ? -23.447 8.740   5.726   1.00 27.93 ? 437 ILE B C     1 
ATOM   6587 O  O     . ILE B 1 458 ? -23.052 8.229   6.783   1.00 28.63 ? 437 ILE B O     1 
ATOM   6588 C  CB    . ILE B 1 458 ? -23.775 11.295  5.303   1.00 29.47 ? 437 ILE B CB    1 
ATOM   6589 C  CG1   . ILE B 1 458 ? -22.987 12.592  5.080   1.00 28.19 ? 437 ILE B CG1   1 
ATOM   6590 C  CG2   . ILE B 1 458 ? -24.600 11.366  6.591   1.00 28.80 ? 437 ILE B CG2   1 
ATOM   6591 C  CD1   . ILE B 1 458 ? -23.793 13.872  5.235   1.00 28.44 ? 437 ILE B CD1   1 
ATOM   6592 N  N     . GLU B 1 459 ? -24.268 8.142   4.862   1.00 28.27 ? 438 GLU B N     1 
ATOM   6593 C  CA    . GLU B 1 459 ? -24.980 6.842   5.070   1.00 32.11 ? 438 GLU B CA    1 
ATOM   6594 C  C     . GLU B 1 459 ? -23.957 5.785   5.486   1.00 30.22 ? 438 GLU B C     1 
ATOM   6595 O  O     . GLU B 1 459 ? -24.216 5.055   6.451   1.00 30.95 ? 438 GLU B O     1 
ATOM   6596 C  CB    . GLU B 1 459 ? -25.736 6.394   3.796   1.00 32.70 ? 438 GLU B CB    1 
ATOM   6597 C  CG    . GLU B 1 459 ? -26.480 5.062   3.907   1.00 32.52 ? 438 GLU B CG    1 
ATOM   6598 C  CD    . GLU B 1 459 ? -26.636 4.210   2.638   1.00 36.43 ? 438 GLU B CD    1 
ATOM   6599 O  OE1   . GLU B 1 459 ? -26.287 3.001   2.696   1.00 35.88 ? 438 GLU B OE1   1 
ATOM   6600 O  OE2   . GLU B 1 459 ? -27.143 4.719   1.588   1.00 33.14 ? 438 GLU B OE2   1 
ATOM   6601 N  N     . SER B 1 460 ? -22.861 5.676   4.739   1.00 30.98 ? 439 SER B N     1 
ATOM   6602 C  CA    . SER B 1 460 ? -21.815 4.639   4.940   1.00 28.83 ? 439 SER B CA    1 
ATOM   6603 C  C     . SER B 1 460 ? -21.191 4.838   6.326   1.00 28.64 ? 439 SER B C     1 
ATOM   6604 O  O     . SER B 1 460 ? -20.946 3.840   6.988   1.00 25.84 ? 439 SER B O     1 
ATOM   6605 C  CB    . SER B 1 460 ? -20.786 4.677   3.825   1.00 30.13 ? 439 SER B CB    1 
ATOM   6606 O  OG    . SER B 1 460 ? -19.922 5.812   3.922   1.00 29.46 ? 439 SER B OG    1 
ATOM   6607 N  N     . GLY B 1 461 ? -20.987 6.095   6.747   1.00 29.67 ? 440 GLY B N     1 
ATOM   6608 C  CA    . GLY B 1 461 ? -20.452 6.436   8.077   1.00 33.05 ? 440 GLY B CA    1 
ATOM   6609 C  C     . GLY B 1 461 ? -21.380 5.967   9.195   1.00 31.87 ? 440 GLY B C     1 
ATOM   6610 O  O     . GLY B 1 461 ? -20.923 5.245   10.099  1.00 28.76 ? 440 GLY B O     1 
ATOM   6611 N  N     . GLN B 1 462 ? -22.651 6.348   9.148   1.00 35.93 ? 441 GLN B N     1 
ATOM   6612 C  CA    . GLN B 1 462 ? -23.672 5.952   10.165  1.00 38.40 ? 441 GLN B CA    1 
ATOM   6613 C  C     . GLN B 1 462 ? -23.683 4.414   10.268  1.00 38.65 ? 441 GLN B C     1 
ATOM   6614 O  O     . GLN B 1 462 ? -23.548 3.871   11.388  1.00 34.92 ? 441 GLN B O     1 
ATOM   6615 C  CB    . GLN B 1 462 ? -25.058 6.492   9.783   1.00 42.77 ? 441 GLN B CB    1 
ATOM   6616 C  CG    . GLN B 1 462 ? -25.173 8.022   9.750   1.00 51.12 ? 441 GLN B CG    1 
ATOM   6617 C  CD    . GLN B 1 462 ? -26.589 8.546   9.601   1.00 55.47 ? 441 GLN B CD    1 
ATOM   6618 O  OE1   . GLN B 1 462 ? -27.097 8.728   8.491   1.00 56.88 ? 441 GLN B OE1   1 
ATOM   6619 N  NE2   . GLN B 1 462 ? -27.236 8.831   10.727  1.00 56.22 ? 441 GLN B NE2   1 
ATOM   6620 N  N     . ARG B 1 463 ? -23.814 3.750   9.114   1.00 34.79 ? 442 ARG B N     1 
ATOM   6621 C  CA    . ARG B 1 463 ? -23.824 2.274   8.964   1.00 35.12 ? 442 ARG B CA    1 
ATOM   6622 C  C     . ARG B 1 463 ? -22.540 1.687   9.575   1.00 31.10 ? 442 ARG B C     1 
ATOM   6623 O  O     . ARG B 1 463 ? -22.665 0.850   10.471  1.00 29.95 ? 442 ARG B O     1 
ATOM   6624 C  CB    . ARG B 1 463 ? -24.038 1.915   7.487   1.00 34.62 ? 442 ARG B CB    1 
ATOM   6625 C  CG    . ARG B 1 463 ? -24.434 0.467   7.219   1.00 36.19 ? 442 ARG B CG    1 
ATOM   6626 C  CD    . ARG B 1 463 ? -23.265 -0.420  6.874   1.00 37.21 ? 442 ARG B CD    1 
ATOM   6627 N  NE    . ARG B 1 463 ? -22.487 0.068   5.729   1.00 38.93 ? 442 ARG B NE    1 
ATOM   6628 C  CZ    . ARG B 1 463 ? -21.175 -0.083  5.587   1.00 36.29 ? 442 ARG B CZ    1 
ATOM   6629 N  NH1   . ARG B 1 463 ? -20.477 -0.744  6.498   1.00 36.36 ? 442 ARG B NH1   1 
ATOM   6630 N  NH2   . ARG B 1 463 ? -20.568 0.433   4.537   1.00 37.48 ? 442 ARG B NH2   1 
ATOM   6631 N  N     . ALA B 1 464 ? -21.351 2.090   9.131   1.00 29.83 ? 443 ALA B N     1 
ATOM   6632 C  CA    . ALA B 1 464 ? -20.075 1.542   9.666   1.00 30.92 ? 443 ALA B CA    1 
ATOM   6633 C  C     . ALA B 1 464 ? -20.051 1.661   11.192  1.00 27.93 ? 443 ALA B C     1 
ATOM   6634 O  O     . ALA B 1 464 ? -19.651 0.712   11.804  1.00 30.61 ? 443 ALA B O     1 
ATOM   6635 C  CB    . ALA B 1 464 ? -18.879 2.236   9.079   1.00 31.07 ? 443 ALA B CB    1 
ATOM   6636 N  N     . ALA B 1 465 ? -20.492 2.797   11.757  1.00 30.73 ? 444 ALA B N     1 
ATOM   6637 C  CA    . ALA B 1 465 ? -20.528 3.110   13.215  1.00 27.07 ? 444 ALA B CA    1 
ATOM   6638 C  C     . ALA B 1 465 ? -21.377 2.079   13.987  1.00 25.95 ? 444 ALA B C     1 
ATOM   6639 O  O     . ALA B 1 465 ? -20.857 1.430   14.928  1.00 23.73 ? 444 ALA B O     1 
ATOM   6640 C  CB    . ALA B 1 465 ? -21.042 4.508   13.407  1.00 25.73 ? 444 ALA B CB    1 
ATOM   6641 N  N     . ALA B 1 466 ? -22.646 1.928   13.607  1.00 25.19 ? 445 ALA B N     1 
ATOM   6642 C  CA    . ALA B 1 466 ? -23.586 0.941   14.185  1.00 26.19 ? 445 ALA B CA    1 
ATOM   6643 C  C     . ALA B 1 466 ? -22.932 -0.454  14.268  1.00 28.68 ? 445 ALA B C     1 
ATOM   6644 O  O     . ALA B 1 466 ? -22.842 -1.012  15.405  1.00 27.25 ? 445 ALA B O     1 
ATOM   6645 C  CB    . ALA B 1 466 ? -24.863 0.932   13.368  1.00 27.78 ? 445 ALA B CB    1 
ATOM   6646 N  N     . GLU B 1 467 ? -22.499 -1.004  13.121  1.00 29.80 ? 446 GLU B N     1 
ATOM   6647 C  CA    . GLU B 1 467 ? -21.748 -2.297  13.025  1.00 32.69 ? 446 GLU B CA    1 
ATOM   6648 C  C     . GLU B 1 467 ? -20.681 -2.420  14.120  1.00 30.98 ? 446 GLU B C     1 
ATOM   6649 O  O     . GLU B 1 467 ? -20.588 -3.496  14.763  1.00 32.49 ? 446 GLU B O     1 
ATOM   6650 C  CB    . GLU B 1 467 ? -20.982 -2.447  11.706  1.00 32.80 ? 446 GLU B CB    1 
ATOM   6651 C  CG    . GLU B 1 467 ? -21.792 -2.973  10.532  1.00 30.88 ? 446 GLU B CG    1 
ATOM   6652 C  CD    . GLU B 1 467 ? -20.958 -2.956  9.259   1.00 30.90 ? 446 GLU B CD    1 
ATOM   6653 O  OE1   . GLU B 1 467 ? -21.566 -2.758  8.195   1.00 34.35 ? 446 GLU B OE1   1 
ATOM   6654 O  OE2   . GLU B 1 467 ? -19.705 -3.094  9.336   1.00 23.97 ? 446 GLU B OE2   1 
ATOM   6655 N  N     . VAL B 1 468 ? -19.854 -1.392  14.277  1.00 32.18 ? 447 VAL B N     1 
ATOM   6656 C  CA    . VAL B 1 468 ? -18.659 -1.463  15.160  1.00 33.60 ? 447 VAL B CA    1 
ATOM   6657 C  C     . VAL B 1 468 ? -19.117 -1.358  16.608  1.00 35.77 ? 447 VAL B C     1 
ATOM   6658 O  O     . VAL B 1 468 ? -18.418 -1.963  17.470  1.00 36.33 ? 447 VAL B O     1 
ATOM   6659 C  CB    . VAL B 1 468 ? -17.619 -0.396  14.792  1.00 36.68 ? 447 VAL B CB    1 
ATOM   6660 C  CG1   . VAL B 1 468 ? -16.423 -0.396  15.729  1.00 38.67 ? 447 VAL B CG1   1 
ATOM   6661 C  CG2   . VAL B 1 468 ? -17.155 -0.625  13.369  1.00 38.45 ? 447 VAL B CG2   1 
ATOM   6662 N  N     . LEU B 1 469 ? -20.230 -0.648  16.870  1.00 36.41 ? 448 LEU B N     1 
ATOM   6663 C  CA    . LEU B 1 469 ? -20.751 -0.438  18.260  1.00 35.35 ? 448 LEU B CA    1 
ATOM   6664 C  C     . LEU B 1 469 ? -21.406 -1.734  18.757  1.00 34.67 ? 448 LEU B C     1 
ATOM   6665 O  O     . LEU B 1 469 ? -21.079 -2.163  19.893  1.00 35.02 ? 448 LEU B O     1 
ATOM   6666 C  CB    . LEU B 1 469 ? -21.743 0.732   18.283  1.00 34.03 ? 448 LEU B CB    1 
ATOM   6667 C  CG    . LEU B 1 469 ? -21.116 2.122   18.220  1.00 31.00 ? 448 LEU B CG    1 
ATOM   6668 C  CD1   . LEU B 1 469 ? -22.190 3.193   18.000  1.00 31.10 ? 448 LEU B CD1   1 
ATOM   6669 C  CD2   . LEU B 1 469 ? -20.276 2.404   19.459  1.00 29.27 ? 448 LEU B CD2   1 
ATOM   6670 N  N     . ALA B 1 470 ? -22.252 -2.329  17.900  1.00 33.36 ? 449 ALA B N     1 
ATOM   6671 C  CA    . ALA B 1 470 ? -22.904 -3.651  18.059  1.00 34.35 ? 449 ALA B CA    1 
ATOM   6672 C  C     . ALA B 1 470 ? -21.844 -4.742  18.310  1.00 34.67 ? 449 ALA B C     1 
ATOM   6673 O  O     . ALA B 1 470 ? -22.073 -5.561  19.194  1.00 36.41 ? 449 ALA B O     1 
ATOM   6674 C  CB    . ALA B 1 470 ? -23.750 -3.952  16.837  1.00 32.10 ? 449 ALA B CB    1 
ATOM   6675 N  N     . ALA B 1 471 ? -20.725 -4.723  17.566  1.00 35.16 ? 450 ALA B N     1 
ATOM   6676 C  CA    . ALA B 1 471 ? -19.574 -5.654  17.664  1.00 32.35 ? 450 ALA B CA    1 
ATOM   6677 C  C     . ALA B 1 471 ? -18.699 -5.362  18.893  1.00 34.06 ? 450 ALA B C     1 
ATOM   6678 O  O     . ALA B 1 471 ? -18.191 -6.330  19.474  1.00 34.48 ? 450 ALA B O     1 
ATOM   6679 C  CB    . ALA B 1 471 ? -18.760 -5.574  16.398  1.00 31.67 ? 450 ALA B CB    1 
ATOM   6680 N  N     . LEU B 1 472 ? -18.482 -4.095  19.274  1.00 37.43 ? 451 LEU B N     1 
ATOM   6681 C  CA    . LEU B 1 472 ? -17.875 -3.759  20.598  1.00 41.78 ? 451 LEU B CA    1 
ATOM   6682 C  C     . LEU B 1 472 ? -18.771 -4.332  21.711  1.00 43.64 ? 451 LEU B C     1 
ATOM   6683 O  O     . LEU B 1 472 ? -18.221 -4.998  22.577  1.00 41.39 ? 451 LEU B O     1 
ATOM   6684 C  CB    . LEU B 1 472 ? -17.704 -2.241  20.775  1.00 45.40 ? 451 LEU B CB    1 
ATOM   6685 C  CG    . LEU B 1 472 ? -16.546 -1.586  20.017  1.00 45.88 ? 451 LEU B CG    1 
ATOM   6686 C  CD1   . LEU B 1 472 ? -16.709 -0.078  19.990  1.00 45.91 ? 451 LEU B CD1   1 
ATOM   6687 C  CD2   . LEU B 1 472 ? -15.198 -1.961  20.611  1.00 43.15 ? 451 LEU B CD2   1 
ATOM   6688 N  N     . GLY B 1 473 ? -20.093 -4.095  21.655  1.00 45.39 ? 452 GLY B N     1 
ATOM   6689 C  CA    . GLY B 1 473 ? -21.060 -4.353  22.749  1.00 50.12 ? 452 GLY B CA    1 
ATOM   6690 C  C     . GLY B 1 473 ? -22.451 -4.704  22.225  1.00 55.69 ? 452 GLY B C     1 
ATOM   6691 O  O     . GLY B 1 473 ? -23.511 -4.350  22.776  1.00 52.33 ? 452 GLY B O     1 
HETATM 6692 P  PA    . FAD C 2 .   ? 6.935   -12.254 -10.401 1.00 17.29 ? 501 FAD A PA    1 
HETATM 6693 O  O1A   . FAD C 2 .   ? 5.684   -11.823 -9.699  1.00 19.60 ? 501 FAD A O1A   1 
HETATM 6694 O  O2A   . FAD C 2 .   ? 7.253   -13.706 -10.598 1.00 16.61 ? 501 FAD A O2A   1 
HETATM 6695 O  O5B   . FAD C 2 .   ? 8.063   -11.525 -9.520  1.00 17.52 ? 501 FAD A O5B   1 
HETATM 6696 C  C5B   . FAD C 2 .   ? 7.796   -10.445 -8.625  1.00 16.46 ? 501 FAD A C5B   1 
HETATM 6697 C  C4B   . FAD C 2 .   ? 8.716   -10.514 -7.403  1.00 17.22 ? 501 FAD A C4B   1 
HETATM 6698 O  O4B   . FAD C 2 .   ? 8.355   -9.281  -6.749  1.00 18.54 ? 501 FAD A O4B   1 
HETATM 6699 C  C3B   . FAD C 2 .   ? 8.342   -11.673 -6.452  1.00 16.87 ? 501 FAD A C3B   1 
HETATM 6700 O  O3B   . FAD C 2 .   ? 9.471   -12.491 -6.083  1.00 17.99 ? 501 FAD A O3B   1 
HETATM 6701 C  C2B   . FAD C 2 .   ? 7.663   -10.964 -5.272  1.00 17.95 ? 501 FAD A C2B   1 
HETATM 6702 O  O2B   . FAD C 2 .   ? 7.783   -11.573 -3.979  1.00 15.69 ? 501 FAD A O2B   1 
HETATM 6703 C  C1B   . FAD C 2 .   ? 8.277   -9.559  -5.338  1.00 17.69 ? 501 FAD A C1B   1 
HETATM 6704 N  N9A   . FAD C 2 .   ? 7.607   -8.381  -4.732  1.00 16.72 ? 501 FAD A N9A   1 
HETATM 6705 C  C8A   . FAD C 2 .   ? 6.331   -7.974  -4.797  1.00 18.51 ? 501 FAD A C8A   1 
HETATM 6706 N  N7A   . FAD C 2 .   ? 6.144   -6.805  -4.140  1.00 16.71 ? 501 FAD A N7A   1 
HETATM 6707 C  C5A   . FAD C 2 .   ? 7.375   -6.475  -3.660  1.00 17.57 ? 501 FAD A C5A   1 
HETATM 6708 C  C6A   . FAD C 2 .   ? 7.864   -5.400  -2.917  1.00 17.85 ? 501 FAD A C6A   1 
HETATM 6709 N  N6A   . FAD C 2 .   ? 7.054   -4.387  -2.497  1.00 17.36 ? 501 FAD A N6A   1 
HETATM 6710 N  N1A   . FAD C 2 .   ? 9.177   -5.388  -2.608  1.00 17.05 ? 501 FAD A N1A   1 
HETATM 6711 C  C2A   . FAD C 2 .   ? 10.001  -6.368  -2.992  1.00 17.30 ? 501 FAD A C2A   1 
HETATM 6712 N  N3A   . FAD C 2 .   ? 9.587   -7.399  -3.702  1.00 16.94 ? 501 FAD A N3A   1 
HETATM 6713 C  C4A   . FAD C 2 .   ? 8.277   -7.455  -4.049  1.00 17.21 ? 501 FAD A C4A   1 
HETATM 6714 N  N1    . FAD C 2 .   ? 4.194   -18.931 -17.096 1.00 17.39 ? 501 FAD A N1    1 
HETATM 6715 C  C2    . FAD C 2 .   ? 4.878   -19.803 -17.879 1.00 18.09 ? 501 FAD A C2    1 
HETATM 6716 O  O2    . FAD C 2 .   ? 5.799   -19.427 -18.633 1.00 15.99 ? 501 FAD A O2    1 
HETATM 6717 N  N3    . FAD C 2 .   ? 4.545   -21.118 -17.849 1.00 18.43 ? 501 FAD A N3    1 
HETATM 6718 C  C4    . FAD C 2 .   ? 3.580   -21.568 -17.052 1.00 17.67 ? 501 FAD A C4    1 
HETATM 6719 O  O4    . FAD C 2 .   ? 3.311   -22.779 -17.123 1.00 18.85 ? 501 FAD A O4    1 
HETATM 6720 C  C4X   . FAD C 2 .   ? 2.834   -20.681 -16.269 1.00 18.90 ? 501 FAD A C4X   1 
HETATM 6721 N  N5    . FAD C 2 .   ? 1.820   -21.105 -15.450 1.00 19.83 ? 501 FAD A N5    1 
HETATM 6722 C  C5X   . FAD C 2 .   ? 1.383   -20.320 -14.438 1.00 19.66 ? 501 FAD A C5X   1 
HETATM 6723 C  C6    . FAD C 2 .   ? 0.585   -20.866 -13.431 1.00 18.68 ? 501 FAD A C6    1 
HETATM 6724 C  C7    . FAD C 2 .   ? 0.375   -20.163 -12.237 1.00 19.73 ? 501 FAD A C7    1 
HETATM 6725 C  C7M   . FAD C 2 .   ? -0.517  -20.791 -11.165 1.00 18.80 ? 501 FAD A C7M   1 
HETATM 6726 C  C8    . FAD C 2 .   ? 0.990   -18.908 -12.059 1.00 19.61 ? 501 FAD A C8    1 
HETATM 6727 C  C8M   . FAD C 2 .   ? 0.826   -18.084 -10.781 1.00 20.49 ? 501 FAD A C8M   1 
HETATM 6728 C  C9    . FAD C 2 .   ? 1.792   -18.370 -13.065 1.00 19.31 ? 501 FAD A C9    1 
HETATM 6729 C  C9A   . FAD C 2 .   ? 1.992   -19.062 -14.279 1.00 20.25 ? 501 FAD A C9A   1 
HETATM 6730 N  N10   . FAD C 2 .   ? 2.544   -18.487 -15.405 1.00 19.91 ? 501 FAD A N10   1 
HETATM 6731 C  C10   . FAD C 2 .   ? 3.176   -19.342 -16.279 1.00 18.55 ? 501 FAD A C10   1 
HETATM 6732 C  "C1'" . FAD C 2 .   ? 3.042   -17.074 -15.340 1.00 18.64 ? 501 FAD A "C1'" 1 
HETATM 6733 C  "C2'" . FAD C 2 .   ? 4.523   -16.953 -14.978 1.00 19.02 ? 501 FAD A "C2'" 1 
HETATM 6734 O  "O2'" . FAD C 2 .   ? 4.752   -17.693 -13.744 1.00 19.98 ? 501 FAD A "O2'" 1 
HETATM 6735 C  "C3'" . FAD C 2 .   ? 4.920   -15.495 -14.783 1.00 18.16 ? 501 FAD A "C3'" 1 
HETATM 6736 O  "O3'" . FAD C 2 .   ? 4.571   -14.753 -15.939 1.00 17.92 ? 501 FAD A "O3'" 1 
HETATM 6737 C  "C4'" . FAD C 2 .   ? 6.376   -15.191 -14.448 1.00 17.15 ? 501 FAD A "C4'" 1 
HETATM 6738 O  "O4'" . FAD C 2 .   ? 6.778   -15.933 -13.319 1.00 15.84 ? 501 FAD A "O4'" 1 
HETATM 6739 C  "C5'" . FAD C 2 .   ? 6.463   -13.680 -14.104 1.00 18.10 ? 501 FAD A "C5'" 1 
HETATM 6740 O  "O5'" . FAD C 2 .   ? 7.729   -13.292 -13.566 1.00 16.76 ? 501 FAD A "O5'" 1 
HETATM 6741 P  P     . FAD C 2 .   ? 7.915   -11.778 -13.133 1.00 18.09 ? 501 FAD A P     1 
HETATM 6742 O  O1P   . FAD C 2 .   ? 9.359   -11.695 -12.629 1.00 16.25 ? 501 FAD A O1P   1 
HETATM 6743 O  O2P   . FAD C 2 .   ? 7.406   -10.792 -14.169 1.00 14.71 ? 501 FAD A O2P   1 
HETATM 6744 O  O3P   . FAD C 2 .   ? 6.924   -11.494 -11.859 1.00 17.89 ? 501 FAD A O3P   1 
HETATM 6745 MG MG    . MG  D 3 .   ? -2.971  -35.131 -25.565 1.00 52.99 ? 502 MG  A MG    1 
HETATM 6746 N  N2    . PUT E 4 .   ? -1.690  -21.919 -17.997 1.00 32.32 ? 503 PUT A N2    1 
HETATM 6747 C  C4    . PUT E 4 .   ? -0.467  -21.174 -17.692 1.00 32.49 ? 503 PUT A C4    1 
HETATM 6748 C  C3    . PUT E 4 .   ? -0.212  -20.044 -18.671 1.00 30.27 ? 503 PUT A C3    1 
HETATM 6749 C  C2    . PUT E 4 .   ? 0.524   -18.846 -18.082 1.00 30.30 ? 503 PUT A C2    1 
HETATM 6750 C  C1    . PUT E 4 .   ? 0.089   -17.489 -18.616 1.00 29.11 ? 503 PUT A C1    1 
HETATM 6751 N  N1    . PUT E 4 .   ? -1.087  -17.468 -19.534 1.00 28.22 ? 503 PUT A N1    1 
HETATM 6752 N  N2    . PUT F 4 .   ? -4.061  -24.559 -21.643 1.00 39.18 ? 504 PUT A N2    1 
HETATM 6753 C  C4    . PUT F 4 .   ? -5.455  -24.510 -22.114 1.00 39.59 ? 504 PUT A C4    1 
HETATM 6754 C  C3    . PUT F 4 .   ? -5.986  -25.810 -22.704 1.00 38.44 ? 504 PUT A C3    1 
HETATM 6755 C  C2    . PUT F 4 .   ? -7.223  -25.633 -23.557 1.00 36.05 ? 504 PUT A C2    1 
HETATM 6756 C  C1    . PUT F 4 .   ? -7.561  -26.872 -24.370 1.00 37.76 ? 504 PUT A C1    1 
HETATM 6757 N  N1    . PUT F 4 .   ? -8.908  -26.862 -24.966 1.00 40.52 ? 504 PUT A N1    1 
HETATM 6758 P  PA    . FAD G 2 .   ? -13.265 10.949  0.783   1.00 23.85 ? 600 FAD B PA    1 
HETATM 6759 O  O1A   . FAD G 2 .   ? -12.617 10.377  -0.416  1.00 27.54 ? 600 FAD B O1A   1 
HETATM 6760 O  O2A   . FAD G 2 .   ? -13.952 12.340  0.670   1.00 26.06 ? 600 FAD B O2A   1 
HETATM 6761 O  O5B   . FAD G 2 .   ? -12.127 11.064  1.906   1.00 21.99 ? 600 FAD B O5B   1 
HETATM 6762 C  C5B   . FAD G 2 .   ? -11.348 9.980   2.393   1.00 23.27 ? 600 FAD B C5B   1 
HETATM 6763 C  C4B   . FAD G 2 .   ? -10.208 10.571  3.213   1.00 25.53 ? 600 FAD B C4B   1 
HETATM 6764 O  O4B   . FAD G 2 .   ? -9.207  9.621   3.611   1.00 25.76 ? 600 FAD B O4B   1 
HETATM 6765 C  C3B   . FAD G 2 .   ? -9.460  11.671  2.461   1.00 24.92 ? 600 FAD B C3B   1 
HETATM 6766 O  O3B   . FAD G 2 .   ? -9.460  12.832  3.257   1.00 29.17 ? 600 FAD B O3B   1 
HETATM 6767 C  C2B   . FAD G 2 .   ? -8.069  11.161  2.320   1.00 26.00 ? 600 FAD B C2B   1 
HETATM 6768 O  O2B   . FAD G 2 .   ? -7.061  12.166  2.308   1.00 25.81 ? 600 FAD B O2B   1 
HETATM 6769 C  C1B   . FAD G 2 .   ? -7.928  10.204  3.500   1.00 26.02 ? 600 FAD B C1B   1 
HETATM 6770 N  N9A   . FAD G 2 .   ? -6.960  9.098   3.285   1.00 26.58 ? 600 FAD B N9A   1 
HETATM 6771 C  C8A   . FAD G 2 .   ? -6.759  8.367   2.179   1.00 26.17 ? 600 FAD B C8A   1 
HETATM 6772 N  N7A   . FAD G 2 .   ? -5.808  7.452   2.377   1.00 26.21 ? 600 FAD B N7A   1 
HETATM 6773 C  C5A   . FAD G 2 .   ? -5.424  7.612   3.641   1.00 27.91 ? 600 FAD B C5A   1 
HETATM 6774 C  C6A   . FAD G 2 .   ? -4.527  6.966   4.430   1.00 26.94 ? 600 FAD B C6A   1 
HETATM 6775 N  N6A   . FAD G 2 .   ? -3.788  5.945   3.947   1.00 25.40 ? 600 FAD B N6A   1 
HETATM 6776 N  N1A   . FAD G 2 .   ? -4.360  7.414   5.693   1.00 27.09 ? 600 FAD B N1A   1 
HETATM 6777 C  C2A   . FAD G 2 .   ? -5.079  8.404   6.210   1.00 28.09 ? 600 FAD B C2A   1 
HETATM 6778 N  N3A   . FAD G 2 .   ? -6.002  9.017   5.488   1.00 28.19 ? 600 FAD B N3A   1 
HETATM 6779 C  C4A   . FAD G 2 .   ? -6.156  8.648   4.204   1.00 28.16 ? 600 FAD B C4A   1 
HETATM 6780 N  N1    . FAD G 2 .   ? -20.474 14.615  -4.648  1.00 29.73 ? 600 FAD B N1    1 
HETATM 6781 C  C2    . FAD G 2 .   ? -21.611 15.287  -4.337  1.00 31.66 ? 600 FAD B C2    1 
HETATM 6782 O  O2    . FAD G 2 .   ? -22.374 14.823  -3.450  1.00 27.27 ? 600 FAD B O2    1 
HETATM 6783 N  N3    . FAD G 2 .   ? -21.909 16.449  -5.018  1.00 32.65 ? 600 FAD B N3    1 
HETATM 6784 C  C4    . FAD G 2 .   ? -21.128 16.918  -6.020  1.00 30.23 ? 600 FAD B C4    1 
HETATM 6785 O  O4    . FAD G 2 .   ? -21.542 17.960  -6.564  1.00 30.50 ? 600 FAD B O4    1 
HETATM 6786 C  C4X   . FAD G 2 .   ? -19.934 16.232  -6.366  1.00 29.88 ? 600 FAD B C4X   1 
HETATM 6787 N  N5    . FAD G 2 .   ? -19.051 16.600  -7.325  1.00 25.84 ? 600 FAD B N5    1 
HETATM 6788 C  C5X   . FAD G 2 .   ? -17.766 16.088  -7.196  1.00 27.61 ? 600 FAD B C5X   1 
HETATM 6789 C  C6    . FAD G 2 .   ? -16.677 16.668  -7.877  1.00 27.59 ? 600 FAD B C6    1 
HETATM 6790 C  C7    . FAD G 2 .   ? -15.359 16.308  -7.616  1.00 28.84 ? 600 FAD B C7    1 
HETATM 6791 C  C7M   . FAD G 2 .   ? -14.277 16.966  -8.451  1.00 30.39 ? 600 FAD B C7M   1 
HETATM 6792 C  C8    . FAD G 2 .   ? -15.060 15.366  -6.621  1.00 26.70 ? 600 FAD B C8    1 
HETATM 6793 C  C8M   . FAD G 2 .   ? -13.632 14.917  -6.297  1.00 27.54 ? 600 FAD B C8M   1 
HETATM 6794 C  C9    . FAD G 2 .   ? -16.121 14.799  -5.962  1.00 23.39 ? 600 FAD B C9    1 
HETATM 6795 C  C9A   . FAD G 2 .   ? -17.462 15.147  -6.226  1.00 24.15 ? 600 FAD B C9A   1 
HETATM 6796 N  N10   . FAD G 2 .   ? -18.513 14.374  -5.857  1.00 25.88 ? 600 FAD B N10   1 
HETATM 6797 C  C10   . FAD G 2 .   ? -19.636 15.056  -5.634  1.00 28.60 ? 600 FAD B C10   1 
HETATM 6798 C  "C1'" . FAD G 2 .   ? -18.320 13.161  -5.004  1.00 25.36 ? 600 FAD B "C1'" 1 
HETATM 6799 C  "C2'" . FAD G 2 .   ? -18.009 13.416  -3.506  1.00 25.41 ? 600 FAD B "C2'" 1 
HETATM 6800 O  "O2'" . FAD G 2 .   ? -16.921 14.367  -3.239  1.00 21.86 ? 600 FAD B "O2'" 1 
HETATM 6801 C  "C3'" . FAD G 2 .   ? -17.737 12.057  -2.814  1.00 26.44 ? 600 FAD B "C3'" 1 
HETATM 6802 O  "O3'" . FAD G 2 .   ? -18.815 11.120  -3.045  1.00 29.04 ? 600 FAD B "O3'" 1 
HETATM 6803 C  "C4'" . FAD G 2 .   ? -17.509 12.164  -1.313  1.00 25.23 ? 600 FAD B "C4'" 1 
HETATM 6804 O  "O4'" . FAD G 2 .   ? -16.539 13.165  -1.034  1.00 26.04 ? 600 FAD B "O4'" 1 
HETATM 6805 C  "C5'" . FAD G 2 .   ? -17.073 10.837  -0.741  1.00 25.55 ? 600 FAD B "C5'" 1 
HETATM 6806 O  "O5'" . FAD G 2 .   ? -16.098 10.989  0.289   1.00 25.37 ? 600 FAD B "O5'" 1 
HETATM 6807 P  P     . FAD G 2 .   ? -15.827 9.891   1.435   1.00 24.71 ? 600 FAD B P     1 
HETATM 6808 O  O1P   . FAD G 2 .   ? -16.277 10.488  2.784   1.00 25.29 ? 600 FAD B O1P   1 
HETATM 6809 O  O2P   . FAD G 2 .   ? -16.336 8.511   1.051   1.00 21.78 ? 600 FAD B O2P   1 
HETATM 6810 O  O3P   . FAD G 2 .   ? -14.217 9.901   1.535   1.00 25.57 ? 600 FAD B O3P   1 
HETATM 6811 N  N2    . PUT H 4 .   ? -27.794 16.524  -19.117 1.00 34.71 ? 601 PUT B N2    1 
HETATM 6812 C  C4    . PUT H 4 .   ? -26.710 17.200  -18.397 1.00 38.69 ? 601 PUT B C4    1 
HETATM 6813 C  C3    . PUT H 4 .   ? -25.956 16.319  -17.406 1.00 39.20 ? 601 PUT B C3    1 
HETATM 6814 C  C2    . PUT H 4 .   ? -25.326 17.108  -16.268 1.00 37.76 ? 601 PUT B C2    1 
HETATM 6815 C  C1    . PUT H 4 .   ? -25.124 16.274  -15.017 1.00 38.64 ? 601 PUT B C1    1 
HETATM 6816 N  N1    . PUT H 4 .   ? -24.006 16.703  -14.172 1.00 36.08 ? 601 PUT B N1    1 
HETATM 6817 O  O     . HOH I 5 .   ? -1.290  -20.942 -22.245 1.00 22.42 ? 601 HOH A O     1 
HETATM 6818 O  O     . HOH I 5 .   ? 4.400   -22.399 -21.381 1.00 8.71  ? 602 HOH A O     1 
HETATM 6819 O  O     . HOH I 5 .   ? -4.091  -37.227 -26.359 1.00 40.93 ? 603 HOH A O     1 
HETATM 6820 O  O     . HOH I 5 .   ? -18.992 -29.920 -17.878 1.00 23.96 ? 604 HOH A O     1 
HETATM 6821 O  O     . HOH I 5 .   ? 8.887   -14.926 -12.029 1.00 18.18 ? 605 HOH A O     1 
HETATM 6822 O  O     . HOH I 5 .   ? -11.510 6.319   -15.351 1.00 29.54 ? 606 HOH A O     1 
HETATM 6823 O  O     . HOH I 5 .   ? 30.250  -10.211 -2.770  1.00 19.19 ? 607 HOH A O     1 
HETATM 6824 O  O     . HOH I 5 .   ? 1.509   -22.503 -19.831 1.00 24.56 ? 608 HOH A O     1 
HETATM 6825 O  O     . HOH I 5 .   ? 17.824  8.644   -13.234 1.00 40.35 ? 609 HOH A O     1 
HETATM 6826 O  O     . HOH I 5 .   ? 4.740   -12.418 -7.198  1.00 9.02  ? 610 HOH A O     1 
HETATM 6827 O  O     . HOH I 5 .   ? 6.552   -34.005 -10.013 1.00 14.86 ? 611 HOH A O     1 
HETATM 6828 O  O     . HOH I 5 .   ? 3.287   -5.549  -23.394 1.00 33.64 ? 612 HOH A O     1 
HETATM 6829 O  O     . HOH I 5 .   ? -9.718  -2.334  -12.498 1.00 18.78 ? 613 HOH A O     1 
HETATM 6830 O  O     . HOH I 5 .   ? -7.938  -8.870  -9.579  1.00 17.07 ? 614 HOH A O     1 
HETATM 6831 O  O     . HOH I 5 .   ? 5.117   -6.993  -14.095 1.00 17.10 ? 615 HOH A O     1 
HETATM 6832 O  O     . HOH I 5 .   ? 9.820   -13.232 -25.064 1.00 19.58 ? 616 HOH A O     1 
HETATM 6833 O  O     . HOH I 5 .   ? 4.868   5.233   -16.968 1.00 20.29 ? 617 HOH A O     1 
HETATM 6834 O  O     . HOH I 5 .   ? -2.415  -27.880 -23.479 1.00 22.12 ? 618 HOH A O     1 
HETATM 6835 O  O     . HOH I 5 .   ? 5.301   -18.384 -30.304 1.00 24.19 ? 619 HOH A O     1 
HETATM 6836 O  O     . HOH I 5 .   ? 17.712  -16.234 -22.027 1.00 38.01 ? 620 HOH A O     1 
HETATM 6837 O  O     . HOH I 5 .   ? -5.106  -16.236 -8.439  1.00 21.40 ? 621 HOH A O     1 
HETATM 6838 O  O     . HOH I 5 .   ? -3.812  -36.151 -23.987 1.00 31.77 ? 622 HOH A O     1 
HETATM 6839 O  O     . HOH I 5 .   ? -12.695 -49.621 -15.632 1.00 36.33 ? 623 HOH A O     1 
HETATM 6840 O  O     . HOH I 5 .   ? -21.592 -35.724 -13.948 1.00 26.03 ? 624 HOH A O     1 
HETATM 6841 O  O     . HOH I 5 .   ? 9.908   -14.896 -4.978  1.00 15.40 ? 625 HOH A O     1 
HETATM 6842 O  O     . HOH I 5 .   ? 6.489   -3.533  -11.965 1.00 21.31 ? 626 HOH A O     1 
HETATM 6843 O  O     . HOH I 5 .   ? -0.428  -32.298 1.958   1.00 21.44 ? 627 HOH A O     1 
HETATM 6844 O  O     . HOH I 5 .   ? 2.892   -14.010 -0.828  1.00 15.56 ? 628 HOH A O     1 
HETATM 6845 O  O     . HOH I 5 .   ? -8.494  -0.640  -9.041  1.00 22.91 ? 629 HOH A O     1 
HETATM 6846 O  O     . HOH I 5 .   ? 9.017   6.602   -7.081  1.00 18.56 ? 630 HOH A O     1 
HETATM 6847 O  O     . HOH I 5 .   ? -9.605  -16.395 -4.465  1.00 20.72 ? 631 HOH A O     1 
HETATM 6848 O  O     . HOH I 5 .   ? -17.543 -42.702 -12.772 1.00 41.56 ? 632 HOH A O     1 
HETATM 6849 O  O     . HOH I 5 .   ? -8.481  -38.712 -19.739 1.00 17.52 ? 633 HOH A O     1 
HETATM 6850 O  O     . HOH I 5 .   ? -3.805  -14.567 -16.177 1.00 16.87 ? 634 HOH A O     1 
HETATM 6851 O  O     . HOH I 5 .   ? 10.788  -9.917  -10.957 1.00 22.86 ? 635 HOH A O     1 
HETATM 6852 O  O     . HOH I 5 .   ? -4.970  -35.033 -26.108 1.00 33.60 ? 636 HOH A O     1 
HETATM 6853 O  O     . HOH I 5 .   ? 9.684   -5.221  -22.101 1.00 20.76 ? 637 HOH A O     1 
HETATM 6854 O  O     . HOH I 5 .   ? 0.753   -30.968 -14.768 1.00 18.49 ? 638 HOH A O     1 
HETATM 6855 O  O     . HOH I 5 .   ? -12.674 -45.874 -11.225 1.00 28.60 ? 639 HOH A O     1 
HETATM 6856 O  O     . HOH I 5 .   ? -15.465 -37.991 -2.357  1.00 13.03 ? 640 HOH A O     1 
HETATM 6857 O  O     . HOH I 5 .   ? 4.248   -3.250  -3.064  1.00 14.01 ? 641 HOH A O     1 
HETATM 6858 O  O     . HOH I 5 .   ? 10.837  1.140   -18.259 1.00 24.81 ? 642 HOH A O     1 
HETATM 6859 O  O     . HOH I 5 .   ? 7.663   -19.354 -20.701 1.00 15.26 ? 643 HOH A O     1 
HETATM 6860 O  O     . HOH I 5 .   ? -6.023  -2.890  -10.522 1.00 27.60 ? 644 HOH A O     1 
HETATM 6861 O  O     . HOH I 5 .   ? 6.045   -22.953 -10.128 1.00 16.60 ? 645 HOH A O     1 
HETATM 6862 O  O     . HOH I 5 .   ? 30.498  -13.028 -4.562  1.00 36.20 ? 646 HOH A O     1 
HETATM 6863 O  O     . HOH I 5 .   ? -1.049  -38.560 -20.468 1.00 27.92 ? 647 HOH A O     1 
HETATM 6864 O  O     . HOH I 5 .   ? 1.068   -24.015 -14.546 1.00 12.58 ? 648 HOH A O     1 
HETATM 6865 O  O     . HOH I 5 .   ? -24.617 -38.112 -22.314 1.00 28.16 ? 649 HOH A O     1 
HETATM 6866 O  O     . HOH I 5 .   ? 14.387  12.069  -11.147 1.00 28.98 ? 650 HOH A O     1 
HETATM 6867 O  O     . HOH I 5 .   ? 0.192   12.539  -9.668  1.00 24.76 ? 651 HOH A O     1 
HETATM 6868 O  O     . HOH I 5 .   ? -3.615  -43.574 -4.049  1.00 20.27 ? 652 HOH A O     1 
HETATM 6869 O  O     . HOH I 5 .   ? 1.435   -14.007 -24.733 1.00 21.08 ? 653 HOH A O     1 
HETATM 6870 O  O     . HOH I 5 .   ? 13.329  9.434   -17.649 1.00 27.64 ? 654 HOH A O     1 
HETATM 6871 O  O     . HOH I 5 .   ? -6.632  -44.824 -6.432  1.00 33.27 ? 655 HOH A O     1 
HETATM 6872 O  O     . HOH I 5 .   ? 24.452  -20.485 -11.963 1.00 39.39 ? 656 HOH A O     1 
HETATM 6873 O  O     . HOH I 5 .   ? 4.613   -4.254  -13.665 1.00 38.32 ? 657 HOH A O     1 
HETATM 6874 O  O     . HOH I 5 .   ? -10.667 -23.240 -17.742 1.00 31.99 ? 658 HOH A O     1 
HETATM 6875 O  O     . HOH I 5 .   ? 6.138   -8.715  -12.406 1.00 24.84 ? 659 HOH A O     1 
HETATM 6876 O  O     . HOH I 5 .   ? -3.307  -20.913 -1.006  1.00 22.95 ? 660 HOH A O     1 
HETATM 6877 O  O     . HOH I 5 .   ? -10.484 -36.929 1.023   1.00 25.39 ? 661 HOH A O     1 
HETATM 6878 O  O     . HOH I 5 .   ? -2.514  -13.659 -18.373 1.00 19.64 ? 662 HOH A O     1 
HETATM 6879 O  O     . HOH I 5 .   ? -16.199 -45.671 -11.907 1.00 27.24 ? 663 HOH A O     1 
HETATM 6880 O  O     . HOH I 5 .   ? -1.320  9.561   -23.515 1.00 24.32 ? 664 HOH A O     1 
HETATM 6881 O  O     . HOH I 5 .   ? 5.370   2.107   5.164   1.00 34.80 ? 665 HOH A O     1 
HETATM 6882 O  O     . HOH I 5 .   ? 10.787  8.909   -19.566 1.00 34.24 ? 666 HOH A O     1 
HETATM 6883 O  O     . HOH I 5 .   ? 18.725  -24.559 -6.726  1.00 30.59 ? 667 HOH A O     1 
HETATM 6884 O  O     . HOH I 5 .   ? 11.024  -38.469 -11.964 1.00 18.96 ? 668 HOH A O     1 
HETATM 6885 O  O     . HOH I 5 .   ? 4.266   -5.668  -33.669 1.00 18.09 ? 669 HOH A O     1 
HETATM 6886 O  O     . HOH I 5 .   ? -3.252  -32.704 -23.824 1.00 35.08 ? 670 HOH A O     1 
HETATM 6887 O  O     . HOH I 5 .   ? -21.965 -32.745 -6.899  1.00 35.86 ? 671 HOH A O     1 
HETATM 6888 O  O     . HOH I 5 .   ? -24.536 -26.061 -29.574 1.00 31.78 ? 672 HOH A O     1 
HETATM 6889 O  O     . HOH I 5 .   ? -0.155  11.704  -16.576 1.00 12.42 ? 673 HOH A O     1 
HETATM 6890 O  O     . HOH I 5 .   ? 7.081   -17.346 0.031   1.00 24.49 ? 674 HOH A O     1 
HETATM 6891 O  O     . HOH I 5 .   ? 22.827  8.632   -13.327 1.00 34.07 ? 675 HOH A O     1 
HETATM 6892 O  O     . HOH I 5 .   ? -13.047 -23.277 -16.700 1.00 22.24 ? 676 HOH A O     1 
HETATM 6893 O  O     . HOH I 5 .   ? 24.102  2.741   -0.564  1.00 32.83 ? 677 HOH A O     1 
HETATM 6894 O  O     . HOH I 5 .   ? -3.791  -45.058 -6.383  1.00 27.76 ? 678 HOH A O     1 
HETATM 6895 O  O     . HOH I 5 .   ? -11.979 -52.140 -15.980 1.00 26.29 ? 679 HOH A O     1 
HETATM 6896 O  O     . HOH I 5 .   ? 23.662  2.923   3.242   1.00 29.05 ? 680 HOH A O     1 
HETATM 6897 O  O     . HOH I 5 .   ? 12.037  -26.195 -24.974 1.00 24.61 ? 681 HOH A O     1 
HETATM 6898 O  O     . HOH I 5 .   ? -17.886 -22.338 -8.907  1.00 23.40 ? 682 HOH A O     1 
HETATM 6899 O  O     . HOH I 5 .   ? 14.291  11.948  -1.368  1.00 42.43 ? 683 HOH A O     1 
HETATM 6900 O  O     . HOH J 5 .   ? -17.285 19.659  -31.259 1.00 27.01 ? 701 HOH B O     1 
HETATM 6901 O  O     . HOH J 5 .   ? -31.640 13.627  -18.814 1.00 28.07 ? 702 HOH B O     1 
HETATM 6902 O  O     . HOH J 5 .   ? -29.890 26.271  -17.420 1.00 23.57 ? 703 HOH B O     1 
HETATM 6903 O  O     . HOH J 5 .   ? -17.521 25.351  -33.386 1.00 34.54 ? 704 HOH B O     1 
HETATM 6904 O  O     . HOH J 5 .   ? -14.183 18.691  21.332  1.00 37.83 ? 705 HOH B O     1 
HETATM 6905 O  O     . HOH J 5 .   ? -14.752 -7.774  3.032   1.00 22.77 ? 706 HOH B O     1 
HETATM 6906 O  O     . HOH J 5 .   ? -16.858 8.840   -10.764 1.00 23.63 ? 707 HOH B O     1 
HETATM 6907 O  O     . HOH J 5 .   ? -4.087  14.073  -2.149  1.00 24.82 ? 708 HOH B O     1 
HETATM 6908 O  O     . HOH J 5 .   ? -3.984  17.176  -8.106  1.00 33.46 ? 709 HOH B O     1 
HETATM 6909 O  O     . HOH J 5 .   ? -9.892  36.257  -1.957  1.00 39.50 ? 710 HOH B O     1 
HETATM 6910 O  O     . HOH J 5 .   ? -37.446 13.516  -4.220  1.00 34.30 ? 711 HOH B O     1 
HETATM 6911 O  O     . HOH J 5 .   ? -34.990 -7.425  -8.304  1.00 20.46 ? 712 HOH B O     1 
HETATM 6912 O  O     . HOH J 5 .   ? 2.426   8.136   8.618   1.00 31.70 ? 713 HOH B O     1 
HETATM 6913 O  O     . HOH J 5 .   ? -17.499 22.838  -39.199 1.00 20.19 ? 714 HOH B O     1 
HETATM 6914 O  O     . HOH J 5 .   ? 0.760   14.505  -7.639  1.00 40.31 ? 715 HOH B O     1 
HETATM 6915 O  O     . HOH J 5 .   ? -31.713 24.945  -8.790  1.00 27.49 ? 716 HOH B O     1 
HETATM 6916 O  O     . HOH J 5 .   ? -35.391 16.375  4.155   1.00 30.79 ? 717 HOH B O     1 
HETATM 6917 O  O     . HOH J 5 .   ? -25.586 16.254  -5.589  1.00 16.54 ? 718 HOH B O     1 
HETATM 6918 O  O     . HOH J 5 .   ? -11.927 2.291   2.764   1.00 23.96 ? 719 HOH B O     1 
HETATM 6919 O  O     . HOH J 5 .   ? -24.087 29.397  -9.272  1.00 35.68 ? 720 HOH B O     1 
HETATM 6920 O  O     . HOH J 5 .   ? -25.516 29.184  -22.094 1.00 30.21 ? 721 HOH B O     1 
HETATM 6921 O  O     . HOH J 5 .   ? -25.880 35.269  -8.995  1.00 36.38 ? 722 HOH B O     1 
HETATM 6922 O  O     . HOH J 5 .   ? -17.777 -3.186  7.287   1.00 23.19 ? 723 HOH B O     1 
HETATM 6923 O  O     . HOH J 5 .   ? -19.370 7.464   -9.173  1.00 30.47 ? 724 HOH B O     1 
HETATM 6924 O  O     . HOH J 5 .   ? -23.272 -0.316  -2.658  1.00 23.67 ? 725 HOH B O     1 
HETATM 6925 O  O     . HOH J 5 .   ? -6.429  18.307  -2.323  1.00 21.67 ? 726 HOH B O     1 
HETATM 6926 O  O     . HOH J 5 .   ? -15.037 15.957  -20.747 1.00 21.41 ? 727 HOH B O     1 
HETATM 6927 O  O     . HOH J 5 .   ? -21.238 -12.693 -15.418 1.00 21.67 ? 728 HOH B O     1 
HETATM 6928 O  O     . HOH J 5 .   ? -5.136  -13.493 1.272   1.00 18.28 ? 729 HOH B O     1 
HETATM 6929 O  O     . HOH J 5 .   ? -20.740 -6.530  0.848   1.00 17.25 ? 730 HOH B O     1 
HETATM 6930 O  O     . HOH J 5 .   ? -20.591 30.261  -5.978  1.00 29.60 ? 731 HOH B O     1 
HETATM 6931 O  O     . HOH J 5 .   ? -13.974 9.564   4.974   1.00 27.97 ? 732 HOH B O     1 
HETATM 6932 O  O     . HOH J 5 .   ? -13.789 39.667  -17.065 1.00 20.95 ? 733 HOH B O     1 
HETATM 6933 O  O     . HOH J 5 .   ? -21.803 -5.625  13.433  1.00 30.12 ? 734 HOH B O     1 
HETATM 6934 O  O     . HOH J 5 .   ? -36.299 20.840  -3.762  1.00 33.75 ? 735 HOH B O     1 
HETATM 6935 O  O     . HOH J 5 .   ? -18.717 35.630  -2.351  1.00 35.38 ? 736 HOH B O     1 
HETATM 6936 O  O     . HOH J 5 .   ? -8.775  23.808  0.988   1.00 31.59 ? 737 HOH B O     1 
HETATM 6937 O  O     . HOH J 5 .   ? -24.567 21.505  -33.311 1.00 31.53 ? 738 HOH B O     1 
HETATM 6938 O  O     . HOH J 5 .   ? -18.989 19.209  -8.473  1.00 14.88 ? 739 HOH B O     1 
HETATM 6939 O  O     . HOH J 5 .   ? -27.195 15.516  10.997  1.00 31.36 ? 740 HOH B O     1 
HETATM 6940 O  O     . HOH J 5 .   ? -15.656 -11.926 -13.244 1.00 19.26 ? 741 HOH B O     1 
HETATM 6941 O  O     . HOH J 5 .   ? -11.378 7.171   -19.399 1.00 25.83 ? 742 HOH B O     1 
HETATM 6942 O  O     . HOH J 5 .   ? -25.285 -4.582  -28.797 1.00 20.10 ? 743 HOH B O     1 
HETATM 6943 O  O     . HOH J 5 .   ? -10.120 -13.739 -5.394  1.00 20.17 ? 744 HOH B O     1 
HETATM 6944 O  O     . HOH J 5 .   ? -13.541 -5.486  21.131  1.00 15.76 ? 745 HOH B O     1 
HETATM 6945 O  O     . HOH J 5 .   ? -20.232 -7.071  23.132  1.00 35.89 ? 746 HOH B O     1 
HETATM 6946 O  O     . HOH J 5 .   ? -35.106 10.307  -11.602 1.00 31.89 ? 747 HOH B O     1 
HETATM 6947 O  O     . HOH J 5 .   ? -8.666  16.962  -22.991 1.00 30.42 ? 748 HOH B O     1 
HETATM 6948 O  O     . HOH J 5 .   ? -1.342  3.421   2.764   1.00 28.31 ? 749 HOH B O     1 
HETATM 6949 O  O     . HOH J 5 .   ? -31.209 24.778  -15.773 1.00 28.13 ? 750 HOH B O     1 
HETATM 6950 O  O     . HOH J 5 .   ? -24.908 -5.619  20.165  1.00 43.70 ? 751 HOH B O     1 
HETATM 6951 O  O     . HOH J 5 .   ? -35.312 16.370  -0.472  1.00 28.56 ? 752 HOH B O     1 
HETATM 6952 O  O     . HOH J 5 .   ? -29.109 29.242  -31.792 1.00 32.54 ? 753 HOH B O     1 
HETATM 6953 O  O     . HOH J 5 .   ? -5.025  32.469  -16.129 1.00 32.36 ? 754 HOH B O     1 
HETATM 6954 O  O     . HOH J 5 .   ? -15.048 8.634   24.545  1.00 37.63 ? 755 HOH B O     1 
HETATM 6955 O  O     . HOH J 5 .   ? -20.843 12.460  -7.635  1.00 21.64 ? 756 HOH B O     1 
HETATM 6956 O  O     . HOH J 5 .   ? -6.645  32.527  -21.766 1.00 31.09 ? 757 HOH B O     1 
HETATM 6957 O  O     . HOH J 5 .   ? -33.100 20.367  -15.081 1.00 35.81 ? 758 HOH B O     1 
HETATM 6958 O  O     . HOH J 5 .   ? -28.609 23.570  -15.654 1.00 27.90 ? 759 HOH B O     1 
HETATM 6959 O  O     . HOH J 5 .   ? -5.919  22.094  24.079  1.00 29.25 ? 760 HOH B O     1 
HETATM 6960 O  O     . HOH J 5 .   ? 2.449   10.378  10.248  1.00 30.15 ? 761 HOH B O     1 
HETATM 6961 O  O     . HOH J 5 .   ? -6.317  18.700  -23.380 1.00 27.67 ? 762 HOH B O     1 
HETATM 6962 O  O     . HOH J 5 .   ? -36.030 10.944  -18.390 1.00 36.77 ? 763 HOH B O     1 
HETATM 6963 O  O     . HOH J 5 .   ? -32.081 11.108  6.865   1.00 31.09 ? 764 HOH B O     1 
HETATM 6964 O  O     . HOH J 5 .   ? -31.550 30.730  -31.288 1.00 41.37 ? 765 HOH B O     1 
HETATM 6965 O  O     . HOH J 5 .   ? -33.372 22.984  -14.263 1.00 22.42 ? 766 HOH B O     1 
HETATM 6966 O  O     . HOH J 5 .   ? -9.269  15.194  -25.073 1.00 28.05 ? 767 HOH B O     1 
HETATM 6967 O  O     . HOH J 5 .   ? -12.697 46.432  -17.469 1.00 29.95 ? 768 HOH B O     1 
# 
