data_9H5Q
# 
_entry.id   9H5Q 
# 
_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   9H5Q         pdb_00009h5q 10.2210/pdb9h5q/pdb 
WWPDB D_1292142661 ?            ?                   
# 
_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                        9H5Q 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9H5P 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              claudia.binda@unipv.it 
_pdbx_contact_author.name_first         Claudia 
_pdbx_contact_author.name_last          Binda 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2038-9845 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Basile, L.'      1 0009-0004-6724-0110 
'Poli, C.'        2 ?                   
'Santema, L.L.'   3 ?                   
'Lesenciuc, R.C.' 4 ?                   
'Fraaije, M.W.'   5 0000-0001-6346-5014 
'Binda, C.'       6 0000-0003-2038-9845 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Arch.Biochem.Biophys. 
_citation.journal_id_ASTM           ABBIA4 
_citation.journal_id_CSD            0158 
_citation.journal_id_ISSN           1096-0384 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            764 
_citation.language                  ? 
_citation.page_first                110276 
_citation.page_last                 110276 
_citation.title                     
'Altering substrate specificity of a thermostable bacterial monoamine oxidase by structure-based mutagenesis.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.abb.2024.110276 
_citation.pdbx_database_id_PubMed   39706511 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Basile, L.'      1 ? 
primary 'Poli, C.'        2 ? 
primary 'Santema, L.L.'   3 ? 
primary 'Lesenciuc, R.C.' 4 ? 
primary 'Fraaije, M.W.'   5 ? 
primary 'Binda, C.'       6 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Monoamine oxidase'           50089.773 2   ? ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   2   ? ? ? ? 
3 non-polymer syn GLYCEROL                      92.094    3   ? ? ? ? 
4 non-polymer syn 1,3-DIAMINOPROPANE            74.125    1   ? ? ? ? 
5 non-polymer syn 4-HYDROXYBUTAN-1-AMINIUM      90.144    1   ? ? ? ? 
6 non-polymer syn 'MAGNESIUM ION'               24.305    3   ? ? ? ? 
7 non-polymer syn SPERMIDINE                    145.246   1   ? ? ? ? 
8 water       nat water                         18.015    518 ? ? ? ? 
# 
_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 GLYCEROL                      GOL 
4 1,3-DIAMINOPROPANE            13D 
5 4-HYDROXYBUTAN-1-AMINIUM      4HA 
6 'MAGNESIUM ION'               MG  
7 SPERMIDINE                    SPD 
8 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 
13D non-polymer         . 1,3-DIAMINOPROPANE            ?                                              'C3 H10 N2'         74.125  
4HA non-polymer         . 4-HYDROXYBUTAN-1-AMINIUM      ?                                              'C4 H12 N O 1'      90.144  
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  
GOL non-polymer         . GLYCEROL                      'GLYCERIN; PROPANE-1,2,3-TRIOL'                'C3 H8 O3'          92.094  
HIS 'L-peptide linking' y HISTIDINE                     ?                                              'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                         ?                                              'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ?                                              'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ?                                              'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ?                                              'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ?                                              'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'               ?                                              'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE                 ?                                              'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ?                                              'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ?                                              'C3 H7 N O3'        105.093 
SPD non-polymer         . SPERMIDINE                    'N-(2-AMINO-PROPYL)-1,4-DIAMINOBUTANE; PA(34)' 'C7 H19 N3'         145.246 
THR 'L-peptide linking' y THREONINE                     ?                                              'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ?                                              'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ?                                              'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ?                                              'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -20 ?   ?   ?   A . n 
A 1 2   GLY 2   -19 ?   ?   ?   A . n 
A 1 3   SER 3   -18 ?   ?   ?   A . n 
A 1 4   SER 4   -17 ?   ?   ?   A . n 
A 1 5   HIS 5   -16 ?   ?   ?   A . n 
A 1 6   HIS 6   -15 ?   ?   ?   A . n 
A 1 7   HIS 7   -14 ?   ?   ?   A . n 
A 1 8   HIS 8   -13 ?   ?   ?   A . n 
A 1 9   HIS 9   -12 ?   ?   ?   A . n 
A 1 10  HIS 10  -11 ?   ?   ?   A . n 
A 1 11  GLY 11  -10 ?   ?   ?   A . n 
A 1 12  SER 12  -9  ?   ?   ?   A . n 
A 1 13  GLY 13  -8  ?   ?   ?   A . n 
A 1 14  LEU 14  -7  ?   ?   ?   A . n 
A 1 15  VAL 15  -6  ?   ?   ?   A . n 
A 1 16  PRO 16  -5  ?   ?   ?   A . n 
A 1 17  ARG 17  -4  ?   ?   ?   A . n 
A 1 18  GLY 18  -3  ?   ?   ?   A . n 
A 1 19  SER 19  -2  ?   ?   ?   A . n 
A 1 20  ALA 20  -1  ?   ?   ?   A . n 
A 1 21  GLY 21  0   ?   ?   ?   A . n 
A 1 22  MET 22  1   ?   ?   ?   A . n 
A 1 23  PRO 23  2   ?   ?   ?   A . n 
A 1 24  SER 24  3   ?   ?   ?   A . n 
A 1 25  GLU 25  4   ?   ?   ?   A . n 
A 1 26  GLN 26  5   5   GLN GLN A . n 
A 1 27  VAL 27  6   6   VAL VAL A . n 
A 1 28  ASP 28  7   7   ASP ASP A . n 
A 1 29  VAL 29  8   8   VAL VAL A . n 
A 1 30  VAL 30  9   9   VAL VAL A . n 
A 1 31  VAL 31  10  10  VAL VAL A . n 
A 1 32  VAL 32  11  11  VAL VAL A . n 
A 1 33  GLY 33  12  12  GLY GLY A . n 
A 1 34  ALA 34  13  13  ALA ALA A . n 
A 1 35  GLY 35  14  14  GLY GLY A . n 
A 1 36  PHE 36  15  15  PHE PHE A . n 
A 1 37  ALA 37  16  16  ALA ALA A . n 
A 1 38  GLY 38  17  17  GLY GLY A . n 
A 1 39  LEU 39  18  18  LEU LEU A . n 
A 1 40  THR 40  19  19  THR THR A . n 
A 1 41  ALA 41  20  20  ALA ALA A . n 
A 1 42  ALA 42  21  21  ALA ALA A . n 
A 1 43  ARG 43  22  22  ARG ARG A . n 
A 1 44  ALA 44  23  23  ALA ALA A . n 
A 1 45  VAL 45  24  24  VAL VAL A . n 
A 1 46  HIS 46  25  25  HIS HIS A . n 
A 1 47  GLU 47  26  26  GLU GLU A . n 
A 1 48  ALA 48  27  27  ALA ALA A . n 
A 1 49  GLY 49  28  28  GLY GLY A . n 
A 1 50  ARG 50  29  29  ARG ARG A . n 
A 1 51  SER 51  30  30  SER SER A . n 
A 1 52  VAL 52  31  31  VAL VAL A . n 
A 1 53  LEU 53  32  32  LEU LEU A . n 
A 1 54  VAL 54  33  33  VAL VAL A . n 
A 1 55  LEU 55  34  34  LEU LEU A . n 
A 1 56  GLU 56  35  35  GLU GLU A . n 
A 1 57  ALA 57  36  36  ALA ALA A . n 
A 1 58  ARG 58  37  37  ARG ARG A . n 
A 1 59  ASP 59  38  38  ASP ASP A . n 
A 1 60  ARG 60  39  39  ARG ARG A . n 
A 1 61  VAL 61  40  40  VAL VAL A . n 
A 1 62  GLY 62  41  41  GLY GLY A . n 
A 1 63  GLY 63  42  42  GLY GLY A . n 
A 1 64  ARG 64  43  43  ARG ARG A . n 
A 1 65  THR 65  44  44  THR THR A . n 
A 1 66  CYS 66  45  45  CYS CYS A . n 
A 1 67  THR 67  46  46  THR THR A . n 
A 1 68  GLU 68  47  47  GLU GLU A . n 
A 1 69  GLU 69  48  48  GLU GLU A . n 
A 1 70  HIS 70  49  49  HIS HIS A . n 
A 1 71  HIS 71  50  50  HIS HIS A . n 
A 1 72  GLY 72  51  51  GLY GLY A . n 
A 1 73  THR 73  52  52  THR THR A . n 
A 1 74  TRP 74  53  53  TRP TRP A . n 
A 1 75  ILE 75  54  54  ILE ILE A . n 
A 1 76  ASP 76  55  55  ASP ASP A . n 
A 1 77  LEU 77  56  56  LEU LEU A . n 
A 1 78  GLY 78  57  57  GLY GLY A . n 
A 1 79  GLY 79  58  58  GLY GLY A . n 
A 1 80  GLN 80  59  59  GLN GLN A . n 
A 1 81  TRP 81  60  60  TRP TRP A . n 
A 1 82  ILE 82  61  61  ILE ILE A . n 
A 1 83  GLY 83  62  62  GLY GLY A . n 
A 1 84  PRO 84  63  63  PRO PRO A . n 
A 1 85  GLY 85  64  64  GLY GLY A . n 
A 1 86  GLN 86  65  65  GLN GLN A . n 
A 1 87  ASP 87  66  66  ASP ASP A . n 
A 1 88  ARG 88  67  67  ARG ARG A . n 
A 1 89  VAL 89  68  68  VAL VAL A . n 
A 1 90  ALA 90  69  69  ALA ALA A . n 
A 1 91  ALA 91  70  70  ALA ALA A . n 
A 1 92  LEU 92  71  71  LEU LEU A . n 
A 1 93  ALA 93  72  72  ALA ALA A . n 
A 1 94  ALA 94  73  73  ALA ALA A . n 
A 1 95  GLU 95  74  74  GLU GLU A . n 
A 1 96  LEU 96  75  75  LEU LEU A . n 
A 1 97  GLY 97  76  76  GLY GLY A . n 
A 1 98  VAL 98  77  77  VAL VAL A . n 
A 1 99  GLU 99  78  78  GLU GLU A . n 
A 1 100 THR 100 79  79  THR THR A . n 
A 1 101 TYR 101 80  80  TYR TYR A . n 
A 1 102 PRO 102 81  81  PRO PRO A . n 
A 1 103 GLN 103 82  82  GLN GLN A . n 
A 1 104 PRO 104 83  83  PRO PRO A . n 
A 1 105 THR 105 84  84  THR THR A . n 
A 1 106 GLU 106 85  85  GLU GLU A . n 
A 1 107 GLY 107 86  86  GLY GLY A . n 
A 1 108 ASP 108 87  87  ASP ASP A . n 
A 1 109 ASP 109 88  88  ASP ASP A . n 
A 1 110 VAL 110 89  89  VAL VAL A . n 
A 1 111 VAL 111 90  90  VAL VAL A . n 
A 1 112 LEU 112 91  91  LEU LEU A . n 
A 1 113 PHE 113 92  92  PHE PHE A . n 
A 1 114 GLY 114 93  93  GLY GLY A . n 
A 1 115 ASP 115 94  94  ASP ASP A . n 
A 1 116 GLY 116 95  95  GLY GLY A . n 
A 1 117 GLU 117 96  96  GLU GLU A . n 
A 1 118 PRO 118 97  97  PRO PRO A . n 
A 1 119 GLN 119 98  98  GLN GLN A . n 
A 1 120 ARG 120 99  99  ARG ARG A . n 
A 1 121 ALA 121 100 100 ALA ALA A . n 
A 1 122 PRO 122 101 101 PRO PRO A . n 
A 1 123 ASP 123 102 102 ASP ASP A . n 
A 1 124 VAL 124 103 103 VAL VAL A . n 
A 1 125 ALA 125 104 104 ALA ALA A . n 
A 1 126 LEU 126 105 105 LEU LEU A . n 
A 1 127 ALA 127 106 106 ALA ALA A . n 
A 1 128 PHE 128 107 107 PHE PHE A . n 
A 1 129 SER 129 108 108 SER SER A . n 
A 1 130 ASP 130 109 109 ASP ASP A . n 
A 1 131 GLU 131 110 110 GLU GLU A . n 
A 1 132 GLU 132 111 111 GLU GLU A . n 
A 1 133 LEU 133 112 112 LEU LEU A . n 
A 1 134 THR 134 113 113 THR THR A . n 
A 1 135 ALA 135 114 114 ALA ALA A . n 
A 1 136 TYR 136 115 115 TYR TYR A . n 
A 1 137 LEU 137 116 116 LEU LEU A . n 
A 1 138 GLU 138 117 117 GLU GLU A . n 
A 1 139 LEU 139 118 118 LEU LEU A . n 
A 1 140 ALA 140 119 119 ALA ALA A . n 
A 1 141 GLY 141 120 120 GLY GLY A . n 
A 1 142 ALA 142 121 121 ALA ALA A . n 
A 1 143 LEU 143 122 122 LEU LEU A . n 
A 1 144 GLU 144 123 123 GLU GLU A . n 
A 1 145 ALA 145 124 124 ALA ALA A . n 
A 1 146 ILE 146 125 125 ILE ILE A . n 
A 1 147 ALA 147 126 126 ALA ALA A . n 
A 1 148 GLU 148 127 127 GLU GLU A . n 
A 1 149 LYS 149 128 128 LYS LYS A . n 
A 1 150 VAL 150 129 129 VAL VAL A . n 
A 1 151 PRO 151 130 130 PRO PRO A . n 
A 1 152 LEU 152 131 131 LEU LEU A . n 
A 1 153 ASP 153 132 132 ASP ASP A . n 
A 1 154 ALA 154 133 133 ALA ALA A . n 
A 1 155 PRO 155 134 134 PRO PRO A . n 
A 1 156 TRP 156 135 135 TRP TRP A . n 
A 1 157 LEU 157 136 136 LEU LEU A . n 
A 1 158 ALA 158 137 137 ALA ALA A . n 
A 1 159 PRO 159 138 138 PRO PRO A . n 
A 1 160 GLU 160 139 139 GLU GLU A . n 
A 1 161 ALA 161 140 140 ALA ALA A . n 
A 1 162 ALA 162 141 141 ALA ALA A . n 
A 1 163 ALA 163 142 142 ALA ALA A . n 
A 1 164 TRP 164 143 143 TRP TRP A . n 
A 1 165 ASP 165 144 144 ASP ASP A . n 
A 1 166 ALA 166 145 145 ALA ALA A . n 
A 1 167 THR 167 146 146 THR THR A . n 
A 1 168 THR 168 147 147 THR THR A . n 
A 1 169 LEU 169 148 148 LEU LEU A . n 
A 1 170 ARG 170 149 149 ARG ARG A . n 
A 1 171 GLU 171 150 150 GLU GLU A . n 
A 1 172 TRP 172 151 151 TRP TRP A . n 
A 1 173 VAL 173 152 152 VAL VAL A . n 
A 1 174 ALA 174 153 153 ALA ALA A . n 
A 1 175 GLY 175 154 154 GLY GLY A . n 
A 1 176 THR 176 155 155 THR THR A . n 
A 1 177 GLY 177 156 156 GLY GLY A . n 
A 1 178 VAL 178 157 157 VAL VAL A . n 
A 1 179 PRO 179 158 158 PRO PRO A . n 
A 1 180 ASP 180 159 159 ASP ASP A . n 
A 1 181 ARG 181 160 160 ARG ARG A . n 
A 1 182 VAL 182 161 161 VAL VAL A . n 
A 1 183 ALA 183 162 162 ALA ALA A . n 
A 1 184 GLY 184 163 163 GLY GLY A . n 
A 1 185 LEU 185 164 164 LEU LEU A . n 
A 1 186 PHE 186 165 165 PHE PHE A . n 
A 1 187 GLU 187 166 166 GLU GLU A . n 
A 1 188 VAL 188 167 167 VAL VAL A . n 
A 1 189 ALA 189 168 168 ALA ALA A . n 
A 1 190 VAL 190 169 169 VAL VAL A . n 
A 1 191 GLN 191 170 170 GLN GLN A . n 
A 1 192 ALA 192 171 171 ALA ALA A . n 
A 1 193 VAL 193 172 172 VAL VAL A . n 
A 1 194 PHE 194 173 173 PHE PHE A . n 
A 1 195 ALA 195 174 174 ALA ALA A . n 
A 1 196 ALA 196 175 175 ALA ALA A . n 
A 1 197 THR 197 176 176 THR THR A . n 
A 1 198 SER 198 177 177 SER SER A . n 
A 1 199 ALA 199 178 178 ALA ALA A . n 
A 1 200 GLN 200 179 179 GLN GLN A . n 
A 1 201 LEU 201 180 180 LEU LEU A . n 
A 1 202 SER 202 181 181 SER SER A . n 
A 1 203 LEU 203 182 182 LEU LEU A . n 
A 1 204 LEU 204 183 183 LEU LEU A . n 
A 1 205 HIS 205 184 184 HIS HIS A . n 
A 1 206 ALA 206 185 185 ALA ALA A . n 
A 1 207 ALA 207 186 186 ALA ALA A . n 
A 1 208 HIS 208 187 187 HIS HIS A . n 
A 1 209 TYR 209 188 188 TYR TYR A . n 
A 1 210 VAL 210 189 189 VAL VAL A . n 
A 1 211 HIS 211 190 190 HIS HIS A . n 
A 1 212 SER 212 191 191 SER SER A . n 
A 1 213 ALA 213 192 192 ALA ALA A . n 
A 1 214 GLY 214 193 193 GLY GLY A . n 
A 1 215 GLY 215 194 194 GLY GLY A . n 
A 1 216 TRP 216 195 195 TRP TRP A . n 
A 1 217 SER 217 196 196 SER SER A . n 
A 1 218 LYS 218 197 197 LYS LYS A . n 
A 1 219 LEU 219 198 198 LEU LEU A . n 
A 1 220 THR 220 199 199 THR THR A . n 
A 1 221 ASP 221 200 200 ASP ASP A . n 
A 1 222 THR 222 201 201 THR THR A . n 
A 1 223 GLU 223 202 202 GLU GLU A . n 
A 1 224 GLY 224 203 203 GLY GLY A . n 
A 1 225 GLY 225 204 204 GLY GLY A . n 
A 1 226 ALA 226 205 205 ALA ALA A . n 
A 1 227 GLN 227 206 206 GLN GLN A . n 
A 1 228 GLN 228 207 207 GLN GLN A . n 
A 1 229 ASP 229 208 208 ASP ASP A . n 
A 1 230 ARG 230 209 209 ARG ARG A . n 
A 1 231 LEU 231 210 210 LEU LEU A . n 
A 1 232 VAL 232 211 211 VAL VAL A . n 
A 1 233 GLY 233 212 212 GLY GLY A . n 
A 1 234 GLY 234 213 213 GLY GLY A . n 
A 1 235 VAL 235 214 214 VAL VAL A . n 
A 1 236 GLN 236 215 215 GLN GLN A . n 
A 1 237 PRO 237 216 216 PRO PRO A . n 
A 1 238 LEU 238 217 217 LEU LEU A . n 
A 1 239 ALA 239 218 218 ALA ALA A . n 
A 1 240 GLU 240 219 219 GLU GLU A . n 
A 1 241 ARG 241 220 220 ARG ARG A . n 
A 1 242 LEU 242 221 221 LEU LEU A . n 
A 1 243 ALA 243 222 222 ALA ALA A . n 
A 1 244 ALA 244 223 223 ALA ALA A . n 
A 1 245 ARG 245 224 224 ARG ARG A . n 
A 1 246 LEU 246 225 225 LEU LEU A . n 
A 1 247 PRO 247 226 226 PRO PRO A . n 
A 1 248 ASP 248 227 227 ASP ASP A . n 
A 1 249 GLY 249 228 228 GLY GLY A . n 
A 1 250 ALA 250 229 229 ALA ALA A . n 
A 1 251 LEU 251 230 230 LEU LEU A . n 
A 1 252 ARG 252 231 231 ARG ARG A . n 
A 1 253 LEU 253 232 232 LEU LEU A . n 
A 1 254 SER 254 233 233 SER SER A . n 
A 1 255 THR 255 234 234 THR THR A . n 
A 1 256 PRO 256 235 235 PRO PRO A . n 
A 1 257 VAL 257 236 236 VAL VAL A . n 
A 1 258 ARG 258 237 237 ARG ARG A . n 
A 1 259 GLY 259 238 238 GLY GLY A . n 
A 1 260 LEU 260 239 239 LEU LEU A . n 
A 1 261 ALA 261 240 240 ALA ALA A . n 
A 1 262 GLN 262 241 241 GLN GLN A . n 
A 1 263 ASP 263 242 242 ASP ASP A . n 
A 1 264 GLY 264 243 243 GLY GLY A . n 
A 1 265 ASP 265 244 244 ASP ASP A . n 
A 1 266 GLY 266 245 245 GLY GLY A . n 
A 1 267 VAL 267 246 246 VAL VAL A . n 
A 1 268 THR 268 247 247 THR THR A . n 
A 1 269 VAL 269 248 248 VAL VAL A . n 
A 1 270 ARG 270 249 249 ARG ARG A . n 
A 1 271 THR 271 250 250 THR THR A . n 
A 1 272 ALA 272 251 251 ALA ALA A . n 
A 1 273 GLY 273 252 252 GLY GLY A . n 
A 1 274 GLY 274 253 253 GLY GLY A . n 
A 1 275 GLU 275 254 254 GLU GLU A . n 
A 1 276 VAL 276 255 255 VAL VAL A . n 
A 1 277 ARG 277 256 256 ARG ARG A . n 
A 1 278 ALA 278 257 257 ALA ALA A . n 
A 1 279 ARG 279 258 258 ARG ARG A . n 
A 1 280 ARG 280 259 259 ARG ARG A . n 
A 1 281 ALA 281 260 260 ALA ALA A . n 
A 1 282 ILE 282 261 261 ILE ILE A . n 
A 1 283 VAL 283 262 262 VAL VAL A . n 
A 1 284 ALA 284 263 263 ALA ALA A . n 
A 1 285 VAL 285 264 264 VAL VAL A . n 
A 1 286 PRO 286 265 265 PRO PRO A . n 
A 1 287 PRO 287 266 266 PRO PRO A . n 
A 1 288 THR 288 267 267 THR THR A . n 
A 1 289 LEU 289 268 268 LEU LEU A . n 
A 1 290 ALA 290 269 269 ALA ALA A . n 
A 1 291 GLY 291 270 270 GLY GLY A . n 
A 1 292 ARG 292 271 271 ARG ARG A . n 
A 1 293 ILE 293 272 272 ILE ILE A . n 
A 1 294 ASP 294 273 273 ASP ASP A . n 
A 1 295 HIS 295 274 274 HIS HIS A . n 
A 1 296 ASP 296 275 275 ASP ASP A . n 
A 1 297 PRO 297 276 276 PRO PRO A . n 
A 1 298 PRO 298 277 277 PRO PRO A . n 
A 1 299 LEU 299 278 278 LEU LEU A . n 
A 1 300 PRO 300 279 279 PRO PRO A . n 
A 1 301 PRO 301 280 280 PRO PRO A . n 
A 1 302 GLN 302 281 281 GLN GLN A . n 
A 1 303 ARG 303 282 282 ARG ARG A . n 
A 1 304 ASP 304 283 283 ASP ASP A . n 
A 1 305 GLN 305 284 284 GLN GLN A . n 
A 1 306 LEU 306 285 285 LEU LEU A . n 
A 1 307 LEU 307 286 286 LEU LEU A . n 
A 1 308 GLN 308 287 287 GLN GLN A . n 
A 1 309 HIS 309 288 288 HIS HIS A . n 
A 1 310 MET 310 289 289 MET MET A . n 
A 1 311 PRO 311 290 290 PRO PRO A . n 
A 1 312 GLN 312 291 291 GLN GLN A . n 
A 1 313 GLY 313 292 292 GLY GLY A . n 
A 1 314 SER 314 293 293 SER SER A . n 
A 1 315 VAL 315 294 294 VAL VAL A . n 
A 1 316 VAL 316 295 295 VAL VAL A . n 
A 1 317 LYS 317 296 296 LYS LYS A . n 
A 1 318 PHE 318 297 297 PHE PHE A . n 
A 1 319 HIS 319 298 298 HIS HIS A . n 
A 1 320 VAL 320 299 299 VAL VAL A . n 
A 1 321 ILE 321 300 300 ILE ILE A . n 
A 1 322 TYR 322 301 301 TYR TYR A . n 
A 1 323 ASP 323 302 302 ASP ASP A . n 
A 1 324 GLU 324 303 303 GLU GLU A . n 
A 1 325 PRO 325 304 304 PRO PRO A . n 
A 1 326 TRP 326 305 305 TRP TRP A . n 
A 1 327 TRP 327 306 306 TRP TRP A . n 
A 1 328 ARG 328 307 307 ARG ARG A . n 
A 1 329 ALA 329 308 308 ALA ALA A . n 
A 1 330 GLU 330 309 309 GLU GLU A . n 
A 1 331 GLY 331 310 310 GLY GLY A . n 
A 1 332 LEU 332 311 311 LEU LEU A . n 
A 1 333 SER 333 312 312 SER SER A . n 
A 1 334 GLY 334 313 313 GLY GLY A . n 
A 1 335 THR 335 314 314 THR THR A . n 
A 1 336 VAL 336 315 315 VAL VAL A . n 
A 1 337 LEU 337 316 316 LEU LEU A . n 
A 1 338 CYS 338 317 317 CYS CYS A . n 
A 1 339 PRO 339 318 318 PRO PRO A . n 
A 1 340 ASP 340 319 319 ASP ASP A . n 
A 1 341 GLU 341 320 320 GLU GLU A . n 
A 1 342 PRO 342 321 321 PRO PRO A . n 
A 1 343 ILE 343 322 322 ILE ILE A . n 
A 1 344 GLY 344 323 323 GLY GLY A . n 
A 1 345 VAL 345 324 324 VAL VAL A . n 
A 1 346 THR 346 325 325 THR THR A . n 
A 1 347 PHE 347 326 326 PHE PHE A . n 
A 1 348 ASP 348 327 327 ASP ASP A . n 
A 1 349 GLY 349 328 328 GLY GLY A . n 
A 1 350 THR 350 329 329 THR THR A . n 
A 1 351 PRO 351 330 330 PRO PRO A . n 
A 1 352 PRO 352 331 331 PRO PRO A . n 
A 1 353 ALA 353 332 332 ALA ALA A . n 
A 1 354 GLY 354 333 333 GLY GLY A . n 
A 1 355 THR 355 334 334 THR THR A . n 
A 1 356 PRO 356 335 335 PRO PRO A . n 
A 1 357 GLY 357 336 336 GLY GLY A . n 
A 1 358 ILE 358 337 337 ILE ILE A . n 
A 1 359 VAL 359 338 338 VAL VAL A . n 
A 1 360 THR 360 339 339 THR THR A . n 
A 1 361 GLY 361 340 340 GLY GLY A . n 
A 1 362 PHE 362 341 341 PHE PHE A . n 
A 1 363 PHE 363 342 342 PHE PHE A . n 
A 1 364 GLU 364 343 343 GLU GLU A . n 
A 1 365 GLY 365 344 344 GLY GLY A . n 
A 1 366 PRO 366 345 345 PRO PRO A . n 
A 1 367 ALA 367 346 346 ALA ALA A . n 
A 1 368 ALA 368 347 347 ALA ALA A . n 
A 1 369 VAL 369 348 348 VAL VAL A . n 
A 1 370 ALA 370 349 349 ALA ALA A . n 
A 1 371 ALA 371 350 350 ALA ALA A . n 
A 1 372 GLY 372 351 351 GLY GLY A . n 
A 1 373 ALA 373 352 352 ALA ALA A . n 
A 1 374 ARG 374 353 353 ARG ARG A . n 
A 1 375 THR 375 354 354 THR THR A . n 
A 1 376 ARG 376 355 355 ARG ARG A . n 
A 1 377 GLU 377 356 356 GLU GLU A . n 
A 1 378 GLU 378 357 357 GLU GLU A . n 
A 1 379 ARG 379 358 358 ARG ARG A . n 
A 1 380 ARG 380 359 359 ARG ARG A . n 
A 1 381 ASP 381 360 360 ASP ASP A . n 
A 1 382 VAL 382 361 361 VAL VAL A . n 
A 1 383 VAL 383 362 362 VAL VAL A . n 
A 1 384 VAL 384 363 363 VAL VAL A . n 
A 1 385 ASP 385 364 364 ASP ASP A . n 
A 1 386 VAL 386 365 365 VAL VAL A . n 
A 1 387 LEU 387 366 366 LEU LEU A . n 
A 1 388 ALA 388 367 367 ALA ALA A . n 
A 1 389 ARG 389 368 368 ARG ARG A . n 
A 1 390 THR 390 369 369 THR THR A . n 
A 1 391 LEU 391 370 370 LEU LEU A . n 
A 1 392 GLY 392 371 371 GLY GLY A . n 
A 1 393 GLU 393 372 372 GLU GLU A . n 
A 1 394 ARG 394 373 373 ARG ARG A . n 
A 1 395 ALA 395 374 374 ALA ALA A . n 
A 1 396 ARG 396 375 375 ARG ARG A . n 
A 1 397 ASP 397 376 376 ASP ASP A . n 
A 1 398 VAL 398 377 377 VAL VAL A . n 
A 1 399 ARG 399 378 378 ARG ARG A . n 
A 1 400 ASP 400 379 379 ASP ASP A . n 
A 1 401 TYR 401 380 380 TYR TYR A . n 
A 1 402 ILE 402 381 381 ILE ILE A . n 
A 1 403 ASP 403 382 382 ASP ASP A . n 
A 1 404 ARG 404 383 383 ARG ARG A . n 
A 1 405 ASP 405 384 384 ASP ASP A . n 
A 1 406 TRP 406 385 385 TRP TRP A . n 
A 1 407 SER 407 386 386 SER SER A . n 
A 1 408 ALA 408 387 387 ALA ALA A . n 
A 1 409 GLU 409 388 388 GLU GLU A . n 
A 1 410 PRO 410 389 389 PRO PRO A . n 
A 1 411 TRP 411 390 390 TRP TRP A . n 
A 1 412 THR 412 391 391 THR THR A . n 
A 1 413 ARG 413 392 392 ARG ARG A . n 
A 1 414 GLY 414 393 393 GLY GLY A . n 
A 1 415 CYS 415 394 394 CYS CYS A . n 
A 1 416 TYR 416 395 395 TYR TYR A . n 
A 1 417 GLY 417 396 396 GLY GLY A . n 
A 1 418 ALA 418 397 397 ALA ALA A . n 
A 1 419 HIS 419 398 398 HIS HIS A . n 
A 1 420 LEU 420 399 399 LEU LEU A . n 
A 1 421 PRO 421 400 400 PRO PRO A . n 
A 1 422 PRO 422 401 401 PRO PRO A . n 
A 1 423 GLY 423 402 402 GLY GLY A . n 
A 1 424 ALA 424 403 403 ALA ALA A . n 
A 1 425 TRP 425 404 404 TRP TRP A . n 
A 1 426 THR 426 405 405 THR THR A . n 
A 1 427 VAL 427 406 406 VAL VAL A . n 
A 1 428 TYR 428 407 407 TYR TYR A . n 
A 1 429 GLY 429 408 408 GLY GLY A . n 
A 1 430 PRO 430 409 409 PRO PRO A . n 
A 1 431 ALA 431 410 410 ALA ALA A . n 
A 1 432 LEU 432 411 411 LEU LEU A . n 
A 1 433 ARG 433 412 412 ARG ARG A . n 
A 1 434 VAL 434 413 413 VAL VAL A . n 
A 1 435 PRO 435 414 414 PRO PRO A . n 
A 1 436 VAL 436 415 415 VAL VAL A . n 
A 1 437 GLY 437 416 416 GLY GLY A . n 
A 1 438 ARG 438 417 417 ARG ARG A . n 
A 1 439 VAL 439 418 418 VAL VAL A . n 
A 1 440 HIS 440 419 419 HIS HIS A . n 
A 1 441 TRP 441 420 420 TRP TRP A . n 
A 1 442 ALA 442 421 421 ALA ALA A . n 
A 1 443 GLY 443 422 422 GLY GLY A . n 
A 1 444 THR 444 423 423 THR THR A . n 
A 1 445 GLU 445 424 424 GLU GLU A . n 
A 1 446 THR 446 425 425 THR THR A . n 
A 1 447 ALA 447 426 426 ALA ALA A . n 
A 1 448 GLU 448 427 427 GLU GLU A . n 
A 1 449 ARG 449 428 428 ARG ARG A . n 
A 1 450 TRP 450 429 429 TRP TRP A . n 
A 1 451 THR 451 430 430 THR THR A . n 
A 1 452 GLY 452 431 431 GLY GLY A . n 
A 1 453 TYR 453 432 432 TYR TYR A . n 
A 1 454 ILE 454 433 433 ILE ILE A . n 
A 1 455 ASP 455 434 434 ASP ASP A . n 
A 1 456 GLY 456 435 435 GLY GLY A . n 
A 1 457 ALA 457 436 436 ALA ALA A . n 
A 1 458 ILE 458 437 437 ILE ILE A . n 
A 1 459 GLU 459 438 438 GLU GLU A . n 
A 1 460 SER 460 439 439 SER SER A . n 
A 1 461 GLY 461 440 440 GLY GLY A . n 
A 1 462 GLN 462 441 441 GLN GLN A . n 
A 1 463 ARG 463 442 442 ARG ARG A . n 
A 1 464 ALA 464 443 443 ALA ALA A . n 
A 1 465 ALA 465 444 444 ALA ALA A . n 
A 1 466 ALA 466 445 445 ALA ALA A . n 
A 1 467 GLU 467 446 446 GLU GLU A . n 
A 1 468 VAL 468 447 447 VAL VAL A . n 
A 1 469 LEU 469 448 448 LEU LEU A . n 
A 1 470 ALA 470 449 449 ALA ALA A . n 
A 1 471 ALA 471 450 450 ALA ALA A . n 
A 1 472 LEU 472 451 451 LEU LEU A . n 
A 1 473 GLY 473 452 452 GLY GLY A . n 
A 1 474 SER 474 453 ?   ?   ?   A . n 
B 1 1   MET 1   -20 ?   ?   ?   B . n 
B 1 2   GLY 2   -19 ?   ?   ?   B . n 
B 1 3   SER 3   -18 ?   ?   ?   B . n 
B 1 4   SER 4   -17 ?   ?   ?   B . n 
B 1 5   HIS 5   -16 ?   ?   ?   B . n 
B 1 6   HIS 6   -15 ?   ?   ?   B . n 
B 1 7   HIS 7   -14 ?   ?   ?   B . n 
B 1 8   HIS 8   -13 ?   ?   ?   B . n 
B 1 9   HIS 9   -12 ?   ?   ?   B . n 
B 1 10  HIS 10  -11 ?   ?   ?   B . n 
B 1 11  GLY 11  -10 ?   ?   ?   B . n 
B 1 12  SER 12  -9  ?   ?   ?   B . n 
B 1 13  GLY 13  -8  ?   ?   ?   B . n 
B 1 14  LEU 14  -7  ?   ?   ?   B . n 
B 1 15  VAL 15  -6  ?   ?   ?   B . n 
B 1 16  PRO 16  -5  ?   ?   ?   B . n 
B 1 17  ARG 17  -4  ?   ?   ?   B . n 
B 1 18  GLY 18  -3  ?   ?   ?   B . n 
B 1 19  SER 19  -2  ?   ?   ?   B . n 
B 1 20  ALA 20  -1  ?   ?   ?   B . n 
B 1 21  GLY 21  0   ?   ?   ?   B . n 
B 1 22  MET 22  1   ?   ?   ?   B . n 
B 1 23  PRO 23  2   ?   ?   ?   B . n 
B 1 24  SER 24  3   3   SER SER B . n 
B 1 25  GLU 25  4   4   GLU GLU 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 SPD ? ? SPD ? ? 'SUBJECT OF INVESTIGATION' ? 
3 4HA ? ? 4HA ? ? '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 GOL 1   502 601 GOL GOL A . 
E 4 13D 1   503 604 13D 13D A . 
F 5 4HA 1   504 605 4HA Z4L A . 
G 6 MG  1   505 606 MG  MG  A . 
H 2 FAD 1   501 600 FAD FAD B . 
I 7 SPD 1   502 601 SPD SPD B . 
J 3 GOL 1   503 602 GOL GOL B . 
K 3 GOL 1   504 603 GOL GOL B . 
L 6 MG  1   505 606 MG  MG  B . 
M 6 MG  1   506 607 MG  MG  B . 
N 8 HOH 1   601 509 HOH HOH A . 
N 8 HOH 2   602 304 HOH HOH A . 
N 8 HOH 3   603 318 HOH HOH A . 
N 8 HOH 4   604 514 HOH HOH A . 
N 8 HOH 5   605 306 HOH HOH A . 
N 8 HOH 6   606 25  HOH HOH A . 
N 8 HOH 7   607 326 HOH HOH A . 
N 8 HOH 8   608 37  HOH HOH A . 
N 8 HOH 9   609 419 HOH HOH A . 
N 8 HOH 10  610 483 HOH HOH A . 
N 8 HOH 11  611 393 HOH HOH A . 
N 8 HOH 12  612 238 HOH HOH A . 
N 8 HOH 13  613 283 HOH HOH A . 
N 8 HOH 14  614 17  HOH HOH A . 
N 8 HOH 15  615 291 HOH HOH A . 
N 8 HOH 16  616 199 HOH HOH A . 
N 8 HOH 17  617 72  HOH HOH A . 
N 8 HOH 18  618 392 HOH HOH A . 
N 8 HOH 19  619 370 HOH HOH A . 
N 8 HOH 20  620 43  HOH HOH A . 
N 8 HOH 21  621 432 HOH HOH A . 
N 8 HOH 22  622 170 HOH HOH A . 
N 8 HOH 23  623 40  HOH HOH A . 
N 8 HOH 24  624 11  HOH HOH A . 
N 8 HOH 25  625 68  HOH HOH A . 
N 8 HOH 26  626 429 HOH HOH A . 
N 8 HOH 27  627 235 HOH HOH A . 
N 8 HOH 28  628 271 HOH HOH A . 
N 8 HOH 29  629 315 HOH HOH A . 
N 8 HOH 30  630 272 HOH HOH A . 
N 8 HOH 31  631 95  HOH HOH A . 
N 8 HOH 32  632 252 HOH HOH A . 
N 8 HOH 33  633 119 HOH HOH A . 
N 8 HOH 34  634 49  HOH HOH A . 
N 8 HOH 35  635 154 HOH HOH A . 
N 8 HOH 36  636 107 HOH HOH A . 
N 8 HOH 37  637 251 HOH HOH A . 
N 8 HOH 38  638 341 HOH HOH A . 
N 8 HOH 39  639 27  HOH HOH A . 
N 8 HOH 40  640 365 HOH HOH A . 
N 8 HOH 41  641 38  HOH HOH A . 
N 8 HOH 42  642 244 HOH HOH A . 
N 8 HOH 43  643 446 HOH HOH A . 
N 8 HOH 44  644 247 HOH HOH A . 
N 8 HOH 45  645 208 HOH HOH A . 
N 8 HOH 46  646 91  HOH HOH A . 
N 8 HOH 47  647 302 HOH HOH A . 
N 8 HOH 48  648 329 HOH HOH A . 
N 8 HOH 49  649 123 HOH HOH A . 
N 8 HOH 50  650 180 HOH HOH A . 
N 8 HOH 51  651 213 HOH HOH A . 
N 8 HOH 52  652 371 HOH HOH A . 
N 8 HOH 53  653 482 HOH HOH A . 
N 8 HOH 54  654 410 HOH HOH A . 
N 8 HOH 55  655 189 HOH HOH A . 
N 8 HOH 56  656 427 HOH HOH A . 
N 8 HOH 57  657 366 HOH HOH A . 
N 8 HOH 58  658 223 HOH HOH A . 
N 8 HOH 59  659 66  HOH HOH A . 
N 8 HOH 60  660 406 HOH HOH A . 
N 8 HOH 61  661 116 HOH HOH A . 
N 8 HOH 62  662 484 HOH HOH A . 
N 8 HOH 63  663 290 HOH HOH A . 
N 8 HOH 64  664 19  HOH HOH A . 
N 8 HOH 65  665 87  HOH HOH A . 
N 8 HOH 66  666 451 HOH HOH A . 
N 8 HOH 67  667 441 HOH HOH A . 
N 8 HOH 68  668 232 HOH HOH A . 
N 8 HOH 69  669 112 HOH HOH A . 
N 8 HOH 70  670 75  HOH HOH A . 
N 8 HOH 71  671 73  HOH HOH A . 
N 8 HOH 72  672 103 HOH HOH A . 
N 8 HOH 73  673 63  HOH HOH A . 
N 8 HOH 74  674 84  HOH HOH A . 
N 8 HOH 75  675 192 HOH HOH A . 
N 8 HOH 76  676 352 HOH HOH A . 
N 8 HOH 77  677 166 HOH HOH A . 
N 8 HOH 78  678 340 HOH HOH A . 
N 8 HOH 79  679 303 HOH HOH A . 
N 8 HOH 80  680 188 HOH HOH A . 
N 8 HOH 81  681 241 HOH HOH A . 
N 8 HOH 82  682 117 HOH HOH A . 
N 8 HOH 83  683 372 HOH HOH A . 
N 8 HOH 84  684 70  HOH HOH A . 
N 8 HOH 85  685 115 HOH HOH A . 
N 8 HOH 86  686 69  HOH HOH A . 
N 8 HOH 87  687 442 HOH HOH A . 
N 8 HOH 88  688 288 HOH HOH A . 
N 8 HOH 89  689 29  HOH HOH A . 
N 8 HOH 90  690 6   HOH HOH A . 
N 8 HOH 91  691 124 HOH HOH A . 
N 8 HOH 92  692 242 HOH HOH A . 
N 8 HOH 93  693 268 HOH HOH A . 
N 8 HOH 94  694 163 HOH HOH A . 
N 8 HOH 95  695 195 HOH HOH A . 
N 8 HOH 96  696 450 HOH HOH A . 
N 8 HOH 97  697 313 HOH HOH A . 
N 8 HOH 98  698 448 HOH HOH A . 
N 8 HOH 99  699 512 HOH HOH A . 
N 8 HOH 100 700 239 HOH HOH A . 
N 8 HOH 101 701 89  HOH HOH A . 
N 8 HOH 102 702 4   HOH HOH A . 
N 8 HOH 103 703 221 HOH HOH A . 
N 8 HOH 104 704 128 HOH HOH A . 
N 8 HOH 105 705 216 HOH HOH A . 
N 8 HOH 106 706 131 HOH HOH A . 
N 8 HOH 107 707 99  HOH HOH A . 
N 8 HOH 108 708 428 HOH HOH A . 
N 8 HOH 109 709 504 HOH HOH A . 
N 8 HOH 110 710 159 HOH HOH A . 
N 8 HOH 111 711 61  HOH HOH A . 
N 8 HOH 112 712 80  HOH HOH A . 
N 8 HOH 113 713 486 HOH HOH A . 
N 8 HOH 114 714 135 HOH HOH A . 
N 8 HOH 115 715 190 HOH HOH A . 
N 8 HOH 116 716 2   HOH HOH A . 
N 8 HOH 117 717 45  HOH HOH A . 
N 8 HOH 118 718 152 HOH HOH A . 
N 8 HOH 119 719 285 HOH HOH A . 
N 8 HOH 120 720 356 HOH HOH A . 
N 8 HOH 121 721 488 HOH HOH A . 
N 8 HOH 122 722 106 HOH HOH A . 
N 8 HOH 123 723 109 HOH HOH A . 
N 8 HOH 124 724 74  HOH HOH A . 
N 8 HOH 125 725 184 HOH HOH A . 
N 8 HOH 126 726 55  HOH HOH A . 
N 8 HOH 127 727 26  HOH HOH A . 
N 8 HOH 128 728 187 HOH HOH A . 
N 8 HOH 129 729 360 HOH HOH A . 
N 8 HOH 130 730 438 HOH HOH A . 
N 8 HOH 131 731 447 HOH HOH A . 
N 8 HOH 132 732 3   HOH HOH A . 
N 8 HOH 133 733 256 HOH HOH A . 
N 8 HOH 134 734 60  HOH HOH A . 
N 8 HOH 135 735 260 HOH HOH A . 
N 8 HOH 136 736 97  HOH HOH A . 
N 8 HOH 137 737 485 HOH HOH A . 
N 8 HOH 138 738 156 HOH HOH A . 
N 8 HOH 139 739 383 HOH HOH A . 
N 8 HOH 140 740 36  HOH HOH A . 
N 8 HOH 141 741 141 HOH HOH A . 
N 8 HOH 142 742 90  HOH HOH A . 
N 8 HOH 143 743 155 HOH HOH A . 
N 8 HOH 144 744 413 HOH HOH A . 
N 8 HOH 145 745 171 HOH HOH A . 
N 8 HOH 146 746 1   HOH HOH A . 
N 8 HOH 147 747 102 HOH HOH A . 
N 8 HOH 148 748 59  HOH HOH A . 
N 8 HOH 149 749 56  HOH HOH A . 
N 8 HOH 150 750 369 HOH HOH A . 
N 8 HOH 151 751 206 HOH HOH A . 
N 8 HOH 152 752 481 HOH HOH A . 
N 8 HOH 153 753 82  HOH HOH A . 
N 8 HOH 154 754 335 HOH HOH A . 
N 8 HOH 155 755 153 HOH HOH A . 
N 8 HOH 156 756 47  HOH HOH A . 
N 8 HOH 157 757 98  HOH HOH A . 
N 8 HOH 158 758 298 HOH HOH A . 
N 8 HOH 159 759 214 HOH HOH A . 
N 8 HOH 160 760 133 HOH HOH A . 
N 8 HOH 161 761 226 HOH HOH A . 
N 8 HOH 162 762 227 HOH HOH A . 
N 8 HOH 163 763 494 HOH HOH A . 
N 8 HOH 164 764 46  HOH HOH A . 
N 8 HOH 165 765 310 HOH HOH A . 
N 8 HOH 166 766 201 HOH HOH A . 
N 8 HOH 167 767 279 HOH HOH A . 
N 8 HOH 168 768 77  HOH HOH A . 
N 8 HOH 169 769 322 HOH HOH A . 
N 8 HOH 170 770 144 HOH HOH A . 
N 8 HOH 171 771 254 HOH HOH A . 
N 8 HOH 172 772 266 HOH HOH A . 
N 8 HOH 173 773 289 HOH HOH A . 
N 8 HOH 174 774 125 HOH HOH A . 
N 8 HOH 175 775 342 HOH HOH A . 
N 8 HOH 176 776 362 HOH HOH A . 
N 8 HOH 177 777 431 HOH HOH A . 
N 8 HOH 178 778 220 HOH HOH A . 
N 8 HOH 179 779 9   HOH HOH A . 
N 8 HOH 180 780 332 HOH HOH A . 
N 8 HOH 181 781 330 HOH HOH A . 
N 8 HOH 182 782 287 HOH HOH A . 
N 8 HOH 183 783 408 HOH HOH A . 
N 8 HOH 184 784 217 HOH HOH A . 
N 8 HOH 185 785 248 HOH HOH A . 
N 8 HOH 186 786 186 HOH HOH A . 
N 8 HOH 187 787 30  HOH HOH A . 
N 8 HOH 188 788 333 HOH HOH A . 
N 8 HOH 189 789 493 HOH HOH A . 
N 8 HOH 190 790 339 HOH HOH A . 
N 8 HOH 191 791 215 HOH HOH A . 
N 8 HOH 192 792 18  HOH HOH A . 
N 8 HOH 193 793 174 HOH HOH A . 
N 8 HOH 194 794 243 HOH HOH A . 
N 8 HOH 195 795 250 HOH HOH A . 
N 8 HOH 196 796 33  HOH HOH A . 
N 8 HOH 197 797 407 HOH HOH A . 
N 8 HOH 198 798 137 HOH HOH A . 
N 8 HOH 199 799 168 HOH HOH A . 
N 8 HOH 200 800 445 HOH HOH A . 
N 8 HOH 201 801 262 HOH HOH A . 
N 8 HOH 202 802 200 HOH HOH A . 
N 8 HOH 203 803 225 HOH HOH A . 
N 8 HOH 204 804 132 HOH HOH A . 
N 8 HOH 205 805 425 HOH HOH A . 
N 8 HOH 206 806 282 HOH HOH A . 
N 8 HOH 207 807 169 HOH HOH A . 
N 8 HOH 208 808 402 HOH HOH A . 
N 8 HOH 209 809 94  HOH HOH A . 
N 8 HOH 210 810 202 HOH HOH A . 
N 8 HOH 211 811 113 HOH HOH A . 
N 8 HOH 212 812 354 HOH HOH A . 
N 8 HOH 213 813 111 HOH HOH A . 
N 8 HOH 214 814 31  HOH HOH A . 
N 8 HOH 215 815 219 HOH HOH A . 
N 8 HOH 216 816 358 HOH HOH A . 
N 8 HOH 217 817 207 HOH HOH A . 
N 8 HOH 218 818 477 HOH HOH A . 
N 8 HOH 219 819 194 HOH HOH A . 
N 8 HOH 220 820 85  HOH HOH A . 
N 8 HOH 221 821 439 HOH HOH A . 
N 8 HOH 222 822 385 HOH HOH A . 
N 8 HOH 223 823 323 HOH HOH A . 
N 8 HOH 224 824 422 HOH HOH A . 
N 8 HOH 225 825 414 HOH HOH A . 
N 8 HOH 226 826 398 HOH HOH A . 
N 8 HOH 227 827 236 HOH HOH A . 
N 8 HOH 228 828 146 HOH HOH A . 
N 8 HOH 229 829 449 HOH HOH A . 
N 8 HOH 230 830 487 HOH HOH A . 
N 8 HOH 231 831 404 HOH HOH A . 
N 8 HOH 232 832 479 HOH HOH A . 
N 8 HOH 233 833 39  HOH HOH A . 
N 8 HOH 234 834 35  HOH HOH A . 
N 8 HOH 235 835 20  HOH HOH A . 
N 8 HOH 236 836 320 HOH HOH A . 
N 8 HOH 237 837 299 HOH HOH A . 
N 8 HOH 238 838 92  HOH HOH A . 
N 8 HOH 239 839 478 HOH HOH A . 
N 8 HOH 240 840 455 HOH HOH A . 
N 8 HOH 241 841 472 HOH HOH A . 
N 8 HOH 242 842 466 HOH HOH A . 
N 8 HOH 243 843 218 HOH HOH A . 
N 8 HOH 244 844 468 HOH HOH A . 
N 8 HOH 245 845 476 HOH HOH A . 
N 8 HOH 246 846 278 HOH HOH A . 
N 8 HOH 247 847 460 HOH HOH A . 
N 8 HOH 248 848 518 HOH HOH A . 
N 8 HOH 249 849 461 HOH HOH A . 
N 8 HOH 250 850 513 HOH HOH A . 
N 8 HOH 251 851 469 HOH HOH A . 
N 8 HOH 252 852 443 HOH HOH A . 
N 8 HOH 253 853 364 HOH HOH A . 
N 8 HOH 254 854 515 HOH HOH A . 
N 8 HOH 255 855 517 HOH HOH A . 
N 8 HOH 256 856 138 HOH HOH A . 
N 8 HOH 257 857 470 HOH HOH A . 
N 8 HOH 258 858 240 HOH HOH A . 
N 8 HOH 259 859 516 HOH HOH A . 
N 8 HOH 260 860 305 HOH HOH A . 
N 8 HOH 261 861 228 HOH HOH A . 
N 8 HOH 262 862 456 HOH HOH A . 
N 8 HOH 263 863 374 HOH HOH A . 
N 8 HOH 264 864 474 HOH HOH A . 
N 8 HOH 265 865 473 HOH HOH A . 
N 8 HOH 266 866 367 HOH HOH A . 
N 8 HOH 267 867 337 HOH HOH A . 
N 8 HOH 268 868 319 HOH HOH A . 
N 8 HOH 269 869 317 HOH HOH A . 
N 8 HOH 270 870 269 HOH HOH A . 
N 8 HOH 271 871 401 HOH HOH A . 
N 8 HOH 272 872 261 HOH HOH A . 
N 8 HOH 273 873 245 HOH HOH A . 
N 8 HOH 274 874 118 HOH HOH A . 
O 8 HOH 1   601 510 HOH HOH B . 
O 8 HOH 2   602 409 HOH HOH B . 
O 8 HOH 3   603 21  HOH HOH B . 
O 8 HOH 4   604 122 HOH HOH B . 
O 8 HOH 5   605 295 HOH HOH B . 
O 8 HOH 6   606 24  HOH HOH B . 
O 8 HOH 7   607 234 HOH HOH B . 
O 8 HOH 8   608 423 HOH HOH B . 
O 8 HOH 9   609 173 HOH HOH B . 
O 8 HOH 10  610 164 HOH HOH B . 
O 8 HOH 11  611 324 HOH HOH B . 
O 8 HOH 12  612 389 HOH HOH B . 
O 8 HOH 13  613 182 HOH HOH B . 
O 8 HOH 14  614 108 HOH HOH B . 
O 8 HOH 15  615 28  HOH HOH B . 
O 8 HOH 16  616 10  HOH HOH B . 
O 8 HOH 17  617 411 HOH HOH B . 
O 8 HOH 18  618 397 HOH HOH B . 
O 8 HOH 19  619 204 HOH HOH B . 
O 8 HOH 20  620 505 HOH HOH B . 
O 8 HOH 21  621 130 HOH HOH B . 
O 8 HOH 22  622 506 HOH HOH B . 
O 8 HOH 23  623 311 HOH HOH B . 
O 8 HOH 24  624 368 HOH HOH B . 
O 8 HOH 25  625 399 HOH HOH B . 
O 8 HOH 26  626 390 HOH HOH B . 
O 8 HOH 27  627 378 HOH HOH B . 
O 8 HOH 28  628 105 HOH HOH B . 
O 8 HOH 29  629 309 HOH HOH B . 
O 8 HOH 30  630 172 HOH HOH B . 
O 8 HOH 31  631 8   HOH HOH B . 
O 8 HOH 32  632 490 HOH HOH B . 
O 8 HOH 33  633 300 HOH HOH B . 
O 8 HOH 34  634 185 HOH HOH B . 
O 8 HOH 35  635 14  HOH HOH B . 
O 8 HOH 36  636 336 HOH HOH B . 
O 8 HOH 37  637 57  HOH HOH B . 
O 8 HOH 38  638 151 HOH HOH B . 
O 8 HOH 39  639 492 HOH HOH B . 
O 8 HOH 40  640 54  HOH HOH B . 
O 8 HOH 41  641 387 HOH HOH B . 
O 8 HOH 42  642 79  HOH HOH B . 
O 8 HOH 43  643 307 HOH HOH B . 
O 8 HOH 44  644 418 HOH HOH B . 
O 8 HOH 45  645 440 HOH HOH B . 
O 8 HOH 46  646 233 HOH HOH B . 
O 8 HOH 47  647 350 HOH HOH B . 
O 8 HOH 48  648 286 HOH HOH B . 
O 8 HOH 49  649 433 HOH HOH B . 
O 8 HOH 50  650 65  HOH HOH B . 
O 8 HOH 51  651 212 HOH HOH B . 
O 8 HOH 52  652 349 HOH HOH B . 
O 8 HOH 53  653 495 HOH HOH B . 
O 8 HOH 54  654 126 HOH HOH B . 
O 8 HOH 55  655 83  HOH HOH B . 
O 8 HOH 56  656 142 HOH HOH B . 
O 8 HOH 57  657 15  HOH HOH B . 
O 8 HOH 58  658 76  HOH HOH B . 
O 8 HOH 59  659 62  HOH HOH B . 
O 8 HOH 60  660 277 HOH HOH B . 
O 8 HOH 61  661 381 HOH HOH B . 
O 8 HOH 62  662 120 HOH HOH B . 
O 8 HOH 63  663 314 HOH HOH B . 
O 8 HOH 64  664 284 HOH HOH B . 
O 8 HOH 65  665 5   HOH HOH B . 
O 8 HOH 66  666 380 HOH HOH B . 
O 8 HOH 67  667 67  HOH HOH B . 
O 8 HOH 68  668 430 HOH HOH B . 
O 8 HOH 69  669 32  HOH HOH B . 
O 8 HOH 70  670 355 HOH HOH B . 
O 8 HOH 71  671 265 HOH HOH B . 
O 8 HOH 72  672 275 HOH HOH B . 
O 8 HOH 73  673 34  HOH HOH B . 
O 8 HOH 74  674 345 HOH HOH B . 
O 8 HOH 75  675 420 HOH HOH B . 
O 8 HOH 76  676 181 HOH HOH B . 
O 8 HOH 77  677 93  HOH HOH B . 
O 8 HOH 78  678 140 HOH HOH B . 
O 8 HOH 79  679 259 HOH HOH B . 
O 8 HOH 80  680 253 HOH HOH B . 
O 8 HOH 81  681 415 HOH HOH B . 
O 8 HOH 82  682 48  HOH HOH B . 
O 8 HOH 83  683 100 HOH HOH B . 
O 8 HOH 84  684 198 HOH HOH B . 
O 8 HOH 85  685 501 HOH HOH B . 
O 8 HOH 86  686 78  HOH HOH B . 
O 8 HOH 87  687 437 HOH HOH B . 
O 8 HOH 88  688 42  HOH HOH B . 
O 8 HOH 89  689 23  HOH HOH B . 
O 8 HOH 90  690 263 HOH HOH B . 
O 8 HOH 91  691 110 HOH HOH B . 
O 8 HOH 92  692 499 HOH HOH B . 
O 8 HOH 93  693 281 HOH HOH B . 
O 8 HOH 94  694 176 HOH HOH B . 
O 8 HOH 95  695 255 HOH HOH B . 
O 8 HOH 96  696 357 HOH HOH B . 
O 8 HOH 97  697 258 HOH HOH B . 
O 8 HOH 98  698 377 HOH HOH B . 
O 8 HOH 99  699 496 HOH HOH B . 
O 8 HOH 100 700 257 HOH HOH B . 
O 8 HOH 101 701 327 HOH HOH B . 
O 8 HOH 102 702 264 HOH HOH B . 
O 8 HOH 103 703 511 HOH HOH B . 
O 8 HOH 104 704 44  HOH HOH B . 
O 8 HOH 105 705 276 HOH HOH B . 
O 8 HOH 106 706 403 HOH HOH B . 
O 8 HOH 107 707 209 HOH HOH B . 
O 8 HOH 108 708 16  HOH HOH B . 
O 8 HOH 109 709 421 HOH HOH B . 
O 8 HOH 110 710 361 HOH HOH B . 
O 8 HOH 111 711 498 HOH HOH B . 
O 8 HOH 112 712 267 HOH HOH B . 
O 8 HOH 113 713 452 HOH HOH B . 
O 8 HOH 114 714 150 HOH HOH B . 
O 8 HOH 115 715 417 HOH HOH B . 
O 8 HOH 116 716 312 HOH HOH B . 
O 8 HOH 117 717 147 HOH HOH B . 
O 8 HOH 118 718 12  HOH HOH B . 
O 8 HOH 119 719 127 HOH HOH B . 
O 8 HOH 120 720 165 HOH HOH B . 
O 8 HOH 121 721 203 HOH HOH B . 
O 8 HOH 122 722 502 HOH HOH B . 
O 8 HOH 123 723 400 HOH HOH B . 
O 8 HOH 124 724 224 HOH HOH B . 
O 8 HOH 125 725 129 HOH HOH B . 
O 8 HOH 126 726 344 HOH HOH B . 
O 8 HOH 127 727 114 HOH HOH B . 
O 8 HOH 128 728 193 HOH HOH B . 
O 8 HOH 129 729 376 HOH HOH B . 
O 8 HOH 130 730 41  HOH HOH B . 
O 8 HOH 131 731 158 HOH HOH B . 
O 8 HOH 132 732 297 HOH HOH B . 
O 8 HOH 133 733 375 HOH HOH B . 
O 8 HOH 134 734 51  HOH HOH B . 
O 8 HOH 135 735 88  HOH HOH B . 
O 8 HOH 136 736 53  HOH HOH B . 
O 8 HOH 137 737 489 HOH HOH B . 
O 8 HOH 138 738 197 HOH HOH B . 
O 8 HOH 139 739 13  HOH HOH B . 
O 8 HOH 140 740 338 HOH HOH B . 
O 8 HOH 141 741 121 HOH HOH B . 
O 8 HOH 142 742 7   HOH HOH B . 
O 8 HOH 143 743 373 HOH HOH B . 
O 8 HOH 144 744 273 HOH HOH B . 
O 8 HOH 145 745 222 HOH HOH B . 
O 8 HOH 146 746 134 HOH HOH B . 
O 8 HOH 147 747 205 HOH HOH B . 
O 8 HOH 148 748 177 HOH HOH B . 
O 8 HOH 149 749 328 HOH HOH B . 
O 8 HOH 150 750 270 HOH HOH B . 
O 8 HOH 151 751 346 HOH HOH B . 
O 8 HOH 152 752 382 HOH HOH B . 
O 8 HOH 153 753 161 HOH HOH B . 
O 8 HOH 154 754 343 HOH HOH B . 
O 8 HOH 155 755 160 HOH HOH B . 
O 8 HOH 156 756 249 HOH HOH B . 
O 8 HOH 157 757 210 HOH HOH B . 
O 8 HOH 158 758 292 HOH HOH B . 
O 8 HOH 159 759 334 HOH HOH B . 
O 8 HOH 160 760 143 HOH HOH B . 
O 8 HOH 161 761 52  HOH HOH B . 
O 8 HOH 162 762 179 HOH HOH B . 
O 8 HOH 163 763 293 HOH HOH B . 
O 8 HOH 164 764 491 HOH HOH B . 
O 8 HOH 165 765 157 HOH HOH B . 
O 8 HOH 166 766 500 HOH HOH B . 
O 8 HOH 167 767 379 HOH HOH B . 
O 8 HOH 168 768 325 HOH HOH B . 
O 8 HOH 169 769 86  HOH HOH B . 
O 8 HOH 170 770 136 HOH HOH B . 
O 8 HOH 171 771 331 HOH HOH B . 
O 8 HOH 172 772 386 HOH HOH B . 
O 8 HOH 173 773 175 HOH HOH B . 
O 8 HOH 174 774 145 HOH HOH B . 
O 8 HOH 175 775 316 HOH HOH B . 
O 8 HOH 176 776 321 HOH HOH B . 
O 8 HOH 177 777 394 HOH HOH B . 
O 8 HOH 178 778 71  HOH HOH B . 
O 8 HOH 179 779 139 HOH HOH B . 
O 8 HOH 180 780 280 HOH HOH B . 
O 8 HOH 181 781 96  HOH HOH B . 
O 8 HOH 182 782 64  HOH HOH B . 
O 8 HOH 183 783 104 HOH HOH B . 
O 8 HOH 184 784 351 HOH HOH B . 
O 8 HOH 185 785 183 HOH HOH B . 
O 8 HOH 186 786 196 HOH HOH B . 
O 8 HOH 187 787 231 HOH HOH B . 
O 8 HOH 188 788 436 HOH HOH B . 
O 8 HOH 189 789 237 HOH HOH B . 
O 8 HOH 190 790 149 HOH HOH B . 
O 8 HOH 191 791 405 HOH HOH B . 
O 8 HOH 192 792 274 HOH HOH B . 
O 8 HOH 193 793 384 HOH HOH B . 
O 8 HOH 194 794 101 HOH HOH B . 
O 8 HOH 195 795 50  HOH HOH B . 
O 8 HOH 196 796 416 HOH HOH B . 
O 8 HOH 197 797 391 HOH HOH B . 
O 8 HOH 198 798 497 HOH HOH B . 
O 8 HOH 199 799 363 HOH HOH B . 
O 8 HOH 200 800 444 HOH HOH B . 
O 8 HOH 201 801 167 HOH HOH B . 
O 8 HOH 202 802 424 HOH HOH B . 
O 8 HOH 203 803 162 HOH HOH B . 
O 8 HOH 204 804 246 HOH HOH B . 
O 8 HOH 205 805 347 HOH HOH B . 
O 8 HOH 206 806 507 HOH HOH B . 
O 8 HOH 207 807 58  HOH HOH B . 
O 8 HOH 208 808 457 HOH HOH B . 
O 8 HOH 209 809 503 HOH HOH B . 
O 8 HOH 210 810 81  HOH HOH B . 
O 8 HOH 211 811 348 HOH HOH B . 
O 8 HOH 212 812 426 HOH HOH B . 
O 8 HOH 213 813 467 HOH HOH B . 
O 8 HOH 214 814 230 HOH HOH B . 
O 8 HOH 215 815 459 HOH HOH B . 
O 8 HOH 216 816 465 HOH HOH B . 
O 8 HOH 217 817 454 HOH HOH B . 
O 8 HOH 218 818 458 HOH HOH B . 
O 8 HOH 219 819 396 HOH HOH B . 
O 8 HOH 220 820 388 HOH HOH B . 
O 8 HOH 221 821 480 HOH HOH B . 
O 8 HOH 222 822 301 HOH HOH B . 
O 8 HOH 223 823 508 HOH HOH B . 
O 8 HOH 224 824 434 HOH HOH B . 
O 8 HOH 225 825 520 HOH HOH B . 
O 8 HOH 226 826 395 HOH HOH B . 
O 8 HOH 227 827 191 HOH HOH B . 
O 8 HOH 228 828 464 HOH HOH B . 
O 8 HOH 229 829 453 HOH HOH B . 
O 8 HOH 230 830 435 HOH HOH B . 
O 8 HOH 231 831 462 HOH HOH B . 
O 8 HOH 232 832 211 HOH HOH B . 
O 8 HOH 233 833 294 HOH HOH B . 
O 8 HOH 234 834 359 HOH HOH B . 
O 8 HOH 235 835 148 HOH HOH B . 
O 8 HOH 236 836 519 HOH HOH B . 
O 8 HOH 237 837 308 HOH HOH B . 
O 8 HOH 238 838 353 HOH HOH B . 
O 8 HOH 239 839 475 HOH HOH B . 
O 8 HOH 240 840 229 HOH HOH B . 
O 8 HOH 241 841 296 HOH HOH B . 
O 8 HOH 242 842 412 HOH HOH B . 
O 8 HOH 243 843 178 HOH HOH B . 
O 8 HOH 244 844 471 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                     9H5Q 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     68.335 
_cell.length_a_esd                 ? 
_cell.length_b                     94.456 
_cell.length_b_esd                 ? 
_cell.length_c                     127.740 
_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                         9H5Q 
_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                   9H5Q 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.06 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.22 
_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                                       9H5Q 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               63.95 
_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                                     77126 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                19.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.3 
_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                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.8 
_reflns_shell.d_res_low                                     1.847 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4508 
_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                                  0.839 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.26 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.11 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.15 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.157 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.970 
_refine.correlation_coeff_Fo_to_Fc_free          0.957 
_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                                 9H5Q 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             63.95 
_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                     73229 
_refine.ls_number_reflns_R_free                  3823 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.72 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.15548 
_refine.ls_R_factor_R_free                       0.18933 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15378 
_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                       0.116 
_refine.pdbx_overall_ESU_R_Free                  0.110 
_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                             2.352 
_refine.overall_SU_ML                            0.072 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        63.95 
_refine_hist.number_atoms_solvent             518 
_refine_hist.number_atoms_total               7381 
_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        6715 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         148 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.013  7047  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.017  6521  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.708  1.668  9656  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.941  1.587  14941 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.264  5.000  900   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 28.800 20.343 379   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.371 15.000 957   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.601 15.000 71    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.083  0.200  888   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  8094  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1610  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.790  2.141  3594  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.781  2.139  3592  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.358  3.203  4490  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.361  3.203  4490  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.985  2.463  3453  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.985  2.464  3454  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.495  3.566  5165  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.200  25.710 7789  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.147  25.499 7697  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.800 
_refine_ls_shell.d_res_low                        1.847 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             284 
_refine_ls_shell.number_reflns_R_work             5375 
_refine_ls_shell.percent_reflns_obs               100.00 
_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                  0.232 
_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                  0.301 
# 
_struct.entry_id                     9H5Q 
_struct.title                        
'Crystal structure of Thermoanaerobacterales bacterium monoamine oxidase in complex with spermidine and its oxidation products' 
_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        9H5Q 
_struct_keywords.text            'monoamine oxidase, Thermoanaerobacterales bacterium, enzyme, spermidine, FLAVOPROTEIN' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 2 ? 
I N N 7 ? 
J N N 3 ? 
K N N 3 ? 
L N N 6 ? 
M N N 6 ? 
N N N 8 ? 
O N N 8 ? 
# 
_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 9H5Q A 22 ? 474 ? A0AAJ6N6J2 1 ? 453 ? 1 453 
2 1 9H5Q 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 9H5Q MET A 1  ? UNP A0AAJ6N6J2 ? ? 'initiating methionine' -20 1  
1 9H5Q GLY A 2  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -19 2  
1 9H5Q SER A 3  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -18 3  
1 9H5Q SER A 4  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -17 4  
1 9H5Q HIS A 5  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -16 5  
1 9H5Q HIS A 6  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -15 6  
1 9H5Q HIS A 7  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -14 7  
1 9H5Q HIS A 8  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -13 8  
1 9H5Q HIS A 9  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -12 9  
1 9H5Q HIS A 10 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -11 10 
1 9H5Q GLY A 11 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -10 11 
1 9H5Q SER A 12 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -9  12 
1 9H5Q GLY A 13 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -8  13 
1 9H5Q LEU A 14 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -7  14 
1 9H5Q VAL A 15 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -6  15 
1 9H5Q PRO A 16 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -5  16 
1 9H5Q ARG A 17 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -4  17 
1 9H5Q GLY A 18 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -3  18 
1 9H5Q SER A 19 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -2  19 
1 9H5Q ALA A 20 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -1  20 
1 9H5Q GLY A 21 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        0   21 
2 9H5Q MET B 1  ? UNP A0AAJ6N6J2 ? ? 'initiating methionine' -20 22 
2 9H5Q GLY B 2  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -19 23 
2 9H5Q SER B 3  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -18 24 
2 9H5Q SER B 4  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -17 25 
2 9H5Q HIS B 5  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -16 26 
2 9H5Q HIS B 6  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -15 27 
2 9H5Q HIS B 7  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -14 28 
2 9H5Q HIS B 8  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -13 29 
2 9H5Q HIS B 9  ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -12 30 
2 9H5Q HIS B 10 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -11 31 
2 9H5Q GLY B 11 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -10 32 
2 9H5Q SER B 12 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -9  33 
2 9H5Q GLY B 13 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -8  34 
2 9H5Q LEU B 14 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -7  35 
2 9H5Q VAL B 15 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -6  36 
2 9H5Q PRO B 16 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -5  37 
2 9H5Q ARG B 17 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -4  38 
2 9H5Q GLY B 18 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -3  39 
2 9H5Q SER B 19 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -2  40 
2 9H5Q ALA B 20 ? UNP A0AAJ6N6J2 ? ? 'expression tag'        -1  41 
2 9H5Q 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)' 8270  ? 
1 MORE         -47   ? 
1 'SSA (A^2)'  29860 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 35  ? ALA A 48  ? GLY A 14  ALA A 27  1 ? 14 
HELX_P HELX_P2  AA2 GLN A 86  ? GLY A 97  ? GLN A 65  GLY A 76  1 ? 12 
HELX_P HELX_P3  AA3 ASP A 123 ? PHE A 128 ? ASP A 102 PHE A 107 5 ? 6  
HELX_P HELX_P4  AA4 SER A 129 ? GLU A 148 ? SER A 108 GLU A 127 1 ? 20 
HELX_P HELX_P5  AA5 ALA A 154 ? ALA A 158 ? ALA A 133 ALA A 137 5 ? 5  
HELX_P HELX_P6  AA6 GLU A 160 ? 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 ? ILE A 293 ? PRO A 265 ILE A 272 1 ? 8  
HELX_P HELX_P13 AB4 PRO A 300 ? HIS A 309 ? PRO A 279 HIS A 288 1 ? 10 
HELX_P HELX_P14 AB5 PRO A 325 ? GLU A 330 ? PRO A 304 GLU A 309 5 ? 6  
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 SER A 407 ? GLU A 409 ? SER A 386 GLU A 388 5 ? 3  
HELX_P HELX_P19 AC1 GLY A 423 ? TYR A 428 ? GLY A 402 TYR A 407 1 ? 6  
HELX_P HELX_P20 AC2 GLY A 429 ? LEU A 432 ? GLY A 408 LEU A 411 5 ? 4  
HELX_P HELX_P21 AC3 GLY A 443 ? ALA A 447 ? GLY A 422 ALA A 426 5 ? 5  
HELX_P HELX_P22 AC4 TYR A 453 ? GLY A 473 ? TYR A 432 GLY A 452 1 ? 21 
HELX_P HELX_P23 AC5 GLY B 35  ? ALA B 48  ? GLY B 14  ALA B 27  1 ? 14 
HELX_P HELX_P24 AC6 GLN B 86  ? LEU B 96  ? GLN B 65  LEU B 75  1 ? 11 
HELX_P HELX_P25 AC7 ASP B 123 ? PHE B 128 ? ASP B 102 PHE B 107 5 ? 6  
HELX_P HELX_P26 AC8 SER B 129 ? LYS B 149 ? SER B 108 LYS B 128 1 ? 21 
HELX_P HELX_P27 AC9 ALA B 154 ? ALA B 158 ? ALA B 133 ALA B 137 5 ? 5  
HELX_P HELX_P28 AD1 GLU B 160 ? ALA B 166 ? GLU B 139 ALA B 145 1 ? 7  
HELX_P HELX_P29 AD2 THR B 168 ? THR B 176 ? THR B 147 THR B 155 1 ? 9  
HELX_P HELX_P30 AD3 PRO B 179 ? ALA B 195 ? PRO B 158 ALA B 174 1 ? 17 
HELX_P HELX_P31 AD4 SER B 202 ? GLY B 214 ? SER B 181 GLY B 193 1 ? 13 
HELX_P HELX_P32 AD5 GLY B 215 ? ASP B 221 ? GLY B 194 ASP B 200 1 ? 7  
HELX_P HELX_P33 AD6 VAL B 235 ? ALA B 244 ? VAL B 214 ALA B 223 1 ? 10 
HELX_P HELX_P34 AD7 PRO B 286 ? GLY B 291 ? PRO B 265 GLY B 270 1 ? 6  
HELX_P HELX_P35 AD8 PRO B 300 ? HIS B 309 ? PRO B 279 HIS B 288 1 ? 10 
HELX_P HELX_P36 AD9 PRO B 325 ? GLU B 330 ? PRO B 304 GLU B 309 5 ? 6  
HELX_P HELX_P37 AE1 GLY B 365 ? ALA B 373 ? GLY B 344 ALA B 352 1 ? 9  
HELX_P HELX_P38 AE2 THR B 375 ? LEU B 391 ? THR B 354 LEU B 370 1 ? 17 
HELX_P HELX_P39 AE3 GLY B 392 ? ASP B 397 ? GLY B 371 ASP B 376 5 ? 6  
HELX_P HELX_P40 AE4 GLY B 423 ? TYR B 428 ? GLY B 402 TYR B 407 1 ? 6  
HELX_P HELX_P41 AE5 GLY B 429 ? LEU B 432 ? GLY B 408 LEU B 411 5 ? 4  
HELX_P HELX_P42 AE6 GLY B 443 ? ALA B 447 ? GLY B 422 ALA B 426 5 ? 5  
HELX_P HELX_P43 AE7 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 ? ? ? ? ? ? ? 1.700 ? ? 
covale2  covale none ? B CYS 415 SG  ? ? ? 1_555 H FAD . C8M ? ? B CYS 394 B FAD 501 1_555 ? ? ? ? ? ? ? 1.702 ? ? 
metalc1  metalc ?    ? A THR 105 O   ? ? ? 1_555 G MG  . MG  ? ? A THR 84  A MG  505 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc2  metalc ?    ? G MG  .   MG  ? ? ? 1_555 N HOH . O   ? ? A MG  505 A HOH 662 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc3  metalc ?    ? G MG  .   MG  ? ? ? 1_555 N HOH . O   ? ? A MG  505 A HOH 713 1_555 ? ? ? ? ? ? ? 2.099 ? ? 
metalc4  metalc ?    ? G MG  .   MG  ? ? ? 1_555 N HOH . O   ? ? A MG  505 A HOH 737 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc5  metalc ?    ? G MG  .   MG  ? ? ? 1_555 N HOH . O   ? ? A MG  505 A HOH 758 1_555 ? ? ? ? ? ? ? 1.987 ? ? 
metalc6  metalc ?    ? G MG  .   MG  ? ? ? 1_555 N HOH . O   ? ? A MG  505 A HOH 830 1_555 ? ? ? ? ? ? ? 2.207 ? ? 
metalc7  metalc ?    ? N HOH .   O   ? ? ? 1_655 M MG  . MG  ? ? A HOH 721 B MG  506 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc8  metalc ?    ? B THR 105 O   ? ? ? 1_555 L MG  . MG  ? ? B THR 84  B MG  505 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc9  metalc ?    ? B GLU 148 OE1 ? ? ? 1_555 M MG  . MG  ? ? B GLU 127 B MG  506 1_555 ? ? ? ? ? ? ? 1.942 ? ? 
metalc10 metalc ?    ? L MG  .   MG  ? ? ? 1_555 O HOH . O   ? ? B MG  505 B HOH 653 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
metalc11 metalc ?    ? L MG  .   MG  ? ? ? 1_555 O HOH . O   ? ? B MG  505 B HOH 692 1_555 ? ? ? ? ? ? ? 2.090 ? ? 
metalc12 metalc ?    ? L MG  .   MG  ? ? ? 1_555 O HOH . O   ? ? B MG  505 B HOH 699 1_555 ? ? ? ? ? ? ? 2.183 ? ? 
metalc13 metalc ?    ? L MG  .   MG  ? ? ? 1_555 O HOH . O   ? ? B MG  505 B HOH 711 1_555 ? ? ? ? ? ? ? 1.980 ? ? 
metalc14 metalc ?    ? L MG  .   MG  ? ? ? 1_555 O HOH . O   ? ? B MG  505 B HOH 798 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc15 metalc ?    ? M MG  .   MG  ? ? ? 1_555 O HOH . O   ? ? B MG  506 B HOH 632 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc16 metalc ?    ? M MG  .   MG  ? ? ? 1_555 O HOH . O   ? ? B MG  506 B HOH 737 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc17 metalc ?    ? M MG  .   MG  ? ? ? 1_555 O HOH . O   ? ? B MG  506 B HOH 764 1_555 ? ? ? ? ? ? ? 1.933 ? ? 
# 
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 ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 662 ? 1_555 177.6 ? 
2  O   ? A THR 105 ? A THR 84  ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 713 ? 1_555 89.7  ? 
3  O   ? N HOH .   ? A HOH 662 ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 713 ? 1_555 88.4  ? 
4  O   ? A THR 105 ? A THR 84  ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 737 ? 1_555 88.2  ? 
5  O   ? N HOH .   ? A HOH 662 ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 737 ? 1_555 90.6  ? 
6  O   ? N HOH .   ? A HOH 713 ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 737 ? 1_555 95.0  ? 
7  O   ? A THR 105 ? A THR 84  ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 758 ? 1_555 88.2  ? 
8  O   ? N HOH .   ? A HOH 662 ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 758 ? 1_555 93.7  ? 
9  O   ? N HOH .   ? A HOH 713 ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 758 ? 1_555 176.5 ? 
10 O   ? N HOH .   ? A HOH 737 ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 758 ? 1_555 87.7  ? 
11 O   ? A THR 105 ? A THR 84  ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 830 ? 1_555 94.0  ? 
12 O   ? N HOH .   ? A HOH 662 ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 830 ? 1_555 87.3  ? 
13 O   ? N HOH .   ? A HOH 713 ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 830 ? 1_555 85.8  ? 
14 O   ? N HOH .   ? A HOH 737 ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 830 ? 1_555 177.7 ? 
15 O   ? N HOH .   ? A HOH 758 ? 1_555 MG ? G MG . ? A MG 505 ? 1_555 O   ? N HOH .   ? A HOH 830 ? 1_555 91.6  ? 
16 O   ? N HOH .   ? A HOH 721 ? 1_655 MG ? M MG . ? B MG 506 ? 1_555 OE1 ? B GLU 148 ? B GLU 127 ? 1_555 89.8  ? 
17 O   ? N HOH .   ? A HOH 721 ? 1_655 MG ? M MG . ? B MG 506 ? 1_555 O   ? O HOH .   ? B HOH 632 ? 1_555 85.5  ? 
18 OE1 ? B GLU 148 ? B GLU 127 ? 1_555 MG ? M MG . ? B MG 506 ? 1_555 O   ? O HOH .   ? B HOH 632 ? 1_555 86.9  ? 
19 O   ? N HOH .   ? A HOH 721 ? 1_655 MG ? M MG . ? B MG 506 ? 1_555 O   ? O HOH .   ? B HOH 737 ? 1_555 91.5  ? 
20 OE1 ? B GLU 148 ? B GLU 127 ? 1_555 MG ? M MG . ? B MG 506 ? 1_555 O   ? O HOH .   ? B HOH 737 ? 1_555 89.8  ? 
21 O   ? O HOH .   ? B HOH 632 ? 1_555 MG ? M MG . ? B MG 506 ? 1_555 O   ? O HOH .   ? B HOH 737 ? 1_555 175.6 ? 
22 O   ? N HOH .   ? A HOH 721 ? 1_655 MG ? M MG . ? B MG 506 ? 1_555 O   ? O HOH .   ? B HOH 764 ? 1_555 89.7  ? 
23 OE1 ? B GLU 148 ? B GLU 127 ? 1_555 MG ? M MG . ? B MG 506 ? 1_555 O   ? O HOH .   ? B HOH 764 ? 1_555 177.2 ? 
24 O   ? O HOH .   ? B HOH 632 ? 1_555 MG ? M MG . ? B MG 506 ? 1_555 O   ? O HOH .   ? B HOH 764 ? 1_555 90.3  ? 
25 O   ? O HOH .   ? B HOH 737 ? 1_555 MG ? M MG . ? B MG 506 ? 1_555 O   ? O HOH .   ? B HOH 764 ? 1_555 92.9  ? 
26 O   ? B THR 105 ? B THR 84  ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 653 ? 1_555 171.4 ? 
27 O   ? B THR 105 ? B THR 84  ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 692 ? 1_555 85.5  ? 
28 O   ? O HOH .   ? B HOH 653 ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 692 ? 1_555 86.0  ? 
29 O   ? B THR 105 ? B THR 84  ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 699 ? 1_555 87.5  ? 
30 O   ? O HOH .   ? B HOH 653 ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 699 ? 1_555 91.9  ? 
31 O   ? O HOH .   ? B HOH 692 ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 699 ? 1_555 90.5  ? 
32 O   ? B THR 105 ? B THR 84  ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 711 ? 1_555 88.6  ? 
33 O   ? O HOH .   ? B HOH 653 ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 711 ? 1_555 93.0  ? 
34 O   ? O HOH .   ? B HOH 692 ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 711 ? 1_555 96.2  ? 
35 O   ? O HOH .   ? B HOH 699 ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 711 ? 1_555 171.9 ? 
36 O   ? B THR 105 ? B THR 84  ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 798 ? 1_555 96.1  ? 
37 O   ? O HOH .   ? B HOH 653 ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 798 ? 1_555 92.4  ? 
38 O   ? O HOH .   ? B HOH 692 ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 798 ? 1_555 177.9 ? 
39 O   ? O HOH .   ? B HOH 699 ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 798 ? 1_555 88.1  ? 
40 O   ? O HOH .   ? B HOH 711 ? 1_555 MG ? L MG . ? B MG 505 ? 1_555 O   ? O HOH .   ? B HOH 798 ? 1_555 85.3  ? 
# 
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 H . ? CYS B 415 ? FAD B 501 ? 1_555 CYS B 394 ? 1_555 C8M SG CYS 3 FAD None Flavin 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASP 296 A . ? ASP 275 A PRO 297 A ? PRO 276 A 1 -3.36 
2 THR 355 A . ? THR 334 A PRO 356 A ? PRO 335 A 1 -7.94 
3 CYS 415 A . ? CYS 394 A TYR 416 A ? TYR 395 A 1 -1.80 
4 ASP 296 B . ? ASP 275 B PRO 297 B ? PRO 276 B 1 -3.53 
5 THR 355 B . ? THR 334 B PRO 356 B ? PRO 335 B 1 -6.96 
6 CYS 415 B . ? CYS 394 B TYR 416 B ? TYR 395 B 1 -0.28 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 3 ? 
AA6 ? 4 ? 
AA7 ? 7 ? 
AA8 ? 5 ? 
AA9 ? 2 ? 
AB1 ? 3 ? 
AB2 ? 3 ? 
AB3 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA7 6 7 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? parallel      
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 251 ? ARG A 252 ? LEU A 230 ARG A 231 
AA1 2 VAL A 52  ? LEU A 55  ? VAL A 31  LEU A 34  
AA1 3 VAL A 27  ? VAL A 32  ? VAL A 6   VAL A 11  
AA1 4 GLY A 274 ? VAL A 283 ? GLY A 253 VAL A 262 
AA1 5 GLY A 266 ? THR A 271 ? GLY A 245 THR A 250 
AA1 6 VAL A 257 ? ASP A 263 ? VAL A 236 ASP A 242 
AA1 7 ASP A 294 ? ASP A 296 ? ASP A 273 ASP A 275 
AA2 1 LEU A 251 ? ARG A 252 ? LEU A 230 ARG A 231 
AA2 2 VAL A 52  ? LEU A 55  ? VAL A 31  LEU A 34  
AA2 3 VAL A 27  ? VAL A 32  ? VAL A 6   VAL A 11  
AA2 4 GLY A 274 ? VAL A 283 ? GLY A 253 VAL A 262 
AA2 5 VAL A 439 ? TRP A 441 ? VAL A 418 TRP A 420 
AA3 1 THR A 67  ? HIS A 70  ? THR A 46  HIS A 49  
AA3 2 THR A 73  ? ASP A 76  ? THR A 52  ASP A 55  
AA4 1 TRP A 81  ? ILE A 82  ? TRP A 60  ILE A 61  
AA4 2 ASP A 229 ? LEU A 231 ? ASP A 208 LEU A 210 
AA4 3 THR A 100 ? PRO A 102 ? THR A 79  PRO A 81  
AA5 1 GLN A 119 ? ALA A 121 ? GLN A 98  ALA A 100 
AA5 2 ASP A 108 ? VAL A 111 ? ASP A 87  VAL A 90  
AA5 3 LEU A 332 ? LEU A 337 ? LEU A 311 LEU A 316 
AA6 1 PHE A 347 ? ASP A 348 ? PHE A 326 ASP A 327 
AA6 2 GLY A 357 ? GLU A 364 ? GLY A 336 GLU A 343 
AA6 3 VAL A 315 ? TYR A 322 ? VAL A 294 TYR A 301 
AA6 4 ASP A 400 ? ASP A 405 ? ASP A 379 ASP A 384 
AA7 1 LEU B 251 ? ARG B 252 ? LEU B 230 ARG B 231 
AA7 2 VAL B 52  ? LEU B 55  ? VAL B 31  LEU B 34  
AA7 3 GLN B 26  ? VAL B 32  ? GLN B 5   VAL B 11  
AA7 4 GLU B 275 ? VAL B 283 ? GLU B 254 VAL B 262 
AA7 5 VAL B 267 ? ARG B 270 ? VAL B 246 ARG B 249 
AA7 6 GLY B 259 ? GLN B 262 ? GLY B 238 GLN B 241 
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 GLN B 26  ? VAL B 32  ? GLN B 5   VAL B 11  
AA8 4 GLU B 275 ? VAL B 283 ? GLU B 254 VAL B 262 
AA8 5 VAL B 439 ? TRP B 441 ? VAL B 418 TRP B 420 
AA9 1 THR B 67  ? HIS B 70  ? THR B 46  HIS B 49  
AA9 2 THR B 73  ? ASP B 76  ? THR B 52  ASP B 55  
AB1 1 TRP B 81  ? ILE B 82  ? TRP B 60  ILE B 61  
AB1 2 ASP B 229 ? LEU B 231 ? ASP B 208 LEU B 210 
AB1 3 THR B 100 ? PRO B 102 ? THR B 79  PRO B 81  
AB2 1 GLN B 119 ? ALA B 121 ? GLN B 98  ALA B 100 
AB2 2 ASP B 108 ? VAL B 111 ? ASP B 87  VAL B 90  
AB2 3 LEU B 332 ? LEU B 337 ? LEU B 311 LEU B 316 
AB3 1 ILE B 343 ? ASP B 348 ? ILE B 322 ASP B 327 
AB3 2 GLY B 357 ? GLU B 364 ? GLY B 336 GLU B 343 
AB3 3 VAL B 315 ? TYR B 322 ? VAL B 294 TYR B 301 
AB3 4 ASP B 400 ? ASP B 405 ? ASP B 379 ASP B 384 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ARG A 252 ? O ARG A 231 N VAL A 54  ? N VAL A 33  
AA1 2 3 O LEU A 55  ? O LEU A 34  N VAL A 31  ? N VAL A 10  
AA1 3 4 N VAL A 32  ? N VAL A 11  O ILE A 282 ? O ILE A 261 
AA1 4 5 O ALA A 278 ? O ALA A 257 N VAL A 267 ? N VAL A 246 
AA1 5 6 O THR A 268 ? O THR A 247 N ALA A 261 ? N ALA A 240 
AA1 6 7 N ARG A 258 ? N ARG A 237 O ASP A 294 ? O ASP A 273 
AA2 1 2 O ARG A 252 ? O ARG A 231 N VAL A 54  ? N VAL A 33  
AA2 2 3 O LEU A 55  ? O LEU A 34  N VAL A 31  ? N VAL A 10  
AA2 3 4 N VAL A 32  ? N VAL A 11  O ILE A 282 ? O ILE A 261 
AA2 4 5 N VAL A 283 ? N VAL A 262 O HIS A 440 ? O HIS A 419 
AA3 1 2 N GLU A 68  ? N GLU A 47  O ILE A 75  ? O ILE A 54  
AA4 1 2 N ILE A 82  ? N ILE A 61  O ASP A 229 ? O ASP A 208 
AA4 2 3 O ARG A 230 ? O ARG A 209 N TYR A 101 ? N TYR A 80  
AA5 1 2 O GLN A 119 ? O GLN A 98  N VAL A 111 ? N VAL A 90  
AA5 2 3 N VAL A 110 ? N VAL A 89  O LEU A 337 ? O LEU A 316 
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 VAL B 276 ? O VAL B 255 N VAL B 269 ? N VAL B 248 
AA7 5 6 O THR B 268 ? O THR B 247 N ALA B 261 ? N ALA B 240 
AA7 6 7 N LEU B 260 ? N LEU B 239 O ASP B 294 ? O ASP B 273 
AA8 1 2 O ARG B 252 ? O ARG B 231 N VAL B 54  ? N VAL B 33  
AA8 2 3 O LEU B 53  ? O LEU B 32  N VAL B 31  ? N VAL B 10  
AA8 3 4 N VAL B 32  ? N VAL B 11  O ILE B 282 ? O ILE B 261 
AA8 4 5 N ALA B 281 ? N ALA B 260 O HIS B 440 ? O HIS B 419 
AA9 1 2 N GLU B 68  ? N GLU B 47  O ILE B 75  ? O ILE B 54  
AB1 1 2 N ILE B 82  ? N ILE B 61  O ASP B 229 ? O ASP B 208 
AB1 2 3 O ARG B 230 ? O ARG B 209 N TYR B 101 ? N TYR B 80  
AB2 1 2 O GLN B 119 ? O GLN B 98  N VAL B 111 ? N VAL B 90  
AB2 2 3 N ASP B 108 ? N ASP B 87  O SER B 333 ? O SER B 312 
AB3 1 2 N PHE B 347 ? N PHE B 326 O THR B 360 ? O THR B 339 
AB3 2 3 O VAL B 359 ? O VAL B 338 N VAL B 320 ? N VAL B 299 
AB3 3 4 N ILE B 321 ? N ILE B 300 O ASP B 400 ? O ASP B 379 
# 
_pdbx_entry_details.entry_id                   9H5Q 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NH1 B ARG 67  ? ? OE1 B GLN 441 ? ? 2.04 
2 1 O   B HOH 825 ? ? O   B HOH 836 ? ? 2.10 
3 1 OE1 A GLU 150 ? ? O   A HOH 601 ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 259 ? ? CZ A ARG 259 ? ? NH1 A ARG 259 ? ? 124.19 120.30 3.89   0.50 N 
2 1 NE A ARG 259 ? ? CZ A ARG 259 ? ? NH2 A ARG 259 ? ? 114.50 120.30 -5.80  0.50 N 
3 1 CG A ARG 412 ? ? CD A ARG 412 ? ? NE  A ARG 412 ? ? 96.35  111.80 -15.45 2.10 N 
4 1 NE B ARG 355 ? ? CZ B ARG 355 ? ? NH1 B ARG 355 ? ? 123.58 120.30 3.28   0.50 N 
5 1 CG B ARG 412 ? ? CD B ARG 412 ? ? NE  B ARG 412 ? ? 97.41  111.80 -14.39 2.10 N 
6 1 NE B ARG 412 ? ? CZ B ARG 412 ? ? NH2 B ARG 412 ? ? 117.12 120.30 -3.18  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 133 ? ? -162.53 73.34  
2 1 THR A 201 ? ? -83.01  -78.51 
3 1 THR A 391 ? ? -133.02 -57.55 
4 1 GLN B 59  ? ? -134.49 -33.58 
5 1 ALA B 133 ? ? -160.09 74.71  
6 1 THR B 201 ? ? -84.80  -81.40 
7 1 THR B 369 ? ? -120.86 -60.67 
8 1 THR B 391 ? ? -124.14 -59.29 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -20 ? A MET 1   
2  1 Y 1 A GLY -19 ? A GLY 2   
3  1 Y 1 A SER -18 ? A SER 3   
4  1 Y 1 A SER -17 ? A SER 4   
5  1 Y 1 A HIS -16 ? A HIS 5   
6  1 Y 1 A HIS -15 ? A HIS 6   
7  1 Y 1 A HIS -14 ? A HIS 7   
8  1 Y 1 A HIS -13 ? A HIS 8   
9  1 Y 1 A HIS -12 ? A HIS 9   
10 1 Y 1 A HIS -11 ? A HIS 10  
11 1 Y 1 A GLY -10 ? A GLY 11  
12 1 Y 1 A SER -9  ? A SER 12  
13 1 Y 1 A GLY -8  ? A GLY 13  
14 1 Y 1 A LEU -7  ? A LEU 14  
15 1 Y 1 A VAL -6  ? A VAL 15  
16 1 Y 1 A PRO -5  ? A PRO 16  
17 1 Y 1 A ARG -4  ? A ARG 17  
18 1 Y 1 A GLY -3  ? A GLY 18  
19 1 Y 1 A SER -2  ? A SER 19  
20 1 Y 1 A ALA -1  ? A ALA 20  
21 1 Y 1 A GLY 0   ? A GLY 21  
22 1 Y 1 A MET 1   ? A MET 22  
23 1 Y 1 A PRO 2   ? A PRO 23  
24 1 Y 1 A SER 3   ? A SER 24  
25 1 Y 1 A GLU 4   ? A GLU 25  
26 1 Y 1 A SER 453 ? A SER 474 
27 1 Y 1 B MET -20 ? B MET 1   
28 1 Y 1 B GLY -19 ? B GLY 2   
29 1 Y 1 B SER -18 ? B SER 3   
30 1 Y 1 B SER -17 ? B SER 4   
31 1 Y 1 B HIS -16 ? B HIS 5   
32 1 Y 1 B HIS -15 ? B HIS 6   
33 1 Y 1 B HIS -14 ? B HIS 7   
34 1 Y 1 B HIS -13 ? B HIS 8   
35 1 Y 1 B HIS -12 ? B HIS 9   
36 1 Y 1 B HIS -11 ? B HIS 10  
37 1 Y 1 B GLY -10 ? B GLY 11  
38 1 Y 1 B SER -9  ? B SER 12  
39 1 Y 1 B GLY -8  ? B GLY 13  
40 1 Y 1 B LEU -7  ? B LEU 14  
41 1 Y 1 B VAL -6  ? B VAL 15  
42 1 Y 1 B PRO -5  ? B PRO 16  
43 1 Y 1 B ARG -4  ? B ARG 17  
44 1 Y 1 B GLY -3  ? B GLY 18  
45 1 Y 1 B SER -2  ? B SER 19  
46 1 Y 1 B ALA -1  ? B ALA 20  
47 1 Y 1 B GLY 0   ? B GLY 21  
48 1 Y 1 B MET 1   ? B MET 22  
49 1 Y 1 B PRO 2   ? B PRO 23  
50 1 Y 1 B SER 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 
13D CA     C  N N 1   
13D CB     C  N N 2   
13D CC     C  N N 3   
13D ND     N  N N 4   
13D NAA    N  N N 5   
13D HAC1   H  N N 6   
13D HAC2   H  N N 7   
13D HBC1   H  N N 8   
13D HBC2   H  N N 9   
13D HCC1   H  N N 10  
13D HCC2   H  N N 11  
13D HDN1   H  N N 12  
13D HDN2   H  N N 13  
13D HAA1   H  N N 14  
13D HAA2   H  N N 15  
4HA OA     O  N N 16  
4HA CB     C  N N 17  
4HA CG     C  N N 18  
4HA CD     C  N N 19  
4HA CE     C  N N 20  
4HA NZ     N  N N 21  
4HA HA     H  N N 22  
4HA HB2    H  N N 23  
4HA HB3    H  N N 24  
4HA HG2    H  N N 25  
4HA HG3    H  N N 26  
4HA HD2    H  N N 27  
4HA HD3    H  N N 28  
4HA HE2    H  N N 29  
4HA HE3    H  N N 30  
4HA HZ1    H  N N 31  
4HA HZ2    H  N N 32  
4HA HZ3    H  N N 33  
ALA N      N  N N 34  
ALA CA     C  N S 35  
ALA C      C  N N 36  
ALA O      O  N N 37  
ALA CB     C  N N 38  
ALA OXT    O  N N 39  
ALA H      H  N N 40  
ALA H2     H  N N 41  
ALA HA     H  N N 42  
ALA HB1    H  N N 43  
ALA HB2    H  N N 44  
ALA HB3    H  N N 45  
ALA HXT    H  N N 46  
ARG N      N  N N 47  
ARG CA     C  N S 48  
ARG C      C  N N 49  
ARG O      O  N N 50  
ARG CB     C  N N 51  
ARG CG     C  N N 52  
ARG CD     C  N N 53  
ARG NE     N  N N 54  
ARG CZ     C  N N 55  
ARG NH1    N  N N 56  
ARG NH2    N  N N 57  
ARG OXT    O  N N 58  
ARG H      H  N N 59  
ARG H2     H  N N 60  
ARG HA     H  N N 61  
ARG HB2    H  N N 62  
ARG HB3    H  N N 63  
ARG HG2    H  N N 64  
ARG HG3    H  N N 65  
ARG HD2    H  N N 66  
ARG HD3    H  N N 67  
ARG HE     H  N N 68  
ARG HH11   H  N N 69  
ARG HH12   H  N N 70  
ARG HH21   H  N N 71  
ARG HH22   H  N N 72  
ARG HXT    H  N N 73  
ASP N      N  N N 74  
ASP CA     C  N S 75  
ASP C      C  N N 76  
ASP O      O  N N 77  
ASP CB     C  N N 78  
ASP CG     C  N N 79  
ASP OD1    O  N N 80  
ASP OD2    O  N N 81  
ASP OXT    O  N N 82  
ASP H      H  N N 83  
ASP H2     H  N N 84  
ASP HA     H  N N 85  
ASP HB2    H  N N 86  
ASP HB3    H  N N 87  
ASP HD2    H  N N 88  
ASP HXT    H  N N 89  
CYS N      N  N N 90  
CYS CA     C  N R 91  
CYS C      C  N N 92  
CYS O      O  N N 93  
CYS CB     C  N N 94  
CYS SG     S  N N 95  
CYS OXT    O  N N 96  
CYS H      H  N N 97  
CYS H2     H  N N 98  
CYS HA     H  N N 99  
CYS HB2    H  N N 100 
CYS HB3    H  N N 101 
CYS HG     H  N N 102 
CYS HXT    H  N N 103 
FAD PA     P  N R 104 
FAD O1A    O  N N 105 
FAD O2A    O  N N 106 
FAD O5B    O  N N 107 
FAD C5B    C  N N 108 
FAD C4B    C  N R 109 
FAD O4B    O  N N 110 
FAD C3B    C  N S 111 
FAD O3B    O  N N 112 
FAD C2B    C  N R 113 
FAD O2B    O  N N 114 
FAD C1B    C  N R 115 
FAD N9A    N  Y N 116 
FAD C8A    C  Y N 117 
FAD N7A    N  Y N 118 
FAD C5A    C  Y N 119 
FAD C6A    C  Y N 120 
FAD N6A    N  N N 121 
FAD N1A    N  Y N 122 
FAD C2A    C  Y N 123 
FAD N3A    N  Y N 124 
FAD C4A    C  Y N 125 
FAD N1     N  N N 126 
FAD C2     C  N N 127 
FAD O2     O  N N 128 
FAD N3     N  N N 129 
FAD C4     C  N N 130 
FAD O4     O  N N 131 
FAD C4X    C  N N 132 
FAD N5     N  N N 133 
FAD C5X    C  Y N 134 
FAD C6     C  Y N 135 
FAD C7     C  Y N 136 
FAD C7M    C  N N 137 
FAD C8     C  Y N 138 
FAD C8M    C  N N 139 
FAD C9     C  Y N 140 
FAD C9A    C  Y N 141 
FAD N10    N  N N 142 
FAD C10    C  N N 143 
FAD "C1'"  C  N N 144 
FAD "C2'"  C  N S 145 
FAD "O2'"  O  N N 146 
FAD "C3'"  C  N S 147 
FAD "O3'"  O  N N 148 
FAD "C4'"  C  N R 149 
FAD "O4'"  O  N N 150 
FAD "C5'"  C  N N 151 
FAD "O5'"  O  N N 152 
FAD P      P  N R 153 
FAD O1P    O  N N 154 
FAD O2P    O  N N 155 
FAD O3P    O  N N 156 
FAD HOA2   H  N N 157 
FAD H51A   H  N N 158 
FAD H52A   H  N N 159 
FAD H4B    H  N N 160 
FAD H3B    H  N N 161 
FAD HO3A   H  N N 162 
FAD H2B    H  N N 163 
FAD HO2A   H  N N 164 
FAD H1B    H  N N 165 
FAD H8A    H  N N 166 
FAD H61A   H  N N 167 
FAD H62A   H  N N 168 
FAD H2A    H  N N 169 
FAD HN3    H  N N 170 
FAD H6     H  N N 171 
FAD HM71   H  N N 172 
FAD HM72   H  N N 173 
FAD HM73   H  N N 174 
FAD HM81   H  N N 175 
FAD HM82   H  N N 176 
FAD HM83   H  N N 177 
FAD H9     H  N N 178 
FAD "H1'1" H  N N 179 
FAD "H1'2" H  N N 180 
FAD "H2'"  H  N N 181 
FAD "HO2'" H  N N 182 
FAD "H3'"  H  N N 183 
FAD "HO3'" H  N N 184 
FAD "H4'"  H  N N 185 
FAD "HO4'" H  N N 186 
FAD "H5'1" H  N N 187 
FAD "H5'2" H  N N 188 
FAD HOP2   H  N N 189 
GLN N      N  N N 190 
GLN CA     C  N S 191 
GLN C      C  N N 192 
GLN O      O  N N 193 
GLN CB     C  N N 194 
GLN CG     C  N N 195 
GLN CD     C  N N 196 
GLN OE1    O  N N 197 
GLN NE2    N  N N 198 
GLN OXT    O  N N 199 
GLN H      H  N N 200 
GLN H2     H  N N 201 
GLN HA     H  N N 202 
GLN HB2    H  N N 203 
GLN HB3    H  N N 204 
GLN HG2    H  N N 205 
GLN HG3    H  N N 206 
GLN HE21   H  N N 207 
GLN HE22   H  N N 208 
GLN HXT    H  N N 209 
GLU N      N  N N 210 
GLU CA     C  N S 211 
GLU C      C  N N 212 
GLU O      O  N N 213 
GLU CB     C  N N 214 
GLU CG     C  N N 215 
GLU CD     C  N N 216 
GLU OE1    O  N N 217 
GLU OE2    O  N N 218 
GLU OXT    O  N N 219 
GLU H      H  N N 220 
GLU H2     H  N N 221 
GLU HA     H  N N 222 
GLU HB2    H  N N 223 
GLU HB3    H  N N 224 
GLU HG2    H  N N 225 
GLU HG3    H  N N 226 
GLU HE2    H  N N 227 
GLU HXT    H  N N 228 
GLY N      N  N N 229 
GLY CA     C  N N 230 
GLY C      C  N N 231 
GLY O      O  N N 232 
GLY OXT    O  N N 233 
GLY H      H  N N 234 
GLY H2     H  N N 235 
GLY HA2    H  N N 236 
GLY HA3    H  N N 237 
GLY HXT    H  N N 238 
GOL C1     C  N N 239 
GOL O1     O  N N 240 
GOL C2     C  N N 241 
GOL O2     O  N N 242 
GOL C3     C  N N 243 
GOL O3     O  N N 244 
GOL H11    H  N N 245 
GOL H12    H  N N 246 
GOL HO1    H  N N 247 
GOL H2     H  N N 248 
GOL HO2    H  N N 249 
GOL H31    H  N N 250 
GOL H32    H  N N 251 
GOL HO3    H  N N 252 
HIS N      N  N N 253 
HIS CA     C  N S 254 
HIS C      C  N N 255 
HIS O      O  N N 256 
HIS CB     C  N N 257 
HIS CG     C  Y N 258 
HIS ND1    N  Y N 259 
HIS CD2    C  Y N 260 
HIS CE1    C  Y N 261 
HIS NE2    N  Y N 262 
HIS OXT    O  N N 263 
HIS H      H  N N 264 
HIS H2     H  N N 265 
HIS HA     H  N N 266 
HIS HB2    H  N N 267 
HIS HB3    H  N N 268 
HIS HD1    H  N N 269 
HIS HD2    H  N N 270 
HIS HE1    H  N N 271 
HIS HE2    H  N N 272 
HIS HXT    H  N N 273 
HOH O      O  N N 274 
HOH H1     H  N N 275 
HOH H2     H  N N 276 
ILE N      N  N N 277 
ILE CA     C  N S 278 
ILE C      C  N N 279 
ILE O      O  N N 280 
ILE CB     C  N S 281 
ILE CG1    C  N N 282 
ILE CG2    C  N N 283 
ILE CD1    C  N N 284 
ILE OXT    O  N N 285 
ILE H      H  N N 286 
ILE H2     H  N N 287 
ILE HA     H  N N 288 
ILE HB     H  N N 289 
ILE HG12   H  N N 290 
ILE HG13   H  N N 291 
ILE HG21   H  N N 292 
ILE HG22   H  N N 293 
ILE HG23   H  N N 294 
ILE HD11   H  N N 295 
ILE HD12   H  N N 296 
ILE HD13   H  N N 297 
ILE HXT    H  N N 298 
LEU N      N  N N 299 
LEU CA     C  N S 300 
LEU C      C  N N 301 
LEU O      O  N N 302 
LEU CB     C  N N 303 
LEU CG     C  N N 304 
LEU CD1    C  N N 305 
LEU CD2    C  N N 306 
LEU OXT    O  N N 307 
LEU H      H  N N 308 
LEU H2     H  N N 309 
LEU HA     H  N N 310 
LEU HB2    H  N N 311 
LEU HB3    H  N N 312 
LEU HG     H  N N 313 
LEU HD11   H  N N 314 
LEU HD12   H  N N 315 
LEU HD13   H  N N 316 
LEU HD21   H  N N 317 
LEU HD22   H  N N 318 
LEU HD23   H  N N 319 
LEU HXT    H  N N 320 
LYS N      N  N N 321 
LYS CA     C  N S 322 
LYS C      C  N N 323 
LYS O      O  N N 324 
LYS CB     C  N N 325 
LYS CG     C  N N 326 
LYS CD     C  N N 327 
LYS CE     C  N N 328 
LYS NZ     N  N N 329 
LYS OXT    O  N N 330 
LYS H      H  N N 331 
LYS H2     H  N N 332 
LYS HA     H  N N 333 
LYS HB2    H  N N 334 
LYS HB3    H  N N 335 
LYS HG2    H  N N 336 
LYS HG3    H  N N 337 
LYS HD2    H  N N 338 
LYS HD3    H  N N 339 
LYS HE2    H  N N 340 
LYS HE3    H  N N 341 
LYS HZ1    H  N N 342 
LYS HZ2    H  N N 343 
LYS HZ3    H  N N 344 
LYS HXT    H  N N 345 
MET N      N  N N 346 
MET CA     C  N S 347 
MET C      C  N N 348 
MET O      O  N N 349 
MET CB     C  N N 350 
MET CG     C  N N 351 
MET SD     S  N N 352 
MET CE     C  N N 353 
MET OXT    O  N N 354 
MET H      H  N N 355 
MET H2     H  N N 356 
MET HA     H  N N 357 
MET HB2    H  N N 358 
MET HB3    H  N N 359 
MET HG2    H  N N 360 
MET HG3    H  N N 361 
MET HE1    H  N N 362 
MET HE2    H  N N 363 
MET HE3    H  N N 364 
MET HXT    H  N N 365 
MG  MG     MG N N 366 
PHE N      N  N N 367 
PHE CA     C  N S 368 
PHE C      C  N N 369 
PHE O      O  N N 370 
PHE CB     C  N N 371 
PHE CG     C  Y N 372 
PHE CD1    C  Y N 373 
PHE CD2    C  Y N 374 
PHE CE1    C  Y N 375 
PHE CE2    C  Y N 376 
PHE CZ     C  Y N 377 
PHE OXT    O  N N 378 
PHE H      H  N N 379 
PHE H2     H  N N 380 
PHE HA     H  N N 381 
PHE HB2    H  N N 382 
PHE HB3    H  N N 383 
PHE HD1    H  N N 384 
PHE HD2    H  N N 385 
PHE HE1    H  N N 386 
PHE HE2    H  N N 387 
PHE HZ     H  N N 388 
PHE HXT    H  N N 389 
PRO N      N  N N 390 
PRO CA     C  N S 391 
PRO C      C  N N 392 
PRO O      O  N N 393 
PRO CB     C  N N 394 
PRO CG     C  N N 395 
PRO CD     C  N N 396 
PRO OXT    O  N N 397 
PRO H      H  N N 398 
PRO HA     H  N N 399 
PRO HB2    H  N N 400 
PRO HB3    H  N N 401 
PRO HG2    H  N N 402 
PRO HG3    H  N N 403 
PRO HD2    H  N N 404 
PRO HD3    H  N N 405 
PRO HXT    H  N N 406 
SER N      N  N N 407 
SER CA     C  N S 408 
SER C      C  N N 409 
SER O      O  N N 410 
SER CB     C  N N 411 
SER OG     O  N N 412 
SER OXT    O  N N 413 
SER H      H  N N 414 
SER H2     H  N N 415 
SER HA     H  N N 416 
SER HB2    H  N N 417 
SER HB3    H  N N 418 
SER HG     H  N N 419 
SER HXT    H  N N 420 
SPD N1     N  N N 421 
SPD C2     C  N N 422 
SPD C3     C  N N 423 
SPD C4     C  N N 424 
SPD C5     C  N N 425 
SPD N6     N  N N 426 
SPD C7     C  N N 427 
SPD C8     C  N N 428 
SPD C9     C  N N 429 
SPD N10    N  N N 430 
SPD HN11   H  N N 431 
SPD HN12   H  N N 432 
SPD H21    H  N N 433 
SPD H22    H  N N 434 
SPD H31    H  N N 435 
SPD H32    H  N N 436 
SPD H41    H  N N 437 
SPD H42    H  N N 438 
SPD H51    H  N N 439 
SPD H52    H  N N 440 
SPD HN6    H  N N 441 
SPD H71    H  N N 442 
SPD H72    H  N N 443 
SPD H81    H  N N 444 
SPD H82    H  N N 445 
SPD H91    H  N N 446 
SPD H92    H  N N 447 
SPD H101   H  N N 448 
SPD H102   H  N N 449 
THR N      N  N N 450 
THR CA     C  N S 451 
THR C      C  N N 452 
THR O      O  N N 453 
THR CB     C  N R 454 
THR OG1    O  N N 455 
THR CG2    C  N N 456 
THR OXT    O  N N 457 
THR H      H  N N 458 
THR H2     H  N N 459 
THR HA     H  N N 460 
THR HB     H  N N 461 
THR HG1    H  N N 462 
THR HG21   H  N N 463 
THR HG22   H  N N 464 
THR HG23   H  N N 465 
THR HXT    H  N N 466 
TRP N      N  N N 467 
TRP CA     C  N S 468 
TRP C      C  N N 469 
TRP O      O  N N 470 
TRP CB     C  N N 471 
TRP CG     C  Y N 472 
TRP CD1    C  Y N 473 
TRP CD2    C  Y N 474 
TRP NE1    N  Y N 475 
TRP CE2    C  Y N 476 
TRP CE3    C  Y N 477 
TRP CZ2    C  Y N 478 
TRP CZ3    C  Y N 479 
TRP CH2    C  Y N 480 
TRP OXT    O  N N 481 
TRP H      H  N N 482 
TRP H2     H  N N 483 
TRP HA     H  N N 484 
TRP HB2    H  N N 485 
TRP HB3    H  N N 486 
TRP HD1    H  N N 487 
TRP HE1    H  N N 488 
TRP HE3    H  N N 489 
TRP HZ2    H  N N 490 
TRP HZ3    H  N N 491 
TRP HH2    H  N N 492 
TRP HXT    H  N N 493 
TYR N      N  N N 494 
TYR CA     C  N S 495 
TYR C      C  N N 496 
TYR O      O  N N 497 
TYR CB     C  N N 498 
TYR CG     C  Y N 499 
TYR CD1    C  Y N 500 
TYR CD2    C  Y N 501 
TYR CE1    C  Y N 502 
TYR CE2    C  Y N 503 
TYR CZ     C  Y N 504 
TYR OH     O  N N 505 
TYR OXT    O  N N 506 
TYR H      H  N N 507 
TYR H2     H  N N 508 
TYR HA     H  N N 509 
TYR HB2    H  N N 510 
TYR HB3    H  N N 511 
TYR HD1    H  N N 512 
TYR HD2    H  N N 513 
TYR HE1    H  N N 514 
TYR HE2    H  N N 515 
TYR HH     H  N N 516 
TYR HXT    H  N N 517 
VAL N      N  N N 518 
VAL CA     C  N S 519 
VAL C      C  N N 520 
VAL O      O  N N 521 
VAL CB     C  N N 522 
VAL CG1    C  N N 523 
VAL CG2    C  N N 524 
VAL OXT    O  N N 525 
VAL H      H  N N 526 
VAL H2     H  N N 527 
VAL HA     H  N N 528 
VAL HB     H  N N 529 
VAL HG11   H  N N 530 
VAL HG12   H  N N 531 
VAL HG13   H  N N 532 
VAL HG21   H  N N 533 
VAL HG22   H  N N 534 
VAL HG23   H  N N 535 
VAL HXT    H  N N 536 
# 
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 
13D CA    CB     sing N N 1   
13D CA    NAA    sing N N 2   
13D CA    HAC1   sing N N 3   
13D CA    HAC2   sing N N 4   
13D CB    CC     sing N N 5   
13D CB    HBC1   sing N N 6   
13D CB    HBC2   sing N N 7   
13D CC    ND     sing N N 8   
13D CC    HCC1   sing N N 9   
13D CC    HCC2   sing N N 10  
13D ND    HDN1   sing N N 11  
13D ND    HDN2   sing N N 12  
13D NAA   HAA1   sing N N 13  
13D NAA   HAA2   sing N N 14  
4HA OA    CB     sing N N 15  
4HA OA    HA     sing N N 16  
4HA CB    CG     sing N N 17  
4HA CB    HB2    sing N N 18  
4HA CB    HB3    sing N N 19  
4HA CG    CD     sing N N 20  
4HA CG    HG2    sing N N 21  
4HA CG    HG3    sing N N 22  
4HA CD    CE     sing N N 23  
4HA CD    HD2    sing N N 24  
4HA CD    HD3    sing N N 25  
4HA CE    NZ     sing N N 26  
4HA CE    HE2    sing N N 27  
4HA CE    HE3    sing N N 28  
4HA NZ    HZ1    sing N N 29  
4HA NZ    HZ2    sing N N 30  
4HA NZ    HZ3    sing N N 31  
ALA N     CA     sing N N 32  
ALA N     H      sing N N 33  
ALA N     H2     sing N N 34  
ALA CA    C      sing N N 35  
ALA CA    CB     sing N N 36  
ALA CA    HA     sing N N 37  
ALA C     O      doub N N 38  
ALA C     OXT    sing N N 39  
ALA CB    HB1    sing N N 40  
ALA CB    HB2    sing N N 41  
ALA CB    HB3    sing N N 42  
ALA OXT   HXT    sing N N 43  
ARG N     CA     sing N N 44  
ARG N     H      sing N N 45  
ARG N     H2     sing N N 46  
ARG CA    C      sing N N 47  
ARG CA    CB     sing N N 48  
ARG CA    HA     sing N N 49  
ARG C     O      doub N N 50  
ARG C     OXT    sing N N 51  
ARG CB    CG     sing N N 52  
ARG CB    HB2    sing N N 53  
ARG CB    HB3    sing N N 54  
ARG CG    CD     sing N N 55  
ARG CG    HG2    sing N N 56  
ARG CG    HG3    sing N N 57  
ARG CD    NE     sing N N 58  
ARG CD    HD2    sing N N 59  
ARG CD    HD3    sing N N 60  
ARG NE    CZ     sing N N 61  
ARG NE    HE     sing N N 62  
ARG CZ    NH1    sing N N 63  
ARG CZ    NH2    doub N N 64  
ARG NH1   HH11   sing N N 65  
ARG NH1   HH12   sing N N 66  
ARG NH2   HH21   sing N N 67  
ARG NH2   HH22   sing N N 68  
ARG OXT   HXT    sing N N 69  
ASP N     CA     sing N N 70  
ASP N     H      sing N N 71  
ASP N     H2     sing N N 72  
ASP CA    C      sing N N 73  
ASP CA    CB     sing N N 74  
ASP CA    HA     sing N N 75  
ASP C     O      doub N N 76  
ASP C     OXT    sing N N 77  
ASP CB    CG     sing N N 78  
ASP CB    HB2    sing N N 79  
ASP CB    HB3    sing N N 80  
ASP CG    OD1    doub N N 81  
ASP CG    OD2    sing N N 82  
ASP OD2   HD2    sing N N 83  
ASP OXT   HXT    sing N N 84  
CYS N     CA     sing N N 85  
CYS N     H      sing N N 86  
CYS N     H2     sing N N 87  
CYS CA    C      sing N N 88  
CYS CA    CB     sing N N 89  
CYS CA    HA     sing N N 90  
CYS C     O      doub N N 91  
CYS C     OXT    sing N N 92  
CYS CB    SG     sing N N 93  
CYS CB    HB2    sing N N 94  
CYS CB    HB3    sing N N 95  
CYS SG    HG     sing N N 96  
CYS OXT   HXT    sing N N 97  
FAD PA    O1A    doub N N 98  
FAD PA    O2A    sing N N 99  
FAD PA    O5B    sing N N 100 
FAD PA    O3P    sing N N 101 
FAD O2A   HOA2   sing N N 102 
FAD O5B   C5B    sing N N 103 
FAD C5B   C4B    sing N N 104 
FAD C5B   H51A   sing N N 105 
FAD C5B   H52A   sing N N 106 
FAD C4B   O4B    sing N N 107 
FAD C4B   C3B    sing N N 108 
FAD C4B   H4B    sing N N 109 
FAD O4B   C1B    sing N N 110 
FAD C3B   O3B    sing N N 111 
FAD C3B   C2B    sing N N 112 
FAD C3B   H3B    sing N N 113 
FAD O3B   HO3A   sing N N 114 
FAD C2B   O2B    sing N N 115 
FAD C2B   C1B    sing N N 116 
FAD C2B   H2B    sing N N 117 
FAD O2B   HO2A   sing N N 118 
FAD C1B   N9A    sing N N 119 
FAD C1B   H1B    sing N N 120 
FAD N9A   C8A    sing Y N 121 
FAD N9A   C4A    sing Y N 122 
FAD C8A   N7A    doub Y N 123 
FAD C8A   H8A    sing N N 124 
FAD N7A   C5A    sing Y N 125 
FAD C5A   C6A    sing Y N 126 
FAD C5A   C4A    doub Y N 127 
FAD C6A   N6A    sing N N 128 
FAD C6A   N1A    doub Y N 129 
FAD N6A   H61A   sing N N 130 
FAD N6A   H62A   sing N N 131 
FAD N1A   C2A    sing Y N 132 
FAD C2A   N3A    doub Y N 133 
FAD C2A   H2A    sing N N 134 
FAD N3A   C4A    sing Y N 135 
FAD N1    C2     sing N N 136 
FAD N1    C10    doub N N 137 
FAD C2    O2     doub N N 138 
FAD C2    N3     sing N N 139 
FAD N3    C4     sing N N 140 
FAD N3    HN3    sing N N 141 
FAD C4    O4     doub N N 142 
FAD C4    C4X    sing N N 143 
FAD C4X   N5     doub N N 144 
FAD C4X   C10    sing N N 145 
FAD N5    C5X    sing N N 146 
FAD C5X   C6     doub Y N 147 
FAD C5X   C9A    sing Y N 148 
FAD C6    C7     sing Y N 149 
FAD C6    H6     sing N N 150 
FAD C7    C7M    sing N N 151 
FAD C7    C8     doub Y N 152 
FAD C7M   HM71   sing N N 153 
FAD C7M   HM72   sing N N 154 
FAD C7M   HM73   sing N N 155 
FAD C8    C8M    sing N N 156 
FAD C8    C9     sing Y N 157 
FAD C8M   HM81   sing N N 158 
FAD C8M   HM82   sing N N 159 
FAD C8M   HM83   sing N N 160 
FAD C9    C9A    doub Y N 161 
FAD C9    H9     sing N N 162 
FAD C9A   N10    sing N N 163 
FAD N10   C10    sing N N 164 
FAD N10   "C1'"  sing N N 165 
FAD "C1'" "C2'"  sing N N 166 
FAD "C1'" "H1'1" sing N N 167 
FAD "C1'" "H1'2" sing N N 168 
FAD "C2'" "O2'"  sing N N 169 
FAD "C2'" "C3'"  sing N N 170 
FAD "C2'" "H2'"  sing N N 171 
FAD "O2'" "HO2'" sing N N 172 
FAD "C3'" "O3'"  sing N N 173 
FAD "C3'" "C4'"  sing N N 174 
FAD "C3'" "H3'"  sing N N 175 
FAD "O3'" "HO3'" sing N N 176 
FAD "C4'" "O4'"  sing N N 177 
FAD "C4'" "C5'"  sing N N 178 
FAD "C4'" "H4'"  sing N N 179 
FAD "O4'" "HO4'" sing N N 180 
FAD "C5'" "O5'"  sing N N 181 
FAD "C5'" "H5'1" sing N N 182 
FAD "C5'" "H5'2" sing N N 183 
FAD "O5'" P      sing N N 184 
FAD P     O1P    doub N N 185 
FAD P     O2P    sing N N 186 
FAD P     O3P    sing N N 187 
FAD O2P   HOP2   sing N N 188 
GLN N     CA     sing N N 189 
GLN N     H      sing N N 190 
GLN N     H2     sing N N 191 
GLN CA    C      sing N N 192 
GLN CA    CB     sing N N 193 
GLN CA    HA     sing N N 194 
GLN C     O      doub N N 195 
GLN C     OXT    sing N N 196 
GLN CB    CG     sing N N 197 
GLN CB    HB2    sing N N 198 
GLN CB    HB3    sing N N 199 
GLN CG    CD     sing N N 200 
GLN CG    HG2    sing N N 201 
GLN CG    HG3    sing N N 202 
GLN CD    OE1    doub N N 203 
GLN CD    NE2    sing N N 204 
GLN NE2   HE21   sing N N 205 
GLN NE2   HE22   sing N N 206 
GLN OXT   HXT    sing N N 207 
GLU N     CA     sing N N 208 
GLU N     H      sing N N 209 
GLU N     H2     sing N N 210 
GLU CA    C      sing N N 211 
GLU CA    CB     sing N N 212 
GLU CA    HA     sing N N 213 
GLU C     O      doub N N 214 
GLU C     OXT    sing N N 215 
GLU CB    CG     sing N N 216 
GLU CB    HB2    sing N N 217 
GLU CB    HB3    sing N N 218 
GLU CG    CD     sing N N 219 
GLU CG    HG2    sing N N 220 
GLU CG    HG3    sing N N 221 
GLU CD    OE1    doub N N 222 
GLU CD    OE2    sing N N 223 
GLU OE2   HE2    sing N N 224 
GLU OXT   HXT    sing N N 225 
GLY N     CA     sing N N 226 
GLY N     H      sing N N 227 
GLY N     H2     sing N N 228 
GLY CA    C      sing N N 229 
GLY CA    HA2    sing N N 230 
GLY CA    HA3    sing N N 231 
GLY C     O      doub N N 232 
GLY C     OXT    sing N N 233 
GLY OXT   HXT    sing N N 234 
GOL C1    O1     sing N N 235 
GOL C1    C2     sing N N 236 
GOL C1    H11    sing N N 237 
GOL C1    H12    sing N N 238 
GOL O1    HO1    sing N N 239 
GOL C2    O2     sing N N 240 
GOL C2    C3     sing N N 241 
GOL C2    H2     sing N N 242 
GOL O2    HO2    sing N N 243 
GOL C3    O3     sing N N 244 
GOL C3    H31    sing N N 245 
GOL C3    H32    sing N N 246 
GOL O3    HO3    sing N N 247 
HIS N     CA     sing N N 248 
HIS N     H      sing N N 249 
HIS N     H2     sing N N 250 
HIS CA    C      sing N N 251 
HIS CA    CB     sing N N 252 
HIS CA    HA     sing N N 253 
HIS C     O      doub N N 254 
HIS C     OXT    sing N N 255 
HIS CB    CG     sing N N 256 
HIS CB    HB2    sing N N 257 
HIS CB    HB3    sing N N 258 
HIS CG    ND1    sing Y N 259 
HIS CG    CD2    doub Y N 260 
HIS ND1   CE1    doub Y N 261 
HIS ND1   HD1    sing N N 262 
HIS CD2   NE2    sing Y N 263 
HIS CD2   HD2    sing N N 264 
HIS CE1   NE2    sing Y N 265 
HIS CE1   HE1    sing N N 266 
HIS NE2   HE2    sing N N 267 
HIS OXT   HXT    sing N N 268 
HOH O     H1     sing N N 269 
HOH O     H2     sing N N 270 
ILE N     CA     sing N N 271 
ILE N     H      sing N N 272 
ILE N     H2     sing N N 273 
ILE CA    C      sing N N 274 
ILE CA    CB     sing N N 275 
ILE CA    HA     sing N N 276 
ILE C     O      doub N N 277 
ILE C     OXT    sing N N 278 
ILE CB    CG1    sing N N 279 
ILE CB    CG2    sing N N 280 
ILE CB    HB     sing N N 281 
ILE CG1   CD1    sing N N 282 
ILE CG1   HG12   sing N N 283 
ILE CG1   HG13   sing N N 284 
ILE CG2   HG21   sing N N 285 
ILE CG2   HG22   sing N N 286 
ILE CG2   HG23   sing N N 287 
ILE CD1   HD11   sing N N 288 
ILE CD1   HD12   sing N N 289 
ILE CD1   HD13   sing N N 290 
ILE OXT   HXT    sing N N 291 
LEU N     CA     sing N N 292 
LEU N     H      sing N N 293 
LEU N     H2     sing N N 294 
LEU CA    C      sing N N 295 
LEU CA    CB     sing N N 296 
LEU CA    HA     sing N N 297 
LEU C     O      doub N N 298 
LEU C     OXT    sing N N 299 
LEU CB    CG     sing N N 300 
LEU CB    HB2    sing N N 301 
LEU CB    HB3    sing N N 302 
LEU CG    CD1    sing N N 303 
LEU CG    CD2    sing N N 304 
LEU CG    HG     sing N N 305 
LEU CD1   HD11   sing N N 306 
LEU CD1   HD12   sing N N 307 
LEU CD1   HD13   sing N N 308 
LEU CD2   HD21   sing N N 309 
LEU CD2   HD22   sing N N 310 
LEU CD2   HD23   sing N N 311 
LEU OXT   HXT    sing N N 312 
LYS N     CA     sing N N 313 
LYS N     H      sing N N 314 
LYS N     H2     sing N N 315 
LYS CA    C      sing N N 316 
LYS CA    CB     sing N N 317 
LYS CA    HA     sing N N 318 
LYS C     O      doub N N 319 
LYS C     OXT    sing N N 320 
LYS CB    CG     sing N N 321 
LYS CB    HB2    sing N N 322 
LYS CB    HB3    sing N N 323 
LYS CG    CD     sing N N 324 
LYS CG    HG2    sing N N 325 
LYS CG    HG3    sing N N 326 
LYS CD    CE     sing N N 327 
LYS CD    HD2    sing N N 328 
LYS CD    HD3    sing N N 329 
LYS CE    NZ     sing N N 330 
LYS CE    HE2    sing N N 331 
LYS CE    HE3    sing N N 332 
LYS NZ    HZ1    sing N N 333 
LYS NZ    HZ2    sing N N 334 
LYS NZ    HZ3    sing N N 335 
LYS OXT   HXT    sing N N 336 
MET N     CA     sing N N 337 
MET N     H      sing N N 338 
MET N     H2     sing N N 339 
MET CA    C      sing N N 340 
MET CA    CB     sing N N 341 
MET CA    HA     sing N N 342 
MET C     O      doub N N 343 
MET C     OXT    sing N N 344 
MET CB    CG     sing N N 345 
MET CB    HB2    sing N N 346 
MET CB    HB3    sing N N 347 
MET CG    SD     sing N N 348 
MET CG    HG2    sing N N 349 
MET CG    HG3    sing N N 350 
MET SD    CE     sing N N 351 
MET CE    HE1    sing N N 352 
MET CE    HE2    sing N N 353 
MET CE    HE3    sing N N 354 
MET OXT   HXT    sing N N 355 
PHE N     CA     sing N N 356 
PHE N     H      sing N N 357 
PHE N     H2     sing N N 358 
PHE CA    C      sing N N 359 
PHE CA    CB     sing N N 360 
PHE CA    HA     sing N N 361 
PHE C     O      doub N N 362 
PHE C     OXT    sing N N 363 
PHE CB    CG     sing N N 364 
PHE CB    HB2    sing N N 365 
PHE CB    HB3    sing N N 366 
PHE CG    CD1    doub Y N 367 
PHE CG    CD2    sing Y N 368 
PHE CD1   CE1    sing Y N 369 
PHE CD1   HD1    sing N N 370 
PHE CD2   CE2    doub Y N 371 
PHE CD2   HD2    sing N N 372 
PHE CE1   CZ     doub Y N 373 
PHE CE1   HE1    sing N N 374 
PHE CE2   CZ     sing Y N 375 
PHE CE2   HE2    sing N N 376 
PHE CZ    HZ     sing N N 377 
PHE OXT   HXT    sing N N 378 
PRO N     CA     sing N N 379 
PRO N     CD     sing N N 380 
PRO N     H      sing N N 381 
PRO CA    C      sing N N 382 
PRO CA    CB     sing N N 383 
PRO CA    HA     sing N N 384 
PRO C     O      doub N N 385 
PRO C     OXT    sing N N 386 
PRO CB    CG     sing N N 387 
PRO CB    HB2    sing N N 388 
PRO CB    HB3    sing N N 389 
PRO CG    CD     sing N N 390 
PRO CG    HG2    sing N N 391 
PRO CG    HG3    sing N N 392 
PRO CD    HD2    sing N N 393 
PRO CD    HD3    sing N N 394 
PRO OXT   HXT    sing N N 395 
SER N     CA     sing N N 396 
SER N     H      sing N N 397 
SER N     H2     sing N N 398 
SER CA    C      sing N N 399 
SER CA    CB     sing N N 400 
SER CA    HA     sing N N 401 
SER C     O      doub N N 402 
SER C     OXT    sing N N 403 
SER CB    OG     sing N N 404 
SER CB    HB2    sing N N 405 
SER CB    HB3    sing N N 406 
SER OG    HG     sing N N 407 
SER OXT   HXT    sing N N 408 
SPD N1    C2     sing N N 409 
SPD N1    HN11   sing N N 410 
SPD N1    HN12   sing N N 411 
SPD C2    C3     sing N N 412 
SPD C2    H21    sing N N 413 
SPD C2    H22    sing N N 414 
SPD C3    C4     sing N N 415 
SPD C3    H31    sing N N 416 
SPD C3    H32    sing N N 417 
SPD C4    C5     sing N N 418 
SPD C4    H41    sing N N 419 
SPD C4    H42    sing N N 420 
SPD C5    N6     sing N N 421 
SPD C5    H51    sing N N 422 
SPD C5    H52    sing N N 423 
SPD N6    C7     sing N N 424 
SPD N6    HN6    sing N N 425 
SPD C7    C8     sing N N 426 
SPD C7    H71    sing N N 427 
SPD C7    H72    sing N N 428 
SPD C8    C9     sing N N 429 
SPD C8    H81    sing N N 430 
SPD C8    H82    sing N N 431 
SPD C9    N10    sing N N 432 
SPD C9    H91    sing N N 433 
SPD C9    H92    sing N N 434 
SPD N10   H101   sing N N 435 
SPD N10   H102   sing N N 436 
THR N     CA     sing N N 437 
THR N     H      sing N N 438 
THR N     H2     sing N N 439 
THR CA    C      sing N N 440 
THR CA    CB     sing N N 441 
THR CA    HA     sing N N 442 
THR C     O      doub N N 443 
THR C     OXT    sing N N 444 
THR CB    OG1    sing N N 445 
THR CB    CG2    sing N N 446 
THR CB    HB     sing N N 447 
THR OG1   HG1    sing N N 448 
THR CG2   HG21   sing N N 449 
THR CG2   HG22   sing N N 450 
THR CG2   HG23   sing N N 451 
THR OXT   HXT    sing N N 452 
TRP N     CA     sing N N 453 
TRP N     H      sing N N 454 
TRP N     H2     sing N N 455 
TRP CA    C      sing N N 456 
TRP CA    CB     sing N N 457 
TRP CA    HA     sing N N 458 
TRP C     O      doub N N 459 
TRP C     OXT    sing N N 460 
TRP CB    CG     sing N N 461 
TRP CB    HB2    sing N N 462 
TRP CB    HB3    sing N N 463 
TRP CG    CD1    doub Y N 464 
TRP CG    CD2    sing Y N 465 
TRP CD1   NE1    sing Y N 466 
TRP CD1   HD1    sing N N 467 
TRP CD2   CE2    doub Y N 468 
TRP CD2   CE3    sing Y N 469 
TRP NE1   CE2    sing Y N 470 
TRP NE1   HE1    sing N N 471 
TRP CE2   CZ2    sing Y N 472 
TRP CE3   CZ3    doub Y N 473 
TRP CE3   HE3    sing N N 474 
TRP CZ2   CH2    doub Y N 475 
TRP CZ2   HZ2    sing N N 476 
TRP CZ3   CH2    sing Y N 477 
TRP CZ3   HZ3    sing N N 478 
TRP CH2   HH2    sing N N 479 
TRP OXT   HXT    sing N N 480 
TYR N     CA     sing N N 481 
TYR N     H      sing N N 482 
TYR N     H2     sing N N 483 
TYR CA    C      sing N N 484 
TYR CA    CB     sing N N 485 
TYR CA    HA     sing N N 486 
TYR C     O      doub N N 487 
TYR C     OXT    sing N N 488 
TYR CB    CG     sing N N 489 
TYR CB    HB2    sing N N 490 
TYR CB    HB3    sing N N 491 
TYR CG    CD1    doub Y N 492 
TYR CG    CD2    sing Y N 493 
TYR CD1   CE1    sing Y N 494 
TYR CD1   HD1    sing N N 495 
TYR CD2   CE2    doub Y N 496 
TYR CD2   HD2    sing N N 497 
TYR CE1   CZ     doub Y N 498 
TYR CE1   HE1    sing N N 499 
TYR CE2   CZ     sing Y N 500 
TYR CE2   HE2    sing N N 501 
TYR CZ    OH     sing N N 502 
TYR OH    HH     sing N N 503 
TYR OXT   HXT    sing N N 504 
VAL N     CA     sing N N 505 
VAL N     H      sing N N 506 
VAL N     H2     sing N N 507 
VAL CA    C      sing N N 508 
VAL CA    CB     sing N N 509 
VAL CA    HA     sing N N 510 
VAL C     O      doub N N 511 
VAL C     OXT    sing N N 512 
VAL CB    CG1    sing N N 513 
VAL CB    CG2    sing N N 514 
VAL CB    HB     sing N N 515 
VAL CG1   HG11   sing N N 516 
VAL CG1   HG12   sing N N 517 
VAL CG1   HG13   sing N N 518 
VAL CG2   HG21   sing N N 519 
VAL CG2   HG22   sing N N 520 
VAL CG2   HG23   sing N N 521 
VAL OXT   HXT    sing N N 522 
# 
_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                    9H5Q 
_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]   0.014634 
_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]   0.010587 
_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]   0.007828 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLN A 1 26  ? -22.131 5.471   1.516   1.00 34.31 ? 5   GLN A N     1 
ATOM   2    C  CA    . GLN A 1 26  ? -21.256 5.524   2.725   1.00 33.55 ? 5   GLN A CA    1 
ATOM   3    C  C     . GLN A 1 26  ? -21.704 4.416   3.695   1.00 32.71 ? 5   GLN A C     1 
ATOM   4    O  O     . GLN A 1 26  ? -22.817 4.528   4.239   1.00 33.75 ? 5   GLN A O     1 
ATOM   5    C  CB    . GLN A 1 26  ? -21.292 6.914   3.373   1.00 37.29 ? 5   GLN A CB    1 
ATOM   6    C  CG    . GLN A 1 26  ? -20.309 7.063   4.541   1.00 38.59 ? 5   GLN A CG    1 
ATOM   7    C  CD    . GLN A 1 26  ? -20.292 8.409   5.227   1.00 42.31 ? 5   GLN A CD    1 
ATOM   8    O  OE1   . GLN A 1 26  ? -19.256 9.054   5.385   1.00 41.51 ? 5   GLN A OE1   1 
ATOM   9    N  NE2   . GLN A 1 26  ? -21.447 8.844   5.687   1.00 43.72 ? 5   GLN A NE2   1 
ATOM   10   N  N     . VAL A 1 27  ? -20.933 3.342   3.853   1.00 26.77 ? 6   VAL A N     1 
ATOM   11   C  CA    . VAL A 1 27  ? -21.204 2.309   4.887   1.00 24.53 ? 6   VAL A CA    1 
ATOM   12   C  C     . VAL A 1 27  ? -20.880 2.922   6.252   1.00 21.27 ? 6   VAL A C     1 
ATOM   13   O  O     . VAL A 1 27  ? -20.120 3.905   6.325   1.00 21.44 ? 6   VAL A O     1 
ATOM   14   C  CB    . VAL A 1 27  ? -20.446 0.992   4.639   1.00 27.57 ? 6   VAL A CB    1 
ATOM   15   C  CG1   . VAL A 1 27  ? -21.010 0.301   3.410   1.00 32.48 ? 6   VAL A CG1   1 
ATOM   16   C  CG2   . VAL A 1 27  ? -18.946 1.162   4.516   1.00 29.32 ? 6   VAL A CG2   1 
ATOM   17   N  N     . ASP A 1 28  ? -21.416 2.353   7.320   1.00 19.12 ? 7   ASP A N     1 
ATOM   18   C  CA    . ASP A 1 28  ? -21.138 2.857   8.680   1.00 18.59 ? 7   ASP A CA    1 
ATOM   19   C  C     . ASP A 1 28  ? -19.664 2.594   9.053   1.00 19.89 ? 7   ASP A C     1 
ATOM   20   O  O     . ASP A 1 28  ? -19.017 3.492   9.627   1.00 18.73 ? 7   ASP A O     1 
ATOM   21   C  CB    . ASP A 1 28  ? -22.072 2.198   9.699   1.00 18.85 ? 7   ASP A CB    1 
ATOM   22   C  CG    . ASP A 1 28  ? -23.515 2.631   9.532   1.00 21.67 ? 7   ASP A CG    1 
ATOM   23   O  OD1   . ASP A 1 28  ? -23.719 3.806   9.167   1.00 23.07 ? 7   ASP A OD1   1 
ATOM   24   O  OD2   . ASP A 1 28  ? -24.415 1.800   9.772   1.00 21.02 ? 7   ASP A OD2   1 
ATOM   25   N  N     . VAL A 1 29  ? -19.155 1.385   8.788   1.00 18.70 ? 8   VAL A N     1 
ATOM   26   C  CA    . VAL A 1 29  ? -17.814 0.962   9.269   1.00 16.34 ? 8   VAL A CA    1 
ATOM   27   C  C     . VAL A 1 29  ? -17.118 0.202   8.134   1.00 17.20 ? 8   VAL A C     1 
ATOM   28   O  O     . VAL A 1 29  ? -17.724 -0.724  7.542   1.00 15.91 ? 8   VAL A O     1 
ATOM   29   C  CB    . VAL A 1 29  ? -17.896 0.060   10.511  1.00 16.76 ? 8   VAL A CB    1 
ATOM   30   C  CG1   . VAL A 1 29  ? -16.510 -0.347  10.950  1.00 18.98 ? 8   VAL A CG1   1 
ATOM   31   C  CG2   . VAL A 1 29  ? -18.681 0.696   11.669  1.00 17.97 ? 8   VAL A CG2   1 
ATOM   32   N  N     . VAL A 1 30  ? -15.875 0.571   7.876   1.00 14.57 ? 9   VAL A N     1 
ATOM   33   C  CA    . VAL A 1 30  ? -14.976 -0.231  7.013   1.00 16.03 ? 9   VAL A CA    1 
ATOM   34   C  C     . VAL A 1 30  ? -13.940 -0.873  7.931   1.00 15.89 ? 9   VAL A C     1 
ATOM   35   O  O     . VAL A 1 30  ? -13.324 -0.163  8.757   1.00 14.68 ? 9   VAL A O     1 
ATOM   36   C  CB    . VAL A 1 30  ? -14.357 0.592   5.869   1.00 17.87 ? 9   VAL A CB    1 
ATOM   37   C  CG1   . VAL A 1 30  ? -13.567 1.791   6.349   1.00 23.00 ? 9   VAL A CG1   1 
ATOM   38   C  CG2   . VAL A 1 30  ? -13.503 -0.268  4.960   1.00 17.94 ? 9   VAL A CG2   1 
ATOM   39   N  N     . VAL A 1 31  ? -13.742 -2.170  7.746   1.00 15.44 ? 10  VAL A N     1 
ATOM   40   C  CA    . VAL A 1 31  ? -12.721 -2.928  8.488   1.00 15.19 ? 10  VAL A CA    1 
ATOM   41   C  C     . VAL A 1 31  ? -11.625 -3.310  7.505   1.00 15.86 ? 10  VAL A C     1 
ATOM   42   O  O     . VAL A 1 31  ? -11.945 -3.883  6.455   1.00 15.74 ? 10  VAL A O     1 
ATOM   43   C  CB    . VAL A 1 31  ? -13.337 -4.168  9.145   1.00 16.90 ? 10  VAL A CB    1 
ATOM   44   C  CG1   . VAL A 1 31  ? -12.289 -4.991  9.860   1.00 17.34 ? 10  VAL A CG1   1 
ATOM   45   C  CG2   . VAL A 1 31  ? -14.459 -3.786  10.081  1.00 16.11 ? 10  VAL A CG2   1 
ATOM   46   N  N     . VAL A 1 32  ? -10.378 -2.999  7.851   1.00 16.43 ? 11  VAL A N     1 
ATOM   47   C  CA    . VAL A 1 32  ? -9.202  -3.392  7.031   1.00 16.31 ? 11  VAL A CA    1 
ATOM   48   C  C     . VAL A 1 32  ? -8.601  -4.655  7.642   1.00 15.21 ? 11  VAL A C     1 
ATOM   49   O  O     . VAL A 1 32  ? -8.053  -4.585  8.745   1.00 14.56 ? 11  VAL A O     1 
ATOM   50   C  CB    . VAL A 1 32  ? -8.178  -2.258  6.951   1.00 18.42 ? 11  VAL A CB    1 
ATOM   51   C  CG1   . VAL A 1 32  ? -7.001  -2.627  6.064   1.00 18.43 ? 11  VAL A CG1   1 
ATOM   52   C  CG2   . VAL A 1 32  ? -8.816  -0.960  6.479   1.00 17.82 ? 11  VAL A CG2   1 
ATOM   53   N  N     . GLY A 1 33  ? -8.680  -5.779  6.915   1.00 15.30 ? 12  GLY A N     1 
ATOM   54   C  CA    . GLY A 1 33  ? -8.121  -7.064  7.362   1.00 15.38 ? 12  GLY A CA    1 
ATOM   55   C  C     . GLY A 1 33  ? -9.203  -8.046  7.815   1.00 16.76 ? 12  GLY A C     1 
ATOM   56   O  O     . GLY A 1 33  ? -10.047 -7.678  8.632   1.00 15.72 ? 12  GLY A O     1 
ATOM   57   N  N     . ALA A 1 34  ? -9.150  -9.274  7.297   1.00 15.99 ? 13  ALA A N     1 
ATOM   58   C  CA    . ALA A 1 34  ? -10.086 -10.364 7.653   1.00 15.53 ? 13  ALA A CA    1 
ATOM   59   C  C     . ALA A 1 34  ? -9.319  -11.487 8.330   1.00 15.02 ? 13  ALA A C     1 
ATOM   60   O  O     . ALA A 1 34  ? -9.592  -12.688 8.047   1.00 15.24 ? 13  ALA A O     1 
ATOM   61   C  CB    . ALA A 1 34  ? -10.839 -10.836 6.448   1.00 15.79 ? 13  ALA A CB    1 
ATOM   62   N  N     . GLY A 1 35  ? -8.400  -11.145 9.234   1.00 14.72 ? 14  GLY A N     1 
ATOM   63   C  CA    . GLY A 1 35  ? -8.007  -12.126 10.265  1.00 13.45 ? 14  GLY A CA    1 
ATOM   64   C  C     . GLY A 1 35  ? -9.095  -12.252 11.349  1.00 14.12 ? 14  GLY A C     1 
ATOM   65   O  O     . GLY A 1 35  ? -10.191 -11.660 11.225  1.00 13.91 ? 14  GLY A O     1 
ATOM   66   N  N     . PHE A 1 36  ? -8.808  -12.958 12.436  1.00 14.46 ? 15  PHE A N     1 
ATOM   67   C  CA    . PHE A 1 36  ? -9.781  -13.124 13.548  1.00 14.24 ? 15  PHE A CA    1 
ATOM   68   C  C     . PHE A 1 36  ? -10.148 -11.758 14.135  1.00 14.92 ? 15  PHE A C     1 
ATOM   69   O  O     . PHE A 1 36  ? -11.312 -11.552 14.491  1.00 13.36 ? 15  PHE A O     1 
ATOM   70   C  CB    . PHE A 1 36  ? -9.285  -14.108 14.603  1.00 14.80 ? 15  PHE A CB    1 
ATOM   71   C  CG    . PHE A 1 36  ? -9.548  -15.536 14.218  1.00 14.03 ? 15  PHE A CG    1 
ATOM   72   C  CD1   . PHE A 1 36  ? -10.728 -16.161 14.586  1.00 16.41 ? 15  PHE A CD1   1 
ATOM   73   C  CD2   . PHE A 1 36  ? -8.578  -16.266 13.555  1.00 15.00 ? 15  PHE A CD2   1 
ATOM   74   C  CE1   . PHE A 1 36  ? -10.981 -17.467 14.196  1.00 16.28 ? 15  PHE A CE1   1 
ATOM   75   C  CE2   . PHE A 1 36  ? -8.839  -17.558 13.130  1.00 15.71 ? 15  PHE A CE2   1 
ATOM   76   C  CZ    . PHE A 1 36  ? -10.033 -18.159 13.491  1.00 15.90 ? 15  PHE A CZ    1 
ATOM   77   N  N     . ALA A 1 37  ? -9.209  -10.813 14.201  1.00 15.04 ? 16  ALA A N     1 
ATOM   78   C  CA    . ALA A 1 37  ? -9.535  -9.494  14.767  1.00 14.49 ? 16  ALA A CA    1 
ATOM   79   C  C     . ALA A 1 37  ? -10.553 -8.770  13.867  1.00 14.75 ? 16  ALA A C     1 
ATOM   80   O  O     . ALA A 1 37  ? -11.623 -8.343  14.410  1.00 14.68 ? 16  ALA A O     1 
ATOM   81   C  CB    . ALA A 1 37  ? -8.294  -8.659  14.997  1.00 14.50 ? 16  ALA A CB    1 
ATOM   82   N  N     . GLY A 1 38  ? -10.243 -8.565  12.583  1.00 14.00 ? 17  GLY A N     1 
ATOM   83   C  CA    . GLY A 1 38  ? -11.128 -7.866  11.626  1.00 13.47 ? 17  GLY A CA    1 
ATOM   84   C  C     . GLY A 1 38  ? -12.496 -8.544  11.502  1.00 13.96 ? 17  GLY A C     1 
ATOM   85   O  O     . GLY A 1 38  ? -13.552 -7.839  11.507  1.00 13.93 ? 17  GLY A O     1 
ATOM   86   N  N     . LEU A 1 39  ? -12.528 -9.873  11.396  1.00 14.53 ? 18  LEU A N     1 
ATOM   87   C  CA    . LEU A 1 39  ? -13.803 -10.628 11.263  1.00 15.33 ? 18  LEU A CA    1 
ATOM   88   C  C     . LEU A 1 39  ? -14.646 -10.528 12.544  1.00 16.75 ? 18  LEU A C     1 
ATOM   89   O  O     . LEU A 1 39  ? -15.877 -10.342 12.410  1.00 14.80 ? 18  LEU A O     1 
ATOM   90   C  CB    . LEU A 1 39  ? -13.542 -12.067 10.890  1.00 14.98 ? 18  LEU A CB    1 
ATOM   91   C  CG    . LEU A 1 39  ? -13.002 -12.319 9.495   1.00 17.22 ? 18  LEU A CG    1 
ATOM   92   C  CD1   . LEU A 1 39  ? -12.667 -13.802 9.359   1.00 17.17 ? 18  LEU A CD1   1 
ATOM   93   C  CD2   . LEU A 1 39  ? -13.978 -11.858 8.388   1.00 17.72 ? 18  LEU A CD2   1 
ATOM   94   N  N     . THR A 1 40  ? -14.027 -10.626 13.727  1.00 15.05 ? 19  THR A N     1 
ATOM   95   C  CA    . THR A 1 40  ? -14.722 -10.422 15.029  1.00 16.39 ? 19  THR A CA    1 
ATOM   96   C  C     . THR A 1 40  ? -15.323 -9.014  15.047  1.00 16.36 ? 19  THR A C     1 
ATOM   97   O  O     . THR A 1 40  ? -16.548 -8.899  15.389  1.00 15.56 ? 19  THR A O     1 
ATOM   98   C  CB    . THR A 1 40  ? -13.830 -10.687 16.251  1.00 16.64 ? 19  THR A CB    1 
ATOM   99   O  OG1   . THR A 1 40  ? -13.432 -12.049 16.238  1.00 15.23 ? 19  THR A OG1   1 
ATOM   100  C  CG2   . THR A 1 40  ? -14.504 -10.347 17.562  1.00 17.38 ? 19  THR A CG2   1 
ATOM   101  N  N     . ALA A 1 41  ? -14.556 -7.965  14.711  1.00 16.21 ? 20  ALA A N     1 
ATOM   102  C  CA    . ALA A 1 41  ? -15.041 -6.559  14.769  1.00 15.81 ? 20  ALA A CA    1 
ATOM   103  C  C     . ALA A 1 41  ? -16.224 -6.422  13.789  1.00 16.51 ? 20  ALA A C     1 
ATOM   104  O  O     . ALA A 1 41  ? -17.258 -5.827  14.160  1.00 16.30 ? 20  ALA A O     1 
ATOM   105  C  CB    . ALA A 1 41  ? -13.938 -5.567  14.447  1.00 15.21 ? 20  ALA A CB    1 
ATOM   106  N  N     . ALA A 1 42  ? -16.092 -6.984  12.591  1.00 16.06 ? 21  ALA A N     1 
ATOM   107  C  CA    . ALA A 1 42  ? -17.112 -6.834  11.523  1.00 16.52 ? 21  ALA A CA    1 
ATOM   108  C  C     . ALA A 1 42  ? -18.414 -7.489  11.976  1.00 16.28 ? 21  ALA A C     1 
ATOM   109  O  O     . ALA A 1 42  ? -19.525 -6.896  11.796  1.00 15.74 ? 21  ALA A O     1 
ATOM   110  C  CB    . ALA A 1 42  ? -16.621 -7.436  10.239  1.00 15.97 ? 21  ALA A CB    1 
ATOM   111  N  N     . ARG A 1 43  ? -18.305 -8.699  12.524  1.00 15.57 ? 22  ARG A N     1 
ATOM   112  C  CA    . ARG A 1 43  ? -19.508 -9.450  12.943  1.00 17.16 ? 22  ARG A CA    1 
ATOM   113  C  C     . ARG A 1 43  ? -20.164 -8.711  14.092  1.00 16.32 ? 22  ARG A C     1 
ATOM   114  O  O     . ARG A 1 43  ? -21.388 -8.628  14.085  1.00 17.18 ? 22  ARG A O     1 
ATOM   115  C  CB    . ARG A 1 43  ? -19.182 -10.896 13.289  1.00 17.48 ? 22  ARG A CB    1 
ATOM   116  C  CG    . ARG A 1 43  ? -20.415 -11.689 13.661  1.00 21.90 ? 22  ARG A CG    1 
ATOM   117  C  CD    . ARG A 1 43  ? -20.076 -12.491 14.884  1.00 29.75 ? 22  ARG A CD    1 
ATOM   118  N  NE    . ARG A 1 43  ? -21.048 -13.538 14.930  1.00 36.02 ? 22  ARG A NE    1 
ATOM   119  C  CZ    . ARG A 1 43  ? -20.942 -14.574 15.711  1.00 32.56 ? 22  ARG A CZ    1 
ATOM   120  N  NH1   . ARG A 1 43  ? -19.873 -14.730 16.475  1.00 37.59 ? 22  ARG A NH1   1 
ATOM   121  N  NH2   . ARG A 1 43  ? -21.910 -15.454 15.694  1.00 40.33 ? 22  ARG A NH2   1 
ATOM   122  N  N     . ALA A 1 44  ? -19.403 -8.121  15.022  1.00 15.73 ? 23  ALA A N     1 
ATOM   123  C  CA    . ALA A 1 44  ? -19.987 -7.368  16.157  1.00 16.16 ? 23  ALA A CA    1 
ATOM   124  C  C     . ALA A 1 44  ? -20.714 -6.107  15.634  1.00 16.54 ? 23  ALA A C     1 
ATOM   125  O  O     . ALA A 1 44  ? -21.834 -5.728  16.166  1.00 16.87 ? 23  ALA A O     1 
ATOM   126  C  CB    . ALA A 1 44  ? -18.928 -7.010  17.172  1.00 16.62 ? 23  ALA A CB    1 
ATOM   127  N  N     . VAL A 1 45  ? -20.135 -5.415  14.662  1.00 15.95 ? 24  VAL A N     1 
ATOM   128  C  CA    . VAL A 1 45  ? -20.782 -4.214  14.068  1.00 16.51 ? 24  VAL A CA    1 
ATOM   129  C  C     . VAL A 1 45  ? -22.095 -4.609  13.370  1.00 16.71 ? 24  VAL A C     1 
ATOM   130  O  O     . VAL A 1 45  ? -23.131 -3.928  13.516  1.00 18.75 ? 24  VAL A O     1 
ATOM   131  C  CB    . VAL A 1 45  ? -19.783 -3.552  13.111  1.00 17.06 ? 24  VAL A CB    1 
ATOM   132  C  CG1   . VAL A 1 45  ? -20.450 -2.518  12.248  1.00 17.60 ? 24  VAL A CG1   1 
ATOM   133  C  CG2   . VAL A 1 45  ? -18.645 -2.960  13.940  1.00 19.03 ? 24  VAL A CG2   1 
ATOM   134  N  N     . HIS A 1 46  ? -22.053 -5.683  12.607  1.00 15.60 ? 25  HIS A N     1 
ATOM   135  C  CA    . HIS A 1 46  ? -23.207 -6.229  11.862  1.00 17.04 ? 25  HIS A CA    1 
ATOM   136  C  C     . HIS A 1 46  ? -24.323 -6.617  12.832  1.00 17.28 ? 25  HIS A C     1 
ATOM   137  O  O     . HIS A 1 46  ? -25.470 -6.259  12.591  1.00 16.23 ? 25  HIS A O     1 
ATOM   138  C  CB    . HIS A 1 46  ? -22.795 -7.439  11.029  1.00 17.74 ? 25  HIS A CB    1 
ATOM   139  C  CG    . HIS A 1 46  ? -23.990 -8.108  10.428  1.00 19.64 ? 25  HIS A CG    1 
ATOM   140  N  ND1   . HIS A 1 46  ? -24.810 -7.469  9.506   1.00 20.42 ? 25  HIS A ND1   1 
ATOM   141  C  CD2   . HIS A 1 46  ? -24.493 -9.344  10.602  1.00 21.86 ? 25  HIS A CD2   1 
ATOM   142  C  CE1   . HIS A 1 46  ? -25.781 -8.300  9.150   1.00 22.33 ? 25  HIS A CE1   1 
ATOM   143  N  NE2   . HIS A 1 46  ? -25.643 -9.427  9.846   1.00 20.92 ? 25  HIS A NE2   1 
ATOM   144  N  N     . GLU A 1 47  ? -23.984 -7.307  13.915  1.00 17.62 ? 26  GLU A N     1 
ATOM   145  C  CA    . GLU A 1 47  ? -24.978 -7.793  14.887  1.00 19.61 ? 26  GLU A CA    1 
ATOM   146  C  C     . GLU A 1 47  ? -25.600 -6.613  15.626  1.00 18.96 ? 26  GLU A C     1 
ATOM   147  O  O     . GLU A 1 47  ? -26.749 -6.765  16.053  1.00 19.23 ? 26  GLU A O     1 
ATOM   148  C  CB    . GLU A 1 47  ? -24.340 -8.803  15.830  1.00 23.14 ? 26  GLU A CB    1 
ATOM   149  C  CG    . GLU A 1 47  ? -24.311 -10.187 15.199  1.00 28.94 ? 26  GLU A CG    1 
ATOM   150  C  CD    . GLU A 1 47  ? -23.899 -11.245 16.220  1.00 36.43 ? 26  GLU A CD    1 
ATOM   151  O  OE1   . GLU A 1 47  ? -24.032 -12.445 15.929  1.00 41.34 ? 26  GLU A OE1   1 
ATOM   152  O  OE2   . GLU A 1 47  ? -23.472 -10.852 17.313  1.00 36.44 ? 26  GLU A OE2   1 
ATOM   153  N  N     . ALA A 1 48  ? -24.910 -5.475  15.748  1.00 17.27 ? 27  ALA A N     1 
ATOM   154  C  CA    . ALA A 1 48  ? -25.488 -4.268  16.373  1.00 17.15 ? 27  ALA A CA    1 
ATOM   155  C  C     . ALA A 1 48  ? -26.445 -3.517  15.417  1.00 19.00 ? 27  ALA A C     1 
ATOM   156  O  O     . ALA A 1 48  ? -27.188 -2.624  15.893  1.00 18.84 ? 27  ALA A O     1 
ATOM   157  C  CB    . ALA A 1 48  ? -24.398 -3.374  16.893  1.00 18.91 ? 27  ALA A CB    1 
ATOM   158  N  N     . GLY A 1 49  ? -26.461 -3.872  14.132  1.00 19.62 ? 28  GLY A N     1 
ATOM   159  C  CA    . GLY A 1 49  ? -27.400 -3.375  13.103  1.00 18.99 ? 28  GLY A CA    1 
ATOM   160  C  C     . GLY A 1 49  ? -26.755 -2.376  12.163  1.00 17.37 ? 28  GLY A C     1 
ATOM   161  O  O     . GLY A 1 49  ? -27.453 -1.831  11.282  1.00 18.01 ? 28  GLY A O     1 
ATOM   162  N  N     . ARG A 1 50  ? -25.452 -2.137  12.294  1.00 18.10 ? 29  ARG A N     1 
ATOM   163  C  CA    . ARG A 1 50  ? -24.759 -1.156  11.430  1.00 17.39 ? 29  ARG A CA    1 
ATOM   164  C  C     . ARG A 1 50  ? -24.265 -1.852  10.151  1.00 18.66 ? 29  ARG A C     1 
ATOM   165  O  O     . ARG A 1 50  ? -24.007 -3.081  10.197  1.00 18.44 ? 29  ARG A O     1 
ATOM   166  C  CB    . ARG A 1 50  ? -23.603 -0.512  12.199  1.00 19.58 ? 29  ARG A CB    1 
ATOM   167  C  CG    . ARG A 1 50  ? -24.014 0.211   13.473  1.00 21.43 ? 29  ARG A CG    1 
ATOM   168  C  CD    . ARG A 1 50  ? -24.562 1.572   13.132  1.00 19.86 ? 29  ARG A CD    1 
ATOM   169  N  NE    . ARG A 1 50  ? -24.703 2.331   14.351  1.00 19.57 ? 29  ARG A NE    1 
ATOM   170  C  CZ    . ARG A 1 50  ? -25.289 3.520   14.423  1.00 21.32 ? 29  ARG A CZ    1 
ATOM   171  N  NH1   . ARG A 1 50  ? -25.682 4.120   13.323  1.00 21.44 ? 29  ARG A NH1   1 
ATOM   172  N  NH2   . ARG A 1 50  ? -25.324 4.184   15.575  1.00 23.49 ? 29  ARG A NH2   1 
ATOM   173  N  N     . SER A 1 51  ? -24.063 -1.075  9.073   1.00 16.97 ? 30  SER A N     1 
ATOM   174  C  CA    . SER A 1 51  ? -23.526 -1.562  7.782   1.00 17.66 ? 30  SER A CA    1 
ATOM   175  C  C     . SER A 1 51  ? -21.999 -1.678  7.889   1.00 16.73 ? 30  SER A C     1 
ATOM   176  O  O     . SER A 1 51  ? -21.367 -0.829  8.543   1.00 16.74 ? 30  SER A O     1 
ATOM   177  C  CB    . SER A 1 51  ? -23.991 -0.710  6.591   1.00 18.77 ? 30  SER A CB    1 
ATOM   178  O  OG    . SER A 1 51  ? -23.679 0.654   6.783   1.00 20.33 ? 30  SER A OG    1 
ATOM   179  N  N     . VAL A 1 52  ? -21.421 -2.684  7.239   1.00 17.90 ? 31  VAL A N     1 
ATOM   180  C  CA    . VAL A 1 52  ? -19.970 -2.983  7.377   1.00 17.54 ? 31  VAL A CA    1 
ATOM   181  C  C     . VAL A 1 52  ? -19.433 -3.558  6.059   1.00 18.41 ? 31  VAL A C     1 
ATOM   182  O  O     . VAL A 1 52  ? -20.199 -4.239  5.310   1.00 18.72 ? 31  VAL A O     1 
ATOM   183  C  CB    . VAL A 1 52  ? -19.708 -3.918  8.573   1.00 18.98 ? 31  VAL A CB    1 
ATOM   184  C  CG1   . VAL A 1 52  ? -20.133 -5.347  8.318   1.00 19.07 ? 31  VAL A CG1   1 
ATOM   185  C  CG2   . VAL A 1 52  ? -18.223 -3.857  8.968   1.00 18.01 ? 31  VAL A CG2   1 
ATOM   186  N  N     . LEU A 1 53  ? -18.232 -3.140  5.689   1.00 18.16 ? 32  LEU A N     1 
ATOM   187  C  CA    . LEU A 1 53  ? -17.485 -3.703  4.543   1.00 19.60 ? 32  LEU A CA    1 
ATOM   188  C  C     . LEU A 1 53  ? -16.150 -4.140  5.117   1.00 19.73 ? 32  LEU A C     1 
ATOM   189  O  O     . LEU A 1 53  ? -15.589 -3.370  5.883   1.00 18.15 ? 32  LEU A O     1 
ATOM   190  C  CB    . LEU A 1 53  ? -17.293 -2.625  3.466   1.00 22.19 ? 32  LEU A CB    1 
ATOM   191  C  CG    . LEU A 1 53  ? -18.214 -2.625  2.250   1.00 32.43 ? 32  LEU A CG    1 
ATOM   192  C  CD1   . LEU A 1 53  ? -17.786 -1.544  1.248   1.00 34.34 ? 32  LEU A CD1   1 
ATOM   193  C  CD2   . LEU A 1 53  ? -18.242 -3.976  1.552   1.00 34.91 ? 32  LEU A CD2   1 
ATOM   194  N  N     . VAL A 1 54  ? -15.672 -5.320  4.760   1.00 16.87 ? 33  VAL A N     1 
ATOM   195  C  CA    . VAL A 1 54  ? -14.354 -5.825  5.198   1.00 15.96 ? 33  VAL A CA    1 
ATOM   196  C  C     . VAL A 1 54  ? -13.477 -5.935  3.956   1.00 17.24 ? 33  VAL A C     1 
ATOM   197  O  O     . VAL A 1 54  ? -13.886 -6.632  3.001   1.00 17.38 ? 33  VAL A O     1 
ATOM   198  C  CB    . VAL A 1 54  ? -14.494 -7.188  5.882   1.00 17.25 ? 33  VAL A CB    1 
ATOM   199  C  CG1   . VAL A 1 54  ? -13.148 -7.710  6.301   1.00 17.55 ? 33  VAL A CG1   1 
ATOM   200  C  CG2   . VAL A 1 54  ? -15.455 -7.067  7.053   1.00 19.22 ? 33  VAL A CG2   1 
ATOM   201  N  N     . LEU A 1 55  ? -12.358 -5.236  3.964   1.00 16.34 ? 34  LEU A N     1 
ATOM   202  C  CA    . LEU A 1 55  ? -11.411 -5.227  2.838   1.00 16.96 ? 34  LEU A CA    1 
ATOM   203  C  C     . LEU A 1 55  ? -10.201 -6.061  3.232   1.00 17.09 ? 34  LEU A C     1 
ATOM   204  O  O     . LEU A 1 55  ? -9.505  -5.691  4.185   1.00 17.47 ? 34  LEU A O     1 
ATOM   205  C  CB    . LEU A 1 55  ? -11.045 -3.785  2.515   1.00 18.40 ? 34  LEU A CB    1 
ATOM   206  C  CG    . LEU A 1 55  ? -12.235 -2.861  2.228   1.00 21.16 ? 34  LEU A CG    1 
ATOM   207  C  CD1   . LEU A 1 55  ? -11.737 -1.483  1.796   1.00 20.29 ? 34  LEU A CD1   1 
ATOM   208  C  CD2   . LEU A 1 55  ? -13.151 -3.441  1.164   1.00 19.86 ? 34  LEU A CD2   1 
ATOM   209  N  N     . GLU A 1 56  ? -10.001 -7.163  2.502   1.00 15.12 ? 35  GLU A N     1 
ATOM   210  C  CA    . GLU A 1 56  ? -8.937  -8.142  2.762   1.00 16.05 ? 35  GLU A CA    1 
ATOM   211  C  C     . GLU A 1 56  ? -7.990  -8.234  1.550   1.00 15.97 ? 35  GLU A C     1 
ATOM   212  O  O     . GLU A 1 56  ? -8.459  -8.463  0.403   1.00 14.71 ? 35  GLU A O     1 
ATOM   213  C  CB    . GLU A 1 56  ? -9.554  -9.507  3.061   1.00 16.93 ? 35  GLU A CB    1 
ATOM   214  C  CG    . GLU A 1 56  ? -8.525  -10.624 3.022   1.00 17.24 ? 35  GLU A CG    1 
ATOM   215  C  CD    . GLU A 1 56  ? -7.344  -10.544 3.994   1.00 15.68 ? 35  GLU A CD    1 
ATOM   216  O  OE1   . GLU A 1 56  ? -6.192  -10.856 3.553   1.00 16.72 ? 35  GLU A OE1   1 
ATOM   217  O  OE2   . GLU A 1 56  ? -7.527  -10.060 5.164   1.00 16.35 ? 35  GLU A OE2   1 
ATOM   218  N  N     . ALA A 1 57  ? -6.680  -8.097  1.813   1.00 15.39 ? 36  ALA A N     1 
ATOM   219  C  CA    . ALA A 1 57  ? -5.624  -8.118  0.768   1.00 15.45 ? 36  ALA A CA    1 
ATOM   220  C  C     . ALA A 1 57  ? -5.563  -9.488  0.072   1.00 17.00 ? 36  ALA A C     1 
ATOM   221  O  O     . ALA A 1 57  ? -5.344  -9.525  -1.142  1.00 15.78 ? 36  ALA A O     1 
ATOM   222  C  CB    . ALA A 1 57  ? -4.256  -7.786  1.328   1.00 16.65 ? 36  ALA A CB    1 
ATOM   223  N  N     . ARG A 1 58  ? -5.677  -10.582 0.832   1.00 15.25 ? 37  ARG A N     1 
ATOM   224  C  CA    . ARG A 1 58  ? -5.472  -11.928 0.285   1.00 15.07 ? 37  ARG A CA    1 
ATOM   225  C  C     . ARG A 1 58  ? -6.757  -12.429 -0.391  1.00 15.60 ? 37  ARG A C     1 
ATOM   226  O  O     . ARG A 1 58  ? -7.835  -11.844 -0.213  1.00 15.84 ? 37  ARG A O     1 
ATOM   227  C  CB    . ARG A 1 58  ? -5.044  -12.842 1.432   1.00 14.55 ? 37  ARG A CB    1 
ATOM   228  C  CG    . ARG A 1 58  ? -3.629  -12.592 1.941   1.00 14.52 ? 37  ARG A CG    1 
ATOM   229  C  CD    . ARG A 1 58  ? -3.312  -13.704 2.928   1.00 15.64 ? 37  ARG A CD    1 
ATOM   230  N  NE    . ARG A 1 58  ? -1.965  -13.888 3.451   1.00 15.51 ? 37  ARG A NE    1 
ATOM   231  C  CZ    . ARG A 1 58  ? -1.493  -13.409 4.615   1.00 15.55 ? 37  ARG A CZ    1 
ATOM   232  N  NH1   . ARG A 1 58  ? -2.192  -12.597 5.392   1.00 16.08 ? 37  ARG A NH1   1 
ATOM   233  N  NH2   . ARG A 1 58  ? -0.288  -13.766 5.004   1.00 17.31 ? 37  ARG A NH2   1 
ATOM   234  N  N     . ASP A 1 59  ? -6.617  -13.500 -1.158  1.00 16.62 ? 38  ASP A N     1 
ATOM   235  C  CA    . ASP A 1 59  ? -7.741  -14.257 -1.772  1.00 18.23 ? 38  ASP A CA    1 
ATOM   236  C  C     . ASP A 1 59  ? -8.455  -15.172 -0.763  1.00 17.60 ? 38  ASP A C     1 
ATOM   237  O  O     . ASP A 1 59  ? -9.204  -16.074 -1.193  1.00 17.61 ? 38  ASP A O     1 
ATOM   238  C  CB    . ASP A 1 59  ? -7.237  -15.084 -2.950  1.00 21.31 ? 38  ASP A CB    1 
ATOM   239  C  CG    . ASP A 1 59  ? -6.263  -16.188 -2.608  1.00 24.14 ? 38  ASP A CG    1 
ATOM   240  O  OD1   . ASP A 1 59  ? -5.965  -16.406 -1.402  1.00 23.42 ? 38  ASP A OD1   1 
ATOM   241  O  OD2   . ASP A 1 59  ? -5.815  -16.837 -3.571  1.00 27.50 ? 38  ASP A OD2   1 
ATOM   242  N  N     . ARG A 1 60  ? -8.255  -14.974 0.530   1.00 16.31 ? 39  ARG A N     1 
ATOM   243  C  CA    . ARG A 1 60  ? -8.812  -15.809 1.622   1.00 16.29 ? 39  ARG A CA    1 
ATOM   244  C  C     . ARG A 1 60  ? -8.925  -14.965 2.895   1.00 16.13 ? 39  ARG A C     1 
ATOM   245  O  O     . ARG A 1 60  ? -8.221  -13.989 3.007   1.00 15.09 ? 39  ARG A O     1 
ATOM   246  C  CB    . ARG A 1 60  ? -7.906  -17.025 1.819   1.00 17.80 ? 39  ARG A CB    1 
ATOM   247  C  CG    . ARG A 1 60  ? -6.533  -16.709 2.398   1.00 16.95 ? 39  ARG A CG    1 
ATOM   248  C  CD    . ARG A 1 60  ? -5.694  -17.912 2.774   1.00 16.58 ? 39  ARG A CD    1 
ATOM   249  N  NE    . ARG A 1 60  ? -4.415  -17.478 3.344   1.00 17.23 ? 39  ARG A NE    1 
ATOM   250  C  CZ    . ARG A 1 60  ? -4.229  -17.193 4.626   1.00 15.50 ? 39  ARG A CZ    1 
ATOM   251  N  NH1   . ARG A 1 60  ? -5.245  -17.281 5.460   1.00 16.51 ? 39  ARG A NH1   1 
ATOM   252  N  NH2   . ARG A 1 60  ? -3.060  -16.765 5.047   1.00 13.92 ? 39  ARG A NH2   1 
ATOM   253  N  N     . VAL A 1 61  ? -9.728  -15.429 3.855   1.00 15.05 ? 40  VAL A N     1 
ATOM   254  C  CA    . VAL A 1 61  ? -9.732  -14.911 5.245   1.00 15.69 ? 40  VAL A CA    1 
ATOM   255  C  C     . VAL A 1 61  ? -8.762  -15.767 6.070   1.00 15.04 ? 40  VAL A C     1 
ATOM   256  O  O     . VAL A 1 61  ? -8.314  -16.834 5.574   1.00 14.51 ? 40  VAL A O     1 
ATOM   257  C  CB    . VAL A 1 61  ? -11.152 -14.865 5.839   1.00 16.07 ? 40  VAL A CB    1 
ATOM   258  C  CG1   . VAL A 1 61  ? -12.121 -14.083 4.946   1.00 16.66 ? 40  VAL A CG1   1 
ATOM   259  C  CG2   . VAL A 1 61  ? -11.711 -16.242 6.115   1.00 16.92 ? 40  VAL A CG2   1 
ATOM   260  N  N     . GLY A 1 62  ? -8.483  -15.303 7.295   1.00 15.36 ? 41  GLY A N     1 
ATOM   261  C  CA    . GLY A 1 62  ? -7.742  -16.070 8.316   1.00 15.89 ? 41  GLY A CA    1 
ATOM   262  C  C     . GLY A 1 62  ? -6.417  -15.444 8.655   1.00 15.76 ? 41  GLY A C     1 
ATOM   263  O  O     . GLY A 1 62  ? -5.974  -15.653 9.794   1.00 15.17 ? 41  GLY A O     1 
ATOM   264  N  N     . GLY A 1 63  ? -5.773  -14.755 7.698   1.00 14.95 ? 42  GLY A N     1 
ATOM   265  C  CA    . GLY A 1 63  ? -4.515  -14.022 7.959   1.00 14.56 ? 42  GLY A CA    1 
ATOM   266  C  C     . GLY A 1 63  ? -3.384  -14.922 8.448   1.00 14.61 ? 42  GLY A C     1 
ATOM   267  O  O     . GLY A 1 63  ? -2.901  -15.798 7.652   1.00 13.07 ? 42  GLY A O     1 
ATOM   268  N  N     . ARG A 1 64  ? -2.939  -14.731 9.691   1.00 13.98 ? 43  ARG A N     1 
ATOM   269  C  CA    . ARG A 1 64  ? -1.868  -15.547 10.317  1.00 13.81 ? 43  ARG A CA    1 
ATOM   270  C  C     . ARG A 1 64  ? -2.339  -16.956 10.679  1.00 14.42 ? 43  ARG A C     1 
ATOM   271  O  O     . ARG A 1 64  ? -1.493  -17.718 11.219  1.00 15.54 ? 43  ARG A O     1 
ATOM   272  C  CB    . ARG A 1 64  ? -1.279  -14.793 11.508  1.00 12.95 ? 43  ARG A CB    1 
ATOM   273  C  CG    . ARG A 1 64  ? -0.331  -13.690 11.080  1.00 13.41 ? 43  ARG A CG    1 
ATOM   274  C  CD    . ARG A 1 64  ? 0.219   -12.904 12.265  1.00 12.84 ? 43  ARG A CD    1 
ATOM   275  N  NE    . ARG A 1 64  ? -0.643  -11.783 12.572  1.00 13.63 ? 43  ARG A NE    1 
ATOM   276  C  CZ    . ARG A 1 64  ? -0.395  -10.890 13.529  1.00 15.65 ? 43  ARG A CZ    1 
ATOM   277  N  NH1   . ARG A 1 64  ? 0.592   -11.097 14.381  1.00 15.61 ? 43  ARG A NH1   1 
ATOM   278  N  NH2   . ARG A 1 64  ? -1.148  -9.803  13.647  1.00 15.52 ? 43  ARG A NH2   1 
ATOM   279  N  N     . THR A 1 65  ? -3.605  -17.306 10.442  1.00 14.19 ? 44  THR A N     1 
ATOM   280  C  CA    . THR A 1 65  ? -4.091  -18.712 10.396  1.00 16.77 ? 44  THR A CA    1 
ATOM   281  C  C     . THR A 1 65  ? -4.325  -19.044 8.925   1.00 16.41 ? 44  THR A C     1 
ATOM   282  O  O     . THR A 1 65  ? -4.903  -18.216 8.182   1.00 15.51 ? 44  THR A O     1 
ATOM   283  C  CB    . THR A 1 65  ? -5.309  -18.920 11.323  1.00 17.01 ? 44  THR A CB    1 
ATOM   284  O  OG1   . THR A 1 65  ? -6.486  -18.344 10.724  1.00 16.68 ? 44  THR A OG1   1 
ATOM   285  C  CG2   . THR A 1 65  ? -5.063  -18.354 12.705  1.00 17.96 ? 44  THR A CG2   1 
ATOM   286  N  N     . CYS A 1 66  ? -3.931  -20.232 8.513   1.00 16.36 ? 45  CYS A N     1 
ATOM   287  C  CA    . CYS A 1 66  ? -3.896  -20.617 7.091   1.00 16.35 ? 45  CYS A CA    1 
ATOM   288  C  C     . CYS A 1 66  ? -3.869  -22.120 7.051   1.00 16.26 ? 45  CYS A C     1 
ATOM   289  O  O     . CYS A 1 66  ? -2.938  -22.702 7.697   1.00 15.38 ? 45  CYS A O     1 
ATOM   290  C  CB    . CYS A 1 66  ? -2.691  -20.031 6.373   1.00 19.03 ? 45  CYS A CB    1 
ATOM   291  S  SG    . CYS A 1 66  ? -2.572  -20.584 4.648   1.00 22.86 ? 45  CYS A SG    1 
ATOM   292  N  N     . THR A 1 67  ? -4.864  -22.718 6.399   1.00 16.47 ? 46  THR A N     1 
ATOM   293  C  CA    . THR A 1 67  ? -4.984  -24.190 6.397   1.00 16.26 ? 46  THR A CA    1 
ATOM   294  C  C     . THR A 1 67  ? -5.085  -24.673 4.947   1.00 16.64 ? 46  THR A C     1 
ATOM   295  O  O     . THR A 1 67  ? -5.861  -24.094 4.183   1.00 16.36 ? 46  THR A O     1 
ATOM   296  C  CB    . THR A 1 67  ? -6.219  -24.638 7.175   1.00 16.68 ? 46  THR A CB    1 
ATOM   297  O  OG1   . THR A 1 67  ? -6.225  -24.043 8.484   1.00 15.96 ? 46  THR A OG1   1 
ATOM   298  C  CG2   . THR A 1 67  ? -6.332  -26.146 7.247   1.00 16.49 ? 46  THR A CG2   1 
ATOM   299  N  N     . GLU A 1 68  ? -4.261  -25.650 4.568   1.00 15.84 ? 47  GLU A N     1 
ATOM   300  C  CA    . GLU A 1 68  ? -4.287  -26.252 3.220   1.00 20.22 ? 47  GLU A CA    1 
ATOM   301  C  C     . GLU A 1 68  ? -4.540  -27.749 3.382   1.00 19.77 ? 47  GLU A C     1 
ATOM   302  O  O     . GLU A 1 68  ? -4.043  -28.342 4.360   1.00 18.25 ? 47  GLU A O     1 
ATOM   303  C  CB    . GLU A 1 68  ? -2.970  -26.025 2.487   1.00 20.79 ? 47  GLU A CB    1 
ATOM   304  C  CG    . GLU A 1 68  ? -2.705  -24.571 2.160   1.00 19.89 ? 47  GLU A CG    1 
ATOM   305  C  CD    . GLU A 1 68  ? -1.382  -24.337 1.447   1.00 24.18 ? 47  GLU A CD    1 
ATOM   306  O  OE1   . GLU A 1 68  ? -1.070  -23.165 1.202   1.00 22.71 ? 47  GLU A OE1   1 
ATOM   307  O  OE2   . GLU A 1 68  ? -0.648  -25.332 1.175   1.00 22.49 ? 47  GLU A OE2   1 
ATOM   308  N  N     . GLU A 1 69  ? -5.228  -28.355 2.419   1.00 19.81 ? 48  GLU A N     1 
ATOM   309  C  CA    . GLU A 1 69  ? -5.481  -29.815 2.390   1.00 21.46 ? 48  GLU A CA    1 
ATOM   310  C  C     . GLU A 1 69  ? -4.307  -30.507 1.662   1.00 20.03 ? 48  GLU A C     1 
ATOM   311  O  O     . GLU A 1 69  ? -4.011  -30.128 0.521   1.00 19.53 ? 48  GLU A O     1 
ATOM   312  C  CB    . GLU A 1 69  ? -6.826  -30.059 1.688   1.00 28.47 ? 48  GLU A CB    1 
ATOM   313  C  CG    . GLU A 1 69  ? -7.205  -31.528 1.568   1.00 34.74 ? 48  GLU A CG    1 
ATOM   314  C  CD    . GLU A 1 69  ? -7.953  -32.081 2.774   1.00 46.71 ? 48  GLU A CD    1 
ATOM   315  O  OE1   . GLU A 1 69  ? -8.368  -33.283 2.730   1.00 43.72 ? 48  GLU A OE1   1 
ATOM   316  O  OE2   . GLU A 1 69  ? -8.141  -31.304 3.757   1.00 52.99 ? 48  GLU A OE2   1 
ATOM   317  N  N     . HIS A 1 70  ? -3.606  -31.429 2.318   1.00 17.85 ? 49  HIS A N     1 
ATOM   318  C  CA    . HIS A 1 70  ? -2.497  -32.236 1.723   1.00 18.21 ? 49  HIS A CA    1 
ATOM   319  C  C     . HIS A 1 70  ? -2.605  -33.633 2.326   1.00 20.27 ? 49  HIS A C     1 
ATOM   320  O  O     . HIS A 1 70  ? -2.964  -33.697 3.501   1.00 20.27 ? 49  HIS A O     1 
ATOM   321  C  CB    . HIS A 1 70  ? -1.102  -31.656 2.045   1.00 19.32 ? 49  HIS A CB    1 
ATOM   322  C  CG    . HIS A 1 70  ? -0.859  -30.287 1.529   1.00 20.44 ? 49  HIS A CG    1 
ATOM   323  N  ND1   . HIS A 1 70  ? -0.274  -30.067 0.316   1.00 23.58 ? 49  HIS A ND1   1 
ATOM   324  C  CD2   . HIS A 1 70  ? -1.110  -29.068 2.056   1.00 20.70 ? 49  HIS A CD2   1 
ATOM   325  C  CE1   . HIS A 1 70  ? -0.189  -28.760 0.098   1.00 22.95 ? 49  HIS A CE1   1 
ATOM   326  N  NE2   . HIS A 1 70  ? -0.685  -28.130 1.161   1.00 20.84 ? 49  HIS A NE2   1 
ATOM   327  N  N     . HIS A 1 71  ? -2.384  -34.704 1.543   1.00 19.59 ? 50  HIS A N     1 
ATOM   328  C  CA    . HIS A 1 71  ? -2.319  -36.074 2.089   1.00 19.28 ? 50  HIS A CA    1 
ATOM   329  C  C     . HIS A 1 71  ? -3.629  -36.425 2.798   1.00 20.01 ? 50  HIS A C     1 
ATOM   330  O  O     . HIS A 1 71  ? -3.583  -37.216 3.748   1.00 18.73 ? 50  HIS A O     1 
ATOM   331  C  CB    . HIS A 1 71  ? -1.067  -36.188 2.961   1.00 20.75 ? 50  HIS A CB    1 
ATOM   332  C  CG    . HIS A 1 71  ? 0.153   -35.859 2.179   1.00 21.26 ? 50  HIS A CG    1 
ATOM   333  N  ND1   . HIS A 1 71  ? 0.589   -36.651 1.131   1.00 23.01 ? 50  HIS A ND1   1 
ATOM   334  C  CD2   . HIS A 1 71  ? 0.977   -34.787 2.218   1.00 23.18 ? 50  HIS A CD2   1 
ATOM   335  C  CE1   . HIS A 1 71  ? 1.631   -36.071 0.560   1.00 26.29 ? 50  HIS A CE1   1 
ATOM   336  N  NE2   . HIS A 1 71  ? 1.906   -34.944 1.213   1.00 25.44 ? 50  HIS A NE2   1 
ATOM   337  N  N     . GLY A 1 72  ? -4.757  -35.892 2.319   1.00 20.24 ? 51  GLY A N     1 
ATOM   338  C  CA    . GLY A 1 72  ? -6.108  -36.193 2.824   1.00 21.81 ? 51  GLY A CA    1 
ATOM   339  C  C     . GLY A 1 72  ? -6.393  -35.613 4.201   1.00 23.04 ? 51  GLY A C     1 
ATOM   340  O  O     . GLY A 1 72  ? -7.272  -36.102 4.865   1.00 22.12 ? 51  GLY A O     1 
ATOM   341  N  N     . THR A 1 73  ? -5.638  -34.622 4.663   1.00 19.68 ? 52  THR A N     1 
ATOM   342  C  CA    . THR A 1 73  ? -5.886  -34.000 5.990   1.00 19.40 ? 52  THR A CA    1 
ATOM   343  C  C     . THR A 1 73  ? -5.566  -32.515 5.888   1.00 18.94 ? 52  THR A C     1 
ATOM   344  O  O     . THR A 1 73  ? -5.101  -32.045 4.844   1.00 19.76 ? 52  THR A O     1 
ATOM   345  C  CB    . THR A 1 73  ? -5.084  -34.710 7.117   1.00 18.68 ? 52  THR A CB    1 
ATOM   346  O  OG1   . THR A 1 73  ? -5.492  -34.303 8.426   1.00 18.17 ? 52  THR A OG1   1 
ATOM   347  C  CG2   . THR A 1 73  ? -3.601  -34.464 6.966   1.00 17.70 ? 52  THR A CG2   1 
ATOM   348  N  N     . TRP A 1 74  ? -5.776  -31.810 6.995   1.00 17.34 ? 53  TRP A N     1 
ATOM   349  C  CA    . TRP A 1 74  ? -5.540  -30.361 7.078   1.00 15.73 ? 53  TRP A CA    1 
ATOM   350  C  C     . TRP A 1 74  ? -4.118  -30.101 7.530   1.00 14.12 ? 53  TRP A C     1 
ATOM   351  O  O     . TRP A 1 74  ? -3.635  -30.771 8.469   1.00 14.66 ? 53  TRP A O     1 
ATOM   352  C  CB    . TRP A 1 74  ? -6.550  -29.720 8.039   1.00 15.77 ? 53  TRP A CB    1 
ATOM   353  C  CG    . TRP A 1 74  ? -6.598  -30.314 9.410   1.00 16.26 ? 53  TRP A CG    1 
ATOM   354  C  CD1   . TRP A 1 74  ? -5.876  -29.930 10.516  1.00 15.41 ? 53  TRP A CD1   1 
ATOM   355  C  CD2   . TRP A 1 74  ? -7.364  -31.456 9.818   1.00 16.40 ? 53  TRP A CD2   1 
ATOM   356  N  NE1   . TRP A 1 74  ? -6.186  -30.737 11.576  1.00 15.92 ? 53  TRP A NE1   1 
ATOM   357  C  CE2   . TRP A 1 74  ? -7.101  -31.665 11.185  1.00 15.78 ? 53  TRP A CE2   1 
ATOM   358  C  CE3   . TRP A 1 74  ? -8.295  -32.266 9.169   1.00 17.42 ? 53  TRP A CE3   1 
ATOM   359  C  CZ2   . TRP A 1 74  ? -7.703  -32.679 11.923  1.00 15.39 ? 53  TRP A CZ2   1 
ATOM   360  C  CZ3   . TRP A 1 74  ? -8.904  -33.258 9.913   1.00 19.54 ? 53  TRP A CZ3   1 
ATOM   361  C  CH2   . TRP A 1 74  ? -8.619  -33.450 11.260  1.00 16.32 ? 53  TRP A CH2   1 
ATOM   362  N  N     . ILE A 1 75  ? -3.482  -29.126 6.893   1.00 15.41 ? 54  ILE A N     1 
ATOM   363  C  CA    . ILE A 1 75  ? -2.133  -28.652 7.299   1.00 14.68 ? 54  ILE A CA    1 
ATOM   364  C  C     . ILE A 1 75  ? -2.322  -27.211 7.756   1.00 14.33 ? 54  ILE A C     1 
ATOM   365  O  O     . ILE A 1 75  ? -2.560  -26.344 6.879   1.00 15.00 ? 54  ILE A O     1 
ATOM   366  C  CB    . ILE A 1 75  ? -1.137  -28.758 6.150   1.00 15.96 ? 54  ILE A CB    1 
ATOM   367  C  CG1   . ILE A 1 75  ? -1.111  -30.168 5.559   1.00 16.77 ? 54  ILE A CG1   1 
ATOM   368  C  CG2   . ILE A 1 75  ? 0.233   -28.288 6.581   1.00 15.66 ? 54  ILE A CG2   1 
ATOM   369  C  CD1   . ILE A 1 75  ? -0.682  -31.243 6.540   1.00 17.10 ? 54  ILE A CD1   1 
ATOM   370  N  N     . ASP A 1 76  ? -2.148  -26.967 9.043   1.00 14.76 ? 55  ASP A N     1 
ATOM   371  C  CA    . ASP A 1 76  ? -2.180  -25.584 9.603   1.00 13.50 ? 55  ASP A CA    1 
ATOM   372  C  C     . ASP A 1 76  ? -0.795  -24.961 9.423   1.00 13.95 ? 55  ASP A C     1 
ATOM   373  O  O     . ASP A 1 76  ? 0.121   -25.265 10.222  1.00 14.79 ? 55  ASP A O     1 
ATOM   374  C  CB    . ASP A 1 76  ? -2.630  -25.581 11.055  1.00 14.06 ? 55  ASP A CB    1 
ATOM   375  C  CG    . ASP A 1 76  ? -4.126  -25.530 11.298  1.00 13.58 ? 55  ASP A CG    1 
ATOM   376  O  OD1   . ASP A 1 76  ? -4.847  -24.737 10.609  1.00 13.75 ? 55  ASP A OD1   1 
ATOM   377  O  OD2   . ASP A 1 76  ? -4.592  -26.355 12.094  1.00 15.72 ? 55  ASP A OD2   1 
ATOM   378  N  N     . LEU A 1 77  ? -0.640  -24.096 8.426   1.00 14.02 ? 56  LEU A N     1 
ATOM   379  C  CA    . LEU A 1 77  ? 0.648   -23.402 8.135   1.00 16.06 ? 56  LEU A CA    1 
ATOM   380  C  C     . LEU A 1 77  ? 0.812   -22.213 9.080   1.00 17.01 ? 56  LEU A C     1 
ATOM   381  O  O     . LEU A 1 77  ? 1.927   -21.793 9.285   1.00 14.50 ? 56  LEU A O     1 
ATOM   382  C  CB    . LEU A 1 77  ? 0.668   -22.967 6.683   1.00 17.64 ? 56  LEU A CB    1 
ATOM   383  C  CG    . LEU A 1 77  ? 0.861   -24.135 5.712   1.00 19.42 ? 56  LEU A CG    1 
ATOM   384  C  CD1   . LEU A 1 77  ? 0.739   -23.633 4.310   1.00 24.99 ? 56  LEU A CD1   1 
ATOM   385  C  CD2   . LEU A 1 77  ? 2.173   -24.850 5.966   1.00 20.70 ? 56  LEU A CD2   1 
ATOM   386  N  N     . GLY A 1 78  ? -0.287  -21.722 9.645   1.00 16.02 ? 57  GLY A N     1 
ATOM   387  C  CA    . GLY A 1 78  ? -0.246  -20.630 10.639  1.00 16.15 ? 57  GLY A CA    1 
ATOM   388  C  C     . GLY A 1 78  ? -0.669  -21.121 12.009  1.00 16.30 ? 57  GLY A C     1 
ATOM   389  O  O     . GLY A 1 78  ? -0.400  -22.302 12.355  1.00 15.99 ? 57  GLY A O     1 
ATOM   390  N  N     . GLY A 1 79  ? -1.327  -20.279 12.801  1.00 14.75 ? 58  GLY A N     1 
ATOM   391  C  CA    . GLY A 1 79  ? -1.699  -20.688 14.160  1.00 15.78 ? 58  GLY A CA    1 
ATOM   392  C  C     . GLY A 1 79  ? -2.615  -21.884 14.198  1.00 14.75 ? 58  GLY A C     1 
ATOM   393  O  O     . GLY A 1 79  ? -3.489  -22.037 13.325  1.00 15.27 ? 58  GLY A O     1 
ATOM   394  N  N     . GLN A 1 80  ? -2.335  -22.797 15.102  1.00 16.34 ? 59  GLN A N     1 
ATOM   395  C  CA    . GLN A 1 80  ? -3.038  -24.103 15.113  1.00 16.91 ? 59  GLN A CA    1 
ATOM   396  C  C     . GLN A 1 80  ? -3.607  -24.487 16.480  1.00 16.90 ? 59  GLN A C     1 
ATOM   397  O  O     . GLN A 1 80  ? -4.537  -25.305 16.465  1.00 16.50 ? 59  GLN A O     1 
ATOM   398  C  CB    . GLN A 1 80  ? -2.137  -25.213 14.580  1.00 16.61 ? 59  GLN A CB    1 
ATOM   399  C  CG    . GLN A 1 80  ? -1.034  -25.695 15.505  1.00 17.70 ? 59  GLN A CG    1 
ATOM   400  C  CD    . GLN A 1 80  ? -0.243  -26.815 14.884  1.00 18.18 ? 59  GLN A CD    1 
ATOM   401  O  OE1   . GLN A 1 80  ? -0.051  -26.889 13.688  1.00 17.10 ? 59  GLN A OE1   1 
ATOM   402  N  NE2   . GLN A 1 80  ? 0.190   -27.754 15.716  1.00 18.41 ? 59  GLN A NE2   1 
ATOM   403  N  N     . TRP A 1 81  ? -3.058  -23.999 17.602  1.00 16.92 ? 60  TRP A N     1 
ATOM   404  C  CA    . TRP A 1 81  ? -3.364  -24.518 18.958  1.00 16.26 ? 60  TRP A CA    1 
ATOM   405  C  C     . TRP A 1 81  ? -4.270  -23.532 19.704  1.00 16.75 ? 60  TRP A C     1 
ATOM   406  O  O     . TRP A 1 81  ? -4.058  -22.296 19.603  1.00 16.72 ? 60  TRP A O     1 
ATOM   407  C  CB    . TRP A 1 81  ? -2.103  -24.694 19.778  1.00 15.35 ? 60  TRP A CB    1 
ATOM   408  C  CG    . TRP A 1 81  ? -1.291  -25.921 19.480  1.00 17.82 ? 60  TRP A CG    1 
ATOM   409  C  CD1   . TRP A 1 81  ? -1.640  -27.233 19.673  1.00 18.73 ? 60  TRP A CD1   1 
ATOM   410  C  CD2   . TRP A 1 81  ? 0.057   -25.931 19.007  1.00 17.06 ? 60  TRP A CD2   1 
ATOM   411  N  NE1   . TRP A 1 81  ? -0.590  -28.058 19.342  1.00 16.72 ? 60  TRP A NE1   1 
ATOM   412  C  CE2   . TRP A 1 81  ? 0.485   -27.283 18.996  1.00 17.65 ? 60  TRP A CE2   1 
ATOM   413  C  CE3   . TRP A 1 81  ? 0.961   -24.917 18.685  1.00 20.49 ? 60  TRP A CE3   1 
ATOM   414  C  CZ2   . TRP A 1 81  ? 1.765   -27.630 18.588  1.00 20.00 ? 60  TRP A CZ2   1 
ATOM   415  C  CZ3   . TRP A 1 81  ? 2.237   -25.263 18.311  1.00 20.45 ? 60  TRP A CZ3   1 
ATOM   416  C  CH2   . TRP A 1 81  ? 2.632   -26.598 18.276  1.00 19.07 ? 60  TRP A CH2   1 
ATOM   417  N  N     . ILE A 1 82  ? -5.131  -24.065 20.555  1.00 15.65 ? 61  ILE A N     1 
ATOM   418  C  CA    . ILE A 1 82  ? -5.849  -23.279 21.587  1.00 17.35 ? 61  ILE A CA    1 
ATOM   419  C  C     . ILE A 1 82  ? -5.709  -24.043 22.900  1.00 16.74 ? 61  ILE A C     1 
ATOM   420  O  O     . ILE A 1 82  ? -5.355  -25.227 22.888  1.00 19.06 ? 61  ILE A O     1 
ATOM   421  C  CB    . ILE A 1 82  ? -7.305  -23.004 21.194  1.00 17.70 ? 61  ILE A CB    1 
ATOM   422  C  CG1   . ILE A 1 82  ? -8.192  -24.244 21.333  1.00 20.47 ? 61  ILE A CG1   1 
ATOM   423  C  CG2   . ILE A 1 82  ? -7.405  -22.357 19.806  1.00 19.10 ? 61  ILE A CG2   1 
ATOM   424  C  CD1   . ILE A 1 82  ? -9.667  -23.927 21.076  1.00 20.48 ? 61  ILE A CD1   1 
ATOM   425  N  N     . GLY A 1 83  ? -5.830  -23.341 24.005  1.00 17.52 ? 62  GLY A N     1 
ATOM   426  C  CA    . GLY A 1 83  ? -5.522  -23.951 25.293  1.00 17.62 ? 62  GLY A CA    1 
ATOM   427  C  C     . GLY A 1 83  ? -6.377  -23.329 26.374  1.00 18.62 ? 62  GLY A C     1 
ATOM   428  O  O     . GLY A 1 83  ? -7.128  -22.382 26.130  1.00 17.02 ? 62  GLY A O     1 
ATOM   429  N  N     . PRO A 1 84  ? -6.331  -23.940 27.559  1.00 19.73 ? 63  PRO A N     1 
ATOM   430  C  CA    . PRO A 1 84  ? -7.155  -23.477 28.679  1.00 21.20 ? 63  PRO A CA    1 
ATOM   431  C  C     . PRO A 1 84  ? -6.824  -22.039 29.048  1.00 18.15 ? 63  PRO A C     1 
ATOM   432  O  O     . PRO A 1 84  ? -5.650  -21.646 29.002  1.00 19.26 ? 63  PRO A O     1 
ATOM   433  C  CB    . PRO A 1 84  ? -6.845  -24.469 29.832  1.00 24.01 ? 63  PRO A CB    1 
ATOM   434  C  CG    . PRO A 1 84  ? -5.667  -25.298 29.359  1.00 22.11 ? 63  PRO A CG    1 
ATOM   435  C  CD    . PRO A 1 84  ? -5.564  -25.164 27.854  1.00 22.46 ? 63  PRO A CD    1 
ATOM   436  N  N     . GLY A 1 85  ? -7.860  -21.251 29.346  1.00 19.21 ? 64  GLY A N     1 
ATOM   437  C  CA    . GLY A 1 85  ? -7.723  -19.812 29.655  1.00 18.56 ? 64  GLY A CA    1 
ATOM   438  C  C     . GLY A 1 85  ? -8.061  -18.942 28.436  1.00 17.98 ? 64  GLY A C     1 
ATOM   439  O  O     . GLY A 1 85  ? -8.408  -17.767 28.638  1.00 17.83 ? 64  GLY A O     1 
ATOM   440  N  N     . GLN A 1 86  ? -8.042  -19.523 27.217  1.00 18.11 ? 65  GLN A N     1 
ATOM   441  C  CA    . GLN A 1 86  ? -8.306  -18.771 25.954  1.00 16.17 ? 65  GLN A CA    1 
ATOM   442  C  C     . GLN A 1 86  ? -9.804  -18.921 25.715  1.00 18.03 ? 65  GLN A C     1 
ATOM   443  O  O     . GLN A 1 86  ? -10.243 -19.738 24.851  1.00 17.44 ? 65  GLN A O     1 
ATOM   444  C  CB    . GLN A 1 86  ? -7.467  -19.322 24.807  1.00 16.24 ? 65  GLN A CB    1 
ATOM   445  C  CG    . GLN A 1 86  ? -5.967  -19.210 25.022  1.00 16.53 ? 65  GLN A CG    1 
ATOM   446  C  CD    . GLN A 1 86  ? -5.190  -19.840 23.890  1.00 16.33 ? 65  GLN A CD    1 
ATOM   447  O  OE1   . GLN A 1 86  ? -5.762  -20.515 23.036  1.00 14.75 ? 65  GLN A OE1   1 
ATOM   448  N  NE2   . GLN A 1 86  ? -3.877  -19.643 23.880  1.00 16.87 ? 65  GLN A NE2   1 
ATOM   449  N  N     . ASP A 1 87  ? -10.576 -18.194 26.486  1.00 17.68 ? 66  ASP A N     1 
ATOM   450  C  CA    . ASP A 1 87  ? -12.049 -18.398 26.526  1.00 20.07 ? 66  ASP A CA    1 
ATOM   451  C  C     . ASP A 1 87  ? -12.738 -17.827 25.268  1.00 17.75 ? 66  ASP A C     1 
ATOM   452  O  O     . ASP A 1 87  ? -13.834 -18.286 24.951  1.00 17.80 ? 66  ASP A O     1 
ATOM   453  C  CB    . ASP A 1 87  ? -12.647 -17.805 27.796  1.00 21.50 ? 66  ASP A CB    1 
ATOM   454  C  CG    . ASP A 1 87  ? -12.307 -16.354 28.064  1.00 23.56 ? 66  ASP A CG    1 
ATOM   455  O  OD1   . ASP A 1 87  ? -13.232 -15.544 28.059  1.00 32.17 ? 66  ASP A OD1   1 
ATOM   456  O  OD2   . ASP A 1 87  ? -11.122 -16.030 28.256  1.00 30.28 ? 66  ASP A OD2   1 
ATOM   457  N  N     . ARG A 1 88  ? -12.180 -16.813 24.602  1.00 16.16 ? 67  ARG A N     1 
ATOM   458  C  CA    . ARG A 1 88  ? -12.867 -16.161 23.471  1.00 17.32 ? 67  ARG A CA    1 
ATOM   459  C  C     . ARG A 1 88  ? -12.846 -17.135 22.278  1.00 17.54 ? 67  ARG A C     1 
ATOM   460  O  O     . ARG A 1 88  ? -13.905 -17.326 21.606  1.00 20.18 ? 67  ARG A O     1 
ATOM   461  C  CB    . ARG A 1 88  ? -12.212 -14.804 23.145  1.00 20.01 ? 67  ARG A CB    1 
ATOM   462  C  CG    . ARG A 1 88  ? -12.428 -13.674 24.160  1.00 23.36 ? 67  ARG A CG    1 
ATOM   463  C  CD    . ARG A 1 88  ? -11.742 -13.788 25.542  1.00 31.10 ? 67  ARG A CD    1 
ATOM   464  N  NE    . ARG A 1 88  ? -10.280 -13.637 25.403  1.00 36.47 ? 67  ARG A NE    1 
ATOM   465  C  CZ    . ARG A 1 88  ? -9.556  -12.504 25.557  1.00 32.76 ? 67  ARG A CZ    1 
ATOM   466  N  NH1   . ARG A 1 88  ? -10.120 -11.384 25.995  1.00 33.16 ? 67  ARG A NH1   1 
ATOM   467  N  NH2   . ARG A 1 88  ? -8.263  -12.509 25.255  1.00 22.40 ? 67  ARG A NH2   1 
ATOM   468  N  N     . VAL A 1 89  ? -11.703 -17.760 22.006  1.00 17.48 ? 68  VAL A N     1 
ATOM   469  C  CA    . VAL A 1 89  ? -11.589 -18.712 20.872  1.00 17.06 ? 68  VAL A CA    1 
ATOM   470  C  C     . VAL A 1 89  ? -12.378 -19.976 21.209  1.00 18.99 ? 68  VAL A C     1 
ATOM   471  O  O     . VAL A 1 89  ? -13.023 -20.554 20.282  1.00 17.86 ? 68  VAL A O     1 
ATOM   472  C  CB    . VAL A 1 89  ? -10.134 -19.002 20.449  1.00 17.01 ? 68  VAL A CB    1 
ATOM   473  C  CG1   . VAL A 1 89  ? -9.333  -19.814 21.455  1.00 17.13 ? 68  VAL A CG1   1 
ATOM   474  C  CG2   . VAL A 1 89  ? -10.134 -19.701 19.092  1.00 17.01 ? 68  VAL A CG2   1 
ATOM   475  N  N     . ALA A 1 90  ? -12.335 -20.417 22.458  1.00 18.33 ? 69  ALA A N     1 
ATOM   476  C  CA    . ALA A 1 90  ? -13.086 -21.620 22.884  1.00 18.15 ? 69  ALA A CA    1 
ATOM   477  C  C     . ALA A 1 90  ? -14.575 -21.377 22.642  1.00 18.19 ? 69  ALA A C     1 
ATOM   478  O  O     . ALA A 1 90  ? -15.241 -22.212 22.023  1.00 16.28 ? 69  ALA A O     1 
ATOM   479  C  CB    . ALA A 1 90  ? -12.794 -21.901 24.322  1.00 20.76 ? 69  ALA A CB    1 
ATOM   480  N  N     . ALA A 1 91  ? -15.108 -20.263 23.133  1.00 17.88 ? 70  ALA A N     1 
ATOM   481  C  CA    . ALA A 1 91  ? -16.517 -19.902 22.903  1.00 18.49 ? 70  ALA A CA    1 
ATOM   482  C  C     . ALA A 1 91  ? -16.837 -19.829 21.401  1.00 18.58 ? 70  ALA A C     1 
ATOM   483  O  O     . ALA A 1 91  ? -17.935 -20.287 21.020  1.00 18.36 ? 70  ALA A O     1 
ATOM   484  C  CB    . ALA A 1 91  ? -16.813 -18.617 23.629  1.00 18.13 ? 70  ALA A CB    1 
ATOM   485  N  N     . LEU A 1 92  ? -15.962 -19.234 20.560  1.00 16.42 ? 71  LEU A N     1 
ATOM   486  C  CA    . LEU A 1 92  ? -16.241 -19.039 19.119  1.00 17.63 ? 71  LEU A CA    1 
ATOM   487  C  C     . LEU A 1 92  ? -16.330 -20.433 18.477  1.00 17.04 ? 71  LEU A C     1 
ATOM   488  O  O     . LEU A 1 92  ? -17.266 -20.700 17.667  1.00 18.99 ? 71  LEU A O     1 
ATOM   489  C  CB    . LEU A 1 92  ? -15.120 -18.223 18.462  1.00 19.24 ? 71  LEU A CB    1 
ATOM   490  C  CG    . LEU A 1 92  ? -15.318 -17.885 16.977  1.00 20.84 ? 71  LEU A CG    1 
ATOM   491  C  CD1   . LEU A 1 92  ? -16.569 -17.023 16.792  1.00 20.73 ? 71  LEU A CD1   1 
ATOM   492  C  CD2   . LEU A 1 92  ? -14.091 -17.162 16.444  1.00 19.74 ? 71  LEU A CD2   1 
ATOM   493  N  N     . ALA A 1 93  ? -15.393 -21.323 18.823  1.00 19.17 ? 72  ALA A N     1 
ATOM   494  C  CA    . ALA A 1 93  ? -15.354 -22.669 18.190  1.00 18.95 ? 72  ALA A CA    1 
ATOM   495  C  C     . ALA A 1 93  ? -16.618 -23.453 18.584  1.00 19.45 ? 72  ALA A C     1 
ATOM   496  O  O     . ALA A 1 93  ? -17.208 -24.150 17.704  1.00 23.42 ? 72  ALA A O     1 
ATOM   497  C  CB    . ALA A 1 93  ? -14.108 -23.450 18.578  1.00 19.34 ? 72  ALA A CB    1 
ATOM   498  N  N     . ALA A 1 94  ? -17.096 -23.288 19.807  1.00 19.98 ? 73  ALA A N     1 
ATOM   499  C  CA    . ALA A 1 94  ? -18.318 -23.989 20.301  1.00 20.13 ? 73  ALA A CA    1 
ATOM   500  C  C     . ALA A 1 94  ? -19.535 -23.380 19.583  1.00 20.28 ? 73  ALA A C     1 
ATOM   501  O  O     . ALA A 1 94  ? -20.374 -24.144 19.078  1.00 20.93 ? 73  ALA A O     1 
ATOM   502  C  CB    . ALA A 1 94  ? -18.422 -23.877 21.795  1.00 20.55 ? 73  ALA A CB    1 
ATOM   503  N  N     . GLU A 1 95  ? -19.577 -22.052 19.467  1.00 18.93 ? 74  GLU A N     1 
ATOM   504  C  CA    . GLU A 1 95  ? -20.671 -21.345 18.749  1.00 21.38 ? 74  GLU A CA    1 
ATOM   505  C  C     . GLU A 1 95  ? -20.773 -21.826 17.296  1.00 24.00 ? 74  GLU A C     1 
ATOM   506  O  O     . GLU A 1 95  ? -21.892 -22.134 16.861  1.00 20.70 ? 74  GLU A O     1 
ATOM   507  C  CB    . GLU A 1 95  ? -20.479 -19.846 18.843  1.00 23.85 ? 74  GLU A CB    1 
ATOM   508  C  CG    . GLU A 1 95  ? -21.590 -19.100 18.135  1.00 27.27 ? 74  GLU A CG    1 
ATOM   509  C  CD    . GLU A 1 95  ? -21.321 -17.641 17.843  1.00 31.83 ? 74  GLU A CD    1 
ATOM   510  O  OE1   . GLU A 1 95  ? -22.274 -16.994 17.357  1.00 35.24 ? 74  GLU A OE1   1 
ATOM   511  O  OE2   . GLU A 1 95  ? -20.190 -17.146 18.110  1.00 29.66 ? 74  GLU A OE2   1 
ATOM   512  N  N     . LEU A 1 96  ? -19.656 -21.917 16.552  1.00 19.70 ? 75  LEU A N     1 
ATOM   513  C  CA    . LEU A 1 96  ? -19.667 -22.172 15.107  1.00 22.21 ? 75  LEU A CA    1 
ATOM   514  C  C     . LEU A 1 96  ? -19.560 -23.650 14.773  1.00 20.87 ? 75  LEU A C     1 
ATOM   515  O  O     . LEU A 1 96  ? -19.520 -23.938 13.588  1.00 23.32 ? 75  LEU A O     1 
ATOM   516  C  CB    . LEU A 1 96  ? -18.562 -21.333 14.479  1.00 21.25 ? 75  LEU A CB    1 
ATOM   517  C  CG    . LEU A 1 96  ? -18.754 -19.824 14.619  1.00 22.79 ? 75  LEU A CG    1 
ATOM   518  C  CD1   . LEU A 1 96  ? -17.609 -19.085 13.937  1.00 22.33 ? 75  LEU A CD1   1 
ATOM   519  C  CD2   . LEU A 1 96  ? -20.087 -19.330 14.084  1.00 25.02 ? 75  LEU A CD2   1 
ATOM   520  N  N     . GLY A 1 97  ? -19.522 -24.537 15.774  1.00 21.83 ? 76  GLY A N     1 
ATOM   521  C  CA    . GLY A 1 97  ? -19.572 -25.996 15.607  1.00 22.96 ? 76  GLY A CA    1 
ATOM   522  C  C     . GLY A 1 97  ? -18.245 -26.626 15.205  1.00 23.21 ? 76  GLY A C     1 
ATOM   523  O  O     . GLY A 1 97  ? -18.279 -27.640 14.496  1.00 23.56 ? 76  GLY A O     1 
ATOM   524  N  N     . VAL A 1 98  ? -17.107 -26.073 15.610  1.00 19.22 ? 77  VAL A N     1 
ATOM   525  C  CA    . VAL A 1 98  ? -15.786 -26.686 15.279  1.00 20.79 ? 77  VAL A CA    1 
ATOM   526  C  C     . VAL A 1 98  ? -15.283 -27.432 16.507  1.00 21.11 ? 77  VAL A C     1 
ATOM   527  O  O     . VAL A 1 98  ? -15.169 -26.797 17.577  1.00 21.45 ? 77  VAL A O     1 
ATOM   528  C  CB    . VAL A 1 98  ? -14.764 -25.646 14.806  1.00 19.05 ? 77  VAL A CB    1 
ATOM   529  C  CG1   . VAL A 1 98  ? -13.395 -26.285 14.594  1.00 20.42 ? 77  VAL A CG1   1 
ATOM   530  C  CG2   . VAL A 1 98  ? -15.242 -24.991 13.522  1.00 19.34 ? 77  VAL A CG2   1 
ATOM   531  N  N     . GLU A 1 99  ? -15.056 -28.724 16.369  1.00 19.80 ? 78  GLU A N     1 
ATOM   532  C  CA    . GLU A 1 99  ? -14.649 -29.617 17.483  1.00 23.64 ? 78  GLU A CA    1 
ATOM   533  C  C     . GLU A 1 99  ? -13.137 -29.510 17.685  1.00 21.45 ? 78  GLU A C     1 
ATOM   534  O  O     . GLU A 1 99  ? -12.440 -29.110 16.766  1.00 20.60 ? 78  GLU A O     1 
ATOM   535  C  CB    . GLU A 1 99  ? -15.073 -31.058 17.172  1.00 29.07 ? 78  GLU A CB    1 
ATOM   536  C  CG    . GLU A 1 99  ? -16.573 -31.215 16.938  1.00 35.23 ? 78  GLU A CG    1 
ATOM   537  C  CD    . GLU A 1 99  ? -17.514 -30.728 18.046  1.00 46.37 ? 78  GLU A CD    1 
ATOM   538  O  OE1   . GLU A 1 99  ? -17.144 -30.782 19.263  1.00 47.10 ? 78  GLU A OE1   1 
ATOM   539  O  OE2   . GLU A 1 99  ? -18.654 -30.305 17.694  1.00 63.43 ? 78  GLU A OE2   1 
ATOM   540  N  N     . THR A 1 100 ? -12.647 -29.857 18.863  1.00 20.67 ? 79  THR A N     1 
ATOM   541  C  CA    . THR A 1 100 ? -11.203 -29.896 19.161  1.00 20.87 ? 79  THR A CA    1 
ATOM   542  C  C     . THR A 1 100 ? -10.726 -31.343 19.196  1.00 20.68 ? 79  THR A C     1 
ATOM   543  O  O     . THR A 1 100 ? -11.537 -32.264 19.371  1.00 20.93 ? 79  THR A O     1 
ATOM   544  C  CB    . THR A 1 100 ? -10.890 -29.171 20.470  1.00 22.71 ? 79  THR A CB    1 
ATOM   545  O  OG1   . THR A 1 100 ? -11.468 -29.878 21.592  1.00 22.79 ? 79  THR A OG1   1 
ATOM   546  C  CG2   . THR A 1 100 ? -11.385 -27.740 20.441  1.00 27.10 ? 79  THR A CG2   1 
ATOM   547  N  N     . TYR A 1 101 ? -9.431  -31.536 19.077  1.00 16.68 ? 80  TYR A N     1 
ATOM   548  C  CA    . TYR A 1 101 ? -8.777  -32.814 19.405  1.00 17.09 ? 80  TYR A CA    1 
ATOM   549  C  C     . TYR A 1 101 ? -7.542  -32.473 20.185  1.00 16.84 ? 80  TYR A C     1 
ATOM   550  O  O     . TYR A 1 101 ? -6.983  -31.390 20.031  1.00 16.56 ? 80  TYR A O     1 
ATOM   551  C  CB    . TYR A 1 101 ? -8.416  -33.669 18.186  1.00 17.59 ? 80  TYR A CB    1 
ATOM   552  C  CG    . TYR A 1 101 ? -7.512  -33.050 17.149  1.00 15.40 ? 80  TYR A CG    1 
ATOM   553  C  CD1   . TYR A 1 101 ? -7.987  -32.114 16.231  1.00 15.04 ? 80  TYR A CD1   1 
ATOM   554  C  CD2   . TYR A 1 101 ? -6.199  -33.441 17.039  1.00 17.16 ? 80  TYR A CD2   1 
ATOM   555  C  CE1   . TYR A 1 101 ? -7.186  -31.608 15.216  1.00 14.91 ? 80  TYR A CE1   1 
ATOM   556  C  CE2   . TYR A 1 101 ? -5.367  -32.912 16.056  1.00 16.23 ? 80  TYR A CE2   1 
ATOM   557  C  CZ    . TYR A 1 101 ? -5.868  -32.028 15.115  1.00 16.57 ? 80  TYR A CZ    1 
ATOM   558  O  OH    . TYR A 1 101 ? -5.016  -31.521 14.169  1.00 18.41 ? 80  TYR A OH    1 
ATOM   559  N  N     . PRO A 1 102 ? -7.115  -33.355 21.098  1.00 17.65 ? 81  PRO A N     1 
ATOM   560  C  CA    . PRO A 1 102 ? -6.001  -33.019 21.966  1.00 18.66 ? 81  PRO A CA    1 
ATOM   561  C  C     . PRO A 1 102 ? -4.662  -33.169 21.246  1.00 17.18 ? 81  PRO A C     1 
ATOM   562  O  O     . PRO A 1 102 ? -4.460  -34.124 20.444  1.00 18.93 ? 81  PRO A O     1 
ATOM   563  C  CB    . PRO A 1 102 ? -6.147  -34.022 23.133  1.00 20.49 ? 81  PRO A CB    1 
ATOM   564  C  CG    . PRO A 1 102 ? -6.829  -35.194 22.511  1.00 21.85 ? 81  PRO A CG    1 
ATOM   565  C  CD    . PRO A 1 102 ? -7.792  -34.598 21.510  1.00 21.35 ? 81  PRO A CD    1 
ATOM   566  N  N     . GLN A 1 103 ? -3.738  -32.242 21.547  1.00 16.22 ? 82  GLN A N     1 
ATOM   567  C  CA    . GLN A 1 103 ? -2.314  -32.442 21.201  1.00 17.39 ? 82  GLN A CA    1 
ATOM   568  C  C     . GLN A 1 103 ? -1.834  -33.721 21.886  1.00 17.70 ? 82  GLN A C     1 
ATOM   569  O  O     . GLN A 1 103 ? -1.890  -33.819 23.101  1.00 19.30 ? 82  GLN A O     1 
ATOM   570  C  CB    . GLN A 1 103 ? -1.490  -31.236 21.659  1.00 17.66 ? 82  GLN A CB    1 
ATOM   571  C  CG    . GLN A 1 103 ? -0.001  -31.439 21.459  1.00 17.54 ? 82  GLN A CG    1 
ATOM   572  C  CD    . GLN A 1 103 ? 0.406   -31.574 20.007  1.00 17.69 ? 82  GLN A CD    1 
ATOM   573  O  OE1   . GLN A 1 103 ? -0.050  -30.833 19.129  1.00 18.07 ? 82  GLN A OE1   1 
ATOM   574  N  NE2   . GLN A 1 103 ? 1.276   -32.523 19.714  1.00 18.88 ? 82  GLN A NE2   1 
ATOM   575  N  N     . PRO A 1 104 ? -1.298  -34.720 21.161  1.00 20.11 ? 83  PRO A N     1 
ATOM   576  C  CA    . PRO A 1 104 ? -0.717  -35.877 21.821  1.00 22.02 ? 83  PRO A CA    1 
ATOM   577  C  C     . PRO A 1 104 ? 0.355   -35.482 22.857  1.00 26.23 ? 83  PRO A C     1 
ATOM   578  O  O     . PRO A 1 104 ? 1.165   -34.589 22.581  1.00 24.31 ? 83  PRO A O     1 
ATOM   579  C  CB    . PRO A 1 104 ? -0.062  -36.652 20.683  1.00 23.93 ? 83  PRO A CB    1 
ATOM   580  C  CG    . PRO A 1 104 ? -0.751  -36.196 19.418  1.00 22.62 ? 83  PRO A CG    1 
ATOM   581  C  CD    . PRO A 1 104 ? -1.301  -34.817 19.700  1.00 19.65 ? 83  PRO A CD    1 
ATOM   582  N  N     . THR A 1 105 ? 0.335   -36.143 24.020  1.00 25.12 ? 84  THR A N     1 
ATOM   583  C  CA    . THR A 1 105 ? 1.179   -35.799 25.190  1.00 27.41 ? 84  THR A CA    1 
ATOM   584  C  C     . THR A 1 105 ? 2.059   -36.987 25.569  1.00 26.57 ? 84  THR A C     1 
ATOM   585  O  O     . THR A 1 105 ? 3.081   -36.713 26.193  1.00 26.37 ? 84  THR A O     1 
ATOM   586  C  CB    . THR A 1 105 ? 0.361   -35.380 26.411  1.00 27.35 ? 84  THR A CB    1 
ATOM   587  O  OG1   . THR A 1 105 ? -0.598  -36.403 26.667  1.00 29.25 ? 84  THR A OG1   1 
ATOM   588  C  CG2   . THR A 1 105 ? -0.348  -34.061 26.242  1.00 29.13 ? 84  THR A CG2   1 
ATOM   589  N  N     . GLU A 1 106 ? 1.719   -38.219 25.157  1.00 24.26 ? 85  GLU A N     1 
ATOM   590  C  CA    . GLU A 1 106 ? 2.314   -39.449 25.742  1.00 26.87 ? 85  GLU A CA    1 
ATOM   591  C  C     . GLU A 1 106 ? 3.516   -39.893 24.912  1.00 27.33 ? 85  GLU A C     1 
ATOM   592  O  O     . GLU A 1 106 ? 3.698   -39.401 23.795  1.00 27.41 ? 85  GLU A O     1 
ATOM   593  C  CB    . GLU A 1 106 ? 1.262   -40.551 25.892  1.00 30.62 ? 85  GLU A CB    1 
ATOM   594  C  CG    . GLU A 1 106 ? 0.195   -40.205 26.921  1.00 32.00 ? 85  GLU A CG    1 
ATOM   595  C  CD    . GLU A 1 106 ? 0.674   -39.518 28.208  1.00 38.78 ? 85  GLU A CD    1 
ATOM   596  O  OE1   . GLU A 1 106 ? 1.584   -40.077 28.919  1.00 33.21 ? 85  GLU A OE1   1 
ATOM   597  O  OE2   . GLU A 1 106 ? 0.130   -38.416 28.522  1.00 40.78 ? 85  GLU A OE2   1 
ATOM   598  N  N     . GLY A 1 107 ? 4.358   -40.724 25.507  1.00 24.92 ? 86  GLY A N     1 
ATOM   599  C  CA    . GLY A 1 107 ? 5.585   -41.245 24.894  1.00 24.26 ? 86  GLY A CA    1 
ATOM   600  C  C     . GLY A 1 107 ? 6.749   -40.429 25.387  1.00 24.52 ? 86  GLY A C     1 
ATOM   601  O  O     . GLY A 1 107 ? 6.509   -39.314 25.893  1.00 25.58 ? 86  GLY A O     1 
ATOM   602  N  N     . ASP A 1 108 ? 7.966   -40.953 25.226  1.00 23.94 ? 87  ASP A N     1 
ATOM   603  C  CA    . ASP A 1 108 ? 9.222   -40.275 25.637  1.00 26.05 ? 87  ASP A CA    1 
ATOM   604  C  C     . ASP A 1 108 ? 9.563   -39.122 24.680  1.00 24.76 ? 87  ASP A C     1 
ATOM   605  O  O     . ASP A 1 108 ? 9.517   -39.332 23.464  1.00 22.63 ? 87  ASP A O     1 
ATOM   606  C  CB    . ASP A 1 108 ? 10.397  -41.239 25.608  1.00 28.56 ? 87  ASP A CB    1 
ATOM   607  C  CG    . ASP A 1 108 ? 10.357  -42.285 26.702  1.00 32.90 ? 87  ASP A CG    1 
ATOM   608  O  OD1   . ASP A 1 108 ? 9.669   -42.062 27.710  1.00 31.99 ? 87  ASP A OD1   1 
ATOM   609  O  OD2   . ASP A 1 108 ? 11.063  -43.283 26.528  1.00 36.07 ? 87  ASP A OD2   1 
ATOM   610  N  N     . ASP A 1 109 ? 9.905   -37.981 25.265  1.00 23.33 ? 88  ASP A N     1 
ATOM   611  C  CA    . ASP A 1 109 ? 10.516  -36.815 24.583  1.00 26.03 ? 88  ASP A CA    1 
ATOM   612  C  C     . ASP A 1 109 ? 11.995  -37.167 24.362  1.00 28.97 ? 88  ASP A C     1 
ATOM   613  O  O     . ASP A 1 109 ? 12.557  -38.026 25.129  1.00 31.02 ? 88  ASP A O     1 
ATOM   614  C  CB    . ASP A 1 109 ? 10.308  -35.552 25.419  1.00 25.83 ? 88  ASP A CB    1 
ATOM   615  C  CG    . ASP A 1 109 ? 8.850   -35.164 25.614  1.00 27.35 ? 88  ASP A CG    1 
ATOM   616  O  OD1   . ASP A 1 109 ? 8.022   -35.528 24.763  1.00 24.84 ? 88  ASP A OD1   1 
ATOM   617  O  OD2   . ASP A 1 109 ? 8.562   -34.515 26.620  1.00 27.03 ? 88  ASP A OD2   1 
ATOM   618  N  N     . VAL A 1 110 ? 12.619  -36.606 23.331  1.00 27.39 ? 89  VAL A N     1 
ATOM   619  C  CA    . VAL A 1 110 ? 14.078  -36.788 23.100  1.00 28.45 ? 89  VAL A CA    1 
ATOM   620  C  C     . VAL A 1 110 ? 14.780  -35.453 23.366  1.00 30.04 ? 89  VAL A C     1 
ATOM   621  O  O     . VAL A 1 110 ? 14.342  -34.403 22.824  1.00 28.55 ? 89  VAL A O     1 
ATOM   622  C  CB    . VAL A 1 110 ? 14.379  -37.356 21.704  1.00 27.14 ? 89  VAL A CB    1 
ATOM   623  C  CG1   . VAL A 1 110 ? 15.866  -37.445 21.451  1.00 25.52 ? 89  VAL A CG1   1 
ATOM   624  C  CG2   . VAL A 1 110 ? 13.741  -38.706 21.496  1.00 28.92 ? 89  VAL A CG2   1 
ATOM   625  N  N     . VAL A 1 111 ? 15.827  -35.476 24.195  1.00 28.53 ? 90  VAL A N     1 
ATOM   626  C  CA    . VAL A 1 111 ? 16.653  -34.264 24.439  1.00 27.52 ? 90  VAL A CA    1 
ATOM   627  C  C     . VAL A 1 111 ? 18.052  -34.514 23.879  1.00 27.64 ? 90  VAL A C     1 
ATOM   628  O  O     . VAL A 1 111 ? 18.623  -35.620 24.094  1.00 27.80 ? 90  VAL A O     1 
ATOM   629  C  CB    . VAL A 1 111 ? 16.633  -33.873 25.920  1.00 32.64 ? 90  VAL A CB    1 
ATOM   630  C  CG1   . VAL A 1 111 ? 17.403  -32.591 26.167  1.00 35.23 ? 90  VAL A CG1   1 
ATOM   631  C  CG2   . VAL A 1 111 ? 15.199  -33.757 26.400  1.00 34.79 ? 90  VAL A CG2   1 
ATOM   632  N  N     . LEU A 1 112 ? 18.554  -33.544 23.117  1.00 26.75 ? 91  LEU A N     1 
ATOM   633  C  CA    . LEU A 1 112 ? 19.912  -33.597 22.520  1.00 29.25 ? 91  LEU A CA    1 
ATOM   634  C  C     . LEU A 1 112 ? 20.677  -32.318 22.882  1.00 27.92 ? 91  LEU A C     1 
ATOM   635  O  O     . LEU A 1 112 ? 20.166  -31.200 22.702  1.00 26.98 ? 91  LEU A O     1 
ATOM   636  C  CB    . LEU A 1 112 ? 19.829  -33.798 21.013  1.00 31.66 ? 91  LEU A CB    1 
ATOM   637  C  CG    . LEU A 1 112 ? 21.182  -33.798 20.311  1.00 33.02 ? 91  LEU A CG    1 
ATOM   638  C  CD1   . LEU A 1 112 ? 21.971  -35.018 20.729  1.00 34.98 ? 91  LEU A CD1   1 
ATOM   639  C  CD2   . LEU A 1 112 ? 21.034  -33.767 18.804  1.00 34.08 ? 91  LEU A CD2   1 
ATOM   640  N  N     . PHE A 1 113 ? 21.858  -32.481 23.481  1.00 29.01 ? 92  PHE A N     1 
ATOM   641  C  CA    . PHE A 1 113 ? 22.745  -31.348 23.865  1.00 28.50 ? 92  PHE A CA    1 
ATOM   642  C  C     . PHE A 1 113 ? 24.025  -31.444 23.045  1.00 26.99 ? 92  PHE A C     1 
ATOM   643  O  O     . PHE A 1 113 ? 24.745  -32.437 23.236  1.00 28.02 ? 92  PHE A O     1 
ATOM   644  C  CB    . PHE A 1 113 ? 23.125  -31.402 25.344  1.00 32.18 ? 92  PHE A CB    1 
ATOM   645  C  CG    . PHE A 1 113 ? 21.961  -31.320 26.299  1.00 34.75 ? 92  PHE A CG    1 
ATOM   646  C  CD1   . PHE A 1 113 ? 21.252  -30.135 26.445  1.00 36.10 ? 92  PHE A CD1   1 
ATOM   647  C  CD2   . PHE A 1 113 ? 21.602  -32.417 27.069  1.00 37.37 ? 92  PHE A CD2   1 
ATOM   648  C  CE1   . PHE A 1 113 ? 20.187  -30.057 27.336  1.00 37.89 ? 92  PHE A CE1   1 
ATOM   649  C  CE2   . PHE A 1 113 ? 20.530  -32.343 27.951  1.00 41.58 ? 92  PHE A CE2   1 
ATOM   650  C  CZ    . PHE A 1 113 ? 19.834  -31.158 28.094  1.00 39.29 ? 92  PHE A CZ    1 
ATOM   651  N  N     . GLY A 1 114 ? 24.299  -30.449 22.200  1.00 27.99 ? 93  GLY A N     1 
ATOM   652  C  CA    . GLY A 1 114 ? 25.594  -30.300 21.507  1.00 29.13 ? 93  GLY A CA    1 
ATOM   653  C  C     . GLY A 1 114 ? 25.971  -31.576 20.784  1.00 32.94 ? 93  GLY A C     1 
ATOM   654  O  O     . GLY A 1 114 ? 25.083  -32.133 20.087  1.00 30.99 ? 93  GLY A O     1 
ATOM   655  N  N     . ASP A 1 115 ? 27.206  -32.074 20.997  1.00 31.62 ? 94  ASP A N     1 
ATOM   656  C  CA    . ASP A 1 115 ? 27.745  -33.292 20.322  1.00 31.49 ? 94  ASP A CA    1 
ATOM   657  C  C     . ASP A 1 115 ? 27.362  -34.594 21.053  1.00 31.41 ? 94  ASP A C     1 
ATOM   658  O  O     . ASP A 1 115 ? 27.905  -35.648 20.683  1.00 33.75 ? 94  ASP A O     1 
ATOM   659  C  CB    . ASP A 1 115 ? 29.274  -33.192 20.167  1.00 34.57 ? 94  ASP A CB    1 
ATOM   660  C  CG    . ASP A 1 115 ? 30.092  -33.282 21.464  1.00 38.17 ? 94  ASP A CG    1 
ATOM   661  O  OD1   . ASP A 1 115 ? 31.316  -33.497 21.348  1.00 41.04 ? 94  ASP A OD1   1 
ATOM   662  O  OD2   . ASP A 1 115 ? 29.500  -33.171 22.593  1.00 32.06 ? 94  ASP A OD2   1 
ATOM   663  N  N     . GLY A 1 116 ? 26.466  -34.548 22.046  1.00 33.27 ? 95  GLY A N     1 
ATOM   664  C  CA    . GLY A 1 116 ? 26.107  -35.718 22.881  1.00 29.09 ? 95  GLY A CA    1 
ATOM   665  C  C     . GLY A 1 116 ? 25.262  -36.738 22.131  1.00 30.95 ? 95  GLY A C     1 
ATOM   666  O  O     . GLY A 1 116 ? 25.028  -36.598 20.911  1.00 33.78 ? 95  GLY A O     1 
ATOM   667  N  N     . GLU A 1 117 ? 24.840  -37.779 22.827  1.00 31.84 ? 96  GLU A N     1 
ATOM   668  C  CA    . GLU A 1 117 ? 23.871  -38.772 22.306  1.00 33.27 ? 96  GLU A CA    1 
ATOM   669  C  C     . GLU A 1 117 ? 22.481  -38.311 22.710  1.00 30.67 ? 96  GLU A C     1 
ATOM   670  O  O     . GLU A 1 117 ? 22.319  -37.699 23.761  1.00 31.28 ? 96  GLU A O     1 
ATOM   671  C  CB    . GLU A 1 117 ? 24.221  -40.167 22.828  1.00 40.33 ? 96  GLU A CB    1 
ATOM   672  C  CG    . GLU A 1 117 ? 25.495  -40.690 22.192  1.00 45.22 ? 96  GLU A CG    1 
ATOM   673  C  CD    . GLU A 1 117 ? 25.781  -42.157 22.477  1.00 56.12 ? 96  GLU A CD    1 
ATOM   674  O  OE1   . GLU A 1 117 ? 26.067  -42.902 21.508  1.00 62.40 ? 96  GLU A OE1   1 
ATOM   675  O  OE2   . GLU A 1 117 ? 25.711  -42.555 23.663  1.00 55.75 ? 96  GLU A OE2   1 
ATOM   676  N  N     . PRO A 1 118 ? 21.440  -38.572 21.887  1.00 28.35 ? 97  PRO A N     1 
ATOM   677  C  CA    . PRO A 1 118 ? 20.074  -38.196 22.266  1.00 29.75 ? 97  PRO A CA    1 
ATOM   678  C  C     . PRO A 1 118 ? 19.597  -38.952 23.525  1.00 29.91 ? 97  PRO A C     1 
ATOM   679  O  O     . PRO A 1 118 ? 19.983  -40.107 23.659  1.00 35.34 ? 97  PRO A O     1 
ATOM   680  C  CB    . PRO A 1 118 ? 19.300  -38.540 20.976  1.00 28.35 ? 97  PRO A CB    1 
ATOM   681  C  CG    . PRO A 1 118 ? 20.099  -39.635 20.319  1.00 29.40 ? 97  PRO A CG    1 
ATOM   682  C  CD    . PRO A 1 118 ? 21.535  -39.242 20.583  1.00 28.31 ? 97  PRO A CD    1 
ATOM   683  N  N     . GLN A 1 119 ? 18.894  -38.279 24.444  1.00 34.63 ? 98  GLN A N     1 
ATOM   684  C  CA    . GLN A 1 119 ? 18.382  -38.851 25.730  1.00 42.38 ? 98  GLN A CA    1 
ATOM   685  C  C     . GLN A 1 119 ? 16.854  -38.992 25.650  1.00 38.50 ? 98  GLN A C     1 
ATOM   686  O  O     . GLN A 1 119 ? 16.202  -37.963 25.442  1.00 32.01 ? 98  GLN A O     1 
ATOM   687  C  CB    . GLN A 1 119 ? 18.692  -37.937 26.929  1.00 51.79 ? 98  GLN A CB    1 
ATOM   688  C  CG    . GLN A 1 119 ? 20.170  -37.650 27.141  1.00 60.17 ? 98  GLN A CG    1 
ATOM   689  C  CD    . GLN A 1 119 ? 20.912  -38.960 27.219  1.00 71.49 ? 98  GLN A CD    1 
ATOM   690  O  OE1   . GLN A 1 119 ? 20.740  -39.730 28.163  1.00 80.89 ? 98  GLN A OE1   1 
ATOM   691  N  NE2   . GLN A 1 119 ? 21.692  -39.261 26.192  1.00 75.60 ? 98  GLN A NE2   1 
ATOM   692  N  N     . ARG A 1 120 ? 16.299  -40.199 25.828  1.00 37.59 ? 99  ARG A N     1 
ATOM   693  C  CA    . ARG A 1 120 ? 14.826  -40.393 25.923  1.00 37.54 ? 99  ARG A CA    1 
ATOM   694  C  C     . ARG A 1 120 ? 14.377  -40.141 27.367  1.00 38.41 ? 99  ARG A C     1 
ATOM   695  O  O     . ARG A 1 120 ? 15.014  -40.651 28.262  1.00 39.51 ? 99  ARG A O     1 
ATOM   696  C  CB    . ARG A 1 120 ? 14.426  -41.820 25.548  1.00 39.47 ? 99  ARG A CB    1 
ATOM   697  C  CG    . ARG A 1 120 ? 14.810  -42.254 24.147  1.00 42.87 ? 99  ARG A CG    1 
ATOM   698  C  CD    . ARG A 1 120 ? 14.399  -43.694 23.903  1.00 42.99 ? 99  ARG A CD    1 
ATOM   699  N  NE    . ARG A 1 120 ? 12.998  -43.934 24.210  1.00 39.96 ? 99  ARG A NE    1 
ATOM   700  C  CZ    . ARG A 1 120 ? 12.192  -44.731 23.511  1.00 37.78 ? 99  ARG A CZ    1 
ATOM   701  N  NH1   . ARG A 1 120 ? 12.640  -45.385 22.455  1.00 36.31 ? 99  ARG A NH1   1 
ATOM   702  N  NH2   . ARG A 1 120 ? 10.925  -44.873 23.869  1.00 39.34 ? 99  ARG A NH2   1 
ATOM   703  N  N     . ALA A 1 121 ? 13.320  -39.385 27.597  1.00 36.13 ? 100 ALA A N     1 
ATOM   704  C  CA    . ALA A 1 121 ? 12.786  -39.138 28.955  1.00 40.28 ? 100 ALA A CA    1 
ATOM   705  C  C     . ALA A 1 121 ? 11.273  -38.993 28.880  1.00 38.87 ? 100 ALA A C     1 
ATOM   706  O  O     . ALA A 1 121 ? 10.756  -38.414 27.921  1.00 34.10 ? 100 ALA A O     1 
ATOM   707  C  CB    . ALA A 1 121 ? 13.439  -37.907 29.533  1.00 42.92 ? 100 ALA A CB    1 
ATOM   708  N  N     . PRO A 1 122 ? 10.524  -39.493 29.890  1.00 38.23 ? 101 PRO A N     1 
ATOM   709  C  CA    . PRO A 1 122 ? 9.071   -39.351 29.926  1.00 39.71 ? 101 PRO A CA    1 
ATOM   710  C  C     . PRO A 1 122 ? 8.638   -37.892 29.819  1.00 39.71 ? 101 PRO A C     1 
ATOM   711  O  O     . PRO A 1 122 ? 7.536   -37.646 29.416  1.00 44.57 ? 101 PRO A O     1 
ATOM   712  C  CB    . PRO A 1 122 ? 8.676   -39.938 31.289  1.00 38.76 ? 101 PRO A CB    1 
ATOM   713  C  CG    . PRO A 1 122 ? 9.756   -40.959 31.556  1.00 40.37 ? 101 PRO A CG    1 
ATOM   714  C  CD    . PRO A 1 122 ? 11.015  -40.323 30.998  1.00 42.43 ? 101 PRO A CD    1 
ATOM   715  N  N     . ASP A 1 123 ? 9.512   -36.973 30.217  1.00 38.75 ? 102 ASP A N     1 
ATOM   716  C  CA    . ASP A 1 123 ? 9.331   -35.523 29.994  1.00 40.78 ? 102 ASP A CA    1 
ATOM   717  C  C     . ASP A 1 123 ? 10.700  -34.891 29.765  1.00 41.25 ? 102 ASP A C     1 
ATOM   718  O  O     . ASP A 1 123 ? 11.712  -35.381 30.297  1.00 38.93 ? 102 ASP A O     1 
ATOM   719  C  CB    . ASP A 1 123 ? 8.648   -34.802 31.157  1.00 47.87 ? 102 ASP A CB    1 
ATOM   720  C  CG    . ASP A 1 123 ? 8.317   -33.364 30.787  1.00 59.85 ? 102 ASP A CG    1 
ATOM   721  O  OD1   . ASP A 1 123 ? 7.706   -33.161 29.711  1.00 68.78 ? 102 ASP A OD1   1 
ATOM   722  O  OD2   . ASP A 1 123 ? 8.706   -32.447 31.539  1.00 64.31 ? 102 ASP A OD2   1 
ATOM   723  N  N     . VAL A 1 124 ? 10.708  -33.828 28.977  1.00 43.92 ? 103 VAL A N     1 
ATOM   724  C  CA    . VAL A 1 124 ? 11.871  -32.917 28.800  1.00 43.33 ? 103 VAL A CA    1 
ATOM   725  C  C     . VAL A 1 124 ? 12.556  -32.651 30.156  1.00 42.84 ? 103 VAL A C     1 
ATOM   726  O  O     . VAL A 1 124 ? 13.798  -32.787 30.222  1.00 43.12 ? 103 VAL A O     1 
ATOM   727  C  CB    . VAL A 1 124 ? 11.377  -31.632 28.109  1.00 41.89 ? 103 VAL A CB    1 
ATOM   728  C  CG1   . VAL A 1 124 ? 12.200  -30.413 28.486  1.00 47.53 ? 103 VAL A CG1   1 
ATOM   729  C  CG2   . VAL A 1 124 ? 11.344  -31.836 26.609  1.00 43.83 ? 103 VAL A CG2   1 
ATOM   730  N  N     . ALA A 1 125 ? 11.809  -32.263 31.195  1.00 38.01 ? 104 ALA A N     1 
ATOM   731  C  CA    . ALA A 1 125 ? 12.364  -31.891 32.525  1.00 39.14 ? 104 ALA A CA    1 
ATOM   732  C  C     . ALA A 1 125 ? 13.429  -32.900 32.986  1.00 43.81 ? 104 ALA A C     1 
ATOM   733  O  O     . ALA A 1 125 ? 14.503  -32.465 33.427  1.00 46.87 ? 104 ALA A O     1 
ATOM   734  C  CB    . ALA A 1 125 ? 11.272  -31.796 33.558  1.00 36.77 ? 104 ALA A CB    1 
ATOM   735  N  N     . LEU A 1 126 ? 13.150  -34.197 32.865  1.00 43.69 ? 105 LEU A N     1 
ATOM   736  C  CA    . LEU A 1 126 ? 13.935  -35.290 33.499  1.00 46.46 ? 105 LEU A CA    1 
ATOM   737  C  C     . LEU A 1 126 ? 15.308  -35.450 32.822  1.00 46.93 ? 105 LEU A C     1 
ATOM   738  O  O     . LEU A 1 126 ? 16.047  -36.318 33.266  1.00 50.64 ? 105 LEU A O     1 
ATOM   739  C  CB    . LEU A 1 126 ? 13.110  -36.585 33.468  1.00 47.25 ? 105 LEU A CB    1 
ATOM   740  C  CG    . LEU A 1 126 ? 11.888  -36.611 34.397  1.00 48.81 ? 105 LEU A CG    1 
ATOM   741  C  CD1   . LEU A 1 126 ? 10.856  -37.653 33.971  1.00 49.39 ? 105 LEU A CD1   1 
ATOM   742  C  CD2   . LEU A 1 126 ? 12.297  -36.856 35.845  1.00 50.96 ? 105 LEU A CD2   1 
ATOM   743  N  N     . ALA A 1 127 ? 15.665  -34.622 31.836  1.00 42.41 ? 106 ALA A N     1 
ATOM   744  C  CA    . ALA A 1 127 ? 16.998  -34.629 31.177  1.00 44.79 ? 106 ALA A CA    1 
ATOM   745  C  C     . ALA A 1 127 ? 17.925  -33.589 31.814  1.00 46.02 ? 106 ALA A C     1 
ATOM   746  O  O     . ALA A 1 127 ? 19.048  -33.374 31.296  1.00 44.61 ? 106 ALA A O     1 
ATOM   747  C  CB    . ALA A 1 127 ? 16.844  -34.355 29.704  1.00 49.12 ? 106 ALA A CB    1 
ATOM   748  N  N     . PHE A 1 128 ? 17.452  -32.935 32.868  1.00 41.90 ? 107 PHE A N     1 
ATOM   749  C  CA    . PHE A 1 128 ? 18.187  -31.907 33.637  1.00 42.06 ? 107 PHE A CA    1 
ATOM   750  C  C     . PHE A 1 128 ? 18.324  -32.397 35.076  1.00 37.22 ? 107 PHE A C     1 
ATOM   751  O  O     . PHE A 1 128 ? 17.442  -33.150 35.526  1.00 38.10 ? 107 PHE A O     1 
ATOM   752  C  CB    . PHE A 1 128 ? 17.447  -30.572 33.512  1.00 42.50 ? 107 PHE A CB    1 
ATOM   753  C  CG    . PHE A 1 128 ? 17.333  -30.120 32.078  1.00 42.66 ? 107 PHE A CG    1 
ATOM   754  C  CD1   . PHE A 1 128 ? 16.322  -30.610 31.257  1.00 42.64 ? 107 PHE A CD1   1 
ATOM   755  C  CD2   . PHE A 1 128 ? 18.266  -29.252 31.531  1.00 43.74 ? 107 PHE A CD2   1 
ATOM   756  C  CE1   . PHE A 1 128 ? 16.234  -30.227 29.923  1.00 44.61 ? 107 PHE A CE1   1 
ATOM   757  C  CE2   . PHE A 1 128 ? 18.172  -28.858 30.201  1.00 44.78 ? 107 PHE A CE2   1 
ATOM   758  C  CZ    . PHE A 1 128 ? 17.146  -29.336 29.399  1.00 42.99 ? 107 PHE A CZ    1 
ATOM   759  N  N     . SER A 1 129 ? 19.376  -31.965 35.770  1.00 37.16 ? 108 SER A N     1 
ATOM   760  C  CA    . SER A 1 129 ? 19.627  -32.319 37.189  1.00 39.73 ? 108 SER A CA    1 
ATOM   761  C  C     . SER A 1 129 ? 18.568  -31.644 38.051  1.00 40.89 ? 108 SER A C     1 
ATOM   762  O  O     . SER A 1 129 ? 17.906  -30.716 37.547  1.00 36.97 ? 108 SER A O     1 
ATOM   763  C  CB    . SER A 1 129 ? 20.991  -31.923 37.626  1.00 39.76 ? 108 SER A CB    1 
ATOM   764  O  OG    . SER A 1 129 ? 21.105  -30.513 37.647  1.00 38.91 ? 108 SER A OG    1 
ATOM   765  N  N     . ASP A 1 130 ? 18.438  -32.082 39.296  1.00 35.33 ? 109 ASP A N     1 
ATOM   766  C  CA    . ASP A 1 130 ? 17.522  -31.477 40.299  1.00 41.68 ? 109 ASP A CA    1 
ATOM   767  C  C     . ASP A 1 130 ? 17.851  -29.997 40.479  1.00 37.21 ? 109 ASP A C     1 
ATOM   768  O  O     . ASP A 1 130 ? 16.900  -29.201 40.536  1.00 34.02 ? 109 ASP A O     1 
ATOM   769  C  CB    . ASP A 1 130 ? 17.620  -32.164 41.661  1.00 49.76 ? 109 ASP A CB    1 
ATOM   770  C  CG    . ASP A 1 130 ? 16.796  -33.434 41.740  1.00 56.87 ? 109 ASP A CG    1 
ATOM   771  O  OD1   . ASP A 1 130 ? 15.916  -33.609 40.882  1.00 56.35 ? 109 ASP A OD1   1 
ATOM   772  O  OD2   . ASP A 1 130 ? 17.052  -34.245 42.660  1.00 70.68 ? 109 ASP A OD2   1 
ATOM   773  N  N     . GLU A 1 131 ? 19.136  -29.663 40.588  1.00 34.13 ? 110 GLU A N     1 
ATOM   774  C  CA    . GLU A 1 131 ? 19.628  -28.274 40.791  1.00 39.21 ? 110 GLU A CA    1 
ATOM   775  C  C     . GLU A 1 131 ? 19.245  -27.413 39.580  1.00 34.19 ? 110 GLU A C     1 
ATOM   776  O  O     . GLU A 1 131 ? 18.788  -26.289 39.762  1.00 31.76 ? 110 GLU A O     1 
ATOM   777  C  CB    . GLU A 1 131 ? 21.142  -28.272 40.975  1.00 47.04 ? 110 GLU A CB    1 
ATOM   778  C  CG    . GLU A 1 131 ? 21.604  -29.146 42.130  1.00 58.24 ? 110 GLU A CG    1 
ATOM   779  C  CD    . GLU A 1 131 ? 23.064  -28.948 42.493  1.00 66.27 ? 110 GLU A CD    1 
ATOM   780  O  OE1   . GLU A 1 131 ? 23.881  -28.768 41.556  1.00 67.48 ? 110 GLU A OE1   1 
ATOM   781  O  OE2   . GLU A 1 131 ? 23.378  -28.960 43.710  1.00 78.13 ? 110 GLU A OE2   1 
ATOM   782  N  N     . GLU A 1 132 ? 19.429  -27.939 38.377  1.00 29.95 ? 111 GLU A N     1 
ATOM   783  C  CA    . GLU A 1 132 ? 19.023  -27.270 37.111  1.00 31.93 ? 111 GLU A CA    1 
ATOM   784  C  C     . GLU A 1 132 ? 17.508  -27.011 37.099  1.00 27.25 ? 111 GLU A C     1 
ATOM   785  O  O     . GLU A 1 132 ? 17.095  -25.918 36.729  1.00 27.10 ? 111 GLU A O     1 
ATOM   786  C  CB    . GLU A 1 132 ? 19.496  -28.127 35.936  1.00 30.26 ? 111 GLU A CB    1 
ATOM   787  C  CG    . GLU A 1 132 ? 20.967  -27.939 35.661  1.00 32.31 ? 111 GLU A CG    1 
ATOM   788  C  CD    . GLU A 1 132 ? 21.549  -28.872 34.614  1.00 34.24 ? 111 GLU A CD    1 
ATOM   789  O  OE1   . GLU A 1 132 ? 22.677  -28.610 34.169  1.00 37.42 ? 111 GLU A OE1   1 
ATOM   790  O  OE2   . GLU A 1 132 ? 20.856  -29.839 34.215  1.00 34.28 ? 111 GLU A OE2   1 
ATOM   791  N  N     . LEU A 1 133 ? 16.689  -28.007 37.392  1.00 30.01 ? 112 LEU A N     1 
ATOM   792  C  CA    . LEU A 1 133 ? 15.204  -27.873 37.378  1.00 32.69 ? 112 LEU A CA    1 
ATOM   793  C  C     . LEU A 1 133 ? 14.779  -26.814 38.412  1.00 33.30 ? 112 LEU A C     1 
ATOM   794  O  O     . LEU A 1 133 ? 13.905  -25.979 38.089  1.00 27.09 ? 112 LEU A O     1 
ATOM   795  C  CB    . LEU A 1 133 ? 14.593  -29.254 37.638  1.00 36.91 ? 112 LEU A CB    1 
ATOM   796  C  CG    . LEU A 1 133 ? 13.071  -29.340 37.683  1.00 46.61 ? 112 LEU A CG    1 
ATOM   797  C  CD1   . LEU A 1 133 ? 12.468  -28.993 36.315  1.00 47.39 ? 112 LEU A CD1   1 
ATOM   798  C  CD2   . LEU A 1 133 ? 12.620  -30.729 38.150  1.00 47.54 ? 112 LEU A CD2   1 
ATOM   799  N  N     . THR A 1 134 ? 15.383  -26.810 39.609  1.00 31.46 ? 113 THR A N     1 
ATOM   800  C  CA    . THR A 1 134 ? 15.102  -25.786 40.662  1.00 30.89 ? 113 THR A CA    1 
ATOM   801  C  C     . THR A 1 134 ? 15.456  -24.388 40.143  1.00 24.75 ? 113 THR A C     1 
ATOM   802  O  O     . THR A 1 134 ? 14.649  -23.490 40.319  1.00 25.99 ? 113 THR A O     1 
ATOM   803  C  CB    . THR A 1 134 ? 15.848  -26.075 41.970  1.00 32.85 ? 113 THR A CB    1 
ATOM   804  O  OG1   . THR A 1 134 ? 15.396  -27.351 42.415  1.00 33.37 ? 113 THR A OG1   1 
ATOM   805  C  CG2   . THR A 1 134 ? 15.603  -25.027 43.034  1.00 34.51 ? 113 THR A CG2   1 
ATOM   806  N  N     . ALA A 1 135 ? 16.597  -24.219 39.503  1.00 25.86 ? 114 ALA A N     1 
ATOM   807  C  CA    . ALA A 1 135 ? 17.041  -22.909 38.964  1.00 25.58 ? 114 ALA A CA    1 
ATOM   808  C  C     . ALA A 1 135 ? 16.061  -22.448 37.859  1.00 25.56 ? 114 ALA A C     1 
ATOM   809  O  O     . ALA A 1 135 ? 15.667  -21.301 37.855  1.00 23.58 ? 114 ALA A O     1 
ATOM   810  C  CB    . ALA A 1 135 ? 18.473  -22.994 38.487  1.00 26.70 ? 114 ALA A CB    1 
ATOM   811  N  N     . TYR A 1 136 ? 15.613  -23.356 36.993  1.00 23.71 ? 115 TYR A N     1 
ATOM   812  C  CA    . TYR A 1 136 ? 14.618  -23.068 35.929  1.00 24.72 ? 115 TYR A CA    1 
ATOM   813  C  C     . TYR A 1 136 ? 13.291  -22.598 36.529  1.00 23.16 ? 115 TYR A C     1 
ATOM   814  O  O     . TYR A 1 136 ? 12.713  -21.586 36.027  1.00 23.92 ? 115 TYR A O     1 
ATOM   815  C  CB    . TYR A 1 136 ? 14.412  -24.271 35.007  1.00 24.18 ? 115 TYR A CB    1 
ATOM   816  C  CG    . TYR A 1 136 ? 13.416  -24.024 33.903  1.00 25.10 ? 115 TYR A CG    1 
ATOM   817  C  CD1   . TYR A 1 136 ? 12.101  -24.430 34.030  1.00 29.88 ? 115 TYR A CD1   1 
ATOM   818  C  CD2   . TYR A 1 136 ? 13.783  -23.371 32.734  1.00 28.63 ? 115 TYR A CD2   1 
ATOM   819  C  CE1   . TYR A 1 136 ? 11.171  -24.189 33.025  1.00 31.74 ? 115 TYR A CE1   1 
ATOM   820  C  CE2   . TYR A 1 136 ? 12.870  -23.123 31.716  1.00 28.45 ? 115 TYR A CE2   1 
ATOM   821  C  CZ    . TYR A 1 136 ? 11.560  -23.541 31.862  1.00 29.52 ? 115 TYR A CZ    1 
ATOM   822  O  OH    . TYR A 1 136 ? 10.643  -23.270 30.883  1.00 29.21 ? 115 TYR A OH    1 
ATOM   823  N  N     . LEU A 1 137 ? 12.767  -23.335 37.495  1.00 24.35 ? 116 LEU A N     1 
ATOM   824  C  CA    . LEU A 1 137 ? 11.467  -23.004 38.120  1.00 25.55 ? 116 LEU A CA    1 
ATOM   825  C  C     . LEU A 1 137 ? 11.609  -21.698 38.904  1.00 24.78 ? 116 LEU A C     1 
ATOM   826  O  O     . LEU A 1 137 ? 10.608  -20.934 38.903  1.00 21.72 ? 116 LEU A O     1 
ATOM   827  C  CB    . LEU A 1 137 ? 10.983  -24.164 38.994  1.00 26.86 ? 116 LEU A CB    1 
ATOM   828  C  CG    . LEU A 1 137 ? 10.549  -25.433 38.249  1.00 31.60 ? 116 LEU A CG    1 
ATOM   829  C  CD1   . LEU A 1 137 ? 10.303  -26.569 39.230  1.00 31.59 ? 116 LEU A CD1   1 
ATOM   830  C  CD2   . LEU A 1 137 ? 9.306   -25.199 37.392  1.00 33.43 ? 116 LEU A CD2   1 
ATOM   831  N  N     . GLU A 1 138 ? 12.782  -21.406 39.496  1.00 23.72 ? 117 GLU A N     1 
ATOM   832  C  CA    . GLU A 1 138 ? 12.956  -20.124 40.243  1.00 24.27 ? 117 GLU A CA    1 
ATOM   833  C  C     . GLU A 1 138 ? 13.066  -18.988 39.220  1.00 21.90 ? 117 GLU A C     1 
ATOM   834  O  O     . GLU A 1 138 ? 12.501  -17.888 39.468  1.00 24.43 ? 117 GLU A O     1 
ATOM   835  C  CB    . GLU A 1 138 ? 14.101  -20.247 41.264  1.00 27.99 ? 117 GLU A CB    1 
ATOM   836  C  CG    . GLU A 1 138 ? 13.625  -20.987 42.532  1.00 33.96 ? 117 GLU A CG    1 
ATOM   837  C  CD    . GLU A 1 138 ? 14.576  -21.174 43.724  1.00 43.67 ? 117 GLU A CD    1 
ATOM   838  O  OE1   . GLU A 1 138 ? 14.165  -21.829 44.727  1.00 48.53 ? 117 GLU A OE1   1 
ATOM   839  O  OE2   . GLU A 1 138 ? 15.714  -20.703 43.670  1.00 43.79 ? 117 GLU A OE2   1 
ATOM   840  N  N     . LEU A 1 139 ? 13.752  -19.206 38.090  1.00 20.58 ? 118 LEU A N     1 
ATOM   841  C  CA    . LEU A 1 139 ? 13.849  -18.193 37.001  1.00 22.37 ? 118 LEU A CA    1 
ATOM   842  C  C     . LEU A 1 139 ? 12.448  -17.884 36.455  1.00 22.29 ? 118 LEU A C     1 
ATOM   843  O  O     . LEU A 1 139 ? 12.108  -16.689 36.338  1.00 23.15 ? 118 LEU A O     1 
ATOM   844  C  CB    . LEU A 1 139 ? 14.759  -18.722 35.886  1.00 23.11 ? 118 LEU A CB    1 
ATOM   845  C  CG    . LEU A 1 139 ? 15.012  -17.792 34.707  1.00 24.25 ? 118 LEU A CG    1 
ATOM   846  C  CD1   . LEU A 1 139 ? 15.695  -16.516 35.138  1.00 26.23 ? 118 LEU A CD1   1 
ATOM   847  C  CD2   . LEU A 1 139 ? 15.845  -18.478 33.618  1.00 26.30 ? 118 LEU A CD2   1 
ATOM   848  N  N     . ALA A 1 140 ? 11.663  -18.901 36.116  1.00 22.65 ? 119 ALA A N     1 
ATOM   849  C  CA    . ALA A 1 140 ? 10.284  -18.703 35.604  1.00 21.96 ? 119 ALA A CA    1 
ATOM   850  C  C     . ALA A 1 140 ? 9.461   -17.973 36.655  1.00 24.51 ? 119 ALA A C     1 
ATOM   851  O  O     . ALA A 1 140 ? 8.679   -17.080 36.302  1.00 21.82 ? 119 ALA A O     1 
ATOM   852  C  CB    . ALA A 1 140 ? 9.664   -20.025 35.246  1.00 23.06 ? 119 ALA A CB    1 
ATOM   853  N  N     . GLY A 1 141 ? 9.561   -18.402 37.920  1.00 23.87 ? 120 GLY A N     1 
ATOM   854  C  CA    . GLY A 1 141 ? 8.831   -17.769 39.030  1.00 22.52 ? 120 GLY A CA    1 
ATOM   855  C  C     . GLY A 1 141 ? 9.159   -16.301 39.181  1.00 21.74 ? 120 GLY A C     1 
ATOM   856  O  O     . GLY A 1 141 ? 8.231   -15.514 39.420  1.00 22.79 ? 120 GLY A O     1 
ATOM   857  N  N     . ALA A 1 142 ? 10.430  -15.931 39.091  1.00 22.81 ? 121 ALA A N     1 
ATOM   858  C  CA    . ALA A 1 142 ? 10.885  -14.532 39.214  1.00 24.09 ? 121 ALA A CA    1 
ATOM   859  C  C     . ALA A 1 142 ? 10.321  -13.694 38.049  1.00 21.78 ? 121 ALA A C     1 
ATOM   860  O  O     . ALA A 1 142 ? 9.904   -12.563 38.300  1.00 21.83 ? 121 ALA A O     1 
ATOM   861  C  CB    . ALA A 1 142 ? 12.389  -14.481 39.212  1.00 25.28 ? 121 ALA A CB    1 
ATOM   862  N  N     . LEU A 1 143 ? 10.283  -14.242 36.832  1.00 22.22 ? 122 LEU A N     1 
ATOM   863  C  CA    . LEU A 1 143 ? 9.686   -13.515 35.664  1.00 22.51 ? 122 LEU A CA    1 
ATOM   864  C  C     . LEU A 1 143 ? 8.173   -13.346 35.873  1.00 22.24 ? 122 LEU A C     1 
ATOM   865  O  O     . LEU A 1 143 ? 7.666   -12.273 35.556  1.00 22.55 ? 122 LEU A O     1 
ATOM   866  C  CB    . LEU A 1 143 ? 9.974   -14.281 34.371  1.00 23.44 ? 122 LEU A CB    1 
ATOM   867  C  CG    . LEU A 1 143 ? 9.503   -13.567 33.099  1.00 22.99 ? 122 LEU A CG    1 
ATOM   868  C  CD1   . LEU A 1 143 ? 10.008  -12.138 33.038  1.00 22.55 ? 122 LEU A CD1   1 
ATOM   869  C  CD2   . LEU A 1 143 ? 9.909   -14.334 31.856  1.00 25.64 ? 122 LEU A CD2   1 
ATOM   870  N  N     . GLU A 1 144 ? 7.467   -14.350 36.415  1.00 22.56 ? 123 GLU A N     1 
ATOM   871  C  CA    . GLU A 1 144 ? 6.032   -14.229 36.770  1.00 22.86 ? 123 GLU A CA    1 
ATOM   872  C  C     . GLU A 1 144 ? 5.819   -13.143 37.827  1.00 21.63 ? 123 GLU A C     1 
ATOM   873  O  O     . GLU A 1 144 ? 4.796   -12.423 37.748  1.00 21.20 ? 123 GLU A O     1 
ATOM   874  C  CB    . GLU A 1 144 ? 5.488   -15.565 37.255  1.00 24.70 ? 123 GLU A CB    1 
ATOM   875  C  CG    . GLU A 1 144 ? 5.321   -16.524 36.104  1.00 27.10 ? 123 GLU A CG    1 
ATOM   876  C  CD    . GLU A 1 144 ? 4.732   -17.851 36.486  1.00 29.26 ? 123 GLU A CD    1 
ATOM   877  O  OE1   . GLU A 1 144 ? 4.361   -18.591 35.607  1.00 30.09 ? 123 GLU A OE1   1 
ATOM   878  O  OE2   . GLU A 1 144 ? 4.756   -18.135 37.672  1.00 31.64 ? 123 GLU A OE2   1 
ATOM   879  N  N     . ALA A 1 145 ? 6.728   -13.027 38.794  1.00 21.80 ? 124 ALA A N     1 
ATOM   880  C  CA    . ALA A 1 145 ? 6.537   -12.053 39.897  1.00 23.59 ? 124 ALA A CA    1 
ATOM   881  C  C     . ALA A 1 145 ? 6.686   -10.652 39.292  1.00 22.01 ? 124 ALA A C     1 
ATOM   882  O  O     . ALA A 1 145 ? 5.959   -9.756  39.738  1.00 25.95 ? 124 ALA A O     1 
ATOM   883  C  CB    . ALA A 1 145 ? 7.494   -12.321 41.049  1.00 26.77 ? 124 ALA A CB    1 
ATOM   884  N  N     . ILE A 1 146 ? 7.569   -10.458 38.304  1.00 20.97 ? 125 ILE A N     1 
ATOM   885  C  CA    . ILE A 1 146 ? 7.704   -9.160  37.565  1.00 20.47 ? 125 ILE A CA    1 
ATOM   886  C  C     . ILE A 1 146 ? 6.420   -8.968  36.742  1.00 19.78 ? 125 ILE A C     1 
ATOM   887  O  O     . ILE A 1 146 ? 5.775   -7.898  36.815  1.00 18.84 ? 125 ILE A O     1 
ATOM   888  C  CB    . ILE A 1 146 ? 8.999   -9.166  36.730  1.00 22.74 ? 125 ILE A CB    1 
ATOM   889  C  CG1   . ILE A 1 146 ? 10.223  -9.090  37.641  1.00 26.78 ? 125 ILE A CG1   1 
ATOM   890  C  CG2   . ILE A 1 146 ? 9.064   -8.092  35.649  1.00 25.00 ? 125 ILE A CG2   1 
ATOM   891  C  CD1   . ILE A 1 146 ? 11.502  -9.343  36.917  1.00 27.36 ? 125 ILE A CD1   1 
ATOM   892  N  N     . ALA A 1 147 ? 6.021   -10.008 36.006  1.00 19.10 ? 126 ALA A N     1 
ATOM   893  C  CA    . ALA A 1 147 ? 4.849   -9.933  35.110  1.00 20.50 ? 126 ALA A CA    1 
ATOM   894  C  C     . ALA A 1 147 ? 3.618   -9.396  35.839  1.00 18.46 ? 126 ALA A C     1 
ATOM   895  O  O     . ALA A 1 147 ? 2.890   -8.566  35.267  1.00 16.19 ? 126 ALA A O     1 
ATOM   896  C  CB    . ALA A 1 147 ? 4.592   -11.287 34.531  1.00 20.64 ? 126 ALA A CB    1 
ATOM   897  N  N     . GLU A 1 148 ? 3.315   -9.939  37.022  1.00 20.81 ? 127 GLU A N     1 
ATOM   898  C  CA    . GLU A 1 148 ? 2.094   -9.596  37.797  1.00 25.36 ? 127 GLU A CA    1 
ATOM   899  C  C     . GLU A 1 148 ? 2.028   -8.103  38.140  1.00 23.97 ? 127 GLU A C     1 
ATOM   900  O  O     . GLU A 1 148 ? 0.897   -7.618  38.344  1.00 21.65 ? 127 GLU A O     1 
ATOM   901  C  CB    . GLU A 1 148 ? 1.952   -10.500 39.036  1.00 32.11 ? 127 GLU A CB    1 
ATOM   902  C  CG    . GLU A 1 148 ? 1.119   -11.763 38.733  1.00 46.72 ? 127 GLU A CG    1 
ATOM   903  C  CD    . GLU A 1 148 ? -0.423  -11.728 38.850  1.00 62.15 ? 127 GLU A CD    1 
ATOM   904  O  OE1   . GLU A 1 148 ? -1.156  -11.149 37.959  1.00 63.00 ? 127 GLU A OE1   1 
ATOM   905  O  OE2   . GLU A 1 148 ? -0.934  -12.336 39.831  1.00 74.66 ? 127 GLU A OE2   1 
ATOM   906  N  N     . LYS A 1 149 ? 3.133   -7.351  38.054  1.00 20.65 ? 128 LYS A N     1 
ATOM   907  C  CA    . LYS A 1 149 ? 3.155   -5.897  38.356  1.00 22.09 ? 128 LYS A CA    1 
ATOM   908  C  C     . LYS A 1 149 ? 2.899   -5.078  37.089  1.00 22.24 ? 128 LYS A C     1 
ATOM   909  O  O     . LYS A 1 149 ? 2.798   -3.869  37.204  1.00 19.93 ? 128 LYS A O     1 
ATOM   910  C  CB    . LYS A 1 149 ? 4.522   -5.477  38.915  1.00 23.15 ? 128 LYS A CB    1 
ATOM   911  C  CG    . LYS A 1 149 ? 4.971   -6.254  40.146  1.00 29.24 ? 128 LYS A CG    1 
ATOM   912  C  CD    . LYS A 1 149 ? 3.855   -6.440  41.150  1.00 32.05 ? 128 LYS A CD    1 
ATOM   913  C  CE    . LYS A 1 149 ? 4.322   -7.149  42.408  1.00 44.57 ? 128 LYS A CE    1 
ATOM   914  N  NZ    . LYS A 1 149 ? 3.176   -7.633  43.215  1.00 43.98 ? 128 LYS A NZ    1 
ATOM   915  N  N     . VAL A 1 150 ? 2.807   -5.713  35.913  1.00 20.09 ? 129 VAL A N     1 
ATOM   916  C  CA    . VAL A 1 150 ? 2.695   -4.962  34.619  1.00 20.05 ? 129 VAL A CA    1 
ATOM   917  C  C     . VAL A 1 150 ? 1.232   -4.885  34.230  1.00 18.94 ? 129 VAL A C     1 
ATOM   918  O  O     . VAL A 1 150 ? 0.622   -5.878  33.854  1.00 20.04 ? 129 VAL A O     1 
ATOM   919  C  CB    . VAL A 1 150 ? 3.502   -5.644  33.497  1.00 18.49 ? 129 VAL A CB    1 
ATOM   920  C  CG1   . VAL A 1 150 ? 3.416   -4.842  32.184  1.00 19.08 ? 129 VAL A CG1   1 
ATOM   921  C  CG2   . VAL A 1 150 ? 4.940   -5.845  33.873  1.00 18.90 ? 129 VAL A CG2   1 
ATOM   922  N  N     . PRO A 1 151 ? 0.624   -3.694  34.211  1.00 19.45 ? 130 PRO A N     1 
ATOM   923  C  CA    . PRO A 1 151 ? -0.791  -3.611  33.873  1.00 20.10 ? 130 PRO A CA    1 
ATOM   924  C  C     . PRO A 1 151 ? -1.049  -4.051  32.432  1.00 21.45 ? 130 PRO A C     1 
ATOM   925  O  O     . PRO A 1 151 ? -0.306  -3.645  31.546  1.00 19.79 ? 130 PRO A O     1 
ATOM   926  C  CB    . PRO A 1 151 ? -1.115  -2.131  34.087  1.00 18.63 ? 130 PRO A CB    1 
ATOM   927  C  CG    . PRO A 1 151 ? -0.038  -1.642  35.037  1.00 19.74 ? 130 PRO A CG    1 
ATOM   928  C  CD    . PRO A 1 151 ? 1.204   -2.401  34.633  1.00 19.92 ? 130 PRO A CD    1 
ATOM   929  N  N     . LEU A 1 152 ? -2.065  -4.901  32.238  1.00 20.04 ? 131 LEU A N     1 
ATOM   930  C  CA    . LEU A 1 152 ? -2.293  -5.505  30.904  1.00 19.40 ? 131 LEU A CA    1 
ATOM   931  C  C     . LEU A 1 152 ? -2.681  -4.401  29.917  1.00 19.54 ? 131 LEU A C     1 
ATOM   932  O  O     . LEU A 1 152 ? -2.392  -4.581  28.741  1.00 20.04 ? 131 LEU A O     1 
ATOM   933  C  CB    . LEU A 1 152 ? -3.389  -6.560  31.011  1.00 20.56 ? 131 LEU A CB    1 
ATOM   934  C  CG    . LEU A 1 152 ? -2.986  -7.794  31.809  1.00 23.30 ? 131 LEU A CG    1 
ATOM   935  C  CD1   . LEU A 1 152 ? -4.119  -8.816  31.787  1.00 26.82 ? 131 LEU A CD1   1 
ATOM   936  C  CD2   . LEU A 1 152 ? -1.680  -8.373  31.281  1.00 23.09 ? 131 LEU A CD2   1 
ATOM   937  N  N     . ASP A 1 153 ? -3.351  -3.332  30.373  1.00 18.62 ? 132 ASP A N     1 
ATOM   938  C  CA    . ASP A 1 153 ? -3.868  -2.294  29.431  1.00 22.30 ? 132 ASP A CA    1 
ATOM   939  C  C     . ASP A 1 153 ? -2.836  -1.167  29.235  1.00 22.71 ? 132 ASP A C     1 
ATOM   940  O  O     . ASP A 1 153 ? -3.052  -0.299  28.378  1.00 25.00 ? 132 ASP A O     1 
ATOM   941  C  CB    . ASP A 1 153 ? -5.207  -1.713  29.888  1.00 26.32 ? 132 ASP A CB    1 
ATOM   942  C  CG    . ASP A 1 153 ? -5.185  -1.074  31.269  1.00 31.38 ? 132 ASP A CG    1 
ATOM   943  O  OD1   . ASP A 1 153 ? -4.303  -1.407  32.070  1.00 30.37 ? 132 ASP A OD1   1 
ATOM   944  O  OD2   . ASP A 1 153 ? -6.023  -0.205  31.510  1.00 37.99 ? 132 ASP A OD2   1 
ATOM   945  N  N     . ALA A 1 154 ? -1.752  -1.148  30.008  1.00 21.01 ? 133 ALA A N     1 
ATOM   946  C  CA    . ALA A 1 154 ? -0.803  -0.019  30.056  1.00 17.79 ? 133 ALA A CA    1 
ATOM   947  C  C     . ALA A 1 154 ? 0.491   -0.508  30.681  1.00 18.28 ? 133 ALA A C     1 
ATOM   948  O  O     . ALA A 1 154 ? 0.807   -0.117  31.800  1.00 19.27 ? 133 ALA A O     1 
ATOM   949  C  CB    . ALA A 1 154 ? -1.402  1.102   30.876  1.00 18.91 ? 133 ALA A CB    1 
ATOM   950  N  N     . PRO A 1 155 ? 1.316   -1.313  29.972  1.00 18.77 ? 134 PRO A N     1 
ATOM   951  C  CA    . PRO A 1 155 ? 2.591   -1.759  30.535  1.00 20.51 ? 134 PRO A CA    1 
ATOM   952  C  C     . PRO A 1 155 ? 3.515   -0.613  30.962  1.00 18.89 ? 134 PRO A C     1 
ATOM   953  O  O     . PRO A 1 155 ? 4.284   -0.820  31.903  1.00 20.16 ? 134 PRO A O     1 
ATOM   954  C  CB    . PRO A 1 155 ? 3.223   -2.629  29.445  1.00 22.26 ? 134 PRO A CB    1 
ATOM   955  C  CG    . PRO A 1 155 ? 2.299   -2.608  28.284  1.00 20.21 ? 134 PRO A CG    1 
ATOM   956  C  CD    . PRO A 1 155 ? 1.002   -1.975  28.703  1.00 20.63 ? 134 PRO A CD    1 
ATOM   957  N  N     . TRP A 1 156 ? 3.402   0.539   30.300  1.00 18.20 ? 135 TRP A N     1 
ATOM   958  C  CA    . TRP A 1 156 ? 4.209   1.758   30.591  1.00 19.63 ? 135 TRP A CA    1 
ATOM   959  C  C     . TRP A 1 156 ? 3.878   2.289   31.999  1.00 21.28 ? 135 TRP A C     1 
ATOM   960  O  O     . TRP A 1 156 ? 4.576   3.194   32.445  1.00 19.49 ? 135 TRP A O     1 
ATOM   961  C  CB    . TRP A 1 156 ? 4.007   2.842   29.513  1.00 19.99 ? 135 TRP A CB    1 
ATOM   962  C  CG    . TRP A 1 156 ? 2.590   3.284   29.333  1.00 19.02 ? 135 TRP A CG    1 
ATOM   963  C  CD1   . TRP A 1 156 ? 1.930   4.292   29.981  1.00 20.24 ? 135 TRP A CD1   1 
ATOM   964  C  CD2   . TRP A 1 156 ? 1.640   2.709   28.416  1.00 17.72 ? 135 TRP A CD2   1 
ATOM   965  N  NE1   . TRP A 1 156 ? 0.647   4.366   29.529  1.00 18.80 ? 135 TRP A NE1   1 
ATOM   966  C  CE2   . TRP A 1 156 ? 0.433   3.394   28.588  1.00 16.60 ? 135 TRP A CE2   1 
ATOM   967  C  CE3   . TRP A 1 156 ? 1.705   1.673   27.473  1.00 16.61 ? 135 TRP A CE3   1 
ATOM   968  C  CZ2   . TRP A 1 156 ? -0.712  3.066   27.871  1.00 19.28 ? 135 TRP A CZ2   1 
ATOM   969  C  CZ3   . TRP A 1 156 ? 0.584   1.361   26.740  1.00 18.47 ? 135 TRP A CZ3   1 
ATOM   970  C  CH2   . TRP A 1 156 ? -0.621  2.032   26.953  1.00 20.01 ? 135 TRP A CH2   1 
ATOM   971  N  N     . LEU A 1 157 ? 2.817   1.805   32.666  1.00 20.76 ? 136 LEU A N     1 
ATOM   972  C  CA    . LEU A 1 157 ? 2.422   2.320   34.008  1.00 20.48 ? 136 LEU A CA    1 
ATOM   973  C  C     . LEU A 1 157 ? 2.872   1.337   35.079  1.00 22.07 ? 136 LEU A C     1 
ATOM   974  O  O     . LEU A 1 157 ? 2.525   1.515   36.239  1.00 20.99 ? 136 LEU A O     1 
ATOM   975  C  CB    . LEU A 1 157 ? 0.911   2.529   34.077  1.00 21.13 ? 136 LEU A CB    1 
ATOM   976  C  CG    . LEU A 1 157 ? 0.356   3.676   33.234  1.00 22.44 ? 136 LEU A CG    1 
ATOM   977  C  CD1   . LEU A 1 157 ? -1.126  3.772   33.427  1.00 26.61 ? 136 LEU A CD1   1 
ATOM   978  C  CD2   . LEU A 1 157 ? 1.022   5.018   33.548  1.00 23.87 ? 136 LEU A CD2   1 
ATOM   979  N  N     . ALA A 1 158 ? 3.637   0.325   34.729  1.00 19.23 ? 137 ALA A N     1 
ATOM   980  C  CA    . ALA A 1 158 ? 4.266   -0.525  35.766  1.00 19.99 ? 137 ALA A CA    1 
ATOM   981  C  C     . ALA A 1 158 ? 5.110   0.383   36.664  1.00 23.94 ? 137 ALA A C     1 
ATOM   982  O  O     . ALA A 1 158 ? 5.806   1.267   36.168  1.00 19.55 ? 137 ALA A O     1 
ATOM   983  C  CB    . ALA A 1 158 ? 5.113   -1.623  35.156  1.00 19.47 ? 137 ALA A CB    1 
ATOM   984  N  N     . PRO A 1 159 ? 5.085   0.203   38.002  1.00 29.03 ? 138 PRO A N     1 
ATOM   985  C  CA    . PRO A 1 159 ? 5.915   1.031   38.895  1.00 28.25 ? 138 PRO A CA    1 
ATOM   986  C  C     . PRO A 1 159 ? 7.396   1.086   38.449  1.00 26.21 ? 138 PRO A C     1 
ATOM   987  O  O     . PRO A 1 159 ? 7.993   2.139   38.487  1.00 26.32 ? 138 PRO A O     1 
ATOM   988  C  CB    . PRO A 1 159 ? 5.796   0.322   40.255  1.00 31.36 ? 138 PRO A CB    1 
ATOM   989  C  CG    . PRO A 1 159 ? 4.482   -0.428  40.190  1.00 35.00 ? 138 PRO A CG    1 
ATOM   990  C  CD    . PRO A 1 159 ? 4.280   -0.796  38.732  1.00 32.71 ? 138 PRO A CD    1 
ATOM   991  N  N     . GLU A 1 160 ? 7.954   -0.029  37.980  1.00 22.69 ? 139 GLU A N     1 
ATOM   992  C  CA    . GLU A 1 160 ? 9.364   -0.105  37.537  1.00 23.30 ? 139 GLU A CA    1 
ATOM   993  C  C     . GLU A 1 160 ? 9.485   -0.040  35.990  1.00 23.67 ? 139 GLU A C     1 
ATOM   994  O  O     . GLU A 1 160 ? 10.493  -0.570  35.468  1.00 21.34 ? 139 GLU A O     1 
ATOM   995  C  CB    . GLU A 1 160 ? 9.952   -1.399  38.109  1.00 26.06 ? 139 GLU A CB    1 
ATOM   996  C  CG    . GLU A 1 160 ? 9.922   -1.496  39.622  1.00 30.15 ? 139 GLU A CG    1 
ATOM   997  C  CD    . GLU A 1 160 ? 10.822  -0.479  40.315  1.00 34.74 ? 139 GLU A CD    1 
ATOM   998  O  OE1   . GLU A 1 160 ? 11.536  0.270   39.612  1.00 36.50 ? 139 GLU A OE1   1 
ATOM   999  O  OE2   . GLU A 1 160 ? 10.794  -0.430  41.545  1.00 36.43 ? 139 GLU A OE2   1 
ATOM   1000 N  N     . ALA A 1 161 ? 8.495   0.521   35.273  1.00 21.92 ? 140 ALA A N     1 
ATOM   1001 C  CA    . ALA A 1 161 ? 8.448   0.493   33.786  1.00 22.89 ? 140 ALA A CA    1 
ATOM   1002 C  C     . ALA A 1 161 ? 9.776   1.023   33.226  1.00 22.44 ? 140 ALA A C     1 
ATOM   1003 O  O     . ALA A 1 161 ? 10.351  0.392   32.323  1.00 21.71 ? 140 ALA A O     1 
ATOM   1004 C  CB    . ALA A 1 161 ? 7.275   1.291   33.278  1.00 21.66 ? 140 ALA A CB    1 
ATOM   1005 N  N     . ALA A 1 162 ? 10.273  2.156   33.723  1.00 21.35 ? 141 ALA A N     1 
ATOM   1006 C  CA    . ALA A 1 162 ? 11.513  2.780   33.192  1.00 22.62 ? 141 ALA A CA    1 
ATOM   1007 C  C     . ALA A 1 162 ? 12.699  1.806   33.213  1.00 22.85 ? 141 ALA A C     1 
ATOM   1008 O  O     . ALA A 1 162 ? 13.411  1.637   32.158  1.00 23.95 ? 141 ALA A O     1 
ATOM   1009 C  CB    . ALA A 1 162 ? 11.841  4.036   33.989  1.00 25.51 ? 141 ALA A CB    1 
ATOM   1010 N  N     . ALA A 1 163 ? 12.931  1.163   34.351  1.00 22.19 ? 142 ALA A N     1 
ATOM   1011 C  CA    . ALA A 1 163 ? 14.059  0.229   34.543  1.00 23.97 ? 142 ALA A CA    1 
ATOM   1012 C  C     . ALA A 1 163 ? 13.825  -0.989  33.651  1.00 21.16 ? 142 ALA A C     1 
ATOM   1013 O  O     . ALA A 1 163 ? 14.775  -1.418  32.938  1.00 21.95 ? 142 ALA A O     1 
ATOM   1014 C  CB    . ALA A 1 163 ? 14.153  -0.154  35.997  1.00 26.21 ? 142 ALA A CB    1 
ATOM   1015 N  N     . TRP A 1 164 ? 12.616  -1.546  33.725  1.00 19.79 ? 143 TRP A N     1 
ATOM   1016 C  CA    . TRP A 1 164 ? 12.301  -2.798  32.993  1.00 18.72 ? 143 TRP A CA    1 
ATOM   1017 C  C     . TRP A 1 164 ? 12.310  -2.558  31.474  1.00 18.89 ? 143 TRP A C     1 
ATOM   1018 O  O     . TRP A 1 164 ? 12.672  -3.482  30.710  1.00 21.79 ? 143 TRP A O     1 
ATOM   1019 C  CB    . TRP A 1 164 ? 10.990  -3.370  33.509  1.00 21.25 ? 143 TRP A CB    1 
ATOM   1020 C  CG    . TRP A 1 164 ? 11.061  -3.854  34.925  1.00 21.91 ? 143 TRP A CG    1 
ATOM   1021 C  CD1   . TRP A 1 164 ? 12.166  -3.938  35.726  1.00 26.52 ? 143 TRP A CD1   1 
ATOM   1022 C  CD2   . TRP A 1 164 ? 9.960   -4.326  35.729  1.00 22.98 ? 143 TRP A CD2   1 
ATOM   1023 N  NE1   . TRP A 1 164 ? 11.837  -4.434  36.965  1.00 24.02 ? 143 TRP A NE1   1 
ATOM   1024 C  CE2   . TRP A 1 164 ? 10.488  -4.666  37.005  1.00 24.01 ? 143 TRP A CE2   1 
ATOM   1025 C  CE3   . TRP A 1 164 ? 8.583   -4.437  35.527  1.00 24.34 ? 143 TRP A CE3   1 
ATOM   1026 C  CZ2   . TRP A 1 164 ? 9.687   -5.158  38.045  1.00 23.38 ? 143 TRP A CZ2   1 
ATOM   1027 C  CZ3   . TRP A 1 164 ? 7.804   -4.979  36.533  1.00 27.74 ? 143 TRP A CZ3   1 
ATOM   1028 C  CH2   . TRP A 1 164 ? 8.344   -5.302  37.786  1.00 27.33 ? 143 TRP A CH2   1 
ATOM   1029 N  N     . ASP A 1 165 ? 12.005  -1.355  31.022  1.00 17.92 ? 144 ASP A N     1 
ATOM   1030 C  CA    . ASP A 1 165 ? 12.006  -1.023  29.574  1.00 20.29 ? 144 ASP A CA    1 
ATOM   1031 C  C     . ASP A 1 165 ? 13.425  -0.740  29.077  1.00 22.33 ? 144 ASP A C     1 
ATOM   1032 O  O     . ASP A 1 165 ? 13.655  -0.862  27.883  1.00 25.30 ? 144 ASP A O     1 
ATOM   1033 C  CB    . ASP A 1 165 ? 11.045  0.118   29.258  1.00 18.97 ? 144 ASP A CB    1 
ATOM   1034 C  CG    . ASP A 1 165 ? 10.571  0.090   27.818  1.00 22.39 ? 144 ASP A CG    1 
ATOM   1035 O  OD1   . ASP A 1 165 ? 10.557  -1.008  27.240  1.00 23.43 ? 144 ASP A OD1   1 
ATOM   1036 O  OD2   . ASP A 1 165 ? 10.235  1.145   27.310  1.00 21.78 ? 144 ASP A OD2   1 
ATOM   1037 N  N     . ALA A 1 166 ? 14.384  -0.508  29.968  1.00 22.43 ? 145 ALA A N     1 
ATOM   1038 C  CA    . ALA A 1 166 ? 15.765  -0.165  29.554  1.00 23.39 ? 145 ALA A CA    1 
ATOM   1039 C  C     . ALA A 1 166 ? 16.644  -1.415  29.527  1.00 27.02 ? 145 ALA A C     1 
ATOM   1040 O  O     . ALA A 1 166 ? 17.889  -1.300  29.326  1.00 30.04 ? 145 ALA A O     1 
ATOM   1041 C  CB    . ALA A 1 166 ? 16.307  0.864   30.497  1.00 21.69 ? 145 ALA A CB    1 
ATOM   1042 N  N     . THR A 1 167 ? 16.074  -2.561  29.882  1.00 21.90 ? 146 THR A N     1 
ATOM   1043 C  CA    . THR A 1 167 ? 16.817  -3.819  30.070  1.00 22.19 ? 146 THR A CA    1 
ATOM   1044 C  C     . THR A 1 167 ? 16.309  -4.828  29.044  1.00 21.37 ? 146 THR A C     1 
ATOM   1045 O  O     . THR A 1 167 ? 15.090  -4.864  28.884  1.00 21.38 ? 146 THR A O     1 
ATOM   1046 C  CB    . THR A 1 167 ? 16.531  -4.397  31.468  1.00 25.76 ? 146 THR A CB    1 
ATOM   1047 O  OG1   . THR A 1 167 ? 16.674  -3.368  32.449  1.00 31.25 ? 146 THR A OG1   1 
ATOM   1048 C  CG2   . THR A 1 167 ? 17.471  -5.524  31.802  1.00 28.90 ? 146 THR A CG2   1 
ATOM   1049 N  N     . THR A 1 168 ? 17.181  -5.619  28.419  1.00 20.04 ? 147 THR A N     1 
ATOM   1050 C  CA    . THR A 1 168 ? 16.734  -6.760  27.570  1.00 16.99 ? 147 THR A CA    1 
ATOM   1051 C  C     . THR A 1 168 ? 16.329  -7.882  28.506  1.00 17.95 ? 147 THR A C     1 
ATOM   1052 O  O     . THR A 1 168 ? 16.873  -7.958  29.664  1.00 16.38 ? 147 THR A O     1 
ATOM   1053 C  CB    . THR A 1 168 ? 17.798  -7.213  26.556  1.00 19.30 ? 147 THR A CB    1 
ATOM   1054 O  OG1   . THR A 1 168 ? 18.892  -7.798  27.271  1.00 18.77 ? 147 THR A OG1   1 
ATOM   1055 C  CG2   . THR A 1 168 ? 18.248  -6.067  25.676  1.00 20.72 ? 147 THR A CG2   1 
ATOM   1056 N  N     . LEU A 1 169 ? 15.532  -8.824  28.000  1.00 16.72 ? 148 LEU A N     1 
ATOM   1057 C  CA    . LEU A 1 169 ? 15.302  -10.073 28.769  1.00 17.21 ? 148 LEU A CA    1 
ATOM   1058 C  C     . LEU A 1 169 ? 16.646  -10.771 28.995  1.00 19.42 ? 148 LEU A C     1 
ATOM   1059 O  O     . LEU A 1 169 ? 16.845  -11.313 30.100  1.00 19.45 ? 148 LEU A O     1 
ATOM   1060 C  CB    . LEU A 1 169 ? 14.339  -10.983 27.999  1.00 15.75 ? 148 LEU A CB    1 
ATOM   1061 C  CG    . LEU A 1 169 ? 13.895  -12.261 28.691  1.00 17.63 ? 148 LEU A CG    1 
ATOM   1062 C  CD1   . LEU A 1 169 ? 13.178  -11.986 30.002  1.00 16.83 ? 148 LEU A CD1   1 
ATOM   1063 C  CD2   . LEU A 1 169 ? 13.026  -13.089 27.735  1.00 17.83 ? 148 LEU A CD2   1 
ATOM   1064 N  N     . ARG A 1 170 ? 17.546  -10.749 28.018  1.00 19.77 ? 149 ARG A N     1 
ATOM   1065 C  CA    . ARG A 1 170 ? 18.817  -11.504 28.125  1.00 22.00 ? 149 ARG A CA    1 
ATOM   1066 C  C     . ARG A 1 170 ? 19.643  -10.934 29.293  1.00 20.04 ? 149 ARG A C     1 
ATOM   1067 O  O     . ARG A 1 170 ? 20.147  -11.755 30.084  1.00 21.40 ? 149 ARG A O     1 
ATOM   1068 C  CB    . ARG A 1 170 ? 19.635  -11.463 26.840  1.00 23.96 ? 149 ARG A CB    1 
ATOM   1069 C  CG    . ARG A 1 170 ? 20.919  -12.284 26.951  1.00 26.22 ? 149 ARG A CG    1 
ATOM   1070 C  CD    . ARG A 1 170 ? 21.557  -12.559 25.626  1.00 28.48 ? 149 ARG A CD    1 
ATOM   1071 N  NE    . ARG A 1 170 ? 20.681  -13.410 24.828  1.00 32.37 ? 149 ARG A NE    1 
ATOM   1072 C  CZ    . ARG A 1 170 ? 20.984  -13.868 23.621  1.00 34.36 ? 149 ARG A CZ    1 
ATOM   1073 N  NH1   . ARG A 1 170 ? 22.140  -13.543 23.067  1.00 35.21 ? 149 ARG A NH1   1 
ATOM   1074 N  NH2   . ARG A 1 170 ? 20.119  -14.614 22.960  1.00 32.85 ? 149 ARG A NH2   1 
ATOM   1075 N  N     . GLU A 1 171 ? 19.761  -9.616  29.401  1.00 22.80 ? 150 GLU A N     1 
ATOM   1076 C  CA    . GLU A 1 171 ? 20.493  -8.972  30.527  1.00 24.24 ? 150 GLU A CA    1 
ATOM   1077 C  C     . GLU A 1 171 ? 19.885  -9.446  31.858  1.00 25.38 ? 150 GLU A C     1 
ATOM   1078 O  O     . GLU A 1 171 ? 20.625  -9.850  32.785  1.00 24.31 ? 150 GLU A O     1 
ATOM   1079 C  CB    . GLU A 1 171 ? 20.507  -7.457  30.375  1.00 26.89 ? 150 GLU A CB    1 
ATOM   1080 C  CG    . GLU A 1 171 ? 21.062  -6.766  31.608  1.00 31.09 ? 150 GLU A CG    1 
ATOM   1081 C  CD    . GLU A 1 171 ? 21.306  -5.270  31.542  1.00 34.83 ? 150 GLU A CD    1 
ATOM   1082 O  OE1   . GLU A 1 171 ? 20.752  -4.615  30.656  1.00 35.12 ? 150 GLU A OE1   1 
ATOM   1083 O  OE2   . GLU A 1 171 ? 22.078  -4.780  32.390  1.00 42.04 ? 150 GLU A OE2   1 
ATOM   1084 N  N     . TRP A 1 172 ? 18.562  -9.419  31.971  1.00 24.26 ? 151 TRP A N     1 
ATOM   1085 C  CA    . TRP A 1 172 ? 17.887  -9.874  33.214  1.00 23.81 ? 151 TRP A CA    1 
ATOM   1086 C  C     . TRP A 1 172 ? 18.231  -11.340 33.521  1.00 24.41 ? 151 TRP A C     1 
ATOM   1087 O  O     . TRP A 1 172 ? 18.580  -11.636 34.705  1.00 26.23 ? 151 TRP A O     1 
ATOM   1088 C  CB    . TRP A 1 172 ? 16.386  -9.613  33.134  1.00 23.34 ? 151 TRP A CB    1 
ATOM   1089 C  CG    . TRP A 1 172 ? 15.668  -10.096 34.349  1.00 23.30 ? 151 TRP A CG    1 
ATOM   1090 C  CD1   . TRP A 1 172 ? 15.554  -9.472  35.565  1.00 23.64 ? 151 TRP A CD1   1 
ATOM   1091 C  CD2   . TRP A 1 172 ? 15.033  -11.371 34.487  1.00 21.21 ? 151 TRP A CD2   1 
ATOM   1092 N  NE1   . TRP A 1 172 ? 14.847  -10.263 36.433  1.00 23.44 ? 151 TRP A NE1   1 
ATOM   1093 C  CE2   . TRP A 1 172 ? 14.531  -11.437 35.811  1.00 21.52 ? 151 TRP A CE2   1 
ATOM   1094 C  CE3   . TRP A 1 172 ? 14.811  -12.434 33.611  1.00 22.12 ? 151 TRP A CE3   1 
ATOM   1095 C  CZ2   . TRP A 1 172 ? 13.799  -12.530 36.268  1.00 23.04 ? 151 TRP A CZ2   1 
ATOM   1096 C  CZ3   . TRP A 1 172 ? 14.128  -13.536 34.089  1.00 23.87 ? 151 TRP A CZ3   1 
ATOM   1097 C  CH2   . TRP A 1 172 ? 13.604  -13.561 35.379  1.00 21.15 ? 151 TRP A CH2   1 
ATOM   1098 N  N     . VAL A 1 173 ? 18.123  -12.254 32.546  1.00 22.77 ? 152 VAL A N     1 
ATOM   1099 C  CA    . VAL A 1 173 ? 18.458  -13.695 32.758  1.00 24.41 ? 152 VAL A CA    1 
ATOM   1100 C  C     . VAL A 1 173 ? 19.910  -13.784 33.248  1.00 25.76 ? 152 VAL A C     1 
ATOM   1101 O  O     . VAL A 1 173 ? 20.180  -14.545 34.182  1.00 25.78 ? 152 VAL A O     1 
ATOM   1102 C  CB    . VAL A 1 173 ? 18.273  -14.524 31.478  1.00 25.38 ? 152 VAL A CB    1 
ATOM   1103 C  CG1   . VAL A 1 173 ? 18.843  -15.932 31.608  1.00 26.38 ? 152 VAL A CG1   1 
ATOM   1104 C  CG2   . VAL A 1 173 ? 16.820  -14.575 31.026  1.00 26.09 ? 152 VAL A CG2   1 
ATOM   1105 N  N     . ALA A 1 174 ? 20.817  -13.032 32.648  1.00 24.49 ? 153 ALA A N     1 
ATOM   1106 C  CA    . ALA A 1 174 ? 22.260  -13.099 32.999  1.00 28.64 ? 153 ALA A CA    1 
ATOM   1107 C  C     . ALA A 1 174 ? 22.460  -12.637 34.448  1.00 34.16 ? 153 ALA A C     1 
ATOM   1108 O  O     . ALA A 1 174 ? 23.238  -13.275 35.180  1.00 31.66 ? 153 ALA A O     1 
ATOM   1109 C  CB    . ALA A 1 174 ? 23.080  -12.296 32.034  1.00 30.32 ? 153 ALA A CB    1 
ATOM   1110 N  N     . GLY A 1 175 ? 21.736  -11.608 34.876  1.00 32.53 ? 154 GLY A N     1 
ATOM   1111 C  CA    . GLY A 1 175 ? 21.785  -11.081 36.254  1.00 35.58 ? 154 GLY A CA    1 
ATOM   1112 C  C     . GLY A 1 175 ? 21.271  -12.053 37.313  1.00 36.81 ? 154 GLY A C     1 
ATOM   1113 O  O     . GLY A 1 175 ? 21.529  -11.801 38.490  1.00 38.02 ? 154 GLY A O     1 
ATOM   1114 N  N     . THR A 1 176 ? 20.538  -13.106 36.949  1.00 35.22 ? 155 THR A N     1 
ATOM   1115 C  CA    . THR A 1 176 ? 19.961  -14.087 37.906  1.00 34.98 ? 155 THR A CA    1 
ATOM   1116 C  C     . THR A 1 176 ? 21.015  -15.121 38.334  1.00 38.27 ? 155 THR A C     1 
ATOM   1117 O  O     . THR A 1 176 ? 20.724  -15.854 39.278  1.00 38.84 ? 155 THR A O     1 
ATOM   1118 C  CB    . THR A 1 176 ? 18.734  -14.827 37.355  1.00 31.09 ? 155 THR A CB    1 
ATOM   1119 O  OG1   . THR A 1 176 ? 19.107  -15.768 36.349  1.00 30.49 ? 155 THR A OG1   1 
ATOM   1120 C  CG2   . THR A 1 176 ? 17.709  -13.863 36.805  1.00 30.63 ? 155 THR A CG2   1 
ATOM   1121 N  N     . GLY A 1 177 ? 22.120  -15.248 37.604  1.00 36.96 ? 156 GLY A N     1 
ATOM   1122 C  CA    . GLY A 1 177 ? 23.200  -16.203 37.918  1.00 39.94 ? 156 GLY A CA    1 
ATOM   1123 C  C     . GLY A 1 177 ? 22.822  -17.658 37.685  1.00 41.24 ? 156 GLY A C     1 
ATOM   1124 O  O     . GLY A 1 177 ? 23.544  -18.516 38.196  1.00 39.67 ? 156 GLY A O     1 
ATOM   1125 N  N     . VAL A 1 178 ? 21.775  -17.965 36.910  1.00 35.36 ? 157 VAL A N     1 
ATOM   1126 C  CA    . VAL A 1 178 ? 21.468  -19.375 36.548  1.00 32.64 ? 157 VAL A CA    1 
ATOM   1127 C  C     . VAL A 1 178 ? 22.616  -19.968 35.737  1.00 35.10 ? 157 VAL A C     1 
ATOM   1128 O  O     . VAL A 1 178 ? 23.299  -19.252 35.001  1.00 35.28 ? 157 VAL A O     1 
ATOM   1129 C  CB    . VAL A 1 178 ? 20.145  -19.549 35.774  1.00 33.15 ? 157 VAL A CB    1 
ATOM   1130 C  CG1   . VAL A 1 178 ? 18.946  -19.197 36.658  1.00 29.88 ? 157 VAL A CG1   1 
ATOM   1131 C  CG2   . VAL A 1 178 ? 20.153  -18.776 34.444  1.00 30.95 ? 157 VAL A CG2   1 
ATOM   1132 N  N     . PRO A 1 179 ? 22.785  -21.306 35.807  1.00 35.93 ? 158 PRO A N     1 
ATOM   1133 C  CA    . PRO A 1 179 ? 23.825  -22.001 35.046  1.00 42.95 ? 158 PRO A CA    1 
ATOM   1134 C  C     . PRO A 1 179 ? 23.564  -21.993 33.532  1.00 44.05 ? 158 PRO A C     1 
ATOM   1135 O  O     . PRO A 1 179 ? 22.408  -21.885 33.120  1.00 37.87 ? 158 PRO A O     1 
ATOM   1136 C  CB    . PRO A 1 179 ? 23.792  -23.465 35.527  1.00 43.14 ? 158 PRO A CB    1 
ATOM   1137 C  CG    . PRO A 1 179 ? 22.690  -23.559 36.582  1.00 42.15 ? 158 PRO A CG    1 
ATOM   1138 C  CD    . PRO A 1 179 ? 21.971  -22.228 36.613  1.00 37.86 ? 158 PRO A CD    1 
ATOM   1139 N  N     . ASP A 1 180 ? 24.642  -22.146 32.758  1.00 41.99 ? 159 ASP A N     1 
ATOM   1140 C  CA    . ASP A 1 180 ? 24.655  -22.228 31.276  1.00 42.57 ? 159 ASP A CA    1 
ATOM   1141 C  C     . ASP A 1 180 ? 23.473  -23.053 30.770  1.00 37.87 ? 159 ASP A C     1 
ATOM   1142 O  O     . ASP A 1 180 ? 22.787  -22.590 29.859  1.00 36.10 ? 159 ASP A O     1 
ATOM   1143 C  CB    . ASP A 1 180 ? 25.950  -22.873 30.758  1.00 46.71 ? 159 ASP A CB    1 
ATOM   1144 C  CG    . ASP A 1 180 ? 25.911  -23.261 29.283  1.00 50.03 ? 159 ASP A CG    1 
ATOM   1145 O  OD1   . ASP A 1 180 ? 26.075  -22.360 28.453  1.00 46.58 ? 159 ASP A OD1   1 
ATOM   1146 O  OD2   . ASP A 1 180 ? 25.700  -24.480 28.976  1.00 54.97 ? 159 ASP A OD2   1 
ATOM   1147 N  N     . ARG A 1 181 ? 23.277  -24.268 31.262  1.00 35.42 ? 160 ARG A N     1 
ATOM   1148 C  CA    . ARG A 1 181 ? 22.281  -25.170 30.643  1.00 38.38 ? 160 ARG A CA    1 
ATOM   1149 C  C     . ARG A 1 181 ? 20.865  -24.643 30.912  1.00 35.91 ? 160 ARG A C     1 
ATOM   1150 O  O     . ARG A 1 181 ? 19.988  -24.824 30.040  1.00 31.88 ? 160 ARG A O     1 
ATOM   1151 C  CB    . ARG A 1 181 ? 22.429  -26.596 31.164  1.00 42.14 ? 160 ARG A CB    1 
ATOM   1152 C  CG    . ARG A 1 181 ? 22.032  -27.666 30.154  1.00 48.03 ? 160 ARG A CG    1 
ATOM   1153 C  CD    . ARG A 1 181 ? 23.210  -28.610 29.906  1.00 54.56 ? 160 ARG A CD    1 
ATOM   1154 N  NE    . ARG A 1 181 ? 22.920  -30.037 29.812  1.00 58.78 ? 160 ARG A NE    1 
ATOM   1155 C  CZ    . ARG A 1 181 ? 22.315  -30.784 30.745  1.00 67.37 ? 160 ARG A CZ    1 
ATOM   1156 N  NH1   . ARG A 1 181 ? 21.870  -30.256 31.872  1.00 70.44 ? 160 ARG A NH1   1 
ATOM   1157 N  NH2   . ARG A 1 181 ? 22.129  -32.077 30.540  1.00 72.70 ? 160 ARG A NH2   1 
ATOM   1158 N  N     . VAL A 1 182 ? 20.645  -24.025 32.074  1.00 33.15 ? 161 VAL A N     1 
ATOM   1159 C  CA    . VAL A 1 182 ? 19.325  -23.444 32.435  1.00 32.31 ? 161 VAL A CA    1 
ATOM   1160 C  C     . VAL A 1 182 ? 19.081  -22.245 31.506  1.00 31.45 ? 161 VAL A C     1 
ATOM   1161 O  O     . VAL A 1 182 ? 17.978  -22.164 30.940  1.00 28.08 ? 161 VAL A O     1 
ATOM   1162 C  CB    . VAL A 1 182 ? 19.251  -23.091 33.935  1.00 33.83 ? 161 VAL A CB    1 
ATOM   1163 C  CG1   . VAL A 1 182 ? 17.995  -22.288 34.297  1.00 33.92 ? 161 VAL A CG1   1 
ATOM   1164 C  CG2   . VAL A 1 182 ? 19.324  -24.358 34.778  1.00 35.72 ? 161 VAL A CG2   1 
ATOM   1165 N  N     . ALA A 1 183 ? 20.059  -21.352 31.338  1.00 29.52 ? 162 ALA A N     1 
ATOM   1166 C  CA    . ALA A 1 183 ? 19.944  -20.215 30.383  1.00 31.58 ? 162 ALA A CA    1 
ATOM   1167 C  C     . ALA A 1 183 ? 19.620  -20.739 28.964  1.00 30.32 ? 162 ALA A C     1 
ATOM   1168 O  O     . ALA A 1 183 ? 18.739  -20.149 28.294  1.00 28.90 ? 162 ALA A O     1 
ATOM   1169 C  CB    . ALA A 1 183 ? 21.181  -19.369 30.416  1.00 32.25 ? 162 ALA A CB    1 
ATOM   1170 N  N     . GLY A 1 184 ? 20.289  -21.796 28.498  1.00 28.21 ? 163 GLY A N     1 
ATOM   1171 C  CA    . GLY A 1 184 ? 20.058  -22.389 27.162  1.00 28.61 ? 163 GLY A CA    1 
ATOM   1172 C  C     . GLY A 1 184 ? 18.655  -22.963 27.011  1.00 30.24 ? 163 GLY A C     1 
ATOM   1173 O  O     . GLY A 1 184 ? 18.047  -22.826 25.915  1.00 27.19 ? 163 GLY A O     1 
ATOM   1174 N  N     . LEU A 1 185 ? 18.160  -23.636 28.048  1.00 25.81 ? 164 LEU A N     1 
ATOM   1175 C  CA    . LEU A 1 185 ? 16.815  -24.256 28.043  1.00 28.83 ? 164 LEU A CA    1 
ATOM   1176 C  C     . LEU A 1 185 ? 15.774  -23.131 27.998  1.00 23.15 ? 164 LEU A C     1 
ATOM   1177 O  O     . LEU A 1 185 ? 14.838  -23.179 27.154  1.00 23.39 ? 164 LEU A O     1 
ATOM   1178 C  CB    . LEU A 1 185 ? 16.658  -25.095 29.313  1.00 31.16 ? 164 LEU A CB    1 
ATOM   1179 C  CG    . LEU A 1 185 ? 15.264  -25.665 29.580  1.00 36.24 ? 164 LEU A CG    1 
ATOM   1180 C  CD1   . LEU A 1 185 ? 14.801  -26.561 28.420  1.00 37.63 ? 164 LEU A CD1   1 
ATOM   1181 C  CD2   . LEU A 1 185 ? 15.248  -26.410 30.913  1.00 36.69 ? 164 LEU A CD2   1 
ATOM   1182 N  N     . PHE A 1 186 ? 15.941  -22.144 28.868  1.00 24.55 ? 165 PHE A N     1 
ATOM   1183 C  CA    . PHE A 1 186 ? 15.054  -20.956 28.896  1.00 23.68 ? 165 PHE A CA    1 
ATOM   1184 C  C     . PHE A 1 186 ? 15.045  -20.311 27.501  1.00 21.88 ? 165 PHE A C     1 
ATOM   1185 O  O     . PHE A 1 186 ? 13.968  -19.916 27.047  1.00 23.68 ? 165 PHE A O     1 
ATOM   1186 C  CB    . PHE A 1 186 ? 15.506  -19.975 29.969  1.00 23.57 ? 165 PHE A CB    1 
ATOM   1187 C  CG    . PHE A 1 186 ? 14.542  -18.858 30.228  1.00 22.91 ? 165 PHE A CG    1 
ATOM   1188 C  CD1   . PHE A 1 186 ? 14.827  -17.568 29.798  1.00 24.05 ? 165 PHE A CD1   1 
ATOM   1189 C  CD2   . PHE A 1 186 ? 13.342  -19.121 30.865  1.00 24.98 ? 165 PHE A CD2   1 
ATOM   1190 C  CE1   . PHE A 1 186 ? 13.949  -16.535 30.060  1.00 26.03 ? 165 PHE A CE1   1 
ATOM   1191 C  CE2   . PHE A 1 186 ? 12.457  -18.087 31.112  1.00 26.42 ? 165 PHE A CE2   1 
ATOM   1192 C  CZ    . PHE A 1 186 ? 12.756  -16.811 30.696  1.00 26.94 ? 165 PHE A CZ    1 
ATOM   1193 N  N     . GLU A 1 187 ? 16.214  -20.152 26.875  1.00 22.52 ? 166 GLU A N     1 
ATOM   1194 C  CA    . GLU A 1 187 ? 16.355  -19.502 25.540  1.00 21.56 ? 166 GLU A CA    1 
ATOM   1195 C  C     . GLU A 1 187 ? 15.543  -20.282 24.498  1.00 20.75 ? 166 GLU A C     1 
ATOM   1196 O  O     . GLU A 1 187 ? 14.873  -19.609 23.693  1.00 21.93 ? 166 GLU A O     1 
ATOM   1197 C  CB    . GLU A 1 187 ? 17.821  -19.391 25.125  1.00 21.22 ? 166 GLU A CB    1 
ATOM   1198 C  CG    . GLU A 1 187 ? 18.026  -18.505 23.902  1.00 21.74 ? 166 GLU A CG    1 
ATOM   1199 C  CD    . GLU A 1 187 ? 17.683  -17.044 24.165  1.00 22.24 ? 166 GLU A CD    1 
ATOM   1200 O  OE1   . GLU A 1 187 ? 17.454  -16.285 23.184  1.00 21.64 ? 166 GLU A OE1   1 
ATOM   1201 O  OE2   . GLU A 1 187 ? 17.649  -16.643 25.352  1.00 21.98 ? 166 GLU A OE2   1 
ATOM   1202 N  N     . VAL A 1 188 ? 15.542  -21.635 24.517  1.00 21.29 ? 167 VAL A N     1 
ATOM   1203 C  CA    . VAL A 1 188 ? 14.676  -22.461 23.617  1.00 22.47 ? 167 VAL A CA    1 
ATOM   1204 C  C     . VAL A 1 188 ? 13.213  -22.041 23.804  1.00 21.02 ? 167 VAL A C     1 
ATOM   1205 O  O     . VAL A 1 188 ? 12.533  -21.799 22.786  1.00 22.48 ? 167 VAL A O     1 
ATOM   1206 C  CB    . VAL A 1 188 ? 14.797  -23.991 23.808  1.00 28.06 ? 167 VAL A CB    1 
ATOM   1207 C  CG1   . VAL A 1 188 ? 13.789  -24.714 22.934  1.00 31.64 ? 167 VAL A CG1   1 
ATOM   1208 C  CG2   . VAL A 1 188 ? 16.181  -24.497 23.490  1.00 29.27 ? 167 VAL A CG2   1 
ATOM   1209 N  N     . ALA A 1 189 ? 12.754  -21.954 25.054  1.00 19.72 ? 168 ALA A N     1 
ATOM   1210 C  CA    . ALA A 1 189 ? 11.382  -21.526 25.419  1.00 20.42 ? 168 ALA A CA    1 
ATOM   1211 C  C     . ALA A 1 189 ? 11.119  -20.100 24.944  1.00 19.41 ? 168 ALA A C     1 
ATOM   1212 O  O     . ALA A 1 189 ? 10.059  -19.870 24.290  1.00 18.04 ? 168 ALA A O     1 
ATOM   1213 C  CB    . ALA A 1 189 ? 11.174  -21.634 26.904  1.00 21.01 ? 168 ALA A CB    1 
ATOM   1214 N  N     . VAL A 1 190 ? 12.027  -19.165 25.249  1.00 19.83 ? 169 VAL A N     1 
ATOM   1215 C  CA    . VAL A 1 190 ? 11.884  -17.769 24.734  1.00 20.05 ? 169 VAL A CA    1 
ATOM   1216 C  C     . VAL A 1 190 ? 11.697  -17.787 23.207  1.00 18.83 ? 169 VAL A C     1 
ATOM   1217 O  O     . VAL A 1 190 ? 10.763  -17.145 22.693  1.00 16.30 ? 169 VAL A O     1 
ATOM   1218 C  CB    . VAL A 1 190 ? 13.031  -16.839 25.180  1.00 21.44 ? 169 VAL A CB    1 
ATOM   1219 C  CG1   . VAL A 1 190 ? 12.910  -15.468 24.531  1.00 19.35 ? 169 VAL A CG1   1 
ATOM   1220 C  CG2   . VAL A 1 190 ? 13.088  -16.665 26.695  1.00 23.65 ? 169 VAL A CG2   1 
ATOM   1221 N  N     . GLN A 1 191 ? 12.543  -18.469 22.452  1.00 17.31 ? 170 GLN A N     1 
ATOM   1222 C  CA    . GLN A 1 191 ? 12.453  -18.432 20.974  1.00 20.50 ? 170 GLN A CA    1 
ATOM   1223 C  C     . GLN A 1 191 ? 11.159  -19.092 20.481  1.00 18.90 ? 170 GLN A C     1 
ATOM   1224 O  O     . GLN A 1 191 ? 10.541  -18.548 19.560  1.00 17.22 ? 170 GLN A O     1 
ATOM   1225 C  CB    . GLN A 1 191 ? 13.750  -18.992 20.396  1.00 19.25 ? 170 GLN A CB    1 
ATOM   1226 C  CG    . GLN A 1 191 ? 14.897  -18.053 20.682  1.00 20.81 ? 170 GLN A CG    1 
ATOM   1227 C  CD    . GLN A 1 191 ? 16.169  -18.368 19.936  1.00 27.03 ? 170 GLN A CD    1 
ATOM   1228 O  OE1   . GLN A 1 191 ? 16.167  -19.137 18.984  1.00 32.04 ? 170 GLN A OE1   1 
ATOM   1229 N  NE2   . GLN A 1 191 ? 17.246  -17.734 20.376  1.00 26.31 ? 170 GLN A NE2   1 
ATOM   1230 N  N     . ALA A 1 192 ? 10.719  -20.178 21.112  1.00 20.01 ? 171 ALA A N     1 
ATOM   1231 C  CA    . ALA A 1 192 ? 9.470   -20.898 20.760  1.00 19.16 ? 171 ALA A CA    1 
ATOM   1232 C  C     . ALA A 1 192 ? 8.246   -20.007 20.995  1.00 20.17 ? 171 ALA A C     1 
ATOM   1233 O  O     . ALA A 1 192 ? 7.274   -20.125 20.221  1.00 20.57 ? 171 ALA A O     1 
ATOM   1234 C  CB    . ALA A 1 192 ? 9.354   -22.149 21.611  1.00 20.81 ? 171 ALA A CB    1 
ATOM   1235 N  N     . VAL A 1 193 ? 8.264   -19.160 22.026  1.00 18.21 ? 172 VAL A N     1 
ATOM   1236 C  CA    . VAL A 1 193 ? 7.116   -18.272 22.392  1.00 18.28 ? 172 VAL A CA    1 
ATOM   1237 C  C     . VAL A 1 193 ? 7.132   -16.969 21.569  1.00 17.57 ? 172 VAL A C     1 
ATOM   1238 O  O     . VAL A 1 193 ? 6.019   -16.517 21.144  1.00 19.51 ? 172 VAL A O     1 
ATOM   1239 C  CB    . VAL A 1 193 ? 7.130   -17.983 23.898  1.00 20.21 ? 172 VAL A CB    1 
ATOM   1240 C  CG1   . VAL A 1 193 ? 6.146   -16.893 24.257  1.00 19.92 ? 172 VAL A CG1   1 
ATOM   1241 C  CG2   . VAL A 1 193 ? 6.850   -19.253 24.707  1.00 19.79 ? 172 VAL A CG2   1 
ATOM   1242 N  N     . PHE A 1 194 ? 8.284   -16.311 21.451  1.00 17.97 ? 173 PHE A N     1 
ATOM   1243 C  CA    . PHE A 1 194 ? 8.396   -14.925 20.916  1.00 17.92 ? 173 PHE A CA    1 
ATOM   1244 C  C     . PHE A 1 194 ? 8.875   -14.895 19.464  1.00 18.17 ? 173 PHE A C     1 
ATOM   1245 O  O     . PHE A 1 194 ? 8.760   -13.853 18.843  1.00 17.04 ? 173 PHE A O     1 
ATOM   1246 C  CB    . PHE A 1 194 ? 9.321   -14.080 21.795  1.00 19.38 ? 173 PHE A CB    1 
ATOM   1247 C  CG    . PHE A 1 194 ? 8.776   -13.767 23.177  1.00 17.93 ? 173 PHE A CG    1 
ATOM   1248 C  CD1   . PHE A 1 194 ? 7.848   -12.759 23.368  1.00 18.89 ? 173 PHE A CD1   1 
ATOM   1249 C  CD2   . PHE A 1 194 ? 9.145   -14.538 24.280  1.00 17.47 ? 173 PHE A CD2   1 
ATOM   1250 C  CE1   . PHE A 1 194 ? 7.343   -12.486 24.635  1.00 17.69 ? 173 PHE A CE1   1 
ATOM   1251 C  CE2   . PHE A 1 194 ? 8.642   -14.271 25.539  1.00 19.32 ? 173 PHE A CE2   1 
ATOM   1252 C  CZ    . PHE A 1 194 ? 7.720   -13.258 25.711  1.00 18.11 ? 173 PHE A CZ    1 
ATOM   1253 N  N     . ALA A 1 195 ? 9.417   -15.995 18.920  1.00 18.46 ? 174 ALA A N     1 
ATOM   1254 C  CA    . ALA A 1 195 ? 9.985   -15.982 17.547  1.00 19.39 ? 174 ALA A CA    1 
ATOM   1255 C  C     . ALA A 1 195 ? 11.061  -14.888 17.466  1.00 17.47 ? 174 ALA A C     1 
ATOM   1256 O  O     . ALA A 1 195 ? 11.199  -14.192 16.431  1.00 17.10 ? 174 ALA A O     1 
ATOM   1257 C  CB    . ALA A 1 195 ? 8.882   -15.826 16.509  1.00 19.49 ? 174 ALA A CB    1 
ATOM   1258 N  N     . ALA A 1 196 ? 11.870  -14.766 18.525  1.00 17.36 ? 175 ALA A N     1 
ATOM   1259 C  CA    . ALA A 1 196 ? 12.890  -13.715 18.694  1.00 16.85 ? 175 ALA A CA    1 
ATOM   1260 C  C     . ALA A 1 196 ? 13.785  -14.157 19.852  1.00 19.50 ? 175 ALA A C     1 
ATOM   1261 O  O     . ALA A 1 196 ? 13.275  -14.964 20.718  1.00 18.31 ? 175 ALA A O     1 
ATOM   1262 C  CB    . ALA A 1 196 ? 12.215  -12.402 18.976  1.00 17.93 ? 175 ALA A CB    1 
ATOM   1263 N  N     . THR A 1 197 ? 15.024  -13.679 19.900  1.00 18.87 ? 176 THR A N     1 
ATOM   1264 C  CA    . THR A 1 197 ? 15.957  -14.069 20.992  1.00 19.98 ? 176 THR A CA    1 
ATOM   1265 C  C     . THR A 1 197 ? 15.678  -13.199 22.231  1.00 17.71 ? 176 THR A C     1 
ATOM   1266 O  O     . THR A 1 197 ? 15.039  -12.129 22.125  1.00 17.94 ? 176 THR A O     1 
ATOM   1267 C  CB    . THR A 1 197 ? 17.435  -13.999 20.581  1.00 19.14 ? 176 THR A CB    1 
ATOM   1268 O  OG1   . THR A 1 197 ? 17.851  -12.649 20.711  1.00 19.27 ? 176 THR A OG1   1 
ATOM   1269 C  CG2   . THR A 1 197 ? 17.729  -14.506 19.188  1.00 19.60 ? 176 THR A CG2   1 
ATOM   1270 N  N     . SER A 1 198 ? 16.174  -13.613 23.385  1.00 17.99 ? 177 SER A N     1 
ATOM   1271 C  CA    . SER A 1 198 ? 16.053  -12.823 24.636  1.00 18.90 ? 177 SER A CA    1 
ATOM   1272 C  C     . SER A 1 198 ? 16.761  -11.470 24.485  1.00 18.07 ? 177 SER A C     1 
ATOM   1273 O  O     . SER A 1 198 ? 16.444  -10.550 25.284  1.00 18.02 ? 177 SER A O     1 
ATOM   1274 C  CB    . SER A 1 198 ? 16.535  -13.606 25.855  1.00 17.82 ? 177 SER A CB    1 
ATOM   1275 O  OG    . SER A 1 198 ? 17.839  -14.088 25.635  1.00 17.25 ? 177 SER A OG    1 
ATOM   1276 N  N     . ALA A 1 199 ? 17.694  -11.314 23.538  1.00 17.64 ? 178 ALA A N     1 
ATOM   1277 C  CA    . ALA A 1 199 ? 18.444  -10.047 23.367  1.00 17.82 ? 178 ALA A CA    1 
ATOM   1278 C  C     . ALA A 1 199 ? 17.575  -9.014  22.660  1.00 18.15 ? 178 ALA A C     1 
ATOM   1279 O  O     . ALA A 1 199 ? 17.834  -7.834  22.813  1.00 20.76 ? 178 ALA A O     1 
ATOM   1280 C  CB    . ALA A 1 199 ? 19.728  -10.297 22.593  1.00 21.19 ? 178 ALA A CB    1 
ATOM   1281 N  N     . GLN A 1 200 ? 16.582  -9.443  21.884  1.00 17.90 ? 179 GLN A N     1 
ATOM   1282 C  CA    . GLN A 1 200 ? 15.790  -8.547  20.990  1.00 18.86 ? 179 GLN A CA    1 
ATOM   1283 C  C     . GLN A 1 200 ? 14.680  -7.875  21.805  1.00 19.01 ? 179 GLN A C     1 
ATOM   1284 O  O     . GLN A 1 200 ? 14.119  -6.854  21.348  1.00 20.08 ? 179 GLN A O     1 
ATOM   1285 C  CB    . GLN A 1 200 ? 15.169  -9.379  19.861  1.00 19.58 ? 179 GLN A CB    1 
ATOM   1286 C  CG    . GLN A 1 200 ? 16.191  -9.894  18.844  1.00 20.59 ? 179 GLN A CG    1 
ATOM   1287 C  CD    . GLN A 1 200 ? 15.489  -10.681 17.752  1.00 22.76 ? 179 GLN A CD    1 
ATOM   1288 O  OE1   . GLN A 1 200 ? 15.455  -11.902 17.763  1.00 25.09 ? 179 GLN A OE1   1 
ATOM   1289 N  NE2   . GLN A 1 200 ? 14.918  -9.961  16.802  1.00 24.23 ? 179 GLN A NE2   1 
ATOM   1290 N  N     . LEU A 1 201 ? 14.265  -8.544  22.875  1.00 18.00 ? 180 LEU A N     1 
ATOM   1291 C  CA    . LEU A 1 201 ? 13.041  -8.194  23.661  1.00 19.15 ? 180 LEU A CA    1 
ATOM   1292 C  C     . LEU A 1 201 ? 13.412  -7.328  24.840  1.00 17.63 ? 180 LEU A C     1 
ATOM   1293 O  O     . LEU A 1 201 ? 14.342  -7.729  25.581  1.00 18.48 ? 180 LEU A O     1 
ATOM   1294 C  CB    . LEU A 1 201 ? 12.397  -9.484  24.221  1.00 22.22 ? 180 LEU A CB    1 
ATOM   1295 C  CG    . LEU A 1 201 ? 12.146  -10.606 23.232  1.00 22.87 ? 180 LEU A CG    1 
ATOM   1296 C  CD1   . LEU A 1 201 ? 11.731  -11.880 23.955  1.00 27.42 ? 180 LEU A CD1   1 
ATOM   1297 C  CD2   . LEU A 1 201 ? 11.079  -10.229 22.247  1.00 26.37 ? 180 LEU A CD2   1 
ATOM   1298 N  N     . SER A 1 202 ? 12.618  -6.308  25.158  1.00 17.75 ? 181 SER A N     1 
ATOM   1299 C  CA    . SER A 1 202 ? 12.728  -5.672  26.495  1.00 18.58 ? 181 SER A CA    1 
ATOM   1300 C  C     . SER A 1 202 ? 12.169  -6.627  27.554  1.00 19.15 ? 181 SER A C     1 
ATOM   1301 O  O     . SER A 1 202 ? 11.295  -7.464  27.249  1.00 17.42 ? 181 SER A O     1 
ATOM   1302 C  CB    . SER A 1 202 ? 12.097  -4.309  26.596  1.00 20.81 ? 181 SER A CB    1 
ATOM   1303 O  OG    . SER A 1 202 ? 10.698  -4.376  26.703  1.00 23.40 ? 181 SER A OG    1 
ATOM   1304 N  N     . LEU A 1 203 ? 12.669  -6.507  28.772  1.00 18.31 ? 182 LEU A N     1 
ATOM   1305 C  CA    . LEU A 1 203 ? 12.144  -7.280  29.905  1.00 19.77 ? 182 LEU A CA    1 
ATOM   1306 C  C     . LEU A 1 203 ? 10.690  -6.834  30.108  1.00 19.80 ? 182 LEU A C     1 
ATOM   1307 O  O     . LEU A 1 203 ? 9.865   -7.700  30.399  1.00 19.05 ? 182 LEU A O     1 
ATOM   1308 C  CB    . LEU A 1 203 ? 12.986  -6.982  31.148  1.00 20.83 ? 182 LEU A CB    1 
ATOM   1309 C  CG    . LEU A 1 203 ? 12.411  -7.509  32.450  1.00 21.82 ? 182 LEU A CG    1 
ATOM   1310 C  CD1   . LEU A 1 203 ? 12.339  -9.037  32.447  1.00 21.79 ? 182 LEU A CD1   1 
ATOM   1311 C  CD2   . LEU A 1 203 ? 13.232  -6.980  33.622  1.00 23.01 ? 182 LEU A CD2   1 
ATOM   1312 N  N     . LEU A 1 204 ? 10.376  -5.535  29.962  1.00 18.29 ? 183 LEU A N     1 
ATOM   1313 C  CA    . LEU A 1 204 ? 8.982   -5.044  30.135  1.00 17.42 ? 183 LEU A CA    1 
ATOM   1314 C  C     . LEU A 1 204 ? 8.062   -5.754  29.120  1.00 17.27 ? 183 LEU A C     1 
ATOM   1315 O  O     . LEU A 1 204 ? 6.956   -6.212  29.512  1.00 16.35 ? 183 LEU A O     1 
ATOM   1316 C  CB    . LEU A 1 204 ? 8.918   -3.524  29.987  1.00 18.56 ? 183 LEU A CB    1 
ATOM   1317 C  CG    . LEU A 1 204 ? 7.554   -2.898  30.233  1.00 18.78 ? 183 LEU A CG    1 
ATOM   1318 C  CD1   . LEU A 1 204 ? 6.972   -3.253  31.609  1.00 19.92 ? 183 LEU A CD1   1 
ATOM   1319 C  CD2   . LEU A 1 204 ? 7.627   -1.392  30.102  1.00 17.73 ? 183 LEU A CD2   1 
ATOM   1320 N  N     . HIS A 1 205 ? 8.518   -5.918  27.870  1.00 17.19 ? 184 HIS A N     1 
ATOM   1321 C  CA    . HIS A 1 205 ? 7.688   -6.588  26.826  1.00 17.62 ? 184 HIS A CA    1 
ATOM   1322 C  C     . HIS A 1 205 ? 7.427   -8.034  27.251  1.00 16.81 ? 184 HIS A C     1 
ATOM   1323 O  O     . HIS A 1 205 ? 6.277   -8.488  27.217  1.00 18.58 ? 184 HIS A O     1 
ATOM   1324 C  CB    . HIS A 1 205 ? 8.395   -6.569  25.468  1.00 16.51 ? 184 HIS A CB    1 
ATOM   1325 C  CG    . HIS A 1 205 ? 7.604   -7.326  24.469  1.00 16.56 ? 184 HIS A CG    1 
ATOM   1326 N  ND1   . HIS A 1 205 ? 6.435   -6.803  23.974  1.00 17.08 ? 184 HIS A ND1   1 
ATOM   1327 C  CD2   . HIS A 1 205 ? 7.775   -8.540  23.903  1.00 17.01 ? 184 HIS A CD2   1 
ATOM   1328 C  CE1   . HIS A 1 205 ? 5.918   -7.681  23.114  1.00 16.47 ? 184 HIS A CE1   1 
ATOM   1329 N  NE2   . HIS A 1 205 ? 6.716   -8.744  23.063  1.00 16.41 ? 184 HIS A NE2   1 
ATOM   1330 N  N     . ALA A 1 206 ? 8.470   -8.770  27.607  1.00 17.13 ? 185 ALA A N     1 
ATOM   1331 C  CA    . ALA A 1 206 ? 8.374   -10.201 27.957  1.00 16.54 ? 185 ALA A CA    1 
ATOM   1332 C  C     . ALA A 1 206 ? 7.456   -10.350 29.166  1.00 16.33 ? 185 ALA A C     1 
ATOM   1333 O  O     . ALA A 1 206 ? 6.598   -11.208 29.111  1.00 16.80 ? 185 ALA A O     1 
ATOM   1334 C  CB    . ALA A 1 206 ? 9.732   -10.787 28.218  1.00 17.27 ? 185 ALA A CB    1 
ATOM   1335 N  N     . ALA A 1 207 ? 7.637   -9.534  30.211  1.00 16.94 ? 186 ALA A N     1 
ATOM   1336 C  CA    . ALA A 1 207 ? 6.793   -9.535  31.434  1.00 16.69 ? 186 ALA A CA    1 
ATOM   1337 C  C     . ALA A 1 207 ? 5.331   -9.265  31.111  1.00 15.17 ? 186 ALA A C     1 
ATOM   1338 O  O     . ALA A 1 207 ? 4.458   -10.007 31.620  1.00 15.40 ? 186 ALA A O     1 
ATOM   1339 C  CB    . ALA A 1 207 ? 7.361   -8.555  32.445  1.00 18.07 ? 186 ALA A CB    1 
ATOM   1340 N  N     . HIS A 1 208 ? 5.017   -8.264  30.284  1.00 15.98 ? 187 HIS A N     1 
ATOM   1341 C  CA    . HIS A 1 208 ? 3.617   -7.991  29.890  1.00 15.90 ? 187 HIS A CA    1 
ATOM   1342 C  C     . HIS A 1 208 ? 3.044   -9.231  29.206  1.00 15.77 ? 187 HIS A C     1 
ATOM   1343 O  O     . HIS A 1 208 ? 1.944   -9.638  29.539  1.00 17.42 ? 187 HIS A O     1 
ATOM   1344 C  CB    . HIS A 1 208 ? 3.539   -6.758  28.995  1.00 17.00 ? 187 HIS A CB    1 
ATOM   1345 C  CG    . HIS A 1 208 ? 2.210   -6.608  28.361  1.00 18.71 ? 187 HIS A CG    1 
ATOM   1346 N  ND1   . HIS A 1 208 ? 1.111   -6.037  29.025  1.00 20.67 ? 187 HIS A ND1   1 
ATOM   1347 C  CD2   . HIS A 1 208 ? 1.761   -7.050  27.166  1.00 19.84 ? 187 HIS A CD2   1 
ATOM   1348 C  CE1   . HIS A 1 208 ? 0.075   -6.082  28.215  1.00 19.68 ? 187 HIS A CE1   1 
ATOM   1349 N  NE2   . HIS A 1 208 ? 0.444   -6.712  27.081  1.00 23.25 ? 187 HIS A NE2   1 
ATOM   1350 N  N     . TYR A 1 209 ? 3.837   -9.868  28.356  1.00 16.98 ? 188 TYR A N     1 
ATOM   1351 C  CA    . TYR A 1 209 ? 3.363   -11.012 27.537  1.00 14.69 ? 188 TYR A CA    1 
ATOM   1352 C  C     . TYR A 1 209 ? 3.014   -12.165 28.470  1.00 15.02 ? 188 TYR A C     1 
ATOM   1353 O  O     . TYR A 1 209 ? 1.978   -12.837 28.253  1.00 17.27 ? 188 TYR A O     1 
ATOM   1354 C  CB    . TYR A 1 209 ? 4.428   -11.418 26.520  1.00 15.71 ? 188 TYR A CB    1 
ATOM   1355 C  CG    . TYR A 1 209 ? 3.931   -12.136 25.290  1.00 16.18 ? 188 TYR A CG    1 
ATOM   1356 C  CD1   . TYR A 1 209 ? 3.983   -13.522 25.178  1.00 17.17 ? 188 TYR A CD1   1 
ATOM   1357 C  CD2   . TYR A 1 209 ? 3.573   -11.421 24.160  1.00 16.48 ? 188 TYR A CD2   1 
ATOM   1358 C  CE1   . TYR A 1 209 ? 3.565   -14.174 24.019  1.00 17.16 ? 188 TYR A CE1   1 
ATOM   1359 C  CE2   . TYR A 1 209 ? 3.225   -12.063 22.976  1.00 17.25 ? 188 TYR A CE2   1 
ATOM   1360 C  CZ    . TYR A 1 209 ? 3.220   -13.434 22.898  1.00 17.54 ? 188 TYR A CZ    1 
ATOM   1361 O  OH    . TYR A 1 209 ? 2.852   -14.074 21.738  1.00 17.28 ? 188 TYR A OH    1 
ATOM   1362 N  N     . VAL A 1 210 ? 3.879   -12.435 29.445  1.00 14.98 ? 189 VAL A N     1 
ATOM   1363 C  CA    . VAL A 1 210 ? 3.673   -13.475 30.498  1.00 16.15 ? 189 VAL A CA    1 
ATOM   1364 C  C     . VAL A 1 210 ? 2.407   -13.183 31.322  1.00 16.84 ? 189 VAL A C     1 
ATOM   1365 O  O     . VAL A 1 210 ? 1.578   -14.108 31.506  1.00 16.99 ? 189 VAL A O     1 
ATOM   1366 C  CB    . VAL A 1 210 ? 4.928   -13.646 31.373  1.00 17.33 ? 189 VAL A CB    1 
ATOM   1367 C  CG1   . VAL A 1 210 ? 4.693   -14.590 32.528  1.00 15.79 ? 189 VAL A CG1   1 
ATOM   1368 C  CG2   . VAL A 1 210 ? 6.120   -14.137 30.544  1.00 19.62 ? 189 VAL A CG2   1 
ATOM   1369 N  N     . HIS A 1 211 ? 2.243   -11.963 31.785  1.00 15.86 ? 190 HIS A N     1 
ATOM   1370 C  CA    . HIS A 1 211 ? 1.021   -11.535 32.491  1.00 17.16 ? 190 HIS A CA    1 
ATOM   1371 C  C     . HIS A 1 211 ? -0.213  -11.746 31.587  1.00 17.36 ? 190 HIS A C     1 
ATOM   1372 O  O     . HIS A 1 211 ? -1.216  -12.316 32.064  1.00 15.08 ? 190 HIS A O     1 
ATOM   1373 C  CB    . HIS A 1 211 ? 1.174   -10.125 32.990  1.00 17.24 ? 190 HIS A CB    1 
ATOM   1374 C  CG    . HIS A 1 211 ? 0.163   -9.789  34.020  1.00 18.01 ? 190 HIS A CG    1 
ATOM   1375 N  ND1   . HIS A 1 211 ? -0.077  -8.501  34.398  1.00 19.65 ? 190 HIS A ND1   1 
ATOM   1376 C  CD2   . HIS A 1 211 ? -0.608  -10.585 34.798  1.00 21.03 ? 190 HIS A CD2   1 
ATOM   1377 C  CE1   . HIS A 1 211 ? -1.025  -8.512  35.340  1.00 21.45 ? 190 HIS A CE1   1 
ATOM   1378 N  NE2   . HIS A 1 211 ? -1.363  -9.779  35.579  1.00 18.63 ? 190 HIS A NE2   1 
ATOM   1379 N  N     . SER A 1 212 ? -0.127  -11.356 30.320  1.00 17.14 ? 191 SER A N     1 
ATOM   1380 C  CA    . SER A 1 212 ? -1.252  -11.432 29.349  1.00 15.75 ? 191 SER A CA    1 
ATOM   1381 C  C     . SER A 1 212 ? -1.734  -12.888 29.197  1.00 16.32 ? 191 SER A C     1 
ATOM   1382 O  O     . SER A 1 212 ? -2.966  -13.126 29.077  1.00 16.52 ? 191 SER A O     1 
ATOM   1383 C  CB    . SER A 1 212 ? -0.820  -10.802 28.037  1.00 16.31 ? 191 SER A CB    1 
ATOM   1384 O  OG    . SER A 1 212 ? -1.899  -10.717 27.125  1.00 16.31 ? 191 SER A OG    1 
ATOM   1385 N  N     . ALA A 1 213 ? -0.822  -13.859 29.235  1.00 15.99 ? 192 ALA A N     1 
ATOM   1386 C  CA    . ALA A 1 213 ? -1.167  -15.286 29.030  1.00 17.92 ? 192 ALA A CA    1 
ATOM   1387 C  C     . ALA A 1 213 ? -1.595  -15.942 30.349  1.00 19.26 ? 192 ALA A C     1 
ATOM   1388 O  O     . ALA A 1 213 ? -2.127  -17.045 30.278  1.00 20.88 ? 192 ALA A O     1 
ATOM   1389 C  CB    . ALA A 1 213 ? -0.005  -16.028 28.426  1.00 16.04 ? 192 ALA A CB    1 
ATOM   1390 N  N     . GLY A 1 214 ? -1.302  -15.326 31.490  1.00 20.78 ? 193 GLY A N     1 
ATOM   1391 C  CA    . GLY A 1 214 ? -1.597  -15.913 32.816  1.00 20.72 ? 193 GLY A CA    1 
ATOM   1392 C  C     . GLY A 1 214 ? -0.458  -16.786 33.298  1.00 21.65 ? 193 GLY A C     1 
ATOM   1393 O  O     . GLY A 1 214 ? -0.696  -17.672 34.132  1.00 22.06 ? 193 GLY A O     1 
ATOM   1394 N  N     . GLY A 1 215 ? 0.768   -16.566 32.840  1.00 18.66 ? 194 GLY A N     1 
ATOM   1395 C  CA    . GLY A 1 215 ? 1.910   -17.233 33.453  1.00 19.52 ? 194 GLY A CA    1 
ATOM   1396 C  C     . GLY A 1 215 ? 2.798   -17.973 32.467  1.00 20.43 ? 194 GLY A C     1 
ATOM   1397 O  O     . GLY A 1 215 ? 2.401   -18.196 31.320  1.00 20.50 ? 194 GLY A O     1 
ATOM   1398 N  N     . TRP A 1 216 ? 3.980   -18.371 32.940  1.00 18.72 ? 195 TRP A N     1 
ATOM   1399 C  CA    . TRP A 1 216 ? 4.999   -19.021 32.090  1.00 20.93 ? 195 TRP A CA    1 
ATOM   1400 C  C     . TRP A 1 216 ? 4.514   -20.425 31.725  1.00 20.24 ? 195 TRP A C     1 
ATOM   1401 O  O     . TRP A 1 216 ? 4.673   -20.820 30.577  1.00 22.46 ? 195 TRP A O     1 
ATOM   1402 C  CB    . TRP A 1 216 ? 6.351   -19.041 32.788  1.00 22.97 ? 195 TRP A CB    1 
ATOM   1403 C  CG    . TRP A 1 216 ? 7.464   -19.464 31.879  1.00 23.16 ? 195 TRP A CG    1 
ATOM   1404 C  CD1   . TRP A 1 216 ? 8.174   -20.619 31.981  1.00 24.90 ? 195 TRP A CD1   1 
ATOM   1405 C  CD2   . TRP A 1 216 ? 8.022   -18.744 30.773  1.00 22.89 ? 195 TRP A CD2   1 
ATOM   1406 N  NE1   . TRP A 1 216 ? 9.125   -20.669 31.016  1.00 23.44 ? 195 TRP A NE1   1 
ATOM   1407 C  CE2   . TRP A 1 216 ? 9.057   -19.542 30.254  1.00 26.56 ? 195 TRP A CE2   1 
ATOM   1408 C  CE3   . TRP A 1 216 ? 7.735   -17.542 30.146  1.00 26.60 ? 195 TRP A CE3   1 
ATOM   1409 C  CZ2   . TRP A 1 216 ? 9.787   -19.172 29.139  1.00 26.49 ? 195 TRP A CZ2   1 
ATOM   1410 C  CZ3   . TRP A 1 216 ? 8.467   -17.161 29.042  1.00 30.94 ? 195 TRP A CZ3   1 
ATOM   1411 C  CH2   . TRP A 1 216 ? 9.473   -17.984 28.535  1.00 30.39 ? 195 TRP A CH2   1 
ATOM   1412 N  N     . SER A 1 217 ? 3.929   -21.171 32.669  1.00 20.42 ? 196 SER A N     1 
ATOM   1413 C  CA    . SER A 1 217 ? 3.301   -22.485 32.383  1.00 23.05 ? 196 SER A CA    1 
ATOM   1414 C  C     . SER A 1 217 ? 2.241   -22.385 31.289  1.00 20.37 ? 196 SER A C     1 
ATOM   1415 O  O     . SER A 1 217 ? 2.170   -23.275 30.415  1.00 20.49 ? 196 SER A O     1 
ATOM   1416 C  CB    . SER A 1 217 ? 2.709   -23.036 33.645  1.00 25.71 ? 196 SER A CB    1 
ATOM   1417 O  OG    . SER A 1 217 ? 3.782   -23.465 34.460  1.00 32.04 ? 196 SER A OG    1 
ATOM   1418 N  N     . LYS A 1 218 ? 1.414   -21.360 31.335  1.00 19.06 ? 197 LYS A N     1 
ATOM   1419 C  CA    . LYS A 1 218 ? 0.345   -21.161 30.313  1.00 20.26 ? 197 LYS A CA    1 
ATOM   1420 C  C     . LYS A 1 218 ? 0.990   -21.027 28.925  1.00 19.26 ? 197 LYS A C     1 
ATOM   1421 O  O     . LYS A 1 218 ? 0.419   -21.587 27.936  1.00 17.28 ? 197 LYS A O     1 
ATOM   1422 C  CB    . LYS A 1 218 ? -0.580  -20.027 30.747  1.00 22.72 ? 197 LYS A CB    1 
ATOM   1423 C  CG    . LYS A 1 218 ? -1.648  -20.477 31.754  1.00 24.03 ? 197 LYS A CG    1 
ATOM   1424 C  CD    . LYS A 1 218 ? -2.726  -21.347 31.061  1.00 25.83 ? 197 LYS A CD    1 
ATOM   1425 C  CE    . LYS A 1 218 ? -3.953  -21.660 31.887  1.00 28.86 ? 197 LYS A CE    1 
ATOM   1426 N  NZ    . LYS A 1 218 ? -4.575  -20.417 32.400  1.00 33.63 ? 197 LYS A NZ    1 
ATOM   1427 N  N     . LEU A 1 219 ? 2.154   -20.399 28.833  1.00 17.41 ? 198 LEU A N     1 
ATOM   1428 C  CA    . LEU A 1 219 ? 2.839   -20.216 27.522  1.00 17.96 ? 198 LEU A CA    1 
ATOM   1429 C  C     . LEU A 1 219 ? 3.510   -21.510 27.083  1.00 18.98 ? 198 LEU A C     1 
ATOM   1430 O  O     . LEU A 1 219 ? 3.514   -21.778 25.882  1.00 20.51 ? 198 LEU A O     1 
ATOM   1431 C  CB    . LEU A 1 219 ? 3.878   -19.099 27.615  1.00 17.75 ? 198 LEU A CB    1 
ATOM   1432 C  CG    . LEU A 1 219 ? 3.282   -17.706 27.758  1.00 16.98 ? 198 LEU A CG    1 
ATOM   1433 C  CD1   . LEU A 1 219 ? 4.352   -16.703 28.163  1.00 18.02 ? 198 LEU A CD1   1 
ATOM   1434 C  CD2   . LEU A 1 219 ? 2.612   -17.292 26.445  1.00 18.16 ? 198 LEU A CD2   1 
ATOM   1435 N  N     . THR A 1 220 ? 4.120   -22.273 27.996  1.00 20.52 ? 199 THR A N     1 
ATOM   1436 C  CA    . THR A 1 220 ? 5.094   -23.319 27.576  1.00 21.76 ? 199 THR A CA    1 
ATOM   1437 C  C     . THR A 1 220 ? 4.522   -24.735 27.693  1.00 22.57 ? 199 THR A C     1 
ATOM   1438 O  O     . THR A 1 220 ? 5.130   -25.610 27.045  1.00 22.73 ? 199 THR A O     1 
ATOM   1439 C  CB    . THR A 1 220 ? 6.407   -23.240 28.372  1.00 23.84 ? 199 THR A CB    1 
ATOM   1440 O  OG1   . THR A 1 220 ? 6.065   -23.409 29.743  1.00 23.23 ? 199 THR A OG1   1 
ATOM   1441 C  CG2   . THR A 1 220 ? 7.143   -21.931 28.149  1.00 20.89 ? 199 THR A CG2   1 
ATOM   1442 N  N     . ASP A 1 221 ? 3.456   -24.961 28.475  1.00 22.60 ? 200 ASP A N     1 
ATOM   1443 C  CA    . ASP A 1 221 ? 2.915   -26.326 28.696  1.00 22.81 ? 200 ASP A CA    1 
ATOM   1444 C  C     . ASP A 1 221 ? 2.057   -26.774 27.495  1.00 22.42 ? 200 ASP A C     1 
ATOM   1445 O  O     . ASP A 1 221 ? 1.439   -25.915 26.800  1.00 18.21 ? 200 ASP A O     1 
ATOM   1446 C  CB    . ASP A 1 221 ? 2.056   -26.408 29.957  1.00 26.16 ? 200 ASP A CB    1 
ATOM   1447 C  CG    . ASP A 1 221 ? 2.794   -26.439 31.297  1.00 30.47 ? 200 ASP A CG    1 
ATOM   1448 O  OD1   . ASP A 1 221 ? 4.025   -26.563 31.295  1.00 32.98 ? 200 ASP A OD1   1 
ATOM   1449 O  OD2   . ASP A 1 221 ? 2.101   -26.314 32.321  1.00 35.63 ? 200 ASP A OD2   1 
ATOM   1450 N  N     . THR A 1 222 ? 2.015   -28.085 27.246  1.00 20.05 ? 201 THR A N     1 
ATOM   1451 C  CA    . THR A 1 222 ? 1.009   -28.710 26.356  1.00 19.03 ? 201 THR A CA    1 
ATOM   1452 C  C     . THR A 1 222 ? -0.257  -28.929 27.184  1.00 19.29 ? 201 THR A C     1 
ATOM   1453 O  O     . THR A 1 222 ? -1.168  -28.108 27.159  1.00 18.43 ? 201 THR A O     1 
ATOM   1454 C  CB    . THR A 1 222 ? 1.621   -29.942 25.689  1.00 18.98 ? 201 THR A CB    1 
ATOM   1455 O  OG1   . THR A 1 222 ? 2.791   -29.510 24.981  1.00 19.05 ? 201 THR A OG1   1 
ATOM   1456 C  CG2   . THR A 1 222 ? 0.624   -30.645 24.793  1.00 18.80 ? 201 THR A CG2   1 
ATOM   1457 N  N     . GLU A 1 223 ? -0.277  -29.968 28.006  1.00 21.09 ? 202 GLU A N     1 
ATOM   1458 C  CA    . GLU A 1 223 ? -1.434  -30.185 28.915  1.00 25.63 ? 202 GLU A CA    1 
ATOM   1459 C  C     . GLU A 1 223 ? -1.498  -29.012 29.902  1.00 22.78 ? 202 GLU A C     1 
ATOM   1460 O  O     . GLU A 1 223 ? -0.456  -28.672 30.485  1.00 21.64 ? 202 GLU A O     1 
ATOM   1461 C  CB    . GLU A 1 223 ? -1.338  -31.542 29.621  1.00 28.70 ? 202 GLU A CB    1 
ATOM   1462 C  CG    . GLU A 1 223 ? -2.664  -31.870 30.276  1.00 38.03 ? 202 GLU A CG    1 
ATOM   1463 C  CD    . GLU A 1 223 ? -2.813  -33.314 30.708  1.00 46.75 ? 202 GLU A CD    1 
ATOM   1464 O  OE1   . GLU A 1 223 ? -3.612  -33.550 31.633  1.00 47.67 ? 202 GLU A OE1   1 
ATOM   1465 O  OE2   . GLU A 1 223 ? -2.126  -34.180 30.117  1.00 54.51 ? 202 GLU A OE2   1 
ATOM   1466 N  N     . GLY A 1 224 ? -2.644  -28.336 29.984  1.00 19.41 ? 203 GLY A N     1 
ATOM   1467 C  CA    . GLY A 1 224 ? -2.834  -27.204 30.909  1.00 21.66 ? 203 GLY A CA    1 
ATOM   1468 C  C     . GLY A 1 224 ? -2.319  -25.895 30.303  1.00 22.89 ? 203 GLY A C     1 
ATOM   1469 O  O     . GLY A 1 224 ? -2.374  -24.846 31.032  1.00 22.17 ? 203 GLY A O     1 
ATOM   1470 N  N     . GLY A 1 225 ? -1.859  -25.913 29.030  1.00 19.85 ? 204 GLY A N     1 
ATOM   1471 C  CA    . GLY A 1 225 ? -1.221  -24.721 28.427  1.00 19.20 ? 204 GLY A CA    1 
ATOM   1472 C  C     . GLY A 1 225 ? -1.689  -24.410 27.012  1.00 18.81 ? 204 GLY A C     1 
ATOM   1473 O  O     . GLY A 1 225 ? -2.595  -25.087 26.478  1.00 17.19 ? 204 GLY A O     1 
ATOM   1474 N  N     . ALA A 1 226 ? -0.981  -23.483 26.366  1.00 16.46 ? 205 ALA A N     1 
ATOM   1475 C  CA    . ALA A 1 226 ? -1.381  -22.924 25.062  1.00 16.87 ? 205 ALA A CA    1 
ATOM   1476 C  C     . ALA A 1 226 ? -1.325  -23.994 23.957  1.00 15.58 ? 205 ALA A C     1 
ATOM   1477 O  O     . ALA A 1 226 ? -2.002  -23.787 22.945  1.00 18.85 ? 205 ALA A O     1 
ATOM   1478 C  CB    . ALA A 1 226 ? -0.520  -21.730 24.729  1.00 16.71 ? 205 ALA A CB    1 
ATOM   1479 N  N     . GLN A 1 227 ? -0.570  -25.081 24.124  1.00 14.02 ? 206 GLN A N     1 
ATOM   1480 C  CA    . GLN A 1 227 ? -0.450  -26.123 23.057  1.00 15.81 ? 206 GLN A CA    1 
ATOM   1481 C  C     . GLN A 1 227 ? -1.353  -27.334 23.351  1.00 16.10 ? 206 GLN A C     1 
ATOM   1482 O  O     . GLN A 1 227 ? -1.157  -28.409 22.713  1.00 14.87 ? 206 GLN A O     1 
ATOM   1483 C  CB    . GLN A 1 227 ? 1.003   -26.534 22.853  1.00 16.27 ? 206 GLN A CB    1 
ATOM   1484 C  CG    . GLN A 1 227 ? 1.841   -25.471 22.197  1.00 17.12 ? 206 GLN A CG    1 
ATOM   1485 C  CD    . GLN A 1 227 ? 2.137   -24.277 23.081  1.00 19.45 ? 206 GLN A CD    1 
ATOM   1486 O  OE1   . GLN A 1 227 ? 2.727   -24.388 24.164  1.00 21.76 ? 206 GLN A OE1   1 
ATOM   1487 N  NE2   . GLN A 1 227 ? 1.751   -23.112 22.612  1.00 16.54 ? 206 GLN A NE2   1 
ATOM   1488 N  N     . GLN A 1 228 ? -2.402  -27.147 24.154  1.00 16.06 ? 207 GLN A N     1 
ATOM   1489 C  CA    . GLN A 1 228 ? -3.204  -28.310 24.612  1.00 16.06 ? 207 GLN A CA    1 
ATOM   1490 C  C     . GLN A 1 228 ? -4.044  -28.912 23.479  1.00 15.97 ? 207 GLN A C     1 
ATOM   1491 O  O     . GLN A 1 228 ? -4.161  -30.149 23.421  1.00 16.21 ? 207 GLN A O     1 
ATOM   1492 C  CB    . GLN A 1 228 ? -4.191  -27.966 25.717  1.00 16.91 ? 207 GLN A CB    1 
ATOM   1493 C  CG    . GLN A 1 228 ? -4.765  -29.239 26.371  1.00 17.76 ? 207 GLN A CG    1 
ATOM   1494 C  CD    . GLN A 1 228 ? -5.555  -28.869 27.600  1.00 19.89 ? 207 GLN A CD    1 
ATOM   1495 O  OE1   . GLN A 1 228 ? -4.975  -28.685 28.674  1.00 19.14 ? 207 GLN A OE1   1 
ATOM   1496 N  NE2   . GLN A 1 228 ? -6.827  -28.599 27.407  1.00 21.98 ? 207 GLN A NE2   1 
ATOM   1497 N  N     . ASP A 1 229 ? -4.671  -28.089 22.657  1.00 16.42 ? 208 ASP A N     1 
ATOM   1498 C  CA    . ASP A 1 229 ? -5.764  -28.565 21.757  1.00 17.65 ? 208 ASP A CA    1 
ATOM   1499 C  C     . ASP A 1 229 ? -5.583  -28.004 20.350  1.00 17.72 ? 208 ASP A C     1 
ATOM   1500 O  O     . ASP A 1 229 ? -4.992  -26.949 20.230  1.00 17.18 ? 208 ASP A O     1 
ATOM   1501 C  CB    . ASP A 1 229 ? -7.141  -28.194 22.307  1.00 18.88 ? 208 ASP A CB    1 
ATOM   1502 C  CG    . ASP A 1 229 ? -7.464  -28.986 23.568  1.00 20.94 ? 208 ASP A CG    1 
ATOM   1503 O  OD1   . ASP A 1 229 ? -7.509  -30.242 23.489  1.00 20.02 ? 208 ASP A OD1   1 
ATOM   1504 O  OD2   . ASP A 1 229 ? -7.692  -28.358 24.597  1.00 22.97 ? 208 ASP A OD2   1 
ATOM   1505 N  N     . ARG A 1 230 ? -6.013  -28.779 19.355  1.00 16.48 ? 209 ARG A N     1 
ATOM   1506 C  CA    . ARG A 1 230 ? -6.113  -28.427 17.914  1.00 17.19 ? 209 ARG A CA    1 
ATOM   1507 C  C     . ARG A 1 230 ? -7.605  -28.394 17.525  1.00 15.85 ? 209 ARG A C     1 
ATOM   1508 O  O     . ARG A 1 230 ? -8.474  -28.917 18.310  1.00 19.80 ? 209 ARG A O     1 
ATOM   1509 C  CB    . ARG A 1 230 ? -5.434  -29.529 17.096  1.00 19.24 ? 209 ARG A CB    1 
ATOM   1510 C  CG    . ARG A 1 230 ? -3.935  -29.730 17.341  1.00 19.65 ? 209 ARG A CG    1 
ATOM   1511 C  CD    . ARG A 1 230 ? -3.083  -28.721 16.623  1.00 20.31 ? 209 ARG A CD    1 
ATOM   1512 N  NE    . ARG A 1 230 ? -3.445  -28.487 15.225  1.00 17.92 ? 209 ARG A NE    1 
ATOM   1513 C  CZ    . ARG A 1 230 ? -2.889  -29.103 14.170  1.00 18.97 ? 209 ARG A CZ    1 
ATOM   1514 N  NH1   . ARG A 1 230 ? -1.940  -29.998 14.333  1.00 19.24 ? 209 ARG A NH1   1 
ATOM   1515 N  NH2   . ARG A 1 230 ? -3.246  -28.796 12.943  1.00 18.09 ? 209 ARG A NH2   1 
ATOM   1516 N  N     . LEU A 1 231 ? -7.922  -27.856 16.356  1.00 15.52 ? 210 LEU A N     1 
ATOM   1517 C  CA    . LEU A 1 231 ? -9.274  -27.783 15.800  1.00 14.93 ? 210 LEU A CA    1 
ATOM   1518 C  C     . LEU A 1 231 ? -9.401  -28.839 14.718  1.00 14.94 ? 210 LEU A C     1 
ATOM   1519 O  O     . LEU A 1 231 ? -8.580  -28.856 13.762  1.00 14.84 ? 210 LEU A O     1 
ATOM   1520 C  CB    . LEU A 1 231 ? -9.543  -26.380 15.251  1.00 17.14 ? 210 LEU A CB    1 
ATOM   1521 C  CG    . LEU A 1 231 ? -9.486  -25.262 16.294  1.00 22.07 ? 210 LEU A CG    1 
ATOM   1522 C  CD1   . LEU A 1 231 ? -9.963  -23.947 15.692  1.00 20.89 ? 210 LEU A CD1   1 
ATOM   1523 C  CD2   . LEU A 1 231 ? -10.306 -25.591 17.500  1.00 23.83 ? 210 LEU A CD2   1 
ATOM   1524 N  N     . VAL A 1 232 ? -10.419 -29.668 14.835  1.00 14.54 ? 211 VAL A N     1 
ATOM   1525 C  CA    . VAL A 1 232 ? -10.721 -30.631 13.738  1.00 15.02 ? 211 VAL A CA    1 
ATOM   1526 C  C     . VAL A 1 232 ? -10.976 -29.855 12.438  1.00 15.90 ? 211 VAL A C     1 
ATOM   1527 O  O     . VAL A 1 232 ? -11.868 -29.010 12.417  1.00 17.09 ? 211 VAL A O     1 
ATOM   1528 C  CB    . VAL A 1 232 ? -11.894 -31.563 14.073  1.00 17.09 ? 211 VAL A CB    1 
ATOM   1529 C  CG1   . VAL A 1 232 ? -12.238 -32.414 12.838  1.00 16.81 ? 211 VAL A CG1   1 
ATOM   1530 C  CG2   . VAL A 1 232 ? -11.601 -32.437 15.282  1.00 17.11 ? 211 VAL A CG2   1 
ATOM   1531 N  N     . GLY A 1 233 ? -10.227 -30.174 11.373  1.00 17.05 ? 212 GLY A N     1 
ATOM   1532 C  CA    . GLY A 1 233 ? -10.297 -29.514 10.055  1.00 16.83 ? 212 GLY A CA    1 
ATOM   1533 C  C     . GLY A 1 233 ? -9.371  -28.312 9.942   1.00 15.96 ? 212 GLY A C     1 
ATOM   1534 O  O     . GLY A 1 233 ? -9.329  -27.684 8.896   1.00 16.09 ? 212 GLY A O     1 
ATOM   1535 N  N     . GLY A 1 234 ? -8.730  -27.902 11.026  1.00 17.19 ? 213 GLY A N     1 
ATOM   1536 C  CA    . GLY A 1 234 ? -7.803  -26.748 10.984  1.00 16.79 ? 213 GLY A CA    1 
ATOM   1537 C  C     . GLY A 1 234 ? -8.473  -25.420 11.319  1.00 16.09 ? 213 GLY A C     1 
ATOM   1538 O  O     . GLY A 1 234 ? -9.694  -25.369 11.588  1.00 15.89 ? 213 GLY A O     1 
ATOM   1539 N  N     . VAL A 1 235 ? -7.670  -24.377 11.416  1.00 16.44 ? 214 VAL A N     1 
ATOM   1540 C  CA    . VAL A 1 235 ? -8.130  -23.095 11.999  1.00 16.40 ? 214 VAL A CA    1 
ATOM   1541 C  C     . VAL A 1 235 ? -8.732  -22.193 10.907  1.00 16.40 ? 214 VAL A C     1 
ATOM   1542 O  O     . VAL A 1 235 ? -9.718  -21.460 11.184  1.00 16.41 ? 214 VAL A O     1 
ATOM   1543 C  CB    . VAL A 1 235 ? -6.983  -22.447 12.778  1.00 17.11 ? 214 VAL A CB    1 
ATOM   1544 C  CG1   . VAL A 1 235 ? -7.434  -21.119 13.338  1.00 15.12 ? 214 VAL A CG1   1 
ATOM   1545 C  CG2   . VAL A 1 235 ? -6.518  -23.381 13.889  1.00 17.91 ? 214 VAL A CG2   1 
ATOM   1546 N  N     . GLN A 1 236 ? -8.196  -22.207 9.694   1.00 17.11 ? 215 GLN A N     1 
ATOM   1547 C  CA    . GLN A 1 236 ? -8.724  -21.269 8.642   1.00 18.66 ? 215 GLN A CA    1 
ATOM   1548 C  C     . GLN A 1 236 ? -10.215 -21.532 8.408   1.00 19.50 ? 215 GLN A C     1 
ATOM   1549 O  O     . GLN A 1 236 ? -10.997 -20.578 8.253   1.00 18.60 ? 215 GLN A O     1 
ATOM   1550 C  CB    . GLN A 1 236 ? -7.923  -21.346 7.350   1.00 20.23 ? 215 GLN A CB    1 
ATOM   1551 C  CG    . GLN A 1 236 ? -8.361  -20.318 6.306   1.00 21.75 ? 215 GLN A CG    1 
ATOM   1552 C  CD    . GLN A 1 236 ? -7.630  -20.512 4.997   1.00 21.50 ? 215 GLN A CD    1 
ATOM   1553 O  OE1   . GLN A 1 236 ? -6.471  -20.902 4.960   1.00 21.74 ? 215 GLN A OE1   1 
ATOM   1554 N  NE2   . GLN A 1 236 ? -8.330  -20.306 3.888   1.00 20.87 ? 215 GLN A NE2   1 
ATOM   1555 N  N     . PRO A 1 237 ? -10.705 -22.799 8.466   1.00 17.26 ? 216 PRO A N     1 
ATOM   1556 C  CA    . PRO A 1 237 ? -12.156 -23.037 8.315   1.00 17.26 ? 216 PRO A CA    1 
ATOM   1557 C  C     . PRO A 1 237 ? -12.997 -22.439 9.456   1.00 17.53 ? 216 PRO A C     1 
ATOM   1558 O  O     . PRO A 1 237 ? -14.195 -22.138 9.243   1.00 17.38 ? 216 PRO A O     1 
ATOM   1559 C  CB    . PRO A 1 237 ? -12.259 -24.550 8.265   1.00 19.55 ? 216 PRO A CB    1 
ATOM   1560 C  CG    . PRO A 1 237 ? -10.902 -24.948 7.680   1.00 19.47 ? 216 PRO A CG    1 
ATOM   1561 C  CD    . PRO A 1 237 ? -9.924  -24.044 8.428   1.00 18.66 ? 216 PRO A CD    1 
ATOM   1562 N  N     . LEU A 1 238 ? -12.407 -22.247 10.637  1.00 16.60 ? 217 LEU A N     1 
ATOM   1563 C  CA    . LEU A 1 238 ? -13.133 -21.535 11.738  1.00 17.32 ? 217 LEU A CA    1 
ATOM   1564 C  C     . LEU A 1 238 ? -13.296 -20.072 11.358  1.00 17.49 ? 217 LEU A C     1 
ATOM   1565 O  O     . LEU A 1 238 ? -14.397 -19.524 11.549  1.00 15.50 ? 217 LEU A O     1 
ATOM   1566 C  CB    . LEU A 1 238 ? -12.428 -21.685 13.089  1.00 18.15 ? 217 LEU A CB    1 
ATOM   1567 C  CG    . LEU A 1 238 ? -13.040 -20.910 14.260  1.00 18.73 ? 217 LEU A CG    1 
ATOM   1568 C  CD1   . LEU A 1 238 ? -14.451 -21.357 14.552  1.00 20.68 ? 217 LEU A CD1   1 
ATOM   1569 C  CD2   . LEU A 1 238 ? -12.187 -21.069 15.520  1.00 20.09 ? 217 LEU A CD2   1 
ATOM   1570 N  N     . ALA A 1 239 ? -12.224 -19.419 10.890  1.00 16.79 ? 218 ALA A N     1 
ATOM   1571 C  CA    . ALA A 1 239 ? -12.320 -18.036 10.396  1.00 16.70 ? 218 ALA A CA    1 
ATOM   1572 C  C     . ALA A 1 239 ? -13.365 -17.960 9.289   1.00 16.26 ? 218 ALA A C     1 
ATOM   1573 O  O     . ALA A 1 239 ? -14.111 -16.972 9.193   1.00 15.80 ? 218 ALA A O     1 
ATOM   1574 C  CB    . ALA A 1 239 ? -10.956 -17.556 9.913   1.00 16.43 ? 218 ALA A CB    1 
ATOM   1575 N  N     . GLU A 1 240 ? -13.403 -18.951 8.407   1.00 15.87 ? 219 GLU A N     1 
ATOM   1576 C  CA    . GLU A 1 240 ? -14.399 -18.962 7.304   1.00 16.41 ? 219 GLU A CA    1 
ATOM   1577 C  C     . GLU A 1 240 ? -15.817 -19.046 7.868   1.00 15.61 ? 219 GLU A C     1 
ATOM   1578 O  O     . GLU A 1 240 ? -16.697 -18.377 7.338   1.00 18.29 ? 219 GLU A O     1 
ATOM   1579 C  CB    . GLU A 1 240 ? -14.021 -20.050 6.301   1.00 16.75 ? 219 GLU A CB    1 
ATOM   1580 C  CG    . GLU A 1 240 ? -12.779 -19.648 5.541   1.00 18.45 ? 219 GLU A CG    1 
ATOM   1581 C  CD    . GLU A 1 240 ? -12.075 -20.633 4.636   1.00 21.69 ? 219 GLU A CD    1 
ATOM   1582 O  OE1   . GLU A 1 240 ? -11.279 -20.144 3.802   1.00 23.62 ? 219 GLU A OE1   1 
ATOM   1583 O  OE2   . GLU A 1 240 ? -12.264 -21.855 4.824   1.00 24.75 ? 219 GLU A OE2   1 
ATOM   1584 N  N     . ARG A 1 241 ? -16.059 -19.869 8.872   1.00 16.46 ? 220 ARG A N     1 
ATOM   1585 C  CA    . ARG A 1 241 ? -17.410 -19.958 9.461   1.00 16.63 ? 220 ARG A CA    1 
ATOM   1586 C  C     . ARG A 1 241 ? -17.766 -18.603 10.064  1.00 16.31 ? 220 ARG A C     1 
ATOM   1587 O  O     . ARG A 1 241 ? -18.936 -18.212 10.007  1.00 17.65 ? 220 ARG A O     1 
ATOM   1588 C  CB    . ARG A 1 241 ? -17.458 -21.065 10.503  1.00 16.73 ? 220 ARG A CB    1 
ATOM   1589 C  CG    . ARG A 1 241 ? -17.402 -22.445 9.896   1.00 19.12 ? 220 ARG A CG    1 
ATOM   1590 C  CD    . ARG A 1 241 ? -17.623 -23.519 10.943  1.00 22.19 ? 220 ARG A CD    1 
ATOM   1591 N  NE    . ARG A 1 241 ? -17.514 -24.803 10.263  1.00 25.26 ? 220 ARG A NE    1 
ATOM   1592 C  CZ    . ARG A 1 241 ? -18.162 -25.907 10.602  1.00 29.56 ? 220 ARG A CZ    1 
ATOM   1593 N  NH1   . ARG A 1 241 ? -18.955 -25.936 11.659  1.00 28.53 ? 220 ARG A NH1   1 
ATOM   1594 N  NH2   . ARG A 1 241 ? -17.976 -27.006 9.892   1.00 29.00 ? 220 ARG A NH2   1 
ATOM   1595 N  N     . LEU A 1 242 ? -16.785 -17.915 10.652  1.00 17.16 ? 221 LEU A N     1 
ATOM   1596 C  CA    . LEU A 1 242 ? -17.041 -16.576 11.246  1.00 16.69 ? 221 LEU A CA    1 
ATOM   1597 C  C     . LEU A 1 242 ? -17.377 -15.596 10.117  1.00 16.69 ? 221 LEU A C     1 
ATOM   1598 O  O     . LEU A 1 242 ? -18.366 -14.821 10.246  1.00 16.33 ? 221 LEU A O     1 
ATOM   1599 C  CB    . LEU A 1 242 ? -15.834 -16.124 12.074  1.00 17.64 ? 221 LEU A CB    1 
ATOM   1600 C  CG    . LEU A 1 242 ? -15.891 -14.707 12.643  1.00 17.63 ? 221 LEU A CG    1 
ATOM   1601 C  CD1   . LEU A 1 242 ? -17.118 -14.448 13.459  1.00 19.49 ? 221 LEU A CD1   1 
ATOM   1602 C  CD2   . LEU A 1 242 ? -14.673 -14.411 13.502  1.00 20.79 ? 221 LEU A CD2   1 
ATOM   1603 N  N     . ALA A 1 243 ? -16.625 -15.614 9.009   1.00 16.90 ? 222 ALA A N     1 
ATOM   1604 C  CA    . ALA A 1 243 ? -16.921 -14.722 7.852   1.00 16.37 ? 222 ALA A CA    1 
ATOM   1605 C  C     . ALA A 1 243 ? -18.298 -15.033 7.233   1.00 16.89 ? 222 ALA A C     1 
ATOM   1606 O  O     . ALA A 1 243 ? -18.964 -14.080 6.728   1.00 16.56 ? 222 ALA A O     1 
ATOM   1607 C  CB    . ALA A 1 243 ? -15.867 -14.849 6.775   1.00 18.73 ? 222 ALA A CB    1 
ATOM   1608 N  N     . ALA A 1 244 ? -18.756 -16.281 7.331   1.00 16.60 ? 223 ALA A N     1 
ATOM   1609 C  CA    . ALA A 1 244 ? -20.074 -16.698 6.815   1.00 18.43 ? 223 ALA A CA    1 
ATOM   1610 C  C     . ALA A 1 244 ? -21.206 -16.094 7.658   1.00 18.14 ? 223 ALA A C     1 
ATOM   1611 O  O     . ALA A 1 244 ? -22.351 -16.128 7.199   1.00 19.67 ? 223 ALA A O     1 
ATOM   1612 C  CB    . ALA A 1 244 ? -20.156 -18.199 6.742   1.00 19.75 ? 223 ALA A CB    1 
ATOM   1613 N  N     . ARG A 1 245 ? -20.919 -15.474 8.797   1.00 18.05 ? 224 ARG A N     1 
ATOM   1614 C  CA    . ARG A 1 245 ? -21.950 -14.750 9.580   1.00 20.29 ? 224 ARG A CA    1 
ATOM   1615 C  C     . ARG A 1 245 ? -22.124 -13.328 9.019   1.00 19.61 ? 224 ARG A C     1 
ATOM   1616 O  O     . ARG A 1 245 ? -23.045 -12.650 9.439   1.00 21.14 ? 224 ARG A O     1 
ATOM   1617 C  CB    . ARG A 1 245 ? -21.630 -14.738 11.076  1.00 20.97 ? 224 ARG A CB    1 
ATOM   1618 C  CG    . ARG A 1 245 ? -21.568 -16.127 11.697  1.00 25.90 ? 224 ARG A CG    1 
ATOM   1619 C  CD    . ARG A 1 245 ? -22.751 -16.997 11.272  1.00 31.98 ? 224 ARG A CD    1 
ATOM   1620 N  NE    . ARG A 1 245 ? -22.800 -18.323 11.852  1.00 40.35 ? 224 ARG A NE    1 
ATOM   1621 C  CZ    . ARG A 1 245 ? -23.412 -18.648 12.994  1.00 45.46 ? 224 ARG A CZ    1 
ATOM   1622 N  NH1   . ARG A 1 245 ? -23.996 -17.727 13.739  1.00 50.72 ? 224 ARG A NH1   1 
ATOM   1623 N  NH2   . ARG A 1 245 ? -23.409 -19.907 13.400  1.00 45.22 ? 224 ARG A NH2   1 
ATOM   1624 N  N     . LEU A 1 246 ? -21.285 -12.862 8.117   1.00 18.30 ? 225 LEU A N     1 
ATOM   1625 C  CA    . LEU A 1 246 ? -21.485 -11.533 7.511   1.00 18.35 ? 225 LEU A CA    1 
ATOM   1626 C  C     . LEU A 1 246 ? -22.447 -11.678 6.349   1.00 19.30 ? 225 LEU A C     1 
ATOM   1627 O  O     . LEU A 1 246 ? -22.425 -12.691 5.647   1.00 20.31 ? 225 LEU A O     1 
ATOM   1628 C  CB    . LEU A 1 246 ? -20.161 -10.935 7.069   1.00 18.69 ? 225 LEU A CB    1 
ATOM   1629 C  CG    . LEU A 1 246 ? -19.099 -10.829 8.155   1.00 19.51 ? 225 LEU A CG    1 
ATOM   1630 C  CD1   . LEU A 1 246 ? -17.797 -10.348 7.517   1.00 20.64 ? 225 LEU A CD1   1 
ATOM   1631 C  CD2   . LEU A 1 246 ? -19.535 -9.861  9.229   1.00 21.66 ? 225 LEU A CD2   1 
ATOM   1632 N  N     . PRO A 1 247 ? -23.197 -10.616 6.010   1.00 20.88 ? 226 PRO A N     1 
ATOM   1633 C  CA    . PRO A 1 247 ? -24.049 -10.655 4.830   1.00 22.31 ? 226 PRO A CA    1 
ATOM   1634 C  C     . PRO A 1 247 ? -23.216 -10.764 3.548   1.00 21.46 ? 226 PRO A C     1 
ATOM   1635 O  O     . PRO A 1 247 ? -22.083 -10.291 3.504   1.00 18.79 ? 226 PRO A O     1 
ATOM   1636 C  CB    . PRO A 1 247 ? -24.830 -9.345  4.831   1.00 24.84 ? 226 PRO A CB    1 
ATOM   1637 C  CG    . PRO A 1 247 ? -24.168 -8.462  5.857   1.00 23.83 ? 226 PRO A CG    1 
ATOM   1638 C  CD    . PRO A 1 247 ? -23.200 -9.310  6.666   1.00 23.36 ? 226 PRO A CD    1 
ATOM   1639 N  N     . ASP A 1 248 ? -23.805 -11.363 2.515   1.00 19.93 ? 227 ASP A N     1 
ATOM   1640 C  CA    . ASP A 1 248 ? -23.205 -11.342 1.164   1.00 21.30 ? 227 ASP A CA    1 
ATOM   1641 C  C     . ASP A 1 248 ? -22.925 -9.873  0.790   1.00 20.63 ? 227 ASP A C     1 
ATOM   1642 O  O     . ASP A 1 248 ? -23.748 -8.958  1.107   1.00 24.06 ? 227 ASP A O     1 
ATOM   1643 C  CB    . ASP A 1 248 ? -24.095 -12.092 0.166   1.00 23.18 ? 227 ASP A CB    1 
ATOM   1644 C  CG    . ASP A 1 248 ? -24.212 -13.593 0.372   1.00 25.24 ? 227 ASP A CG    1 
ATOM   1645 O  OD1   . ASP A 1 248 ? -23.352 -14.199 1.007   1.00 22.80 ? 227 ASP A OD1   1 
ATOM   1646 O  OD2   . ASP A 1 248 ? -25.146 -14.167 -0.205  1.00 28.40 ? 227 ASP A OD2   1 
ATOM   1647 N  N     . GLY A 1 249 ? -21.783 -9.632  0.173   1.00 19.39 ? 228 GLY A N     1 
ATOM   1648 C  CA    . GLY A 1 249 ? -21.372 -8.290  -0.254  1.00 20.89 ? 228 GLY A CA    1 
ATOM   1649 C  C     . GLY A 1 249 ? -20.497 -7.601  0.777   1.00 20.37 ? 228 GLY A C     1 
ATOM   1650 O  O     . GLY A 1 249 ? -19.844 -6.610  0.395   1.00 21.83 ? 228 GLY A O     1 
ATOM   1651 N  N     . ALA A 1 250 ? -20.498 -8.037  2.025   1.00 18.89 ? 229 ALA A N     1 
ATOM   1652 C  CA    . ALA A 1 250 ? -19.745 -7.361  3.113   1.00 18.84 ? 229 ALA A CA    1 
ATOM   1653 C  C     . ALA A 1 250 ? -18.234 -7.596  2.920   1.00 20.70 ? 229 ALA A C     1 
ATOM   1654 O  O     . ALA A 1 250 ? -17.453 -6.684  3.222   1.00 22.31 ? 229 ALA A O     1 
ATOM   1655 C  CB    . ALA A 1 250 ? -20.247 -7.808  4.481   1.00 17.94 ? 229 ALA A CB    1 
ATOM   1656 N  N     . LEU A 1 251 ? -17.820 -8.762  2.447   1.00 20.45 ? 230 LEU A N     1 
ATOM   1657 C  CA    . LEU A 1 251 ? -16.390 -9.153  2.352   1.00 21.58 ? 230 LEU A CA    1 
ATOM   1658 C  C     . LEU A 1 251 ? -15.906 -8.866  0.940   1.00 23.06 ? 230 LEU A C     1 
ATOM   1659 O  O     . LEU A 1 251 ? -16.562 -9.319  -0.035  1.00 24.14 ? 230 LEU A O     1 
ATOM   1660 C  CB    . LEU A 1 251 ? -16.257 -10.645 2.676   1.00 22.11 ? 230 LEU A CB    1 
ATOM   1661 C  CG    . LEU A 1 251 ? -14.842 -11.235 2.616   1.00 23.20 ? 230 LEU A CG    1 
ATOM   1662 C  CD1   . LEU A 1 251 ? -13.924 -10.556 3.651   1.00 20.75 ? 230 LEU A CD1   1 
ATOM   1663 C  CD2   . LEU A 1 251 ? -14.873 -12.751 2.837   1.00 22.61 ? 230 LEU A CD2   1 
ATOM   1664 N  N     . ARG A 1 252 ? -14.802 -8.158  0.808   1.00 18.46 ? 231 ARG A N     1 
ATOM   1665 C  CA    . ARG A 1 252 ? -14.105 -8.002  -0.488  1.00 18.90 ? 231 ARG A CA    1 
ATOM   1666 C  C     . ARG A 1 252 ? -12.705 -8.605  -0.338  1.00 19.84 ? 231 ARG A C     1 
ATOM   1667 O  O     . ARG A 1 252 ? -11.857 -7.963  0.306   1.00 18.54 ? 231 ARG A O     1 
ATOM   1668 C  CB    . ARG A 1 252 ? -14.030 -6.530  -0.881  1.00 20.68 ? 231 ARG A CB    1 
ATOM   1669 C  CG    . ARG A 1 252 ? -15.383 -5.807  -0.917  1.00 22.15 ? 231 ARG A CG    1 
ATOM   1670 C  CD    . ARG A 1 252 ? -16.408 -6.405  -1.889  1.00 26.69 ? 231 ARG A CD    1 
ATOM   1671 N  NE    . ARG A 1 252 ? -17.812 -5.988  -1.672  1.00 22.06 ? 231 ARG A NE    1 
ATOM   1672 C  CZ    . ARG A 1 252 ? -18.356 -4.928  -2.263  1.00 27.20 ? 231 ARG A CZ    1 
ATOM   1673 N  NH1   . ARG A 1 252 ? -17.632 -4.163  -3.050  1.00 32.14 ? 231 ARG A NH1   1 
ATOM   1674 N  NH2   . ARG A 1 252 ? -19.604 -4.590  -2.034  1.00 28.00 ? 231 ARG A NH2   1 
ATOM   1675 N  N     . LEU A 1 253 ? -12.460 -9.748  -0.988  1.00 18.09 ? 232 LEU A N     1 
ATOM   1676 C  CA    . LEU A 1 253 ? -11.120 -10.387 -1.021  1.00 16.66 ? 232 LEU A CA    1 
ATOM   1677 C  C     . LEU A 1 253 ? -10.278 -9.795  -2.148  1.00 17.66 ? 232 LEU A C     1 
ATOM   1678 O  O     . LEU A 1 253 ? -10.827 -9.058  -3.013  1.00 16.91 ? 232 LEU A O     1 
ATOM   1679 C  CB    . LEU A 1 253 ? -11.300 -11.897 -1.208  1.00 18.43 ? 232 LEU A CB    1 
ATOM   1680 C  CG    . LEU A 1 253 ? -12.042 -12.621 -0.080  1.00 19.41 ? 232 LEU A CG    1 
ATOM   1681 C  CD1   . LEU A 1 253 ? -12.283 -14.087 -0.475  1.00 21.85 ? 232 LEU A CD1   1 
ATOM   1682 C  CD2   . LEU A 1 253 ? -11.251 -12.580 1.205   1.00 19.53 ? 232 LEU A CD2   1 
ATOM   1683 N  N     . SER A 1 254 ? -8.982  -10.071 -2.119  1.00 17.37 ? 233 SER A N     1 
ATOM   1684 C  CA    . SER A 1 254 ? -7.975  -9.593  -3.100  1.00 17.90 ? 233 SER A CA    1 
ATOM   1685 C  C     . SER A 1 254 ? -8.098  -8.094  -3.277  1.00 18.63 ? 233 SER A C     1 
ATOM   1686 O  O     . SER A 1 254 ? -8.024  -7.634  -4.440  1.00 18.91 ? 233 SER A O     1 
ATOM   1687 C  CB    . SER A 1 254 ? -8.124  -10.367 -4.440  1.00 20.51 ? 233 SER A CB    1 
ATOM   1688 O  OG    . SER A 1 254 ? -7.908  -11.743 -4.150  1.00 19.42 ? 233 SER A OG    1 
ATOM   1689 N  N     . THR A 1 255 ? -8.295  -7.357  -2.181  1.00 16.38 ? 234 THR A N     1 
ATOM   1690 C  CA    . THR A 1 255 ? -8.500  -5.883  -2.205  1.00 17.81 ? 234 THR A CA    1 
ATOM   1691 C  C     . THR A 1 255 ? -7.624  -5.237  -1.139  1.00 17.48 ? 234 THR A C     1 
ATOM   1692 O  O     . THR A 1 255 ? -8.100  -4.836  -0.079  1.00 18.52 ? 234 THR A O     1 
ATOM   1693 C  CB    . THR A 1 255 ? -9.989  -5.538  -2.060  1.00 19.15 ? 234 THR A CB    1 
ATOM   1694 O  OG1   . THR A 1 255 ? -10.759 -6.292  -3.011  1.00 21.09 ? 234 THR A OG1   1 
ATOM   1695 C  CG2   . THR A 1 255 ? -10.255 -4.069  -2.273  1.00 20.74 ? 234 THR A CG2   1 
ATOM   1696 N  N     . PRO A 1 256 ? -6.301  -5.128  -1.389  1.00 18.01 ? 235 PRO A N     1 
ATOM   1697 C  CA    . PRO A 1 256 ? -5.410  -4.437  -0.466  1.00 20.14 ? 235 PRO A CA    1 
ATOM   1698 C  C     . PRO A 1 256 ? -5.865  -2.990  -0.292  1.00 19.22 ? 235 PRO A C     1 
ATOM   1699 O  O     . PRO A 1 256 ? -6.209  -2.313  -1.284  1.00 18.89 ? 235 PRO A O     1 
ATOM   1700 C  CB    . PRO A 1 256 ? -4.048  -4.471  -1.181  1.00 19.35 ? 235 PRO A CB    1 
ATOM   1701 C  CG    . PRO A 1 256 ? -4.133  -5.710  -2.054  1.00 21.68 ? 235 PRO A CG    1 
ATOM   1702 C  CD    . PRO A 1 256 ? -5.562  -5.688  -2.535  1.00 19.73 ? 235 PRO A CD    1 
ATOM   1703 N  N     . VAL A 1 257 ? -5.808  -2.515  0.939   1.00 18.90 ? 236 VAL A N     1 
ATOM   1704 C  CA    . VAL A 1 257 ? -6.030  -1.089  1.247   1.00 17.76 ? 236 VAL A CA    1 
ATOM   1705 C  C     . VAL A 1 257 ? -4.685  -0.386  1.120   1.00 18.23 ? 236 VAL A C     1 
ATOM   1706 O  O     . VAL A 1 257 ? -3.753  -0.772  1.850   1.00 17.91 ? 236 VAL A O     1 
ATOM   1707 C  CB    . VAL A 1 257 ? -6.678  -0.921  2.617   1.00 19.29 ? 236 VAL A CB    1 
ATOM   1708 C  CG1   . VAL A 1 257 ? -6.618  0.515   3.115   1.00 20.64 ? 236 VAL A CG1   1 
ATOM   1709 C  CG2   . VAL A 1 257 ? -8.087  -1.458  2.617   1.00 20.16 ? 236 VAL A CG2   1 
ATOM   1710 N  N     . ARG A 1 258 ? -4.649  0.648   0.260   1.00 17.12 ? 237 ARG A N     1 
ATOM   1711 C  CA    A ARG A 1 258 ? -3.455  1.484   -0.046  0.50 18.08 ? 237 ARG A CA    1 
ATOM   1712 C  CA    B ARG A 1 258 ? -3.447  1.473   -0.029  0.50 17.79 ? 237 ARG A CA    1 
ATOM   1713 C  C     . ARG A 1 258 ? -3.476  2.783   0.759   1.00 17.91 ? 237 ARG A C     1 
ATOM   1714 O  O     . ARG A 1 258 ? -2.419  3.201   1.205   1.00 18.19 ? 237 ARG A O     1 
ATOM   1715 C  CB    A ARG A 1 258 ? -3.410  1.885   -1.521  0.50 20.06 ? 237 ARG A CB    1 
ATOM   1716 C  CB    B ARG A 1 258 ? -3.363  1.759   -1.527  0.50 19.39 ? 237 ARG A CB    1 
ATOM   1717 C  CG    A ARG A 1 258 ? -3.082  0.747   -2.474  0.50 23.18 ? 237 ARG A CG    1 
ATOM   1718 C  CG    B ARG A 1 258 ? -3.274  0.486   -2.357  0.50 21.58 ? 237 ARG A CG    1 
ATOM   1719 C  CD    A ARG A 1 258 ? -3.279  1.201   -3.907  0.50 23.62 ? 237 ARG A CD    1 
ATOM   1720 C  CD    B ARG A 1 258 ? -2.058  -0.326  -1.980  0.50 21.68 ? 237 ARG A CD    1 
ATOM   1721 N  NE    A ARG A 1 258 ? -2.818  0.164   -4.806  0.50 24.86 ? 237 ARG A NE    1 
ATOM   1722 N  NE    B ARG A 1 258 ? -1.995  -1.541  -2.782  0.50 24.41 ? 237 ARG A NE    1 
ATOM   1723 C  CZ    A ARG A 1 258 ? -2.530  0.365   -6.077  0.50 23.10 ? 237 ARG A CZ    1 
ATOM   1724 C  CZ    B ARG A 1 258 ? -1.081  -2.467  -2.627  0.50 22.36 ? 237 ARG A CZ    1 
ATOM   1725 N  NH1   A ARG A 1 258 ? -2.694  1.562   -6.594  0.50 23.11 ? 237 ARG A NH1   1 
ATOM   1726 N  NH1   B ARG A 1 258 ? -0.144  -2.293  -1.719  0.50 23.53 ? 237 ARG A NH1   1 
ATOM   1727 N  NH2   A ARG A 1 258 ? -2.105  -0.636  -6.820  0.50 23.28 ? 237 ARG A NH2   1 
ATOM   1728 N  NH2   B ARG A 1 258 ? -1.119  -3.560  -3.358  0.50 23.59 ? 237 ARG A NH2   1 
ATOM   1729 N  N     . GLY A 1 259 ? -4.651  3.385   0.904   1.00 17.71 ? 238 GLY A N     1 
ATOM   1730 C  CA    . GLY A 1 259 ? -4.778  4.654   1.628   1.00 17.33 ? 238 GLY A CA    1 
ATOM   1731 C  C     . GLY A 1 259 ? -5.995  4.697   2.527   1.00 18.47 ? 238 GLY A C     1 
ATOM   1732 O  O     . GLY A 1 259 ? -7.031  4.027   2.273   1.00 17.51 ? 238 GLY A O     1 
ATOM   1733 N  N     . LEU A 1 260 ? -5.924  5.570   3.517   1.00 18.57 ? 239 LEU A N     1 
ATOM   1734 C  CA    . LEU A 1 260 ? -7.032  5.775   4.460   1.00 19.64 ? 239 LEU A CA    1 
ATOM   1735 C  C     . LEU A 1 260 ? -7.020  7.250   4.841   1.00 19.71 ? 239 LEU A C     1 
ATOM   1736 O  O     . LEU A 1 260 ? -6.072  7.702   5.495   1.00 18.28 ? 239 LEU A O     1 
ATOM   1737 C  CB    . LEU A 1 260 ? -6.800  4.829   5.642   1.00 21.23 ? 239 LEU A CB    1 
ATOM   1738 C  CG    . LEU A 1 260 ? -7.903  4.861   6.693   1.00 25.77 ? 239 LEU A CG    1 
ATOM   1739 C  CD1   . LEU A 1 260 ? -9.245  4.512   6.062   1.00 29.83 ? 239 LEU A CD1   1 
ATOM   1740 C  CD2   . LEU A 1 260 ? -7.539  3.896   7.815   1.00 25.54 ? 239 LEU A CD2   1 
ATOM   1741 N  N     . ALA A 1 261 ? -7.951  8.006   4.266   1.00 19.17 ? 240 ALA A N     1 
ATOM   1742 C  CA    . ALA A 1 261 ? -8.099  9.451   4.518   1.00 19.85 ? 240 ALA A CA    1 
ATOM   1743 C  C     . ALA A 1 261 ? -9.282  9.659   5.444   1.00 20.19 ? 240 ALA A C     1 
ATOM   1744 O  O     . ALA A 1 261 ? -10.216 8.829   5.507   1.00 21.85 ? 240 ALA A O     1 
ATOM   1745 C  CB    . ALA A 1 261 ? -8.285  10.198  3.203   1.00 19.28 ? 240 ALA A CB    1 
ATOM   1746 N  N     . GLN A 1 262 ? -9.255  10.744  6.186   1.00 19.26 ? 241 GLN A N     1 
ATOM   1747 C  CA    . GLN A 1 262 ? -10.408 11.064  7.060   1.00 19.58 ? 241 GLN A CA    1 
ATOM   1748 C  C     . GLN A 1 262 ? -10.563 12.576  7.174   1.00 20.69 ? 241 GLN A C     1 
ATOM   1749 O  O     . GLN A 1 262 ? -9.550  13.322  6.986   1.00 20.15 ? 241 GLN A O     1 
ATOM   1750 C  CB    . GLN A 1 262 ? -10.204 10.449  8.439   1.00 19.53 ? 241 GLN A CB    1 
ATOM   1751 C  CG    . GLN A 1 262 ? -9.059  11.065  9.246   1.00 20.12 ? 241 GLN A CG    1 
ATOM   1752 C  CD    . GLN A 1 262 ? -9.065  10.517  10.650  1.00 20.53 ? 241 GLN A CD    1 
ATOM   1753 O  OE1   . GLN A 1 262 ? -10.091 10.541  11.341  1.00 19.29 ? 241 GLN A OE1   1 
ATOM   1754 N  NE2   . GLN A 1 262 ? -7.930  9.984   11.076  1.00 19.99 ? 241 GLN A NE2   1 
ATOM   1755 N  N     . ASP A 1 263 ? -11.801 12.983  7.395   1.00 22.01 ? 242 ASP A N     1 
ATOM   1756 C  CA    . ASP A 1 263 ? -12.148 14.413  7.608   1.00 25.01 ? 242 ASP A CA    1 
ATOM   1757 C  C     . ASP A 1 263 ? -13.224 14.492  8.693   1.00 26.13 ? 242 ASP A C     1 
ATOM   1758 O  O     . ASP A 1 263 ? -13.474 13.483  9.361   1.00 23.40 ? 242 ASP A O     1 
ATOM   1759 C  CB    . ASP A 1 263 ? -12.538 15.058  6.277   1.00 24.89 ? 242 ASP A CB    1 
ATOM   1760 C  CG    . ASP A 1 263 ? -13.765 14.489  5.578   1.00 29.14 ? 242 ASP A CG    1 
ATOM   1761 O  OD1   . ASP A 1 263 ? -14.597 13.822  6.230   1.00 29.73 ? 242 ASP A OD1   1 
ATOM   1762 O  OD2   . ASP A 1 263 ? -13.873 14.706  4.370   1.00 35.03 ? 242 ASP A OD2   1 
ATOM   1763 N  N     . GLY A 1 264 ? -13.862 15.658  8.850   1.00 26.45 ? 243 GLY A N     1 
ATOM   1764 C  CA    . GLY A 1 264 ? -14.945 15.847  9.832   1.00 30.25 ? 243 GLY A CA    1 
ATOM   1765 C  C     . GLY A 1 264 ? -16.177 14.963  9.621   1.00 31.67 ? 243 GLY A C     1 
ATOM   1766 O  O     . GLY A 1 264 ? -16.942 14.835  10.595  1.00 36.77 ? 243 GLY A O     1 
ATOM   1767 N  N     . ASP A 1 265 ? -16.423 14.431  8.418   1.00 33.37 ? 244 ASP A N     1 
ATOM   1768 C  CA    . ASP A 1 265 ? -17.678 13.712  8.065   1.00 32.59 ? 244 ASP A CA    1 
ATOM   1769 C  C     . ASP A 1 265 ? -17.450 12.193  7.926   1.00 32.36 ? 244 ASP A C     1 
ATOM   1770 O  O     . ASP A 1 265 ? -18.438 11.464  7.811   1.00 32.55 ? 244 ASP A O     1 
ATOM   1771 C  CB    . ASP A 1 265 ? -18.255 14.211  6.733   1.00 36.55 ? 244 ASP A CB    1 
ATOM   1772 C  CG    . ASP A 1 265 ? -18.526 15.708  6.668   1.00 45.06 ? 244 ASP A CG    1 
ATOM   1773 O  OD1   . ASP A 1 265 ? -18.924 16.268  7.717   1.00 38.43 ? 244 ASP A OD1   1 
ATOM   1774 O  OD2   . ASP A 1 265 ? -18.297 16.305  5.566   1.00 43.91 ? 244 ASP A OD2   1 
ATOM   1775 N  N     . GLY A 1 266 ? -16.221 11.698  7.787   1.00 25.97 ? 245 GLY A N     1 
ATOM   1776 C  CA    . GLY A 1 266 ? -16.036 10.254  7.568   1.00 21.99 ? 245 GLY A CA    1 
ATOM   1777 C  C     . GLY A 1 266 ? -14.627 9.883   7.143   1.00 21.24 ? 245 GLY A C     1 
ATOM   1778 O  O     . GLY A 1 266 ? -13.690 10.694  7.281   1.00 20.69 ? 245 GLY A O     1 
ATOM   1779 N  N     . VAL A 1 267 ? -14.511 8.698   6.592   1.00 19.34 ? 246 VAL A N     1 
ATOM   1780 C  CA    . VAL A 1 267 ? -13.226 8.146   6.096   1.00 20.23 ? 246 VAL A CA    1 
ATOM   1781 C  C     . VAL A 1 267 ? -13.422 7.774   4.636   1.00 21.56 ? 246 VAL A C     1 
ATOM   1782 O  O     . VAL A 1 267 ? -14.557 7.459   4.222   1.00 21.56 ? 246 VAL A O     1 
ATOM   1783 C  CB    . VAL A 1 267 ? -12.752 6.958   6.956   1.00 19.82 ? 246 VAL A CB    1 
ATOM   1784 C  CG1   . VAL A 1 267 ? -12.648 7.331   8.411   1.00 20.62 ? 246 VAL A CG1   1 
ATOM   1785 C  CG2   . VAL A 1 267 ? -13.624 5.724   6.767   1.00 23.43 ? 246 VAL A CG2   1 
ATOM   1786 N  N     . THR A 1 268 ? -12.332 7.778   3.892   1.00 20.09 ? 247 THR A N     1 
ATOM   1787 C  CA    . THR A 1 268 ? -12.281 7.280   2.511   1.00 20.44 ? 247 THR A CA    1 
ATOM   1788 C  C     . THR A 1 268 ? -11.116 6.311   2.397   1.00 20.25 ? 247 THR A C     1 
ATOM   1789 O  O     . THR A 1 268 ? -9.974  6.739   2.634   1.00 18.54 ? 247 THR A O     1 
ATOM   1790 C  CB    . THR A 1 268 ? -12.106 8.427   1.526   1.00 23.99 ? 247 THR A CB    1 
ATOM   1791 O  OG1   . THR A 1 268 ? -13.123 9.384   1.800   1.00 23.23 ? 247 THR A OG1   1 
ATOM   1792 C  CG2   . THR A 1 268 ? -12.190 8.003   0.081   1.00 24.80 ? 247 THR A CG2   1 
ATOM   1793 N  N     . VAL A 1 269 ? -11.408 5.097   1.945   1.00 19.07 ? 248 VAL A N     1 
ATOM   1794 C  CA    . VAL A 1 269 ? -10.425 4.007   1.780   1.00 21.70 ? 248 VAL A CA    1 
ATOM   1795 C  C     . VAL A 1 269 ? -10.098 3.912   0.310   1.00 24.63 ? 248 VAL A C     1 
ATOM   1796 O  O     . VAL A 1 269 ? -11.044 3.776   -0.482  1.00 26.96 ? 248 VAL A O     1 
ATOM   1797 C  CB    . VAL A 1 269 ? -10.974 2.689   2.348   1.00 21.99 ? 248 VAL A CB    1 
ATOM   1798 C  CG1   . VAL A 1 269 ? -9.885  1.642   2.383   1.00 27.65 ? 248 VAL A CG1   1 
ATOM   1799 C  CG2   . VAL A 1 269 ? -11.539 2.896   3.737   1.00 25.29 ? 248 VAL A CG2   1 
ATOM   1800 N  N     . ARG A 1 270 ? -8.809  4.023   -0.022  1.00 22.46 ? 249 ARG A N     1 
ATOM   1801 C  CA    . ARG A 1 270 ? -8.291  3.931   -1.387  1.00 23.63 ? 249 ARG A CA    1 
ATOM   1802 C  C     . ARG A 1 270 ? -7.737  2.527   -1.619  1.00 23.41 ? 249 ARG A C     1 
ATOM   1803 O  O     . ARG A 1 270 ? -6.929  2.060   -0.790  1.00 19.40 ? 249 ARG A O     1 
ATOM   1804 C  CB    . ARG A 1 270 ? -7.213  4.978   -1.669  1.00 25.49 ? 249 ARG A CB    1 
ATOM   1805 C  CG    . ARG A 1 270 ? -6.795  5.025   -3.135  1.00 29.54 ? 249 ARG A CG    1 
ATOM   1806 C  CD    . ARG A 1 270 ? -5.740  6.079   -3.502  1.00 29.31 ? 249 ARG A CD    1 
ATOM   1807 N  NE    . ARG A 1 270 ? -4.670  6.259   -2.526  1.00 34.88 ? 249 ARG A NE    1 
ATOM   1808 C  CZ    . ARG A 1 270 ? -3.509  5.627   -2.551  1.00 35.42 ? 249 ARG A CZ    1 
ATOM   1809 N  NH1   . ARG A 1 270 ? -3.266  4.715   -3.479  1.00 43.46 ? 249 ARG A NH1   1 
ATOM   1810 N  NH2   . ARG A 1 270 ? -2.586  5.903   -1.648  1.00 34.83 ? 249 ARG A NH2   1 
ATOM   1811 N  N     . THR A 1 271 ? -8.243  1.869   -2.645  1.00 22.64 ? 250 THR A N     1 
ATOM   1812 C  CA    . THR A 1 271 ? -7.760  0.551   -3.139  1.00 25.13 ? 250 THR A CA    1 
ATOM   1813 C  C     . THR A 1 271 ? -7.276  0.760   -4.574  1.00 26.78 ? 250 THR A C     1 
ATOM   1814 O  O     . THR A 1 271 ? -7.621  1.811   -5.142  1.00 31.79 ? 250 THR A O     1 
ATOM   1815 C  CB    . THR A 1 271 ? -8.863  -0.525  -3.033  1.00 24.61 ? 250 THR A CB    1 
ATOM   1816 O  OG1   . THR A 1 271 ? -9.875  -0.279  -4.010  1.00 22.91 ? 250 THR A OG1   1 
ATOM   1817 C  CG2   . THR A 1 271 ? -9.523  -0.593  -1.672  1.00 23.55 ? 250 THR A CG2   1 
ATOM   1818 N  N     . ALA A 1 272 ? -6.677  -0.258  -5.215  1.00 29.10 ? 251 ALA A N     1 
ATOM   1819 C  CA    . ALA A 1 272 ? -6.331  -0.217  -6.662  1.00 30.43 ? 251 ALA A CA    1 
ATOM   1820 C  C     . ALA A 1 272 ? -7.613  -0.061  -7.496  1.00 33.28 ? 251 ALA A C     1 
ATOM   1821 O  O     . ALA A 1 272 ? -7.580  0.633   -8.515  1.00 34.18 ? 251 ALA A O     1 
ATOM   1822 C  CB    . ALA A 1 272 ? -5.582  -1.467  -7.054  1.00 29.31 ? 251 ALA A CB    1 
ATOM   1823 N  N     . GLY A 1 273 ? -8.706  -0.687  -7.065  1.00 35.36 ? 252 GLY A N     1 
ATOM   1824 C  CA    . GLY A 1 273 ? -9.958  -0.782  -7.832  1.00 38.97 ? 252 GLY A CA    1 
ATOM   1825 C  C     . GLY A 1 273 ? -10.973 0.284   -7.475  1.00 43.47 ? 252 GLY A C     1 
ATOM   1826 O  O     . GLY A 1 273 ? -12.106 0.190   -8.009  1.00 48.26 ? 252 GLY A O     1 
ATOM   1827 N  N     . GLY A 1 274 ? -10.607 1.249   -6.610  1.00 33.97 ? 253 GLY A N     1 
ATOM   1828 C  CA    . GLY A 1 274 ? -11.386 2.474   -6.354  1.00 34.92 ? 253 GLY A CA    1 
ATOM   1829 C  C     . GLY A 1 274 ? -11.455 2.801   -4.872  1.00 35.60 ? 253 GLY A C     1 
ATOM   1830 O  O     . GLY A 1 274 ? -10.500 2.467   -4.139  1.00 36.81 ? 253 GLY A O     1 
ATOM   1831 N  N     . GLU A 1 275 ? -12.510 3.485   -4.434  1.00 33.75 ? 254 GLU A N     1 
ATOM   1832 C  CA    . GLU A 1 275 ? -12.582 4.057   -3.062  1.00 35.45 ? 254 GLU A CA    1 
ATOM   1833 C  C     . GLU A 1 275 ? -13.860 3.579   -2.371  1.00 33.84 ? 254 GLU A C     1 
ATOM   1834 O  O     . GLU A 1 275 ? -14.821 3.359   -3.068  1.00 32.90 ? 254 GLU A O     1 
ATOM   1835 C  CB    . GLU A 1 275 ? -12.525 5.582   -3.133  1.00 38.38 ? 254 GLU A CB    1 
ATOM   1836 C  CG    . GLU A 1 275 ? -11.217 6.084   -3.705  1.00 41.47 ? 254 GLU A CG    1 
ATOM   1837 C  CD    . GLU A 1 275 ? -11.028 7.594   -3.608  1.00 48.58 ? 254 GLU A CD    1 
ATOM   1838 O  OE1   . GLU A 1 275 ? -9.849  8.015   -3.544  1.00 51.52 ? 254 GLU A OE1   1 
ATOM   1839 O  OE2   . GLU A 1 275 ? -12.054 8.341   -3.553  1.00 42.25 ? 254 GLU A OE2   1 
ATOM   1840 N  N     . VAL A 1 276 ? -13.832 3.432   -1.052  1.00 28.60 ? 255 VAL A N     1 
ATOM   1841 C  CA    . VAL A 1 276 ? -14.997 3.100   -0.182  1.00 28.32 ? 255 VAL A CA    1 
ATOM   1842 C  C     . VAL A 1 276 ? -15.119 4.271   0.787   1.00 25.87 ? 255 VAL A C     1 
ATOM   1843 O  O     . VAL A 1 276 ? -14.103 4.664   1.366   1.00 23.10 ? 255 VAL A O     1 
ATOM   1844 C  CB    . VAL A 1 276 ? -14.777 1.775   0.582   1.00 32.66 ? 255 VAL A CB    1 
ATOM   1845 C  CG1   . VAL A 1 276 ? -15.703 1.640   1.790   1.00 37.92 ? 255 VAL A CG1   1 
ATOM   1846 C  CG2   . VAL A 1 276 ? -14.923 0.562   -0.316  1.00 35.83 ? 255 VAL A CG2   1 
ATOM   1847 N  N     . ARG A 1 277 ? -16.311 4.818   0.949   1.00 24.10 ? 256 ARG A N     1 
ATOM   1848 C  CA    . ARG A 1 277 ? -16.600 5.878   1.939   1.00 24.42 ? 256 ARG A CA    1 
ATOM   1849 C  C     . ARG A 1 277 ? -17.234 5.210   3.161   1.00 21.10 ? 256 ARG A C     1 
ATOM   1850 O  O     . ARG A 1 277 ? -18.090 4.342   2.969   1.00 23.76 ? 256 ARG A O     1 
ATOM   1851 C  CB    . ARG A 1 277 ? -17.481 6.937   1.276   1.00 27.79 ? 256 ARG A CB    1 
ATOM   1852 C  CG    . ARG A 1 277 ? -17.815 8.114   2.169   1.00 41.20 ? 256 ARG A CG    1 
ATOM   1853 C  CD    . ARG A 1 277 ? -16.700 9.147   2.194   1.00 51.02 ? 256 ARG A CD    1 
ATOM   1854 N  NE    . ARG A 1 277 ? -16.502 9.867   3.463   1.00 48.23 ? 256 ARG A NE    1 
ATOM   1855 C  CZ    . ARG A 1 277 ? -16.140 11.154  3.522   1.00 52.70 ? 256 ARG A CZ    1 
ATOM   1856 N  NH1   . ARG A 1 277 ? -16.020 11.867  2.414   1.00 65.00 ? 256 ARG A NH1   1 
ATOM   1857 N  NH2   . ARG A 1 277 ? -15.892 11.746  4.670   1.00 48.30 ? 256 ARG A NH2   1 
ATOM   1858 N  N     . ALA A 1 278 ? -16.839 5.598   4.366   1.00 20.39 ? 257 ALA A N     1 
ATOM   1859 C  CA    . ALA A 1 278 ? -17.466 5.112   5.613   1.00 20.34 ? 257 ALA A CA    1 
ATOM   1860 C  C     . ALA A 1 278 ? -17.435 6.192   6.684   1.00 20.56 ? 257 ALA A C     1 
ATOM   1861 O  O     . ALA A 1 278 ? -16.749 7.214   6.523   1.00 23.72 ? 257 ALA A O     1 
ATOM   1862 C  CB    . ALA A 1 278 ? -16.812 3.866   6.132   1.00 22.12 ? 257 ALA A CB    1 
ATOM   1863 N  N     . ARG A 1 279 ? -18.184 5.959   7.740   1.00 18.55 ? 258 ARG A N     1 
ATOM   1864 C  CA    . ARG A 1 279 ? -18.210 6.880   8.891   1.00 18.36 ? 258 ARG A CA    1 
ATOM   1865 C  C     . ARG A 1 279 ? -16.957 6.668   9.729   1.00 21.24 ? 258 ARG A C     1 
ATOM   1866 O  O     . ARG A 1 279 ? -16.361 7.685   10.130  1.00 21.54 ? 258 ARG A O     1 
ATOM   1867 C  CB    . ARG A 1 279 ? -19.527 6.750   9.650   1.00 19.97 ? 258 ARG A CB    1 
ATOM   1868 C  CG    . ARG A 1 279 ? -20.727 7.182   8.816   1.00 23.42 ? 258 ARG A CG    1 
ATOM   1869 C  CD    . ARG A 1 279 ? -22.072 7.089   9.539   1.00 26.34 ? 258 ARG A CD    1 
ATOM   1870 N  NE    . ARG A 1 279 ? -22.011 7.846   10.777  1.00 29.79 ? 258 ARG A NE    1 
ATOM   1871 C  CZ    . ARG A 1 279 ? -22.859 7.701   11.797  1.00 33.21 ? 258 ARG A CZ    1 
ATOM   1872 N  NH1   . ARG A 1 279 ? -23.850 6.838   11.715  1.00 34.00 ? 258 ARG A NH1   1 
ATOM   1873 N  NH2   . ARG A 1 279 ? -22.698 8.402   12.906  1.00 36.52 ? 258 ARG A NH2   1 
ATOM   1874 N  N     . ARG A 1 280 ? -16.611 5.404   10.003  1.00 19.31 ? 259 ARG A N     1 
ATOM   1875 C  CA    . ARG A 1 280 ? -15.464 5.067   10.853  1.00 19.51 ? 259 ARG A CA    1 
ATOM   1876 C  C     . ARG A 1 280 ? -14.733 3.876   10.250  1.00 18.28 ? 259 ARG A C     1 
ATOM   1877 O  O     . ARG A 1 280 ? -15.349 3.128   9.461   1.00 16.27 ? 259 ARG A O     1 
ATOM   1878 C  CB    . ARG A 1 280 ? -15.905 4.762   12.276  1.00 22.22 ? 259 ARG A CB    1 
ATOM   1879 C  CG    . ARG A 1 280 ? -16.598 5.951   12.923  1.00 26.44 ? 259 ARG A CG    1 
ATOM   1880 C  CD    . ARG A 1 280 ? -16.293 6.003   14.386  1.00 31.47 ? 259 ARG A CD    1 
ATOM   1881 N  NE    . ARG A 1 280 ? -16.601 7.361   14.733  1.00 35.60 ? 259 ARG A NE    1 
ATOM   1882 C  CZ    . ARG A 1 280 ? -15.792 8.204   15.338  1.00 30.59 ? 259 ARG A CZ    1 
ATOM   1883 N  NH1   . ARG A 1 280 ? -14.578 7.879   15.807  1.00 25.78 ? 259 ARG A NH1   1 
ATOM   1884 N  NH2   . ARG A 1 280 ? -16.295 9.386   15.536  1.00 28.91 ? 259 ARG A NH2   1 
ATOM   1885 N  N     . ALA A 1 281 ? -13.478 3.720   10.652  1.00 18.70 ? 260 ALA A N     1 
ATOM   1886 C  CA    . ALA A 1 281 ? -12.652 2.594   10.177  1.00 17.04 ? 260 ALA A CA    1 
ATOM   1887 C  C     . ALA A 1 281 ? -12.058 1.846   11.364  1.00 16.25 ? 260 ALA A C     1 
ATOM   1888 O  O     . ALA A 1 281 ? -11.756 2.466   12.407  1.00 15.43 ? 260 ALA A O     1 
ATOM   1889 C  CB    . ALA A 1 281 ? -11.584 3.046   9.212   1.00 17.64 ? 260 ALA A CB    1 
ATOM   1890 N  N     . ILE A 1 282 ? -11.883 0.546   11.166  1.00 14.37 ? 261 ILE A N     1 
ATOM   1891 C  CA    . ILE A 1 282 ? -11.131 -0.332  12.100  1.00 14.35 ? 261 ILE A CA    1 
ATOM   1892 C  C     . ILE A 1 282 ? -9.998  -0.944  11.290  1.00 15.66 ? 261 ILE A C     1 
ATOM   1893 O  O     . ILE A 1 282 ? -10.278 -1.674  10.361  1.00 16.86 ? 261 ILE A O     1 
ATOM   1894 C  CB    . ILE A 1 282 ? -12.016 -1.394  12.775  1.00 14.98 ? 261 ILE A CB    1 
ATOM   1895 C  CG1   . ILE A 1 282 ? -13.128 -0.753  13.612  1.00 16.08 ? 261 ILE A CG1   1 
ATOM   1896 C  CG2   . ILE A 1 282 ? -11.176 -2.352  13.594  1.00 15.23 ? 261 ILE A CG2   1 
ATOM   1897 C  CD1   . ILE A 1 282 ? -14.136 -1.749  14.148  1.00 17.63 ? 261 ILE A CD1   1 
ATOM   1898 N  N     . VAL A 1 283 ? -8.761  -0.608  11.619  1.00 15.32 ? 262 VAL A N     1 
ATOM   1899 C  CA    . VAL A 1 283 ? -7.580  -1.190  10.945  1.00 15.10 ? 262 VAL A CA    1 
ATOM   1900 C  C     . VAL A 1 283 ? -7.102  -2.341  11.803  1.00 14.89 ? 262 VAL A C     1 
ATOM   1901 O  O     . VAL A 1 283 ? -6.789  -2.102  12.947  1.00 14.72 ? 262 VAL A O     1 
ATOM   1902 C  CB    . VAL A 1 283 ? -6.473  -0.141  10.721  1.00 16.99 ? 262 VAL A CB    1 
ATOM   1903 C  CG1   . VAL A 1 283 ? -5.226  -0.776  10.085  1.00 17.04 ? 262 VAL A CG1   1 
ATOM   1904 C  CG2   . VAL A 1 283 ? -6.992  1.008   9.863   1.00 17.97 ? 262 VAL A CG2   1 
ATOM   1905 N  N     . ALA A 1 284 ? -7.137  -3.563  11.257  1.00 15.02 ? 263 ALA A N     1 
ATOM   1906 C  CA    . ALA A 1 284 ? -6.930  -4.799  12.041  1.00 15.29 ? 263 ALA A CA    1 
ATOM   1907 C  C     . ALA A 1 284 ? -5.799  -5.617  11.387  1.00 16.61 ? 263 ALA A C     1 
ATOM   1908 O  O     . ALA A 1 284 ? -5.993  -6.804  11.162  1.00 18.48 ? 263 ALA A O     1 
ATOM   1909 C  CB    . ALA A 1 284 ? -8.247  -5.562  12.035  1.00 15.75 ? 263 ALA A CB    1 
ATOM   1910 N  N     . VAL A 1 285 ? -4.692  -4.972  11.016  1.00 17.51 ? 264 VAL A N     1 
ATOM   1911 C  CA    . VAL A 1 285 ? -3.523  -5.637  10.343  1.00 16.85 ? 264 VAL A CA    1 
ATOM   1912 C  C     . VAL A 1 285 ? -2.328  -5.578  11.281  1.00 17.06 ? 264 VAL A C     1 
ATOM   1913 O  O     . VAL A 1 285 ? -2.295  -4.808  12.235  1.00 17.98 ? 264 VAL A O     1 
ATOM   1914 C  CB    . VAL A 1 285 ? -3.247  -4.941  8.988   1.00 17.78 ? 264 VAL A CB    1 
ATOM   1915 C  CG1   . VAL A 1 285 ? -4.496  -4.950  8.109   1.00 18.58 ? 264 VAL A CG1   1 
ATOM   1916 C  CG2   . VAL A 1 285 ? -2.706  -3.510  9.145   1.00 18.08 ? 264 VAL A CG2   1 
ATOM   1917 N  N     . PRO A 1 286 ? -1.263  -6.359  11.027  1.00 17.06 ? 265 PRO A N     1 
ATOM   1918 C  CA    . PRO A 1 286 ? -0.041  -6.265  11.813  1.00 17.14 ? 265 PRO A CA    1 
ATOM   1919 C  C     . PRO A 1 286 ? 0.546   -4.862  11.822  1.00 17.54 ? 265 PRO A C     1 
ATOM   1920 O  O     . PRO A 1 286 ? 0.422   -4.118  10.845  1.00 14.07 ? 265 PRO A O     1 
ATOM   1921 C  CB    . PRO A 1 286 ? 0.926   -7.238  11.115  1.00 16.12 ? 265 PRO A CB    1 
ATOM   1922 C  CG    . PRO A 1 286 ? 0.027   -8.198  10.415  1.00 17.98 ? 265 PRO A CG    1 
ATOM   1923 C  CD    . PRO A 1 286 ? -1.220  -7.436  10.015  1.00 18.93 ? 265 PRO A CD    1 
ATOM   1924 N  N     . PRO A 1 287 ? 1.137   -4.437  12.960  1.00 17.29 ? 266 PRO A N     1 
ATOM   1925 C  CA    . PRO A 1 287 ? 1.608   -3.054  13.110  1.00 20.92 ? 266 PRO A CA    1 
ATOM   1926 C  C     . PRO A 1 287 ? 2.480   -2.541  11.955  1.00 17.22 ? 266 PRO A C     1 
ATOM   1927 O  O     . PRO A 1 287 ? 2.237   -1.429  11.465  1.00 18.72 ? 266 PRO A O     1 
ATOM   1928 C  CB    . PRO A 1 287 ? 2.418   -3.130  14.413  1.00 22.06 ? 266 PRO A CB    1 
ATOM   1929 C  CG    . PRO A 1 287 ? 1.719   -4.198  15.218  1.00 21.88 ? 266 PRO A CG    1 
ATOM   1930 C  CD    . PRO A 1 287 ? 1.333   -5.243  14.188  1.00 19.59 ? 266 PRO A CD    1 
ATOM   1931 N  N     . THR A 1 288 ? 3.467   -3.330  11.501  1.00 20.07 ? 267 THR A N     1 
ATOM   1932 C  CA    . THR A 1 288 ? 4.370   -2.862  10.414  1.00 18.90 ? 267 THR A CA    1 
ATOM   1933 C  C     . THR A 1 288 ? 3.528   -2.614  9.144   1.00 18.99 ? 267 THR A C     1 
ATOM   1934 O  O     . THR A 1 288 ? 3.823   -1.686  8.437   1.00 21.21 ? 267 THR A O     1 
ATOM   1935 C  CB    . THR A 1 288 ? 5.531   -3.839  10.159  1.00 20.99 ? 267 THR A CB    1 
ATOM   1936 O  OG1   . THR A 1 288 ? 6.324   -3.302  9.095   1.00 22.12 ? 267 THR A OG1   1 
ATOM   1937 C  CG2   . THR A 1 288 ? 5.052   -5.181  9.664   1.00 19.19 ? 267 THR A CG2   1 
ATOM   1938 N  N     . LEU A 1 289 ? 2.476   -3.400  8.860   1.00 17.70 ? 268 LEU A N     1 
ATOM   1939 C  CA    . LEU A 1 289 ? 1.603   -3.175  7.680   1.00 17.33 ? 268 LEU A CA    1 
ATOM   1940 C  C     . LEU A 1 289 ? 0.660   -1.981  7.906   1.00 16.87 ? 268 LEU A C     1 
ATOM   1941 O  O     . LEU A 1 289 ? 0.389   -1.267  6.942   1.00 17.73 ? 268 LEU A O     1 
ATOM   1942 C  CB    . LEU A 1 289 ? 0.837   -4.449  7.320   1.00 18.04 ? 268 LEU A CB    1 
ATOM   1943 C  CG    . LEU A 1 289 ? 1.743   -5.643  6.987   1.00 21.13 ? 268 LEU A CG    1 
ATOM   1944 C  CD1   . LEU A 1 289 ? 0.959   -6.845  6.547   1.00 22.45 ? 268 LEU A CD1   1 
ATOM   1945 C  CD2   . LEU A 1 289 ? 2.751   -5.290  5.910   1.00 25.00 ? 268 LEU A CD2   1 
ATOM   1946 N  N     . ALA A 1 290 ? 0.214   -1.737  9.122   1.00 16.47 ? 269 ALA A N     1 
ATOM   1947 C  CA    . ALA A 1 290 ? -0.656  -0.578  9.438   1.00 16.61 ? 269 ALA A CA    1 
ATOM   1948 C  C     . ALA A 1 290 ? 0.093   0.720   9.128   1.00 18.73 ? 269 ALA A C     1 
ATOM   1949 O  O     . ALA A 1 290 ? -0.540  1.664   8.612   1.00 18.45 ? 269 ALA A O     1 
ATOM   1950 C  CB    . ALA A 1 290 ? -1.114  -0.677  10.853  1.00 17.52 ? 269 ALA A CB    1 
ATOM   1951 N  N     . GLY A 1 291 ? 1.397   0.727   9.389   1.00 18.74 ? 270 GLY A N     1 
ATOM   1952 C  CA    . GLY A 1 291 ? 2.285   1.895   9.144   1.00 22.42 ? 270 GLY A CA    1 
ATOM   1953 C  C     . GLY A 1 291 ? 2.487   2.194   7.661   1.00 21.26 ? 270 GLY A C     1 
ATOM   1954 O  O     . GLY A 1 291 ? 2.774   3.370   7.290   1.00 22.62 ? 270 GLY A O     1 
ATOM   1955 N  N     . ARG A 1 292 ? 2.302   1.206   6.794   1.00 18.61 ? 271 ARG A N     1 
ATOM   1956 C  CA    . ARG A 1 292 ? 2.605   1.350   5.353   1.00 18.64 ? 271 ARG A CA    1 
ATOM   1957 C  C     . ARG A 1 292 ? 1.409   1.932   4.603   1.00 18.35 ? 271 ARG A C     1 
ATOM   1958 O  O     . ARG A 1 292 ? 1.593   2.376   3.487   1.00 19.42 ? 271 ARG A O     1 
ATOM   1959 C  CB    . ARG A 1 292 ? 3.027   0.007   4.761   1.00 18.63 ? 271 ARG A CB    1 
ATOM   1960 C  CG    . ARG A 1 292 ? 4.187   -0.579  5.548   1.00 19.03 ? 271 ARG A CG    1 
ATOM   1961 C  CD    . ARG A 1 292 ? 4.728   -1.836  4.906   1.00 20.68 ? 271 ARG A CD    1 
ATOM   1962 N  NE    . ARG A 1 292 ? 5.509   -2.615  5.859   1.00 20.99 ? 271 ARG A NE    1 
ATOM   1963 C  CZ    . ARG A 1 292 ? 6.242   -3.701  5.541   1.00 23.37 ? 271 ARG A CZ    1 
ATOM   1964 N  NH1   . ARG A 1 292 ? 6.322   -4.116  4.299   1.00 22.15 ? 271 ARG A NH1   1 
ATOM   1965 N  NH2   . ARG A 1 292 ? 6.878   -4.380  6.493   1.00 24.85 ? 271 ARG A NH2   1 
ATOM   1966 N  N     . ILE A 1 293 ? 0.224   1.930   5.208   1.00 18.08 ? 272 ILE A N     1 
ATOM   1967 C  CA    . ILE A 1 293 ? -0.985  2.537   4.592   1.00 18.47 ? 272 ILE A CA    1 
ATOM   1968 C  C     . ILE A 1 293 ? -0.759  4.053   4.478   1.00 19.33 ? 272 ILE A C     1 
ATOM   1969 O  O     . ILE A 1 293 ? -0.138  4.678   5.404   1.00 18.32 ? 272 ILE A O     1 
ATOM   1970 C  CB    . ILE A 1 293 ? -2.235  2.163   5.409   1.00 18.17 ? 272 ILE A CB    1 
ATOM   1971 C  CG1   . ILE A 1 293 ? -2.528  0.671   5.305   1.00 16.64 ? 272 ILE A CG1   1 
ATOM   1972 C  CG2   . ILE A 1 293 ? -3.436  3.025   5.014   1.00 21.26 ? 272 ILE A CG2   1 
ATOM   1973 C  CD1   . ILE A 1 293 ? -3.554  0.204   6.323   1.00 18.02 ? 272 ILE A CD1   1 
ATOM   1974 N  N     . ASP A 1 294 ? -1.176  4.616   3.353   1.00 19.39 ? 273 ASP A N     1 
ATOM   1975 C  CA    . ASP A 1 294 ? -1.070  6.063   3.105   1.00 21.27 ? 273 ASP A CA    1 
ATOM   1976 C  C     . ASP A 1 294 ? -2.180  6.735   3.941   1.00 19.53 ? 273 ASP A C     1 
ATOM   1977 O  O     . ASP A 1 294 ? -3.328  6.790   3.491   1.00 19.96 ? 273 ASP A O     1 
ATOM   1978 C  CB    . ASP A 1 294 ? -1.157  6.323   1.599   1.00 22.19 ? 273 ASP A CB    1 
ATOM   1979 C  CG    . ASP A 1 294 ? -1.262  7.793   1.236   1.00 27.98 ? 273 ASP A CG    1 
ATOM   1980 O  OD1   . ASP A 1 294 ? -0.863  8.613   2.065   1.00 28.36 ? 273 ASP A OD1   1 
ATOM   1981 O  OD2   . ASP A 1 294 ? -1.796  8.095   0.148   1.00 34.37 ? 273 ASP A OD2   1 
ATOM   1982 N  N     . HIS A 1 295 ? -1.837  7.233   5.118   1.00 19.90 ? 274 HIS A N     1 
ATOM   1983 C  CA    . HIS A 1 295 ? -2.798  7.892   6.042   1.00 18.69 ? 274 HIS A CA    1 
ATOM   1984 C  C     . HIS A 1 295 ? -2.879  9.380   5.705   1.00 18.23 ? 274 HIS A C     1 
ATOM   1985 O  O     . HIS A 1 295 ? -1.842  10.062  5.575   1.00 18.06 ? 274 HIS A O     1 
ATOM   1986 C  CB    . HIS A 1 295 ? -2.460  7.650   7.485   1.00 20.18 ? 274 HIS A CB    1 
ATOM   1987 C  CG    . HIS A 1 295 ? -2.497  6.215   7.883   1.00 20.97 ? 274 HIS A CG    1 
ATOM   1988 N  ND1   . HIS A 1 295 ? -3.663  5.605   8.297   1.00 21.47 ? 274 HIS A ND1   1 
ATOM   1989 C  CD2   . HIS A 1 295 ? -1.500  5.308   7.999   1.00 21.25 ? 274 HIS A CD2   1 
ATOM   1990 C  CE1   . HIS A 1 295 ? -3.407  4.372   8.643   1.00 19.87 ? 274 HIS A CE1   1 
ATOM   1991 N  NE2   . HIS A 1 295 ? -2.048  4.167   8.493   1.00 22.40 ? 274 HIS A NE2   1 
ATOM   1992 N  N     . ASP A 1 296 ? -4.102  9.887   5.632   1.00 18.77 ? 275 ASP A N     1 
ATOM   1993 C  CA    . ASP A 1 296 ? -4.320  11.340  5.446   1.00 20.80 ? 275 ASP A CA    1 
ATOM   1994 C  C     . ASP A 1 296 ? -5.374  11.794  6.450   1.00 21.62 ? 275 ASP A C     1 
ATOM   1995 O  O     . ASP A 1 296 ? -6.512  11.346  6.404   1.00 21.14 ? 275 ASP A O     1 
ATOM   1996 C  CB    . ASP A 1 296 ? -4.770  11.617  4.026   1.00 23.52 ? 275 ASP A CB    1 
ATOM   1997 C  CG    . ASP A 1 296 ? -5.158  13.060  3.807   1.00 26.92 ? 275 ASP A CG    1 
ATOM   1998 O  OD1   . ASP A 1 296 ? -4.676  13.895  4.540   1.00 29.50 ? 275 ASP A OD1   1 
ATOM   1999 O  OD2   . ASP A 1 296 ? -5.978  13.313  2.896   1.00 34.84 ? 275 ASP A OD2   1 
ATOM   2000 N  N     . PRO A 1 297 ? -5.058  12.685  7.398   1.00 20.89 ? 276 PRO A N     1 
ATOM   2001 C  CA    . PRO A 1 297 ? -3.707  13.219  7.585   1.00 20.87 ? 276 PRO A CA    1 
ATOM   2002 C  C     . PRO A 1 297 ? -2.724  12.135  8.024   1.00 20.40 ? 276 PRO A C     1 
ATOM   2003 O  O     . PRO A 1 297 ? -3.116  11.063  8.500   1.00 19.57 ? 276 PRO A O     1 
ATOM   2004 C  CB    . PRO A 1 297 ? -3.852  14.275  8.702   1.00 23.21 ? 276 PRO A CB    1 
ATOM   2005 C  CG    . PRO A 1 297 ? -5.264  14.198  9.234   1.00 23.35 ? 276 PRO A CG    1 
ATOM   2006 C  CD    . PRO A 1 297 ? -6.024  13.207  8.371   1.00 22.31 ? 276 PRO A CD    1 
ATOM   2007 N  N     . PRO A 1 298 ? -1.403  12.395  7.914   1.00 21.43 ? 277 PRO A N     1 
ATOM   2008 C  CA    . PRO A 1 298 ? -0.413  11.437  8.403   1.00 21.22 ? 277 PRO A CA    1 
ATOM   2009 C  C     . PRO A 1 298 ? -0.669  11.062  9.863   1.00 18.69 ? 277 PRO A C     1 
ATOM   2010 O  O     . PRO A 1 298 ? -1.163  11.899  10.667  1.00 17.31 ? 277 PRO A O     1 
ATOM   2011 C  CB    . PRO A 1 298 ? 0.894   12.224  8.277   1.00 25.66 ? 277 PRO A CB    1 
ATOM   2012 C  CG    . PRO A 1 298 ? 0.625   13.233  7.164   1.00 26.56 ? 277 PRO A CG    1 
ATOM   2013 C  CD    . PRO A 1 298 ? -0.813  13.629  7.371   1.00 23.88 ? 277 PRO A CD    1 
ATOM   2014 N  N     . LEU A 1 299 ? -0.306  9.848   10.259  1.00 19.37 ? 278 LEU A N     1 
ATOM   2015 C  CA    . LEU A 1 299 ? -0.485  9.470   11.687  1.00 20.18 ? 278 LEU A CA    1 
ATOM   2016 C  C     . LEU A 1 299 ? 0.348   10.413  12.570  1.00 20.77 ? 278 LEU A C     1 
ATOM   2017 O  O     . LEU A 1 299 ? 1.390   10.948  12.160  1.00 20.70 ? 278 LEU A O     1 
ATOM   2018 C  CB    . LEU A 1 299 ? -0.083  8.023   11.923  1.00 21.19 ? 278 LEU A CB    1 
ATOM   2019 C  CG    . LEU A 1 299 ? -0.874  6.963   11.160  1.00 21.35 ? 278 LEU A CG    1 
ATOM   2020 C  CD1   . LEU A 1 299 ? -0.315  5.602   11.499  1.00 22.28 ? 278 LEU A CD1   1 
ATOM   2021 C  CD2   . LEU A 1 299 ? -2.367  7.057   11.455  1.00 21.54 ? 278 LEU A CD2   1 
ATOM   2022 N  N     . PRO A 1 300 ? -0.103  10.672  13.804  1.00 20.66 ? 279 PRO A N     1 
ATOM   2023 C  CA    . PRO A 1 300 ? 0.687   11.463  14.757  1.00 20.30 ? 279 PRO A CA    1 
ATOM   2024 C  C     . PRO A 1 300 ? 2.038   10.779  14.970  1.00 20.60 ? 279 PRO A C     1 
ATOM   2025 O  O     . PRO A 1 300 ? 2.140   9.538   14.835  1.00 18.23 ? 279 PRO A O     1 
ATOM   2026 C  CB    . PRO A 1 300 ? -0.083  11.443  16.069  1.00 20.85 ? 279 PRO A CB    1 
ATOM   2027 C  CG    . PRO A 1 300 ? -1.459  10.874  15.716  1.00 24.23 ? 279 PRO A CG    1 
ATOM   2028 C  CD    . PRO A 1 300 ? -1.361  10.174  14.383  1.00 21.44 ? 279 PRO A CD    1 
ATOM   2029 N  N     . PRO A 1 301 ? 3.109   11.553  15.262  1.00 17.26 ? 280 PRO A N     1 
ATOM   2030 C  CA    . PRO A 1 301 ? 4.461   11.012  15.210  1.00 17.13 ? 280 PRO A CA    1 
ATOM   2031 C  C     . PRO A 1 301 ? 4.693   9.923   16.260  1.00 17.83 ? 280 PRO A C     1 
ATOM   2032 O  O     . PRO A 1 301 ? 5.491   9.014   15.986  1.00 17.26 ? 280 PRO A O     1 
ATOM   2033 C  CB    . PRO A 1 301 ? 5.349   12.222  15.502  1.00 18.78 ? 280 PRO A CB    1 
ATOM   2034 C  CG    . PRO A 1 301 ? 4.437   13.244  16.147  1.00 19.09 ? 280 PRO A CG    1 
ATOM   2035 C  CD    . PRO A 1 301 ? 3.084   13.002  15.514  1.00 19.07 ? 280 PRO A CD    1 
ATOM   2036 N  N     . GLN A 1 302 ? 4.060   10.010  17.436  1.00 16.92 ? 281 GLN A N     1 
ATOM   2037 C  CA    . GLN A 1 302 ? 4.256   8.952   18.450  1.00 17.30 ? 281 GLN A CA    1 
ATOM   2038 C  C     . GLN A 1 302 ? 3.749   7.614   17.885  1.00 16.59 ? 281 GLN A C     1 
ATOM   2039 O  O     . GLN A 1 302 ? 4.448   6.569   18.131  1.00 15.72 ? 281 GLN A O     1 
ATOM   2040 C  CB    . GLN A 1 302 ? 3.585   9.247   19.772  1.00 16.94 ? 281 GLN A CB    1 
ATOM   2041 C  CG    . GLN A 1 302 ? 3.863   8.191   20.835  1.00 15.63 ? 281 GLN A CG    1 
ATOM   2042 C  CD    . GLN A 1 302 ? 3.090   8.525   22.091  1.00 19.55 ? 281 GLN A CD    1 
ATOM   2043 O  OE1   . GLN A 1 302 ? 1.958   8.956   22.007  1.00 19.24 ? 281 GLN A OE1   1 
ATOM   2044 N  NE2   . GLN A 1 302 ? 3.667   8.267   23.253  1.00 18.81 ? 281 GLN A NE2   1 
ATOM   2045 N  N     . ARG A 1 303 ? 2.612   7.619   17.177  1.00 17.27 ? 282 ARG A N     1 
ATOM   2046 C  CA    . ARG A 1 303 ? 2.040   6.346   16.625  1.00 17.70 ? 282 ARG A CA    1 
ATOM   2047 C  C     . ARG A 1 303 ? 2.901   5.866   15.456  1.00 17.36 ? 282 ARG A C     1 
ATOM   2048 O  O     . ARG A 1 303 ? 3.185   4.652   15.384  1.00 17.45 ? 282 ARG A O     1 
ATOM   2049 C  CB    . ARG A 1 303 ? 0.567   6.416   16.185  1.00 22.12 ? 282 ARG A CB    1 
ATOM   2050 C  CG    . ARG A 1 303 ? 0.027   4.997   15.936  1.00 25.30 ? 282 ARG A CG    1 
ATOM   2051 C  CD    . ARG A 1 303 ? -1.453  4.676   16.016  1.00 27.91 ? 282 ARG A CD    1 
ATOM   2052 N  NE    . ARG A 1 303 ? -1.722  3.333   16.569  1.00 30.20 ? 282 ARG A NE    1 
ATOM   2053 C  CZ    . ARG A 1 303 ? -1.732  2.200   15.884  1.00 30.73 ? 282 ARG A CZ    1 
ATOM   2054 N  NH1   . ARG A 1 303 ? -1.987  1.053   16.488  1.00 36.39 ? 282 ARG A NH1   1 
ATOM   2055 N  NH2   . ARG A 1 303 ? -1.584  2.199   14.582  1.00 31.28 ? 282 ARG A NH2   1 
ATOM   2056 N  N     . ASP A 1 304 ? 3.299   6.737   14.516  1.00 16.48 ? 283 ASP A N     1 
ATOM   2057 C  CA    . ASP A 1 304 ? 4.195   6.286   13.426  1.00 16.30 ? 283 ASP A CA    1 
ATOM   2058 C  C     . ASP A 1 304 ? 5.467   5.653   14.010  1.00 16.41 ? 283 ASP A C     1 
ATOM   2059 O  O     . ASP A 1 304 ? 5.851   4.541   13.583  1.00 17.43 ? 283 ASP A O     1 
ATOM   2060 C  CB    . ASP A 1 304 ? 4.571   7.412   12.463  1.00 18.11 ? 283 ASP A CB    1 
ATOM   2061 C  CG    . ASP A 1 304 ? 5.184   6.837   11.206  1.00 19.73 ? 283 ASP A CG    1 
ATOM   2062 O  OD1   . ASP A 1 304 ? 4.402   6.388   10.311  1.00 22.52 ? 283 ASP A OD1   1 
ATOM   2063 O  OD2   . ASP A 1 304 ? 6.394   6.738   11.166  1.00 18.59 ? 283 ASP A OD2   1 
ATOM   2064 N  N     . GLN A 1 305 ? 6.110   6.281   14.992  1.00 15.95 ? 284 GLN A N     1 
ATOM   2065 C  CA    . GLN A 1 305 ? 7.379   5.741   15.539  1.00 15.78 ? 284 GLN A CA    1 
ATOM   2066 C  C     . GLN A 1 305 ? 7.100   4.505   16.400  1.00 14.50 ? 284 GLN A C     1 
ATOM   2067 O  O     . GLN A 1 305 ? 7.940   3.558   16.370  1.00 16.21 ? 284 GLN A O     1 
ATOM   2068 C  CB    . GLN A 1 305 ? 8.175   6.854   16.218  1.00 16.16 ? 284 GLN A CB    1 
ATOM   2069 C  CG    . GLN A 1 305 ? 8.627   7.894   15.217  1.00 16.10 ? 284 GLN A CG    1 
ATOM   2070 C  CD    . GLN A 1 305 ? 9.871   8.649   15.651  1.00 19.58 ? 284 GLN A CD    1 
ATOM   2071 O  OE1   . GLN A 1 305 ? 10.843  8.840   14.895  1.00 21.91 ? 284 GLN A OE1   1 
ATOM   2072 N  NE2   . GLN A 1 305 ? 9.854   9.076   16.879  1.00 18.20 ? 284 GLN A NE2   1 
ATOM   2073 N  N     . LEU A 1 306 ? 5.929   4.410   17.016  1.00 15.23 ? 285 LEU A N     1 
ATOM   2074 C  CA    . LEU A 1 306 ? 5.585   3.134   17.692  1.00 14.61 ? 285 LEU A CA    1 
ATOM   2075 C  C     . LEU A 1 306 ? 5.657   2.000   16.662  1.00 14.82 ? 285 LEU A C     1 
ATOM   2076 O  O     . LEU A 1 306 ? 6.281   0.941   16.970  1.00 15.70 ? 285 LEU A O     1 
ATOM   2077 C  CB    . LEU A 1 306 ? 4.204   3.177   18.321  1.00 14.93 ? 285 LEU A CB    1 
ATOM   2078 C  CG    . LEU A 1 306 ? 3.749   1.826   18.891  1.00 16.20 ? 285 LEU A CG    1 
ATOM   2079 C  CD1   . LEU A 1 306 ? 4.743   1.275   19.909  1.00 16.84 ? 285 LEU A CD1   1 
ATOM   2080 C  CD2   . LEU A 1 306 ? 2.371   1.937   19.481  1.00 16.76 ? 285 LEU A CD2   1 
ATOM   2081 N  N     . LEU A 1 307 ? 5.059   2.173   15.489  1.00 15.83 ? 286 LEU A N     1 
ATOM   2082 C  CA    . LEU A 1 307 ? 5.000   1.020   14.523  1.00 16.02 ? 286 LEU A CA    1 
ATOM   2083 C  C     . LEU A 1 307 ? 6.416   0.709   14.014  1.00 17.65 ? 286 LEU A C     1 
ATOM   2084 O  O     . LEU A 1 307 ? 6.763   -0.496  13.859  1.00 19.64 ? 286 LEU A O     1 
ATOM   2085 C  CB    . LEU A 1 307 ? 4.004   1.335   13.407  1.00 17.62 ? 286 LEU A CB    1 
ATOM   2086 C  CG    . LEU A 1 307 ? 2.584   1.728   13.859  1.00 17.13 ? 286 LEU A CG    1 
ATOM   2087 C  CD1   . LEU A 1 307 ? 1.747   2.206   12.674  1.00 17.84 ? 286 LEU A CD1   1 
ATOM   2088 C  CD2   . LEU A 1 307 ? 1.902   0.610   14.626  1.00 17.14 ? 286 LEU A CD2   1 
ATOM   2089 N  N     . GLN A 1 308 ? 7.287   1.719   13.877  1.00 15.95 ? 287 GLN A N     1 
ATOM   2090 C  CA    . GLN A 1 308 ? 8.716   1.550   13.564  1.00 15.21 ? 287 GLN A CA    1 
ATOM   2091 C  C     . GLN A 1 308 ? 9.403   0.694   14.654  1.00 16.04 ? 287 GLN A C     1 
ATOM   2092 O  O     . GLN A 1 308 ? 10.411  -0.002  14.304  1.00 18.09 ? 287 GLN A O     1 
ATOM   2093 C  CB    . GLN A 1 308 ? 9.398   2.916   13.455  1.00 16.43 ? 287 GLN A CB    1 
ATOM   2094 C  CG    . GLN A 1 308 ? 8.905   3.731   12.249  1.00 16.63 ? 287 GLN A CG    1 
ATOM   2095 C  CD    . GLN A 1 308 ? 9.801   4.932   12.112  1.00 17.43 ? 287 GLN A CD    1 
ATOM   2096 O  OE1   . GLN A 1 308 ? 11.003  4.795   12.273  1.00 19.02 ? 287 GLN A OE1   1 
ATOM   2097 N  NE2   . GLN A 1 308 ? 9.231   6.108   11.874  1.00 17.36 ? 287 GLN A NE2   1 
ATOM   2098 N  N     . HIS A 1 309 ? 8.857   0.667   15.876  1.00 16.08 ? 288 HIS A N     1 
ATOM   2099 C  CA    . HIS A 1 309 ? 9.428   -0.016  17.076  1.00 16.84 ? 288 HIS A CA    1 
ATOM   2100 C  C     . HIS A 1 309 ? 8.619   -1.269  17.430  1.00 18.15 ? 288 HIS A C     1 
ATOM   2101 O  O     . HIS A 1 309 ? 8.813   -1.801  18.553  1.00 18.70 ? 288 HIS A O     1 
ATOM   2102 C  CB    . HIS A 1 309 ? 9.502   0.979   18.276  1.00 17.89 ? 288 HIS A CB    1 
ATOM   2103 C  CG    . HIS A 1 309 ? 10.580  2.013   18.163  1.00 20.77 ? 288 HIS A CG    1 
ATOM   2104 N  ND1   . HIS A 1 309 ? 11.938  1.741   18.450  1.00 22.87 ? 288 HIS A ND1   1 
ATOM   2105 C  CD2   . HIS A 1 309 ? 10.534  3.311   17.803  1.00 19.86 ? 288 HIS A CD2   1 
ATOM   2106 C  CE1   . HIS A 1 309 ? 12.651  2.841   18.251  1.00 19.08 ? 288 HIS A CE1   1 
ATOM   2107 N  NE2   . HIS A 1 309 ? 11.812  3.815   17.866  1.00 19.08 ? 288 HIS A NE2   1 
ATOM   2108 N  N     . MET A 1 310 ? 7.802   -1.809  16.505  1.00 17.43 ? 289 MET A N     1 
ATOM   2109 C  CA    . MET A 1 310 ? 7.035   -3.058  16.749  1.00 16.92 ? 289 MET A CA    1 
ATOM   2110 C  C     . MET A 1 310 ? 7.349   -4.062  15.645  1.00 15.63 ? 289 MET A C     1 
ATOM   2111 O  O     . MET A 1 310 ? 6.462   -4.507  14.918  1.00 16.80 ? 289 MET A O     1 
ATOM   2112 C  CB    . MET A 1 310 ? 5.534   -2.806  16.821  1.00 17.34 ? 289 MET A CB    1 
ATOM   2113 C  CG    . MET A 1 310 ? 5.145   -1.987  18.032  1.00 18.95 ? 289 MET A CG    1 
ATOM   2114 S  SD    . MET A 1 310 ? 3.368   -1.743  18.162  1.00 19.79 ? 289 MET A SD    1 
ATOM   2115 C  CE    . MET A 1 310 ? 2.779   -3.325  18.793  1.00 19.74 ? 289 MET A CE    1 
ATOM   2116 N  N     . PRO A 1 311 ? 8.622   -4.481  15.504  1.00 17.19 ? 290 PRO A N     1 
ATOM   2117 C  CA    . PRO A 1 311 ? 8.970   -5.460  14.468  1.00 16.66 ? 290 PRO A CA    1 
ATOM   2118 C  C     . PRO A 1 311 ? 8.262   -6.803  14.674  1.00 17.60 ? 290 PRO A C     1 
ATOM   2119 O  O     . PRO A 1 311 ? 8.142   -7.219  15.772  1.00 19.02 ? 290 PRO A O     1 
ATOM   2120 C  CB    . PRO A 1 311 ? 10.471  -5.591  14.592  1.00 18.09 ? 290 PRO A CB    1 
ATOM   2121 C  CG    . PRO A 1 311 ? 10.732  -5.239  16.040  1.00 18.78 ? 290 PRO A CG    1 
ATOM   2122 C  CD    . PRO A 1 311 ? 9.776   -4.095  16.327  1.00 17.54 ? 290 PRO A CD    1 
ATOM   2123 N  N     . GLN A 1 312 ? 7.843   -7.475  13.594  1.00 18.43 ? 291 GLN A N     1 
ATOM   2124 C  CA    . GLN A 1 312 ? 7.316   -8.853  13.695  1.00 18.78 ? 291 GLN A CA    1 
ATOM   2125 C  C     . GLN A 1 312 ? 8.468   -9.830  13.985  1.00 18.58 ? 291 GLN A C     1 
ATOM   2126 O  O     . GLN A 1 312 ? 9.633   -9.613  13.563  1.00 15.90 ? 291 GLN A O     1 
ATOM   2127 C  CB    . GLN A 1 312 ? 6.616   -9.313  12.419  1.00 20.32 ? 291 GLN A CB    1 
ATOM   2128 C  CG    . GLN A 1 312 ? 5.443   -8.480  11.919  1.00 21.51 ? 291 GLN A CG    1 
ATOM   2129 C  CD    . GLN A 1 312 ? 4.243   -8.603  12.805  1.00 26.68 ? 291 GLN A CD    1 
ATOM   2130 O  OE1   . GLN A 1 312 ? 3.918   -7.663  13.559  1.00 26.83 ? 291 GLN A OE1   1 
ATOM   2131 N  NE2   . GLN A 1 312 ? 3.620   -9.789  12.781  1.00 27.62 ? 291 GLN A NE2   1 
ATOM   2132 N  N     . GLY A 1 313 ? 8.121   -10.919 14.671  1.00 16.68 ? 292 GLY A N     1 
ATOM   2133 C  CA    . GLY A 1 313 ? 9.012   -12.085 14.856  1.00 17.49 ? 292 GLY A CA    1 
ATOM   2134 C  C     . GLY A 1 313 ? 9.436   -12.751 13.551  1.00 16.57 ? 292 GLY A C     1 
ATOM   2135 O  O     . GLY A 1 313 ? 9.025   -12.308 12.467  1.00 15.11 ? 292 GLY A O     1 
ATOM   2136 N  N     . SER A 1 314 ? 10.316  -13.734 13.643  1.00 14.21 ? 293 SER A N     1 
ATOM   2137 C  CA    . SER A 1 314 ? 10.874  -14.490 12.505  1.00 14.94 ? 293 SER A CA    1 
ATOM   2138 C  C     . SER A 1 314 ? 10.605  -15.968 12.756  1.00 15.59 ? 293 SER A C     1 
ATOM   2139 O  O     . SER A 1 314 ? 11.149  -16.473 13.728  1.00 16.56 ? 293 SER A O     1 
ATOM   2140 C  CB    . SER A 1 314 ? 12.366  -14.192 12.341  1.00 18.11 ? 293 SER A CB    1 
ATOM   2141 O  OG    . SER A 1 314 ? 12.571  -12.792 12.092  1.00 17.66 ? 293 SER A OG    1 
ATOM   2142 N  N     . VAL A 1 315 ? 9.785   -16.624 11.932  1.00 15.00 ? 294 VAL A N     1 
ATOM   2143 C  CA    . VAL A 1 315 ? 9.489   -18.065 12.131  1.00 16.51 ? 294 VAL A CA    1 
ATOM   2144 C  C     . VAL A 1 315 ? 9.201   -18.708 10.771  1.00 15.67 ? 294 VAL A C     1 
ATOM   2145 O  O     . VAL A 1 315 ? 8.505   -18.138 9.899   1.00 15.93 ? 294 VAL A O     1 
ATOM   2146 C  CB    . VAL A 1 315 ? 8.381   -18.314 13.172  1.00 18.91 ? 294 VAL A CB    1 
ATOM   2147 C  CG1   . VAL A 1 315 ? 7.092   -17.609 12.844  1.00 18.51 ? 294 VAL A CG1   1 
ATOM   2148 C  CG2   . VAL A 1 315 ? 8.119   -19.795 13.371  1.00 20.81 ? 294 VAL A CG2   1 
ATOM   2149 N  N     . VAL A 1 316 ? 9.839   -19.837 10.564  1.00 13.79 ? 295 VAL A N     1 
ATOM   2150 C  CA    . VAL A 1 316 ? 9.454   -20.785 9.487   1.00 14.33 ? 295 VAL A CA    1 
ATOM   2151 C  C     . VAL A 1 316 ? 8.803   -21.962 10.181  1.00 14.33 ? 295 VAL A C     1 
ATOM   2152 O  O     . VAL A 1 316 ? 9.465   -22.644 10.997  1.00 15.31 ? 295 VAL A O     1 
ATOM   2153 C  CB    . VAL A 1 316 ? 10.654  -21.226 8.627   1.00 14.29 ? 295 VAL A CB    1 
ATOM   2154 C  CG1   . VAL A 1 316 ? 10.178  -22.161 7.528   1.00 14.09 ? 295 VAL A CG1   1 
ATOM   2155 C  CG2   . VAL A 1 316 ? 11.393  -20.043 8.009   1.00 15.64 ? 295 VAL A CG2   1 
ATOM   2156 N  N     . LYS A 1 317 ? 7.557   -22.246 9.827   1.00 15.70 ? 296 LYS A N     1 
ATOM   2157 C  CA    . LYS A 1 317 ? 6.826   -23.386 10.423  1.00 14.15 ? 296 LYS A CA    1 
ATOM   2158 C  C     . LYS A 1 317 ? 6.795   -24.509 9.395   1.00 13.94 ? 296 LYS A C     1 
ATOM   2159 O  O     . LYS A 1 317 ? 6.510   -24.266 8.222   1.00 14.02 ? 296 LYS A O     1 
ATOM   2160 C  CB    . LYS A 1 317 ? 5.396   -22.987 10.770  1.00 14.16 ? 296 LYS A CB    1 
ATOM   2161 C  CG    . LYS A 1 317 ? 4.563   -24.108 11.368  1.00 14.71 ? 296 LYS A CG    1 
ATOM   2162 C  CD    . LYS A 1 317 ? 3.211   -23.672 11.879  1.00 16.99 ? 296 LYS A CD    1 
ATOM   2163 C  CE    . LYS A 1 317 ? 2.459   -24.849 12.447  1.00 16.02 ? 296 LYS A CE    1 
ATOM   2164 N  NZ    . LYS A 1 317 ? 1.151   -24.433 13.013  1.00 15.45 ? 296 LYS A NZ    1 
ATOM   2165 N  N     . PHE A 1 318 ? 7.048   -25.724 9.844   1.00 14.32 ? 297 PHE A N     1 
ATOM   2166 C  CA    . PHE A 1 318 ? 7.057   -26.889 8.935   1.00 14.75 ? 297 PHE A CA    1 
ATOM   2167 C  C     . PHE A 1 318 ? 6.244   -28.042 9.498   1.00 14.62 ? 297 PHE A C     1 
ATOM   2168 O  O     . PHE A 1 318 ? 6.054   -28.179 10.716  1.00 15.49 ? 297 PHE A O     1 
ATOM   2169 C  CB    . PHE A 1 318 ? 8.492   -27.303 8.630   1.00 15.29 ? 297 PHE A CB    1 
ATOM   2170 C  CG    . PHE A 1 318 ? 9.298   -27.745 9.825   1.00 15.22 ? 297 PHE A CG    1 
ATOM   2171 C  CD1   . PHE A 1 318 ? 10.223  -26.908 10.426  1.00 17.19 ? 297 PHE A CD1   1 
ATOM   2172 C  CD2   . PHE A 1 318 ? 9.083   -28.991 10.392  1.00 17.08 ? 297 PHE A CD2   1 
ATOM   2173 C  CE1   . PHE A 1 318 ? 10.918  -27.335 11.542  1.00 16.95 ? 297 PHE A CE1   1 
ATOM   2174 C  CE2   . PHE A 1 318 ? 9.811   -29.424 11.487  1.00 17.46 ? 297 PHE A CE2   1 
ATOM   2175 C  CZ    . PHE A 1 318 ? 10.695  -28.580 12.079  1.00 17.90 ? 297 PHE A CZ    1 
ATOM   2176 N  N     . HIS A 1 319 ? 5.861   -28.919 8.568   1.00 15.89 ? 298 HIS A N     1 
ATOM   2177 C  CA    . HIS A 1 319 ? 5.185   -30.209 8.820   1.00 15.96 ? 298 HIS A CA    1 
ATOM   2178 C  C     . HIS A 1 319 ? 5.902   -31.258 7.969   1.00 14.97 ? 298 HIS A C     1 
ATOM   2179 O  O     . HIS A 1 319 ? 5.986   -31.116 6.738   1.00 16.07 ? 298 HIS A O     1 
ATOM   2180 C  CB    . HIS A 1 319 ? 3.688   -30.162 8.502   1.00 15.54 ? 298 HIS A CB    1 
ATOM   2181 C  CG    . HIS A 1 319 ? 2.900   -29.189 9.301   1.00 17.43 ? 298 HIS A CG    1 
ATOM   2182 N  ND1   . HIS A 1 319 ? 2.290   -29.532 10.496  1.00 16.89 ? 298 HIS A ND1   1 
ATOM   2183 C  CD2   . HIS A 1 319 ? 2.548   -27.913 9.038   1.00 18.20 ? 298 HIS A CD2   1 
ATOM   2184 C  CE1   . HIS A 1 319 ? 1.628   -28.465 10.964  1.00 18.24 ? 298 HIS A CE1   1 
ATOM   2185 N  NE2   . HIS A 1 319 ? 1.786   -27.458 10.090  1.00 17.93 ? 298 HIS A NE2   1 
ATOM   2186 N  N     . VAL A 1 320 ? 6.534   -32.217 8.619   1.00 15.52 ? 299 VAL A N     1 
ATOM   2187 C  CA    . VAL A 1 320 ? 7.214   -33.338 7.902   1.00 15.56 ? 299 VAL A CA    1 
ATOM   2188 C  C     . VAL A 1 320 ? 6.205   -34.476 7.849   1.00 16.25 ? 299 VAL A C     1 
ATOM   2189 O  O     . VAL A 1 320 ? 5.697   -34.865 8.950   1.00 15.96 ? 299 VAL A O     1 
ATOM   2190 C  CB    . VAL A 1 320 ? 8.506   -33.771 8.619   1.00 16.82 ? 299 VAL A CB    1 
ATOM   2191 C  CG1   . VAL A 1 320 ? 9.284   -34.719 7.722   1.00 19.04 ? 299 VAL A CG1   1 
ATOM   2192 C  CG2   . VAL A 1 320 ? 9.368   -32.619 9.062   1.00 18.18 ? 299 VAL A CG2   1 
ATOM   2193 N  N     . ILE A 1 321 ? 5.910   -35.004 6.656   1.00 17.97 ? 300 ILE A N     1 
ATOM   2194 C  CA    . ILE A 1 321 ? 4.818   -35.991 6.454   1.00 18.80 ? 300 ILE A CA    1 
ATOM   2195 C  C     . ILE A 1 321 ? 5.411   -37.377 6.230   1.00 19.36 ? 300 ILE A C     1 
ATOM   2196 O  O     . ILE A 1 321 ? 6.334   -37.507 5.398   1.00 19.63 ? 300 ILE A O     1 
ATOM   2197 C  CB    . ILE A 1 321 ? 3.926   -35.629 5.262   1.00 19.99 ? 300 ILE A CB    1 
ATOM   2198 C  CG1   . ILE A 1 321 ? 3.547   -34.151 5.241   1.00 21.59 ? 300 ILE A CG1   1 
ATOM   2199 C  CG2   . ILE A 1 321 ? 2.727   -36.538 5.258   1.00 20.43 ? 300 ILE A CG2   1 
ATOM   2200 C  CD1   . ILE A 1 321 ? 2.886   -33.674 6.482   1.00 21.80 ? 300 ILE A CD1   1 
ATOM   2201 N  N     . TYR A 1 322 ? 4.884   -38.356 6.963   1.00 19.13 ? 301 TYR A N     1 
ATOM   2202 C  CA    . TYR A 1 322 ? 5.237   -39.784 6.841   1.00 19.81 ? 301 TYR A CA    1 
ATOM   2203 C  C     . TYR A 1 322 ? 3.947   -40.584 6.628   1.00 20.96 ? 301 TYR A C     1 
ATOM   2204 O  O     . TYR A 1 322 ? 2.854   -40.124 6.940   1.00 20.24 ? 301 TYR A O     1 
ATOM   2205 C  CB    . TYR A 1 322 ? 5.962   -40.242 8.112   1.00 20.28 ? 301 TYR A CB    1 
ATOM   2206 C  CG    . TYR A 1 322 ? 7.278   -39.543 8.352   1.00 19.85 ? 301 TYR A CG    1 
ATOM   2207 C  CD1   . TYR A 1 322 ? 8.448   -40.017 7.787   1.00 20.37 ? 301 TYR A CD1   1 
ATOM   2208 C  CD2   . TYR A 1 322 ? 7.356   -38.400 9.125   1.00 18.65 ? 301 TYR A CD2   1 
ATOM   2209 C  CE1   . TYR A 1 322 ? 9.662   -39.379 8.001   1.00 21.22 ? 301 TYR A CE1   1 
ATOM   2210 C  CE2   . TYR A 1 322 ? 8.553   -37.741 9.341   1.00 18.05 ? 301 TYR A CE2   1 
ATOM   2211 C  CZ    . TYR A 1 322 ? 9.711   -38.222 8.769   1.00 19.08 ? 301 TYR A CZ    1 
ATOM   2212 O  OH    . TYR A 1 322 ? 10.889  -37.557 8.963   1.00 20.06 ? 301 TYR A OH    1 
ATOM   2213 N  N     . ASP A 1 323 ? 4.057   -41.788 6.081   1.00 20.83 ? 302 ASP A N     1 
ATOM   2214 C  CA    . ASP A 1 323 ? 2.851   -42.619 5.864   1.00 24.15 ? 302 ASP A CA    1 
ATOM   2215 C  C     . ASP A 1 323 ? 2.196   -42.942 7.214   1.00 22.91 ? 302 ASP A C     1 
ATOM   2216 O  O     . ASP A 1 323 ? 0.951   -43.035 7.253   1.00 22.84 ? 302 ASP A O     1 
ATOM   2217 C  CB    . ASP A 1 323 ? 3.211   -43.860 5.040   1.00 27.71 ? 302 ASP A CB    1 
ATOM   2218 C  CG    . ASP A 1 323 ? 3.740   -43.589 3.633   1.00 32.88 ? 302 ASP A CG    1 
ATOM   2219 O  OD1   . ASP A 1 323 ? 3.448   -42.527 3.043   1.00 36.30 ? 302 ASP A OD1   1 
ATOM   2220 O  OD2   . ASP A 1 323 ? 4.431   -44.477 3.122   1.00 37.50 ? 302 ASP A OD2   1 
ATOM   2221 N  N     . GLU A 1 324 ? 2.977   -43.081 8.287   1.00 22.39 ? 303 GLU A N     1 
ATOM   2222 C  CA    . GLU A 1 324 ? 2.494   -43.444 9.641   1.00 24.22 ? 303 GLU A CA    1 
ATOM   2223 C  C     . GLU A 1 324 ? 3.324   -42.706 10.678  1.00 22.52 ? 303 GLU A C     1 
ATOM   2224 O  O     . GLU A 1 324 ? 4.447   -42.349 10.390  1.00 20.99 ? 303 GLU A O     1 
ATOM   2225 C  CB    . GLU A 1 324 ? 2.692   -44.940 9.887   1.00 32.67 ? 303 GLU A CB    1 
ATOM   2226 C  CG    . GLU A 1 324 ? 2.242   -45.774 8.711   1.00 44.26 ? 303 GLU A CG    1 
ATOM   2227 C  CD    . GLU A 1 324 ? 1.873   -47.188 9.081   1.00 52.72 ? 303 GLU A CD    1 
ATOM   2228 O  OE1   . GLU A 1 324 ? 0.668   -47.527 8.991   1.00 62.53 ? 303 GLU A OE1   1 
ATOM   2229 O  OE2   . GLU A 1 324 ? 2.785   -47.925 9.475   1.00 61.26 ? 303 GLU A OE2   1 
ATOM   2230 N  N     . PRO A 1 325 ? 2.782   -42.453 11.884  1.00 20.00 ? 304 PRO A N     1 
ATOM   2231 C  CA    . PRO A 1 325 ? 3.544   -41.882 13.011  1.00 19.16 ? 304 PRO A CA    1 
ATOM   2232 C  C     . PRO A 1 325 ? 4.370   -43.002 13.641  1.00 19.58 ? 304 PRO A C     1 
ATOM   2233 O  O     . PRO A 1 325 ? 4.012   -43.490 14.722  1.00 20.07 ? 304 PRO A O     1 
ATOM   2234 C  CB    . PRO A 1 325 ? 2.439   -41.357 13.934  1.00 19.25 ? 304 PRO A CB    1 
ATOM   2235 C  CG    . PRO A 1 325 ? 1.276   -42.282 13.685  1.00 19.16 ? 304 PRO A CG    1 
ATOM   2236 C  CD    . PRO A 1 325 ? 1.369   -42.677 12.231  1.00 20.15 ? 304 PRO A CD    1 
ATOM   2237 N  N     . TRP A 1 326 ? 5.403   -43.421 12.894  1.00 21.10 ? 305 TRP A N     1 
ATOM   2238 C  CA    . TRP A 1 326 ? 6.276   -44.586 13.178  1.00 20.78 ? 305 TRP A CA    1 
ATOM   2239 C  C     . TRP A 1 326 ? 6.969   -44.434 14.533  1.00 21.57 ? 305 TRP A C     1 
ATOM   2240 O  O     . TRP A 1 326 ? 7.247   -45.479 15.192  1.00 24.02 ? 305 TRP A O     1 
ATOM   2241 C  CB    . TRP A 1 326 ? 7.262   -44.778 12.021  1.00 22.19 ? 305 TRP A CB    1 
ATOM   2242 C  CG    . TRP A 1 326 ? 8.098   -43.566 11.744  1.00 19.37 ? 305 TRP A CG    1 
ATOM   2243 C  CD1   . TRP A 1 326 ? 7.886   -42.648 10.766  1.00 20.88 ? 305 TRP A CD1   1 
ATOM   2244 C  CD2   . TRP A 1 326 ? 9.262   -43.118 12.456  1.00 21.87 ? 305 TRP A CD2   1 
ATOM   2245 N  NE1   . TRP A 1 326 ? 8.834   -41.660 10.820  1.00 22.11 ? 305 TRP A NE1   1 
ATOM   2246 C  CE2   . TRP A 1 326 ? 9.729   -41.956 11.799  1.00 22.91 ? 305 TRP A CE2   1 
ATOM   2247 C  CE3   . TRP A 1 326 ? 10.012  -43.630 13.524  1.00 24.33 ? 305 TRP A CE3   1 
ATOM   2248 C  CZ2   . TRP A 1 326 ? 10.852  -41.255 12.240  1.00 25.76 ? 305 TRP A CZ2   1 
ATOM   2249 C  CZ3   . TRP A 1 326 ? 11.131  -42.952 13.946  1.00 24.69 ? 305 TRP A CZ3   1 
ATOM   2250 C  CH2   . TRP A 1 326 ? 11.519  -41.761 13.337  1.00 25.03 ? 305 TRP A CH2   1 
ATOM   2251 N  N     . TRP A 1 327 ? 7.190   -43.211 15.007  1.00 21.57 ? 306 TRP A N     1 
ATOM   2252 C  CA    . TRP A 1 327 ? 7.838   -42.972 16.320  1.00 22.64 ? 306 TRP A CA    1 
ATOM   2253 C  C     . TRP A 1 327 ? 6.989   -43.571 17.464  1.00 23.14 ? 306 TRP A C     1 
ATOM   2254 O  O     . TRP A 1 327 ? 7.584   -43.976 18.471  1.00 25.03 ? 306 TRP A O     1 
ATOM   2255 C  CB    . TRP A 1 327 ? 8.116   -41.471 16.559  1.00 20.58 ? 306 TRP A CB    1 
ATOM   2256 C  CG    . TRP A 1 327 ? 6.949   -40.589 16.249  1.00 19.31 ? 306 TRP A CG    1 
ATOM   2257 C  CD1   . TRP A 1 327 ? 5.999   -40.145 17.124  1.00 17.96 ? 306 TRP A CD1   1 
ATOM   2258 C  CD2   . TRP A 1 327 ? 6.613   -40.030 14.969  1.00 17.96 ? 306 TRP A CD2   1 
ATOM   2259 N  NE1   . TRP A 1 327 ? 5.103   -39.357 16.472  1.00 20.80 ? 306 TRP A NE1   1 
ATOM   2260 C  CE2   . TRP A 1 327 ? 5.434   -39.278 15.152  1.00 18.75 ? 306 TRP A CE2   1 
ATOM   2261 C  CE3   . TRP A 1 327 ? 7.154   -40.140 13.688  1.00 18.28 ? 306 TRP A CE3   1 
ATOM   2262 C  CZ2   . TRP A 1 327 ? 4.832   -38.571 14.116  1.00 18.17 ? 306 TRP A CZ2   1 
ATOM   2263 C  CZ3   . TRP A 1 327 ? 6.543   -39.470 12.651  1.00 19.59 ? 306 TRP A CZ3   1 
ATOM   2264 C  CH2   . TRP A 1 327 ? 5.375   -38.716 12.872  1.00 18.70 ? 306 TRP A CH2   1 
ATOM   2265 N  N     . ARG A 1 328 ? 5.657   -43.587 17.324  1.00 21.95 ? 307 ARG A N     1 
ATOM   2266 C  CA    . ARG A 1 328 ? 4.752   -43.966 18.440  1.00 25.72 ? 307 ARG A CA    1 
ATOM   2267 C  C     . ARG A 1 328 ? 5.008   -45.438 18.783  1.00 27.68 ? 307 ARG A C     1 
ATOM   2268 O  O     . ARG A 1 328 ? 4.933   -45.744 19.951  1.00 27.59 ? 307 ARG A O     1 
ATOM   2269 C  CB    . ARG A 1 328 ? 3.285   -43.756 18.080  1.00 24.41 ? 307 ARG A CB    1 
ATOM   2270 C  CG    . ARG A 1 328 ? 2.886   -42.304 17.854  1.00 24.63 ? 307 ARG A CG    1 
ATOM   2271 C  CD    . ARG A 1 328 ? 1.430   -42.168 17.509  1.00 25.53 ? 307 ARG A CD    1 
ATOM   2272 N  NE    . ARG A 1 328 ? 1.021   -40.766 17.421  1.00 23.24 ? 307 ARG A NE    1 
ATOM   2273 C  CZ    . ARG A 1 328 ? -0.223  -40.380 17.193  1.00 24.69 ? 307 ARG A CZ    1 
ATOM   2274 N  NH1   . ARG A 1 328 ? -1.140  -41.292 16.958  1.00 23.86 ? 307 ARG A NH1   1 
ATOM   2275 N  NH2   . ARG A 1 328 ? -0.540  -39.099 17.112  1.00 24.30 ? 307 ARG A NH2   1 
ATOM   2276 N  N     . ALA A 1 329 ? 5.328   -46.280 17.794  1.00 30.37 ? 308 ALA A N     1 
ATOM   2277 C  CA    . ALA A 1 329 ? 5.565   -47.729 17.999  1.00 34.38 ? 308 ALA A CA    1 
ATOM   2278 C  C     . ALA A 1 329 ? 6.904   -47.939 18.720  1.00 32.74 ? 308 ALA A C     1 
ATOM   2279 O  O     . ALA A 1 329 ? 7.093   -49.034 19.279  1.00 34.03 ? 308 ALA A O     1 
ATOM   2280 C  CB    . ALA A 1 329 ? 5.520   -48.477 16.687  1.00 35.66 ? 308 ALA A CB    1 
ATOM   2281 N  N     . GLU A 1 330 ? 7.777   -46.934 18.761  1.00 28.97 ? 309 GLU A N     1 
ATOM   2282 C  CA    . GLU A 1 330 ? 9.071   -46.989 19.472  1.00 28.83 ? 309 GLU A CA    1 
ATOM   2283 C  C     . GLU A 1 330 ? 8.889   -46.378 20.862  1.00 28.72 ? 309 GLU A C     1 
ATOM   2284 O  O     . GLU A 1 330 ? 9.921   -46.213 21.559  1.00 30.41 ? 309 GLU A O     1 
ATOM   2285 C  CB    . GLU A 1 330 ? 10.182  -46.253 18.705  1.00 30.53 ? 309 GLU A CB    1 
ATOM   2286 C  CG    . GLU A 1 330 ? 10.382  -46.729 17.279  1.00 34.16 ? 309 GLU A CG    1 
ATOM   2287 C  CD    . GLU A 1 330 ? 10.975  -48.117 17.096  1.00 42.57 ? 309 GLU A CD    1 
ATOM   2288 O  OE1   . GLU A 1 330 ? 11.166  -48.513 15.939  1.00 51.04 ? 309 GLU A OE1   1 
ATOM   2289 O  OE2   . GLU A 1 330 ? 11.244  -48.804 18.095  1.00 43.45 ? 309 GLU A OE2   1 
ATOM   2290 N  N     . GLY A 1 331 ? 7.663   -45.967 21.203  1.00 27.13 ? 310 GLY A N     1 
ATOM   2291 C  CA    . GLY A 1 331 ? 7.331   -45.350 22.504  1.00 26.09 ? 310 GLY A CA    1 
ATOM   2292 C  C     . GLY A 1 331 ? 7.834   -43.917 22.608  1.00 26.26 ? 310 GLY A C     1 
ATOM   2293 O  O     . GLY A 1 331 ? 8.075   -43.481 23.724  1.00 26.56 ? 310 GLY A O     1 
ATOM   2294 N  N     . LEU A 1 332 ? 7.959   -43.205 21.475  1.00 23.41 ? 311 LEU A N     1 
ATOM   2295 C  CA    . LEU A 1 332 ? 8.392   -41.788 21.414  1.00 22.82 ? 311 LEU A CA    1 
ATOM   2296 C  C     . LEU A 1 332 ? 7.172   -40.890 21.167  1.00 21.59 ? 311 LEU A C     1 
ATOM   2297 O  O     . LEU A 1 332 ? 6.222   -41.323 20.447  1.00 23.34 ? 311 LEU A O     1 
ATOM   2298 C  CB    . LEU A 1 332 ? 9.432   -41.571 20.302  1.00 23.84 ? 311 LEU A CB    1 
ATOM   2299 C  CG    . LEU A 1 332 ? 10.759  -42.320 20.458  1.00 26.79 ? 311 LEU A CG    1 
ATOM   2300 C  CD1   . LEU A 1 332 ? 11.574  -42.286 19.173  1.00 27.31 ? 311 LEU A CD1   1 
ATOM   2301 C  CD2   . LEU A 1 332 ? 11.559  -41.744 21.608  1.00 28.56 ? 311 LEU A CD2   1 
ATOM   2302 N  N     . SER A 1 333 ? 7.159   -39.727 21.808  1.00 20.80 ? 312 SER A N     1 
ATOM   2303 C  CA    . SER A 1 333 ? 6.106   -38.681 21.668  1.00 19.81 ? 312 SER A CA    1 
ATOM   2304 C  C     . SER A 1 333 ? 6.190   -38.010 20.288  1.00 20.61 ? 312 SER A C     1 
ATOM   2305 O  O     . SER A 1 333 ? 5.191   -37.412 19.869  1.00 19.50 ? 312 SER A O     1 
ATOM   2306 C  CB    . SER A 1 333 ? 6.213   -37.643 22.757  1.00 20.00 ? 312 SER A CB    1 
ATOM   2307 O  OG    . SER A 1 333 ? 7.386   -36.836 22.598  1.00 20.09 ? 312 SER A OG    1 
ATOM   2308 N  N     . GLY A 1 334 ? 7.385   -37.924 19.693  1.00 19.45 ? 313 GLY A N     1 
ATOM   2309 C  CA    . GLY A 1 334 ? 7.619   -37.111 18.483  1.00 19.27 ? 313 GLY A CA    1 
ATOM   2310 C  C     . GLY A 1 334 ? 8.129   -35.723 18.830  1.00 19.31 ? 313 GLY A C     1 
ATOM   2311 O  O     . GLY A 1 334 ? 8.374   -34.911 17.890  1.00 19.96 ? 313 GLY A O     1 
ATOM   2312 N  N     . THR A 1 335 ? 8.277   -35.437 20.111  1.00 20.77 ? 314 THR A N     1 
ATOM   2313 C  CA    . THR A 1 335 ? 8.826   -34.147 20.612  1.00 20.72 ? 314 THR A CA    1 
ATOM   2314 C  C     . THR A 1 335 ? 10.341  -34.294 20.787  1.00 21.31 ? 314 THR A C     1 
ATOM   2315 O  O     . THR A 1 335 ? 10.780  -35.234 21.504  1.00 21.89 ? 314 THR A O     1 
ATOM   2316 C  CB    . THR A 1 335 ? 8.104   -33.676 21.881  1.00 24.74 ? 314 THR A CB    1 
ATOM   2317 O  OG1   . THR A 1 335 ? 6.874   -33.050 21.504  1.00 26.13 ? 314 THR A OG1   1 
ATOM   2318 C  CG2   . THR A 1 335 ? 8.922   -32.639 22.611  1.00 25.54 ? 314 THR A CG2   1 
ATOM   2319 N  N     . VAL A 1 336 ? 11.114  -33.426 20.146  1.00 21.07 ? 315 VAL A N     1 
ATOM   2320 C  CA    . VAL A 1 336 ? 12.587  -33.339 20.349  1.00 21.24 ? 315 VAL A CA    1 
ATOM   2321 C  C     . VAL A 1 336 ? 12.895  -31.949 20.878  1.00 21.50 ? 315 VAL A C     1 
ATOM   2322 O  O     . VAL A 1 336 ? 12.233  -30.980 20.462  1.00 20.94 ? 315 VAL A O     1 
ATOM   2323 C  CB    . VAL A 1 336 ? 13.397  -33.681 19.085  1.00 24.63 ? 315 VAL A CB    1 
ATOM   2324 C  CG1   . VAL A 1 336 ? 12.880  -34.945 18.441  1.00 23.35 ? 315 VAL A CG1   1 
ATOM   2325 C  CG2   . VAL A 1 336 ? 13.401  -32.539 18.093  1.00 26.78 ? 315 VAL A CG2   1 
ATOM   2326 N  N     . LEU A 1 337 ? 13.854  -31.864 21.795  1.00 24.37 ? 316 LEU A N     1 
ATOM   2327 C  CA    . LEU A 1 337 ? 14.354  -30.582 22.355  1.00 27.61 ? 316 LEU A CA    1 
ATOM   2328 C  C     . LEU A 1 337 ? 15.851  -30.562 22.089  1.00 27.10 ? 316 LEU A C     1 
ATOM   2329 O  O     . LEU A 1 337 ? 16.559  -31.421 22.657  1.00 27.41 ? 316 LEU A O     1 
ATOM   2330 C  CB    . LEU A 1 337 ? 14.071  -30.526 23.861  1.00 32.36 ? 316 LEU A CB    1 
ATOM   2331 C  CG    . LEU A 1 337 ? 14.886  -29.475 24.617  1.00 39.70 ? 316 LEU A CG    1 
ATOM   2332 C  CD1   . LEU A 1 337 ? 14.447  -28.089 24.221  1.00 38.11 ? 316 LEU A CD1   1 
ATOM   2333 C  CD2   . LEU A 1 337 ? 14.793  -29.677 26.127  1.00 44.67 ? 316 LEU A CD2   1 
ATOM   2334 N  N     . CYS A 1 338 ? 16.317  -29.632 21.267  1.00 26.71 ? 317 CYS A N     1 
ATOM   2335 C  CA    A CYS A 1 338 ? 17.724  -29.613 20.796  0.50 29.62 ? 317 CYS A CA    1 
ATOM   2336 C  CA    B CYS A 1 338 ? 17.722  -29.633 20.800  0.50 30.01 ? 317 CYS A CA    1 
ATOM   2337 C  C     . CYS A 1 338 ? 18.239  -28.192 20.801  1.00 30.73 ? 317 CYS A C     1 
ATOM   2338 O  O     . CYS A 1 338 ? 18.268  -27.559 19.751  1.00 34.29 ? 317 CYS A O     1 
ATOM   2339 C  CB    A CYS A 1 338 ? 17.853  -30.110 19.368  0.50 28.76 ? 317 CYS A CB    1 
ATOM   2340 C  CB    B CYS A 1 338 ? 17.795  -30.370 19.463  0.50 28.53 ? 317 CYS A CB    1 
ATOM   2341 S  SG    A CYS A 1 338 ? 17.178  -31.757 19.142  0.50 27.05 ? 317 CYS A SG    1 
ATOM   2342 S  SG    B CYS A 1 338 ? 16.414  -30.026 18.336  0.50 31.69 ? 317 CYS A SG    1 
ATOM   2343 N  N     . PRO A 1 339 ? 18.661  -27.656 21.974  1.00 29.64 ? 318 PRO A N     1 
ATOM   2344 C  CA    . PRO A 1 339 ? 19.039  -26.247 22.075  1.00 27.98 ? 318 PRO A CA    1 
ATOM   2345 C  C     . PRO A 1 339 ? 20.169  -25.790 21.125  1.00 26.64 ? 318 PRO A C     1 
ATOM   2346 O  O     . PRO A 1 339 ? 20.253  -24.617 20.881  1.00 29.30 ? 318 PRO A O     1 
ATOM   2347 C  CB    . PRO A 1 339 ? 19.470  -26.067 23.539  1.00 30.81 ? 318 PRO A CB    1 
ATOM   2348 C  CG    . PRO A 1 339 ? 18.880  -27.281 24.272  1.00 33.13 ? 318 PRO A CG    1 
ATOM   2349 C  CD    . PRO A 1 339 ? 18.804  -28.383 23.246  1.00 31.42 ? 318 PRO A CD    1 
ATOM   2350 N  N     . ASP A 1 340 ? 20.997  -26.692 20.623  1.00 23.99 ? 319 ASP A N     1 
ATOM   2351 C  CA    . ASP A 1 340 ? 22.184  -26.358 19.789  1.00 27.92 ? 319 ASP A CA    1 
ATOM   2352 C  C     . ASP A 1 340 ? 21.868  -26.584 18.301  1.00 27.60 ? 319 ASP A C     1 
ATOM   2353 O  O     . ASP A 1 340 ? 22.750  -26.352 17.477  1.00 27.49 ? 319 ASP A O     1 
ATOM   2354 C  CB    . ASP A 1 340 ? 23.431  -27.113 20.271  1.00 28.19 ? 319 ASP A CB    1 
ATOM   2355 C  CG    . ASP A 1 340 ? 23.717  -26.810 21.736  1.00 31.12 ? 319 ASP A CG    1 
ATOM   2356 O  OD1   . ASP A 1 340 ? 23.718  -25.623 22.109  1.00 30.12 ? 319 ASP A OD1   1 
ATOM   2357 O  OD2   . ASP A 1 340 ? 23.797  -27.757 22.524  1.00 32.13 ? 319 ASP A OD2   1 
ATOM   2358 N  N     . GLU A 1 341 ? 20.658  -27.034 17.945  1.00 26.72 ? 320 GLU A N     1 
ATOM   2359 C  CA    . GLU A 1 341 ? 20.293  -27.270 16.527  1.00 23.06 ? 320 GLU A CA    1 
ATOM   2360 C  C     . GLU A 1 341 ? 19.517  -26.067 16.004  1.00 21.66 ? 320 GLU A C     1 
ATOM   2361 O  O     . GLU A 1 341 ? 19.015  -25.283 16.799  1.00 22.75 ? 320 GLU A O     1 
ATOM   2362 C  CB    . GLU A 1 341 ? 19.469  -28.556 16.418  1.00 25.15 ? 320 GLU A CB    1 
ATOM   2363 C  CG    . GLU A 1 341 ? 20.244  -29.807 16.856  1.00 26.95 ? 320 GLU A CG    1 
ATOM   2364 C  CD    . GLU A 1 341 ? 21.362  -30.233 15.926  1.00 30.07 ? 320 GLU A CD    1 
ATOM   2365 O  OE1   . GLU A 1 341 ? 22.282  -30.956 16.389  1.00 29.52 ? 320 GLU A OE1   1 
ATOM   2366 O  OE2   . GLU A 1 341 ? 21.255  -29.925 14.712  1.00 27.98 ? 320 GLU A OE2   1 
ATOM   2367 N  N     . PRO A 1 342 ? 19.342  -25.914 14.673  1.00 22.82 ? 321 PRO A N     1 
ATOM   2368 C  CA    . PRO A 1 342 ? 18.578  -24.798 14.111  1.00 22.98 ? 321 PRO A CA    1 
ATOM   2369 C  C     . PRO A 1 342 ? 17.069  -24.867 14.402  1.00 23.93 ? 321 PRO A C     1 
ATOM   2370 O  O     . PRO A 1 342 ? 16.374  -23.850 14.348  1.00 21.84 ? 321 PRO A O     1 
ATOM   2371 C  CB    . PRO A 1 342 ? 18.800  -24.871 12.590  1.00 27.24 ? 321 PRO A CB    1 
ATOM   2372 C  CG    . PRO A 1 342 ? 19.813  -25.954 12.351  1.00 28.37 ? 321 PRO A CG    1 
ATOM   2373 C  CD    . PRO A 1 342 ? 19.886  -26.785 13.624  1.00 23.93 ? 321 PRO A CD    1 
ATOM   2374 N  N     . ILE A 1 343 ? 16.546  -26.052 14.711  1.00 20.60 ? 322 ILE A N     1 
ATOM   2375 C  CA    . ILE A 1 343 ? 15.095  -26.134 15.002  1.00 23.02 ? 322 ILE A CA    1 
ATOM   2376 C  C     . ILE A 1 343 ? 14.878  -26.188 16.510  1.00 28.56 ? 322 ILE A C     1 
ATOM   2377 O  O     . ILE A 1 343 ? 15.686  -26.741 17.253  1.00 29.48 ? 322 ILE A O     1 
ATOM   2378 C  CB    . ILE A 1 343 ? 14.386  -27.276 14.248  1.00 23.68 ? 322 ILE A CB    1 
ATOM   2379 C  CG1   . ILE A 1 343 ? 14.844  -28.654 14.704  1.00 26.58 ? 322 ILE A CG1   1 
ATOM   2380 C  CG2   . ILE A 1 343 ? 14.541  -27.095 12.752  1.00 25.48 ? 322 ILE A CG2   1 
ATOM   2381 C  CD1   . ILE A 1 343 ? 14.032  -29.780 14.146  1.00 26.45 ? 322 ILE A CD1   1 
ATOM   2382 N  N     . GLY A 1 344 ? 13.750  -25.630 16.912  1.00 30.12 ? 323 GLY A N     1 
ATOM   2383 C  CA    . GLY A 1 344 ? 13.314  -25.691 18.309  1.00 34.57 ? 323 GLY A CA    1 
ATOM   2384 C  C     . GLY A 1 344 ? 12.528  -26.961 18.541  1.00 26.24 ? 323 GLY A C     1 
ATOM   2385 O  O     . GLY A 1 344 ? 12.774  -28.011 17.856  1.00 28.37 ? 323 GLY A O     1 
ATOM   2386 N  N     . VAL A 1 345 ? 11.545  -26.855 19.399  1.00 28.72 ? 324 VAL A N     1 
ATOM   2387 C  CA    . VAL A 1 345 ? 10.848  -28.037 19.924  1.00 25.99 ? 324 VAL A CA    1 
ATOM   2388 C  C     . VAL A 1 345 ? 10.001  -28.576 18.769  1.00 24.62 ? 324 VAL A C     1 
ATOM   2389 O  O     . VAL A 1 345 ? 9.457   -27.760 17.999  1.00 27.73 ? 324 VAL A O     1 
ATOM   2390 C  CB    . VAL A 1 345 ? 10.000  -27.615 21.128  1.00 31.50 ? 324 VAL A CB    1 
ATOM   2391 C  CG1   . VAL A 1 345 ? 9.357   -28.804 21.783  1.00 31.77 ? 324 VAL A CG1   1 
ATOM   2392 C  CG2   . VAL A 1 345 ? 10.819  -26.839 22.145  1.00 38.73 ? 324 VAL A CG2   1 
ATOM   2393 N  N     . THR A 1 346 ? 9.888   -29.886 18.634  1.00 20.28 ? 325 THR A N     1 
ATOM   2394 C  CA    . THR A 1 346 ? 8.925   -30.474 17.687  1.00 17.19 ? 325 THR A CA    1 
ATOM   2395 C  C     . THR A 1 346 ? 7.736   -31.057 18.426  1.00 18.74 ? 325 THR A C     1 
ATOM   2396 O  O     . THR A 1 346 ? 7.805   -31.253 19.643  1.00 18.84 ? 325 THR A O     1 
ATOM   2397 C  CB    . THR A 1 346 ? 9.564   -31.556 16.812  1.00 16.65 ? 325 THR A CB    1 
ATOM   2398 O  OG1   . THR A 1 346 ? 10.004  -32.628 17.654  1.00 17.92 ? 325 THR A OG1   1 
ATOM   2399 C  CG2   . THR A 1 346 ? 10.688  -30.989 15.986  1.00 17.06 ? 325 THR A CG2   1 
ATOM   2400 N  N     . PHE A 1 347 ? 6.689   -31.338 17.658  1.00 18.81 ? 326 PHE A N     1 
ATOM   2401 C  CA    . PHE A 1 347 ? 5.419   -31.871 18.176  1.00 16.87 ? 326 PHE A CA    1 
ATOM   2402 C  C     . PHE A 1 347 ? 4.908   -32.929 17.191  1.00 17.98 ? 326 PHE A C     1 
ATOM   2403 O  O     . PHE A 1 347 ? 4.993   -32.757 16.002  1.00 18.36 ? 326 PHE A O     1 
ATOM   2404 C  CB    . PHE A 1 347 ? 4.369   -30.779 18.330  1.00 17.74 ? 326 PHE A CB    1 
ATOM   2405 C  CG    . PHE A 1 347 ? 4.662   -29.766 19.397  1.00 19.18 ? 326 PHE A CG    1 
ATOM   2406 C  CD1   . PHE A 1 347 ? 4.120   -29.915 20.667  1.00 20.34 ? 326 PHE A CD1   1 
ATOM   2407 C  CD2   . PHE A 1 347 ? 5.511   -28.702 19.136  1.00 22.70 ? 326 PHE A CD2   1 
ATOM   2408 C  CE1   . PHE A 1 347 ? 4.402   -28.969 21.650  1.00 23.53 ? 326 PHE A CE1   1 
ATOM   2409 C  CE2   . PHE A 1 347 ? 5.797   -27.764 20.120  1.00 23.08 ? 326 PHE A CE2   1 
ATOM   2410 C  CZ    . PHE A 1 347 ? 5.237   -27.895 21.371  1.00 23.10 ? 326 PHE A CZ    1 
ATOM   2411 N  N     . ASP A 1 348 ? 4.259   -33.964 17.729  1.00 16.51 ? 327 ASP A N     1 
ATOM   2412 C  CA    . ASP A 1 348 ? 3.486   -34.921 16.913  1.00 17.35 ? 327 ASP A CA    1 
ATOM   2413 C  C     . ASP A 1 348 ? 2.244   -34.178 16.390  1.00 19.94 ? 327 ASP A C     1 
ATOM   2414 O  O     . ASP A 1 348 ? 1.386   -33.775 17.232  1.00 21.94 ? 327 ASP A O     1 
ATOM   2415 C  CB    . ASP A 1 348 ? 3.182   -36.140 17.789  1.00 18.60 ? 327 ASP A CB    1 
ATOM   2416 C  CG    . ASP A 1 348 ? 2.517   -37.294 17.037  1.00 22.39 ? 327 ASP A CG    1 
ATOM   2417 O  OD1   . ASP A 1 348 ? 1.800   -37.018 16.098  1.00 20.17 ? 327 ASP A OD1   1 
ATOM   2418 O  OD2   . ASP A 1 348 ? 2.648   -38.454 17.506  1.00 23.83 ? 327 ASP A OD2   1 
ATOM   2419 N  N     . GLY A 1 349 ? 2.162   -33.981 15.078  1.00 18.07 ? 328 GLY A N     1 
ATOM   2420 C  CA    . GLY A 1 349 ? 1.099   -33.232 14.392  1.00 16.45 ? 328 GLY A CA    1 
ATOM   2421 C  C     . GLY A 1 349 ? 0.091   -34.125 13.696  1.00 15.59 ? 328 GLY A C     1 
ATOM   2422 O  O     . GLY A 1 349 ? -0.666  -33.635 12.857  1.00 16.32 ? 328 GLY A O     1 
ATOM   2423 N  N     . THR A 1 350 ? 0.063   -35.400 14.055  1.00 15.89 ? 329 THR A N     1 
ATOM   2424 C  CA    . THR A 1 350 ? -0.769  -36.441 13.393  1.00 15.08 ? 329 THR A CA    1 
ATOM   2425 C  C     . THR A 1 350 ? -2.235  -36.165 13.714  1.00 16.64 ? 329 THR A C     1 
ATOM   2426 O  O     . THR A 1 350 ? -2.544  -35.888 14.871  1.00 17.68 ? 329 THR A O     1 
ATOM   2427 C  CB    . THR A 1 350 ? -0.328  -37.820 13.893  1.00 17.88 ? 329 THR A CB    1 
ATOM   2428 O  OG1   . THR A 1 350 ? 1.049   -38.018 13.580  1.00 17.78 ? 329 THR A OG1   1 
ATOM   2429 C  CG2   . THR A 1 350 ? -1.128  -38.951 13.256  1.00 17.12 ? 329 THR A CG2   1 
ATOM   2430 N  N     . PRO A 1 351 ? -3.185  -36.207 12.729  1.00 17.42 ? 330 PRO A N     1 
ATOM   2431 C  CA    . PRO A 1 351 ? -4.603  -35.969 13.006  1.00 16.89 ? 330 PRO A CA    1 
ATOM   2432 C  C     . PRO A 1 351 ? -5.239  -37.152 13.735  1.00 17.00 ? 330 PRO A C     1 
ATOM   2433 O  O     . PRO A 1 351 ? -4.619  -38.200 13.886  1.00 17.85 ? 330 PRO A O     1 
ATOM   2434 C  CB    . PRO A 1 351 ? -5.236  -35.806 11.623  1.00 16.80 ? 330 PRO A CB    1 
ATOM   2435 C  CG    . PRO A 1 351 ? -4.367  -36.691 10.752  1.00 16.31 ? 330 PRO A CG    1 
ATOM   2436 C  CD    . PRO A 1 351 ? -2.950  -36.519 11.313  1.00 16.74 ? 330 PRO A CD    1 
ATOM   2437 N  N     . PRO A 1 352 ? -6.503  -37.031 14.191  1.00 17.71 ? 331 PRO A N     1 
ATOM   2438 C  CA    . PRO A 1 352 ? -7.168  -38.130 14.913  1.00 18.60 ? 331 PRO A CA    1 
ATOM   2439 C  C     . PRO A 1 352 ? -7.240  -39.465 14.158  1.00 19.43 ? 331 PRO A C     1 
ATOM   2440 O  O     . PRO A 1 352 ? -7.265  -40.508 14.822  1.00 19.72 ? 331 PRO A O     1 
ATOM   2441 C  CB    . PRO A 1 352 ? -8.574  -37.570 15.196  1.00 20.84 ? 331 PRO A CB    1 
ATOM   2442 C  CG    . PRO A 1 352 ? -8.338  -36.076 15.299  1.00 20.83 ? 331 PRO A CG    1 
ATOM   2443 C  CD    . PRO A 1 352 ? -7.295  -35.781 14.240  1.00 18.51 ? 331 PRO A CD    1 
ATOM   2444 N  N     . ALA A 1 353 ? -7.229  -39.419 12.832  1.00 19.83 ? 332 ALA A N     1 
ATOM   2445 C  CA    . ALA A 1 353 ? -7.287  -40.628 11.967  1.00 18.91 ? 332 ALA A CA    1 
ATOM   2446 C  C     . ALA A 1 353 ? -6.049  -41.504 12.233  1.00 20.80 ? 332 ALA A C     1 
ATOM   2447 O  O     . ALA A 1 353 ? -6.114  -42.716 11.962  1.00 21.75 ? 332 ALA A O     1 
ATOM   2448 C  CB    . ALA A 1 353 ? -7.391  -40.197 10.522  1.00 20.23 ? 332 ALA A CB    1 
ATOM   2449 N  N     . GLY A 1 354 ? -4.961  -40.922 12.746  1.00 18.81 ? 333 GLY A N     1 
ATOM   2450 C  CA    . GLY A 1 354 ? -3.713  -41.636 13.092  1.00 17.61 ? 333 GLY A CA    1 
ATOM   2451 C  C     . GLY A 1 354 ? -2.819  -41.842 11.873  1.00 19.16 ? 333 GLY A C     1 
ATOM   2452 O  O     . GLY A 1 354 ? -1.705  -42.375 12.032  1.00 20.16 ? 333 GLY A O     1 
ATOM   2453 N  N     . THR A 1 355 ? -3.201  -41.313 10.698  1.00 18.15 ? 334 THR A N     1 
ATOM   2454 C  CA    . THR A 1 355 ? -2.317  -41.161 9.526   1.00 18.41 ? 334 THR A CA    1 
ATOM   2455 C  C     . THR A 1 355 ? -2.802  -39.940 8.766   1.00 18.76 ? 334 THR A C     1 
ATOM   2456 O  O     . THR A 1 355 ? -3.931  -39.495 8.965   1.00 19.03 ? 334 THR A O     1 
ATOM   2457 C  CB    . THR A 1 355 ? -2.342  -42.354 8.537   1.00 20.65 ? 334 THR A CB    1 
ATOM   2458 O  OG1   . THR A 1 355 ? -3.633  -42.381 7.937   1.00 21.45 ? 334 THR A OG1   1 
ATOM   2459 C  CG2   . THR A 1 355 ? -2.076  -43.682 9.208   1.00 21.70 ? 334 THR A CG2   1 
ATOM   2460 N  N     . PRO A 1 356 ? -1.940  -39.302 7.958   1.00 17.70 ? 335 PRO A N     1 
ATOM   2461 C  CA    . PRO A 1 356 ? -0.507  -39.616 7.894   1.00 17.88 ? 335 PRO A CA    1 
ATOM   2462 C  C     . PRO A 1 356 ? 0.252   -39.184 9.161   1.00 17.66 ? 335 PRO A C     1 
ATOM   2463 O  O     . PRO A 1 356 ? -0.274  -38.358 9.923   1.00 17.19 ? 335 PRO A O     1 
ATOM   2464 C  CB    . PRO A 1 356 ? -0.048  -38.737 6.716   1.00 16.86 ? 335 PRO A CB    1 
ATOM   2465 C  CG    . PRO A 1 356 ? -0.937  -37.536 6.792   1.00 17.80 ? 335 PRO A CG    1 
ATOM   2466 C  CD    . PRO A 1 356 ? -2.288  -38.085 7.205   1.00 17.99 ? 335 PRO A CD    1 
ATOM   2467 N  N     . GLY A 1 357 ? 1.420   -39.769 9.443   1.00 17.24 ? 336 GLY A N     1 
ATOM   2468 C  CA    . GLY A 1 357 ? 2.268   -39.300 10.565  1.00 15.73 ? 336 GLY A CA    1 
ATOM   2469 C  C     . GLY A 1 357 ? 2.773   -37.895 10.255  1.00 15.85 ? 336 GLY A C     1 
ATOM   2470 O  O     . GLY A 1 357 ? 3.180   -37.692 9.131   1.00 18.52 ? 336 GLY A O     1 
ATOM   2471 N  N     . ILE A 1 358 ? 2.719   -36.955 11.197  1.00 15.62 ? 337 ILE A N     1 
ATOM   2472 C  CA    . ILE A 1 358 ? 3.302   -35.602 10.999  1.00 17.89 ? 337 ILE A CA    1 
ATOM   2473 C  C     . ILE A 1 358 ? 4.179   -35.225 12.178  1.00 17.84 ? 337 ILE A C     1 
ATOM   2474 O  O     . ILE A 1 358 ? 3.762   -35.429 13.343  1.00 17.64 ? 337 ILE A O     1 
ATOM   2475 C  CB    . ILE A 1 358 ? 2.193   -34.583 10.800  1.00 17.79 ? 337 ILE A CB    1 
ATOM   2476 C  CG1   . ILE A 1 358 ? 1.323   -34.983 9.613   1.00 18.18 ? 337 ILE A CG1   1 
ATOM   2477 C  CG2   . ILE A 1 358 ? 2.775   -33.182 10.646  1.00 18.67 ? 337 ILE A CG2   1 
ATOM   2478 C  CD1   . ILE A 1 358 ? 0.150   -34.040 9.363   1.00 18.48 ? 337 ILE A CD1   1 
ATOM   2479 N  N     . VAL A 1 359 ? 5.352   -34.670 11.881  1.00 16.54 ? 338 VAL A N     1 
ATOM   2480 C  CA    . VAL A 1 359 ? 6.172   -33.954 12.881  1.00 16.45 ? 338 VAL A CA    1 
ATOM   2481 C  C     . VAL A 1 359 ? 6.107   -32.487 12.519  1.00 17.92 ? 338 VAL A C     1 
ATOM   2482 O  O     . VAL A 1 359 ? 6.564   -32.140 11.411  1.00 17.22 ? 338 VAL A O     1 
ATOM   2483 C  CB    . VAL A 1 359 ? 7.618   -34.451 12.967  1.00 17.75 ? 338 VAL A CB    1 
ATOM   2484 C  CG1   . VAL A 1 359 ? 8.358   -33.691 14.043  1.00 16.74 ? 338 VAL A CG1   1 
ATOM   2485 C  CG2   . VAL A 1 359 ? 7.662   -35.951 13.211  1.00 16.87 ? 338 VAL A CG2   1 
ATOM   2486 N  N     . THR A 1 360 ? 5.651   -31.697 13.497  1.00 16.64 ? 339 THR A N     1 
ATOM   2487 C  CA    . THR A 1 360 ? 5.467   -30.259 13.357  1.00 16.74 ? 339 THR A CA    1 
ATOM   2488 C  C     . THR A 1 360 ? 6.624   -29.596 14.085  1.00 16.85 ? 339 THR A C     1 
ATOM   2489 O  O     . THR A 1 360 ? 6.963   -30.001 15.199  1.00 16.04 ? 339 THR A O     1 
ATOM   2490 C  CB    . THR A 1 360 ? 4.119   -29.748 13.882  1.00 17.65 ? 339 THR A CB    1 
ATOM   2491 O  OG1   . THR A 1 360 ? 3.113   -30.512 13.201  1.00 17.65 ? 339 THR A OG1   1 
ATOM   2492 C  CG2   . THR A 1 360 ? 3.943   -28.269 13.588  1.00 17.54 ? 339 THR A CG2   1 
ATOM   2493 N  N     . GLY A 1 361 ? 7.214   -28.586 13.466  1.00 15.72 ? 340 GLY A N     1 
ATOM   2494 C  CA    . GLY A 1 361 ? 8.121   -27.715 14.234  1.00 15.97 ? 340 GLY A CA    1 
ATOM   2495 C  C     . GLY A 1 361 ? 8.471   -26.408 13.539  1.00 15.30 ? 340 GLY A C     1 
ATOM   2496 O  O     . GLY A 1 361 ? 7.760   -25.963 12.655  1.00 15.07 ? 340 GLY A O     1 
ATOM   2497 N  N     . PHE A 1 362 ? 9.485   -25.736 14.058  1.00 16.21 ? 341 PHE A N     1 
ATOM   2498 C  CA    . PHE A 1 362 ? 9.744   -24.298 13.787  1.00 16.24 ? 341 PHE A CA    1 
ATOM   2499 C  C     . PHE A 1 362 ? 11.237  -24.055 13.700  1.00 15.75 ? 341 PHE A C     1 
ATOM   2500 O  O     . PHE A 1 362 ? 12.000  -24.575 14.550  1.00 17.79 ? 341 PHE A O     1 
ATOM   2501 C  CB    . PHE A 1 362 ? 9.193   -23.420 14.912  1.00 18.52 ? 341 PHE A CB    1 
ATOM   2502 C  CG    . PHE A 1 362 ? 7.768   -23.741 15.283  1.00 18.82 ? 341 PHE A CG    1 
ATOM   2503 C  CD1   . PHE A 1 362 ? 6.709   -23.095 14.663  1.00 19.21 ? 341 PHE A CD1   1 
ATOM   2504 C  CD2   . PHE A 1 362 ? 7.483   -24.743 16.208  1.00 21.39 ? 341 PHE A CD2   1 
ATOM   2505 C  CE1   . PHE A 1 362 ? 5.396   -23.403 14.982  1.00 20.26 ? 341 PHE A CE1   1 
ATOM   2506 C  CE2   . PHE A 1 362 ? 6.162   -25.069 16.506  1.00 23.42 ? 341 PHE A CE2   1 
ATOM   2507 C  CZ    . PHE A 1 362 ? 5.122   -24.403 15.887  1.00 20.78 ? 341 PHE A CZ    1 
ATOM   2508 N  N     . PHE A 1 363 ? 11.640  -23.229 12.732  1.00 15.09 ? 342 PHE A N     1 
ATOM   2509 C  CA    . PHE A 1 363 ? 12.870  -22.390 12.832  1.00 15.92 ? 342 PHE A CA    1 
ATOM   2510 C  C     . PHE A 1 363 ? 12.445  -21.063 13.456  1.00 15.11 ? 342 PHE A C     1 
ATOM   2511 O  O     . PHE A 1 363 ? 11.458  -20.456 12.941  1.00 15.80 ? 342 PHE A O     1 
ATOM   2512 C  CB    . PHE A 1 363 ? 13.445  -22.117 11.437  1.00 15.09 ? 342 PHE A CB    1 
ATOM   2513 C  CG    . PHE A 1 363 ? 13.884  -23.325 10.645  1.00 15.29 ? 342 PHE A CG    1 
ATOM   2514 C  CD1   . PHE A 1 363 ? 15.228  -23.691 10.594  1.00 14.00 ? 342 PHE A CD1   1 
ATOM   2515 C  CD2   . PHE A 1 363 ? 12.963  -24.037 9.892   1.00 14.22 ? 342 PHE A CD2   1 
ATOM   2516 C  CE1   . PHE A 1 363 ? 15.637  -24.738 9.777   1.00 15.69 ? 342 PHE A CE1   1 
ATOM   2517 C  CE2   . PHE A 1 363 ? 13.372  -25.110 9.121   1.00 14.09 ? 342 PHE A CE2   1 
ATOM   2518 C  CZ    . PHE A 1 363 ? 14.712  -25.423 9.035   1.00 15.68 ? 342 PHE A CZ    1 
ATOM   2519 N  N     . GLU A 1 364 ? 13.144  -20.586 14.471  1.00 16.27 ? 343 GLU A N     1 
ATOM   2520 C  CA    . GLU A 1 364 ? 12.769  -19.368 15.224  1.00 17.69 ? 343 GLU A CA    1 
ATOM   2521 C  C     . GLU A 1 364 ? 13.908  -18.351 15.180  1.00 19.25 ? 343 GLU A C     1 
ATOM   2522 O  O     . GLU A 1 364 ? 15.102  -18.782 15.266  1.00 18.53 ? 343 GLU A O     1 
ATOM   2523 C  CB    . GLU A 1 364 ? 12.556  -19.710 16.709  1.00 22.46 ? 343 GLU A CB    1 
ATOM   2524 C  CG    . GLU A 1 364 ? 11.534  -20.797 16.970  1.00 25.75 ? 343 GLU A CG    1 
ATOM   2525 C  CD    . GLU A 1 364 ? 10.096  -20.363 16.822  1.00 29.04 ? 343 GLU A CD    1 
ATOM   2526 O  OE1   . GLU A 1 364 ? 9.173   -21.143 17.337  1.00 26.31 ? 343 GLU A OE1   1 
ATOM   2527 O  OE2   . GLU A 1 364 ? 9.880   -19.228 16.255  1.00 26.58 ? 343 GLU A OE2   1 
ATOM   2528 N  N     . GLY A 1 365 ? 13.566  -17.061 15.178  1.00 17.86 ? 344 GLY A N     1 
ATOM   2529 C  CA    . GLY A 1 365 ? 14.570  -15.992 15.368  1.00 18.40 ? 344 GLY A CA    1 
ATOM   2530 C  C     . GLY A 1 365 ? 15.658  -16.071 14.307  1.00 19.98 ? 344 GLY A C     1 
ATOM   2531 O  O     . GLY A 1 365 ? 15.354  -16.258 13.127  1.00 19.87 ? 344 GLY A O     1 
ATOM   2532 N  N     . PRO A 1 366 ? 16.945  -15.957 14.696  1.00 19.01 ? 345 PRO A N     1 
ATOM   2533 C  CA    . PRO A 1 366 ? 18.064  -15.966 13.741  1.00 19.31 ? 345 PRO A CA    1 
ATOM   2534 C  C     . PRO A 1 366 ? 18.047  -17.193 12.802  1.00 17.06 ? 345 PRO A C     1 
ATOM   2535 O  O     . PRO A 1 366 ? 18.376  -17.066 11.602  1.00 16.87 ? 345 PRO A O     1 
ATOM   2536 C  CB    . PRO A 1 366 ? 19.277  -15.929 14.684  1.00 21.72 ? 345 PRO A CB    1 
ATOM   2537 C  CG    . PRO A 1 366 ? 18.766  -15.138 15.864  1.00 21.27 ? 345 PRO A CG    1 
ATOM   2538 C  CD    . PRO A 1 366 ? 17.401  -15.750 16.091  1.00 21.81 ? 345 PRO A CD    1 
ATOM   2539 N  N     . ALA A 1 367 ? 17.703  -18.372 13.340  1.00 15.80 ? 346 ALA A N     1 
ATOM   2540 C  CA    . ALA A 1 367 ? 17.619  -19.613 12.544  1.00 15.08 ? 346 ALA A CA    1 
ATOM   2541 C  C     . ALA A 1 367 ? 16.556  -19.468 11.438  1.00 13.85 ? 346 ALA A C     1 
ATOM   2542 O  O     . ALA A 1 367 ? 16.736  -20.089 10.367  1.00 16.43 ? 346 ALA A O     1 
ATOM   2543 C  CB    . ALA A 1 367 ? 17.335  -20.815 13.449  1.00 15.04 ? 346 ALA A CB    1 
ATOM   2544 N  N     . ALA A 1 368 ? 15.427  -18.796 11.706  1.00 16.18 ? 347 ALA A N     1 
ATOM   2545 C  CA    . ALA A 1 368 ? 14.317  -18.591 10.746  1.00 15.98 ? 347 ALA A CA    1 
ATOM   2546 C  C     . ALA A 1 368 ? 14.850  -17.697 9.629   1.00 17.15 ? 347 ALA A C     1 
ATOM   2547 O  O     . ALA A 1 368 ? 14.535  -17.918 8.488   1.00 16.02 ? 347 ALA A O     1 
ATOM   2548 C  CB    . ALA A 1 368 ? 13.072  -17.975 11.367  1.00 17.26 ? 347 ALA A CB    1 
ATOM   2549 N  N     . VAL A 1 369 ? 15.598  -16.673 9.989   1.00 16.18 ? 348 VAL A N     1 
ATOM   2550 C  CA    . VAL A 1 369 ? 16.121  -15.725 8.961   1.00 16.79 ? 348 VAL A CA    1 
ATOM   2551 C  C     . VAL A 1 369 ? 17.149  -16.438 8.059   1.00 18.07 ? 348 VAL A C     1 
ATOM   2552 O  O     . VAL A 1 369 ? 17.106  -16.234 6.822   1.00 18.06 ? 348 VAL A O     1 
ATOM   2553 C  CB    . VAL A 1 369 ? 16.653  -14.436 9.597   1.00 17.75 ? 348 VAL A CB    1 
ATOM   2554 C  CG1   . VAL A 1 369 ? 17.107  -13.467 8.506   1.00 19.96 ? 348 VAL A CG1   1 
ATOM   2555 C  CG2   . VAL A 1 369 ? 15.565  -13.783 10.431  1.00 19.81 ? 348 VAL A CG2   1 
ATOM   2556 N  N     . ALA A 1 370 ? 18.013  -17.290 8.623   1.00 16.83 ? 349 ALA A N     1 
ATOM   2557 C  CA    . ALA A 1 370 ? 19.013  -18.051 7.852   1.00 17.90 ? 349 ALA A CA    1 
ATOM   2558 C  C     . ALA A 1 370 ? 18.265  -19.034 6.961   1.00 18.07 ? 349 ALA A C     1 
ATOM   2559 O  O     . ALA A 1 370 ? 18.599  -19.128 5.729   1.00 19.93 ? 349 ALA A O     1 
ATOM   2560 C  CB    . ALA A 1 370 ? 20.005  -18.721 8.775   1.00 19.75 ? 349 ALA A CB    1 
ATOM   2561 N  N     . ALA A 1 371 ? 17.252  -19.712 7.510   1.00 16.98 ? 350 ALA A N     1 
ATOM   2562 C  CA    . ALA A 1 371 ? 16.514  -20.771 6.773   1.00 16.52 ? 350 ALA A CA    1 
ATOM   2563 C  C     . ALA A 1 371 ? 15.664  -20.160 5.662   1.00 16.44 ? 350 ALA A C     1 
ATOM   2564 O  O     . ALA A 1 371 ? 15.540  -20.785 4.583   1.00 15.61 ? 350 ALA A O     1 
ATOM   2565 C  CB    . ALA A 1 371 ? 15.672  -21.591 7.706   1.00 17.11 ? 350 ALA A CB    1 
ATOM   2566 N  N     . GLY A 1 372 ? 15.059  -18.997 5.921   1.00 16.61 ? 351 GLY A N     1 
ATOM   2567 C  CA    . GLY A 1 372 ? 14.266  -18.240 4.934   1.00 17.29 ? 351 GLY A CA    1 
ATOM   2568 C  C     . GLY A 1 372 ? 15.047  -17.845 3.680   1.00 17.99 ? 351 GLY A C     1 
ATOM   2569 O  O     . GLY A 1 372 ? 14.441  -17.631 2.652   1.00 18.21 ? 351 GLY A O     1 
ATOM   2570 N  N     . ALA A 1 373 ? 16.349  -17.729 3.756   1.00 19.53 ? 352 ALA A N     1 
ATOM   2571 C  CA    . ALA A 1 373 ? 17.191  -17.309 2.622   1.00 20.38 ? 352 ALA A CA    1 
ATOM   2572 C  C     . ALA A 1 373 ? 17.511  -18.559 1.798   1.00 21.69 ? 352 ALA A C     1 
ATOM   2573 O  O     . ALA A 1 373 ? 18.165  -18.434 0.758   1.00 22.43 ? 352 ALA A O     1 
ATOM   2574 C  CB    . ALA A 1 373 ? 18.421  -16.598 3.141   1.00 23.41 ? 352 ALA A CB    1 
ATOM   2575 N  N     . ARG A 1 374 ? 17.128  -19.733 2.288   1.00 20.76 ? 353 ARG A N     1 
ATOM   2576 C  CA    . ARG A 1 374 ? 17.448  -21.029 1.640   1.00 19.91 ? 353 ARG A CA    1 
ATOM   2577 C  C     . ARG A 1 374 ? 16.181  -21.555 0.972   1.00 21.12 ? 353 ARG A C     1 
ATOM   2578 O  O     . ARG A 1 374 ? 15.142  -20.907 1.046   1.00 19.99 ? 353 ARG A O     1 
ATOM   2579 C  CB    . ARG A 1 374 ? 18.070  -21.980 2.671   1.00 22.90 ? 353 ARG A CB    1 
ATOM   2580 C  CG    . ARG A 1 374 ? 19.384  -21.471 3.245   1.00 27.93 ? 353 ARG A CG    1 
ATOM   2581 C  CD    . ARG A 1 374 ? 19.966  -22.433 4.251   1.00 34.32 ? 353 ARG A CD    1 
ATOM   2582 N  NE    . ARG A 1 374 ? 20.802  -23.330 3.482   1.00 43.24 ? 353 ARG A NE    1 
ATOM   2583 C  CZ    . ARG A 1 374 ? 21.183  -24.553 3.831   1.00 43.09 ? 353 ARG A CZ    1 
ATOM   2584 N  NH1   . ARG A 1 374 ? 20.778  -25.107 4.960   1.00 47.12 ? 353 ARG A NH1   1 
ATOM   2585 N  NH2   . ARG A 1 374 ? 21.957  -25.230 3.006   1.00 41.75 ? 353 ARG A NH2   1 
ATOM   2586 N  N     . THR A 1 375 ? 16.322  -22.609 0.172   1.00 17.53 ? 354 THR A N     1 
ATOM   2587 C  CA    . THR A 1 375 ? 15.211  -23.239 -0.568  1.00 18.35 ? 354 THR A CA    1 
ATOM   2588 C  C     . THR A 1 375 ? 14.478  -24.213 0.403   1.00 15.16 ? 354 THR A C     1 
ATOM   2589 O  O     . THR A 1 375 ? 15.052  -24.598 1.425   1.00 15.35 ? 354 THR A O     1 
ATOM   2590 C  CB    . THR A 1 375 ? 15.682  -24.090 -1.751  1.00 17.96 ? 354 THR A CB    1 
ATOM   2591 O  OG1   . THR A 1 375 ? 16.467  -25.175 -1.260  1.00 18.55 ? 354 THR A OG1   1 
ATOM   2592 C  CG2   . THR A 1 375 ? 16.511  -23.334 -2.773  1.00 20.59 ? 354 THR A CG2   1 
ATOM   2593 N  N     . ARG A 1 376 ? 13.254  -24.564 0.045   1.00 14.99 ? 355 ARG A N     1 
ATOM   2594 C  CA    . ARG A 1 376 ? 12.437  -25.592 0.758   1.00 17.51 ? 355 ARG A CA    1 
ATOM   2595 C  C     . ARG A 1 376 ? 13.280  -26.864 0.930   1.00 16.88 ? 355 ARG A C     1 
ATOM   2596 O  O     . ARG A 1 376 ? 13.213  -27.521 1.996   1.00 15.78 ? 355 ARG A O     1 
ATOM   2597 C  CB    . ARG A 1 376 ? 11.154  -25.881 -0.023  1.00 18.80 ? 355 ARG A CB    1 
ATOM   2598 C  CG    . ARG A 1 376 ? 10.177  -26.764 0.746   1.00 18.33 ? 355 ARG A CG    1 
ATOM   2599 C  CD    . ARG A 1 376 ? 9.076   -27.433 -0.070  1.00 21.83 ? 355 ARG A CD    1 
ATOM   2600 N  NE    . ARG A 1 376 ? 9.714   -28.320 -1.010  1.00 21.76 ? 355 ARG A NE    1 
ATOM   2601 C  CZ    . ARG A 1 376 ? 9.858   -29.644 -0.899  1.00 23.17 ? 355 ARG A CZ    1 
ATOM   2602 N  NH1   . ARG A 1 376 ? 9.298   -30.328 0.086   1.00 21.89 ? 355 ARG A NH1   1 
ATOM   2603 N  NH2   . ARG A 1 376 ? 10.566  -30.282 -1.821  1.00 23.66 ? 355 ARG A NH2   1 
ATOM   2604 N  N     . GLU A 1 377 ? 13.923  -27.279 -0.152  1.00 17.39 ? 356 GLU A N     1 
ATOM   2605 C  CA    . GLU A 1 377 ? 14.746  -28.521 -0.169  1.00 17.83 ? 356 GLU A CA    1 
ATOM   2606 C  C     . GLU A 1 377 ? 15.859  -28.430 0.880   1.00 17.57 ? 356 GLU A C     1 
ATOM   2607 O  O     . GLU A 1 377 ? 16.067  -29.423 1.611   1.00 17.64 ? 356 GLU A O     1 
ATOM   2608 C  CB    . GLU A 1 377 ? 15.222  -28.817 -1.578  1.00 19.14 ? 356 GLU A CB    1 
ATOM   2609 C  CG    . GLU A 1 377 ? 14.090  -29.206 -2.510  1.00 20.67 ? 356 GLU A CG    1 
ATOM   2610 C  CD    . GLU A 1 377 ? 13.234  -28.056 -3.025  1.00 19.79 ? 356 GLU A CD    1 
ATOM   2611 O  OE1   . GLU A 1 377 ? 12.080  -28.305 -3.386  1.00 23.21 ? 356 GLU A OE1   1 
ATOM   2612 O  OE2   . GLU A 1 377 ? 13.714  -26.915 -3.048  1.00 20.54 ? 356 GLU A OE2   1 
ATOM   2613 N  N     . GLU A 1 378 ? 16.555  -27.310 0.966   1.00 17.70 ? 357 GLU A N     1 
ATOM   2614 C  CA    . GLU A 1 378 ? 17.642  -27.157 1.962   1.00 17.45 ? 357 GLU A CA    1 
ATOM   2615 C  C     . GLU A 1 378 ? 17.070  -27.182 3.390   1.00 17.51 ? 357 GLU A C     1 
ATOM   2616 O  O     . GLU A 1 378 ? 17.701  -27.777 4.268   1.00 17.50 ? 357 GLU A O     1 
ATOM   2617 C  CB    . GLU A 1 378 ? 18.359  -25.844 1.709   1.00 19.68 ? 357 GLU A CB    1 
ATOM   2618 C  CG    . GLU A 1 378 ? 19.265  -25.887 0.482   1.00 24.04 ? 357 GLU A CG    1 
ATOM   2619 C  CD    . GLU A 1 378 ? 19.883  -24.560 0.031   1.00 27.27 ? 357 GLU A CD    1 
ATOM   2620 O  OE1   . GLU A 1 378 ? 21.098  -24.553 -0.283  1.00 29.34 ? 357 GLU A OE1   1 
ATOM   2621 O  OE2   . GLU A 1 378 ? 19.172  -23.534 -0.039  1.00 32.96 ? 357 GLU A OE2   1 
ATOM   2622 N  N     . ARG A 1 379 ? 15.934  -26.524 3.624   1.00 16.77 ? 358 ARG A N     1 
ATOM   2623 C  CA    . ARG A 1 379 ? 15.251  -26.564 4.938   1.00 17.91 ? 358 ARG A CA    1 
ATOM   2624 C  C     . ARG A 1 379 ? 14.830  -27.997 5.264   1.00 17.51 ? 358 ARG A C     1 
ATOM   2625 O  O     . ARG A 1 379 ? 15.084  -28.425 6.371   1.00 18.09 ? 358 ARG A O     1 
ATOM   2626 C  CB    . ARG A 1 379 ? 14.082  -25.584 4.965   1.00 18.51 ? 358 ARG A CB    1 
ATOM   2627 C  CG    . ARG A 1 379 ? 14.550  -24.137 4.977   1.00 18.86 ? 358 ARG A CG    1 
ATOM   2628 C  CD    . ARG A 1 379 ? 13.443  -23.118 5.256   1.00 18.62 ? 358 ARG A CD    1 
ATOM   2629 N  NE    . ARG A 1 379 ? 12.310  -23.208 4.346   1.00 17.72 ? 358 ARG A NE    1 
ATOM   2630 C  CZ    . ARG A 1 379 ? 12.122  -22.478 3.251   1.00 18.86 ? 358 ARG A CZ    1 
ATOM   2631 N  NH1   . ARG A 1 379 ? 13.032  -21.600 2.847   1.00 20.67 ? 358 ARG A NH1   1 
ATOM   2632 N  NH2   . ARG A 1 379 ? 11.007  -22.624 2.559   1.00 20.70 ? 358 ARG A NH2   1 
ATOM   2633 N  N     . ARG A 1 380 ? 14.188  -28.689 4.311   1.00 17.12 ? 359 ARG A N     1 
ATOM   2634 C  CA    . ARG A 1 380 ? 13.824  -30.107 4.442   1.00 17.27 ? 359 ARG A CA    1 
ATOM   2635 C  C     . ARG A 1 380 ? 15.035  -30.906 4.946   1.00 17.27 ? 359 ARG A C     1 
ATOM   2636 O  O     . ARG A 1 380 ? 14.919  -31.674 5.981   1.00 17.43 ? 359 ARG A O     1 
ATOM   2637 C  CB    . ARG A 1 380 ? 13.349  -30.658 3.092   1.00 17.72 ? 359 ARG A CB    1 
ATOM   2638 C  CG    . ARG A 1 380 ? 13.166  -32.176 3.107   1.00 18.62 ? 359 ARG A CG    1 
ATOM   2639 C  CD    . ARG A 1 380 ? 13.007  -32.767 1.700   1.00 19.63 ? 359 ARG A CD    1 
ATOM   2640 N  NE    . ARG A 1 380 ? 14.293  -32.637 1.023   1.00 21.05 ? 359 ARG A NE    1 
ATOM   2641 C  CZ    . ARG A 1 380 ? 14.525  -32.640 -0.295  1.00 22.01 ? 359 ARG A CZ    1 
ATOM   2642 N  NH1   . ARG A 1 380 ? 13.553  -32.732 -1.207  1.00 20.90 ? 359 ARG A NH1   1 
ATOM   2643 N  NH2   . ARG A 1 380 ? 15.780  -32.538 -0.698  1.00 21.34 ? 359 ARG A NH2   1 
ATOM   2644 N  N     . ASP A 1 381 ? 16.178  -30.738 4.276   1.00 17.51 ? 360 ASP A N     1 
ATOM   2645 C  CA    . ASP A 1 381 ? 17.391  -31.535 4.562   1.00 17.89 ? 360 ASP A CA    1 
ATOM   2646 C  C     . ASP A 1 381 ? 17.849  -31.284 6.006   1.00 17.20 ? 360 ASP A C     1 
ATOM   2647 O  O     . ASP A 1 381 ? 18.235  -32.227 6.666   1.00 17.07 ? 360 ASP A O     1 
ATOM   2648 C  CB    . ASP A 1 381 ? 18.493  -31.241 3.545   1.00 17.90 ? 360 ASP A CB    1 
ATOM   2649 C  CG    . ASP A 1 381 ? 18.216  -31.665 2.105   1.00 21.10 ? 360 ASP A CG    1 
ATOM   2650 O  OD1   . ASP A 1 381 ? 17.252  -32.410 1.867   1.00 20.44 ? 360 ASP A OD1   1 
ATOM   2651 O  OD2   . ASP A 1 381 ? 18.941  -31.179 1.228   1.00 26.59 ? 360 ASP A OD2   1 
ATOM   2652 N  N     . VAL A 1 382 ? 17.814  -30.043 6.469   1.00 17.37 ? 361 VAL A N     1 
ATOM   2653 C  CA    . VAL A 1 382 ? 18.214  -29.679 7.854   1.00 19.53 ? 361 VAL A CA    1 
ATOM   2654 C  C     . VAL A 1 382 ? 17.260  -30.370 8.826   1.00 17.52 ? 361 VAL A C     1 
ATOM   2655 O  O     . VAL A 1 382 ? 17.735  -30.988 9.774   1.00 16.83 ? 361 VAL A O     1 
ATOM   2656 C  CB    . VAL A 1 382 ? 18.209  -28.166 8.044   1.00 19.56 ? 361 VAL A CB    1 
ATOM   2657 C  CG1   . VAL A 1 382 ? 18.232  -27.768 9.524   1.00 22.72 ? 361 VAL A CG1   1 
ATOM   2658 C  CG2   . VAL A 1 382 ? 19.361  -27.542 7.276   1.00 21.97 ? 361 VAL A CG2   1 
ATOM   2659 N  N     . VAL A 1 383 ? 15.959  -30.236 8.614   1.00 17.65 ? 362 VAL A N     1 
ATOM   2660 C  CA    . VAL A 1 383 ? 14.943  -30.828 9.531   1.00 17.63 ? 362 VAL A CA    1 
ATOM   2661 C  C     . VAL A 1 383 ? 15.087  -32.351 9.567   1.00 20.10 ? 362 VAL A C     1 
ATOM   2662 O  O     . VAL A 1 383 ? 15.145  -32.931 10.671  1.00 18.79 ? 362 VAL A O     1 
ATOM   2663 C  CB    . VAL A 1 383 ? 13.515  -30.421 9.138   1.00 18.84 ? 362 VAL A CB    1 
ATOM   2664 C  CG1   . VAL A 1 383 ? 12.476  -31.171 9.975   1.00 18.66 ? 362 VAL A CG1   1 
ATOM   2665 C  CG2   . VAL A 1 383 ? 13.303  -28.928 9.266   1.00 18.21 ? 362 VAL A CG2   1 
ATOM   2666 N  N     . VAL A 1 384 ? 15.090  -33.004 8.405   1.00 18.15 ? 363 VAL A N     1 
ATOM   2667 C  CA    . VAL A 1 384 ? 15.147  -34.480 8.336   1.00 19.84 ? 363 VAL A CA    1 
ATOM   2668 C  C     . VAL A 1 384 ? 16.422  -34.969 9.040   1.00 20.76 ? 363 VAL A C     1 
ATOM   2669 O  O     . VAL A 1 384 ? 16.350  -35.981 9.823   1.00 19.09 ? 363 VAL A O     1 
ATOM   2670 C  CB    . VAL A 1 384 ? 15.006  -34.967 6.884   1.00 21.95 ? 363 VAL A CB    1 
ATOM   2671 C  CG1   . VAL A 1 384 ? 15.394  -36.432 6.773   1.00 22.74 ? 363 VAL A CG1   1 
ATOM   2672 C  CG2   . VAL A 1 384 ? 13.582  -34.736 6.376   1.00 21.86 ? 363 VAL A CG2   1 
ATOM   2673 N  N     . ASP A 1 385 ? 17.552  -34.263 8.876   1.00 22.53 ? 364 ASP A N     1 
ATOM   2674 C  CA    . ASP A 1 385 ? 18.841  -34.618 9.545   1.00 23.45 ? 364 ASP A CA    1 
ATOM   2675 C  C     . ASP A 1 385 ? 18.713  -34.521 11.082  1.00 22.01 ? 364 ASP A C     1 
ATOM   2676 O  O     . ASP A 1 385 ? 19.215  -35.437 11.784  1.00 22.85 ? 364 ASP A O     1 
ATOM   2677 C  CB    . ASP A 1 385 ? 20.010  -33.775 9.013   1.00 24.79 ? 364 ASP A CB    1 
ATOM   2678 C  CG    . ASP A 1 385 ? 21.272  -33.938 9.831   1.00 27.98 ? 364 ASP A CG    1 
ATOM   2679 O  OD1   . ASP A 1 385 ? 21.778  -35.054 9.865   1.00 32.09 ? 364 ASP A OD1   1 
ATOM   2680 O  OD2   . ASP A 1 385 ? 21.690  -32.964 10.479  1.00 29.76 ? 364 ASP A OD2   1 
ATOM   2681 N  N     . VAL A 1 386 ? 18.070  -33.485 11.633  1.00 21.10 ? 365 VAL A N     1 
ATOM   2682 C  CA    . VAL A 1 386 ? 17.886  -33.376 13.104  1.00 21.14 ? 365 VAL A CA    1 
ATOM   2683 C  C     . VAL A 1 386 ? 17.029  -34.551 13.568  1.00 21.62 ? 365 VAL A C     1 
ATOM   2684 O  O     . VAL A 1 386 ? 17.402  -35.217 14.591  1.00 19.33 ? 365 VAL A O     1 
ATOM   2685 C  CB    . VAL A 1 386 ? 17.281  -32.028 13.531  1.00 20.76 ? 365 VAL A CB    1 
ATOM   2686 C  CG1   . VAL A 1 386 ? 16.959  -31.980 15.013  1.00 23.30 ? 365 VAL A CG1   1 
ATOM   2687 C  CG2   . VAL A 1 386 ? 18.182  -30.876 13.137  1.00 21.78 ? 365 VAL A CG2   1 
ATOM   2688 N  N     . LEU A 1 387 ? 15.914  -34.809 12.871  1.00 21.72 ? 366 LEU A N     1 
ATOM   2689 C  CA    . LEU A 1 387 ? 14.980  -35.877 13.304  1.00 20.50 ? 366 LEU A CA    1 
ATOM   2690 C  C     . LEU A 1 387 ? 15.701  -37.238 13.215  1.00 22.36 ? 366 LEU A C     1 
ATOM   2691 O  O     . LEU A 1 387 ? 15.473  -38.120 14.125  1.00 20.91 ? 366 LEU A O     1 
ATOM   2692 C  CB    . LEU A 1 387 ? 13.709  -35.875 12.458  1.00 19.46 ? 366 LEU A CB    1 
ATOM   2693 C  CG    . LEU A 1 387 ? 12.875  -34.612 12.574  1.00 19.59 ? 366 LEU A CG    1 
ATOM   2694 C  CD1   . LEU A 1 387 ? 11.643  -34.767 11.718  1.00 21.22 ? 366 LEU A CD1   1 
ATOM   2695 C  CD2   . LEU A 1 387 ? 12.519  -34.271 14.025  1.00 19.29 ? 366 LEU A CD2   1 
ATOM   2696 N  N     . ALA A 1 388 ? 16.501  -37.449 12.174  1.00 21.20 ? 367 ALA A N     1 
ATOM   2697 C  CA    . ALA A 1 388 ? 17.255  -38.720 12.018  1.00 23.85 ? 367 ALA A CA    1 
ATOM   2698 C  C     . ALA A 1 388 ? 18.181  -38.932 13.232  1.00 22.99 ? 367 ALA A C     1 
ATOM   2699 O  O     . ALA A 1 388 ? 18.305  -40.087 13.681  1.00 24.01 ? 367 ALA A O     1 
ATOM   2700 C  CB    . ALA A 1 388 ? 18.016  -38.762 10.702  1.00 25.07 ? 367 ALA A CB    1 
ATOM   2701 N  N     . ARG A 1 389 ? 18.748  -37.873 13.821  1.00 22.48 ? 368 ARG A N     1 
ATOM   2702 C  CA    . ARG A 1 389 ? 19.725  -37.993 14.949  1.00 24.68 ? 368 ARG A CA    1 
ATOM   2703 C  C     . ARG A 1 389 ? 19.022  -38.040 16.307  1.00 27.34 ? 368 ARG A C     1 
ATOM   2704 O  O     . ARG A 1 389 ? 19.733  -38.112 17.328  1.00 30.99 ? 368 ARG A O     1 
ATOM   2705 C  CB    . ARG A 1 389 ? 20.703  -36.815 14.891  1.00 23.74 ? 368 ARG A CB    1 
ATOM   2706 C  CG    . ARG A 1 389 ? 21.619  -36.905 13.681  1.00 24.28 ? 368 ARG A CG    1 
ATOM   2707 C  CD    . ARG A 1 389 ? 22.747  -35.913 13.701  1.00 27.18 ? 368 ARG A CD    1 
ATOM   2708 N  NE    . ARG A 1 389 ? 22.274  -34.639 13.177  1.00 27.27 ? 368 ARG A NE    1 
ATOM   2709 C  CZ    . ARG A 1 389 ? 22.121  -33.534 13.897  1.00 28.57 ? 368 ARG A CZ    1 
ATOM   2710 N  NH1   . ARG A 1 389 ? 22.457  -33.509 15.171  1.00 28.30 ? 368 ARG A NH1   1 
ATOM   2711 N  NH2   . ARG A 1 389 ? 21.654  -32.430 13.340  1.00 30.13 ? 368 ARG A NH2   1 
ATOM   2712 N  N     . THR A 1 390 ? 17.699  -37.823 16.332  1.00 21.61 ? 369 THR A N     1 
ATOM   2713 C  CA    . THR A 1 390 ? 16.906  -37.679 17.570  1.00 24.73 ? 369 THR A CA    1 
ATOM   2714 C  C     . THR A 1 390 ? 15.862  -38.787 17.624  1.00 25.64 ? 369 THR A C     1 
ATOM   2715 O  O     . THR A 1 390 ? 15.986  -39.678 18.505  1.00 25.30 ? 369 THR A O     1 
ATOM   2716 C  CB    . THR A 1 390 ? 16.333  -36.269 17.721  1.00 24.59 ? 369 THR A CB    1 
ATOM   2717 O  OG1   . THR A 1 390 ? 15.578  -35.901 16.573  1.00 22.18 ? 369 THR A OG1   1 
ATOM   2718 C  CG2   . THR A 1 390 ? 17.398  -35.236 17.995  1.00 22.93 ? 369 THR A CG2   1 
ATOM   2719 N  N     . LEU A 1 391 ? 14.873  -38.736 16.739  1.00 21.39 ? 370 LEU A N     1 
ATOM   2720 C  CA    . LEU A 1 391 ? 13.767  -39.724 16.677  1.00 23.50 ? 370 LEU A CA    1 
ATOM   2721 C  C     . LEU A 1 391 ? 14.247  -41.042 16.075  1.00 27.65 ? 370 LEU A C     1 
ATOM   2722 O  O     . LEU A 1 391 ? 13.707  -42.085 16.519  1.00 27.59 ? 370 LEU A O     1 
ATOM   2723 C  CB    . LEU A 1 391 ? 12.615  -39.170 15.841  1.00 24.35 ? 370 LEU A CB    1 
ATOM   2724 C  CG    . LEU A 1 391 ? 11.845  -38.006 16.440  1.00 24.14 ? 370 LEU A CG    1 
ATOM   2725 C  CD1   . LEU A 1 391 ? 10.662  -37.658 15.543  1.00 25.11 ? 370 LEU A CD1   1 
ATOM   2726 C  CD2   . LEU A 1 391 ? 11.337  -38.293 17.849  1.00 26.28 ? 370 LEU A CD2   1 
ATOM   2727 N  N     . GLY A 1 392 ? 15.206  -41.006 15.141  1.00 25.85 ? 371 GLY A N     1 
ATOM   2728 C  CA    . GLY A 1 392 ? 15.794  -42.215 14.524  1.00 27.56 ? 371 GLY A CA    1 
ATOM   2729 C  C     . GLY A 1 392 ? 15.914  -42.149 13.023  1.00 28.78 ? 371 GLY A C     1 
ATOM   2730 O  O     . GLY A 1 392 ? 15.291  -41.270 12.405  1.00 25.29 ? 371 GLY A O     1 
ATOM   2731 N  N     . GLU A 1 393 ? 16.639  -43.115 12.457  1.00 29.22 ? 372 GLU A N     1 
ATOM   2732 C  CA    . GLU A 1 393 ? 17.050  -43.195 11.038  1.00 33.22 ? 372 GLU A CA    1 
ATOM   2733 C  C     . GLU A 1 393 ? 15.809  -43.293 10.141  1.00 29.12 ? 372 GLU A C     1 
ATOM   2734 O  O     . GLU A 1 393 ? 15.878  -42.833 9.006   1.00 28.49 ? 372 GLU A O     1 
ATOM   2735 C  CB    . GLU A 1 393 ? 18.006  -44.382 10.867  1.00 40.61 ? 372 GLU A CB    1 
ATOM   2736 C  CG    . GLU A 1 393 ? 18.667  -44.467 9.497   1.00 53.08 ? 372 GLU A CG    1 
ATOM   2737 C  CD    . GLU A 1 393 ? 19.757  -43.450 9.158   1.00 61.75 ? 372 GLU A CD    1 
ATOM   2738 O  OE1   . GLU A 1 393 ? 19.992  -42.487 9.954   1.00 62.17 ? 372 GLU A OE1   1 
ATOM   2739 O  OE2   . GLU A 1 393 ? 20.393  -43.631 8.093   1.00 70.42 ? 372 GLU A OE2   1 
ATOM   2740 N  N     . ARG A 1 394 ? 14.668  -43.786 10.622  1.00 25.82 ? 373 ARG A N     1 
ATOM   2741 C  CA    . ARG A 1 394 ? 13.457  -43.841 9.756   1.00 26.30 ? 373 ARG A CA    1 
ATOM   2742 C  C     . ARG A 1 394 ? 12.964  -42.430 9.347   1.00 21.72 ? 373 ARG A C     1 
ATOM   2743 O  O     . ARG A 1 394 ? 12.163  -42.338 8.413   1.00 21.42 ? 373 ARG A O     1 
ATOM   2744 C  CB    . ARG A 1 394 ? 12.283  -44.627 10.361  1.00 32.52 ? 373 ARG A CB    1 
ATOM   2745 C  CG    . ARG A 1 394 ? 11.251  -44.955 9.283   1.00 43.79 ? 373 ARG A CG    1 
ATOM   2746 C  CD    . ARG A 1 394 ? 10.014  -45.743 9.662   1.00 51.24 ? 373 ARG A CD    1 
ATOM   2747 N  NE    . ARG A 1 394 ? 10.448  -47.015 10.195  1.00 63.59 ? 373 ARG A NE    1 
ATOM   2748 C  CZ    . ARG A 1 394 ? 9.643   -47.989 10.585  1.00 68.44 ? 373 ARG A CZ    1 
ATOM   2749 N  NH1   . ARG A 1 394 ? 8.328   -47.848 10.499  1.00 64.77 ? 373 ARG A NH1   1 
ATOM   2750 N  NH2   . ARG A 1 394 ? 10.175  -49.109 11.046  1.00 71.73 ? 373 ARG A NH2   1 
ATOM   2751 N  N     . ALA A 1 395 ? 13.330  -41.382 10.055  1.00 22.41 ? 374 ALA A N     1 
ATOM   2752 C  CA    . ALA A 1 395 ? 12.967  -39.980 9.708   1.00 21.02 ? 374 ALA A CA    1 
ATOM   2753 C  C     . ALA A 1 395 ? 13.396  -39.650 8.277   1.00 21.18 ? 374 ALA A C     1 
ATOM   2754 O  O     . ALA A 1 395 ? 12.810  -38.750 7.647   1.00 20.04 ? 374 ALA A O     1 
ATOM   2755 C  CB    . ALA A 1 395 ? 13.613  -39.057 10.712  1.00 20.79 ? 374 ALA A CB    1 
ATOM   2756 N  N     . ARG A 1 396 ? 14.374  -40.373 7.734   1.00 22.34 ? 375 ARG A N     1 
ATOM   2757 C  CA    . ARG A 1 396 ? 14.911  -40.111 6.370   1.00 24.34 ? 375 ARG A CA    1 
ATOM   2758 C  C     . ARG A 1 396 ? 13.911  -40.579 5.313   1.00 24.67 ? 375 ARG A C     1 
ATOM   2759 O  O     . ARG A 1 396 ? 13.941  -40.084 4.159   1.00 22.22 ? 375 ARG A O     1 
ATOM   2760 C  CB    . ARG A 1 396 ? 16.307  -40.725 6.199   1.00 24.18 ? 375 ARG A CB    1 
ATOM   2761 C  CG    . ARG A 1 396 ? 17.348  -40.057 7.087   1.00 25.45 ? 375 ARG A CG    1 
ATOM   2762 C  CD    . ARG A 1 396 ? 18.807  -40.413 6.842   1.00 28.28 ? 375 ARG A CD    1 
ATOM   2763 N  NE    . ARG A 1 396 ? 19.704  -39.754 7.791   1.00 32.70 ? 375 ARG A NE    1 
ATOM   2764 C  CZ    . ARG A 1 396 ? 20.002  -38.435 7.804   1.00 35.49 ? 375 ARG A CZ    1 
ATOM   2765 N  NH1   . ARG A 1 396 ? 19.416  -37.619 6.947   1.00 38.75 ? 375 ARG A NH1   1 
ATOM   2766 N  NH2   . ARG A 1 396 ? 20.834  -37.906 8.705   1.00 36.40 ? 375 ARG A NH2   1 
ATOM   2767 N  N     . ASP A 1 397 ? 13.016  -41.482 5.681   1.00 26.02 ? 376 ASP A N     1 
ATOM   2768 C  CA    . ASP A 1 397 ? 12.016  -42.054 4.743   1.00 25.11 ? 376 ASP A CA    1 
ATOM   2769 C  C     . ASP A 1 397 ? 10.774  -41.156 4.773   1.00 24.78 ? 376 ASP A C     1 
ATOM   2770 O  O     . ASP A 1 397 ? 9.701   -41.594 5.166   1.00 25.23 ? 376 ASP A O     1 
ATOM   2771 C  CB    . ASP A 1 397 ? 11.748  -43.527 5.075   1.00 31.49 ? 376 ASP A CB    1 
ATOM   2772 C  CG    . ASP A 1 397 ? 10.930  -44.221 3.997   1.00 35.89 ? 376 ASP A CG    1 
ATOM   2773 O  OD1   . ASP A 1 397 ? 10.908  -43.708 2.864   1.00 39.40 ? 376 ASP A OD1   1 
ATOM   2774 O  OD2   . ASP A 1 397 ? 10.285  -45.228 4.312   1.00 41.76 ? 376 ASP A OD2   1 
ATOM   2775 N  N     . VAL A 1 398 ? 10.944  -39.921 4.300   1.00 23.06 ? 377 VAL A N     1 
ATOM   2776 C  CA    . VAL A 1 398 ? 9.922   -38.854 4.309   1.00 24.50 ? 377 VAL A CA    1 
ATOM   2777 C  C     . VAL A 1 398 ? 9.031   -39.002 3.068   1.00 25.55 ? 377 VAL A C     1 
ATOM   2778 O  O     . VAL A 1 398 ? 9.513   -39.313 1.963   1.00 24.75 ? 377 VAL A O     1 
ATOM   2779 C  CB    . VAL A 1 398 ? 10.604  -37.475 4.417   1.00 27.78 ? 377 VAL A CB    1 
ATOM   2780 C  CG1   . VAL A 1 398 ? 11.697  -37.301 3.394   1.00 26.73 ? 377 VAL A CG1   1 
ATOM   2781 C  CG2   . VAL A 1 398 ? 9.611   -36.323 4.307   1.00 29.44 ? 377 VAL A CG2   1 
ATOM   2782 N  N     . ARG A 1 399 ? 7.751   -38.759 3.250   1.00 21.69 ? 378 ARG A N     1 
ATOM   2783 C  CA    . ARG A 1 399 ? 6.758   -38.680 2.154   1.00 24.07 ? 378 ARG A CA    1 
ATOM   2784 C  C     . ARG A 1 399 ? 6.734   -37.266 1.601   1.00 22.60 ? 378 ARG A C     1 
ATOM   2785 O  O     . ARG A 1 399 ? 6.536   -37.120 0.395   1.00 21.27 ? 378 ARG A O     1 
ATOM   2786 C  CB    . ARG A 1 399 ? 5.375   -39.047 2.671   1.00 31.52 ? 378 ARG A CB    1 
ATOM   2787 C  CG    . ARG A 1 399 ? 4.321   -39.167 1.580   1.00 41.01 ? 378 ARG A CG    1 
ATOM   2788 C  CD    . ARG A 1 399 ? 4.649   -40.357 0.705   1.00 53.51 ? 378 ARG A CD    1 
ATOM   2789 N  NE    . ARG A 1 399 ? 3.568   -40.759 -0.191  1.00 71.66 ? 378 ARG A NE    1 
ATOM   2790 C  CZ    . ARG A 1 399 ? 3.453   -41.969 -0.743  1.00 75.88 ? 378 ARG A CZ    1 
ATOM   2791 N  NH1   . ARG A 1 399 ? 4.338   -42.915 -0.463  1.00 78.65 ? 378 ARG A NH1   1 
ATOM   2792 N  NH2   . ARG A 1 399 ? 2.442   -42.232 -1.560  1.00 77.99 ? 378 ARG A NH2   1 
ATOM   2793 N  N     . ASP A 1 400 ? 6.773   -36.240 2.467   1.00 20.04 ? 379 ASP A N     1 
ATOM   2794 C  CA    . ASP A 1 400 ? 6.595   -34.838 1.995   1.00 18.89 ? 379 ASP A CA    1 
ATOM   2795 C  C     . ASP A 1 400 ? 7.061   -33.903 3.098   1.00 18.51 ? 379 ASP A C     1 
ATOM   2796 O  O     . ASP A 1 400 ? 7.201   -34.341 4.254   1.00 19.58 ? 379 ASP A O     1 
ATOM   2797 C  CB    . ASP A 1 400 ? 5.156   -34.557 1.600   1.00 19.37 ? 379 ASP A CB    1 
ATOM   2798 C  CG    . ASP A 1 400 ? 4.909   -33.365 0.686   1.00 23.42 ? 379 ASP A CG    1 
ATOM   2799 O  OD1   . ASP A 1 400 ? 5.876   -32.709 0.274   1.00 22.50 ? 379 ASP A OD1   1 
ATOM   2800 O  OD2   . ASP A 1 400 ? 3.716   -33.144 0.393   1.00 27.71 ? 379 ASP A OD2   1 
ATOM   2801 N  N     . TYR A 1 401 ? 7.396   -32.678 2.736   1.00 17.75 ? 380 TYR A N     1 
ATOM   2802 C  CA    . TYR A 1 401 ? 7.841   -31.636 3.686   1.00 16.94 ? 380 TYR A CA    1 
ATOM   2803 C  C     . TYR A 1 401 ? 7.124   -30.357 3.237   1.00 17.66 ? 380 TYR A C     1 
ATOM   2804 O  O     . TYR A 1 401 ? 7.302   -29.992 2.053   1.00 17.43 ? 380 TYR A O     1 
ATOM   2805 C  CB    . TYR A 1 401 ? 9.370   -31.567 3.697   1.00 18.76 ? 380 TYR A CB    1 
ATOM   2806 C  CG    . TYR A 1 401 ? 9.889   -30.377 4.448   1.00 17.34 ? 380 TYR A CG    1 
ATOM   2807 C  CD1   . TYR A 1 401 ? 10.095  -29.178 3.790   1.00 19.30 ? 380 TYR A CD1   1 
ATOM   2808 C  CD2   . TYR A 1 401 ? 10.084  -30.411 5.820   1.00 17.61 ? 380 TYR A CD2   1 
ATOM   2809 C  CE1   . TYR A 1 401 ? 10.516  -28.052 4.474   1.00 18.62 ? 380 TYR A CE1   1 
ATOM   2810 C  CE2   . TYR A 1 401 ? 10.555  -29.303 6.507   1.00 18.42 ? 380 TYR A CE2   1 
ATOM   2811 C  CZ    . TYR A 1 401 ? 10.753  -28.109 5.833   1.00 17.08 ? 380 TYR A CZ    1 
ATOM   2812 O  OH    . TYR A 1 401 ? 11.136  -27.003 6.521   1.00 18.54 ? 380 TYR A OH    1 
ATOM   2813 N  N     . ILE A 1 402 ? 6.323   -29.747 4.122   1.00 16.41 ? 381 ILE A N     1 
ATOM   2814 C  CA    . ILE A 1 402 ? 5.479   -28.567 3.805   1.00 18.18 ? 381 ILE A CA    1 
ATOM   2815 C  C     . ILE A 1 402 ? 5.871   -27.484 4.799   1.00 17.80 ? 381 ILE A C     1 
ATOM   2816 O  O     . ILE A 1 402 ? 5.870   -27.750 6.008   1.00 18.52 ? 381 ILE A O     1 
ATOM   2817 C  CB    . ILE A 1 402 ? 3.988   -28.914 3.855   1.00 17.45 ? 381 ILE A CB    1 
ATOM   2818 C  CG1   . ILE A 1 402 ? 3.683   -30.075 2.897   1.00 18.77 ? 381 ILE A CG1   1 
ATOM   2819 C  CG2   . ILE A 1 402 ? 3.141   -27.699 3.497   1.00 18.08 ? 381 ILE A CG2   1 
ATOM   2820 C  CD1   . ILE A 1 402 ? 2.271   -30.618 3.047   1.00 20.04 ? 381 ILE A CD1   1 
ATOM   2821 N  N     . ASP A 1 403 ? 6.228   -26.313 4.292   1.00 16.49 ? 382 ASP A N     1 
ATOM   2822 C  CA    . ASP A 1 403 ? 6.586   -25.231 5.234   1.00 16.83 ? 382 ASP A CA    1 
ATOM   2823 C  C     . ASP A 1 403 ? 6.141   -23.872 4.718   1.00 16.91 ? 382 ASP A C     1 
ATOM   2824 O  O     . ASP A 1 403 ? 5.660   -23.746 3.591   1.00 17.32 ? 382 ASP A O     1 
ATOM   2825 C  CB    . ASP A 1 403 ? 8.066   -25.324 5.625   1.00 17.40 ? 382 ASP A CB    1 
ATOM   2826 C  CG    . ASP A 1 403 ? 9.142   -24.789 4.683   1.00 18.07 ? 382 ASP A CG    1 
ATOM   2827 O  OD1   . ASP A 1 403 ? 8.800   -24.114 3.662   1.00 16.97 ? 382 ASP A OD1   1 
ATOM   2828 O  OD2   . ASP A 1 403 ? 10.358  -25.007 5.029   1.00 18.67 ? 382 ASP A OD2   1 
ATOM   2829 N  N     . ARG A 1 404 ? 6.263   -22.886 5.596   1.00 16.30 ? 383 ARG A N     1 
ATOM   2830 C  CA    . ARG A 1 404 ? 5.875   -21.499 5.265   1.00 17.00 ? 383 ARG A CA    1 
ATOM   2831 C  C     . ARG A 1 404 ? 6.781   -20.561 6.053   1.00 16.31 ? 383 ARG A C     1 
ATOM   2832 O  O     . ARG A 1 404 ? 6.863   -20.690 7.307   1.00 16.49 ? 383 ARG A O     1 
ATOM   2833 C  CB    . ARG A 1 404 ? 4.406   -21.205 5.572   1.00 18.14 ? 383 ARG A CB    1 
ATOM   2834 C  CG    . ARG A 1 404 ? 4.055   -19.785 5.141   1.00 21.74 ? 383 ARG A CG    1 
ATOM   2835 C  CD    . ARG A 1 404 ? 2.862   -19.586 4.258   1.00 27.90 ? 383 ARG A CD    1 
ATOM   2836 N  NE    . ARG A 1 404 ? 2.764   -20.560 3.208   1.00 30.11 ? 383 ARG A NE    1 
ATOM   2837 C  CZ    . ARG A 1 404 ? 1.624   -20.895 2.621   1.00 37.81 ? 383 ARG A CZ    1 
ATOM   2838 N  NH1   . ARG A 1 404 ? 0.504   -20.256 2.933   1.00 35.42 ? 383 ARG A NH1   1 
ATOM   2839 N  NH2   . ARG A 1 404 ? 1.634   -21.847 1.694   1.00 34.55 ? 383 ARG A NH2   1 
ATOM   2840 N  N     . ASP A 1 405 ? 7.435   -19.660 5.327   1.00 15.63 ? 384 ASP A N     1 
ATOM   2841 C  CA    . ASP A 1 405 ? 8.254   -18.581 5.915   1.00 15.22 ? 384 ASP A CA    1 
ATOM   2842 C  C     . ASP A 1 405 ? 7.315   -17.375 6.075   1.00 15.59 ? 384 ASP A C     1 
ATOM   2843 O  O     . ASP A 1 405 ? 7.001   -16.712 5.060   1.00 14.22 ? 384 ASP A O     1 
ATOM   2844 C  CB    . ASP A 1 405 ? 9.506   -18.245 5.107   1.00 15.78 ? 384 ASP A CB    1 
ATOM   2845 C  CG    . ASP A 1 405 ? 10.220  -17.048 5.731   1.00 16.66 ? 384 ASP A CG    1 
ATOM   2846 O  OD1   . ASP A 1 405 ? 9.763   -16.555 6.852   1.00 18.52 ? 384 ASP A OD1   1 
ATOM   2847 O  OD2   . ASP A 1 405 ? 11.184  -16.567 5.111   1.00 19.18 ? 384 ASP A OD2   1 
ATOM   2848 N  N     . TRP A 1 406 ? 6.816   -17.123 7.295   1.00 13.66 ? 385 TRP A N     1 
ATOM   2849 C  CA    . TRP A 1 406 ? 5.823   -16.044 7.497   1.00 16.04 ? 385 TRP A CA    1 
ATOM   2850 C  C     . TRP A 1 406 ? 6.437   -14.650 7.276   1.00 16.35 ? 385 TRP A C     1 
ATOM   2851 O  O     . TRP A 1 406 ? 5.694   -13.741 6.971   1.00 14.40 ? 385 TRP A O     1 
ATOM   2852 C  CB    . TRP A 1 406 ? 5.097   -16.216 8.829   1.00 14.80 ? 385 TRP A CB    1 
ATOM   2853 C  CG    . TRP A 1 406 ? 4.074   -17.307 8.706   1.00 14.53 ? 385 TRP A CG    1 
ATOM   2854 C  CD1   . TRP A 1 406 ? 4.250   -18.635 8.949   1.00 15.89 ? 385 TRP A CD1   1 
ATOM   2855 C  CD2   . TRP A 1 406 ? 2.712   -17.159 8.277   1.00 15.27 ? 385 TRP A CD2   1 
ATOM   2856 N  NE1   . TRP A 1 406 ? 3.092   -19.319 8.706   1.00 14.81 ? 385 TRP A NE1   1 
ATOM   2857 C  CE2   . TRP A 1 406 ? 2.123   -18.441 8.293   1.00 15.64 ? 385 TRP A CE2   1 
ATOM   2858 C  CE3   . TRP A 1 406 ? 1.942   -16.071 7.853   1.00 15.43 ? 385 TRP A CE3   1 
ATOM   2859 C  CZ2   . TRP A 1 406 ? 0.782   -18.659 7.940   1.00 15.49 ? 385 TRP A CZ2   1 
ATOM   2860 C  CZ3   . TRP A 1 406 ? 0.612   -16.280 7.522   1.00 17.01 ? 385 TRP A CZ3   1 
ATOM   2861 C  CH2   . TRP A 1 406 ? 0.036   -17.565 7.557   1.00 16.23 ? 385 TRP A CH2   1 
ATOM   2862 N  N     . SER A 1 407 ? 7.758   -14.527 7.328   1.00 16.15 ? 386 SER A N     1 
ATOM   2863 C  CA    . SER A 1 407 ? 8.454   -13.248 7.048   1.00 17.08 ? 386 SER A CA    1 
ATOM   2864 C  C     . SER A 1 407 ? 8.349   -12.945 5.551   1.00 17.03 ? 386 SER A C     1 
ATOM   2865 O  O     . SER A 1 407 ? 8.517   -11.736 5.202   1.00 16.17 ? 386 SER A O     1 
ATOM   2866 C  CB    . SER A 1 407 ? 9.884   -13.298 7.511   1.00 16.94 ? 386 SER A CB    1 
ATOM   2867 O  OG    . SER A 1 407 ? 9.960   -13.739 8.868   1.00 19.40 ? 386 SER A OG    1 
ATOM   2868 N  N     . ALA A 1 408 ? 8.157   -13.968 4.690   1.00 14.70 ? 387 ALA A N     1 
ATOM   2869 C  CA    . ALA A 1 408 ? 8.091   -13.796 3.212   1.00 16.71 ? 387 ALA A CA    1 
ATOM   2870 C  C     . ALA A 1 408 ? 6.658   -13.489 2.750   1.00 19.24 ? 387 ALA A C     1 
ATOM   2871 O  O     . ALA A 1 408 ? 6.459   -13.166 1.594   1.00 20.89 ? 387 ALA A O     1 
ATOM   2872 C  CB    . ALA A 1 408 ? 8.634   -15.035 2.513   1.00 17.35 ? 387 ALA A CB    1 
ATOM   2873 N  N     . GLU A 1 409 ? 5.674   -13.571 3.650   1.00 17.65 ? 388 GLU A N     1 
ATOM   2874 C  CA    . GLU A 1 409 ? 4.257   -13.265 3.339   1.00 17.06 ? 388 GLU A CA    1 
ATOM   2875 C  C     . GLU A 1 409 ? 4.094   -11.757 3.291   1.00 16.09 ? 388 GLU A C     1 
ATOM   2876 O  O     . GLU A 1 409 ? 4.210   -11.091 4.307   1.00 14.72 ? 388 GLU A O     1 
ATOM   2877 C  CB    . GLU A 1 409 ? 3.354   -13.874 4.415   1.00 16.66 ? 388 GLU A CB    1 
ATOM   2878 C  CG    . GLU A 1 409 ? 3.255   -15.372 4.332   1.00 17.12 ? 388 GLU A CG    1 
ATOM   2879 C  CD    . GLU A 1 409 ? 2.396   -15.879 3.183   1.00 21.60 ? 388 GLU A CD    1 
ATOM   2880 O  OE1   . GLU A 1 409 ? 2.859   -16.803 2.499   1.00 21.79 ? 388 GLU A OE1   1 
ATOM   2881 O  OE2   . GLU A 1 409 ? 1.259   -15.349 2.975   1.00 18.38 ? 388 GLU A OE2   1 
ATOM   2882 N  N     . PRO A 1 410 ? 3.848   -11.121 2.118   1.00 17.21 ? 389 PRO A N     1 
ATOM   2883 C  CA    . PRO A 1 410 ? 3.762   -9.666  2.090   1.00 15.99 ? 389 PRO A CA    1 
ATOM   2884 C  C     . PRO A 1 410 ? 2.639   -9.090  2.977   1.00 16.18 ? 389 PRO A C     1 
ATOM   2885 O  O     . PRO A 1 410 ? 2.738   -7.952  3.354   1.00 14.57 ? 389 PRO A O     1 
ATOM   2886 C  CB    . PRO A 1 410 ? 3.504   -9.326  0.617   1.00 18.09 ? 389 PRO A CB    1 
ATOM   2887 C  CG    . PRO A 1 410 ? 3.137   -10.613 -0.040  1.00 18.36 ? 389 PRO A CG    1 
ATOM   2888 C  CD    . PRO A 1 410 ? 3.755   -11.732 0.785   1.00 17.67 ? 389 PRO A CD    1 
ATOM   2889 N  N     . TRP A 1 411 ? 1.588   -9.869  3.273   1.00 15.67 ? 390 TRP A N     1 
ATOM   2890 C  CA    . TRP A 1 411 ? 0.429   -9.398  4.077   1.00 17.80 ? 390 TRP A CA    1 
ATOM   2891 C  C     . TRP A 1 411 ? 0.522   -9.878  5.541   1.00 18.92 ? 390 TRP A C     1 
ATOM   2892 O  O     . TRP A 1 411 ? -0.433  -9.683  6.342   1.00 18.45 ? 390 TRP A O     1 
ATOM   2893 C  CB    . TRP A 1 411 ? -0.863  -9.812  3.353   1.00 19.11 ? 390 TRP A CB    1 
ATOM   2894 C  CG    . TRP A 1 411 ? -0.937  -9.214  1.978   1.00 18.97 ? 390 TRP A CG    1 
ATOM   2895 C  CD1   . TRP A 1 411 ? -0.992  -9.881  0.782   1.00 18.80 ? 390 TRP A CD1   1 
ATOM   2896 C  CD2   . TRP A 1 411 ? -0.910  -7.815  1.655   1.00 17.45 ? 390 TRP A CD2   1 
ATOM   2897 N  NE1   . TRP A 1 411 ? -0.990  -8.981  -0.257  1.00 19.10 ? 390 TRP A NE1   1 
ATOM   2898 C  CE2   . TRP A 1 411 ? -0.936  -7.712  0.247   1.00 17.90 ? 390 TRP A CE2   1 
ATOM   2899 C  CE3   . TRP A 1 411 ? -0.799  -6.638  2.410   1.00 18.10 ? 390 TRP A CE3   1 
ATOM   2900 C  CZ2   . TRP A 1 411 ? -0.883  -6.476  -0.410  1.00 19.35 ? 390 TRP A CZ2   1 
ATOM   2901 C  CZ3   . TRP A 1 411 ? -0.779  -5.422  1.758   1.00 19.75 ? 390 TRP A CZ3   1 
ATOM   2902 C  CH2   . TRP A 1 411 ? -0.823  -5.348  0.364   1.00 18.96 ? 390 TRP A CH2   1 
ATOM   2903 N  N     . THR A 1 412 ? 1.678   -10.348 5.962   1.00 17.02 ? 391 THR A N     1 
ATOM   2904 C  CA    . THR A 1 412 ? 1.998   -10.594 7.384   1.00 16.04 ? 391 THR A CA    1 
ATOM   2905 C  C     . THR A 1 412 ? 3.382   -10.015 7.746   1.00 15.82 ? 391 THR A C     1 
ATOM   2906 O  O     . THR A 1 412 ? 3.461   -9.226  8.689   1.00 15.02 ? 391 THR A O     1 
ATOM   2907 C  CB    . THR A 1 412 ? 2.004   -12.083 7.735   1.00 15.25 ? 391 THR A CB    1 
ATOM   2908 O  OG1   . THR A 1 412 ? 0.791   -12.733 7.371   1.00 14.28 ? 391 THR A OG1   1 
ATOM   2909 C  CG2   . THR A 1 412 ? 2.257   -12.306 9.200   1.00 15.98 ? 391 THR A CG2   1 
ATOM   2910 N  N     . ARG A 1 413 ? 4.446   -10.432 7.062   1.00 14.81 ? 392 ARG A N     1 
ATOM   2911 C  CA    . ARG A 1 413 ? 5.833   -9.908  7.261   1.00 15.48 ? 392 ARG A CA    1 
ATOM   2912 C  C     . ARG A 1 413 ? 6.338   -10.293 8.658   1.00 15.78 ? 392 ARG A C     1 
ATOM   2913 O  O     . ARG A 1 413 ? 7.163   -9.572  9.245   1.00 16.31 ? 392 ARG A O     1 
ATOM   2914 C  CB    . ARG A 1 413 ? 5.922   -8.410  6.967   1.00 17.84 ? 392 ARG A CB    1 
ATOM   2915 C  CG    . ARG A 1 413 ? 5.845   -8.083  5.485   1.00 16.83 ? 392 ARG A CG    1 
ATOM   2916 C  CD    . ARG A 1 413 ? 6.823   -8.898  4.641   1.00 18.43 ? 392 ARG A CD    1 
ATOM   2917 N  NE    . ARG A 1 413 ? 7.103   -8.304  3.347   1.00 18.91 ? 392 ARG A NE    1 
ATOM   2918 C  CZ    . ARG A 1 413 ? 7.955   -8.832  2.470   1.00 18.75 ? 392 ARG A CZ    1 
ATOM   2919 N  NH1   . ARG A 1 413 ? 8.598   -9.961  2.753   1.00 19.01 ? 392 ARG A NH1   1 
ATOM   2920 N  NH2   . ARG A 1 413 ? 8.160   -8.230  1.316   1.00 20.16 ? 392 ARG A NH2   1 
ATOM   2921 N  N     . GLY A 1 414 ? 5.914   -11.458 9.135   1.00 14.67 ? 393 GLY A N     1 
ATOM   2922 C  CA    . GLY A 1 414 ? 6.533   -12.169 10.263  1.00 14.47 ? 393 GLY A CA    1 
ATOM   2923 C  C     . GLY A 1 414 ? 5.483   -12.714 11.221  1.00 14.89 ? 393 GLY A C     1 
ATOM   2924 O  O     . GLY A 1 414 ? 4.522   -11.981 11.610  1.00 16.59 ? 393 GLY A O     1 
ATOM   2925 N  N     . CYS A 1 415 ? 5.724   -13.907 11.714  1.00 17.26 ? 394 CYS A N     1 
ATOM   2926 C  CA    . CYS A 1 415 ? 4.976   -14.513 12.832  1.00 16.93 ? 394 CYS A CA    1 
ATOM   2927 C  C     . CYS A 1 415 ? 5.900   -14.650 14.040  1.00 18.35 ? 394 CYS A C     1 
ATOM   2928 O  O     . CYS A 1 415 ? 7.123   -14.488 13.907  1.00 16.85 ? 394 CYS A O     1 
ATOM   2929 C  CB    . CYS A 1 415 ? 4.359   -15.839 12.384  1.00 16.99 ? 394 CYS A CB    1 
ATOM   2930 S  SG    . CYS A 1 415 ? 2.651   -15.604 11.803  1.00 17.35 ? 394 CYS A SG    1 
ATOM   2931 N  N     . TYR A 1 416 ? 5.325   -14.875 15.227  1.00 16.56 ? 395 TYR A N     1 
ATOM   2932 C  CA    . TYR A 1 416 ? 3.881   -14.962 15.459  1.00 17.36 ? 395 TYR A CA    1 
ATOM   2933 C  C     . TYR A 1 416 ? 3.216   -13.586 15.491  1.00 18.67 ? 395 TYR A C     1 
ATOM   2934 O  O     . TYR A 1 416 ? 2.038   -13.451 15.085  1.00 18.91 ? 395 TYR A O     1 
ATOM   2935 C  CB    . TYR A 1 416 ? 3.613   -15.675 16.778  1.00 17.40 ? 395 TYR A CB    1 
ATOM   2936 C  CG    . TYR A 1 416 ? 4.433   -16.916 16.914  1.00 17.64 ? 395 TYR A CG    1 
ATOM   2937 C  CD1   . TYR A 1 416 ? 4.322   -17.949 15.998  1.00 17.27 ? 395 TYR A CD1   1 
ATOM   2938 C  CD2   . TYR A 1 416 ? 5.349   -17.056 17.941  1.00 20.44 ? 395 TYR A CD2   1 
ATOM   2939 C  CE1   . TYR A 1 416 ? 5.083   -19.101 16.108  1.00 17.95 ? 395 TYR A CE1   1 
ATOM   2940 C  CE2   . TYR A 1 416 ? 6.153   -18.179 18.031  1.00 19.62 ? 395 TYR A CE2   1 
ATOM   2941 C  CZ    . TYR A 1 416 ? 6.000   -19.221 17.131  1.00 20.58 ? 395 TYR A CZ    1 
ATOM   2942 O  OH    . TYR A 1 416 ? 6.741   -20.379 17.214  1.00 24.28 ? 395 TYR A OH    1 
ATOM   2943 N  N     . GLY A 1 417 ? 3.942   -12.600 16.017  1.00 19.58 ? 396 GLY A N     1 
ATOM   2944 C  CA    . GLY A 1 417 ? 3.458   -11.219 16.095  1.00 19.03 ? 396 GLY A CA    1 
ATOM   2945 C  C     . GLY A 1 417 ? 4.602   -10.274 16.385  1.00 20.64 ? 396 GLY A C     1 
ATOM   2946 O  O     . GLY A 1 417 ? 5.781   -10.692 16.362  1.00 18.91 ? 396 GLY A O     1 
ATOM   2947 N  N     . ALA A 1 418 ? 4.269   -9.056  16.766  1.00 18.62 ? 397 ALA A N     1 
ATOM   2948 C  CA    . ALA A 1 418 ? 5.287   -8.011  17.003  1.00 17.61 ? 397 ALA A CA    1 
ATOM   2949 C  C     . ALA A 1 418 ? 5.920   -8.230  18.385  1.00 17.94 ? 397 ALA A C     1 
ATOM   2950 O  O     . ALA A 1 418 ? 5.275   -8.796  19.329  1.00 16.25 ? 397 ALA A O     1 
ATOM   2951 C  CB    . ALA A 1 418 ? 4.660   -6.664  16.873  1.00 19.55 ? 397 ALA A CB    1 
ATOM   2952 N  N     . HIS A 1 419 ? 7.157   -7.789  18.524  1.00 17.45 ? 398 HIS A N     1 
ATOM   2953 C  CA    . HIS A 1 419 ? 7.811   -7.585  19.843  1.00 18.57 ? 398 HIS A CA    1 
ATOM   2954 C  C     . HIS A 1 419 ? 8.348   -6.156  19.905  1.00 18.81 ? 398 HIS A C     1 
ATOM   2955 O  O     . HIS A 1 419 ? 8.356   -5.440  18.866  1.00 19.69 ? 398 HIS A O     1 
ATOM   2956 C  CB    . HIS A 1 419 ? 8.888   -8.629  20.108  1.00 18.56 ? 398 HIS A CB    1 
ATOM   2957 C  CG    . HIS A 1 419 ? 10.047  -8.536  19.170  1.00 19.15 ? 398 HIS A CG    1 
ATOM   2958 N  ND1   . HIS A 1 419 ? 10.148  -9.296  18.051  1.00 20.38 ? 398 HIS A ND1   1 
ATOM   2959 C  CD2   . HIS A 1 419 ? 11.144  -7.746  19.195  1.00 22.74 ? 398 HIS A CD2   1 
ATOM   2960 C  CE1   . HIS A 1 419 ? 11.239  -8.957  17.387  1.00 21.03 ? 398 HIS A CE1   1 
ATOM   2961 N  NE2   . HIS A 1 419 ? 11.896  -8.034  18.101  1.00 19.65 ? 398 HIS A NE2   1 
ATOM   2962 N  N     . LEU A 1 420 ? 8.671   -5.727  21.119  1.00 17.34 ? 399 LEU A N     1 
ATOM   2963 C  CA    . LEU A 1 420 ? 9.133   -4.357  21.376  1.00 17.12 ? 399 LEU A CA    1 
ATOM   2964 C  C     . LEU A 1 420 ? 10.488  -4.433  22.026  1.00 16.82 ? 399 LEU A C     1 
ATOM   2965 O  O     . LEU A 1 420 ? 10.693  -5.067  23.066  1.00 17.50 ? 399 LEU A O     1 
ATOM   2966 C  CB    . LEU A 1 420 ? 8.107   -3.591  22.210  1.00 19.65 ? 399 LEU A CB    1 
ATOM   2967 C  CG    . LEU A 1 420 ? 6.891   -3.096  21.414  1.00 20.43 ? 399 LEU A CG    1 
ATOM   2968 C  CD1   . LEU A 1 420 ? 5.847   -4.197  21.299  1.00 22.25 ? 399 LEU A CD1   1 
ATOM   2969 C  CD2   . LEU A 1 420 ? 6.302   -1.846  22.034  1.00 21.14 ? 399 LEU A CD2   1 
ATOM   2970 N  N     . PRO A 1 421 ? 11.485  -3.781  21.394  1.00 18.69 ? 400 PRO A N     1 
ATOM   2971 C  CA    . PRO A 1 421 ? 12.843  -3.742  21.928  1.00 18.65 ? 400 PRO A CA    1 
ATOM   2972 C  C     . PRO A 1 421 ? 12.903  -2.768  23.085  1.00 16.13 ? 400 PRO A C     1 
ATOM   2973 O  O     . PRO A 1 421 ? 11.953  -2.013  23.345  1.00 15.77 ? 400 PRO A O     1 
ATOM   2974 C  CB    . PRO A 1 421 ? 13.671  -3.197  20.736  1.00 19.17 ? 400 PRO A CB    1 
ATOM   2975 C  CG    . PRO A 1 421 ? 12.684  -2.256  20.126  1.00 22.79 ? 400 PRO A CG    1 
ATOM   2976 C  CD    . PRO A 1 421 ? 11.373  -3.035  20.133  1.00 21.60 ? 400 PRO A CD    1 
ATOM   2977 N  N     . PRO A 1 422 ? 14.049  -2.709  23.787  1.00 18.33 ? 401 PRO A N     1 
ATOM   2978 C  CA    . PRO A 1 422 ? 14.216  -1.726  24.866  1.00 17.92 ? 401 PRO A CA    1 
ATOM   2979 C  C     . PRO A 1 422 ? 13.878  -0.300  24.451  1.00 19.21 ? 401 PRO A C     1 
ATOM   2980 O  O     . PRO A 1 422 ? 14.305  0.159   23.364  1.00 16.68 ? 401 PRO A O     1 
ATOM   2981 C  CB    . PRO A 1 422 ? 15.694  -1.861  25.302  1.00 18.91 ? 401 PRO A CB    1 
ATOM   2982 C  CG    . PRO A 1 422 ? 16.066  -3.223  24.817  1.00 20.83 ? 401 PRO A CG    1 
ATOM   2983 C  CD    . PRO A 1 422 ? 15.263  -3.514  23.567  1.00 18.56 ? 401 PRO A CD    1 
ATOM   2984 N  N     . GLY A 1 423 ? 13.124  0.356   25.327  1.00 19.61 ? 402 GLY A N     1 
ATOM   2985 C  CA    . GLY A 1 423 ? 12.787  1.783   25.258  1.00 19.54 ? 402 GLY A CA    1 
ATOM   2986 C  C     . GLY A 1 423 ? 11.514  2.062   24.484  1.00 21.02 ? 402 GLY A C     1 
ATOM   2987 O  O     . GLY A 1 423 ? 11.159  3.229   24.423  1.00 26.55 ? 402 GLY A O     1 
ATOM   2988 N  N     . ALA A 1 424 ? 10.844  1.058   23.908  1.00 17.98 ? 403 ALA A N     1 
ATOM   2989 C  CA    . ALA A 1 424 ? 9.675   1.266   23.019  1.00 17.88 ? 403 ALA A CA    1 
ATOM   2990 C  C     . ALA A 1 424 ? 8.375   1.337   23.822  1.00 19.75 ? 403 ALA A C     1 
ATOM   2991 O  O     . ALA A 1 424 ? 7.601   2.268   23.574  1.00 19.28 ? 403 ALA A O     1 
ATOM   2992 C  CB    . ALA A 1 424 ? 9.602   0.188   21.948  1.00 19.72 ? 403 ALA A CB    1 
ATOM   2993 N  N     . TRP A 1 425 ? 8.140   0.436   24.785  1.00 17.12 ? 404 TRP A N     1 
ATOM   2994 C  CA    . TRP A 1 425 ? 6.837   0.408   25.512  1.00 18.09 ? 404 TRP A CA    1 
ATOM   2995 C  C     . TRP A 1 425 ? 6.614   1.724   26.251  1.00 18.44 ? 404 TRP A C     1 
ATOM   2996 O  O     . TRP A 1 425 ? 5.515   2.203   26.205  1.00 18.07 ? 404 TRP A O     1 
ATOM   2997 C  CB    . TRP A 1 425 ? 6.756   -0.792  26.482  1.00 17.93 ? 404 TRP A CB    1 
ATOM   2998 C  CG    . TRP A 1 425 ? 6.075   -1.996  25.912  1.00 19.63 ? 404 TRP A CG    1 
ATOM   2999 C  CD1   . TRP A 1 425 ? 6.626   -3.238  25.720  1.00 19.58 ? 404 TRP A CD1   1 
ATOM   3000 C  CD2   . TRP A 1 425 ? 4.716   -2.094  25.454  1.00 20.60 ? 404 TRP A CD2   1 
ATOM   3001 N  NE1   . TRP A 1 425 ? 5.685   -4.103  25.223  1.00 20.06 ? 404 TRP A NE1   1 
ATOM   3002 C  CE2   . TRP A 1 425 ? 4.517   -3.417  25.025  1.00 19.66 ? 404 TRP A CE2   1 
ATOM   3003 C  CE3   . TRP A 1 425 ? 3.656   -1.187  25.390  1.00 22.52 ? 404 TRP A CE3   1 
ATOM   3004 C  CZ2   . TRP A 1 425 ? 3.314   -3.856  24.487  1.00 22.57 ? 404 TRP A CZ2   1 
ATOM   3005 C  CZ3   . TRP A 1 425 ? 2.456   -1.622  24.860  1.00 24.45 ? 404 TRP A CZ3   1 
ATOM   3006 C  CH2   . TRP A 1 425 ? 2.293   -2.941  24.421  1.00 24.66 ? 404 TRP A CH2   1 
ATOM   3007 N  N     . THR A 1 426 ? 7.620   2.281   26.940  1.00 19.87 ? 405 THR A N     1 
ATOM   3008 C  CA    . THR A 1 426 ? 7.420   3.491   27.781  1.00 20.00 ? 405 THR A CA    1 
ATOM   3009 C  C     . THR A 1 426 ? 7.321   4.749   26.919  1.00 19.66 ? 405 THR A C     1 
ATOM   3010 O  O     . THR A 1 426 ? 6.565   5.596   27.292  1.00 22.23 ? 405 THR A O     1 
ATOM   3011 C  CB    . THR A 1 426 ? 8.489   3.615   28.870  1.00 20.54 ? 405 THR A CB    1 
ATOM   3012 O  OG1   . THR A 1 426 ? 9.768   3.503   28.248  1.00 21.45 ? 405 THR A OG1   1 
ATOM   3013 C  CG2   . THR A 1 426 ? 8.283   2.533   29.903  1.00 19.91 ? 405 THR A CG2   1 
ATOM   3014 N  N     . VAL A 1 427 ? 8.074   4.881   25.835  1.00 16.86 ? 406 VAL A N     1 
ATOM   3015 C  CA    . VAL A 1 427 ? 8.105   6.160   25.091  1.00 16.48 ? 406 VAL A CA    1 
ATOM   3016 C  C     . VAL A 1 427 ? 7.028   6.186   24.002  1.00 17.93 ? 406 VAL A C     1 
ATOM   3017 O  O     . VAL A 1 427 ? 6.399   7.241   23.830  1.00 19.64 ? 406 VAL A O     1 
ATOM   3018 C  CB    . VAL A 1 427 ? 9.519   6.365   24.532  1.00 16.58 ? 406 VAL A CB    1 
ATOM   3019 C  CG1   . VAL A 1 427 ? 9.622   7.596   23.645  1.00 16.90 ? 406 VAL A CG1   1 
ATOM   3020 C  CG2   . VAL A 1 427 ? 10.531  6.418   25.665  1.00 17.86 ? 406 VAL A CG2   1 
ATOM   3021 N  N     . TYR A 1 428 ? 6.807   5.075   23.290  1.00 16.73 ? 407 TYR A N     1 
ATOM   3022 C  CA    . TYR A 1 428 ? 5.936   5.028   22.086  1.00 16.34 ? 407 TYR A CA    1 
ATOM   3023 C  C     . TYR A 1 428 ? 4.668   4.217   22.373  1.00 15.86 ? 407 TYR A C     1 
ATOM   3024 O  O     . TYR A 1 428 ? 3.640   4.540   21.802  1.00 16.05 ? 407 TYR A O     1 
ATOM   3025 C  CB    . TYR A 1 428 ? 6.709   4.434   20.886  1.00 15.99 ? 407 TYR A CB    1 
ATOM   3026 C  CG    . TYR A 1 428 ? 8.023   5.114   20.622  1.00 15.56 ? 407 TYR A CG    1 
ATOM   3027 C  CD1   . TYR A 1 428 ? 8.094   6.254   19.858  1.00 16.64 ? 407 TYR A CD1   1 
ATOM   3028 C  CD2   . TYR A 1 428 ? 9.211   4.592   21.101  1.00 17.15 ? 407 TYR A CD2   1 
ATOM   3029 C  CE1   . TYR A 1 428 ? 9.305   6.907   19.649  1.00 17.34 ? 407 TYR A CE1   1 
ATOM   3030 C  CE2   . TYR A 1 428 ? 10.417  5.239   20.920  1.00 18.40 ? 407 TYR A CE2   1 
ATOM   3031 C  CZ    . TYR A 1 428 ? 10.463  6.405   20.189  1.00 18.59 ? 407 TYR A CZ    1 
ATOM   3032 O  OH    . TYR A 1 428 ? 11.659  7.036   20.020  1.00 20.37 ? 407 TYR A OH    1 
ATOM   3033 N  N     . GLY A 1 429 ? 4.753   3.253   23.293  1.00 17.26 ? 408 GLY A N     1 
ATOM   3034 C  CA    . GLY A 1 429 ? 3.659   2.319   23.625  1.00 17.23 ? 408 GLY A CA    1 
ATOM   3035 C  C     . GLY A 1 429 ? 2.306   2.962   23.858  1.00 16.80 ? 408 GLY A C     1 
ATOM   3036 O  O     . GLY A 1 429 ? 1.273   2.372   23.479  1.00 18.26 ? 408 GLY A O     1 
ATOM   3037 N  N     . PRO A 1 430 ? 2.228   4.111   24.576  1.00 16.46 ? 409 PRO A N     1 
ATOM   3038 C  CA    . PRO A 1 430 ? 0.919   4.706   24.895  1.00 17.01 ? 409 PRO A CA    1 
ATOM   3039 C  C     . PRO A 1 430 ? 0.009   4.994   23.692  1.00 19.68 ? 409 PRO A C     1 
ATOM   3040 O  O     . PRO A 1 430 ? -1.200  5.098   23.860  1.00 18.67 ? 409 PRO A O     1 
ATOM   3041 C  CB    . PRO A 1 430 ? 1.340   5.986   25.631  1.00 17.59 ? 409 PRO A CB    1 
ATOM   3042 C  CG    . PRO A 1 430 ? 2.607   5.589   26.323  1.00 16.44 ? 409 PRO A CG    1 
ATOM   3043 C  CD    . PRO A 1 430 ? 3.356   4.841   25.234  1.00 17.39 ? 409 PRO A CD    1 
ATOM   3044 N  N     . ALA A 1 431 ? 0.570   5.033   22.478  1.00 19.70 ? 410 ALA A N     1 
ATOM   3045 C  CA    . ALA A 1 431 ? -0.198  5.280   21.235  1.00 18.67 ? 410 ALA A CA    1 
ATOM   3046 C  C     . ALA A 1 431 ? -0.798  3.970   20.676  1.00 18.15 ? 410 ALA A C     1 
ATOM   3047 O  O     . ALA A 1 431 ? -1.436  4.036   19.602  1.00 21.51 ? 410 ALA A O     1 
ATOM   3048 C  CB    . ALA A 1 431 ? 0.685   5.932   20.203  1.00 18.86 ? 410 ALA A CB    1 
ATOM   3049 N  N     . LEU A 1 432 ? -0.604  2.830   21.331  1.00 16.68 ? 411 LEU A N     1 
ATOM   3050 C  CA    . LEU A 1 432 ? -0.929  1.493   20.776  1.00 18.50 ? 411 LEU A CA    1 
ATOM   3051 C  C     . LEU A 1 432 ? -2.392  1.392   20.338  1.00 20.03 ? 411 LEU A C     1 
ATOM   3052 O  O     . LEU A 1 432 ? -2.654  0.859   19.236  1.00 19.48 ? 411 LEU A O     1 
ATOM   3053 C  CB    . LEU A 1 432 ? -0.644  0.423   21.830  1.00 19.58 ? 411 LEU A CB    1 
ATOM   3054 C  CG    . LEU A 1 432 ? -0.976  -0.993  21.387  1.00 20.04 ? 411 LEU A CG    1 
ATOM   3055 C  CD1   . LEU A 1 432 ? -0.158  -1.378  20.153  1.00 21.26 ? 411 LEU A CD1   1 
ATOM   3056 C  CD2   . LEU A 1 432 ? -0.753  -1.966  22.514  1.00 22.02 ? 411 LEU A CD2   1 
ATOM   3057 N  N     . ARG A 1 433 ? -3.327  1.786   21.199  1.00 18.52 ? 412 ARG A N     1 
ATOM   3058 C  CA    . ARG A 1 433 ? -4.767  1.494   20.992  1.00 24.44 ? 412 ARG A CA    1 
ATOM   3059 C  C     . ARG A 1 433 ? -5.574  2.752   20.716  1.00 22.06 ? 412 ARG A C     1 
ATOM   3060 O  O     . ARG A 1 433 ? -6.764  2.598   20.397  1.00 23.48 ? 412 ARG A O     1 
ATOM   3061 C  CB    . ARG A 1 433 ? -5.396  0.948   22.272  1.00 26.09 ? 412 ARG A CB    1 
ATOM   3062 C  CG    . ARG A 1 433 ? -5.314  -0.538  22.404  1.00 31.65 ? 412 ARG A CG    1 
ATOM   3063 C  CD    . ARG A 1 433 ? -6.072  -0.884  23.667  1.00 30.02 ? 412 ARG A CD    1 
ATOM   3064 N  NE    . ARG A 1 433 ? -5.250  -1.950  24.054  1.00 33.42 ? 412 ARG A NE    1 
ATOM   3065 C  CZ    . ARG A 1 433 ? -4.260  -1.877  24.914  1.00 33.33 ? 412 ARG A CZ    1 
ATOM   3066 N  NH1   . ARG A 1 433 ? -4.033  -0.779  25.615  1.00 32.16 ? 412 ARG A NH1   1 
ATOM   3067 N  NH2   . ARG A 1 433 ? -3.549  -2.967  25.118  1.00 36.11 ? 412 ARG A NH2   1 
ATOM   3068 N  N     . VAL A 1 434 ? -5.023  3.916   21.029  1.00 21.16 ? 413 VAL A N     1 
ATOM   3069 C  CA    . VAL A 1 434 ? -5.772  5.206   21.025  1.00 23.95 ? 413 VAL A CA    1 
ATOM   3070 C  C     . VAL A 1 434 ? -6.282  5.473   19.614  1.00 20.13 ? 413 VAL A C     1 
ATOM   3071 O  O     . VAL A 1 434 ? -5.499  5.571   18.670  1.00 19.47 ? 413 VAL A O     1 
ATOM   3072 C  CB    . VAL A 1 434 ? -4.893  6.378   21.503  1.00 28.93 ? 413 VAL A CB    1 
ATOM   3073 C  CG1   . VAL A 1 434 ? -5.643  7.692   21.457  1.00 31.56 ? 413 VAL A CG1   1 
ATOM   3074 C  CG2   . VAL A 1 434 ? -4.324  6.122   22.879  1.00 35.66 ? 413 VAL A CG2   1 
ATOM   3075 N  N     . PRO A 1 435 ? -7.602  5.701   19.408  1.00 20.05 ? 414 PRO A N     1 
ATOM   3076 C  CA    . PRO A 1 435 ? -8.088  6.011   18.068  1.00 19.88 ? 414 PRO A CA    1 
ATOM   3077 C  C     . PRO A 1 435 ? -7.450  7.313   17.575  1.00 19.98 ? 414 PRO A C     1 
ATOM   3078 O  O     . PRO A 1 435 ? -7.214  8.217   18.362  1.00 18.00 ? 414 PRO A O     1 
ATOM   3079 C  CB    . PRO A 1 435 ? -9.605  6.191   18.209  1.00 21.13 ? 414 PRO A CB    1 
ATOM   3080 C  CG    . PRO A 1 435 ? -9.940  5.575   19.523  1.00 24.29 ? 414 PRO A CG    1 
ATOM   3081 C  CD    . PRO A 1 435 ? -8.693  5.584   20.391  1.00 22.80 ? 414 PRO A CD    1 
ATOM   3082 N  N     . VAL A 1 436 ? -7.224  7.396   16.282  1.00 18.35 ? 415 VAL A N     1 
ATOM   3083 C  CA    . VAL A 1 436 ? -6.776  8.632   15.609  1.00 19.24 ? 415 VAL A CA    1 
ATOM   3084 C  C     . VAL A 1 436 ? -7.986  9.161   14.844  1.00 17.26 ? 415 VAL A C     1 
ATOM   3085 O  O     . VAL A 1 436 ? -8.280  8.717   13.735  1.00 17.60 ? 415 VAL A O     1 
ATOM   3086 C  CB    . VAL A 1 436 ? -5.519  8.377   14.755  1.00 18.74 ? 415 VAL A CB    1 
ATOM   3087 C  CG1   . VAL A 1 436 ? -5.136  9.592   13.934  1.00 19.90 ? 415 VAL A CG1   1 
ATOM   3088 C  CG2   . VAL A 1 436 ? -4.353  7.857   15.594  1.00 20.88 ? 415 VAL A CG2   1 
ATOM   3089 N  N     . GLY A 1 437 ? -8.728  10.075  15.452  1.00 18.76 ? 416 GLY A N     1 
ATOM   3090 C  CA    . GLY A 1 437 ? -9.965  10.594  14.848  1.00 18.85 ? 416 GLY A CA    1 
ATOM   3091 C  C     . GLY A 1 437 ? -10.971 9.479   14.626  1.00 18.88 ? 416 GLY A C     1 
ATOM   3092 O  O     . GLY A 1 437 ? -11.309 8.771   15.617  1.00 19.70 ? 416 GLY A O     1 
ATOM   3093 N  N     . ARG A 1 438 ? -11.287 9.168   13.378  1.00 18.51 ? 417 ARG A N     1 
ATOM   3094 C  CA    . ARG A 1 438 ? -12.330 8.148   13.055  1.00 18.76 ? 417 ARG A CA    1 
ATOM   3095 C  C     . ARG A 1 438 ? -11.696 6.780   12.735  1.00 18.41 ? 417 ARG A C     1 
ATOM   3096 O  O     . ARG A 1 438 ? -12.426 5.896   12.254  1.00 18.61 ? 417 ARG A O     1 
ATOM   3097 C  CB    . ARG A 1 438 ? -13.115 8.629   11.842  1.00 17.98 ? 417 ARG A CB    1 
ATOM   3098 C  CG    . ARG A 1 438 ? -14.010 9.830   12.133  1.00 20.18 ? 417 ARG A CG    1 
ATOM   3099 C  CD    . ARG A 1 438 ? -14.588 10.386  10.852  1.00 21.02 ? 417 ARG A CD    1 
ATOM   3100 N  NE    . ARG A 1 438 ? -15.530 11.441  11.182  1.00 24.94 ? 417 ARG A NE    1 
ATOM   3101 C  CZ    . ARG A 1 438 ? -16.811 11.265  11.419  1.00 30.05 ? 417 ARG A CZ    1 
ATOM   3102 N  NH1   . ARG A 1 438 ? -17.362 10.063  11.326  1.00 26.19 ? 417 ARG A NH1   1 
ATOM   3103 N  NH2   . ARG A 1 438 ? -17.551 12.315  11.726  1.00 32.40 ? 417 ARG A NH2   1 
ATOM   3104 N  N     . VAL A 1 439 ? -10.396 6.636   12.958  1.00 17.81 ? 418 VAL A N     1 
ATOM   3105 C  CA    . VAL A 1 439 ? -9.629  5.380   12.698  1.00 17.03 ? 418 VAL A CA    1 
ATOM   3106 C  C     . VAL A 1 439 ? -9.309  4.692   14.017  1.00 15.08 ? 418 VAL A C     1 
ATOM   3107 O  O     . VAL A 1 439 ? -8.612  5.270   14.883  1.00 17.36 ? 418 VAL A O     1 
ATOM   3108 C  CB    . VAL A 1 439 ? -8.369  5.646   11.855  1.00 18.87 ? 418 VAL A CB    1 
ATOM   3109 C  CG1   . VAL A 1 439 ? -7.561  4.377   11.606  1.00 17.62 ? 418 VAL A CG1   1 
ATOM   3110 C  CG2   . VAL A 1 439 ? -8.716  6.335   10.571  1.00 19.65 ? 418 VAL A CG2   1 
ATOM   3111 N  N     . HIS A 1 440 ? -9.856  3.503   14.204  1.00 14.15 ? 419 HIS A N     1 
ATOM   3112 C  CA    . HIS A 1 440 ? -9.672  2.677   15.413  1.00 14.79 ? 419 HIS A CA    1 
ATOM   3113 C  C     . HIS A 1 440 ? -8.780  1.493   15.044  1.00 16.39 ? 419 HIS A C     1 
ATOM   3114 O  O     . HIS A 1 440 ? -8.670  1.165   13.817  1.00 16.99 ? 419 HIS A O     1 
ATOM   3115 C  CB    . HIS A 1 440 ? -11.017 2.220   15.941  1.00 17.20 ? 419 HIS A CB    1 
ATOM   3116 C  CG    . HIS A 1 440 ? -11.916 3.354   16.271  1.00 17.96 ? 419 HIS A CG    1 
ATOM   3117 N  ND1   . HIS A 1 440 ? -12.312 3.589   17.552  1.00 18.96 ? 419 HIS A ND1   1 
ATOM   3118 C  CD2   . HIS A 1 440 ? -12.578 4.244   15.498  1.00 18.68 ? 419 HIS A CD2   1 
ATOM   3119 C  CE1   . HIS A 1 440 ? -13.148 4.628   17.567  1.00 19.18 ? 419 HIS A CE1   1 
ATOM   3120 N  NE2   . HIS A 1 440 ? -13.318 5.044   16.343  1.00 18.54 ? 419 HIS A NE2   1 
ATOM   3121 N  N     . TRP A 1 441 ? -8.201  0.864   16.049  1.00 16.51 ? 420 TRP A N     1 
ATOM   3122 C  CA    . TRP A 1 441 ? -7.125  -0.143  15.904  1.00 15.70 ? 420 TRP A CA    1 
ATOM   3123 C  C     . TRP A 1 441 ? -7.553  -1.455  16.551  1.00 16.10 ? 420 TRP A C     1 
ATOM   3124 O  O     . TRP A 1 441 ? -8.045  -1.428  17.668  1.00 15.93 ? 420 TRP A O     1 
ATOM   3125 C  CB    . TRP A 1 441 ? -5.828  0.380   16.522  1.00 17.30 ? 420 TRP A CB    1 
ATOM   3126 C  CG    . TRP A 1 441 ? -5.486  1.767   16.096  1.00 17.63 ? 420 TRP A CG    1 
ATOM   3127 C  CD1   . TRP A 1 441 ? -5.574  2.885   16.872  1.00 17.32 ? 420 TRP A CD1   1 
ATOM   3128 C  CD2   . TRP A 1 441 ? -5.003  2.200   14.807  1.00 17.42 ? 420 TRP A CD2   1 
ATOM   3129 N  NE1   . TRP A 1 441 ? -5.207  3.985   16.137  1.00 19.18 ? 420 TRP A NE1   1 
ATOM   3130 C  CE2   . TRP A 1 441 ? -4.850  3.598   14.869  1.00 18.88 ? 420 TRP A CE2   1 
ATOM   3131 C  CE3   . TRP A 1 441 ? -4.676  1.546   13.617  1.00 18.42 ? 420 TRP A CE3   1 
ATOM   3132 C  CZ2   . TRP A 1 441 ? -4.400  4.351   13.779  1.00 18.19 ? 420 TRP A CZ2   1 
ATOM   3133 C  CZ3   . TRP A 1 441 ? -4.234  2.283   12.543  1.00 19.37 ? 420 TRP A CZ3   1 
ATOM   3134 C  CH2   . TRP A 1 441 ? -4.069  3.663   12.630  1.00 19.67 ? 420 TRP A CH2   1 
ATOM   3135 N  N     . ALA A 1 442 ? -7.386  -2.552  15.810  1.00 14.37 ? 421 ALA A N     1 
ATOM   3136 C  CA    . ALA A 1 442 ? -7.528  -3.909  16.340  1.00 15.86 ? 421 ALA A CA    1 
ATOM   3137 C  C     . ALA A 1 442 ? -6.349  -4.750  15.855  1.00 15.23 ? 421 ALA A C     1 
ATOM   3138 O  O     . ALA A 1 442 ? -5.430  -4.233  15.240  1.00 15.37 ? 421 ALA A O     1 
ATOM   3139 C  CB    . ALA A 1 442 ? -8.847  -4.499  15.927  1.00 15.08 ? 421 ALA A CB    1 
ATOM   3140 N  N     . GLY A 1 443 ? -6.349  -5.997  16.281  1.00 15.49 ? 422 GLY A N     1 
ATOM   3141 C  CA    . GLY A 1 443 ? -5.271  -6.955  16.027  1.00 14.97 ? 422 GLY A CA    1 
ATOM   3142 C  C     . GLY A 1 443 ? -4.760  -7.482  17.339  1.00 14.58 ? 422 GLY A C     1 
ATOM   3143 O  O     . GLY A 1 443 ? -4.835  -6.772  18.379  1.00 16.15 ? 422 GLY A O     1 
ATOM   3144 N  N     . THR A 1 444 ? -4.211  -8.673  17.305  1.00 15.01 ? 423 THR A N     1 
ATOM   3145 C  CA    . THR A 1 444 ? -3.745  -9.386  18.521  1.00 15.94 ? 423 THR A CA    1 
ATOM   3146 C  C     . THR A 1 444 ? -2.757  -8.527  19.318  1.00 15.97 ? 423 THR A C     1 
ATOM   3147 O  O     . THR A 1 444 ? -2.738  -8.608  20.572  1.00 17.20 ? 423 THR A O     1 
ATOM   3148 C  CB    . THR A 1 444 ? -3.174  -10.750 18.156  1.00 14.05 ? 423 THR A CB    1 
ATOM   3149 O  OG1   . THR A 1 444 ? -3.139  -11.450 19.417  1.00 15.28 ? 423 THR A OG1   1 
ATOM   3150 C  CG2   . THR A 1 444 ? -1.824  -10.691 17.476  1.00 14.95 ? 423 THR A CG2   1 
ATOM   3151 N  N     . GLU A 1 445 ? -1.972  -7.723  18.621  1.00 16.24 ? 424 GLU A N     1 
ATOM   3152 C  CA    . GLU A 1 445 ? -0.956  -6.849  19.246  1.00 17.16 ? 424 GLU A CA    1 
ATOM   3153 C  C     . GLU A 1 445 ? -1.618  -5.772  20.114  1.00 17.84 ? 424 GLU A C     1 
ATOM   3154 O  O     . GLU A 1 445 ? -0.888  -5.199  20.964  1.00 17.18 ? 424 GLU A O     1 
ATOM   3155 C  CB    . GLU A 1 445 ? -0.103  -6.214  18.159  1.00 16.35 ? 424 GLU A CB    1 
ATOM   3156 C  CG    . GLU A 1 445 ? 0.939   -7.150  17.574  1.00 17.31 ? 424 GLU A CG    1 
ATOM   3157 C  CD    . GLU A 1 445 ? 0.514   -8.073  16.446  1.00 18.70 ? 424 GLU A CD    1 
ATOM   3158 O  OE1   . GLU A 1 445 ? 1.361   -8.915  16.061  1.00 19.30 ? 424 GLU A OE1   1 
ATOM   3159 O  OE2   . GLU A 1 445 ? -0.659  -7.960  15.954  1.00 20.02 ? 424 GLU A OE2   1 
ATOM   3160 N  N     . THR A 1 446 ? -2.932  -5.538  20.009  1.00 16.57 ? 425 THR A N     1 
ATOM   3161 C  CA    . THR A 1 446 ? -3.643  -4.539  20.868  1.00 17.75 ? 425 THR A CA    1 
ATOM   3162 C  C     . THR A 1 446 ? -4.448  -5.195  21.997  1.00 15.85 ? 425 THR A C     1 
ATOM   3163 O  O     . THR A 1 446 ? -5.097  -4.451  22.762  1.00 16.50 ? 425 THR A O     1 
ATOM   3164 C  CB    . THR A 1 446 ? -4.576  -3.631  20.062  1.00 17.04 ? 425 THR A CB    1 
ATOM   3165 O  OG1   . THR A 1 446 ? -5.633  -4.396  19.456  1.00 17.96 ? 425 THR A OG1   1 
ATOM   3166 C  CG2   . THR A 1 446 ? -3.841  -2.878  18.980  1.00 19.57 ? 425 THR A CG2   1 
ATOM   3167 N  N     . ALA A 1 447 ? -4.384  -6.506  22.149  1.00 16.21 ? 426 ALA A N     1 
ATOM   3168 C  CA    . ALA A 1 447 ? -5.110  -7.283  23.181  1.00 17.24 ? 426 ALA A CA    1 
ATOM   3169 C  C     . ALA A 1 447 ? -4.434  -7.100  24.541  1.00 17.23 ? 426 ALA A C     1 
ATOM   3170 O  O     . ALA A 1 447 ? -3.172  -7.029  24.600  1.00 17.16 ? 426 ALA A O     1 
ATOM   3171 C  CB    . ALA A 1 447 ? -5.208  -8.746  22.825  1.00 19.78 ? 426 ALA A CB    1 
ATOM   3172 N  N     . GLU A 1 448 ? -5.263  -7.065  25.592  1.00 17.70 ? 427 GLU A N     1 
ATOM   3173 C  CA    . GLU A 1 448 ? -4.824  -7.098  26.995  1.00 18.45 ? 427 GLU A CA    1 
ATOM   3174 C  C     . GLU A 1 448 ? -4.499  -8.540  27.375  1.00 17.39 ? 427 GLU A C     1 
ATOM   3175 O  O     . GLU A 1 448 ? -3.495  -8.716  28.043  1.00 18.08 ? 427 GLU A O     1 
ATOM   3176 C  CB    . GLU A 1 448 ? -5.911  -6.549  27.931  1.00 21.51 ? 427 GLU A CB    1 
ATOM   3177 C  CG    . GLU A 1 448 ? -6.277  -5.107  27.660  1.00 22.79 ? 427 GLU A CG    1 
ATOM   3178 C  CD    . GLU A 1 448 ? -7.280  -4.515  28.659  1.00 28.45 ? 427 GLU A CD    1 
ATOM   3179 O  OE1   . GLU A 1 448 ? -7.965  -3.588  28.287  1.00 35.53 ? 427 GLU A OE1   1 
ATOM   3180 O  OE2   . GLU A 1 448 ? -7.425  -5.043  29.761  1.00 33.91 ? 427 GLU A OE2   1 
ATOM   3181 N  N     . ARG A 1 449 ? -5.363  -9.512  27.035  1.00 17.26 ? 428 ARG A N     1 
ATOM   3182 C  CA    . ARG A 1 449 ? -5.213  -10.928 27.408  1.00 17.95 ? 428 ARG A CA    1 
ATOM   3183 C  C     . ARG A 1 449 ? -4.893  -11.784 26.166  1.00 16.20 ? 428 ARG A C     1 
ATOM   3184 O  O     . ARG A 1 449 ? -5.525  -11.595 25.107  1.00 17.10 ? 428 ARG A O     1 
ATOM   3185 C  CB    . ARG A 1 449 ? -6.451  -11.464 28.152  1.00 20.69 ? 428 ARG A CB    1 
ATOM   3186 C  CG    . ARG A 1 449 ? -6.721  -10.809 29.515  1.00 22.62 ? 428 ARG A CG    1 
ATOM   3187 C  CD    . ARG A 1 449 ? -7.901  -11.444 30.235  1.00 24.60 ? 428 ARG A CD    1 
ATOM   3188 N  NE    . ARG A 1 449 ? -7.702  -12.880 30.210  1.00 28.03 ? 428 ARG A NE    1 
ATOM   3189 C  CZ    . ARG A 1 449 ? -8.405  -13.750 29.468  1.00 28.04 ? 428 ARG A CZ    1 
ATOM   3190 N  NH1   . ARG A 1 449 ? -8.085  -15.034 29.485  1.00 23.34 ? 428 ARG A NH1   1 
ATOM   3191 N  NH2   . ARG A 1 449 ? -9.449  -13.346 28.755  1.00 31.36 ? 428 ARG A NH2   1 
ATOM   3192 N  N     . TRP A 1 450 ? -3.934  -12.703 26.294  1.00 15.64 ? 429 TRP A N     1 
ATOM   3193 C  CA    . TRP A 1 450 ? -3.469  -13.593 25.207  1.00 14.79 ? 429 TRP A CA    1 
ATOM   3194 C  C     . TRP A 1 450 ? -3.078  -12.753 23.972  1.00 14.00 ? 429 TRP A C     1 
ATOM   3195 O  O     . TRP A 1 450 ? -3.339  -13.181 22.834  1.00 15.42 ? 429 TRP A O     1 
ATOM   3196 C  CB    . TRP A 1 450 ? -4.529  -14.647 24.899  1.00 15.03 ? 429 TRP A CB    1 
ATOM   3197 C  CG    . TRP A 1 450 ? -4.583  -15.710 25.970  1.00 14.80 ? 429 TRP A CG    1 
ATOM   3198 C  CD1   . TRP A 1 450 ? -5.565  -15.935 26.884  1.00 16.23 ? 429 TRP A CD1   1 
ATOM   3199 C  CD2   . TRP A 1 450 ? -3.576  -16.704 26.209  1.00 15.17 ? 429 TRP A CD2   1 
ATOM   3200 N  NE1   . TRP A 1 450 ? -5.228  -16.982 27.715  1.00 16.10 ? 429 TRP A NE1   1 
ATOM   3201 C  CE2   . TRP A 1 450 ? -4.028  -17.500 27.294  1.00 17.26 ? 429 TRP A CE2   1 
ATOM   3202 C  CE3   . TRP A 1 450 ? -2.374  -17.032 25.563  1.00 16.99 ? 429 TRP A CE3   1 
ATOM   3203 C  CZ2   . TRP A 1 450 ? -3.304  -18.600 27.750  1.00 16.42 ? 429 TRP A CZ2   1 
ATOM   3204 C  CZ3   . TRP A 1 450 ? -1.641  -18.107 26.029  1.00 16.68 ? 429 TRP A CZ3   1 
ATOM   3205 C  CH2   . TRP A 1 450 ? -2.096  -18.865 27.117  1.00 17.15 ? 429 TRP A CH2   1 
ATOM   3206 N  N     . THR A 1 451 ? -2.384  -11.630 24.195  1.00 14.29 ? 430 THR A N     1 
ATOM   3207 C  CA    . THR A 1 451 ? -1.718  -10.857 23.124  1.00 14.46 ? 430 THR A CA    1 
ATOM   3208 C  C     . THR A 1 451 ? -0.744  -11.820 22.410  1.00 14.20 ? 430 THR A C     1 
ATOM   3209 O  O     . THR A 1 451 ? -0.056  -12.612 23.076  1.00 13.49 ? 430 THR A O     1 
ATOM   3210 C  CB    . THR A 1 451 ? -1.069  -9.556  23.614  1.00 15.05 ? 430 THR A CB    1 
ATOM   3211 O  OG1   . THR A 1 451 ? -0.750  -8.808  22.427  1.00 14.98 ? 430 THR A OG1   1 
ATOM   3212 C  CG2   . THR A 1 451 ? 0.127   -9.769  24.512  1.00 14.98 ? 430 THR A CG2   1 
ATOM   3213 N  N     . GLY A 1 452 ? -0.749  -11.774 21.083  1.00 14.24 ? 431 GLY A N     1 
ATOM   3214 C  CA    . GLY A 1 452 ? 0.062   -12.661 20.212  1.00 14.65 ? 431 GLY A CA    1 
ATOM   3215 C  C     . GLY A 1 452 ? -0.678  -13.896 19.761  1.00 15.89 ? 431 GLY A C     1 
ATOM   3216 O  O     . GLY A 1 452 ? -0.071  -14.651 18.937  1.00 16.06 ? 431 GLY A O     1 
ATOM   3217 N  N     . TYR A 1 453 ? -1.876  -14.174 20.293  1.00 14.45 ? 432 TYR A N     1 
ATOM   3218 C  CA    . TYR A 1 453 ? -2.626  -15.423 20.024  1.00 15.47 ? 432 TYR A CA    1 
ATOM   3219 C  C     . TYR A 1 453 ? -3.950  -15.089 19.336  1.00 15.40 ? 432 TYR A C     1 
ATOM   3220 O  O     . TYR A 1 453 ? -4.343  -13.919 19.291  1.00 15.44 ? 432 TYR A O     1 
ATOM   3221 C  CB    . TYR A 1 453 ? -2.866  -16.224 21.322  1.00 14.37 ? 432 TYR A CB    1 
ATOM   3222 C  CG    . TYR A 1 453 ? -1.603  -16.743 21.955  1.00 15.90 ? 432 TYR A CG    1 
ATOM   3223 C  CD1   . TYR A 1 453 ? -1.197  -18.052 21.781  1.00 15.59 ? 432 TYR A CD1   1 
ATOM   3224 C  CD2   . TYR A 1 453 ? -0.737  -15.898 22.651  1.00 14.27 ? 432 TYR A CD2   1 
ATOM   3225 C  CE1   . TYR A 1 453 ? -0.011  -18.534 22.318  1.00 15.30 ? 432 TYR A CE1   1 
ATOM   3226 C  CE2   . TYR A 1 453 ? 0.484   -16.355 23.128  1.00 15.73 ? 432 TYR A CE2   1 
ATOM   3227 C  CZ    . TYR A 1 453 ? 0.838   -17.679 23.007  1.00 16.51 ? 432 TYR A CZ    1 
ATOM   3228 O  OH    . TYR A 1 453 ? 2.061   -18.151 23.434  1.00 18.70 ? 432 TYR A OH    1 
ATOM   3229 N  N     . ILE A 1 454 ? -4.574  -16.127 18.801  1.00 14.98 ? 433 ILE A N     1 
ATOM   3230 C  CA    . ILE A 1 454 ? -5.926  -16.040 18.177  1.00 15.69 ? 433 ILE A CA    1 
ATOM   3231 C  C     . ILE A 1 454 ? -6.901  -15.426 19.199  1.00 15.15 ? 433 ILE A C     1 
ATOM   3232 O  O     . ILE A 1 454 ? -7.697  -14.559 18.844  1.00 13.87 ? 433 ILE A O     1 
ATOM   3233 C  CB    . ILE A 1 454 ? -6.373  -17.410 17.640  1.00 15.42 ? 433 ILE A CB    1 
ATOM   3234 C  CG1   . ILE A 1 454 ? -5.447  -17.941 16.529  1.00 17.13 ? 433 ILE A CG1   1 
ATOM   3235 C  CG2   . ILE A 1 454 ? -7.810  -17.292 17.161  1.00 16.94 ? 433 ILE A CG2   1 
ATOM   3236 C  CD1   . ILE A 1 454 ? -5.586  -19.437 16.252  1.00 18.30 ? 433 ILE A CD1   1 
ATOM   3237 N  N     . ASP A 1 455 ? -6.841  -15.866 20.446  1.00 16.52 ? 434 ASP A N     1 
ATOM   3238 C  CA    . ASP A 1 455 ? -7.763  -15.447 21.516  1.00 16.26 ? 434 ASP A CA    1 
ATOM   3239 C  C     . ASP A 1 455 ? -7.645  -13.930 21.689  1.00 17.21 ? 434 ASP A C     1 
ATOM   3240 O  O     . ASP A 1 455 ? -8.671  -13.259 21.765  1.00 15.89 ? 434 ASP A O     1 
ATOM   3241 C  CB    . ASP A 1 455 ? -7.428  -16.209 22.807  1.00 17.18 ? 434 ASP A CB    1 
ATOM   3242 C  CG    . ASP A 1 455 ? -8.504  -16.050 23.847  1.00 19.19 ? 434 ASP A CG    1 
ATOM   3243 O  OD1   . ASP A 1 455 ? -8.304  -15.224 24.771  1.00 17.60 ? 434 ASP A OD1   1 
ATOM   3244 O  OD2   . ASP A 1 455 ? -9.539  -16.719 23.701  1.00 18.38 ? 434 ASP A OD2   1 
ATOM   3245 N  N     . GLY A 1 456 ? -6.417  -13.396 21.712  1.00 16.11 ? 435 GLY A N     1 
ATOM   3246 C  CA    . GLY A 1 456 ? -6.161  -11.943 21.751  1.00 17.40 ? 435 GLY A CA    1 
ATOM   3247 C  C     . GLY A 1 456 ? -6.698  -11.229 20.514  1.00 16.56 ? 435 GLY A C     1 
ATOM   3248 O  O     . GLY A 1 456 ? -7.241  -10.117 20.655  1.00 14.06 ? 435 GLY A O     1 
ATOM   3249 N  N     . ALA A 1 457 ? -6.539  -11.797 19.318  1.00 15.63 ? 436 ALA A N     1 
ATOM   3250 C  CA    . ALA A 1 457 ? -7.079  -11.164 18.091  1.00 14.83 ? 436 ALA A CA    1 
ATOM   3251 C  C     . ALA A 1 457 ? -8.599  -10.949 18.265  1.00 14.21 ? 436 ALA A C     1 
ATOM   3252 O  O     . ALA A 1 457 ? -9.120  -9.861  17.970  1.00 14.48 ? 436 ALA A O     1 
ATOM   3253 C  CB    . ALA A 1 457 ? -6.768  -12.038 16.891  1.00 14.18 ? 436 ALA A CB    1 
ATOM   3254 N  N     . ILE A 1 458 ? -9.305  -11.954 18.783  1.00 15.93 ? 437 ILE A N     1 
ATOM   3255 C  CA    . ILE A 1 458 ? -10.781 -11.893 18.976  1.00 14.46 ? 437 ILE A CA    1 
ATOM   3256 C  C     . ILE A 1 458 ? -11.122 -10.808 20.007  1.00 15.44 ? 437 ILE A C     1 
ATOM   3257 O  O     . ILE A 1 458 ? -11.961 -9.932  19.713  1.00 16.61 ? 437 ILE A O     1 
ATOM   3258 C  CB    . ILE A 1 458 ? -11.323 -13.261 19.377  1.00 15.55 ? 437 ILE A CB    1 
ATOM   3259 C  CG1   . ILE A 1 458 ? -11.153 -14.307 18.276  1.00 15.08 ? 437 ILE A CG1   1 
ATOM   3260 C  CG2   . ILE A 1 458 ? -12.794 -13.174 19.758  1.00 15.69 ? 437 ILE A CG2   1 
ATOM   3261 C  CD1   . ILE A 1 458 ? -11.313 -15.738 18.819  1.00 17.58 ? 437 ILE A CD1   1 
ATOM   3262 N  N     . GLU A 1 459 ? -10.413 -10.782 21.130  1.00 15.15 ? 438 GLU A N     1 
ATOM   3263 C  CA    . GLU A 1 459 ? -10.572 -9.704  22.136  1.00 15.06 ? 438 GLU A CA    1 
ATOM   3264 C  C     . GLU A 1 459 ? -10.496 -8.339  21.428  1.00 14.52 ? 438 GLU A C     1 
ATOM   3265 O  O     . GLU A 1 459 ? -11.366 -7.439  21.668  1.00 14.67 ? 438 GLU A O     1 
ATOM   3266 C  CB    . GLU A 1 459 ? -9.501  -9.757  23.230  1.00 16.81 ? 438 GLU A CB    1 
ATOM   3267 C  CG    . GLU A 1 459 ? -9.715  -8.646  24.248  1.00 18.22 ? 438 GLU A CG    1 
ATOM   3268 C  CD    . GLU A 1 459 ? -8.499  -8.338  25.110  1.00 20.63 ? 438 GLU A CD    1 
ATOM   3269 O  OE1   . GLU A 1 459 ? -8.030  -7.186  25.085  1.00 23.15 ? 438 GLU A OE1   1 
ATOM   3270 O  OE2   . GLU A 1 459 ? -8.072  -9.239  25.806  1.00 22.97 ? 438 GLU A OE2   1 
ATOM   3271 N  N     . SER A 1 460 ? -9.442  -8.114  20.660  1.00 14.48 ? 439 SER A N     1 
ATOM   3272 C  CA    . SER A 1 460 ? -9.162  -6.786  20.041  1.00 14.92 ? 439 SER A CA    1 
ATOM   3273 C  C     . SER A 1 460 ? -10.304 -6.387  19.104  1.00 15.54 ? 439 SER A C     1 
ATOM   3274 O  O     . SER A 1 460 ? -10.680 -5.216  19.101  1.00 14.41 ? 439 SER A O     1 
ATOM   3275 C  CB    . SER A 1 460 ? -7.829  -6.783  19.336  1.00 15.43 ? 439 SER A CB    1 
ATOM   3276 O  OG    . SER A 1 460 ? -7.943  -7.471  18.078  1.00 15.06 ? 439 SER A OG    1 
ATOM   3277 N  N     . GLY A 1 461 ? -10.884 -7.326  18.358  1.00 15.49 ? 440 GLY A N     1 
ATOM   3278 C  CA    . GLY A 1 461 ? -12.021 -7.023  17.469  1.00 16.54 ? 440 GLY A CA    1 
ATOM   3279 C  C     . GLY A 1 461 ? -13.247 -6.640  18.274  1.00 15.84 ? 440 GLY A C     1 
ATOM   3280 O  O     . GLY A 1 461 ? -13.964 -5.722  17.869  1.00 15.64 ? 440 GLY A O     1 
ATOM   3281 N  N     . GLN A 1 462 ? -13.501 -7.329  19.385  1.00 17.68 ? 441 GLN A N     1 
ATOM   3282 C  CA    . GLN A 1 462 ? -14.682 -7.011  20.242  1.00 18.09 ? 441 GLN A CA    1 
ATOM   3283 C  C     . GLN A 1 462 ? -14.500 -5.584  20.763  1.00 18.49 ? 441 GLN A C     1 
ATOM   3284 O  O     . GLN A 1 462 ? -15.477 -4.800  20.745  1.00 18.16 ? 441 GLN A O     1 
ATOM   3285 C  CB    . GLN A 1 462 ? -14.779 -7.998  21.404  1.00 19.70 ? 441 GLN A CB    1 
ATOM   3286 C  CG    . GLN A 1 462 ? -15.143 -9.401  20.984  1.00 22.61 ? 441 GLN A CG    1 
ATOM   3287 C  CD    . GLN A 1 462 ? -14.972 -10.401 22.117  1.00 29.72 ? 441 GLN A CD    1 
ATOM   3288 O  OE1   . GLN A 1 462 ? -14.381 -10.115 23.164  1.00 34.96 ? 441 GLN A OE1   1 
ATOM   3289 N  NE2   . GLN A 1 462 ? -15.460 -11.612 21.913  1.00 33.55 ? 441 GLN A NE2   1 
ATOM   3290 N  N     . ARG A 1 463 ? -13.292 -5.266  21.206  1.00 17.13 ? 442 ARG A N     1 
ATOM   3291 C  CA    . ARG A 1 463 ? -12.990 -3.947  21.830  1.00 18.57 ? 442 ARG A CA    1 
ATOM   3292 C  C     . ARG A 1 463 ? -13.185 -2.846  20.774  1.00 17.93 ? 442 ARG A C     1 
ATOM   3293 O  O     . ARG A 1 463 ? -13.915 -1.820  21.079  1.00 17.17 ? 442 ARG A O     1 
ATOM   3294 C  CB    . ARG A 1 463 ? -11.591 -3.849  22.442  1.00 20.82 ? 442 ARG A CB    1 
ATOM   3295 C  CG    . ARG A 1 463 ? -11.358 -2.431  22.968  1.00 24.36 ? 442 ARG A CG    1 
ATOM   3296 C  CD    . ARG A 1 463 ? -9.969  -1.846  23.060  1.00 25.08 ? 442 ARG A CD    1 
ATOM   3297 N  NE    . ARG A 1 463 ? -9.048  -2.464  22.133  1.00 22.02 ? 442 ARG A NE    1 
ATOM   3298 C  CZ    . ARG A 1 463 ? -8.706  -2.000  20.943  1.00 21.27 ? 442 ARG A CZ    1 
ATOM   3299 N  NH1   . ARG A 1 463 ? -9.233  -0.878  20.471  1.00 19.39 ? 442 ARG A NH1   1 
ATOM   3300 N  NH2   . ARG A 1 463 ? -7.812  -2.694  20.233  1.00 20.85 ? 442 ARG A NH2   1 
ATOM   3301 N  N     . ALA A 1 464 ? -12.558 -2.982  19.591  1.00 16.86 ? 443 ALA A N     1 
ATOM   3302 C  CA    . ALA A 1 464 ? -12.649 -1.958  18.518  1.00 16.84 ? 443 ALA A CA    1 
ATOM   3303 C  C     . ALA A 1 464 ? -14.113 -1.777  18.075  1.00 16.86 ? 443 ALA A C     1 
ATOM   3304 O  O     . ALA A 1 464 ? -14.538 -0.620  17.797  1.00 16.75 ? 443 ALA A O     1 
ATOM   3305 C  CB    . ALA A 1 464 ? -11.743 -2.302  17.375  1.00 16.35 ? 443 ALA A CB    1 
ATOM   3306 N  N     . ALA A 1 465 ? -14.868 -2.870  17.911  1.00 17.72 ? 444 ALA A N     1 
ATOM   3307 C  CA    . ALA A 1 465 ? -16.307 -2.798  17.573  1.00 18.53 ? 444 ALA A CA    1 
ATOM   3308 C  C     . ALA A 1 465 ? -17.052 -1.968  18.624  1.00 17.23 ? 444 ALA A C     1 
ATOM   3309 O  O     . ALA A 1 465 ? -17.839 -1.072  18.196  1.00 17.28 ? 444 ALA A O     1 
ATOM   3310 C  CB    . ALA A 1 465 ? -16.894 -4.177  17.435  1.00 18.46 ? 444 ALA A CB    1 
ATOM   3311 N  N     . ALA A 1 466 ? -16.874 -2.267  19.915  1.00 18.54 ? 445 ALA A N     1 
ATOM   3312 C  CA    . ALA A 1 466 ? -17.590 -1.568  21.016  1.00 18.93 ? 445 ALA A CA    1 
ATOM   3313 C  C     . ALA A 1 466 ? -17.243 -0.071  20.959  1.00 20.16 ? 445 ALA A C     1 
ATOM   3314 O  O     . ALA A 1 466 ? -18.167 0.800   20.989  1.00 18.89 ? 445 ALA A O     1 
ATOM   3315 C  CB    . ALA A 1 466 ? -17.279 -2.218  22.356  1.00 18.94 ? 445 ALA A CB    1 
ATOM   3316 N  N     . GLU A 1 467 ? -15.986 0.266   20.665  1.00 19.74 ? 446 GLU A N     1 
ATOM   3317 C  CA    . GLU A 1 467 ? -15.570 1.691   20.543  1.00 20.57 ? 446 GLU A CA    1 
ATOM   3318 C  C     . GLU A 1 467 ? -16.289 2.386   19.399  1.00 19.40 ? 446 GLU A C     1 
ATOM   3319 O  O     . GLU A 1 467 ? -16.741 3.529   19.523  1.00 19.69 ? 446 GLU A O     1 
ATOM   3320 C  CB    . GLU A 1 467 ? -14.087 1.830   20.207  1.00 22.26 ? 446 GLU A CB    1 
ATOM   3321 C  CG    . GLU A 1 467 ? -13.174 1.669   21.369  1.00 23.89 ? 446 GLU A CG    1 
ATOM   3322 C  CD    . GLU A 1 467 ? -11.700 1.631   20.976  1.00 23.81 ? 446 GLU A CD    1 
ATOM   3323 O  OE1   . GLU A 1 467 ? -10.908 1.107   21.810  1.00 22.39 ? 446 GLU A OE1   1 
ATOM   3324 O  OE2   . GLU A 1 467 ? -11.367 2.071   19.838  1.00 23.59 ? 446 GLU A OE2   1 
ATOM   3325 N  N     . VAL A 1 468 ? -16.316 1.758   18.243  1.00 18.54 ? 447 VAL A N     1 
ATOM   3326 C  CA    . VAL A 1 468 ? -16.910 2.351   17.026  1.00 17.47 ? 447 VAL A CA    1 
ATOM   3327 C  C     . VAL A 1 468 ? -18.417 2.447   17.227  1.00 17.04 ? 447 VAL A C     1 
ATOM   3328 O  O     . VAL A 1 468 ? -19.029 3.497   16.819  1.00 17.35 ? 447 VAL A O     1 
ATOM   3329 C  CB    . VAL A 1 468 ? -16.489 1.528   15.797  1.00 20.92 ? 447 VAL A CB    1 
ATOM   3330 C  CG1   . VAL A 1 468 ? -17.422 1.687   14.629  1.00 25.77 ? 447 VAL A CG1   1 
ATOM   3331 C  CG2   . VAL A 1 468 ? -15.058 1.869   15.393  1.00 20.62 ? 447 VAL A CG2   1 
ATOM   3332 N  N     . LEU A 1 469 ? -19.032 1.440   17.832  1.00 17.55 ? 448 LEU A N     1 
ATOM   3333 C  CA    . LEU A 1 469 ? -20.509 1.448   17.996  1.00 18.38 ? 448 LEU A CA    1 
ATOM   3334 C  C     . LEU A 1 469 ? -20.932 2.571   18.944  1.00 18.16 ? 448 LEU A C     1 
ATOM   3335 O  O     . LEU A 1 469 ? -21.957 3.226   18.653  1.00 18.32 ? 448 LEU A O     1 
ATOM   3336 C  CB    . LEU A 1 469 ? -20.995 0.090   18.489  1.00 17.84 ? 448 LEU A CB    1 
ATOM   3337 C  CG    . LEU A 1 469 ? -20.895 -1.041  17.452  1.00 16.52 ? 448 LEU A CG    1 
ATOM   3338 C  CD1   . LEU A 1 469 ? -21.194 -2.397  18.072  1.00 17.44 ? 448 LEU A CD1   1 
ATOM   3339 C  CD2   . LEU A 1 469 ? -21.820 -0.789  16.301  1.00 18.90 ? 448 LEU A CD2   1 
ATOM   3340 N  N     . ALA A 1 470 ? -20.149 2.848   19.977  1.00 18.66 ? 449 ALA A N     1 
ATOM   3341 C  CA    . ALA A 1 470 ? -20.418 3.955   20.917  1.00 21.45 ? 449 ALA A CA    1 
ATOM   3342 C  C     . ALA A 1 470 ? -20.210 5.291   20.183  1.00 24.34 ? 449 ALA A C     1 
ATOM   3343 O  O     . ALA A 1 470 ? -21.030 6.192   20.326  1.00 23.75 ? 449 ALA A O     1 
ATOM   3344 C  CB    . ALA A 1 470 ? -19.546 3.827   22.119  1.00 23.17 ? 449 ALA A CB    1 
ATOM   3345 N  N     . ALA A 1 471 ? -19.158 5.410   19.386  1.00 23.26 ? 450 ALA A N     1 
ATOM   3346 C  CA    . ALA A 1 471 ? -18.840 6.622   18.595  1.00 21.98 ? 450 ALA A CA    1 
ATOM   3347 C  C     . ALA A 1 471 ? -19.934 6.927   17.568  1.00 24.94 ? 450 ALA A C     1 
ATOM   3348 O  O     . ALA A 1 471 ? -20.240 8.127   17.396  1.00 24.81 ? 450 ALA A O     1 
ATOM   3349 C  CB    . ALA A 1 471 ? -17.493 6.524   17.938  1.00 22.41 ? 450 ALA A CB    1 
ATOM   3350 N  N     . LEU A 1 472 ? -20.491 5.930   16.878  1.00 21.78 ? 451 LEU A N     1 
ATOM   3351 C  CA    . LEU A 1 472 ? -21.537 6.187   15.854  1.00 23.45 ? 451 LEU A CA    1 
ATOM   3352 C  C     . LEU A 1 472 ? -22.825 6.696   16.550  1.00 26.95 ? 451 LEU A C     1 
ATOM   3353 O  O     . LEU A 1 472 ? -23.566 7.398   15.857  1.00 28.20 ? 451 LEU A O     1 
ATOM   3354 C  CB    . LEU A 1 472 ? -21.827 4.912   15.066  1.00 21.91 ? 451 LEU A CB    1 
ATOM   3355 C  CG    . LEU A 1 472 ? -20.712 4.370   14.167  1.00 20.09 ? 451 LEU A CG    1 
ATOM   3356 C  CD1   . LEU A 1 472 ? -20.992 2.942   13.794  1.00 20.55 ? 451 LEU A CD1   1 
ATOM   3357 C  CD2   . LEU A 1 472 ? -20.556 5.183   12.928  1.00 22.23 ? 451 LEU A CD2   1 
ATOM   3358 N  N     . GLY A 1 473 ? -23.106 6.266   17.802  1.00 29.22 ? 452 GLY A N     1 
ATOM   3359 C  CA    . GLY A 1 473 ? -24.377 6.466   18.562  1.00 33.30 ? 452 GLY A CA    1 
ATOM   3360 C  C     . GLY A 1 473 ? -24.449 7.785   19.342  1.00 37.38 ? 452 GLY A C     1 
ATOM   3361 O  O     . GLY A 1 473 ? -23.452 8.516   19.502  1.00 43.62 ? 452 GLY A O     1 
ATOM   3362 N  N     . SER B 1 24  ? 3.844   6.403   -21.602 1.00 63.11 ? 3   SER B N     1 
ATOM   3363 C  CA    . SER B 1 24  ? 4.535   6.793   -20.324 1.00 57.05 ? 3   SER B CA    1 
ATOM   3364 C  C     . SER B 1 24  ? 6.052   6.877   -20.575 1.00 54.34 ? 3   SER B C     1 
ATOM   3365 O  O     . SER B 1 24  ? 6.556   6.115   -21.439 1.00 48.76 ? 3   SER B O     1 
ATOM   3366 C  CB    . SER B 1 24  ? 4.170   5.846   -19.204 1.00 54.42 ? 3   SER B CB    1 
ATOM   3367 O  OG    . SER B 1 24  ? 4.899   4.634   -19.293 1.00 46.88 ? 3   SER B OG    1 
ATOM   3368 N  N     . GLU B 1 25  ? 6.753   7.779   -19.875 1.00 48.16 ? 4   GLU B N     1 
ATOM   3369 C  CA    . GLU B 1 25  ? 8.190   8.104   -20.114 1.00 46.25 ? 4   GLU B CA    1 
ATOM   3370 C  C     . GLU B 1 25  ? 9.102   6.918   -19.785 1.00 43.05 ? 4   GLU B C     1 
ATOM   3371 O  O     . GLU B 1 25  ? 8.804   6.177   -18.819 1.00 33.70 ? 4   GLU B O     1 
ATOM   3372 C  CB    . GLU B 1 25  ? 8.635   9.287   -19.261 1.00 52.40 ? 4   GLU B CB    1 
ATOM   3373 C  CG    . GLU B 1 25  ? 8.131   10.609  -19.782 1.00 62.89 ? 4   GLU B CG    1 
ATOM   3374 C  CD    . GLU B 1 25  ? 8.380   11.733  -18.801 1.00 64.61 ? 4   GLU B CD    1 
ATOM   3375 O  OE1   . GLU B 1 25  ? 9.467   11.732  -18.202 1.00 69.02 ? 4   GLU B OE1   1 
ATOM   3376 O  OE2   . GLU B 1 25  ? 7.488   12.581  -18.627 1.00 68.95 ? 4   GLU B OE2   1 
ATOM   3377 N  N     . GLN B 1 26  ? 10.188  6.788   -20.552 1.00 39.21 ? 5   GLN B N     1 
ATOM   3378 C  CA    . GLN B 1 26  ? 11.206  5.711   -20.473 1.00 39.76 ? 5   GLN B CA    1 
ATOM   3379 C  C     . GLN B 1 26  ? 12.581  6.359   -20.220 1.00 40.99 ? 5   GLN B C     1 
ATOM   3380 O  O     . GLN B 1 26  ? 12.901  7.319   -20.922 1.00 38.32 ? 5   GLN B O     1 
ATOM   3381 C  CB    . GLN B 1 26  ? 11.118  4.888   -21.763 1.00 43.45 ? 5   GLN B CB    1 
ATOM   3382 C  CG    . GLN B 1 26  ? 12.354  4.049   -22.041 1.00 54.50 ? 5   GLN B CG    1 
ATOM   3383 C  CD    . GLN B 1 26  ? 12.360  2.736   -21.297 1.00 59.30 ? 5   GLN B CD    1 
ATOM   3384 O  OE1   . GLN B 1 26  ? 11.471  1.907   -21.494 1.00 71.49 ? 5   GLN B OE1   1 
ATOM   3385 N  NE2   . GLN B 1 26  ? 13.383  2.512   -20.470 1.00 53.08 ? 5   GLN B NE2   1 
ATOM   3386 N  N     . VAL B 1 27  ? 13.375  5.889   -19.248 1.00 30.81 ? 6   VAL B N     1 
ATOM   3387 C  CA    . VAL B 1 27  ? 14.722  6.463   -18.979 1.00 25.30 ? 6   VAL B CA    1 
ATOM   3388 C  C     . VAL B 1 27  ? 15.629  5.329   -18.526 1.00 26.35 ? 6   VAL B C     1 
ATOM   3389 O  O     . VAL B 1 27  ? 15.109  4.265   -18.167 1.00 26.80 ? 6   VAL B O     1 
ATOM   3390 C  CB    . VAL B 1 27  ? 14.717  7.619   -17.957 1.00 29.99 ? 6   VAL B CB    1 
ATOM   3391 C  CG1   . VAL B 1 27  ? 14.059  8.860   -18.518 1.00 33.05 ? 6   VAL B CG1   1 
ATOM   3392 C  CG2   . VAL B 1 27  ? 14.083  7.234   -16.619 1.00 29.17 ? 6   VAL B CG2   1 
ATOM   3393 N  N     . ASP B 1 28  ? 16.926  5.556   -18.515 1.00 22.38 ? 7   ASP B N     1 
ATOM   3394 C  CA    . ASP B 1 28  ? 17.930  4.574   -18.018 1.00 22.75 ? 7   ASP B CA    1 
ATOM   3395 C  C     . ASP B 1 28  ? 17.725  4.348   -16.512 1.00 25.18 ? 7   ASP B C     1 
ATOM   3396 O  O     . ASP B 1 28  ? 17.617  3.165   -16.084 1.00 21.72 ? 7   ASP B O     1 
ATOM   3397 C  CB    . ASP B 1 28  ? 19.362  5.002   -18.343 1.00 24.98 ? 7   ASP B CB    1 
ATOM   3398 C  CG    . ASP B 1 28  ? 19.720  4.989   -19.831 1.00 28.74 ? 7   ASP B CG    1 
ATOM   3399 O  OD1   . ASP B 1 28  ? 19.162  4.115   -20.552 1.00 26.72 ? 7   ASP B OD1   1 
ATOM   3400 O  OD2   . ASP B 1 28  ? 20.576  5.846   -20.249 1.00 28.29 ? 7   ASP B OD2   1 
ATOM   3401 N  N     . VAL B 1 29  ? 17.679  5.425   -15.717 1.00 23.39 ? 8   VAL B N     1 
ATOM   3402 C  CA    . VAL B 1 29  ? 17.754  5.310   -14.234 1.00 23.89 ? 8   VAL B CA    1 
ATOM   3403 C  C     . VAL B 1 29  ? 16.694  6.228   -13.623 1.00 24.06 ? 8   VAL B C     1 
ATOM   3404 O  O     . VAL B 1 29  ? 16.587  7.365   -14.063 1.00 20.24 ? 8   VAL B O     1 
ATOM   3405 C  CB    . VAL B 1 29  ? 19.155  5.614   -13.680 1.00 23.38 ? 8   VAL B CB    1 
ATOM   3406 C  CG1   . VAL B 1 29  ? 19.195  5.482   -12.167 1.00 24.92 ? 8   VAL B CG1   1 
ATOM   3407 C  CG2   . VAL B 1 29  ? 20.243  4.749   -14.305 1.00 22.76 ? 8   VAL B CG2   1 
ATOM   3408 N  N     . VAL B 1 30  ? 15.889  5.690   -12.711 1.00 19.42 ? 9   VAL B N     1 
ATOM   3409 C  CA    . VAL B 1 30  ? 15.000  6.512   -11.850 1.00 19.97 ? 9   VAL B CA    1 
ATOM   3410 C  C     . VAL B 1 30  ? 15.577  6.484   -10.436 1.00 21.11 ? 9   VAL B C     1 
ATOM   3411 O  O     . VAL B 1 30  ? 15.900  5.390   -9.884  1.00 19.97 ? 9   VAL B O     1 
ATOM   3412 C  CB    . VAL B 1 30  ? 13.538  6.061   -11.891 1.00 22.33 ? 9   VAL B CB    1 
ATOM   3413 C  CG1   . VAL B 1 30  ? 13.419  4.610   -11.511 1.00 27.68 ? 9   VAL B CG1   1 
ATOM   3414 C  CG2   . VAL B 1 30  ? 12.645  6.884   -10.987 1.00 22.60 ? 9   VAL B CG2   1 
ATOM   3415 N  N     . VAL B 1 31  ? 15.702  7.680   -9.875  1.00 20.06 ? 10  VAL B N     1 
ATOM   3416 C  CA    . VAL B 1 31  ? 16.172  7.909   -8.494  1.00 19.98 ? 10  VAL B CA    1 
ATOM   3417 C  C     . VAL B 1 31  ? 14.952  8.353   -7.669  1.00 18.40 ? 10  VAL B C     1 
ATOM   3418 O  O     . VAL B 1 31  ? 14.219  9.267   -8.069  1.00 18.17 ? 10  VAL B O     1 
ATOM   3419 C  CB    . VAL B 1 31  ? 17.301  8.939   -8.439  1.00 19.27 ? 10  VAL B CB    1 
ATOM   3420 C  CG1   . VAL B 1 31  ? 17.669  9.252   -7.002  1.00 19.66 ? 10  VAL B CG1   1 
ATOM   3421 C  CG2   . VAL B 1 31  ? 18.542  8.460   -9.205  1.00 21.39 ? 10  VAL B CG2   1 
ATOM   3422 N  N     . VAL B 1 32  ? 14.675  7.634   -6.608  1.00 17.47 ? 11  VAL B N     1 
ATOM   3423 C  CA    . VAL B 1 32  ? 13.582  7.981   -5.665  1.00 16.32 ? 11  VAL B CA    1 
ATOM   3424 C  C     . VAL B 1 32  ? 14.212  8.774   -4.524  1.00 16.61 ? 11  VAL B C     1 
ATOM   3425 O  O     . VAL B 1 32  ? 15.000  8.185   -3.726  1.00 18.20 ? 11  VAL B O     1 
ATOM   3426 C  CB    . VAL B 1 32  ? 12.869  6.715   -5.175  1.00 17.27 ? 11  VAL B CB    1 
ATOM   3427 C  CG1   . VAL B 1 32  ? 11.682  7.094   -4.326  1.00 16.21 ? 11  VAL B CG1   1 
ATOM   3428 C  CG2   . VAL B 1 32  ? 12.384  5.850   -6.352  1.00 18.82 ? 11  VAL B CG2   1 
ATOM   3429 N  N     . GLY B 1 33  ? 13.892  10.063  -4.469  1.00 16.94 ? 12  GLY B N     1 
ATOM   3430 C  CA    . GLY B 1 33  ? 14.316  10.972  -3.386  1.00 16.57 ? 12  GLY B CA    1 
ATOM   3431 C  C     . GLY B 1 33  ? 15.396  11.935  -3.838  1.00 17.25 ? 12  GLY B C     1 
ATOM   3432 O  O     . GLY B 1 33  ? 16.370  11.510  -4.469  1.00 18.73 ? 12  GLY B O     1 
ATOM   3433 N  N     . ALA B 1 34  ? 15.238  13.209  -3.465  1.00 16.64 ? 13  ALA B N     1 
ATOM   3434 C  CA    . ALA B 1 34  ? 16.169  14.293  -3.813  1.00 18.83 ? 13  ALA B CA    1 
ATOM   3435 C  C     . ALA B 1 34  ? 16.769  14.897  -2.544  1.00 18.86 ? 13  ALA B C     1 
ATOM   3436 O  O     . ALA B 1 34  ? 16.875  16.108  -2.450  1.00 20.11 ? 13  ALA B O     1 
ATOM   3437 C  CB    . ALA B 1 34  ? 15.457  15.323  -4.662  1.00 20.03 ? 13  ALA B CB    1 
ATOM   3438 N  N     . GLY B 1 35  ? 17.195  14.029  -1.615  1.00 17.57 ? 14  GLY B N     1 
ATOM   3439 C  CA    . GLY B 1 35  ? 18.176  14.361  -0.585  1.00 16.40 ? 14  GLY B CA    1 
ATOM   3440 C  C     . GLY B 1 35  ? 19.574  14.400  -1.188  1.00 18.34 ? 14  GLY B C     1 
ATOM   3441 O  O     . GLY B 1 35  ? 19.719  14.160  -2.425  1.00 18.56 ? 14  GLY B O     1 
ATOM   3442 N  N     . PHE B 1 36  ? 20.597  14.597  -0.363  1.00 16.99 ? 15  PHE B N     1 
ATOM   3443 C  CA    . PHE B 1 36  ? 21.996  14.621  -0.868  1.00 17.61 ? 15  PHE B CA    1 
ATOM   3444 C  C     . PHE B 1 36  ? 22.331  13.268  -1.504  1.00 17.60 ? 15  PHE B C     1 
ATOM   3445 O  O     . PHE B 1 36  ? 23.074  13.235  -2.480  1.00 18.66 ? 15  PHE B O     1 
ATOM   3446 C  CB    . PHE B 1 36  ? 22.991  14.962  0.232   1.00 17.41 ? 15  PHE B CB    1 
ATOM   3447 C  CG    . PHE B 1 36  ? 23.114  16.452  0.367   1.00 18.86 ? 15  PHE B CG    1 
ATOM   3448 C  CD1   . PHE B 1 36  ? 23.975  17.174  -0.455  1.00 18.74 ? 15  PHE B CD1   1 
ATOM   3449 C  CD2   . PHE B 1 36  ? 22.309  17.129  1.268   1.00 18.83 ? 15  PHE B CD2   1 
ATOM   3450 C  CE1   . PHE B 1 36  ? 24.054  18.544  -0.323  1.00 19.09 ? 15  PHE B CE1   1 
ATOM   3451 C  CE2   . PHE B 1 36  ? 22.365  18.504  1.368   1.00 18.72 ? 15  PHE B CE2   1 
ATOM   3452 C  CZ    . PHE B 1 36  ? 23.245  19.210  0.575   1.00 19.54 ? 15  PHE B CZ    1 
ATOM   3453 N  N     . ALA B 1 37  ? 21.799  12.155  -0.974  1.00 17.33 ? 16  ALA B N     1 
ATOM   3454 C  CA    . ALA B 1 37  ? 22.116  10.831  -1.564  1.00 16.15 ? 16  ALA B CA    1 
ATOM   3455 C  C     . ALA B 1 37  ? 21.513  10.718  -2.976  1.00 16.87 ? 16  ALA B C     1 
ATOM   3456 O  O     . ALA B 1 37  ? 22.259  10.410  -3.914  1.00 17.59 ? 16  ALA B O     1 
ATOM   3457 C  CB    . ALA B 1 37  ? 21.636  9.718   -0.668  1.00 17.34 ? 16  ALA B CB    1 
ATOM   3458 N  N     . GLY B 1 38  ? 20.218  10.981  -3.157  1.00 15.77 ? 17  GLY B N     1 
ATOM   3459 C  CA    . GLY B 1 38  ? 19.560  10.819  -4.455  1.00 16.28 ? 17  GLY B CA    1 
ATOM   3460 C  C     . GLY B 1 38  ? 20.115  11.801  -5.476  1.00 17.95 ? 17  GLY B C     1 
ATOM   3461 O  O     . GLY B 1 38  ? 20.345  11.411  -6.613  1.00 18.29 ? 17  GLY B O     1 
ATOM   3462 N  N     . LEU B 1 39  ? 20.375  13.041  -5.065  1.00 19.60 ? 18  LEU B N     1 
ATOM   3463 C  CA    . LEU B 1 39  ? 20.911  14.080  -6.004  1.00 18.63 ? 18  LEU B CA    1 
ATOM   3464 C  C     . LEU B 1 39  ? 22.351  13.765  -6.404  1.00 17.76 ? 18  LEU B C     1 
ATOM   3465 O  O     . LEU B 1 39  ? 22.674  13.971  -7.574  1.00 19.22 ? 18  LEU B O     1 
ATOM   3466 C  CB    . LEU B 1 39  ? 20.844  15.447  -5.331  1.00 18.07 ? 18  LEU B CB    1 
ATOM   3467 C  CG    . LEU B 1 39  ? 19.440  16.016  -5.177  1.00 20.41 ? 18  LEU B CG    1 
ATOM   3468 C  CD1   . LEU B 1 39  ? 19.536  17.324  -4.400  1.00 21.01 ? 18  LEU B CD1   1 
ATOM   3469 C  CD2   . LEU B 1 39  ? 18.776  16.243  -6.520  1.00 21.00 ? 18  LEU B CD2   1 
ATOM   3470 N  N     . THR B 1 40  ? 23.166  13.238  -5.504  1.00 16.39 ? 19  THR B N     1 
ATOM   3471 C  CA    . THR B 1 40  ? 24.564  12.834  -5.783  1.00 17.54 ? 19  THR B CA    1 
ATOM   3472 C  C     . THR B 1 40  ? 24.526  11.717  -6.833  1.00 18.24 ? 19  THR B C     1 
ATOM   3473 O  O     . THR B 1 40  ? 25.349  11.712  -7.807  1.00 18.39 ? 19  THR B O     1 
ATOM   3474 C  CB    . THR B 1 40  ? 25.321  12.445  -4.514  1.00 17.58 ? 19  THR B CB    1 
ATOM   3475 O  OG1   . THR B 1 40  ? 25.526  13.585  -3.668  1.00 20.11 ? 19  THR B OG1   1 
ATOM   3476 C  CG2   . THR B 1 40  ? 26.683  11.847  -4.823  1.00 21.54 ? 19  THR B CG2   1 
ATOM   3477 N  N     . ALA B 1 41  ? 23.677  10.735  -6.606  1.00 17.30 ? 20  ALA B N     1 
ATOM   3478 C  CA    . ALA B 1 41  ? 23.518  9.602   -7.538  1.00 17.95 ? 20  ALA B CA    1 
ATOM   3479 C  C     . ALA B 1 41  ? 23.074  10.102  -8.912  1.00 18.11 ? 20  ALA B C     1 
ATOM   3480 O  O     . ALA B 1 41  ? 23.676  9.696   -9.923  1.00 18.22 ? 20  ALA B O     1 
ATOM   3481 C  CB    . ALA B 1 41  ? 22.538  8.626   -6.976  1.00 18.29 ? 20  ALA B CB    1 
ATOM   3482 N  N     . ALA B 1 42  ? 21.995  10.859  -8.969  1.00 18.49 ? 21  ALA B N     1 
ATOM   3483 C  CA    . ALA B 1 42  ? 21.399  11.376  -10.218 1.00 19.87 ? 21  ALA B CA    1 
ATOM   3484 C  C     . ALA B 1 42  ? 22.441  12.177  -11.003 1.00 20.04 ? 21  ALA B C     1 
ATOM   3485 O  O     . ALA B 1 42  ? 22.528  11.996  -12.229 1.00 21.10 ? 21  ALA B O     1 
ATOM   3486 C  CB    . ALA B 1 42  ? 20.197  12.224  -9.925  1.00 21.97 ? 21  ALA B CB    1 
ATOM   3487 N  N     . ARG B 1 43  ? 23.225  13.005  -10.331 1.00 20.09 ? 22  ARG B N     1 
ATOM   3488 C  CA    . ARG B 1 43  ? 24.246  13.816  -11.058 1.00 22.20 ? 22  ARG B CA    1 
ATOM   3489 C  C     . ARG B 1 43  ? 25.338  12.901  -11.643 1.00 23.74 ? 22  ARG B C     1 
ATOM   3490 O  O     . ARG B 1 43  ? 25.816  13.159  -12.781 1.00 22.60 ? 22  ARG B O     1 
ATOM   3491 C  CB    . ARG B 1 43  ? 24.877  14.852  -10.136 1.00 23.31 ? 22  ARG B CB    1 
ATOM   3492 C  CG    . ARG B 1 43  ? 25.889  15.717  -10.880 1.00 27.58 ? 22  ARG B CG    1 
ATOM   3493 C  CD    . ARG B 1 43  ? 26.950  16.163  -9.934  1.00 33.64 ? 22  ARG B CD    1 
ATOM   3494 N  NE    . ARG B 1 43  ? 27.642  17.300  -10.499 1.00 40.11 ? 22  ARG B NE    1 
ATOM   3495 C  CZ    . ARG B 1 43  ? 28.480  18.050  -9.825  1.00 36.35 ? 22  ARG B CZ    1 
ATOM   3496 N  NH1   . ARG B 1 43  ? 28.688  17.825  -8.543  1.00 42.34 ? 22  ARG B NH1   1 
ATOM   3497 N  NH2   . ARG B 1 43  ? 29.101  19.033  -10.440 1.00 48.53 ? 22  ARG B NH2   1 
ATOM   3498 N  N     . ALA B 1 44  ? 25.775  11.876  -10.910 1.00 20.45 ? 23  ALA B N     1 
ATOM   3499 C  CA    . ALA B 1 44  ? 26.839  10.956  -11.366 1.00 21.01 ? 23  ALA B CA    1 
ATOM   3500 C  C     . ALA B 1 44  ? 26.338  10.188  -12.602 1.00 20.88 ? 23  ALA B C     1 
ATOM   3501 O  O     . ALA B 1 44  ? 27.121  9.987   -13.563 1.00 21.84 ? 23  ALA B O     1 
ATOM   3502 C  CB    . ALA B 1 44  ? 27.228  10.046  -10.215 1.00 21.31 ? 23  ALA B CB    1 
ATOM   3503 N  N     . VAL B 1 45  ? 25.084  9.750   -12.590 1.00 18.77 ? 24  VAL B N     1 
ATOM   3504 C  CA    . VAL B 1 45  ? 24.460  8.981   -13.686 1.00 20.85 ? 24  VAL B CA    1 
ATOM   3505 C  C     . VAL B 1 45  ? 24.348  9.919   -14.888 1.00 23.83 ? 24  VAL B C     1 
ATOM   3506 O  O     . VAL B 1 45  ? 24.745  9.506   -15.995 1.00 20.69 ? 24  VAL B O     1 
ATOM   3507 C  CB    . VAL B 1 45  ? 23.125  8.397   -13.229 1.00 24.32 ? 24  VAL B CB    1 
ATOM   3508 C  CG1   . VAL B 1 45  ? 22.287  7.892   -14.371 1.00 25.05 ? 24  VAL B CG1   1 
ATOM   3509 C  CG2   . VAL B 1 45  ? 23.421  7.283   -12.223 1.00 24.33 ? 24  VAL B CG2   1 
ATOM   3510 N  N     . HIS B 1 46  ? 23.947  11.155  -14.648 1.00 22.77 ? 25  HIS B N     1 
ATOM   3511 C  CA    . HIS B 1 46  ? 23.825  12.176  -15.729 1.00 25.77 ? 25  HIS B CA    1 
ATOM   3512 C  C     . HIS B 1 46  ? 25.188  12.402  -16.377 1.00 26.18 ? 25  HIS B C     1 
ATOM   3513 O  O     . HIS B 1 46  ? 25.273  12.336  -17.609 1.00 28.13 ? 25  HIS B O     1 
ATOM   3514 C  CB    . HIS B 1 46  ? 23.290  13.503  -15.202 1.00 25.84 ? 25  HIS B CB    1 
ATOM   3515 C  CG    . HIS B 1 46  ? 23.379  14.598  -16.219 1.00 24.93 ? 25  HIS B CG    1 
ATOM   3516 N  ND1   . HIS B 1 46  ? 22.656  14.558  -17.406 1.00 25.34 ? 25  HIS B ND1   1 
ATOM   3517 C  CD2   . HIS B 1 46  ? 24.096  15.743  -16.224 1.00 26.82 ? 25  HIS B CD2   1 
ATOM   3518 C  CE1   . HIS B 1 46  ? 22.955  15.625  -18.132 1.00 28.51 ? 25  HIS B CE1   1 
ATOM   3519 N  NE2   . HIS B 1 46  ? 23.806  16.387  -17.406 1.00 25.95 ? 25  HIS B NE2   1 
ATOM   3520 N  N     . GLU B 1 47  ? 26.207  12.644  -15.578 1.00 27.05 ? 26  GLU B N     1 
ATOM   3521 C  CA    . GLU B 1 47  ? 27.549  13.008  -16.095 1.00 30.80 ? 26  GLU B CA    1 
ATOM   3522 C  C     . GLU B 1 47  ? 28.220  11.814  -16.763 1.00 32.35 ? 26  GLU B C     1 
ATOM   3523 O  O     . GLU B 1 47  ? 29.096  12.044  -17.594 1.00 27.40 ? 26  GLU B O     1 
ATOM   3524 C  CB    . GLU B 1 47  ? 28.375  13.631  -14.995 1.00 35.08 ? 26  GLU B CB    1 
ATOM   3525 C  CG    . GLU B 1 47  ? 27.800  15.000  -14.676 1.00 42.75 ? 26  GLU B CG    1 
ATOM   3526 C  CD    . GLU B 1 47  ? 28.631  15.850  -13.746 1.00 50.84 ? 26  GLU B CD    1 
ATOM   3527 O  OE1   . GLU B 1 47  ? 29.614  15.291  -13.204 1.00 51.93 ? 26  GLU B OE1   1 
ATOM   3528 O  OE2   . GLU B 1 47  ? 28.270  17.061  -13.550 1.00 55.56 ? 26  GLU B OE2   1 
ATOM   3529 N  N     . ALA B 1 48  ? 27.812  10.587  -16.455 1.00 26.21 ? 27  ALA B N     1 
ATOM   3530 C  CA    . ALA B 1 48  ? 28.315  9.382   -17.150 1.00 27.30 ? 27  ALA B CA    1 
ATOM   3531 C  C     . ALA B 1 48  ? 27.605  9.221   -18.483 1.00 27.18 ? 27  ALA B C     1 
ATOM   3532 O  O     . ALA B 1 48  ? 27.961  8.260   -19.173 1.00 30.55 ? 27  ALA B O     1 
ATOM   3533 C  CB    . ALA B 1 48  ? 28.157  8.138   -16.272 1.00 27.63 ? 27  ALA B CB    1 
ATOM   3534 N  N     . GLY B 1 49  ? 26.578  10.024  -18.792 1.00 28.57 ? 28  GLY B N     1 
ATOM   3535 C  CA    . GLY B 1 49  ? 25.869  10.034  -20.087 1.00 27.67 ? 28  GLY B CA    1 
ATOM   3536 C  C     . GLY B 1 49  ? 24.598  9.191   -20.151 1.00 28.35 ? 28  GLY B C     1 
ATOM   3537 O  O     . GLY B 1 49  ? 24.087  8.952   -21.257 1.00 31.72 ? 28  GLY B O     1 
ATOM   3538 N  N     . ARG B 1 50  ? 24.043  8.750   -19.029 1.00 23.53 ? 29  ARG B N     1 
ATOM   3539 C  CA    . ARG B 1 50  ? 22.733  8.041   -18.995 1.00 24.10 ? 29  ARG B CA    1 
ATOM   3540 C  C     . ARG B 1 50  ? 21.585  9.011   -18.697 1.00 24.39 ? 29  ARG B C     1 
ATOM   3541 O  O     . ARG B 1 50  ? 21.829  10.037  -18.000 1.00 23.75 ? 29  ARG B O     1 
ATOM   3542 C  CB    . ARG B 1 50  ? 22.780  6.949   -17.913 1.00 24.31 ? 29  ARG B CB    1 
ATOM   3543 C  CG    . ARG B 1 50  ? 23.938  5.985   -18.073 1.00 27.30 ? 29  ARG B CG    1 
ATOM   3544 C  CD    . ARG B 1 50  ? 23.718  5.100   -19.271 1.00 30.11 ? 29  ARG B CD    1 
ATOM   3545 N  NE    . ARG B 1 50  ? 24.632  3.994   -19.252 1.00 30.52 ? 29  ARG B NE    1 
ATOM   3546 C  CZ    . ARG B 1 50  ? 24.510  2.931   -20.026 1.00 32.54 ? 29  ARG B CZ    1 
ATOM   3547 N  NH1   . ARG B 1 50  ? 23.505  2.823   -20.873 1.00 34.52 ? 29  ARG B NH1   1 
ATOM   3548 N  NH2   . ARG B 1 50  ? 25.389  1.970   -19.926 1.00 34.03 ? 29  ARG B NH2   1 
ATOM   3549 N  N     . SER B 1 51  ? 20.391  8.691   -19.193 1.00 24.83 ? 30  SER B N     1 
ATOM   3550 C  CA    . SER B 1 51  ? 19.139  9.439   -18.945 1.00 24.26 ? 30  SER B CA    1 
ATOM   3551 C  C     . SER B 1 51  ? 18.703  9.127   -17.500 1.00 25.48 ? 30  SER B C     1 
ATOM   3552 O  O     . SER B 1 51  ? 18.958  7.994   -17.027 1.00 24.74 ? 30  SER B O     1 
ATOM   3553 C  CB    . SER B 1 51  ? 18.059  9.185   -19.966 1.00 26.31 ? 30  SER B CB    1 
ATOM   3554 O  OG    . SER B 1 51  ? 17.738  7.808   -20.077 1.00 26.85 ? 30  SER B OG    1 
ATOM   3555 N  N     . VAL B 1 52  ? 18.249  10.136  -16.751 1.00 25.98 ? 31  VAL B N     1 
ATOM   3556 C  CA    . VAL B 1 52  ? 17.911  9.960   -15.298 1.00 25.38 ? 31  VAL B CA    1 
ATOM   3557 C  C     . VAL B 1 52  ? 16.681  10.810  -14.989 1.00 25.12 ? 31  VAL B C     1 
ATOM   3558 O  O     . VAL B 1 52  ? 16.576  11.918  -15.540 1.00 26.16 ? 31  VAL B O     1 
ATOM   3559 C  CB    . VAL B 1 52  ? 19.109  10.266  -14.379 1.00 25.41 ? 31  VAL B CB    1 
ATOM   3560 C  CG1   . VAL B 1 52  ? 19.565  11.718  -14.475 1.00 28.34 ? 31  VAL B CG1   1 
ATOM   3561 C  CG2   . VAL B 1 52  ? 18.837  9.875   -12.924 1.00 24.68 ? 31  VAL B CG2   1 
ATOM   3562 N  N     . LEU B 1 53  ? 15.734  10.276  -14.220 1.00 23.88 ? 32  LEU B N     1 
ATOM   3563 C  CA    . LEU B 1 53  ? 14.663  11.069  -13.564 1.00 23.89 ? 32  LEU B CA    1 
ATOM   3564 C  C     . LEU B 1 53  ? 14.810  10.951  -12.045 1.00 24.19 ? 32  LEU B C     1 
ATOM   3565 O  O     . LEU B 1 53  ? 15.112  9.856   -11.547 1.00 24.88 ? 32  LEU B O     1 
ATOM   3566 C  CB    . LEU B 1 53  ? 13.277  10.557  -13.943 1.00 29.17 ? 32  LEU B CB    1 
ATOM   3567 C  CG    . LEU B 1 53  ? 12.766  10.824  -15.347 1.00 35.12 ? 32  LEU B CG    1 
ATOM   3568 C  CD1   . LEU B 1 53  ? 11.308  10.400  -15.422 1.00 39.18 ? 32  LEU B CD1   1 
ATOM   3569 C  CD2   . LEU B 1 53  ? 12.896  12.290  -15.716 1.00 35.86 ? 32  LEU B CD2   1 
ATOM   3570 N  N     . VAL B 1 54  ? 14.538  12.039  -11.336 1.00 23.14 ? 33  VAL B N     1 
ATOM   3571 C  CA    . VAL B 1 54  ? 14.551  12.110  -9.861  1.00 21.51 ? 33  VAL B CA    1 
ATOM   3572 C  C     . VAL B 1 54  ? 13.127  12.402  -9.423  1.00 19.92 ? 33  VAL B C     1 
ATOM   3573 O  O     . VAL B 1 54  ? 12.555  13.443  -9.829  1.00 20.56 ? 33  VAL B O     1 
ATOM   3574 C  CB    . VAL B 1 54  ? 15.507  13.167  -9.300  1.00 23.38 ? 33  VAL B CB    1 
ATOM   3575 C  CG1   . VAL B 1 54  ? 15.486  13.114  -7.793  1.00 25.37 ? 33  VAL B CG1   1 
ATOM   3576 C  CG2   . VAL B 1 54  ? 16.914  13.005  -9.838  1.00 25.54 ? 33  VAL B CG2   1 
ATOM   3577 N  N     . LEU B 1 55  ? 12.509  11.472  -8.704  1.00 18.63 ? 34  LEU B N     1 
ATOM   3578 C  CA    . LEU B 1 55  ? 11.122  11.677  -8.231  1.00 18.83 ? 34  LEU B CA    1 
ATOM   3579 C  C     . LEU B 1 55  ? 11.195  12.006  -6.753  1.00 20.06 ? 34  LEU B C     1 
ATOM   3580 O  O     . LEU B 1 55  ? 11.677  11.131  -5.963  1.00 19.76 ? 34  LEU B O     1 
ATOM   3581 C  CB    . LEU B 1 55  ? 10.256  10.435  -8.518  1.00 21.17 ? 34  LEU B CB    1 
ATOM   3582 C  CG    . LEU B 1 55  ? 10.327  9.892   -9.936  1.00 23.71 ? 34  LEU B CG    1 
ATOM   3583 C  CD1   . LEU B 1 55  ? 9.361   8.763   -10.156 1.00 24.28 ? 34  LEU B CD1   1 
ATOM   3584 C  CD2   . LEU B 1 55  ? 10.085  10.984  -10.951 1.00 23.19 ? 34  LEU B CD2   1 
ATOM   3585 N  N     . GLU B 1 56  ? 10.707  13.184  -6.369  1.00 19.50 ? 35  GLU B N     1 
ATOM   3586 C  CA    . GLU B 1 56  ? 10.819  13.702  -4.986  1.00 19.41 ? 35  GLU B CA    1 
ATOM   3587 C  C     . GLU B 1 56  ? 9.421   13.945  -4.453  1.00 19.52 ? 35  GLU B C     1 
ATOM   3588 O  O     . GLU B 1 56  ? 8.625   14.587  -5.146  1.00 20.29 ? 35  GLU B O     1 
ATOM   3589 C  CB    . GLU B 1 56  ? 11.694  14.952  -4.962  1.00 18.71 ? 35  GLU B CB    1 
ATOM   3590 C  CG    . GLU B 1 56  ? 11.642  15.729  -3.654  1.00 17.95 ? 35  GLU B CG    1 
ATOM   3591 C  CD    . GLU B 1 56  ? 11.932  14.917  -2.386  1.00 18.43 ? 35  GLU B CD    1 
ATOM   3592 O  OE1   . GLU B 1 56  ? 11.169  15.038  -1.361  1.00 19.04 ? 35  GLU B OE1   1 
ATOM   3593 O  OE2   . GLU B 1 56  ? 12.958  14.215  -2.380  1.00 17.98 ? 35  GLU B OE2   1 
ATOM   3594 N  N     . ALA B 1 57  ? 9.107   13.422  -3.264  1.00 18.71 ? 36  ALA B N     1 
ATOM   3595 C  CA    . ALA B 1 57  ? 7.759   13.572  -2.661  1.00 17.63 ? 36  ALA B CA    1 
ATOM   3596 C  C     . ALA B 1 57  ? 7.445   15.037  -2.298  1.00 18.09 ? 36  ALA B C     1 
ATOM   3597 O  O     . ALA B 1 57  ? 6.288   15.481  -2.498  1.00 16.78 ? 36  ALA B O     1 
ATOM   3598 C  CB    . ALA B 1 57  ? 7.631   12.672  -1.441  1.00 17.22 ? 36  ALA B CB    1 
ATOM   3599 N  N     . ARG B 1 58  ? 8.401   15.765  -1.751  1.00 17.35 ? 37  ARG B N     1 
ATOM   3600 C  CA    . ARG B 1 58  ? 8.179   17.141  -1.250  1.00 17.22 ? 37  ARG B CA    1 
ATOM   3601 C  C     . ARG B 1 58  ? 8.235   18.161  -2.395  1.00 19.99 ? 37  ARG B C     1 
ATOM   3602 O  O     . ARG B 1 58  ? 8.760   17.854  -3.465  1.00 16.97 ? 37  ARG B O     1 
ATOM   3603 C  CB    . ARG B 1 58  ? 9.274   17.456  -0.263  1.00 18.33 ? 37  ARG B CB    1 
ATOM   3604 C  CG    . ARG B 1 58  ? 9.169   16.663  1.041   1.00 19.23 ? 37  ARG B CG    1 
ATOM   3605 C  CD    . ARG B 1 58  ? 10.210  17.238  1.993   1.00 18.58 ? 37  ARG B CD    1 
ATOM   3606 N  NE    . ARG B 1 58  ? 10.105  16.899  3.406   1.00 18.07 ? 37  ARG B NE    1 
ATOM   3607 C  CZ    . ARG B 1 58  ? 10.898  16.035  4.028   1.00 17.42 ? 37  ARG B CZ    1 
ATOM   3608 N  NH1   . ARG B 1 58  ? 11.714  15.260  3.339   1.00 17.91 ? 37  ARG B NH1   1 
ATOM   3609 N  NH2   . ARG B 1 58  ? 10.822  15.907  5.332   1.00 18.87 ? 37  ARG B NH2   1 
ATOM   3610 N  N     . ASP B 1 59  ? 7.768   19.380  -2.129  1.00 21.79 ? 38  ASP B N     1 
ATOM   3611 C  CA    . ASP B 1 59  ? 7.848   20.506  -3.110  1.00 23.30 ? 38  ASP B CA    1 
ATOM   3612 C  C     . ASP B 1 59  ? 9.244   21.150  -3.093  1.00 24.93 ? 38  ASP B C     1 
ATOM   3613 O  O     . ASP B 1 59  ? 9.393   22.295  -3.568  1.00 21.49 ? 38  ASP B O     1 
ATOM   3614 C  CB    . ASP B 1 59  ? 6.737   21.491  -2.792  1.00 26.79 ? 38  ASP B CB    1 
ATOM   3615 C  CG    . ASP B 1 59  ? 6.990   22.221  -1.489  1.00 33.00 ? 38  ASP B CG    1 
ATOM   3616 O  OD1   . ASP B 1 59  ? 8.001   21.911  -0.807  1.00 32.77 ? 38  ASP B OD1   1 
ATOM   3617 O  OD2   . ASP B 1 59  ? 6.178   23.099  -1.178  1.00 40.01 ? 38  ASP B OD2   1 
ATOM   3618 N  N     . ARG B 1 60  ? 10.257  20.453  -2.581  1.00 20.94 ? 39  ARG B N     1 
ATOM   3619 C  CA    . ARG B 1 60  ? 11.636  20.953  -2.485  1.00 19.16 ? 39  ARG B CA    1 
ATOM   3620 C  C     . ARG B 1 60  ? 12.604  19.776  -2.516  1.00 18.52 ? 39  ARG B C     1 
ATOM   3621 O  O     . ARG B 1 60  ? 12.208  18.656  -2.181  1.00 19.93 ? 39  ARG B O     1 
ATOM   3622 C  CB    . ARG B 1 60  ? 11.868  21.720  -1.191  1.00 19.73 ? 39  ARG B CB    1 
ATOM   3623 C  CG    . ARG B 1 60  ? 11.780  20.859  0.071   1.00 20.00 ? 39  ARG B CG    1 
ATOM   3624 C  CD    . ARG B 1 60  ? 11.960  21.660  1.342   1.00 19.64 ? 39  ARG B CD    1 
ATOM   3625 N  NE    . ARG B 1 60  ? 11.880  20.758  2.488   1.00 20.00 ? 39  ARG B NE    1 
ATOM   3626 C  CZ    . ARG B 1 60  ? 12.883  20.006  2.933   1.00 17.30 ? 39  ARG B CZ    1 
ATOM   3627 N  NH1   . ARG B 1 60  ? 14.055  20.030  2.315   1.00 17.81 ? 39  ARG B NH1   1 
ATOM   3628 N  NH2   . ARG B 1 60  ? 12.708  19.243  4.011   1.00 18.98 ? 39  ARG B NH2   1 
ATOM   3629 N  N     . VAL B 1 61  ? 13.862  20.093  -2.742  1.00 16.92 ? 40  VAL B N     1 
ATOM   3630 C  CA    . VAL B 1 61  ? 14.991  19.161  -2.525  1.00 18.56 ? 40  VAL B CA    1 
ATOM   3631 C  C     . VAL B 1 61  ? 15.563  19.380  -1.129  1.00 17.66 ? 40  VAL B C     1 
ATOM   3632 O  O     . VAL B 1 61  ? 15.191  20.381  -0.428  1.00 17.76 ? 40  VAL B O     1 
ATOM   3633 C  CB    . VAL B 1 61  ? 16.043  19.300  -3.641  1.00 19.70 ? 40  VAL B CB    1 
ATOM   3634 C  CG1   . VAL B 1 61  ? 15.376  19.141  -4.993  1.00 22.14 ? 40  VAL B CG1   1 
ATOM   3635 C  CG2   . VAL B 1 61  ? 16.877  20.566  -3.515  1.00 20.52 ? 40  VAL B CG2   1 
ATOM   3636 N  N     . GLY B 1 62  ? 16.430  18.466  -0.715  1.00 16.47 ? 41  GLY B N     1 
ATOM   3637 C  CA    . GLY B 1 62  ? 17.263  18.585  0.477   1.00 15.33 ? 41  GLY B CA    1 
ATOM   3638 C  C     . GLY B 1 62  ? 16.925  17.529  1.524   1.00 15.10 ? 41  GLY B C     1 
ATOM   3639 O  O     . GLY B 1 62  ? 17.791  17.233  2.339   1.00 16.60 ? 41  GLY B O     1 
ATOM   3640 N  N     . GLY B 1 63  ? 15.686  17.071  1.573   1.00 16.46 ? 42  GLY B N     1 
ATOM   3641 C  CA    . GLY B 1 63  ? 15.259  16.030  2.541   1.00 16.45 ? 42  GLY B CA    1 
ATOM   3642 C  C     . GLY B 1 63  ? 15.427  16.419  4.009   1.00 17.47 ? 42  GLY B C     1 
ATOM   3643 O  O     . GLY B 1 63  ? 14.716  17.337  4.525   1.00 15.99 ? 42  GLY B O     1 
ATOM   3644 N  N     . ARG B 1 64  ? 16.324  15.726  4.703   1.00 16.34 ? 43  ARG B N     1 
ATOM   3645 C  CA    . ARG B 1 64  ? 16.657  15.952  6.112   1.00 16.54 ? 43  ARG B CA    1 
ATOM   3646 C  C     . ARG B 1 64  ? 17.527  17.205  6.277   1.00 15.89 ? 43  ARG B C     1 
ATOM   3647 O  O     . ARG B 1 64  ? 17.805  17.547  7.435   1.00 18.77 ? 43  ARG B O     1 
ATOM   3648 C  CB    . ARG B 1 64  ? 17.342  14.713  6.715   1.00 16.12 ? 43  ARG B CB    1 
ATOM   3649 C  CG    . ARG B 1 64  ? 16.332  13.636  7.072   1.00 15.77 ? 43  ARG B CG    1 
ATOM   3650 C  CD    . ARG B 1 64  ? 17.053  12.356  7.489   1.00 17.05 ? 43  ARG B CD    1 
ATOM   3651 N  NE    . ARG B 1 64  ? 17.256  11.404  6.401   1.00 16.06 ? 43  ARG B NE    1 
ATOM   3652 C  CZ    . ARG B 1 64  ? 17.808  10.209  6.541   1.00 16.36 ? 43  ARG B CZ    1 
ATOM   3653 N  NH1   . ARG B 1 64  ? 18.303  9.843   7.706   1.00 16.01 ? 43  ARG B NH1   1 
ATOM   3654 N  NH2   . ARG B 1 64  ? 17.882  9.373   5.516   1.00 18.81 ? 43  ARG B NH2   1 
ATOM   3655 N  N     . THR B 1 65  ? 17.866  17.894  5.189   1.00 16.19 ? 44  THR B N     1 
ATOM   3656 C  CA    . THR B 1 65  ? 18.377  19.282  5.218   1.00 17.81 ? 44  THR B CA    1 
ATOM   3657 C  C     . THR B 1 65  ? 17.272  20.195  4.709   1.00 17.64 ? 44  THR B C     1 
ATOM   3658 O  O     . THR B 1 65  ? 16.578  19.837  3.768   1.00 17.71 ? 44  THR B O     1 
ATOM   3659 C  CB    . THR B 1 65  ? 19.709  19.453  4.457   1.00 17.43 ? 44  THR B CB    1 
ATOM   3660 O  OG1   . THR B 1 65  ? 19.520  19.443  3.041   1.00 17.42 ? 44  THR B OG1   1 
ATOM   3661 C  CG2   . THR B 1 65  ? 20.731  18.422  4.879   1.00 17.94 ? 44  THR B CG2   1 
ATOM   3662 N  N     . CYS B 1 66  ? 17.040  21.280  5.413   1.00 17.70 ? 45  CYS B N     1 
ATOM   3663 C  CA    . CYS B 1 66  ? 15.899  22.180  5.149   1.00 17.56 ? 45  CYS B CA    1 
ATOM   3664 C  C     . CYS B 1 66  ? 16.238  23.549  5.729   1.00 18.18 ? 45  CYS B C     1 
ATOM   3665 O  O     . CYS B 1 66  ? 16.594  23.600  6.904   1.00 17.60 ? 45  CYS B O     1 
ATOM   3666 C  CB    . CYS B 1 66  ? 14.644  21.607  5.762   1.00 20.61 ? 45  CYS B CB    1 
ATOM   3667 S  SG    . CYS B 1 66  ? 13.230  22.713  5.549   1.00 24.51 ? 45  CYS B SG    1 
ATOM   3668 N  N     . THR B 1 67  ? 16.120  24.586  4.891   1.00 19.56 ? 46  THR B N     1 
ATOM   3669 C  CA    . THR B 1 67  ? 16.525  25.973  5.223   1.00 19.15 ? 46  THR B CA    1 
ATOM   3670 C  C     . THR B 1 67  ? 15.366  26.888  4.874   1.00 19.97 ? 46  THR B C     1 
ATOM   3671 O  O     . THR B 1 67  ? 14.887  26.835  3.733   1.00 21.20 ? 46  THR B O     1 
ATOM   3672 C  CB    . THR B 1 67  ? 17.827  26.375  4.512   1.00 18.20 ? 46  THR B CB    1 
ATOM   3673 O  OG1   . THR B 1 67  ? 18.810  25.349  4.719   1.00 20.08 ? 46  THR B OG1   1 
ATOM   3674 C  CG2   . THR B 1 67  ? 18.401  27.669  5.053   1.00 19.97 ? 46  THR B CG2   1 
ATOM   3675 N  N     . GLU B 1 68  ? 14.948  27.695  5.847   1.00 21.79 ? 47  GLU B N     1 
ATOM   3676 C  CA    . GLU B 1 68  ? 13.913  28.735  5.674   1.00 22.04 ? 47  GLU B CA    1 
ATOM   3677 C  C     . GLU B 1 68  ? 14.554  30.082  5.987   1.00 24.86 ? 47  GLU B C     1 
ATOM   3678 O  O     . GLU B 1 68  ? 15.425  30.155  6.860   1.00 23.55 ? 47  GLU B O     1 
ATOM   3679 C  CB    . GLU B 1 68  ? 12.715  28.482  6.590   1.00 24.21 ? 47  GLU B CB    1 
ATOM   3680 C  CG    . GLU B 1 68  ? 11.919  27.248  6.215   1.00 25.81 ? 47  GLU B CG    1 
ATOM   3681 C  CD    . GLU B 1 68  ? 10.748  26.950  7.136   1.00 28.59 ? 47  GLU B CD    1 
ATOM   3682 O  OE1   . GLU B 1 68  ? 10.036  25.939  6.885   1.00 31.84 ? 47  GLU B OE1   1 
ATOM   3683 O  OE2   . GLU B 1 68  ? 10.534  27.730  8.084   1.00 26.40 ? 47  GLU B OE2   1 
ATOM   3684 N  N     . GLU B 1 69  ? 14.099  31.132  5.323   1.00 24.41 ? 48  GLU B N     1 
ATOM   3685 C  CA    . GLU B 1 69  ? 14.580  32.514  5.603   1.00 26.08 ? 48  GLU B CA    1 
ATOM   3686 C  C     . GLU B 1 69  ? 13.662  33.127  6.660   1.00 25.10 ? 48  GLU B C     1 
ATOM   3687 O  O     . GLU B 1 69  ? 12.455  33.209  6.406   1.00 25.37 ? 48  GLU B O     1 
ATOM   3688 C  CB    . GLU B 1 69  ? 14.669  33.284  4.280   1.00 30.86 ? 48  GLU B CB    1 
ATOM   3689 C  CG    . GLU B 1 69  ? 15.005  34.766  4.439   1.00 39.99 ? 48  GLU B CG    1 
ATOM   3690 C  CD    . GLU B 1 69  ? 16.454  35.223  4.308   1.00 45.93 ? 48  GLU B CD    1 
ATOM   3691 O  OE1   . GLU B 1 69  ? 16.687  36.460  4.332   1.00 44.99 ? 48  GLU B OE1   1 
ATOM   3692 O  OE2   . GLU B 1 69  ? 17.347  34.367  4.148   1.00 53.78 ? 48  GLU B OE2   1 
ATOM   3693 N  N     . HIS B 1 70  ? 14.218  33.537  7.802   1.00 24.85 ? 49  HIS B N     1 
ATOM   3694 C  CA    . HIS B 1 70  ? 13.495  34.244  8.890   1.00 25.77 ? 49  HIS B CA    1 
ATOM   3695 C  C     . HIS B 1 70  ? 14.409  35.334  9.472   1.00 24.72 ? 49  HIS B C     1 
ATOM   3696 O  O     . HIS B 1 70  ? 15.635  35.109  9.549   1.00 24.00 ? 49  HIS B O     1 
ATOM   3697 C  CB    . HIS B 1 70  ? 13.053  33.278  9.994   1.00 26.84 ? 49  HIS B CB    1 
ATOM   3698 C  CG    . HIS B 1 70  ? 12.146  32.174  9.569   1.00 27.94 ? 49  HIS B CG    1 
ATOM   3699 N  ND1   . HIS B 1 70  ? 10.791  32.250  9.729   1.00 31.13 ? 49  HIS B ND1   1 
ATOM   3700 C  CD2   . HIS B 1 70  ? 12.403  30.943  9.071   1.00 28.24 ? 49  HIS B CD2   1 
ATOM   3701 C  CE1   . HIS B 1 70  ? 10.231  31.130  9.297   1.00 31.57 ? 49  HIS B CE1   1 
ATOM   3702 N  NE2   . HIS B 1 70  ? 11.212  30.316  8.886   1.00 28.13 ? 49  HIS B NE2   1 
ATOM   3703 N  N     . HIS B 1 71  ? 13.840  36.486  9.875   1.00 25.42 ? 50  HIS B N     1 
ATOM   3704 C  CA    . HIS B 1 71  ? 14.596  37.568  10.574  1.00 25.83 ? 50  HIS B CA    1 
ATOM   3705 C  C     . HIS B 1 71  ? 15.822  37.985  9.748   1.00 24.83 ? 50  HIS B C     1 
ATOM   3706 O  O     . HIS B 1 71  ? 16.849  38.311  10.344  1.00 29.05 ? 50  HIS B O     1 
ATOM   3707 C  CB    . HIS B 1 71  ? 14.889  37.101  12.003  1.00 27.53 ? 50  HIS B CB    1 
ATOM   3708 C  CG    . HIS B 1 71  ? 13.621  36.826  12.721  1.00 31.35 ? 50  HIS B CG    1 
ATOM   3709 N  ND1   . HIS B 1 71  ? 12.743  37.846  13.055  1.00 32.27 ? 50  HIS B ND1   1 
ATOM   3710 C  CD2   . HIS B 1 71  ? 12.994  35.666  13.013  1.00 31.74 ? 50  HIS B CD2   1 
ATOM   3711 C  CE1   . HIS B 1 71  ? 11.661  37.322  13.592  1.00 33.75 ? 50  HIS B CE1   1 
ATOM   3712 N  NE2   . HIS B 1 71  ? 11.784  35.986  13.555  1.00 34.27 ? 50  HIS B NE2   1 
ATOM   3713 N  N     . GLY B 1 72  ? 15.730  37.901  8.417   1.00 25.47 ? 51  GLY B N     1 
ATOM   3714 C  CA    . GLY B 1 72  ? 16.797  38.322  7.482   1.00 24.47 ? 51  GLY B CA    1 
ATOM   3715 C  C     . GLY B 1 72  ? 18.026  37.407  7.478   1.00 26.16 ? 51  GLY B C     1 
ATOM   3716 O  O     . GLY B 1 72  ? 19.097  37.868  7.092   1.00 26.74 ? 51  GLY B O     1 
ATOM   3717 N  N     . THR B 1 73  ? 17.914  36.151  7.919   1.00 24.23 ? 52  THR B N     1 
ATOM   3718 C  CA    . THR B 1 73  ? 19.022  35.169  7.919   1.00 21.20 ? 52  THR B CA    1 
ATOM   3719 C  C     . THR B 1 73  ? 18.486  33.769  7.614   1.00 21.21 ? 52  THR B C     1 
ATOM   3720 O  O     . THR B 1 73  ? 17.255  33.588  7.460   1.00 22.01 ? 52  THR B O     1 
ATOM   3721 C  CB    . THR B 1 73  ? 19.801  35.167  9.242   1.00 21.67 ? 52  THR B CB    1 
ATOM   3722 O  OG1   . THR B 1 73  ? 21.018  34.465  9.007   1.00 22.71 ? 52  THR B OG1   1 
ATOM   3723 C  CG2   . THR B 1 73  ? 19.075  34.530  10.409  1.00 21.36 ? 52  THR B CG2   1 
ATOM   3724 N  N     . TRP B 1 74  ? 19.389  32.802  7.527   1.00 21.11 ? 53  TRP B N     1 
ATOM   3725 C  CA    . TRP B 1 74  ? 19.007  31.394  7.220   1.00 19.60 ? 53  TRP B CA    1 
ATOM   3726 C  C     . TRP B 1 74  ? 18.732  30.648  8.534   1.00 17.74 ? 53  TRP B C     1 
ATOM   3727 O  O     . TRP B 1 74  ? 19.513  30.766  9.495   1.00 19.88 ? 53  TRP B O     1 
ATOM   3728 C  CB    . TRP B 1 74  ? 20.070  30.699  6.349   1.00 20.09 ? 53  TRP B CB    1 
ATOM   3729 C  CG    . TRP B 1 74  ? 21.449  30.762  6.937   1.00 20.65 ? 53  TRP B CG    1 
ATOM   3730 C  CD1   . TRP B 1 74  ? 22.043  29.823  7.720   1.00 20.99 ? 53  TRP B CD1   1 
ATOM   3731 C  CD2   . TRP B 1 74  ? 22.409  31.833  6.817   1.00 20.72 ? 53  TRP B CD2   1 
ATOM   3732 N  NE1   . TRP B 1 74  ? 23.270  30.244  8.129   1.00 19.93 ? 53  TRP B NE1   1 
ATOM   3733 C  CE2   . TRP B 1 74  ? 23.531  31.469  7.587   1.00 21.99 ? 53  TRP B CE2   1 
ATOM   3734 C  CE3   . TRP B 1 74  ? 22.428  33.064  6.151   1.00 23.00 ? 53  TRP B CE3   1 
ATOM   3735 C  CZ2   . TRP B 1 74  ? 24.642  32.297  7.742   1.00 23.03 ? 53  TRP B CZ2   1 
ATOM   3736 C  CZ3   . TRP B 1 74  ? 23.538  33.865  6.276   1.00 24.43 ? 53  TRP B CZ3   1 
ATOM   3737 C  CH2   . TRP B 1 74  ? 24.638  33.488  7.045   1.00 23.84 ? 53  TRP B CH2   1 
ATOM   3738 N  N     . ILE B 1 75  ? 17.689  29.840  8.526   1.00 18.41 ? 54  ILE B N     1 
ATOM   3739 C  CA    . ILE B 1 75  ? 17.346  28.917  9.640   1.00 19.21 ? 54  ILE B CA    1 
ATOM   3740 C  C     . ILE B 1 75  ? 17.476  27.479  9.126   1.00 16.75 ? 54  ILE B C     1 
ATOM   3741 O  O     . ILE B 1 75  ? 16.569  27.013  8.389   1.00 20.40 ? 54  ILE B O     1 
ATOM   3742 C  CB    . ILE B 1 75  ? 15.954  29.206  10.242  1.00 20.64 ? 54  ILE B CB    1 
ATOM   3743 C  CG1   . ILE B 1 75  ? 15.777  30.672  10.625  1.00 22.06 ? 54  ILE B CG1   1 
ATOM   3744 C  CG2   . ILE B 1 75  ? 15.695  28.313  11.448  1.00 23.15 ? 54  ILE B CG2   1 
ATOM   3745 C  CD1   . ILE B 1 75  ? 16.729  31.132  11.720  1.00 22.39 ? 54  ILE B CD1   1 
ATOM   3746 N  N     . ASP B 1 76  ? 18.501  26.760  9.569   1.00 19.17 ? 55  ASP B N     1 
ATOM   3747 C  CA    . ASP B 1 76  ? 18.652  25.335  9.173   1.00 18.00 ? 55  ASP B CA    1 
ATOM   3748 C  C     . ASP B 1 76  ? 17.809  24.501  10.145  1.00 16.21 ? 55  ASP B C     1 
ATOM   3749 O  O     . ASP B 1 76  ? 18.231  24.277  11.291  1.00 19.15 ? 55  ASP B O     1 
ATOM   3750 C  CB    . ASP B 1 76  ? 20.096  24.857  9.154   1.00 18.15 ? 55  ASP B CB    1 
ATOM   3751 C  CG    . ASP B 1 76  ? 20.871  25.203  7.882   1.00 19.52 ? 55  ASP B CG    1 
ATOM   3752 O  OD1   . ASP B 1 76  ? 20.377  24.859  6.773   1.00 19.14 ? 55  ASP B OD1   1 
ATOM   3753 O  OD2   . ASP B 1 76  ? 22.011  25.710  8.023   1.00 19.23 ? 55  ASP B OD2   1 
ATOM   3754 N  N     . LEU B 1 77  ? 16.641  24.066  9.685   1.00 18.45 ? 56  LEU B N     1 
ATOM   3755 C  CA    . LEU B 1 77  ? 15.739  23.180  10.471  1.00 19.10 ? 56  LEU B CA    1 
ATOM   3756 C  C     . LEU B 1 77  ? 16.231  21.734  10.489  1.00 18.97 ? 56  LEU B C     1 
ATOM   3757 O  O     . LEU B 1 77  ? 15.838  21.002  11.429  1.00 17.70 ? 56  LEU B O     1 
ATOM   3758 C  CB    . LEU B 1 77  ? 14.322  23.276  9.925   1.00 21.16 ? 56  LEU B CB    1 
ATOM   3759 C  CG    . LEU B 1 77  ? 13.664  24.626  10.200  1.00 26.27 ? 56  LEU B CG    1 
ATOM   3760 C  CD1   . LEU B 1 77  ? 12.292  24.687  9.572   1.00 32.50 ? 56  LEU B CD1   1 
ATOM   3761 C  CD2   . LEU B 1 77  ? 13.594  24.900  11.689  1.00 26.47 ? 56  LEU B CD2   1 
ATOM   3762 N  N     . GLY B 1 78  ? 16.995  21.342  9.479   1.00 19.28 ? 57  GLY B N     1 
ATOM   3763 C  CA    . GLY B 1 78  ? 17.632  20.028  9.381   1.00 18.92 ? 57  GLY B CA    1 
ATOM   3764 C  C     . GLY B 1 78  ? 19.122  20.097  9.582   1.00 19.13 ? 57  GLY B C     1 
ATOM   3765 O  O     . GLY B 1 78  ? 19.593  20.950  10.372  1.00 16.15 ? 57  GLY B O     1 
ATOM   3766 N  N     . GLY B 1 79  ? 19.849  19.192  8.914   1.00 17.52 ? 58  GLY B N     1 
ATOM   3767 C  CA    . GLY B 1 79  ? 21.313  19.128  8.964   1.00 19.14 ? 58  GLY B CA    1 
ATOM   3768 C  C     . GLY B 1 79  ? 21.963  20.471  8.704   1.00 17.09 ? 58  GLY B C     1 
ATOM   3769 O  O     . GLY B 1 79  ? 21.519  21.165  7.760   1.00 17.84 ? 58  GLY B O     1 
ATOM   3770 N  N     . GLN B 1 80  ? 22.954  20.828  9.515   1.00 16.49 ? 59  GLN B N     1 
ATOM   3771 C  CA    . GLN B 1 80  ? 23.593  22.175  9.441   1.00 17.33 ? 59  GLN B CA    1 
ATOM   3772 C  C     . GLN B 1 80  ? 25.122  22.149  9.489   1.00 18.64 ? 59  GLN B C     1 
ATOM   3773 O  O     . GLN B 1 80  ? 25.691  23.112  8.906   1.00 20.13 ? 59  GLN B O     1 
ATOM   3774 C  CB    . GLN B 1 80  ? 23.013  23.105  10.527  1.00 18.27 ? 59  GLN B CB    1 
ATOM   3775 C  CG    . GLN B 1 80  ? 23.524  22.965  11.946  1.00 19.97 ? 59  GLN B CG    1 
ATOM   3776 C  CD    . GLN B 1 80  ? 22.927  24.053  12.828  1.00 21.46 ? 59  GLN B CD    1 
ATOM   3777 O  OE1   . GLN B 1 80  ? 21.815  24.560  12.601  1.00 20.72 ? 59  GLN B OE1   1 
ATOM   3778 N  NE2   . GLN B 1 80  ? 23.668  24.422  13.848  1.00 21.05 ? 59  GLN B NE2   1 
ATOM   3779 N  N     . TRP B 1 81  ? 25.760  21.213  10.220  1.00 17.82 ? 60  TRP B N     1 
ATOM   3780 C  CA    . TRP B 1 81  ? 27.219  21.250  10.506  1.00 17.47 ? 60  TRP B CA    1 
ATOM   3781 C  C     . TRP B 1 81  ? 27.999  20.350  9.538   1.00 19.47 ? 60  TRP B C     1 
ATOM   3782 O  O     . TRP B 1 81  ? 27.515  19.274  9.182   1.00 18.89 ? 60  TRP B O     1 
ATOM   3783 C  CB    . TRP B 1 81  ? 27.488  20.811  11.942  1.00 17.31 ? 60  TRP B CB    1 
ATOM   3784 C  CG    . TRP B 1 81  ? 27.212  21.829  13.008  1.00 18.41 ? 60  TRP B CG    1 
ATOM   3785 C  CD1   . TRP B 1 81  ? 27.833  23.025  13.209  1.00 18.20 ? 60  TRP B CD1   1 
ATOM   3786 C  CD2   . TRP B 1 81  ? 26.268  21.673  14.071  1.00 19.76 ? 60  TRP B CD2   1 
ATOM   3787 N  NE1   . TRP B 1 81  ? 27.316  23.640  14.322  1.00 19.54 ? 60  TRP B NE1   1 
ATOM   3788 C  CE2   . TRP B 1 81  ? 26.377  22.819  14.898  1.00 20.36 ? 60  TRP B CE2   1 
ATOM   3789 C  CE3   . TRP B 1 81  ? 25.398  20.638  14.440  1.00 21.55 ? 60  TRP B CE3   1 
ATOM   3790 C  CZ2   . TRP B 1 81  ? 25.607  22.973  16.058  1.00 20.50 ? 60  TRP B CZ2   1 
ATOM   3791 C  CZ3   . TRP B 1 81  ? 24.614  20.810  15.564  1.00 21.74 ? 60  TRP B CZ3   1 
ATOM   3792 C  CH2   . TRP B 1 81  ? 24.717  21.965  16.352  1.00 21.46 ? 60  TRP B CH2   1 
ATOM   3793 N  N     . ILE B 1 82  ? 29.227  20.739  9.223   1.00 17.32 ? 61  ILE B N     1 
ATOM   3794 C  CA    . ILE B 1 82  ? 30.230  19.842  8.607   1.00 18.69 ? 61  ILE B CA    1 
ATOM   3795 C  C     . ILE B 1 82  ? 31.518  20.030  9.390   1.00 20.95 ? 61  ILE B C     1 
ATOM   3796 O  O     . ILE B 1 82  ? 31.660  21.062  10.088  1.00 21.61 ? 61  ILE B O     1 
ATOM   3797 C  CB    . ILE B 1 82  ? 30.404  20.127  7.115   1.00 21.06 ? 61  ILE B CB    1 
ATOM   3798 C  CG1   . ILE B 1 82  ? 31.086  21.485  6.884   1.00 23.21 ? 61  ILE B CG1   1 
ATOM   3799 C  CG2   . ILE B 1 82  ? 29.097  20.002  6.353   1.00 21.04 ? 61  ILE B CG2   1 
ATOM   3800 C  CD1   . ILE B 1 82  ? 31.455  21.737  5.417   1.00 25.97 ? 61  ILE B CD1   1 
ATOM   3801 N  N     . GLY B 1 83  ? 32.374  19.021  9.377   1.00 19.22 ? 62  GLY B N     1 
ATOM   3802 C  CA    . GLY B 1 83  ? 33.631  19.102  10.131  1.00 19.71 ? 62  GLY B CA    1 
ATOM   3803 C  C     . GLY B 1 83  ? 34.770  18.416  9.405   1.00 22.09 ? 62  GLY B C     1 
ATOM   3804 O  O     . GLY B 1 83  ? 34.569  17.752  8.395   1.00 20.70 ? 62  GLY B O     1 
ATOM   3805 N  N     . PRO B 1 84  ? 35.980  18.490  9.984   1.00 22.27 ? 63  PRO B N     1 
ATOM   3806 C  CA    . PRO B 1 84  ? 37.154  17.805  9.439   1.00 23.95 ? 63  PRO B CA    1 
ATOM   3807 C  C     . PRO B 1 84  ? 36.969  16.290  9.334   1.00 22.81 ? 63  PRO B C     1 
ATOM   3808 O  O     . PRO B 1 84  ? 36.381  15.654  10.228  1.00 21.64 ? 63  PRO B O     1 
ATOM   3809 C  CB    . PRO B 1 84  ? 38.301  18.167  10.403  1.00 26.69 ? 63  PRO B CB    1 
ATOM   3810 C  CG    . PRO B 1 84  ? 37.627  18.743  11.630  1.00 26.53 ? 63  PRO B CG    1 
ATOM   3811 C  CD    . PRO B 1 84  ? 36.288  19.280  11.171  1.00 23.32 ? 63  PRO B CD    1 
ATOM   3812 N  N     . GLY B 1 85  ? 37.456  15.727  8.235   1.00 21.76 ? 64  GLY B N     1 
ATOM   3813 C  CA    . GLY B 1 85  ? 37.312  14.284  7.946   1.00 23.03 ? 64  GLY B CA    1 
ATOM   3814 C  C     . GLY B 1 85  ? 36.092  14.027  7.092   1.00 21.64 ? 64  GLY B C     1 
ATOM   3815 O  O     . GLY B 1 85  ? 36.000  12.926  6.534   1.00 21.31 ? 64  GLY B O     1 
ATOM   3816 N  N     . GLN B 1 86  ? 35.160  14.991  6.977   1.00 20.26 ? 65  GLN B N     1 
ATOM   3817 C  CA    . GLN B 1 86  ? 34.006  14.922  6.028   1.00 20.07 ? 65  GLN B CA    1 
ATOM   3818 C  C     . GLN B 1 86  ? 34.438  15.519  4.671   1.00 20.07 ? 65  GLN B C     1 
ATOM   3819 O  O     . GLN B 1 86  ? 34.053  16.640  4.343   1.00 20.66 ? 65  GLN B O     1 
ATOM   3820 C  CB    . GLN B 1 86  ? 32.796  15.628  6.646   1.00 19.74 ? 65  GLN B CB    1 
ATOM   3821 C  CG    . GLN B 1 86  ? 32.295  14.965  7.923   1.00 18.11 ? 65  GLN B CG    1 
ATOM   3822 C  CD    . GLN B 1 86  ? 31.187  15.786  8.533   1.00 17.43 ? 65  GLN B CD    1 
ATOM   3823 O  OE1   . GLN B 1 86  ? 30.784  16.790  7.992   1.00 18.06 ? 65  GLN B OE1   1 
ATOM   3824 N  NE2   . GLN B 1 86  ? 30.692  15.359  9.665   1.00 19.17 ? 65  GLN B NE2   1 
ATOM   3825 N  N     . ASP B 1 87  ? 35.178  14.749  3.870   1.00 20.99 ? 66  ASP B N     1 
ATOM   3826 C  CA    . ASP B 1 87  ? 35.874  15.294  2.678   1.00 22.11 ? 66  ASP B CA    1 
ATOM   3827 C  C     . ASP B 1 87  ? 34.901  15.439  1.521   1.00 21.03 ? 66  ASP B C     1 
ATOM   3828 O  O     . ASP B 1 87  ? 35.165  16.287  0.634   1.00 21.59 ? 66  ASP B O     1 
ATOM   3829 C  CB    . ASP B 1 87  ? 37.063  14.418  2.258   1.00 26.33 ? 66  ASP B CB    1 
ATOM   3830 C  CG    . ASP B 1 87  ? 38.156  14.382  3.318   1.00 28.77 ? 66  ASP B CG    1 
ATOM   3831 O  OD1   . ASP B 1 87  ? 38.299  15.357  4.052   1.00 31.48 ? 66  ASP B OD1   1 
ATOM   3832 O  OD2   . ASP B 1 87  ? 38.811  13.347  3.428   1.00 36.46 ? 66  ASP B OD2   1 
ATOM   3833 N  N     . ARG B 1 88  ? 33.825  14.642  1.470   1.00 20.83 ? 67  ARG B N     1 
ATOM   3834 C  CA    . ARG B 1 88  ? 32.889  14.670  0.314   1.00 21.15 ? 67  ARG B CA    1 
ATOM   3835 C  C     . ARG B 1 88  ? 32.031  15.926  0.380   1.00 19.75 ? 67  ARG B C     1 
ATOM   3836 O  O     . ARG B 1 88  ? 31.843  16.616  -0.662  1.00 21.05 ? 67  ARG B O     1 
ATOM   3837 C  CB    . ARG B 1 88  ? 32.025  13.402  0.298   1.00 22.40 ? 67  ARG B CB    1 
ATOM   3838 C  CG    . ARG B 1 88  ? 32.867  12.132  0.151   1.00 25.52 ? 67  ARG B CG    1 
ATOM   3839 C  CD    . ARG B 1 88  ? 32.031  10.854  0.061   1.00 27.29 ? 67  ARG B CD    1 
ATOM   3840 N  NE    . ARG B 1 88  ? 32.891  9.661   0.098   1.00 33.38 ? 67  ARG B NE    1 
ATOM   3841 C  CZ    . ARG B 1 88  ? 33.463  9.104   -0.969  1.00 36.95 ? 67  ARG B CZ    1 
ATOM   3842 N  NH1   . ARG B 1 88  ? 33.260  9.607   -2.171  1.00 45.30 ? 67  ARG B NH1   1 
ATOM   3843 N  NH2   . ARG B 1 88  ? 34.246  8.048   -0.852  1.00 38.27 ? 67  ARG B NH2   1 
ATOM   3844 N  N     . VAL B 1 89  ? 31.461  16.229  1.539   1.00 20.20 ? 68  VAL B N     1 
ATOM   3845 C  CA    . VAL B 1 89  ? 30.594  17.443  1.621   1.00 19.95 ? 68  VAL B CA    1 
ATOM   3846 C  C     . VAL B 1 89  ? 31.484  18.692  1.495   1.00 20.00 ? 68  VAL B C     1 
ATOM   3847 O  O     . VAL B 1 89  ? 31.052  19.668  0.808   1.00 20.19 ? 68  VAL B O     1 
ATOM   3848 C  CB    . VAL B 1 89  ? 29.729  17.470  2.893   1.00 19.71 ? 68  VAL B CB    1 
ATOM   3849 C  CG1   . VAL B 1 89  ? 30.572  17.556  4.155   1.00 19.19 ? 68  VAL B CG1   1 
ATOM   3850 C  CG2   . VAL B 1 89  ? 28.688  18.578  2.804   1.00 19.54 ? 68  VAL B CG2   1 
ATOM   3851 N  N     . ALA B 1 90  ? 32.687  18.658  2.064   1.00 21.47 ? 69  ALA B N     1 
ATOM   3852 C  CA    . ALA B 1 90  ? 33.604  19.823  1.977   1.00 22.09 ? 69  ALA B CA    1 
ATOM   3853 C  C     . ALA B 1 90  ? 33.938  20.047  0.490   1.00 22.39 ? 69  ALA B C     1 
ATOM   3854 O  O     . ALA B 1 90  ? 33.906  21.213  0.062   1.00 22.46 ? 69  ALA B O     1 
ATOM   3855 C  CB    . ALA B 1 90  ? 34.816  19.637  2.859   1.00 23.54 ? 69  ALA B CB    1 
ATOM   3856 N  N     . ALA B 1 91  ? 34.241  18.984  -0.284  1.00 23.63 ? 70  ALA B N     1 
ATOM   3857 C  CA    . ALA B 1 91  ? 34.532  19.069  -1.739  1.00 23.36 ? 70  ALA B CA    1 
ATOM   3858 C  C     . ALA B 1 91  ? 33.305  19.595  -2.495  1.00 24.23 ? 70  ALA B C     1 
ATOM   3859 O  O     . ALA B 1 91  ? 33.499  20.441  -3.389  1.00 21.77 ? 70  ALA B O     1 
ATOM   3860 C  CB    . ALA B 1 91  ? 35.009  17.737  -2.290  1.00 25.02 ? 70  ALA B CB    1 
ATOM   3861 N  N     . LEU B 1 92  ? 32.077  19.144  -2.178  1.00 21.81 ? 71  LEU B N     1 
ATOM   3862 C  CA    . LEU B 1 92  ? 30.847  19.590  -2.883  1.00 21.87 ? 71  LEU B CA    1 
ATOM   3863 C  C     . LEU B 1 92  ? 30.605  21.078  -2.613  1.00 21.69 ? 71  LEU B C     1 
ATOM   3864 O  O     . LEU B 1 92  ? 30.236  21.822  -3.562  1.00 22.17 ? 71  LEU B O     1 
ATOM   3865 C  CB    . LEU B 1 92  ? 29.635  18.765  -2.408  1.00 21.57 ? 71  LEU B CB    1 
ATOM   3866 C  CG    . LEU B 1 92  ? 28.351  18.982  -3.195  1.00 23.35 ? 71  LEU B CG    1 
ATOM   3867 C  CD1   . LEU B 1 92  ? 28.480  18.448  -4.625  1.00 24.39 ? 71  LEU B CD1   1 
ATOM   3868 C  CD2   . LEU B 1 92  ? 27.153  18.340  -2.500  1.00 23.44 ? 71  LEU B CD2   1 
ATOM   3869 N  N     . ALA B 1 93  ? 30.745  21.514  -1.368  1.00 22.03 ? 72  ALA B N     1 
ATOM   3870 C  CA    . ALA B 1 93  ? 30.494  22.932  -1.016  1.00 21.72 ? 72  ALA B CA    1 
ATOM   3871 C  C     . ALA B 1 93  ? 31.467  23.808  -1.830  1.00 25.55 ? 72  ALA B C     1 
ATOM   3872 O  O     . ALA B 1 93  ? 31.012  24.817  -2.419  1.00 23.68 ? 72  ALA B O     1 
ATOM   3873 C  CB    . ALA B 1 93  ? 30.670  23.171  0.472   1.00 23.42 ? 72  ALA B CB    1 
ATOM   3874 N  N     . ALA B 1 94  ? 32.748  23.443  -1.828  1.00 25.45 ? 73  ALA B N     1 
ATOM   3875 C  CA    . ALA B 1 94  ? 33.818  24.154  -2.577  1.00 26.82 ? 73  ALA B CA    1 
ATOM   3876 C  C     . ALA B 1 94  ? 33.490  24.162  -4.074  1.00 26.83 ? 73  ALA B C     1 
ATOM   3877 O  O     . ALA B 1 94  ? 33.499  25.246  -4.701  1.00 27.61 ? 73  ALA B O     1 
ATOM   3878 C  CB    . ALA B 1 94  ? 35.145  23.512  -2.276  1.00 29.90 ? 73  ALA B CB    1 
ATOM   3879 N  N     . GLU B 1 95  ? 33.095  23.018  -4.620  1.00 27.42 ? 74  GLU B N     1 
ATOM   3880 C  CA    . GLU B 1 95  ? 32.728  22.878  -6.044  1.00 27.02 ? 74  GLU B CA    1 
ATOM   3881 C  C     . GLU B 1 95  ? 31.581  23.822  -6.374  1.00 26.07 ? 74  GLU B C     1 
ATOM   3882 O  O     . GLU B 1 95  ? 31.663  24.526  -7.417  1.00 24.26 ? 74  GLU B O     1 
ATOM   3883 C  CB    . GLU B 1 95  ? 32.399  21.433  -6.404  1.00 28.21 ? 74  GLU B CB    1 
ATOM   3884 C  CG    . GLU B 1 95  ? 31.977  21.314  -7.844  1.00 34.31 ? 74  GLU B CG    1 
ATOM   3885 C  CD    . GLU B 1 95  ? 31.412  19.974  -8.264  1.00 38.75 ? 74  GLU B CD    1 
ATOM   3886 O  OE1   . GLU B 1 95  ? 31.457  19.710  -9.469  1.00 44.57 ? 74  GLU B OE1   1 
ATOM   3887 O  OE2   . GLU B 1 95  ? 30.907  19.226  -7.410  1.00 37.11 ? 74  GLU B OE2   1 
ATOM   3888 N  N     . LEU B 1 96  ? 30.555  23.918  -5.535  1.00 23.19 ? 75  LEU B N     1 
ATOM   3889 C  CA    . LEU B 1 96  ? 29.323  24.620  -5.924  1.00 24.25 ? 75  LEU B CA    1 
ATOM   3890 C  C     . LEU B 1 96  ? 29.311  26.029  -5.327  1.00 23.06 ? 75  LEU B C     1 
ATOM   3891 O  O     . LEU B 1 96  ? 28.273  26.672  -5.434  1.00 29.76 ? 75  LEU B O     1 
ATOM   3892 C  CB    . LEU B 1 96  ? 28.113  23.784  -5.495  1.00 24.68 ? 75  LEU B CB    1 
ATOM   3893 C  CG    . LEU B 1 96  ? 28.000  22.420  -6.168  1.00 27.58 ? 75  LEU B CG    1 
ATOM   3894 C  CD1   . LEU B 1 96  ? 26.746  21.684  -5.670  1.00 28.35 ? 75  LEU B CD1   1 
ATOM   3895 C  CD2   . LEU B 1 96  ? 28.001  22.538  -7.687  1.00 28.86 ? 75  LEU B CD2   1 
ATOM   3896 N  N     . GLY B 1 97  ? 30.436  26.474  -4.781  1.00 24.00 ? 76  GLY B N     1 
ATOM   3897 C  CA    . GLY B 1 97  ? 30.702  27.871  -4.355  1.00 25.08 ? 76  GLY B CA    1 
ATOM   3898 C  C     . GLY B 1 97  ? 29.956  28.272  -3.086  1.00 25.71 ? 76  GLY B C     1 
ATOM   3899 O  O     . GLY B 1 97  ? 29.548  29.439  -2.971  1.00 25.89 ? 76  GLY B O     1 
ATOM   3900 N  N     . VAL B 1 98  ? 29.724  27.330  -2.171  1.00 22.29 ? 77  VAL B N     1 
ATOM   3901 C  CA    . VAL B 1 98  ? 29.097  27.619  -0.842  1.00 25.15 ? 77  VAL B CA    1 
ATOM   3902 C  C     . VAL B 1 98  ? 30.218  27.759  0.187   1.00 24.28 ? 77  VAL B C     1 
ATOM   3903 O  O     . VAL B 1 98  ? 30.945  26.800  0.429   1.00 27.40 ? 77  VAL B O     1 
ATOM   3904 C  CB    . VAL B 1 98  ? 28.046  26.545  -0.467  1.00 22.80 ? 77  VAL B CB    1 
ATOM   3905 C  CG1   . VAL B 1 98  ? 27.396  26.830  0.871   1.00 26.35 ? 77  VAL B CG1   1 
ATOM   3906 C  CG2   . VAL B 1 98  ? 26.970  26.444  -1.537  1.00 23.39 ? 77  VAL B CG2   1 
ATOM   3907 N  N     . GLU B 1 99  ? 30.327  28.928  0.804   1.00 26.89 ? 78  GLU B N     1 
ATOM   3908 C  CA    . GLU B 1 99  ? 31.371  29.254  1.794   1.00 29.95 ? 78  GLU B CA    1 
ATOM   3909 C  C     . GLU B 1 99  ? 30.984  28.659  3.153   1.00 25.87 ? 78  GLU B C     1 
ATOM   3910 O  O     . GLU B 1 99  ? 29.790  28.514  3.373   1.00 25.12 ? 78  GLU B O     1 
ATOM   3911 C  CB    . GLU B 1 99  ? 31.532  30.780  1.923   1.00 36.99 ? 78  GLU B CB    1 
ATOM   3912 C  CG    . GLU B 1 99  ? 32.977  31.192  2.182   1.00 46.12 ? 78  GLU B CG    1 
ATOM   3913 C  CD    . GLU B 1 99  ? 33.994  30.238  1.567   1.00 55.14 ? 78  GLU B CD    1 
ATOM   3914 O  OE1   . GLU B 1 99  ? 34.718  29.507  2.347   1.00 58.84 ? 78  GLU B OE1   1 
ATOM   3915 O  OE2   . GLU B 1 99  ? 34.027  30.177  0.309   1.00 53.23 ? 78  GLU B OE2   1 
ATOM   3916 N  N     . THR B 1 100 ? 31.956  28.397  4.021   1.00 24.53 ? 79  THR B N     1 
ATOM   3917 C  CA    . THR B 1 100 ? 31.710  27.968  5.421   1.00 25.42 ? 79  THR B CA    1 
ATOM   3918 C  C     . THR B 1 100 ? 31.895  29.162  6.354   1.00 28.31 ? 79  THR B C     1 
ATOM   3919 O  O     . THR B 1 100 ? 32.580  30.113  5.960   1.00 25.01 ? 79  THR B O     1 
ATOM   3920 C  CB    . THR B 1 100 ? 32.596  26.777  5.788   1.00 28.05 ? 79  THR B CB    1 
ATOM   3921 O  OG1   . THR B 1 100 ? 33.966  27.174  5.815   1.00 25.96 ? 79  THR B OG1   1 
ATOM   3922 C  CG2   . THR B 1 100 ? 32.441  25.660  4.787   1.00 28.77 ? 79  THR B CG2   1 
ATOM   3923 N  N     . TYR B 1 101 ? 31.321  29.084  7.556   1.00 22.71 ? 80  TYR B N     1 
ATOM   3924 C  CA    . TYR B 1 101 ? 31.712  29.920  8.715   1.00 23.65 ? 80  TYR B CA    1 
ATOM   3925 C  C     . TYR B 1 101 ? 31.860  29.013  9.920   1.00 24.10 ? 80  TYR B C     1 
ATOM   3926 O  O     . TYR B 1 101 ? 31.155  28.000  10.017  1.00 22.93 ? 80  TYR B O     1 
ATOM   3927 C  CB    . TYR B 1 101 ? 30.716  31.052  8.984   1.00 24.08 ? 80  TYR B CB    1 
ATOM   3928 C  CG    . TYR B 1 101 ? 29.292  30.682  9.327   1.00 22.91 ? 80  TYR B CG    1 
ATOM   3929 C  CD1   . TYR B 1 101 ? 28.412  30.261  8.332   1.00 20.83 ? 80  TYR B CD1   1 
ATOM   3930 C  CD2   . TYR B 1 101 ? 28.787  30.867  10.611  1.00 22.82 ? 80  TYR B CD2   1 
ATOM   3931 C  CE1   . TYR B 1 101 ? 27.089  29.958  8.625   1.00 23.66 ? 80  TYR B CE1   1 
ATOM   3932 C  CE2   . TYR B 1 101 ? 27.460  30.573  10.910  1.00 22.45 ? 80  TYR B CE2   1 
ATOM   3933 C  CZ    . TYR B 1 101 ? 26.607  30.115  9.916   1.00 22.25 ? 80  TYR B CZ    1 
ATOM   3934 O  OH    . TYR B 1 101 ? 25.294  29.782  10.187  1.00 23.43 ? 80  TYR B OH    1 
ATOM   3935 N  N     . PRO B 1 102 ? 32.779  29.351  10.839  1.00 21.97 ? 81  PRO B N     1 
ATOM   3936 C  CA    . PRO B 1 102 ? 33.006  28.532  12.023  1.00 22.84 ? 81  PRO B CA    1 
ATOM   3937 C  C     . PRO B 1 102 ? 31.849  28.652  13.013  1.00 22.88 ? 81  PRO B C     1 
ATOM   3938 O  O     . PRO B 1 102 ? 31.281  29.738  13.206  1.00 23.92 ? 81  PRO B O     1 
ATOM   3939 C  CB    . PRO B 1 102 ? 34.349  29.040  12.558  1.00 24.19 ? 81  PRO B CB    1 
ATOM   3940 C  CG    . PRO B 1 102 ? 34.408  30.453  12.091  1.00 24.86 ? 81  PRO B CG    1 
ATOM   3941 C  CD    . PRO B 1 102 ? 33.709  30.499  10.751  1.00 23.43 ? 81  PRO B CD    1 
ATOM   3942 N  N     . GLN B 1 103 ? 31.474  27.516  13.590  1.00 19.32 ? 82  GLN B N     1 
ATOM   3943 C  CA    . GLN B 1 103 ? 30.677  27.491  14.830  1.00 20.70 ? 82  GLN B CA    1 
ATOM   3944 C  C     . GLN B 1 103 ? 31.448  28.273  15.903  1.00 19.42 ? 82  GLN B C     1 
ATOM   3945 O  O     . GLN B 1 103 ? 32.584  27.933  16.237  1.00 20.02 ? 82  GLN B O     1 
ATOM   3946 C  CB    . GLN B 1 103 ? 30.453  26.043  15.277  1.00 19.62 ? 82  GLN B CB    1 
ATOM   3947 C  CG    . GLN B 1 103 ? 29.772  25.895  16.634  1.00 20.01 ? 82  GLN B CG    1 
ATOM   3948 C  CD    . GLN B 1 103 ? 28.352  26.394  16.624  1.00 19.28 ? 82  GLN B CD    1 
ATOM   3949 O  OE1   . GLN B 1 103 ? 27.590  26.157  15.693  1.00 20.98 ? 82  GLN B OE1   1 
ATOM   3950 N  NE2   . GLN B 1 103 ? 28.003  27.210  17.609  1.00 20.66 ? 82  GLN B NE2   1 
ATOM   3951 N  N     . PRO B 1 104 ? 30.806  29.269  16.546  1.00 21.85 ? 83  PRO B N     1 
ATOM   3952 C  CA    . PRO B 1 104 ? 31.403  29.942  17.701  1.00 24.09 ? 83  PRO B CA    1 
ATOM   3953 C  C     . PRO B 1 104 ? 31.827  28.961  18.805  1.00 26.62 ? 83  PRO B C     1 
ATOM   3954 O  O     . PRO B 1 104 ? 31.094  28.028  19.102  1.00 27.89 ? 83  PRO B O     1 
ATOM   3955 C  CB    . PRO B 1 104 ? 30.283  30.894  18.143  1.00 25.66 ? 83  PRO B CB    1 
ATOM   3956 C  CG    . PRO B 1 104 ? 29.508  31.172  16.893  1.00 23.04 ? 83  PRO B CG    1 
ATOM   3957 C  CD    . PRO B 1 104 ? 29.521  29.855  16.141  1.00 22.15 ? 83  PRO B CD    1 
ATOM   3958 N  N     . THR B 1 105 ? 33.020  29.165  19.351  1.00 25.48 ? 84  THR B N     1 
ATOM   3959 C  CA    . THR B 1 105 ? 33.704  28.273  20.317  1.00 26.38 ? 84  THR B CA    1 
ATOM   3960 C  C     . THR B 1 105 ? 33.967  28.967  21.668  1.00 26.74 ? 84  THR B C     1 
ATOM   3961 O  O     . THR B 1 105 ? 34.107  28.247  22.705  1.00 27.16 ? 84  THR B O     1 
ATOM   3962 C  CB    . THR B 1 105 ? 35.034  27.799  19.720  1.00 26.82 ? 84  THR B CB    1 
ATOM   3963 O  OG1   . THR B 1 105 ? 35.718  28.981  19.308  1.00 30.42 ? 84  THR B OG1   1 
ATOM   3964 C  CG2   . THR B 1 105 ? 34.854  26.868  18.534  1.00 26.55 ? 84  THR B CG2   1 
ATOM   3965 N  N     . GLU B 1 106 ? 34.025  30.296  21.660  1.00 28.26 ? 85  GLU B N     1 
ATOM   3966 C  CA    . GLU B 1 106 ? 34.582  31.097  22.790  1.00 29.03 ? 85  GLU B CA    1 
ATOM   3967 C  C     . GLU B 1 106 ? 33.468  31.400  23.800  1.00 27.21 ? 85  GLU B C     1 
ATOM   3968 O  O     . GLU B 1 106 ? 32.280  31.341  23.431  1.00 27.48 ? 85  GLU B O     1 
ATOM   3969 C  CB    . GLU B 1 106 ? 35.297  32.319  22.207  1.00 34.68 ? 85  GLU B CB    1 
ATOM   3970 C  CG    . GLU B 1 106 ? 36.517  31.954  21.337  1.00 40.07 ? 85  GLU B CG    1 
ATOM   3971 C  CD    . GLU B 1 106 ? 37.432  30.814  21.805  1.00 48.56 ? 85  GLU B CD    1 
ATOM   3972 O  OE1   . GLU B 1 106 ? 37.474  29.729  21.123  1.00 44.65 ? 85  GLU B OE1   1 
ATOM   3973 O  OE2   . GLU B 1 106 ? 38.109  30.984  22.858  1.00 47.95 ? 85  GLU B OE2   1 
ATOM   3974 N  N     . GLY B 1 107 ? 33.855  31.767  25.025  1.00 25.08 ? 86  GLY B N     1 
ATOM   3975 C  CA    . GLY B 1 107 ? 32.947  32.039  26.152  1.00 25.82 ? 86  GLY B CA    1 
ATOM   3976 C  C     . GLY B 1 107 ? 32.758  30.807  27.024  1.00 24.69 ? 86  GLY B C     1 
ATOM   3977 O  O     . GLY B 1 107 ? 33.060  29.650  26.591  1.00 27.29 ? 86  GLY B O     1 
ATOM   3978 N  N     . ASP B 1 108 ? 32.210  31.011  28.208  1.00 25.11 ? 87  ASP B N     1 
ATOM   3979 C  CA    . ASP B 1 108 ? 31.984  29.897  29.155  1.00 24.20 ? 87  ASP B CA    1 
ATOM   3980 C  C     . ASP B 1 108 ? 30.759  29.077  28.748  1.00 22.18 ? 87  ASP B C     1 
ATOM   3981 O  O     . ASP B 1 108 ? 29.722  29.671  28.413  1.00 23.38 ? 87  ASP B O     1 
ATOM   3982 C  CB    . ASP B 1 108 ? 31.737  30.397  30.560  1.00 27.79 ? 87  ASP B CB    1 
ATOM   3983 C  CG    . ASP B 1 108 ? 32.981  30.963  31.203  1.00 33.26 ? 87  ASP B CG    1 
ATOM   3984 O  OD1   . ASP B 1 108 ? 34.107  30.577  30.798  1.00 31.72 ? 87  ASP B OD1   1 
ATOM   3985 O  OD2   . ASP B 1 108 ? 32.801  31.765  32.107  1.00 34.15 ? 87  ASP B OD2   1 
ATOM   3986 N  N     . ASP B 1 109 ? 30.893  27.756  28.833  1.00 26.12 ? 88  ASP B N     1 
ATOM   3987 C  CA    . ASP B 1 109 ? 29.755  26.808  28.713  1.00 24.11 ? 88  ASP B CA    1 
ATOM   3988 C  C     . ASP B 1 109 ? 29.118  26.716  30.101  1.00 26.04 ? 88  ASP B C     1 
ATOM   3989 O  O     . ASP B 1 109 ? 29.850  26.873  31.118  1.00 27.15 ? 88  ASP B O     1 
ATOM   3990 C  CB    . ASP B 1 109 ? 30.196  25.439  28.181  1.00 24.42 ? 88  ASP B CB    1 
ATOM   3991 C  CG    . ASP B 1 109 ? 30.912  25.473  26.832  1.00 26.39 ? 88  ASP B CG    1 
ATOM   3992 O  OD1   . ASP B 1 109 ? 30.518  26.271  25.963  1.00 26.04 ? 88  ASP B OD1   1 
ATOM   3993 O  OD2   . ASP B 1 109 ? 31.858  24.698  26.677  1.00 31.41 ? 88  ASP B OD2   1 
ATOM   3994 N  N     . VAL B 1 110 ? 27.823  26.421  30.160  1.00 25.50 ? 89  VAL B N     1 
ATOM   3995 C  CA    . VAL B 1 110 ? 27.099  26.238  31.449  1.00 25.27 ? 89  VAL B CA    1 
ATOM   3996 C  C     . VAL B 1 110 ? 26.709  24.777  31.570  1.00 26.47 ? 89  VAL B C     1 
ATOM   3997 O  O     . VAL B 1 110 ? 26.074  24.259  30.658  1.00 27.74 ? 89  VAL B O     1 
ATOM   3998 C  CB    . VAL B 1 110 ? 25.864  27.143  31.583  1.00 23.77 ? 89  VAL B CB    1 
ATOM   3999 C  CG1   . VAL B 1 110 ? 25.167  26.922  32.925  1.00 24.06 ? 89  VAL B CG1   1 
ATOM   4000 C  CG2   . VAL B 1 110 ? 26.237  28.591  31.401  1.00 24.46 ? 89  VAL B CG2   1 
ATOM   4001 N  N     . VAL B 1 111 ? 27.078  24.159  32.671  1.00 24.87 ? 90  VAL B N     1 
ATOM   4002 C  CA    . VAL B 1 111 ? 26.704  22.758  32.957  1.00 26.06 ? 90  VAL B CA    1 
ATOM   4003 C  C     . VAL B 1 111 ? 25.768  22.774  34.166  1.00 25.01 ? 90  VAL B C     1 
ATOM   4004 O  O     . VAL B 1 111 ? 26.111  23.390  35.226  1.00 25.57 ? 90  VAL B O     1 
ATOM   4005 C  CB    . VAL B 1 111 ? 27.933  21.869  33.187  1.00 28.61 ? 90  VAL B CB    1 
ATOM   4006 C  CG1   . VAL B 1 111 ? 27.497  20.444  33.447  1.00 28.41 ? 90  VAL B CG1   1 
ATOM   4007 C  CG2   . VAL B 1 111 ? 28.882  21.936  31.997  1.00 28.75 ? 90  VAL B CG2   1 
ATOM   4008 N  N     . LEU B 1 112 ? 24.615  22.143  34.001  1.00 23.14 ? 91  LEU B N     1 
ATOM   4009 C  CA    . LEU B 1 112 ? 23.637  21.978  35.101  1.00 24.34 ? 91  LEU B CA    1 
ATOM   4010 C  C     . LEU B 1 112 ? 23.407  20.490  35.308  1.00 23.48 ? 91  LEU B C     1 
ATOM   4011 O  O     . LEU B 1 112 ? 22.829  19.814  34.431  1.00 24.58 ? 91  LEU B O     1 
ATOM   4012 C  CB    . LEU B 1 112 ? 22.362  22.753  34.764  1.00 23.99 ? 91  LEU B CB    1 
ATOM   4013 C  CG    . LEU B 1 112 ? 21.214  22.560  35.756  1.00 23.51 ? 91  LEU B CG    1 
ATOM   4014 C  CD1   . LEU B 1 112 ? 21.564  23.125  37.128  1.00 25.42 ? 91  LEU B CD1   1 
ATOM   4015 C  CD2   . LEU B 1 112 ? 19.959  23.207  35.177  1.00 23.57 ? 91  LEU B CD2   1 
ATOM   4016 N  N     . PHE B 1 113 ? 23.951  19.975  36.407  1.00 29.34 ? 92  PHE B N     1 
ATOM   4017 C  CA    . PHE B 1 113 ? 23.813  18.555  36.826  1.00 30.23 ? 92  PHE B CA    1 
ATOM   4018 C  C     . PHE B 1 113 ? 22.469  18.342  37.529  1.00 31.48 ? 92  PHE B C     1 
ATOM   4019 O  O     . PHE B 1 113 ? 21.812  19.332  37.916  1.00 29.41 ? 92  PHE B O     1 
ATOM   4020 C  CB    . PHE B 1 113 ? 24.996  18.162  37.712  1.00 30.88 ? 92  PHE B CB    1 
ATOM   4021 C  CG    . PHE B 1 113 ? 26.327  18.137  37.012  1.00 28.97 ? 92  PHE B CG    1 
ATOM   4022 C  CD1   . PHE B 1 113 ? 27.289  19.104  37.271  1.00 32.96 ? 92  PHE B CD1   1 
ATOM   4023 C  CD2   . PHE B 1 113 ? 26.629  17.138  36.106  1.00 29.71 ? 92  PHE B CD2   1 
ATOM   4024 C  CE1   . PHE B 1 113 ? 28.530  19.065  36.640  1.00 30.30 ? 92  PHE B CE1   1 
ATOM   4025 C  CE2   . PHE B 1 113 ? 27.855  17.112  35.464  1.00 32.50 ? 92  PHE B CE2   1 
ATOM   4026 C  CZ    . PHE B 1 113 ? 28.815  18.068  35.743  1.00 31.67 ? 92  PHE B CZ    1 
ATOM   4027 N  N     . GLY B 1 114 ? 22.106  17.071  37.763  1.00 37.22 ? 93  GLY B N     1 
ATOM   4028 C  CA    . GLY B 1 114 ? 20.857  16.674  38.453  1.00 36.41 ? 93  GLY B CA    1 
ATOM   4029 C  C     . GLY B 1 114 ? 20.700  17.348  39.806  1.00 36.83 ? 93  GLY B C     1 
ATOM   4030 O  O     . GLY B 1 114 ? 19.553  17.647  40.170  1.00 40.10 ? 93  GLY B O     1 
ATOM   4031 N  N     . ASP B 1 115 ? 21.819  17.632  40.501  1.00 40.18 ? 94  ASP B N     1 
ATOM   4032 C  CA    . ASP B 1 115 ? 21.846  18.390  41.784  1.00 39.87 ? 94  ASP B CA    1 
ATOM   4033 C  C     . ASP B 1 115 ? 22.650  19.693  41.629  1.00 39.41 ? 94  ASP B C     1 
ATOM   4034 O  O     . ASP B 1 115 ? 23.553  19.759  40.731  1.00 35.75 ? 94  ASP B O     1 
ATOM   4035 C  CB    . ASP B 1 115 ? 22.412  17.549  42.935  1.00 47.13 ? 94  ASP B CB    1 
ATOM   4036 C  CG    . ASP B 1 115 ? 23.807  16.992  42.683  1.00 52.50 ? 94  ASP B CG    1 
ATOM   4037 O  OD1   . ASP B 1 115 ? 24.176  16.825  41.499  1.00 59.64 ? 94  ASP B OD1   1 
ATOM   4038 O  OD2   . ASP B 1 115 ? 24.511  16.710  43.677  1.00 70.80 ? 94  ASP B OD2   1 
ATOM   4039 N  N     . GLY B 1 116 ? 22.316  20.688  42.463  1.00 35.31 ? 95  GLY B N     1 
ATOM   4040 C  CA    . GLY B 1 116 ? 23.101  21.917  42.671  1.00 34.37 ? 95  GLY B CA    1 
ATOM   4041 C  C     . GLY B 1 116 ? 22.834  22.965  41.610  1.00 33.60 ? 95  GLY B C     1 
ATOM   4042 O  O     . GLY B 1 116 ? 21.949  22.754  40.727  1.00 28.82 ? 95  GLY B O     1 
ATOM   4043 N  N     . GLU B 1 117 ? 23.572  24.072  41.721  1.00 33.30 ? 96  GLU B N     1 
ATOM   4044 C  CA    . GLU B 1 117 ? 23.493  25.276  40.864  1.00 32.71 ? 96  GLU B CA    1 
ATOM   4045 C  C     . GLU B 1 117 ? 24.187  25.006  39.530  1.00 31.58 ? 96  GLU B C     1 
ATOM   4046 O  O     . GLU B 1 117 ? 25.025  24.114  39.432  1.00 30.82 ? 96  GLU B O     1 
ATOM   4047 C  CB    . GLU B 1 117 ? 24.237  26.457  41.495  1.00 39.17 ? 96  GLU B CB    1 
ATOM   4048 C  CG    . GLU B 1 117 ? 23.812  26.805  42.900  1.00 45.14 ? 96  GLU B CG    1 
ATOM   4049 C  CD    . GLU B 1 117 ? 24.647  27.942  43.467  1.00 47.32 ? 96  GLU B CD    1 
ATOM   4050 O  OE1   . GLU B 1 117 ? 25.442  27.679  44.384  1.00 52.98 ? 96  GLU B OE1   1 
ATOM   4051 O  OE2   . GLU B 1 117 ? 24.499  29.075  43.003  1.00 43.95 ? 96  GLU B OE2   1 
ATOM   4052 N  N     . PRO B 1 118 ? 23.873  25.792  38.478  1.00 31.53 ? 97  PRO B N     1 
ATOM   4053 C  CA    . PRO B 1 118 ? 24.602  25.711  37.210  1.00 29.34 ? 97  PRO B CA    1 
ATOM   4054 C  C     . PRO B 1 118 ? 26.067  26.131  37.406  1.00 30.80 ? 97  PRO B C     1 
ATOM   4055 O  O     . PRO B 1 118 ? 26.296  27.006  38.159  1.00 27.84 ? 97  PRO B O     1 
ATOM   4056 C  CB    . PRO B 1 118 ? 23.876  26.680  36.259  1.00 29.64 ? 97  PRO B CB    1 
ATOM   4057 C  CG    . PRO B 1 118 ? 22.902  27.458  37.098  1.00 32.34 ? 97  PRO B CG    1 
ATOM   4058 C  CD    . PRO B 1 118 ? 22.773  26.764  38.433  1.00 30.41 ? 97  PRO B CD    1 
ATOM   4059 N  N     . GLN B 1 119 ? 27.011  25.457  36.744  1.00 30.09 ? 98  GLN B N     1 
ATOM   4060 C  CA    . GLN B 1 119 ? 28.468  25.775  36.790  1.00 30.15 ? 98  GLN B CA    1 
ATOM   4061 C  C     . GLN B 1 119 ? 28.881  26.390  35.445  1.00 28.65 ? 98  GLN B C     1 
ATOM   4062 O  O     . GLN B 1 119 ? 28.516  25.822  34.409  1.00 29.46 ? 98  GLN B O     1 
ATOM   4063 C  CB    . GLN B 1 119 ? 29.278  24.498  37.056  1.00 30.47 ? 98  GLN B CB    1 
ATOM   4064 C  CG    . GLN B 1 119 ? 28.766  23.660  38.217  1.00 33.29 ? 98  GLN B CG    1 
ATOM   4065 C  CD    . GLN B 1 119 ? 29.060  24.323  39.539  1.00 41.99 ? 98  GLN B CD    1 
ATOM   4066 O  OE1   . GLN B 1 119 ? 30.219  24.526  39.894  1.00 46.91 ? 98  GLN B OE1   1 
ATOM   4067 N  NE2   . GLN B 1 119 ? 28.015  24.655  40.291  1.00 41.62 ? 98  GLN B NE2   1 
ATOM   4068 N  N     . ARG B 1 120 ? 29.593  27.506  35.450  1.00 29.14 ? 99  ARG B N     1 
ATOM   4069 C  CA    . ARG B 1 120 ? 30.208  28.100  34.230  1.00 33.25 ? 99  ARG B CA    1 
ATOM   4070 C  C     . ARG B 1 120 ? 31.643  27.598  34.119  1.00 34.28 ? 99  ARG B C     1 
ATOM   4071 O  O     . ARG B 1 120 ? 32.342  27.659  35.126  1.00 36.72 ? 99  ARG B O     1 
ATOM   4072 C  CB    . ARG B 1 120 ? 30.328  29.621  34.302  1.00 32.99 ? 99  ARG B CB    1 
ATOM   4073 C  CG    . ARG B 1 120 ? 29.045  30.388  34.041  1.00 41.29 ? 99  ARG B CG    1 
ATOM   4074 C  CD    . ARG B 1 120 ? 29.226  31.840  34.436  1.00 38.28 ? 99  ARG B CD    1 
ATOM   4075 N  NE    . ARG B 1 120 ? 30.227  32.459  33.581  1.00 35.55 ? 99  ARG B NE    1 
ATOM   4076 C  CZ    . ARG B 1 120 ? 30.093  33.612  32.954  1.00 34.50 ? 99  ARG B CZ    1 
ATOM   4077 N  NH1   . ARG B 1 120 ? 29.000  34.334  33.106  1.00 39.79 ? 99  ARG B NH1   1 
ATOM   4078 N  NH2   . ARG B 1 120 ? 31.054  34.056  32.170  1.00 36.84 ? 99  ARG B NH2   1 
ATOM   4079 N  N     . ALA B 1 121 ? 32.084  27.181  32.945  1.00 37.10 ? 100 ALA B N     1 
ATOM   4080 C  CA    . ALA B 1 121 ? 33.491  26.789  32.729  1.00 40.52 ? 100 ALA B CA    1 
ATOM   4081 C  C     . ALA B 1 121 ? 33.897  27.046  31.287  1.00 41.74 ? 100 ALA B C     1 
ATOM   4082 O  O     . ALA B 1 121 ? 33.109  26.765  30.376  1.00 35.00 ? 100 ALA B O     1 
ATOM   4083 C  CB    . ALA B 1 121 ? 33.662  25.337  33.076  1.00 42.19 ? 100 ALA B CB    1 
ATOM   4084 N  N     . PRO B 1 122 ? 35.166  27.485  31.064  1.00 44.89 ? 101 PRO B N     1 
ATOM   4085 C  CA    . PRO B 1 122 ? 35.705  27.703  29.719  1.00 42.56 ? 101 PRO B CA    1 
ATOM   4086 C  C     . PRO B 1 122 ? 35.509  26.479  28.810  1.00 39.13 ? 101 PRO B C     1 
ATOM   4087 O  O     . PRO B 1 122 ? 35.458  26.571  27.625  1.00 37.01 ? 101 PRO B O     1 
ATOM   4088 C  CB    . PRO B 1 122 ? 37.218  27.950  29.923  1.00 42.69 ? 101 PRO B CB    1 
ATOM   4089 C  CG    . PRO B 1 122 ? 37.396  28.244  31.401  1.00 48.20 ? 101 PRO B CG    1 
ATOM   4090 C  CD    . PRO B 1 122 ? 36.150  27.771  32.127  1.00 45.76 ? 101 PRO B CD    1 
ATOM   4091 N  N     . ASP B 1 123 ? 35.446  25.298  29.394  1.00 38.88 ? 102 ASP B N     1 
ATOM   4092 C  CA    . ASP B 1 123 ? 35.042  24.113  28.618  1.00 43.18 ? 102 ASP B CA    1 
ATOM   4093 C  C     . ASP B 1 123 ? 34.230  23.217  29.544  1.00 41.03 ? 102 ASP B C     1 
ATOM   4094 O  O     . ASP B 1 123 ? 34.380  23.297  30.774  1.00 33.24 ? 102 ASP B O     1 
ATOM   4095 C  CB    . ASP B 1 123 ? 36.229  23.397  27.972  1.00 50.55 ? 102 ASP B CB    1 
ATOM   4096 C  CG    . ASP B 1 123 ? 35.770  22.273  27.056  1.00 60.49 ? 102 ASP B CG    1 
ATOM   4097 O  OD1   . ASP B 1 123 ? 35.883  21.102  27.470  1.00 70.77 ? 102 ASP B OD1   1 
ATOM   4098 O  OD2   . ASP B 1 123 ? 35.256  22.573  25.953  1.00 67.58 ? 102 ASP B OD2   1 
ATOM   4099 N  N     . VAL B 1 124 ? 33.395  22.389  28.941  1.00 37.17 ? 103 VAL B N     1 
ATOM   4100 C  CA    . VAL B 1 124 ? 32.501  21.460  29.686  1.00 39.34 ? 103 VAL B CA    1 
ATOM   4101 C  C     . VAL B 1 124 ? 33.362  20.567  30.594  1.00 36.26 ? 103 VAL B C     1 
ATOM   4102 O  O     . VAL B 1 124 ? 32.975  20.325  31.742  1.00 32.81 ? 103 VAL B O     1 
ATOM   4103 C  CB    . VAL B 1 124 ? 31.658  20.659  28.670  1.00 38.58 ? 103 VAL B CB    1 
ATOM   4104 C  CG1   . VAL B 1 124 ? 31.053  19.417  29.288  1.00 39.92 ? 103 VAL B CG1   1 
ATOM   4105 C  CG2   . VAL B 1 124 ? 30.580  21.541  28.043  1.00 44.34 ? 103 VAL B CG2   1 
ATOM   4106 N  N     . ALA B 1 125 ? 34.492  20.070  30.096  1.00 34.85 ? 104 ALA B N     1 
ATOM   4107 C  CA    . ALA B 1 125 ? 35.376  19.139  30.827  1.00 36.53 ? 104 ALA B CA    1 
ATOM   4108 C  C     . ALA B 1 125 ? 35.763  19.727  32.183  1.00 33.04 ? 104 ALA B C     1 
ATOM   4109 O  O     . ALA B 1 125 ? 36.008  18.935  33.079  1.00 36.64 ? 104 ALA B O     1 
ATOM   4110 C  CB    . ALA B 1 125 ? 36.609  18.825  30.024  1.00 39.35 ? 104 ALA B CB    1 
ATOM   4111 N  N     . LEU B 1 126 ? 35.845  21.051  32.312  1.00 31.63 ? 105 LEU B N     1 
ATOM   4112 C  CA    . LEU B 1 126 ? 36.261  21.685  33.587  1.00 34.03 ? 105 LEU B CA    1 
ATOM   4113 C  C     . LEU B 1 126 ? 35.125  21.600  34.614  1.00 33.03 ? 105 LEU B C     1 
ATOM   4114 O  O     . LEU B 1 126 ? 35.380  21.929  35.757  1.00 32.34 ? 105 LEU B O     1 
ATOM   4115 C  CB    . LEU B 1 126 ? 36.691  23.128  33.327  1.00 38.21 ? 105 LEU B CB    1 
ATOM   4116 C  CG    . LEU B 1 126 ? 37.986  23.306  32.533  1.00 39.29 ? 105 LEU B CG    1 
ATOM   4117 C  CD1   . LEU B 1 126 ? 38.329  24.784  32.406  1.00 41.02 ? 105 LEU B CD1   1 
ATOM   4118 C  CD2   . LEU B 1 126 ? 39.140  22.551  33.176  1.00 40.40 ? 105 LEU B CD2   1 
ATOM   4119 N  N     . ALA B 1 127 ? 33.921  21.170  34.221  1.00 31.06 ? 106 ALA B N     1 
ATOM   4120 C  CA    . ALA B 1 127 ? 32.773  20.938  35.136  1.00 31.22 ? 106 ALA B CA    1 
ATOM   4121 C  C     . ALA B 1 127 ? 32.957  19.625  35.896  1.00 25.72 ? 106 ALA B C     1 
ATOM   4122 O  O     . ALA B 1 127 ? 32.245  19.381  36.869  1.00 30.08 ? 106 ALA B O     1 
ATOM   4123 C  CB    . ALA B 1 127 ? 31.485  20.913  34.353  1.00 31.17 ? 106 ALA B CB    1 
ATOM   4124 N  N     . PHE B 1 128 ? 33.799  18.739  35.393  1.00 27.50 ? 107 PHE B N     1 
ATOM   4125 C  CA    . PHE B 1 128 ? 34.059  17.404  35.985  1.00 26.40 ? 107 PHE B CA    1 
ATOM   4126 C  C     . PHE B 1 128 ? 35.208  17.487  37.004  1.00 24.64 ? 107 PHE B C     1 
ATOM   4127 O  O     . PHE B 1 128 ? 36.162  18.233  36.750  1.00 26.90 ? 107 PHE B O     1 
ATOM   4128 C  CB    . PHE B 1 128 ? 34.548  16.421  34.914  1.00 28.11 ? 107 PHE B CB    1 
ATOM   4129 C  CG    . PHE B 1 128 ? 33.565  15.665  34.057  1.00 35.13 ? 107 PHE B CG    1 
ATOM   4130 C  CD1   . PHE B 1 128 ? 33.952  15.266  32.776  1.00 37.11 ? 107 PHE B CD1   1 
ATOM   4131 C  CD2   . PHE B 1 128 ? 32.325  15.255  34.533  1.00 35.84 ? 107 PHE B CD2   1 
ATOM   4132 C  CE1   . PHE B 1 128 ? 33.110  14.493  31.984  1.00 40.25 ? 107 PHE B CE1   1 
ATOM   4133 C  CE2   . PHE B 1 128 ? 31.491  14.483  33.741  1.00 42.02 ? 107 PHE B CE2   1 
ATOM   4134 C  CZ    . PHE B 1 128 ? 31.871  14.125  32.461  1.00 40.95 ? 107 PHE B CZ    1 
ATOM   4135 N  N     . SER B 1 129 ? 35.195  16.622  38.010  1.00 25.39 ? 108 SER B N     1 
ATOM   4136 C  CA    . SER B 1 129 ? 36.379  16.321  38.857  1.00 28.27 ? 108 SER B CA    1 
ATOM   4137 C  C     . SER B 1 129 ? 37.475  15.657  38.001  1.00 30.88 ? 108 SER B C     1 
ATOM   4138 O  O     . SER B 1 129 ? 37.193  15.106  36.880  1.00 24.51 ? 108 SER B O     1 
ATOM   4139 C  CB    . SER B 1 129 ? 35.992  15.490  40.032  1.00 29.88 ? 108 SER B CB    1 
ATOM   4140 O  OG    . SER B 1 129 ? 35.701  14.148  39.638  1.00 28.80 ? 108 SER B OG    1 
ATOM   4141 N  N     . ASP B 1 130 ? 38.709  15.664  38.491  1.00 30.64 ? 109 ASP B N     1 
ATOM   4142 C  CA    . ASP B 1 130 ? 39.780  14.871  37.831  1.00 29.81 ? 109 ASP B CA    1 
ATOM   4143 C  C     . ASP B 1 130 ? 39.392  13.394  37.687  1.00 26.13 ? 109 ASP B C     1 
ATOM   4144 O  O     . ASP B 1 130 ? 39.621  12.860  36.619  1.00 29.60 ? 109 ASP B O     1 
ATOM   4145 C  CB    . ASP B 1 130 ? 41.119  15.064  38.531  1.00 32.97 ? 109 ASP B CB    1 
ATOM   4146 C  CG    . ASP B 1 130 ? 41.695  16.410  38.127  1.00 35.60 ? 109 ASP B CG    1 
ATOM   4147 O  OD1   . ASP B 1 130 ? 42.126  16.532  36.964  1.00 41.11 ? 109 ASP B OD1   1 
ATOM   4148 O  OD2   . ASP B 1 130 ? 41.678  17.337  38.973  1.00 40.69 ? 109 ASP B OD2   1 
ATOM   4149 N  N     . GLU B 1 131 ? 38.865  12.751  38.716  1.00 26.50 ? 110 GLU B N     1 
ATOM   4150 C  CA    . GLU B 1 131 ? 38.407  11.340  38.684  1.00 30.62 ? 110 GLU B CA    1 
ATOM   4151 C  C     . GLU B 1 131 ? 37.332  11.184  37.593  1.00 28.07 ? 110 GLU B C     1 
ATOM   4152 O  O     . GLU B 1 131 ? 37.384  10.213  36.828  1.00 24.19 ? 110 GLU B O     1 
ATOM   4153 C  CB    . GLU B 1 131 ? 37.831  10.981  40.046  1.00 31.33 ? 110 GLU B CB    1 
ATOM   4154 C  CG    . GLU B 1 131 ? 37.201  9.618   40.120  1.00 38.50 ? 110 GLU B CG    1 
ATOM   4155 C  CD    . GLU B 1 131 ? 36.708  9.316   41.529  1.00 46.29 ? 110 GLU B CD    1 
ATOM   4156 O  OE1   . GLU B 1 131 ? 35.652  9.853   41.912  1.00 54.80 ? 110 GLU B OE1   1 
ATOM   4157 O  OE2   . GLU B 1 131 ? 37.423  8.608   42.263  1.00 59.45 ? 110 GLU B OE2   1 
ATOM   4158 N  N     . GLU B 1 132 ? 36.407  12.131  37.520  1.00 28.34 ? 111 GLU B N     1 
ATOM   4159 C  CA    . GLU B 1 132 ? 35.276  12.080  36.546  1.00 28.08 ? 111 GLU B CA    1 
ATOM   4160 C  C     . GLU B 1 132 ? 35.815  12.223  35.116  1.00 26.73 ? 111 GLU B C     1 
ATOM   4161 O  O     . GLU B 1 132 ? 35.480  11.386  34.272  1.00 22.44 ? 111 GLU B O     1 
ATOM   4162 C  CB    . GLU B 1 132 ? 34.219  13.120  36.926  1.00 25.23 ? 111 GLU B CB    1 
ATOM   4163 C  CG    . GLU B 1 132 ? 33.445  12.762  38.184  1.00 26.31 ? 111 GLU B CG    1 
ATOM   4164 C  CD    . GLU B 1 132 ? 32.496  13.855  38.663  1.00 28.23 ? 111 GLU B CD    1 
ATOM   4165 O  OE1   . GLU B 1 132 ? 31.587  13.543  39.450  1.00 29.58 ? 111 GLU B OE1   1 
ATOM   4166 O  OE2   . GLU B 1 132 ? 32.642  15.001  38.221  1.00 27.27 ? 111 GLU B OE2   1 
ATOM   4167 N  N     . LEU B 1 133 ? 36.670  13.206  34.859  1.00 24.86 ? 112 LEU B N     1 
ATOM   4168 C  CA    . LEU B 1 133 ? 37.277  13.413  33.521  1.00 28.61 ? 112 LEU B CA    1 
ATOM   4169 C  C     . LEU B 1 133 ? 38.056  12.161  33.091  1.00 26.73 ? 112 LEU B C     1 
ATOM   4170 O  O     . LEU B 1 133 ? 37.858  11.686  31.935  1.00 25.02 ? 112 LEU B O     1 
ATOM   4171 C  CB    . LEU B 1 133 ? 38.158  14.666  33.553  1.00 29.75 ? 112 LEU B CB    1 
ATOM   4172 C  CG    . LEU B 1 133 ? 38.861  14.996  32.239  1.00 35.09 ? 112 LEU B CG    1 
ATOM   4173 C  CD1   . LEU B 1 133 ? 37.856  15.186  31.100  1.00 37.11 ? 112 LEU B CD1   1 
ATOM   4174 C  CD2   . LEU B 1 133 ? 39.722  16.242  32.386  1.00 36.76 ? 112 LEU B CD2   1 
ATOM   4175 N  N     . THR B 1 134 ? 38.851  11.571  33.988  1.00 29.31 ? 113 THR B N     1 
ATOM   4176 C  CA    . THR B 1 134 ? 39.637  10.337  33.690  1.00 28.67 ? 113 THR B CA    1 
ATOM   4177 C  C     . THR B 1 134 ? 38.697  9.197   33.290  1.00 26.97 ? 113 THR B C     1 
ATOM   4178 O  O     . THR B 1 134 ? 38.917  8.527   32.233  1.00 23.65 ? 113 THR B O     1 
ATOM   4179 C  CB    . THR B 1 134 ? 40.457  9.911   34.909  1.00 31.37 ? 113 THR B CB    1 
ATOM   4180 O  OG1   . THR B 1 134 ? 41.339  11.009  35.093  1.00 31.35 ? 113 THR B OG1   1 
ATOM   4181 C  CG2   . THR B 1 134 ? 41.240  8.630   34.722  1.00 36.17 ? 113 THR B CG2   1 
ATOM   4182 N  N     . ALA B 1 135 ? 37.667  8.978   34.102  1.00 25.54 ? 114 ALA B N     1 
ATOM   4183 C  CA    . ALA B 1 135 ? 36.631  7.957   33.837  1.00 24.45 ? 114 ALA B CA    1 
ATOM   4184 C  C     . ALA B 1 135 ? 36.005  8.201   32.450  1.00 22.20 ? 114 ALA B C     1 
ATOM   4185 O  O     . ALA B 1 135 ? 35.905  7.228   31.699  1.00 22.36 ? 114 ALA B O     1 
ATOM   4186 C  CB    . ALA B 1 135 ? 35.644  7.950   34.984  1.00 26.56 ? 114 ALA B CB    1 
ATOM   4187 N  N     . TYR B 1 136 ? 35.629  9.435   32.114  1.00 22.12 ? 115 TYR B N     1 
ATOM   4188 C  CA    . TYR B 1 136 ? 35.006  9.794   30.816  1.00 24.24 ? 115 TYR B CA    1 
ATOM   4189 C  C     . TYR B 1 136 ? 35.942  9.435   29.652  1.00 26.29 ? 115 TYR B C     1 
ATOM   4190 O  O     . TYR B 1 136 ? 35.523  8.703   28.719  1.00 23.33 ? 115 TYR B O     1 
ATOM   4191 C  CB    . TYR B 1 136 ? 34.620  11.260  30.743  1.00 25.11 ? 115 TYR B CB    1 
ATOM   4192 C  CG    . TYR B 1 136 ? 33.929  11.634  29.459  1.00 26.10 ? 115 TYR B CG    1 
ATOM   4193 C  CD1   . TYR B 1 136 ? 34.643  12.122  28.380  1.00 26.18 ? 115 TYR B CD1   1 
ATOM   4194 C  CD2   . TYR B 1 136 ? 32.555  11.499  29.328  1.00 26.52 ? 115 TYR B CD2   1 
ATOM   4195 C  CE1   . TYR B 1 136 ? 34.016  12.422  27.183  1.00 28.20 ? 115 TYR B CE1   1 
ATOM   4196 C  CE2   . TYR B 1 136 ? 31.916  11.813  28.144  1.00 27.21 ? 115 TYR B CE2   1 
ATOM   4197 C  CZ    . TYR B 1 136 ? 32.650  12.270  27.069  1.00 24.98 ? 115 TYR B CZ    1 
ATOM   4198 O  OH    . TYR B 1 136 ? 32.016  12.622  25.918  1.00 25.73 ? 115 TYR B OH    1 
ATOM   4199 N  N     . LEU B 1 137 ? 37.182  9.909   29.717  1.00 23.88 ? 116 LEU B N     1 
ATOM   4200 C  CA    . LEU B 1 137 ? 38.190  9.657   28.652  1.00 26.66 ? 116 LEU B CA    1 
ATOM   4201 C  C     . LEU B 1 137 ? 38.487  8.159   28.559  1.00 25.74 ? 116 LEU B C     1 
ATOM   4202 O  O     . LEU B 1 137 ? 38.652  7.664   27.409  1.00 23.82 ? 116 LEU B O     1 
ATOM   4203 C  CB    . LEU B 1 137 ? 39.445  10.491  28.936  1.00 28.02 ? 116 LEU B CB    1 
ATOM   4204 C  CG    . LEU B 1 137 ? 39.220  12.005  28.884  1.00 31.12 ? 116 LEU B CG    1 
ATOM   4205 C  CD1   . LEU B 1 137 ? 40.487  12.722  29.299  1.00 34.61 ? 116 LEU B CD1   1 
ATOM   4206 C  CD2   . LEU B 1 137 ? 38.746  12.490  27.524  1.00 32.83 ? 116 LEU B CD2   1 
ATOM   4207 N  N     . GLU B 1 138 ? 38.491  7.421   29.668  1.00 23.91 ? 117 GLU B N     1 
ATOM   4208 C  CA    . GLU B 1 138 ? 38.761  5.956   29.576  1.00 26.18 ? 117 GLU B CA    1 
ATOM   4209 C  C     . GLU B 1 138 ? 37.543  5.258   28.955  1.00 25.91 ? 117 GLU B C     1 
ATOM   4210 O  O     . GLU B 1 138 ? 37.731  4.286   28.198  1.00 22.97 ? 117 GLU B O     1 
ATOM   4211 C  CB    . GLU B 1 138 ? 39.156  5.349   30.920  1.00 30.47 ? 117 GLU B CB    1 
ATOM   4212 C  CG    . GLU B 1 138 ? 40.602  5.681   31.294  1.00 34.66 ? 117 GLU B CG    1 
ATOM   4213 C  CD    . GLU B 1 138 ? 40.992  5.307   32.717  1.00 44.61 ? 117 GLU B CD    1 
ATOM   4214 O  OE1   . GLU B 1 138 ? 42.150  5.577   33.081  1.00 53.02 ? 117 GLU B OE1   1 
ATOM   4215 O  OE2   . GLU B 1 138 ? 40.131  4.789   33.473  1.00 46.92 ? 117 GLU B OE2   1 
ATOM   4216 N  N     . LEU B 1 139 ? 36.339  5.727   29.257  1.00 23.01 ? 118 LEU B N     1 
ATOM   4217 C  CA    . LEU B 1 139 ? 35.099  5.138   28.678  1.00 23.73 ? 118 LEU B CA    1 
ATOM   4218 C  C     . LEU B 1 139 ? 35.113  5.398   27.164  1.00 20.84 ? 118 LEU B C     1 
ATOM   4219 O  O     . LEU B 1 139 ? 34.878  4.436   26.387  1.00 20.31 ? 118 LEU B O     1 
ATOM   4220 C  CB    . LEU B 1 139 ? 33.878  5.775   29.369  1.00 26.52 ? 118 LEU B CB    1 
ATOM   4221 C  CG    . LEU B 1 139 ? 32.497  5.322   28.891  1.00 26.72 ? 118 LEU B CG    1 
ATOM   4222 C  CD1   . LEU B 1 139 ? 32.184  3.913   29.346  1.00 30.18 ? 118 LEU B CD1   1 
ATOM   4223 C  CD2   . LEU B 1 139 ? 31.399  6.254   29.402  1.00 27.96 ? 118 LEU B CD2   1 
ATOM   4224 N  N     . ALA B 1 140 ? 35.423  6.621   26.717  1.00 21.64 ? 119 ALA B N     1 
ATOM   4225 C  CA    . ALA B 1 140 ? 35.455  6.953   25.271  1.00 22.79 ? 119 ALA B CA    1 
ATOM   4226 C  C     . ALA B 1 140 ? 36.542  6.110   24.572  1.00 20.57 ? 119 ALA B C     1 
ATOM   4227 O  O     . ALA B 1 140 ? 36.276  5.510   23.511  1.00 21.26 ? 119 ALA B O     1 
ATOM   4228 C  CB    . ALA B 1 140 ? 35.698  8.413   25.065  1.00 24.84 ? 119 ALA B CB    1 
ATOM   4229 N  N     . GLY B 1 141 ? 37.695  5.968   25.217  1.00 22.99 ? 120 GLY B N     1 
ATOM   4230 C  CA    . GLY B 1 141 ? 38.811  5.158   24.688  1.00 22.19 ? 120 GLY B CA    1 
ATOM   4231 C  C     . GLY B 1 141 ? 38.453  3.689   24.572  1.00 22.89 ? 120 GLY B C     1 
ATOM   4232 O  O     . GLY B 1 141 ? 38.818  3.093   23.540  1.00 20.63 ? 120 GLY B O     1 
ATOM   4233 N  N     . ALA B 1 142 ? 37.774  3.099   25.569  1.00 21.42 ? 121 ALA B N     1 
ATOM   4234 C  CA    . ALA B 1 142 ? 37.356  1.680   25.529  1.00 20.97 ? 121 ALA B CA    1 
ATOM   4235 C  C     . ALA B 1 142 ? 36.350  1.494   24.379  1.00 20.56 ? 121 ALA B C     1 
ATOM   4236 O  O     . ALA B 1 142 ? 36.399  0.425   23.673  1.00 19.21 ? 121 ALA B O     1 
ATOM   4237 C  CB    . ALA B 1 142 ? 36.771  1.235   26.858  1.00 21.85 ? 121 ALA B CB    1 
ATOM   4238 N  N     . LEU B 1 143 ? 35.452  2.463   24.168  1.00 18.67 ? 122 LEU B N     1 
ATOM   4239 C  CA    . LEU B 1 143 ? 34.456  2.371   23.064  1.00 19.17 ? 122 LEU B CA    1 
ATOM   4240 C  C     . LEU B 1 143 ? 35.166  2.454   21.706  1.00 18.78 ? 122 LEU B C     1 
ATOM   4241 O  O     . LEU B 1 143 ? 34.822  1.699   20.796  1.00 17.60 ? 122 LEU B O     1 
ATOM   4242 C  CB    . LEU B 1 143 ? 33.365  3.429   23.241  1.00 19.29 ? 122 LEU B CB    1 
ATOM   4243 C  CG    . LEU B 1 143 ? 32.250  3.379   22.199  1.00 21.87 ? 122 LEU B CG    1 
ATOM   4244 C  CD1   . LEU B 1 143 ? 31.593  2.017   22.121  1.00 22.69 ? 122 LEU B CD1   1 
ATOM   4245 C  CD2   . LEU B 1 143 ? 31.213  4.464   22.462  1.00 22.76 ? 122 LEU B CD2   1 
ATOM   4246 N  N     . GLU B 1 144 ? 36.184  3.286   21.594  1.00 17.16 ? 123 GLU B N     1 
ATOM   4247 C  CA    . GLU B 1 144 ? 36.959  3.454   20.341  1.00 20.77 ? 123 GLU B CA    1 
ATOM   4248 C  C     . GLU B 1 144 ? 37.686  2.153   20.013  1.00 19.74 ? 123 GLU B C     1 
ATOM   4249 O  O     . GLU B 1 144 ? 37.782  1.819   18.792  1.00 21.50 ? 123 GLU B O     1 
ATOM   4250 C  CB    . GLU B 1 144 ? 37.928  4.636   20.475  1.00 19.89 ? 123 GLU B CB    1 
ATOM   4251 C  CG    . GLU B 1 144 ? 37.189  5.943   20.292  1.00 19.52 ? 123 GLU B CG    1 
ATOM   4252 C  CD    . GLU B 1 144 ? 37.991  7.196   20.544  1.00 24.31 ? 123 GLU B CD    1 
ATOM   4253 O  OE1   . GLU B 1 144 ? 37.488  8.280   20.221  1.00 23.94 ? 123 GLU B OE1   1 
ATOM   4254 O  OE2   . GLU B 1 144 ? 39.094  7.059   21.083  1.00 24.20 ? 123 GLU B OE2   1 
ATOM   4255 N  N     . ALA B 1 145 ? 38.188  1.460   21.037  1.00 19.96 ? 124 ALA B N     1 
ATOM   4256 C  CA    . ALA B 1 145 ? 38.934  0.199   20.834  1.00 20.92 ? 124 ALA B CA    1 
ATOM   4257 C  C     . ALA B 1 145 ? 37.995  -0.852  20.244  1.00 20.76 ? 124 ALA B C     1 
ATOM   4258 O  O     . ALA B 1 145 ? 38.423  -1.586  19.341  1.00 19.47 ? 124 ALA B O     1 
ATOM   4259 C  CB    . ALA B 1 145 ? 39.582  -0.283  22.107  1.00 21.84 ? 124 ALA B CB    1 
ATOM   4260 N  N     . ILE B 1 146 ? 36.769  -0.968  20.784  1.00 19.13 ? 125 ILE B N     1 
ATOM   4261 C  CA    . ILE B 1 146 ? 35.720  -1.849  20.205  1.00 19.26 ? 125 ILE B CA    1 
ATOM   4262 C  C     . ILE B 1 146 ? 35.394  -1.371  18.777  1.00 17.68 ? 125 ILE B C     1 
ATOM   4263 O  O     . ILE B 1 146 ? 35.357  -2.212  17.844  1.00 18.33 ? 125 ILE B O     1 
ATOM   4264 C  CB    . ILE B 1 146 ? 34.484  -1.918  21.151  1.00 20.70 ? 125 ILE B CB    1 
ATOM   4265 C  CG1   . ILE B 1 146 ? 34.837  -2.659  22.445  1.00 22.23 ? 125 ILE B CG1   1 
ATOM   4266 C  CG2   . ILE B 1 146 ? 33.309  -2.606  20.507  1.00 20.21 ? 125 ILE B CG2   1 
ATOM   4267 C  CD1   . ILE B 1 146 ? 33.853  -2.379  23.566  1.00 23.84 ? 125 ILE B CD1   1 
ATOM   4268 N  N     . ALA B 1 147 ? 35.114  -0.077  18.610  1.00 17.97 ? 126 ALA B N     1 
ATOM   4269 C  CA    . ALA B 1 147 ? 34.702  0.515   17.315  1.00 17.58 ? 126 ALA B CA    1 
ATOM   4270 C  C     . ALA B 1 147 ? 35.709  0.149   16.211  1.00 18.32 ? 126 ALA B C     1 
ATOM   4271 O  O     . ALA B 1 147 ? 35.282  -0.233  15.139  1.00 15.76 ? 126 ALA B O     1 
ATOM   4272 C  CB    . ALA B 1 147 ? 34.486  1.981   17.442  1.00 18.05 ? 126 ALA B CB    1 
ATOM   4273 N  N     . GLU B 1 148 ? 37.008  0.238   16.481  1.00 19.16 ? 127 GLU B N     1 
ATOM   4274 C  CA    . GLU B 1 148 ? 38.047  -0.004  15.443  1.00 18.16 ? 127 GLU B CA    1 
ATOM   4275 C  C     . GLU B 1 148 ? 37.943  -1.450  14.913  1.00 18.83 ? 127 GLU B C     1 
ATOM   4276 O  O     . GLU B 1 148 ? 38.241  -1.693  13.711  1.00 18.93 ? 127 GLU B O     1 
ATOM   4277 C  CB    . GLU B 1 148 ? 39.429  0.308   16.002  1.00 18.76 ? 127 GLU B CB    1 
ATOM   4278 C  CG    . GLU B 1 148 ? 40.492  0.498   14.901  1.00 18.49 ? 127 GLU B CG    1 
ATOM   4279 C  CD    . GLU B 1 148 ? 40.212  1.671   13.963  1.00 18.91 ? 127 GLU B CD    1 
ATOM   4280 O  OE1   . GLU B 1 148 ? 40.410  1.549   12.754  1.00 19.48 ? 127 GLU B OE1   1 
ATOM   4281 O  OE2   . GLU B 1 148 ? 39.823  2.763   14.480  1.00 21.96 ? 127 GLU B OE2   1 
ATOM   4282 N  N     . LYS B 1 149 ? 37.504  -2.388  15.758  1.00 18.76 ? 128 LYS B N     1 
ATOM   4283 C  CA    . LYS B 1 149 ? 37.379  -3.813  15.351  1.00 19.41 ? 128 LYS B CA    1 
ATOM   4284 C  C     . LYS B 1 149 ? 36.112  -4.072  14.528  1.00 20.93 ? 128 LYS B C     1 
ATOM   4285 O  O     . LYS B 1 149 ? 35.989  -5.204  13.983  1.00 19.12 ? 128 LYS B O     1 
ATOM   4286 C  CB    . LYS B 1 149 ? 37.447  -4.713  16.583  1.00 19.56 ? 128 LYS B CB    1 
ATOM   4287 C  CG    . LYS B 1 149 ? 38.806  -4.715  17.270  1.00 20.85 ? 128 LYS B CG    1 
ATOM   4288 C  CD    . LYS B 1 149 ? 38.748  -5.407  18.597  1.00 24.08 ? 128 LYS B CD    1 
ATOM   4289 C  CE    . LYS B 1 149 ? 40.096  -5.481  19.285  1.00 28.52 ? 128 LYS B CE    1 
ATOM   4290 N  NZ    . LYS B 1 149 ? 40.109  -6.597  20.251  1.00 30.72 ? 128 LYS B NZ    1 
ATOM   4291 N  N     . VAL B 1 150 ? 35.226  -3.089  14.379  1.00 18.32 ? 129 VAL B N     1 
ATOM   4292 C  CA    . VAL B 1 150 ? 33.972  -3.272  13.613  1.00 17.87 ? 129 VAL B CA    1 
ATOM   4293 C  C     . VAL B 1 150 ? 34.232  -2.876  12.168  1.00 18.52 ? 129 VAL B C     1 
ATOM   4294 O  O     . VAL B 1 150 ? 34.410  -1.702  11.861  1.00 20.20 ? 129 VAL B O     1 
ATOM   4295 C  CB    . VAL B 1 150 ? 32.811  -2.446  14.211  1.00 18.55 ? 129 VAL B CB    1 
ATOM   4296 C  CG1   . VAL B 1 150 ? 31.534  -2.729  13.451  1.00 18.62 ? 129 VAL B CG1   1 
ATOM   4297 C  CG2   . VAL B 1 150 ? 32.593  -2.791  15.675  1.00 18.45 ? 129 VAL B CG2   1 
ATOM   4298 N  N     . PRO B 1 151 ? 34.192  -3.819  11.208  1.00 18.15 ? 130 PRO B N     1 
ATOM   4299 C  CA    . PRO B 1 151 ? 34.420  -3.461  9.802   1.00 18.66 ? 130 PRO B CA    1 
ATOM   4300 C  C     . PRO B 1 151 ? 33.371  -2.457  9.295   1.00 18.02 ? 130 PRO B C     1 
ATOM   4301 O  O     . PRO B 1 151 ? 32.177  -2.653  9.552   1.00 18.69 ? 130 PRO B O     1 
ATOM   4302 C  CB    . PRO B 1 151 ? 34.313  -4.809  9.067   1.00 19.59 ? 130 PRO B CB    1 
ATOM   4303 C  CG    . PRO B 1 151 ? 34.669  -5.823  10.153  1.00 19.09 ? 130 PRO B CG    1 
ATOM   4304 C  CD    . PRO B 1 151 ? 34.046  -5.263  11.420  1.00 18.40 ? 130 PRO B CD    1 
ATOM   4305 N  N     . LEU B 1 152 ? 33.807  -1.385  8.639   1.00 17.45 ? 131 LEU B N     1 
ATOM   4306 C  CA    . LEU B 1 152 ? 32.828  -0.335  8.266   1.00 17.25 ? 131 LEU B CA    1 
ATOM   4307 C  C     . LEU B 1 152 ? 31.859  -0.860  7.207   1.00 18.70 ? 131 LEU B C     1 
ATOM   4308 O  O     . LEU B 1 152 ? 30.750  -0.299  7.108   1.00 19.10 ? 131 LEU B O     1 
ATOM   4309 C  CB    . LEU B 1 152 ? 33.555  0.888   7.719   1.00 17.68 ? 131 LEU B CB    1 
ATOM   4310 C  CG    . LEU B 1 152 ? 34.429  1.655   8.700   1.00 18.38 ? 131 LEU B CG    1 
ATOM   4311 C  CD1   . LEU B 1 152 ? 35.086  2.821   7.994   1.00 22.66 ? 131 LEU B CD1   1 
ATOM   4312 C  CD2   . LEU B 1 152 ? 33.665  2.098   9.922   1.00 19.97 ? 131 LEU B CD2   1 
ATOM   4313 N  N     . ASP B 1 153 ? 32.284  -1.808  6.373   1.00 18.95 ? 132 ASP B N     1 
ATOM   4314 C  CA    . ASP B 1 153 ? 31.472  -2.335  5.252   1.00 22.52 ? 132 ASP B CA    1 
ATOM   4315 C  C     . ASP B 1 153 ? 30.582  -3.482  5.731   1.00 23.08 ? 132 ASP B C     1 
ATOM   4316 O  O     . ASP B 1 153 ? 29.682  -3.882  4.976   1.00 22.27 ? 132 ASP B O     1 
ATOM   4317 C  CB    . ASP B 1 153 ? 32.353  -2.791  4.077   1.00 24.90 ? 132 ASP B CB    1 
ATOM   4318 C  CG    . ASP B 1 153 ? 33.384  -3.856  4.385   1.00 27.60 ? 132 ASP B CG    1 
ATOM   4319 O  OD1   . ASP B 1 153 ? 33.768  -4.026  5.571   1.00 27.01 ? 132 ASP B OD1   1 
ATOM   4320 O  OD2   . ASP B 1 153 ? 33.832  -4.477  3.411   1.00 32.45 ? 132 ASP B OD2   1 
ATOM   4321 N  N     . ALA B 1 154 ? 30.856  -4.042  6.902   1.00 21.57 ? 133 ALA B N     1 
ATOM   4322 C  CA    . ALA B 1 154 ? 30.200  -5.299  7.351   1.00 21.71 ? 133 ALA B CA    1 
ATOM   4323 C  C     . ALA B 1 154 ? 30.306  -5.452  8.863   1.00 19.87 ? 133 ALA B C     1 
ATOM   4324 O  O     . ALA B 1 154 ? 31.058  -6.284  9.370   1.00 20.84 ? 133 ALA B O     1 
ATOM   4325 C  CB    . ALA B 1 154 ? 30.828  -6.471  6.609   1.00 22.11 ? 133 ALA B CB    1 
ATOM   4326 N  N     . PRO B 1 155 ? 29.516  -4.683  9.643   1.00 18.94 ? 134 PRO B N     1 
ATOM   4327 C  CA    . PRO B 1 155 ? 29.629  -4.731  11.085  1.00 20.85 ? 134 PRO B CA    1 
ATOM   4328 C  C     . PRO B 1 155 ? 29.401  -6.140  11.634  1.00 18.34 ? 134 PRO B C     1 
ATOM   4329 O  O     . PRO B 1 155 ? 29.939  -6.466  12.700  1.00 20.76 ? 134 PRO B O     1 
ATOM   4330 C  CB    . PRO B 1 155 ? 28.574  -3.763  11.626  1.00 20.19 ? 134 PRO B CB    1 
ATOM   4331 C  CG    . PRO B 1 155 ? 27.930  -3.097  10.417  1.00 22.06 ? 134 PRO B CG    1 
ATOM   4332 C  CD    . PRO B 1 155 ? 28.627  -3.604  9.169   1.00 21.26 ? 134 PRO B CD    1 
ATOM   4333 N  N     . TRP B 1 156 ? 28.600  -6.922  10.908  1.00 19.95 ? 135 TRP B N     1 
ATOM   4334 C  CA    . TRP B 1 156 ? 28.266  -8.322  11.288  1.00 20.91 ? 135 TRP B CA    1 
ATOM   4335 C  C     . TRP B 1 156 ? 29.510  -9.216  11.209  1.00 22.38 ? 135 TRP B C     1 
ATOM   4336 O  O     . TRP B 1 156 ? 29.436  -10.348 11.763  1.00 21.38 ? 135 TRP B O     1 
ATOM   4337 C  CB    . TRP B 1 156 ? 27.106  -8.907  10.445  1.00 20.62 ? 135 TRP B CB    1 
ATOM   4338 C  CG    . TRP B 1 156 ? 27.354  -8.882  8.972   1.00 19.25 ? 135 TRP B CG    1 
ATOM   4339 C  CD1   . TRP B 1 156 ? 27.966  -9.843  8.224   1.00 21.07 ? 135 TRP B CD1   1 
ATOM   4340 C  CD2   . TRP B 1 156 ? 27.070  -7.790  8.076   1.00 20.70 ? 135 TRP B CD2   1 
ATOM   4341 N  NE1   . TRP B 1 156 ? 28.036  -9.444  6.925   1.00 21.56 ? 135 TRP B NE1   1 
ATOM   4342 C  CE2   . TRP B 1 156 ? 27.513  -8.192  6.798   1.00 20.61 ? 135 TRP B CE2   1 
ATOM   4343 C  CE3   . TRP B 1 156 ? 26.451  -6.541  8.222   1.00 20.87 ? 135 TRP B CE3   1 
ATOM   4344 C  CZ2   . TRP B 1 156 ? 27.390  -7.374  5.679   1.00 21.60 ? 135 TRP B CZ2   1 
ATOM   4345 C  CZ3   . TRP B 1 156 ? 26.334  -5.726  7.117   1.00 21.20 ? 135 TRP B CZ3   1 
ATOM   4346 C  CH2   . TRP B 1 156 ? 26.765  -6.153  5.867   1.00 22.99 ? 135 TRP B CH2   1 
ATOM   4347 N  N     . LEU B 1 157 ? 30.621  -8.766  10.606  1.00 21.06 ? 136 LEU B N     1 
ATOM   4348 C  CA    . LEU B 1 157 ? 31.847  -9.602  10.521  1.00 22.71 ? 136 LEU B CA    1 
ATOM   4349 C  C     . LEU B 1 157 ? 32.827  -9.220  11.628  1.00 21.66 ? 136 LEU B C     1 
ATOM   4350 O  O     . LEU B 1 157 ? 33.936  -9.755  11.649  1.00 21.36 ? 136 LEU B O     1 
ATOM   4351 C  CB    . LEU B 1 157 ? 32.457  -9.487  9.114   1.00 23.00 ? 136 LEU B CB    1 
ATOM   4352 C  CG    . LEU B 1 157 ? 31.589  -10.027 7.969   1.00 25.81 ? 136 LEU B CG    1 
ATOM   4353 C  CD1   . LEU B 1 157 ? 32.344  -9.948  6.645   1.00 29.47 ? 136 LEU B CD1   1 
ATOM   4354 C  CD2   . LEU B 1 157 ? 31.135  -11.466 8.215   1.00 27.88 ? 136 LEU B CD2   1 
ATOM   4355 N  N     . ALA B 1 158 ? 32.446  -8.346  12.561  1.00 22.21 ? 137 ALA B N     1 
ATOM   4356 C  CA    . ALA B 1 158 ? 33.305  -8.060  13.734  1.00 21.21 ? 137 ALA B CA    1 
ATOM   4357 C  C     . ALA B 1 158 ? 33.581  -9.391  14.435  1.00 23.75 ? 137 ALA B C     1 
ATOM   4358 O  O     . ALA B 1 158 ? 32.675  -10.234 14.527  1.00 20.35 ? 137 ALA B O     1 
ATOM   4359 C  CB    . ALA B 1 158 ? 32.646  -7.045  14.645  1.00 22.24 ? 137 ALA B CB    1 
ATOM   4360 N  N     . PRO B 1 159 ? 34.789  -9.608  15.003  1.00 28.62 ? 138 PRO B N     1 
ATOM   4361 C  CA    . PRO B 1 159 ? 35.137  -10.902 15.605  1.00 30.84 ? 138 PRO B CA    1 
ATOM   4362 C  C     . PRO B 1 159 ? 34.192  -11.294 16.756  1.00 30.06 ? 138 PRO B C     1 
ATOM   4363 O  O     . PRO B 1 159 ? 33.804  -12.455 16.859  1.00 30.35 ? 138 PRO B O     1 
ATOM   4364 C  CB    . PRO B 1 159 ? 36.585  -10.665 16.084  1.00 34.14 ? 138 PRO B CB    1 
ATOM   4365 C  CG    . PRO B 1 159 ? 36.637  -9.156  16.358  1.00 37.72 ? 138 PRO B CG    1 
ATOM   4366 C  CD    . PRO B 1 159 ? 35.826  -8.576  15.213  1.00 33.61 ? 138 PRO B CD    1 
ATOM   4367 N  N     . GLU B 1 160 ? 33.747  -10.314 17.535  1.00 25.28 ? 139 GLU B N     1 
ATOM   4368 C  CA    . GLU B 1 160 ? 32.780  -10.492 18.653  1.00 27.35 ? 139 GLU B CA    1 
ATOM   4369 C  C     . GLU B 1 160 ? 31.386  -9.951  18.288  1.00 23.55 ? 139 GLU B C     1 
ATOM   4370 O  O     . GLU B 1 160 ? 30.647  -9.502  19.228  1.00 21.12 ? 139 GLU B O     1 
ATOM   4371 C  CB    . GLU B 1 160 ? 33.308  -9.761  19.890  1.00 30.06 ? 139 GLU B CB    1 
ATOM   4372 C  CG    . GLU B 1 160 ? 34.624  -10.304 20.406  1.00 39.44 ? 139 GLU B CG    1 
ATOM   4373 C  CD    . GLU B 1 160 ? 34.584  -11.748 20.864  1.00 49.16 ? 139 GLU B CD    1 
ATOM   4374 O  OE1   . GLU B 1 160 ? 35.677  -12.311 21.067  1.00 56.59 ? 139 GLU B OE1   1 
ATOM   4375 O  OE2   . GLU B 1 160 ? 33.469  -12.323 21.005  1.00 53.78 ? 139 GLU B OE2   1 
ATOM   4376 N  N     . ALA B 1 161 ? 31.003  -9.997  17.009  1.00 22.62 ? 140 ALA B N     1 
ATOM   4377 C  CA    . ALA B 1 161 ? 29.737  -9.386  16.527  1.00 20.96 ? 140 ALA B CA    1 
ATOM   4378 C  C     . ALA B 1 161 ? 28.565  -9.904  17.349  1.00 21.04 ? 140 ALA B C     1 
ATOM   4379 O  O     . ALA B 1 161 ? 27.724  -9.076  17.761  1.00 20.46 ? 140 ALA B O     1 
ATOM   4380 C  CB    . ALA B 1 161 ? 29.501  -9.654  15.069  1.00 20.70 ? 140 ALA B CB    1 
ATOM   4381 N  N     . ALA B 1 162 ? 28.481  -11.218 17.531  1.00 23.24 ? 141 ALA B N     1 
ATOM   4382 C  CA    . ALA B 1 162 ? 27.326  -11.863 18.206  1.00 24.99 ? 141 ALA B CA    1 
ATOM   4383 C  C     . ALA B 1 162 ? 27.183  -11.258 19.614  1.00 24.59 ? 141 ALA B C     1 
ATOM   4384 O  O     . ALA B 1 162 ? 26.059  -10.869 19.982  1.00 24.38 ? 141 ALA B O     1 
ATOM   4385 C  CB    . ALA B 1 162 ? 27.481  -13.366 18.241  1.00 27.15 ? 141 ALA B CB    1 
ATOM   4386 N  N     . ALA B 1 163 ? 28.274  -11.146 20.372  1.00 23.05 ? 142 ALA B N     1 
ATOM   4387 C  CA    . ALA B 1 163 ? 28.243  -10.637 21.763  1.00 24.39 ? 142 ALA B CA    1 
ATOM   4388 C  C     . ALA B 1 163 ? 27.918  -9.149  21.748  1.00 21.57 ? 142 ALA B C     1 
ATOM   4389 O  O     . ALA B 1 163 ? 27.043  -8.707  22.519  1.00 21.63 ? 142 ALA B O     1 
ATOM   4390 C  CB    . ALA B 1 163 ? 29.554  -10.904 22.481  1.00 26.04 ? 142 ALA B CB    1 
ATOM   4391 N  N     . TRP B 1 164 ? 28.575  -8.378  20.893  1.00 19.98 ? 143 TRP B N     1 
ATOM   4392 C  CA    . TRP B 1 164 ? 28.333  -6.921  20.852  1.00 19.88 ? 143 TRP B CA    1 
ATOM   4393 C  C     . TRP B 1 164 ? 26.927  -6.601  20.331  1.00 18.79 ? 143 TRP B C     1 
ATOM   4394 O  O     . TRP B 1 164 ? 26.364  -5.559  20.737  1.00 19.63 ? 143 TRP B O     1 
ATOM   4395 C  CB    . TRP B 1 164 ? 29.425  -6.238  20.031  1.00 19.89 ? 143 TRP B CB    1 
ATOM   4396 C  CG    . TRP B 1 164 ? 30.793  -6.400  20.604  1.00 21.62 ? 143 TRP B CG    1 
ATOM   4397 C  CD1   . TRP B 1 164 ? 31.137  -6.805  21.862  1.00 24.64 ? 143 TRP B CD1   1 
ATOM   4398 C  CD2   . TRP B 1 164 ? 32.027  -6.130  19.911  1.00 21.09 ? 143 TRP B CD2   1 
ATOM   4399 N  NE1   . TRP B 1 164 ? 32.502  -6.784  22.009  1.00 24.39 ? 143 TRP B NE1   1 
ATOM   4400 C  CE2   . TRP B 1 164 ? 33.075  -6.387  20.829  1.00 23.15 ? 143 TRP B CE2   1 
ATOM   4401 C  CE3   . TRP B 1 164 ? 32.339  -5.732  18.607  1.00 21.88 ? 143 TRP B CE3   1 
ATOM   4402 C  CZ2   . TRP B 1 164 ? 34.416  -6.250  20.473  1.00 24.46 ? 143 TRP B CZ2   1 
ATOM   4403 C  CZ3   . TRP B 1 164 ? 33.668  -5.586  18.259  1.00 23.66 ? 143 TRP B CZ3   1 
ATOM   4404 C  CH2   . TRP B 1 164 ? 34.687  -5.848  19.180  1.00 23.58 ? 143 TRP B CH2   1 
ATOM   4405 N  N     . ASP B 1 165 ? 26.372  -7.428  19.467  1.00 17.29 ? 144 ASP B N     1 
ATOM   4406 C  CA    . ASP B 1 165 ? 25.019  -7.192  18.910  1.00 20.49 ? 144 ASP B CA    1 
ATOM   4407 C  C     . ASP B 1 165 ? 23.952  -7.639  19.941  1.00 22.68 ? 144 ASP B C     1 
ATOM   4408 O  O     . ASP B 1 165 ? 22.798  -7.250  19.804  1.00 25.89 ? 144 ASP B O     1 
ATOM   4409 C  CB    . ASP B 1 165 ? 24.774  -7.947  17.607  1.00 19.10 ? 144 ASP B CB    1 
ATOM   4410 C  CG    . ASP B 1 165 ? 23.685  -7.266  16.784  1.00 20.03 ? 144 ASP B CG    1 
ATOM   4411 O  OD1   . ASP B 1 165 ? 23.511  -6.064  16.959  1.00 25.26 ? 144 ASP B OD1   1 
ATOM   4412 O  OD2   . ASP B 1 165 ? 23.037  -7.933  16.017  1.00 21.77 ? 144 ASP B OD2   1 
ATOM   4413 N  N     . ALA B 1 166 ? 24.316  -8.449  20.921  1.00 22.78 ? 145 ALA B N     1 
ATOM   4414 C  CA    . ALA B 1 166 ? 23.379  -8.915  21.974  1.00 25.70 ? 145 ALA B CA    1 
ATOM   4415 C  C     . ALA B 1 166 ? 23.306  -7.935  23.156  1.00 27.31 ? 145 ALA B C     1 
ATOM   4416 O  O     . ALA B 1 166 ? 22.533  -8.221  24.089  1.00 27.60 ? 145 ALA B O     1 
ATOM   4417 C  CB    . ALA B 1 166 ? 23.786  -10.284 22.445  1.00 25.51 ? 145 ALA B CB    1 
ATOM   4418 N  N     . THR B 1 167 ? 24.147  -6.907  23.205  1.00 19.46 ? 146 THR B N     1 
ATOM   4419 C  CA    . THR B 1 167 ? 24.284  -5.986  24.369  1.00 22.73 ? 146 THR B CA    1 
ATOM   4420 C  C     . THR B 1 167 ? 23.753  -4.624  23.962  1.00 21.62 ? 146 THR B C     1 
ATOM   4421 O  O     . THR B 1 167 ? 24.131  -4.182  22.870  1.00 21.20 ? 146 THR B O     1 
ATOM   4422 C  CB    . THR B 1 167 ? 25.760  -5.851  24.782  1.00 24.34 ? 146 THR B CB    1 
ATOM   4423 O  OG1   . THR B 1 167 ? 26.233  -7.195  24.852  1.00 30.19 ? 146 THR B OG1   1 
ATOM   4424 C  CG2   . THR B 1 167 ? 25.970  -5.204  26.129  1.00 26.96 ? 146 THR B CG2   1 
ATOM   4425 N  N     . THR B 1 168 ? 23.024  -3.918  24.827  1.00 22.50 ? 147 THR B N     1 
ATOM   4426 C  CA    . THR B 1 168 ? 22.756  -2.476  24.594  1.00 20.11 ? 147 THR B CA    1 
ATOM   4427 C  C     . THR B 1 168 ? 24.001  -1.645  24.935  1.00 19.28 ? 147 THR B C     1 
ATOM   4428 O  O     . THR B 1 168 ? 24.830  -2.040  25.807  1.00 18.94 ? 147 THR B O     1 
ATOM   4429 C  CB    . THR B 1 168 ? 21.577  -1.904  25.399  1.00 21.89 ? 147 THR B CB    1 
ATOM   4430 O  OG1   . THR B 1 168 ? 21.894  -1.978  26.793  1.00 19.71 ? 147 THR B OG1   1 
ATOM   4431 C  CG2   . THR B 1 168 ? 20.277  -2.641  25.120  1.00 23.90 ? 147 THR B CG2   1 
ATOM   4432 N  N     . LEU B 1 169 ? 24.096  -0.453  24.371  1.00 16.92 ? 148 LEU B N     1 
ATOM   4433 C  CA    . LEU B 1 169 ? 25.175  0.467   24.783  1.00 18.06 ? 148 LEU B CA    1 
ATOM   4434 C  C     . LEU B 1 169 ? 25.023  0.779   26.279  1.00 20.18 ? 148 LEU B C     1 
ATOM   4435 O  O     . LEU B 1 169 ? 26.076  0.868   26.985  1.00 21.22 ? 148 LEU B O     1 
ATOM   4436 C  CB    . LEU B 1 169 ? 25.143  1.709   23.894  1.00 18.53 ? 148 LEU B CB    1 
ATOM   4437 C  CG    . LEU B 1 169 ? 26.206  2.758   24.216  1.00 19.32 ? 148 LEU B CG    1 
ATOM   4438 C  CD1   . LEU B 1 169 ? 27.596  2.213   23.923  1.00 19.97 ? 148 LEU B CD1   1 
ATOM   4439 C  CD2   . LEU B 1 169 ? 25.944  4.040   23.428  1.00 17.33 ? 148 LEU B CD2   1 
ATOM   4440 N  N     . ARG B 1 170 ? 23.793  0.898   26.786  1.00 20.09 ? 149 ARG B N     1 
ATOM   4441 C  CA    . ARG B 1 170 ? 23.535  1.204   28.209  1.00 20.81 ? 149 ARG B CA    1 
ATOM   4442 C  C     . ARG B 1 170 ? 24.161  0.101   29.079  1.00 20.05 ? 149 ARG B C     1 
ATOM   4443 O  O     . ARG B 1 170 ? 24.902  0.434   30.023  1.00 22.25 ? 149 ARG B O     1 
ATOM   4444 C  CB    . ARG B 1 170 ? 22.055  1.303   28.575  1.00 22.05 ? 149 ARG B CB    1 
ATOM   4445 C  CG    . ARG B 1 170 ? 21.900  1.775   30.014  1.00 24.33 ? 149 ARG B CG    1 
ATOM   4446 C  CD    . ARG B 1 170 ? 20.588  2.437   30.262  1.00 27.03 ? 149 ARG B CD    1 
ATOM   4447 N  NE    . ARG B 1 170 ? 20.381  3.630   29.437  1.00 26.75 ? 149 ARG B NE    1 
ATOM   4448 C  CZ    . ARG B 1 170 ? 19.338  4.429   29.547  1.00 25.77 ? 149 ARG B CZ    1 
ATOM   4449 N  NH1   . ARG B 1 170 ? 18.386  4.127   30.403  1.00 25.37 ? 149 ARG B NH1   1 
ATOM   4450 N  NH2   . ARG B 1 170 ? 19.219  5.503   28.787  1.00 27.11 ? 149 ARG B NH2   1 
ATOM   4451 N  N     . GLU B 1 171 ? 23.898  -1.155  28.746  1.00 21.30 ? 150 GLU B N     1 
ATOM   4452 C  CA    . GLU B 1 171 ? 24.412  -2.316  29.516  1.00 24.63 ? 150 GLU B CA    1 
ATOM   4453 C  C     . GLU B 1 171 ? 25.950  -2.253  29.544  1.00 23.72 ? 150 GLU B C     1 
ATOM   4454 O  O     . GLU B 1 171 ? 26.594  -2.478  30.636  1.00 22.06 ? 150 GLU B O     1 
ATOM   4455 C  CB    . GLU B 1 171 ? 23.987  -3.664  28.924  1.00 25.71 ? 150 GLU B CB    1 
ATOM   4456 C  CG    . GLU B 1 171 ? 24.424  -4.818  29.831  1.00 28.90 ? 150 GLU B CG    1 
ATOM   4457 C  CD    . GLU B 1 171 ? 24.261  -6.283  29.449  1.00 36.66 ? 150 GLU B CD    1 
ATOM   4458 O  OE1   . GLU B 1 171 ? 23.632  -6.602  28.433  1.00 31.19 ? 150 GLU B OE1   1 
ATOM   4459 O  OE2   . GLU B 1 171 ? 24.785  -7.131  30.241  1.00 47.16 ? 150 GLU B OE2   1 
ATOM   4460 N  N     . TRP B 1 172 ? 26.552  -1.955  28.400  1.00 21.42 ? 151 TRP B N     1 
ATOM   4461 C  CA    . TRP B 1 172 ? 28.026  -1.839  28.270  1.00 21.79 ? 151 TRP B CA    1 
ATOM   4462 C  C     . TRP B 1 172 ? 28.556  -0.724  29.188  1.00 22.85 ? 151 TRP B C     1 
ATOM   4463 O  O     . TRP B 1 172 ? 29.539  -0.986  29.916  1.00 23.45 ? 151 TRP B O     1 
ATOM   4464 C  CB    . TRP B 1 172 ? 28.442  -1.631  26.810  1.00 21.34 ? 151 TRP B CB    1 
ATOM   4465 C  CG    . TRP B 1 172 ? 29.917  -1.500  26.701  1.00 20.80 ? 151 TRP B CG    1 
ATOM   4466 C  CD1   . TRP B 1 172 ? 30.836  -2.503  26.695  1.00 25.42 ? 151 TRP B CD1   1 
ATOM   4467 C  CD2   . TRP B 1 172 ? 30.656  -0.278  26.603  1.00 22.38 ? 151 TRP B CD2   1 
ATOM   4468 N  NE1   . TRP B 1 172 ? 32.105  -1.982  26.636  1.00 24.12 ? 151 TRP B NE1   1 
ATOM   4469 C  CE2   . TRP B 1 172 ? 32.029  -0.625  26.584  1.00 22.91 ? 151 TRP B CE2   1 
ATOM   4470 C  CE3   . TRP B 1 172 ? 30.310  1.065   26.593  1.00 23.05 ? 151 TRP B CE3   1 
ATOM   4471 C  CZ2   . TRP B 1 172 ? 33.037  0.335   26.494  1.00 23.10 ? 151 TRP B CZ2   1 
ATOM   4472 C  CZ3   . TRP B 1 172 ? 31.310  2.020   26.504  1.00 24.41 ? 151 TRP B CZ3   1 
ATOM   4473 C  CH2   . TRP B 1 172 ? 32.652  1.653   26.483  1.00 22.82 ? 151 TRP B CH2   1 
ATOM   4474 N  N     . VAL B 1 173 ? 27.945  0.448   29.158  1.00 23.46 ? 152 VAL B N     1 
ATOM   4475 C  CA    . VAL B 1 173 ? 28.296  1.608   30.044  1.00 23.88 ? 152 VAL B CA    1 
ATOM   4476 C  C     . VAL B 1 173 ? 28.208  1.171   31.526  1.00 26.97 ? 152 VAL B C     1 
ATOM   4477 O  O     . VAL B 1 173 ? 29.165  1.427   32.311  1.00 24.95 ? 152 VAL B O     1 
ATOM   4478 C  CB    . VAL B 1 173 ? 27.399  2.829   29.764  1.00 23.60 ? 152 VAL B CB    1 
ATOM   4479 C  CG1   . VAL B 1 173 ? 27.616  3.927   30.787  1.00 25.28 ? 152 VAL B CG1   1 
ATOM   4480 C  CG2   . VAL B 1 173 ? 27.618  3.388   28.362  1.00 24.79 ? 152 VAL B CG2   1 
ATOM   4481 N  N     . ALA B 1 174 ? 27.110  0.541   31.919  1.00 26.59 ? 153 ALA B N     1 
ATOM   4482 C  CA    . ALA B 1 174 ? 26.867  0.100   33.314  1.00 28.38 ? 153 ALA B CA    1 
ATOM   4483 C  C     . ALA B 1 174 ? 28.012  -0.828  33.745  1.00 28.78 ? 153 ALA B C     1 
ATOM   4484 O  O     . ALA B 1 174 ? 28.477  -0.676  34.858  1.00 32.70 ? 153 ALA B O     1 
ATOM   4485 C  CB    . ALA B 1 174 ? 25.503  -0.562  33.457  1.00 27.00 ? 153 ALA B CB    1 
ATOM   4486 N  N     . GLY B 1 175 ? 28.496  -1.703  32.867  1.00 26.55 ? 154 GLY B N     1 
ATOM   4487 C  CA    . GLY B 1 175 ? 29.558  -2.683  33.156  1.00 29.70 ? 154 GLY B CA    1 
ATOM   4488 C  C     . GLY B 1 175 ? 30.874  -2.012  33.483  1.00 33.38 ? 154 GLY B C     1 
ATOM   4489 O  O     . GLY B 1 175 ? 31.655  -2.626  34.202  1.00 31.78 ? 154 GLY B O     1 
ATOM   4490 N  N     . THR B 1 176 ? 31.105  -0.785  32.997  1.00 31.92 ? 155 THR B N     1 
ATOM   4491 C  CA    . THR B 1 176 ? 32.416  -0.098  33.121  1.00 32.73 ? 155 THR B CA    1 
ATOM   4492 C  C     . THR B 1 176 ? 32.621  0.432   34.543  1.00 35.95 ? 155 THR B C     1 
ATOM   4493 O  O     . THR B 1 176 ? 33.768  0.692   34.869  1.00 36.33 ? 155 THR B O     1 
ATOM   4494 C  CB    . THR B 1 176 ? 32.590  1.055   32.125  1.00 30.18 ? 155 THR B CB    1 
ATOM   4495 O  OG1   . THR B 1 176 ? 31.703  2.132   32.465  1.00 30.86 ? 155 THR B OG1   1 
ATOM   4496 C  CG2   . THR B 1 176 ? 32.376  0.608   30.700  1.00 31.81 ? 155 THR B CG2   1 
ATOM   4497 N  N     . GLY B 1 177 ? 31.550  0.680   35.290  1.00 37.80 ? 156 GLY B N     1 
ATOM   4498 C  CA    . GLY B 1 177 ? 31.585  1.229   36.656  1.00 36.76 ? 156 GLY B CA    1 
ATOM   4499 C  C     . GLY B 1 177 ? 31.866  2.728   36.734  1.00 38.79 ? 156 GLY B C     1 
ATOM   4500 O  O     . GLY B 1 177 ? 32.223  3.180   37.820  1.00 33.01 ? 156 GLY B O     1 
ATOM   4501 N  N     . VAL B 1 178 ? 31.706  3.522   35.673  1.00 33.07 ? 157 VAL B N     1 
ATOM   4502 C  CA    . VAL B 1 178 ? 31.988  4.986   35.758  1.00 34.39 ? 157 VAL B CA    1 
ATOM   4503 C  C     . VAL B 1 178 ? 31.073  5.607   36.807  1.00 32.95 ? 157 VAL B C     1 
ATOM   4504 O  O     . VAL B 1 178 ? 29.993  5.081   37.055  1.00 37.84 ? 157 VAL B O     1 
ATOM   4505 C  CB    . VAL B 1 178 ? 31.822  5.701   34.404  1.00 34.33 ? 157 VAL B CB    1 
ATOM   4506 C  CG1   . VAL B 1 178 ? 32.894  5.249   33.432  1.00 34.80 ? 157 VAL B CG1   1 
ATOM   4507 C  CG2   . VAL B 1 178 ? 30.429  5.523   33.815  1.00 32.69 ? 157 VAL B CG2   1 
ATOM   4508 N  N     . PRO B 1 179 ? 31.431  6.777   37.383  1.00 31.85 ? 158 PRO B N     1 
ATOM   4509 C  CA    . PRO B 1 179 ? 30.532  7.524   38.270  1.00 31.92 ? 158 PRO B CA    1 
ATOM   4510 C  C     . PRO B 1 179 ? 29.253  8.024   37.590  1.00 33.06 ? 158 PRO B C     1 
ATOM   4511 O  O     . PRO B 1 179 ? 29.273  8.205   36.410  1.00 29.73 ? 158 PRO B O     1 
ATOM   4512 C  CB    . PRO B 1 179 ? 31.310  8.792   38.644  1.00 29.61 ? 158 PRO B CB    1 
ATOM   4513 C  CG    . PRO B 1 179 ? 32.746  8.445   38.388  1.00 32.32 ? 158 PRO B CG    1 
ATOM   4514 C  CD    . PRO B 1 179 ? 32.711  7.474   37.217  1.00 30.38 ? 158 PRO B CD    1 
ATOM   4515 N  N     . ASP B 1 180 ? 28.247  8.382   38.387  1.00 34.38 ? 159 ASP B N     1 
ATOM   4516 C  CA    . ASP B 1 180 ? 26.906  8.821   37.924  1.00 36.33 ? 159 ASP B CA    1 
ATOM   4517 C  C     . ASP B 1 180 ? 27.009  10.036  37.003  1.00 31.44 ? 159 ASP B C     1 
ATOM   4518 O  O     . ASP B 1 180 ? 26.329  9.994   35.956  1.00 30.11 ? 159 ASP B O     1 
ATOM   4519 C  CB    . ASP B 1 180 ? 25.970  9.113   39.104  1.00 39.44 ? 159 ASP B CB    1 
ATOM   4520 C  CG    . ASP B 1 180 ? 25.364  7.855   39.693  1.00 45.85 ? 159 ASP B CG    1 
ATOM   4521 O  OD1   . ASP B 1 180 ? 25.865  6.769   39.378  1.00 50.16 ? 159 ASP B OD1   1 
ATOM   4522 O  OD2   . ASP B 1 180 ? 24.381  7.970   40.460  1.00 60.60 ? 159 ASP B OD2   1 
ATOM   4523 N  N     . ARG B 1 181 ? 27.801  11.065  37.343  1.00 27.40 ? 160 ARG B N     1 
ATOM   4524 C  CA    . ARG B 1 181 ? 27.889  12.289  36.523  1.00 28.76 ? 160 ARG B CA    1 
ATOM   4525 C  C     . ARG B 1 181 ? 28.529  11.932  35.187  1.00 27.47 ? 160 ARG B C     1 
ATOM   4526 O  O     . ARG B 1 181 ? 28.288  12.663  34.206  1.00 26.93 ? 160 ARG B O     1 
ATOM   4527 C  CB    . ARG B 1 181 ? 28.673  13.440  37.163  1.00 29.23 ? 160 ARG B CB    1 
ATOM   4528 C  CG    . ARG B 1 181 ? 27.839  14.190  38.180  1.00 31.36 ? 160 ARG B CG    1 
ATOM   4529 C  CD    . ARG B 1 181 ? 28.548  15.358  38.791  1.00 32.01 ? 160 ARG B CD    1 
ATOM   4530 N  NE    . ARG B 1 181 ? 27.590  16.079  39.621  1.00 32.56 ? 160 ARG B NE    1 
ATOM   4531 C  CZ    . ARG B 1 181 ? 27.822  17.258  40.177  1.00 36.43 ? 160 ARG B CZ    1 
ATOM   4532 N  NH1   . ARG B 1 181 ? 28.992  17.842  39.993  1.00 36.06 ? 160 ARG B NH1   1 
ATOM   4533 N  NH2   . ARG B 1 181 ? 26.878  17.871  40.887  1.00 37.32 ? 160 ARG B NH2   1 
ATOM   4534 N  N     . VAL B 1 182 ? 29.373  10.907  35.179  1.00 26.20 ? 161 VAL B N     1 
ATOM   4535 C  CA    . VAL B 1 182 ? 30.085  10.520  33.937  1.00 26.46 ? 161 VAL B CA    1 
ATOM   4536 C  C     . VAL B 1 182 ? 29.085  9.799   33.037  1.00 25.40 ? 161 VAL B C     1 
ATOM   4537 O  O     . VAL B 1 182 ? 29.038  10.164  31.880  1.00 24.19 ? 161 VAL B O     1 
ATOM   4538 C  CB    . VAL B 1 182 ? 31.336  9.674   34.195  1.00 26.00 ? 161 VAL B CB    1 
ATOM   4539 C  CG1   . VAL B 1 182 ? 31.952  9.204   32.890  1.00 25.19 ? 161 VAL B CG1   1 
ATOM   4540 C  CG2   . VAL B 1 182 ? 32.342  10.510  34.969  1.00 28.65 ? 161 VAL B CG2   1 
ATOM   4541 N  N     . ALA B 1 183 ? 28.350  8.819   33.556  1.00 24.84 ? 162 ALA B N     1 
ATOM   4542 C  CA    . ALA B 1 183 ? 27.241  8.161   32.800  1.00 26.41 ? 162 ALA B CA    1 
ATOM   4543 C  C     . ALA B 1 183 ? 26.261  9.222   32.270  1.00 26.01 ? 162 ALA B C     1 
ATOM   4544 O  O     . ALA B 1 183 ? 25.827  9.117   31.081  1.00 25.82 ? 162 ALA B O     1 
ATOM   4545 C  CB    . ALA B 1 183 ? 26.554  7.143   33.689  1.00 27.97 ? 162 ALA B CB    1 
ATOM   4546 N  N     . GLY B 1 184 ? 25.909  10.205  33.111  1.00 25.01 ? 163 GLY B N     1 
ATOM   4547 C  CA    . GLY B 1 184 ? 24.959  11.291  32.802  1.00 26.22 ? 163 GLY B CA    1 
ATOM   4548 C  C     . GLY B 1 184 ? 25.405  12.155  31.635  1.00 25.06 ? 163 GLY B C     1 
ATOM   4549 O  O     . GLY B 1 184 ? 24.601  12.456  30.753  1.00 23.58 ? 163 GLY B O     1 
ATOM   4550 N  N     . LEU B 1 185 ? 26.653  12.610  31.650  1.00 23.32 ? 164 LEU B N     1 
ATOM   4551 C  CA    . LEU B 1 185 ? 27.198  13.428  30.538  1.00 26.36 ? 164 LEU B CA    1 
ATOM   4552 C  C     . LEU B 1 185 ? 27.328  12.596  29.259  1.00 22.37 ? 164 LEU B C     1 
ATOM   4553 O  O     . LEU B 1 185 ? 27.075  13.135  28.196  1.00 25.92 ? 164 LEU B O     1 
ATOM   4554 C  CB    . LEU B 1 185 ? 28.573  13.951  30.930  1.00 34.21 ? 164 LEU B CB    1 
ATOM   4555 C  CG    . LEU B 1 185 ? 28.817  15.395  30.539  1.00 46.58 ? 164 LEU B CG    1 
ATOM   4556 C  CD1   . LEU B 1 185 ? 28.704  16.301  31.772  1.00 50.03 ? 164 LEU B CD1   1 
ATOM   4557 C  CD2   . LEU B 1 185 ? 30.185  15.522  29.874  1.00 57.21 ? 164 LEU B CD2   1 
ATOM   4558 N  N     . PHE B 1 186 ? 27.864  11.402  29.375  1.00 21.52 ? 165 PHE B N     1 
ATOM   4559 C  CA    . PHE B 1 186 ? 27.976  10.427  28.255  1.00 20.86 ? 165 PHE B CA    1 
ATOM   4560 C  C     . PHE B 1 186 ? 26.580  10.236  27.630  1.00 22.03 ? 165 PHE B C     1 
ATOM   4561 O  O     . PHE B 1 186 ? 26.450  10.265  26.383  1.00 22.37 ? 165 PHE B O     1 
ATOM   4562 C  CB    . PHE B 1 186 ? 28.619  9.133   28.737  1.00 20.84 ? 165 PHE B CB    1 
ATOM   4563 C  CG    . PHE B 1 186 ? 28.909  8.188   27.593  1.00 20.39 ? 165 PHE B CG    1 
ATOM   4564 C  CD1   . PHE B 1 186 ? 28.084  7.107   27.319  1.00 22.28 ? 165 PHE B CD1   1 
ATOM   4565 C  CD2   . PHE B 1 186 ? 29.965  8.440   26.723  1.00 24.36 ? 165 PHE B CD2   1 
ATOM   4566 C  CE1   . PHE B 1 186 ? 28.346  6.250   26.254  1.00 22.93 ? 165 PHE B CE1   1 
ATOM   4567 C  CE2   . PHE B 1 186 ? 30.226  7.571   25.668  1.00 24.89 ? 165 PHE B CE2   1 
ATOM   4568 C  CZ    . PHE B 1 186 ? 29.391  6.512   25.409  1.00 23.99 ? 165 PHE B CZ    1 
ATOM   4569 N  N     . GLU B 1 187 ? 25.535  10.076  28.463  1.00 20.77 ? 166 GLU B N     1 
ATOM   4570 C  CA    . GLU B 1 187 ? 24.128  9.943   27.970  1.00 19.78 ? 166 GLU B CA    1 
ATOM   4571 C  C     . GLU B 1 187 ? 23.710  11.171  27.155  1.00 19.60 ? 166 GLU B C     1 
ATOM   4572 O  O     . GLU B 1 187 ? 23.065  10.981  26.128  1.00 18.13 ? 166 GLU B O     1 
ATOM   4573 C  CB    . GLU B 1 187 ? 23.110  9.732   29.092  1.00 21.06 ? 166 GLU B CB    1 
ATOM   4574 C  CG    . GLU B 1 187 ? 21.795  9.196   28.571  1.00 20.92 ? 166 GLU B CG    1 
ATOM   4575 C  CD    . GLU B 1 187 ? 21.860  7.833   27.888  1.00 21.15 ? 166 GLU B CD    1 
ATOM   4576 O  OE1   . GLU B 1 187 ? 20.866  7.479   27.148  1.00 22.21 ? 166 GLU B OE1   1 
ATOM   4577 O  OE2   . GLU B 1 187 ? 22.850  7.084   28.107  1.00 24.66 ? 166 GLU B OE2   1 
ATOM   4578 N  N     . VAL B 1 188 ? 24.011  12.403  27.596  1.00 17.54 ? 167 VAL B N     1 
ATOM   4579 C  CA    . VAL B 1 188 ? 23.701  13.634  26.832  1.00 19.48 ? 167 VAL B CA    1 
ATOM   4580 C  C     . VAL B 1 188 ? 24.329  13.568  25.440  1.00 19.18 ? 167 VAL B C     1 
ATOM   4581 O  O     . VAL B 1 188 ? 23.642  13.891  24.438  1.00 19.83 ? 167 VAL B O     1 
ATOM   4582 C  CB    . VAL B 1 188 ? 24.181  14.903  27.560  1.00 21.81 ? 167 VAL B CB    1 
ATOM   4583 C  CG1   . VAL B 1 188 ? 24.028  16.129  26.684  1.00 23.92 ? 167 VAL B CG1   1 
ATOM   4584 C  CG2   . VAL B 1 188 ? 23.387  15.052  28.825  1.00 23.53 ? 167 VAL B CG2   1 
ATOM   4585 N  N     . ALA B 1 189 ? 25.582  13.141  25.362  1.00 19.77 ? 168 ALA B N     1 
ATOM   4586 C  CA    . ALA B 1 189 ? 26.337  13.057  24.088  1.00 21.48 ? 168 ALA B CA    1 
ATOM   4587 C  C     . ALA B 1 189 ? 25.709  11.965  23.211  1.00 20.01 ? 168 ALA B C     1 
ATOM   4588 O  O     . ALA B 1 189 ? 25.466  12.202  22.039  1.00 21.41 ? 168 ALA B O     1 
ATOM   4589 C  CB    . ALA B 1 189 ? 27.795  12.758  24.352  1.00 22.05 ? 168 ALA B CB    1 
ATOM   4590 N  N     . VAL B 1 190 ? 25.473  10.789  23.787  1.00 19.57 ? 169 VAL B N     1 
ATOM   4591 C  CA    . VAL B 1 190 ? 24.767  9.685   23.066  1.00 18.01 ? 169 VAL B CA    1 
ATOM   4592 C  C     . VAL B 1 190 ? 23.442  10.235  22.500  1.00 16.79 ? 169 VAL B C     1 
ATOM   4593 O  O     . VAL B 1 190 ? 23.122  9.981   21.322  1.00 16.89 ? 169 VAL B O     1 
ATOM   4594 C  CB    . VAL B 1 190 ? 24.539  8.456   23.955  1.00 17.82 ? 169 VAL B CB    1 
ATOM   4595 C  CG1   . VAL B 1 190 ? 23.560  7.491   23.309  1.00 20.03 ? 169 VAL B CG1   1 
ATOM   4596 C  CG2   . VAL B 1 190 ? 25.835  7.748   24.338  1.00 20.73 ? 169 VAL B CG2   1 
ATOM   4597 N  N     . GLN B 1 191 ? 22.619  10.908  23.305  1.00 16.56 ? 170 GLN B N     1 
ATOM   4598 C  CA    . GLN B 1 191 ? 21.288  11.335  22.817  1.00 16.52 ? 170 GLN B CA    1 
ATOM   4599 C  C     . GLN B 1 191 ? 21.485  12.423  21.746  1.00 17.15 ? 170 GLN B C     1 
ATOM   4600 O  O     . GLN B 1 191 ? 20.746  12.445  20.750  1.00 17.52 ? 170 GLN B O     1 
ATOM   4601 C  CB    . GLN B 1 191 ? 20.367  11.679  23.986  1.00 17.22 ? 170 GLN B CB    1 
ATOM   4602 C  CG    . GLN B 1 191 ? 20.085  10.470  24.860  1.00 18.97 ? 170 GLN B CG    1 
ATOM   4603 C  CD    . GLN B 1 191 ? 18.952  10.678  25.833  1.00 22.87 ? 170 GLN B CD    1 
ATOM   4604 O  OE1   . GLN B 1 191 ? 18.230  11.662  25.755  1.00 26.67 ? 170 GLN B OE1   1 
ATOM   4605 N  NE2   . GLN B 1 191 ? 18.843  9.791   26.807  1.00 22.85 ? 170 GLN B NE2   1 
ATOM   4606 N  N     . ALA B 1 192 ? 22.474  13.294  21.897  1.00 16.90 ? 171 ALA B N     1 
ATOM   4607 C  CA    . ALA B 1 192 ? 22.726  14.376  20.920  1.00 18.37 ? 171 ALA B CA    1 
ATOM   4608 C  C     . ALA B 1 192 ? 23.303  13.809  19.603  1.00 17.89 ? 171 ALA B C     1 
ATOM   4609 O  O     . ALA B 1 192 ? 23.091  14.427  18.546  1.00 19.56 ? 171 ALA B O     1 
ATOM   4610 C  CB    . ALA B 1 192 ? 23.698  15.352  21.532  1.00 19.06 ? 171 ALA B CB    1 
ATOM   4611 N  N     . VAL B 1 193 ? 23.975  12.657  19.653  1.00 16.73 ? 172 VAL B N     1 
ATOM   4612 C  CA    . VAL B 1 193 ? 24.597  12.045  18.446  1.00 18.57 ? 172 VAL B CA    1 
ATOM   4613 C  C     . VAL B 1 193 ? 23.594  11.104  17.749  1.00 18.42 ? 172 VAL B C     1 
ATOM   4614 O  O     . VAL B 1 193 ? 23.511  11.153  16.519  1.00 19.17 ? 172 VAL B O     1 
ATOM   4615 C  CB    . VAL B 1 193 ? 25.898  11.314  18.803  1.00 17.65 ? 172 VAL B CB    1 
ATOM   4616 C  CG1   . VAL B 1 193 ? 26.402  10.449  17.669  1.00 18.96 ? 172 VAL B CG1   1 
ATOM   4617 C  CG2   . VAL B 1 193 ? 26.956  12.335  19.249  1.00 20.73 ? 172 VAL B CG2   1 
ATOM   4618 N  N     . PHE B 1 194 ? 22.854  10.285  18.497  1.00 17.53 ? 173 PHE B N     1 
ATOM   4619 C  CA    . PHE B 1 194 ? 21.990  9.229   17.923  1.00 17.86 ? 173 PHE B CA    1 
ATOM   4620 C  C     . PHE B 1 194 ? 20.498  9.586   17.898  1.00 18.70 ? 173 PHE B C     1 
ATOM   4621 O  O     . PHE B 1 194 ? 19.707  8.812   17.225  1.00 17.85 ? 173 PHE B O     1 
ATOM   4622 C  CB    . PHE B 1 194 ? 22.219  7.942   18.725  1.00 19.32 ? 173 PHE B CB    1 
ATOM   4623 C  CG    . PHE B 1 194 ? 23.599  7.339   18.590  1.00 18.10 ? 173 PHE B CG    1 
ATOM   4624 C  CD1   . PHE B 1 194 ? 23.892  6.484   17.530  1.00 18.61 ? 173 PHE B CD1   1 
ATOM   4625 C  CD2   . PHE B 1 194 ? 24.595  7.579   19.535  1.00 17.43 ? 173 PHE B CD2   1 
ATOM   4626 C  CE1   . PHE B 1 194 ? 25.161  5.931   17.379  1.00 18.73 ? 173 PHE B CE1   1 
ATOM   4627 C  CE2   . PHE B 1 194 ? 25.855  7.006   19.408  1.00 20.62 ? 173 PHE B CE2   1 
ATOM   4628 C  CZ    . PHE B 1 194 ? 26.134  6.156   18.330  1.00 19.04 ? 173 PHE B CZ    1 
ATOM   4629 N  N     . ALA B 1 195 ? 20.047  10.608  18.653  1.00 17.22 ? 174 ALA B N     1 
ATOM   4630 C  CA    . ALA B 1 195 ? 18.607  10.948  18.772  1.00 16.12 ? 174 ALA B CA    1 
ATOM   4631 C  C     . ALA B 1 195 ? 17.845  9.723   19.324  1.00 16.37 ? 174 ALA B C     1 
ATOM   4632 O  O     . ALA B 1 195 ? 16.688  9.402   18.890  1.00 16.51 ? 174 ALA B O     1 
ATOM   4633 C  CB    . ALA B 1 195 ? 18.026  11.441  17.460  1.00 16.60 ? 174 ALA B CB    1 
ATOM   4634 N  N     . ALA B 1 196 ? 18.484  9.039   20.270  1.00 16.06 ? 175 ALA B N     1 
ATOM   4635 C  CA    . ALA B 1 196 ? 18.014  7.790   20.888  1.00 16.99 ? 175 ALA B CA    1 
ATOM   4636 C  C     . ALA B 1 196 ? 18.820  7.609   22.177  1.00 17.84 ? 175 ALA B C     1 
ATOM   4637 O  O     . ALA B 1 196 ? 19.930  8.133   22.259  1.00 16.51 ? 175 ALA B O     1 
ATOM   4638 C  CB    . ALA B 1 196 ? 18.235  6.619   19.947  1.00 17.22 ? 175 ALA B CB    1 
ATOM   4639 N  N     . THR B 1 197 ? 18.297  6.883   23.134  1.00 18.48 ? 176 THR B N     1 
ATOM   4640 C  CA    . THR B 1 197 ? 18.979  6.625   24.411  1.00 19.04 ? 176 THR B CA    1 
ATOM   4641 C  C     . THR B 1 197 ? 19.938  5.467   24.189  1.00 20.43 ? 176 THR B C     1 
ATOM   4642 O  O     . THR B 1 197 ? 19.749  4.675   23.246  1.00 17.33 ? 176 THR B O     1 
ATOM   4643 C  CB    . THR B 1 197 ? 17.978  6.338   25.534  1.00 19.71 ? 176 THR B CB    1 
ATOM   4644 O  OG1   . THR B 1 197 ? 17.581  4.985   25.368  1.00 18.69 ? 176 THR B OG1   1 
ATOM   4645 C  CG2   . THR B 1 197 ? 16.809  7.298   25.534  1.00 21.49 ? 176 THR B CG2   1 
ATOM   4646 N  N     . SER B 1 198 ? 20.875  5.313   25.105  1.00 20.96 ? 177 SER B N     1 
ATOM   4647 C  CA    . SER B 1 198 ? 21.846  4.198   25.123  1.00 20.38 ? 177 SER B CA    1 
ATOM   4648 C  C     . SER B 1 198 ? 21.118  2.861   25.293  1.00 20.10 ? 177 SER B C     1 
ATOM   4649 O  O     . SER B 1 198 ? 21.697  1.812   24.928  1.00 18.26 ? 177 SER B O     1 
ATOM   4650 C  CB    . SER B 1 198 ? 22.892  4.411   26.177  1.00 20.94 ? 177 SER B CB    1 
ATOM   4651 O  OG    . SER B 1 198 ? 22.314  4.702   27.445  1.00 20.35 ? 177 SER B OG    1 
ATOM   4652 N  N     . ALA B 1 199 ? 19.924  2.843   25.881  1.00 18.18 ? 178 ALA B N     1 
ATOM   4653 C  CA    . ALA B 1 199 ? 19.160  1.570   26.022  1.00 18.29 ? 178 ALA B CA    1 
ATOM   4654 C  C     . ALA B 1 199 ? 18.614  1.110   24.654  1.00 17.08 ? 178 ALA B C     1 
ATOM   4655 O  O     . ALA B 1 199 ? 18.314  -0.109  24.439  1.00 17.62 ? 178 ALA B O     1 
ATOM   4656 C  CB    . ALA B 1 199 ? 18.065  1.749   27.053  1.00 19.44 ? 178 ALA B CB    1 
ATOM   4657 N  N     . GLN B 1 200 ? 18.354  2.029   23.725  1.00 17.62 ? 179 GLN B N     1 
ATOM   4658 C  CA    . GLN B 1 200 ? 17.678  1.690   22.457  1.00 17.45 ? 179 GLN B CA    1 
ATOM   4659 C  C     . GLN B 1 200 ? 18.695  1.091   21.461  1.00 18.51 ? 179 GLN B C     1 
ATOM   4660 O  O     . GLN B 1 200 ? 18.255  0.418   20.545  1.00 19.34 ? 179 GLN B O     1 
ATOM   4661 C  CB    . GLN B 1 200 ? 17.082  2.943   21.809  1.00 20.06 ? 179 GLN B CB    1 
ATOM   4662 C  CG    . GLN B 1 200 ? 15.852  3.450   22.548  1.00 19.59 ? 179 GLN B CG    1 
ATOM   4663 C  CD    . GLN B 1 200 ? 15.319  4.674   21.858  1.00 20.75 ? 179 GLN B CD    1 
ATOM   4664 O  OE1   . GLN B 1 200 ? 15.710  5.802   22.163  1.00 23.73 ? 179 GLN B OE1   1 
ATOM   4665 N  NE2   . GLN B 1 200 ? 14.374  4.448   20.962  1.00 22.81 ? 179 GLN B NE2   1 
ATOM   4666 N  N     . LEU B 1 201 ? 19.986  1.369   21.651  1.00 18.87 ? 180 LEU B N     1 
ATOM   4667 C  CA    . LEU B 1 201 ? 21.062  1.092   20.659  1.00 20.08 ? 180 LEU B CA    1 
ATOM   4668 C  C     . LEU B 1 201 ? 21.781  -0.199  21.017  1.00 18.94 ? 180 LEU B C     1 
ATOM   4669 O  O     . LEU B 1 201 ? 22.157  -0.313  22.159  1.00 19.02 ? 180 LEU B O     1 
ATOM   4670 C  CB    . LEU B 1 201 ? 22.103  2.223   20.707  1.00 22.46 ? 180 LEU B CB    1 
ATOM   4671 C  CG    . LEU B 1 201 ? 21.590  3.640   20.558  1.00 24.27 ? 180 LEU B CG    1 
ATOM   4672 C  CD1   . LEU B 1 201 ? 22.699  4.628   20.895  1.00 24.41 ? 180 LEU B CD1   1 
ATOM   4673 C  CD2   . LEU B 1 201 ? 21.039  3.874   19.168  1.00 26.36 ? 180 LEU B CD2   1 
ATOM   4674 N  N     . SER B 1 202 ? 22.064  -1.092  20.061  1.00 17.91 ? 181 SER B N     1 
ATOM   4675 C  CA    . SER B 1 202 ? 23.057  -2.170  20.288  1.00 17.98 ? 181 SER B CA    1 
ATOM   4676 C  C     . SER B 1 202 ? 24.455  -1.560  20.423  1.00 17.72 ? 181 SER B C     1 
ATOM   4677 O  O     . SER B 1 202 ? 24.758  -0.493  19.847  1.00 17.04 ? 181 SER B O     1 
ATOM   4678 C  CB    . SER B 1 202 ? 23.031  -3.241  19.285  1.00 19.08 ? 181 SER B CB    1 
ATOM   4679 O  OG    . SER B 1 202 ? 23.683  -2.860  18.120  1.00 22.26 ? 181 SER B OG    1 
ATOM   4680 N  N     . LEU B 1 203 ? 25.282  -2.178  21.242  1.00 17.45 ? 182 LEU B N     1 
ATOM   4681 C  CA    . LEU B 1 203 ? 26.712  -1.797  21.331  1.00 17.86 ? 182 LEU B CA    1 
ATOM   4682 C  C     . LEU B 1 203 ? 27.348  -1.930  19.935  1.00 17.54 ? 182 LEU B C     1 
ATOM   4683 O  O     . LEU B 1 203 ? 28.135  -1.053  19.569  1.00 15.56 ? 182 LEU B O     1 
ATOM   4684 C  CB    . LEU B 1 203 ? 27.407  -2.697  22.355  1.00 18.90 ? 182 LEU B CB    1 
ATOM   4685 C  CG    . LEU B 1 203 ? 28.915  -2.535  22.455  1.00 19.09 ? 182 LEU B CG    1 
ATOM   4686 C  CD1   . LEU B 1 203 ? 29.285  -1.146  22.943  1.00 20.40 ? 182 LEU B CD1   1 
ATOM   4687 C  CD2   . LEU B 1 203 ? 29.469  -3.603  23.389  1.00 19.36 ? 182 LEU B CD2   1 
ATOM   4688 N  N     . LEU B 1 204 ? 27.005  -2.953  19.150  1.00 15.83 ? 183 LEU B N     1 
ATOM   4689 C  CA    . LEU B 1 204 ? 27.603  -3.096  17.808  1.00 17.57 ? 183 LEU B CA    1 
ATOM   4690 C  C     . LEU B 1 204 ? 27.237  -1.881  16.941  1.00 16.38 ? 183 LEU B C     1 
ATOM   4691 O  O     . LEU B 1 204 ? 28.115  -1.356  16.176  1.00 17.20 ? 183 LEU B O     1 
ATOM   4692 C  CB    . LEU B 1 204 ? 27.122  -4.396  17.165  1.00 18.52 ? 183 LEU B CB    1 
ATOM   4693 C  CG    . LEU B 1 204 ? 27.723  -4.711  15.807  1.00 17.32 ? 183 LEU B CG    1 
ATOM   4694 C  CD1   . LEU B 1 204 ? 29.248  -4.759  15.839  1.00 19.08 ? 183 LEU B CD1   1 
ATOM   4695 C  CD2   . LEU B 1 204 ? 27.194  -6.046  15.334  1.00 18.41 ? 183 LEU B CD2   1 
ATOM   4696 N  N     . HIS B 1 205 ? 25.988  -1.419  17.031  1.00 16.39 ? 184 HIS B N     1 
ATOM   4697 C  CA    . HIS B 1 205 ? 25.531  -0.268  16.216  1.00 16.86 ? 184 HIS B CA    1 
ATOM   4698 C  C     . HIS B 1 205 ? 26.331  0.972   16.626  1.00 17.22 ? 184 HIS B C     1 
ATOM   4699 O  O     . HIS B 1 205 ? 26.836  1.707   15.725  1.00 16.16 ? 184 HIS B O     1 
ATOM   4700 C  CB    . HIS B 1 205 ? 24.038  0.005   16.412  1.00 15.54 ? 184 HIS B CB    1 
ATOM   4701 C  CG    . HIS B 1 205 ? 23.618  1.210   15.664  1.00 16.22 ? 184 HIS B CG    1 
ATOM   4702 N  ND1   . HIS B 1 205 ? 23.457  1.180   14.317  1.00 16.99 ? 184 HIS B ND1   1 
ATOM   4703 C  CD2   . HIS B 1 205 ? 23.316  2.461   16.074  1.00 17.02 ? 184 HIS B CD2   1 
ATOM   4704 C  CE1   . HIS B 1 205 ? 23.155  2.392   13.896  1.00 19.47 ? 184 HIS B CE1   1 
ATOM   4705 N  NE2   . HIS B 1 205 ? 23.075  3.211   14.981  1.00 17.33 ? 184 HIS B NE2   1 
ATOM   4706 N  N     . ALA B 1 206 ? 26.413  1.229   17.931  1.00 16.32 ? 185 ALA B N     1 
ATOM   4707 C  CA    . ALA B 1 206 ? 27.098  2.438   18.428  1.00 15.22 ? 185 ALA B CA    1 
ATOM   4708 C  C     . ALA B 1 206 ? 28.569  2.388   17.979  1.00 14.03 ? 185 ALA B C     1 
ATOM   4709 O  O     . ALA B 1 206 ? 29.125  3.427   17.590  1.00 15.64 ? 185 ALA B O     1 
ATOM   4710 C  CB    . ALA B 1 206 ? 26.926  2.517   19.895  1.00 17.26 ? 185 ALA B CB    1 
ATOM   4711 N  N     . ALA B 1 207 ? 29.190  1.241   18.103  1.00 16.53 ? 186 ALA B N     1 
ATOM   4712 C  CA    . ALA B 1 207 ? 30.620  1.033   17.801  1.00 18.15 ? 186 ALA B CA    1 
ATOM   4713 C  C     . ALA B 1 207 ? 30.881  1.236   16.315  1.00 15.82 ? 186 ALA B C     1 
ATOM   4714 O  O     . ALA B 1 207 ? 31.862  1.917   15.943  1.00 16.05 ? 186 ALA B O     1 
ATOM   4715 C  CB    . ALA B 1 207 ? 31.075  -0.302  18.317  1.00 19.29 ? 186 ALA B CB    1 
ATOM   4716 N  N     . HIS B 1 208 ? 30.063  0.653   15.461  1.00 17.07 ? 187 HIS B N     1 
ATOM   4717 C  CA    . HIS B 1 208 ? 30.149  0.904   13.996  1.00 16.18 ? 187 HIS B CA    1 
ATOM   4718 C  C     . HIS B 1 208 ? 30.074  2.407   13.722  1.00 16.82 ? 187 HIS B C     1 
ATOM   4719 O  O     . HIS B 1 208 ? 30.889  2.938   12.976  1.00 16.18 ? 187 HIS B O     1 
ATOM   4720 C  CB    . HIS B 1 208 ? 29.057  0.141   13.255  1.00 16.92 ? 187 HIS B CB    1 
ATOM   4721 C  CG    . HIS B 1 208 ? 29.029  0.522   11.818  1.00 18.38 ? 187 HIS B CG    1 
ATOM   4722 N  ND1   . HIS B 1 208 ? 29.904  -0.026  10.867  1.00 20.23 ? 187 HIS B ND1   1 
ATOM   4723 C  CD2   . HIS B 1 208 ? 28.284  1.442   11.173  1.00 17.79 ? 187 HIS B CD2   1 
ATOM   4724 C  CE1   . HIS B 1 208 ? 29.633  0.516   9.686   1.00 17.38 ? 187 HIS B CE1   1 
ATOM   4725 N  NE2   . HIS B 1 208 ? 28.692  1.451   9.865   1.00 23.95 ? 187 HIS B NE2   1 
ATOM   4726 N  N     . TYR B 1 209 ? 29.113  3.108   14.327  1.00 17.84 ? 188 TYR B N     1 
ATOM   4727 C  CA    . TYR B 1 209 ? 28.891  4.559   14.107  1.00 16.43 ? 188 TYR B CA    1 
ATOM   4728 C  C     . TYR B 1 209 ? 30.151  5.349   14.492  1.00 17.27 ? 188 TYR B C     1 
ATOM   4729 O  O     . TYR B 1 209 ? 30.568  6.275   13.789  1.00 16.65 ? 188 TYR B O     1 
ATOM   4730 C  CB    . TYR B 1 209 ? 27.731  5.059   14.965  1.00 17.16 ? 188 TYR B CB    1 
ATOM   4731 C  CG    . TYR B 1 209 ? 26.962  6.219   14.403  1.00 17.27 ? 188 TYR B CG    1 
ATOM   4732 C  CD1   . TYR B 1 209 ? 27.192  7.510   14.851  1.00 18.03 ? 188 TYR B CD1   1 
ATOM   4733 C  CD2   . TYR B 1 209 ? 25.932  6.015   13.501  1.00 16.96 ? 188 TYR B CD2   1 
ATOM   4734 C  CE1   . TYR B 1 209 ? 26.467  8.584   14.352  1.00 16.53 ? 188 TYR B CE1   1 
ATOM   4735 C  CE2   . TYR B 1 209 ? 25.176  7.075   13.014  1.00 17.56 ? 188 TYR B CE2   1 
ATOM   4736 C  CZ    . TYR B 1 209 ? 25.420  8.363   13.471  1.00 17.67 ? 188 TYR B CZ    1 
ATOM   4737 O  OH    . TYR B 1 209 ? 24.655  9.387   12.983  1.00 17.60 ? 188 TYR B OH    1 
ATOM   4738 N  N     . VAL B 1 210 ? 30.762  4.970   15.607  1.00 16.65 ? 189 VAL B N     1 
ATOM   4739 C  CA    . VAL B 1 210 ? 31.985  5.637   16.133  1.00 17.08 ? 189 VAL B CA    1 
ATOM   4740 C  C     . VAL B 1 210 ? 33.130  5.381   15.148  1.00 15.61 ? 189 VAL B C     1 
ATOM   4741 O  O     . VAL B 1 210 ? 33.885  6.306   14.818  1.00 15.38 ? 189 VAL B O     1 
ATOM   4742 C  CB    . VAL B 1 210 ? 32.278  5.142   17.575  1.00 15.99 ? 189 VAL B CB    1 
ATOM   4743 C  CG1   . VAL B 1 210 ? 33.655  5.598   18.083  1.00 17.33 ? 189 VAL B CG1   1 
ATOM   4744 C  CG2   . VAL B 1 210 ? 31.215  5.664   18.535  1.00 16.89 ? 189 VAL B CG2   1 
ATOM   4745 N  N     . HIS B 1 211 ? 33.282  4.144   14.682  1.00 15.70 ? 190 HIS B N     1 
ATOM   4746 C  CA    . HIS B 1 211 ? 34.350  3.842   13.689  1.00 15.75 ? 190 HIS B CA    1 
ATOM   4747 C  C     . HIS B 1 211 ? 34.119  4.649   12.413  1.00 16.33 ? 190 HIS B C     1 
ATOM   4748 O  O     . HIS B 1 211 ? 35.050  5.271   11.894  1.00 16.54 ? 190 HIS B O     1 
ATOM   4749 C  CB    . HIS B 1 211 ? 34.439  2.328   13.455  1.00 16.09 ? 190 HIS B CB    1 
ATOM   4750 C  CG    . HIS B 1 211 ? 35.685  1.941   12.751  1.00 15.27 ? 190 HIS B CG    1 
ATOM   4751 N  ND1   . HIS B 1 211 ? 35.837  0.677   12.230  1.00 14.73 ? 190 HIS B ND1   1 
ATOM   4752 C  CD2   . HIS B 1 211 ? 36.801  2.639   12.414  1.00 16.97 ? 190 HIS B CD2   1 
ATOM   4753 C  CE1   . HIS B 1 211 ? 36.998  0.620   11.618  1.00 15.37 ? 190 HIS B CE1   1 
ATOM   4754 N  NE2   . HIS B 1 211 ? 37.619  1.790   11.727  1.00 15.78 ? 190 HIS B NE2   1 
ATOM   4755 N  N     . SER B 1 212 ? 32.868  4.715   11.960  1.00 16.36 ? 191 SER B N     1 
ATOM   4756 C  CA    . SER B 1 212 ? 32.441  5.388   10.723  1.00 16.57 ? 191 SER B CA    1 
ATOM   4757 C  C     . SER B 1 212 ? 32.833  6.866   10.783  1.00 18.25 ? 191 SER B C     1 
ATOM   4758 O  O     . SER B 1 212 ? 33.242  7.428   9.700   1.00 16.98 ? 191 SER B O     1 
ATOM   4759 C  CB    . SER B 1 212 ? 30.958  5.176   10.519  1.00 17.74 ? 191 SER B CB    1 
ATOM   4760 O  OG    . SER B 1 212 ? 30.606  5.655   9.246   1.00 17.96 ? 191 SER B OG    1 
ATOM   4761 N  N     . ALA B 1 213 ? 32.746  7.483   11.979  1.00 16.96 ? 192 ALA B N     1 
ATOM   4762 C  CA    . ALA B 1 213 ? 33.051  8.918   12.169  1.00 18.48 ? 192 ALA B CA    1 
ATOM   4763 C  C     . ALA B 1 213 ? 34.544  9.161   12.393  1.00 21.16 ? 192 ALA B C     1 
ATOM   4764 O  O     . ALA B 1 213 ? 34.960  10.303  12.272  1.00 21.48 ? 192 ALA B O     1 
ATOM   4765 C  CB    . ALA B 1 213 ? 32.280  9.488   13.314  1.00 18.22 ? 192 ALA B CB    1 
ATOM   4766 N  N     . GLY B 1 214 ? 35.304  8.154   12.810  1.00 21.78 ? 193 GLY B N     1 
ATOM   4767 C  CA    . GLY B 1 214 ? 36.725  8.336   13.138  1.00 21.03 ? 193 GLY B CA    1 
ATOM   4768 C  C     . GLY B 1 214 ? 36.903  8.604   14.622  1.00 21.97 ? 193 GLY B C     1 
ATOM   4769 O  O     . GLY B 1 214 ? 37.943  9.104   14.979  1.00 21.72 ? 193 GLY B O     1 
ATOM   4770 N  N     . GLY B 1 215 ? 35.959  8.223   15.494  1.00 18.60 ? 194 GLY B N     1 
ATOM   4771 C  CA    . GLY B 1 215 ? 36.155  8.309   16.938  1.00 19.65 ? 194 GLY B CA    1 
ATOM   4772 C  C     . GLY B 1 215 ? 35.128  9.160   17.672  1.00 18.89 ? 194 GLY B C     1 
ATOM   4773 O  O     . GLY B 1 215 ? 34.337  9.894   17.031  1.00 19.23 ? 194 GLY B O     1 
ATOM   4774 N  N     . TRP B 1 216 ? 35.166  9.070   19.000  1.00 20.46 ? 195 TRP B N     1 
ATOM   4775 C  CA    . TRP B 1 216 ? 34.205  9.776   19.896  1.00 21.89 ? 195 TRP B CA    1 
ATOM   4776 C  C     . TRP B 1 216 ? 34.408  11.291  19.797  1.00 23.57 ? 195 TRP B C     1 
ATOM   4777 O  O     . TRP B 1 216 ? 33.394  12.031  19.714  1.00 21.48 ? 195 TRP B O     1 
ATOM   4778 C  CB    . TRP B 1 216 ? 34.327  9.277   21.328  1.00 21.30 ? 195 TRP B CB    1 
ATOM   4779 C  CG    . TRP B 1 216 ? 33.191  9.702   22.197  1.00 21.99 ? 195 TRP B CG    1 
ATOM   4780 C  CD1   . TRP B 1 216 ? 33.231  10.529  23.275  1.00 22.88 ? 195 TRP B CD1   1 
ATOM   4781 C  CD2   . TRP B 1 216 ? 31.819  9.335   22.028  1.00 20.11 ? 195 TRP B CD2   1 
ATOM   4782 N  NE1   . TRP B 1 216 ? 31.979  10.698  23.795  1.00 22.90 ? 195 TRP B NE1   1 
ATOM   4783 C  CE2   . TRP B 1 216 ? 31.092  9.974   23.059  1.00 23.63 ? 195 TRP B CE2   1 
ATOM   4784 C  CE3   . TRP B 1 216 ? 31.131  8.563   21.094  1.00 22.63 ? 195 TRP B CE3   1 
ATOM   4785 C  CZ2   . TRP B 1 216 ? 29.717  9.830   23.185  1.00 24.91 ? 195 TRP B CZ2   1 
ATOM   4786 C  CZ3   . TRP B 1 216 ? 29.771  8.413   21.224  1.00 26.76 ? 195 TRP B CZ3   1 
ATOM   4787 C  CH2   . TRP B 1 216 ? 29.075  9.037   22.261  1.00 28.81 ? 195 TRP B CH2   1 
ATOM   4788 N  N     . SER B 1 217 ? 35.654  11.752  19.786  1.00 22.93 ? 196 SER B N     1 
ATOM   4789 C  CA    . SER B 1 217 ? 35.995  13.189  19.626  1.00 25.24 ? 196 SER B CA    1 
ATOM   4790 C  C     . SER B 1 217 ? 35.420  13.740  18.320  1.00 23.57 ? 196 SER B C     1 
ATOM   4791 O  O     . SER B 1 217 ? 34.916  14.855  18.335  1.00 23.40 ? 196 SER B O     1 
ATOM   4792 C  CB    . SER B 1 217 ? 37.508  13.390  19.663  1.00 27.67 ? 196 SER B CB    1 
ATOM   4793 O  OG    . SER B 1 217 ? 37.963  13.131  20.970  1.00 32.62 ? 196 SER B OG    1 
ATOM   4794 N  N     . LYS B 1 218 ? 35.585  13.017  17.201  1.00 20.73 ? 197 LYS B N     1 
ATOM   4795 C  CA    . LYS B 1 218 ? 35.033  13.465  15.900  1.00 21.36 ? 197 LYS B CA    1 
ATOM   4796 C  C     . LYS B 1 218 ? 33.516  13.676  16.019  1.00 19.13 ? 197 LYS B C     1 
ATOM   4797 O  O     . LYS B 1 218 ? 33.025  14.584  15.388  1.00 20.23 ? 197 LYS B O     1 
ATOM   4798 C  CB    . LYS B 1 218 ? 35.367  12.470  14.772  1.00 21.26 ? 197 LYS B CB    1 
ATOM   4799 C  CG    . LYS B 1 218 ? 36.755  12.673  14.175  1.00 25.59 ? 197 LYS B CG    1 
ATOM   4800 C  CD    . LYS B 1 218 ? 36.809  13.991  13.427  1.00 26.77 ? 197 LYS B CD    1 
ATOM   4801 C  CE    . LYS B 1 218 ? 38.154  14.379  12.868  1.00 33.24 ? 197 LYS B CE    1 
ATOM   4802 N  NZ    . LYS B 1 218 ? 38.681  13.288  12.034  1.00 35.80 ? 197 LYS B NZ    1 
ATOM   4803 N  N     . LEU B 1 219 ? 32.802  12.873  16.796  1.00 20.10 ? 198 LEU B N     1 
ATOM   4804 C  CA    . LEU B 1 219 ? 31.328  13.006  16.923  1.00 19.45 ? 198 LEU B CA    1 
ATOM   4805 C  C     . LEU B 1 219 ? 30.957  14.155  17.858  1.00 19.23 ? 198 LEU B C     1 
ATOM   4806 O  O     . LEU B 1 219 ? 29.904  14.789  17.634  1.00 21.11 ? 198 LEU B O     1 
ATOM   4807 C  CB    . LEU B 1 219 ? 30.763  11.704  17.479  1.00 18.68 ? 198 LEU B CB    1 
ATOM   4808 C  CG    . LEU B 1 219 ? 30.767  10.545  16.481  1.00 20.04 ? 198 LEU B CG    1 
ATOM   4809 C  CD1   . LEU B 1 219 ? 30.487  9.245   17.209  1.00 21.11 ? 198 LEU B CD1   1 
ATOM   4810 C  CD2   . LEU B 1 219 ? 29.773  10.787  15.345  1.00 19.93 ? 198 LEU B CD2   1 
ATOM   4811 N  N     . THR B 1 220 ? 31.723  14.357  18.915  1.00 20.08 ? 199 THR B N     1 
ATOM   4812 C  CA    . THR B 1 220 ? 31.278  15.243  20.037  1.00 20.64 ? 199 THR B CA    1 
ATOM   4813 C  C     . THR B 1 220 ? 31.970  16.608  20.024  1.00 24.25 ? 199 THR B C     1 
ATOM   4814 O  O     . THR B 1 220 ? 31.480  17.502  20.769  1.00 20.50 ? 199 THR B O     1 
ATOM   4815 C  CB    . THR B 1 220 ? 31.450  14.572  21.404  1.00 23.09 ? 199 THR B CB    1 
ATOM   4816 O  OG1   . THR B 1 220 ? 32.829  14.248  21.602  1.00 23.16 ? 199 THR B OG1   1 
ATOM   4817 C  CG2   . THR B 1 220 ? 30.593  13.333  21.551  1.00 24.10 ? 199 THR B CG2   1 
ATOM   4818 N  N     . ASP B 1 221 ? 33.082  16.759  19.320  1.00 22.62 ? 200 ASP B N     1 
ATOM   4819 C  CA    . ASP B 1 221 ? 33.873  18.012  19.380  1.00 23.89 ? 200 ASP B CA    1 
ATOM   4820 C  C     . ASP B 1 221 ? 33.227  19.055  18.460  1.00 21.58 ? 200 ASP B C     1 
ATOM   4821 O  O     . ASP B 1 221 ? 32.671  18.720  17.404  1.00 21.39 ? 200 ASP B O     1 
ATOM   4822 C  CB    . ASP B 1 221 ? 35.365  17.800  19.050  1.00 25.93 ? 200 ASP B CB    1 
ATOM   4823 C  CG    . ASP B 1 221 ? 36.209  17.191  20.168  1.00 28.96 ? 200 ASP B CG    1 
ATOM   4824 O  OD1   . ASP B 1 221 ? 35.658  16.939  21.269  1.00 29.19 ? 200 ASP B OD1   1 
ATOM   4825 O  OD2   . ASP B 1 221 ? 37.385  16.887  19.892  1.00 33.11 ? 200 ASP B OD2   1 
ATOM   4826 N  N     . THR B 1 222 ? 33.365  20.323  18.828  1.00 20.62 ? 201 THR B N     1 
ATOM   4827 C  CA    . THR B 1 222 ? 33.119  21.468  17.927  1.00 20.42 ? 201 THR B CA    1 
ATOM   4828 C  C     . THR B 1 222 ? 34.417  21.702  17.132  1.00 21.45 ? 201 THR B C     1 
ATOM   4829 O  O     . THR B 1 222 ? 34.533  21.176  16.019  1.00 19.85 ? 201 THR B O     1 
ATOM   4830 C  CB    . THR B 1 222 ? 32.616  22.671  18.735  1.00 20.78 ? 201 THR B CB    1 
ATOM   4831 O  OG1   . THR B 1 222 ? 31.399  22.297  19.388  1.00 22.19 ? 201 THR B OG1   1 
ATOM   4832 C  CG2   . THR B 1 222 ? 32.414  23.889  17.869  1.00 22.55 ? 201 THR B CG2   1 
ATOM   4833 N  N     . GLU B 1 223 ? 35.400  22.393  17.714  1.00 21.31 ? 202 GLU B N     1 
ATOM   4834 C  CA    . GLU B 1 223 ? 36.725  22.557  17.052  1.00 25.35 ? 202 GLU B CA    1 
ATOM   4835 C  C     . GLU B 1 223 ? 37.322  21.156  16.866  1.00 21.55 ? 202 GLU B C     1 
ATOM   4836 O  O     . GLU B 1 223 ? 37.449  20.407  17.829  1.00 21.82 ? 202 GLU B O     1 
ATOM   4837 C  CB    . GLU B 1 223 ? 37.661  23.526  17.780  1.00 29.66 ? 202 GLU B CB    1 
ATOM   4838 C  CG    . GLU B 1 223 ? 38.968  23.742  17.010  1.00 36.40 ? 202 GLU B CG    1 
ATOM   4839 C  CD    . GLU B 1 223 ? 39.999  24.736  17.570  1.00 46.04 ? 202 GLU B CD    1 
ATOM   4840 O  OE1   . GLU B 1 223 ? 40.517  25.543  16.776  1.00 47.96 ? 202 GLU B OE1   1 
ATOM   4841 O  OE2   . GLU B 1 223 ? 40.326  24.675  18.780  1.00 54.32 ? 202 GLU B OE2   1 
ATOM   4842 N  N     . GLY B 1 224 ? 37.567  20.779  15.620  1.00 23.41 ? 203 GLY B N     1 
ATOM   4843 C  CA    . GLY B 1 224 ? 38.203  19.490  15.292  1.00 24.61 ? 203 GLY B CA    1 
ATOM   4844 C  C     . GLY B 1 224 ? 37.211  18.350  15.127  1.00 24.00 ? 203 GLY B C     1 
ATOM   4845 O  O     . GLY B 1 224 ? 37.681  17.206  14.902  1.00 23.64 ? 203 GLY B O     1 
ATOM   4846 N  N     . GLY B 1 225 ? 35.907  18.622  15.230  1.00 22.35 ? 204 GLY B N     1 
ATOM   4847 C  CA    . GLY B 1 225 ? 34.852  17.580  15.163  1.00 20.53 ? 204 GLY B CA    1 
ATOM   4848 C  C     . GLY B 1 225 ? 33.686  17.984  14.272  1.00 18.61 ? 204 GLY B C     1 
ATOM   4849 O  O     . GLY B 1 225 ? 33.780  18.987  13.498  1.00 18.44 ? 204 GLY B O     1 
ATOM   4850 N  N     . ALA B 1 226 ? 32.607  17.195  14.329  1.00 18.67 ? 205 ALA B N     1 
ATOM   4851 C  CA    . ALA B 1 226 ? 31.482  17.222  13.363  1.00 17.97 ? 205 ALA B CA    1 
ATOM   4852 C  C     . ALA B 1 226 ? 30.717  18.562  13.462  1.00 16.96 ? 205 ALA B C     1 
ATOM   4853 O  O     . ALA B 1 226 ? 30.049  18.934  12.486  1.00 19.03 ? 205 ALA B O     1 
ATOM   4854 C  CB    . ALA B 1 226 ? 30.557  16.050  13.654  1.00 17.60 ? 205 ALA B CB    1 
ATOM   4855 N  N     . GLN B 1 227 ? 30.868  19.319  14.545  1.00 17.53 ? 206 GLN B N     1 
ATOM   4856 C  CA    . GLN B 1 227 ? 30.131  20.609  14.752  1.00 17.01 ? 206 GLN B CA    1 
ATOM   4857 C  C     . GLN B 1 227 ? 31.061  21.804  14.476  1.00 19.68 ? 206 GLN B C     1 
ATOM   4858 O  O     . GLN B 1 227 ? 30.743  22.942  14.879  1.00 19.63 ? 206 GLN B O     1 
ATOM   4859 C  CB    . GLN B 1 227 ? 29.546  20.692  16.165  1.00 18.26 ? 206 GLN B CB    1 
ATOM   4860 C  CG    . GLN B 1 227 ? 28.359  19.790  16.432  1.00 18.96 ? 206 GLN B CG    1 
ATOM   4861 C  CD    . GLN B 1 227 ? 28.745  18.329  16.495  1.00 18.61 ? 206 GLN B CD    1 
ATOM   4862 O  OE1   . GLN B 1 227 ? 29.480  17.871  17.382  1.00 22.26 ? 206 GLN B OE1   1 
ATOM   4863 N  NE2   . GLN B 1 227 ? 28.188  17.577  15.589  1.00 18.04 ? 206 GLN B NE2   1 
ATOM   4864 N  N     . GLN B 1 228 ? 32.138  21.603  13.718  1.00 19.75 ? 207 GLN B N     1 
ATOM   4865 C  CA    . GLN B 1 228 ? 33.138  22.688  13.574  1.00 20.29 ? 207 GLN B CA    1 
ATOM   4866 C  C     . GLN B 1 228 ? 32.620  23.850  12.726  1.00 19.87 ? 207 GLN B C     1 
ATOM   4867 O  O     . GLN B 1 228 ? 32.912  25.004  13.068  1.00 20.68 ? 207 GLN B O     1 
ATOM   4868 C  CB    . GLN B 1 228 ? 34.426  22.183  12.930  1.00 20.55 ? 207 GLN B CB    1 
ATOM   4869 C  CG    . GLN B 1 228 ? 35.525  23.221  13.033  1.00 22.03 ? 207 GLN B CG    1 
ATOM   4870 C  CD    . GLN B 1 228 ? 36.853  22.731  12.534  1.00 22.27 ? 207 GLN B CD    1 
ATOM   4871 O  OE1   . GLN B 1 228 ? 37.605  22.093  13.261  1.00 22.86 ? 207 GLN B OE1   1 
ATOM   4872 N  NE2   . GLN B 1 228 ? 37.111  22.999  11.269  1.00 25.03 ? 207 GLN B NE2   1 
ATOM   4873 N  N     . ASP B 1 229 ? 31.941  23.570  11.625  1.00 18.77 ? 208 ASP B N     1 
ATOM   4874 C  CA    . ASP B 1 229 ? 31.649  24.571  10.569  1.00 20.60 ? 208 ASP B CA    1 
ATOM   4875 C  C     . ASP B 1 229 ? 30.174  24.538  10.163  1.00 22.26 ? 208 ASP B C     1 
ATOM   4876 O  O     . ASP B 1 229 ? 29.544  23.474  10.175  1.00 21.11 ? 208 ASP B O     1 
ATOM   4877 C  CB    . ASP B 1 229 ? 32.563  24.370  9.359   1.00 24.80 ? 208 ASP B CB    1 
ATOM   4878 C  CG    . ASP B 1 229 ? 34.015  24.708  9.679   1.00 27.50 ? 208 ASP B CG    1 
ATOM   4879 O  OD1   . ASP B 1 229 ? 34.276  25.870  10.045  1.00 28.74 ? 208 ASP B OD1   1 
ATOM   4880 O  OD2   . ASP B 1 229 ? 34.859  23.788  9.634   1.00 27.68 ? 208 ASP B OD2   1 
ATOM   4881 N  N     . ARG B 1 230 ? 29.681  25.681  9.711   1.00 19.77 ? 209 ARG B N     1 
ATOM   4882 C  CA    . ARG B 1 230 ? 28.357  25.877  9.102   1.00 19.97 ? 209 ARG B CA    1 
ATOM   4883 C  C     . ARG B 1 230 ? 28.557  26.359  7.665   1.00 20.84 ? 209 ARG B C     1 
ATOM   4884 O  O     . ARG B 1 230 ? 29.708  26.725  7.294   1.00 23.22 ? 209 ARG B O     1 
ATOM   4885 C  CB    . ARG B 1 230 ? 27.582  26.928  9.906   1.00 20.71 ? 209 ARG B CB    1 
ATOM   4886 C  CG    . ARG B 1 230 ? 27.261  26.574  11.351  1.00 24.88 ? 209 ARG B CG    1 
ATOM   4887 C  CD    . ARG B 1 230 ? 25.960  25.830  11.620  1.00 23.88 ? 209 ARG B CD    1 
ATOM   4888 N  NE    . ARG B 1 230 ? 24.825  26.266  10.815  1.00 20.64 ? 209 ARG B NE    1 
ATOM   4889 C  CZ    . ARG B 1 230 ? 23.822  27.038  11.198  1.00 23.23 ? 209 ARG B CZ    1 
ATOM   4890 N  NH1   . ARG B 1 230 ? 23.760  27.593  12.409  1.00 21.58 ? 209 ARG B NH1   1 
ATOM   4891 N  NH2   . ARG B 1 230 ? 22.862  27.269  10.323  1.00 21.01 ? 209 ARG B NH2   1 
ATOM   4892 N  N     . LEU B 1 231 ? 27.496  26.361  6.877   1.00 20.32 ? 210 LEU B N     1 
ATOM   4893 C  CA    . LEU B 1 231 ? 27.449  26.893  5.495   1.00 21.79 ? 210 LEU B CA    1 
ATOM   4894 C  C     . LEU B 1 231 ? 26.756  28.261  5.475   1.00 22.00 ? 210 LEU B C     1 
ATOM   4895 O  O     . LEU B 1 231 ? 25.620  28.352  5.898   1.00 19.97 ? 210 LEU B O     1 
ATOM   4896 C  CB    . LEU B 1 231 ? 26.688  25.908  4.607   1.00 21.28 ? 210 LEU B CB    1 
ATOM   4897 C  CG    . LEU B 1 231 ? 27.258  24.489  4.576   1.00 22.66 ? 210 LEU B CG    1 
ATOM   4898 C  CD1   . LEU B 1 231 ? 26.744  23.737  3.360   1.00 24.50 ? 210 LEU B CD1   1 
ATOM   4899 C  CD2   . LEU B 1 231 ? 28.764  24.487  4.623   1.00 24.38 ? 210 LEU B CD2   1 
ATOM   4900 N  N     . VAL B 1 232 ? 27.413  29.278  4.929   1.00 22.42 ? 211 VAL B N     1 
ATOM   4901 C  CA    . VAL B 1 232 ? 26.785  30.625  4.725   1.00 23.11 ? 211 VAL B CA    1 
ATOM   4902 C  C     . VAL B 1 232 ? 25.565  30.437  3.837   1.00 21.69 ? 211 VAL B C     1 
ATOM   4903 O  O     . VAL B 1 232 ? 25.746  29.878  2.736   1.00 24.56 ? 211 VAL B O     1 
ATOM   4904 C  CB    . VAL B 1 232 ? 27.778  31.592  4.060   1.00 22.60 ? 211 VAL B CB    1 
ATOM   4905 C  CG1   . VAL B 1 232 ? 27.100  32.907  3.685   1.00 24.32 ? 211 VAL B CG1   1 
ATOM   4906 C  CG2   . VAL B 1 232 ? 28.998  31.789  4.951   1.00 24.38 ? 211 VAL B CG2   1 
ATOM   4907 N  N     . GLY B 1 233 ? 24.373  30.859  4.276   1.00 20.22 ? 212 GLY B N     1 
ATOM   4908 C  CA    . GLY B 1 233 ? 23.143  30.667  3.476   1.00 19.87 ? 212 GLY B CA    1 
ATOM   4909 C  C     . GLY B 1 233 ? 22.372  29.406  3.856   1.00 19.55 ? 212 GLY B C     1 
ATOM   4910 O  O     . GLY B 1 233 ? 21.204  29.246  3.425   1.00 20.30 ? 212 GLY B O     1 
ATOM   4911 N  N     . GLY B 1 234 ? 23.014  28.522  4.616   1.00 20.67 ? 213 GLY B N     1 
ATOM   4912 C  CA    . GLY B 1 234 ? 22.379  27.258  5.059   1.00 19.98 ? 213 GLY B CA    1 
ATOM   4913 C  C     . GLY B 1 234 ? 22.595  26.118  4.083   1.00 21.08 ? 213 GLY B C     1 
ATOM   4914 O  O     . GLY B 1 234 ? 23.254  26.300  3.023   1.00 19.84 ? 213 GLY B O     1 
ATOM   4915 N  N     . VAL B 1 235 ? 22.089  24.941  4.437   1.00 19.10 ? 214 VAL B N     1 
ATOM   4916 C  CA    . VAL B 1 235 ? 22.435  23.694  3.697   1.00 18.91 ? 214 VAL B CA    1 
ATOM   4917 C  C     . VAL B 1 235 ? 21.477  23.455  2.527   1.00 20.32 ? 214 VAL B C     1 
ATOM   4918 O  O     . VAL B 1 235 ? 21.940  22.932  1.490   1.00 18.81 ? 214 VAL B O     1 
ATOM   4919 C  CB    . VAL B 1 235 ? 22.535  22.490  4.663   1.00 18.35 ? 214 VAL B CB    1 
ATOM   4920 C  CG1   . VAL B 1 235 ? 22.927  21.227  3.907   1.00 21.98 ? 214 VAL B CG1   1 
ATOM   4921 C  CG2   . VAL B 1 235 ? 23.562  22.763  5.743   1.00 19.77 ? 214 VAL B CG2   1 
ATOM   4922 N  N     . GLN B 1 236 ? 20.182  23.759  2.618   1.00 18.97 ? 215 GLN B N     1 
ATOM   4923 C  CA    . GLN B 1 236 ? 19.272  23.456  1.481   1.00 21.47 ? 215 GLN B CA    1 
ATOM   4924 C  C     . GLN B 1 236 ? 19.712  24.150  0.171   1.00 23.67 ? 215 GLN B C     1 
ATOM   4925 O  O     . GLN B 1 236 ? 19.647  23.519  -0.926  1.00 21.58 ? 215 GLN B O     1 
ATOM   4926 C  CB    . GLN B 1 236 ? 17.834  23.803  1.826   1.00 22.00 ? 215 GLN B CB    1 
ATOM   4927 C  CG    . GLN B 1 236 ? 16.828  23.310  0.808   1.00 22.70 ? 215 GLN B CG    1 
ATOM   4928 C  CD    . GLN B 1 236 ? 15.436  23.799  1.159   1.00 22.45 ? 215 GLN B CD    1 
ATOM   4929 O  OE1   . GLN B 1 236 ? 15.014  23.726  2.301   1.00 23.94 ? 215 GLN B OE1   1 
ATOM   4930 N  NE2   . GLN B 1 236 ? 14.690  24.283  0.169   1.00 25.09 ? 215 GLN B NE2   1 
ATOM   4931 N  N     . PRO B 1 237 ? 20.238  25.387  0.197   1.00 21.65 ? 216 PRO B N     1 
ATOM   4932 C  CA    . PRO B 1 237 ? 20.788  25.993  -1.029  1.00 22.34 ? 216 PRO B CA    1 
ATOM   4933 C  C     . PRO B 1 237 ? 21.904  25.157  -1.673  1.00 22.43 ? 216 PRO B C     1 
ATOM   4934 O  O     . PRO B 1 237 ? 22.004  25.134  -2.907  1.00 22.91 ? 216 PRO B O     1 
ATOM   4935 C  CB    . PRO B 1 237 ? 21.315  27.338  -0.521  1.00 22.86 ? 216 PRO B CB    1 
ATOM   4936 C  CG    . PRO B 1 237 ? 20.303  27.657  0.536   1.00 22.20 ? 216 PRO B CG    1 
ATOM   4937 C  CD    . PRO B 1 237 ? 20.197  26.350  1.311   1.00 20.35 ? 216 PRO B CD    1 
ATOM   4938 N  N     . LEU B 1 238 ? 22.699  24.446  -0.868  1.00 19.94 ? 217 LEU B N     1 
ATOM   4939 C  CA    . LEU B 1 238 ? 23.739  23.556  -1.454  1.00 19.50 ? 217 LEU B CA    1 
ATOM   4940 C  C     . LEU B 1 238 ? 23.012  22.469  -2.252  1.00 20.67 ? 217 LEU B C     1 
ATOM   4941 O  O     . LEU B 1 238 ? 23.439  22.167  -3.407  1.00 20.02 ? 217 LEU B O     1 
ATOM   4942 C  CB    . LEU B 1 238 ? 24.660  22.941  -0.397  1.00 21.84 ? 217 LEU B CB    1 
ATOM   4943 C  CG    . LEU B 1 238 ? 25.802  22.070  -0.910  1.00 22.77 ? 217 LEU B CG    1 
ATOM   4944 C  CD1   . LEU B 1 238 ? 26.723  22.802  -1.911  1.00 23.79 ? 217 LEU B CD1   1 
ATOM   4945 C  CD2   . LEU B 1 238 ? 26.614  21.564  0.258   1.00 24.07 ? 217 LEU B CD2   1 
ATOM   4946 N  N     . ALA B 1 239 ? 21.997  21.834  -1.659  1.00 19.95 ? 218 ALA B N     1 
ATOM   4947 C  CA    . ALA B 1 239 ? 21.244  20.758  -2.349  1.00 20.26 ? 218 ALA B CA    1 
ATOM   4948 C  C     . ALA B 1 239 ? 20.620  21.333  -3.620  1.00 20.71 ? 218 ALA B C     1 
ATOM   4949 O  O     . ALA B 1 239 ? 20.552  20.634  -4.654  1.00 20.37 ? 218 ALA B O     1 
ATOM   4950 C  CB    . ALA B 1 239 ? 20.183  20.145  -1.458  1.00 19.90 ? 218 ALA B CB    1 
ATOM   4951 N  N     . GLU B 1 240 ? 20.103  22.555  -3.550  1.00 20.69 ? 219 GLU B N     1 
ATOM   4952 C  CA    . GLU B 1 240 ? 19.503  23.230  -4.732  1.00 21.70 ? 219 GLU B CA    1 
ATOM   4953 C  C     . GLU B 1 240 ? 20.539  23.473  -5.837  1.00 21.81 ? 219 GLU B C     1 
ATOM   4954 O  O     . GLU B 1 240 ? 20.179  23.260  -7.048  1.00 22.56 ? 219 GLU B O     1 
ATOM   4955 C  CB    . GLU B 1 240 ? 18.765  24.493  -4.286  1.00 24.51 ? 219 GLU B CB    1 
ATOM   4956 C  CG    . GLU B 1 240 ? 17.493  24.127  -3.581  1.00 26.51 ? 219 GLU B CG    1 
ATOM   4957 C  CD    . GLU B 1 240 ? 16.752  25.261  -2.920  1.00 27.71 ? 219 GLU B CD    1 
ATOM   4958 O  OE1   . GLU B 1 240 ? 15.587  25.042  -2.574  1.00 29.07 ? 219 GLU B OE1   1 
ATOM   4959 O  OE2   . GLU B 1 240 ? 17.357  26.334  -2.749  1.00 31.46 ? 219 GLU B OE2   1 
ATOM   4960 N  N     . ARG B 1 241 ? 21.762  23.846  -5.492  1.00 21.23 ? 220 ARG B N     1 
ATOM   4961 C  CA    . ARG B 1 241 ? 22.849  23.999  -6.504  1.00 22.87 ? 220 ARG B CA    1 
ATOM   4962 C  C     . ARG B 1 241 ? 23.222  22.638  -7.112  1.00 22.82 ? 220 ARG B C     1 
ATOM   4963 O  O     . ARG B 1 241 ? 23.550  22.574  -8.336  1.00 22.07 ? 220 ARG B O     1 
ATOM   4964 C  CB    . ARG B 1 241 ? 24.058  24.671  -5.870  1.00 22.67 ? 220 ARG B CB    1 
ATOM   4965 C  CG    . ARG B 1 241 ? 23.812  26.127  -5.502  1.00 24.11 ? 220 ARG B CG    1 
ATOM   4966 C  CD    . ARG B 1 241 ? 24.916  26.710  -4.643  1.00 27.21 ? 220 ARG B CD    1 
ATOM   4967 N  NE    . ARG B 1 241 ? 24.581  28.092  -4.291  1.00 26.92 ? 220 ARG B NE    1 
ATOM   4968 C  CZ    . ARG B 1 241 ? 25.389  29.156  -4.410  1.00 28.49 ? 220 ARG B CZ    1 
ATOM   4969 N  NH1   . ARG B 1 241 ? 26.631  29.039  -4.850  1.00 29.39 ? 220 ARG B NH1   1 
ATOM   4970 N  NH2   . ARG B 1 241 ? 24.932  30.363  -4.107  1.00 30.35 ? 220 ARG B NH2   1 
ATOM   4971 N  N     . LEU B 1 242 ? 23.215  21.566  -6.300  1.00 21.20 ? 221 LEU B N     1 
ATOM   4972 C  CA    . LEU B 1 242 ? 23.490  20.207  -6.820  1.00 20.63 ? 221 LEU B CA    1 
ATOM   4973 C  C     . LEU B 1 242 ? 22.359  19.790  -7.765  1.00 21.56 ? 221 LEU B C     1 
ATOM   4974 O  O     . LEU B 1 242 ? 22.669  19.282  -8.865  1.00 22.10 ? 221 LEU B O     1 
ATOM   4975 C  CB    . LEU B 1 242 ? 23.713  19.234  -5.644  1.00 21.79 ? 221 LEU B CB    1 
ATOM   4976 C  CG    . LEU B 1 242 ? 23.845  17.767  -6.044  1.00 22.29 ? 221 LEU B CG    1 
ATOM   4977 C  CD1   . LEU B 1 242 ? 25.019  17.579  -6.992  1.00 23.13 ? 221 LEU B CD1   1 
ATOM   4978 C  CD2   . LEU B 1 242 ? 23.984  16.887  -4.813  1.00 22.13 ? 221 LEU B CD2   1 
ATOM   4979 N  N     . ALA B 1 243 ? 21.095  20.075  -7.438  1.00 21.57 ? 222 ALA B N     1 
ATOM   4980 C  CA    . ALA B 1 243 ? 19.953  19.726  -8.306  1.00 22.71 ? 222 ALA B CA    1 
ATOM   4981 C  C     . ALA B 1 243 ? 20.085  20.499  -9.636  1.00 25.63 ? 222 ALA B C     1 
ATOM   4982 O  O     . ALA B 1 243 ? 19.789  19.922  -10.690 1.00 23.57 ? 222 ALA B O     1 
ATOM   4983 C  CB    . ALA B 1 243 ? 18.641  20.022  -7.636  1.00 23.05 ? 222 ALA B CB    1 
ATOM   4984 N  N     . ALA B 1 244 ? 20.609  21.720  -9.591  1.00 23.01 ? 223 ALA B N     1 
ATOM   4985 C  CA    . ALA B 1 244 ? 20.745  22.587  -10.789 1.00 23.52 ? 223 ALA B CA    1 
ATOM   4986 C  C     . ALA B 1 244 ? 21.782  21.978  -11.745 1.00 26.05 ? 223 ALA B C     1 
ATOM   4987 O  O     . ALA B 1 244 ? 21.810  22.417  -12.883 1.00 28.26 ? 223 ALA B O     1 
ATOM   4988 C  CB    . ALA B 1 244 ? 21.112  23.987  -10.398 1.00 26.68 ? 223 ALA B CB    1 
ATOM   4989 N  N     . ARG B 1 245 ? 22.569  20.974  -11.339 1.00 25.07 ? 224 ARG B N     1 
ATOM   4990 C  CA    . ARG B 1 245 ? 23.543  20.317  -12.240 1.00 27.02 ? 224 ARG B CA    1 
ATOM   4991 C  C     . ARG B 1 245 ? 22.827  19.278  -13.112 1.00 27.96 ? 224 ARG B C     1 
ATOM   4992 O  O     . ARG B 1 245 ? 23.479  18.780  -14.040 1.00 29.83 ? 224 ARG B O     1 
ATOM   4993 C  CB    . ARG B 1 245 ? 24.725  19.742  -11.462 1.00 30.59 ? 224 ARG B CB    1 
ATOM   4994 C  CG    . ARG B 1 245 ? 25.634  20.786  -10.819 1.00 34.08 ? 224 ARG B CG    1 
ATOM   4995 C  CD    . ARG B 1 245 ? 26.296  21.658  -11.859 1.00 37.55 ? 224 ARG B CD    1 
ATOM   4996 N  NE    . ARG B 1 245 ? 26.947  22.861  -11.357 1.00 40.66 ? 224 ARG B NE    1 
ATOM   4997 C  CZ    . ARG B 1 245 ? 28.268  23.004  -11.233 1.00 44.28 ? 224 ARG B CZ    1 
ATOM   4998 N  NH1   . ARG B 1 245 ? 29.076  21.988  -11.485 1.00 44.70 ? 224 ARG B NH1   1 
ATOM   4999 N  NH2   . ARG B 1 245 ? 28.786  24.152  -10.821 1.00 45.87 ? 224 ARG B NH2   1 
ATOM   5000 N  N     . LEU B 1 246 ? 21.550  18.972  -12.862 1.00 23.88 ? 225 LEU B N     1 
ATOM   5001 C  CA    . LEU B 1 246 ? 20.768  18.014  -13.688 1.00 26.14 ? 225 LEU B CA    1 
ATOM   5002 C  C     . LEU B 1 246 ? 20.169  18.762  -14.867 1.00 25.77 ? 225 LEU B C     1 
ATOM   5003 O  O     . LEU B 1 246 ? 19.891  19.953  -14.786 1.00 26.33 ? 225 LEU B O     1 
ATOM   5004 C  CB    . LEU B 1 246 ? 19.668  17.356  -12.848 1.00 25.91 ? 225 LEU B CB    1 
ATOM   5005 C  CG    . LEU B 1 246 ? 20.149  16.686  -11.560 1.00 26.67 ? 225 LEU B CG    1 
ATOM   5006 C  CD1   . LEU B 1 246 ? 18.960  16.163  -10.763 1.00 25.28 ? 225 LEU B CD1   1 
ATOM   5007 C  CD2   . LEU B 1 246 ? 21.139  15.565  -11.859 1.00 28.25 ? 225 LEU B CD2   1 
ATOM   5008 N  N     . PRO B 1 247 ? 19.928  18.077  -15.996 1.00 28.26 ? 226 PRO B N     1 
ATOM   5009 C  CA    . PRO B 1 247 ? 19.254  18.719  -17.117 1.00 29.86 ? 226 PRO B CA    1 
ATOM   5010 C  C     . PRO B 1 247 ? 17.783  19.060  -16.820 1.00 30.62 ? 226 PRO B C     1 
ATOM   5011 O  O     . PRO B 1 247 ? 17.154  18.503  -15.919 1.00 24.85 ? 226 PRO B O     1 
ATOM   5012 C  CB    . PRO B 1 247 ? 19.407  17.683  -18.251 1.00 32.03 ? 226 PRO B CB    1 
ATOM   5013 C  CG    . PRO B 1 247 ? 19.601  16.344  -17.561 1.00 33.08 ? 226 PRO B CG    1 
ATOM   5014 C  CD    . PRO B 1 247 ? 20.229  16.655  -16.213 1.00 29.45 ? 226 PRO B CD    1 
ATOM   5015 N  N     . ASP B 1 248 ? 17.247  20.021  -17.559 1.00 30.63 ? 227 ASP B N     1 
ATOM   5016 C  CA    . ASP B 1 248 ? 15.842  20.483  -17.439 1.00 35.14 ? 227 ASP B CA    1 
ATOM   5017 C  C     . ASP B 1 248 ? 14.912  19.265  -17.568 1.00 34.21 ? 227 ASP B C     1 
ATOM   5018 O  O     . ASP B 1 248 ? 15.154  18.434  -18.466 1.00 36.42 ? 227 ASP B O     1 
ATOM   5019 C  CB    . ASP B 1 248 ? 15.536  21.540  -18.515 1.00 40.67 ? 227 ASP B CB    1 
ATOM   5020 C  CG    . ASP B 1 248 ? 14.114  22.096  -18.459 1.00 48.84 ? 227 ASP B CG    1 
ATOM   5021 O  OD1   . ASP B 1 248 ? 13.752  22.645  -17.414 1.00 53.89 ? 227 ASP B OD1   1 
ATOM   5022 O  OD2   . ASP B 1 248 ? 13.365  21.960  -19.458 1.00 55.62 ? 227 ASP B OD2   1 
ATOM   5023 N  N     . GLY B 1 249 ? 13.886  19.156  -16.724 1.00 33.81 ? 228 GLY B N     1 
ATOM   5024 C  CA    . GLY B 1 249 ? 12.913  18.044  -16.766 1.00 30.38 ? 228 GLY B CA    1 
ATOM   5025 C  C     . GLY B 1 249 ? 13.330  16.806  -15.973 1.00 28.42 ? 228 GLY B C     1 
ATOM   5026 O  O     . GLY B 1 249 ? 12.500  15.915  -15.874 1.00 31.91 ? 228 GLY B O     1 
ATOM   5027 N  N     . ALA B 1 250 ? 14.560  16.713  -15.470 1.00 26.20 ? 229 ALA B N     1 
ATOM   5028 C  CA    . ALA B 1 250 ? 15.048  15.502  -14.764 1.00 25.29 ? 229 ALA B CA    1 
ATOM   5029 C  C     . ALA B 1 250 ? 14.420  15.435  -13.366 1.00 25.11 ? 229 ALA B C     1 
ATOM   5030 O  O     . ALA B 1 250 ? 14.051  14.341  -12.918 1.00 27.38 ? 229 ALA B O     1 
ATOM   5031 C  CB    . ALA B 1 250 ? 16.557  15.490  -14.675 1.00 25.69 ? 229 ALA B CB    1 
ATOM   5032 N  N     . LEU B 1 251 ? 14.304  16.568  -12.673 1.00 23.85 ? 230 LEU B N     1 
ATOM   5033 C  CA    . LEU B 1 251 ? 13.784  16.566  -11.284 1.00 23.87 ? 230 LEU B CA    1 
ATOM   5034 C  C     . LEU B 1 251 ? 12.262  16.720  -11.333 1.00 24.62 ? 230 LEU B C     1 
ATOM   5035 O  O     . LEU B 1 251 ? 11.791  17.665  -11.948 1.00 26.19 ? 230 LEU B O     1 
ATOM   5036 C  CB    . LEU B 1 251 ? 14.482  17.702  -10.534 1.00 24.14 ? 230 LEU B CB    1 
ATOM   5037 C  CG    . LEU B 1 251 ? 13.941  17.943  -9.144  1.00 22.85 ? 230 LEU B CG    1 
ATOM   5038 C  CD1   . LEU B 1 251 ? 14.225  16.726  -8.262  1.00 23.62 ? 230 LEU B CD1   1 
ATOM   5039 C  CD2   . LEU B 1 251 ? 14.587  19.183  -8.538  1.00 27.04 ? 230 LEU B CD2   1 
ATOM   5040 N  N     . ARG B 1 252 ? 11.505  15.856  -10.665 1.00 23.33 ? 231 ARG B N     1 
ATOM   5041 C  CA    . ARG B 1 252 ? 10.036  15.974  -10.543 1.00 24.37 ? 231 ARG B CA    1 
ATOM   5042 C  C     . ARG B 1 252 ? 9.666   16.133  -9.081  1.00 25.03 ? 231 ARG B C     1 
ATOM   5043 O  O     . ARG B 1 252 ? 9.668   15.107  -8.354  1.00 21.99 ? 231 ARG B O     1 
ATOM   5044 C  CB    . ARG B 1 252 ? 9.336   14.736  -11.113 1.00 30.15 ? 231 ARG B CB    1 
ATOM   5045 C  CG    . ARG B 1 252 ? 9.783   14.368  -12.517 1.00 35.43 ? 231 ARG B CG    1 
ATOM   5046 C  CD    . ARG B 1 252 ? 9.242   15.352  -13.533 1.00 40.72 ? 231 ARG B CD    1 
ATOM   5047 N  NE    . ARG B 1 252 ? 9.799   15.071  -14.844 1.00 42.74 ? 231 ARG B NE    1 
ATOM   5048 C  CZ    . ARG B 1 252 ? 9.328   14.167  -15.694 1.00 43.60 ? 231 ARG B CZ    1 
ATOM   5049 N  NH1   . ARG B 1 252 ? 8.268   13.442  -15.389 1.00 38.26 ? 231 ARG B NH1   1 
ATOM   5050 N  NH2   . ARG B 1 252 ? 9.934   13.990  -16.859 1.00 46.12 ? 231 ARG B NH2   1 
ATOM   5051 N  N     . LEU B 1 253 ? 9.363   17.368  -8.658  1.00 23.07 ? 232 LEU B N     1 
ATOM   5052 C  CA    . LEU B 1 253 ? 8.974   17.622  -7.251  1.00 22.35 ? 232 LEU B CA    1 
ATOM   5053 C  C     . LEU B 1 253 ? 7.513   17.250  -7.061  1.00 22.73 ? 232 LEU B C     1 
ATOM   5054 O  O     . LEU B 1 253 ? 6.805   17.043  -8.066  1.00 22.82 ? 232 LEU B O     1 
ATOM   5055 C  CB    . LEU B 1 253 ? 9.258   19.080  -6.849  1.00 21.67 ? 232 LEU B CB    1 
ATOM   5056 C  CG    . LEU B 1 253 ? 10.702  19.557  -6.970  1.00 22.89 ? 232 LEU B CG    1 
ATOM   5057 C  CD1   . LEU B 1 253 ? 10.795  21.056  -6.703  1.00 25.95 ? 232 LEU B CD1   1 
ATOM   5058 C  CD2   . LEU B 1 253 ? 11.598  18.819  -5.996  1.00 23.60 ? 232 LEU B CD2   1 
ATOM   5059 N  N     . SER B 1 254 ? 7.105   17.085  -5.804  1.00 20.20 ? 233 SER B N     1 
ATOM   5060 C  CA    . SER B 1 254 ? 5.707   16.859  -5.410  1.00 22.43 ? 233 SER B CA    1 
ATOM   5061 C  C     . SER B 1 254 ? 5.239   15.618  -6.144  1.00 22.85 ? 233 SER B C     1 
ATOM   5062 O  O     . SER B 1 254 ? 4.090   15.612  -6.599  1.00 21.12 ? 233 SER B O     1 
ATOM   5063 C  CB    . SER B 1 254 ? 4.837   18.075  -5.711  1.00 23.80 ? 233 SER B CB    1 
ATOM   5064 O  OG    . SER B 1 254 ? 5.331   19.191  -4.992  1.00 30.24 ? 233 SER B OG    1 
ATOM   5065 N  N     . THR B 1 255 ? 6.106   14.610  -6.247  1.00 21.26 ? 234 THR B N     1 
ATOM   5066 C  CA    . THR B 1 255 ? 5.772   13.340  -6.943  1.00 21.73 ? 234 THR B CA    1 
ATOM   5067 C  C     . THR B 1 255 ? 6.199   12.159  -6.074  1.00 21.22 ? 234 THR B C     1 
ATOM   5068 O  O     . THR B 1 255 ? 7.215   11.534  -6.345  1.00 22.11 ? 234 THR B O     1 
ATOM   5069 C  CB    . THR B 1 255 ? 6.433   13.325  -8.319  1.00 21.47 ? 234 THR B CB    1 
ATOM   5070 O  OG1   . THR B 1 255 ? 6.081   14.551  -8.956  1.00 22.56 ? 234 THR B OG1   1 
ATOM   5071 C  CG2   . THR B 1 255 ? 5.946   12.183  -9.190  1.00 23.28 ? 234 THR B CG2   1 
ATOM   5072 N  N     . PRO B 1 256 ? 5.457   11.836  -4.999  1.00 21.09 ? 235 PRO B N     1 
ATOM   5073 C  CA    . PRO B 1 256 ? 5.784   10.676  -4.184  1.00 21.73 ? 235 PRO B CA    1 
ATOM   5074 C  C     . PRO B 1 256 ? 5.742   9.391   -5.014  1.00 20.49 ? 235 PRO B C     1 
ATOM   5075 O  O     . PRO B 1 256 ? 4.835   9.230   -5.796  1.00 20.96 ? 235 PRO B O     1 
ATOM   5076 C  CB    . PRO B 1 256 ? 4.685   10.657  -3.118  1.00 23.40 ? 235 PRO B CB    1 
ATOM   5077 C  CG    . PRO B 1 256 ? 4.154   12.066  -3.077  1.00 22.38 ? 235 PRO B CG    1 
ATOM   5078 C  CD    . PRO B 1 256 ? 4.286   12.571  -4.496  1.00 21.87 ? 235 PRO B CD    1 
ATOM   5079 N  N     . VAL B 1 257 ? 6.665   8.469   -4.742  1.00 20.18 ? 236 VAL B N     1 
ATOM   5080 C  CA    . VAL B 1 257 ? 6.634   7.123   -5.374  1.00 20.32 ? 236 VAL B CA    1 
ATOM   5081 C  C     . VAL B 1 257 ? 5.800   6.201   -4.487  1.00 21.05 ? 236 VAL B C     1 
ATOM   5082 O  O     . VAL B 1 257 ? 6.151   6.068   -3.330  1.00 20.25 ? 236 VAL B O     1 
ATOM   5083 C  CB    . VAL B 1 257 ? 8.052   6.590   -5.591  1.00 19.25 ? 236 VAL B CB    1 
ATOM   5084 C  CG1   . VAL B 1 257 ? 8.043   5.129   -5.955  1.00 19.95 ? 236 VAL B CG1   1 
ATOM   5085 C  CG2   . VAL B 1 257 ? 8.766   7.433   -6.639  1.00 19.25 ? 236 VAL B CG2   1 
ATOM   5086 N  N     . ARG B 1 258 ? 4.805   5.529   -5.064  1.00 20.01 ? 237 ARG B N     1 
ATOM   5087 C  CA    . ARG B 1 258 ? 3.871   4.641   -4.341  1.00 20.32 ? 237 ARG B CA    1 
ATOM   5088 C  C     . ARG B 1 258 ? 4.239   3.179   -4.575  1.00 20.25 ? 237 ARG B C     1 
ATOM   5089 O  O     . ARG B 1 258 ? 4.040   2.376   -3.674  1.00 20.77 ? 237 ARG B O     1 
ATOM   5090 C  CB    . ARG B 1 258 ? 2.467   4.924   -4.869  1.00 24.03 ? 237 ARG B CB    1 
ATOM   5091 C  CG    . ARG B 1 258 ? 1.878   6.246   -4.409  1.00 27.13 ? 237 ARG B CG    1 
ATOM   5092 C  CD    . ARG B 1 258 ? 0.440   6.287   -4.896  1.00 32.29 ? 237 ARG B CD    1 
ATOM   5093 N  NE    . ARG B 1 258 ? -0.246  7.441   -4.315  1.00 37.50 ? 237 ARG B NE    1 
ATOM   5094 C  CZ    . ARG B 1 258 ? -1.494  7.797   -4.569  1.00 34.81 ? 237 ARG B CZ    1 
ATOM   5095 N  NH1   . ARG B 1 258 ? -2.224  7.108   -5.428  1.00 36.86 ? 237 ARG B NH1   1 
ATOM   5096 N  NH2   . ARG B 1 258 ? -1.984  8.886   -4.005  1.00 37.90 ? 237 ARG B NH2   1 
ATOM   5097 N  N     . GLY B 1 259 ? 4.791   2.866   -5.738  1.00 20.78 ? 238 GLY B N     1 
ATOM   5098 C  CA    . GLY B 1 259 ? 4.988   1.473   -6.187  1.00 19.14 ? 238 GLY B CA    1 
ATOM   5099 C  C     . GLY B 1 259 ? 6.223   1.320   -7.030  1.00 19.74 ? 238 GLY B C     1 
ATOM   5100 O  O     . GLY B 1 259 ? 6.591   2.266   -7.744  1.00 17.79 ? 238 GLY B O     1 
ATOM   5101 N  N     . LEU B 1 260 ? 6.852   0.143   -6.976  1.00 18.53 ? 239 LEU B N     1 
ATOM   5102 C  CA    . LEU B 1 260 ? 8.086   -0.138  -7.747  1.00 20.44 ? 239 LEU B CA    1 
ATOM   5103 C  C     . LEU B 1 260 ? 7.972   -1.599  -8.180  1.00 19.67 ? 239 LEU B C     1 
ATOM   5104 O  O     . LEU B 1 260 ? 8.056   -2.474  -7.305  1.00 19.71 ? 239 LEU B O     1 
ATOM   5105 C  CB    . LEU B 1 260 ? 9.299   0.096   -6.836  1.00 24.74 ? 239 LEU B CB    1 
ATOM   5106 C  CG    . LEU B 1 260 ? 10.600  0.531   -7.478  1.00 29.52 ? 239 LEU B CG    1 
ATOM   5107 C  CD1   . LEU B 1 260 ? 10.416  1.851   -8.229  1.00 31.49 ? 239 LEU B CD1   1 
ATOM   5108 C  CD2   . LEU B 1 260 ? 11.666  0.707   -6.417  1.00 28.97 ? 239 LEU B CD2   1 
ATOM   5109 N  N     . ALA B 1 261 ? 7.645   -1.821  -9.444  1.00 20.68 ? 240 ALA B N     1 
ATOM   5110 C  CA    . ALA B 1 261 ? 7.408   -3.152  -10.021 1.00 20.11 ? 240 ALA B CA    1 
ATOM   5111 C  C     . ALA B 1 261 ? 8.625   -3.474  -10.881 1.00 22.46 ? 240 ALA B C     1 
ATOM   5112 O  O     . ALA B 1 261 ? 9.191   -2.530  -11.484 1.00 29.73 ? 240 ALA B O     1 
ATOM   5113 C  CB    . ALA B 1 261 ? 6.121   -3.168  -10.792 1.00 23.35 ? 240 ALA B CB    1 
ATOM   5114 N  N     . GLN B 1 262 ? 9.119   -4.700  -10.864 1.00 19.50 ? 241 GLN B N     1 
ATOM   5115 C  CA    . GLN B 1 262 ? 10.277  -4.959  -11.745 1.00 20.72 ? 241 GLN B CA    1 
ATOM   5116 C  C     . GLN B 1 262 ? 10.084  -6.301  -12.421 1.00 22.40 ? 241 GLN B C     1 
ATOM   5117 O  O     . GLN B 1 262 ? 9.362   -7.140  -11.876 1.00 20.36 ? 241 GLN B O     1 
ATOM   5118 C  CB    . GLN B 1 262 ? 11.599  -4.934  -10.999 1.00 19.56 ? 241 GLN B CB    1 
ATOM   5119 C  CG    . GLN B 1 262 ? 11.712  -5.962  -9.865  1.00 19.75 ? 241 GLN B CG    1 
ATOM   5120 C  CD    . GLN B 1 262 ? 13.117  -5.890  -9.297  1.00 23.14 ? 241 GLN B CD    1 
ATOM   5121 O  OE1   . GLN B 1 262 ? 14.114  -5.922  -10.020 1.00 22.14 ? 241 GLN B OE1   1 
ATOM   5122 N  NE2   . GLN B 1 262 ? 13.236  -5.750  -7.989  1.00 22.50 ? 241 GLN B NE2   1 
ATOM   5123 N  N     . ASP B 1 263 ? 10.821  -6.486  -13.506 1.00 23.04 ? 242 ASP B N     1 
ATOM   5124 C  CA    . ASP B 1 263 ? 10.831  -7.758  -14.258 1.00 25.27 ? 242 ASP B CA    1 
ATOM   5125 C  C     . ASP B 1 263 ? 12.248  -7.943  -14.788 1.00 26.29 ? 242 ASP B C     1 
ATOM   5126 O  O     . ASP B 1 263 ? 13.168  -7.170  -14.389 1.00 26.46 ? 242 ASP B O     1 
ATOM   5127 C  CB    . ASP B 1 263 ? 9.733   -7.772  -15.330 1.00 28.77 ? 242 ASP B CB    1 
ATOM   5128 C  CG    . ASP B 1 263 ? 9.863   -6.731  -16.432 1.00 32.71 ? 242 ASP B CG    1 
ATOM   5129 O  OD1   . ASP B 1 263 ? 10.936  -6.109  -16.581 1.00 31.52 ? 242 ASP B OD1   1 
ATOM   5130 O  OD2   . ASP B 1 263 ? 8.882   -6.537  -17.155 1.00 42.98 ? 242 ASP B OD2   1 
ATOM   5131 N  N     . GLY B 1 264 ? 12.405  -8.837  -15.759 1.00 25.78 ? 243 GLY B N     1 
ATOM   5132 C  CA    . GLY B 1 264 ? 13.743  -9.172  -16.247 1.00 28.70 ? 243 GLY B CA    1 
ATOM   5133 C  C     . GLY B 1 264 ? 14.392  -8.021  -16.987 1.00 31.09 ? 243 GLY B C     1 
ATOM   5134 O  O     . GLY B 1 264 ? 15.624  -8.064  -17.110 1.00 38.36 ? 243 GLY B O     1 
ATOM   5135 N  N     . ASP B 1 265 ? 13.623  -7.042  -17.486 1.00 29.11 ? 244 ASP B N     1 
ATOM   5136 C  CA    . ASP B 1 265 ? 14.144  -6.021  -18.446 1.00 33.08 ? 244 ASP B CA    1 
ATOM   5137 C  C     . ASP B 1 265 ? 14.134  -4.613  -17.833 1.00 28.56 ? 244 ASP B C     1 
ATOM   5138 O  O     . ASP B 1 265 ? 14.864  -3.726  -18.334 1.00 28.34 ? 244 ASP B O     1 
ATOM   5139 C  CB    . ASP B 1 265 ? 13.370  -6.097  -19.769 1.00 36.49 ? 244 ASP B CB    1 
ATOM   5140 C  CG    . ASP B 1 265 ? 13.396  -7.503  -20.370 1.00 42.45 ? 244 ASP B CG    1 
ATOM   5141 O  OD1   . ASP B 1 265 ? 14.447  -8.175  -20.251 1.00 46.12 ? 244 ASP B OD1   1 
ATOM   5142 O  OD2   . ASP B 1 265 ? 12.338  -7.954  -20.847 1.00 49.36 ? 244 ASP B OD2   1 
ATOM   5143 N  N     . GLY B 1 266 ? 13.376  -4.377  -16.764 1.00 25.79 ? 245 GLY B N     1 
ATOM   5144 C  CA    . GLY B 1 266 ? 13.356  -3.023  -16.172 1.00 23.67 ? 245 GLY B CA    1 
ATOM   5145 C  C     . GLY B 1 266 ? 12.476  -2.940  -14.949 1.00 23.36 ? 245 GLY B C     1 
ATOM   5146 O  O     . GLY B 1 266 ? 12.030  -3.990  -14.419 1.00 23.12 ? 245 GLY B O     1 
ATOM   5147 N  N     . VAL B 1 267 ? 12.217  -1.700  -14.556 1.00 23.28 ? 246 VAL B N     1 
ATOM   5148 C  CA    . VAL B 1 267 ? 11.420  -1.336  -13.364 1.00 22.94 ? 246 VAL B CA    1 
ATOM   5149 C  C     . VAL B 1 267 ? 10.336  -0.355  -13.833 1.00 23.96 ? 246 VAL B C     1 
ATOM   5150 O  O     . VAL B 1 267 ? 10.596  0.472   -14.710 1.00 27.73 ? 246 VAL B O     1 
ATOM   5151 C  CB    . VAL B 1 267 ? 12.320  -0.751  -12.253 1.00 25.46 ? 246 VAL B CB    1 
ATOM   5152 C  CG1   . VAL B 1 267 ? 13.455  -1.687  -11.893 1.00 23.26 ? 246 VAL B CG1   1 
ATOM   5153 C  CG2   . VAL B 1 267 ? 12.897  0.602   -12.636 1.00 32.16 ? 246 VAL B CG2   1 
ATOM   5154 N  N     . THR B 1 268 ? 9.147   -0.484  -13.295 1.00 20.63 ? 247 THR B N     1 
ATOM   5155 C  CA    . THR B 1 268 ? 8.032   0.453   -13.530 1.00 20.07 ? 247 THR B CA    1 
ATOM   5156 C  C     . THR B 1 268 ? 7.731   1.161   -12.210 1.00 21.12 ? 247 THR B C     1 
ATOM   5157 O  O     . THR B 1 268 ? 7.376   0.487   -11.235 1.00 19.47 ? 247 THR B O     1 
ATOM   5158 C  CB    . THR B 1 268 ? 6.787   -0.261  -14.043 1.00 22.82 ? 247 THR B CB    1 
ATOM   5159 O  OG1   . THR B 1 268 ? 7.195   -0.857  -15.267 1.00 25.06 ? 247 THR B OG1   1 
ATOM   5160 C  CG2   . THR B 1 268 ? 5.628   0.682   -14.266 1.00 23.47 ? 247 THR B CG2   1 
ATOM   5161 N  N     . VAL B 1 269 ? 7.874   2.460   -12.207 1.00 20.73 ? 248 VAL B N     1 
ATOM   5162 C  CA    . VAL B 1 269 ? 7.669   3.299   -10.995 1.00 23.31 ? 248 VAL B CA    1 
ATOM   5163 C  C     . VAL B 1 269 ? 6.244   3.846   -11.039 1.00 23.98 ? 248 VAL B C     1 
ATOM   5164 O  O     . VAL B 1 269 ? 5.907   4.515   -12.058 1.00 25.58 ? 248 VAL B O     1 
ATOM   5165 C  CB    . VAL B 1 269 ? 8.703   4.426   -10.949 1.00 26.78 ? 248 VAL B CB    1 
ATOM   5166 C  CG1   . VAL B 1 269 ? 8.607   5.165   -9.631  1.00 29.14 ? 248 VAL B CG1   1 
ATOM   5167 C  CG2   . VAL B 1 269 ? 10.107  3.895   -11.192 1.00 31.76 ? 248 VAL B CG2   1 
ATOM   5168 N  N     . ARG B 1 270 ? 5.443   3.588   -10.006 1.00 22.97 ? 249 ARG B N     1 
ATOM   5169 C  CA    . ARG B 1 270 ? 4.046   4.074   -9.927  1.00 23.13 ? 249 ARG B CA    1 
ATOM   5170 C  C     . ARG B 1 270 ? 3.973   5.313   -9.022  1.00 24.62 ? 249 ARG B C     1 
ATOM   5171 O  O     . ARG B 1 270 ? 4.405   5.206   -7.861  1.00 20.38 ? 249 ARG B O     1 
ATOM   5172 C  CB    . ARG B 1 270 ? 3.137   2.974   -9.379  1.00 26.50 ? 249 ARG B CB    1 
ATOM   5173 C  CG    . ARG B 1 270 ? 1.665   3.355   -9.245  1.00 32.17 ? 249 ARG B CG    1 
ATOM   5174 C  CD    . ARG B 1 270 ? 0.746   2.146   -9.014  1.00 32.18 ? 249 ARG B CD    1 
ATOM   5175 N  NE    . ARG B 1 270 ? 1.053   1.390   -7.792  1.00 36.28 ? 249 ARG B NE    1 
ATOM   5176 C  CZ    . ARG B 1 270 ? 0.672   1.739   -6.564  1.00 38.93 ? 249 ARG B CZ    1 
ATOM   5177 N  NH1   . ARG B 1 270 ? -0.007  2.860   -6.367  1.00 44.61 ? 249 ARG B NH1   1 
ATOM   5178 N  NH2   . ARG B 1 270 ? 0.987   0.980   -5.532  1.00 39.07 ? 249 ARG B NH2   1 
ATOM   5179 N  N     . THR B 1 271 ? 3.376   6.405   -9.517  1.00 22.53 ? 250 THR B N     1 
ATOM   5180 C  CA    . THR B 1 271 ? 3.016   7.625   -8.740  1.00 24.55 ? 250 THR B CA    1 
ATOM   5181 C  C     . THR B 1 271 ? 1.488   7.788   -8.773  1.00 25.27 ? 250 THR B C     1 
ATOM   5182 O  O     . THR B 1 271 ? 0.826   6.971   -9.455  1.00 25.30 ? 250 THR B O     1 
ATOM   5183 C  CB    . THR B 1 271 ? 3.692   8.867   -9.329  1.00 25.84 ? 250 THR B CB    1 
ATOM   5184 O  OG1   . THR B 1 271 ? 3.120   9.102   -10.609 1.00 23.28 ? 250 THR B OG1   1 
ATOM   5185 C  CG2   . THR B 1 271 ? 5.180   8.707   -9.499  1.00 25.64 ? 250 THR B CG2   1 
ATOM   5186 N  N     . ALA B 1 272 ? 0.909   8.811   -8.113  1.00 27.05 ? 251 ALA B N     1 
ATOM   5187 C  CA    . ALA B 1 272 ? -0.565  9.008   -8.064  1.00 29.38 ? 251 ALA B CA    1 
ATOM   5188 C  C     . ALA B 1 272 ? -1.154  9.112   -9.474  1.00 30.49 ? 251 ALA B C     1 
ATOM   5189 O  O     . ALA B 1 272 ? -2.250  8.574   -9.673  1.00 33.55 ? 251 ALA B O     1 
ATOM   5190 C  CB    . ALA B 1 272 ? -0.944  10.237  -7.267  1.00 31.23 ? 251 ALA B CB    1 
ATOM   5191 N  N     . GLY B 1 273 ? -0.477  9.832   -10.371 1.00 33.18 ? 252 GLY B N     1 
ATOM   5192 C  CA    . GLY B 1 273 ? -1.002  10.206  -11.693 1.00 35.52 ? 252 GLY B CA    1 
ATOM   5193 C  C     . GLY B 1 273 ? -0.515  9.299   -12.803 1.00 34.77 ? 252 GLY B C     1 
ATOM   5194 O  O     . GLY B 1 273 ? -1.146  9.293   -13.893 1.00 31.71 ? 252 GLY B O     1 
ATOM   5195 N  N     . GLY B 1 274 ? 0.579   8.577   -12.606 1.00 30.68 ? 253 GLY B N     1 
ATOM   5196 C  CA    . GLY B 1 274 ? 1.129   7.809   -13.737 1.00 31.53 ? 253 GLY B CA    1 
ATOM   5197 C  C     . GLY B 1 274 ? 2.211   6.839   -13.351 1.00 33.56 ? 253 GLY B C     1 
ATOM   5198 O  O     . GLY B 1 274 ? 2.316   6.438   -12.168 1.00 32.52 ? 253 GLY B O     1 
ATOM   5199 N  N     . GLU B 1 275 ? 3.025   6.517   -14.341 1.00 32.17 ? 254 GLU B N     1 
ATOM   5200 C  CA    . GLU B 1 275 ? 4.088   5.499   -14.240 1.00 29.88 ? 254 GLU B CA    1 
ATOM   5201 C  C     . GLU B 1 275 ? 5.278   6.033   -15.015 1.00 32.11 ? 254 GLU B C     1 
ATOM   5202 O  O     . GLU B 1 275 ? 5.045   6.739   -16.015 1.00 29.80 ? 254 GLU B O     1 
ATOM   5203 C  CB    . GLU B 1 275 ? 3.691   4.181   -14.889 1.00 34.56 ? 254 GLU B CB    1 
ATOM   5204 C  CG    . GLU B 1 275 ? 2.639   3.390   -14.140 1.00 39.73 ? 254 GLU B CG    1 
ATOM   5205 C  CD    . GLU B 1 275 ? 2.297   2.118   -14.896 1.00 42.10 ? 254 GLU B CD    1 
ATOM   5206 O  OE1   . GLU B 1 275 ? 1.581   1.271   -14.338 1.00 48.93 ? 254 GLU B OE1   1 
ATOM   5207 O  OE2   . GLU B 1 275 ? 2.805   1.971   -16.024 1.00 43.13 ? 254 GLU B OE2   1 
ATOM   5208 N  N     . VAL B 1 276 ? 6.479   5.651   -14.589 1.00 26.01 ? 255 VAL B N     1 
ATOM   5209 C  CA    . VAL B 1 276 ? 7.745   5.890   -15.322 1.00 28.75 ? 255 VAL B CA    1 
ATOM   5210 C  C     . VAL B 1 276 ? 8.386   4.520   -15.506 1.00 27.87 ? 255 VAL B C     1 
ATOM   5211 O  O     . VAL B 1 276 ? 8.408   3.766   -14.532 1.00 29.20 ? 255 VAL B O     1 
ATOM   5212 C  CB    . VAL B 1 276 ? 8.670   6.820   -14.508 1.00 30.85 ? 255 VAL B CB    1 
ATOM   5213 C  CG1   . VAL B 1 276 ? 10.014  7.048   -15.201 1.00 35.75 ? 255 VAL B CG1   1 
ATOM   5214 C  CG2   . VAL B 1 276 ? 7.999   8.128   -14.168 1.00 33.14 ? 255 VAL B CG2   1 
ATOM   5215 N  N     . ARG B 1 277 ? 8.938   4.249   -16.671 1.00 24.47 ? 256 ARG B N     1 
ATOM   5216 C  CA    . ARG B 1 277 ? 9.672   2.996   -16.951 1.00 26.34 ? 256 ARG B CA    1 
ATOM   5217 C  C     . ARG B 1 277 ? 11.165  3.331   -16.934 1.00 25.86 ? 256 ARG B C     1 
ATOM   5218 O  O     . ARG B 1 277 ? 11.572  4.375   -17.513 1.00 28.93 ? 256 ARG B O     1 
ATOM   5219 C  CB    . ARG B 1 277 ? 9.087   2.364   -18.221 1.00 28.87 ? 256 ARG B CB    1 
ATOM   5220 C  CG    . ARG B 1 277 ? 9.811   1.099   -18.668 1.00 37.00 ? 256 ARG B CG    1 
ATOM   5221 C  CD    . ARG B 1 277 ? 9.709   -0.013  -17.630 1.00 38.49 ? 256 ARG B CD    1 
ATOM   5222 N  NE    . ARG B 1 277 ? 10.244  -1.317  -17.988 1.00 38.62 ? 256 ARG B NE    1 
ATOM   5223 C  CZ    . ARG B 1 277 ? 9.889   -2.490  -17.430 1.00 40.42 ? 256 ARG B CZ    1 
ATOM   5224 N  NH1   . ARG B 1 277 ? 8.979   -2.549  -16.470 1.00 43.85 ? 256 ARG B NH1   1 
ATOM   5225 N  NH2   . ARG B 1 277 ? 10.446  -3.610  -17.833 1.00 37.48 ? 256 ARG B NH2   1 
ATOM   5226 N  N     . ALA B 1 278 ? 11.976  2.510   -16.251 1.00 24.65 ? 257 ALA B N     1 
ATOM   5227 C  CA    . ALA B 1 278 ? 13.443  2.659   -16.242 1.00 21.29 ? 257 ALA B CA    1 
ATOM   5228 C  C     . ALA B 1 278 ? 14.105  1.286   -16.373 1.00 20.64 ? 257 ALA B C     1 
ATOM   5229 O  O     . ALA B 1 278 ? 13.456  0.262   -16.176 1.00 23.49 ? 257 ALA B O     1 
ATOM   5230 C  CB    . ALA B 1 278 ? 13.898  3.369   -15.000 1.00 23.43 ? 257 ALA B CB    1 
ATOM   5231 N  N     . ARG B 1 279 ? 15.380  1.274   -16.672 1.00 21.76 ? 258 ARG B N     1 
ATOM   5232 C  CA    . ARG B 1 279 ? 16.171  0.018   -16.672 1.00 20.83 ? 258 ARG B CA    1 
ATOM   5233 C  C     . ARG B 1 279 ? 16.540  -0.356  -15.233 1.00 20.73 ? 258 ARG B C     1 
ATOM   5234 O  O     . ARG B 1 279 ? 16.421  -1.545  -14.929 1.00 18.40 ? 258 ARG B O     1 
ATOM   5235 C  CB    . ARG B 1 279 ? 17.375  0.148   -17.620 1.00 23.10 ? 258 ARG B CB    1 
ATOM   5236 C  CG    . ARG B 1 279 ? 16.930  0.399   -19.050 1.00 24.47 ? 258 ARG B CG    1 
ATOM   5237 C  CD    . ARG B 1 279 ? 18.066  0.855   -19.930 1.00 27.20 ? 258 ARG B CD    1 
ATOM   5238 N  NE    . ARG B 1 279 ? 19.116  -0.128  -20.016 1.00 31.20 ? 258 ARG B NE    1 
ATOM   5239 C  CZ    . ARG B 1 279 ? 20.273  0.092   -20.670 1.00 37.51 ? 258 ARG B CZ    1 
ATOM   5240 N  NH1   . ARG B 1 279 ? 20.495  1.259   -21.256 1.00 40.16 ? 258 ARG B NH1   1 
ATOM   5241 N  NH2   . ARG B 1 279 ? 21.214  -0.836  -20.698 1.00 40.69 ? 258 ARG B NH2   1 
ATOM   5242 N  N     . ARG B 1 280 ? 16.938  0.622   -14.388 1.00 19.67 ? 259 ARG B N     1 
ATOM   5243 C  CA    . ARG B 1 280 ? 17.312  0.376   -12.979 1.00 19.95 ? 259 ARG B CA    1 
ATOM   5244 C  C     . ARG B 1 280 ? 16.789  1.550   -12.134 1.00 19.28 ? 259 ARG B C     1 
ATOM   5245 O  O     . ARG B 1 280 ? 16.596  2.633   -12.682 1.00 18.33 ? 259 ARG B O     1 
ATOM   5246 C  CB    . ARG B 1 280 ? 18.814  0.180   -12.772 1.00 20.98 ? 259 ARG B CB    1 
ATOM   5247 C  CG    . ARG B 1 280 ? 19.333  -1.032  -13.524 1.00 22.74 ? 259 ARG B CG    1 
ATOM   5248 C  CD    . ARG B 1 280 ? 20.715  -1.499  -13.155 1.00 26.79 ? 259 ARG B CD    1 
ATOM   5249 N  NE    . ARG B 1 280 ? 20.827  -2.802  -13.781 1.00 29.99 ? 259 ARG B NE    1 
ATOM   5250 C  CZ    . ARG B 1 280 ? 20.766  -3.972  -13.143 1.00 27.67 ? 259 ARG B CZ    1 
ATOM   5251 N  NH1   . ARG B 1 280 ? 20.623  -4.076  -11.828 1.00 24.06 ? 259 ARG B NH1   1 
ATOM   5252 N  NH2   . ARG B 1 280 ? 20.809  -5.058  -13.861 1.00 27.09 ? 259 ARG B NH2   1 
ATOM   5253 N  N     . ALA B 1 281 ? 16.549  1.292   -10.864 1.00 20.18 ? 260 ALA B N     1 
ATOM   5254 C  CA    . ALA B 1 281 ? 16.142  2.330   -9.883  1.00 18.57 ? 260 ALA B CA    1 
ATOM   5255 C  C     . ALA B 1 281 ? 17.178  2.420   -8.772  1.00 19.83 ? 260 ALA B C     1 
ATOM   5256 O  O     . ALA B 1 281 ? 17.737  1.381   -8.361  1.00 19.90 ? 260 ALA B O     1 
ATOM   5257 C  CB    . ALA B 1 281 ? 14.790  1.988   -9.319  1.00 20.34 ? 260 ALA B CB    1 
ATOM   5258 N  N     . ILE B 1 282 ? 17.323  3.627   -8.223  1.00 19.09 ? 261 ILE B N     1 
ATOM   5259 C  CA    . ILE B 1 282 ? 18.067  3.857   -6.974  1.00 18.99 ? 261 ILE B CA    1 
ATOM   5260 C  C     . ILE B 1 282 ? 17.052  4.399   -5.980  1.00 19.03 ? 261 ILE B C     1 
ATOM   5261 O  O     . ILE B 1 282 ? 16.486  5.462   -6.259  1.00 19.18 ? 261 ILE B O     1 
ATOM   5262 C  CB    . ILE B 1 282 ? 19.261  4.790   -7.163  1.00 18.13 ? 261 ILE B CB    1 
ATOM   5263 C  CG1   . ILE B 1 282 ? 20.338  4.143   -8.040  1.00 18.44 ? 261 ILE B CG1   1 
ATOM   5264 C  CG2   . ILE B 1 282 ? 19.784  5.227   -5.811  1.00 18.54 ? 261 ILE B CG2   1 
ATOM   5265 C  CD1   . ILE B 1 282 ? 21.350  5.108   -8.630  1.00 19.40 ? 261 ILE B CD1   1 
ATOM   5266 N  N     . VAL B 1 283 ? 16.756  3.633   -4.935  1.00 17.18 ? 262 VAL B N     1 
ATOM   5267 C  CA    . VAL B 1 283 ? 15.846  4.147   -3.880  1.00 17.61 ? 262 VAL B CA    1 
ATOM   5268 C  C     . VAL B 1 283 ? 16.729  4.799   -2.816  1.00 16.57 ? 262 VAL B C     1 
ATOM   5269 O  O     . VAL B 1 283 ? 17.596  4.107   -2.206  1.00 17.07 ? 262 VAL B O     1 
ATOM   5270 C  CB    . VAL B 1 283 ? 14.937  3.035   -3.321  1.00 17.52 ? 262 VAL B CB    1 
ATOM   5271 C  CG1   . VAL B 1 283 ? 14.105  3.581   -2.170  1.00 17.33 ? 262 VAL B CG1   1 
ATOM   5272 C  CG2   . VAL B 1 283 ? 14.059  2.436   -4.418  1.00 18.58 ? 262 VAL B CG2   1 
ATOM   5273 N  N     . ALA B 1 284 ? 16.559  6.111   -2.604  1.00 17.78 ? 263 ALA B N     1 
ATOM   5274 C  CA    . ALA B 1 284 ? 17.479  6.901   -1.751  1.00 16.37 ? 263 ALA B CA    1 
ATOM   5275 C  C     . ALA B 1 284 ? 16.706  7.599   -0.619  1.00 18.69 ? 263 ALA B C     1 
ATOM   5276 O  O     . ALA B 1 284 ? 16.988  8.740   -0.308  1.00 21.19 ? 263 ALA B O     1 
ATOM   5277 C  CB    . ALA B 1 284 ? 18.268  7.872   -2.592  1.00 17.99 ? 263 ALA B CB    1 
ATOM   5278 N  N     . VAL B 1 285 ? 15.773  6.897   -0.004  1.00 19.72 ? 264 VAL B N     1 
ATOM   5279 C  CA    . VAL B 1 285 ? 14.856  7.436   1.050   1.00 19.14 ? 264 VAL B CA    1 
ATOM   5280 C  C     . VAL B 1 285 ? 15.207  6.772   2.388   1.00 20.15 ? 264 VAL B C     1 
ATOM   5281 O  O     . VAL B 1 285 ? 15.864  5.733   2.405   1.00 16.30 ? 264 VAL B O     1 
ATOM   5282 C  CB    . VAL B 1 285 ? 13.388  7.203   0.620   1.00 19.58 ? 264 VAL B CB    1 
ATOM   5283 C  CG1   . VAL B 1 285 ? 13.071  7.699   -0.788  1.00 18.93 ? 264 VAL B CG1   1 
ATOM   5284 C  CG2   . VAL B 1 285 ? 12.964  5.767   0.770   1.00 19.86 ? 264 VAL B CG2   1 
ATOM   5285 N  N     . PRO B 1 286 ? 14.755  7.309   3.554   1.00 20.04 ? 265 PRO B N     1 
ATOM   5286 C  CA    . PRO B 1 286 ? 14.985  6.678   4.849   1.00 20.31 ? 265 PRO B CA    1 
ATOM   5287 C  C     . PRO B 1 286 ? 14.467  5.249   4.867   1.00 20.50 ? 265 PRO B C     1 
ATOM   5288 O  O     . PRO B 1 286 ? 13.453  4.956   4.232   1.00 17.50 ? 265 PRO B O     1 
ATOM   5289 C  CB    . PRO B 1 286 ? 14.159  7.538   5.835   1.00 20.82 ? 265 PRO B CB    1 
ATOM   5290 C  CG    . PRO B 1 286 ? 14.126  8.873   5.175   1.00 20.69 ? 265 PRO B CG    1 
ATOM   5291 C  CD    . PRO B 1 286 ? 14.034  8.578   3.694   1.00 20.45 ? 265 PRO B CD    1 
ATOM   5292 N  N     . PRO B 1 287 ? 15.165  4.337   5.570   1.00 20.64 ? 266 PRO B N     1 
ATOM   5293 C  CA    . PRO B 1 287 ? 14.803  2.920   5.583   1.00 20.76 ? 266 PRO B CA    1 
ATOM   5294 C  C     . PRO B 1 287 ? 13.311  2.675   5.874   1.00 20.11 ? 266 PRO B C     1 
ATOM   5295 O  O     . PRO B 1 287 ? 12.674  1.927   5.118   1.00 19.60 ? 266 PRO B O     1 
ATOM   5296 C  CB    . PRO B 1 287 ? 15.693  2.346   6.699   1.00 23.70 ? 266 PRO B CB    1 
ATOM   5297 C  CG    . PRO B 1 287 ? 16.886  3.253   6.745   1.00 23.65 ? 266 PRO B CG    1 
ATOM   5298 C  CD    . PRO B 1 287 ? 16.395  4.619   6.345   1.00 22.00 ? 266 PRO B CD    1 
ATOM   5299 N  N     . THR B 1 288 ? 12.733  3.386   6.848   1.00 20.87 ? 267 THR B N     1 
ATOM   5300 C  CA    . THR B 1 288 ? 11.296  3.209   7.209   1.00 22.77 ? 267 THR B CA    1 
ATOM   5301 C  C     . THR B 1 288 ? 10.408  3.534   5.989   1.00 20.93 ? 267 THR B C     1 
ATOM   5302 O  O     . THR B 1 288 ? 9.429   2.820   5.748   1.00 21.42 ? 267 THR B O     1 
ATOM   5303 C  CB    . THR B 1 288 ? 10.900  3.968   8.497   1.00 23.37 ? 267 THR B CB    1 
ATOM   5304 O  OG1   . THR B 1 288 ? 9.548   3.587   8.782   1.00 22.17 ? 267 THR B OG1   1 
ATOM   5305 C  CG2   . THR B 1 288 ? 10.962  5.473   8.419   1.00 23.59 ? 267 THR B CG2   1 
ATOM   5306 N  N     . LEU B 1 289 ? 10.745  4.551   5.186   1.00 18.47 ? 268 LEU B N     1 
ATOM   5307 C  CA    . LEU B 1 289 ? 9.904   4.907   4.023   1.00 17.71 ? 268 LEU B CA    1 
ATOM   5308 C  C     . LEU B 1 289 ? 10.167  3.963   2.848   1.00 16.33 ? 268 LEU B C     1 
ATOM   5309 O  O     . LEU B 1 289 ? 9.202   3.734   2.080   1.00 19.63 ? 268 LEU B O     1 
ATOM   5310 C  CB    . LEU B 1 289 ? 10.159  6.359   3.656   1.00 20.07 ? 268 LEU B CB    1 
ATOM   5311 C  CG    . LEU B 1 289 ? 9.636   7.323   4.737   1.00 25.56 ? 268 LEU B CG    1 
ATOM   5312 C  CD1   . LEU B 1 289 ? 10.108  8.725   4.447   1.00 28.03 ? 268 LEU B CD1   1 
ATOM   5313 C  CD2   . LEU B 1 289 ? 8.102   7.289   4.790   1.00 29.74 ? 268 LEU B CD2   1 
ATOM   5314 N  N     . ALA B 1 290 ? 11.388  3.456   2.700   1.00 16.68 ? 269 ALA B N     1 
ATOM   5315 C  CA    . ALA B 1 290 ? 11.688  2.477   1.616   1.00 17.61 ? 269 ALA B CA    1 
ATOM   5316 C  C     . ALA B 1 290 ? 10.756  1.275   1.765   1.00 18.67 ? 269 ALA B C     1 
ATOM   5317 O  O     . ALA B 1 290 ? 10.340  0.710   0.741   1.00 20.76 ? 269 ALA B O     1 
ATOM   5318 C  CB    . ALA B 1 290 ? 13.121  2.027   1.671   1.00 19.63 ? 269 ALA B CB    1 
ATOM   5319 N  N     . GLY B 1 291 ? 10.544  0.840   3.001   1.00 21.10 ? 270 GLY B N     1 
ATOM   5320 C  CA    . GLY B 1 291 ? 9.735   -0.351  3.311   1.00 23.38 ? 270 GLY B CA    1 
ATOM   5321 C  C     . GLY B 1 291 ? 8.243   -0.140  3.021   1.00 24.80 ? 270 GLY B C     1 
ATOM   5322 O  O     . GLY B 1 291 ? 7.528   -1.172  2.847   1.00 28.29 ? 270 GLY B O     1 
ATOM   5323 N  N     . ARG B 1 292 ? 7.792   1.109   2.880   1.00 21.18 ? 271 ARG B N     1 
ATOM   5324 C  CA    . ARG B 1 292 ? 6.358   1.435   2.677   1.00 19.99 ? 271 ARG B CA    1 
ATOM   5325 C  C     . ARG B 1 292 ? 6.000   1.437   1.201   1.00 20.74 ? 271 ARG B C     1 
ATOM   5326 O  O     . ARG B 1 292 ? 4.825   1.391   0.907   1.00 20.70 ? 271 ARG B O     1 
ATOM   5327 C  CB    . ARG B 1 292 ? 5.990   2.775   3.312   1.00 19.44 ? 271 ARG B CB    1 
ATOM   5328 C  CG    . ARG B 1 292 ? 6.274   2.775   4.801   1.00 21.54 ? 271 ARG B CG    1 
ATOM   5329 C  CD    . ARG B 1 292 ? 5.924   4.073   5.511   1.00 21.57 ? 271 ARG B CD    1 
ATOM   5330 N  NE    . ARG B 1 292 ? 6.670   4.178   6.770   1.00 21.62 ? 271 ARG B NE    1 
ATOM   5331 C  CZ    . ARG B 1 292 ? 6.340   4.986   7.774   1.00 19.97 ? 271 ARG B CZ    1 
ATOM   5332 N  NH1   . ARG B 1 292 ? 5.256   5.729   7.702   1.00 19.80 ? 271 ARG B NH1   1 
ATOM   5333 N  NH2   . ARG B 1 292 ? 7.107   5.048   8.850   1.00 23.82 ? 271 ARG B NH2   1 
ATOM   5334 N  N     . ILE B 1 293 ? 6.980   1.490   0.304   1.00 20.49 ? 272 ILE B N     1 
ATOM   5335 C  CA    . ILE B 1 293 ? 6.722   1.492   -1.161  1.00 19.92 ? 272 ILE B CA    1 
ATOM   5336 C  C     . ILE B 1 293 ? 6.203   0.093   -1.513  1.00 19.87 ? 272 ILE B C     1 
ATOM   5337 O  O     . ILE B 1 293 ? 6.683   -0.904  -0.940  1.00 19.86 ? 272 ILE B O     1 
ATOM   5338 C  CB    . ILE B 1 293 ? 8.021   1.856   -1.901  1.00 20.97 ? 272 ILE B CB    1 
ATOM   5339 C  CG1   . ILE B 1 293 ? 8.471   3.303   -1.627  1.00 20.63 ? 272 ILE B CG1   1 
ATOM   5340 C  CG2   . ILE B 1 293 ? 7.871   1.562   -3.387  1.00 22.81 ? 272 ILE B CG2   1 
ATOM   5341 C  CD1   . ILE B 1 293 ? 9.854   3.617   -2.168  1.00 21.81 ? 272 ILE B CD1   1 
ATOM   5342 N  N     . ASP B 1 294 ? 5.227   0.027   -2.387  1.00 18.65 ? 273 ASP B N     1 
ATOM   5343 C  CA    . ASP B 1 294 ? 4.625   -1.224  -2.875  1.00 21.68 ? 273 ASP B CA    1 
ATOM   5344 C  C     . ASP B 1 294 ? 5.630   -1.860  -3.852  1.00 20.88 ? 273 ASP B C     1 
ATOM   5345 O  O     . ASP B 1 294 ? 5.654   -1.479  -5.032  1.00 22.23 ? 273 ASP B O     1 
ATOM   5346 C  CB    . ASP B 1 294 ? 3.240   -0.903  -3.432  1.00 24.44 ? 273 ASP B CB    1 
ATOM   5347 C  CG    . ASP B 1 294 ? 2.560   -2.040  -4.179  1.00 29.58 ? 273 ASP B CG    1 
ATOM   5348 O  OD1   . ASP B 1 294 ? 2.895   -3.211  -3.922  1.00 30.67 ? 273 ASP B OD1   1 
ATOM   5349 O  OD2   . ASP B 1 294 ? 1.757   -1.724  -5.085  1.00 33.95 ? 273 ASP B OD2   1 
ATOM   5350 N  N     . HIS B 1 295 ? 6.382   -2.853  -3.399  1.00 20.89 ? 274 HIS B N     1 
ATOM   5351 C  CA    . HIS B 1 295 ? 7.370   -3.585  -4.248  1.00 20.73 ? 274 HIS B CA    1 
ATOM   5352 C  C     . HIS B 1 295 ? 6.697   -4.803  -4.892  1.00 21.90 ? 274 HIS B C     1 
ATOM   5353 O  O     . HIS B 1 295 ? 6.024   -5.556  -4.205  1.00 19.08 ? 274 HIS B O     1 
ATOM   5354 C  CB    . HIS B 1 295 ? 8.604   -3.973  -3.429  1.00 21.08 ? 274 HIS B CB    1 
ATOM   5355 C  CG    . HIS B 1 295 ? 9.366   -2.805  -2.876  1.00 22.18 ? 274 HIS B CG    1 
ATOM   5356 N  ND1   . HIS B 1 295 ? 10.305  -2.124  -3.604  1.00 21.49 ? 274 HIS B ND1   1 
ATOM   5357 C  CD2   . HIS B 1 295 ? 9.274   -2.178  -1.677  1.00 23.00 ? 274 HIS B CD2   1 
ATOM   5358 C  CE1   . HIS B 1 295 ? 10.815  -1.156  -2.870  1.00 22.16 ? 274 HIS B CE1   1 
ATOM   5359 N  NE2   . HIS B 1 295 ? 10.155  -1.123  -1.683  1.00 23.19 ? 274 HIS B NE2   1 
ATOM   5360 N  N     . ASP B 1 296 ? 6.886   -5.003  -6.193  1.00 22.01 ? 275 ASP B N     1 
ATOM   5361 C  CA    . ASP B 1 296 ? 6.417   -6.208  -6.924  1.00 23.81 ? 275 ASP B CA    1 
ATOM   5362 C  C     . ASP B 1 296 ? 7.581   -6.693  -7.785  1.00 24.26 ? 275 ASP B C     1 
ATOM   5363 O  O     . ASP B 1 296 ? 8.039   -5.936  -8.640  1.00 23.38 ? 275 ASP B O     1 
ATOM   5364 C  CB    . ASP B 1 296 ? 5.214   -5.820  -7.771  1.00 28.57 ? 275 ASP B CB    1 
ATOM   5365 C  CG    . ASP B 1 296 ? 4.583   -6.959  -8.530  1.00 36.85 ? 275 ASP B CG    1 
ATOM   5366 O  OD1   . ASP B 1 296 ? 4.926   -8.114  -8.235  1.00 35.43 ? 275 ASP B OD1   1 
ATOM   5367 O  OD2   . ASP B 1 296 ? 3.745   -6.659  -9.408  1.00 51.23 ? 275 ASP B OD2   1 
ATOM   5368 N  N     . PRO B 1 297 ? 8.152   -7.895  -7.567  1.00 22.64 ? 276 PRO B N     1 
ATOM   5369 C  CA    . PRO B 1 297 ? 7.775   -8.791  -6.471  1.00 22.36 ? 276 PRO B CA    1 
ATOM   5370 C  C     . PRO B 1 297 ? 8.055   -8.227  -5.079  1.00 22.10 ? 276 PRO B C     1 
ATOM   5371 O  O     . PRO B 1 297 ? 8.820   -7.270  -4.933  1.00 20.26 ? 276 PRO B O     1 
ATOM   5372 C  CB    . PRO B 1 297 ? 8.659   -10.041 -6.647  1.00 23.24 ? 276 PRO B CB    1 
ATOM   5373 C  CG    . PRO B 1 297 ? 9.336   -9.899  -7.989  1.00 23.12 ? 276 PRO B CG    1 
ATOM   5374 C  CD    . PRO B 1 297 ? 9.260   -8.433  -8.373  1.00 23.31 ? 276 PRO B CD    1 
ATOM   5375 N  N     . PRO B 1 298 ? 7.439   -8.777  -4.007  1.00 21.20 ? 277 PRO B N     1 
ATOM   5376 C  CA    . PRO B 1 298 ? 7.735   -8.296  -2.667  1.00 22.36 ? 277 PRO B CA    1 
ATOM   5377 C  C     . PRO B 1 298 ? 9.249   -8.399  -2.407  1.00 18.72 ? 277 PRO B C     1 
ATOM   5378 O  O     . PRO B 1 298 ? 9.892   -9.258  -2.996  1.00 18.22 ? 277 PRO B O     1 
ATOM   5379 C  CB    . PRO B 1 298 ? 6.898   -9.208  -1.734  1.00 21.75 ? 277 PRO B CB    1 
ATOM   5380 C  CG    . PRO B 1 298 ? 5.853   -9.827  -2.644  1.00 23.44 ? 277 PRO B CG    1 
ATOM   5381 C  CD    . PRO B 1 298 ? 6.528   -9.940  -3.996  1.00 22.76 ? 277 PRO B CD    1 
ATOM   5382 N  N     . LEU B 1 299 ? 9.791   -7.498  -1.587  1.00 18.09 ? 278 LEU B N     1 
ATOM   5383 C  CA    . LEU B 1 299 ? 11.190  -7.545  -1.116  1.00 20.30 ? 278 LEU B CA    1 
ATOM   5384 C  C     . LEU B 1 299 ? 11.385  -8.893  -0.438  1.00 18.23 ? 278 LEU B C     1 
ATOM   5385 O  O     . LEU B 1 299 ? 10.441  -9.451  0.143   1.00 18.29 ? 278 LEU B O     1 
ATOM   5386 C  CB    . LEU B 1 299 ? 11.491  -6.398  -0.140  1.00 19.47 ? 278 LEU B CB    1 
ATOM   5387 C  CG    . LEU B 1 299 ? 11.471  -4.990  -0.736  1.00 22.61 ? 278 LEU B CG    1 
ATOM   5388 C  CD1   . LEU B 1 299 ? 11.994  -3.990  0.286   1.00 23.06 ? 278 LEU B CD1   1 
ATOM   5389 C  CD2   . LEU B 1 299 ? 12.285  -4.920  -2.020  1.00 22.11 ? 278 LEU B CD2   1 
ATOM   5390 N  N     . PRO B 1 300 ? 12.612  -9.450  -0.537  1.00 18.10 ? 279 PRO B N     1 
ATOM   5391 C  CA    . PRO B 1 300 ? 12.994  -10.633 0.209   1.00 17.62 ? 279 PRO B CA    1 
ATOM   5392 C  C     . PRO B 1 300 ? 12.812  -10.408 1.701   1.00 16.90 ? 279 PRO B C     1 
ATOM   5393 O  O     . PRO B 1 300 ? 12.950  -9.294  2.218   1.00 16.61 ? 279 PRO B O     1 
ATOM   5394 C  CB    . PRO B 1 300 ? 14.486  -10.890 -0.097  1.00 17.98 ? 279 PRO B CB    1 
ATOM   5395 C  CG    . PRO B 1 300 ? 14.781  -10.026 -1.255  1.00 19.90 ? 279 PRO B CG    1 
ATOM   5396 C  CD    . PRO B 1 300 ? 13.716  -8.968  -1.365  1.00 19.27 ? 279 PRO B CD    1 
ATOM   5397 N  N     . PRO B 1 301 ? 12.491  -11.488 2.435   1.00 16.44 ? 280 PRO B N     1 
ATOM   5398 C  CA    . PRO B 1 301 ? 12.139  -11.355 3.853   1.00 18.07 ? 280 PRO B CA    1 
ATOM   5399 C  C     . PRO B 1 301 ? 13.243  -10.752 4.728   1.00 17.07 ? 280 PRO B C     1 
ATOM   5400 O  O     . PRO B 1 301 ? 12.895  -9.976  5.586   1.00 16.61 ? 280 PRO B O     1 
ATOM   5401 C  CB    . PRO B 1 301 ? 11.814  -12.780 4.311   1.00 17.75 ? 280 PRO B CB    1 
ATOM   5402 C  CG    . PRO B 1 301 ? 12.404  -13.684 3.203   1.00 17.45 ? 280 PRO B CG    1 
ATOM   5403 C  CD    . PRO B 1 301 ? 12.382  -12.855 1.926   1.00 18.27 ? 280 PRO B CD    1 
ATOM   5404 N  N     . GLN B 1 302 ? 14.519  -11.115 4.521   1.00 16.72 ? 281 GLN B N     1 
ATOM   5405 C  CA    . GLN B 1 302 ? 15.628  -10.509 5.315   1.00 17.15 ? 281 GLN B CA    1 
ATOM   5406 C  C     . GLN B 1 302 ? 15.619  -8.989  5.172   1.00 16.06 ? 281 GLN B C     1 
ATOM   5407 O  O     . GLN B 1 302 ? 15.793  -8.249  6.197   1.00 16.72 ? 281 GLN B O     1 
ATOM   5408 C  CB    . GLN B 1 302 ? 16.997  -11.100 4.944   1.00 16.27 ? 281 GLN B CB    1 
ATOM   5409 C  CG    . GLN B 1 302 ? 18.089  -10.589 5.895   1.00 17.82 ? 281 GLN B CG    1 
ATOM   5410 C  CD    . GLN B 1 302 ? 19.466  -11.071 5.492   1.00 19.40 ? 281 GLN B CD    1 
ATOM   5411 O  OE1   . GLN B 1 302 ? 19.736  -11.228 4.302   1.00 19.50 ? 281 GLN B OE1   1 
ATOM   5412 N  NE2   . GLN B 1 302 ? 20.300  -11.410 6.472   1.00 20.30 ? 281 GLN B NE2   1 
ATOM   5413 N  N     . ARG B 1 303 ? 15.450  -8.517  3.932   1.00 16.84 ? 282 ARG B N     1 
ATOM   5414 C  CA    . ARG B 1 303 ? 15.429  -7.057  3.694   1.00 17.25 ? 282 ARG B CA    1 
ATOM   5415 C  C     . ARG B 1 303 ? 14.195  -6.416  4.347   1.00 15.10 ? 282 ARG B C     1 
ATOM   5416 O  O     . ARG B 1 303 ? 14.318  -5.313  4.970   1.00 15.60 ? 282 ARG B O     1 
ATOM   5417 C  CB    . ARG B 1 303 ? 15.482  -6.826  2.196   1.00 19.77 ? 282 ARG B CB    1 
ATOM   5418 C  CG    . ARG B 1 303 ? 15.132  -5.414  1.803   1.00 28.06 ? 282 ARG B CG    1 
ATOM   5419 C  CD    . ARG B 1 303 ? 16.397  -4.671  1.590   1.00 32.39 ? 282 ARG B CD    1 
ATOM   5420 N  NE    . ARG B 1 303 ? 16.062  -3.303  1.318   1.00 36.50 ? 282 ARG B NE    1 
ATOM   5421 C  CZ    . ARG B 1 303 ? 16.895  -2.319  1.544   1.00 32.89 ? 282 ARG B CZ    1 
ATOM   5422 N  NH1   . ARG B 1 303 ? 18.119  -2.587  1.952   1.00 39.00 ? 282 ARG B NH1   1 
ATOM   5423 N  NH2   . ARG B 1 303 ? 16.502  -1.090  1.335   1.00 31.05 ? 282 ARG B NH2   1 
ATOM   5424 N  N     . ASP B 1 304 ? 13.006  -6.976  4.136   1.00 14.56 ? 283 ASP B N     1 
ATOM   5425 C  CA    . ASP B 1 304 ? 11.784  -6.395  4.765   1.00 15.49 ? 283 ASP B CA    1 
ATOM   5426 C  C     . ASP B 1 304 ? 11.995  -6.323  6.278   1.00 16.35 ? 283 ASP B C     1 
ATOM   5427 O  O     . ASP B 1 304 ? 11.667  -5.237  6.898   1.00 17.06 ? 283 ASP B O     1 
ATOM   5428 C  CB    . ASP B 1 304 ? 10.474  -7.084  4.372   1.00 15.32 ? 283 ASP B CB    1 
ATOM   5429 C  CG    . ASP B 1 304 ? 9.245   -6.272  4.806   1.00 18.50 ? 283 ASP B CG    1 
ATOM   5430 O  OD1   . ASP B 1 304 ? 8.777   -5.369  4.032   1.00 20.72 ? 283 ASP B OD1   1 
ATOM   5431 O  OD2   . ASP B 1 304 ? 8.782   -6.491  5.951   1.00 18.27 ? 283 ASP B OD2   1 
ATOM   5432 N  N     . GLN B 1 305 ? 12.445  -7.415  6.902   1.00 16.10 ? 284 GLN B N     1 
ATOM   5433 C  CA    . GLN B 1 305 ? 12.613  -7.448  8.365   1.00 15.72 ? 284 GLN B CA    1 
ATOM   5434 C  C     . GLN B 1 305 ? 13.774  -6.540  8.802   1.00 14.77 ? 284 GLN B C     1 
ATOM   5435 O  O     . GLN B 1 305 ? 13.619  -5.911  9.821   1.00 15.67 ? 284 GLN B O     1 
ATOM   5436 C  CB    . GLN B 1 305 ? 12.648  -8.880  8.888   1.00 16.10 ? 284 GLN B CB    1 
ATOM   5437 C  CG    . GLN B 1 305 ? 11.341  -9.576  8.623   1.00 17.28 ? 284 GLN B CG    1 
ATOM   5438 C  CD    . GLN B 1 305 ? 11.068  -10.687 9.592   1.00 17.66 ? 284 GLN B CD    1 
ATOM   5439 O  OE1   . GLN B 1 305 ? 9.987   -10.742 10.205  1.00 22.23 ? 284 GLN B OE1   1 
ATOM   5440 N  NE2   . GLN B 1 305 ? 12.059  -11.517 9.800   1.00 16.31 ? 284 GLN B NE2   1 
ATOM   5441 N  N     . LEU B 1 306 ? 14.812  -6.335  7.981   1.00 15.14 ? 285 LEU B N     1 
ATOM   5442 C  CA    . LEU B 1 306 ? 15.835  -5.320  8.347   1.00 14.38 ? 285 LEU B CA    1 
ATOM   5443 C  C     . LEU B 1 306 ? 15.166  -3.951  8.477   1.00 14.98 ? 285 LEU B C     1 
ATOM   5444 O  O     . LEU B 1 306 ? 15.480  -3.250  9.451   1.00 15.45 ? 285 LEU B O     1 
ATOM   5445 C  CB    . LEU B 1 306 ? 16.940  -5.244  7.311   1.00 16.09 ? 285 LEU B CB    1 
ATOM   5446 C  CG    . LEU B 1 306 ? 17.927  -4.102  7.497   1.00 16.92 ? 285 LEU B CG    1 
ATOM   5447 C  CD1   . LEU B 1 306 ? 18.619  -4.181  8.875   1.00 15.82 ? 285 LEU B CD1   1 
ATOM   5448 C  CD2   . LEU B 1 306 ? 18.930  -4.116  6.317   1.00 17.05 ? 285 LEU B CD2   1 
ATOM   5449 N  N     . LEU B 1 307 ? 14.318  -3.554  7.539   1.00 15.95 ? 286 LEU B N     1 
ATOM   5450 C  CA    . LEU B 1 307 ? 13.687  -2.207  7.607   1.00 17.13 ? 286 LEU B CA    1 
ATOM   5451 C  C     . LEU B 1 307 ? 12.799  -2.108  8.851   1.00 16.59 ? 286 LEU B C     1 
ATOM   5452 O  O     . LEU B 1 307 ? 12.777  -1.032  9.475   1.00 16.94 ? 286 LEU B O     1 
ATOM   5453 C  CB    . LEU B 1 307 ? 12.928  -1.922  6.303   1.00 17.78 ? 286 LEU B CB    1 
ATOM   5454 C  CG    . LEU B 1 307 ? 13.783  -2.020  5.022   1.00 21.66 ? 286 LEU B CG    1 
ATOM   5455 C  CD1   . LEU B 1 307 ? 12.925  -1.862  3.773   1.00 23.62 ? 286 LEU B CD1   1 
ATOM   5456 C  CD2   . LEU B 1 307 ? 14.933  -1.021  5.040   1.00 22.83 ? 286 LEU B CD2   1 
ATOM   5457 N  N     . GLN B 1 308 ? 12.131  -3.184  9.262   1.00 15.93 ? 287 GLN B N     1 
ATOM   5458 C  CA    . GLN B 1 308 ? 11.341  -3.182  10.508  1.00 15.79 ? 287 GLN B CA    1 
ATOM   5459 C  C     . GLN B 1 308 ? 12.257  -2.964  11.726  1.00 17.25 ? 287 GLN B C     1 
ATOM   5460 O  O     . GLN B 1 308 ? 11.761  -2.575  12.767  1.00 16.55 ? 287 GLN B O     1 
ATOM   5461 C  CB    . GLN B 1 308 ? 10.608  -4.513  10.654  1.00 15.39 ? 287 GLN B CB    1 
ATOM   5462 C  CG    . GLN B 1 308 ? 9.573   -4.773  9.550   1.00 15.09 ? 287 GLN B CG    1 
ATOM   5463 C  CD    . GLN B 1 308 ? 8.832   -6.041  9.874   1.00 16.20 ? 287 GLN B CD    1 
ATOM   5464 O  OE1   . GLN B 1 308 ? 8.488   -6.277  11.032  1.00 19.07 ? 287 GLN B OE1   1 
ATOM   5465 N  NE2   . GLN B 1 308 ? 8.530   -6.847  8.867   1.00 16.39 ? 287 GLN B NE2   1 
ATOM   5466 N  N     . HIS B 1 309 ? 13.546  -3.301  11.605  1.00 16.71 ? 288 HIS B N     1 
ATOM   5467 C  CA    . HIS B 1 309 ? 14.563  -3.200  12.672  1.00 16.50 ? 288 HIS B CA    1 
ATOM   5468 C  C     . HIS B 1 309 ? 15.471  -1.984  12.462  1.00 16.26 ? 288 HIS B C     1 
ATOM   5469 O  O     . HIS B 1 309 ? 16.558  -1.965  13.074  1.00 17.41 ? 288 HIS B O     1 
ATOM   5470 C  CB    . HIS B 1 309 ? 15.384  -4.494  12.725  1.00 16.36 ? 288 HIS B CB    1 
ATOM   5471 C  CG    . HIS B 1 309 ? 14.637  -5.669  13.262  1.00 17.43 ? 288 HIS B CG    1 
ATOM   5472 N  ND1   . HIS B 1 309 ? 14.516  -5.947  14.611  1.00 21.97 ? 288 HIS B ND1   1 
ATOM   5473 C  CD2   . HIS B 1 309 ? 13.973  -6.649  12.629  1.00 16.75 ? 288 HIS B CD2   1 
ATOM   5474 C  CE1   . HIS B 1 309 ? 13.824  -7.050  14.776  1.00 18.50 ? 288 HIS B CE1   1 
ATOM   5475 N  NE2   . HIS B 1 309 ? 13.463  -7.492  13.596  1.00 19.22 ? 288 HIS B NE2   1 
ATOM   5476 N  N     . MET B 1 310 ? 15.087  -1.008  11.636  1.00 15.34 ? 289 MET B N     1 
ATOM   5477 C  CA    . MET B 1 310 ? 15.878  0.249   11.434  1.00 16.07 ? 289 MET B CA    1 
ATOM   5478 C  C     . MET B 1 310 ? 15.003  1.468   11.732  1.00 15.31 ? 289 MET B C     1 
ATOM   5479 O  O     . MET B 1 310 ? 14.801  2.317   10.868  1.00 16.71 ? 289 MET B O     1 
ATOM   5480 C  CB    . MET B 1 310 ? 16.440  0.331   10.012  1.00 17.62 ? 289 MET B CB    1 
ATOM   5481 C  CG    . MET B 1 310 ? 17.548  -0.665  9.772   1.00 17.15 ? 289 MET B CG    1 
ATOM   5482 S  SD    . MET B 1 310 ? 18.302  -0.551  8.118   1.00 18.97 ? 289 MET B SD    1 
ATOM   5483 C  CE    . MET B 1 310 ? 19.332  0.906   8.345   1.00 19.88 ? 289 MET B CE    1 
ATOM   5484 N  N     . PRO B 1 311 ? 14.484  1.600   12.972  1.00 17.34 ? 290 PRO B N     1 
ATOM   5485 C  CA    . PRO B 1 311 ? 13.673  2.760   13.366  1.00 17.23 ? 290 PRO B CA    1 
ATOM   5486 C  C     . PRO B 1 311 ? 14.491  4.053   13.319  1.00 18.01 ? 290 PRO B C     1 
ATOM   5487 O  O     . PRO B 1 311 ? 15.675  4.000   13.661  1.00 16.77 ? 290 PRO B O     1 
ATOM   5488 C  CB    . PRO B 1 311 ? 13.271  2.481   14.805  1.00 18.32 ? 290 PRO B CB    1 
ATOM   5489 C  CG    . PRO B 1 311 ? 14.372  1.576   15.312  1.00 18.98 ? 290 PRO B CG    1 
ATOM   5490 C  CD    . PRO B 1 311 ? 14.726  0.701   14.121  1.00 16.15 ? 290 PRO B CD    1 
ATOM   5491 N  N     . GLN B 1 312 ? 13.887  5.142   12.843  1.00 18.08 ? 291 GLN B N     1 
ATOM   5492 C  CA    . GLN B 1 312 ? 14.534  6.478   12.836  1.00 18.00 ? 291 GLN B CA    1 
ATOM   5493 C  C     . GLN B 1 312 ? 14.537  7.033   14.268  1.00 16.69 ? 291 GLN B C     1 
ATOM   5494 O  O     . GLN B 1 312 ? 13.681  6.655   15.125  1.00 16.59 ? 291 GLN B O     1 
ATOM   5495 C  CB    . GLN B 1 312 ? 13.809  7.474   11.926  1.00 20.42 ? 291 GLN B CB    1 
ATOM   5496 C  CG    . GLN B 1 312 ? 13.633  7.073   10.467  1.00 27.32 ? 291 GLN B CG    1 
ATOM   5497 C  CD    . GLN B 1 312 ? 14.879  7.360   9.674   1.00 31.75 ? 291 GLN B CD    1 
ATOM   5498 O  OE1   . GLN B 1 312 ? 15.298  8.517   9.481   1.00 37.69 ? 291 GLN B OE1   1 
ATOM   5499 N  NE2   . GLN B 1 312 ? 15.499  6.305   9.208   1.00 29.67 ? 291 GLN B NE2   1 
ATOM   5500 N  N     . GLY B 1 313 ? 15.454  7.962   14.502  1.00 16.49 ? 292 GLY B N     1 
ATOM   5501 C  CA    . GLY B 1 313 ? 15.594  8.643   15.784  1.00 16.78 ? 292 GLY B CA    1 
ATOM   5502 C  C     . GLY B 1 313 ? 14.444  9.591   16.034  1.00 15.75 ? 292 GLY B C     1 
ATOM   5503 O  O     . GLY B 1 313 ? 13.564  9.763   15.148  1.00 17.39 ? 292 GLY B O     1 
ATOM   5504 N  N     . SER B 1 314 ? 14.455  10.220  17.206  1.00 15.94 ? 293 SER B N     1 
ATOM   5505 C  CA    . SER B 1 314 ? 13.409  11.169  17.655  1.00 15.51 ? 293 SER B CA    1 
ATOM   5506 C  C     . SER B 1 314 ? 14.095  12.480  18.064  1.00 17.10 ? 293 SER B C     1 
ATOM   5507 O  O     . SER B 1 314 ? 14.861  12.460  19.038  1.00 17.56 ? 293 SER B O     1 
ATOM   5508 C  CB    . SER B 1 314 ? 12.549  10.608  18.761  1.00 17.03 ? 293 SER B CB    1 
ATOM   5509 O  OG    . SER B 1 314 ? 11.997  9.335   18.417  1.00 19.00 ? 293 SER B OG    1 
ATOM   5510 N  N     . VAL B 1 315 ? 13.932  13.532  17.260  1.00 15.36 ? 294 VAL B N     1 
ATOM   5511 C  CA    . VAL B 1 315 ? 14.519  14.866  17.611  1.00 16.58 ? 294 VAL B CA    1 
ATOM   5512 C  C     . VAL B 1 315 ? 13.542  15.958  17.181  1.00 15.42 ? 294 VAL B C     1 
ATOM   5513 O  O     . VAL B 1 315 ? 12.915  15.857  16.106  1.00 16.72 ? 294 VAL B O     1 
ATOM   5514 C  CB    . VAL B 1 315 ? 15.909  15.013  16.969  1.00 17.35 ? 294 VAL B CB    1 
ATOM   5515 C  CG1   . VAL B 1 315 ? 15.869  14.777  15.473  1.00 19.93 ? 294 VAL B CG1   1 
ATOM   5516 C  CG2   . VAL B 1 315 ? 16.543  16.340  17.289  1.00 17.72 ? 294 VAL B CG2   1 
ATOM   5517 N  N     . VAL B 1 316 ? 13.411  16.971  18.036  1.00 15.25 ? 295 VAL B N     1 
ATOM   5518 C  CA    . VAL B 1 316 ? 12.812  18.264  17.697  1.00 16.91 ? 295 VAL B CA    1 
ATOM   5519 C  C     . VAL B 1 316 ? 13.962  19.256  17.747  1.00 16.84 ? 295 VAL B C     1 
ATOM   5520 O  O     . VAL B 1 316 ? 14.619  19.342  18.830  1.00 16.78 ? 295 VAL B O     1 
ATOM   5521 C  CB    . VAL B 1 316 ? 11.667  18.643  18.648  1.00 20.19 ? 295 VAL B CB    1 
ATOM   5522 C  CG1   . VAL B 1 316 ? 11.049  19.967  18.224  1.00 20.06 ? 295 VAL B CG1   1 
ATOM   5523 C  CG2   . VAL B 1 316 ? 10.603  17.518  18.705  1.00 19.58 ? 295 VAL B CG2   1 
ATOM   5524 N  N     . LYS B 1 317 ? 14.245  19.917  16.623  1.00 17.15 ? 296 LYS B N     1 
ATOM   5525 C  CA    . LYS B 1 317 ? 15.354  20.893  16.572  1.00 16.43 ? 296 LYS B CA    1 
ATOM   5526 C  C     . LYS B 1 317 ? 14.771  22.306  16.653  1.00 15.92 ? 296 LYS B C     1 
ATOM   5527 O  O     . LYS B 1 317 ? 13.785  22.592  15.994  1.00 17.04 ? 296 LYS B O     1 
ATOM   5528 C  CB    . LYS B 1 317 ? 16.199  20.741  15.309  1.00 17.09 ? 296 LYS B CB    1 
ATOM   5529 C  CG    . LYS B 1 317 ? 17.299  21.787  15.182  1.00 17.79 ? 296 LYS B CG    1 
ATOM   5530 C  CD    . LYS B 1 317 ? 18.199  21.530  13.956  1.00 18.80 ? 296 LYS B CD    1 
ATOM   5531 C  CE    . LYS B 1 317 ? 19.333  22.529  13.884  1.00 19.46 ? 296 LYS B CE    1 
ATOM   5532 N  NZ    . LYS B 1 317 ? 20.129  22.326  12.650  1.00 21.08 ? 296 LYS B NZ    1 
ATOM   5533 N  N     . PHE B 1 318 ? 15.387  23.187  17.431  1.00 16.96 ? 297 PHE B N     1 
ATOM   5534 C  CA    . PHE B 1 318 ? 14.814  24.535  17.601  1.00 16.81 ? 297 PHE B CA    1 
ATOM   5535 C  C     . PHE B 1 318 ? 15.883  25.603  17.442  1.00 16.75 ? 297 PHE B C     1 
ATOM   5536 O  O     . PHE B 1 318 ? 17.083  25.342  17.712  1.00 17.05 ? 297 PHE B O     1 
ATOM   5537 C  CB    . PHE B 1 318 ? 14.092  24.672  18.946  1.00 18.23 ? 297 PHE B CB    1 
ATOM   5538 C  CG    . PHE B 1 318 ? 14.957  24.471  20.158  1.00 19.06 ? 297 PHE B CG    1 
ATOM   5539 C  CD1   . PHE B 1 318 ? 14.966  23.263  20.820  1.00 19.26 ? 297 PHE B CD1   1 
ATOM   5540 C  CD2   . PHE B 1 318 ? 15.754  25.500  20.639  1.00 18.63 ? 297 PHE B CD2   1 
ATOM   5541 C  CE1   . PHE B 1 318 ? 15.775  23.074  21.920  1.00 18.49 ? 297 PHE B CE1   1 
ATOM   5542 C  CE2   . PHE B 1 318 ? 16.532  25.321  21.761  1.00 18.99 ? 297 PHE B CE2   1 
ATOM   5543 C  CZ    . PHE B 1 318 ? 16.519  24.111  22.411  1.00 19.39 ? 297 PHE B CZ    1 
ATOM   5544 N  N     . HIS B 1 319 ? 15.405  26.776  17.077  1.00 18.50 ? 298 HIS B N     1 
ATOM   5545 C  CA    . HIS B 1 319 ? 16.187  28.033  17.076  1.00 20.10 ? 298 HIS B CA    1 
ATOM   5546 C  C     . HIS B 1 319 ? 15.373  29.065  17.853  1.00 19.89 ? 298 HIS B C     1 
ATOM   5547 O  O     . HIS B 1 319 ? 14.261  29.460  17.369  1.00 19.73 ? 298 HIS B O     1 
ATOM   5548 C  CB    . HIS B 1 319 ? 16.489  28.495  15.631  1.00 20.16 ? 298 HIS B CB    1 
ATOM   5549 C  CG    . HIS B 1 319 ? 17.276  27.511  14.800  1.00 20.41 ? 298 HIS B CG    1 
ATOM   5550 N  ND1   . HIS B 1 319 ? 18.665  27.523  14.729  1.00 20.25 ? 298 HIS B ND1   1 
ATOM   5551 C  CD2   . HIS B 1 319 ? 16.870  26.512  13.981  1.00 19.29 ? 298 HIS B CD2   1 
ATOM   5552 C  CE1   . HIS B 1 319 ? 19.066  26.557  13.906  1.00 23.21 ? 298 HIS B CE1   1 
ATOM   5553 N  NE2   . HIS B 1 319 ? 17.988  25.939  13.427  1.00 21.15 ? 298 HIS B NE2   1 
ATOM   5554 N  N     . VAL B 1 320 ? 15.950  29.565  18.943  1.00 19.06 ? 299 VAL B N     1 
ATOM   5555 C  CA    . VAL B 1 320 ? 15.347  30.684  19.721  1.00 20.99 ? 299 VAL B CA    1 
ATOM   5556 C  C     . VAL B 1 320 ? 16.010  31.966  19.204  1.00 20.60 ? 299 VAL B C     1 
ATOM   5557 O  O     . VAL B 1 320 ? 17.266  32.014  19.194  1.00 21.12 ? 299 VAL B O     1 
ATOM   5558 C  CB    . VAL B 1 320 ? 15.578  30.563  21.230  1.00 22.30 ? 299 VAL B CB    1 
ATOM   5559 C  CG1   . VAL B 1 320 ? 14.680  31.540  21.983  1.00 22.58 ? 299 VAL B CG1   1 
ATOM   5560 C  CG2   . VAL B 1 320 ? 15.431  29.155  21.769  1.00 24.10 ? 299 VAL B CG2   1 
ATOM   5561 N  N     . ILE B 1 321 ? 15.210  32.931  18.773  1.00 21.66 ? 300 ILE B N     1 
ATOM   5562 C  CA    . ILE B 1 321 ? 15.696  34.177  18.109  1.00 20.56 ? 300 ILE B CA    1 
ATOM   5563 C  C     . ILE B 1 321 ? 15.668  35.333  19.134  1.00 21.04 ? 300 ILE B C     1 
ATOM   5564 O  O     . ILE B 1 321 ? 14.658  35.502  19.829  1.00 23.71 ? 300 ILE B O     1 
ATOM   5565 C  CB    . ILE B 1 321 ? 14.865  34.511  16.859  1.00 21.18 ? 300 ILE B CB    1 
ATOM   5566 C  CG1   . ILE B 1 321 ? 14.560  33.273  16.005  1.00 22.42 ? 300 ILE B CG1   1 
ATOM   5567 C  CG2   . ILE B 1 321 ? 15.567  35.590  16.051  1.00 21.38 ? 300 ILE B CG2   1 
ATOM   5568 C  CD1   . ILE B 1 321 ? 15.786  32.621  15.450  1.00 24.18 ? 300 ILE B CD1   1 
ATOM   5569 N  N     . TYR B 1 322 ? 16.772  36.059  19.250  1.00 24.39 ? 301 TYR B N     1 
ATOM   5570 C  CA    . TYR B 1 322 ? 16.919  37.250  20.136  1.00 23.63 ? 301 TYR B CA    1 
ATOM   5571 C  C     . TYR B 1 322 ? 17.370  38.390  19.241  1.00 25.28 ? 301 TYR B C     1 
ATOM   5572 O  O     . TYR B 1 322 ? 17.947  38.114  18.200  1.00 23.68 ? 301 TYR B O     1 
ATOM   5573 C  CB    . TYR B 1 322 ? 17.948  36.969  21.233  1.00 23.00 ? 301 TYR B CB    1 
ATOM   5574 C  CG    . TYR B 1 322 ? 17.509  35.912  22.214  1.00 23.87 ? 301 TYR B CG    1 
ATOM   5575 C  CD1   . TYR B 1 322 ? 16.692  36.229  23.280  1.00 23.20 ? 301 TYR B CD1   1 
ATOM   5576 C  CD2   . TYR B 1 322 ? 17.843  34.576  22.032  1.00 25.71 ? 301 TYR B CD2   1 
ATOM   5577 C  CE1   . TYR B 1 322 ? 16.261  35.263  24.181  1.00 26.60 ? 301 TYR B CE1   1 
ATOM   5578 C  CE2   . TYR B 1 322 ? 17.381  33.585  22.897  1.00 25.48 ? 301 TYR B CE2   1 
ATOM   5579 C  CZ    . TYR B 1 322 ? 16.607  33.931  23.992  1.00 27.53 ? 301 TYR B CZ    1 
ATOM   5580 O  OH    . TYR B 1 322 ? 16.172  32.984  24.873  1.00 23.45 ? 301 TYR B OH    1 
ATOM   5581 N  N     . ASP B 1 323 ? 17.134  39.642  19.624  1.00 28.55 ? 302 ASP B N     1 
ATOM   5582 C  CA    . ASP B 1 323 ? 17.632  40.788  18.808  1.00 29.25 ? 302 ASP B CA    1 
ATOM   5583 C  C     . ASP B 1 323 ? 19.153  40.704  18.674  1.00 26.18 ? 302 ASP B C     1 
ATOM   5584 O  O     . ASP B 1 323 ? 19.662  41.032  17.607  1.00 25.76 ? 302 ASP B O     1 
ATOM   5585 C  CB    . ASP B 1 323 ? 17.189  42.110  19.426  1.00 30.60 ? 302 ASP B CB    1 
ATOM   5586 C  CG    . ASP B 1 323 ? 15.714  42.341  19.220  1.00 35.11 ? 302 ASP B CG    1 
ATOM   5587 O  OD1   . ASP B 1 323 ? 15.138  41.700  18.298  1.00 40.08 ? 302 ASP B OD1   1 
ATOM   5588 O  OD2   . ASP B 1 323 ? 15.147  43.106  19.987  1.00 42.27 ? 302 ASP B OD2   1 
ATOM   5589 N  N     . GLU B 1 324 ? 19.856  40.291  19.728  1.00 28.34 ? 303 GLU B N     1 
ATOM   5590 C  CA    . GLU B 1 324 ? 21.338  40.241  19.768  1.00 30.39 ? 303 GLU B CA    1 
ATOM   5591 C  C     . GLU B 1 324 ? 21.778  39.007  20.529  1.00 27.14 ? 303 GLU B C     1 
ATOM   5592 O  O     . GLU B 1 324 ? 21.030  38.534  21.377  1.00 25.62 ? 303 GLU B O     1 
ATOM   5593 C  CB    . GLU B 1 324 ? 21.886  41.446  20.530  1.00 36.59 ? 303 GLU B CB    1 
ATOM   5594 C  CG    . GLU B 1 324 ? 21.556  42.762  19.878  1.00 46.11 ? 303 GLU B CG    1 
ATOM   5595 C  CD    . GLU B 1 324 ? 22.187  43.943  20.595  1.00 55.44 ? 303 GLU B CD    1 
ATOM   5596 O  OE1   . GLU B 1 324 ? 22.757  44.822  19.903  1.00 63.83 ? 303 GLU B OE1   1 
ATOM   5597 O  OE2   . GLU B 1 324 ? 22.118  43.974  21.846  1.00 61.90 ? 303 GLU B OE2   1 
ATOM   5598 N  N     . PRO B 1 325 ? 22.998  38.477  20.263  1.00 24.44 ? 304 PRO B N     1 
ATOM   5599 C  CA    . PRO B 1 325 ? 23.578  37.404  21.069  1.00 23.15 ? 304 PRO B CA    1 
ATOM   5600 C  C     . PRO B 1 325 ? 24.106  37.940  22.412  1.00 24.46 ? 304 PRO B C     1 
ATOM   5601 O  O     . PRO B 1 325 ? 25.334  37.963  22.643  1.00 22.99 ? 304 PRO B O     1 
ATOM   5602 C  CB    . PRO B 1 325 ? 24.698  36.879  20.163  1.00 24.05 ? 304 PRO B CB    1 
ATOM   5603 C  CG    . PRO B 1 325 ? 25.178  38.131  19.448  1.00 23.30 ? 304 PRO B CG    1 
ATOM   5604 C  CD    . PRO B 1 325 ? 23.906  38.919  19.194  1.00 23.52 ? 304 PRO B CD    1 
ATOM   5605 N  N     . TRP B 1 326 ? 23.155  38.233  23.311  1.00 26.53 ? 305 TRP B N     1 
ATOM   5606 C  CA    . TRP B 1 326 ? 23.349  39.007  24.565  1.00 24.30 ? 305 TRP B CA    1 
ATOM   5607 C  C     . TRP B 1 326 ? 24.265  38.220  25.505  1.00 30.19 ? 305 TRP B C     1 
ATOM   5608 O  O     . TRP B 1 326 ? 25.042  38.846  26.291  1.00 28.87 ? 305 TRP B O     1 
ATOM   5609 C  CB    . TRP B 1 326 ? 21.988  39.344  25.210  1.00 25.35 ? 305 TRP B CB    1 
ATOM   5610 C  CG    . TRP B 1 326 ? 21.075  38.180  25.446  1.00 25.20 ? 305 TRP B CG    1 
ATOM   5611 C  CD1   . TRP B 1 326 ? 20.054  37.774  24.636  1.00 26.93 ? 305 TRP B CD1   1 
ATOM   5612 C  CD2   . TRP B 1 326 ? 21.093  37.250  26.544  1.00 24.40 ? 305 TRP B CD2   1 
ATOM   5613 N  NE1   . TRP B 1 326 ? 19.442  36.666  25.147  1.00 24.37 ? 305 TRP B NE1   1 
ATOM   5614 C  CE2   . TRP B 1 326 ? 20.072  36.299  26.299  1.00 26.95 ? 305 TRP B CE2   1 
ATOM   5615 C  CE3   . TRP B 1 326 ? 21.905  37.072  27.666  1.00 27.36 ? 305 TRP B CE3   1 
ATOM   5616 C  CZ2   . TRP B 1 326 ? 19.843  35.207  27.138  1.00 26.91 ? 305 TRP B CZ2   1 
ATOM   5617 C  CZ3   . TRP B 1 326 ? 21.676  35.997  28.500  1.00 25.99 ? 305 TRP B CZ3   1 
ATOM   5618 C  CH2   . TRP B 1 326 ? 20.638  35.100  28.253  1.00 26.04 ? 305 TRP B CH2   1 
ATOM   5619 N  N     . TRP B 1 327 ? 24.210  36.891  25.436  1.00 24.87 ? 306 TRP B N     1 
ATOM   5620 C  CA    . TRP B 1 327 ? 25.024  36.028  26.334  1.00 23.70 ? 306 TRP B CA    1 
ATOM   5621 C  C     . TRP B 1 327 ? 26.527  36.309  26.101  1.00 24.98 ? 306 TRP B C     1 
ATOM   5622 O  O     . TRP B 1 327 ? 27.307  36.112  27.051  1.00 25.02 ? 306 TRP B O     1 
ATOM   5623 C  CB    . TRP B 1 327 ? 24.634  34.561  26.106  1.00 27.02 ? 306 TRP B CB    1 
ATOM   5624 C  CG    . TRP B 1 327 ? 24.683  34.158  24.664  1.00 23.93 ? 306 TRP B CG    1 
ATOM   5625 C  CD1   . TRP B 1 327 ? 25.763  33.680  23.984  1.00 25.26 ? 306 TRP B CD1   1 
ATOM   5626 C  CD2   . TRP B 1 327 ? 23.603  34.204  23.712  1.00 23.45 ? 306 TRP B CD2   1 
ATOM   5627 N  NE1   . TRP B 1 327 ? 25.437  33.439  22.680  1.00 26.44 ? 306 TRP B NE1   1 
ATOM   5628 C  CE2   . TRP B 1 327 ? 24.108  33.737  22.479  1.00 24.42 ? 306 TRP B CE2   1 
ATOM   5629 C  CE3   . TRP B 1 327 ? 22.276  34.601  23.783  1.00 23.67 ? 306 TRP B CE3   1 
ATOM   5630 C  CZ2   . TRP B 1 327 ? 23.327  33.677  21.332  1.00 23.18 ? 306 TRP B CZ2   1 
ATOM   5631 C  CZ3   . TRP B 1 327 ? 21.495  34.528  22.660  1.00 24.41 ? 306 TRP B CZ3   1 
ATOM   5632 C  CH2   . TRP B 1 327 ? 22.013  34.059  21.456  1.00 26.52 ? 306 TRP B CH2   1 
ATOM   5633 N  N     . ARG B 1 328 ? 26.933  36.760  24.893  1.00 25.12 ? 307 ARG B N     1 
ATOM   5634 C  CA    . ARG B 1 328 ? 28.364  36.989  24.531  1.00 26.90 ? 307 ARG B CA    1 
ATOM   5635 C  C     . ARG B 1 328 ? 28.932  38.126  25.411  1.00 26.89 ? 307 ARG B C     1 
ATOM   5636 O  O     . ARG B 1 328 ? 30.055  37.982  25.930  1.00 28.22 ? 307 ARG B O     1 
ATOM   5637 C  CB    . ARG B 1 328 ? 28.515  37.353  23.054  1.00 28.06 ? 307 ARG B CB    1 
ATOM   5638 C  CG    . ARG B 1 328 ? 28.284  36.187  22.097  1.00 26.02 ? 307 ARG B CG    1 
ATOM   5639 C  CD    . ARG B 1 328 ? 28.408  36.625  20.668  1.00 28.93 ? 307 ARG B CD    1 
ATOM   5640 N  NE    . ARG B 1 328 ? 28.122  35.497  19.775  1.00 27.97 ? 307 ARG B NE    1 
ATOM   5641 C  CZ    . ARG B 1 328 ? 28.296  35.522  18.472  1.00 26.65 ? 307 ARG B CZ    1 
ATOM   5642 N  NH1   . ARG B 1 328 ? 28.710  36.642  17.898  1.00 26.91 ? 307 ARG B NH1   1 
ATOM   5643 N  NH2   . ARG B 1 328 ? 28.035  34.454  17.738  1.00 27.66 ? 307 ARG B NH2   1 
ATOM   5644 N  N     . ALA B 1 329 ? 28.139  39.166  25.657  1.00 31.86 ? 308 ALA B N     1 
ATOM   5645 C  CA    . ALA B 1 329 ? 28.518  40.314  26.523  1.00 32.04 ? 308 ALA B CA    1 
ATOM   5646 C  C     . ALA B 1 329 ? 28.706  39.859  27.972  1.00 34.95 ? 308 ALA B C     1 
ATOM   5647 O  O     . ALA B 1 329 ? 29.429  40.544  28.713  1.00 40.16 ? 308 ALA B O     1 
ATOM   5648 C  CB    . ALA B 1 329 ? 27.480  41.404  26.420  1.00 32.13 ? 308 ALA B CB    1 
ATOM   5649 N  N     . GLU B 1 330 ? 28.147  38.717  28.370  1.00 33.92 ? 309 GLU B N     1 
ATOM   5650 C  CA    . GLU B 1 330 ? 28.324  38.157  29.743  1.00 34.44 ? 309 GLU B CA    1 
ATOM   5651 C  C     . GLU B 1 330 ? 29.457  37.134  29.801  1.00 32.84 ? 309 GLU B C     1 
ATOM   5652 O  O     . GLU B 1 330 ? 29.575  36.456  30.843  1.00 33.40 ? 309 GLU B O     1 
ATOM   5653 C  CB    . GLU B 1 330 ? 27.035  37.484  30.161  1.00 36.94 ? 309 GLU B CB    1 
ATOM   5654 C  CG    . GLU B 1 330 ? 25.831  38.285  29.743  1.00 44.68 ? 309 GLU B CG    1 
ATOM   5655 C  CD    . GLU B 1 330 ? 25.052  38.830  30.911  1.00 53.06 ? 309 GLU B CD    1 
ATOM   5656 O  OE1   . GLU B 1 330 ? 23.801  38.782  30.845  1.00 68.72 ? 309 GLU B OE1   1 
ATOM   5657 O  OE2   . GLU B 1 330 ? 25.705  39.294  31.874  1.00 59.70 ? 309 GLU B OE2   1 
ATOM   5658 N  N     . GLY B 1 331 ? 30.197  36.960  28.702  1.00 33.06 ? 310 GLY B N     1 
ATOM   5659 C  CA    . GLY B 1 331 ? 31.296  35.978  28.606  1.00 31.73 ? 310 GLY B CA    1 
ATOM   5660 C  C     . GLY B 1 331 ? 30.776  34.548  28.492  1.00 28.78 ? 310 GLY B C     1 
ATOM   5661 O  O     . GLY B 1 331 ? 31.524  33.614  28.881  1.00 26.96 ? 310 GLY B O     1 
ATOM   5662 N  N     . LEU B 1 332 ? 29.551  34.345  27.982  1.00 26.07 ? 311 LEU B N     1 
ATOM   5663 C  CA    . LEU B 1 332 ? 28.976  32.974  27.851  1.00 25.47 ? 311 LEU B CA    1 
ATOM   5664 C  C     . LEU B 1 332 ? 29.017  32.547  26.381  1.00 24.78 ? 311 LEU B C     1 
ATOM   5665 O  O     . LEU B 1 332 ? 28.814  33.411  25.511  1.00 23.35 ? 311 LEU B O     1 
ATOM   5666 C  CB    . LEU B 1 332 ? 27.525  32.960  28.347  1.00 26.33 ? 311 LEU B CB    1 
ATOM   5667 C  CG    . LEU B 1 332 ? 27.358  33.183  29.849  1.00 27.18 ? 311 LEU B CG    1 
ATOM   5668 C  CD1   . LEU B 1 332 ? 25.894  33.421  30.207  1.00 29.49 ? 311 LEU B CD1   1 
ATOM   5669 C  CD2   . LEU B 1 332 ? 27.909  31.997  30.622  1.00 27.31 ? 311 LEU B CD2   1 
ATOM   5670 N  N     . SER B 1 333 ? 29.194  31.244  26.130  1.00 24.87 ? 312 SER B N     1 
ATOM   5671 C  CA    . SER B 1 333 ? 29.293  30.676  24.761  1.00 22.88 ? 312 SER B CA    1 
ATOM   5672 C  C     . SER B 1 333 ? 27.903  30.557  24.137  1.00 24.25 ? 312 SER B C     1 
ATOM   5673 O  O     . SER B 1 333 ? 27.809  30.452  22.889  1.00 27.63 ? 312 SER B O     1 
ATOM   5674 C  CB    . SER B 1 333 ? 29.955  29.330  24.788  1.00 22.96 ? 312 SER B CB    1 
ATOM   5675 O  OG    . SER B 1 333 ? 29.223  28.424  25.621  1.00 24.44 ? 312 SER B OG    1 
ATOM   5676 N  N     . GLY B 1 334 ? 26.868  30.448  24.975  1.00 20.80 ? 313 GLY B N     1 
ATOM   5677 C  CA    . GLY B 1 334 ? 25.516  30.070  24.541  1.00 20.07 ? 313 GLY B CA    1 
ATOM   5678 C  C     . GLY B 1 334 ? 25.310  28.571  24.539  1.00 19.07 ? 313 GLY B C     1 
ATOM   5679 O  O     . GLY B 1 334 ? 24.177  28.139  24.218  1.00 21.89 ? 313 GLY B O     1 
ATOM   5680 N  N     . THR B 1 335 ? 26.333  27.787  24.906  1.00 19.92 ? 314 THR B N     1 
ATOM   5681 C  CA    . THR B 1 335 ? 26.194  26.334  25.132  1.00 21.29 ? 314 THR B CA    1 
ATOM   5682 C  C     . THR B 1 335 ? 25.793  26.106  26.578  1.00 22.24 ? 314 THR B C     1 
ATOM   5683 O  O     . THR B 1 335 ? 26.513  26.600  27.494  1.00 22.38 ? 314 THR B O     1 
ATOM   5684 C  CB    . THR B 1 335 ? 27.437  25.540  24.725  1.00 22.77 ? 314 THR B CB    1 
ATOM   5685 O  OG1   . THR B 1 335 ? 27.442  25.546  23.287  1.00 26.30 ? 314 THR B OG1   1 
ATOM   5686 C  CG2   . THR B 1 335 ? 27.434  24.123  25.260  1.00 23.12 ? 314 THR B CG2   1 
ATOM   5687 N  N     . VAL B 1 336 ? 24.730  25.314  26.764  1.00 21.15 ? 315 VAL B N     1 
ATOM   5688 C  CA    . VAL B 1 336 ? 24.351  24.751  28.080  1.00 21.47 ? 315 VAL B CA    1 
ATOM   5689 C  C     . VAL B 1 336 ? 24.348  23.231  27.916  1.00 22.47 ? 315 VAL B C     1 
ATOM   5690 O  O     . VAL B 1 336 ? 23.980  22.737  26.804  1.00 24.05 ? 315 VAL B O     1 
ATOM   5691 C  CB    . VAL B 1 336 ? 22.997  25.286  28.604  1.00 24.60 ? 315 VAL B CB    1 
ATOM   5692 C  CG1   . VAL B 1 336 ? 22.941  26.791  28.458  1.00 24.42 ? 315 VAL B CG1   1 
ATOM   5693 C  CG2   . VAL B 1 336 ? 21.786  24.649  27.901  1.00 27.22 ? 315 VAL B CG2   1 
ATOM   5694 N  N     . LEU B 1 337 ? 24.707  22.510  28.978  1.00 23.32 ? 316 LEU B N     1 
ATOM   5695 C  CA    . LEU B 1 337 ? 24.658  21.030  29.024  1.00 26.88 ? 316 LEU B CA    1 
ATOM   5696 C  C     . LEU B 1 337 ? 23.865  20.603  30.259  1.00 26.41 ? 316 LEU B C     1 
ATOM   5697 O  O     . LEU B 1 337 ? 24.290  20.932  31.347  1.00 26.58 ? 316 LEU B O     1 
ATOM   5698 C  CB    . LEU B 1 337 ? 26.086  20.475  29.063  1.00 32.37 ? 316 LEU B CB    1 
ATOM   5699 C  CG    . LEU B 1 337 ? 26.225  19.086  28.463  1.00 42.99 ? 316 LEU B CG    1 
ATOM   5700 C  CD1   . LEU B 1 337 ? 26.489  19.190  26.969  1.00 50.41 ? 316 LEU B CD1   1 
ATOM   5701 C  CD2   . LEU B 1 337 ? 27.317  18.298  29.165  1.00 49.64 ? 316 LEU B CD2   1 
ATOM   5702 N  N     . CYS B 1 338 ? 22.764  19.870  30.077  1.00 24.68 ? 317 CYS B N     1 
ATOM   5703 C  CA    . CYS B 1 338 ? 21.795  19.548  31.158  1.00 27.40 ? 317 CYS B CA    1 
ATOM   5704 C  C     . CYS B 1 338 ? 21.406  18.082  31.063  1.00 25.47 ? 317 CYS B C     1 
ATOM   5705 O  O     . CYS B 1 338 ? 20.465  17.720  30.355  1.00 26.59 ? 317 CYS B O     1 
ATOM   5706 C  CB    . CYS B 1 338 ? 20.546  20.419  31.031  1.00 28.69 ? 317 CYS B CB    1 
ATOM   5707 S  SG    . CYS B 1 338 ? 20.882  22.195  31.080  1.00 29.89 ? 317 CYS B SG    1 
ATOM   5708 N  N     . PRO B 1 339 ? 22.090  17.176  31.796  1.00 27.78 ? 318 PRO B N     1 
ATOM   5709 C  CA    . PRO B 1 339 ? 21.745  15.764  31.756  1.00 28.99 ? 318 PRO B CA    1 
ATOM   5710 C  C     . PRO B 1 339 ? 20.356  15.428  32.307  1.00 31.00 ? 318 PRO B C     1 
ATOM   5711 O  O     . PRO B 1 339 ? 19.828  14.360  31.974  1.00 36.21 ? 318 PRO B O     1 
ATOM   5712 C  CB    . PRO B 1 339 ? 22.806  15.102  32.652  1.00 32.47 ? 318 PRO B CB    1 
ATOM   5713 C  CG    . PRO B 1 339 ? 23.929  16.102  32.718  1.00 35.26 ? 318 PRO B CG    1 
ATOM   5714 C  CD    . PRO B 1 339 ? 23.241  17.443  32.663  1.00 30.36 ? 318 PRO B CD    1 
ATOM   5715 N  N     . ASP B 1 340 ? 19.774  16.311  33.104  1.00 26.92 ? 319 ASP B N     1 
ATOM   5716 C  CA    . ASP B 1 340 ? 18.479  16.011  33.772  1.00 31.20 ? 319 ASP B CA    1 
ATOM   5717 C  C     . ASP B 1 340 ? 17.384  16.981  33.293  1.00 31.26 ? 319 ASP B C     1 
ATOM   5718 O  O     . ASP B 1 340 ? 16.467  17.232  34.078  1.00 32.34 ? 319 ASP B O     1 
ATOM   5719 C  CB    . ASP B 1 340 ? 18.638  16.090  35.293  1.00 34.04 ? 319 ASP B CB    1 
ATOM   5720 C  CG    . ASP B 1 340 ? 17.584  15.331  36.082  1.00 37.67 ? 319 ASP B CG    1 
ATOM   5721 O  OD1   . ASP B 1 340 ? 16.945  14.458  35.468  1.00 39.15 ? 319 ASP B OD1   1 
ATOM   5722 O  OD2   . ASP B 1 340 ? 17.423  15.611  37.317  1.00 40.28 ? 319 ASP B OD2   1 
ATOM   5723 N  N     . GLU B 1 341 ? 17.495  17.543  32.086  1.00 26.42 ? 320 GLU B N     1 
ATOM   5724 C  CA    . GLU B 1 341 ? 16.484  18.477  31.527  1.00 22.32 ? 320 GLU B CA    1 
ATOM   5725 C  C     . GLU B 1 341 ? 16.020  17.947  30.183  1.00 22.86 ? 320 GLU B C     1 
ATOM   5726 O  O     . GLU B 1 341 ? 16.705  17.142  29.566  1.00 22.36 ? 320 GLU B O     1 
ATOM   5727 C  CB    . GLU B 1 341 ? 17.039  19.889  31.328  1.00 24.27 ? 320 GLU B CB    1 
ATOM   5728 C  CG    . GLU B 1 341 ? 17.432  20.561  32.630  1.00 24.19 ? 320 GLU B CG    1 
ATOM   5729 C  CD    . GLU B 1 341 ? 16.288  20.966  33.538  1.00 26.16 ? 320 GLU B CD    1 
ATOM   5730 O  OE1   . GLU B 1 341 ? 16.544  21.130  34.764  1.00 23.80 ? 320 GLU B OE1   1 
ATOM   5731 O  OE2   . GLU B 1 341 ? 15.116  21.122  33.014  1.00 26.11 ? 320 GLU B OE2   1 
ATOM   5732 N  N     . PRO B 1 342 ? 14.855  18.411  29.698  1.00 22.70 ? 321 PRO B N     1 
ATOM   5733 C  CA    . PRO B 1 342 ? 14.336  17.965  28.402  1.00 23.18 ? 321 PRO B CA    1 
ATOM   5734 C  C     . PRO B 1 342 ? 15.230  18.367  27.223  1.00 22.56 ? 321 PRO B C     1 
ATOM   5735 O  O     . PRO B 1 342 ? 15.145  17.702  26.166  1.00 22.86 ? 321 PRO B O     1 
ATOM   5736 C  CB    . PRO B 1 342 ? 12.974  18.642  28.262  1.00 23.61 ? 321 PRO B CB    1 
ATOM   5737 C  CG    . PRO B 1 342 ? 12.739  19.458  29.533  1.00 26.35 ? 321 PRO B CG    1 
ATOM   5738 C  CD    . PRO B 1 342 ? 13.942  19.300  30.433  1.00 23.89 ? 321 PRO B CD    1 
ATOM   5739 N  N     . ILE B 1 343 ? 15.987  19.458  27.391  1.00 20.71 ? 322 ILE B N     1 
ATOM   5740 C  CA    . ILE B 1 343 ? 16.977  19.993  26.402  1.00 23.60 ? 322 ILE B CA    1 
ATOM   5741 C  C     . ILE B 1 343 ? 18.355  19.627  26.951  1.00 24.55 ? 322 ILE B C     1 
ATOM   5742 O  O     . ILE B 1 343 ? 18.716  20.136  28.029  1.00 26.59 ? 322 ILE B O     1 
ATOM   5743 C  CB    . ILE B 1 343 ? 16.869  21.525  26.201  1.00 28.50 ? 322 ILE B CB    1 
ATOM   5744 C  CG1   . ILE B 1 343 ? 15.457  21.984  25.834  1.00 30.64 ? 322 ILE B CG1   1 
ATOM   5745 C  CG2   . ILE B 1 343 ? 17.887  22.061  25.214  1.00 32.29 ? 322 ILE B CG2   1 
ATOM   5746 C  CD1   . ILE B 1 343 ? 14.848  21.203  24.744  1.00 36.72 ? 322 ILE B CD1   1 
ATOM   5747 N  N     . GLY B 1 344 ? 19.091  18.788  26.232  1.00 24.13 ? 323 GLY B N     1 
ATOM   5748 C  CA    . GLY B 1 344 ? 20.393  18.292  26.709  1.00 25.71 ? 323 GLY B CA    1 
ATOM   5749 C  C     . GLY B 1 344 ? 21.529  19.243  26.359  1.00 26.51 ? 323 GLY B C     1 
ATOM   5750 O  O     . GLY B 1 344 ? 22.460  19.349  27.195  1.00 23.27 ? 323 GLY B O     1 
ATOM   5751 N  N     . VAL B 1 345 ? 21.506  19.833  25.153  1.00 23.91 ? 324 VAL B N     1 
ATOM   5752 C  CA    . VAL B 1 345 ? 22.650  20.656  24.653  1.00 25.37 ? 324 VAL B CA    1 
ATOM   5753 C  C     . VAL B 1 345 ? 22.132  21.775  23.750  1.00 22.06 ? 324 VAL B C     1 
ATOM   5754 O  O     . VAL B 1 345 ? 21.145  21.558  22.999  1.00 24.69 ? 324 VAL B O     1 
ATOM   5755 C  CB    . VAL B 1 345 ? 23.704  19.800  23.923  1.00 26.51 ? 324 VAL B CB    1 
ATOM   5756 C  CG1   . VAL B 1 345 ? 23.149  19.275  22.611  1.00 27.59 ? 324 VAL B CG1   1 
ATOM   5757 C  CG2   . VAL B 1 345 ? 24.992  20.608  23.715  1.00 27.21 ? 324 VAL B CG2   1 
ATOM   5758 N  N     . THR B 1 346 ? 22.802  22.932  23.829  1.00 19.52 ? 325 THR B N     1 
ATOM   5759 C  CA    . THR B 1 346 ? 22.549  24.082  22.956  1.00 16.67 ? 325 THR B CA    1 
ATOM   5760 C  C     . THR B 1 346 ? 23.863  24.601  22.346  1.00 16.95 ? 325 THR B C     1 
ATOM   5761 O  O     . THR B 1 346 ? 24.974  24.334  22.869  1.00 18.77 ? 325 THR B O     1 
ATOM   5762 C  CB    . THR B 1 346 ? 21.836  25.218  23.714  1.00 17.47 ? 325 THR B CB    1 
ATOM   5763 O  OG1   . THR B 1 346 ? 22.754  25.757  24.660  1.00 19.71 ? 325 THR B OG1   1 
ATOM   5764 C  CG2   . THR B 1 346 ? 20.551  24.783  24.380  1.00 19.43 ? 325 THR B CG2   1 
ATOM   5765 N  N     . PHE B 1 347 ? 23.703  25.421  21.334  1.00 18.24 ? 326 PHE B N     1 
ATOM   5766 C  CA    . PHE B 1 347 ? 24.819  26.074  20.617  1.00 21.44 ? 326 PHE B CA    1 
ATOM   5767 C  C     . PHE B 1 347 ? 24.432  27.508  20.278  1.00 21.79 ? 326 PHE B C     1 
ATOM   5768 O  O     . PHE B 1 347 ? 23.264  27.806  19.999  1.00 23.07 ? 326 PHE B O     1 
ATOM   5769 C  CB    . PHE B 1 347 ? 25.160  25.322  19.331  1.00 22.09 ? 326 PHE B CB    1 
ATOM   5770 C  CG    . PHE B 1 347 ? 25.782  23.967  19.547  1.00 21.89 ? 326 PHE B CG    1 
ATOM   5771 C  CD1   . PHE B 1 347 ? 27.160  23.819  19.626  1.00 23.98 ? 326 PHE B CD1   1 
ATOM   5772 C  CD2   . PHE B 1 347 ? 24.991  22.843  19.749  1.00 22.62 ? 326 PHE B CD2   1 
ATOM   5773 C  CE1   . PHE B 1 347 ? 27.738  22.570  19.791  1.00 22.53 ? 326 PHE B CE1   1 
ATOM   5774 C  CE2   . PHE B 1 347 ? 25.573  21.598  19.941  1.00 22.35 ? 326 PHE B CE2   1 
ATOM   5775 C  CZ    . PHE B 1 347 ? 26.932  21.468  19.993  1.00 23.95 ? 326 PHE B CZ    1 
ATOM   5776 N  N     . ASP B 1 348 ? 25.430  28.381  20.251  1.00 21.29 ? 327 ASP B N     1 
ATOM   5777 C  CA    . ASP B 1 348 ? 25.280  29.724  19.634  1.00 21.25 ? 327 ASP B CA    1 
ATOM   5778 C  C     . ASP B 1 348 ? 25.054  29.550  18.135  1.00 22.09 ? 327 ASP B C     1 
ATOM   5779 O  O     . ASP B 1 348 ? 25.974  29.053  17.457  1.00 24.50 ? 327 ASP B O     1 
ATOM   5780 C  CB    . ASP B 1 348 ? 26.447  30.625  20.034  1.00 20.17 ? 327 ASP B CB    1 
ATOM   5781 C  CG    . ASP B 1 348 ? 26.309  32.080  19.593  1.00 25.14 ? 327 ASP B CG    1 
ATOM   5782 O  OD1   . ASP B 1 348 ? 25.576  32.334  18.653  1.00 24.50 ? 327 ASP B OD1   1 
ATOM   5783 O  OD2   . ASP B 1 348 ? 26.999  32.943  20.188  1.00 25.85 ? 327 ASP B OD2   1 
ATOM   5784 N  N     . GLY B 1 349 ? 23.886  29.972  17.632  1.00 20.60 ? 328 GLY B N     1 
ATOM   5785 C  CA    . GLY B 1 349 ? 23.450  29.761  16.233  1.00 21.12 ? 328 GLY B CA    1 
ATOM   5786 C  C     . GLY B 1 349 ? 23.548  31.035  15.415  1.00 19.88 ? 328 GLY B C     1 
ATOM   5787 O  O     . GLY B 1 349 ? 23.011  31.054  14.332  1.00 20.55 ? 328 GLY B O     1 
ATOM   5788 N  N     . THR B 1 350 ? 24.116  32.092  16.017  1.00 22.24 ? 329 THR B N     1 
ATOM   5789 C  CA    . THR B 1 350 ? 24.132  33.465  15.472  1.00 22.59 ? 329 THR B CA    1 
ATOM   5790 C  C     . THR B 1 350 ? 24.935  33.457  14.174  1.00 22.38 ? 329 THR B C     1 
ATOM   5791 O  O     . THR B 1 350 ? 26.019  32.897  14.171  1.00 21.89 ? 329 THR B O     1 
ATOM   5792 C  CB    . THR B 1 350 ? 24.774  34.414  16.501  1.00 23.75 ? 329 THR B CB    1 
ATOM   5793 O  OG1   . THR B 1 350 ? 24.070  34.329  17.718  1.00 21.27 ? 329 THR B OG1   1 
ATOM   5794 C  CG2   . THR B 1 350 ? 24.782  35.869  16.092  1.00 24.84 ? 329 THR B CG2   1 
ATOM   5795 N  N     . PRO B 1 351 ? 24.469  34.120  13.082  1.00 22.44 ? 330 PRO B N     1 
ATOM   5796 C  CA    . PRO B 1 351 ? 25.224  34.184  11.834  1.00 23.52 ? 330 PRO B CA    1 
ATOM   5797 C  C     . PRO B 1 351 ? 26.398  35.162  11.914  1.00 25.06 ? 330 PRO B C     1 
ATOM   5798 O  O     . PRO B 1 351 ? 26.498  35.950  12.863  1.00 24.27 ? 330 PRO B O     1 
ATOM   5799 C  CB    . PRO B 1 351 ? 24.206  34.691  10.809  1.00 22.87 ? 330 PRO B CB    1 
ATOM   5800 C  CG    . PRO B 1 351 ? 23.254  35.555  11.625  1.00 23.25 ? 330 PRO B CG    1 
ATOM   5801 C  CD    . PRO B 1 351 ? 23.192  34.852  12.984  1.00 22.99 ? 330 PRO B CD    1 
ATOM   5802 N  N     . PRO B 1 352 ? 27.354  35.081  10.967  1.00 26.11 ? 331 PRO B N     1 
ATOM   5803 C  CA    . PRO B 1 352 ? 28.545  35.929  11.017  1.00 27.74 ? 331 PRO B CA    1 
ATOM   5804 C  C     . PRO B 1 352 ? 28.245  37.427  11.216  1.00 25.57 ? 331 PRO B C     1 
ATOM   5805 O  O     . PRO B 1 352 ? 29.043  38.113  11.833  1.00 25.90 ? 331 PRO B O     1 
ATOM   5806 C  CB    . PRO B 1 352 ? 29.144  35.698  9.631   1.00 28.12 ? 331 PRO B CB    1 
ATOM   5807 C  CG    . PRO B 1 352 ? 28.818  34.232  9.362   1.00 27.83 ? 331 PRO B CG    1 
ATOM   5808 C  CD    . PRO B 1 352 ? 27.380  34.155  9.821   1.00 26.35 ? 331 PRO B CD    1 
ATOM   5809 N  N     . ALA B 1 353 ? 27.151  37.925  10.660  1.00 26.38 ? 332 ALA B N     1 
ATOM   5810 C  CA    . ALA B 1 353 ? 26.807  39.370  10.772  1.00 30.79 ? 332 ALA B CA    1 
ATOM   5811 C  C     . ALA B 1 353 ? 26.575  39.753  12.247  1.00 30.47 ? 332 ALA B C     1 
ATOM   5812 O  O     . ALA B 1 353 ? 26.667  40.942  12.576  1.00 29.23 ? 332 ALA B O     1 
ATOM   5813 C  CB    . ALA B 1 353 ? 25.625  39.701  9.890   1.00 29.68 ? 332 ALA B CB    1 
ATOM   5814 N  N     . GLY B 1 354 ? 26.326  38.803  13.161  1.00 27.34 ? 333 GLY B N     1 
ATOM   5815 C  CA    . GLY B 1 354 ? 26.303  39.105  14.601  1.00 24.86 ? 333 GLY B CA    1 
ATOM   5816 C  C     . GLY B 1 354 ? 24.899  39.357  15.136  1.00 26.34 ? 333 GLY B C     1 
ATOM   5817 O  O     . GLY B 1 354 ? 24.793  39.497  16.345  1.00 27.51 ? 333 GLY B O     1 
ATOM   5818 N  N     . THR B 1 355 ? 23.880  39.449  14.271  1.00 23.41 ? 334 THR B N     1 
ATOM   5819 C  CA    . THR B 1 355 ? 22.445  39.564  14.616  1.00 26.62 ? 334 THR B CA    1 
ATOM   5820 C  C     . THR B 1 355 ? 21.665  38.843  13.538  1.00 26.63 ? 334 THR B C     1 
ATOM   5821 O  O     . THR B 1 355 ? 22.175  38.717  12.425  1.00 26.53 ? 334 THR B O     1 
ATOM   5822 C  CB    . THR B 1 355 ? 21.957  41.022  14.705  1.00 28.64 ? 334 THR B CB    1 
ATOM   5823 O  OG1   . THR B 1 355 ? 22.087  41.576  13.396  1.00 28.11 ? 334 THR B OG1   1 
ATOM   5824 C  CG2   . THR B 1 355 ? 22.730  41.823  15.734  1.00 28.99 ? 334 THR B CG2   1 
ATOM   5825 N  N     . PRO B 1 356 ? 20.471  38.281  13.823  1.00 25.76 ? 335 PRO B N     1 
ATOM   5826 C  CA    . PRO B 1 356 ? 19.923  38.193  15.181  1.00 25.11 ? 335 PRO B CA    1 
ATOM   5827 C  C     . PRO B 1 356 ? 20.714  37.198  16.053  1.00 25.21 ? 335 PRO B C     1 
ATOM   5828 O  O     . PRO B 1 356 ? 21.470  36.394  15.488  1.00 25.95 ? 335 PRO B O     1 
ATOM   5829 C  CB    . PRO B 1 356 ? 18.514  37.643  14.936  1.00 24.55 ? 335 PRO B CB    1 
ATOM   5830 C  CG    . PRO B 1 356 ? 18.693  36.769  13.696  1.00 26.48 ? 335 PRO B CG    1 
ATOM   5831 C  CD    . PRO B 1 356 ? 19.631  37.586  12.824  1.00 24.59 ? 335 PRO B CD    1 
ATOM   5832 N  N     . GLY B 1 357 ? 20.601  37.299  17.379  1.00 23.25 ? 336 GLY B N     1 
ATOM   5833 C  CA    . GLY B 1 357 ? 21.148  36.289  18.298  1.00 25.00 ? 336 GLY B CA    1 
ATOM   5834 C  C     . GLY B 1 357 ? 20.352  34.999  18.143  1.00 22.18 ? 336 GLY B C     1 
ATOM   5835 O  O     . GLY B 1 357 ? 19.110  35.098  18.061  1.00 23.02 ? 336 GLY B O     1 
ATOM   5836 N  N     . ILE B 1 358 ? 21.019  33.848  18.069  1.00 21.57 ? 337 ILE B N     1 
ATOM   5837 C  CA    . ILE B 1 358 ? 20.245  32.574  17.967  1.00 21.37 ? 337 ILE B CA    1 
ATOM   5838 C  C     . ILE B 1 358 ? 20.810  31.586  18.983  1.00 19.18 ? 337 ILE B C     1 
ATOM   5839 O  O     . ILE B 1 358 ? 22.018  31.450  19.065  1.00 19.16 ? 337 ILE B O     1 
ATOM   5840 C  CB    . ILE B 1 358 ? 20.245  32.022  16.528  1.00 21.03 ? 337 ILE B CB    1 
ATOM   5841 C  CG1   . ILE B 1 358 ? 19.614  33.003  15.528  1.00 20.97 ? 337 ILE B CG1   1 
ATOM   5842 C  CG2   . ILE B 1 358 ? 19.542  30.682  16.501  1.00 20.81 ? 337 ILE B CG2   1 
ATOM   5843 C  CD1   . ILE B 1 358 ? 19.597  32.486  14.106  1.00 22.84 ? 337 ILE B CD1   1 
ATOM   5844 N  N     . VAL B 1 359 ? 19.934  30.920  19.726  1.00 20.71 ? 338 VAL B N     1 
ATOM   5845 C  CA    . VAL B 1 359 ? 20.296  29.744  20.552  1.00 20.04 ? 338 VAL B CA    1 
ATOM   5846 C  C     . VAL B 1 359 ? 19.651  28.512  19.904  1.00 20.01 ? 338 VAL B C     1 
ATOM   5847 O  O     . VAL B 1 359 ? 18.416  28.486  19.816  1.00 18.48 ? 338 VAL B O     1 
ATOM   5848 C  CB    . VAL B 1 359 ? 19.855  29.871  22.009  1.00 22.22 ? 338 VAL B CB    1 
ATOM   5849 C  CG1   . VAL B 1 359 ? 20.249  28.614  22.755  1.00 20.26 ? 338 VAL B CG1   1 
ATOM   5850 C  CG2   . VAL B 1 359 ? 20.495  31.089  22.689  1.00 23.03 ? 338 VAL B CG2   1 
ATOM   5851 N  N     . THR B 1 360 ? 20.479  27.611  19.399  1.00 19.72 ? 339 THR B N     1 
ATOM   5852 C  CA    . THR B 1 360 ? 20.031  26.381  18.697  1.00 17.85 ? 339 THR B CA    1 
ATOM   5853 C  C     . THR B 1 360 ? 20.096  25.220  19.681  1.00 18.51 ? 339 THR B C     1 
ATOM   5854 O  O     . THR B 1 360 ? 21.061  25.111  20.464  1.00 17.76 ? 339 THR B O     1 
ATOM   5855 C  CB    . THR B 1 360 ? 20.904  26.088  17.470  1.00 18.40 ? 339 THR B CB    1 
ATOM   5856 O  OG1   . THR B 1 360 ? 20.898  27.223  16.597  1.00 18.38 ? 339 THR B OG1   1 
ATOM   5857 C  CG2   . THR B 1 360 ? 20.405  24.887  16.689  1.00 18.30 ? 339 THR B CG2   1 
ATOM   5858 N  N     . GLY B 1 361 ? 19.115  24.319  19.639  1.00 17.79 ? 340 GLY B N     1 
ATOM   5859 C  CA    . GLY B 1 361 ? 19.206  23.158  20.520  1.00 18.33 ? 340 GLY B CA    1 
ATOM   5860 C  C     . GLY B 1 361 ? 18.247  22.083  20.091  1.00 17.15 ? 340 GLY B C     1 
ATOM   5861 O  O     . GLY B 1 361 ? 17.620  22.201  19.008  1.00 16.55 ? 340 GLY B O     1 
ATOM   5862 N  N     . PHE B 1 362 ? 18.172  21.048  20.905  1.00 16.59 ? 341 PHE B N     1 
ATOM   5863 C  CA    . PHE B 1 362 ? 17.438  19.816  20.542  1.00 17.79 ? 341 PHE B CA    1 
ATOM   5864 C  C     . PHE B 1 362 ? 16.722  19.244  21.747  1.00 18.27 ? 341 PHE B C     1 
ATOM   5865 O  O     . PHE B 1 362 ? 17.290  19.199  22.826  1.00 17.51 ? 341 PHE B O     1 
ATOM   5866 C  CB    . PHE B 1 362 ? 18.449  18.781  20.035  1.00 19.04 ? 341 PHE B CB    1 
ATOM   5867 C  CG    . PHE B 1 362 ? 19.364  19.305  18.963  1.00 19.99 ? 341 PHE B CG    1 
ATOM   5868 C  CD1   . PHE B 1 362 ? 19.086  19.080  17.631  1.00 20.54 ? 341 PHE B CD1   1 
ATOM   5869 C  CD2   . PHE B 1 362 ? 20.517  20.010  19.289  1.00 24.64 ? 341 PHE B CD2   1 
ATOM   5870 C  CE1   . PHE B 1 362 ? 19.893  19.608  16.633  1.00 23.43 ? 341 PHE B CE1   1 
ATOM   5871 C  CE2   . PHE B 1 362 ? 21.322  20.540  18.287  1.00 24.17 ? 341 PHE B CE2   1 
ATOM   5872 C  CZ    . PHE B 1 362 ? 21.006  20.336  16.969  1.00 24.58 ? 341 PHE B CZ    1 
ATOM   5873 N  N     . PHE B 1 363 ? 15.503  18.769  21.517  1.00 16.72 ? 342 PHE B N     1 
ATOM   5874 C  CA    . PHE B 1 363 ? 14.866  17.708  22.331  1.00 16.79 ? 342 PHE B CA    1 
ATOM   5875 C  C     . PHE B 1 363 ? 15.257  16.382  21.667  1.00 15.93 ? 342 PHE B C     1 
ATOM   5876 O  O     . PHE B 1 363 ? 15.020  16.288  20.482  1.00 17.45 ? 342 PHE B O     1 
ATOM   5877 C  CB    . PHE B 1 363 ? 13.344  17.857  22.344  1.00 18.45 ? 342 PHE B CB    1 
ATOM   5878 C  CG    . PHE B 1 363 ? 12.749  19.138  22.899  1.00 17.45 ? 342 PHE B CG    1 
ATOM   5879 C  CD1   . PHE B 1 363 ? 12.183  19.150  24.158  1.00 18.76 ? 342 PHE B CD1   1 
ATOM   5880 C  CD2   . PHE B 1 363 ? 12.692  20.287  22.132  1.00 19.05 ? 342 PHE B CD2   1 
ATOM   5881 C  CE1   . PHE B 1 363 ? 11.580  20.292  24.662  1.00 18.66 ? 342 PHE B CE1   1 
ATOM   5882 C  CE2   . PHE B 1 363 ? 12.066  21.428  22.630  1.00 19.56 ? 342 PHE B CE2   1 
ATOM   5883 C  CZ    . PHE B 1 363 ? 11.505  21.426  23.877  1.00 17.80 ? 342 PHE B CZ    1 
ATOM   5884 N  N     . GLU B 1 364 ? 15.768  15.409  22.416  1.00 16.11 ? 343 GLU B N     1 
ATOM   5885 C  CA    . GLU B 1 364 ? 16.251  14.119  21.864  1.00 17.65 ? 343 GLU B CA    1 
ATOM   5886 C  C     . GLU B 1 364 ? 15.471  12.962  22.484  1.00 18.17 ? 343 GLU B C     1 
ATOM   5887 O  O     . GLU B 1 364 ? 15.185  13.003  23.697  1.00 16.42 ? 343 GLU B O     1 
ATOM   5888 C  CB    . GLU B 1 364 ? 17.736  13.968  22.171  1.00 20.15 ? 343 GLU B CB    1 
ATOM   5889 C  CG    . GLU B 1 364 ? 18.579  15.113  21.631  1.00 21.64 ? 343 GLU B CG    1 
ATOM   5890 C  CD    . GLU B 1 364 ? 18.886  15.031  20.156  1.00 21.09 ? 343 GLU B CD    1 
ATOM   5891 O  OE1   . GLU B 1 364 ? 18.256  14.171  19.464  1.00 21.53 ? 343 GLU B OE1   1 
ATOM   5892 O  OE2   . GLU B 1 364 ? 19.771  15.830  19.693  1.00 20.58 ? 343 GLU B OE2   1 
ATOM   5893 N  N     . GLY B 1 365 ? 15.273  11.879  21.720  1.00 17.45 ? 344 GLY B N     1 
ATOM   5894 C  CA    . GLY B 1 365 ? 14.792  10.629  22.313  1.00 18.22 ? 344 GLY B CA    1 
ATOM   5895 C  C     . GLY B 1 365 ? 13.479  10.843  23.038  1.00 18.69 ? 344 GLY B C     1 
ATOM   5896 O  O     . GLY B 1 365 ? 12.579  11.458  22.484  1.00 18.83 ? 344 GLY B O     1 
ATOM   5897 N  N     . PRO B 1 366 ? 13.321  10.309  24.266  1.00 18.21 ? 345 PRO B N     1 
ATOM   5898 C  CA    . PRO B 1 366 ? 12.068  10.430  25.011  1.00 21.18 ? 345 PRO B CA    1 
ATOM   5899 C  C     . PRO B 1 366 ? 11.588  11.877  25.149  1.00 19.88 ? 345 PRO B C     1 
ATOM   5900 O  O     . PRO B 1 366 ? 10.385  12.106  25.043  1.00 19.18 ? 345 PRO B O     1 
ATOM   5901 C  CB    . PRO B 1 366 ? 12.386  9.801   26.368  1.00 20.83 ? 345 PRO B CB    1 
ATOM   5902 C  CG    . PRO B 1 366 ? 13.478  8.830   26.024  1.00 22.28 ? 345 PRO B CG    1 
ATOM   5903 C  CD    . PRO B 1 366 ? 14.343  9.607   25.051  1.00 20.66 ? 345 PRO B CD    1 
ATOM   5904 N  N     . ALA B 1 367 ? 12.506  12.822  25.354  1.00 16.87 ? 346 ALA B N     1 
ATOM   5905 C  CA    . ALA B 1 367 ? 12.143  14.254  25.455  1.00 17.80 ? 346 ALA B CA    1 
ATOM   5906 C  C     . ALA B 1 367 ? 11.539  14.743  24.118  1.00 17.41 ? 346 ALA B C     1 
ATOM   5907 O  O     . ALA B 1 367 ? 10.593  15.552  24.183  1.00 17.79 ? 346 ALA B O     1 
ATOM   5908 C  CB    . ALA B 1 367 ? 13.331  15.096  25.876  1.00 18.48 ? 346 ALA B CB    1 
ATOM   5909 N  N     . ALA B 1 368 ? 12.017  14.251  22.951  1.00 18.01 ? 347 ALA B N     1 
ATOM   5910 C  CA    . ALA B 1 368 ? 11.506  14.639  21.615  1.00 18.37 ? 347 ALA B CA    1 
ATOM   5911 C  C     . ALA B 1 368 ? 10.087  14.096  21.445  1.00 17.14 ? 347 ALA B C     1 
ATOM   5912 O  O     . ALA B 1 368 ? 9.264   14.811  20.936  1.00 16.83 ? 347 ALA B O     1 
ATOM   5913 C  CB    . ALA B 1 368 ? 12.403  14.093  20.525  1.00 17.28 ? 347 ALA B CB    1 
ATOM   5914 N  N     . VAL B 1 369 ? 9.826   12.868  21.893  1.00 16.08 ? 348 VAL B N     1 
ATOM   5915 C  CA    . VAL B 1 369 ? 8.483   12.235  21.707  1.00 16.51 ? 348 VAL B CA    1 
ATOM   5916 C  C     . VAL B 1 369 ? 7.493   12.973  22.619  1.00 17.25 ? 348 VAL B C     1 
ATOM   5917 O  O     . VAL B 1 369 ? 6.374   13.275  22.172  1.00 17.85 ? 348 VAL B O     1 
ATOM   5918 C  CB    . VAL B 1 369 ? 8.545   10.721  21.959  1.00 17.20 ? 348 VAL B CB    1 
ATOM   5919 C  CG1   . VAL B 1 369 ? 7.166   10.103  21.722  1.00 18.84 ? 348 VAL B CG1   1 
ATOM   5920 C  CG2   . VAL B 1 369 ? 9.609   10.070  21.076  1.00 16.78 ? 348 VAL B CG2   1 
ATOM   5921 N  N     . ALA B 1 370 ? 7.881   13.305  23.843  1.00 17.19 ? 349 ALA B N     1 
ATOM   5922 C  CA    . ALA B 1 370 ? 7.009   14.071  24.779  1.00 21.12 ? 349 ALA B CA    1 
ATOM   5923 C  C     . ALA B 1 370 ? 6.724   15.455  24.186  1.00 20.52 ? 349 ALA B C     1 
ATOM   5924 O  O     . ALA B 1 370 ? 5.571   15.874  24.156  1.00 20.45 ? 349 ALA B O     1 
ATOM   5925 C  CB    . ALA B 1 370 ? 7.657   14.213  26.127  1.00 20.68 ? 349 ALA B CB    1 
ATOM   5926 N  N     . ALA B 1 371 ? 7.764   16.150  23.707  1.00 20.77 ? 350 ALA B N     1 
ATOM   5927 C  CA    . ALA B 1 371 ? 7.616   17.529  23.185  1.00 20.07 ? 350 ALA B CA    1 
ATOM   5928 C  C     . ALA B 1 371 ? 6.810   17.523  21.889  1.00 19.27 ? 350 ALA B C     1 
ATOM   5929 O  O     . ALA B 1 371 ? 6.034   18.470  21.610  1.00 19.14 ? 350 ALA B O     1 
ATOM   5930 C  CB    . ALA B 1 371 ? 8.975   18.169  23.021  1.00 21.31 ? 350 ALA B CB    1 
ATOM   5931 N  N     . GLY B 1 372 ? 6.992   16.505  21.046  1.00 18.38 ? 351 GLY B N     1 
ATOM   5932 C  CA    . GLY B 1 372 ? 6.287   16.467  19.757  1.00 20.08 ? 351 GLY B CA    1 
ATOM   5933 C  C     . GLY B 1 372 ? 4.781   16.358  19.953  1.00 19.91 ? 351 GLY B C     1 
ATOM   5934 O  O     . GLY B 1 372 ? 4.027   16.683  19.028  1.00 21.77 ? 351 GLY B O     1 
ATOM   5935 N  N     . ALA B 1 373 ? 4.325   15.892  21.112  1.00 22.46 ? 352 ALA B N     1 
ATOM   5936 C  CA    . ALA B 1 373 ? 2.885   15.745  21.430  1.00 22.53 ? 352 ALA B CA    1 
ATOM   5937 C  C     . ALA B 1 373 ? 2.284   17.079  21.891  1.00 27.25 ? 352 ALA B C     1 
ATOM   5938 O  O     . ALA B 1 373 ? 1.061   17.183  22.027  1.00 23.76 ? 352 ALA B O     1 
ATOM   5939 C  CB    . ALA B 1 373 ? 2.745   14.663  22.469  1.00 25.37 ? 352 ALA B CB    1 
ATOM   5940 N  N     . ARG B 1 374 ? 3.110   18.096  22.107  1.00 24.08 ? 353 ARG B N     1 
ATOM   5941 C  CA    . ARG B 1 374 ? 2.668   19.409  22.626  1.00 25.37 ? 353 ARG B CA    1 
ATOM   5942 C  C     . ARG B 1 374 ? 2.702   20.419  21.481  1.00 23.93 ? 353 ARG B C     1 
ATOM   5943 O  O     . ARG B 1 374 ? 3.156   20.041  20.418  1.00 22.62 ? 353 ARG B O     1 
ATOM   5944 C  CB    . ARG B 1 374 ? 3.608   19.769  23.776  1.00 25.86 ? 353 ARG B CB    1 
ATOM   5945 C  CG    . ARG B 1 374 ? 3.545   18.744  24.904  1.00 27.79 ? 353 ARG B CG    1 
ATOM   5946 C  CD    . ARG B 1 374 ? 4.311   19.185  26.104  1.00 33.28 ? 353 ARG B CD    1 
ATOM   5947 N  NE    . ARG B 1 374 ? 3.533   20.138  26.881  1.00 33.69 ? 353 ARG B NE    1 
ATOM   5948 C  CZ    . ARG B 1 374 ? 4.032   20.977  27.791  1.00 36.40 ? 353 ARG B CZ    1 
ATOM   5949 N  NH1   . ARG B 1 374 ? 5.326   21.013  28.058  1.00 36.74 ? 353 ARG B NH1   1 
ATOM   5950 N  NH2   . ARG B 1 374 ? 3.216   21.796  28.432  1.00 34.03 ? 353 ARG B NH2   1 
ATOM   5951 N  N     . THR B 1 375 ? 2.272   21.653  21.711  1.00 21.23 ? 354 THR B N     1 
ATOM   5952 C  CA    . THR B 1 375 ? 2.254   22.716  20.673  1.00 22.48 ? 354 THR B CA    1 
ATOM   5953 C  C     . THR B 1 375 ? 3.638   23.362  20.587  1.00 21.56 ? 354 THR B C     1 
ATOM   5954 O  O     . THR B 1 375 ? 4.408   23.253  21.558  1.00 20.28 ? 354 THR B O     1 
ATOM   5955 C  CB    . THR B 1 375 ? 1.208   23.802  20.929  1.00 23.35 ? 354 THR B CB    1 
ATOM   5956 O  OG1   . THR B 1 375 ? 1.642   24.501  22.094  1.00 25.63 ? 354 THR B OG1   1 
ATOM   5957 C  CG2   . THR B 1 375 ? -0.208  23.278  21.041  1.00 25.78 ? 354 THR B CG2   1 
ATOM   5958 N  N     . ARG B 1 376 ? 3.903   24.057  19.476  1.00 22.37 ? 355 ARG B N     1 
ATOM   5959 C  CA    . ARG B 1 376 ? 5.111   24.901  19.302  1.00 24.84 ? 355 ARG B CA    1 
ATOM   5960 C  C     . ARG B 1 376 ? 5.253   25.852  20.508  1.00 23.29 ? 355 ARG B C     1 
ATOM   5961 O  O     . ARG B 1 376 ? 6.353   25.956  21.040  1.00 22.15 ? 355 ARG B O     1 
ATOM   5962 C  CB    . ARG B 1 376 ? 5.062   25.707  18.007  1.00 26.86 ? 355 ARG B CB    1 
ATOM   5963 C  CG    . ARG B 1 376 ? 6.323   26.534  17.750  1.00 33.16 ? 355 ARG B CG    1 
ATOM   5964 C  CD    . ARG B 1 376 ? 6.212   27.573  16.631  1.00 39.36 ? 355 ARG B CD    1 
ATOM   5965 N  NE    . ARG B 1 376 ? 5.259   28.649  16.950  1.00 44.40 ? 355 ARG B NE    1 
ATOM   5966 C  CZ    . ARG B 1 376 ? 5.521   29.831  17.550  1.00 43.28 ? 355 ARG B CZ    1 
ATOM   5967 N  NH1   . ARG B 1 376 ? 6.738   30.214  17.918  1.00 37.27 ? 355 ARG B NH1   1 
ATOM   5968 N  NH2   . ARG B 1 376 ? 4.517   30.648  17.800  1.00 43.47 ? 355 ARG B NH2   1 
ATOM   5969 N  N     . GLU B 1 377 ? 4.194   26.548  20.897  1.00 21.46 ? 356 GLU B N     1 
ATOM   5970 C  CA    . GLU B 1 377 ? 4.250   27.527  22.008  1.00 25.07 ? 356 GLU B CA    1 
ATOM   5971 C  C     . GLU B 1 377 ? 4.601   26.814  23.315  1.00 19.92 ? 356 GLU B C     1 
ATOM   5972 O  O     . GLU B 1 377 ? 5.385   27.366  24.108  1.00 24.07 ? 356 GLU B O     1 
ATOM   5973 C  CB    . GLU B 1 377 ? 2.927   28.293  22.098  1.00 30.33 ? 356 GLU B CB    1 
ATOM   5974 C  CG    . GLU B 1 377 ? 2.633   29.122  20.862  1.00 35.71 ? 356 GLU B CG    1 
ATOM   5975 C  CD    . GLU B 1 377 ? 2.048   28.382  19.649  1.00 48.43 ? 356 GLU B CD    1 
ATOM   5976 O  OE1   . GLU B 1 377 ? 2.085   28.978  18.518  1.00 47.08 ? 356 GLU B OE1   1 
ATOM   5977 O  OE2   . GLU B 1 377 ? 1.569   27.193  19.802  1.00 40.98 ? 356 GLU B OE2   1 
ATOM   5978 N  N     . GLU B 1 378 ? 4.095   25.615  23.524  1.00 21.85 ? 357 GLU B N     1 
ATOM   5979 C  CA    . GLU B 1 378 ? 4.440   24.835  24.741  1.00 23.99 ? 357 GLU B CA    1 
ATOM   5980 C  C     . GLU B 1 378 ? 5.920   24.434  24.710  1.00 21.50 ? 357 GLU B C     1 
ATOM   5981 O  O     . GLU B 1 378 ? 6.589   24.533  25.769  1.00 20.19 ? 357 GLU B O     1 
ATOM   5982 C  CB    . GLU B 1 378 ? 3.531   23.619  24.889  1.00 25.38 ? 357 GLU B CB    1 
ATOM   5983 C  CG    . GLU B 1 378 ? 2.096   24.034  25.168  1.00 26.50 ? 357 GLU B CG    1 
ATOM   5984 C  CD    . GLU B 1 378 ? 1.066   22.920  25.249  1.00 32.22 ? 357 GLU B CD    1 
ATOM   5985 O  OE1   . GLU B 1 378 ? 0.131   23.086  26.018  1.00 38.73 ? 357 GLU B OE1   1 
ATOM   5986 O  OE2   . GLU B 1 378 ? 1.203   21.909  24.559  1.00 29.29 ? 357 GLU B OE2   1 
ATOM   5987 N  N     . ARG B 1 379 ? 6.438   24.006  23.549  1.00 21.57 ? 358 ARG B N     1 
ATOM   5988 C  CA    . ARG B 1 379 ? 7.881   23.653  23.431  1.00 20.80 ? 358 ARG B CA    1 
ATOM   5989 C  C     . ARG B 1 379 ? 8.745   24.890  23.690  1.00 19.35 ? 358 ARG B C     1 
ATOM   5990 O  O     . ARG B 1 379 ? 9.742   24.786  24.468  1.00 18.39 ? 358 ARG B O     1 
ATOM   5991 C  CB    . ARG B 1 379 ? 8.181   23.042  22.060  1.00 21.74 ? 358 ARG B CB    1 
ATOM   5992 C  CG    . ARG B 1 379 ? 7.570   21.660  21.900  1.00 21.43 ? 358 ARG B CG    1 
ATOM   5993 C  CD    . ARG B 1 379 ? 8.156   20.928  20.699  1.00 21.54 ? 358 ARG B CD    1 
ATOM   5994 N  NE    . ARG B 1 379 ? 7.804   21.578  19.444  1.00 23.13 ? 358 ARG B NE    1 
ATOM   5995 C  CZ    . ARG B 1 379 ? 6.748   21.262  18.706  1.00 24.16 ? 358 ARG B CZ    1 
ATOM   5996 N  NH1   . ARG B 1 379 ? 5.894   20.334  19.111  1.00 26.41 ? 358 ARG B NH1   1 
ATOM   5997 N  NH2   . ARG B 1 379 ? 6.532   21.889  17.573  1.00 24.79 ? 358 ARG B NH2   1 
ATOM   5998 N  N     . ARG B 1 380 ? 8.358   26.039  23.133  1.00 19.83 ? 359 ARG B N     1 
ATOM   5999 C  CA    . ARG B 1 380 ? 9.056   27.326  23.367  1.00 21.94 ? 359 ARG B CA    1 
ATOM   6000 C  C     . ARG B 1 380 ? 9.194   27.556  24.884  1.00 19.83 ? 359 ARG B C     1 
ATOM   6001 O  O     . ARG B 1 380 ? 10.304  27.971  25.353  1.00 20.67 ? 359 ARG B O     1 
ATOM   6002 C  CB    . ARG B 1 380 ? 8.324   28.492  22.694  1.00 22.49 ? 359 ARG B CB    1 
ATOM   6003 C  CG    . ARG B 1 380 ? 8.930   29.837  23.074  1.00 25.55 ? 359 ARG B CG    1 
ATOM   6004 C  CD    . ARG B 1 380 ? 7.994   31.014  22.813  1.00 28.90 ? 359 ARG B CD    1 
ATOM   6005 N  NE    . ARG B 1 380 ? 6.860   30.896  23.715  1.00 31.43 ? 359 ARG B NE    1 
ATOM   6006 C  CZ    . ARG B 1 380 ? 5.632   31.335  23.464  1.00 35.96 ? 359 ARG B CZ    1 
ATOM   6007 N  NH1   . ARG B 1 380 ? 5.374   31.986  22.340  1.00 33.96 ? 359 ARG B NH1   1 
ATOM   6008 N  NH2   . ARG B 1 380 ? 4.667   31.130  24.347  1.00 33.08 ? 359 ARG B NH2   1 
ATOM   6009 N  N     . ASP B 1 381 ? 8.110   27.378  25.637  1.00 21.32 ? 360 ASP B N     1 
ATOM   6010 C  CA    . ASP B 1 381 ? 8.060   27.717  27.079  1.00 22.21 ? 360 ASP B CA    1 
ATOM   6011 C  C     . ASP B 1 381 ? 8.951   26.740  27.867  1.00 19.80 ? 360 ASP B C     1 
ATOM   6012 O  O     . ASP B 1 381 ? 9.595   27.167  28.852  1.00 17.95 ? 360 ASP B O     1 
ATOM   6013 C  CB    . ASP B 1 381 ? 6.608   27.792  27.550  1.00 24.69 ? 360 ASP B CB    1 
ATOM   6014 C  CG    . ASP B 1 381 ? 5.845   28.979  26.970  1.00 29.05 ? 360 ASP B CG    1 
ATOM   6015 O  OD1   . ASP B 1 381 ? 6.470   29.867  26.306  1.00 29.30 ? 360 ASP B OD1   1 
ATOM   6016 O  OD2   . ASP B 1 381 ? 4.643   29.016  27.184  1.00 34.29 ? 360 ASP B OD2   1 
ATOM   6017 N  N     . VAL B 1 382 ? 9.071   25.494  27.404  1.00 18.69 ? 361 VAL B N     1 
ATOM   6018 C  CA    . VAL B 1 382 ? 10.039  24.534  28.002  1.00 20.53 ? 361 VAL B CA    1 
ATOM   6019 C  C     . VAL B 1 382 ? 11.464  25.041  27.739  1.00 18.99 ? 361 VAL B C     1 
ATOM   6020 O  O     . VAL B 1 382 ? 12.264  25.059  28.688  1.00 21.53 ? 361 VAL B O     1 
ATOM   6021 C  CB    . VAL B 1 382 ? 9.861   23.106  27.465  1.00 21.22 ? 361 VAL B CB    1 
ATOM   6022 C  CG1   . VAL B 1 382 ? 11.008  22.208  27.883  1.00 23.52 ? 361 VAL B CG1   1 
ATOM   6023 C  CG2   . VAL B 1 382 ? 8.530   22.508  27.872  1.00 23.99 ? 361 VAL B CG2   1 
ATOM   6024 N  N     . VAL B 1 383 ? 11.788  25.420  26.506  1.00 19.73 ? 362 VAL B N     1 
ATOM   6025 C  CA    . VAL B 1 383 ? 13.177  25.836  26.156  1.00 21.17 ? 362 VAL B CA    1 
ATOM   6026 C  C     . VAL B 1 383 ? 13.548  27.081  26.987  1.00 21.19 ? 362 VAL B C     1 
ATOM   6027 O  O     . VAL B 1 383 ? 14.611  27.108  27.640  1.00 19.74 ? 362 VAL B O     1 
ATOM   6028 C  CB    . VAL B 1 383 ? 13.268  26.091  24.656  1.00 20.40 ? 362 VAL B CB    1 
ATOM   6029 C  CG1   . VAL B 1 383 ? 14.601  26.659  24.295  1.00 22.66 ? 362 VAL B CG1   1 
ATOM   6030 C  CG2   . VAL B 1 383 ? 13.008  24.829  23.850  1.00 20.96 ? 362 VAL B CG2   1 
ATOM   6031 N  N     . VAL B 1 384 ? 12.666  28.074  26.996  1.00 21.97 ? 363 VAL B N     1 
ATOM   6032 C  CA    . VAL B 1 384 ? 12.932  29.370  27.696  1.00 25.54 ? 363 VAL B CA    1 
ATOM   6033 C  C     . VAL B 1 384 ? 13.130  29.111  29.192  1.00 24.03 ? 363 VAL B C     1 
ATOM   6034 O  O     . VAL B 1 384 ? 14.009  29.747  29.799  1.00 25.76 ? 363 VAL B O     1 
ATOM   6035 C  CB    . VAL B 1 384 ? 11.830  30.399  27.375  1.00 27.82 ? 363 VAL B CB    1 
ATOM   6036 C  CG1   . VAL B 1 384 ? 11.944  31.611  28.264  1.00 31.36 ? 363 VAL B CG1   1 
ATOM   6037 C  CG2   . VAL B 1 384 ? 11.912  30.806  25.916  1.00 28.82 ? 363 VAL B CG2   1 
ATOM   6038 N  N     . ASP B 1 385 ? 12.421  28.146  29.775  1.00 22.93 ? 364 ASP B N     1 
ATOM   6039 C  CA    . ASP B 1 385 ? 12.564  27.819  31.198  1.00 24.52 ? 364 ASP B CA    1 
ATOM   6040 C  C     . ASP B 1 385 ? 13.972  27.272  31.430  1.00 24.86 ? 364 ASP B C     1 
ATOM   6041 O  O     . ASP B 1 385 ? 14.605  27.670  32.422  1.00 24.33 ? 364 ASP B O     1 
ATOM   6042 C  CB    . ASP B 1 385 ? 11.515  26.817  31.671  1.00 25.20 ? 364 ASP B CB    1 
ATOM   6043 C  CG    . ASP B 1 385 ? 11.691  26.436  33.119  1.00 30.18 ? 364 ASP B CG    1 
ATOM   6044 O  OD1   . ASP B 1 385 ? 11.316  27.238  33.990  1.00 34.36 ? 364 ASP B OD1   1 
ATOM   6045 O  OD2   . ASP B 1 385 ? 12.252  25.383  33.357  1.00 32.65 ? 364 ASP B OD2   1 
ATOM   6046 N  N     . VAL B 1 386 ? 14.456  26.390  30.559  1.00 22.21 ? 365 VAL B N     1 
ATOM   6047 C  CA    . VAL B 1 386 ? 15.832  25.841  30.733  1.00 22.66 ? 365 VAL B CA    1 
ATOM   6048 C  C     . VAL B 1 386 ? 16.848  26.972  30.571  1.00 20.34 ? 365 VAL B C     1 
ATOM   6049 O  O     . VAL B 1 386 ? 17.740  27.124  31.482  1.00 22.24 ? 365 VAL B O     1 
ATOM   6050 C  CB    . VAL B 1 386 ? 16.111  24.665  29.779  1.00 23.23 ? 365 VAL B CB    1 
ATOM   6051 C  CG1   . VAL B 1 386 ? 17.579  24.270  29.848  1.00 26.72 ? 365 VAL B CG1   1 
ATOM   6052 C  CG2   . VAL B 1 386 ? 15.219  23.485  30.147  1.00 24.34 ? 365 VAL B CG2   1 
ATOM   6053 N  N     . LEU B 1 387 ? 16.694  27.787  29.535  1.00 20.28 ? 366 LEU B N     1 
ATOM   6054 C  CA    . LEU B 1 387 ? 17.675  28.851  29.225  1.00 19.43 ? 366 LEU B CA    1 
ATOM   6055 C  C     . LEU B 1 387 ? 17.657  29.913  30.339  1.00 21.44 ? 366 LEU B C     1 
ATOM   6056 O  O     . LEU B 1 387 ? 18.727  30.473  30.644  1.00 23.98 ? 366 LEU B O     1 
ATOM   6057 C  CB    . LEU B 1 387 ? 17.360  29.466  27.865  1.00 21.95 ? 366 LEU B CB    1 
ATOM   6058 C  CG    . LEU B 1 387 ? 17.547  28.575  26.617  1.00 21.48 ? 366 LEU B CG    1 
ATOM   6059 C  CD1   . LEU B 1 387 ? 17.377  29.420  25.366  1.00 22.21 ? 366 LEU B CD1   1 
ATOM   6060 C  CD2   . LEU B 1 387 ? 18.887  27.847  26.577  1.00 24.04 ? 366 LEU B CD2   1 
ATOM   6061 N  N     . ALA B 1 388 ? 16.502  30.222  30.916  1.00 21.94 ? 367 ALA B N     1 
ATOM   6062 C  CA    . ALA B 1 388 ? 16.399  31.243  32.000  1.00 21.85 ? 367 ALA B CA    1 
ATOM   6063 C  C     . ALA B 1 388 ? 17.238  30.793  33.198  1.00 21.68 ? 367 ALA B C     1 
ATOM   6064 O  O     . ALA B 1 388 ? 17.913  31.663  33.799  1.00 25.66 ? 367 ALA B O     1 
ATOM   6065 C  CB    . ALA B 1 388 ? 14.971  31.498  32.384  1.00 24.22 ? 367 ALA B CB    1 
ATOM   6066 N  N     . ARG B 1 389 ? 17.249  29.509  33.507  1.00 23.64 ? 368 ARG B N     1 
ATOM   6067 C  CA    . ARG B 1 389 ? 17.968  28.918  34.659  1.00 22.57 ? 368 ARG B CA    1 
ATOM   6068 C  C     . ARG B 1 389 ? 19.453  28.666  34.387  1.00 27.25 ? 368 ARG B C     1 
ATOM   6069 O  O     . ARG B 1 389 ? 20.141  28.370  35.369  1.00 31.06 ? 368 ARG B O     1 
ATOM   6070 C  CB    . ARG B 1 389 ? 17.296  27.614  35.070  1.00 24.78 ? 368 ARG B CB    1 
ATOM   6071 C  CG    . ARG B 1 389 ? 16.024  27.854  35.868  1.00 25.42 ? 368 ARG B CG    1 
ATOM   6072 C  CD    . ARG B 1 389 ? 15.402  26.541  36.288  1.00 25.95 ? 368 ARG B CD    1 
ATOM   6073 N  NE    . ARG B 1 389 ? 14.821  25.774  35.189  1.00 28.27 ? 368 ARG B NE    1 
ATOM   6074 C  CZ    . ARG B 1 389 ? 15.161  24.520  34.867  1.00 27.84 ? 368 ARG B CZ    1 
ATOM   6075 N  NH1   . ARG B 1 389 ? 16.068  23.892  35.575  1.00 27.01 ? 368 ARG B NH1   1 
ATOM   6076 N  NH2   . ARG B 1 389 ? 14.612  23.898  33.829  1.00 27.94 ? 368 ARG B NH2   1 
ATOM   6077 N  N     . THR B 1 390 ? 19.924  28.796  33.148  1.00 24.73 ? 369 THR B N     1 
ATOM   6078 C  CA    . THR B 1 390 ? 21.312  28.466  32.742  1.00 23.14 ? 369 THR B CA    1 
ATOM   6079 C  C     . THR B 1 390 ? 21.975  29.713  32.165  1.00 25.69 ? 369 THR B C     1 
ATOM   6080 O  O     . THR B 1 390 ? 22.954  30.121  32.757  1.00 27.44 ? 369 THR B O     1 
ATOM   6081 C  CB    . THR B 1 390 ? 21.318  27.271  31.780  1.00 21.31 ? 369 THR B CB    1 
ATOM   6082 O  OG1   . THR B 1 390 ? 20.380  27.505  30.727  1.00 19.91 ? 369 THR B OG1   1 
ATOM   6083 C  CG2   . THR B 1 390 ? 20.975  25.980  32.492  1.00 22.84 ? 369 THR B CG2   1 
ATOM   6084 N  N     . LEU B 1 391 ? 21.466  30.310  31.080  1.00 25.77 ? 370 LEU B N     1 
ATOM   6085 C  CA    . LEU B 1 391 ? 22.053  31.540  30.486  1.00 24.47 ? 370 LEU B CA    1 
ATOM   6086 C  C     . LEU B 1 391 ? 21.623  32.766  31.298  1.00 28.52 ? 370 LEU B C     1 
ATOM   6087 O  O     . LEU B 1 391 ? 22.417  33.711  31.378  1.00 25.40 ? 370 LEU B O     1 
ATOM   6088 C  CB    . LEU B 1 391 ? 21.656  31.676  29.019  1.00 26.58 ? 370 LEU B CB    1 
ATOM   6089 C  CG    . LEU B 1 391 ? 22.199  30.605  28.072  1.00 27.14 ? 370 LEU B CG    1 
ATOM   6090 C  CD1   . LEU B 1 391 ? 21.800  30.942  26.646  1.00 25.77 ? 370 LEU B CD1   1 
ATOM   6091 C  CD2   . LEU B 1 391 ? 23.725  30.478  28.164  1.00 27.93 ? 370 LEU B CD2   1 
ATOM   6092 N  N     . GLY B 1 392 ? 20.425  32.756  31.876  1.00 27.58 ? 371 GLY B N     1 
ATOM   6093 C  CA    . GLY B 1 392 ? 19.969  33.835  32.778  1.00 30.09 ? 371 GLY B CA    1 
ATOM   6094 C  C     . GLY B 1 392 ? 18.705  34.530  32.304  1.00 28.36 ? 371 GLY B C     1 
ATOM   6095 O  O     . GLY B 1 392 ? 18.087  34.097  31.334  1.00 27.23 ? 371 GLY B O     1 
ATOM   6096 N  N     . GLU B 1 393 ? 18.363  35.609  33.000  1.00 29.90 ? 372 GLU B N     1 
ATOM   6097 C  CA    . GLU B 1 393 ? 17.068  36.316  32.960  1.00 32.10 ? 372 GLU B CA    1 
ATOM   6098 C  C     . GLU B 1 393 ? 16.755  36.778  31.542  1.00 29.04 ? 372 GLU B C     1 
ATOM   6099 O  O     . GLU B 1 393 ? 15.585  36.688  31.146  1.00 29.15 ? 372 GLU B O     1 
ATOM   6100 C  CB    . GLU B 1 393 ? 17.145  37.512  33.927  1.00 37.00 ? 372 GLU B CB    1 
ATOM   6101 C  CG    . GLU B 1 393 ? 15.798  38.093  34.285  1.00 46.21 ? 372 GLU B CG    1 
ATOM   6102 C  CD    . GLU B 1 393 ? 14.858  37.016  34.799  1.00 48.26 ? 372 GLU B CD    1 
ATOM   6103 O  OE1   . GLU B 1 393 ? 13.722  36.938  34.296  1.00 52.16 ? 372 GLU B OE1   1 
ATOM   6104 O  OE2   . GLU B 1 393 ? 15.301  36.217  35.649  1.00 53.69 ? 372 GLU B OE2   1 
ATOM   6105 N  N     . ARG B 1 394 ? 17.743  37.293  30.801  1.00 29.83 ? 373 ARG B N     1 
ATOM   6106 C  CA    . ARG B 1 394 ? 17.500  37.850  29.441  1.00 30.09 ? 373 ARG B CA    1 
ATOM   6107 C  C     . ARG B 1 394 ? 16.999  36.743  28.492  1.00 29.36 ? 373 ARG B C     1 
ATOM   6108 O  O     . ARG B 1 394 ? 16.421  37.084  27.436  1.00 30.99 ? 373 ARG B O     1 
ATOM   6109 C  CB    . ARG B 1 394 ? 18.725  38.584  28.902  1.00 38.68 ? 373 ARG B CB    1 
ATOM   6110 C  CG    . ARG B 1 394 ? 18.580  40.100  28.937  1.00 51.67 ? 373 ARG B CG    1 
ATOM   6111 C  CD    . ARG B 1 394 ? 19.802  40.825  28.406  1.00 56.68 ? 373 ARG B CD    1 
ATOM   6112 N  NE    . ARG B 1 394 ? 20.828  40.819  29.441  1.00 63.29 ? 373 ARG B NE    1 
ATOM   6113 C  CZ    . ARG B 1 394 ? 22.114  41.116  29.259  1.00 73.54 ? 373 ARG B CZ    1 
ATOM   6114 N  NH1   . ARG B 1 394 ? 22.575  41.456  28.064  1.00 69.50 ? 373 ARG B NH1   1 
ATOM   6115 N  NH2   . ARG B 1 394 ? 22.943  41.058  30.286  1.00 79.77 ? 373 ARG B NH2   1 
ATOM   6116 N  N     . ALA B 1 395 ? 17.068  35.468  28.864  1.00 26.86 ? 374 ALA B N     1 
ATOM   6117 C  CA    . ALA B 1 395 ? 16.576  34.392  27.954  1.00 27.04 ? 374 ALA B CA    1 
ATOM   6118 C  C     . ALA B 1 395 ? 15.055  34.492  27.730  1.00 26.96 ? 374 ALA B C     1 
ATOM   6119 O  O     . ALA B 1 395 ? 14.580  33.953  26.756  1.00 27.29 ? 374 ALA B O     1 
ATOM   6120 C  CB    . ALA B 1 395 ? 16.975  33.045  28.494  1.00 25.60 ? 374 ALA B CB    1 
ATOM   6121 N  N     . ARG B 1 396 ? 14.319  35.216  28.583  1.00 31.60 ? 375 ARG B N     1 
ATOM   6122 C  CA    . ARG B 1 396 ? 12.854  35.451  28.417  1.00 34.80 ? 375 ARG B CA    1 
ATOM   6123 C  C     . ARG B 1 396 ? 12.535  36.467  27.321  1.00 33.54 ? 375 ARG B C     1 
ATOM   6124 O  O     . ARG B 1 396 ? 11.377  36.429  26.859  1.00 32.63 ? 375 ARG B O     1 
ATOM   6125 C  CB    . ARG B 1 396 ? 12.219  35.954  29.710  1.00 36.48 ? 375 ARG B CB    1 
ATOM   6126 C  CG    . ARG B 1 396 ? 12.250  34.896  30.788  1.00 43.41 ? 375 ARG B CG    1 
ATOM   6127 C  CD    . ARG B 1 396 ? 11.294  35.093  31.938  1.00 43.90 ? 375 ARG B CD    1 
ATOM   6128 N  NE    . ARG B 1 396 ? 11.485  33.833  32.622  1.00 48.91 ? 375 ARG B NE    1 
ATOM   6129 C  CZ    . ARG B 1 396 ? 10.878  32.701  32.285  1.00 45.93 ? 375 ARG B CZ    1 
ATOM   6130 N  NH1   . ARG B 1 396 ? 9.949   32.694  31.341  1.00 40.22 ? 375 ARG B NH1   1 
ATOM   6131 N  NH2   . ARG B 1 396 ? 11.170  31.590  32.933  1.00 46.49 ? 375 ARG B NH2   1 
ATOM   6132 N  N     . ASP B 1 397 ? 13.482  37.326  26.952  1.00 33.58 ? 376 ASP B N     1 
ATOM   6133 C  CA    . ASP B 1 397 ? 13.293  38.412  25.945  1.00 35.89 ? 376 ASP B CA    1 
ATOM   6134 C  C     . ASP B 1 397 ? 13.344  37.831  24.527  1.00 31.56 ? 376 ASP B C     1 
ATOM   6135 O  O     . ASP B 1 397 ? 14.129  38.316  23.717  1.00 29.94 ? 376 ASP B O     1 
ATOM   6136 C  CB    . ASP B 1 397 ? 14.360  39.511  26.049  1.00 41.06 ? 376 ASP B CB    1 
ATOM   6137 C  CG    . ASP B 1 397 ? 14.498  40.138  27.427  1.00 47.97 ? 376 ASP B CG    1 
ATOM   6138 O  OD1   . ASP B 1 397 ? 13.572  39.965  28.234  1.00 49.96 ? 376 ASP B OD1   1 
ATOM   6139 O  OD2   . ASP B 1 397 ? 15.537  40.793  27.683  1.00 54.11 ? 376 ASP B OD2   1 
ATOM   6140 N  N     . VAL B 1 398 ? 12.455  36.898  24.212  1.00 32.23 ? 377 VAL B N     1 
ATOM   6141 C  CA    . VAL B 1 398 ? 12.464  36.131  22.928  1.00 31.73 ? 377 VAL B CA    1 
ATOM   6142 C  C     . VAL B 1 398 ? 11.832  36.980  21.825  1.00 32.34 ? 377 VAL B C     1 
ATOM   6143 O  O     . VAL B 1 398 ? 10.748  37.457  22.024  1.00 33.28 ? 377 VAL B O     1 
ATOM   6144 C  CB    . VAL B 1 398 ? 11.730  34.796  23.120  1.00 32.60 ? 377 VAL B CB    1 
ATOM   6145 C  CG1   . VAL B 1 398 ? 11.433  34.089  21.799  1.00 31.60 ? 377 VAL B CG1   1 
ATOM   6146 C  CG2   . VAL B 1 398 ? 12.547  33.907  24.040  1.00 35.28 ? 377 VAL B CG2   1 
ATOM   6147 N  N     . ARG B 1 399 ? 12.483  37.116  20.682  1.00 27.18 ? 378 ARG B N     1 
ATOM   6148 C  CA    . ARG B 1 399 ? 11.905  37.771  19.486  1.00 32.39 ? 378 ARG B CA    1 
ATOM   6149 C  C     . ARG B 1 399 ? 11.025  36.719  18.781  1.00 32.91 ? 378 ARG B C     1 
ATOM   6150 O  O     . ARG B 1 399 ? 9.911   37.038  18.339  1.00 23.58 ? 378 ARG B O     1 
ATOM   6151 C  CB    . ARG B 1 399 ? 13.065  38.327  18.647  1.00 33.93 ? 378 ARG B CB    1 
ATOM   6152 C  CG    . ARG B 1 399 ? 12.724  38.674  17.202  1.00 42.04 ? 378 ARG B CG    1 
ATOM   6153 C  CD    . ARG B 1 399 ? 11.847  39.901  17.023  1.00 49.76 ? 378 ARG B CD    1 
ATOM   6154 N  NE    . ARG B 1 399 ? 12.409  41.079  17.685  1.00 53.12 ? 378 ARG B NE    1 
ATOM   6155 C  CZ    . ARG B 1 399 ? 11.785  42.247  17.862  1.00 52.43 ? 378 ARG B CZ    1 
ATOM   6156 N  NH1   . ARG B 1 399 ? 10.547  42.435  17.436  1.00 50.17 ? 378 ARG B NH1   1 
ATOM   6157 N  NH2   . ARG B 1 399 ? 12.410  43.226  18.484  1.00 47.40 ? 378 ARG B NH2   1 
ATOM   6158 N  N     . ASP B 1 400 ? 11.505  35.475  18.675  1.00 25.67 ? 379 ASP B N     1 
ATOM   6159 C  CA    . ASP B 1 400 ? 10.752  34.439  17.928  1.00 25.16 ? 379 ASP B CA    1 
ATOM   6160 C  C     . ASP B 1 400 ? 11.276  33.068  18.336  1.00 23.74 ? 379 ASP B C     1 
ATOM   6161 O  O     . ASP B 1 400 ? 12.348  33.002  18.940  1.00 21.99 ? 379 ASP B O     1 
ATOM   6162 C  CB    . ASP B 1 400 ? 10.922  34.648  16.421  1.00 26.96 ? 379 ASP B CB    1 
ATOM   6163 C  CG    . ASP B 1 400 ? 9.863   33.961  15.589  1.00 27.05 ? 379 ASP B CG    1 
ATOM   6164 O  OD1   . ASP B 1 400 ? 8.976   33.299  16.173  1.00 27.62 ? 379 ASP B OD1   1 
ATOM   6165 O  OD2   . ASP B 1 400 ? 9.900   34.159  14.398  1.00 30.64 ? 379 ASP B OD2   1 
ATOM   6166 N  N     . TYR B 1 401 ? 10.560  32.014  17.957  1.00 22.78 ? 380 TYR B N     1 
ATOM   6167 C  CA    . TYR B 1 401 ? 10.934  30.615  18.272  1.00 21.17 ? 380 TYR B CA    1 
ATOM   6168 C  C     . TYR B 1 401 ? 10.518  29.772  17.064  1.00 22.48 ? 380 TYR B C     1 
ATOM   6169 O  O     . TYR B 1 401 ? 9.342   29.818  16.631  1.00 21.06 ? 380 TYR B O     1 
ATOM   6170 C  CB    . TYR B 1 401 ? 10.332  30.172  19.605  1.00 21.44 ? 380 TYR B CB    1 
ATOM   6171 C  CG    . TYR B 1 401 ? 10.526  28.694  19.859  1.00 20.50 ? 380 TYR B CG    1 
ATOM   6172 C  CD1   . TYR B 1 401 ? 9.591   27.764  19.424  1.00 21.21 ? 380 TYR B CD1   1 
ATOM   6173 C  CD2   . TYR B 1 401 ? 11.649  28.220  20.499  1.00 20.77 ? 380 TYR B CD2   1 
ATOM   6174 C  CE1   . TYR B 1 401 ? 9.762   26.407  19.621  1.00 21.49 ? 380 TYR B CE1   1 
ATOM   6175 C  CE2   . TYR B 1 401 ? 11.825  26.860  20.731  1.00 20.33 ? 380 TYR B CE2   1 
ATOM   6176 C  CZ    . TYR B 1 401 ? 10.891  25.947  20.265  1.00 21.30 ? 380 TYR B CZ    1 
ATOM   6177 O  OH    . TYR B 1 401 ? 11.081  24.610  20.457  1.00 18.73 ? 380 TYR B OH    1 
ATOM   6178 N  N     . ILE B 1 402 ? 11.494  29.074  16.485  1.00 20.84 ? 381 ILE B N     1 
ATOM   6179 C  CA    . ILE B 1 402 ? 11.252  28.288  15.253  1.00 21.28 ? 381 ILE B CA    1 
ATOM   6180 C  C     . ILE B 1 402 ? 11.708  26.855  15.506  1.00 20.72 ? 381 ILE B C     1 
ATOM   6181 O  O     . ILE B 1 402 ? 12.809  26.673  16.018  1.00 21.47 ? 381 ILE B O     1 
ATOM   6182 C  CB    . ILE B 1 402 ? 11.976  28.960  14.081  1.00 22.81 ? 381 ILE B CB    1 
ATOM   6183 C  CG1   . ILE B 1 402 ? 11.552  30.431  13.939  1.00 24.16 ? 381 ILE B CG1   1 
ATOM   6184 C  CG2   . ILE B 1 402 ? 11.714  28.181  12.812  1.00 25.07 ? 381 ILE B CG2   1 
ATOM   6185 C  CD1   . ILE B 1 402 ? 12.441  31.234  13.030  1.00 25.66 ? 381 ILE B CD1   1 
ATOM   6186 N  N     . ASP B 1 403 ? 10.883  25.869  15.200  1.00 18.36 ? 382 ASP B N     1 
ATOM   6187 C  CA    . ASP B 1 403 ? 11.283  24.473  15.499  1.00 18.13 ? 382 ASP B CA    1 
ATOM   6188 C  C     . ASP B 1 403 ? 10.668  23.512  14.487  1.00 19.56 ? 382 ASP B C     1 
ATOM   6189 O  O     . ASP B 1 403 ? 9.815   23.911  13.709  1.00 16.57 ? 382 ASP B O     1 
ATOM   6190 C  CB    . ASP B 1 403 ? 11.077  24.146  16.982  1.00 18.27 ? 382 ASP B CB    1 
ATOM   6191 C  CG    . ASP B 1 403 ? 9.727   23.624  17.430  1.00 18.34 ? 382 ASP B CG    1 
ATOM   6192 O  OD1   . ASP B 1 403 ? 8.788   23.518  16.587  1.00 21.43 ? 382 ASP B OD1   1 
ATOM   6193 O  OD2   . ASP B 1 403 ? 9.624   23.315  18.625  1.00 20.87 ? 382 ASP B OD2   1 
ATOM   6194 N  N     . ARG B 1 404 ? 11.195  22.304  14.475  1.00 19.17 ? 383 ARG B N     1 
ATOM   6195 C  CA    . ARG B 1 404 ? 10.697  21.231  13.583  1.00 18.59 ? 383 ARG B CA    1 
ATOM   6196 C  C     . ARG B 1 404 ? 10.825  19.916  14.337  1.00 17.80 ? 383 ARG B C     1 
ATOM   6197 O  O     . ARG B 1 404 ? 11.923  19.563  14.759  1.00 17.88 ? 383 ARG B O     1 
ATOM   6198 C  CB    . ARG B 1 404 ? 11.443  21.194  12.247  1.00 22.42 ? 383 ARG B CB    1 
ATOM   6199 C  CG    . ARG B 1 404 ? 10.890  20.098  11.334  1.00 24.46 ? 383 ARG B CG    1 
ATOM   6200 C  CD    . ARG B 1 404 ? 10.688  20.433  9.889   1.00 30.59 ? 383 ARG B CD    1 
ATOM   6201 N  NE    . ARG B 1 404 ? 9.910   21.640  9.714   1.00 27.48 ? 383 ARG B NE    1 
ATOM   6202 C  CZ    . ARG B 1 404 ? 9.924   22.387  8.617   1.00 35.23 ? 383 ARG B CZ    1 
ATOM   6203 N  NH1   . ARG B 1 404 ? 10.612  22.008  7.555   1.00 40.54 ? 383 ARG B NH1   1 
ATOM   6204 N  NH2   . ARG B 1 404 ? 9.255   23.529  8.604   1.00 44.17 ? 383 ARG B NH2   1 
ATOM   6205 N  N     . ASP B 1 405 ? 9.703   19.208  14.422  1.00 20.70 ? 384 ASP B N     1 
ATOM   6206 C  CA    . ASP B 1 405 ? 9.626   17.812  14.883  1.00 19.67 ? 384 ASP B CA    1 
ATOM   6207 C  C     . ASP B 1 405 ? 9.792   16.910  13.655  1.00 18.45 ? 384 ASP B C     1 
ATOM   6208 O  O     . ASP B 1 405 ? 8.816   16.747  12.882  1.00 19.47 ? 384 ASP B O     1 
ATOM   6209 C  CB    . ASP B 1 405 ? 8.303   17.502  15.577  1.00 19.91 ? 384 ASP B CB    1 
ATOM   6210 C  CG    . ASP B 1 405 ? 8.271   16.065  16.080  1.00 19.58 ? 384 ASP B CG    1 
ATOM   6211 O  OD1   . ASP B 1 405 ? 9.276   15.332  15.847  1.00 19.68 ? 384 ASP B OD1   1 
ATOM   6212 O  OD2   . ASP B 1 405 ? 7.241   15.662  16.645  1.00 21.40 ? 384 ASP B OD2   1 
ATOM   6213 N  N     . TRP B 1 406 ? 10.997  16.368  13.477  1.00 16.08 ? 385 TRP B N     1 
ATOM   6214 C  CA    . TRP B 1 406 ? 11.341  15.557  12.283  1.00 16.98 ? 385 TRP B CA    1 
ATOM   6215 C  C     . TRP B 1 406 ? 10.555  14.240  12.267  1.00 16.85 ? 385 TRP B C     1 
ATOM   6216 O  O     . TRP B 1 406 ? 10.403  13.637  11.172  1.00 18.91 ? 385 TRP B O     1 
ATOM   6217 C  CB    . TRP B 1 406 ? 12.868  15.419  12.167  1.00 17.22 ? 385 TRP B CB    1 
ATOM   6218 C  CG    . TRP B 1 406 ? 13.422  16.684  11.586  1.00 15.92 ? 385 TRP B CG    1 
ATOM   6219 C  CD1   . TRP B 1 406 ? 13.879  17.772  12.275  1.00 17.03 ? 385 TRP B CD1   1 
ATOM   6220 C  CD2   . TRP B 1 406 ? 13.466  17.036  10.200  1.00 15.83 ? 385 TRP B CD2   1 
ATOM   6221 N  NE1   . TRP B 1 406 ? 14.226  18.766  11.390  1.00 17.01 ? 385 TRP B NE1   1 
ATOM   6222 C  CE2   . TRP B 1 406 ? 14.036  18.317  10.112  1.00 17.31 ? 385 TRP B CE2   1 
ATOM   6223 C  CE3   . TRP B 1 406 ? 13.160  16.356  9.007   1.00 15.93 ? 385 TRP B CE3   1 
ATOM   6224 C  CZ2   . TRP B 1 406 ? 14.254  18.953  8.888   1.00 16.93 ? 385 TRP B CZ2   1 
ATOM   6225 C  CZ3   . TRP B 1 406 ? 13.373  16.984  7.796   1.00 17.45 ? 385 TRP B CZ3   1 
ATOM   6226 C  CH2   . TRP B 1 406 ? 13.941  18.256  7.745   1.00 17.92 ? 385 TRP B CH2   1 
ATOM   6227 N  N     . SER B 1 407 ? 10.044  13.801  13.414  1.00 16.71 ? 386 SER B N     1 
ATOM   6228 C  CA    . SER B 1 407 ? 9.223   12.579  13.509  1.00 17.04 ? 386 SER B CA    1 
ATOM   6229 C  C     . SER B 1 407 ? 7.857   12.812  12.861  1.00 18.23 ? 386 SER B C     1 
ATOM   6230 O  O     . SER B 1 407 ? 7.234   11.826  12.447  1.00 18.15 ? 386 SER B O     1 
ATOM   6231 C  CB    . SER B 1 407 ? 9.111   12.131  14.939  1.00 18.74 ? 386 SER B CB    1 
ATOM   6232 O  OG    . SER B 1 407 ? 10.405  11.931  15.543  1.00 20.69 ? 386 SER B OG    1 
ATOM   6233 N  N     . ALA B 1 408 ? 7.374   14.059  12.834  1.00 19.34 ? 387 ALA B N     1 
ATOM   6234 C  CA    . ALA B 1 408 ? 6.052   14.459  12.288  1.00 18.98 ? 387 ALA B CA    1 
ATOM   6235 C  C     . ALA B 1 408 ? 6.146   14.733  10.778  1.00 21.51 ? 387 ALA B C     1 
ATOM   6236 O  O     . ALA B 1 408 ? 5.113   14.885  10.141  1.00 22.68 ? 387 ALA B O     1 
ATOM   6237 C  CB    . ALA B 1 408 ? 5.515   15.678  13.035  1.00 19.17 ? 387 ALA B CB    1 
ATOM   6238 N  N     . GLU B 1 409 ? 7.343   14.743  10.203  1.00 19.10 ? 388 GLU B N     1 
ATOM   6239 C  CA    . GLU B 1 409 ? 7.548   14.941  8.744   1.00 19.00 ? 388 GLU B CA    1 
ATOM   6240 C  C     . GLU B 1 409 ? 7.211   13.640  8.039   1.00 17.66 ? 388 GLU B C     1 
ATOM   6241 O  O     . GLU B 1 409 ? 7.900   12.654  8.226   1.00 17.28 ? 388 GLU B O     1 
ATOM   6242 C  CB    . GLU B 1 409 ? 8.998   15.285  8.442   1.00 19.34 ? 388 GLU B CB    1 
ATOM   6243 C  CG    . GLU B 1 409 ? 9.284   16.698  8.871   1.00 20.36 ? 388 GLU B CG    1 
ATOM   6244 C  CD    . GLU B 1 409 ? 8.767   17.733  7.898   1.00 22.56 ? 388 GLU B CD    1 
ATOM   6245 O  OE1   . GLU B 1 409 ? 8.194   18.714  8.377   1.00 22.97 ? 388 GLU B OE1   1 
ATOM   6246 O  OE2   . GLU B 1 409 ? 9.002   17.571  6.680   1.00 23.21 ? 388 GLU B OE2   1 
ATOM   6247 N  N     . PRO B 1 410 ? 6.121   13.565  7.269   1.00 18.03 ? 389 PRO B N     1 
ATOM   6248 C  CA    . PRO B 1 410 ? 5.745   12.281  6.659   1.00 19.07 ? 389 PRO B CA    1 
ATOM   6249 C  C     . PRO B 1 410 ? 6.798   11.723  5.699   1.00 17.01 ? 389 PRO B C     1 
ATOM   6250 O  O     . PRO B 1 410 ? 6.869   10.489  5.495   1.00 18.66 ? 389 PRO B O     1 
ATOM   6251 C  CB    . PRO B 1 410 ? 4.435   12.577  5.917   1.00 21.63 ? 389 PRO B CB    1 
ATOM   6252 C  CG    . PRO B 1 410 ? 4.217   14.053  6.001   1.00 22.74 ? 389 PRO B CG    1 
ATOM   6253 C  CD    . PRO B 1 410 ? 5.164   14.635  7.011   1.00 18.86 ? 389 PRO B CD    1 
ATOM   6254 N  N     . TRP B 1 411 ? 7.641   12.593  5.141   1.00 15.18 ? 390 TRP B N     1 
ATOM   6255 C  CA    . TRP B 1 411 ? 8.680   12.131  4.185   1.00 16.29 ? 390 TRP B CA    1 
ATOM   6256 C  C     . TRP B 1 411 ? 10.071  11.969  4.840   1.00 15.68 ? 390 TRP B C     1 
ATOM   6257 O  O     . TRP B 1 411 ? 11.067  11.712  4.104   1.00 16.86 ? 390 TRP B O     1 
ATOM   6258 C  CB    . TRP B 1 411 ? 8.659   13.044  2.953   1.00 16.87 ? 390 TRP B CB    1 
ATOM   6259 C  CG    . TRP B 1 411 ? 7.322   13.058  2.287   1.00 16.61 ? 390 TRP B CG    1 
ATOM   6260 C  CD1   . TRP B 1 411 ? 6.469   14.110  2.142   1.00 18.08 ? 390 TRP B CD1   1 
ATOM   6261 C  CD2   . TRP B 1 411 ? 6.648   11.918  1.721   1.00 18.79 ? 390 TRP B CD2   1 
ATOM   6262 N  NE1   . TRP B 1 411 ? 5.337   13.715  1.483   1.00 18.92 ? 390 TRP B NE1   1 
ATOM   6263 C  CE2   . TRP B 1 411 ? 5.411   12.377  1.214   1.00 19.04 ? 390 TRP B CE2   1 
ATOM   6264 C  CE3   . TRP B 1 411 ? 6.970   10.566  1.568   1.00 21.77 ? 390 TRP B CE3   1 
ATOM   6265 C  CZ2   . TRP B 1 411 ? 4.499   11.523  0.593   1.00 20.88 ? 390 TRP B CZ2   1 
ATOM   6266 C  CZ3   . TRP B 1 411 ? 6.074   9.726   0.942   1.00 20.05 ? 390 TRP B CZ3   1 
ATOM   6267 C  CH2   . TRP B 1 411 ? 4.849   10.200  0.478   1.00 22.17 ? 390 TRP B CH2   1 
ATOM   6268 N  N     . THR B 1 412 ? 10.161  12.048  6.159   1.00 15.10 ? 391 THR B N     1 
ATOM   6269 C  CA    . THR B 1 412 ? 11.335  11.603  6.947   1.00 15.83 ? 391 THR B CA    1 
ATOM   6270 C  C     . THR B 1 412 ? 10.943  10.573  8.026   1.00 15.14 ? 391 THR B C     1 
ATOM   6271 O  O     . THR B 1 412 ? 11.599  9.526   8.067   1.00 15.28 ? 391 THR B O     1 
ATOM   6272 C  CB    . THR B 1 412 ? 12.044  12.784  7.602   1.00 14.89 ? 391 THR B CB    1 
ATOM   6273 O  OG1   . THR B 1 412 ? 12.301  13.794  6.633   1.00 15.92 ? 391 THR B OG1   1 
ATOM   6274 C  CG2   . THR B 1 412 ? 13.339  12.370  8.234   1.00 16.03 ? 391 THR B CG2   1 
ATOM   6275 N  N     . ARG B 1 413 ? 10.053  10.937  8.948   1.00 15.27 ? 392 ARG B N     1 
ATOM   6276 C  CA    . ARG B 1 413 ? 9.604   10.081  10.084  1.00 15.15 ? 392 ARG B CA    1 
ATOM   6277 C  C     . ARG B 1 413 ? 10.759  9.776   11.038  1.00 15.91 ? 392 ARG B C     1 
ATOM   6278 O  O     . ARG B 1 413 ? 10.799  8.705   11.669  1.00 15.65 ? 392 ARG B O     1 
ATOM   6279 C  CB    . ARG B 1 413 ? 8.931   8.818   9.541   1.00 17.41 ? 392 ARG B CB    1 
ATOM   6280 C  CG    . ARG B 1 413 ? 7.617   9.101   8.824   1.00 19.86 ? 392 ARG B CG    1 
ATOM   6281 C  CD    . ARG B 1 413 ? 6.665   9.836   9.743   1.00 19.47 ? 392 ARG B CD    1 
ATOM   6282 N  NE    . ARG B 1 413 ? 5.241   9.697   9.473   1.00 18.98 ? 392 ARG B NE    1 
ATOM   6283 C  CZ    . ARG B 1 413 ? 4.284   10.213  10.262  1.00 19.61 ? 392 ARG B CZ    1 
ATOM   6284 N  NH1   . ARG B 1 413 ? 4.579   10.927  11.341  1.00 20.07 ? 392 ARG B NH1   1 
ATOM   6285 N  NH2   . ARG B 1 413 ? 3.022   10.034  9.967   1.00 20.82 ? 392 ARG B NH2   1 
ATOM   6286 N  N     . GLY B 1 414 ? 11.632  10.757  11.211  1.00 15.60 ? 393 GLY B N     1 
ATOM   6287 C  CA    . GLY B 1 414 ? 12.564  10.843  12.319  1.00 16.68 ? 393 GLY B CA    1 
ATOM   6288 C  C     . GLY B 1 414 ? 13.960  11.194  11.859  1.00 16.55 ? 393 GLY B C     1 
ATOM   6289 O  O     . GLY B 1 414 ? 14.443  10.590  10.872  1.00 19.69 ? 393 GLY B O     1 
ATOM   6290 N  N     . CYS B 1 415 ? 14.589  12.096  12.592  1.00 17.69 ? 394 CYS B N     1 
ATOM   6291 C  CA    . CYS B 1 415 ? 16.015  12.449  12.437  1.00 18.51 ? 394 CYS B CA    1 
ATOM   6292 C  C     . CYS B 1 415 ? 16.782  11.899  13.630  1.00 19.84 ? 394 CYS B C     1 
ATOM   6293 O  O     . CYS B 1 415 ? 16.180  11.501  14.628  1.00 19.52 ? 394 CYS B O     1 
ATOM   6294 C  CB    . CYS B 1 415 ? 16.199  13.953  12.253  1.00 18.35 ? 394 CYS B CB    1 
ATOM   6295 S  SG    . CYS B 1 415 ? 16.267  14.393  10.498  1.00 18.18 ? 394 CYS B SG    1 
ATOM   6296 N  N     . TYR B 1 416 ? 18.116  11.822  13.510  1.00 18.70 ? 395 TYR B N     1 
ATOM   6297 C  CA    . TYR B 1 416 ? 18.900  12.208  12.348  1.00 17.74 ? 395 TYR B CA    1 
ATOM   6298 C  C     . TYR B 1 416 ? 18.831  11.104  11.282  1.00 17.86 ? 395 TYR B C     1 
ATOM   6299 O  O     . TYR B 1 416 ? 18.857  11.381  10.082  1.00 17.76 ? 395 TYR B O     1 
ATOM   6300 C  CB    . TYR B 1 416 ? 20.356  12.343  12.772  1.00 18.33 ? 395 TYR B CB    1 
ATOM   6301 C  CG    . TYR B 1 416 ? 20.523  13.240  13.967  1.00 19.03 ? 395 TYR B CG    1 
ATOM   6302 C  CD1   . TYR B 1 416 ? 19.952  14.505  13.984  1.00 18.31 ? 395 TYR B CD1   1 
ATOM   6303 C  CD2   . TYR B 1 416 ? 21.148  12.786  15.116  1.00 19.89 ? 395 TYR B CD2   1 
ATOM   6304 C  CE1   . TYR B 1 416 ? 20.069  15.318  15.095  1.00 17.53 ? 395 TYR B CE1   1 
ATOM   6305 C  CE2   . TYR B 1 416 ? 21.287  13.594  16.222  1.00 19.13 ? 395 TYR B CE2   1 
ATOM   6306 C  CZ    . TYR B 1 416 ? 20.745  14.858  16.215  1.00 20.05 ? 395 TYR B CZ    1 
ATOM   6307 O  OH    . TYR B 1 416 ? 20.874  15.662  17.314  1.00 22.79 ? 395 TYR B OH    1 
ATOM   6308 N  N     . GLY B 1 417 ? 18.744  9.867   11.753  1.00 17.27 ? 396 GLY B N     1 
ATOM   6309 C  CA    . GLY B 1 417 ? 18.704  8.679   10.890  1.00 17.15 ? 396 GLY B CA    1 
ATOM   6310 C  C     . GLY B 1 417 ? 18.314  7.440   11.663  1.00 18.92 ? 396 GLY B C     1 
ATOM   6311 O  O     . GLY B 1 417 ? 17.901  7.541   12.840  1.00 18.12 ? 396 GLY B O     1 
ATOM   6312 N  N     . ALA B 1 418 ? 18.417  6.287   11.027  1.00 15.59 ? 397 ALA B N     1 
ATOM   6313 C  CA    . ALA B 1 418 ? 18.073  5.010   11.678  1.00 16.46 ? 397 ALA B CA    1 
ATOM   6314 C  C     . ALA B 1 418 ? 19.112  4.629   12.738  1.00 17.46 ? 397 ALA B C     1 
ATOM   6315 O  O     . ALA B 1 418 ? 20.292  4.948   12.621  1.00 18.80 ? 397 ALA B O     1 
ATOM   6316 C  CB    . ALA B 1 418 ? 17.961  3.952   10.624  1.00 16.59 ? 397 ALA B CB    1 
ATOM   6317 N  N     . HIS B 1 419 ? 18.688  3.844   13.703  1.00 17.21 ? 398 HIS B N     1 
ATOM   6318 C  CA    . HIS B 1 419 ? 19.595  3.083   14.590  1.00 18.53 ? 398 HIS B CA    1 
ATOM   6319 C  C     . HIS B 1 419 ? 19.097  1.645   14.574  1.00 20.01 ? 398 HIS B C     1 
ATOM   6320 O  O     . HIS B 1 419 ? 17.988  1.393   13.999  1.00 16.85 ? 398 HIS B O     1 
ATOM   6321 C  CB    . HIS B 1 419 ? 19.637  3.675   16.005  1.00 19.12 ? 398 HIS B CB    1 
ATOM   6322 C  CG    . HIS B 1 419 ? 18.327  3.588   16.708  1.00 19.04 ? 398 HIS B CG    1 
ATOM   6323 N  ND1   . HIS B 1 419 ? 17.388  4.581   16.622  1.00 18.96 ? 398 HIS B ND1   1 
ATOM   6324 C  CD2   . HIS B 1 419 ? 17.803  2.642   17.518  1.00 19.77 ? 398 HIS B CD2   1 
ATOM   6325 C  CE1   . HIS B 1 419 ? 16.354  4.263   17.372  1.00 19.43 ? 398 HIS B CE1   1 
ATOM   6326 N  NE2   . HIS B 1 419 ? 16.578  3.094   17.921  1.00 18.45 ? 398 HIS B NE2   1 
ATOM   6327 N  N     . LEU B 1 420 ? 19.904  0.739   15.111  1.00 17.80 ? 399 LEU B N     1 
ATOM   6328 C  CA    . LEU B 1 420 ? 19.545  -0.685  15.104  1.00 19.97 ? 399 LEU B CA    1 
ATOM   6329 C  C     . LEU B 1 420 ? 19.580  -1.161  16.546  1.00 19.38 ? 399 LEU B C     1 
ATOM   6330 O  O     . LEU B 1 420 ? 20.554  -0.936  17.273  1.00 18.75 ? 399 LEU B O     1 
ATOM   6331 C  CB    . LEU B 1 420 ? 20.472  -1.477  14.190  1.00 19.58 ? 399 LEU B CB    1 
ATOM   6332 C  CG    . LEU B 1 420 ? 20.154  -1.375  12.690  1.00 20.42 ? 399 LEU B CG    1 
ATOM   6333 C  CD1   . LEU B 1 420 ? 20.736  -0.107  12.117  1.00 19.86 ? 399 LEU B CD1   1 
ATOM   6334 C  CD2   . LEU B 1 420 ? 20.685  -2.569  11.923  1.00 22.52 ? 399 LEU B CD2   1 
ATOM   6335 N  N     . PRO B 1 421 ? 18.479  -1.784  17.004  1.00 17.69 ? 400 PRO B N     1 
ATOM   6336 C  CA    . PRO B 1 421 ? 18.419  -2.342  18.347  1.00 18.69 ? 400 PRO B CA    1 
ATOM   6337 C  C     . PRO B 1 421 ? 19.209  -3.643  18.436  1.00 18.23 ? 400 PRO B C     1 
ATOM   6338 O  O     . PRO B 1 421 ? 19.636  -4.175  17.421  1.00 18.45 ? 400 PRO B O     1 
ATOM   6339 C  CB    . PRO B 1 421 ? 16.928  -2.659  18.498  1.00 20.66 ? 400 PRO B CB    1 
ATOM   6340 C  CG    . PRO B 1 421 ? 16.585  -3.158  17.097  1.00 22.34 ? 400 PRO B CG    1 
ATOM   6341 C  CD    . PRO B 1 421 ? 17.270  -2.111  16.218  1.00 19.89 ? 400 PRO B CD    1 
ATOM   6342 N  N     . PRO B 1 422 ? 19.396  -4.201  19.648  1.00 20.94 ? 401 PRO B N     1 
ATOM   6343 C  CA    . PRO B 1 422 ? 20.138  -5.440  19.797  1.00 19.60 ? 401 PRO B CA    1 
ATOM   6344 C  C     . PRO B 1 422 ? 19.587  -6.546  18.896  1.00 19.42 ? 401 PRO B C     1 
ATOM   6345 O  O     . PRO B 1 422 ? 18.360  -6.669  18.781  1.00 18.45 ? 401 PRO B O     1 
ATOM   6346 C  CB    . PRO B 1 422 ? 20.033  -5.799  21.275  1.00 21.63 ? 401 PRO B CB    1 
ATOM   6347 C  CG    . PRO B 1 422 ? 19.679  -4.520  21.934  1.00 23.25 ? 401 PRO B CG    1 
ATOM   6348 C  CD    . PRO B 1 422 ? 18.976  -3.630  20.931  1.00 21.56 ? 401 PRO B CD    1 
ATOM   6349 N  N     . GLY B 1 423 ? 20.500  -7.312  18.303  1.00 18.37 ? 402 GLY B N     1 
ATOM   6350 C  CA    . GLY B 1 423 ? 20.168  -8.466  17.458  1.00 20.69 ? 402 GLY B CA    1 
ATOM   6351 C  C     . GLY B 1 423 ? 19.946  -8.146  15.997  1.00 23.67 ? 402 GLY B C     1 
ATOM   6352 O  O     . GLY B 1 423 ? 19.859  -9.084  15.231  1.00 24.83 ? 402 GLY B O     1 
ATOM   6353 N  N     . ALA B 1 424 ? 19.892  -6.883  15.589  1.00 20.75 ? 403 ALA B N     1 
ATOM   6354 C  CA    . ALA B 1 424 ? 19.480  -6.520  14.221  1.00 22.90 ? 403 ALA B CA    1 
ATOM   6355 C  C     . ALA B 1 424 ? 20.657  -6.595  13.240  1.00 21.49 ? 403 ALA B C     1 
ATOM   6356 O  O     . ALA B 1 424 ? 20.472  -7.165  12.140  1.00 18.52 ? 403 ALA B O     1 
ATOM   6357 C  CB    . ALA B 1 424 ? 18.832  -5.165  14.232  1.00 21.66 ? 403 ALA B CB    1 
ATOM   6358 N  N     . TRP B 1 425 ? 21.814  -6.013  13.594  1.00 20.75 ? 404 TRP B N     1 
ATOM   6359 C  CA    . TRP B 1 425 ? 22.981  -5.945  12.681  1.00 19.98 ? 404 TRP B CA    1 
ATOM   6360 C  C     . TRP B 1 425 ? 23.413  -7.338  12.245  1.00 19.41 ? 404 TRP B C     1 
ATOM   6361 O  O     . TRP B 1 425 ? 23.734  -7.451  11.058  1.00 19.15 ? 404 TRP B O     1 
ATOM   6362 C  CB    . TRP B 1 425 ? 24.161  -5.192  13.304  1.00 19.05 ? 404 TRP B CB    1 
ATOM   6363 C  CG    . TRP B 1 425 ? 24.244  -3.760  12.909  1.00 19.13 ? 404 TRP B CG    1 
ATOM   6364 C  CD1   . TRP B 1 425 ? 24.169  -2.699  13.769  1.00 19.90 ? 404 TRP B CD1   1 
ATOM   6365 C  CD2   . TRP B 1 425 ? 24.416  -3.205  11.592  1.00 21.74 ? 404 TRP B CD2   1 
ATOM   6366 N  NE1   . TRP B 1 425 ? 24.297  -1.524  13.070  1.00 20.70 ? 404 TRP B NE1   1 
ATOM   6367 C  CE2   . TRP B 1 425 ? 24.471  -1.798  11.747  1.00 21.14 ? 404 TRP B CE2   1 
ATOM   6368 C  CE3   . TRP B 1 425 ? 24.515  -3.734  10.295  1.00 21.62 ? 404 TRP B CE3   1 
ATOM   6369 C  CZ2   . TRP B 1 425 ? 24.585  -0.920  10.671  1.00 25.37 ? 404 TRP B CZ2   1 
ATOM   6370 C  CZ3   . TRP B 1 425 ? 24.628  -2.858  9.233   1.00 25.05 ? 404 TRP B CZ3   1 
ATOM   6371 C  CH2   . TRP B 1 425 ? 24.685  -1.478  9.418   1.00 26.07 ? 404 TRP B CH2   1 
ATOM   6372 N  N     . THR B 1 426 ? 23.484  -8.330  13.144  1.00 17.91 ? 405 THR B N     1 
ATOM   6373 C  CA    . THR B 1 426 ? 24.056  -9.656  12.759  1.00 19.86 ? 405 THR B CA    1 
ATOM   6374 C  C     . THR B 1 426 ? 23.022  -10.493 12.006  1.00 21.35 ? 405 THR B C     1 
ATOM   6375 O  O     . THR B 1 426 ? 23.403  -11.307 11.138  1.00 25.01 ? 405 THR B O     1 
ATOM   6376 C  CB    . THR B 1 426 ? 24.626  -10.421 13.967  1.00 20.79 ? 405 THR B CB    1 
ATOM   6377 O  OG1   . THR B 1 426 ? 23.594  -10.508 14.960  1.00 20.53 ? 405 THR B OG1   1 
ATOM   6378 C  CG2   . THR B 1 426 ? 25.841  -9.696  14.521  1.00 21.52 ? 405 THR B CG2   1 
ATOM   6379 N  N     . VAL B 1 427 ? 21.740  -10.320 12.276  1.00 16.90 ? 406 VAL B N     1 
ATOM   6380 C  CA    . VAL B 1 427 ? 20.712  -11.212 11.668  1.00 17.78 ? 406 VAL B CA    1 
ATOM   6381 C  C     . VAL B 1 427 ? 20.111  -10.616 10.388  1.00 17.33 ? 406 VAL B C     1 
ATOM   6382 O  O     . VAL B 1 427 ? 19.942  -11.351 9.383   1.00 17.67 ? 406 VAL B O     1 
ATOM   6383 C  CB    . VAL B 1 427 ? 19.658  -11.513 12.734  1.00 17.88 ? 406 VAL B CB    1 
ATOM   6384 C  CG1   . VAL B 1 427 ? 18.476  -12.249 12.122  1.00 18.22 ? 406 VAL B CG1   1 
ATOM   6385 C  CG2   . VAL B 1 427 ? 20.304  -12.272 13.877  1.00 19.72 ? 406 VAL B CG2   1 
ATOM   6386 N  N     . TYR B 1 428 ? 19.782  -9.334  10.406  1.00 14.99 ? 407 TYR B N     1 
ATOM   6387 C  CA    . TYR B 1 428 ? 19.096  -8.649  9.285   1.00 14.89 ? 407 TYR B CA    1 
ATOM   6388 C  C     . TYR B 1 428 ? 20.076  -7.767  8.498   1.00 15.63 ? 407 TYR B C     1 
ATOM   6389 O  O     . TYR B 1 428 ? 19.872  -7.514  7.271   1.00 16.09 ? 407 TYR B O     1 
ATOM   6390 C  CB    . TYR B 1 428 ? 17.916  -7.829  9.823   1.00 16.45 ? 407 TYR B CB    1 
ATOM   6391 C  CG    . TYR B 1 428 ? 16.990  -8.641  10.683  1.00 15.37 ? 407 TYR B CG    1 
ATOM   6392 C  CD1   . TYR B 1 428 ? 16.039  -9.478  10.100  1.00 16.07 ? 407 TYR B CD1   1 
ATOM   6393 C  CD2   . TYR B 1 428 ? 17.133  -8.670  12.053  1.00 19.51 ? 407 TYR B CD2   1 
ATOM   6394 C  CE1   . TYR B 1 428 ? 15.211  -10.254 10.885  1.00 17.92 ? 407 TYR B CE1   1 
ATOM   6395 C  CE2   . TYR B 1 428 ? 16.317  -9.465  12.855  1.00 20.50 ? 407 TYR B CE2   1 
ATOM   6396 C  CZ    . TYR B 1 428 ? 15.418  -10.326 12.250  1.00 21.33 ? 407 TYR B CZ    1 
ATOM   6397 O  OH    . TYR B 1 428 ? 14.628  -11.157 13.009  1.00 21.98 ? 407 TYR B OH    1 
ATOM   6398 N  N     . GLY B 1 429 ? 21.068  -7.218  9.207   1.00 18.11 ? 408 GLY B N     1 
ATOM   6399 C  CA    . GLY B 1 429 ? 22.003  -6.219  8.666   1.00 18.29 ? 408 GLY B CA    1 
ATOM   6400 C  C     . GLY B 1 429 ? 22.628  -6.575  7.326   1.00 15.80 ? 408 GLY B C     1 
ATOM   6401 O  O     . GLY B 1 429 ? 22.843  -5.678  6.507   1.00 17.29 ? 408 GLY B O     1 
ATOM   6402 N  N     . PRO B 1 430 ? 23.010  -7.843  7.032   1.00 17.48 ? 409 PRO B N     1 
ATOM   6403 C  CA    . PRO B 1 430 ? 23.652  -8.148  5.747   1.00 18.39 ? 409 PRO B CA    1 
ATOM   6404 C  C     . PRO B 1 430 ? 22.861  -7.751  4.485   1.00 20.42 ? 409 PRO B C     1 
ATOM   6405 O  O     . PRO B 1 430 ? 23.473  -7.636  3.391   1.00 21.27 ? 409 PRO B O     1 
ATOM   6406 C  CB    . PRO B 1 430 ? 23.914  -9.651  5.829   1.00 20.78 ? 409 PRO B CB    1 
ATOM   6407 C  CG    . PRO B 1 430 ? 24.018  -9.940  7.315   1.00 19.08 ? 409 PRO B CG    1 
ATOM   6408 C  CD    . PRO B 1 430 ? 23.027  -8.988  7.960   1.00 17.67 ? 409 PRO B CD    1 
ATOM   6409 N  N     . ALA B 1 431 ? 21.554  -7.507  4.624   1.00 17.41 ? 410 ALA B N     1 
ATOM   6410 C  CA    . ALA B 1 431 ? 20.677  -7.088  3.507   1.00 20.51 ? 410 ALA B CA    1 
ATOM   6411 C  C     . ALA B 1 431 ? 20.737  -5.568  3.278   1.00 20.82 ? 410 ALA B C     1 
ATOM   6412 O  O     . ALA B 1 431 ? 20.064  -5.119  2.354   1.00 24.07 ? 410 ALA B O     1 
ATOM   6413 C  CB    . ALA B 1 431 ? 19.256  -7.528  3.728   1.00 17.94 ? 410 ALA B CB    1 
ATOM   6414 N  N     . LEU B 1 432 ? 21.471  -4.806  4.094   1.00 17.52 ? 411 LEU B N     1 
ATOM   6415 C  CA    . LEU B 1 432 ? 21.446  -3.319  4.056   1.00 19.29 ? 411 LEU B CA    1 
ATOM   6416 C  C     . LEU B 1 432 ? 21.629  -2.769  2.641   1.00 18.63 ? 411 LEU B C     1 
ATOM   6417 O  O     . LEU B 1 432 ? 20.821  -1.902  2.261   1.00 21.59 ? 411 LEU B O     1 
ATOM   6418 C  CB    . LEU B 1 432 ? 22.578  -2.809  4.937   1.00 18.82 ? 411 LEU B CB    1 
ATOM   6419 C  CG    . LEU B 1 432 ? 22.735  -1.305  5.005   1.00 20.55 ? 411 LEU B CG    1 
ATOM   6420 C  CD1   . LEU B 1 432 ? 21.512  -0.660  5.638   1.00 20.88 ? 411 LEU B CD1   1 
ATOM   6421 C  CD2   . LEU B 1 432 ? 23.989  -0.957  5.785   1.00 23.78 ? 411 LEU B CD2   1 
ATOM   6422 N  N     . ARG B 1 433 ? 22.666  -3.190  1.906   1.00 18.84 ? 412 ARG B N     1 
ATOM   6423 C  CA    . ARG B 1 433 ? 23.088  -2.507  0.630   1.00 21.19 ? 412 ARG B CA    1 
ATOM   6424 C  C     . ARG B 1 433 ? 22.868  -3.355  -0.618  1.00 20.98 ? 412 ARG B C     1 
ATOM   6425 O  O     . ARG B 1 433 ? 23.098  -2.841  -1.741  1.00 22.81 ? 412 ARG B O     1 
ATOM   6426 C  CB    . ARG B 1 433 ? 24.606  -2.340  0.528   1.00 25.40 ? 412 ARG B CB    1 
ATOM   6427 C  CG    . ARG B 1 433 ? 25.136  -1.103  1.190   1.00 30.71 ? 412 ARG B CG    1 
ATOM   6428 C  CD    . ARG B 1 433 ? 26.640  -1.134  1.057   1.00 29.38 ? 412 ARG B CD    1 
ATOM   6429 N  NE    . ARG B 1 433 ? 26.945  -0.465  2.271   1.00 35.42 ? 412 ARG B NE    1 
ATOM   6430 C  CZ    . ARG B 1 433 ? 27.392  -0.995  3.379   1.00 32.20 ? 412 ARG B CZ    1 
ATOM   6431 N  NH1   . ARG B 1 433 ? 27.743  -2.266  3.475   1.00 31.24 ? 412 ARG B NH1   1 
ATOM   6432 N  NH2   . ARG B 1 433 ? 27.536  -0.198  4.405   1.00 33.84 ? 412 ARG B NH2   1 
ATOM   6433 N  N     . VAL B 1 434 ? 22.577  -4.634  -0.426  1.00 19.63 ? 413 VAL B N     1 
ATOM   6434 C  CA    . VAL B 1 434 ? 22.493  -5.638  -1.534  1.00 21.21 ? 413 VAL B CA    1 
ATOM   6435 C  C     . VAL B 1 434 ? 21.325  -5.258  -2.434  1.00 20.66 ? 413 VAL B C     1 
ATOM   6436 O  O     . VAL B 1 434 ? 20.168  -5.214  -2.024  1.00 19.24 ? 413 VAL B O     1 
ATOM   6437 C  CB    . VAL B 1 434 ? 22.314  -7.070  -0.993  1.00 23.23 ? 413 VAL B CB    1 
ATOM   6438 C  CG1   . VAL B 1 434 ? 22.074  -8.082  -2.121  1.00 27.49 ? 413 VAL B CG1   1 
ATOM   6439 C  CG2   . VAL B 1 434 ? 23.484  -7.489  -0.139  1.00 25.89 ? 413 VAL B CG2   1 
ATOM   6440 N  N     . PRO B 1 435 ? 21.564  -5.035  -3.720  1.00 19.76 ? 414 PRO B N     1 
ATOM   6441 C  CA    . PRO B 1 435 ? 20.467  -4.743  -4.635  1.00 20.33 ? 414 PRO B CA    1 
ATOM   6442 C  C     . PRO B 1 435 ? 19.479  -5.906  -4.735  1.00 20.45 ? 414 PRO B C     1 
ATOM   6443 O  O     . PRO B 1 435 ? 19.849  -7.044  -4.556  1.00 20.85 ? 414 PRO B O     1 
ATOM   6444 C  CB    . PRO B 1 435 ? 21.125  -4.483  -6.005  1.00 21.03 ? 414 PRO B CB    1 
ATOM   6445 C  CG    . PRO B 1 435 ? 22.552  -4.878  -5.853  1.00 23.27 ? 414 PRO B CG    1 
ATOM   6446 C  CD    . PRO B 1 435 ? 22.875  -5.087  -4.383  1.00 22.94 ? 414 PRO B CD    1 
ATOM   6447 N  N     . VAL B 1 436 ? 18.222  -5.562  -4.985  1.00 18.11 ? 415 VAL B N     1 
ATOM   6448 C  CA    . VAL B 1 436 ? 17.128  -6.540  -5.175  1.00 19.32 ? 415 VAL B CA    1 
ATOM   6449 C  C     . VAL B 1 436 ? 16.774  -6.445  -6.638  1.00 19.29 ? 415 VAL B C     1 
ATOM   6450 O  O     . VAL B 1 436 ? 16.119  -5.462  -7.055  1.00 18.22 ? 415 VAL B O     1 
ATOM   6451 C  CB    . VAL B 1 436 ? 15.964  -6.317  -4.200  1.00 19.22 ? 415 VAL B CB    1 
ATOM   6452 C  CG1   . VAL B 1 436 ? 14.780  -7.232  -4.516  1.00 20.97 ? 415 VAL B CG1   1 
ATOM   6453 C  CG2   . VAL B 1 436 ? 16.448  -6.516  -2.772  1.00 20.09 ? 415 VAL B CG2   1 
ATOM   6454 N  N     . GLY B 1 437 ? 17.403  -7.341  -7.414  1.00 21.97 ? 416 GLY B N     1 
ATOM   6455 C  CA    . GLY B 1 437 ? 17.272  -7.315  -8.883  1.00 22.06 ? 416 GLY B CA    1 
ATOM   6456 C  C     . GLY B 1 437 ? 17.768  -5.989  -9.442  1.00 20.48 ? 416 GLY B C     1 
ATOM   6457 O  O     . GLY B 1 437 ? 18.943  -5.684  -9.316  1.00 21.85 ? 416 GLY B O     1 
ATOM   6458 N  N     . ARG B 1 438 ? 16.884  -5.210  -10.040 1.00 18.09 ? 417 ARG B N     1 
ATOM   6459 C  CA    . ARG B 1 438 ? 17.225  -3.919  -10.677 1.00 18.60 ? 417 ARG B CA    1 
ATOM   6460 C  C     . ARG B 1 438 ? 16.949  -2.735  -9.734  1.00 18.43 ? 417 ARG B C     1 
ATOM   6461 O  O     . ARG B 1 438 ? 17.030  -1.586  -10.190 1.00 17.94 ? 417 ARG B O     1 
ATOM   6462 C  CB    . ARG B 1 438 ? 16.399  -3.789  -11.943 1.00 19.42 ? 417 ARG B CB    1 
ATOM   6463 C  CG    . ARG B 1 438 ? 16.800  -4.755  -13.053 1.00 19.50 ? 417 ARG B CG    1 
ATOM   6464 C  CD    . ARG B 1 438 ? 15.782  -4.740  -14.202 1.00 20.72 ? 417 ARG B CD    1 
ATOM   6465 N  NE    . ARG B 1 438 ? 16.305  -5.518  -15.333 1.00 23.26 ? 417 ARG B NE    1 
ATOM   6466 C  CZ    . ARG B 1 438 ? 17.224  -5.100  -16.182 1.00 29.04 ? 417 ARG B CZ    1 
ATOM   6467 N  NH1   . ARG B 1 438 ? 17.707  -3.870  -16.140 1.00 26.88 ? 417 ARG B NH1   1 
ATOM   6468 N  NH2   . ARG B 1 438 ? 17.684  -5.939  -17.093 1.00 30.29 ? 417 ARG B NH2   1 
ATOM   6469 N  N     . VAL B 1 439 ? 16.662  -3.005  -8.469  1.00 19.47 ? 418 VAL B N     1 
ATOM   6470 C  CA    . VAL B 1 439 ? 16.454  -1.940  -7.449  1.00 18.66 ? 418 VAL B CA    1 
ATOM   6471 C  C     . VAL B 1 439 ? 17.685  -1.850  -6.554  1.00 17.55 ? 418 VAL B C     1 
ATOM   6472 O  O     . VAL B 1 439 ? 17.995  -2.798  -5.790  1.00 20.28 ? 418 VAL B O     1 
ATOM   6473 C  CB    . VAL B 1 439 ? 15.156  -2.170  -6.655  1.00 19.97 ? 418 VAL B CB    1 
ATOM   6474 C  CG1   . VAL B 1 439 ? 14.986  -1.084  -5.588  1.00 19.82 ? 418 VAL B CG1   1 
ATOM   6475 C  CG2   . VAL B 1 439 ? 13.951  -2.200  -7.575  1.00 21.10 ? 418 VAL B CG2   1 
ATOM   6476 N  N     . HIS B 1 440 ? 18.341  -0.686  -6.572  1.00 17.61 ? 419 HIS B N     1 
ATOM   6477 C  CA    . HIS B 1 440 ? 19.557  -0.412  -5.789  1.00 15.69 ? 419 HIS B CA    1 
ATOM   6478 C  C     . HIS B 1 440 ? 19.216  0.620   -4.707  1.00 16.71 ? 419 HIS B C     1 
ATOM   6479 O  O     . HIS B 1 440 ? 18.179  1.249   -4.832  1.00 18.12 ? 419 HIS B O     1 
ATOM   6480 C  CB    . HIS B 1 440 ? 20.656  0.098   -6.695  1.00 17.09 ? 419 HIS B CB    1 
ATOM   6481 C  CG    . HIS B 1 440 ? 21.003  -0.818  -7.812  1.00 17.80 ? 419 HIS B CG    1 
ATOM   6482 N  ND1   . HIS B 1 440 ? 22.216  -1.434  -7.892  1.00 19.17 ? 419 HIS B ND1   1 
ATOM   6483 C  CD2   . HIS B 1 440 ? 20.338  -1.165  -8.923  1.00 19.27 ? 419 HIS B CD2   1 
ATOM   6484 C  CE1   . HIS B 1 440 ? 22.248  -2.188  -8.980  1.00 20.33 ? 419 HIS B CE1   1 
ATOM   6485 N  NE2   . HIS B 1 440 ? 21.127  -2.015  -9.637  1.00 19.74 ? 419 HIS B NE2   1 
ATOM   6486 N  N     . TRP B 1 441 ? 20.054  0.708   -3.690  1.00 16.43 ? 420 TRP B N     1 
ATOM   6487 C  CA    . TRP B 1 441 ? 19.770  1.425   -2.411  1.00 17.51 ? 420 TRP B CA    1 
ATOM   6488 C  C     . TRP B 1 441 ? 20.845  2.473   -2.192  1.00 18.06 ? 420 TRP B C     1 
ATOM   6489 O  O     . TRP B 1 441 ? 22.049  2.128   -2.265  1.00 18.68 ? 420 TRP B O     1 
ATOM   6490 C  CB    . TRP B 1 441 ? 19.751  0.446   -1.230  1.00 18.77 ? 420 TRP B CB    1 
ATOM   6491 C  CG    . TRP B 1 441 ? 18.882  -0.749  -1.480  1.00 18.40 ? 420 TRP B CG    1 
ATOM   6492 C  CD1   . TRP B 1 441 ? 19.324  -2.018  -1.703  1.00 18.71 ? 420 TRP B CD1   1 
ATOM   6493 C  CD2   . TRP B 1 441 ? 17.443  -0.792  -1.569  1.00 18.55 ? 420 TRP B CD2   1 
ATOM   6494 N  NE1   . TRP B 1 441 ? 18.260  -2.835  -1.974  1.00 20.65 ? 420 TRP B NE1   1 
ATOM   6495 C  CE2   . TRP B 1 441 ? 17.098  -2.124  -1.863  1.00 20.13 ? 420 TRP B CE2   1 
ATOM   6496 C  CE3   . TRP B 1 441 ? 16.411  0.157   -1.435  1.00 18.63 ? 420 TRP B CE3   1 
ATOM   6497 C  CZ2   . TRP B 1 441 ? 15.767  -2.540  -2.031  1.00 22.13 ? 420 TRP B CZ2   1 
ATOM   6498 C  CZ3   . TRP B 1 441 ? 15.105  -0.256  -1.567  1.00 17.64 ? 420 TRP B CZ3   1 
ATOM   6499 C  CH2   . TRP B 1 441 ? 14.792  -1.579  -1.875  1.00 20.59 ? 420 TRP B CH2   1 
ATOM   6500 N  N     . ALA B 1 442 ? 20.409  3.658   -1.784  1.00 17.58 ? 421 ALA B N     1 
ATOM   6501 C  CA    . ALA B 1 442 ? 21.293  4.731   -1.334  1.00 17.96 ? 421 ALA B CA    1 
ATOM   6502 C  C     . ALA B 1 442 ? 20.641  5.412   -0.130  1.00 18.34 ? 421 ALA B C     1 
ATOM   6503 O  O     . ALA B 1 442 ? 19.573  4.986   0.309   1.00 19.15 ? 421 ALA B O     1 
ATOM   6504 C  CB    . ALA B 1 442 ? 21.565  5.707   -2.474  1.00 17.96 ? 421 ALA B CB    1 
ATOM   6505 N  N     . GLY B 1 443 ? 21.350  6.367   0.448   1.00 16.15 ? 422 GLY B N     1 
ATOM   6506 C  CA    . GLY B 1 443 ? 20.962  7.016   1.697   1.00 16.43 ? 422 GLY B CA    1 
ATOM   6507 C  C     . GLY B 1 443 ? 22.090  6.921   2.699   1.00 16.69 ? 422 GLY B C     1 
ATOM   6508 O  O     . GLY B 1 443 ? 22.911  5.977   2.650   1.00 17.88 ? 422 GLY B O     1 
ATOM   6509 N  N     . THR B 1 444 ? 22.140  7.864   3.633   1.00 14.13 ? 423 THR B N     1 
ATOM   6510 C  CA    . THR B 1 444 ? 23.233  7.977   4.599   1.00 14.75 ? 423 THR B CA    1 
ATOM   6511 C  C     . THR B 1 444 ? 23.383  6.685   5.410   1.00 15.94 ? 423 THR B C     1 
ATOM   6512 O  O     . THR B 1 444 ? 24.527  6.333   5.792   1.00 17.37 ? 423 THR B O     1 
ATOM   6513 C  CB    . THR B 1 444 ? 23.027  9.221   5.460   1.00 15.47 ? 423 THR B CB    1 
ATOM   6514 O  OG1   . THR B 1 444 ? 24.269  9.416   6.110   1.00 16.30 ? 423 THR B OG1   1 
ATOM   6515 C  CG2   . THR B 1 444 ? 21.905  9.135   6.470   1.00 15.41 ? 423 THR B CG2   1 
ATOM   6516 N  N     . GLU B 1 445 ? 22.262  5.994   5.662   1.00 16.37 ? 424 GLU B N     1 
ATOM   6517 C  CA    . GLU B 1 445 ? 22.228  4.719   6.421   1.00 17.47 ? 424 GLU B CA    1 
ATOM   6518 C  C     . GLU B 1 445 ? 23.011  3.615   5.701   1.00 18.98 ? 424 GLU B C     1 
ATOM   6519 O  O     . GLU B 1 445 ? 23.314  2.625   6.356   1.00 18.32 ? 424 GLU B O     1 
ATOM   6520 C  CB    . GLU B 1 445 ? 20.773  4.302   6.626   1.00 19.86 ? 424 GLU B CB    1 
ATOM   6521 C  CG    . GLU B 1 445 ? 20.081  5.169   7.670   1.00 20.03 ? 424 GLU B CG    1 
ATOM   6522 C  CD    . GLU B 1 445 ? 19.422  6.458   7.219   1.00 22.40 ? 424 GLU B CD    1 
ATOM   6523 O  OE1   . GLU B 1 445 ? 18.903  7.190   8.133   1.00 22.33 ? 424 GLU B OE1   1 
ATOM   6524 O  OE2   . GLU B 1 445 ? 19.424  6.737   5.988   1.00 19.46 ? 424 GLU B OE2   1 
ATOM   6525 N  N     . THR B 1 446 ? 23.354  3.771   4.430   1.00 17.22 ? 425 THR B N     1 
ATOM   6526 C  CA    . THR B 1 446 ? 24.135  2.731   3.674   1.00 15.93 ? 425 THR B CA    1 
ATOM   6527 C  C     . THR B 1 446 ? 25.602  3.125   3.530   1.00 16.74 ? 425 THR B C     1 
ATOM   6528 O  O     . THR B 1 446 ? 26.365  2.363   2.913   1.00 19.11 ? 425 THR B O     1 
ATOM   6529 C  CB    . THR B 1 446 ? 23.475  2.411   2.330   1.00 17.41 ? 425 THR B CB    1 
ATOM   6530 O  OG1   . THR B 1 446 ? 23.544  3.571   1.498   1.00 17.99 ? 425 THR B OG1   1 
ATOM   6531 C  CG2   . THR B 1 446 ? 22.018  2.008   2.439   1.00 19.04 ? 425 THR B CG2   1 
ATOM   6532 N  N     . ALA B 1 447 ? 26.031  4.258   4.092   1.00 18.50 ? 426 ALA B N     1 
ATOM   6533 C  CA    . ALA B 1 447 ? 27.410  4.765   3.934   1.00 18.07 ? 426 ALA B CA    1 
ATOM   6534 C  C     . ALA B 1 447 ? 28.337  3.984   4.849   1.00 19.64 ? 426 ALA B C     1 
ATOM   6535 O  O     . ALA B 1 447 ? 27.890  3.585   5.943   1.00 18.23 ? 426 ALA B O     1 
ATOM   6536 C  CB    . ALA B 1 447 ? 27.489  6.213   4.323   1.00 19.49 ? 426 ALA B CB    1 
ATOM   6537 N  N     . GLU B 1 448 ? 29.600  3.810   4.438   1.00 17.94 ? 427 GLU B N     1 
ATOM   6538 C  CA    . GLU B 1 448 ? 30.659  3.197   5.299   1.00 19.71 ? 427 GLU B CA    1 
ATOM   6539 C  C     . GLU B 1 448 ? 31.239  4.302   6.177   1.00 19.34 ? 427 GLU B C     1 
ATOM   6540 O  O     . GLU B 1 448 ? 31.539  4.042   7.340   1.00 16.64 ? 427 GLU B O     1 
ATOM   6541 C  CB    . GLU B 1 448 ? 31.746  2.544   4.435   1.00 20.66 ? 427 GLU B CB    1 
ATOM   6542 C  CG    . GLU B 1 448 ? 31.194  1.398   3.639   1.00 22.14 ? 427 GLU B CG    1 
ATOM   6543 C  CD    . GLU B 1 448 ? 32.224  0.627   2.819   1.00 28.12 ? 427 GLU B CD    1 
ATOM   6544 O  OE1   . GLU B 1 448 ? 31.803  -0.043  1.885   1.00 34.67 ? 427 GLU B OE1   1 
ATOM   6545 O  OE2   . GLU B 1 448 ? 33.407  0.717   3.126   1.00 28.26 ? 427 GLU B OE2   1 
ATOM   6546 N  N     . ARG B 1 449 ? 31.422  5.501   5.613   1.00 18.09 ? 428 ARG B N     1 
ATOM   6547 C  CA    . ARG B 1 449 ? 32.077  6.589   6.369   1.00 19.73 ? 428 ARG B CA    1 
ATOM   6548 C  C     . ARG B 1 449 ? 31.090  7.708   6.650   1.00 16.53 ? 428 ARG B C     1 
ATOM   6549 O  O     . ARG B 1 449 ? 30.345  8.095   5.700   1.00 17.96 ? 428 ARG B O     1 
ATOM   6550 C  CB    . ARG B 1 449 ? 33.278  7.128   5.597   1.00 24.15 ? 428 ARG B CB    1 
ATOM   6551 C  CG    . ARG B 1 449 ? 34.458  6.172   5.639   1.00 33.27 ? 428 ARG B CG    1 
ATOM   6552 C  CD    . ARG B 1 449 ? 35.251  6.209   4.336   1.00 46.10 ? 428 ARG B CD    1 
ATOM   6553 N  NE    . ARG B 1 449 ? 36.362  5.278   4.454   1.00 59.21 ? 428 ARG B NE    1 
ATOM   6554 C  CZ    . ARG B 1 449 ? 37.507  5.544   5.081   1.00 67.60 ? 428 ARG B CZ    1 
ATOM   6555 N  NH1   . ARG B 1 449 ? 37.715  6.732   5.632   1.00 78.27 ? 428 ARG B NH1   1 
ATOM   6556 N  NH2   . ARG B 1 449 ? 38.446  4.615   5.151   1.00 72.60 ? 428 ARG B NH2   1 
ATOM   6557 N  N     . TRP B 1 450 ? 31.138  8.240   7.865   1.00 16.28 ? 429 TRP B N     1 
ATOM   6558 C  CA    . TRP B 1 450 ? 30.197  9.314   8.291   1.00 16.15 ? 429 TRP B CA    1 
ATOM   6559 C  C     . TRP B 1 450 ? 28.764  8.893   7.986   1.00 16.12 ? 429 TRP B C     1 
ATOM   6560 O  O     . TRP B 1 450 ? 27.924  9.744   7.578   1.00 16.83 ? 429 TRP B O     1 
ATOM   6561 C  CB    . TRP B 1 450 ? 30.612  10.627  7.599   1.00 16.81 ? 429 TRP B CB    1 
ATOM   6562 C  CG    . TRP B 1 450 ? 31.832  11.201  8.260   1.00 16.68 ? 429 TRP B CG    1 
ATOM   6563 C  CD1   . TRP B 1 450 ? 33.094  11.297  7.744   1.00 17.63 ? 429 TRP B CD1   1 
ATOM   6564 C  CD2   . TRP B 1 450 ? 31.885  11.811  9.556   1.00 17.09 ? 429 TRP B CD2   1 
ATOM   6565 N  NE1   . TRP B 1 450 ? 33.932  11.900  8.654   1.00 17.91 ? 429 TRP B NE1   1 
ATOM   6566 C  CE2   . TRP B 1 450 ? 33.213  12.241  9.765   1.00 17.89 ? 429 TRP B CE2   1 
ATOM   6567 C  CE3   . TRP B 1 450 ? 30.945  12.008  10.579  1.00 16.38 ? 429 TRP B CE3   1 
ATOM   6568 C  CZ2   . TRP B 1 450 ? 33.614  12.858  10.953  1.00 18.05 ? 429 TRP B CZ2   1 
ATOM   6569 C  CZ3   . TRP B 1 450 ? 31.339  12.654  11.729  1.00 17.96 ? 429 TRP B CZ3   1 
ATOM   6570 C  CH2   . TRP B 1 450 ? 32.656  13.083  11.914  1.00 17.58 ? 429 TRP B CH2   1 
ATOM   6571 N  N     . THR B 1 451 ? 28.436  7.631   8.254   1.00 16.92 ? 430 THR B N     1 
ATOM   6572 C  CA    . THR B 1 451 ? 27.033  7.197   8.243   1.00 16.82 ? 430 THR B CA    1 
ATOM   6573 C  C     . THR B 1 451 ? 26.242  8.112   9.206   1.00 15.92 ? 430 THR B C     1 
ATOM   6574 O  O     . THR B 1 451 ? 26.738  8.429   10.328  1.00 16.32 ? 430 THR B O     1 
ATOM   6575 C  CB    . THR B 1 451 ? 26.850  5.702   8.559   1.00 19.13 ? 430 THR B CB    1 
ATOM   6576 O  OG1   . THR B 1 451 ? 25.499  5.332   8.233   1.00 16.99 ? 430 THR B OG1   1 
ATOM   6577 C  CG2   . THR B 1 451 ? 27.151  5.328   9.992   1.00 17.35 ? 430 THR B CG2   1 
ATOM   6578 N  N     . GLY B 1 452 ? 25.056  8.517   8.777   1.00 14.86 ? 431 GLY B N     1 
ATOM   6579 C  CA    . GLY B 1 452 ? 24.126  9.363   9.549   1.00 15.91 ? 431 GLY B CA    1 
ATOM   6580 C  C     . GLY B 1 452 ? 24.317  10.842  9.291   1.00 17.59 ? 431 GLY B C     1 
ATOM   6581 O  O     . GLY B 1 452 ? 23.467  11.644  9.759   1.00 19.78 ? 431 GLY B O     1 
ATOM   6582 N  N     . TYR B 1 453 ? 25.343  11.218  8.517   1.00 17.05 ? 432 TYR B N     1 
ATOM   6583 C  CA    . TYR B 1 453 ? 25.686  12.625  8.174   1.00 16.91 ? 432 TYR B CA    1 
ATOM   6584 C  C     . TYR B 1 453 ? 25.457  12.879  6.670   1.00 17.30 ? 432 TYR B C     1 
ATOM   6585 O  O     . TYR B 1 453 ? 25.345  11.913  5.833   1.00 17.25 ? 432 TYR B O     1 
ATOM   6586 C  CB    . TYR B 1 453 ? 27.121  12.901  8.630   1.00 16.56 ? 432 TYR B CB    1 
ATOM   6587 C  CG    . TYR B 1 453 ? 27.300  12.863  10.121  1.00 16.96 ? 432 TYR B CG    1 
ATOM   6588 C  CD1   . TYR B 1 453 ? 27.294  14.022  10.886  1.00 15.51 ? 432 TYR B CD1   1 
ATOM   6589 C  CD2   . TYR B 1 453 ? 27.345  11.660  10.810  1.00 16.43 ? 432 TYR B CD2   1 
ATOM   6590 C  CE1   . TYR B 1 453 ? 27.453  13.996  12.257  1.00 16.57 ? 432 TYR B CE1   1 
ATOM   6591 C  CE2   . TYR B 1 453 ? 27.495  11.622  12.175  1.00 16.84 ? 432 TYR B CE2   1 
ATOM   6592 C  CZ    . TYR B 1 453 ? 27.499  12.792  12.915  1.00 17.28 ? 432 TYR B CZ    1 
ATOM   6593 O  OH    . TYR B 1 453 ? 27.562  12.735  14.272  1.00 19.65 ? 432 TYR B OH    1 
ATOM   6594 N  N     . ILE B 1 454 ? 25.431  14.162  6.309   1.00 16.89 ? 433 ILE B N     1 
ATOM   6595 C  CA    . ILE B 1 454 ? 25.391  14.622  4.903   1.00 16.95 ? 433 ILE B CA    1 
ATOM   6596 C  C     . ILE B 1 454 ? 26.571  13.996  4.135   1.00 15.51 ? 433 ILE B C     1 
ATOM   6597 O  O     . ILE B 1 454 ? 26.334  13.459  3.009   1.00 15.78 ? 433 ILE B O     1 
ATOM   6598 C  CB    . ILE B 1 454 ? 25.422  16.147  4.837   1.00 18.20 ? 433 ILE B CB    1 
ATOM   6599 C  CG1   . ILE B 1 454 ? 24.257  16.793  5.585   1.00 18.68 ? 433 ILE B CG1   1 
ATOM   6600 C  CG2   . ILE B 1 454 ? 25.451  16.610  3.405   1.00 18.47 ? 433 ILE B CG2   1 
ATOM   6601 C  CD1   . ILE B 1 454 ? 24.581  18.213  5.957   1.00 18.48 ? 433 ILE B CD1   1 
ATOM   6602 N  N     . ASP B 1 455 ? 27.757  13.985  4.738   1.00 17.06 ? 434 ASP B N     1 
ATOM   6603 C  CA    . ASP B 1 455 ? 28.961  13.387  4.101   1.00 17.39 ? 434 ASP B CA    1 
ATOM   6604 C  C     . ASP B 1 455 ? 28.647  11.938  3.694   1.00 17.82 ? 434 ASP B C     1 
ATOM   6605 O  O     . ASP B 1 455 ? 28.952  11.566  2.555   1.00 17.71 ? 434 ASP B O     1 
ATOM   6606 C  CB    . ASP B 1 455 ? 30.192  13.480  4.993   1.00 19.16 ? 434 ASP B CB    1 
ATOM   6607 C  CG    . ASP B 1 455 ? 31.479  13.200  4.237   1.00 19.28 ? 434 ASP B CG    1 
ATOM   6608 O  OD1   . ASP B 1 455 ? 32.041  12.106  4.394   1.00 19.57 ? 434 ASP B OD1   1 
ATOM   6609 O  OD2   . ASP B 1 455 ? 31.912  14.113  3.490   1.00 22.13 ? 434 ASP B OD2   1 
ATOM   6610 N  N     . GLY B 1 456 ? 28.108  11.112  4.602   1.00 17.99 ? 435 GLY B N     1 
ATOM   6611 C  CA    . GLY B 1 456 ? 27.700  9.726   4.271   1.00 18.81 ? 435 GLY B CA    1 
ATOM   6612 C  C     . GLY B 1 456 ? 26.577  9.661   3.257   1.00 17.56 ? 435 GLY B C     1 
ATOM   6613 O  O     . GLY B 1 456 ? 26.601  8.737   2.376   1.00 17.77 ? 435 GLY B O     1 
ATOM   6614 N  N     . ALA B 1 457 ? 25.611  10.583  3.258   1.00 17.45 ? 436 ALA B N     1 
ATOM   6615 C  CA    . ALA B 1 457 ? 24.588  10.607  2.183   1.00 17.68 ? 436 ALA B CA    1 
ATOM   6616 C  C     . ALA B 1 457 ? 25.296  10.727  0.820   1.00 18.71 ? 436 ALA B C     1 
ATOM   6617 O  O     . ALA B 1 457 ? 24.956  9.967   -0.126  1.00 17.84 ? 436 ALA B O     1 
ATOM   6618 C  CB    . ALA B 1 457 ? 23.556  11.677  2.370   1.00 17.20 ? 436 ALA B CB    1 
ATOM   6619 N  N     . ILE B 1 458 ? 26.312  11.580  0.734   1.00 17.47 ? 437 ILE B N     1 
ATOM   6620 C  CA    . ILE B 1 458 ? 27.013  11.832  -0.563  1.00 17.66 ? 437 ILE B CA    1 
ATOM   6621 C  C     . ILE B 1 458 ? 27.782  10.564  -0.943  1.00 16.68 ? 437 ILE B C     1 
ATOM   6622 O  O     . ILE B 1 458 ? 27.588  10.076  -2.075  1.00 20.34 ? 437 ILE B O     1 
ATOM   6623 C  CB    . ILE B 1 458 ? 27.912  13.086  -0.502  1.00 18.38 ? 437 ILE B CB    1 
ATOM   6624 C  CG1   . ILE B 1 458 ? 27.110  14.378  -0.290  1.00 18.36 ? 437 ILE B CG1   1 
ATOM   6625 C  CG2   . ILE B 1 458 ? 28.775  13.173  -1.745  1.00 17.57 ? 437 ILE B CG2   1 
ATOM   6626 C  CD1   . ILE B 1 458 ? 27.999  15.525  0.136   1.00 18.42 ? 437 ILE B CD1   1 
ATOM   6627 N  N     . GLU B 1 459 ? 28.524  9.972   -0.013  1.00 18.27 ? 438 GLU B N     1 
ATOM   6628 C  CA    . GLU B 1 459 ? 29.217  8.688   -0.268  1.00 18.13 ? 438 GLU B CA    1 
ATOM   6629 C  C     . GLU B 1 459 ? 28.246  7.656   -0.854  1.00 17.31 ? 438 GLU B C     1 
ATOM   6630 O  O     . GLU B 1 459 ? 28.584  6.978   -1.868  1.00 17.10 ? 438 GLU B O     1 
ATOM   6631 C  CB    . GLU B 1 459 ? 29.792  8.103   1.015   1.00 19.80 ? 438 GLU B CB    1 
ATOM   6632 C  CG    . GLU B 1 459 ? 30.589  6.851   0.729   1.00 21.91 ? 438 GLU B CG    1 
ATOM   6633 C  CD    . GLU B 1 459 ? 30.866  6.013   1.968   1.00 25.75 ? 438 GLU B CD    1 
ATOM   6634 O  OE1   . GLU B 1 459 ? 30.434  4.856   2.004   1.00 32.86 ? 438 GLU B OE1   1 
ATOM   6635 O  OE2   . GLU B 1 459 ? 31.461  6.545   2.900   1.00 29.44 ? 438 GLU B OE2   1 
ATOM   6636 N  N     . SER B 1 460 ? 27.080  7.501   -0.240  1.00 17.39 ? 439 SER B N     1 
ATOM   6637 C  CA    . SER B 1 460 ? 26.101  6.453   -0.637  1.00 18.00 ? 439 SER B CA    1 
ATOM   6638 C  C     . SER B 1 460 ? 25.594  6.705   -2.066  1.00 18.94 ? 439 SER B C     1 
ATOM   6639 O  O     . SER B 1 460 ? 25.376  5.726   -2.798  1.00 19.26 ? 439 SER B O     1 
ATOM   6640 C  CB    . SER B 1 460 ? 24.964  6.374   0.373   1.00 19.21 ? 439 SER B CB    1 
ATOM   6641 O  OG    . SER B 1 460 ? 24.029  7.444   0.146   1.00 21.89 ? 439 SER B OG    1 
ATOM   6642 N  N     . GLY B 1 461 ? 25.353  7.964   -2.436  1.00 18.80 ? 440 GLY B N     1 
ATOM   6643 C  CA    . GLY B 1 461 ? 24.949  8.357   -3.800  1.00 18.13 ? 440 GLY B CA    1 
ATOM   6644 C  C     . GLY B 1 461 ? 26.012  7.998   -4.820  1.00 19.44 ? 440 GLY B C     1 
ATOM   6645 O  O     . GLY B 1 461 ? 25.658  7.410   -5.868  1.00 17.41 ? 440 GLY B O     1 
ATOM   6646 N  N     . GLN B 1 462 ? 27.285  8.273   -4.513  1.00 21.39 ? 441 GLN B N     1 
ATOM   6647 C  CA    . GLN B 1 462 ? 28.404  7.942   -5.452  1.00 23.56 ? 441 GLN B CA    1 
ATOM   6648 C  C     . GLN B 1 462 ? 28.474  6.420   -5.585  1.00 23.11 ? 441 GLN B C     1 
ATOM   6649 O  O     . GLN B 1 462 ? 28.617  5.893   -6.734  1.00 21.93 ? 441 GLN B O     1 
ATOM   6650 C  CB    . GLN B 1 462 ? 29.748  8.518   -5.022  1.00 26.63 ? 441 GLN B CB    1 
ATOM   6651 C  CG    . GLN B 1 462 ? 29.739  10.023  -4.818  1.00 27.81 ? 441 GLN B CG    1 
ATOM   6652 C  CD    . GLN B 1 462 ? 30.941  10.507  -4.039  1.00 39.74 ? 441 GLN B CD    1 
ATOM   6653 O  OE1   . GLN B 1 462 ? 31.605  9.735   -3.349  1.00 44.92 ? 441 GLN B OE1   1 
ATOM   6654 N  NE2   . GLN B 1 462 ? 31.229  11.802  -4.096  1.00 44.46 ? 441 GLN B NE2   1 
ATOM   6655 N  N     . ARG B 1 463 ? 28.314  5.705   -4.472  1.00 19.56 ? 442 ARG B N     1 
ATOM   6656 C  CA    . ARG B 1 463 ? 28.431  4.233   -4.508  1.00 20.44 ? 442 ARG B CA    1 
ATOM   6657 C  C     . ARG B 1 463 ? 27.292  3.670   -5.369  1.00 19.28 ? 442 ARG B C     1 
ATOM   6658 O  O     . ARG B 1 463 ? 27.541  2.806   -6.208  1.00 19.01 ? 442 ARG B O     1 
ATOM   6659 C  CB    . ARG B 1 463 ? 28.376  3.649   -3.100  1.00 22.40 ? 442 ARG B CB    1 
ATOM   6660 C  CG    . ARG B 1 463 ? 28.736  2.168   -3.055  1.00 25.17 ? 442 ARG B CG    1 
ATOM   6661 C  CD    . ARG B 1 463 ? 27.585  1.247   -2.829  1.00 26.91 ? 442 ARG B CD    1 
ATOM   6662 N  NE    . ARG B 1 463 ? 26.657  1.802   -1.848  1.00 25.05 ? 442 ARG B NE    1 
ATOM   6663 C  CZ    . ARG B 1 463 ? 25.336  1.685   -1.927  1.00 23.05 ? 442 ARG B CZ    1 
ATOM   6664 N  NH1   . ARG B 1 463 ? 24.783  0.944   -2.887  1.00 22.47 ? 442 ARG B NH1   1 
ATOM   6665 N  NH2   . ARG B 1 463 ? 24.588  2.253   -0.992  1.00 20.58 ? 442 ARG B NH2   1 
ATOM   6666 N  N     . ALA B 1 464 ? 26.055  4.085   -5.136  1.00 19.22 ? 443 ALA B N     1 
ATOM   6667 C  CA    . ALA B 1 464 ? 24.870  3.542   -5.825  1.00 19.87 ? 443 ALA B CA    1 
ATOM   6668 C  C     . ALA B 1 464 ? 24.913  3.914   -7.306  1.00 19.13 ? 443 ALA B C     1 
ATOM   6669 O  O     . ALA B 1 464 ? 24.594  3.047   -8.135  1.00 19.42 ? 443 ALA B O     1 
ATOM   6670 C  CB    . ALA B 1 464 ? 23.584  4.020   -5.170  1.00 20.03 ? 443 ALA B CB    1 
ATOM   6671 N  N     . ALA B 1 465 ? 25.350  5.126   -7.654  1.00 20.54 ? 444 ALA B N     1 
ATOM   6672 C  CA    . ALA B 1 465 ? 25.545  5.484   -9.075  1.00 20.27 ? 444 ALA B CA    1 
ATOM   6673 C  C     . ALA B 1 465 ? 26.584  4.555   -9.737  1.00 17.11 ? 444 ALA B C     1 
ATOM   6674 O  O     . ALA B 1 465 ? 26.259  4.030   -10.814 1.00 20.46 ? 444 ALA B O     1 
ATOM   6675 C  CB    . ALA B 1 465 ? 25.933  6.915   -9.231  1.00 19.05 ? 444 ALA B CB    1 
ATOM   6676 N  N     . ALA B 1 466 ? 27.736  4.318   -9.118  1.00 19.82 ? 445 ALA B N     1 
ATOM   6677 C  CA    . ALA B 1 466 ? 28.821  3.452   -9.677  1.00 20.72 ? 445 ALA B CA    1 
ATOM   6678 C  C     . ALA B 1 466 ? 28.282  2.039   -9.860  1.00 22.42 ? 445 ALA B C     1 
ATOM   6679 O  O     . ALA B 1 466 ? 28.518  1.395   -10.890 1.00 19.29 ? 445 ALA B O     1 
ATOM   6680 C  CB    . ALA B 1 466 ? 30.018  3.438   -8.770  1.00 24.15 ? 445 ALA B CB    1 
ATOM   6681 N  N     . GLU B 1 467 ? 27.497  1.568   -8.902  1.00 21.24 ? 446 GLU B N     1 
ATOM   6682 C  CA    . GLU B 1 467 ? 26.874  0.229   -8.977  1.00 21.03 ? 446 GLU B CA    1 
ATOM   6683 C  C     . GLU B 1 467 ? 25.921  0.136   -10.162 1.00 18.09 ? 446 GLU B C     1 
ATOM   6684 O  O     . GLU B 1 467 ? 25.967  -0.843  -10.950 1.00 20.81 ? 446 GLU B O     1 
ATOM   6685 C  CB    . GLU B 1 467 ? 26.181  0.084   -7.630  1.00 23.50 ? 446 GLU B CB    1 
ATOM   6686 C  CG    . GLU B 1 467 ? 25.842  -1.261  -7.200  1.00 27.31 ? 446 GLU B CG    1 
ATOM   6687 C  CD    . GLU B 1 467 ? 25.226  -1.179  -5.796  1.00 25.60 ? 446 GLU B CD    1 
ATOM   6688 O  OE1   . GLU B 1 467 ? 25.993  -1.017  -4.784  1.00 23.42 ? 446 GLU B OE1   1 
ATOM   6689 O  OE2   . GLU B 1 467 ? 23.982  -1.264  -5.746  1.00 23.69 ? 446 GLU B OE2   1 
ATOM   6690 N  N     . VAL B 1 468 ? 25.055  1.101   -10.325 1.00 18.08 ? 447 VAL B N     1 
ATOM   6691 C  CA    . VAL B 1 468 ? 24.053  1.096   -11.404 1.00 19.48 ? 447 VAL B CA    1 
ATOM   6692 C  C     . VAL B 1 468 ? 24.773  1.203   -12.763 1.00 21.48 ? 447 VAL B C     1 
ATOM   6693 O  O     . VAL B 1 468 ? 24.402  0.453   -13.693 1.00 21.51 ? 447 VAL B O     1 
ATOM   6694 C  CB    . VAL B 1 468 ? 22.984  2.183   -11.195 1.00 22.44 ? 447 VAL B CB    1 
ATOM   6695 C  CG1   . VAL B 1 468 ? 22.131  2.353   -12.429 1.00 23.19 ? 447 VAL B CG1   1 
ATOM   6696 C  CG2   . VAL B 1 468 ? 22.115  1.828   -9.997  1.00 23.04 ? 447 VAL B CG2   1 
ATOM   6697 N  N     . LEU B 1 469 ? 25.759  2.078   -12.858 1.00 19.92 ? 448 LEU B N     1 
ATOM   6698 C  CA    . LEU B 1 469 ? 26.489  2.295   -14.134 1.00 21.77 ? 448 LEU B CA    1 
ATOM   6699 C  C     . LEU B 1 469 ? 27.240  1.003   -14.476 1.00 23.51 ? 448 LEU B C     1 
ATOM   6700 O  O     . LEU B 1 469 ? 27.215  0.664   -15.661 1.00 25.02 ? 448 LEU B O     1 
ATOM   6701 C  CB    . LEU B 1 469 ? 27.444  3.476   -14.008 1.00 21.85 ? 448 LEU B CB    1 
ATOM   6702 C  CG    . LEU B 1 469 ? 26.751  4.833   -13.894 1.00 20.71 ? 448 LEU B CG    1 
ATOM   6703 C  CD1   . LEU B 1 469 ? 27.757  5.897   -13.492 1.00 22.18 ? 448 LEU B CD1   1 
ATOM   6704 C  CD2   . LEU B 1 469 ? 26.013  5.221   -15.163 1.00 22.75 ? 448 LEU B CD2   1 
ATOM   6705 N  N     . ALA B 1 470 ? 27.819  0.292   -13.496 1.00 23.50 ? 449 ALA B N     1 
ATOM   6706 C  CA    . ALA B 1 470 ? 28.530  -0.986  -13.773 1.00 22.20 ? 449 ALA B CA    1 
ATOM   6707 C  C     . ALA B 1 470 ? 27.505  -2.040  -14.234 1.00 23.53 ? 449 ALA B C     1 
ATOM   6708 O  O     . ALA B 1 470 ? 27.801  -2.850  -15.148 1.00 23.46 ? 449 ALA B O     1 
ATOM   6709 C  CB    . ALA B 1 470 ? 29.317  -1.411  -12.557 1.00 23.66 ? 449 ALA B CB    1 
ATOM   6710 N  N     . ALA B 1 471 ? 26.319  -2.088  -13.649 1.00 21.17 ? 450 ALA B N     1 
ATOM   6711 C  CA    . ALA B 1 471 ? 25.311  -3.131  -13.979 1.00 23.93 ? 450 ALA B CA    1 
ATOM   6712 C  C     . ALA B 1 471 ? 24.591  -2.850  -15.306 1.00 26.50 ? 450 ALA B C     1 
ATOM   6713 O  O     . ALA B 1 471 ? 24.077  -3.829  -15.913 1.00 26.94 ? 450 ALA B O     1 
ATOM   6714 C  CB    . ALA B 1 471 ? 24.316  -3.271  -12.862 1.00 24.21 ? 450 ALA B CB    1 
ATOM   6715 N  N     . LEU B 1 472 ? 24.465  -1.595  -15.745 1.00 25.17 ? 451 LEU B N     1 
ATOM   6716 C  CA    . LEU B 1 472 ? 23.907  -1.309  -17.103 1.00 29.71 ? 451 LEU B CA    1 
ATOM   6717 C  C     . LEU B 1 472 ? 24.946  -1.749  -18.160 1.00 32.45 ? 451 LEU B C     1 
ATOM   6718 O  O     . LEU B 1 472 ? 24.541  -2.046  -19.236 1.00 34.95 ? 451 LEU B O     1 
ATOM   6719 C  CB    . LEU B 1 472 ? 23.615  0.184   -17.283 1.00 27.26 ? 451 LEU B CB    1 
ATOM   6720 C  CG    . LEU B 1 472 ? 22.482  0.804   -16.442 1.00 27.86 ? 451 LEU B CG    1 
ATOM   6721 C  CD1   . LEU B 1 472 ? 22.659  2.313   -16.299 1.00 27.61 ? 451 LEU B CD1   1 
ATOM   6722 C  CD2   . LEU B 1 472 ? 21.111  0.479   -17.024 1.00 31.87 ? 451 LEU B CD2   1 
ATOM   6723 N  N     . GLY B 1 473 ? 26.245  -1.674  -17.837 1.00 41.32 ? 452 GLY B N     1 
ATOM   6724 C  CA    . GLY B 1 473 ? 27.382  -1.713  -18.782 1.00 49.40 ? 452 GLY B CA    1 
ATOM   6725 C  C     . GLY B 1 473 ? 28.391  -0.622  -18.453 1.00 46.02 ? 452 GLY B C     1 
ATOM   6726 O  O     . GLY B 1 473 ? 29.040  -0.066  -19.335 1.00 52.79 ? 452 GLY B O     1 
HETATM 6727 P  PA    . FAD C 2 .   ? -3.888  -11.331 11.066  1.00 14.41 ? 501 FAD A PA    1 
HETATM 6728 O  O1A   . FAD C 2 .   ? -2.507  -10.959 10.581  1.00 16.12 ? 501 FAD A O1A   1 
HETATM 6729 O  O2A   . FAD C 2 .   ? -4.286  -12.768 11.137  1.00 14.33 ? 501 FAD A O2A   1 
HETATM 6730 O  O5B   . FAD C 2 .   ? -4.938  -10.589 10.115  1.00 13.49 ? 501 FAD A O5B   1 
HETATM 6731 C  C5B   . FAD C 2 .   ? -4.638  -9.393  9.380   1.00 14.45 ? 501 FAD A C5B   1 
HETATM 6732 C  C4B   . FAD C 2 .   ? -5.289  -9.482  8.027   1.00 14.78 ? 501 FAD A C4B   1 
HETATM 6733 O  O4B   . FAD C 2 .   ? -5.061  -8.204  7.321   1.00 15.92 ? 501 FAD A O4B   1 
HETATM 6734 C  C3B   . FAD C 2 .   ? -4.692  -10.558 7.125   1.00 13.91 ? 501 FAD A C3B   1 
HETATM 6735 O  O3B   . FAD C 2 .   ? -5.751  -11.411 6.580   1.00 15.52 ? 501 FAD A O3B   1 
HETATM 6736 C  C2B   . FAD C 2 .   ? -3.984  -9.790  6.022   1.00 15.11 ? 501 FAD A C2B   1 
HETATM 6737 O  O2B   . FAD C 2 .   ? -3.994  -10.406 4.753   1.00 15.94 ? 501 FAD A O2B   1 
HETATM 6738 C  C1B   . FAD C 2 .   ? -4.694  -8.487  5.947   1.00 14.20 ? 501 FAD A C1B   1 
HETATM 6739 N  N9A   . FAD C 2 .   ? -3.985  -7.317  5.429   1.00 14.53 ? 501 FAD A N9A   1 
HETATM 6740 C  C8A   . FAD C 2 .   ? -2.755  -6.843  5.803   1.00 15.05 ? 501 FAD A C8A   1 
HETATM 6741 N  N7A   . FAD C 2 .   ? -2.475  -5.641  5.209   1.00 14.43 ? 501 FAD A N7A   1 
HETATM 6742 C  C5A   . FAD C 2 .   ? -3.597  -5.340  4.517   1.00 13.39 ? 501 FAD A C5A   1 
HETATM 6743 C  C6A   . FAD C 2 .   ? -3.990  -4.242  3.788   1.00 14.98 ? 501 FAD A C6A   1 
HETATM 6744 N  N6A   . FAD C 2 .   ? -3.158  -3.204  3.612   1.00 14.61 ? 501 FAD A N6A   1 
HETATM 6745 N  N1A   . FAD C 2 .   ? -5.205  -4.191  3.207   1.00 14.59 ? 501 FAD A N1A   1 
HETATM 6746 C  C2A   . FAD C 2 .   ? -6.106  -5.190  3.415   1.00 14.23 ? 501 FAD A C2A   1 
HETATM 6747 N  N3A   . FAD C 2 .   ? -5.782  -6.291  4.134   1.00 14.39 ? 501 FAD A N3A   1 
HETATM 6748 C  C4A   . FAD C 2 .   ? -4.556  -6.352  4.705   1.00 14.60 ? 501 FAD A C4A   1 
HETATM 6749 N  N1    . FAD C 2 .   ? -1.806  -18.268 17.699  1.00 13.95 ? 501 FAD A N1    1 
HETATM 6750 C  C2    . FAD C 2 .   ? -2.528  -19.190 18.415  1.00 14.49 ? 501 FAD A C2    1 
HETATM 6751 O  O2    . FAD C 2 .   ? -3.521  -18.792 19.107  1.00 13.47 ? 501 FAD A O2    1 
HETATM 6752 N  N3    . FAD C 2 .   ? -2.203  -20.518 18.424  1.00 14.54 ? 501 FAD A N3    1 
HETATM 6753 C  C4    . FAD C 2 .   ? -1.084  -20.931 17.725  1.00 15.23 ? 501 FAD A C4    1 
HETATM 6754 O  O4    . FAD C 2 .   ? -0.787  -22.169 17.616  1.00 15.28 ? 501 FAD A O4    1 
HETATM 6755 C  C4X   . FAD C 2 .   ? -0.329  -19.968 17.002  1.00 14.54 ? 501 FAD A C4X   1 
HETATM 6756 N  N5    . FAD C 2 .   ? 0.808   -20.359 16.294  1.00 15.20 ? 501 FAD A N5    1 
HETATM 6757 C  C5X   . FAD C 2 .   ? 1.266   -19.478 15.305  1.00 14.71 ? 501 FAD A C5X   1 
HETATM 6758 C  C6    . FAD C 2 .   ? 2.138   -19.988 14.306  1.00 15.12 ? 501 FAD A C6    1 
HETATM 6759 C  C7    . FAD C 2 .   ? 2.472   -19.247 13.182  1.00 14.39 ? 501 FAD A C7    1 
HETATM 6760 C  C7M   . FAD C 2 .   ? 3.491   -19.871 12.187  1.00 14.69 ? 501 FAD A C7M   1 
HETATM 6761 C  C8    . FAD C 2 .   ? 1.809   -18.046 12.959  1.00 15.32 ? 501 FAD A C8    1 
HETATM 6762 C  C8M   . FAD C 2 .   ? 2.036   -17.187 11.728  1.00 15.60 ? 501 FAD A C8M   1 
HETATM 6763 C  C9    . FAD C 2 .   ? 0.946   -17.534 13.932  1.00 14.02 ? 501 FAD A C9    1 
HETATM 6764 C  C9A   . FAD C 2 .   ? 0.651   -18.266 15.128  1.00 14.55 ? 501 FAD A C9A   1 
HETATM 6765 N  N10   . FAD C 2 .   ? -0.088  -17.731 16.182  1.00 14.42 ? 501 FAD A N10   1 
HETATM 6766 C  C10   . FAD C 2 .   ? -0.746  -18.652 16.978  1.00 14.43 ? 501 FAD A C10   1 
HETATM 6767 C  "C1'" . FAD C 2 .   ? -0.550  -16.348 16.210  1.00 14.49 ? 501 FAD A "C1'" 1 
HETATM 6768 C  "C2'" . FAD C 2 .   ? -1.916  -16.086 15.501  1.00 14.66 ? 501 FAD A "C2'" 1 
HETATM 6769 O  "O2'" . FAD C 2 .   ? -2.027  -16.747 14.248  1.00 14.32 ? 501 FAD A "O2'" 1 
HETATM 6770 C  "C3'" . FAD C 2 .   ? -2.167  -14.615 15.426  1.00 14.32 ? 501 FAD A "C3'" 1 
HETATM 6771 O  "O3'" . FAD C 2 .   ? -2.129  -13.984 16.738  1.00 16.03 ? 501 FAD A "O3'" 1 
HETATM 6772 C  "C4'" . FAD C 2 .   ? -3.587  -14.202 14.938  1.00 13.32 ? 501 FAD A "C4'" 1 
HETATM 6773 O  "O4'" . FAD C 2 .   ? -4.001  -15.029 13.863  1.00 14.22 ? 501 FAD A "O4'" 1 
HETATM 6774 C  "C5'" . FAD C 2 .   ? -3.553  -12.761 14.498  1.00 13.46 ? 501 FAD A "C5'" 1 
HETATM 6775 O  "O5'" . FAD C 2 .   ? -4.870  -12.320 14.129  1.00 14.57 ? 501 FAD A "O5'" 1 
HETATM 6776 P  P     . FAD C 2 .   ? -5.149  -10.804 13.665  1.00 14.16 ? 501 FAD A P     1 
HETATM 6777 O  O1P   . FAD C 2 .   ? -6.499  -10.796 13.092  1.00 13.34 ? 501 FAD A O1P   1 
HETATM 6778 O  O2P   . FAD C 2 .   ? -4.667  -9.839  14.737  1.00 14.17 ? 501 FAD A O2P   1 
HETATM 6779 O  O3P   . FAD C 2 .   ? -4.020  -10.519 12.512  1.00 13.64 ? 501 FAD A O3P   1 
HETATM 6780 C  C1    . GOL D 3 .   ? -12.818 -17.120 2.524   1.00 27.43 ? 502 GOL A C1    1 
HETATM 6781 O  O1    . GOL D 3 .   ? -11.510 -17.651 2.781   1.00 19.55 ? 502 GOL A O1    1 
HETATM 6782 C  C2    . GOL D 3 .   ? -13.703 -18.048 1.700   1.00 28.91 ? 502 GOL A C2    1 
HETATM 6783 O  O2    . GOL D 3 .   ? -13.770 -19.332 2.303   1.00 30.75 ? 502 GOL A O2    1 
HETATM 6784 C  C3    . GOL D 3 .   ? -15.142 -17.607 1.541   1.00 26.42 ? 502 GOL A C3    1 
HETATM 6785 O  O3    . GOL D 3 .   ? -15.289 -16.202 1.366   1.00 24.76 ? 502 GOL A O3    1 
HETATM 6786 C  CA    . 13D E 4 .   ? 2.436   -20.995 19.057  1.00 38.34 ? 503 13D A CA    1 
HETATM 6787 C  CB    . 13D E 4 .   ? 2.679   -19.554 19.377  1.00 33.05 ? 503 13D A CB    1 
HETATM 6788 C  CC    . 13D E 4 .   ? 1.480   -18.702 19.663  1.00 35.78 ? 503 13D A CC    1 
HETATM 6789 N  ND    . 13D E 4 .   ? 1.608   -17.242 19.346  1.00 24.42 ? 503 13D A ND    1 
HETATM 6790 N  NAA   . 13D E 4 .   ? 3.409   -21.644 18.160  1.00 35.74 ? 503 13D A NAA   1 
HETATM 6791 O  OA    . 4HA F 5 .   ? 5.482   -23.013 21.829  1.00 51.55 ? 504 4HA A OA    1 
HETATM 6792 C  CB    . 4HA F 5 .   ? 5.989   -23.205 22.901  1.00 54.02 ? 504 4HA A CB    1 
HETATM 6793 C  CG    . 4HA F 5 .   ? 6.657   -24.461 23.350  1.00 51.85 ? 504 4HA A CG    1 
HETATM 6794 C  CD    . 4HA F 5 .   ? 7.533   -24.282 24.574  1.00 50.13 ? 504 4HA A CD    1 
HETATM 6795 C  CE    . 4HA F 5 .   ? 8.433   -25.469 24.844  1.00 51.17 ? 504 4HA A CE    1 
HETATM 6796 N  NZ    . 4HA F 5 .   ? 9.554   -25.213 25.757  1.00 50.23 ? 504 4HA A NZ    1 
HETATM 6797 MG MG    . MG  G 6 .   ? 4.569   -35.418 26.908  1.00 31.13 ? 505 MG  A MG    1 
HETATM 6798 P  PA    . FAD H 2 .   ? 17.052  12.403  2.949   1.00 16.74 ? 501 FAD B PA    1 
HETATM 6799 O  O1A   . FAD H 2 .   ? 16.057  11.891  3.972   1.00 16.37 ? 501 FAD B O1A   1 
HETATM 6800 O  O2A   . FAD H 2 .   ? 17.730  13.723  3.182   1.00 17.79 ? 501 FAD B O2A   1 
HETATM 6801 O  O5B   . FAD H 2 .   ? 16.408  12.344  1.510   1.00 17.15 ? 501 FAD B O5B   1 
HETATM 6802 C  C5B   . FAD H 2 .   ? 15.436  11.396  1.105   1.00 16.67 ? 501 FAD B C5B   1 
HETATM 6803 C  C4B   . FAD H 2 .   ? 14.430  12.086  0.229   1.00 16.68 ? 501 FAD B C4B   1 
HETATM 6804 O  O4B   . FAD H 2 .   ? 13.411  11.142  -0.165  1.00 17.31 ? 501 FAD B O4B   1 
HETATM 6805 C  C3B   . FAD H 2 .   ? 13.673  13.269  0.870   1.00 15.69 ? 501 FAD B C3B   1 
HETATM 6806 O  O3B   . FAD H 2 .   ? 13.789  14.457  0.060   1.00 16.91 ? 501 FAD B O3B   1 
HETATM 6807 C  C2B   . FAD H 2 .   ? 12.254  12.785  0.936   1.00 16.89 ? 501 FAD B C2B   1 
HETATM 6808 O  O2B   . FAD H 2 .   ? 11.230  13.748  0.764   1.00 17.46 ? 501 FAD B O2B   1 
HETATM 6809 C  C1B   . FAD H 2 .   ? 12.143  11.797  -0.203  1.00 17.94 ? 501 FAD B C1B   1 
HETATM 6810 N  N9A   . FAD H 2 .   ? 11.151  10.739  -0.113  1.00 16.80 ? 501 FAD B N9A   1 
HETATM 6811 C  C8A   . FAD H 2 .   ? 10.887  9.932   0.932   1.00 17.95 ? 501 FAD B C8A   1 
HETATM 6812 N  N7A   . FAD H 2 .   ? 9.953   8.990   0.567   1.00 18.48 ? 501 FAD B N7A   1 
HETATM 6813 C  C5A   . FAD H 2 .   ? 9.689   9.209   -0.753  1.00 17.08 ? 501 FAD B C5A   1 
HETATM 6814 C  C6A   . FAD H 2 .   ? 8.915   8.561   -1.703  1.00 18.21 ? 501 FAD B C6A   1 
HETATM 6815 N  N6A   . FAD H 2 .   ? 8.148   7.500   -1.340  1.00 18.01 ? 501 FAD B N6A   1 
HETATM 6816 N  N1A   . FAD H 2 .   ? 8.871   9.049   -2.985  1.00 17.38 ? 501 FAD B N1A   1 
HETATM 6817 C  C2A   . FAD H 2 .   ? 9.595   10.116  -3.351  1.00 17.91 ? 501 FAD B C2A   1 
HETATM 6818 N  N3A   . FAD H 2 .   ? 10.422  10.710  -2.473  1.00 16.69 ? 501 FAD B N3A   1 
HETATM 6819 C  C4A   . FAD H 2 .   ? 10.472  10.285  -1.172  1.00 16.93 ? 501 FAD B C4A   1 
HETATM 6820 N  N1    . FAD H 2 .   ? 23.928  15.725  9.218   1.00 17.50 ? 501 FAD B N1    1 
HETATM 6821 C  C2    . FAD H 2 .   ? 25.076  16.447  9.175   1.00 17.29 ? 501 FAD B C2    1 
HETATM 6822 O  O2    . FAD H 2 .   ? 25.994  16.091  8.408   1.00 14.64 ? 501 FAD B O2    1 
HETATM 6823 N  N3    . FAD H 2 .   ? 25.290  17.563  9.960   1.00 16.23 ? 501 FAD B N3    1 
HETATM 6824 C  C4    . FAD H 2 .   ? 24.318  17.924  10.844  1.00 16.91 ? 501 FAD B C4    1 
HETATM 6825 O  O4    . FAD H 2 .   ? 24.470  18.998  11.504  1.00 16.68 ? 501 FAD B O4    1 
HETATM 6826 C  C4X   . FAD H 2 .   ? 23.162  17.129  10.990  1.00 16.13 ? 501 FAD B C4X   1 
HETATM 6827 N  N5    . FAD H 2 .   ? 22.158  17.478  11.814  1.00 17.03 ? 501 FAD B N5    1 
HETATM 6828 C  C5X   . FAD H 2 .   ? 20.912  16.947  11.716  1.00 16.91 ? 501 FAD B C5X   1 
HETATM 6829 C  C6    . FAD H 2 .   ? 19.816  17.539  12.374  1.00 16.60 ? 501 FAD B C6    1 
HETATM 6830 C  C7    . FAD H 2 .   ? 18.493  17.206  12.073  1.00 15.92 ? 501 FAD B C7    1 
HETATM 6831 C  C7M   . FAD H 2 .   ? 17.337  17.796  12.856  1.00 15.73 ? 501 FAD B C7M   1 
HETATM 6832 C  C8    . FAD H 2 .   ? 18.223  16.347  11.004  1.00 15.86 ? 501 FAD B C8    1 
HETATM 6833 C  C8M   . FAD H 2 .   ? 16.876  15.982  10.462  1.00 18.11 ? 501 FAD B C8M   1 
HETATM 6834 C  C9    . FAD H 2 .   ? 19.324  15.796  10.319  1.00 15.31 ? 501 FAD B C9    1 
HETATM 6835 C  C9A   . FAD H 2 .   ? 20.650  16.081  10.646  1.00 16.94 ? 501 FAD B C9A   1 
HETATM 6836 N  N10   . FAD H 2 .   ? 21.751  15.439  10.122  1.00 16.47 ? 501 FAD B N10   1 
HETATM 6837 C  C10   . FAD H 2 .   ? 22.908  16.110  10.063  1.00 15.83 ? 501 FAD B C10   1 
HETATM 6838 C  "C1'" . FAD H 2 .   ? 21.631  14.287  9.188   1.00 14.68 ? 501 FAD B "C1'" 1 
HETATM 6839 C  "C2'" . FAD H 2 .   ? 21.550  14.650  7.719   1.00 15.31 ? 501 FAD B "C2'" 1 
HETATM 6840 O  "O2'" . FAD H 2 .   ? 20.544  15.669  7.445   1.00 15.55 ? 501 FAD B "O2'" 1 
HETATM 6841 C  "C3'" . FAD H 2 .   ? 21.206  13.370  6.882   1.00 16.39 ? 501 FAD B "C3'" 1 
HETATM 6842 O  "O3'" . FAD H 2 .   ? 22.178  12.382  7.180   1.00 15.98 ? 501 FAD B "O3'" 1 
HETATM 6843 C  "C4'" . FAD H 2 .   ? 21.231  13.591  5.386   1.00 15.27 ? 501 FAD B "C4'" 1 
HETATM 6844 O  "O4'" . FAD H 2 .   ? 20.516  14.759  4.947   1.00 16.54 ? 501 FAD B "O4'" 1 
HETATM 6845 C  "C5'" . FAD H 2 .   ? 20.478  12.347  4.801   1.00 16.81 ? 501 FAD B "C5'" 1 
HETATM 6846 O  "O5'" . FAD H 2 .   ? 20.368  12.441  3.409   1.00 15.86 ? 501 FAD B "O5'" 1 
HETATM 6847 P  P     . FAD H 2 .   ? 19.751  11.308  2.428   1.00 16.04 ? 501 FAD B P     1 
HETATM 6848 O  O1P   . FAD H 2 .   ? 19.821  11.860  1.048   1.00 17.79 ? 501 FAD B O1P   1 
HETATM 6849 O  O2P   . FAD H 2 .   ? 20.345  9.978   2.853   1.00 15.71 ? 501 FAD B O2P   1 
HETATM 6850 O  O3P   . FAD H 2 .   ? 18.240  11.296  2.929   1.00 17.03 ? 501 FAD B O3P   1 
HETATM 6851 N  N1    . SPD I 7 .   ? 31.678  16.229  27.107  1.00 49.65 ? 502 SPD B N1    1 
HETATM 6852 C  C2    . SPD I 7 .   ? 30.253  16.167  26.758  1.00 51.84 ? 502 SPD B C2    1 
HETATM 6853 C  C3    . SPD I 7 .   ? 29.964  16.482  25.301  1.00 51.50 ? 502 SPD B C3    1 
HETATM 6854 C  C4    . SPD I 7 .   ? 28.495  16.693  25.028  1.00 51.86 ? 502 SPD B C4    1 
HETATM 6855 C  C5    . SPD I 7 .   ? 28.273  17.658  23.878  1.00 49.10 ? 502 SPD B C5    1 
HETATM 6856 N  N6    . SPD I 7 .   ? 28.394  16.946  22.610  1.00 46.74 ? 502 SPD B N6    1 
HETATM 6857 C  C7    . SPD I 7 .   ? 27.140  16.861  21.859  1.00 48.42 ? 502 SPD B C7    1 
HETATM 6858 C  C8    . SPD I 7 .   ? 27.349  16.741  20.367  1.00 41.97 ? 502 SPD B C8    1 
HETATM 6859 C  C9    . SPD I 7 .   ? 26.308  17.496  19.568  1.00 42.24 ? 502 SPD B C9    1 
HETATM 6860 N  N10   . SPD I 7 .   ? 25.893  16.780  18.361  1.00 40.23 ? 502 SPD B N10   1 
HETATM 6861 C  C1    . GOL J 3 .   ? 39.712  6.328   16.705  1.00 36.18 ? 503 GOL B C1    1 
HETATM 6862 O  O1    . GOL J 3 .   ? 41.081  6.520   16.357  1.00 34.81 ? 503 GOL B O1    1 
HETATM 6863 C  C2    . GOL J 3 .   ? 39.238  5.051   16.076  1.00 30.69 ? 503 GOL B C2    1 
HETATM 6864 O  O2    . GOL J 3 .   ? 39.708  3.969   16.869  1.00 25.64 ? 503 GOL B O2    1 
HETATM 6865 C  C3    . GOL J 3 .   ? 37.741  4.968   15.862  1.00 28.38 ? 503 GOL B C3    1 
HETATM 6866 O  O3    . GOL J 3 .   ? 37.100  4.298   16.931  1.00 26.66 ? 503 GOL B O3    1 
HETATM 6867 C  C1    . GOL K 3 .   ? 36.575  6.139   8.962   1.00 34.36 ? 504 GOL B C1    1 
HETATM 6868 O  O1    . GOL K 3 .   ? 36.961  5.303   10.053  1.00 28.16 ? 504 GOL B O1    1 
HETATM 6869 C  C2    . GOL K 3 .   ? 36.774  7.609   9.247   1.00 38.56 ? 504 GOL B C2    1 
HETATM 6870 O  O2    . GOL K 3 .   ? 38.147  7.925   9.502   1.00 40.41 ? 504 GOL B O2    1 
HETATM 6871 C  C3    . GOL K 3 .   ? 36.284  8.482   8.114   1.00 40.48 ? 504 GOL B C3    1 
HETATM 6872 O  O3    . GOL K 3 .   ? 35.112  9.170   8.506   1.00 45.31 ? 504 GOL B O3    1 
HETATM 6873 MG MG    . MG  L 6 .   ? 33.867  26.430  23.528  1.00 28.49 ? 505 MG  B MG    1 
HETATM 6874 MG MG    . MG  M 6 .   ? 39.683  2.372   11.152  1.00 17.09 ? 506 MG  B MG    1 
HETATM 6875 O  O     . HOH N 8 .   ? 20.005  -4.650  28.607  1.00 24.70 ? 601 HOH A O     1 
HETATM 6876 O  O     . HOH N 8 .   ? 20.087  -1.837  28.551  1.00 28.87 ? 602 HOH A O     1 
HETATM 6877 O  O     . HOH N 8 .   ? -23.851 -13.628 13.851  1.00 36.79 ? 603 HOH A O     1 
HETATM 6878 O  O     . HOH N 8 .   ? 9.846   -2.149  25.221  1.00 19.32 ? 604 HOH A O     1 
HETATM 6879 O  O     . HOH N 8 .   ? 22.484  -26.469 -0.981  1.00 31.25 ? 605 HOH A O     1 
HETATM 6880 O  O     . HOH N 8 .   ? 4.559   -5.322  13.111  1.00 22.08 ? 606 HOH A O     1 
HETATM 6881 O  O     . HOH N 8 .   ? -8.473  9.528   20.082  1.00 35.65 ? 607 HOH A O     1 
HETATM 6882 O  O     . HOH N 8 .   ? -3.417  -32.848 12.768  1.00 18.91 ? 608 HOH A O     1 
HETATM 6883 O  O     . HOH N 8 .   ? 5.918   3.764   35.962  1.00 40.47 ? 609 HOH A O     1 
HETATM 6884 O  O     . HOH N 8 .   ? 2.700   -20.580 23.483  1.00 18.85 ? 610 HOH A O     1 
HETATM 6885 O  O     . HOH N 8 .   ? 2.518   -39.256 19.891  1.00 35.21 ? 611 HOH A O     1 
HETATM 6886 O  O     . HOH N 8 .   ? 18.815  -10.145 36.737  1.00 32.81 ? 612 HOH A O     1 
HETATM 6887 O  O     . HOH N 8 .   ? 1.451   -2.781  39.083  1.00 34.49 ? 613 HOH A O     1 
HETATM 6888 O  O     . HOH N 8 .   ? -5.698  -26.788 14.729  1.00 15.90 ? 614 HOH A O     1 
HETATM 6889 O  O     . HOH N 8 .   ? 21.079  -18.909 5.125   1.00 30.27 ? 615 HOH A O     1 
HETATM 6890 O  O     . HOH N 8 .   ? 2.197   5.764   9.116   1.00 23.84 ? 616 HOH A O     1 
HETATM 6891 O  O     . HOH N 8 .   ? 14.916  -22.382 15.910  1.00 21.67 ? 617 HOH A O     1 
HETATM 6892 O  O     . HOH N 8 .   ? -9.920  -13.306 -4.633  1.00 35.61 ? 618 HOH A O     1 
HETATM 6893 O  O     . HOH N 8 .   ? -20.517 -26.714 19.415  1.00 25.50 ? 619 HOH A O     1 
HETATM 6894 O  O     . HOH N 8 .   ? -5.071  -39.001 4.920   1.00 28.67 ? 620 HOH A O     1 
HETATM 6895 O  O     . HOH N 8 .   ? -23.119 -16.503 4.739   1.00 39.01 ? 621 HOH A O     1 
HETATM 6896 O  O     . HOH N 8 .   ? -11.424 9.649   18.067  1.00 31.84 ? 622 HOH A O     1 
HETATM 6897 O  O     . HOH N 8 .   ? -2.181  -6.026  15.094  1.00 20.49 ? 623 HOH A O     1 
HETATM 6898 O  O     . HOH N 8 .   ? -6.142  -14.269 12.193  1.00 12.84 ? 624 HOH A O     1 
HETATM 6899 O  O     . HOH N 8 .   ? -7.387  -44.021 10.093  1.00 19.86 ? 625 HOH A O     1 
HETATM 6900 O  O     . HOH N 8 .   ? -2.382  6.364   25.817  1.00 31.00 ? 626 HOH A O     1 
HETATM 6901 O  O     . HOH N 8 .   ? -4.930  -14.227 30.426  1.00 25.67 ? 627 HOH A O     1 
HETATM 6902 O  O     . HOH N 8 .   ? 7.775   -24.070 1.243   1.00 27.21 ? 628 HOH A O     1 
HETATM 6903 O  O     . HOH N 8 .   ? 11.354  4.772   29.919  1.00 33.35 ? 629 HOH A O     1 
HETATM 6904 O  O     . HOH N 8 .   ? -1.374  -3.159  26.588  1.00 30.25 ? 630 HOH A O     1 
HETATM 6905 O  O     . HOH N 8 .   ? -4.919  -36.436 19.268  1.00 25.92 ? 631 HOH A O     1 
HETATM 6906 O  O     . HOH N 8 .   ? 13.605  3.373   30.186  1.00 25.92 ? 632 HOH A O     1 
HETATM 6907 O  O     . HOH N 8 .   ? -27.302 -1.827  18.404  1.00 19.37 ? 633 HOH A O     1 
HETATM 6908 O  O     . HOH N 8 .   ? -25.746 2.237   6.350   1.00 40.46 ? 634 HOH A O     1 
HETATM 6909 O  O     . HOH N 8 .   ? -2.899  6.014   18.563  1.00 23.79 ? 635 HOH A O     1 
HETATM 6910 O  O     . HOH N 8 .   ? -15.966 5.223   21.396  1.00 23.66 ? 636 HOH A O     1 
HETATM 6911 O  O     . HOH N 8 .   ? -0.432  -24.501 32.794  1.00 33.35 ? 637 HOH A O     1 
HETATM 6912 O  O     . HOH N 8 .   ? -10.687 -23.258 3.228   1.00 30.79 ? 638 HOH A O     1 
HETATM 6913 O  O     . HOH N 8 .   ? 0.527   -5.921  23.081  1.00 33.63 ? 639 HOH A O     1 
HETATM 6914 O  O     . HOH N 8 .   ? 7.782   -38.578 -1.434  1.00 30.36 ? 640 HOH A O     1 
HETATM 6915 O  O     . HOH N 8 .   ? -3.596  -21.971 27.359  1.00 27.18 ? 641 HOH A O     1 
HETATM 6916 O  O     . HOH N 8 .   ? -14.563 -23.139 4.525   1.00 30.11 ? 642 HOH A O     1 
HETATM 6917 O  O     . HOH N 8 .   ? -1.484  -4.985  24.620  1.00 26.63 ? 643 HOH A O     1 
HETATM 6918 O  O     . HOH N 8 .   ? 5.471   -17.117 2.169   1.00 32.30 ? 644 HOH A O     1 
HETATM 6919 O  O     . HOH N 8 .   ? -8.798  2.557   22.508  1.00 27.81 ? 645 HOH A O     1 
HETATM 6920 O  O     . HOH N 8 .   ? -0.865  -31.390 16.665  1.00 18.85 ? 646 HOH A O     1 
HETATM 6921 O  O     . HOH N 8 .   ? -21.254 -19.633 10.135  1.00 27.64 ? 647 HOH A O     1 
HETATM 6922 O  O     . HOH N 8 .   ? 24.876  -34.510 18.920  1.00 34.78 ? 648 HOH A O     1 
HETATM 6923 O  O     . HOH N 8 .   ? -11.875 0.973   24.288  1.00 26.50 ? 649 HOH A O     1 
HETATM 6924 O  O     . HOH N 8 .   ? -22.310 -6.303  18.728  1.00 22.81 ? 650 HOH A O     1 
HETATM 6925 O  O     . HOH N 8 .   ? -5.185  -44.538 8.192   1.00 22.29 ? 651 HOH A O     1 
HETATM 6926 O  O     . HOH N 8 .   ? -12.074 -34.765 18.603  1.00 37.86 ? 652 HOH A O     1 
HETATM 6927 O  O     . HOH N 8 .   ? 3.366   -16.697 21.431  1.00 20.29 ? 653 HOH A O     1 
HETATM 6928 O  O     . HOH N 8 .   ? -24.213 -5.166  8.283   1.00 31.75 ? 654 HOH A O     1 
HETATM 6929 O  O     . HOH N 8 .   ? -15.789 -26.677 20.181  1.00 21.10 ? 655 HOH A O     1 
HETATM 6930 O  O     . HOH N 8 .   ? 2.937   -5.635  2.021   1.00 33.01 ? 656 HOH A O     1 
HETATM 6931 O  O     . HOH N 8 .   ? 8.122   -24.016 31.408  1.00 36.69 ? 657 HOH A O     1 
HETATM 6932 O  O     . HOH N 8 .   ? -9.955  -28.534 6.430   1.00 23.35 ? 658 HOH A O     1 
HETATM 6933 O  O     . HOH N 8 .   ? -17.929 -5.857  21.028  1.00 25.54 ? 659 HOH A O     1 
HETATM 6934 O  O     . HOH N 8 .   ? 17.432  -19.279 16.510  1.00 29.82 ? 660 HOH A O     1 
HETATM 6935 O  O     . HOH N 8 .   ? -20.317 0.102   22.445  1.00 22.89 ? 661 HOH A O     1 
HETATM 6936 O  O     . HOH N 8 .   ? 6.054   -34.204 27.541  1.00 29.95 ? 662 HOH A O     1 
HETATM 6937 O  O     . HOH N 8 .   ? 12.977  -12.438 15.418  1.00 26.28 ? 663 HOH A O     1 
HETATM 6938 O  O     . HOH N 8 .   ? -1.440  -11.428 8.141   1.00 14.09 ? 664 HOH A O     1 
HETATM 6939 O  O     . HOH N 8 .   ? 3.753   -41.579 28.344  1.00 31.85 ? 665 HOH A O     1 
HETATM 6940 O  O     . HOH N 8 .   ? 12.899  -32.700 -3.827  1.00 37.75 ? 666 HOH A O     1 
HETATM 6941 O  O     . HOH N 8 .   ? 20.495  -30.549 10.276  1.00 32.94 ? 667 HOH A O     1 
HETATM 6942 O  O     . HOH N 8 .   ? 3.387   -46.104 15.032  1.00 39.67 ? 668 HOH A O     1 
HETATM 6943 O  O     . HOH N 8 .   ? -7.743  -31.731 25.743  1.00 24.83 ? 669 HOH A O     1 
HETATM 6944 O  O     . HOH N 8 .   ? 11.616  -17.421 2.571   1.00 17.49 ? 670 HOH A O     1 
HETATM 6945 O  O     . HOH N 8 .   ? -20.128 -20.452 22.616  1.00 24.82 ? 671 HOH A O     1 
HETATM 6946 O  O     . HOH N 8 .   ? 20.371  -28.063 3.851   1.00 22.95 ? 672 HOH A O     1 
HETATM 6947 O  O     . HOH N 8 .   ? 4.826   -34.561 20.546  1.00 17.48 ? 673 HOH A O     1 
HETATM 6948 O  O     . HOH N 8 .   ? -3.804  -33.007 10.121  1.00 19.42 ? 674 HOH A O     1 
HETATM 6949 O  O     . HOH N 8 .   ? -6.034  -19.075 -0.877  1.00 37.24 ? 675 HOH A O     1 
HETATM 6950 O  O     . HOH N 8 .   ? -15.366 -13.817 16.972  1.00 28.26 ? 676 HOH A O     1 
HETATM 6951 O  O     . HOH N 8 .   ? 8.066   -15.108 10.269  1.00 21.90 ? 677 HOH A O     1 
HETATM 6952 O  O     . HOH N 8 .   ? -3.894  -9.536  -3.451  1.00 35.21 ? 678 HOH A O     1 
HETATM 6953 O  O     . HOH N 8 .   ? -4.698  -17.866 30.677  1.00 26.06 ? 679 HOH A O     1 
HETATM 6954 O  O     . HOH N 8 .   ? 20.528  -15.471 11.081  1.00 20.51 ? 680 HOH A O     1 
HETATM 6955 O  O     . HOH N 8 .   ? 18.446  -25.986 -2.961  1.00 24.31 ? 681 HOH A O     1 
HETATM 6956 O  O     . HOH N 8 .   ? -12.091 -26.589 11.103  1.00 18.92 ? 682 HOH A O     1 
HETATM 6957 O  O     . HOH N 8 .   ? 1.147   -17.037 0.381   1.00 32.73 ? 683 HOH A O     1 
HETATM 6958 O  O     . HOH N 8 .   ? -7.403  -36.238 8.702   1.00 20.00 ? 684 HOH A O     1 
HETATM 6959 O  O     . HOH N 8 .   ? 6.117   -10.721 21.078  1.00 20.10 ? 685 HOH A O     1 
HETATM 6960 O  O     . HOH N 8 .   ? -5.327  9.802   9.498   1.00 23.01 ? 686 HOH A O     1 
HETATM 6961 O  O     . HOH N 8 .   ? -18.484 -13.395 4.124   1.00 33.56 ? 687 HOH A O     1 
HETATM 6962 O  O     . HOH N 8 .   ? 12.222  -10.100 14.305  1.00 29.75 ? 688 HOH A O     1 
HETATM 6963 O  O     . HOH N 8 .   ? 10.883  -8.036  11.706  1.00 22.68 ? 689 HOH A O     1 
HETATM 6964 O  O     . HOH N 8 .   ? -2.509  -21.327 21.852  1.00 14.80 ? 690 HOH A O     1 
HETATM 6965 O  O     . HOH N 8 .   ? -7.791  -4.921  22.579  1.00 24.32 ? 691 HOH A O     1 
HETATM 6966 O  O     . HOH N 8 .   ? 23.115  -30.503 19.094  1.00 27.66 ? 692 HOH A O     1 
HETATM 6967 O  O     . HOH N 8 .   ? 6.192   -16.124 41.151  1.00 33.63 ? 693 HOH A O     1 
HETATM 6968 O  O     . HOH N 8 .   ? 6.346   9.581   25.261  1.00 25.12 ? 694 HOH A O     1 
HETATM 6969 O  O     . HOH N 8 .   ? 19.450  -11.804 18.648  1.00 23.94 ? 695 HOH A O     1 
HETATM 6970 O  O     . HOH N 8 .   ? -17.065 -15.433 3.312   1.00 24.37 ? 696 HOH A O     1 
HETATM 6971 O  O     . HOH N 8 .   ? -18.834 10.363  18.142  1.00 39.95 ? 697 HOH A O     1 
HETATM 6972 O  O     . HOH N 8 .   ? -22.281 -4.053  3.531   1.00 43.29 ? 698 HOH A O     1 
HETATM 6973 O  O     . HOH N 8 .   ? -8.863  1.799   18.747  1.00 21.24 ? 699 HOH A O     1 
HETATM 6974 O  O     . HOH N 8 .   ? -4.316  2.135   28.504  1.00 29.74 ? 700 HOH A O     1 
HETATM 6975 O  O     . HOH N 8 .   ? -9.596  -31.748 22.331  1.00 22.07 ? 701 HOH A O     1 
HETATM 6976 O  O     . HOH N 8 .   ? 0.254   -21.698 20.790  1.00 17.28 ? 702 HOH A O     1 
HETATM 6977 O  O     . HOH N 8 .   ? -2.915  -21.128 1.298   1.00 29.75 ? 703 HOH A O     1 
HETATM 6978 O  O     . HOH N 8 .   ? 1.564   -30.136 15.614  1.00 21.10 ? 704 HOH A O     1 
HETATM 6979 O  O     . HOH N 8 .   ? -12.419 -28.612 23.843  1.00 27.32 ? 705 HOH A O     1 
HETATM 6980 O  O     . HOH N 8 .   ? -12.669 11.064  3.934   1.00 33.20 ? 706 HOH A O     1 
HETATM 6981 O  O     . HOH N 8 .   ? 13.262  4.995   24.207  1.00 28.83 ? 707 HOH A O     1 
HETATM 6982 O  O     . HOH N 8 .   ? 3.754   -33.781 23.063  1.00 34.59 ? 708 HOH A O     1 
HETATM 6983 O  O     . HOH N 8 .   ? 4.188   -31.828 24.466  1.00 30.14 ? 709 HOH A O     1 
HETATM 6984 O  O     . HOH N 8 .   ? -1.303  -34.088 16.548  1.00 23.29 ? 710 HOH A O     1 
HETATM 6985 O  O     . HOH N 8 .   ? -7.690  -9.054  11.316  1.00 14.82 ? 711 HOH A O     1 
HETATM 6986 O  O     . HOH N 8 .   ? 2.963   -10.304 19.337  1.00 22.53 ? 712 HOH A O     1 
HETATM 6987 O  O     . HOH N 8 .   ? 5.289   -35.182 24.951  1.00 29.06 ? 713 HOH A O     1 
HETATM 6988 O  O     . HOH N 8 .   ? 8.222   -11.275 17.950  1.00 20.74 ? 714 HOH A O     1 
HETATM 6989 O  O     . HOH N 8 .   ? -2.929  2.945   23.752  1.00 24.15 ? 715 HOH A O     1 
HETATM 6990 O  O     . HOH N 8 .   ? -5.642  -18.710 20.879  1.00 14.49 ? 716 HOH A O     1 
HETATM 6991 O  O     . HOH N 8 .   ? -16.020 -15.553 21.430  1.00 27.43 ? 717 HOH A O     1 
HETATM 6992 O  O     . HOH N 8 .   ? -3.348  -37.378 17.058  1.00 32.30 ? 718 HOH A O     1 
HETATM 6993 O  O     . HOH N 8 .   ? 18.038  -17.392 27.987  1.00 27.04 ? 719 HOH A O     1 
HETATM 6994 O  O     . HOH N 8 .   ? 1.575   -9.055  20.945  1.00 32.66 ? 720 HOH A O     1 
HETATM 6995 O  O     . HOH N 8 .   ? -26.709 3.081   10.644  1.00 19.81 ? 721 HOH A O     1 
HETATM 6996 O  O     . HOH N 8 .   ? -5.831  7.326   8.350   1.00 22.09 ? 722 HOH A O     1 
HETATM 6997 O  O     . HOH N 8 .   ? 1.090   8.285   8.447   1.00 20.32 ? 723 HOH A O     1 
HETATM 6998 O  O     . HOH N 8 .   ? 0.441   -32.072 -1.458  1.00 36.77 ? 724 HOH A O     1 
HETATM 6999 O  O     . HOH N 8 .   ? -14.823 -24.948 22.176  1.00 22.27 ? 725 HOH A O     1 
HETATM 7000 O  O     . HOH N 8 .   ? -6.084  -38.414 7.593   1.00 18.72 ? 726 HOH A O     1 
HETATM 7001 O  O     . HOH N 8 .   ? -16.977 -17.836 4.633   1.00 19.45 ? 727 HOH A O     1 
HETATM 7002 O  O     . HOH N 8 .   ? -3.608  -12.502 33.454  1.00 32.83 ? 728 HOH A O     1 
HETATM 7003 O  O     . HOH N 8 .   ? 3.687   -42.003 21.342  1.00 37.21 ? 729 HOH A O     1 
HETATM 7004 O  O     . HOH N 8 .   ? 22.564  -35.094 24.702  1.00 29.67 ? 730 HOH A O     1 
HETATM 7005 O  O     . HOH N 8 .   ? -8.388  15.812  7.422   1.00 34.31 ? 731 HOH A O     1 
HETATM 7006 O  O     . HOH N 8 .   ? -3.303  -22.139 10.550  1.00 15.69 ? 732 HOH A O     1 
HETATM 7007 O  O     . HOH N 8 .   ? 11.786  -15.849 8.849   1.00 24.36 ? 733 HOH A O     1 
HETATM 7008 O  O     . HOH N 8 .   ? -24.047 2.094   17.189  1.00 20.56 ? 734 HOH A O     1 
HETATM 7009 O  O     . HOH N 8 .   ? 5.464   -6.376  2.166   1.00 29.94 ? 735 HOH A O     1 
HETATM 7010 O  O     . HOH N 8 .   ? 4.178   -27.092 24.761  1.00 23.09 ? 736 HOH A O     1 
HETATM 7011 O  O     . HOH N 8 .   ? 5.700   -37.048 27.318  1.00 25.48 ? 737 HOH A O     1 
HETATM 7012 O  O     . HOH N 8 .   ? 16.195  -12.673 15.177  1.00 21.73 ? 738 HOH A O     1 
HETATM 7013 O  O     . HOH N 8 .   ? -9.338  -22.336 24.326  1.00 28.14 ? 739 HOH A O     1 
HETATM 7014 O  O     . HOH N 8 .   ? -2.985  -32.106 25.045  1.00 18.00 ? 740 HOH A O     1 
HETATM 7015 O  O     . HOH N 8 .   ? -3.716  -2.462  12.815  1.00 20.02 ? 741 HOH A O     1 
HETATM 7016 O  O     . HOH N 8 .   ? 21.093  -29.619 20.579  1.00 27.84 ? 742 HOH A O     1 
HETATM 7017 O  O     . HOH N 8 .   ? -19.594 -11.378 2.800   1.00 16.52 ? 743 HOH A O     1 
HETATM 7018 O  O     . HOH N 8 .   ? 15.773  -5.691  19.396  1.00 31.35 ? 744 HOH A O     1 
HETATM 7019 O  O     . HOH N 8 .   ? 18.665  -22.133 10.266  1.00 22.94 ? 745 HOH A O     1 
HETATM 7020 O  O     . HOH N 8 .   ? -6.203  -13.744 5.075   1.00 13.67 ? 746 HOH A O     1 
HETATM 7021 O  O     . HOH N 8 .   ? 7.517   10.301  17.857  1.00 28.63 ? 747 HOH A O     1 
HETATM 7022 O  O     . HOH N 8 .   ? 15.426  -14.662 5.197   1.00 19.51 ? 748 HOH A O     1 
HETATM 7023 O  O     . HOH N 8 .   ? -18.040 -10.811 16.822  1.00 20.90 ? 749 HOH A O     1 
HETATM 7024 O  O     . HOH N 8 .   ? -24.538 -12.631 11.828  1.00 36.16 ? 750 HOH A O     1 
HETATM 7025 O  O     . HOH N 8 .   ? 15.135  -21.747 18.719  1.00 39.22 ? 751 HOH A O     1 
HETATM 7026 O  O     . HOH N 8 .   ? 1.566   -23.257 15.552  1.00 13.01 ? 752 HOH A O     1 
HETATM 7027 O  O     . HOH N 8 .   ? -0.980  -0.457  2.328   1.00 20.01 ? 753 HOH A O     1 
HETATM 7028 O  O     . HOH N 8 .   ? -10.978 -16.126 -3.400  1.00 34.85 ? 754 HOH A O     1 
HETATM 7029 O  O     . HOH N 8 .   ? 2.802   13.390  11.887  1.00 24.39 ? 755 HOH A O     1 
HETATM 7030 O  O     . HOH N 8 .   ? 0.910   -12.667 2.113   1.00 16.06 ? 756 HOH A O     1 
HETATM 7031 O  O     . HOH N 8 .   ? 6.157   -13.606 17.737  1.00 20.50 ? 757 HOH A O     1 
HETATM 7032 O  O     . HOH N 8 .   ? 3.778   -35.611 28.721  1.00 31.88 ? 758 HOH A O     1 
HETATM 7033 O  O     . HOH N 8 .   ? -8.232  13.992  4.551   1.00 30.80 ? 759 HOH A O     1 
HETATM 7034 O  O     . HOH N 8 .   ? 4.458   -12.744 19.797  1.00 23.15 ? 760 HOH A O     1 
HETATM 7035 O  O     . HOH N 8 .   ? -18.722 -16.945 20.545  1.00 31.99 ? 761 HOH A O     1 
HETATM 7036 O  O     . HOH N 8 .   ? -14.534 -29.468 13.325  1.00 27.76 ? 762 HOH A O     1 
HETATM 7037 O  O     . HOH N 8 .   ? 14.210  -27.770 20.311  1.00 34.98 ? 763 HOH A O     1 
HETATM 7038 O  O     . HOH N 8 .   ? -1.952  -29.583 10.523  1.00 14.77 ? 764 HOH A O     1 
HETATM 7039 O  O     . HOH N 8 .   ? 0.847   11.280  20.767  1.00 32.27 ? 765 HOH A O     1 
HETATM 7040 O  O     . HOH N 8 .   ? -1.123  12.267  3.892   1.00 34.37 ? 766 HOH A O     1 
HETATM 7041 O  O     . HOH N 8 .   ? -6.254  -26.607 0.390   1.00 35.43 ? 767 HOH A O     1 
HETATM 7042 O  O     . HOH N 8 .   ? -0.184  -30.970 11.912  1.00 19.22 ? 768 HOH A O     1 
HETATM 7043 O  O     . HOH N 8 .   ? 19.945  -21.416 -1.814  1.00 42.62 ? 769 HOH A O     1 
HETATM 7044 O  O     . HOH N 8 .   ? 16.335  -27.028 -4.211  1.00 23.33 ? 770 HOH A O     1 
HETATM 7045 O  O     . HOH N 8 .   ? 21.146  -29.579 2.132   1.00 24.09 ? 771 HOH A O     1 
HETATM 7046 O  O     . HOH N 8 .   ? 7.261   -19.507 2.465   1.00 22.04 ? 772 HOH A O     1 
HETATM 7047 O  O     . HOH N 8 .   ? 2.727   5.723   5.642   1.00 28.41 ? 773 HOH A O     1 
HETATM 7048 O  O     . HOH N 8 .   ? 6.810   -2.653  38.259  1.00 31.53 ? 774 HOH A O     1 
HETATM 7049 O  O     . HOH N 8 .   ? -8.072  11.493  17.872  1.00 37.66 ? 775 HOH A O     1 
HETATM 7050 O  O     . HOH N 8 .   ? -1.591  5.963   30.389  1.00 30.34 ? 776 HOH A O     1 
HETATM 7051 O  O     . HOH N 8 .   ? -21.248 -22.362 11.898  1.00 37.01 ? 777 HOH A O     1 
HETATM 7052 O  O     . HOH N 8 .   ? -3.407  -7.713  13.236  1.00 21.37 ? 778 HOH A O     1 
HETATM 7053 O  O     . HOH N 8 .   ? 0.080   -13.378 25.861  1.00 15.03 ? 779 HOH A O     1 
HETATM 7054 O  O     . HOH N 8 .   ? 8.802   -2.274  12.830  1.00 22.57 ? 780 HOH A O     1 
HETATM 7055 O  O     . HOH N 8 .   ? -3.768  11.069  11.618  1.00 28.92 ? 781 HOH A O     1 
HETATM 7056 O  O     . HOH N 8 .   ? 9.404   3.470   36.159  1.00 36.59 ? 782 HOH A O     1 
HETATM 7057 O  O     . HOH N 8 .   ? -14.621 -30.898 20.728  1.00 31.30 ? 783 HOH A O     1 
HETATM 7058 O  O     . HOH N 8 .   ? -5.218  -21.768 2.477   1.00 26.23 ? 784 HOH A O     1 
HETATM 7059 O  O     . HOH N 8 .   ? 3.919   -29.666 28.783  1.00 30.97 ? 785 HOH A O     1 
HETATM 7060 O  O     . HOH N 8 .   ? -7.504  7.198   1.155   1.00 33.36 ? 786 HOH A O     1 
HETATM 7061 O  O     . HOH N 8 .   ? 13.114  -14.969 6.604   1.00 21.96 ? 787 HOH A O     1 
HETATM 7062 O  O     . HOH N 8 .   ? -13.453 -8.479  -4.150  1.00 31.62 ? 788 HOH A O     1 
HETATM 7063 O  O     . HOH N 8 .   ? 12.840  -22.606 19.990  1.00 23.90 ? 789 HOH A O     1 
HETATM 7064 O  O     . HOH N 8 .   ? -26.602 -12.167 2.851   1.00 34.38 ? 790 HOH A O     1 
HETATM 7065 O  O     . HOH N 8 .   ? -0.267  -2.287  4.274   1.00 18.40 ? 791 HOH A O     1 
HETATM 7066 O  O     . HOH N 8 .   ? 10.078  -38.154 20.831  1.00 21.69 ? 792 HOH A O     1 
HETATM 7067 O  O     . HOH N 8 .   ? 0.844   8.229   5.777   1.00 29.37 ? 793 HOH A O     1 
HETATM 7068 O  O     . HOH N 8 .   ? 13.399  -3.701  39.344  1.00 29.10 ? 794 HOH A O     1 
HETATM 7069 O  O     . HOH N 8 .   ? 2.537   9.319   25.761  1.00 26.32 ? 795 HOH A O     1 
HETATM 7070 O  O     . HOH N 8 .   ? -5.409  -34.257 -0.045  1.00 33.31 ? 796 HOH A O     1 
HETATM 7071 O  O     . HOH N 8 .   ? -14.325 -0.690  23.771  1.00 34.60 ? 797 HOH A O     1 
HETATM 7072 O  O     . HOH N 8 .   ? 20.588  -23.262 18.269  1.00 39.56 ? 798 HOH A O     1 
HETATM 7073 O  O     . HOH N 8 .   ? 6.845   -42.349 5.120   1.00 22.48 ? 799 HOH A O     1 
HETATM 7074 O  O     . HOH N 8 .   ? -4.980  -12.064 -4.419  1.00 38.74 ? 800 HOH A O     1 
HETATM 7075 O  O     . HOH N 8 .   ? -2.117  -1.034  14.383  1.00 29.05 ? 801 HOH A O     1 
HETATM 7076 O  O     . HOH N 8 .   ? -15.605 -23.321 6.912   1.00 26.62 ? 802 HOH A O     1 
HETATM 7077 O  O     . HOH N 8 .   ? -4.956  8.626   1.817   1.00 26.72 ? 803 HOH A O     1 
HETATM 7078 O  O     . HOH N 8 .   ? 7.886   -5.670  -0.167  1.00 20.73 ? 804 HOH A O     1 
HETATM 7079 O  O     . HOH N 8 .   ? 13.232  -0.843  17.758  1.00 30.79 ? 805 HOH A O     1 
HETATM 7080 O  O     . HOH N 8 .   ? 12.036  2.090   37.035  1.00 28.56 ? 806 HOH A O     1 
HETATM 7081 O  O     . HOH N 8 .   ? 11.461  -20.698 0.327   1.00 34.34 ? 807 HOH A O     1 
HETATM 7082 O  O     . HOH N 8 .   ? -8.778  -23.879 4.802   1.00 34.22 ? 808 HOH A O     1 
HETATM 7083 O  O     . HOH N 8 .   ? 6.028   -26.208 1.310   1.00 22.54 ? 809 HOH A O     1 
HETATM 7084 O  O     . HOH N 8 .   ? -0.665  -39.005 23.523  1.00 26.88 ? 810 HOH A O     1 
HETATM 7085 O  O     . HOH N 8 .   ? -1.128  -15.153 0.843   1.00 26.25 ? 811 HOH A O     1 
HETATM 7086 O  O     . HOH N 8 .   ? 17.174  -24.769 19.140  1.00 36.69 ? 812 HOH A O     1 
HETATM 7087 O  O     . HOH N 8 .   ? 12.186  -22.829 -2.191  1.00 25.62 ? 813 HOH A O     1 
HETATM 7088 O  O     . HOH N 8 .   ? -3.826  -5.468  34.638  1.00 22.02 ? 814 HOH A O     1 
HETATM 7089 O  O     . HOH N 8 .   ? -7.381  -20.506 1.010   1.00 28.54 ? 815 HOH A O     1 
HETATM 7090 O  O     . HOH N 8 .   ? -15.778 -25.842 7.996   1.00 28.46 ? 816 HOH A O     1 
HETATM 7091 O  O     . HOH N 8 .   ? 14.472  -45.321 13.248  1.00 32.28 ? 817 HOH A O     1 
HETATM 7092 O  O     . HOH N 8 .   ? -23.497 -4.561  6.028   1.00 33.02 ? 818 HOH A O     1 
HETATM 7093 O  O     . HOH N 8 .   ? -16.384 -13.543 19.730  1.00 27.71 ? 819 HOH A O     1 
HETATM 7094 O  O     . HOH N 8 .   ? -1.447  -34.091 -1.308  1.00 26.38 ? 820 HOH A O     1 
HETATM 7095 O  O     . HOH N 8 .   ? 2.701   5.210   3.020   1.00 39.60 ? 821 HOH A O     1 
HETATM 7096 O  O     . HOH N 8 .   ? -14.984 13.665  13.248  1.00 41.50 ? 822 HOH A O     1 
HETATM 7097 O  O     . HOH N 8 .   ? -8.685  -28.037 29.805  1.00 31.93 ? 823 HOH A O     1 
HETATM 7098 O  O     . HOH N 8 .   ? -9.464  -35.609 6.987   1.00 30.50 ? 824 HOH A O     1 
HETATM 7099 O  O     . HOH N 8 .   ? -2.244  -18.576 1.388   1.00 33.34 ? 825 HOH A O     1 
HETATM 7100 O  O     . HOH N 8 .   ? -6.789  -22.474 33.219  1.00 39.18 ? 826 HOH A O     1 
HETATM 7101 O  O     . HOH N 8 .   ? -10.440 -29.363 25.739  1.00 36.33 ? 827 HOH A O     1 
HETATM 7102 O  O     . HOH N 8 .   ? 1.782   -32.311 28.398  1.00 25.98 ? 828 HOH A O     1 
HETATM 7103 O  O     . HOH N 8 .   ? 4.945   3.292   10.491  1.00 33.66 ? 829 HOH A O     1 
HETATM 7104 O  O     . HOH N 8 .   ? 3.386   -33.596 26.520  1.00 27.00 ? 830 HOH A O     1 
HETATM 7105 O  O     . HOH N 8 .   ? -2.061  -47.292 10.550  1.00 36.53 ? 831 HOH A O     1 
HETATM 7106 O  O     . HOH N 8 .   ? 22.385  -24.651 14.847  1.00 44.96 ? 832 HOH A O     1 
HETATM 7107 O  O     . HOH N 8 .   ? -3.568  -14.047 -1.759  1.00 25.80 ? 833 HOH A O     1 
HETATM 7108 O  O     . HOH N 8 .   ? 2.482   12.319  18.898  1.00 17.00 ? 834 HOH A O     1 
HETATM 7109 O  O     . HOH N 8 .   ? -8.756  -37.118 11.280  1.00 16.41 ? 835 HOH A O     1 
HETATM 7110 O  O     . HOH N 8 .   ? -4.831  2.320   25.707  1.00 30.76 ? 836 HOH A O     1 
HETATM 7111 O  O     . HOH N 8 .   ? -16.018 -16.158 26.040  1.00 36.59 ? 837 HOH A O     1 
HETATM 7112 O  O     . HOH N 8 .   ? -9.470  -8.281  28.580  1.00 42.55 ? 838 HOH A O     1 
HETATM 7113 O  O     . HOH N 8 .   ? 26.034  -37.670 25.898  1.00 35.87 ? 839 HOH A O     1 
HETATM 7114 O  O     . HOH N 8 .   ? 3.637   -7.981  25.308  1.00 19.03 ? 840 HOH A O     1 
HETATM 7115 O  O     . HOH N 8 .   ? 6.829   -42.490 1.755   1.00 41.76 ? 841 HOH A O     1 
HETATM 7116 O  O     . HOH N 8 .   ? 15.033  -14.968 0.661   1.00 30.13 ? 842 HOH A O     1 
HETATM 7117 O  O     . HOH N 8 .   ? 6.219   -44.108 7.660   1.00 29.08 ? 843 HOH A O     1 
HETATM 7118 O  O     . HOH N 8 .   ? -16.321 1.137   24.057  1.00 30.69 ? 844 HOH A O     1 
HETATM 7119 O  O     . HOH N 8 .   ? -14.674 -5.495  24.455  1.00 42.23 ? 845 HOH A O     1 
HETATM 7120 O  O     . HOH N 8 .   ? -18.084 -21.632 6.559   1.00 28.43 ? 846 HOH A O     1 
HETATM 7121 O  O     . HOH N 8 .   ? -10.752 -39.913 12.353  1.00 28.73 ? 847 HOH A O     1 
HETATM 7122 O  O     . HOH N 8 .   ? 5.558   -31.103 26.662  1.00 40.88 ? 848 HOH A O     1 
HETATM 7123 O  O     . HOH N 8 .   ? -17.498 7.535   21.788  1.00 36.60 ? 849 HOH A O     1 
HETATM 7124 O  O     . HOH N 8 .   ? 2.657   -7.267  22.871  1.00 28.26 ? 850 HOH A O     1 
HETATM 7125 O  O     . HOH N 8 .   ? -8.896  -26.379 4.188   1.00 44.04 ? 851 HOH A O     1 
HETATM 7126 O  O     . HOH N 8 .   ? -4.140  -37.847 21.418  1.00 39.83 ? 852 HOH A O     1 
HETATM 7127 O  O     . HOH N 8 .   ? 11.881  -15.798 0.310   1.00 37.39 ? 853 HOH A O     1 
HETATM 7128 O  O     . HOH N 8 .   ? 21.914  -17.129 25.454  1.00 47.34 ? 854 HOH A O     1 
HETATM 7129 O  O     . HOH N 8 .   ? 7.758   -29.994 27.194  1.00 36.65 ? 855 HOH A O     1 
HETATM 7130 O  O     . HOH N 8 .   ? -27.702 0.351   7.474   1.00 33.43 ? 856 HOH A O     1 
HETATM 7131 O  O     . HOH N 8 .   ? 2.291   -7.814  -2.446  1.00 36.91 ? 857 HOH A O     1 
HETATM 7132 O  O     . HOH N 8 .   ? -13.364 5.717   20.922  1.00 34.10 ? 858 HOH A O     1 
HETATM 7133 O  O     . HOH N 8 .   ? 11.300  -27.348 30.664  1.00 45.64 ? 859 HOH A O     1 
HETATM 7134 O  O     . HOH N 8 .   ? 0.074   -13.030 -0.621  1.00 29.88 ? 860 HOH A O     1 
HETATM 7135 O  O     . HOH N 8 .   ? 9.744   -18.765 1.429   1.00 32.01 ? 861 HOH A O     1 
HETATM 7136 O  O     . HOH N 8 .   ? -10.442 -24.776 24.685  1.00 30.90 ? 862 HOH A O     1 
HETATM 7137 O  O     . HOH N 8 .   ? -4.666  -32.934 26.776  1.00 32.27 ? 863 HOH A O     1 
HETATM 7138 O  O     . HOH N 8 .   ? -4.783  13.127  12.895  1.00 31.68 ? 864 HOH A O     1 
HETATM 7139 O  O     . HOH N 8 .   ? -14.761 -2.875  25.321  1.00 38.82 ? 865 HOH A O     1 
HETATM 7140 O  O     . HOH N 8 .   ? -2.132  8.560   18.849  1.00 33.34 ? 866 HOH A O     1 
HETATM 7141 O  O     . HOH N 8 .   ? -21.037 -2.505  22.091  1.00 33.89 ? 867 HOH A O     1 
HETATM 7142 O  O     . HOH N 8 .   ? -27.759 -10.621 13.873  1.00 41.11 ? 868 HOH A O     1 
HETATM 7143 O  O     . HOH N 8 .   ? 14.149  -23.935 -6.492  1.00 38.40 ? 869 HOH A O     1 
HETATM 7144 O  O     . HOH N 8 .   ? -12.605 -27.684 5.702   1.00 32.52 ? 870 HOH A O     1 
HETATM 7145 O  O     . HOH N 8 .   ? 20.817  -21.479 11.951  1.00 26.17 ? 871 HOH A O     1 
HETATM 7146 O  O     . HOH N 8 .   ? 1.982   -3.092  2.876   1.00 24.40 ? 872 HOH A O     1 
HETATM 7147 O  O     . HOH N 8 .   ? -7.582  -37.614 18.918  1.00 29.06 ? 873 HOH A O     1 
HETATM 7148 O  O     . HOH N 8 .   ? -11.126 -36.251 12.320  1.00 34.91 ? 874 HOH A O     1 
HETATM 7149 O  O     . HOH O 8 .   ? 22.052  -5.531  27.071  1.00 26.56 ? 601 HOH B O     1 
HETATM 7150 O  O     . HOH O 8 .   ? 18.382  19.571  41.097  1.00 32.92 ? 602 HOH B O     1 
HETATM 7151 O  O     . HOH O 8 .   ? 22.190  -4.149  16.150  1.00 19.34 ? 603 HOH B O     1 
HETATM 7152 O  O     . HOH O 8 .   ? 20.545  20.948  39.809  1.00 32.22 ? 604 HOH B O     1 
HETATM 7153 O  O     . HOH O 8 .   ? 30.020  26.753  20.924  1.00 31.67 ? 605 HOH B O     1 
HETATM 7154 O  O     . HOH O 8 .   ? 23.890  31.198  11.659  1.00 22.76 ? 606 HOH B O     1 
HETATM 7155 O  O     . HOH O 8 .   ? 19.618  30.912  2.473   1.00 26.22 ? 607 HOH B O     1 
HETATM 7156 O  O     . HOH O 8 .   ? 26.384  40.883  17.673  1.00 40.99 ? 608 HOH B O     1 
HETATM 7157 O  O     . HOH O 8 .   ? 4.056   15.428  26.119  1.00 26.76 ? 609 HOH B O     1 
HETATM 7158 O  O     . HOH O 8 .   ? 28.126  -1.069  6.704   1.00 27.42 ? 610 HOH B O     1 
HETATM 7159 O  O     . HOH O 8 .   ? 23.873  -11.857 19.145  1.00 30.01 ? 611 HOH B O     1 
HETATM 7160 O  O     . HOH O 8 .   ? 29.916  3.207   0.141   1.00 34.59 ? 612 HOH B O     1 
HETATM 7161 O  O     . HOH O 8 .   ? 27.758  14.788  15.769  1.00 20.07 ? 613 HOH B O     1 
HETATM 7162 O  O     . HOH O 8 .   ? 18.784  5.593   3.798   1.00 20.73 ? 614 HOH B O     1 
HETATM 7163 O  O     . HOH O 8 .   ? 14.288  4.073   8.940   1.00 31.59 ? 615 HOH B O     1 
HETATM 7164 O  O     . HOH O 8 .   ? 19.209  22.143  7.245   1.00 18.53 ? 616 HOH B O     1 
HETATM 7165 O  O     . HOH O 8 .   ? 21.438  -8.429  -6.019  1.00 29.41 ? 617 HOH B O     1 
HETATM 7166 O  O     . HOH O 8 .   ? 31.163  32.308  13.247  1.00 34.05 ? 618 HOH B O     1 
HETATM 7167 O  O     . HOH O 8 .   ? 15.435  39.820  22.073  1.00 34.58 ? 619 HOH B O     1 
HETATM 7168 O  O     . HOH O 8 .   ? 34.518  11.780  3.735   1.00 23.87 ? 620 HOH B O     1 
HETATM 7169 O  O     . HOH O 8 .   ? 14.458  -7.533  -12.177 1.00 25.67 ? 621 HOH B O     1 
HETATM 7170 O  O     . HOH O 8 .   ? 34.317  23.332  1.492   1.00 28.87 ? 622 HOH B O     1 
HETATM 7171 O  O     . HOH O 8 .   ? -0.934  20.528  24.050  1.00 36.65 ? 623 HOH B O     1 
HETATM 7172 O  O     . HOH O 8 .   ? 36.586  26.442  11.080  1.00 31.03 ? 624 HOH B O     1 
HETATM 7173 O  O     . HOH O 8 .   ? 37.363  17.679  0.632   1.00 33.24 ? 625 HOH B O     1 
HETATM 7174 O  O     . HOH O 8 .   ? 24.800  21.570  38.923  1.00 28.74 ? 626 HOH B O     1 
HETATM 7175 O  O     . HOH O 8 .   ? 24.735  24.398  -9.768  1.00 37.48 ? 627 HOH B O     1 
HETATM 7176 O  O     . HOH O 8 .   ? 33.572  13.852  24.071  1.00 26.46 ? 628 HOH B O     1 
HETATM 7177 O  O     . HOH O 8 .   ? 12.525  20.856  33.187  1.00 35.05 ? 629 HOH B O     1 
HETATM 7178 O  O     . HOH O 8 .   ? 31.437  17.257  38.776  1.00 25.69 ? 630 HOH B O     1 
HETATM 7179 O  O     . HOH O 8 .   ? 22.384  -1.191  -3.645  1.00 18.80 ? 631 HOH B O     1 
HETATM 7180 O  O     . HOH O 8 .   ? 39.519  4.078   12.234  1.00 19.69 ? 632 HOH B O     1 
HETATM 7181 O  O     . HOH O 8 .   ? 25.445  -9.088  2.458   1.00 28.57 ? 633 HOH B O     1 
HETATM 7182 O  O     . HOH O 8 .   ? 2.094   -5.060  -5.606  1.00 42.80 ? 634 HOH B O     1 
HETATM 7183 O  O     . HOH O 8 .   ? 19.730  15.215  2.363   1.00 16.73 ? 635 HOH B O     1 
HETATM 7184 O  O     . HOH O 8 .   ? 28.555  33.588  14.250  1.00 38.55 ? 636 HOH B O     1 
HETATM 7185 O  O     . HOH O 8 .   ? 27.774  27.727  21.847  1.00 22.56 ? 637 HOH B O     1 
HETATM 7186 O  O     . HOH O 8 .   ? 5.057   17.116  16.404  1.00 21.34 ? 638 HOH B O     1 
HETATM 7187 O  O     . HOH O 8 .   ? 31.678  9.614   3.613   1.00 20.14 ? 639 HOH B O     1 
HETATM 7188 O  O     . HOH O 8 .   ? 25.789  27.709  14.550  1.00 19.63 ? 640 HOH B O     1 
HETATM 7189 O  O     . HOH O 8 .   ? 35.754  20.605  -4.758  1.00 29.49 ? 641 HOH B O     1 
HETATM 7190 O  O     . HOH O 8 .   ? 18.963  -6.095  0.158   1.00 20.89 ? 642 HOH B O     1 
HETATM 7191 O  O     . HOH O 8 .   ? 18.457  19.924  36.141  1.00 24.88 ? 643 HOH B O     1 
HETATM 7192 O  O     . HOH O 8 .   ? -1.127  4.769   -7.823  1.00 39.02 ? 644 HOH B O     1 
HETATM 7193 O  O     . HOH O 8 .   ? 32.327  18.681  22.987  1.00 36.69 ? 645 HOH B O     1 
HETATM 7194 O  O     . HOH O 8 .   ? 27.039  2.436   -17.629 1.00 30.16 ? 646 HOH B O     1 
HETATM 7195 O  O     . HOH O 8 .   ? 37.867  -6.661  12.797  1.00 35.90 ? 647 HOH B O     1 
HETATM 7196 O  O     . HOH O 8 .   ? 13.520  6.228   17.744  1.00 27.96 ? 648 HOH B O     1 
HETATM 7197 O  O     . HOH O 8 .   ? 17.088  -3.593  -19.792 1.00 36.36 ? 649 HOH B O     1 
HETATM 7198 O  O     . HOH O 8 .   ? 24.838  11.885  14.327  1.00 19.68 ? 650 HOH B O     1 
HETATM 7199 O  O     . HOH O 8 .   ? 37.981  -2.779  11.291  1.00 24.46 ? 651 HOH B O     1 
HETATM 7200 O  O     . HOH O 8 .   ? 24.117  -12.503 16.654  1.00 34.57 ? 652 HOH B O     1 
HETATM 7201 O  O     . HOH O 8 .   ? 33.623  24.664  24.674  1.00 29.79 ? 653 HOH B O     1 
HETATM 7202 O  O     . HOH O 8 .   ? 15.107  4.518   26.258  1.00 21.28 ? 654 HOH B O     1 
HETATM 7203 O  O     . HOH O 8 .   ? 31.019  -3.199  30.141  1.00 30.99 ? 655 HOH B O     1 
HETATM 7204 O  O     . HOH O 8 .   ? 34.229  25.968  15.197  1.00 23.36 ? 656 HOH B O     1 
HETATM 7205 O  O     . HOH O 8 .   ? 24.805  25.459  7.954   1.00 20.16 ? 657 HOH B O     1 
HETATM 7206 O  O     . HOH O 8 .   ? 22.513  36.572  8.276   1.00 24.15 ? 658 HOH B O     1 
HETATM 7207 O  O     . HOH O 8 .   ? 23.951  28.203  1.261   1.00 20.81 ? 659 HOH B O     1 
HETATM 7208 O  O     . HOH O 8 .   ? 8.669   -3.871  1.801   1.00 23.96 ? 660 HOH B O     1 
HETATM 7209 O  O     . HOH O 8 .   ? 19.103  15.882  28.940  1.00 32.00 ? 661 HOH B O     1 
HETATM 7210 O  O     . HOH O 8 .   ? 10.679  -3.246  -6.022  1.00 27.26 ? 662 HOH B O     1 
HETATM 7211 O  O     . HOH O 8 .   ? 33.452  25.933  0.887   1.00 28.70 ? 663 HOH B O     1 
HETATM 7212 O  O     . HOH O 8 .   ? 16.899  16.115  24.880  1.00 20.78 ? 664 HOH B O     1 
HETATM 7213 O  O     . HOH O 8 .   ? 13.584  12.876  4.377   1.00 17.05 ? 665 HOH B O     1 
HETATM 7214 O  O     . HOH O 8 .   ? 10.510  24.383  4.737   1.00 33.46 ? 666 HOH B O     1 
HETATM 7215 O  O     . HOH O 8 .   ? 19.773  9.558   14.628  1.00 18.38 ? 667 HOH B O     1 
HETATM 7216 O  O     . HOH O 8 .   ? 21.021  -7.291  -8.668  1.00 26.67 ? 668 HOH B O     1 
HETATM 7217 O  O     . HOH O 8 .   ? 28.637  -1.472  -5.150  1.00 32.58 ? 669 HOH B O     1 
HETATM 7218 O  O     . HOH O 8 .   ? 41.178  3.211   22.211  1.00 31.10 ? 670 HOH B O     1 
HETATM 7219 O  O     . HOH O 8 .   ? 2.385   10.257  -6.347  1.00 32.45 ? 671 HOH B O     1 
HETATM 7220 O  O     . HOH O 8 .   ? 6.972   20.014  6.332   1.00 35.55 ? 672 HOH B O     1 
HETATM 7221 O  O     . HOH O 8 .   ? 28.254  16.008  6.902   1.00 17.14 ? 673 HOH B O     1 
HETATM 7222 O  O     . HOH O 8 .   ? 37.523  15.307  22.537  1.00 36.40 ? 674 HOH B O     1 
HETATM 7223 O  O     . HOH O 8 .   ? 19.125  39.773  10.081  1.00 37.10 ? 675 HOH B O     1 
HETATM 7224 O  O     . HOH O 8 .   ? 30.690  2.086   -12.373 1.00 25.22 ? 676 HOH B O     1 
HETATM 7225 O  O     . HOH O 8 .   ? 14.165  22.968  -3.612  1.00 21.07 ? 677 HOH B O     1 
HETATM 7226 O  O     . HOH O 8 .   ? 18.423  6.931   15.717  1.00 19.77 ? 678 HOH B O     1 
HETATM 7227 O  O     . HOH O 8 .   ? 37.529  -1.784  24.795  1.00 27.75 ? 679 HOH B O     1 
HETATM 7228 O  O     . HOH O 8 .   ? 40.207  16.963  13.909  1.00 37.11 ? 680 HOH B O     1 
HETATM 7229 O  O     . HOH O 8 .   ? 6.108   21.278  -6.564  1.00 39.65 ? 681 HOH B O     1 
HETATM 7230 O  O     . HOH O 8 .   ? 28.683  17.168  10.920  1.00 18.02 ? 682 HOH B O     1 
HETATM 7231 O  O     . HOH O 8 .   ? 27.553  13.297  -8.077  1.00 23.08 ? 683 HOH B O     1 
HETATM 7232 O  O     . HOH O 8 .   ? 23.434  5.541   10.012  1.00 29.14 ? 684 HOH B O     1 
HETATM 7233 O  O     . HOH O 8 .   ? 31.018  24.081  21.425  1.00 30.51 ? 685 HOH B O     1 
HETATM 7234 O  O     . HOH O 8 .   ? 12.791  13.043  14.802  1.00 22.20 ? 686 HOH B O     1 
HETATM 7235 O  O     . HOH O 8 .   ? 29.463  -5.876  3.117   1.00 35.77 ? 687 HOH B O     1 
HETATM 7236 O  O     . HOH O 8 .   ? 21.338  28.994  13.660  1.00 19.95 ? 688 HOH B O     1 
HETATM 7237 O  O     . HOH O 8 .   ? 34.241  16.295  11.828  1.00 26.79 ? 689 HOH B O     1 
HETATM 7238 O  O     . HOH O 8 .   ? 26.850  1.221   6.883   1.00 26.64 ? 690 HOH B O     1 
HETATM 7239 O  O     . HOH O 8 .   ? 20.247  18.883  34.286  1.00 24.72 ? 691 HOH B O     1 
HETATM 7240 O  O     . HOH O 8 .   ? 34.081  27.414  25.359  1.00 28.56 ? 692 HOH B O     1 
HETATM 7241 O  O     . HOH O 8 .   ? 11.106  5.677   15.184  1.00 25.00 ? 693 HOH B O     1 
HETATM 7242 O  O     . HOH O 8 .   ? 23.567  26.366  15.798  1.00 25.27 ? 694 HOH B O     1 
HETATM 7243 O  O     . HOH O 8 .   ? 10.227  19.674  5.388   1.00 27.70 ? 695 HOH B O     1 
HETATM 7244 O  O     . HOH O 8 .   ? 33.973  18.886  5.955   1.00 31.43 ? 696 HOH B O     1 
HETATM 7245 O  O     . HOH O 8 .   ? 5.400   24.483  28.256  1.00 26.05 ? 697 HOH B O     1 
HETATM 7246 O  O     . HOH O 8 .   ? 28.297  31.081  -5.659  1.00 32.28 ? 698 HOH B O     1 
HETATM 7247 O  O     . HOH O 8 .   ? 31.720  26.825  23.544  1.00 26.72 ? 699 HOH B O     1 
HETATM 7248 O  O     . HOH O 8 .   ? 17.598  23.628  -7.961  1.00 31.02 ? 700 HOH B O     1 
HETATM 7249 O  O     . HOH O 8 .   ? 30.552  30.312  21.537  1.00 35.60 ? 701 HOH B O     1 
HETATM 7250 O  O     . HOH O 8 .   ? 14.671  7.640   19.571  1.00 23.05 ? 702 HOH B O     1 
HETATM 7251 O  O     . HOH O 8 .   ? 21.594  32.201  10.613  1.00 20.90 ? 703 HOH B O     1 
HETATM 7252 O  O     . HOH O 8 .   ? 26.509  30.299  14.992  1.00 24.69 ? 704 HOH B O     1 
HETATM 7253 O  O     . HOH O 8 .   ? 11.877  -8.034  -4.493  1.00 29.17 ? 705 HOH B O     1 
HETATM 7254 O  O     . HOH O 8 .   ? 21.579  38.554  9.721   1.00 26.27 ? 706 HOH B O     1 
HETATM 7255 O  O     . HOH O 8 .   ? 12.344  -1.732  15.348  1.00 21.51 ? 707 HOH B O     1 
HETATM 7256 O  O     . HOH O 8 .   ? 13.222  17.284  0.011   1.00 15.48 ? 708 HOH B O     1 
HETATM 7257 O  O     . HOH O 8 .   ? 32.554  32.869  6.332   1.00 39.86 ? 709 HOH B O     1 
HETATM 7258 O  O     . HOH O 8 .   ? 20.720  -13.992 8.964   1.00 26.35 ? 710 HOH B O     1 
HETATM 7259 O  O     . HOH O 8 .   ? 35.797  26.098  23.237  1.00 28.88 ? 711 HOH B O     1 
HETATM 7260 O  O     . HOH O 8 .   ? 14.567  20.648  36.666  1.00 36.15 ? 712 HOH B O     1 
HETATM 7261 O  O     . HOH O 8 .   ? 3.206   19.946  -3.356  1.00 42.39 ? 713 HOH B O     1 
HETATM 7262 O  O     . HOH O 8 .   ? 18.317  -11.031 16.501  1.00 29.27 ? 714 HOH B O     1 
HETATM 7263 O  O     . HOH O 8 .   ? 39.803  10.673  13.614  1.00 34.80 ? 715 HOH B O     1 
HETATM 7264 O  O     . HOH O 8 .   ? 8.817   29.316  30.455  1.00 35.19 ? 716 HOH B O     1 
HETATM 7265 O  O     . HOH O 8 .   ? 10.294  17.000  26.554  1.00 19.96 ? 717 HOH B O     1 
HETATM 7266 O  O     . HOH O 8 .   ? 18.173  11.126  -1.156  1.00 16.04 ? 718 HOH B O     1 
HETATM 7267 O  O     . HOH O 8 .   ? 5.256   12.919  19.631  1.00 18.82 ? 719 HOH B O     1 
HETATM 7268 O  O     . HOH O 8 .   ? 22.037  8.498   13.427  1.00 26.59 ? 720 HOH B O     1 
HETATM 7269 O  O     . HOH O 8 .   ? 4.317   8.823   6.978   1.00 27.28 ? 721 HOH B O     1 
HETATM 7270 O  O     . HOH O 8 .   ? 16.382  3.805   0.438   1.00 22.93 ? 722 HOH B O     1 
HETATM 7271 O  O     . HOH O 8 .   ? 15.905  19.003  -13.460 1.00 26.98 ? 723 HOH B O     1 
HETATM 7272 O  O     . HOH O 8 .   ? -0.407  26.239  22.900  1.00 33.67 ? 724 HOH B O     1 
HETATM 7273 O  O     . HOH O 8 .   ? 10.918  -5.925  -6.226  1.00 26.70 ? 725 HOH B O     1 
HETATM 7274 O  O     . HOH O 8 .   ? 9.374   19.502  -10.485 1.00 30.04 ? 726 HOH B O     1 
HETATM 7275 O  O     . HOH O 8 .   ? 34.447  28.212  8.502   1.00 27.89 ? 727 HOH B O     1 
HETATM 7276 O  O     . HOH O 8 .   ? 9.254   -11.963 0.563   1.00 23.43 ? 728 HOH B O     1 
HETATM 7277 O  O     . HOH O 8 .   ? 3.781   -7.125  -4.845  1.00 35.11 ? 729 HOH B O     1 
HETATM 7278 O  O     . HOH O 8 .   ? 22.108  5.867   14.562  1.00 19.90 ? 730 HOH B O     1 
HETATM 7279 O  O     . HOH O 8 .   ? 27.384  3.381   0.496   1.00 23.68 ? 731 HOH B O     1 
HETATM 7280 O  O     . HOH O 8 .   ? 8.695   10.213  26.259  1.00 25.80 ? 732 HOH B O     1 
HETATM 7281 O  O     . HOH O 8 .   ? 18.745  -9.104  -2.986  1.00 34.38 ? 733 HOH B O     1 
HETATM 7282 O  O     . HOH O 8 .   ? 36.634  11.442  10.314  1.00 23.87 ? 734 HOH B O     1 
HETATM 7283 O  O     . HOH O 8 .   ? 13.377  7.311   22.626  1.00 21.19 ? 735 HOH B O     1 
HETATM 7284 O  O     . HOH O 8 .   ? 7.576   15.628  5.220   1.00 18.50 ? 736 HOH B O     1 
HETATM 7285 O  O     . HOH O 8 .   ? 39.991  0.624   10.122  1.00 20.33 ? 737 HOH B O     1 
HETATM 7286 O  O     . HOH O 8 .   ? 30.111  19.802  19.681  1.00 21.51 ? 738 HOH B O     1 
HETATM 7287 O  O     . HOH O 8 .   ? 29.267  8.054   11.529  1.00 17.28 ? 739 HOH B O     1 
HETATM 7288 O  O     . HOH O 8 .   ? 35.181  21.340  8.256   1.00 39.79 ? 740 HOH B O     1 
HETATM 7289 O  O     . HOH O 8 .   ? 9.748   0.930   9.748   1.00 32.66 ? 741 HOH B O     1 
HETATM 7290 O  O     . HOH O 8 .   ? 26.986  29.406  27.720  1.00 25.35 ? 742 HOH B O     1 
HETATM 7291 O  O     . HOH O 8 .   ? 20.661  12.663  -18.105 1.00 41.39 ? 743 HOH B O     1 
HETATM 7292 O  O     . HOH O 8 .   ? 12.593  25.383  2.902   1.00 30.57 ? 744 HOH B O     1 
HETATM 7293 O  O     . HOH O 8 .   ? 24.641  -5.149  2.664   1.00 22.21 ? 745 HOH B O     1 
HETATM 7294 O  O     . HOH O 8 .   ? 13.743  37.131  6.529   1.00 31.86 ? 746 HOH B O     1 
HETATM 7295 O  O     . HOH O 8 .   ? 21.480  7.058   11.122  1.00 22.43 ? 747 HOH B O     1 
HETATM 7296 O  O     . HOH O 8 .   ? 18.721  -9.797  -6.823  1.00 33.77 ? 748 HOH B O     1 
HETATM 7297 O  O     . HOH O 8 .   ? 21.788  12.217  31.142  1.00 36.09 ? 749 HOH B O     1 
HETATM 7298 O  O     . HOH O 8 .   ? 42.332  7.046   13.849  1.00 31.82 ? 750 HOH B O     1 
HETATM 7299 O  O     . HOH O 8 .   ? 5.594   -2.741  1.456   1.00 29.44 ? 751 HOH B O     1 
HETATM 7300 O  O     . HOH O 8 .   ? 30.182  14.413  -4.572  1.00 35.30 ? 752 HOH B O     1 
HETATM 7301 O  O     . HOH O 8 .   ? 7.459   5.749   1.048   1.00 17.83 ? 753 HOH B O     1 
HETATM 7302 O  O     . HOH O 8 .   ? 25.233  6.711   29.643  1.00 24.30 ? 754 HOH B O     1 
HETATM 7303 O  O     . HOH O 8 .   ? 18.044  8.285   2.718   1.00 24.16 ? 755 HOH B O     1 
HETATM 7304 O  O     . HOH O 8 .   ? 11.049  36.868  9.361   1.00 34.50 ? 756 HOH B O     1 
HETATM 7305 O  O     . HOH O 8 .   ? 10.226  13.456  17.962  1.00 26.42 ? 757 HOH B O     1 
HETATM 7306 O  O     . HOH O 8 .   ? 40.336  3.158   27.807  1.00 33.44 ? 758 HOH B O     1 
HETATM 7307 O  O     . HOH O 8 .   ? 21.356  36.878  5.629   1.00 33.81 ? 759 HOH B O     1 
HETATM 7308 O  O     . HOH O 8 .   ? 18.394  -12.908 2.404   1.00 33.93 ? 760 HOH B O     1 
HETATM 7309 O  O     . HOH O 8 .   ? 26.717  17.332  13.137  1.00 21.01 ? 761 HOH B O     1 
HETATM 7310 O  O     . HOH O 8 .   ? 11.476  0.417   11.593  1.00 20.75 ? 762 HOH B O     1 
HETATM 7311 O  O     . HOH O 8 .   ? 22.681  -12.893 5.825   1.00 30.00 ? 763 HOH B O     1 
HETATM 7312 O  O     . HOH O 8 .   ? 38.961  3.274   9.602   1.00 21.47 ? 764 HOH B O     1 
HETATM 7313 O  O     . HOH O 8 .   ? 7.387   13.164  18.080  1.00 22.43 ? 765 HOH B O     1 
HETATM 7314 O  O     . HOH O 8 .   ? 35.725  23.837  20.205  1.00 28.57 ? 766 HOH B O     1 
HETATM 7315 O  O     . HOH O 8 .   ? 11.973  23.463  31.095  1.00 33.62 ? 767 HOH B O     1 
HETATM 7316 O  O     . HOH O 8 .   ? 5.812   -4.506  -1.082  1.00 25.43 ? 768 HOH B O     1 
HETATM 7317 O  O     . HOH O 8 .   ? 20.368  28.520  11.125  1.00 19.79 ? 769 HOH B O     1 
HETATM 7318 O  O     . HOH O 8 .   ? 31.299  15.391  41.671  1.00 36.13 ? 770 HOH B O     1 
HETATM 7319 O  O     . HOH O 8 .   ? 5.580   14.694  -11.817 1.00 36.49 ? 771 HOH B O     1 
HETATM 7320 O  O     . HOH O 8 .   ? 27.627  15.375  -4.607  1.00 27.83 ? 772 HOH B O     1 
HETATM 7321 O  O     . HOH O 8 .   ? 34.107  -7.116  24.433  1.00 39.95 ? 773 HOH B O     1 
HETATM 7322 O  O     . HOH O 8 .   ? 7.219   20.208  13.240  1.00 24.05 ? 774 HOH B O     1 
HETATM 7323 O  O     . HOH O 8 .   ? 11.884  25.114  0.241   1.00 28.87 ? 775 HOH B O     1 
HETATM 7324 O  O     . HOH O 8 .   ? 19.747  17.745  23.576  1.00 34.46 ? 776 HOH B O     1 
HETATM 7325 O  O     . HOH O 8 .   ? 14.499  18.000  36.109  1.00 36.46 ? 777 HOH B O     1 
HETATM 7326 O  O     . HOH O 8 .   ? 27.787  30.555  0.739   1.00 32.38 ? 778 HOH B O     1 
HETATM 7327 O  O     . HOH O 8 .   ? 36.705  -1.158  8.229   1.00 21.92 ? 779 HOH B O     1 
HETATM 7328 O  O     . HOH O 8 .   ? 7.897   18.835  3.729   1.00 34.26 ? 780 HOH B O     1 
HETATM 7329 O  O     . HOH O 8 .   ? 1.884   23.831  17.331  1.00 27.02 ? 781 HOH B O     1 
HETATM 7330 O  O     . HOH O 8 .   ? 21.931  20.099  13.411  1.00 18.40 ? 782 HOH B O     1 
HETATM 7331 O  O     . HOH O 8 .   ? 34.409  20.863  21.551  1.00 26.67 ? 783 HOH B O     1 
HETATM 7332 O  O     . HOH O 8 .   ? 5.542   4.893   -0.674  1.00 25.11 ? 784 HOH B O     1 
HETATM 7333 O  O     . HOH O 8 .   ? 21.079  15.387  24.377  1.00 23.89 ? 785 HOH B O     1 
HETATM 7334 O  O     . HOH O 8 .   ? 18.441  2.357   32.787  1.00 35.48 ? 786 HOH B O     1 
HETATM 7335 O  O     . HOH O 8 .   ? 30.738  -12.851 19.954  1.00 30.27 ? 787 HOH B O     1 
HETATM 7336 O  O     . HOH O 8 .   ? 28.654  36.406  14.933  1.00 37.79 ? 788 HOH B O     1 
HETATM 7337 O  O     . HOH O 8 .   ? 8.484   27.013  13.838  1.00 27.48 ? 789 HOH B O     1 
HETATM 7338 O  O     . HOH O 8 .   ? 17.402  24.572  38.159  1.00 27.56 ? 790 HOH B O     1 
HETATM 7339 O  O     . HOH O 8 .   ? 30.470  -13.219 16.516  1.00 33.17 ? 791 HOH B O     1 
HETATM 7340 O  O     . HOH O 8 .   ? 37.953  11.053  17.270  1.00 34.68 ? 792 HOH B O     1 
HETATM 7341 O  O     . HOH O 8 .   ? 39.461  17.096  41.058  1.00 34.17 ? 793 HOH B O     1 
HETATM 7342 O  O     . HOH O 8 .   ? 25.643  36.868  8.242   1.00 22.18 ? 794 HOH B O     1 
HETATM 7343 O  O     . HOH O 8 .   ? 6.232   19.429  0.496   1.00 32.12 ? 795 HOH B O     1 
HETATM 7344 O  O     . HOH O 8 .   ? 29.091  39.493  18.901  1.00 40.93 ? 796 HOH B O     1 
HETATM 7345 O  O     . HOH O 8 .   ? 24.437  2.573   32.183  1.00 37.23 ? 797 HOH B O     1 
HETATM 7346 O  O     . HOH O 8 .   ? 33.587  25.372  21.669  1.00 24.47 ? 798 HOH B O     1 
HETATM 7347 O  O     . HOH O 8 .   ? 35.110  -2.706  26.984  1.00 40.82 ? 799 HOH B O     1 
HETATM 7348 O  O     . HOH O 8 .   ? 8.761   20.589  2.272   1.00 31.50 ? 800 HOH B O     1 
HETATM 7349 O  O     . HOH O 8 .   ? 33.828  32.217  19.172  1.00 31.07 ? 801 HOH B O     1 
HETATM 7350 O  O     . HOH O 8 .   ? 9.519   21.862  4.290   1.00 38.85 ? 802 HOH B O     1 
HETATM 7351 O  O     . HOH O 8 .   ? 23.635  13.512  12.333  1.00 24.78 ? 803 HOH B O     1 
HETATM 7352 O  O     . HOH O 8 .   ? 19.278  14.660  26.246  1.00 31.69 ? 804 HOH B O     1 
HETATM 7353 O  O     . HOH O 8 .   ? 3.252   -1.413  0.995   1.00 34.20 ? 805 HOH B O     1 
HETATM 7354 O  O     . HOH O 8 .   ? 26.162  2.503   12.665  1.00 22.83 ? 806 HOH B O     1 
HETATM 7355 O  O     . HOH O 8 .   ? 24.217  15.722  13.628  1.00 28.77 ? 807 HOH B O     1 
HETATM 7356 O  O     . HOH O 8 .   ? 15.898  -13.429 2.631   1.00 15.19 ? 808 HOH B O     1 
HETATM 7357 O  O     . HOH O 8 .   ? 24.044  14.607  36.611  1.00 29.38 ? 809 HOH B O     1 
HETATM 7358 O  O     . HOH O 8 .   ? 7.483   33.104  19.983  1.00 30.15 ? 810 HOH B O     1 
HETATM 7359 O  O     . HOH O 8 .   ? 1.454   14.769  18.041  1.00 31.07 ? 811 HOH B O     1 
HETATM 7360 O  O     . HOH O 8 .   ? 0.936   10.735  -4.011  1.00 36.09 ? 812 HOH B O     1 
HETATM 7361 O  O     . HOH O 8 .   ? 7.135   29.284  13.998  1.00 47.51 ? 813 HOH B O     1 
HETATM 7362 O  O     . HOH O 8 .   ? 0.683   24.591  29.168  1.00 31.64 ? 814 HOH B O     1 
HETATM 7363 O  O     . HOH O 8 .   ? 7.821   18.790  26.861  1.00 18.33 ? 815 HOH B O     1 
HETATM 7364 O  O     . HOH O 8 .   ? 27.152  -5.239  1.587   1.00 35.18 ? 816 HOH B O     1 
HETATM 7365 O  O     . HOH O 8 .   ? 18.312  40.522  22.949  1.00 28.99 ? 817 HOH B O     1 
HETATM 7366 O  O     . HOH O 8 .   ? 36.444  1.704   30.419  1.00 36.50 ? 818 HOH B O     1 
HETATM 7367 O  O     . HOH O 8 .   ? 21.337  -14.523 4.210   1.00 36.18 ? 819 HOH B O     1 
HETATM 7368 O  O     . HOH O 8 .   ? 19.074  26.429  38.400  1.00 34.01 ? 820 HOH B O     1 
HETATM 7369 O  O     . HOH O 8 .   ? 24.258  29.189  -7.879  1.00 42.11 ? 821 HOH B O     1 
HETATM 7370 O  O     . HOH O 8 .   ? 2.499   12.250  -7.934  1.00 35.81 ? 822 HOH B O     1 
HETATM 7371 O  O     . HOH O 8 .   ? 24.109  2.969   10.857  1.00 22.87 ? 823 HOH B O     1 
HETATM 7372 O  O     . HOH O 8 .   ? 20.873  29.229  41.702  1.00 42.30 ? 824 HOH B O     1 
HETATM 7373 O  O     . HOH O 8 .   ? 31.870  22.404  23.219  1.00 42.06 ? 825 HOH B O     1 
HETATM 7374 O  O     . HOH O 8 .   ? 5.037   19.303  14.986  1.00 31.07 ? 826 HOH B O     1 
HETATM 7375 O  O     . HOH O 8 .   ? 5.464   16.955  3.792   1.00 27.08 ? 827 HOH B O     1 
HETATM 7376 O  O     . HOH O 8 .   ? 13.345  14.706  29.716  1.00 38.54 ? 828 HOH B O     1 
HETATM 7377 O  O     . HOH O 8 .   ? -2.387  13.256  -11.249 1.00 48.64 ? 829 HOH B O     1 
HETATM 7378 O  O     . HOH O 8 .   ? 2.318   16.343  15.325  1.00 34.26 ? 830 HOH B O     1 
HETATM 7379 O  O     . HOH O 8 .   ? 2.864   -5.778  -0.699  1.00 31.22 ? 831 HOH B O     1 
HETATM 7380 O  O     . HOH O 8 .   ? 22.753  30.295  -0.253  1.00 31.76 ? 832 HOH B O     1 
HETATM 7381 O  O     . HOH O 8 .   ? 24.973  -4.460  -8.596  1.00 27.17 ? 833 HOH B O     1 
HETATM 7382 O  O     . HOH O 8 .   ? 12.347  22.516  37.028  1.00 34.69 ? 834 HOH B O     1 
HETATM 7383 O  O     . HOH O 8 .   ? 18.400  21.905  38.440  1.00 28.23 ? 835 HOH B O     1 
HETATM 7384 O  O     . HOH O 8 .   ? 31.374  20.970  24.667  1.00 39.11 ? 836 HOH B O     1 
HETATM 7385 O  O     . HOH O 8 .   ? 18.525  -8.676  -0.054  1.00 29.84 ? 837 HOH B O     1 
HETATM 7386 O  O     . HOH O 8 .   ? 36.811  26.595  14.817  1.00 37.55 ? 838 HOH B O     1 
HETATM 7387 O  O     . HOH O 8 .   ? 8.965   19.318  29.795  1.00 31.10 ? 839 HOH B O     1 
HETATM 7388 O  O     . HOH O 8 .   ? 10.751  15.351  28.672  1.00 32.63 ? 840 HOH B O     1 
HETATM 7389 O  O     . HOH O 8 .   ? 14.881  22.779  -6.410  1.00 35.11 ? 841 HOH B O     1 
HETATM 7390 O  O     . HOH O 8 .   ? 35.299  23.162  4.176   1.00 34.37 ? 842 HOH B O     1 
HETATM 7391 O  O     . HOH O 8 .   ? 5.374   6.529   2.896   1.00 28.85 ? 843 HOH B O     1 
HETATM 7392 O  O     . HOH O 8 .   ? -2.746  13.331  -2.300  1.00 39.46 ? 844 HOH B O     1 
# 
