data_9HH3
# 
_entry.id   9HH3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9HH3         pdb_00009hh3 10.2210/pdb9hh3/pdb 
WWPDB D_1292142747 ?            ?                   
# 
_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       2025-06-04 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HH3 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              elizabeth.ficko-blean@sb-roscoff.fr 
_pdbx_contact_author.name_first         Elizabeth 
_pdbx_contact_author.name_last          Ficko-Blean 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3915-4715 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chevenier, A.'   1 0000-0002-0510-7929 
'Czjzek, M.'      2 0000-0002-7483-2841 
'Michel, G.'      3 0000-0002-3009-6205 
'Ficko-Blean, E.' 4 0000-0002-3915-4715 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Carbohydr Polym' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1879-1344 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            358 
_citation.language                  ? 
_citation.page_first                123487 
_citation.page_last                 123487 
_citation.title                     
;Structure, function and catalytic mechanism of the carrageenan-sulfatases from the marine bacterium Zobellia galactanivorans Dsij T.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.carbpol.2025.123487 
_citation.pdbx_database_id_PubMed   40383559 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chevenier, A.'    1  ? 
primary 'Fanuel, M.'       2  ? 
primary 'Sokolova, E.'     3  ? 
primary 'Mico Latorre, D.' 4  ? 
primary 'Jouanneau, D.'    5  ? 
primary 'Jeudy, A.'        6  ? 
primary 'Prechoux, A.'     7  ? 
primary 'Zuhlke, M.K.'     8  ? 
primary 'Bartel, J.'       9  ? 
primary 'Becher, D.'       10 ? 
primary 'Czjzek, M.'       11 ? 
primary 'Ropartz, D.'      12 ? 
primary 'Michel, G.'       13 ? 
primary 'Ficko-Blean, E.'  14 ? 
# 
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 'Sulfatase, family S1-19' 54714.480 4   3.1.6.- ? ? ? 
2 non-polymer syn 'BROMIDE ION'             79.904    10  ?       ? ? ? 
3 non-polymer syn 'CHLORIDE ION'            35.453    25  ?       ? ? ? 
4 non-polymer syn 'CALCIUM ION'             40.078    4   ?       ? ? ? 
5 water       nat water                     18.015    456 ?       ? ? ? 
# 
_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       
;MGSSHHHHHHGSQETRPNILVVLCDDLGYADVGFNGSTDILTPELDNLAQNGSIFTSAYVAHPFCGPSRSAILTGRYPHL
TGTAYNLFHNSSEDDKDNMGVPVEETYMSKVLQNAGYYTSAIGKWHLGAAPKFHPNKRGFDDFYGFLGGGHDYFPSEYQK
TYKAQKKAGNPNIRDYVFPMEHNGKPANETEYITDGFSREAIKNIKIAAAKKQPFFIYLAYNAPHVPLQAKAEDVAKFAH
IKDKDRRTYAAMVYAVDRGVGKIVQTLKETKQFDNTLIVFLSDNGGNFNHGANNYPLKGTKGDTWEGGYRVPMFFHWPKK
IKKDQRFDFPVSSLDLYPTFTGLAEAKLPKGKQLDGKNIMDDVLKNTEPYKDEMIYSLRYREGYNDVGARMGDWKITRMG
NEPWRLHNITQDIGEKKNLAGRYPDRLKEMIAKTQEWTKSFVKPLWVYSVKDKELWESGQMPNYEATFEVDKLVDSPYHK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHGSQETRPNILVVLCDDLGYADVGFNGSTDILTPELDNLAQNGSIFTSAYVAHPFCGPSRSAILTGRYPHL
TGTAYNLFHNSSEDDKDNMGVPVEETYMSKVLQNAGYYTSAIGKWHLGAAPKFHPNKRGFDDFYGFLGGGHDYFPSEYQK
TYKAQKKAGNPNIRDYVFPMEHNGKPANETEYITDGFSREAIKNIKIAAAKKQPFFIYLAYNAPHVPLQAKAEDVAKFAH
IKDKDRRTYAAMVYAVDRGVGKIVQTLKETKQFDNTLIVFLSDNGGNFNHGANNYPLKGTKGDTWEGGYRVPMFFHWPKK
IKKDQRFDFPVSSLDLYPTFTGLAEAKLPKGKQLDGKNIMDDVLKNTEPYKDEMIYSLRYREGYNDVGARMGDWKITRMG
NEPWRLHNITQDIGEKKNLAGRYPDRLKEMIAKTQEWTKSFVKPLWVYSVKDKELWESGQMPNYEATFEVDKLVDSPYHK
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'BROMIDE ION'  BR  
3 'CHLORIDE ION' CL  
4 'CALCIUM ION'  CA  
5 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  GLY n 
1 12  SER n 
1 13  GLN n 
1 14  GLU n 
1 15  THR n 
1 16  ARG n 
1 17  PRO n 
1 18  ASN n 
1 19  ILE n 
1 20  LEU n 
1 21  VAL n 
1 22  VAL n 
1 23  LEU n 
1 24  CYS n 
1 25  ASP n 
1 26  ASP n 
1 27  LEU n 
1 28  GLY n 
1 29  TYR n 
1 30  ALA n 
1 31  ASP n 
1 32  VAL n 
1 33  GLY n 
1 34  PHE n 
1 35  ASN n 
1 36  GLY n 
1 37  SER n 
1 38  THR n 
1 39  ASP n 
1 40  ILE n 
1 41  LEU n 
1 42  THR n 
1 43  PRO n 
1 44  GLU n 
1 45  LEU n 
1 46  ASP n 
1 47  ASN n 
1 48  LEU n 
1 49  ALA n 
1 50  GLN n 
1 51  ASN n 
1 52  GLY n 
1 53  SER n 
1 54  ILE n 
1 55  PHE n 
1 56  THR n 
1 57  SER n 
1 58  ALA n 
1 59  TYR n 
1 60  VAL n 
1 61  ALA n 
1 62  HIS n 
1 63  PRO n 
1 64  PHE n 
1 65  CYS y 
1 65  DDZ y 
1 66  GLY n 
1 67  PRO n 
1 68  SER n 
1 69  ARG n 
1 70  SER n 
1 71  ALA n 
1 72  ILE n 
1 73  LEU n 
1 74  THR n 
1 75  GLY n 
1 76  ARG n 
1 77  TYR n 
1 78  PRO n 
1 79  HIS n 
1 80  LEU n 
1 81  THR n 
1 82  GLY n 
1 83  THR n 
1 84  ALA n 
1 85  TYR n 
1 86  ASN n 
1 87  LEU n 
1 88  PHE n 
1 89  HIS n 
1 90  ASN n 
1 91  SER n 
1 92  SER n 
1 93  GLU n 
1 94  ASP n 
1 95  ASP n 
1 96  LYS n 
1 97  ASP n 
1 98  ASN n 
1 99  MET n 
1 100 GLY n 
1 101 VAL n 
1 102 PRO n 
1 103 VAL n 
1 104 GLU n 
1 105 GLU n 
1 106 THR n 
1 107 TYR n 
1 108 MET n 
1 109 SER n 
1 110 LYS n 
1 111 VAL n 
1 112 LEU n 
1 113 GLN n 
1 114 ASN n 
1 115 ALA n 
1 116 GLY n 
1 117 TYR n 
1 118 TYR n 
1 119 THR n 
1 120 SER n 
1 121 ALA n 
1 122 ILE n 
1 123 GLY n 
1 124 LYS n 
1 125 TRP n 
1 126 HIS n 
1 127 LEU n 
1 128 GLY n 
1 129 ALA n 
1 130 ALA n 
1 131 PRO n 
1 132 LYS n 
1 133 PHE n 
1 134 HIS n 
1 135 PRO n 
1 136 ASN n 
1 137 LYS n 
1 138 ARG n 
1 139 GLY n 
1 140 PHE n 
1 141 ASP n 
1 142 ASP n 
1 143 PHE n 
1 144 TYR n 
1 145 GLY n 
1 146 PHE n 
1 147 LEU n 
1 148 GLY n 
1 149 GLY n 
1 150 GLY n 
1 151 HIS n 
1 152 ASP n 
1 153 TYR n 
1 154 PHE n 
1 155 PRO n 
1 156 SER n 
1 157 GLU n 
1 158 TYR n 
1 159 GLN n 
1 160 LYS n 
1 161 THR n 
1 162 TYR n 
1 163 LYS n 
1 164 ALA n 
1 165 GLN n 
1 166 LYS n 
1 167 LYS n 
1 168 ALA n 
1 169 GLY n 
1 170 ASN n 
1 171 PRO n 
1 172 ASN n 
1 173 ILE n 
1 174 ARG n 
1 175 ASP n 
1 176 TYR n 
1 177 VAL n 
1 178 PHE n 
1 179 PRO n 
1 180 MET n 
1 181 GLU n 
1 182 HIS n 
1 183 ASN n 
1 184 GLY n 
1 185 LYS n 
1 186 PRO n 
1 187 ALA n 
1 188 ASN n 
1 189 GLU n 
1 190 THR n 
1 191 GLU n 
1 192 TYR n 
1 193 ILE n 
1 194 THR n 
1 195 ASP n 
1 196 GLY n 
1 197 PHE n 
1 198 SER n 
1 199 ARG n 
1 200 GLU n 
1 201 ALA n 
1 202 ILE n 
1 203 LYS n 
1 204 ASN n 
1 205 ILE n 
1 206 LYS n 
1 207 ILE n 
1 208 ALA n 
1 209 ALA n 
1 210 ALA n 
1 211 LYS n 
1 212 LYS n 
1 213 GLN n 
1 214 PRO n 
1 215 PHE n 
1 216 PHE n 
1 217 ILE n 
1 218 TYR n 
1 219 LEU n 
1 220 ALA n 
1 221 TYR n 
1 222 ASN n 
1 223 ALA n 
1 224 PRO n 
1 225 HIS n 
1 226 VAL n 
1 227 PRO n 
1 228 LEU n 
1 229 GLN n 
1 230 ALA n 
1 231 LYS n 
1 232 ALA n 
1 233 GLU n 
1 234 ASP n 
1 235 VAL n 
1 236 ALA n 
1 237 LYS n 
1 238 PHE n 
1 239 ALA n 
1 240 HIS n 
1 241 ILE n 
1 242 LYS n 
1 243 ASP n 
1 244 LYS n 
1 245 ASP n 
1 246 ARG n 
1 247 ARG n 
1 248 THR n 
1 249 TYR n 
1 250 ALA n 
1 251 ALA n 
1 252 MET n 
1 253 VAL n 
1 254 TYR n 
1 255 ALA n 
1 256 VAL n 
1 257 ASP n 
1 258 ARG n 
1 259 GLY n 
1 260 VAL n 
1 261 GLY n 
1 262 LYS n 
1 263 ILE n 
1 264 VAL n 
1 265 GLN n 
1 266 THR n 
1 267 LEU n 
1 268 LYS n 
1 269 GLU n 
1 270 THR n 
1 271 LYS n 
1 272 GLN n 
1 273 PHE n 
1 274 ASP n 
1 275 ASN n 
1 276 THR n 
1 277 LEU n 
1 278 ILE n 
1 279 VAL n 
1 280 PHE n 
1 281 LEU n 
1 282 SER n 
1 283 ASP n 
1 284 ASN n 
1 285 GLY n 
1 286 GLY n 
1 287 ASN n 
1 288 PHE n 
1 289 ASN n 
1 290 HIS n 
1 291 GLY n 
1 292 ALA n 
1 293 ASN n 
1 294 ASN n 
1 295 TYR n 
1 296 PRO n 
1 297 LEU n 
1 298 LYS n 
1 299 GLY n 
1 300 THR n 
1 301 LYS n 
1 302 GLY n 
1 303 ASP n 
1 304 THR n 
1 305 TRP n 
1 306 GLU n 
1 307 GLY n 
1 308 GLY n 
1 309 TYR n 
1 310 ARG n 
1 311 VAL n 
1 312 PRO n 
1 313 MET n 
1 314 PHE n 
1 315 PHE n 
1 316 HIS n 
1 317 TRP n 
1 318 PRO n 
1 319 LYS n 
1 320 LYS n 
1 321 ILE n 
1 322 LYS n 
1 323 LYS n 
1 324 ASP n 
1 325 GLN n 
1 326 ARG n 
1 327 PHE n 
1 328 ASP n 
1 329 PHE n 
1 330 PRO n 
1 331 VAL n 
1 332 SER n 
1 333 SER n 
1 334 LEU n 
1 335 ASP n 
1 336 LEU n 
1 337 TYR n 
1 338 PRO n 
1 339 THR n 
1 340 PHE n 
1 341 THR n 
1 342 GLY n 
1 343 LEU n 
1 344 ALA n 
1 345 GLU n 
1 346 ALA n 
1 347 LYS n 
1 348 LEU n 
1 349 PRO n 
1 350 LYS n 
1 351 GLY n 
1 352 LYS n 
1 353 GLN n 
1 354 LEU n 
1 355 ASP n 
1 356 GLY n 
1 357 LYS n 
1 358 ASN n 
1 359 ILE n 
1 360 MET n 
1 361 ASP n 
1 362 ASP n 
1 363 VAL n 
1 364 LEU n 
1 365 LYS n 
1 366 ASN n 
1 367 THR n 
1 368 GLU n 
1 369 PRO n 
1 370 TYR n 
1 371 LYS n 
1 372 ASP n 
1 373 GLU n 
1 374 MET n 
1 375 ILE n 
1 376 TYR n 
1 377 SER n 
1 378 LEU n 
1 379 ARG n 
1 380 TYR n 
1 381 ARG n 
1 382 GLU n 
1 383 GLY n 
1 384 TYR n 
1 385 ASN n 
1 386 ASP n 
1 387 VAL n 
1 388 GLY n 
1 389 ALA n 
1 390 ARG n 
1 391 MET n 
1 392 GLY n 
1 393 ASP n 
1 394 TRP n 
1 395 LYS n 
1 396 ILE n 
1 397 THR n 
1 398 ARG n 
1 399 MET n 
1 400 GLY n 
1 401 ASN n 
1 402 GLU n 
1 403 PRO n 
1 404 TRP n 
1 405 ARG n 
1 406 LEU n 
1 407 HIS n 
1 408 ASN n 
1 409 ILE n 
1 410 THR n 
1 411 GLN n 
1 412 ASP n 
1 413 ILE n 
1 414 GLY n 
1 415 GLU n 
1 416 LYS n 
1 417 LYS n 
1 418 ASN n 
1 419 LEU n 
1 420 ALA n 
1 421 GLY n 
1 422 ARG n 
1 423 TYR n 
1 424 PRO n 
1 425 ASP n 
1 426 ARG n 
1 427 LEU n 
1 428 LYS n 
1 429 GLU n 
1 430 MET n 
1 431 ILE n 
1 432 ALA n 
1 433 LYS n 
1 434 THR n 
1 435 GLN n 
1 436 GLU n 
1 437 TRP n 
1 438 THR n 
1 439 LYS n 
1 440 SER n 
1 441 PHE n 
1 442 VAL n 
1 443 LYS n 
1 444 PRO n 
1 445 LEU n 
1 446 TRP n 
1 447 VAL n 
1 448 TYR n 
1 449 SER n 
1 450 VAL n 
1 451 LYS n 
1 452 ASP n 
1 453 LYS n 
1 454 GLU n 
1 455 LEU n 
1 456 TRP n 
1 457 GLU n 
1 458 SER n 
1 459 GLY n 
1 460 GLN n 
1 461 MET n 
1 462 PRO n 
1 463 ASN n 
1 464 TYR n 
1 465 GLU n 
1 466 ALA n 
1 467 THR n 
1 468 PHE n 
1 469 GLU n 
1 470 VAL n 
1 471 ASP n 
1 472 LYS n 
1 473 LEU n 
1 474 VAL n 
1 475 ASP n 
1 476 SER n 
1 477 PRO n 
1 478 TYR n 
1 479 HIS n 
1 480 LYS 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                   480 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 zobellia_3145 
_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      'Zobellia galactanivorans' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     63186 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                   ?                  'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                  ?                  'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                ?                  'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'           ?                  'C4 H7 N O4'     133.103 
BR  non-polymer         . 'BROMIDE ION'             ?                  'Br -1'          79.904  
CA  non-polymer         . 'CALCIUM ION'             ?                  'Ca 2'           40.078  
CL  non-polymer         . 'CHLORIDE ION'            ?                  'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                  ?                  'C3 H7 N O2 S'   121.158 
DDZ 'L-peptide linking' n '3,3-DIHYDROXY L-ALANINE' 3-HYDROXY-L-SERINE 'C3 H7 N O4'     121.092 
GLN 'L-peptide linking' y GLUTAMINE                 ?                  'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'           ?                  'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                   ?                  'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                 ?                  'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                     ?                  'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                ?                  'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                   ?                  'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                    ?                  'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                ?                  'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE             ?                  'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                   ?                  'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                    ?                  'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                 ?                  'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                ?                  'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                  ?                  'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                    ?                  'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   32  ?   ?   ?   A . n 
A 1 2   GLY 2   33  ?   ?   ?   A . n 
A 1 3   SER 3   34  ?   ?   ?   A . n 
A 1 4   SER 4   35  ?   ?   ?   A . n 
A 1 5   HIS 5   36  ?   ?   ?   A . n 
A 1 6   HIS 6   37  ?   ?   ?   A . n 
A 1 7   HIS 7   38  ?   ?   ?   A . n 
A 1 8   HIS 8   39  ?   ?   ?   A . n 
A 1 9   HIS 9   40  ?   ?   ?   A . n 
A 1 10  HIS 10  41  ?   ?   ?   A . n 
A 1 11  GLY 11  42  ?   ?   ?   A . n 
A 1 12  SER 12  43  ?   ?   ?   A . n 
A 1 13  GLN 13  44  ?   ?   ?   A . n 
A 1 14  GLU 14  45  ?   ?   ?   A . n 
A 1 15  THR 15  46  46  THR THR A . n 
A 1 16  ARG 16  47  47  ARG ARG A . n 
A 1 17  PRO 17  48  48  PRO PRO A . n 
A 1 18  ASN 18  49  49  ASN ASN A . n 
A 1 19  ILE 19  50  50  ILE ILE A . n 
A 1 20  LEU 20  51  51  LEU LEU A . n 
A 1 21  VAL 21  52  52  VAL VAL A . n 
A 1 22  VAL 22  53  53  VAL VAL A . n 
A 1 23  LEU 23  54  54  LEU LEU A . n 
A 1 24  CYS 24  55  55  CYS CYS A . n 
A 1 25  ASP 25  56  56  ASP ASP A . n 
A 1 26  ASP 26  57  57  ASP ASP A . n 
A 1 27  LEU 27  58  58  LEU LEU A . n 
A 1 28  GLY 28  59  59  GLY GLY A . n 
A 1 29  TYR 29  60  60  TYR TYR A . n 
A 1 30  ALA 30  61  61  ALA ALA A . n 
A 1 31  ASP 31  62  62  ASP ASP A . n 
A 1 32  VAL 32  63  63  VAL VAL A . n 
A 1 33  GLY 33  64  64  GLY GLY A . n 
A 1 34  PHE 34  65  65  PHE PHE A . n 
A 1 35  ASN 35  66  66  ASN ASN A . n 
A 1 36  GLY 36  67  67  GLY GLY A . n 
A 1 37  SER 37  68  68  SER SER A . n 
A 1 38  THR 38  69  69  THR THR A . n 
A 1 39  ASP 39  70  70  ASP ASP A . n 
A 1 40  ILE 40  71  71  ILE ILE A . n 
A 1 41  LEU 41  72  72  LEU LEU A . n 
A 1 42  THR 42  73  73  THR THR A . n 
A 1 43  PRO 43  74  74  PRO PRO A . n 
A 1 44  GLU 44  75  75  GLU GLU A . n 
A 1 45  LEU 45  76  76  LEU LEU A . n 
A 1 46  ASP 46  77  77  ASP ASP A . n 
A 1 47  ASN 47  78  78  ASN ASN A . n 
A 1 48  LEU 48  79  79  LEU LEU A . n 
A 1 49  ALA 49  80  80  ALA ALA A . n 
A 1 50  GLN 50  81  81  GLN GLN A . n 
A 1 51  ASN 51  82  82  ASN ASN A . n 
A 1 52  GLY 52  83  83  GLY GLY A . n 
A 1 53  SER 53  84  84  SER SER A . n 
A 1 54  ILE 54  85  85  ILE ILE A . n 
A 1 55  PHE 55  86  86  PHE PHE A . n 
A 1 56  THR 56  87  87  THR THR A . n 
A 1 57  SER 57  88  88  SER SER A . n 
A 1 58  ALA 58  89  89  ALA ALA A . n 
A 1 59  TYR 59  90  90  TYR TYR A . n 
A 1 60  VAL 60  91  91  VAL VAL A . n 
A 1 61  ALA 61  92  92  ALA ALA A . n 
A 1 62  HIS 62  93  93  HIS HIS A . n 
A 1 63  PRO 63  94  94  PRO PRO A . n 
A 1 64  PHE 64  95  95  PHE PHE A . n 
A 1 65  CYS 65  96  96  CYS CYS A . y 
A 1 65  DDZ 65  96  96  DDZ DDZ A . y 
A 1 66  GLY 66  97  97  GLY GLY A . n 
A 1 67  PRO 67  98  98  PRO PRO A . n 
A 1 68  SER 68  99  99  SER SER A . n 
A 1 69  ARG 69  100 100 ARG ARG A . n 
A 1 70  SER 70  101 101 SER SER A . n 
A 1 71  ALA 71  102 102 ALA ALA A . n 
A 1 72  ILE 72  103 103 ILE ILE A . n 
A 1 73  LEU 73  104 104 LEU LEU A . n 
A 1 74  THR 74  105 105 THR THR A . n 
A 1 75  GLY 75  106 106 GLY GLY A . n 
A 1 76  ARG 76  107 107 ARG ARG A . n 
A 1 77  TYR 77  108 108 TYR TYR A . n 
A 1 78  PRO 78  109 109 PRO PRO A . n 
A 1 79  HIS 79  110 110 HIS HIS A . n 
A 1 80  LEU 80  111 111 LEU LEU A . n 
A 1 81  THR 81  112 112 THR THR A . n 
A 1 82  GLY 82  113 113 GLY GLY A . n 
A 1 83  THR 83  114 114 THR THR A . n 
A 1 84  ALA 84  115 115 ALA ALA A . n 
A 1 85  TYR 85  116 116 TYR TYR A . n 
A 1 86  ASN 86  117 117 ASN ASN A . n 
A 1 87  LEU 87  118 118 LEU LEU A . n 
A 1 88  PHE 88  119 119 PHE PHE A . n 
A 1 89  HIS 89  120 120 HIS HIS A . n 
A 1 90  ASN 90  121 121 ASN ASN A . n 
A 1 91  SER 91  122 122 SER SER A . n 
A 1 92  SER 92  123 123 SER SER A . n 
A 1 93  GLU 93  124 124 GLU GLU A . n 
A 1 94  ASP 94  125 125 ASP ASP A . n 
A 1 95  ASP 95  126 126 ASP ASP A . n 
A 1 96  LYS 96  127 127 LYS LYS A . n 
A 1 97  ASP 97  128 128 ASP ASP A . n 
A 1 98  ASN 98  129 129 ASN ASN A . n 
A 1 99  MET 99  130 130 MET MET A . n 
A 1 100 GLY 100 131 131 GLY GLY A . n 
A 1 101 VAL 101 132 132 VAL VAL A . n 
A 1 102 PRO 102 133 133 PRO PRO A . n 
A 1 103 VAL 103 134 134 VAL VAL A . n 
A 1 104 GLU 104 135 135 GLU GLU A . n 
A 1 105 GLU 105 136 136 GLU GLU A . n 
A 1 106 THR 106 137 137 THR THR A . n 
A 1 107 TYR 107 138 138 TYR TYR A . n 
A 1 108 MET 108 139 139 MET MET A . n 
A 1 109 SER 109 140 140 SER SER A . n 
A 1 110 LYS 110 141 141 LYS LYS A . n 
A 1 111 VAL 111 142 142 VAL VAL A . n 
A 1 112 LEU 112 143 143 LEU LEU A . n 
A 1 113 GLN 113 144 144 GLN GLN A . n 
A 1 114 ASN 114 145 145 ASN ASN A . n 
A 1 115 ALA 115 146 146 ALA ALA A . n 
A 1 116 GLY 116 147 147 GLY GLY A . n 
A 1 117 TYR 117 148 148 TYR TYR A . n 
A 1 118 TYR 118 149 149 TYR TYR A . n 
A 1 119 THR 119 150 150 THR THR A . n 
A 1 120 SER 120 151 151 SER SER A . n 
A 1 121 ALA 121 152 152 ALA ALA A . n 
A 1 122 ILE 122 153 153 ILE ILE A . n 
A 1 123 GLY 123 154 154 GLY GLY A . n 
A 1 124 LYS 124 155 155 LYS LYS A . n 
A 1 125 TRP 125 156 156 TRP TRP A . n 
A 1 126 HIS 126 157 157 HIS HIS A . n 
A 1 127 LEU 127 158 158 LEU LEU A . n 
A 1 128 GLY 128 159 159 GLY GLY A . n 
A 1 129 ALA 129 160 160 ALA ALA A . n 
A 1 130 ALA 130 161 161 ALA ALA A . n 
A 1 131 PRO 131 162 162 PRO PRO A . n 
A 1 132 LYS 132 163 163 LYS LYS A . n 
A 1 133 PHE 133 164 164 PHE PHE A . n 
A 1 134 HIS 134 165 165 HIS HIS A . n 
A 1 135 PRO 135 166 166 PRO PRO A . n 
A 1 136 ASN 136 167 167 ASN ASN A . n 
A 1 137 LYS 137 168 168 LYS LYS A . n 
A 1 138 ARG 138 169 169 ARG ARG A . n 
A 1 139 GLY 139 170 170 GLY GLY A . n 
A 1 140 PHE 140 171 171 PHE PHE A . n 
A 1 141 ASP 141 172 172 ASP ASP A . n 
A 1 142 ASP 142 173 173 ASP ASP A . n 
A 1 143 PHE 143 174 174 PHE PHE A . n 
A 1 144 TYR 144 175 175 TYR TYR A . n 
A 1 145 GLY 145 176 176 GLY GLY A . n 
A 1 146 PHE 146 177 177 PHE PHE A . n 
A 1 147 LEU 147 178 178 LEU LEU A . n 
A 1 148 GLY 148 179 179 GLY GLY A . n 
A 1 149 GLY 149 180 180 GLY GLY A . n 
A 1 150 GLY 150 181 181 GLY GLY A . n 
A 1 151 HIS 151 182 182 HIS HIS A . n 
A 1 152 ASP 152 183 183 ASP ASP A . n 
A 1 153 TYR 153 184 184 TYR TYR A . n 
A 1 154 PHE 154 185 185 PHE PHE A . n 
A 1 155 PRO 155 186 186 PRO PRO A . n 
A 1 156 SER 156 187 187 SER SER A . n 
A 1 157 GLU 157 188 188 GLU GLU A . n 
A 1 158 TYR 158 189 189 TYR TYR A . n 
A 1 159 GLN 159 190 190 GLN GLN A . n 
A 1 160 LYS 160 191 191 LYS LYS A . n 
A 1 161 THR 161 192 192 THR THR A . n 
A 1 162 TYR 162 193 193 TYR TYR A . n 
A 1 163 LYS 163 194 194 LYS LYS A . n 
A 1 164 ALA 164 195 195 ALA ALA A . n 
A 1 165 GLN 165 196 196 GLN GLN A . n 
A 1 166 LYS 166 197 197 LYS LYS A . n 
A 1 167 LYS 167 198 198 LYS LYS A . n 
A 1 168 ALA 168 199 199 ALA ALA A . n 
A 1 169 GLY 169 200 200 GLY GLY A . n 
A 1 170 ASN 170 201 201 ASN ASN A . n 
A 1 171 PRO 171 202 202 PRO PRO A . n 
A 1 172 ASN 172 203 203 ASN ASN A . n 
A 1 173 ILE 173 204 204 ILE ILE A . n 
A 1 174 ARG 174 205 205 ARG ARG A . n 
A 1 175 ASP 175 206 206 ASP ASP A . n 
A 1 176 TYR 176 207 207 TYR TYR A . n 
A 1 177 VAL 177 208 208 VAL VAL A . n 
A 1 178 PHE 178 209 209 PHE PHE A . n 
A 1 179 PRO 179 210 210 PRO PRO A . n 
A 1 180 MET 180 211 211 MET MET A . n 
A 1 181 GLU 181 212 212 GLU GLU A . n 
A 1 182 HIS 182 213 213 HIS HIS A . n 
A 1 183 ASN 183 214 214 ASN ASN A . n 
A 1 184 GLY 184 215 215 GLY GLY A . n 
A 1 185 LYS 185 216 216 LYS LYS A . n 
A 1 186 PRO 186 217 217 PRO PRO A . n 
A 1 187 ALA 187 218 218 ALA ALA A . n 
A 1 188 ASN 188 219 219 ASN ASN A . n 
A 1 189 GLU 189 220 220 GLU GLU A . n 
A 1 190 THR 190 221 221 THR THR A . n 
A 1 191 GLU 191 222 222 GLU GLU A . n 
A 1 192 TYR 192 223 223 TYR TYR A . n 
A 1 193 ILE 193 224 224 ILE ILE A . n 
A 1 194 THR 194 225 225 THR THR A . n 
A 1 195 ASP 195 226 226 ASP ASP A . n 
A 1 196 GLY 196 227 227 GLY GLY A . n 
A 1 197 PHE 197 228 228 PHE PHE A . n 
A 1 198 SER 198 229 229 SER SER A . n 
A 1 199 ARG 199 230 230 ARG ARG A . n 
A 1 200 GLU 200 231 231 GLU GLU A . n 
A 1 201 ALA 201 232 232 ALA ALA A . n 
A 1 202 ILE 202 233 233 ILE ILE A . n 
A 1 203 LYS 203 234 234 LYS LYS A . n 
A 1 204 ASN 204 235 235 ASN ASN A . n 
A 1 205 ILE 205 236 236 ILE ILE A . n 
A 1 206 LYS 206 237 237 LYS LYS A . n 
A 1 207 ILE 207 238 238 ILE ILE A . n 
A 1 208 ALA 208 239 239 ALA ALA A . n 
A 1 209 ALA 209 240 240 ALA ALA A . n 
A 1 210 ALA 210 241 241 ALA ALA A . n 
A 1 211 LYS 211 242 242 LYS LYS A . n 
A 1 212 LYS 212 243 243 LYS LYS A . n 
A 1 213 GLN 213 244 244 GLN GLN A . n 
A 1 214 PRO 214 245 245 PRO PRO A . n 
A 1 215 PHE 215 246 246 PHE PHE A . n 
A 1 216 PHE 216 247 247 PHE PHE A . n 
A 1 217 ILE 217 248 248 ILE ILE A . n 
A 1 218 TYR 218 249 249 TYR TYR A . n 
A 1 219 LEU 219 250 250 LEU LEU A . n 
A 1 220 ALA 220 251 251 ALA ALA A . n 
A 1 221 TYR 221 252 252 TYR TYR A . n 
A 1 222 ASN 222 253 253 ASN ASN A . n 
A 1 223 ALA 223 254 254 ALA ALA A . n 
A 1 224 PRO 224 255 255 PRO PRO A . n 
A 1 225 HIS 225 256 256 HIS HIS A . n 
A 1 226 VAL 226 257 257 VAL VAL A . n 
A 1 227 PRO 227 258 258 PRO PRO A . n 
A 1 228 LEU 228 259 259 LEU LEU A . n 
A 1 229 GLN 229 260 260 GLN GLN A . n 
A 1 230 ALA 230 261 261 ALA ALA A . n 
A 1 231 LYS 231 262 262 LYS LYS A . n 
A 1 232 ALA 232 263 263 ALA ALA A . n 
A 1 233 GLU 233 264 264 GLU GLU A . n 
A 1 234 ASP 234 265 265 ASP ASP A . n 
A 1 235 VAL 235 266 266 VAL VAL A . n 
A 1 236 ALA 236 267 267 ALA ALA A . n 
A 1 237 LYS 237 268 268 LYS LYS A . n 
A 1 238 PHE 238 269 269 PHE PHE A . n 
A 1 239 ALA 239 270 270 ALA ALA A . n 
A 1 240 HIS 240 271 271 HIS HIS A . n 
A 1 241 ILE 241 272 272 ILE ILE A . n 
A 1 242 LYS 242 273 273 LYS LYS A . n 
A 1 243 ASP 243 274 274 ASP ASP A . n 
A 1 244 LYS 244 275 275 LYS LYS A . n 
A 1 245 ASP 245 276 276 ASP ASP A . n 
A 1 246 ARG 246 277 277 ARG ARG A . n 
A 1 247 ARG 247 278 278 ARG ARG A . n 
A 1 248 THR 248 279 279 THR THR A . n 
A 1 249 TYR 249 280 280 TYR TYR A . n 
A 1 250 ALA 250 281 281 ALA ALA A . n 
A 1 251 ALA 251 282 282 ALA ALA A . n 
A 1 252 MET 252 283 283 MET MET A . n 
A 1 253 VAL 253 284 284 VAL VAL A . n 
A 1 254 TYR 254 285 285 TYR TYR A . n 
A 1 255 ALA 255 286 286 ALA ALA A . n 
A 1 256 VAL 256 287 287 VAL VAL A . n 
A 1 257 ASP 257 288 288 ASP ASP A . n 
A 1 258 ARG 258 289 289 ARG ARG A . n 
A 1 259 GLY 259 290 290 GLY GLY A . n 
A 1 260 VAL 260 291 291 VAL VAL A . n 
A 1 261 GLY 261 292 292 GLY GLY A . n 
A 1 262 LYS 262 293 293 LYS LYS A . n 
A 1 263 ILE 263 294 294 ILE ILE A . n 
A 1 264 VAL 264 295 295 VAL VAL A . n 
A 1 265 GLN 265 296 296 GLN GLN A . n 
A 1 266 THR 266 297 297 THR THR A . n 
A 1 267 LEU 267 298 298 LEU LEU A . n 
A 1 268 LYS 268 299 299 LYS LYS A . n 
A 1 269 GLU 269 300 300 GLU GLU A . n 
A 1 270 THR 270 301 301 THR THR A . n 
A 1 271 LYS 271 302 302 LYS LYS A . n 
A 1 272 GLN 272 303 303 GLN GLN A . n 
A 1 273 PHE 273 304 304 PHE PHE A . n 
A 1 274 ASP 274 305 305 ASP ASP A . n 
A 1 275 ASN 275 306 306 ASN ASN A . n 
A 1 276 THR 276 307 307 THR THR A . n 
A 1 277 LEU 277 308 308 LEU LEU A . n 
A 1 278 ILE 278 309 309 ILE ILE A . n 
A 1 279 VAL 279 310 310 VAL VAL A . n 
A 1 280 PHE 280 311 311 PHE PHE A . n 
A 1 281 LEU 281 312 312 LEU LEU A . n 
A 1 282 SER 282 313 313 SER SER A . n 
A 1 283 ASP 283 314 314 ASP ASP A . n 
A 1 284 ASN 284 315 315 ASN ASN A . n 
A 1 285 GLY 285 316 316 GLY GLY A . n 
A 1 286 GLY 286 317 317 GLY GLY A . n 
A 1 287 ASN 287 318 318 ASN ASN A . n 
A 1 288 PHE 288 319 319 PHE PHE A . n 
A 1 289 ASN 289 320 320 ASN ASN A . n 
A 1 290 HIS 290 321 321 HIS HIS A . n 
A 1 291 GLY 291 322 322 GLY GLY A . n 
A 1 292 ALA 292 323 323 ALA ALA A . n 
A 1 293 ASN 293 324 324 ASN ASN A . n 
A 1 294 ASN 294 325 325 ASN ASN A . n 
A 1 295 TYR 295 326 326 TYR TYR A . n 
A 1 296 PRO 296 327 327 PRO PRO A . n 
A 1 297 LEU 297 328 328 LEU LEU A . n 
A 1 298 LYS 298 329 329 LYS LYS A . n 
A 1 299 GLY 299 330 330 GLY GLY A . n 
A 1 300 THR 300 331 331 THR THR A . n 
A 1 301 LYS 301 332 332 LYS LYS A . n 
A 1 302 GLY 302 333 333 GLY GLY A . n 
A 1 303 ASP 303 334 334 ASP ASP A . n 
A 1 304 THR 304 335 335 THR THR A . n 
A 1 305 TRP 305 336 336 TRP TRP A . n 
A 1 306 GLU 306 337 337 GLU GLU A . n 
A 1 307 GLY 307 338 338 GLY GLY A . n 
A 1 308 GLY 308 339 339 GLY GLY A . n 
A 1 309 TYR 309 340 340 TYR TYR A . n 
A 1 310 ARG 310 341 341 ARG ARG A . n 
A 1 311 VAL 311 342 342 VAL VAL A . n 
A 1 312 PRO 312 343 343 PRO PRO A . n 
A 1 313 MET 313 344 344 MET MET A . n 
A 1 314 PHE 314 345 345 PHE PHE A . n 
A 1 315 PHE 315 346 346 PHE PHE A . n 
A 1 316 HIS 316 347 347 HIS HIS A . n 
A 1 317 TRP 317 348 348 TRP TRP A . n 
A 1 318 PRO 318 349 349 PRO PRO A . n 
A 1 319 LYS 319 350 350 LYS LYS A . n 
A 1 320 LYS 320 351 351 LYS LYS A . n 
A 1 321 ILE 321 352 352 ILE ILE A . n 
A 1 322 LYS 322 353 353 LYS LYS A . n 
A 1 323 LYS 323 354 354 LYS LYS A . n 
A 1 324 ASP 324 355 355 ASP ASP A . n 
A 1 325 GLN 325 356 356 GLN GLN A . n 
A 1 326 ARG 326 357 357 ARG ARG A . n 
A 1 327 PHE 327 358 358 PHE PHE A . n 
A 1 328 ASP 328 359 359 ASP ASP A . n 
A 1 329 PHE 329 360 360 PHE PHE A . n 
A 1 330 PRO 330 361 361 PRO PRO A . n 
A 1 331 VAL 331 362 362 VAL VAL A . n 
A 1 332 SER 332 363 363 SER SER A . n 
A 1 333 SER 333 364 364 SER SER A . n 
A 1 334 LEU 334 365 365 LEU LEU A . n 
A 1 335 ASP 335 366 366 ASP ASP A . n 
A 1 336 LEU 336 367 367 LEU LEU A . n 
A 1 337 TYR 337 368 368 TYR TYR A . n 
A 1 338 PRO 338 369 369 PRO PRO A . n 
A 1 339 THR 339 370 370 THR THR A . n 
A 1 340 PHE 340 371 371 PHE PHE A . n 
A 1 341 THR 341 372 372 THR THR A . n 
A 1 342 GLY 342 373 373 GLY GLY A . n 
A 1 343 LEU 343 374 374 LEU LEU A . n 
A 1 344 ALA 344 375 375 ALA ALA A . n 
A 1 345 GLU 345 376 376 GLU GLU A . n 
A 1 346 ALA 346 377 377 ALA ALA A . n 
A 1 347 LYS 347 378 378 LYS LYS A . n 
A 1 348 LEU 348 379 379 LEU LEU A . n 
A 1 349 PRO 349 380 380 PRO PRO A . n 
A 1 350 LYS 350 381 381 LYS LYS A . n 
A 1 351 GLY 351 382 382 GLY GLY A . n 
A 1 352 LYS 352 383 383 LYS LYS A . n 
A 1 353 GLN 353 384 384 GLN GLN A . n 
A 1 354 LEU 354 385 385 LEU LEU A . n 
A 1 355 ASP 355 386 386 ASP ASP A . n 
A 1 356 GLY 356 387 387 GLY GLY A . n 
A 1 357 LYS 357 388 388 LYS LYS A . n 
A 1 358 ASN 358 389 389 ASN ASN A . n 
A 1 359 ILE 359 390 390 ILE ILE A . n 
A 1 360 MET 360 391 391 MET MET A . n 
A 1 361 ASP 361 392 392 ASP ASP A . n 
A 1 362 ASP 362 393 393 ASP ASP A . n 
A 1 363 VAL 363 394 394 VAL VAL A . n 
A 1 364 LEU 364 395 395 LEU LEU A . n 
A 1 365 LYS 365 396 396 LYS LYS A . n 
A 1 366 ASN 366 397 397 ASN ASN A . n 
A 1 367 THR 367 398 398 THR THR A . n 
A 1 368 GLU 368 399 399 GLU GLU A . n 
A 1 369 PRO 369 400 400 PRO PRO A . n 
A 1 370 TYR 370 401 401 TYR TYR A . n 
A 1 371 LYS 371 402 402 LYS LYS A . n 
A 1 372 ASP 372 403 403 ASP ASP A . n 
A 1 373 GLU 373 404 404 GLU GLU A . n 
A 1 374 MET 374 405 405 MET MET A . n 
A 1 375 ILE 375 406 406 ILE ILE A . n 
A 1 376 TYR 376 407 407 TYR TYR A . n 
A 1 377 SER 377 408 408 SER SER A . n 
A 1 378 LEU 378 409 409 LEU LEU A . n 
A 1 379 ARG 379 410 410 ARG ARG A . n 
A 1 380 TYR 380 411 411 TYR TYR A . n 
A 1 381 ARG 381 412 412 ARG ARG A . n 
A 1 382 GLU 382 413 413 GLU GLU A . n 
A 1 383 GLY 383 414 414 GLY GLY A . n 
A 1 384 TYR 384 415 415 TYR TYR A . n 
A 1 385 ASN 385 416 416 ASN ASN A . n 
A 1 386 ASP 386 417 417 ASP ASP A . n 
A 1 387 VAL 387 418 418 VAL VAL A . n 
A 1 388 GLY 388 419 419 GLY GLY A . n 
A 1 389 ALA 389 420 420 ALA ALA A . n 
A 1 390 ARG 390 421 421 ARG ARG A . n 
A 1 391 MET 391 422 422 MET MET A . n 
A 1 392 GLY 392 423 423 GLY GLY A . n 
A 1 393 ASP 393 424 424 ASP ASP A . n 
A 1 394 TRP 394 425 425 TRP TRP A . n 
A 1 395 LYS 395 426 426 LYS LYS A . n 
A 1 396 ILE 396 427 427 ILE ILE A . n 
A 1 397 THR 397 428 428 THR THR A . n 
A 1 398 ARG 398 429 429 ARG ARG A . n 
A 1 399 MET 399 430 430 MET MET A . n 
A 1 400 GLY 400 431 431 GLY GLY A . n 
A 1 401 ASN 401 432 432 ASN ASN A . n 
A 1 402 GLU 402 433 433 GLU GLU A . n 
A 1 403 PRO 403 434 434 PRO PRO A . n 
A 1 404 TRP 404 435 435 TRP TRP A . n 
A 1 405 ARG 405 436 436 ARG ARG A . n 
A 1 406 LEU 406 437 437 LEU LEU A . n 
A 1 407 HIS 407 438 438 HIS HIS A . n 
A 1 408 ASN 408 439 439 ASN ASN A . n 
A 1 409 ILE 409 440 440 ILE ILE A . n 
A 1 410 THR 410 441 441 THR THR A . n 
A 1 411 GLN 411 442 442 GLN GLN A . n 
A 1 412 ASP 412 443 443 ASP ASP A . n 
A 1 413 ILE 413 444 444 ILE ILE A . n 
A 1 414 GLY 414 445 445 GLY GLY A . n 
A 1 415 GLU 415 446 446 GLU GLU A . n 
A 1 416 LYS 416 447 447 LYS LYS A . n 
A 1 417 LYS 417 448 448 LYS LYS A . n 
A 1 418 ASN 418 449 449 ASN ASN A . n 
A 1 419 LEU 419 450 450 LEU LEU A . n 
A 1 420 ALA 420 451 451 ALA ALA A . n 
A 1 421 GLY 421 452 452 GLY GLY A . n 
A 1 422 ARG 422 453 453 ARG ARG A . n 
A 1 423 TYR 423 454 454 TYR TYR A . n 
A 1 424 PRO 424 455 455 PRO PRO A . n 
A 1 425 ASP 425 456 456 ASP ASP A . n 
A 1 426 ARG 426 457 457 ARG ARG A . n 
A 1 427 LEU 427 458 458 LEU LEU A . n 
A 1 428 LYS 428 459 459 LYS LYS A . n 
A 1 429 GLU 429 460 460 GLU GLU A . n 
A 1 430 MET 430 461 461 MET MET A . n 
A 1 431 ILE 431 462 462 ILE ILE A . n 
A 1 432 ALA 432 463 463 ALA ALA A . n 
A 1 433 LYS 433 464 464 LYS LYS A . n 
A 1 434 THR 434 465 465 THR THR A . n 
A 1 435 GLN 435 466 466 GLN GLN A . n 
A 1 436 GLU 436 467 467 GLU GLU A . n 
A 1 437 TRP 437 468 468 TRP TRP A . n 
A 1 438 THR 438 469 469 THR THR A . n 
A 1 439 LYS 439 470 470 LYS LYS A . n 
A 1 440 SER 440 471 471 SER SER A . n 
A 1 441 PHE 441 472 472 PHE PHE A . n 
A 1 442 VAL 442 473 473 VAL VAL A . n 
A 1 443 LYS 443 474 474 LYS LYS A . n 
A 1 444 PRO 444 475 475 PRO PRO A . n 
A 1 445 LEU 445 476 476 LEU LEU A . n 
A 1 446 TRP 446 477 477 TRP TRP A . n 
A 1 447 VAL 447 478 478 VAL VAL A . n 
A 1 448 TYR 448 479 479 TYR TYR A . n 
A 1 449 SER 449 480 480 SER SER A . n 
A 1 450 VAL 450 481 481 VAL VAL A . n 
A 1 451 LYS 451 482 482 LYS LYS A . n 
A 1 452 ASP 452 483 483 ASP ASP A . n 
A 1 453 LYS 453 484 484 LYS LYS A . n 
A 1 454 GLU 454 485 485 GLU GLU A . n 
A 1 455 LEU 455 486 486 LEU LEU A . n 
A 1 456 TRP 456 487 487 TRP TRP A . n 
A 1 457 GLU 457 488 488 GLU GLU A . n 
A 1 458 SER 458 489 489 SER SER A . n 
A 1 459 GLY 459 490 490 GLY GLY A . n 
A 1 460 GLN 460 491 491 GLN GLN A . n 
A 1 461 MET 461 492 492 MET MET A . n 
A 1 462 PRO 462 493 493 PRO PRO A . n 
A 1 463 ASN 463 494 494 ASN ASN A . n 
A 1 464 TYR 464 495 495 TYR TYR A . n 
A 1 465 GLU 465 496 496 GLU GLU A . n 
A 1 466 ALA 466 497 497 ALA ALA A . n 
A 1 467 THR 467 498 498 THR THR A . n 
A 1 468 PHE 468 499 499 PHE PHE A . n 
A 1 469 GLU 469 500 500 GLU GLU A . n 
A 1 470 VAL 470 501 501 VAL VAL A . n 
A 1 471 ASP 471 502 502 ASP ASP A . n 
A 1 472 LYS 472 503 503 LYS LYS A . n 
A 1 473 LEU 473 504 504 LEU LEU A . n 
A 1 474 VAL 474 505 505 VAL VAL A . n 
A 1 475 ASP 475 506 506 ASP ASP A . n 
A 1 476 SER 476 507 507 SER SER A . n 
A 1 477 PRO 477 508 508 PRO PRO A . n 
A 1 478 TYR 478 509 509 TYR TYR A . n 
A 1 479 HIS 479 510 ?   ?   ?   A . n 
A 1 480 LYS 480 511 ?   ?   ?   A . n 
B 1 1   MET 1   32  ?   ?   ?   B . n 
B 1 2   GLY 2   33  ?   ?   ?   B . n 
B 1 3   SER 3   34  ?   ?   ?   B . n 
B 1 4   SER 4   35  ?   ?   ?   B . n 
B 1 5   HIS 5   36  ?   ?   ?   B . n 
B 1 6   HIS 6   37  ?   ?   ?   B . n 
B 1 7   HIS 7   38  ?   ?   ?   B . n 
B 1 8   HIS 8   39  ?   ?   ?   B . n 
B 1 9   HIS 9   40  ?   ?   ?   B . n 
B 1 10  HIS 10  41  ?   ?   ?   B . n 
B 1 11  GLY 11  42  ?   ?   ?   B . n 
B 1 12  SER 12  43  ?   ?   ?   B . n 
B 1 13  GLN 13  44  ?   ?   ?   B . n 
B 1 14  GLU 14  45  ?   ?   ?   B . n 
B 1 15  THR 15  46  46  THR THR B . n 
B 1 16  ARG 16  47  47  ARG ARG B . n 
B 1 17  PRO 17  48  48  PRO PRO B . n 
B 1 18  ASN 18  49  49  ASN ASN B . n 
B 1 19  ILE 19  50  50  ILE ILE B . n 
B 1 20  LEU 20  51  51  LEU LEU B . n 
B 1 21  VAL 21  52  52  VAL VAL B . n 
B 1 22  VAL 22  53  53  VAL VAL B . n 
B 1 23  LEU 23  54  54  LEU LEU B . n 
B 1 24  CYS 24  55  55  CYS CYS B . n 
B 1 25  ASP 25  56  56  ASP ASP B . n 
B 1 26  ASP 26  57  57  ASP ASP B . n 
B 1 27  LEU 27  58  58  LEU LEU B . n 
B 1 28  GLY 28  59  59  GLY GLY B . n 
B 1 29  TYR 29  60  60  TYR TYR B . n 
B 1 30  ALA 30  61  61  ALA ALA B . n 
B 1 31  ASP 31  62  62  ASP ASP B . n 
B 1 32  VAL 32  63  63  VAL VAL B . n 
B 1 33  GLY 33  64  64  GLY GLY B . n 
B 1 34  PHE 34  65  65  PHE PHE B . n 
B 1 35  ASN 35  66  66  ASN ASN B . n 
B 1 36  GLY 36  67  67  GLY GLY B . n 
B 1 37  SER 37  68  68  SER SER B . n 
B 1 38  THR 38  69  69  THR THR B . n 
B 1 39  ASP 39  70  70  ASP ASP B . n 
B 1 40  ILE 40  71  71  ILE ILE B . n 
B 1 41  LEU 41  72  72  LEU LEU B . n 
B 1 42  THR 42  73  73  THR THR B . n 
B 1 43  PRO 43  74  74  PRO PRO B . n 
B 1 44  GLU 44  75  75  GLU GLU B . n 
B 1 45  LEU 45  76  76  LEU LEU B . n 
B 1 46  ASP 46  77  77  ASP ASP B . n 
B 1 47  ASN 47  78  78  ASN ASN B . n 
B 1 48  LEU 48  79  79  LEU LEU B . n 
B 1 49  ALA 49  80  80  ALA ALA B . n 
B 1 50  GLN 50  81  81  GLN GLN B . n 
B 1 51  ASN 51  82  82  ASN ASN B . n 
B 1 52  GLY 52  83  83  GLY GLY B . n 
B 1 53  SER 53  84  84  SER SER B . n 
B 1 54  ILE 54  85  85  ILE ILE B . n 
B 1 55  PHE 55  86  86  PHE PHE B . n 
B 1 56  THR 56  87  87  THR THR B . n 
B 1 57  SER 57  88  88  SER SER B . n 
B 1 58  ALA 58  89  89  ALA ALA B . n 
B 1 59  TYR 59  90  90  TYR TYR B . n 
B 1 60  VAL 60  91  91  VAL VAL B . n 
B 1 61  ALA 61  92  92  ALA ALA B . n 
B 1 62  HIS 62  93  93  HIS HIS B . n 
B 1 63  PRO 63  94  94  PRO PRO B . n 
B 1 64  PHE 64  95  95  PHE PHE B . n 
B 1 65  CYS 65  96  96  CYS CYS B . y 
B 1 65  DDZ 65  96  96  DDZ DDZ B . y 
B 1 66  GLY 66  97  97  GLY GLY B . n 
B 1 67  PRO 67  98  98  PRO PRO B . n 
B 1 68  SER 68  99  99  SER SER B . n 
B 1 69  ARG 69  100 100 ARG ARG B . n 
B 1 70  SER 70  101 101 SER SER B . n 
B 1 71  ALA 71  102 102 ALA ALA B . n 
B 1 72  ILE 72  103 103 ILE ILE B . n 
B 1 73  LEU 73  104 104 LEU LEU B . n 
B 1 74  THR 74  105 105 THR THR B . n 
B 1 75  GLY 75  106 106 GLY GLY B . n 
B 1 76  ARG 76  107 107 ARG ARG B . n 
B 1 77  TYR 77  108 108 TYR TYR B . n 
B 1 78  PRO 78  109 109 PRO PRO B . n 
B 1 79  HIS 79  110 110 HIS HIS B . n 
B 1 80  LEU 80  111 111 LEU LEU B . n 
B 1 81  THR 81  112 112 THR THR B . n 
B 1 82  GLY 82  113 113 GLY GLY B . n 
B 1 83  THR 83  114 114 THR THR B . n 
B 1 84  ALA 84  115 115 ALA ALA B . n 
B 1 85  TYR 85  116 116 TYR TYR B . n 
B 1 86  ASN 86  117 117 ASN ASN B . n 
B 1 87  LEU 87  118 118 LEU LEU B . n 
B 1 88  PHE 88  119 119 PHE PHE B . n 
B 1 89  HIS 89  120 120 HIS HIS B . n 
B 1 90  ASN 90  121 121 ASN ASN B . n 
B 1 91  SER 91  122 122 SER SER B . n 
B 1 92  SER 92  123 123 SER SER B . n 
B 1 93  GLU 93  124 124 GLU GLU B . n 
B 1 94  ASP 94  125 125 ASP ASP B . n 
B 1 95  ASP 95  126 126 ASP ASP B . n 
B 1 96  LYS 96  127 127 LYS LYS B . n 
B 1 97  ASP 97  128 128 ASP ASP B . n 
B 1 98  ASN 98  129 129 ASN ASN B . n 
B 1 99  MET 99  130 130 MET MET B . n 
B 1 100 GLY 100 131 131 GLY GLY B . n 
B 1 101 VAL 101 132 132 VAL VAL B . n 
B 1 102 PRO 102 133 133 PRO PRO B . n 
B 1 103 VAL 103 134 134 VAL VAL B . n 
B 1 104 GLU 104 135 135 GLU GLU B . n 
B 1 105 GLU 105 136 136 GLU GLU B . n 
B 1 106 THR 106 137 137 THR THR B . n 
B 1 107 TYR 107 138 138 TYR TYR B . n 
B 1 108 MET 108 139 139 MET MET B . n 
B 1 109 SER 109 140 140 SER SER B . n 
B 1 110 LYS 110 141 141 LYS LYS B . n 
B 1 111 VAL 111 142 142 VAL VAL B . n 
B 1 112 LEU 112 143 143 LEU LEU B . n 
B 1 113 GLN 113 144 144 GLN GLN B . n 
B 1 114 ASN 114 145 145 ASN ASN B . n 
B 1 115 ALA 115 146 146 ALA ALA B . n 
B 1 116 GLY 116 147 147 GLY GLY B . n 
B 1 117 TYR 117 148 148 TYR TYR B . n 
B 1 118 TYR 118 149 149 TYR TYR B . n 
B 1 119 THR 119 150 150 THR THR B . n 
B 1 120 SER 120 151 151 SER SER B . n 
B 1 121 ALA 121 152 152 ALA ALA B . n 
B 1 122 ILE 122 153 153 ILE ILE B . n 
B 1 123 GLY 123 154 154 GLY GLY B . n 
B 1 124 LYS 124 155 155 LYS LYS B . n 
B 1 125 TRP 125 156 156 TRP TRP B . n 
B 1 126 HIS 126 157 157 HIS HIS B . n 
B 1 127 LEU 127 158 158 LEU LEU B . n 
B 1 128 GLY 128 159 159 GLY GLY B . n 
B 1 129 ALA 129 160 160 ALA ALA B . n 
B 1 130 ALA 130 161 161 ALA ALA B . n 
B 1 131 PRO 131 162 162 PRO PRO B . n 
B 1 132 LYS 132 163 163 LYS LYS B . n 
B 1 133 PHE 133 164 164 PHE PHE B . n 
B 1 134 HIS 134 165 165 HIS HIS B . n 
B 1 135 PRO 135 166 166 PRO PRO B . n 
B 1 136 ASN 136 167 167 ASN ASN B . n 
B 1 137 LYS 137 168 168 LYS LYS B . n 
B 1 138 ARG 138 169 169 ARG ARG B . n 
B 1 139 GLY 139 170 170 GLY GLY B . n 
B 1 140 PHE 140 171 171 PHE PHE B . n 
B 1 141 ASP 141 172 172 ASP ASP B . n 
B 1 142 ASP 142 173 173 ASP ASP B . n 
B 1 143 PHE 143 174 174 PHE PHE B . n 
B 1 144 TYR 144 175 175 TYR TYR B . n 
B 1 145 GLY 145 176 176 GLY GLY B . n 
B 1 146 PHE 146 177 177 PHE PHE B . n 
B 1 147 LEU 147 178 178 LEU LEU B . n 
B 1 148 GLY 148 179 179 GLY GLY B . n 
B 1 149 GLY 149 180 180 GLY GLY B . n 
B 1 150 GLY 150 181 181 GLY GLY B . n 
B 1 151 HIS 151 182 182 HIS HIS B . n 
B 1 152 ASP 152 183 183 ASP ASP B . n 
B 1 153 TYR 153 184 184 TYR TYR B . n 
B 1 154 PHE 154 185 185 PHE PHE B . n 
B 1 155 PRO 155 186 186 PRO PRO B . n 
B 1 156 SER 156 187 187 SER SER B . n 
B 1 157 GLU 157 188 188 GLU GLU B . n 
B 1 158 TYR 158 189 189 TYR TYR B . n 
B 1 159 GLN 159 190 190 GLN GLN B . n 
B 1 160 LYS 160 191 191 LYS LYS B . n 
B 1 161 THR 161 192 192 THR THR B . n 
B 1 162 TYR 162 193 193 TYR TYR B . n 
B 1 163 LYS 163 194 194 LYS LYS B . n 
B 1 164 ALA 164 195 195 ALA ALA B . n 
B 1 165 GLN 165 196 196 GLN GLN B . n 
B 1 166 LYS 166 197 197 LYS LYS B . n 
B 1 167 LYS 167 198 198 LYS LYS B . n 
B 1 168 ALA 168 199 199 ALA ALA B . n 
B 1 169 GLY 169 200 200 GLY GLY B . n 
B 1 170 ASN 170 201 201 ASN ASN B . n 
B 1 171 PRO 171 202 202 PRO PRO B . n 
B 1 172 ASN 172 203 203 ASN ASN B . n 
B 1 173 ILE 173 204 204 ILE ILE B . n 
B 1 174 ARG 174 205 205 ARG ARG B . n 
B 1 175 ASP 175 206 206 ASP ASP B . n 
B 1 176 TYR 176 207 207 TYR TYR B . n 
B 1 177 VAL 177 208 208 VAL VAL B . n 
B 1 178 PHE 178 209 209 PHE PHE B . n 
B 1 179 PRO 179 210 210 PRO PRO B . n 
B 1 180 MET 180 211 211 MET MET B . n 
B 1 181 GLU 181 212 212 GLU GLU B . n 
B 1 182 HIS 182 213 213 HIS HIS B . n 
B 1 183 ASN 183 214 214 ASN ASN B . n 
B 1 184 GLY 184 215 215 GLY GLY B . n 
B 1 185 LYS 185 216 216 LYS LYS B . n 
B 1 186 PRO 186 217 217 PRO PRO B . n 
B 1 187 ALA 187 218 218 ALA ALA B . n 
B 1 188 ASN 188 219 219 ASN ASN B . n 
B 1 189 GLU 189 220 220 GLU GLU B . n 
B 1 190 THR 190 221 221 THR THR B . n 
B 1 191 GLU 191 222 222 GLU GLU B . n 
B 1 192 TYR 192 223 223 TYR TYR B . n 
B 1 193 ILE 193 224 224 ILE ILE B . n 
B 1 194 THR 194 225 225 THR THR B . n 
B 1 195 ASP 195 226 226 ASP ASP B . n 
B 1 196 GLY 196 227 227 GLY GLY B . n 
B 1 197 PHE 197 228 228 PHE PHE B . n 
B 1 198 SER 198 229 229 SER SER B . n 
B 1 199 ARG 199 230 230 ARG ARG B . n 
B 1 200 GLU 200 231 231 GLU GLU B . n 
B 1 201 ALA 201 232 232 ALA ALA B . n 
B 1 202 ILE 202 233 233 ILE ILE B . n 
B 1 203 LYS 203 234 234 LYS LYS B . n 
B 1 204 ASN 204 235 235 ASN ASN B . n 
B 1 205 ILE 205 236 236 ILE ILE B . n 
B 1 206 LYS 206 237 237 LYS LYS B . n 
B 1 207 ILE 207 238 238 ILE ILE B . n 
B 1 208 ALA 208 239 239 ALA ALA B . n 
B 1 209 ALA 209 240 240 ALA ALA B . n 
B 1 210 ALA 210 241 241 ALA ALA B . n 
B 1 211 LYS 211 242 242 LYS LYS B . n 
B 1 212 LYS 212 243 243 LYS LYS B . n 
B 1 213 GLN 213 244 244 GLN GLN B . n 
B 1 214 PRO 214 245 245 PRO PRO B . n 
B 1 215 PHE 215 246 246 PHE PHE B . n 
B 1 216 PHE 216 247 247 PHE PHE B . n 
B 1 217 ILE 217 248 248 ILE ILE B . n 
B 1 218 TYR 218 249 249 TYR TYR B . n 
B 1 219 LEU 219 250 250 LEU LEU B . n 
B 1 220 ALA 220 251 251 ALA ALA B . n 
B 1 221 TYR 221 252 252 TYR TYR B . n 
B 1 222 ASN 222 253 253 ASN ASN B . n 
B 1 223 ALA 223 254 254 ALA ALA B . n 
B 1 224 PRO 224 255 255 PRO PRO B . n 
B 1 225 HIS 225 256 256 HIS HIS B . n 
B 1 226 VAL 226 257 257 VAL VAL B . n 
B 1 227 PRO 227 258 258 PRO PRO B . n 
B 1 228 LEU 228 259 259 LEU LEU B . n 
B 1 229 GLN 229 260 260 GLN GLN B . n 
B 1 230 ALA 230 261 261 ALA ALA B . n 
B 1 231 LYS 231 262 262 LYS LYS B . n 
B 1 232 ALA 232 263 263 ALA ALA B . n 
B 1 233 GLU 233 264 264 GLU GLU B . n 
B 1 234 ASP 234 265 265 ASP ASP B . n 
B 1 235 VAL 235 266 266 VAL VAL B . n 
B 1 236 ALA 236 267 267 ALA ALA B . n 
B 1 237 LYS 237 268 268 LYS LYS B . n 
B 1 238 PHE 238 269 269 PHE PHE B . n 
B 1 239 ALA 239 270 270 ALA ALA B . n 
B 1 240 HIS 240 271 271 HIS HIS B . n 
B 1 241 ILE 241 272 272 ILE ILE B . n 
B 1 242 LYS 242 273 273 LYS LYS B . n 
B 1 243 ASP 243 274 274 ASP ASP B . n 
B 1 244 LYS 244 275 275 LYS LYS B . n 
B 1 245 ASP 245 276 276 ASP ASP B . n 
B 1 246 ARG 246 277 277 ARG ARG B . n 
B 1 247 ARG 247 278 278 ARG ARG B . n 
B 1 248 THR 248 279 279 THR THR B . n 
B 1 249 TYR 249 280 280 TYR TYR B . n 
B 1 250 ALA 250 281 281 ALA ALA B . n 
B 1 251 ALA 251 282 282 ALA ALA B . n 
B 1 252 MET 252 283 283 MET MET B . n 
B 1 253 VAL 253 284 284 VAL VAL B . n 
B 1 254 TYR 254 285 285 TYR TYR B . n 
B 1 255 ALA 255 286 286 ALA ALA B . n 
B 1 256 VAL 256 287 287 VAL VAL B . n 
B 1 257 ASP 257 288 288 ASP ASP B . n 
B 1 258 ARG 258 289 289 ARG ARG B . n 
B 1 259 GLY 259 290 290 GLY GLY B . n 
B 1 260 VAL 260 291 291 VAL VAL B . n 
B 1 261 GLY 261 292 292 GLY GLY B . n 
B 1 262 LYS 262 293 293 LYS LYS B . n 
B 1 263 ILE 263 294 294 ILE ILE B . n 
B 1 264 VAL 264 295 295 VAL VAL B . n 
B 1 265 GLN 265 296 296 GLN GLN B . n 
B 1 266 THR 266 297 297 THR THR B . n 
B 1 267 LEU 267 298 298 LEU LEU B . n 
B 1 268 LYS 268 299 299 LYS LYS B . n 
B 1 269 GLU 269 300 300 GLU GLU B . n 
B 1 270 THR 270 301 301 THR THR B . n 
B 1 271 LYS 271 302 302 LYS LYS B . n 
B 1 272 GLN 272 303 303 GLN GLN B . n 
B 1 273 PHE 273 304 304 PHE PHE B . n 
B 1 274 ASP 274 305 305 ASP ASP B . n 
B 1 275 ASN 275 306 306 ASN ASN B . n 
B 1 276 THR 276 307 307 THR THR B . n 
B 1 277 LEU 277 308 308 LEU LEU B . n 
B 1 278 ILE 278 309 309 ILE ILE B . n 
B 1 279 VAL 279 310 310 VAL VAL B . n 
B 1 280 PHE 280 311 311 PHE PHE B . n 
B 1 281 LEU 281 312 312 LEU LEU B . n 
B 1 282 SER 282 313 313 SER SER B . n 
B 1 283 ASP 283 314 314 ASP ASP B . n 
B 1 284 ASN 284 315 315 ASN ASN B . n 
B 1 285 GLY 285 316 316 GLY GLY B . n 
B 1 286 GLY 286 317 317 GLY GLY B . n 
B 1 287 ASN 287 318 318 ASN ASN B . n 
B 1 288 PHE 288 319 319 PHE PHE B . n 
B 1 289 ASN 289 320 320 ASN ASN B . n 
B 1 290 HIS 290 321 321 HIS HIS B . n 
B 1 291 GLY 291 322 322 GLY GLY B . n 
B 1 292 ALA 292 323 323 ALA ALA B . n 
B 1 293 ASN 293 324 324 ASN ASN B . n 
B 1 294 ASN 294 325 325 ASN ASN B . n 
B 1 295 TYR 295 326 326 TYR TYR B . n 
B 1 296 PRO 296 327 327 PRO PRO B . n 
B 1 297 LEU 297 328 328 LEU LEU B . n 
B 1 298 LYS 298 329 329 LYS LYS B . n 
B 1 299 GLY 299 330 330 GLY GLY B . n 
B 1 300 THR 300 331 331 THR THR B . n 
B 1 301 LYS 301 332 332 LYS LYS B . n 
B 1 302 GLY 302 333 333 GLY GLY B . n 
B 1 303 ASP 303 334 334 ASP ASP B . n 
B 1 304 THR 304 335 335 THR THR B . n 
B 1 305 TRP 305 336 336 TRP TRP B . n 
B 1 306 GLU 306 337 337 GLU GLU B . n 
B 1 307 GLY 307 338 338 GLY GLY B . n 
B 1 308 GLY 308 339 339 GLY GLY B . n 
B 1 309 TYR 309 340 340 TYR TYR B . n 
B 1 310 ARG 310 341 341 ARG ARG B . n 
B 1 311 VAL 311 342 342 VAL VAL B . n 
B 1 312 PRO 312 343 343 PRO PRO B . n 
B 1 313 MET 313 344 344 MET MET B . n 
B 1 314 PHE 314 345 345 PHE PHE B . n 
B 1 315 PHE 315 346 346 PHE PHE B . n 
B 1 316 HIS 316 347 347 HIS HIS B . n 
B 1 317 TRP 317 348 348 TRP TRP B . n 
B 1 318 PRO 318 349 349 PRO PRO B . n 
B 1 319 LYS 319 350 350 LYS LYS B . n 
B 1 320 LYS 320 351 351 LYS LYS B . n 
B 1 321 ILE 321 352 352 ILE ILE B . n 
B 1 322 LYS 322 353 353 LYS LYS B . n 
B 1 323 LYS 323 354 354 LYS LYS B . n 
B 1 324 ASP 324 355 355 ASP ASP B . n 
B 1 325 GLN 325 356 356 GLN GLN B . n 
B 1 326 ARG 326 357 357 ARG ARG B . n 
B 1 327 PHE 327 358 358 PHE PHE B . n 
B 1 328 ASP 328 359 359 ASP ASP B . n 
B 1 329 PHE 329 360 360 PHE PHE B . n 
B 1 330 PRO 330 361 361 PRO PRO B . n 
B 1 331 VAL 331 362 362 VAL VAL B . n 
B 1 332 SER 332 363 363 SER SER B . n 
B 1 333 SER 333 364 364 SER SER B . n 
B 1 334 LEU 334 365 365 LEU LEU B . n 
B 1 335 ASP 335 366 366 ASP ASP B . n 
B 1 336 LEU 336 367 367 LEU LEU B . n 
B 1 337 TYR 337 368 368 TYR TYR B . n 
B 1 338 PRO 338 369 369 PRO PRO B . n 
B 1 339 THR 339 370 370 THR THR B . n 
B 1 340 PHE 340 371 371 PHE PHE B . n 
B 1 341 THR 341 372 372 THR THR B . n 
B 1 342 GLY 342 373 373 GLY GLY B . n 
B 1 343 LEU 343 374 374 LEU LEU B . n 
B 1 344 ALA 344 375 375 ALA ALA B . n 
B 1 345 GLU 345 376 376 GLU GLU B . n 
B 1 346 ALA 346 377 377 ALA ALA B . n 
B 1 347 LYS 347 378 378 LYS LYS B . n 
B 1 348 LEU 348 379 379 LEU LEU B . n 
B 1 349 PRO 349 380 380 PRO PRO B . n 
B 1 350 LYS 350 381 381 LYS LYS B . n 
B 1 351 GLY 351 382 382 GLY GLY B . n 
B 1 352 LYS 352 383 383 LYS LYS B . n 
B 1 353 GLN 353 384 384 GLN GLN B . n 
B 1 354 LEU 354 385 385 LEU LEU B . n 
B 1 355 ASP 355 386 386 ASP ASP B . n 
B 1 356 GLY 356 387 387 GLY GLY B . n 
B 1 357 LYS 357 388 388 LYS LYS B . n 
B 1 358 ASN 358 389 389 ASN ASN B . n 
B 1 359 ILE 359 390 390 ILE ILE B . n 
B 1 360 MET 360 391 391 MET MET B . n 
B 1 361 ASP 361 392 392 ASP ASP B . n 
B 1 362 ASP 362 393 393 ASP ASP B . n 
B 1 363 VAL 363 394 394 VAL VAL B . n 
B 1 364 LEU 364 395 395 LEU LEU B . n 
B 1 365 LYS 365 396 396 LYS LYS B . n 
B 1 366 ASN 366 397 397 ASN ASN B . n 
B 1 367 THR 367 398 398 THR THR B . n 
B 1 368 GLU 368 399 399 GLU GLU B . n 
B 1 369 PRO 369 400 400 PRO PRO B . n 
B 1 370 TYR 370 401 401 TYR TYR B . n 
B 1 371 LYS 371 402 402 LYS LYS B . n 
B 1 372 ASP 372 403 403 ASP ASP B . n 
B 1 373 GLU 373 404 404 GLU GLU B . n 
B 1 374 MET 374 405 405 MET MET B . n 
B 1 375 ILE 375 406 406 ILE ILE B . n 
B 1 376 TYR 376 407 407 TYR TYR B . n 
B 1 377 SER 377 408 408 SER SER B . n 
B 1 378 LEU 378 409 409 LEU LEU B . n 
B 1 379 ARG 379 410 410 ARG ARG B . n 
B 1 380 TYR 380 411 411 TYR TYR B . n 
B 1 381 ARG 381 412 412 ARG ARG B . n 
B 1 382 GLU 382 413 413 GLU GLU B . n 
B 1 383 GLY 383 414 414 GLY GLY B . n 
B 1 384 TYR 384 415 415 TYR TYR B . n 
B 1 385 ASN 385 416 416 ASN ASN B . n 
B 1 386 ASP 386 417 417 ASP ASP B . n 
B 1 387 VAL 387 418 418 VAL VAL B . n 
B 1 388 GLY 388 419 419 GLY GLY B . n 
B 1 389 ALA 389 420 420 ALA ALA B . n 
B 1 390 ARG 390 421 421 ARG ARG B . n 
B 1 391 MET 391 422 422 MET MET B . n 
B 1 392 GLY 392 423 423 GLY GLY B . n 
B 1 393 ASP 393 424 424 ASP ASP B . n 
B 1 394 TRP 394 425 425 TRP TRP B . n 
B 1 395 LYS 395 426 426 LYS LYS B . n 
B 1 396 ILE 396 427 427 ILE ILE B . n 
B 1 397 THR 397 428 428 THR THR B . n 
B 1 398 ARG 398 429 429 ARG ARG B . n 
B 1 399 MET 399 430 430 MET MET B . n 
B 1 400 GLY 400 431 431 GLY GLY B . n 
B 1 401 ASN 401 432 432 ASN ASN B . n 
B 1 402 GLU 402 433 433 GLU GLU B . n 
B 1 403 PRO 403 434 434 PRO PRO B . n 
B 1 404 TRP 404 435 435 TRP TRP B . n 
B 1 405 ARG 405 436 436 ARG ARG B . n 
B 1 406 LEU 406 437 437 LEU LEU B . n 
B 1 407 HIS 407 438 438 HIS HIS B . n 
B 1 408 ASN 408 439 439 ASN ASN B . n 
B 1 409 ILE 409 440 440 ILE ILE B . n 
B 1 410 THR 410 441 441 THR THR B . n 
B 1 411 GLN 411 442 442 GLN GLN B . n 
B 1 412 ASP 412 443 443 ASP ASP B . n 
B 1 413 ILE 413 444 444 ILE ILE B . n 
B 1 414 GLY 414 445 445 GLY GLY B . n 
B 1 415 GLU 415 446 446 GLU GLU B . n 
B 1 416 LYS 416 447 447 LYS LYS B . n 
B 1 417 LYS 417 448 448 LYS LYS B . n 
B 1 418 ASN 418 449 449 ASN ASN B . n 
B 1 419 LEU 419 450 450 LEU LEU B . n 
B 1 420 ALA 420 451 451 ALA ALA B . n 
B 1 421 GLY 421 452 452 GLY GLY B . n 
B 1 422 ARG 422 453 453 ARG ARG B . n 
B 1 423 TYR 423 454 454 TYR TYR B . n 
B 1 424 PRO 424 455 455 PRO PRO B . n 
B 1 425 ASP 425 456 456 ASP ASP B . n 
B 1 426 ARG 426 457 457 ARG ARG B . n 
B 1 427 LEU 427 458 458 LEU LEU B . n 
B 1 428 LYS 428 459 459 LYS LYS B . n 
B 1 429 GLU 429 460 460 GLU GLU B . n 
B 1 430 MET 430 461 461 MET MET B . n 
B 1 431 ILE 431 462 462 ILE ILE B . n 
B 1 432 ALA 432 463 463 ALA ALA B . n 
B 1 433 LYS 433 464 464 LYS LYS B . n 
B 1 434 THR 434 465 465 THR THR B . n 
B 1 435 GLN 435 466 466 GLN GLN B . n 
B 1 436 GLU 436 467 467 GLU GLU B . n 
B 1 437 TRP 437 468 468 TRP TRP B . n 
B 1 438 THR 438 469 469 THR THR B . n 
B 1 439 LYS 439 470 470 LYS LYS B . n 
B 1 440 SER 440 471 471 SER SER B . n 
B 1 441 PHE 441 472 472 PHE PHE B . n 
B 1 442 VAL 442 473 473 VAL VAL B . n 
B 1 443 LYS 443 474 474 LYS LYS B . n 
B 1 444 PRO 444 475 475 PRO PRO B . n 
B 1 445 LEU 445 476 476 LEU LEU B . n 
B 1 446 TRP 446 477 477 TRP TRP B . n 
B 1 447 VAL 447 478 478 VAL VAL B . n 
B 1 448 TYR 448 479 479 TYR TYR B . n 
B 1 449 SER 449 480 480 SER SER B . n 
B 1 450 VAL 450 481 481 VAL VAL B . n 
B 1 451 LYS 451 482 482 LYS LYS B . n 
B 1 452 ASP 452 483 483 ASP ASP B . n 
B 1 453 LYS 453 484 484 LYS LYS B . n 
B 1 454 GLU 454 485 485 GLU GLU B . n 
B 1 455 LEU 455 486 486 LEU LEU B . n 
B 1 456 TRP 456 487 487 TRP TRP B . n 
B 1 457 GLU 457 488 488 GLU GLU B . n 
B 1 458 SER 458 489 489 SER SER B . n 
B 1 459 GLY 459 490 490 GLY GLY B . n 
B 1 460 GLN 460 491 491 GLN GLN B . n 
B 1 461 MET 461 492 492 MET MET B . n 
B 1 462 PRO 462 493 493 PRO PRO B . n 
B 1 463 ASN 463 494 494 ASN ASN B . n 
B 1 464 TYR 464 495 495 TYR TYR B . n 
B 1 465 GLU 465 496 496 GLU GLU B . n 
B 1 466 ALA 466 497 497 ALA ALA B . n 
B 1 467 THR 467 498 498 THR THR B . n 
B 1 468 PHE 468 499 499 PHE PHE B . n 
B 1 469 GLU 469 500 500 GLU GLU B . n 
B 1 470 VAL 470 501 501 VAL VAL B . n 
B 1 471 ASP 471 502 502 ASP ASP B . n 
B 1 472 LYS 472 503 503 LYS LYS B . n 
B 1 473 LEU 473 504 504 LEU LEU B . n 
B 1 474 VAL 474 505 505 VAL VAL B . n 
B 1 475 ASP 475 506 506 ASP ASP B . n 
B 1 476 SER 476 507 507 SER SER B . n 
B 1 477 PRO 477 508 508 PRO PRO B . n 
B 1 478 TYR 478 509 509 TYR TYR B . n 
B 1 479 HIS 479 510 ?   ?   ?   B . n 
B 1 480 LYS 480 511 ?   ?   ?   B . n 
C 1 1   MET 1   32  ?   ?   ?   C . n 
C 1 2   GLY 2   33  ?   ?   ?   C . n 
C 1 3   SER 3   34  ?   ?   ?   C . n 
C 1 4   SER 4   35  ?   ?   ?   C . n 
C 1 5   HIS 5   36  ?   ?   ?   C . n 
C 1 6   HIS 6   37  ?   ?   ?   C . n 
C 1 7   HIS 7   38  ?   ?   ?   C . n 
C 1 8   HIS 8   39  ?   ?   ?   C . n 
C 1 9   HIS 9   40  ?   ?   ?   C . n 
C 1 10  HIS 10  41  ?   ?   ?   C . n 
C 1 11  GLY 11  42  ?   ?   ?   C . n 
C 1 12  SER 12  43  ?   ?   ?   C . n 
C 1 13  GLN 13  44  ?   ?   ?   C . n 
C 1 14  GLU 14  45  ?   ?   ?   C . n 
C 1 15  THR 15  46  46  THR THR C . n 
C 1 16  ARG 16  47  47  ARG ARG C . n 
C 1 17  PRO 17  48  48  PRO PRO C . n 
C 1 18  ASN 18  49  49  ASN ASN C . n 
C 1 19  ILE 19  50  50  ILE ILE C . n 
C 1 20  LEU 20  51  51  LEU LEU C . n 
C 1 21  VAL 21  52  52  VAL VAL C . n 
C 1 22  VAL 22  53  53  VAL VAL C . n 
C 1 23  LEU 23  54  54  LEU LEU C . n 
C 1 24  CYS 24  55  55  CYS CYS C . n 
C 1 25  ASP 25  56  56  ASP ASP C . n 
C 1 26  ASP 26  57  57  ASP ASP C . n 
C 1 27  LEU 27  58  58  LEU LEU C . n 
C 1 28  GLY 28  59  59  GLY GLY C . n 
C 1 29  TYR 29  60  60  TYR TYR C . n 
C 1 30  ALA 30  61  61  ALA ALA C . n 
C 1 31  ASP 31  62  62  ASP ASP C . n 
C 1 32  VAL 32  63  63  VAL VAL C . n 
C 1 33  GLY 33  64  64  GLY GLY C . n 
C 1 34  PHE 34  65  65  PHE PHE C . n 
C 1 35  ASN 35  66  66  ASN ASN C . n 
C 1 36  GLY 36  67  67  GLY GLY C . n 
C 1 37  SER 37  68  68  SER SER C . n 
C 1 38  THR 38  69  69  THR THR C . n 
C 1 39  ASP 39  70  70  ASP ASP C . n 
C 1 40  ILE 40  71  71  ILE ILE C . n 
C 1 41  LEU 41  72  72  LEU LEU C . n 
C 1 42  THR 42  73  73  THR THR C . n 
C 1 43  PRO 43  74  74  PRO PRO C . n 
C 1 44  GLU 44  75  75  GLU GLU C . n 
C 1 45  LEU 45  76  76  LEU LEU C . n 
C 1 46  ASP 46  77  77  ASP ASP C . n 
C 1 47  ASN 47  78  78  ASN ASN C . n 
C 1 48  LEU 48  79  79  LEU LEU C . n 
C 1 49  ALA 49  80  80  ALA ALA C . n 
C 1 50  GLN 50  81  81  GLN GLN C . n 
C 1 51  ASN 51  82  82  ASN ASN C . n 
C 1 52  GLY 52  83  83  GLY GLY C . n 
C 1 53  SER 53  84  84  SER SER C . n 
C 1 54  ILE 54  85  85  ILE ILE C . n 
C 1 55  PHE 55  86  86  PHE PHE C . n 
C 1 56  THR 56  87  87  THR THR C . n 
C 1 57  SER 57  88  88  SER SER C . n 
C 1 58  ALA 58  89  89  ALA ALA C . n 
C 1 59  TYR 59  90  90  TYR TYR C . n 
C 1 60  VAL 60  91  91  VAL VAL C . n 
C 1 61  ALA 61  92  92  ALA ALA C . n 
C 1 62  HIS 62  93  93  HIS HIS C . n 
C 1 63  PRO 63  94  94  PRO PRO C . n 
C 1 64  PHE 64  95  95  PHE PHE C . n 
C 1 65  CYS 65  96  96  CYS CYS C . y 
C 1 65  DDZ 65  96  96  DDZ DDZ C . y 
C 1 66  GLY 66  97  97  GLY GLY C . n 
C 1 67  PRO 67  98  98  PRO PRO C . n 
C 1 68  SER 68  99  99  SER SER C . n 
C 1 69  ARG 69  100 100 ARG ARG C . n 
C 1 70  SER 70  101 101 SER SER C . n 
C 1 71  ALA 71  102 102 ALA ALA C . n 
C 1 72  ILE 72  103 103 ILE ILE C . n 
C 1 73  LEU 73  104 104 LEU LEU C . n 
C 1 74  THR 74  105 105 THR THR C . n 
C 1 75  GLY 75  106 106 GLY GLY C . n 
C 1 76  ARG 76  107 107 ARG ARG C . n 
C 1 77  TYR 77  108 108 TYR TYR C . n 
C 1 78  PRO 78  109 109 PRO PRO C . n 
C 1 79  HIS 79  110 110 HIS HIS C . n 
C 1 80  LEU 80  111 111 LEU LEU C . n 
C 1 81  THR 81  112 112 THR THR C . n 
C 1 82  GLY 82  113 113 GLY GLY C . n 
C 1 83  THR 83  114 114 THR THR C . n 
C 1 84  ALA 84  115 115 ALA ALA C . n 
C 1 85  TYR 85  116 116 TYR TYR C . n 
C 1 86  ASN 86  117 117 ASN ASN C . n 
C 1 87  LEU 87  118 118 LEU LEU C . n 
C 1 88  PHE 88  119 119 PHE PHE C . n 
C 1 89  HIS 89  120 120 HIS HIS C . n 
C 1 90  ASN 90  121 121 ASN ASN C . n 
C 1 91  SER 91  122 122 SER SER C . n 
C 1 92  SER 92  123 123 SER SER C . n 
C 1 93  GLU 93  124 124 GLU GLU C . n 
C 1 94  ASP 94  125 125 ASP ASP C . n 
C 1 95  ASP 95  126 126 ASP ASP C . n 
C 1 96  LYS 96  127 127 LYS LYS C . n 
C 1 97  ASP 97  128 128 ASP ASP C . n 
C 1 98  ASN 98  129 129 ASN ASN C . n 
C 1 99  MET 99  130 130 MET MET C . n 
C 1 100 GLY 100 131 131 GLY GLY C . n 
C 1 101 VAL 101 132 132 VAL VAL C . n 
C 1 102 PRO 102 133 133 PRO PRO C . n 
C 1 103 VAL 103 134 134 VAL VAL C . n 
C 1 104 GLU 104 135 135 GLU GLU C . n 
C 1 105 GLU 105 136 136 GLU GLU C . n 
C 1 106 THR 106 137 137 THR THR C . n 
C 1 107 TYR 107 138 138 TYR TYR C . n 
C 1 108 MET 108 139 139 MET MET C . n 
C 1 109 SER 109 140 140 SER SER C . n 
C 1 110 LYS 110 141 141 LYS LYS C . n 
C 1 111 VAL 111 142 142 VAL VAL C . n 
C 1 112 LEU 112 143 143 LEU LEU C . n 
C 1 113 GLN 113 144 144 GLN GLN C . n 
C 1 114 ASN 114 145 145 ASN ASN C . n 
C 1 115 ALA 115 146 146 ALA ALA C . n 
C 1 116 GLY 116 147 147 GLY GLY C . n 
C 1 117 TYR 117 148 148 TYR TYR C . n 
C 1 118 TYR 118 149 149 TYR TYR C . n 
C 1 119 THR 119 150 150 THR THR C . n 
C 1 120 SER 120 151 151 SER SER C . n 
C 1 121 ALA 121 152 152 ALA ALA C . n 
C 1 122 ILE 122 153 153 ILE ILE C . n 
C 1 123 GLY 123 154 154 GLY GLY C . n 
C 1 124 LYS 124 155 155 LYS LYS C . n 
C 1 125 TRP 125 156 156 TRP TRP C . n 
C 1 126 HIS 126 157 157 HIS HIS C . n 
C 1 127 LEU 127 158 158 LEU LEU C . n 
C 1 128 GLY 128 159 159 GLY GLY C . n 
C 1 129 ALA 129 160 160 ALA ALA C . n 
C 1 130 ALA 130 161 161 ALA ALA C . n 
C 1 131 PRO 131 162 162 PRO PRO C . n 
C 1 132 LYS 132 163 163 LYS LYS C . n 
C 1 133 PHE 133 164 164 PHE PHE C . n 
C 1 134 HIS 134 165 165 HIS HIS C . n 
C 1 135 PRO 135 166 166 PRO PRO C . n 
C 1 136 ASN 136 167 167 ASN ASN C . n 
C 1 137 LYS 137 168 168 LYS LYS C . n 
C 1 138 ARG 138 169 169 ARG ARG C . n 
C 1 139 GLY 139 170 170 GLY GLY C . n 
C 1 140 PHE 140 171 171 PHE PHE C . n 
C 1 141 ASP 141 172 172 ASP ASP C . n 
C 1 142 ASP 142 173 173 ASP ASP C . n 
C 1 143 PHE 143 174 174 PHE PHE C . n 
C 1 144 TYR 144 175 175 TYR TYR C . n 
C 1 145 GLY 145 176 176 GLY GLY C . n 
C 1 146 PHE 146 177 177 PHE PHE C . n 
C 1 147 LEU 147 178 178 LEU LEU C . n 
C 1 148 GLY 148 179 179 GLY GLY C . n 
C 1 149 GLY 149 180 180 GLY GLY C . n 
C 1 150 GLY 150 181 181 GLY GLY C . n 
C 1 151 HIS 151 182 182 HIS HIS C . n 
C 1 152 ASP 152 183 183 ASP ASP C . n 
C 1 153 TYR 153 184 184 TYR TYR C . n 
C 1 154 PHE 154 185 185 PHE PHE C . n 
C 1 155 PRO 155 186 186 PRO PRO C . n 
C 1 156 SER 156 187 187 SER SER C . n 
C 1 157 GLU 157 188 188 GLU GLU C . n 
C 1 158 TYR 158 189 189 TYR TYR C . n 
C 1 159 GLN 159 190 190 GLN GLN C . n 
C 1 160 LYS 160 191 191 LYS LYS C . n 
C 1 161 THR 161 192 192 THR THR C . n 
C 1 162 TYR 162 193 193 TYR TYR C . n 
C 1 163 LYS 163 194 194 LYS LYS C . n 
C 1 164 ALA 164 195 195 ALA ALA C . n 
C 1 165 GLN 165 196 196 GLN GLN C . n 
C 1 166 LYS 166 197 197 LYS LYS C . n 
C 1 167 LYS 167 198 198 LYS LYS C . n 
C 1 168 ALA 168 199 199 ALA ALA C . n 
C 1 169 GLY 169 200 200 GLY GLY C . n 
C 1 170 ASN 170 201 201 ASN ASN C . n 
C 1 171 PRO 171 202 202 PRO PRO C . n 
C 1 172 ASN 172 203 203 ASN ASN C . n 
C 1 173 ILE 173 204 204 ILE ILE C . n 
C 1 174 ARG 174 205 205 ARG ARG C . n 
C 1 175 ASP 175 206 206 ASP ASP C . n 
C 1 176 TYR 176 207 207 TYR TYR C . n 
C 1 177 VAL 177 208 208 VAL VAL C . n 
C 1 178 PHE 178 209 209 PHE PHE C . n 
C 1 179 PRO 179 210 210 PRO PRO C . n 
C 1 180 MET 180 211 211 MET MET C . n 
C 1 181 GLU 181 212 212 GLU GLU C . n 
C 1 182 HIS 182 213 213 HIS HIS C . n 
C 1 183 ASN 183 214 214 ASN ASN C . n 
C 1 184 GLY 184 215 215 GLY GLY C . n 
C 1 185 LYS 185 216 216 LYS LYS C . n 
C 1 186 PRO 186 217 217 PRO PRO C . n 
C 1 187 ALA 187 218 218 ALA ALA C . n 
C 1 188 ASN 188 219 219 ASN ASN C . n 
C 1 189 GLU 189 220 220 GLU GLU C . n 
C 1 190 THR 190 221 221 THR THR C . n 
C 1 191 GLU 191 222 222 GLU GLU C . n 
C 1 192 TYR 192 223 223 TYR TYR C . n 
C 1 193 ILE 193 224 224 ILE ILE C . n 
C 1 194 THR 194 225 225 THR THR C . n 
C 1 195 ASP 195 226 226 ASP ASP C . n 
C 1 196 GLY 196 227 227 GLY GLY C . n 
C 1 197 PHE 197 228 228 PHE PHE C . n 
C 1 198 SER 198 229 229 SER SER C . n 
C 1 199 ARG 199 230 230 ARG ARG C . n 
C 1 200 GLU 200 231 231 GLU GLU C . n 
C 1 201 ALA 201 232 232 ALA ALA C . n 
C 1 202 ILE 202 233 233 ILE ILE C . n 
C 1 203 LYS 203 234 234 LYS LYS C . n 
C 1 204 ASN 204 235 235 ASN ASN C . n 
C 1 205 ILE 205 236 236 ILE ILE C . n 
C 1 206 LYS 206 237 237 LYS LYS C . n 
C 1 207 ILE 207 238 238 ILE ILE C . n 
C 1 208 ALA 208 239 239 ALA ALA C . n 
C 1 209 ALA 209 240 240 ALA ALA C . n 
C 1 210 ALA 210 241 241 ALA ALA C . n 
C 1 211 LYS 211 242 242 LYS LYS C . n 
C 1 212 LYS 212 243 243 LYS LYS C . n 
C 1 213 GLN 213 244 244 GLN GLN C . n 
C 1 214 PRO 214 245 245 PRO PRO C . n 
C 1 215 PHE 215 246 246 PHE PHE C . n 
C 1 216 PHE 216 247 247 PHE PHE C . n 
C 1 217 ILE 217 248 248 ILE ILE C . n 
C 1 218 TYR 218 249 249 TYR TYR C . n 
C 1 219 LEU 219 250 250 LEU LEU C . n 
C 1 220 ALA 220 251 251 ALA ALA C . n 
C 1 221 TYR 221 252 252 TYR TYR C . n 
C 1 222 ASN 222 253 253 ASN ASN C . n 
C 1 223 ALA 223 254 254 ALA ALA C . n 
C 1 224 PRO 224 255 255 PRO PRO C . n 
C 1 225 HIS 225 256 256 HIS HIS C . n 
C 1 226 VAL 226 257 257 VAL VAL C . n 
C 1 227 PRO 227 258 258 PRO PRO C . n 
C 1 228 LEU 228 259 259 LEU LEU C . n 
C 1 229 GLN 229 260 260 GLN GLN C . n 
C 1 230 ALA 230 261 261 ALA ALA C . n 
C 1 231 LYS 231 262 262 LYS LYS C . n 
C 1 232 ALA 232 263 263 ALA ALA C . n 
C 1 233 GLU 233 264 264 GLU GLU C . n 
C 1 234 ASP 234 265 265 ASP ASP C . n 
C 1 235 VAL 235 266 266 VAL VAL C . n 
C 1 236 ALA 236 267 267 ALA ALA C . n 
C 1 237 LYS 237 268 268 LYS LYS C . n 
C 1 238 PHE 238 269 269 PHE PHE C . n 
C 1 239 ALA 239 270 270 ALA ALA C . n 
C 1 240 HIS 240 271 271 HIS HIS C . n 
C 1 241 ILE 241 272 272 ILE ILE C . n 
C 1 242 LYS 242 273 273 LYS LYS C . n 
C 1 243 ASP 243 274 274 ASP ASP C . n 
C 1 244 LYS 244 275 275 LYS LYS C . n 
C 1 245 ASP 245 276 276 ASP ASP C . n 
C 1 246 ARG 246 277 277 ARG ARG C . n 
C 1 247 ARG 247 278 278 ARG ARG C . n 
C 1 248 THR 248 279 279 THR THR C . n 
C 1 249 TYR 249 280 280 TYR TYR C . n 
C 1 250 ALA 250 281 281 ALA ALA C . n 
C 1 251 ALA 251 282 282 ALA ALA C . n 
C 1 252 MET 252 283 283 MET MET C . n 
C 1 253 VAL 253 284 284 VAL VAL C . n 
C 1 254 TYR 254 285 285 TYR TYR C . n 
C 1 255 ALA 255 286 286 ALA ALA C . n 
C 1 256 VAL 256 287 287 VAL VAL C . n 
C 1 257 ASP 257 288 288 ASP ASP C . n 
C 1 258 ARG 258 289 289 ARG ARG C . n 
C 1 259 GLY 259 290 290 GLY GLY C . n 
C 1 260 VAL 260 291 291 VAL VAL C . n 
C 1 261 GLY 261 292 292 GLY GLY C . n 
C 1 262 LYS 262 293 293 LYS LYS C . n 
C 1 263 ILE 263 294 294 ILE ILE C . n 
C 1 264 VAL 264 295 295 VAL VAL C . n 
C 1 265 GLN 265 296 296 GLN GLN C . n 
C 1 266 THR 266 297 297 THR THR C . n 
C 1 267 LEU 267 298 298 LEU LEU C . n 
C 1 268 LYS 268 299 299 LYS LYS C . n 
C 1 269 GLU 269 300 300 GLU GLU C . n 
C 1 270 THR 270 301 301 THR THR C . n 
C 1 271 LYS 271 302 302 LYS LYS C . n 
C 1 272 GLN 272 303 303 GLN GLN C . n 
C 1 273 PHE 273 304 304 PHE PHE C . n 
C 1 274 ASP 274 305 305 ASP ASP C . n 
C 1 275 ASN 275 306 306 ASN ASN C . n 
C 1 276 THR 276 307 307 THR THR C . n 
C 1 277 LEU 277 308 308 LEU LEU C . n 
C 1 278 ILE 278 309 309 ILE ILE C . n 
C 1 279 VAL 279 310 310 VAL VAL C . n 
C 1 280 PHE 280 311 311 PHE PHE C . n 
C 1 281 LEU 281 312 312 LEU LEU C . n 
C 1 282 SER 282 313 313 SER SER C . n 
C 1 283 ASP 283 314 314 ASP ASP C . n 
C 1 284 ASN 284 315 315 ASN ASN C . n 
C 1 285 GLY 285 316 316 GLY GLY C . n 
C 1 286 GLY 286 317 317 GLY GLY C . n 
C 1 287 ASN 287 318 318 ASN ASN C . n 
C 1 288 PHE 288 319 319 PHE PHE C . n 
C 1 289 ASN 289 320 320 ASN ASN C . n 
C 1 290 HIS 290 321 321 HIS HIS C . n 
C 1 291 GLY 291 322 322 GLY GLY C . n 
C 1 292 ALA 292 323 323 ALA ALA C . n 
C 1 293 ASN 293 324 324 ASN ASN C . n 
C 1 294 ASN 294 325 325 ASN ASN C . n 
C 1 295 TYR 295 326 326 TYR TYR C . n 
C 1 296 PRO 296 327 327 PRO PRO C . n 
C 1 297 LEU 297 328 328 LEU LEU C . n 
C 1 298 LYS 298 329 329 LYS LYS C . n 
C 1 299 GLY 299 330 330 GLY GLY C . n 
C 1 300 THR 300 331 331 THR THR C . n 
C 1 301 LYS 301 332 332 LYS LYS C . n 
C 1 302 GLY 302 333 333 GLY GLY C . n 
C 1 303 ASP 303 334 334 ASP ASP C . n 
C 1 304 THR 304 335 335 THR THR C . n 
C 1 305 TRP 305 336 336 TRP TRP C . n 
C 1 306 GLU 306 337 337 GLU GLU C . n 
C 1 307 GLY 307 338 338 GLY GLY C . n 
C 1 308 GLY 308 339 339 GLY GLY C . n 
C 1 309 TYR 309 340 340 TYR TYR C . n 
C 1 310 ARG 310 341 341 ARG ARG C . n 
C 1 311 VAL 311 342 342 VAL VAL C . n 
C 1 312 PRO 312 343 343 PRO PRO C . n 
C 1 313 MET 313 344 344 MET MET C . n 
C 1 314 PHE 314 345 345 PHE PHE C . n 
C 1 315 PHE 315 346 346 PHE PHE C . n 
C 1 316 HIS 316 347 347 HIS HIS C . n 
C 1 317 TRP 317 348 348 TRP TRP C . n 
C 1 318 PRO 318 349 349 PRO PRO C . n 
C 1 319 LYS 319 350 350 LYS LYS C . n 
C 1 320 LYS 320 351 351 LYS LYS C . n 
C 1 321 ILE 321 352 352 ILE ILE C . n 
C 1 322 LYS 322 353 353 LYS LYS C . n 
C 1 323 LYS 323 354 354 LYS LYS C . n 
C 1 324 ASP 324 355 355 ASP ASP C . n 
C 1 325 GLN 325 356 356 GLN GLN C . n 
C 1 326 ARG 326 357 357 ARG ARG C . n 
C 1 327 PHE 327 358 358 PHE PHE C . n 
C 1 328 ASP 328 359 359 ASP ASP C . n 
C 1 329 PHE 329 360 360 PHE PHE C . n 
C 1 330 PRO 330 361 361 PRO PRO C . n 
C 1 331 VAL 331 362 362 VAL VAL C . n 
C 1 332 SER 332 363 363 SER SER C . n 
C 1 333 SER 333 364 364 SER SER C . n 
C 1 334 LEU 334 365 365 LEU LEU C . n 
C 1 335 ASP 335 366 366 ASP ASP C . n 
C 1 336 LEU 336 367 367 LEU LEU C . n 
C 1 337 TYR 337 368 368 TYR TYR C . n 
C 1 338 PRO 338 369 369 PRO PRO C . n 
C 1 339 THR 339 370 370 THR THR C . n 
C 1 340 PHE 340 371 371 PHE PHE C . n 
C 1 341 THR 341 372 372 THR THR C . n 
C 1 342 GLY 342 373 373 GLY GLY C . n 
C 1 343 LEU 343 374 374 LEU LEU C . n 
C 1 344 ALA 344 375 375 ALA ALA C . n 
C 1 345 GLU 345 376 376 GLU GLU C . n 
C 1 346 ALA 346 377 377 ALA ALA C . n 
C 1 347 LYS 347 378 378 LYS LYS C . n 
C 1 348 LEU 348 379 379 LEU LEU C . n 
C 1 349 PRO 349 380 380 PRO PRO C . n 
C 1 350 LYS 350 381 381 LYS LYS C . n 
C 1 351 GLY 351 382 382 GLY GLY C . n 
C 1 352 LYS 352 383 383 LYS LYS C . n 
C 1 353 GLN 353 384 384 GLN GLN C . n 
C 1 354 LEU 354 385 385 LEU LEU C . n 
C 1 355 ASP 355 386 386 ASP ASP C . n 
C 1 356 GLY 356 387 387 GLY GLY C . n 
C 1 357 LYS 357 388 388 LYS LYS C . n 
C 1 358 ASN 358 389 389 ASN ASN C . n 
C 1 359 ILE 359 390 390 ILE ILE C . n 
C 1 360 MET 360 391 391 MET MET C . n 
C 1 361 ASP 361 392 392 ASP ASP C . n 
C 1 362 ASP 362 393 393 ASP ASP C . n 
C 1 363 VAL 363 394 394 VAL VAL C . n 
C 1 364 LEU 364 395 395 LEU LEU C . n 
C 1 365 LYS 365 396 396 LYS LYS C . n 
C 1 366 ASN 366 397 397 ASN ASN C . n 
C 1 367 THR 367 398 398 THR THR C . n 
C 1 368 GLU 368 399 399 GLU GLU C . n 
C 1 369 PRO 369 400 400 PRO PRO C . n 
C 1 370 TYR 370 401 401 TYR TYR C . n 
C 1 371 LYS 371 402 402 LYS LYS C . n 
C 1 372 ASP 372 403 403 ASP ASP C . n 
C 1 373 GLU 373 404 404 GLU GLU C . n 
C 1 374 MET 374 405 405 MET MET C . n 
C 1 375 ILE 375 406 406 ILE ILE C . n 
C 1 376 TYR 376 407 407 TYR TYR C . n 
C 1 377 SER 377 408 408 SER SER C . n 
C 1 378 LEU 378 409 409 LEU LEU C . n 
C 1 379 ARG 379 410 410 ARG ARG C . n 
C 1 380 TYR 380 411 411 TYR TYR C . n 
C 1 381 ARG 381 412 412 ARG ARG C . n 
C 1 382 GLU 382 413 413 GLU GLU C . n 
C 1 383 GLY 383 414 414 GLY GLY C . n 
C 1 384 TYR 384 415 415 TYR TYR C . n 
C 1 385 ASN 385 416 416 ASN ASN C . n 
C 1 386 ASP 386 417 417 ASP ASP C . n 
C 1 387 VAL 387 418 418 VAL VAL C . n 
C 1 388 GLY 388 419 419 GLY GLY C . n 
C 1 389 ALA 389 420 420 ALA ALA C . n 
C 1 390 ARG 390 421 421 ARG ARG C . n 
C 1 391 MET 391 422 422 MET MET C . n 
C 1 392 GLY 392 423 423 GLY GLY C . n 
C 1 393 ASP 393 424 424 ASP ASP C . n 
C 1 394 TRP 394 425 425 TRP TRP C . n 
C 1 395 LYS 395 426 426 LYS LYS C . n 
C 1 396 ILE 396 427 427 ILE ILE C . n 
C 1 397 THR 397 428 428 THR THR C . n 
C 1 398 ARG 398 429 429 ARG ARG C . n 
C 1 399 MET 399 430 430 MET MET C . n 
C 1 400 GLY 400 431 431 GLY GLY C . n 
C 1 401 ASN 401 432 432 ASN ASN C . n 
C 1 402 GLU 402 433 433 GLU GLU C . n 
C 1 403 PRO 403 434 434 PRO PRO C . n 
C 1 404 TRP 404 435 435 TRP TRP C . n 
C 1 405 ARG 405 436 436 ARG ARG C . n 
C 1 406 LEU 406 437 437 LEU LEU C . n 
C 1 407 HIS 407 438 438 HIS HIS C . n 
C 1 408 ASN 408 439 439 ASN ASN C . n 
C 1 409 ILE 409 440 440 ILE ILE C . n 
C 1 410 THR 410 441 441 THR THR C . n 
C 1 411 GLN 411 442 442 GLN GLN C . n 
C 1 412 ASP 412 443 443 ASP ASP C . n 
C 1 413 ILE 413 444 444 ILE ILE C . n 
C 1 414 GLY 414 445 445 GLY GLY C . n 
C 1 415 GLU 415 446 446 GLU GLU C . n 
C 1 416 LYS 416 447 447 LYS LYS C . n 
C 1 417 LYS 417 448 448 LYS LYS C . n 
C 1 418 ASN 418 449 449 ASN ASN C . n 
C 1 419 LEU 419 450 450 LEU LEU C . n 
C 1 420 ALA 420 451 451 ALA ALA C . n 
C 1 421 GLY 421 452 452 GLY GLY C . n 
C 1 422 ARG 422 453 453 ARG ARG C . n 
C 1 423 TYR 423 454 454 TYR TYR C . n 
C 1 424 PRO 424 455 455 PRO PRO C . n 
C 1 425 ASP 425 456 456 ASP ASP C . n 
C 1 426 ARG 426 457 457 ARG ARG C . n 
C 1 427 LEU 427 458 458 LEU LEU C . n 
C 1 428 LYS 428 459 459 LYS LYS C . n 
C 1 429 GLU 429 460 460 GLU GLU C . n 
C 1 430 MET 430 461 461 MET MET C . n 
C 1 431 ILE 431 462 462 ILE ILE C . n 
C 1 432 ALA 432 463 463 ALA ALA C . n 
C 1 433 LYS 433 464 464 LYS LYS C . n 
C 1 434 THR 434 465 465 THR THR C . n 
C 1 435 GLN 435 466 466 GLN GLN C . n 
C 1 436 GLU 436 467 467 GLU GLU C . n 
C 1 437 TRP 437 468 468 TRP TRP C . n 
C 1 438 THR 438 469 469 THR THR C . n 
C 1 439 LYS 439 470 470 LYS LYS C . n 
C 1 440 SER 440 471 471 SER SER C . n 
C 1 441 PHE 441 472 472 PHE PHE C . n 
C 1 442 VAL 442 473 473 VAL VAL C . n 
C 1 443 LYS 443 474 474 LYS LYS C . n 
C 1 444 PRO 444 475 475 PRO PRO C . n 
C 1 445 LEU 445 476 476 LEU LEU C . n 
C 1 446 TRP 446 477 477 TRP TRP C . n 
C 1 447 VAL 447 478 478 VAL VAL C . n 
C 1 448 TYR 448 479 479 TYR TYR C . n 
C 1 449 SER 449 480 480 SER SER C . n 
C 1 450 VAL 450 481 481 VAL VAL C . n 
C 1 451 LYS 451 482 482 LYS LYS C . n 
C 1 452 ASP 452 483 483 ASP ASP C . n 
C 1 453 LYS 453 484 484 LYS LYS C . n 
C 1 454 GLU 454 485 485 GLU GLU C . n 
C 1 455 LEU 455 486 486 LEU LEU C . n 
C 1 456 TRP 456 487 487 TRP TRP C . n 
C 1 457 GLU 457 488 488 GLU GLU C . n 
C 1 458 SER 458 489 489 SER SER C . n 
C 1 459 GLY 459 490 490 GLY GLY C . n 
C 1 460 GLN 460 491 491 GLN GLN C . n 
C 1 461 MET 461 492 492 MET MET C . n 
C 1 462 PRO 462 493 493 PRO PRO C . n 
C 1 463 ASN 463 494 494 ASN ASN C . n 
C 1 464 TYR 464 495 495 TYR TYR C . n 
C 1 465 GLU 465 496 496 GLU GLU C . n 
C 1 466 ALA 466 497 497 ALA ALA C . n 
C 1 467 THR 467 498 498 THR THR C . n 
C 1 468 PHE 468 499 499 PHE PHE C . n 
C 1 469 GLU 469 500 500 GLU GLU C . n 
C 1 470 VAL 470 501 501 VAL VAL C . n 
C 1 471 ASP 471 502 502 ASP ASP C . n 
C 1 472 LYS 472 503 503 LYS LYS C . n 
C 1 473 LEU 473 504 504 LEU LEU C . n 
C 1 474 VAL 474 505 505 VAL VAL C . n 
C 1 475 ASP 475 506 506 ASP ASP C . n 
C 1 476 SER 476 507 507 SER SER C . n 
C 1 477 PRO 477 508 508 PRO PRO C . n 
C 1 478 TYR 478 509 509 TYR TYR C . n 
C 1 479 HIS 479 510 ?   ?   ?   C . n 
C 1 480 LYS 480 511 ?   ?   ?   C . n 
D 1 1   MET 1   32  ?   ?   ?   D . n 
D 1 2   GLY 2   33  ?   ?   ?   D . n 
D 1 3   SER 3   34  ?   ?   ?   D . n 
D 1 4   SER 4   35  ?   ?   ?   D . n 
D 1 5   HIS 5   36  ?   ?   ?   D . n 
D 1 6   HIS 6   37  ?   ?   ?   D . n 
D 1 7   HIS 7   38  ?   ?   ?   D . n 
D 1 8   HIS 8   39  ?   ?   ?   D . n 
D 1 9   HIS 9   40  ?   ?   ?   D . n 
D 1 10  HIS 10  41  ?   ?   ?   D . n 
D 1 11  GLY 11  42  ?   ?   ?   D . n 
D 1 12  SER 12  43  ?   ?   ?   D . n 
D 1 13  GLN 13  44  ?   ?   ?   D . n 
D 1 14  GLU 14  45  ?   ?   ?   D . n 
D 1 15  THR 15  46  46  THR THR D . n 
D 1 16  ARG 16  47  47  ARG ARG D . n 
D 1 17  PRO 17  48  48  PRO PRO D . n 
D 1 18  ASN 18  49  49  ASN ASN D . n 
D 1 19  ILE 19  50  50  ILE ILE D . n 
D 1 20  LEU 20  51  51  LEU LEU D . n 
D 1 21  VAL 21  52  52  VAL VAL D . n 
D 1 22  VAL 22  53  53  VAL VAL D . n 
D 1 23  LEU 23  54  54  LEU LEU D . n 
D 1 24  CYS 24  55  55  CYS CYS D . n 
D 1 25  ASP 25  56  56  ASP ASP D . n 
D 1 26  ASP 26  57  57  ASP ASP D . n 
D 1 27  LEU 27  58  58  LEU LEU D . n 
D 1 28  GLY 28  59  59  GLY GLY D . n 
D 1 29  TYR 29  60  60  TYR TYR D . n 
D 1 30  ALA 30  61  61  ALA ALA D . n 
D 1 31  ASP 31  62  62  ASP ASP D . n 
D 1 32  VAL 32  63  63  VAL VAL D . n 
D 1 33  GLY 33  64  64  GLY GLY D . n 
D 1 34  PHE 34  65  65  PHE PHE D . n 
D 1 35  ASN 35  66  66  ASN ASN D . n 
D 1 36  GLY 36  67  67  GLY GLY D . n 
D 1 37  SER 37  68  68  SER SER D . n 
D 1 38  THR 38  69  69  THR THR D . n 
D 1 39  ASP 39  70  70  ASP ASP D . n 
D 1 40  ILE 40  71  71  ILE ILE D . n 
D 1 41  LEU 41  72  72  LEU LEU D . n 
D 1 42  THR 42  73  73  THR THR D . n 
D 1 43  PRO 43  74  74  PRO PRO D . n 
D 1 44  GLU 44  75  75  GLU GLU D . n 
D 1 45  LEU 45  76  76  LEU LEU D . n 
D 1 46  ASP 46  77  77  ASP ASP D . n 
D 1 47  ASN 47  78  78  ASN ASN D . n 
D 1 48  LEU 48  79  79  LEU LEU D . n 
D 1 49  ALA 49  80  80  ALA ALA D . n 
D 1 50  GLN 50  81  81  GLN GLN D . n 
D 1 51  ASN 51  82  82  ASN ASN D . n 
D 1 52  GLY 52  83  83  GLY GLY D . n 
D 1 53  SER 53  84  84  SER SER D . n 
D 1 54  ILE 54  85  85  ILE ILE D . n 
D 1 55  PHE 55  86  86  PHE PHE D . n 
D 1 56  THR 56  87  87  THR THR D . n 
D 1 57  SER 57  88  88  SER SER D . n 
D 1 58  ALA 58  89  89  ALA ALA D . n 
D 1 59  TYR 59  90  90  TYR TYR D . n 
D 1 60  VAL 60  91  91  VAL VAL D . n 
D 1 61  ALA 61  92  92  ALA ALA D . n 
D 1 62  HIS 62  93  93  HIS HIS D . n 
D 1 63  PRO 63  94  94  PRO PRO D . n 
D 1 64  PHE 64  95  95  PHE PHE D . n 
D 1 65  CYS 65  96  96  CYS CYS D . y 
D 1 65  DDZ 65  96  96  DDZ DDZ D . y 
D 1 66  GLY 66  97  97  GLY GLY D . n 
D 1 67  PRO 67  98  98  PRO PRO D . n 
D 1 68  SER 68  99  99  SER SER D . n 
D 1 69  ARG 69  100 100 ARG ARG D . n 
D 1 70  SER 70  101 101 SER SER D . n 
D 1 71  ALA 71  102 102 ALA ALA D . n 
D 1 72  ILE 72  103 103 ILE ILE D . n 
D 1 73  LEU 73  104 104 LEU LEU D . n 
D 1 74  THR 74  105 105 THR THR D . n 
D 1 75  GLY 75  106 106 GLY GLY D . n 
D 1 76  ARG 76  107 107 ARG ARG D . n 
D 1 77  TYR 77  108 108 TYR TYR D . n 
D 1 78  PRO 78  109 109 PRO PRO D . n 
D 1 79  HIS 79  110 110 HIS HIS D . n 
D 1 80  LEU 80  111 111 LEU LEU D . n 
D 1 81  THR 81  112 112 THR THR D . n 
D 1 82  GLY 82  113 113 GLY GLY D . n 
D 1 83  THR 83  114 114 THR THR D . n 
D 1 84  ALA 84  115 115 ALA ALA D . n 
D 1 85  TYR 85  116 116 TYR TYR D . n 
D 1 86  ASN 86  117 117 ASN ASN D . n 
D 1 87  LEU 87  118 118 LEU LEU D . n 
D 1 88  PHE 88  119 119 PHE PHE D . n 
D 1 89  HIS 89  120 120 HIS HIS D . n 
D 1 90  ASN 90  121 121 ASN ASN D . n 
D 1 91  SER 91  122 122 SER SER D . n 
D 1 92  SER 92  123 123 SER SER D . n 
D 1 93  GLU 93  124 124 GLU GLU D . n 
D 1 94  ASP 94  125 125 ASP ASP D . n 
D 1 95  ASP 95  126 126 ASP ASP D . n 
D 1 96  LYS 96  127 127 LYS LYS D . n 
D 1 97  ASP 97  128 128 ASP ASP D . n 
D 1 98  ASN 98  129 129 ASN ASN D . n 
D 1 99  MET 99  130 130 MET MET D . n 
D 1 100 GLY 100 131 131 GLY GLY D . n 
D 1 101 VAL 101 132 132 VAL VAL D . n 
D 1 102 PRO 102 133 133 PRO PRO D . n 
D 1 103 VAL 103 134 134 VAL VAL D . n 
D 1 104 GLU 104 135 135 GLU GLU D . n 
D 1 105 GLU 105 136 136 GLU GLU D . n 
D 1 106 THR 106 137 137 THR THR D . n 
D 1 107 TYR 107 138 138 TYR TYR D . n 
D 1 108 MET 108 139 139 MET MET D . n 
D 1 109 SER 109 140 140 SER SER D . n 
D 1 110 LYS 110 141 141 LYS LYS D . n 
D 1 111 VAL 111 142 142 VAL VAL D . n 
D 1 112 LEU 112 143 143 LEU LEU D . n 
D 1 113 GLN 113 144 144 GLN GLN D . n 
D 1 114 ASN 114 145 145 ASN ASN D . n 
D 1 115 ALA 115 146 146 ALA ALA D . n 
D 1 116 GLY 116 147 147 GLY GLY D . n 
D 1 117 TYR 117 148 148 TYR TYR D . n 
D 1 118 TYR 118 149 149 TYR TYR D . n 
D 1 119 THR 119 150 150 THR THR D . n 
D 1 120 SER 120 151 151 SER SER D . n 
D 1 121 ALA 121 152 152 ALA ALA D . n 
D 1 122 ILE 122 153 153 ILE ILE D . n 
D 1 123 GLY 123 154 154 GLY GLY D . n 
D 1 124 LYS 124 155 155 LYS LYS D . n 
D 1 125 TRP 125 156 156 TRP TRP D . n 
D 1 126 HIS 126 157 157 HIS HIS D . n 
D 1 127 LEU 127 158 158 LEU LEU D . n 
D 1 128 GLY 128 159 159 GLY GLY D . n 
D 1 129 ALA 129 160 160 ALA ALA D . n 
D 1 130 ALA 130 161 161 ALA ALA D . n 
D 1 131 PRO 131 162 162 PRO PRO D . n 
D 1 132 LYS 132 163 163 LYS LYS D . n 
D 1 133 PHE 133 164 164 PHE PHE D . n 
D 1 134 HIS 134 165 165 HIS HIS D . n 
D 1 135 PRO 135 166 166 PRO PRO D . n 
D 1 136 ASN 136 167 167 ASN ASN D . n 
D 1 137 LYS 137 168 168 LYS LYS D . n 
D 1 138 ARG 138 169 169 ARG ARG D . n 
D 1 139 GLY 139 170 170 GLY GLY D . n 
D 1 140 PHE 140 171 171 PHE PHE D . n 
D 1 141 ASP 141 172 172 ASP ASP D . n 
D 1 142 ASP 142 173 173 ASP ASP D . n 
D 1 143 PHE 143 174 174 PHE PHE D . n 
D 1 144 TYR 144 175 175 TYR TYR D . n 
D 1 145 GLY 145 176 176 GLY GLY D . n 
D 1 146 PHE 146 177 177 PHE PHE D . n 
D 1 147 LEU 147 178 178 LEU LEU D . n 
D 1 148 GLY 148 179 179 GLY GLY D . n 
D 1 149 GLY 149 180 180 GLY GLY D . n 
D 1 150 GLY 150 181 181 GLY GLY D . n 
D 1 151 HIS 151 182 182 HIS HIS D . n 
D 1 152 ASP 152 183 183 ASP ASP D . n 
D 1 153 TYR 153 184 184 TYR TYR D . n 
D 1 154 PHE 154 185 185 PHE PHE D . n 
D 1 155 PRO 155 186 186 PRO PRO D . n 
D 1 156 SER 156 187 187 SER SER D . n 
D 1 157 GLU 157 188 188 GLU GLU D . n 
D 1 158 TYR 158 189 189 TYR TYR D . n 
D 1 159 GLN 159 190 190 GLN GLN D . n 
D 1 160 LYS 160 191 191 LYS LYS D . n 
D 1 161 THR 161 192 192 THR THR D . n 
D 1 162 TYR 162 193 193 TYR TYR D . n 
D 1 163 LYS 163 194 194 LYS LYS D . n 
D 1 164 ALA 164 195 195 ALA ALA D . n 
D 1 165 GLN 165 196 196 GLN GLN D . n 
D 1 166 LYS 166 197 197 LYS LYS D . n 
D 1 167 LYS 167 198 198 LYS LYS D . n 
D 1 168 ALA 168 199 199 ALA ALA D . n 
D 1 169 GLY 169 200 200 GLY GLY D . n 
D 1 170 ASN 170 201 201 ASN ASN D . n 
D 1 171 PRO 171 202 202 PRO PRO D . n 
D 1 172 ASN 172 203 203 ASN ASN D . n 
D 1 173 ILE 173 204 204 ILE ILE D . n 
D 1 174 ARG 174 205 205 ARG ARG D . n 
D 1 175 ASP 175 206 206 ASP ASP D . n 
D 1 176 TYR 176 207 207 TYR TYR D . n 
D 1 177 VAL 177 208 208 VAL VAL D . n 
D 1 178 PHE 178 209 209 PHE PHE D . n 
D 1 179 PRO 179 210 210 PRO PRO D . n 
D 1 180 MET 180 211 211 MET MET D . n 
D 1 181 GLU 181 212 212 GLU GLU D . n 
D 1 182 HIS 182 213 213 HIS HIS D . n 
D 1 183 ASN 183 214 214 ASN ASN D . n 
D 1 184 GLY 184 215 215 GLY GLY D . n 
D 1 185 LYS 185 216 216 LYS LYS D . n 
D 1 186 PRO 186 217 217 PRO PRO D . n 
D 1 187 ALA 187 218 218 ALA ALA D . n 
D 1 188 ASN 188 219 219 ASN ASN D . n 
D 1 189 GLU 189 220 220 GLU GLU D . n 
D 1 190 THR 190 221 221 THR THR D . n 
D 1 191 GLU 191 222 222 GLU GLU D . n 
D 1 192 TYR 192 223 223 TYR TYR D . n 
D 1 193 ILE 193 224 224 ILE ILE D . n 
D 1 194 THR 194 225 225 THR THR D . n 
D 1 195 ASP 195 226 226 ASP ASP D . n 
D 1 196 GLY 196 227 227 GLY GLY D . n 
D 1 197 PHE 197 228 228 PHE PHE D . n 
D 1 198 SER 198 229 229 SER SER D . n 
D 1 199 ARG 199 230 230 ARG ARG D . n 
D 1 200 GLU 200 231 231 GLU GLU D . n 
D 1 201 ALA 201 232 232 ALA ALA D . n 
D 1 202 ILE 202 233 233 ILE ILE D . n 
D 1 203 LYS 203 234 234 LYS LYS D . n 
D 1 204 ASN 204 235 235 ASN ASN D . n 
D 1 205 ILE 205 236 236 ILE ILE D . n 
D 1 206 LYS 206 237 237 LYS LYS D . n 
D 1 207 ILE 207 238 238 ILE ILE D . n 
D 1 208 ALA 208 239 239 ALA ALA D . n 
D 1 209 ALA 209 240 240 ALA ALA D . n 
D 1 210 ALA 210 241 241 ALA ALA D . n 
D 1 211 LYS 211 242 242 LYS LYS D . n 
D 1 212 LYS 212 243 243 LYS LYS D . n 
D 1 213 GLN 213 244 244 GLN GLN D . n 
D 1 214 PRO 214 245 245 PRO PRO D . n 
D 1 215 PHE 215 246 246 PHE PHE D . n 
D 1 216 PHE 216 247 247 PHE PHE D . n 
D 1 217 ILE 217 248 248 ILE ILE D . n 
D 1 218 TYR 218 249 249 TYR TYR D . n 
D 1 219 LEU 219 250 250 LEU LEU D . n 
D 1 220 ALA 220 251 251 ALA ALA D . n 
D 1 221 TYR 221 252 252 TYR TYR D . n 
D 1 222 ASN 222 253 253 ASN ASN D . n 
D 1 223 ALA 223 254 254 ALA ALA D . n 
D 1 224 PRO 224 255 255 PRO PRO D . n 
D 1 225 HIS 225 256 256 HIS HIS D . n 
D 1 226 VAL 226 257 257 VAL VAL D . n 
D 1 227 PRO 227 258 258 PRO PRO D . n 
D 1 228 LEU 228 259 259 LEU LEU D . n 
D 1 229 GLN 229 260 260 GLN GLN D . n 
D 1 230 ALA 230 261 261 ALA ALA D . n 
D 1 231 LYS 231 262 262 LYS LYS D . n 
D 1 232 ALA 232 263 263 ALA ALA D . n 
D 1 233 GLU 233 264 264 GLU GLU D . n 
D 1 234 ASP 234 265 265 ASP ASP D . n 
D 1 235 VAL 235 266 266 VAL VAL D . n 
D 1 236 ALA 236 267 267 ALA ALA D . n 
D 1 237 LYS 237 268 268 LYS LYS D . n 
D 1 238 PHE 238 269 269 PHE PHE D . n 
D 1 239 ALA 239 270 270 ALA ALA D . n 
D 1 240 HIS 240 271 271 HIS HIS D . n 
D 1 241 ILE 241 272 272 ILE ILE D . n 
D 1 242 LYS 242 273 273 LYS LYS D . n 
D 1 243 ASP 243 274 274 ASP ASP D . n 
D 1 244 LYS 244 275 275 LYS LYS D . n 
D 1 245 ASP 245 276 276 ASP ASP D . n 
D 1 246 ARG 246 277 277 ARG ARG D . n 
D 1 247 ARG 247 278 278 ARG ARG D . n 
D 1 248 THR 248 279 279 THR THR D . n 
D 1 249 TYR 249 280 280 TYR TYR D . n 
D 1 250 ALA 250 281 281 ALA ALA D . n 
D 1 251 ALA 251 282 282 ALA ALA D . n 
D 1 252 MET 252 283 283 MET MET D . n 
D 1 253 VAL 253 284 284 VAL VAL D . n 
D 1 254 TYR 254 285 285 TYR TYR D . n 
D 1 255 ALA 255 286 286 ALA ALA D . n 
D 1 256 VAL 256 287 287 VAL VAL D . n 
D 1 257 ASP 257 288 288 ASP ASP D . n 
D 1 258 ARG 258 289 289 ARG ARG D . n 
D 1 259 GLY 259 290 290 GLY GLY D . n 
D 1 260 VAL 260 291 291 VAL VAL D . n 
D 1 261 GLY 261 292 292 GLY GLY D . n 
D 1 262 LYS 262 293 293 LYS LYS D . n 
D 1 263 ILE 263 294 294 ILE ILE D . n 
D 1 264 VAL 264 295 295 VAL VAL D . n 
D 1 265 GLN 265 296 296 GLN GLN D . n 
D 1 266 THR 266 297 297 THR THR D . n 
D 1 267 LEU 267 298 298 LEU LEU D . n 
D 1 268 LYS 268 299 299 LYS LYS D . n 
D 1 269 GLU 269 300 300 GLU GLU D . n 
D 1 270 THR 270 301 301 THR THR D . n 
D 1 271 LYS 271 302 302 LYS LYS D . n 
D 1 272 GLN 272 303 303 GLN GLN D . n 
D 1 273 PHE 273 304 304 PHE PHE D . n 
D 1 274 ASP 274 305 305 ASP ASP D . n 
D 1 275 ASN 275 306 306 ASN ASN D . n 
D 1 276 THR 276 307 307 THR THR D . n 
D 1 277 LEU 277 308 308 LEU LEU D . n 
D 1 278 ILE 278 309 309 ILE ILE D . n 
D 1 279 VAL 279 310 310 VAL VAL D . n 
D 1 280 PHE 280 311 311 PHE PHE D . n 
D 1 281 LEU 281 312 312 LEU LEU D . n 
D 1 282 SER 282 313 313 SER SER D . n 
D 1 283 ASP 283 314 314 ASP ASP D . n 
D 1 284 ASN 284 315 315 ASN ASN D . n 
D 1 285 GLY 285 316 316 GLY GLY D . n 
D 1 286 GLY 286 317 317 GLY GLY D . n 
D 1 287 ASN 287 318 318 ASN ASN D . n 
D 1 288 PHE 288 319 319 PHE PHE D . n 
D 1 289 ASN 289 320 320 ASN ASN D . n 
D 1 290 HIS 290 321 321 HIS HIS D . n 
D 1 291 GLY 291 322 322 GLY GLY D . n 
D 1 292 ALA 292 323 323 ALA ALA D . n 
D 1 293 ASN 293 324 324 ASN ASN D . n 
D 1 294 ASN 294 325 325 ASN ASN D . n 
D 1 295 TYR 295 326 326 TYR TYR D . n 
D 1 296 PRO 296 327 327 PRO PRO D . n 
D 1 297 LEU 297 328 328 LEU LEU D . n 
D 1 298 LYS 298 329 329 LYS LYS D . n 
D 1 299 GLY 299 330 330 GLY GLY D . n 
D 1 300 THR 300 331 331 THR THR D . n 
D 1 301 LYS 301 332 332 LYS LYS D . n 
D 1 302 GLY 302 333 333 GLY GLY D . n 
D 1 303 ASP 303 334 334 ASP ASP D . n 
D 1 304 THR 304 335 335 THR THR D . n 
D 1 305 TRP 305 336 336 TRP TRP D . n 
D 1 306 GLU 306 337 337 GLU GLU D . n 
D 1 307 GLY 307 338 338 GLY GLY D . n 
D 1 308 GLY 308 339 339 GLY GLY D . n 
D 1 309 TYR 309 340 340 TYR TYR D . n 
D 1 310 ARG 310 341 341 ARG ARG D . n 
D 1 311 VAL 311 342 342 VAL VAL D . n 
D 1 312 PRO 312 343 343 PRO PRO D . n 
D 1 313 MET 313 344 344 MET MET D . n 
D 1 314 PHE 314 345 345 PHE PHE D . n 
D 1 315 PHE 315 346 346 PHE PHE D . n 
D 1 316 HIS 316 347 347 HIS HIS D . n 
D 1 317 TRP 317 348 348 TRP TRP D . n 
D 1 318 PRO 318 349 349 PRO PRO D . n 
D 1 319 LYS 319 350 350 LYS LYS D . n 
D 1 320 LYS 320 351 351 LYS LYS D . n 
D 1 321 ILE 321 352 352 ILE ILE D . n 
D 1 322 LYS 322 353 353 LYS LYS D . n 
D 1 323 LYS 323 354 354 LYS LYS D . n 
D 1 324 ASP 324 355 355 ASP ASP D . n 
D 1 325 GLN 325 356 356 GLN GLN D . n 
D 1 326 ARG 326 357 357 ARG ARG D . n 
D 1 327 PHE 327 358 358 PHE PHE D . n 
D 1 328 ASP 328 359 359 ASP ASP D . n 
D 1 329 PHE 329 360 360 PHE PHE D . n 
D 1 330 PRO 330 361 361 PRO PRO D . n 
D 1 331 VAL 331 362 362 VAL VAL D . n 
D 1 332 SER 332 363 363 SER SER D . n 
D 1 333 SER 333 364 364 SER SER D . n 
D 1 334 LEU 334 365 365 LEU LEU D . n 
D 1 335 ASP 335 366 366 ASP ASP D . n 
D 1 336 LEU 336 367 367 LEU LEU D . n 
D 1 337 TYR 337 368 368 TYR TYR D . n 
D 1 338 PRO 338 369 369 PRO PRO D . n 
D 1 339 THR 339 370 370 THR THR D . n 
D 1 340 PHE 340 371 371 PHE PHE D . n 
D 1 341 THR 341 372 372 THR THR D . n 
D 1 342 GLY 342 373 373 GLY GLY D . n 
D 1 343 LEU 343 374 374 LEU LEU D . n 
D 1 344 ALA 344 375 375 ALA ALA D . n 
D 1 345 GLU 345 376 376 GLU GLU D . n 
D 1 346 ALA 346 377 377 ALA ALA D . n 
D 1 347 LYS 347 378 378 LYS LYS D . n 
D 1 348 LEU 348 379 379 LEU LEU D . n 
D 1 349 PRO 349 380 380 PRO PRO D . n 
D 1 350 LYS 350 381 381 LYS LYS D . n 
D 1 351 GLY 351 382 382 GLY GLY D . n 
D 1 352 LYS 352 383 383 LYS LYS D . n 
D 1 353 GLN 353 384 384 GLN GLN D . n 
D 1 354 LEU 354 385 385 LEU LEU D . n 
D 1 355 ASP 355 386 386 ASP ASP D . n 
D 1 356 GLY 356 387 387 GLY GLY D . n 
D 1 357 LYS 357 388 388 LYS LYS D . n 
D 1 358 ASN 358 389 389 ASN ASN D . n 
D 1 359 ILE 359 390 390 ILE ILE D . n 
D 1 360 MET 360 391 391 MET MET D . n 
D 1 361 ASP 361 392 392 ASP ASP D . n 
D 1 362 ASP 362 393 393 ASP ASP D . n 
D 1 363 VAL 363 394 394 VAL VAL D . n 
D 1 364 LEU 364 395 395 LEU LEU D . n 
D 1 365 LYS 365 396 396 LYS LYS D . n 
D 1 366 ASN 366 397 397 ASN ASN D . n 
D 1 367 THR 367 398 398 THR THR D . n 
D 1 368 GLU 368 399 399 GLU GLU D . n 
D 1 369 PRO 369 400 400 PRO PRO D . n 
D 1 370 TYR 370 401 401 TYR TYR D . n 
D 1 371 LYS 371 402 402 LYS LYS D . n 
D 1 372 ASP 372 403 403 ASP ASP D . n 
D 1 373 GLU 373 404 404 GLU GLU D . n 
D 1 374 MET 374 405 405 MET MET D . n 
D 1 375 ILE 375 406 406 ILE ILE D . n 
D 1 376 TYR 376 407 407 TYR TYR D . n 
D 1 377 SER 377 408 408 SER SER D . n 
D 1 378 LEU 378 409 409 LEU LEU D . n 
D 1 379 ARG 379 410 410 ARG ARG D . n 
D 1 380 TYR 380 411 411 TYR TYR D . n 
D 1 381 ARG 381 412 412 ARG ARG D . n 
D 1 382 GLU 382 413 413 GLU GLU D . n 
D 1 383 GLY 383 414 414 GLY GLY D . n 
D 1 384 TYR 384 415 415 TYR TYR D . n 
D 1 385 ASN 385 416 416 ASN ASN D . n 
D 1 386 ASP 386 417 417 ASP ASP D . n 
D 1 387 VAL 387 418 418 VAL VAL D . n 
D 1 388 GLY 388 419 419 GLY GLY D . n 
D 1 389 ALA 389 420 420 ALA ALA D . n 
D 1 390 ARG 390 421 421 ARG ARG D . n 
D 1 391 MET 391 422 422 MET MET D . n 
D 1 392 GLY 392 423 423 GLY GLY D . n 
D 1 393 ASP 393 424 424 ASP ASP D . n 
D 1 394 TRP 394 425 425 TRP TRP D . n 
D 1 395 LYS 395 426 426 LYS LYS D . n 
D 1 396 ILE 396 427 427 ILE ILE D . n 
D 1 397 THR 397 428 428 THR THR D . n 
D 1 398 ARG 398 429 429 ARG ARG D . n 
D 1 399 MET 399 430 430 MET MET D . n 
D 1 400 GLY 400 431 431 GLY GLY D . n 
D 1 401 ASN 401 432 432 ASN ASN D . n 
D 1 402 GLU 402 433 433 GLU GLU D . n 
D 1 403 PRO 403 434 434 PRO PRO D . n 
D 1 404 TRP 404 435 435 TRP TRP D . n 
D 1 405 ARG 405 436 436 ARG ARG D . n 
D 1 406 LEU 406 437 437 LEU LEU D . n 
D 1 407 HIS 407 438 438 HIS HIS D . n 
D 1 408 ASN 408 439 439 ASN ASN D . n 
D 1 409 ILE 409 440 440 ILE ILE D . n 
D 1 410 THR 410 441 441 THR THR D . n 
D 1 411 GLN 411 442 442 GLN GLN D . n 
D 1 412 ASP 412 443 443 ASP ASP D . n 
D 1 413 ILE 413 444 444 ILE ILE D . n 
D 1 414 GLY 414 445 445 GLY GLY D . n 
D 1 415 GLU 415 446 446 GLU GLU D . n 
D 1 416 LYS 416 447 447 LYS LYS D . n 
D 1 417 LYS 417 448 448 LYS LYS D . n 
D 1 418 ASN 418 449 449 ASN ASN D . n 
D 1 419 LEU 419 450 450 LEU LEU D . n 
D 1 420 ALA 420 451 451 ALA ALA D . n 
D 1 421 GLY 421 452 452 GLY GLY D . n 
D 1 422 ARG 422 453 453 ARG ARG D . n 
D 1 423 TYR 423 454 454 TYR TYR D . n 
D 1 424 PRO 424 455 455 PRO PRO D . n 
D 1 425 ASP 425 456 456 ASP ASP D . n 
D 1 426 ARG 426 457 457 ARG ARG D . n 
D 1 427 LEU 427 458 458 LEU LEU D . n 
D 1 428 LYS 428 459 459 LYS LYS D . n 
D 1 429 GLU 429 460 460 GLU GLU D . n 
D 1 430 MET 430 461 461 MET MET D . n 
D 1 431 ILE 431 462 462 ILE ILE D . n 
D 1 432 ALA 432 463 463 ALA ALA D . n 
D 1 433 LYS 433 464 464 LYS LYS D . n 
D 1 434 THR 434 465 465 THR THR D . n 
D 1 435 GLN 435 466 466 GLN GLN D . n 
D 1 436 GLU 436 467 467 GLU GLU D . n 
D 1 437 TRP 437 468 468 TRP TRP D . n 
D 1 438 THR 438 469 469 THR THR D . n 
D 1 439 LYS 439 470 470 LYS LYS D . n 
D 1 440 SER 440 471 471 SER SER D . n 
D 1 441 PHE 441 472 472 PHE PHE D . n 
D 1 442 VAL 442 473 473 VAL VAL D . n 
D 1 443 LYS 443 474 474 LYS LYS D . n 
D 1 444 PRO 444 475 475 PRO PRO D . n 
D 1 445 LEU 445 476 476 LEU LEU D . n 
D 1 446 TRP 446 477 477 TRP TRP D . n 
D 1 447 VAL 447 478 478 VAL VAL D . n 
D 1 448 TYR 448 479 479 TYR TYR D . n 
D 1 449 SER 449 480 480 SER SER D . n 
D 1 450 VAL 450 481 481 VAL VAL D . n 
D 1 451 LYS 451 482 482 LYS LYS D . n 
D 1 452 ASP 452 483 483 ASP ASP D . n 
D 1 453 LYS 453 484 484 LYS LYS D . n 
D 1 454 GLU 454 485 485 GLU GLU D . n 
D 1 455 LEU 455 486 486 LEU LEU D . n 
D 1 456 TRP 456 487 487 TRP TRP D . n 
D 1 457 GLU 457 488 488 GLU GLU D . n 
D 1 458 SER 458 489 489 SER SER D . n 
D 1 459 GLY 459 490 490 GLY GLY D . n 
D 1 460 GLN 460 491 491 GLN GLN D . n 
D 1 461 MET 461 492 492 MET MET D . n 
D 1 462 PRO 462 493 493 PRO PRO D . n 
D 1 463 ASN 463 494 494 ASN ASN D . n 
D 1 464 TYR 464 495 495 TYR TYR D . n 
D 1 465 GLU 465 496 496 GLU GLU D . n 
D 1 466 ALA 466 497 497 ALA ALA D . n 
D 1 467 THR 467 498 498 THR THR D . n 
D 1 468 PHE 468 499 499 PHE PHE D . n 
D 1 469 GLU 469 500 500 GLU GLU D . n 
D 1 470 VAL 470 501 501 VAL VAL D . n 
D 1 471 ASP 471 502 502 ASP ASP D . n 
D 1 472 LYS 472 503 503 LYS LYS D . n 
D 1 473 LEU 473 504 504 LEU LEU D . n 
D 1 474 VAL 474 505 505 VAL VAL D . n 
D 1 475 ASP 475 506 506 ASP ASP D . n 
D 1 476 SER 476 507 507 SER SER D . n 
D 1 477 PRO 477 508 508 PRO PRO D . n 
D 1 478 TYR 478 509 509 TYR TYR D . n 
D 1 479 HIS 479 510 ?   ?   ?   D . n 
D 1 480 LYS 480 511 ?   ?   ?   D . 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 DDZ ? ? DDZ ? ? 'SUBJECT OF INVESTIGATION' ? 
2 CA  ? ? CA  ? ? '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 
E  2 BR  1   601 1   BR  BR  A . 
F  2 BR  1   602 3   BR  BR  A . 
G  3 CL  1   603 2   CL  CL  A . 
H  3 CL  1   604 3   CL  CL  A . 
I  3 CL  1   605 5   CL  CL  A . 
J  3 CL  1   606 6   CL  CL  A . 
K  3 CL  1   607 9   CL  CL  A . 
L  3 CL  1   608 13  CL  CL  A . 
M  3 CL  1   609 15  CL  CL  A . 
N  3 CL  1   610 19  CL  CL  A . 
O  3 CL  1   611 24  CL  CL  A . 
P  4 CA  1   612 4   CA  CA  A . 
Q  2 BR  1   601 2   BR  BR  B . 
R  2 BR  1   602 5   BR  BR  B . 
S  2 BR  1   603 8   BR  BR  B . 
T  2 BR  1   604 10  BR  BR  B . 
U  3 CL  1   605 4   CL  CL  B . 
V  3 CL  1   606 7   CL  CL  B . 
W  3 CL  1   607 14  CL  CL  B . 
X  3 CL  1   608 18  CL  CL  B . 
Y  3 CL  1   609 20  CL  CL  B . 
Z  4 CA  1   610 6   CA  CA  B . 
AA 2 BR  1   601 6   BR  BR  C . 
BA 2 BR  1   602 9   BR  BR  C . 
CA 3 CL  1   603 8   CL  CL  C . 
DA 3 CL  1   604 12  CL  CL  C . 
EA 3 CL  1   605 16  CL  CL  C . 
FA 3 CL  1   606 17  CL  CL  C . 
GA 3 CL  1   607 26  CL  CL  C . 
HA 4 CA  1   608 7   CA  CA  C . 
IA 2 BR  1   601 4   BR  BR  D . 
JA 2 BR  1   602 7   BR  BR  D . 
KA 3 CL  1   603 10  CL  CL  D . 
LA 3 CL  1   604 11  CL  CL  D . 
MA 3 CL  1   605 21  CL  CL  D . 
NA 3 CL  1   606 22  CL  CL  D . 
OA 3 CL  1   607 23  CL  CL  D . 
PA 3 CL  1   608 25  CL  CL  D . 
QA 4 CA  1   609 5   CA  CA  D . 
RA 5 HOH 1   701 307 HOH HOH A . 
RA 5 HOH 2   702 288 HOH HOH A . 
RA 5 HOH 3   703 376 HOH HOH A . 
RA 5 HOH 4   704 260 HOH HOH A . 
RA 5 HOH 5   705 55  HOH HOH A . 
RA 5 HOH 6   706 297 HOH HOH A . 
RA 5 HOH 7   707 144 HOH HOH A . 
RA 5 HOH 8   708 224 HOH HOH A . 
RA 5 HOH 9   709 221 HOH HOH A . 
RA 5 HOH 10  710 511 HOH HOH A . 
RA 5 HOH 11  711 391 HOH HOH A . 
RA 5 HOH 12  712 122 HOH HOH A . 
RA 5 HOH 13  713 238 HOH HOH A . 
RA 5 HOH 14  714 52  HOH HOH A . 
RA 5 HOH 15  715 121 HOH HOH A . 
RA 5 HOH 16  716 499 HOH HOH A . 
RA 5 HOH 17  717 441 HOH HOH A . 
RA 5 HOH 18  718 364 HOH HOH A . 
RA 5 HOH 19  719 343 HOH HOH A . 
RA 5 HOH 20  720 114 HOH HOH A . 
RA 5 HOH 21  721 117 HOH HOH A . 
RA 5 HOH 22  722 109 HOH HOH A . 
RA 5 HOH 23  723 36  HOH HOH A . 
RA 5 HOH 24  724 220 HOH HOH A . 
RA 5 HOH 25  725 41  HOH HOH A . 
RA 5 HOH 26  726 49  HOH HOH A . 
RA 5 HOH 27  727 135 HOH HOH A . 
RA 5 HOH 28  728 100 HOH HOH A . 
RA 5 HOH 29  729 362 HOH HOH A . 
RA 5 HOH 30  730 60  HOH HOH A . 
RA 5 HOH 31  731 47  HOH HOH A . 
RA 5 HOH 32  732 549 HOH HOH A . 
RA 5 HOH 33  733 111 HOH HOH A . 
RA 5 HOH 34  734 181 HOH HOH A . 
RA 5 HOH 35  735 92  HOH HOH A . 
RA 5 HOH 36  736 384 HOH HOH A . 
RA 5 HOH 37  737 241 HOH HOH A . 
RA 5 HOH 38  738 352 HOH HOH A . 
RA 5 HOH 39  739 407 HOH HOH A . 
RA 5 HOH 40  740 74  HOH HOH A . 
RA 5 HOH 41  741 67  HOH HOH A . 
RA 5 HOH 42  742 383 HOH HOH A . 
RA 5 HOH 43  743 538 HOH HOH A . 
RA 5 HOH 44  744 69  HOH HOH A . 
RA 5 HOH 45  745 81  HOH HOH A . 
RA 5 HOH 46  746 379 HOH HOH A . 
RA 5 HOH 47  747 406 HOH HOH A . 
RA 5 HOH 48  748 78  HOH HOH A . 
RA 5 HOH 49  749 57  HOH HOH A . 
RA 5 HOH 50  750 25  HOH HOH A . 
RA 5 HOH 51  751 77  HOH HOH A . 
RA 5 HOH 52  752 309 HOH HOH A . 
RA 5 HOH 53  753 174 HOH HOH A . 
RA 5 HOH 54  754 203 HOH HOH A . 
RA 5 HOH 55  755 66  HOH HOH A . 
RA 5 HOH 56  756 427 HOH HOH A . 
RA 5 HOH 57  757 152 HOH HOH A . 
RA 5 HOH 58  758 201 HOH HOH A . 
RA 5 HOH 59  759 84  HOH HOH A . 
RA 5 HOH 60  760 374 HOH HOH A . 
RA 5 HOH 61  761 62  HOH HOH A . 
RA 5 HOH 62  762 31  HOH HOH A . 
RA 5 HOH 63  763 115 HOH HOH A . 
RA 5 HOH 64  764 223 HOH HOH A . 
RA 5 HOH 65  765 470 HOH HOH A . 
RA 5 HOH 66  766 228 HOH HOH A . 
RA 5 HOH 67  767 311 HOH HOH A . 
RA 5 HOH 68  768 296 HOH HOH A . 
RA 5 HOH 69  769 142 HOH HOH A . 
RA 5 HOH 70  770 496 HOH HOH A . 
RA 5 HOH 71  771 106 HOH HOH A . 
RA 5 HOH 72  772 457 HOH HOH A . 
RA 5 HOH 73  773 134 HOH HOH A . 
RA 5 HOH 74  774 387 HOH HOH A . 
RA 5 HOH 75  775 116 HOH HOH A . 
RA 5 HOH 76  776 159 HOH HOH A . 
RA 5 HOH 77  777 216 HOH HOH A . 
RA 5 HOH 78  778 409 HOH HOH A . 
RA 5 HOH 79  779 416 HOH HOH A . 
RA 5 HOH 80  780 97  HOH HOH A . 
RA 5 HOH 81  781 435 HOH HOH A . 
RA 5 HOH 82  782 182 HOH HOH A . 
RA 5 HOH 83  783 270 HOH HOH A . 
RA 5 HOH 84  784 301 HOH HOH A . 
RA 5 HOH 85  785 171 HOH HOH A . 
RA 5 HOH 86  786 194 HOH HOH A . 
RA 5 HOH 87  787 351 HOH HOH A . 
RA 5 HOH 88  788 404 HOH HOH A . 
RA 5 HOH 89  789 304 HOH HOH A . 
RA 5 HOH 90  790 526 HOH HOH A . 
RA 5 HOH 91  791 524 HOH HOH A . 
RA 5 HOH 92  792 146 HOH HOH A . 
RA 5 HOH 93  793 520 HOH HOH A . 
RA 5 HOH 94  794 131 HOH HOH A . 
RA 5 HOH 95  795 353 HOH HOH A . 
RA 5 HOH 96  796 107 HOH HOH A . 
RA 5 HOH 97  797 129 HOH HOH A . 
RA 5 HOH 98  798 76  HOH HOH A . 
RA 5 HOH 99  799 489 HOH HOH A . 
RA 5 HOH 100 800 40  HOH HOH A . 
RA 5 HOH 101 801 276 HOH HOH A . 
RA 5 HOH 102 802 315 HOH HOH A . 
RA 5 HOH 103 803 209 HOH HOH A . 
RA 5 HOH 104 804 80  HOH HOH A . 
RA 5 HOH 105 805 286 HOH HOH A . 
RA 5 HOH 106 806 179 HOH HOH A . 
RA 5 HOH 107 807 235 HOH HOH A . 
RA 5 HOH 108 808 112 HOH HOH A . 
RA 5 HOH 109 809 37  HOH HOH A . 
RA 5 HOH 110 810 456 HOH HOH A . 
RA 5 HOH 111 811 10  HOH HOH A . 
RA 5 HOH 112 812 277 HOH HOH A . 
RA 5 HOH 113 813 125 HOH HOH A . 
RA 5 HOH 114 814 160 HOH HOH A . 
RA 5 HOH 115 815 492 HOH HOH A . 
RA 5 HOH 116 816 438 HOH HOH A . 
RA 5 HOH 117 817 519 HOH HOH A . 
RA 5 HOH 118 818 185 HOH HOH A . 
RA 5 HOH 119 819 128 HOH HOH A . 
RA 5 HOH 120 820 349 HOH HOH A . 
RA 5 HOH 121 821 322 HOH HOH A . 
RA 5 HOH 122 822 488 HOH HOH A . 
RA 5 HOH 123 823 497 HOH HOH A . 
RA 5 HOH 124 824 87  HOH HOH A . 
RA 5 HOH 125 825 342 HOH HOH A . 
RA 5 HOH 126 826 257 HOH HOH A . 
RA 5 HOH 127 827 341 HOH HOH A . 
RA 5 HOH 128 828 394 HOH HOH A . 
RA 5 HOH 129 829 444 HOH HOH A . 
RA 5 HOH 130 830 468 HOH HOH A . 
RA 5 HOH 131 831 79  HOH HOH A . 
RA 5 HOH 132 832 521 HOH HOH A . 
RA 5 HOH 133 833 443 HOH HOH A . 
RA 5 HOH 134 834 525 HOH HOH A . 
RA 5 HOH 135 835 285 HOH HOH A . 
RA 5 HOH 136 836 19  HOH HOH A . 
RA 5 HOH 137 837 279 HOH HOH A . 
RA 5 HOH 138 838 155 HOH HOH A . 
RA 5 HOH 139 839 491 HOH HOH A . 
RA 5 HOH 140 840 166 HOH HOH A . 
RA 5 HOH 141 841 177 HOH HOH A . 
RA 5 HOH 142 842 517 HOH HOH A . 
RA 5 HOH 143 843 527 HOH HOH A . 
RA 5 HOH 144 844 54  HOH HOH A . 
RA 5 HOH 145 845 514 HOH HOH A . 
RA 5 HOH 146 846 72  HOH HOH A . 
RA 5 HOH 147 847 493 HOH HOH A . 
RA 5 HOH 148 848 338 HOH HOH A . 
RA 5 HOH 149 849 258 HOH HOH A . 
RA 5 HOH 150 850 472 HOH HOH A . 
RA 5 HOH 151 851 554 HOH HOH A . 
RA 5 HOH 152 852 90  HOH HOH A . 
RA 5 HOH 153 853 317 HOH HOH A . 
RA 5 HOH 154 854 243 HOH HOH A . 
RA 5 HOH 155 855 272 HOH HOH A . 
RA 5 HOH 156 856 278 HOH HOH A . 
RA 5 HOH 157 857 518 HOH HOH A . 
RA 5 HOH 158 858 332 HOH HOH A . 
RA 5 HOH 159 859 528 HOH HOH A . 
RA 5 HOH 160 860 71  HOH HOH A . 
RA 5 HOH 161 861 490 HOH HOH A . 
RA 5 HOH 162 862 467 HOH HOH A . 
RA 5 HOH 163 863 473 HOH HOH A . 
RA 5 HOH 164 864 501 HOH HOH A . 
RA 5 HOH 165 865 515 HOH HOH A . 
RA 5 HOH 166 866 513 HOH HOH A . 
RA 5 HOH 167 867 214 HOH HOH A . 
RA 5 HOH 168 868 510 HOH HOH A . 
RA 5 HOH 169 869 523 HOH HOH A . 
RA 5 HOH 170 870 165 HOH HOH A . 
RA 5 HOH 171 871 508 HOH HOH A . 
RA 5 HOH 172 872 367 HOH HOH A . 
RA 5 HOH 173 873 372 HOH HOH A . 
RA 5 HOH 174 874 469 HOH HOH A . 
RA 5 HOH 175 875 553 HOH HOH A . 
RA 5 HOH 176 876 348 HOH HOH A . 
RA 5 HOH 177 877 293 HOH HOH A . 
RA 5 HOH 178 878 512 HOH HOH A . 
RA 5 HOH 179 879 392 HOH HOH A . 
RA 5 HOH 180 880 234 HOH HOH A . 
RA 5 HOH 181 881 509 HOH HOH A . 
RA 5 HOH 182 882 340 HOH HOH A . 
RA 5 HOH 183 883 465 HOH HOH A . 
RA 5 HOH 184 884 328 HOH HOH A . 
RA 5 HOH 185 885 373 HOH HOH A . 
RA 5 HOH 186 886 522 HOH HOH A . 
RA 5 HOH 187 887 500 HOH HOH A . 
RA 5 HOH 188 888 466 HOH HOH A . 
RA 5 HOH 189 889 119 HOH HOH A . 
RA 5 HOH 190 890 494 HOH HOH A . 
RA 5 HOH 191 891 516 HOH HOH A . 
RA 5 HOH 192 892 471 HOH HOH A . 
RA 5 HOH 193 893 498 HOH HOH A . 
RA 5 HOH 194 894 460 HOH HOH A . 
SA 5 HOH 1   701 442 HOH HOH B . 
SA 5 HOH 2   702 252 HOH HOH B . 
SA 5 HOH 3   703 89  HOH HOH B . 
SA 5 HOH 4   704 359 HOH HOH B . 
SA 5 HOH 5   705 541 HOH HOH B . 
SA 5 HOH 6   706 96  HOH HOH B . 
SA 5 HOH 7   707 44  HOH HOH B . 
SA 5 HOH 8   708 169 HOH HOH B . 
SA 5 HOH 9   709 58  HOH HOH B . 
SA 5 HOH 10  710 140 HOH HOH B . 
SA 5 HOH 11  711 289 HOH HOH B . 
SA 5 HOH 12  712 85  HOH HOH B . 
SA 5 HOH 13  713 188 HOH HOH B . 
SA 5 HOH 14  714 339 HOH HOH B . 
SA 5 HOH 15  715 253 HOH HOH B . 
SA 5 HOH 16  716 151 HOH HOH B . 
SA 5 HOH 17  717 380 HOH HOH B . 
SA 5 HOH 18  718 64  HOH HOH B . 
SA 5 HOH 19  719 206 HOH HOH B . 
SA 5 HOH 20  720 346 HOH HOH B . 
SA 5 HOH 21  721 35  HOH HOH B . 
SA 5 HOH 22  722 568 HOH HOH B . 
SA 5 HOH 23  723 156 HOH HOH B . 
SA 5 HOH 24  724 330 HOH HOH B . 
SA 5 HOH 25  725 248 HOH HOH B . 
SA 5 HOH 26  726 318 HOH HOH B . 
SA 5 HOH 27  727 27  HOH HOH B . 
SA 5 HOH 28  728 263 HOH HOH B . 
SA 5 HOH 29  729 178 HOH HOH B . 
SA 5 HOH 30  730 173 HOH HOH B . 
SA 5 HOH 31  731 483 HOH HOH B . 
SA 5 HOH 32  732 244 HOH HOH B . 
SA 5 HOH 33  733 202 HOH HOH B . 
SA 5 HOH 34  734 268 HOH HOH B . 
SA 5 HOH 35  735 445 HOH HOH B . 
SA 5 HOH 36  736 361 HOH HOH B . 
SA 5 HOH 37  737 149 HOH HOH B . 
SA 5 HOH 38  738 99  HOH HOH B . 
SA 5 HOH 39  739 45  HOH HOH B . 
SA 5 HOH 40  740 345 HOH HOH B . 
SA 5 HOH 41  741 24  HOH HOH B . 
SA 5 HOH 42  742 481 HOH HOH B . 
SA 5 HOH 43  743 369 HOH HOH B . 
SA 5 HOH 44  744 567 HOH HOH B . 
SA 5 HOH 45  745 295 HOH HOH B . 
SA 5 HOH 46  746 143 HOH HOH B . 
SA 5 HOH 47  747 388 HOH HOH B . 
SA 5 HOH 48  748 199 HOH HOH B . 
SA 5 HOH 49  749 164 HOH HOH B . 
SA 5 HOH 50  750 65  HOH HOH B . 
SA 5 HOH 51  751 212 HOH HOH B . 
SA 5 HOH 52  752 153 HOH HOH B . 
SA 5 HOH 53  753 464 HOH HOH B . 
SA 5 HOH 54  754 93  HOH HOH B . 
SA 5 HOH 55  755 415 HOH HOH B . 
SA 5 HOH 56  756 53  HOH HOH B . 
SA 5 HOH 57  757 290 HOH HOH B . 
SA 5 HOH 58  758 344 HOH HOH B . 
SA 5 HOH 59  759 132 HOH HOH B . 
SA 5 HOH 60  760 105 HOH HOH B . 
SA 5 HOH 61  761 59  HOH HOH B . 
SA 5 HOH 62  762 566 HOH HOH B . 
SA 5 HOH 63  763 17  HOH HOH B . 
SA 5 HOH 64  764 150 HOH HOH B . 
SA 5 HOH 65  765 370 HOH HOH B . 
SA 5 HOH 66  766 402 HOH HOH B . 
SA 5 HOH 67  767 316 HOH HOH B . 
SA 5 HOH 68  768 275 HOH HOH B . 
SA 5 HOH 69  769 120 HOH HOH B . 
SA 5 HOH 70  770 237 HOH HOH B . 
SA 5 HOH 71  771 141 HOH HOH B . 
SA 5 HOH 72  772 192 HOH HOH B . 
SA 5 HOH 73  773 291 HOH HOH B . 
SA 5 HOH 74  774 30  HOH HOH B . 
SA 5 HOH 75  775 226 HOH HOH B . 
SA 5 HOH 76  776 505 HOH HOH B . 
SA 5 HOH 77  777 190 HOH HOH B . 
SA 5 HOH 78  778 355 HOH HOH B . 
SA 5 HOH 79  779 187 HOH HOH B . 
SA 5 HOH 80  780 101 HOH HOH B . 
SA 5 HOH 81  781 200 HOH HOH B . 
SA 5 HOH 82  782 42  HOH HOH B . 
SA 5 HOH 83  783 251 HOH HOH B . 
SA 5 HOH 84  784 313 HOH HOH B . 
SA 5 HOH 85  785 46  HOH HOH B . 
SA 5 HOH 86  786 424 HOH HOH B . 
SA 5 HOH 87  787 123 HOH HOH B . 
SA 5 HOH 88  788 563 HOH HOH B . 
SA 5 HOH 89  789 239 HOH HOH B . 
SA 5 HOH 90  790 246 HOH HOH B . 
SA 5 HOH 91  791 265 HOH HOH B . 
SA 5 HOH 92  792 274 HOH HOH B . 
SA 5 HOH 93  793 138 HOH HOH B . 
SA 5 HOH 94  794 163 HOH HOH B . 
SA 5 HOH 95  795 139 HOH HOH B . 
SA 5 HOH 96  796 137 HOH HOH B . 
SA 5 HOH 97  797 82  HOH HOH B . 
SA 5 HOH 98  798 176 HOH HOH B . 
SA 5 HOH 99  799 357 HOH HOH B . 
SA 5 HOH 100 800 102 HOH HOH B . 
SA 5 HOH 101 801 232 HOH HOH B . 
SA 5 HOH 102 802 204 HOH HOH B . 
SA 5 HOH 103 803 485 HOH HOH B . 
SA 5 HOH 104 804 83  HOH HOH B . 
SA 5 HOH 105 805 423 HOH HOH B . 
SA 5 HOH 106 806 61  HOH HOH B . 
SA 5 HOH 107 807 504 HOH HOH B . 
SA 5 HOH 108 808 255 HOH HOH B . 
SA 5 HOH 109 809 347 HOH HOH B . 
SA 5 HOH 110 810 207 HOH HOH B . 
SA 5 HOH 111 811 420 HOH HOH B . 
SA 5 HOH 112 812 447 HOH HOH B . 
SA 5 HOH 113 813 189 HOH HOH B . 
SA 5 HOH 114 814 154 HOH HOH B . 
SA 5 HOH 115 815 145 HOH HOH B . 
SA 5 HOH 116 816 565 HOH HOH B . 
SA 5 HOH 117 817 437 HOH HOH B . 
SA 5 HOH 118 818 227 HOH HOH B . 
SA 5 HOH 119 819 68  HOH HOH B . 
SA 5 HOH 120 820 495 HOH HOH B . 
SA 5 HOH 121 821 205 HOH HOH B . 
SA 5 HOH 122 822 175 HOH HOH B . 
SA 5 HOH 123 823 39  HOH HOH B . 
SA 5 HOH 124 824 271 HOH HOH B . 
SA 5 HOH 125 825 261 HOH HOH B . 
SA 5 HOH 126 826 411 HOH HOH B . 
SA 5 HOH 127 827 73  HOH HOH B . 
SA 5 HOH 128 828 193 HOH HOH B . 
SA 5 HOH 129 829 412 HOH HOH B . 
SA 5 HOH 130 830 371 HOH HOH B . 
SA 5 HOH 131 831 298 HOH HOH B . 
SA 5 HOH 132 832 32  HOH HOH B . 
SA 5 HOH 133 833 103 HOH HOH B . 
SA 5 HOH 134 834 86  HOH HOH B . 
SA 5 HOH 135 835 507 HOH HOH B . 
SA 5 HOH 136 836 215 HOH HOH B . 
SA 5 HOH 137 837 118 HOH HOH B . 
SA 5 HOH 138 838 405 HOH HOH B . 
SA 5 HOH 139 839 231 HOH HOH B . 
SA 5 HOH 140 840 147 HOH HOH B . 
SA 5 HOH 141 841 476 HOH HOH B . 
SA 5 HOH 142 842 560 HOH HOH B . 
SA 5 HOH 143 843 461 HOH HOH B . 
SA 5 HOH 144 844 18  HOH HOH B . 
SA 5 HOH 145 845 389 HOH HOH B . 
SA 5 HOH 146 846 283 HOH HOH B . 
SA 5 HOH 147 847 256 HOH HOH B . 
SA 5 HOH 148 848 459 HOH HOH B . 
SA 5 HOH 149 849 534 HOH HOH B . 
SA 5 HOH 150 850 126 HOH HOH B . 
SA 5 HOH 151 851 417 HOH HOH B . 
SA 5 HOH 152 852 502 HOH HOH B . 
SA 5 HOH 153 853 329 HOH HOH B . 
SA 5 HOH 154 854 446 HOH HOH B . 
SA 5 HOH 155 855 484 HOH HOH B . 
SA 5 HOH 156 856 562 HOH HOH B . 
SA 5 HOH 157 857 543 HOH HOH B . 
SA 5 HOH 158 858 463 HOH HOH B . 
SA 5 HOH 159 859 537 HOH HOH B . 
SA 5 HOH 160 860 545 HOH HOH B . 
SA 5 HOH 161 861 542 HOH HOH B . 
SA 5 HOH 162 862 439 HOH HOH B . 
SA 5 HOH 163 863 363 HOH HOH B . 
SA 5 HOH 164 864 555 HOH HOH B . 
SA 5 HOH 165 865 530 HOH HOH B . 
SA 5 HOH 166 866 558 HOH HOH B . 
SA 5 HOH 167 867 486 HOH HOH B . 
SA 5 HOH 168 868 474 HOH HOH B . 
SA 5 HOH 169 869 124 HOH HOH B . 
SA 5 HOH 170 870 477 HOH HOH B . 
SA 5 HOH 171 871 482 HOH HOH B . 
SA 5 HOH 172 872 462 HOH HOH B . 
SA 5 HOH 173 873 559 HOH HOH B . 
SA 5 HOH 174 874 503 HOH HOH B . 
SA 5 HOH 175 875 458 HOH HOH B . 
SA 5 HOH 176 876 487 HOH HOH B . 
SA 5 HOH 177 877 393 HOH HOH B . 
SA 5 HOH 178 878 385 HOH HOH B . 
SA 5 HOH 179 879 382 HOH HOH B . 
SA 5 HOH 180 880 478 HOH HOH B . 
SA 5 HOH 181 881 375 HOH HOH B . 
SA 5 HOH 182 882 426 HOH HOH B . 
SA 5 HOH 183 883 436 HOH HOH B . 
SA 5 HOH 184 884 535 HOH HOH B . 
SA 5 HOH 185 885 479 HOH HOH B . 
SA 5 HOH 186 886 321 HOH HOH B . 
SA 5 HOH 187 887 557 HOH HOH B . 
TA 5 HOH 1   701 136 HOH HOH C . 
TA 5 HOH 2   702 250 HOH HOH C . 
TA 5 HOH 3   703 350 HOH HOH C . 
TA 5 HOH 4   704 448 HOH HOH C . 
TA 5 HOH 5   705 358 HOH HOH C . 
TA 5 HOH 6   706 506 HOH HOH C . 
TA 5 HOH 7   707 242 HOH HOH C . 
TA 5 HOH 8   708 98  HOH HOH C . 
TA 5 HOH 9   709 550 HOH HOH C . 
TA 5 HOH 10  710 440 HOH HOH C . 
TA 5 HOH 11  711 230 HOH HOH C . 
TA 5 HOH 12  712 75  HOH HOH C . 
TA 5 HOH 13  713 247 HOH HOH C . 
TA 5 HOH 14  714 547 HOH HOH C . 
TA 5 HOH 15  715 162 HOH HOH C . 
TA 5 HOH 16  716 172 HOH HOH C . 
TA 5 HOH 17  717 218 HOH HOH C . 
TA 5 HOH 18  718 556 HOH HOH C . 
TA 5 HOH 19  719 422 HOH HOH C . 
TA 5 HOH 20  720 104 HOH HOH C . 
TA 5 HOH 21  721 302 HOH HOH C . 
TA 5 HOH 22  722 433 HOH HOH C . 
TA 5 HOH 23  723 365 HOH HOH C . 
TA 5 HOH 24  724 28  HOH HOH C . 
TA 5 HOH 25  725 254 HOH HOH C . 
TA 5 HOH 26  726 453 HOH HOH C . 
TA 5 HOH 27  727 331 HOH HOH C . 
TA 5 HOH 28  728 312 HOH HOH C . 
TA 5 HOH 29  729 108 HOH HOH C . 
TA 5 HOH 30  730 95  HOH HOH C . 
TA 5 HOH 31  731 536 HOH HOH C . 
TA 5 HOH 32  732 217 HOH HOH C . 
TA 5 HOH 33  733 418 HOH HOH C . 
TA 5 HOH 34  734 233 HOH HOH C . 
TA 5 HOH 35  735 540 HOH HOH C . 
TA 5 HOH 36  736 551 HOH HOH C . 
TA 5 HOH 37  737 325 HOH HOH C . 
TA 5 HOH 38  738 213 HOH HOH C . 
TA 5 HOH 39  739 452 HOH HOH C . 
TA 5 HOH 40  740 552 HOH HOH C . 
UA 5 HOH 1   701 455 HOH HOH D . 
UA 5 HOH 2   702 168 HOH HOH D . 
UA 5 HOH 3   703 401 HOH HOH D . 
UA 5 HOH 4   704 432 HOH HOH D . 
UA 5 HOH 5   705 281 HOH HOH D . 
UA 5 HOH 6   706 356 HOH HOH D . 
UA 5 HOH 7   707 229 HOH HOH D . 
UA 5 HOH 8   708 264 HOH HOH D . 
UA 5 HOH 9   709 130 HOH HOH D . 
UA 5 HOH 10  710 532 HOH HOH D . 
UA 5 HOH 11  711 287 HOH HOH D . 
UA 5 HOH 12  712 127 HOH HOH D . 
UA 5 HOH 13  713 410 HOH HOH D . 
UA 5 HOH 14  714 282 HOH HOH D . 
UA 5 HOH 15  715 170 HOH HOH D . 
UA 5 HOH 16  716 158 HOH HOH D . 
UA 5 HOH 17  717 544 HOH HOH D . 
UA 5 HOH 18  718 91  HOH HOH D . 
UA 5 HOH 19  719 377 HOH HOH D . 
UA 5 HOH 20  720 161 HOH HOH D . 
UA 5 HOH 21  721 303 HOH HOH D . 
UA 5 HOH 22  722 539 HOH HOH D . 
UA 5 HOH 23  723 529 HOH HOH D . 
UA 5 HOH 24  724 225 HOH HOH D . 
UA 5 HOH 25  725 113 HOH HOH D . 
UA 5 HOH 26  726 157 HOH HOH D . 
UA 5 HOH 27  727 434 HOH HOH D . 
UA 5 HOH 28  728 397 HOH HOH D . 
UA 5 HOH 29  729 425 HOH HOH D . 
UA 5 HOH 30  730 561 HOH HOH D . 
UA 5 HOH 31  731 480 HOH HOH D . 
UA 5 HOH 32  732 222 HOH HOH D . 
UA 5 HOH 33  733 22  HOH HOH D . 
UA 5 HOH 34  734 564 HOH HOH D . 
UA 5 HOH 35  735 533 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 127 ? CG  ? A LYS 96  CG  
2   1 Y 1 A LYS 127 ? CD  ? A LYS 96  CD  
3   1 Y 1 A LYS 127 ? CE  ? A LYS 96  CE  
4   1 Y 1 A LYS 127 ? NZ  ? A LYS 96  NZ  
5   1 Y 1 A LYS 273 ? CG  ? A LYS 242 CG  
6   1 Y 1 A LYS 273 ? CD  ? A LYS 242 CD  
7   1 Y 1 A LYS 273 ? CE  ? A LYS 242 CE  
8   1 Y 1 A LYS 273 ? NZ  ? A LYS 242 NZ  
9   1 Y 1 A LYS 275 ? CG  ? A LYS 244 CG  
10  1 Y 1 A LYS 275 ? CD  ? A LYS 244 CD  
11  1 Y 1 A LYS 275 ? CE  ? A LYS 244 CE  
12  1 Y 1 A LYS 275 ? NZ  ? A LYS 244 NZ  
13  1 Y 1 A LYS 302 ? CG  ? A LYS 271 CG  
14  1 Y 1 A LYS 302 ? CD  ? A LYS 271 CD  
15  1 Y 1 A LYS 302 ? CE  ? A LYS 271 CE  
16  1 Y 1 A LYS 302 ? NZ  ? A LYS 271 NZ  
17  1 Y 1 A LYS 353 ? CG  ? A LYS 322 CG  
18  1 Y 1 A LYS 353 ? CD  ? A LYS 322 CD  
19  1 Y 1 A LYS 353 ? CE  ? A LYS 322 CE  
20  1 Y 1 A LYS 353 ? NZ  ? A LYS 322 NZ  
21  1 Y 1 A LYS 354 ? CG  ? A LYS 323 CG  
22  1 Y 1 A LYS 354 ? CD  ? A LYS 323 CD  
23  1 Y 1 A LYS 354 ? CE  ? A LYS 323 CE  
24  1 Y 1 A LYS 354 ? NZ  ? A LYS 323 NZ  
25  1 Y 1 A LYS 378 ? CG  ? A LYS 347 CG  
26  1 Y 1 A LYS 378 ? CD  ? A LYS 347 CD  
27  1 Y 1 A LYS 378 ? CE  ? A LYS 347 CE  
28  1 Y 1 A LYS 378 ? NZ  ? A LYS 347 NZ  
29  1 Y 1 A LYS 381 ? CG  ? A LYS 350 CG  
30  1 Y 1 A LYS 381 ? CD  ? A LYS 350 CD  
31  1 Y 1 A LYS 381 ? CE  ? A LYS 350 CE  
32  1 Y 1 A LYS 381 ? NZ  ? A LYS 350 NZ  
33  1 Y 1 A LYS 448 ? CG  ? A LYS 417 CG  
34  1 Y 1 A LYS 448 ? CD  ? A LYS 417 CD  
35  1 Y 1 A LYS 448 ? CE  ? A LYS 417 CE  
36  1 Y 1 A LYS 448 ? NZ  ? A LYS 417 NZ  
37  1 Y 1 A LYS 474 ? CG  ? A LYS 443 CG  
38  1 Y 1 A LYS 474 ? CD  ? A LYS 443 CD  
39  1 Y 1 A LYS 474 ? CE  ? A LYS 443 CE  
40  1 Y 1 A LYS 474 ? NZ  ? A LYS 443 NZ  
41  1 Y 1 A LYS 484 ? CG  ? A LYS 453 CG  
42  1 Y 1 A LYS 484 ? CD  ? A LYS 453 CD  
43  1 Y 1 A LYS 484 ? CE  ? A LYS 453 CE  
44  1 Y 1 A LYS 484 ? NZ  ? A LYS 453 NZ  
45  1 Y 1 B LYS 127 ? CG  ? B LYS 96  CG  
46  1 Y 1 B LYS 127 ? CD  ? B LYS 96  CD  
47  1 Y 1 B LYS 127 ? CE  ? B LYS 96  CE  
48  1 Y 1 B LYS 127 ? NZ  ? B LYS 96  NZ  
49  1 Y 1 B LYS 194 ? CG  ? B LYS 163 CG  
50  1 Y 1 B LYS 194 ? CD  ? B LYS 163 CD  
51  1 Y 1 B LYS 194 ? CE  ? B LYS 163 CE  
52  1 Y 1 B LYS 194 ? NZ  ? B LYS 163 NZ  
53  1 Y 1 B LYS 197 ? CG  ? B LYS 166 CG  
54  1 Y 1 B LYS 197 ? CD  ? B LYS 166 CD  
55  1 Y 1 B LYS 197 ? CE  ? B LYS 166 CE  
56  1 Y 1 B LYS 197 ? NZ  ? B LYS 166 NZ  
57  1 Y 1 B LYS 198 ? CG  ? B LYS 167 CG  
58  1 Y 1 B LYS 198 ? CD  ? B LYS 167 CD  
59  1 Y 1 B LYS 198 ? CE  ? B LYS 167 CE  
60  1 Y 1 B LYS 198 ? NZ  ? B LYS 167 NZ  
61  1 Y 1 B LYS 243 ? CG  ? B LYS 212 CG  
62  1 Y 1 B LYS 243 ? CD  ? B LYS 212 CD  
63  1 Y 1 B LYS 243 ? CE  ? B LYS 212 CE  
64  1 Y 1 B LYS 243 ? NZ  ? B LYS 212 NZ  
65  1 Y 1 B LYS 268 ? CG  ? B LYS 237 CG  
66  1 Y 1 B LYS 268 ? CD  ? B LYS 237 CD  
67  1 Y 1 B LYS 268 ? CE  ? B LYS 237 CE  
68  1 Y 1 B LYS 268 ? NZ  ? B LYS 237 NZ  
69  1 Y 1 B LYS 273 ? CG  ? B LYS 242 CG  
70  1 Y 1 B LYS 273 ? CD  ? B LYS 242 CD  
71  1 Y 1 B LYS 273 ? CE  ? B LYS 242 CE  
72  1 Y 1 B LYS 273 ? NZ  ? B LYS 242 NZ  
73  1 Y 1 B LYS 302 ? CG  ? B LYS 271 CG  
74  1 Y 1 B LYS 302 ? CD  ? B LYS 271 CD  
75  1 Y 1 B LYS 302 ? CE  ? B LYS 271 CE  
76  1 Y 1 B LYS 302 ? NZ  ? B LYS 271 NZ  
77  1 Y 1 B LYS 353 ? CG  ? B LYS 322 CG  
78  1 Y 1 B LYS 353 ? CD  ? B LYS 322 CD  
79  1 Y 1 B LYS 353 ? CE  ? B LYS 322 CE  
80  1 Y 1 B LYS 353 ? NZ  ? B LYS 322 NZ  
81  1 Y 1 B LYS 378 ? CG  ? B LYS 347 CG  
82  1 Y 1 B LYS 378 ? CD  ? B LYS 347 CD  
83  1 Y 1 B LYS 378 ? CE  ? B LYS 347 CE  
84  1 Y 1 B LYS 378 ? NZ  ? B LYS 347 NZ  
85  1 Y 1 B LYS 381 ? CG  ? B LYS 350 CG  
86  1 Y 1 B LYS 381 ? CD  ? B LYS 350 CD  
87  1 Y 1 B LYS 381 ? CE  ? B LYS 350 CE  
88  1 Y 1 B LYS 381 ? NZ  ? B LYS 350 NZ  
89  1 Y 1 B LYS 448 ? CG  ? B LYS 417 CG  
90  1 Y 1 B LYS 448 ? CD  ? B LYS 417 CD  
91  1 Y 1 B LYS 448 ? CE  ? B LYS 417 CE  
92  1 Y 1 B LYS 448 ? NZ  ? B LYS 417 NZ  
93  1 Y 1 B GLU 460 ? CG  ? B GLU 429 CG  
94  1 Y 1 B GLU 460 ? CD  ? B GLU 429 CD  
95  1 Y 1 B GLU 460 ? OE1 ? B GLU 429 OE1 
96  1 Y 1 B GLU 460 ? OE2 ? B GLU 429 OE2 
97  1 Y 1 B LYS 474 ? CG  ? B LYS 443 CG  
98  1 Y 1 B LYS 474 ? CD  ? B LYS 443 CD  
99  1 Y 1 B LYS 474 ? CE  ? B LYS 443 CE  
100 1 Y 1 B LYS 474 ? NZ  ? B LYS 443 NZ  
101 1 Y 1 B LYS 484 ? CG  ? B LYS 453 CG  
102 1 Y 1 B LYS 484 ? CD  ? B LYS 453 CD  
103 1 Y 1 B LYS 484 ? CE  ? B LYS 453 CE  
104 1 Y 1 B LYS 484 ? NZ  ? B LYS 453 NZ  
105 1 Y 1 C ASP 125 ? CG  ? C ASP 94  CG  
106 1 Y 1 C ASP 125 ? OD1 ? C ASP 94  OD1 
107 1 Y 1 C ASP 125 ? OD2 ? C ASP 94  OD2 
108 1 Y 1 C LYS 127 ? CG  ? C LYS 96  CG  
109 1 Y 1 C LYS 127 ? CD  ? C LYS 96  CD  
110 1 Y 1 C LYS 127 ? CE  ? C LYS 96  CE  
111 1 Y 1 C LYS 127 ? NZ  ? C LYS 96  NZ  
112 1 Y 1 C ASN 129 ? CG  ? C ASN 98  CG  
113 1 Y 1 C ASN 129 ? OD1 ? C ASN 98  OD1 
114 1 Y 1 C ASN 129 ? ND2 ? C ASN 98  ND2 
115 1 Y 1 C GLU 135 ? CG  ? C GLU 104 CG  
116 1 Y 1 C GLU 135 ? CD  ? C GLU 104 CD  
117 1 Y 1 C GLU 135 ? OE1 ? C GLU 104 OE1 
118 1 Y 1 C GLU 135 ? OE2 ? C GLU 104 OE2 
119 1 Y 1 C LYS 141 ? CG  ? C LYS 110 CG  
120 1 Y 1 C LYS 141 ? CD  ? C LYS 110 CD  
121 1 Y 1 C LYS 141 ? CE  ? C LYS 110 CE  
122 1 Y 1 C LYS 141 ? NZ  ? C LYS 110 NZ  
123 1 Y 1 C LYS 168 ? CG  ? C LYS 137 CG  
124 1 Y 1 C LYS 168 ? CD  ? C LYS 137 CD  
125 1 Y 1 C LYS 168 ? CE  ? C LYS 137 CE  
126 1 Y 1 C LYS 168 ? NZ  ? C LYS 137 NZ  
127 1 Y 1 C LYS 194 ? CG  ? C LYS 163 CG  
128 1 Y 1 C LYS 194 ? CD  ? C LYS 163 CD  
129 1 Y 1 C LYS 194 ? CE  ? C LYS 163 CE  
130 1 Y 1 C LYS 194 ? NZ  ? C LYS 163 NZ  
131 1 Y 1 C GLN 196 ? CG  ? C GLN 165 CG  
132 1 Y 1 C GLN 196 ? CD  ? C GLN 165 CD  
133 1 Y 1 C GLN 196 ? OE1 ? C GLN 165 OE1 
134 1 Y 1 C GLN 196 ? NE2 ? C GLN 165 NE2 
135 1 Y 1 C LYS 197 ? CG  ? C LYS 166 CG  
136 1 Y 1 C LYS 197 ? CD  ? C LYS 166 CD  
137 1 Y 1 C LYS 197 ? CE  ? C LYS 166 CE  
138 1 Y 1 C LYS 197 ? NZ  ? C LYS 166 NZ  
139 1 Y 1 C LYS 198 ? CG  ? C LYS 167 CG  
140 1 Y 1 C LYS 198 ? CD  ? C LYS 167 CD  
141 1 Y 1 C LYS 198 ? CE  ? C LYS 167 CE  
142 1 Y 1 C LYS 198 ? NZ  ? C LYS 167 NZ  
143 1 Y 1 C ILE 204 ? CG1 ? C ILE 173 CG1 
144 1 Y 1 C ILE 204 ? CG2 ? C ILE 173 CG2 
145 1 Y 1 C ILE 204 ? CD1 ? C ILE 173 CD1 
146 1 Y 1 C ARG 205 ? CG  ? C ARG 174 CG  
147 1 Y 1 C ARG 205 ? CD  ? C ARG 174 CD  
148 1 Y 1 C ARG 205 ? NE  ? C ARG 174 NE  
149 1 Y 1 C ARG 205 ? CZ  ? C ARG 174 CZ  
150 1 Y 1 C ARG 205 ? NH1 ? C ARG 174 NH1 
151 1 Y 1 C ARG 205 ? NH2 ? C ARG 174 NH2 
152 1 Y 1 C LYS 216 ? CG  ? C LYS 185 CG  
153 1 Y 1 C LYS 216 ? CD  ? C LYS 185 CD  
154 1 Y 1 C LYS 216 ? CE  ? C LYS 185 CE  
155 1 Y 1 C LYS 216 ? NZ  ? C LYS 185 NZ  
156 1 Y 1 C LYS 262 ? CG  ? C LYS 231 CG  
157 1 Y 1 C LYS 262 ? CD  ? C LYS 231 CD  
158 1 Y 1 C LYS 262 ? CE  ? C LYS 231 CE  
159 1 Y 1 C LYS 262 ? NZ  ? C LYS 231 NZ  
160 1 Y 1 C LYS 268 ? CG  ? C LYS 237 CG  
161 1 Y 1 C LYS 268 ? CD  ? C LYS 237 CD  
162 1 Y 1 C LYS 268 ? CE  ? C LYS 237 CE  
163 1 Y 1 C LYS 268 ? NZ  ? C LYS 237 NZ  
164 1 Y 1 C HIS 271 ? CG  ? C HIS 240 CG  
165 1 Y 1 C HIS 271 ? ND1 ? C HIS 240 ND1 
166 1 Y 1 C HIS 271 ? CD2 ? C HIS 240 CD2 
167 1 Y 1 C HIS 271 ? CE1 ? C HIS 240 CE1 
168 1 Y 1 C HIS 271 ? NE2 ? C HIS 240 NE2 
169 1 Y 1 C LYS 273 ? CG  ? C LYS 242 CG  
170 1 Y 1 C LYS 273 ? CD  ? C LYS 242 CD  
171 1 Y 1 C LYS 273 ? CE  ? C LYS 242 CE  
172 1 Y 1 C LYS 273 ? NZ  ? C LYS 242 NZ  
173 1 Y 1 C LYS 302 ? CG  ? C LYS 271 CG  
174 1 Y 1 C LYS 302 ? CD  ? C LYS 271 CD  
175 1 Y 1 C LYS 302 ? CE  ? C LYS 271 CE  
176 1 Y 1 C LYS 302 ? NZ  ? C LYS 271 NZ  
177 1 Y 1 C LYS 378 ? CG  ? C LYS 347 CG  
178 1 Y 1 C LYS 378 ? CD  ? C LYS 347 CD  
179 1 Y 1 C LYS 378 ? CE  ? C LYS 347 CE  
180 1 Y 1 C LYS 378 ? NZ  ? C LYS 347 NZ  
181 1 Y 1 C LYS 381 ? CG  ? C LYS 350 CG  
182 1 Y 1 C LYS 381 ? CD  ? C LYS 350 CD  
183 1 Y 1 C LYS 381 ? CE  ? C LYS 350 CE  
184 1 Y 1 C LYS 381 ? NZ  ? C LYS 350 NZ  
185 1 Y 1 C LYS 388 ? CG  ? C LYS 357 CG  
186 1 Y 1 C LYS 388 ? CD  ? C LYS 357 CD  
187 1 Y 1 C LYS 388 ? CE  ? C LYS 357 CE  
188 1 Y 1 C LYS 388 ? NZ  ? C LYS 357 NZ  
189 1 Y 1 C LYS 396 ? CG  ? C LYS 365 CG  
190 1 Y 1 C LYS 396 ? CD  ? C LYS 365 CD  
191 1 Y 1 C LYS 396 ? CE  ? C LYS 365 CE  
192 1 Y 1 C LYS 396 ? NZ  ? C LYS 365 NZ  
193 1 Y 1 C LYS 402 ? CG  ? C LYS 371 CG  
194 1 Y 1 C LYS 402 ? CD  ? C LYS 371 CD  
195 1 Y 1 C LYS 402 ? CE  ? C LYS 371 CE  
196 1 Y 1 C LYS 402 ? NZ  ? C LYS 371 NZ  
197 1 Y 1 C ASP 403 ? CG  ? C ASP 372 CG  
198 1 Y 1 C ASP 403 ? OD1 ? C ASP 372 OD1 
199 1 Y 1 C ASP 403 ? OD2 ? C ASP 372 OD2 
200 1 Y 1 C GLU 404 ? CG  ? C GLU 373 CG  
201 1 Y 1 C GLU 404 ? CD  ? C GLU 373 CD  
202 1 Y 1 C GLU 404 ? OE1 ? C GLU 373 OE1 
203 1 Y 1 C GLU 404 ? OE2 ? C GLU 373 OE2 
204 1 Y 1 C GLU 460 ? CG  ? C GLU 429 CG  
205 1 Y 1 C GLU 460 ? CD  ? C GLU 429 CD  
206 1 Y 1 C GLU 460 ? OE1 ? C GLU 429 OE1 
207 1 Y 1 C GLU 460 ? OE2 ? C GLU 429 OE2 
208 1 Y 1 C LYS 470 ? CG  ? C LYS 439 CG  
209 1 Y 1 C LYS 470 ? CD  ? C LYS 439 CD  
210 1 Y 1 C LYS 470 ? CE  ? C LYS 439 CE  
211 1 Y 1 C LYS 470 ? NZ  ? C LYS 439 NZ  
212 1 Y 1 C LYS 474 ? CG  ? C LYS 443 CG  
213 1 Y 1 C LYS 474 ? CD  ? C LYS 443 CD  
214 1 Y 1 C LYS 474 ? CE  ? C LYS 443 CE  
215 1 Y 1 C LYS 474 ? NZ  ? C LYS 443 NZ  
216 1 Y 1 C LYS 484 ? CG  ? C LYS 453 CG  
217 1 Y 1 C LYS 484 ? CD  ? C LYS 453 CD  
218 1 Y 1 C LYS 484 ? CE  ? C LYS 453 CE  
219 1 Y 1 C LYS 484 ? NZ  ? C LYS 453 NZ  
220 1 Y 1 C LYS 503 ? CG  ? C LYS 472 CG  
221 1 Y 1 C LYS 503 ? CD  ? C LYS 472 CD  
222 1 Y 1 C LYS 503 ? CE  ? C LYS 472 CE  
223 1 Y 1 C LYS 503 ? NZ  ? C LYS 472 NZ  
224 1 Y 1 D LYS 127 ? CG  ? D LYS 96  CG  
225 1 Y 1 D LYS 127 ? CD  ? D LYS 96  CD  
226 1 Y 1 D LYS 127 ? CE  ? D LYS 96  CE  
227 1 Y 1 D LYS 127 ? NZ  ? D LYS 96  NZ  
228 1 Y 1 D GLU 135 ? CG  ? D GLU 104 CG  
229 1 Y 1 D GLU 135 ? CD  ? D GLU 104 CD  
230 1 Y 1 D GLU 135 ? OE1 ? D GLU 104 OE1 
231 1 Y 1 D GLU 135 ? OE2 ? D GLU 104 OE2 
232 1 Y 1 D LYS 141 ? CG  ? D LYS 110 CG  
233 1 Y 1 D LYS 141 ? CD  ? D LYS 110 CD  
234 1 Y 1 D LYS 141 ? CE  ? D LYS 110 CE  
235 1 Y 1 D LYS 141 ? NZ  ? D LYS 110 NZ  
236 1 Y 1 D LYS 194 ? CG  ? D LYS 163 CG  
237 1 Y 1 D LYS 194 ? CD  ? D LYS 163 CD  
238 1 Y 1 D LYS 194 ? CE  ? D LYS 163 CE  
239 1 Y 1 D LYS 194 ? NZ  ? D LYS 163 NZ  
240 1 Y 1 D LYS 197 ? CG  ? D LYS 166 CG  
241 1 Y 1 D LYS 197 ? CD  ? D LYS 166 CD  
242 1 Y 1 D LYS 197 ? CE  ? D LYS 166 CE  
243 1 Y 1 D LYS 197 ? NZ  ? D LYS 166 NZ  
244 1 Y 1 D GLU 264 ? CG  ? D GLU 233 CG  
245 1 Y 1 D GLU 264 ? CD  ? D GLU 233 CD  
246 1 Y 1 D GLU 264 ? OE1 ? D GLU 233 OE1 
247 1 Y 1 D GLU 264 ? OE2 ? D GLU 233 OE2 
248 1 Y 1 D LYS 268 ? CG  ? D LYS 237 CG  
249 1 Y 1 D LYS 268 ? CD  ? D LYS 237 CD  
250 1 Y 1 D LYS 268 ? CE  ? D LYS 237 CE  
251 1 Y 1 D LYS 268 ? NZ  ? D LYS 237 NZ  
252 1 Y 1 D HIS 271 ? CG  ? D HIS 240 CG  
253 1 Y 1 D HIS 271 ? ND1 ? D HIS 240 ND1 
254 1 Y 1 D HIS 271 ? CD2 ? D HIS 240 CD2 
255 1 Y 1 D HIS 271 ? CE1 ? D HIS 240 CE1 
256 1 Y 1 D HIS 271 ? NE2 ? D HIS 240 NE2 
257 1 Y 1 D LYS 273 ? CG  ? D LYS 242 CG  
258 1 Y 1 D LYS 273 ? CD  ? D LYS 242 CD  
259 1 Y 1 D LYS 273 ? CE  ? D LYS 242 CE  
260 1 Y 1 D LYS 273 ? NZ  ? D LYS 242 NZ  
261 1 Y 1 D LYS 299 ? CG  ? D LYS 268 CG  
262 1 Y 1 D LYS 299 ? CD  ? D LYS 268 CD  
263 1 Y 1 D LYS 299 ? CE  ? D LYS 268 CE  
264 1 Y 1 D LYS 299 ? NZ  ? D LYS 268 NZ  
265 1 Y 1 D GLU 300 ? CG  ? D GLU 269 CG  
266 1 Y 1 D GLU 300 ? CD  ? D GLU 269 CD  
267 1 Y 1 D GLU 300 ? OE1 ? D GLU 269 OE1 
268 1 Y 1 D GLU 300 ? OE2 ? D GLU 269 OE2 
269 1 Y 1 D LYS 302 ? CG  ? D LYS 271 CG  
270 1 Y 1 D LYS 302 ? CD  ? D LYS 271 CD  
271 1 Y 1 D LYS 302 ? CE  ? D LYS 271 CE  
272 1 Y 1 D LYS 302 ? NZ  ? D LYS 271 NZ  
273 1 Y 1 D LYS 350 ? CG  ? D LYS 319 CG  
274 1 Y 1 D LYS 350 ? CD  ? D LYS 319 CD  
275 1 Y 1 D LYS 350 ? CE  ? D LYS 319 CE  
276 1 Y 1 D LYS 350 ? NZ  ? D LYS 319 NZ  
277 1 Y 1 D LYS 351 ? CG  ? D LYS 320 CG  
278 1 Y 1 D LYS 351 ? CD  ? D LYS 320 CD  
279 1 Y 1 D LYS 351 ? CE  ? D LYS 320 CE  
280 1 Y 1 D LYS 351 ? NZ  ? D LYS 320 NZ  
281 1 Y 1 D ILE 352 ? CG1 ? D ILE 321 CG1 
282 1 Y 1 D ILE 352 ? CG2 ? D ILE 321 CG2 
283 1 Y 1 D ILE 352 ? CD1 ? D ILE 321 CD1 
284 1 Y 1 D LYS 353 ? CG  ? D LYS 322 CG  
285 1 Y 1 D LYS 353 ? CD  ? D LYS 322 CD  
286 1 Y 1 D LYS 353 ? CE  ? D LYS 322 CE  
287 1 Y 1 D LYS 353 ? NZ  ? D LYS 322 NZ  
288 1 Y 1 D GLN 356 ? CG  ? D GLN 325 CG  
289 1 Y 1 D GLN 356 ? CD  ? D GLN 325 CD  
290 1 Y 1 D GLN 356 ? OE1 ? D GLN 325 OE1 
291 1 Y 1 D GLN 356 ? NE2 ? D GLN 325 NE2 
292 1 Y 1 D LYS 378 ? CG  ? D LYS 347 CG  
293 1 Y 1 D LYS 378 ? CD  ? D LYS 347 CD  
294 1 Y 1 D LYS 378 ? CE  ? D LYS 347 CE  
295 1 Y 1 D LYS 378 ? NZ  ? D LYS 347 NZ  
296 1 Y 1 D LYS 381 ? CG  ? D LYS 350 CG  
297 1 Y 1 D LYS 381 ? CD  ? D LYS 350 CD  
298 1 Y 1 D LYS 381 ? CE  ? D LYS 350 CE  
299 1 Y 1 D LYS 381 ? NZ  ? D LYS 350 NZ  
300 1 Y 1 D LYS 383 ? CG  ? D LYS 352 CG  
301 1 Y 1 D LYS 383 ? CD  ? D LYS 352 CD  
302 1 Y 1 D LYS 383 ? CE  ? D LYS 352 CE  
303 1 Y 1 D LYS 383 ? NZ  ? D LYS 352 NZ  
304 1 Y 1 D GLN 384 ? CG  ? D GLN 353 CG  
305 1 Y 1 D GLN 384 ? CD  ? D GLN 353 CD  
306 1 Y 1 D GLN 384 ? OE1 ? D GLN 353 OE1 
307 1 Y 1 D GLN 384 ? NE2 ? D GLN 353 NE2 
308 1 Y 1 D LYS 402 ? CG  ? D LYS 371 CG  
309 1 Y 1 D LYS 402 ? CD  ? D LYS 371 CD  
310 1 Y 1 D LYS 402 ? CE  ? D LYS 371 CE  
311 1 Y 1 D LYS 402 ? NZ  ? D LYS 371 NZ  
312 1 Y 1 D GLU 460 ? CG  ? D GLU 429 CG  
313 1 Y 1 D GLU 460 ? CD  ? D GLU 429 CD  
314 1 Y 1 D GLU 460 ? OE1 ? D GLU 429 OE1 
315 1 Y 1 D GLU 460 ? OE2 ? D GLU 429 OE2 
316 1 Y 1 D LYS 470 ? CG  ? D LYS 439 CG  
317 1 Y 1 D LYS 470 ? CD  ? D LYS 439 CD  
318 1 Y 1 D LYS 470 ? CE  ? D LYS 439 CE  
319 1 Y 1 D LYS 470 ? NZ  ? D LYS 439 NZ  
320 1 Y 1 D LYS 482 ? CG  ? D LYS 451 CG  
321 1 Y 1 D LYS 482 ? CD  ? D LYS 451 CD  
322 1 Y 1 D LYS 482 ? CE  ? D LYS 451 CE  
323 1 Y 1 D LYS 482 ? NZ  ? D LYS 451 NZ  
324 1 Y 1 D LYS 484 ? CG  ? D LYS 453 CG  
325 1 Y 1 D LYS 484 ? CD  ? D LYS 453 CD  
326 1 Y 1 D LYS 484 ? CE  ? D LYS 453 CE  
327 1 Y 1 D LYS 484 ? NZ  ? D LYS 453 NZ  
328 1 Y 1 D GLU 488 ? CG  ? D GLU 457 CG  
329 1 Y 1 D GLU 488 ? CD  ? D GLU 457 CD  
330 1 Y 1 D GLU 488 ? OE1 ? D GLU 457 OE1 
331 1 Y 1 D GLU 488 ? OE2 ? D GLU 457 OE2 
332 1 Y 1 D GLN 491 ? CG  ? D GLN 460 CG  
333 1 Y 1 D GLN 491 ? CD  ? D GLN 460 CD  
334 1 Y 1 D GLN 491 ? OE1 ? D GLN 460 OE1 
335 1 Y 1 D GLN 491 ? NE2 ? D GLN 460 NE2 
336 1 Y 1 D GLU 496 ? CG  ? D GLU 465 CG  
337 1 Y 1 D GLU 496 ? CD  ? D GLU 465 CD  
338 1 Y 1 D GLU 496 ? OE1 ? D GLU 465 OE1 
339 1 Y 1 D GLU 496 ? OE2 ? D GLU 465 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   99.330 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HH3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     73.800 
_cell.length_a_esd                 ? 
_cell.length_b                     199.150 
_cell.length_b_esd                 ? 
_cell.length_c                     75.350 
_cell.length_c_esd                 ? 
_cell.volume                       1092788.942 
_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                         9HH3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9HH3 
_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             2.56 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.4 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Bis-Tris Propane pH 7.5, 0.2 M NaBr, 10 % PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     80 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-15 
_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   0.978565 
_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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978565 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          48.63 
_reflns.entry_id                                       9HH3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.26 
_reflns.d_resolution_low                               49.36 
_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                                     99086 
_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                           99.62 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.37 
_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                                0.1159 
_reflns.pdbx_Rpim_I_all                                0.0417 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1079 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.264 
_reflns_shell.d_res_low                                     2.345 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             9564 
_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                               7.4 
_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                               0.518 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.564 
_reflns_shell.pdbx_CC_star                                  0.849 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.66 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.321 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               56.55 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 9HH3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.26 
_refine.ls_d_res_low                             49.36 
_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                     99063 
_refine.ls_number_reflns_R_free                  4954 
_refine.ls_number_reflns_R_work                  94109 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.63 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1975 
_refine.ls_R_factor_R_free                       0.2459 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1950 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.35 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 26.3706 
_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                             ? 
_refine.overall_SU_ML                            0.3278 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.26 
_refine_hist.d_res_low                        49.36 
_refine_hist.number_atoms_solvent             456 
_refine_hist.number_atoms_total               15112 
_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        14617 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_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' ? 0.0077  ? 15043 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9474  ? 20467 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0582  ? 2118  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0090  ? 2704  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.2179 ? 5387  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_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 
_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 
'X-RAY DIFFRACTION' 2.26 2.29  . . 151 2851 90.20  . . . . 0.3241 . . . . . . . . . . . 0.3711 
'X-RAY DIFFRACTION' 2.29 2.32  . . 165 3133 99.94  . . . . 0.2991 . . . . . . . . . . . 0.3142 
'X-RAY DIFFRACTION' 2.32 2.35  . . 163 3101 99.97  . . . . 0.2821 . . . . . . . . . . . 0.3173 
'X-RAY DIFFRACTION' 2.35 2.37  . . 167 3182 99.94  . . . . 0.2759 . . . . . . . . . . . 0.3044 
'X-RAY DIFFRACTION' 2.37 2.41  . . 164 3111 99.91  . . . . 0.2709 . . . . . . . . . . . 0.3405 
'X-RAY DIFFRACTION' 2.41 2.44  . . 167 3166 100.00 . . . . 0.2727 . . . . . . . . . . . 0.2947 
'X-RAY DIFFRACTION' 2.44 2.47  . . 166 3149 100.00 . . . . 0.2713 . . . . . . . . . . . 0.3471 
'X-RAY DIFFRACTION' 2.47 2.51  . . 164 3124 100.00 . . . . 0.2646 . . . . . . . . . . . 0.3136 
'X-RAY DIFFRACTION' 2.51 2.55  . . 166 3146 100.00 . . . . 0.2479 . . . . . . . . . . . 0.2921 
'X-RAY DIFFRACTION' 2.55 2.59  . . 164 3121 100.00 . . . . 0.2380 . . . . . . . . . . . 0.2936 
'X-RAY DIFFRACTION' 2.59 2.64  . . 166 3157 100.00 . . . . 0.2186 . . . . . . . . . . . 0.3054 
'X-RAY DIFFRACTION' 2.64 2.68  . . 165 3140 99.97  . . . . 0.2136 . . . . . . . . . . . 0.2657 
'X-RAY DIFFRACTION' 2.68 2.74  . . 165 3129 100.00 . . . . 0.2112 . . . . . . . . . . . 0.2891 
'X-RAY DIFFRACTION' 2.74 2.79  . . 166 3150 99.97  . . . . 0.2203 . . . . . . . . . . . 0.2611 
'X-RAY DIFFRACTION' 2.79 2.85  . . 165 3147 100.00 . . . . 0.2148 . . . . . . . . . . . 0.2657 
'X-RAY DIFFRACTION' 2.85 2.92  . . 167 3158 100.00 . . . . 0.2227 . . . . . . . . . . . 0.2875 
'X-RAY DIFFRACTION' 2.92 2.99  . . 165 3138 100.00 . . . . 0.2296 . . . . . . . . . . . 0.2818 
'X-RAY DIFFRACTION' 2.99 3.07  . . 166 3161 100.00 . . . . 0.2334 . . . . . . . . . . . 0.2847 
'X-RAY DIFFRACTION' 3.07 3.16  . . 164 3113 99.97  . . . . 0.2269 . . . . . . . . . . . 0.2839 
'X-RAY DIFFRACTION' 3.16 3.27  . . 166 3160 99.97  . . . . 0.2146 . . . . . . . . . . . 0.2645 
'X-RAY DIFFRACTION' 3.27 3.38  . . 166 3142 99.97  . . . . 0.2155 . . . . . . . . . . . 0.2798 
'X-RAY DIFFRACTION' 3.38 3.52  . . 165 3145 99.97  . . . . 0.2031 . . . . . . . . . . . 0.2541 
'X-RAY DIFFRACTION' 3.52 3.68  . . 167 3165 99.94  . . . . 0.1901 . . . . . . . . . . . 0.2360 
'X-RAY DIFFRACTION' 3.68 3.87  . . 165 3145 99.94  . . . . 0.1816 . . . . . . . . . . . 0.2209 
'X-RAY DIFFRACTION' 3.87 4.11  . . 166 3140 100.00 . . . . 0.1600 . . . . . . . . . . . 0.2127 
'X-RAY DIFFRACTION' 4.11 4.43  . . 167 3170 100.00 . . . . 0.1483 . . . . . . . . . . . 0.2085 
'X-RAY DIFFRACTION' 4.43 4.88  . . 165 3141 99.88  . . . . 0.1444 . . . . . . . . . . . 0.1726 
'X-RAY DIFFRACTION' 4.88 5.58  . . 166 3157 99.97  . . . . 0.1653 . . . . . . . . . . . 0.2090 
'X-RAY DIFFRACTION' 5.58 7.03  . . 167 3173 100.00 . . . . 0.1827 . . . . . . . . . . . 0.2378 
'X-RAY DIFFRACTION' 7.03 49.36 . . 168 3194 99.61  . . . . 0.1700 . . . . . . . . . . . 0.2216 
# 
_struct.entry_id                     9HH3 
_struct.title                        
'Structure of the apo ZgCgsA carrageenan-sulfatase (S1_19) from the marine bacterium Zobellia galactanivorans' 
_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        9HH3 
_struct_keywords.text            'Bacterial metabolism, carrageenan, sulfatases, formylglycine, S1_19, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 2 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 3 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 4 ? 
Q  N N 2 ? 
R  N N 2 ? 
S  N N 2 ? 
T  N N 2 ? 
U  N N 3 ? 
V  N N 3 ? 
W  N N 3 ? 
X  N N 3 ? 
Y  N N 3 ? 
Z  N N 4 ? 
AA N N 2 ? 
BA N N 2 ? 
CA N N 3 ? 
DA N N 3 ? 
EA N N 3 ? 
FA N N 3 ? 
GA N N 3 ? 
HA N N 4 ? 
IA N N 2 ? 
JA N N 2 ? 
KA N N 3 ? 
LA N N 3 ? 
MA N N 3 ? 
NA N N 3 ? 
OA N N 3 ? 
PA N N 3 ? 
QA N N 4 ? 
RA N N 5 ? 
SA N N 5 ? 
TA N N 5 ? 
UA N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    G0L000_ZOBGA 
_struct_ref.pdbx_db_accession          G0L000 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QETRPNILVVLCDDLGYADVGFNGSTDILTPELDNLAQNGSIFTSAYVAHPFCGPSRSAILTGRYPHLTGTAYNLFHNSS
EDDKDNMGVPVEETYMSKVLQNAGYYTSAIGKWHLGAAPKFHPNKRGFDDFYGFLGGGHDYFPSEYQKTYKAQKKAGNPN
IRDYVFPMEHNGKPANETEYITDGFSREAIKNIKIAAAKKQPFFIYLAYNAPHVPLQAKAEDVAKFAHIKDKDRRTYAAM
VYAVDRGVGKIVQTLKETKQFDNTLIVFLSDNGGNFNHGANNYPLKGTKGDTWEGGYRVPMFFHWPKKIKKDQRFDFPVS
SLDLYPTFTGLAEAKLPKGKQLDGKNIMDDVLKNTEPYKDEMIYSLRYREGYNDVGARMGDWKITRMGNEPWRLHNITQD
IGEKKNLAGRYPDRLKEMIAKTQEWTKSFVKPLWVYSVKDKELWESGQMPNYEATFEVDKLVDSPYHK
;
_struct_ref.pdbx_align_begin           44 
# 
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 9HH3 A 13 ? 480 ? G0L000 44 ? 511 ? 44 511 
2 1 9HH3 B 13 ? 480 ? G0L000 44 ? 511 ? 44 511 
3 1 9HH3 C 13 ? 480 ? G0L000 44 ? 511 ? 44 511 
4 1 9HH3 D 13 ? 480 ? G0L000 44 ? 511 ? 44 511 
# 
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 9HH3 MET A 1  ? UNP G0L000 ? ? 'initiating methionine' 32 1  
1 9HH3 GLY A 2  ? UNP G0L000 ? ? 'expression tag'        33 2  
1 9HH3 SER A 3  ? UNP G0L000 ? ? 'expression tag'        34 3  
1 9HH3 SER A 4  ? UNP G0L000 ? ? 'expression tag'        35 4  
1 9HH3 HIS A 5  ? UNP G0L000 ? ? 'expression tag'        36 5  
1 9HH3 HIS A 6  ? UNP G0L000 ? ? 'expression tag'        37 6  
1 9HH3 HIS A 7  ? UNP G0L000 ? ? 'expression tag'        38 7  
1 9HH3 HIS A 8  ? UNP G0L000 ? ? 'expression tag'        39 8  
1 9HH3 HIS A 9  ? UNP G0L000 ? ? 'expression tag'        40 9  
1 9HH3 HIS A 10 ? UNP G0L000 ? ? 'expression tag'        41 10 
1 9HH3 GLY A 11 ? UNP G0L000 ? ? 'expression tag'        42 11 
1 9HH3 SER A 12 ? UNP G0L000 ? ? 'expression tag'        43 12 
2 9HH3 MET B 1  ? UNP G0L000 ? ? 'initiating methionine' 32 13 
2 9HH3 GLY B 2  ? UNP G0L000 ? ? 'expression tag'        33 14 
2 9HH3 SER B 3  ? UNP G0L000 ? ? 'expression tag'        34 15 
2 9HH3 SER B 4  ? UNP G0L000 ? ? 'expression tag'        35 16 
2 9HH3 HIS B 5  ? UNP G0L000 ? ? 'expression tag'        36 17 
2 9HH3 HIS B 6  ? UNP G0L000 ? ? 'expression tag'        37 18 
2 9HH3 HIS B 7  ? UNP G0L000 ? ? 'expression tag'        38 19 
2 9HH3 HIS B 8  ? UNP G0L000 ? ? 'expression tag'        39 20 
2 9HH3 HIS B 9  ? UNP G0L000 ? ? 'expression tag'        40 21 
2 9HH3 HIS B 10 ? UNP G0L000 ? ? 'expression tag'        41 22 
2 9HH3 GLY B 11 ? UNP G0L000 ? ? 'expression tag'        42 23 
2 9HH3 SER B 12 ? UNP G0L000 ? ? 'expression tag'        43 24 
3 9HH3 MET C 1  ? UNP G0L000 ? ? 'initiating methionine' 32 25 
3 9HH3 GLY C 2  ? UNP G0L000 ? ? 'expression tag'        33 26 
3 9HH3 SER C 3  ? UNP G0L000 ? ? 'expression tag'        34 27 
3 9HH3 SER C 4  ? UNP G0L000 ? ? 'expression tag'        35 28 
3 9HH3 HIS C 5  ? UNP G0L000 ? ? 'expression tag'        36 29 
3 9HH3 HIS C 6  ? UNP G0L000 ? ? 'expression tag'        37 30 
3 9HH3 HIS C 7  ? UNP G0L000 ? ? 'expression tag'        38 31 
3 9HH3 HIS C 8  ? UNP G0L000 ? ? 'expression tag'        39 32 
3 9HH3 HIS C 9  ? UNP G0L000 ? ? 'expression tag'        40 33 
3 9HH3 HIS C 10 ? UNP G0L000 ? ? 'expression tag'        41 34 
3 9HH3 GLY C 11 ? UNP G0L000 ? ? 'expression tag'        42 35 
3 9HH3 SER C 12 ? UNP G0L000 ? ? 'expression tag'        43 36 
4 9HH3 MET D 1  ? UNP G0L000 ? ? 'initiating methionine' 32 37 
4 9HH3 GLY D 2  ? UNP G0L000 ? ? 'expression tag'        33 38 
4 9HH3 SER D 3  ? UNP G0L000 ? ? 'expression tag'        34 39 
4 9HH3 SER D 4  ? UNP G0L000 ? ? 'expression tag'        35 40 
4 9HH3 HIS D 5  ? UNP G0L000 ? ? 'expression tag'        36 41 
4 9HH3 HIS D 6  ? UNP G0L000 ? ? 'expression tag'        37 42 
4 9HH3 HIS D 7  ? UNP G0L000 ? ? 'expression tag'        38 43 
4 9HH3 HIS D 8  ? UNP G0L000 ? ? 'expression tag'        39 44 
4 9HH3 HIS D 9  ? UNP G0L000 ? ? 'expression tag'        40 45 
4 9HH3 HIS D 10 ? UNP G0L000 ? ? 'expression tag'        41 46 
4 9HH3 GLY D 11 ? UNP G0L000 ? ? 'expression tag'        42 47 
4 9HH3 SER D 12 ? UNP G0L000 ? ? 'expression tag'        43 48 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 software_defined_assembly PISA dimeric 2 
2 software_defined_assembly PISA dimeric 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)' 5600  ? 
1 MORE         -143  ? 
1 'SSA (A^2)'  33520 ? 
2 'ABSA (A^2)' 4800  ? 
2 MORE         -112  ? 
2 'SSA (A^2)'  33060 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,RA,SA 
2 1 D,IA,JA,KA,LA,MA,NA,OA,PA,QA,UA                       
2 2 C,AA,BA,CA,DA,EA,FA,GA,HA,TA                          
# 
_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                'single peak at the size of a monomer.' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000 0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000  
2 'crystal symmetry operation' 1_556 x,y,z+1 1.0000000000 0.0000000000 0.0000000000 -12.2157808333 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 74.3531922558 
# 
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 VAL A 32  ? GLY A 36  ? VAL A 63  GLY A 67  5 ? 5  
HELX_P HELX_P2  AA2 THR A 42  ? ASN A 51  ? THR A 73  ASN A 82  1 ? 10 
HELX_P HELX_P3  AA3 PHE A 64  ? GLY A 75  ? PHE A 95  GLY A 106 1 ? 12 
HELX_P HELX_P4  AA4 TYR A 77  ? GLY A 82  ? TYR A 108 GLY A 113 1 ? 6  
HELX_P HELX_P5  AA5 ASP A 94  ? ASN A 98  ? ASP A 125 ASN A 129 5 ? 5  
HELX_P HELX_P6  AA6 TYR A 107 ? ASN A 114 ? TYR A 138 ASN A 145 1 ? 8  
HELX_P HELX_P7  AA7 ALA A 130 ? ARG A 138 ? ALA A 161 ARG A 169 5 ? 9  
HELX_P HELX_P8  AA8 PHE A 154 ? ALA A 168 ? PHE A 185 ALA A 199 1 ? 15 
HELX_P HELX_P9  AA9 ARG A 174 ? PHE A 178 ? ARG A 205 PHE A 209 5 ? 5  
HELX_P HELX_P10 AB1 TYR A 192 ? LYS A 211 ? TYR A 223 LYS A 242 1 ? 20 
HELX_P HELX_P11 AB2 LYS A 231 ? LYS A 237 ? LYS A 262 LYS A 268 1 ? 7  
HELX_P HELX_P12 AB3 ASP A 243 ? THR A 270 ? ASP A 274 THR A 301 1 ? 28 
HELX_P HELX_P13 AB4 TRP A 305 ? TYR A 309 ? TRP A 336 TYR A 340 1 ? 5  
HELX_P HELX_P14 AB5 ASP A 335 ? GLU A 345 ? ASP A 366 GLU A 376 1 ? 11 
HELX_P HELX_P15 AB6 ILE A 359 ? ASN A 366 ? ILE A 390 ASN A 397 1 ? 8  
HELX_P HELX_P16 AB7 TYR A 423 ? LYS A 439 ? TYR A 454 LYS A 470 1 ? 17 
HELX_P HELX_P17 AB8 SER A 449 ? SER A 458 ? SER A 480 SER A 489 1 ? 10 
HELX_P HELX_P18 AB9 ASN A 463 ? PHE A 468 ? ASN A 494 PHE A 499 1 ? 6  
HELX_P HELX_P19 AC1 VAL A 470 ? ASP A 475 ? VAL A 501 ASP A 506 1 ? 6  
HELX_P HELX_P20 AC2 VAL B 32  ? GLY B 36  ? VAL B 63  GLY B 67  5 ? 5  
HELX_P HELX_P21 AC3 THR B 42  ? ASN B 51  ? THR B 73  ASN B 82  1 ? 10 
HELX_P HELX_P22 AC4 PHE B 64  ? GLY B 75  ? PHE B 95  GLY B 106 1 ? 12 
HELX_P HELX_P23 AC5 TYR B 77  ? GLY B 82  ? TYR B 108 GLY B 113 1 ? 6  
HELX_P HELX_P24 AC6 TYR B 107 ? ALA B 115 ? TYR B 138 ALA B 146 1 ? 9  
HELX_P HELX_P25 AC7 ALA B 130 ? ARG B 138 ? ALA B 161 ARG B 169 5 ? 9  
HELX_P HELX_P26 AC8 PHE B 154 ? ALA B 168 ? PHE B 185 ALA B 199 1 ? 15 
HELX_P HELX_P27 AC9 ARG B 174 ? PHE B 178 ? ARG B 205 PHE B 209 5 ? 5  
HELX_P HELX_P28 AD1 TYR B 192 ? LYS B 211 ? TYR B 223 LYS B 242 1 ? 20 
HELX_P HELX_P29 AD2 LYS B 231 ? ALA B 236 ? LYS B 262 ALA B 267 1 ? 6  
HELX_P HELX_P30 AD3 LYS B 237 ? ALA B 239 ? LYS B 268 ALA B 270 5 ? 3  
HELX_P HELX_P31 AD4 ASP B 243 ? THR B 270 ? ASP B 274 THR B 301 1 ? 28 
HELX_P HELX_P32 AD5 TRP B 305 ? TYR B 309 ? TRP B 336 TYR B 340 1 ? 5  
HELX_P HELX_P33 AD6 ASP B 335 ? ALA B 344 ? ASP B 366 ALA B 375 1 ? 10 
HELX_P HELX_P34 AD7 ILE B 359 ? ASN B 366 ? ILE B 390 ASN B 397 1 ? 8  
HELX_P HELX_P35 AD8 TYR B 423 ? LYS B 439 ? TYR B 454 LYS B 470 1 ? 17 
HELX_P HELX_P36 AD9 SER B 449 ? SER B 458 ? SER B 480 SER B 489 1 ? 10 
HELX_P HELX_P37 AE1 ASN B 463 ? PHE B 468 ? ASN B 494 PHE B 499 1 ? 6  
HELX_P HELX_P38 AE2 VAL B 470 ? VAL B 474 ? VAL B 501 VAL B 505 5 ? 5  
HELX_P HELX_P39 AE3 VAL C 32  ? GLY C 36  ? VAL C 63  GLY C 67  5 ? 5  
HELX_P HELX_P40 AE4 THR C 42  ? ASN C 51  ? THR C 73  ASN C 82  1 ? 10 
HELX_P HELX_P41 AE5 PHE C 64  ? GLY C 75  ? PHE C 95  GLY C 106 1 ? 12 
HELX_P HELX_P42 AE6 TYR C 77  ? GLY C 82  ? TYR C 108 GLY C 113 1 ? 6  
HELX_P HELX_P43 AE7 TYR C 107 ? ASN C 114 ? TYR C 138 ASN C 145 1 ? 8  
HELX_P HELX_P44 AE8 ALA C 130 ? ARG C 138 ? ALA C 161 ARG C 169 5 ? 9  
HELX_P HELX_P45 AE9 PHE C 154 ? ALA C 168 ? PHE C 185 ALA C 199 1 ? 15 
HELX_P HELX_P46 AF1 ARG C 174 ? PHE C 178 ? ARG C 205 PHE C 209 5 ? 5  
HELX_P HELX_P47 AF2 TYR C 192 ? LYS C 212 ? TYR C 223 LYS C 243 1 ? 21 
HELX_P HELX_P48 AF3 LYS C 231 ? ALA C 236 ? LYS C 262 ALA C 267 1 ? 6  
HELX_P HELX_P49 AF4 LYS C 237 ? ALA C 239 ? LYS C 268 ALA C 270 5 ? 3  
HELX_P HELX_P50 AF5 ASP C 243 ? THR C 270 ? ASP C 274 THR C 301 1 ? 28 
HELX_P HELX_P51 AF6 TRP C 305 ? TYR C 309 ? TRP C 336 TYR C 340 1 ? 5  
HELX_P HELX_P52 AF7 ASP C 335 ? ALA C 344 ? ASP C 366 ALA C 375 1 ? 10 
HELX_P HELX_P53 AF8 ILE C 359 ? ASN C 366 ? ILE C 390 ASN C 397 1 ? 8  
HELX_P HELX_P54 AF9 TYR C 423 ? LYS C 439 ? TYR C 454 LYS C 470 1 ? 17 
HELX_P HELX_P55 AG1 SER C 449 ? SER C 458 ? SER C 480 SER C 489 1 ? 10 
HELX_P HELX_P56 AG2 ASN C 463 ? PHE C 468 ? ASN C 494 PHE C 499 1 ? 6  
HELX_P HELX_P57 AG3 VAL C 470 ? VAL C 474 ? VAL C 501 VAL C 505 5 ? 5  
HELX_P HELX_P58 AG4 VAL D 32  ? GLY D 36  ? VAL D 63  GLY D 67  5 ? 5  
HELX_P HELX_P59 AG5 THR D 42  ? ASN D 51  ? THR D 73  ASN D 82  1 ? 10 
HELX_P HELX_P60 AG6 PHE D 64  ? GLY D 75  ? PHE D 95  GLY D 106 1 ? 12 
HELX_P HELX_P61 AG7 TYR D 77  ? GLY D 82  ? TYR D 108 GLY D 113 1 ? 6  
HELX_P HELX_P62 AG8 TYR D 107 ? ALA D 115 ? TYR D 138 ALA D 146 1 ? 9  
HELX_P HELX_P63 AG9 ALA D 130 ? ARG D 138 ? ALA D 161 ARG D 169 5 ? 9  
HELX_P HELX_P64 AH1 PHE D 154 ? ALA D 168 ? PHE D 185 ALA D 199 1 ? 15 
HELX_P HELX_P65 AH2 ARG D 174 ? PHE D 178 ? ARG D 205 PHE D 209 5 ? 5  
HELX_P HELX_P66 AH3 TYR D 192 ? LYS D 212 ? TYR D 223 LYS D 243 1 ? 21 
HELX_P HELX_P67 AH4 LYS D 231 ? LYS D 237 ? LYS D 262 LYS D 268 1 ? 7  
HELX_P HELX_P68 AH5 ASP D 243 ? THR D 270 ? ASP D 274 THR D 301 1 ? 28 
HELX_P HELX_P69 AH6 TRP D 305 ? TYR D 309 ? TRP D 336 TYR D 340 1 ? 5  
HELX_P HELX_P70 AH7 ASP D 335 ? GLU D 345 ? ASP D 366 GLU D 376 1 ? 11 
HELX_P HELX_P71 AH8 ILE D 359 ? ASN D 366 ? ILE D 390 ASN D 397 1 ? 8  
HELX_P HELX_P72 AH9 TYR D 423 ? LYS D 439 ? TYR D 454 LYS D 470 1 ? 17 
HELX_P HELX_P73 AI1 SER D 449 ? GLY D 459 ? SER D 480 GLY D 490 1 ? 11 
HELX_P HELX_P74 AI2 ASN D 463 ? PHE D 468 ? ASN D 494 PHE D 499 1 ? 6  
HELX_P HELX_P75 AI3 VAL D 470 ? ASP D 475 ? VAL D 501 ASP D 506 1 ? 6  
# 
_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 both ? A PHE 64  C   ? ? ? 1_555 A  DDZ 65 N  B ? A PHE 95  A DDZ 96  1_555 ? ? ? ? ? ? ? 1.346 ? ? 
covale2  covale both ? A DDZ 65  C   B ? ? 1_555 A  GLY 66 N  ? ? A DDZ 96  A GLY 97  1_555 ? ? ? ? ? ? ? 1.323 ? ? 
covale3  covale both ? B PHE 64  C   ? ? ? 1_555 B  DDZ 65 N  B ? B PHE 95  B DDZ 96  1_555 ? ? ? ? ? ? ? 1.345 ? ? 
covale4  covale both ? B DDZ 65  C   B ? ? 1_555 B  GLY 66 N  ? ? B DDZ 96  B GLY 97  1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale5  covale both ? C PHE 64  C   ? ? ? 1_555 C  DDZ 65 N  B ? C PHE 95  C DDZ 96  1_555 ? ? ? ? ? ? ? 1.340 ? ? 
covale6  covale both ? C DDZ 65  C   B ? ? 1_555 C  GLY 66 N  ? ? C DDZ 96  C GLY 97  1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale7  covale both ? D PHE 64  C   ? ? ? 1_555 D  DDZ 65 N  B ? D PHE 95  D DDZ 96  1_555 ? ? ? ? ? ? ? 1.341 ? ? 
covale8  covale both ? D DDZ 65  C   B ? ? 1_555 D  GLY 66 N  ? ? D DDZ 96  D GLY 97  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
metalc1  metalc ?    ? A ASP 25  OD1 ? ? ? 1_555 P  CA  .  CA ? ? A ASP 56  A CA  612 1_555 ? ? ? ? ? ? ? 2.235 ? ? 
metalc2  metalc ?    ? A ASP 26  OD1 ? ? ? 1_555 P  CA  .  CA ? ? A ASP 57  A CA  612 1_555 ? ? ? ? ? ? ? 2.284 ? ? 
metalc3  metalc ?    ? A DDZ 65  OG1 B ? ? 1_555 P  CA  .  CA ? ? A DDZ 96  A CA  612 1_555 ? ? ? ? ? ? ? 2.881 ? ? 
metalc4  metalc ?    ? A ASP 283 OD1 ? ? ? 1_555 P  CA  .  CA ? ? A ASP 314 A CA  612 1_555 ? ? ? ? ? ? ? 2.680 ? ? 
metalc5  metalc ?    ? A ASP 283 OD2 ? ? ? 1_555 P  CA  .  CA ? ? A ASP 314 A CA  612 1_555 ? ? ? ? ? ? ? 2.361 ? ? 
metalc6  metalc ?    ? A ASN 284 OD1 ? ? ? 1_555 P  CA  .  CA ? ? A ASN 315 A CA  612 1_555 ? ? ? ? ? ? ? 2.489 ? ? 
metalc7  metalc ?    ? B ASP 25  OD1 ? ? ? 1_555 Z  CA  .  CA ? ? B ASP 56  B CA  610 1_555 ? ? ? ? ? ? ? 2.390 ? ? 
metalc8  metalc ?    ? B ASP 26  OD1 ? ? ? 1_555 Z  CA  .  CA ? ? B ASP 57  B CA  610 1_555 ? ? ? ? ? ? ? 2.274 ? ? 
metalc9  metalc ?    ? B DDZ 65  OG2 B ? ? 1_555 Z  CA  .  CA ? ? B DDZ 96  B CA  610 1_555 ? ? ? ? ? ? ? 3.041 ? ? 
metalc10 metalc ?    ? B ASP 283 OD1 ? ? ? 1_555 Z  CA  .  CA ? ? B ASP 314 B CA  610 1_555 ? ? ? ? ? ? ? 2.558 ? ? 
metalc11 metalc ?    ? B ASP 283 OD2 ? ? ? 1_555 Z  CA  .  CA ? ? B ASP 314 B CA  610 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc12 metalc ?    ? C ASP 25  OD1 ? ? ? 1_555 HA CA  .  CA ? ? C ASP 56  C CA  608 1_555 ? ? ? ? ? ? ? 2.243 ? ? 
metalc13 metalc ?    ? C ASP 26  OD1 ? ? ? 1_555 HA CA  .  CA ? ? C ASP 57  C CA  608 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc14 metalc ?    ? C DDZ 65  OG1 B ? ? 1_555 HA CA  .  CA ? ? C DDZ 96  C CA  608 1_555 ? ? ? ? ? ? ? 2.524 ? ? 
metalc15 metalc ?    ? C ASP 283 OD1 ? ? ? 1_555 HA CA  .  CA ? ? C ASP 314 C CA  608 1_555 ? ? ? ? ? ? ? 2.632 ? ? 
metalc16 metalc ?    ? C ASP 283 OD2 ? ? ? 1_555 HA CA  .  CA ? ? C ASP 314 C CA  608 1_555 ? ? ? ? ? ? ? 2.243 ? ? 
metalc17 metalc ?    ? D ASP 25  OD1 ? ? ? 1_555 QA CA  .  CA ? ? D ASP 56  D CA  609 1_555 ? ? ? ? ? ? ? 2.203 ? ? 
metalc18 metalc ?    ? D ASP 26  OD1 ? ? ? 1_555 QA CA  .  CA ? ? D ASP 57  D CA  609 1_555 ? ? ? ? ? ? ? 2.354 ? ? 
metalc19 metalc ?    ? D DDZ 65  OG2 B ? ? 1_555 QA CA  .  CA ? ? D DDZ 96  D CA  609 1_555 ? ? ? ? ? ? ? 3.165 ? ? 
metalc20 metalc ?    ? D ASP 283 OD1 ? ? ? 1_555 QA CA  .  CA ? ? D ASP 314 D CA  609 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc21 metalc ?    ? D ASP 283 OD2 ? ? ? 1_555 QA CA  .  CA ? ? D ASP 314 D CA  609 1_555 ? ? ? ? ? ? ? 2.448 ? ? 
metalc22 metalc ?    ? D ASN 284 OD1 ? ? ? 1_555 QA CA  .  CA ? ? D ASN 315 D CA  609 1_555 ? ? ? ? ? ? ? 2.532 ? ? 
# 
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  OD1 ? A ASP 25  ? A ASP 56  ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD1 ? A ASP 26  ? A ASP 57  ? 1_555 87.5  ? 
2  OD1 ? A ASP 25  ? A ASP 56  ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OG1 B A DDZ 65  ? A DDZ 96  ? 1_555 98.1  ? 
3  OD1 ? A ASP 26  ? A ASP 57  ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OG1 B A DDZ 65  ? A DDZ 96  ? 1_555 110.4 ? 
4  OD1 ? A ASP 25  ? A ASP 56  ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD1 ? A ASP 283 ? A ASP 314 ? 1_555 87.4  ? 
5  OD1 ? A ASP 26  ? A ASP 57  ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD1 ? A ASP 283 ? A ASP 314 ? 1_555 102.8 ? 
6  OG1 B A DDZ 65  ? A DDZ 96  ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD1 ? A ASP 283 ? A ASP 314 ? 1_555 146.6 ? 
7  OD1 ? A ASP 25  ? A ASP 56  ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD2 ? A ASP 283 ? A ASP 314 ? 1_555 90.2  ? 
8  OD1 ? A ASP 26  ? A ASP 57  ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD2 ? A ASP 283 ? A ASP 314 ? 1_555 154.0 ? 
9  OG1 B A DDZ 65  ? A DDZ 96  ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD2 ? A ASP 283 ? A ASP 314 ? 1_555 95.6  ? 
10 OD1 ? A ASP 283 ? A ASP 314 ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD2 ? A ASP 283 ? A ASP 314 ? 1_555 51.2  ? 
11 OD1 ? A ASP 25  ? A ASP 56  ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD1 ? A ASN 284 ? A ASN 315 ? 1_555 163.1 ? 
12 OD1 ? A ASP 26  ? A ASP 57  ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD1 ? A ASN 284 ? A ASN 315 ? 1_555 94.6  ? 
13 OG1 B A DDZ 65  ? A DDZ 96  ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD1 ? A ASN 284 ? A ASN 315 ? 1_555 96.8  ? 
14 OD1 ? A ASP 283 ? A ASP 314 ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD1 ? A ASN 284 ? A ASN 315 ? 1_555 75.8  ? 
15 OD2 ? A ASP 283 ? A ASP 314 ? 1_555 CA ? P  CA . ? A CA 612 ? 1_555 OD1 ? A ASN 284 ? A ASN 315 ? 1_555 80.5  ? 
16 OD1 ? B ASP 25  ? B ASP 56  ? 1_555 CA ? Z  CA . ? B CA 610 ? 1_555 OD1 ? B ASP 26  ? B ASP 57  ? 1_555 83.6  ? 
17 OD1 ? B ASP 25  ? B ASP 56  ? 1_555 CA ? Z  CA . ? B CA 610 ? 1_555 OG2 B B DDZ 65  ? B DDZ 96  ? 1_555 91.4  ? 
18 OD1 ? B ASP 26  ? B ASP 57  ? 1_555 CA ? Z  CA . ? B CA 610 ? 1_555 OG2 B B DDZ 65  ? B DDZ 96  ? 1_555 109.5 ? 
19 OD1 ? B ASP 25  ? B ASP 56  ? 1_555 CA ? Z  CA . ? B CA 610 ? 1_555 OD1 ? B ASP 283 ? B ASP 314 ? 1_555 86.3  ? 
20 OD1 ? B ASP 26  ? B ASP 57  ? 1_555 CA ? Z  CA . ? B CA 610 ? 1_555 OD1 ? B ASP 283 ? B ASP 314 ? 1_555 103.9 ? 
21 OG2 B B DDZ 65  ? B DDZ 96  ? 1_555 CA ? Z  CA . ? B CA 610 ? 1_555 OD1 ? B ASP 283 ? B ASP 314 ? 1_555 146.0 ? 
22 OD1 ? B ASP 25  ? B ASP 56  ? 1_555 CA ? Z  CA . ? B CA 610 ? 1_555 OD2 ? B ASP 283 ? B ASP 314 ? 1_555 86.6  ? 
23 OD1 ? B ASP 26  ? B ASP 57  ? 1_555 CA ? Z  CA . ? B CA 610 ? 1_555 OD2 ? B ASP 283 ? B ASP 314 ? 1_555 155.2 ? 
24 OG2 B B DDZ 65  ? B DDZ 96  ? 1_555 CA ? Z  CA . ? B CA 610 ? 1_555 OD2 ? B ASP 283 ? B ASP 314 ? 1_555 93.4  ? 
25 OD1 ? B ASP 283 ? B ASP 314 ? 1_555 CA ? Z  CA . ? B CA 610 ? 1_555 OD2 ? B ASP 283 ? B ASP 314 ? 1_555 52.6  ? 
26 OD1 ? C ASP 25  ? C ASP 56  ? 1_555 CA ? HA CA . ? C CA 608 ? 1_555 OD1 ? C ASP 26  ? C ASP 57  ? 1_555 79.5  ? 
27 OD1 ? C ASP 25  ? C ASP 56  ? 1_555 CA ? HA CA . ? C CA 608 ? 1_555 OG1 B C DDZ 65  ? C DDZ 96  ? 1_555 96.1  ? 
28 OD1 ? C ASP 26  ? C ASP 57  ? 1_555 CA ? HA CA . ? C CA 608 ? 1_555 OG1 B C DDZ 65  ? C DDZ 96  ? 1_555 117.8 ? 
29 OD1 ? C ASP 25  ? C ASP 56  ? 1_555 CA ? HA CA . ? C CA 608 ? 1_555 OD1 ? C ASP 283 ? C ASP 314 ? 1_555 83.2  ? 
30 OD1 ? C ASP 26  ? C ASP 57  ? 1_555 CA ? HA CA . ? C CA 608 ? 1_555 OD1 ? C ASP 283 ? C ASP 314 ? 1_555 95.8  ? 
31 OG1 B C DDZ 65  ? C DDZ 96  ? 1_555 CA ? HA CA . ? C CA 608 ? 1_555 OD1 ? C ASP 283 ? C ASP 314 ? 1_555 145.7 ? 
32 OD1 ? C ASP 25  ? C ASP 56  ? 1_555 CA ? HA CA . ? C CA 608 ? 1_555 OD2 ? C ASP 283 ? C ASP 314 ? 1_555 87.2  ? 
33 OD1 ? C ASP 26  ? C ASP 57  ? 1_555 CA ? HA CA . ? C CA 608 ? 1_555 OD2 ? C ASP 283 ? C ASP 314 ? 1_555 147.1 ? 
34 OG1 B C DDZ 65  ? C DDZ 96  ? 1_555 CA ? HA CA . ? C CA 608 ? 1_555 OD2 ? C ASP 283 ? C ASP 314 ? 1_555 93.3  ? 
35 OD1 ? C ASP 283 ? C ASP 314 ? 1_555 CA ? HA CA . ? C CA 608 ? 1_555 OD2 ? C ASP 283 ? C ASP 314 ? 1_555 52.5  ? 
36 OD1 ? D ASP 25  ? D ASP 56  ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD1 ? D ASP 26  ? D ASP 57  ? 1_555 93.2  ? 
37 OD1 ? D ASP 25  ? D ASP 56  ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OG2 B D DDZ 65  ? D DDZ 96  ? 1_555 95.4  ? 
38 OD1 ? D ASP 26  ? D ASP 57  ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OG2 B D DDZ 65  ? D DDZ 96  ? 1_555 108.4 ? 
39 OD1 ? D ASP 25  ? D ASP 56  ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD1 ? D ASP 283 ? D ASP 314 ? 1_555 90.7  ? 
40 OD1 ? D ASP 26  ? D ASP 57  ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD1 ? D ASP 283 ? D ASP 314 ? 1_555 107.7 ? 
41 OG2 B D DDZ 65  ? D DDZ 96  ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD1 ? D ASP 283 ? D ASP 314 ? 1_555 143.0 ? 
42 OD1 ? D ASP 25  ? D ASP 56  ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD2 ? D ASP 283 ? D ASP 314 ? 1_555 89.7  ? 
43 OD1 ? D ASP 26  ? D ASP 57  ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD2 ? D ASP 283 ? D ASP 314 ? 1_555 161.5 ? 
44 OG2 B D DDZ 65  ? D DDZ 96  ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD2 ? D ASP 283 ? D ASP 314 ? 1_555 89.5  ? 
45 OD1 ? D ASP 283 ? D ASP 314 ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD2 ? D ASP 283 ? D ASP 314 ? 1_555 54.0  ? 
46 OD1 ? D ASP 25  ? D ASP 56  ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD1 ? D ASN 284 ? D ASN 315 ? 1_555 166.8 ? 
47 OD1 ? D ASP 26  ? D ASP 57  ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD1 ? D ASN 284 ? D ASN 315 ? 1_555 91.5  ? 
48 OG2 B D DDZ 65  ? D DDZ 96  ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD1 ? D ASN 284 ? D ASN 315 ? 1_555 94.7  ? 
49 OD1 ? D ASP 283 ? D ASP 314 ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD1 ? D ASN 284 ? D ASN 315 ? 1_555 76.2  ? 
50 OD2 ? D ASP 283 ? D ASP 314 ? 1_555 CA ? QA CA . ? D CA 609 ? 1_555 OD1 ? D ASN 284 ? D ASN 315 ? 1_555 82.1  ? 
# 
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 DDZ A 65 B . . . . DDZ A 96 ? 1_555 . . . . . . . ALA 1 DDZ Hydroxylation 'Named protein modification' 
2 DDZ B 65 B . . . . DDZ B 96 ? 1_555 . . . . . . . ALA 1 DDZ Hydroxylation 'Named protein modification' 
3 DDZ C 65 B . . . . DDZ C 96 ? 1_555 . . . . . . . ALA 1 DDZ Hydroxylation 'Named protein modification' 
4 DDZ D 65 B . . . . DDZ D 96 ? 1_555 . . . . . . . ALA 1 DDZ Hydroxylation 'Named protein modification' 
# 
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  ALA 223 A . ? ALA 254 A PRO 224 A ? PRO 255 A 1 -2.96 
2  VAL 226 A . ? VAL 257 A PRO 227 A ? PRO 258 A 1 0.24  
3  TYR 295 A . ? TYR 326 A PRO 296 A ? PRO 327 A 1 3.44  
4  MET 461 A . ? MET 492 A PRO 462 A ? PRO 493 A 1 2.84  
5  ALA 223 B . ? ALA 254 B PRO 224 B ? PRO 255 B 1 -3.97 
6  VAL 226 B . ? VAL 257 B PRO 227 B ? PRO 258 B 1 1.04  
7  TYR 295 B . ? TYR 326 B PRO 296 B ? PRO 327 B 1 1.29  
8  MET 461 B . ? MET 492 B PRO 462 B ? PRO 493 B 1 4.40  
9  ALA 223 C . ? ALA 254 C PRO 224 C ? PRO 255 C 1 -7.25 
10 VAL 226 C . ? VAL 257 C PRO 227 C ? PRO 258 C 1 0.89  
11 TYR 295 C . ? TYR 326 C PRO 296 C ? PRO 327 C 1 0.18  
12 MET 461 C . ? MET 492 C PRO 462 C ? PRO 493 C 1 1.43  
13 ALA 223 D . ? ALA 254 D PRO 224 D ? PRO 255 D 1 -4.70 
14 VAL 226 D . ? VAL 257 D PRO 227 D ? PRO 258 D 1 -0.32 
15 TYR 295 D . ? TYR 326 D PRO 296 D ? PRO 327 D 1 0.43  
16 MET 461 D . ? MET 492 D PRO 462 D ? PRO 493 D 1 3.58  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 10 ? 
AA3 ? 4  ? 
AA4 ? 10 ? 
AA5 ? 3  ? 
AA6 ? 4  ? 
AA7 ? 10 ? 
AA8 ? 3  ? 
AA9 ? 4  ? 
AB1 ? 9  ? 
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  ? anti-parallel 
AA1 2 3  ? anti-parallel 
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
AA1 6 7  ? parallel      
AA1 7 8  ? anti-parallel 
AA1 8 9  ? anti-parallel 
AA1 9 10 ? parallel      
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? parallel      
AA2 4 5  ? parallel      
AA2 5 6  ? parallel      
AA2 6 7  ? parallel      
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? parallel      
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA4 1 2  ? anti-parallel 
AA4 2 3  ? anti-parallel 
AA4 3 4  ? parallel      
AA4 4 5  ? parallel      
AA4 5 6  ? parallel      
AA4 6 7  ? parallel      
AA4 7 8  ? anti-parallel 
AA4 8 9  ? anti-parallel 
AA4 9 10 ? 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  ? anti-parallel 
AA7 2 3  ? anti-parallel 
AA7 3 4  ? parallel      
AA7 4 5  ? parallel      
AA7 5 6  ? parallel      
AA7 6 7  ? parallel      
AA7 7 8  ? anti-parallel 
AA7 8 9  ? anti-parallel 
AA7 9 10 ? parallel      
AA8 1 2  ? anti-parallel 
AA8 2 3  ? parallel      
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AB1 1 2  ? anti-parallel 
AB1 2 3  ? parallel      
AB1 3 4  ? parallel      
AB1 4 5  ? parallel      
AB1 5 6  ? parallel      
AB1 6 7  ? anti-parallel 
AB1 7 8  ? anti-parallel 
AB1 8 9  ? 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  LYS A 185 ? PRO A 186 ? LYS A 216 PRO A 217 
AA1 2  GLU A 181 ? HIS A 182 ? GLU A 212 HIS A 213 
AA1 3  ASP A 142 ? PHE A 146 ? ASP A 173 PHE A 177 
AA1 4  TYR A 118 ? LYS A 124 ? TYR A 149 LYS A 155 
AA1 5  PHE A 215 ? ALA A 220 ? PHE A 246 ALA A 251 
AA1 6  ASN A 18  ? CYS A 24  ? ASN A 49  CYS A 55  
AA1 7  THR A 276 ? SER A 282 ? THR A 307 SER A 313 
AA1 8  ARG A 310 ? HIS A 316 ? ARG A 341 HIS A 347 
AA1 9  SER A 53  ? TYR A 59  ? SER A 84  TYR A 90  
AA1 10 GLN A 325 ? PHE A 327 ? GLN A 356 PHE A 358 
AA2 1  LYS A 185 ? PRO A 186 ? LYS A 216 PRO A 217 
AA2 2  GLU A 181 ? HIS A 182 ? GLU A 212 HIS A 213 
AA2 3  ASP A 142 ? PHE A 146 ? ASP A 173 PHE A 177 
AA2 4  TYR A 118 ? LYS A 124 ? TYR A 149 LYS A 155 
AA2 5  PHE A 215 ? ALA A 220 ? PHE A 246 ALA A 251 
AA2 6  ASN A 18  ? CYS A 24  ? ASN A 49  CYS A 55  
AA2 7  THR A 276 ? SER A 282 ? THR A 307 SER A 313 
AA2 8  ARG A 310 ? HIS A 316 ? ARG A 341 HIS A 347 
AA2 9  SER A 53  ? TYR A 59  ? SER A 84  TYR A 90  
AA2 10 VAL A 331 ? SER A 332 ? VAL A 362 SER A 363 
AA3 1  ILE A 375 ? TYR A 380 ? ILE A 406 TYR A 411 
AA3 2  ASN A 385 ? MET A 391 ? ASN A 416 MET A 422 
AA3 3  TRP A 394 ? ARG A 398 ? TRP A 425 ARG A 429 
AA3 4  ARG A 405 ? ASN A 408 ? ARG A 436 ASN A 439 
AA4 1  LYS B 185 ? PRO B 186 ? LYS B 216 PRO B 217 
AA4 2  GLU B 181 ? HIS B 182 ? GLU B 212 HIS B 213 
AA4 3  ASP B 142 ? PHE B 146 ? ASP B 173 PHE B 177 
AA4 4  TYR B 118 ? LYS B 124 ? TYR B 149 LYS B 155 
AA4 5  PHE B 215 ? ALA B 220 ? PHE B 246 ALA B 251 
AA4 6  ASN B 18  ? CYS B 24  ? ASN B 49  CYS B 55  
AA4 7  THR B 276 ? SER B 282 ? THR B 307 SER B 313 
AA4 8  MET B 313 ? HIS B 316 ? MET B 344 HIS B 347 
AA4 9  SER B 53  ? PHE B 55  ? SER B 84  PHE B 86  
AA4 10 GLN B 325 ? PHE B 327 ? GLN B 356 PHE B 358 
AA5 1  ARG B 310 ? VAL B 311 ? ARG B 341 VAL B 342 
AA5 2  ALA B 58  ? TYR B 59  ? ALA B 89  TYR B 90  
AA5 3  VAL B 331 ? SER B 332 ? VAL B 362 SER B 363 
AA6 1  ILE B 375 ? TYR B 380 ? ILE B 406 TYR B 411 
AA6 2  ASN B 385 ? MET B 391 ? ASN B 416 MET B 422 
AA6 3  TRP B 394 ? ARG B 398 ? TRP B 425 ARG B 429 
AA6 4  ARG B 405 ? ASN B 408 ? ARG B 436 ASN B 439 
AA7 1  LYS C 185 ? PRO C 186 ? LYS C 216 PRO C 217 
AA7 2  GLU C 181 ? HIS C 182 ? GLU C 212 HIS C 213 
AA7 3  ASP C 142 ? PHE C 146 ? ASP C 173 PHE C 177 
AA7 4  TYR C 118 ? LYS C 124 ? TYR C 149 LYS C 155 
AA7 5  PHE C 215 ? ALA C 220 ? PHE C 246 ALA C 251 
AA7 6  ASN C 18  ? CYS C 24  ? ASN C 49  CYS C 55  
AA7 7  THR C 276 ? SER C 282 ? THR C 307 SER C 313 
AA7 8  MET C 313 ? HIS C 316 ? MET C 344 HIS C 347 
AA7 9  SER C 53  ? PHE C 55  ? SER C 84  PHE C 86  
AA7 10 GLN C 325 ? PHE C 327 ? GLN C 356 PHE C 358 
AA8 1  ARG C 310 ? VAL C 311 ? ARG C 341 VAL C 342 
AA8 2  ALA C 58  ? TYR C 59  ? ALA C 89  TYR C 90  
AA8 3  VAL C 331 ? SER C 332 ? VAL C 362 SER C 363 
AA9 1  ILE C 375 ? TYR C 380 ? ILE C 406 TYR C 411 
AA9 2  ASN C 385 ? MET C 391 ? ASN C 416 MET C 422 
AA9 3  TRP C 394 ? ARG C 398 ? TRP C 425 ARG C 429 
AA9 4  ARG C 405 ? ASN C 408 ? ARG C 436 ASN C 439 
AB1 1  GLU D 181 ? HIS D 182 ? GLU D 212 HIS D 213 
AB1 2  ASP D 142 ? PHE D 146 ? ASP D 173 PHE D 177 
AB1 3  TYR D 118 ? LYS D 124 ? TYR D 149 LYS D 155 
AB1 4  PHE D 215 ? ALA D 220 ? PHE D 246 ALA D 251 
AB1 5  ASN D 18  ? CYS D 24  ? ASN D 49  CYS D 55  
AB1 6  THR D 276 ? SER D 282 ? THR D 307 SER D 313 
AB1 7  MET D 313 ? HIS D 316 ? MET D 344 HIS D 347 
AB1 8  SER D 53  ? PHE D 55  ? SER D 84  PHE D 86  
AB1 9  GLN D 325 ? PHE D 327 ? GLN D 356 PHE D 358 
AB2 1  ARG D 310 ? VAL D 311 ? ARG D 341 VAL D 342 
AB2 2  ALA D 58  ? TYR D 59  ? ALA D 89  TYR D 90  
AB2 3  VAL D 331 ? SER D 332 ? VAL D 362 SER D 363 
AB3 1  ILE D 375 ? TYR D 380 ? ILE D 406 TYR D 411 
AB3 2  ASN D 385 ? MET D 391 ? ASN D 416 MET D 422 
AB3 3  TRP D 394 ? ARG D 398 ? TRP D 425 ARG D 429 
AB3 4  ARG D 405 ? ASN D 408 ? ARG D 436 ASN D 439 
# 
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 LYS A 185 ? O LYS A 216 N HIS A 182 ? N HIS A 213 
AA1 2 3  O GLU A 181 ? O GLU A 212 N GLY A 145 ? N GLY A 176 
AA1 3 4  O TYR A 144 ? O TYR A 175 N GLY A 123 ? N GLY A 154 
AA1 4 5  N SER A 120 ? N SER A 151 O TYR A 218 ? O TYR A 249 
AA1 5 6  O PHE A 215 ? O PHE A 246 N ILE A 19  ? N ILE A 50  
AA1 6 7  N VAL A 22  ? N VAL A 53  O VAL A 279 ? O VAL A 310 
AA1 7 8  N ILE A 278 ? N ILE A 309 O HIS A 316 ? O HIS A 347 
AA1 8 9  O MET A 313 ? O MET A 344 N PHE A 55  ? N PHE A 86  
AA1 9 10 N ILE A 54  ? N ILE A 85  O PHE A 327 ? O PHE A 358 
AA2 1 2  O LYS A 185 ? O LYS A 216 N HIS A 182 ? N HIS A 213 
AA2 2 3  O GLU A 181 ? O GLU A 212 N GLY A 145 ? N GLY A 176 
AA2 3 4  O TYR A 144 ? O TYR A 175 N GLY A 123 ? N GLY A 154 
AA2 4 5  N SER A 120 ? N SER A 151 O TYR A 218 ? O TYR A 249 
AA2 5 6  O PHE A 215 ? O PHE A 246 N ILE A 19  ? N ILE A 50  
AA2 6 7  N VAL A 22  ? N VAL A 53  O VAL A 279 ? O VAL A 310 
AA2 7 8  N ILE A 278 ? N ILE A 309 O HIS A 316 ? O HIS A 347 
AA2 8 9  O MET A 313 ? O MET A 344 N PHE A 55  ? N PHE A 86  
AA2 9 10 N SER A 57  ? N SER A 88  O VAL A 331 ? O VAL A 362 
AA3 1 2  N ILE A 375 ? N ILE A 406 O ARG A 390 ? O ARG A 421 
AA3 2 3  N MET A 391 ? N MET A 422 O TRP A 394 ? O TRP A 425 
AA3 3 4  N LYS A 395 ? N LYS A 426 O HIS A 407 ? O HIS A 438 
AA4 1 2  O LYS B 185 ? O LYS B 216 N HIS B 182 ? N HIS B 213 
AA4 2 3  O GLU B 181 ? O GLU B 212 N GLY B 145 ? N GLY B 176 
AA4 3 4  O TYR B 144 ? O TYR B 175 N GLY B 123 ? N GLY B 154 
AA4 4 5  N SER B 120 ? N SER B 151 O TYR B 218 ? O TYR B 249 
AA4 5 6  O PHE B 215 ? O PHE B 246 N ILE B 19  ? N ILE B 50  
AA4 6 7  N LEU B 20  ? N LEU B 51  O VAL B 279 ? O VAL B 310 
AA4 7 8  N ILE B 278 ? N ILE B 309 O HIS B 316 ? O HIS B 347 
AA4 8 9  O MET B 313 ? O MET B 344 N PHE B 55  ? N PHE B 86  
AA4 9 10 N ILE B 54  ? N ILE B 85  O PHE B 327 ? O PHE B 358 
AA5 1 2  O VAL B 311 ? O VAL B 342 N ALA B 58  ? N ALA B 89  
AA5 2 3  N TYR B 59  ? N TYR B 90  O VAL B 331 ? O VAL B 362 
AA6 1 2  N ILE B 375 ? N ILE B 406 O ARG B 390 ? O ARG B 421 
AA6 2 3  N ALA B 389 ? N ALA B 420 O ILE B 396 ? O ILE B 427 
AA6 3 4  N LYS B 395 ? N LYS B 426 O HIS B 407 ? O HIS B 438 
AA7 1 2  O LYS C 185 ? O LYS C 216 N HIS C 182 ? N HIS C 213 
AA7 2 3  O GLU C 181 ? O GLU C 212 N GLY C 145 ? N GLY C 176 
AA7 3 4  O ASP C 142 ? O ASP C 173 N ALA C 121 ? N ALA C 152 
AA7 4 5  N SER C 120 ? N SER C 151 O TYR C 218 ? O TYR C 249 
AA7 5 6  O PHE C 215 ? O PHE C 246 N ILE C 19  ? N ILE C 50  
AA7 6 7  N ASN C 18  ? N ASN C 49  O LEU C 277 ? O LEU C 308 
AA7 7 8  N ILE C 278 ? N ILE C 309 O HIS C 316 ? O HIS C 347 
AA7 8 9  O MET C 313 ? O MET C 344 N PHE C 55  ? N PHE C 86  
AA7 9 10 N ILE C 54  ? N ILE C 85  O PHE C 327 ? O PHE C 358 
AA8 1 2  O VAL C 311 ? O VAL C 342 N ALA C 58  ? N ALA C 89  
AA8 2 3  N TYR C 59  ? N TYR C 90  O VAL C 331 ? O VAL C 362 
AA9 1 2  N SER C 377 ? N SER C 408 O GLY C 388 ? O GLY C 419 
AA9 2 3  N MET C 391 ? N MET C 422 O TRP C 394 ? O TRP C 425 
AA9 3 4  N LYS C 395 ? N LYS C 426 O HIS C 407 ? O HIS C 438 
AB1 1 2  O GLU D 181 ? O GLU D 212 N GLY D 145 ? N GLY D 176 
AB1 2 3  O TYR D 144 ? O TYR D 175 N GLY D 123 ? N GLY D 154 
AB1 3 4  N SER D 120 ? N SER D 151 O TYR D 218 ? O TYR D 249 
AB1 4 5  O LEU D 219 ? O LEU D 250 N LEU D 23  ? N LEU D 54  
AB1 5 6  N ASN D 18  ? N ASN D 49  O LEU D 277 ? O LEU D 308 
AB1 6 7  N ILE D 278 ? N ILE D 309 O HIS D 316 ? O HIS D 347 
AB1 7 8  O MET D 313 ? O MET D 344 N PHE D 55  ? N PHE D 86  
AB1 8 9  N ILE D 54  ? N ILE D 85  O PHE D 327 ? O PHE D 358 
AB2 1 2  O VAL D 311 ? O VAL D 342 N ALA D 58  ? N ALA D 89  
AB2 2 3  N TYR D 59  ? N TYR D 90  O VAL D 331 ? O VAL D 362 
AB3 1 2  N ARG D 379 ? N ARG D 410 O ASP D 386 ? O ASP D 417 
AB3 2 3  N ALA D 389 ? N ALA D 420 O ILE D 396 ? O ILE D 427 
AB3 3 4  N LYS D 395 ? N LYS D 426 O HIS D 407 ? O HIS D 438 
# 
_pdbx_entry_details.entry_id                   9HH3 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 CYS A 96  ? A -34.61  -81.28 
2  1 DDZ A 96  ? B -29.17  -79.94 
3  1 TRP A 156 ? ? -111.21 -82.78 
4  1 TYR A 223 ? ? -32.28  116.93 
5  1 ALA A 251 ? ? -102.32 74.43  
6  1 PRO A 255 ? ? -96.99  36.65  
7  1 TRP A 348 ? ? -156.91 83.84  
8  1 LYS A 351 ? ? -133.72 -32.46 
9  1 VAL A 501 ? ? -132.67 -60.85 
10 1 CYS B 96  ? A -53.18  -76.05 
11 1 DDZ B 96  ? B -45.40  -84.08 
12 1 ASN B 129 ? ? -95.85  57.07  
13 1 TRP B 156 ? ? -110.66 -82.08 
14 1 TYR B 223 ? ? -31.37  117.51 
15 1 ALA B 251 ? ? -100.72 75.62  
16 1 PRO B 255 ? ? -94.64  36.79  
17 1 TRP B 348 ? ? -157.67 85.49  
18 1 LYS B 351 ? ? -137.61 -33.79 
19 1 VAL B 501 ? ? -132.63 -60.44 
20 1 CYS C 96  ? A -40.33  -83.02 
21 1 DDZ C 96  ? B -50.96  -75.57 
22 1 ASN C 129 ? ? -38.60  58.32  
23 1 TRP C 156 ? ? -110.02 -84.54 
24 1 TYR C 223 ? ? -35.26  113.52 
25 1 ALA C 251 ? ? -100.97 78.76  
26 1 PRO C 255 ? ? -96.91  36.10  
27 1 TRP C 348 ? ? -155.82 87.23  
28 1 LYS C 351 ? ? -135.82 -32.96 
29 1 VAL C 501 ? ? -132.45 -62.34 
30 1 CYS D 96  ? A -43.58  -73.88 
31 1 DDZ D 96  ? B -41.95  -76.42 
32 1 ASN D 129 ? ? -67.32  55.51  
33 1 TRP D 156 ? ? -111.05 -81.90 
34 1 PRO D 217 ? ? -55.25  -1.81  
35 1 ALA D 218 ? ? 58.55   -48.29 
36 1 TYR D 223 ? ? -37.84  115.04 
37 1 ALA D 251 ? ? -101.77 75.97  
38 1 PRO D 255 ? ? -96.35  35.89  
39 1 TRP D 348 ? ? -157.55 87.59  
40 1 VAL D 501 ? ? -132.57 -62.39 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
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 32  ? A MET 1   
2  1 Y 1 A GLY 33  ? A GLY 2   
3  1 Y 1 A SER 34  ? A SER 3   
4  1 Y 1 A SER 35  ? A SER 4   
5  1 Y 1 A HIS 36  ? A HIS 5   
6  1 Y 1 A HIS 37  ? A HIS 6   
7  1 Y 1 A HIS 38  ? A HIS 7   
8  1 Y 1 A HIS 39  ? A HIS 8   
9  1 Y 1 A HIS 40  ? A HIS 9   
10 1 Y 1 A HIS 41  ? A HIS 10  
11 1 Y 1 A GLY 42  ? A GLY 11  
12 1 Y 1 A SER 43  ? A SER 12  
13 1 Y 1 A GLN 44  ? A GLN 13  
14 1 Y 1 A GLU 45  ? A GLU 14  
15 1 Y 1 A HIS 510 ? A HIS 479 
16 1 Y 1 A LYS 511 ? A LYS 480 
17 1 Y 1 B MET 32  ? B MET 1   
18 1 Y 1 B GLY 33  ? B GLY 2   
19 1 Y 1 B SER 34  ? B SER 3   
20 1 Y 1 B SER 35  ? B SER 4   
21 1 Y 1 B HIS 36  ? B HIS 5   
22 1 Y 1 B HIS 37  ? B HIS 6   
23 1 Y 1 B HIS 38  ? B HIS 7   
24 1 Y 1 B HIS 39  ? B HIS 8   
25 1 Y 1 B HIS 40  ? B HIS 9   
26 1 Y 1 B HIS 41  ? B HIS 10  
27 1 Y 1 B GLY 42  ? B GLY 11  
28 1 Y 1 B SER 43  ? B SER 12  
29 1 Y 1 B GLN 44  ? B GLN 13  
30 1 Y 1 B GLU 45  ? B GLU 14  
31 1 Y 1 B HIS 510 ? B HIS 479 
32 1 Y 1 B LYS 511 ? B LYS 480 
33 1 Y 1 C MET 32  ? C MET 1   
34 1 Y 1 C GLY 33  ? C GLY 2   
35 1 Y 1 C SER 34  ? C SER 3   
36 1 Y 1 C SER 35  ? C SER 4   
37 1 Y 1 C HIS 36  ? C HIS 5   
38 1 Y 1 C HIS 37  ? C HIS 6   
39 1 Y 1 C HIS 38  ? C HIS 7   
40 1 Y 1 C HIS 39  ? C HIS 8   
41 1 Y 1 C HIS 40  ? C HIS 9   
42 1 Y 1 C HIS 41  ? C HIS 10  
43 1 Y 1 C GLY 42  ? C GLY 11  
44 1 Y 1 C SER 43  ? C SER 12  
45 1 Y 1 C GLN 44  ? C GLN 13  
46 1 Y 1 C GLU 45  ? C GLU 14  
47 1 Y 1 C HIS 510 ? C HIS 479 
48 1 Y 1 C LYS 511 ? C LYS 480 
49 1 Y 1 D MET 32  ? D MET 1   
50 1 Y 1 D GLY 33  ? D GLY 2   
51 1 Y 1 D SER 34  ? D SER 3   
52 1 Y 1 D SER 35  ? D SER 4   
53 1 Y 1 D HIS 36  ? D HIS 5   
54 1 Y 1 D HIS 37  ? D HIS 6   
55 1 Y 1 D HIS 38  ? D HIS 7   
56 1 Y 1 D HIS 39  ? D HIS 8   
57 1 Y 1 D HIS 40  ? D HIS 9   
58 1 Y 1 D HIS 41  ? D HIS 10  
59 1 Y 1 D GLY 42  ? D GLY 11  
60 1 Y 1 D SER 43  ? D SER 12  
61 1 Y 1 D GLN 44  ? D GLN 13  
62 1 Y 1 D GLU 45  ? D GLU 14  
63 1 Y 1 D HIS 510 ? D HIS 479 
64 1 Y 1 D LYS 511 ? D LYS 480 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BR  BR   BR N N 74  
CA  CA   CA N N 75  
CL  CL   CL N N 76  
CYS N    N  N N 77  
CYS CA   C  N R 78  
CYS C    C  N N 79  
CYS O    O  N N 80  
CYS CB   C  N N 81  
CYS SG   S  N N 82  
CYS OXT  O  N N 83  
CYS H    H  N N 84  
CYS H2   H  N N 85  
CYS HA   H  N N 86  
CYS HB2  H  N N 87  
CYS HB3  H  N N 88  
CYS HG   H  N N 89  
CYS HXT  H  N N 90  
DDZ N    N  N N 91  
DDZ CA   C  N S 92  
DDZ C    C  N N 93  
DDZ O    O  N N 94  
DDZ OG1  O  N N 95  
DDZ OG2  O  N N 96  
DDZ CB   C  N N 97  
DDZ OXT  O  N N 98  
DDZ H    H  N N 99  
DDZ H2   H  N N 100 
DDZ HA   H  N N 101 
DDZ HB   H  N N 102 
DDZ HXT  H  N N 103 
DDZ HG1  H  N N 104 
DDZ HG2  H  N N 105 
GLN N    N  N N 106 
GLN CA   C  N S 107 
GLN C    C  N N 108 
GLN O    O  N N 109 
GLN CB   C  N N 110 
GLN CG   C  N N 111 
GLN CD   C  N N 112 
GLN OE1  O  N N 113 
GLN NE2  N  N N 114 
GLN OXT  O  N N 115 
GLN H    H  N N 116 
GLN H2   H  N N 117 
GLN HA   H  N N 118 
GLN HB2  H  N N 119 
GLN HB3  H  N N 120 
GLN HG2  H  N N 121 
GLN HG3  H  N N 122 
GLN HE21 H  N N 123 
GLN HE22 H  N N 124 
GLN HXT  H  N N 125 
GLU N    N  N N 126 
GLU CA   C  N S 127 
GLU C    C  N N 128 
GLU O    O  N N 129 
GLU CB   C  N N 130 
GLU CG   C  N N 131 
GLU CD   C  N N 132 
GLU OE1  O  N N 133 
GLU OE2  O  N N 134 
GLU OXT  O  N N 135 
GLU H    H  N N 136 
GLU H2   H  N N 137 
GLU HA   H  N N 138 
GLU HB2  H  N N 139 
GLU HB3  H  N N 140 
GLU HG2  H  N N 141 
GLU HG3  H  N N 142 
GLU HE2  H  N N 143 
GLU HXT  H  N N 144 
GLY N    N  N N 145 
GLY CA   C  N N 146 
GLY C    C  N N 147 
GLY O    O  N N 148 
GLY OXT  O  N N 149 
GLY H    H  N N 150 
GLY H2   H  N N 151 
GLY HA2  H  N N 152 
GLY HA3  H  N N 153 
GLY HXT  H  N N 154 
HIS N    N  N N 155 
HIS CA   C  N S 156 
HIS C    C  N N 157 
HIS O    O  N N 158 
HIS CB   C  N N 159 
HIS CG   C  Y N 160 
HIS ND1  N  Y N 161 
HIS CD2  C  Y N 162 
HIS CE1  C  Y N 163 
HIS NE2  N  Y N 164 
HIS OXT  O  N N 165 
HIS H    H  N N 166 
HIS H2   H  N N 167 
HIS HA   H  N N 168 
HIS HB2  H  N N 169 
HIS HB3  H  N N 170 
HIS HD1  H  N N 171 
HIS HD2  H  N N 172 
HIS HE1  H  N N 173 
HIS HE2  H  N N 174 
HIS HXT  H  N N 175 
HOH O    O  N N 176 
HOH H1   H  N N 177 
HOH H2   H  N N 178 
ILE N    N  N N 179 
ILE CA   C  N S 180 
ILE C    C  N N 181 
ILE O    O  N N 182 
ILE CB   C  N S 183 
ILE CG1  C  N N 184 
ILE CG2  C  N N 185 
ILE CD1  C  N N 186 
ILE OXT  O  N N 187 
ILE H    H  N N 188 
ILE H2   H  N N 189 
ILE HA   H  N N 190 
ILE HB   H  N N 191 
ILE HG12 H  N N 192 
ILE HG13 H  N N 193 
ILE HG21 H  N N 194 
ILE HG22 H  N N 195 
ILE HG23 H  N N 196 
ILE HD11 H  N N 197 
ILE HD12 H  N N 198 
ILE HD13 H  N N 199 
ILE HXT  H  N N 200 
LEU N    N  N N 201 
LEU CA   C  N S 202 
LEU C    C  N N 203 
LEU O    O  N N 204 
LEU CB   C  N N 205 
LEU CG   C  N N 206 
LEU CD1  C  N N 207 
LEU CD2  C  N N 208 
LEU OXT  O  N N 209 
LEU H    H  N N 210 
LEU H2   H  N N 211 
LEU HA   H  N N 212 
LEU HB2  H  N N 213 
LEU HB3  H  N N 214 
LEU HG   H  N N 215 
LEU HD11 H  N N 216 
LEU HD12 H  N N 217 
LEU HD13 H  N N 218 
LEU HD21 H  N N 219 
LEU HD22 H  N N 220 
LEU HD23 H  N N 221 
LEU HXT  H  N N 222 
LYS N    N  N N 223 
LYS CA   C  N S 224 
LYS C    C  N N 225 
LYS O    O  N N 226 
LYS CB   C  N N 227 
LYS CG   C  N N 228 
LYS CD   C  N N 229 
LYS CE   C  N N 230 
LYS NZ   N  N N 231 
LYS OXT  O  N N 232 
LYS H    H  N N 233 
LYS H2   H  N N 234 
LYS HA   H  N N 235 
LYS HB2  H  N N 236 
LYS HB3  H  N N 237 
LYS HG2  H  N N 238 
LYS HG3  H  N N 239 
LYS HD2  H  N N 240 
LYS HD3  H  N N 241 
LYS HE2  H  N N 242 
LYS HE3  H  N N 243 
LYS HZ1  H  N N 244 
LYS HZ2  H  N N 245 
LYS HZ3  H  N N 246 
LYS HXT  H  N N 247 
MET N    N  N N 248 
MET CA   C  N S 249 
MET C    C  N N 250 
MET O    O  N N 251 
MET CB   C  N N 252 
MET CG   C  N N 253 
MET SD   S  N N 254 
MET CE   C  N N 255 
MET OXT  O  N N 256 
MET H    H  N N 257 
MET H2   H  N N 258 
MET HA   H  N N 259 
MET HB2  H  N N 260 
MET HB3  H  N N 261 
MET HG2  H  N N 262 
MET HG3  H  N N 263 
MET HE1  H  N N 264 
MET HE2  H  N N 265 
MET HE3  H  N N 266 
MET HXT  H  N N 267 
PHE N    N  N N 268 
PHE CA   C  N S 269 
PHE C    C  N N 270 
PHE O    O  N N 271 
PHE CB   C  N N 272 
PHE CG   C  Y N 273 
PHE CD1  C  Y N 274 
PHE CD2  C  Y N 275 
PHE CE1  C  Y N 276 
PHE CE2  C  Y N 277 
PHE CZ   C  Y N 278 
PHE OXT  O  N N 279 
PHE H    H  N N 280 
PHE H2   H  N N 281 
PHE HA   H  N N 282 
PHE HB2  H  N N 283 
PHE HB3  H  N N 284 
PHE HD1  H  N N 285 
PHE HD2  H  N N 286 
PHE HE1  H  N N 287 
PHE HE2  H  N N 288 
PHE HZ   H  N N 289 
PHE HXT  H  N N 290 
PRO N    N  N N 291 
PRO CA   C  N S 292 
PRO C    C  N N 293 
PRO O    O  N N 294 
PRO CB   C  N N 295 
PRO CG   C  N N 296 
PRO CD   C  N N 297 
PRO OXT  O  N N 298 
PRO H    H  N N 299 
PRO HA   H  N N 300 
PRO HB2  H  N N 301 
PRO HB3  H  N N 302 
PRO HG2  H  N N 303 
PRO HG3  H  N N 304 
PRO HD2  H  N N 305 
PRO HD3  H  N N 306 
PRO HXT  H  N N 307 
SER N    N  N N 308 
SER CA   C  N S 309 
SER C    C  N N 310 
SER O    O  N N 311 
SER CB   C  N N 312 
SER OG   O  N N 313 
SER OXT  O  N N 314 
SER H    H  N N 315 
SER H2   H  N N 316 
SER HA   H  N N 317 
SER HB2  H  N N 318 
SER HB3  H  N N 319 
SER HG   H  N N 320 
SER HXT  H  N N 321 
THR N    N  N N 322 
THR CA   C  N S 323 
THR C    C  N N 324 
THR O    O  N N 325 
THR CB   C  N R 326 
THR OG1  O  N N 327 
THR CG2  C  N N 328 
THR OXT  O  N N 329 
THR H    H  N N 330 
THR H2   H  N N 331 
THR HA   H  N N 332 
THR HB   H  N N 333 
THR HG1  H  N N 334 
THR HG21 H  N N 335 
THR HG22 H  N N 336 
THR HG23 H  N N 337 
THR HXT  H  N N 338 
TRP N    N  N N 339 
TRP CA   C  N S 340 
TRP C    C  N N 341 
TRP O    O  N N 342 
TRP CB   C  N N 343 
TRP CG   C  Y N 344 
TRP CD1  C  Y N 345 
TRP CD2  C  Y N 346 
TRP NE1  N  Y N 347 
TRP CE2  C  Y N 348 
TRP CE3  C  Y N 349 
TRP CZ2  C  Y N 350 
TRP CZ3  C  Y N 351 
TRP CH2  C  Y N 352 
TRP OXT  O  N N 353 
TRP H    H  N N 354 
TRP H2   H  N N 355 
TRP HA   H  N N 356 
TRP HB2  H  N N 357 
TRP HB3  H  N N 358 
TRP HD1  H  N N 359 
TRP HE1  H  N N 360 
TRP HE3  H  N N 361 
TRP HZ2  H  N N 362 
TRP HZ3  H  N N 363 
TRP HH2  H  N N 364 
TRP HXT  H  N N 365 
TYR N    N  N N 366 
TYR CA   C  N S 367 
TYR C    C  N N 368 
TYR O    O  N N 369 
TYR CB   C  N N 370 
TYR CG   C  Y N 371 
TYR CD1  C  Y N 372 
TYR CD2  C  Y N 373 
TYR CE1  C  Y N 374 
TYR CE2  C  Y N 375 
TYR CZ   C  Y N 376 
TYR OH   O  N N 377 
TYR OXT  O  N N 378 
TYR H    H  N N 379 
TYR H2   H  N N 380 
TYR HA   H  N N 381 
TYR HB2  H  N N 382 
TYR HB3  H  N N 383 
TYR HD1  H  N N 384 
TYR HD2  H  N N 385 
TYR HE1  H  N N 386 
TYR HE2  H  N N 387 
TYR HH   H  N N 388 
TYR HXT  H  N N 389 
VAL N    N  N N 390 
VAL CA   C  N S 391 
VAL C    C  N N 392 
VAL O    O  N N 393 
VAL CB   C  N N 394 
VAL CG1  C  N N 395 
VAL CG2  C  N N 396 
VAL OXT  O  N N 397 
VAL H    H  N N 398 
VAL H2   H  N N 399 
VAL HA   H  N N 400 
VAL HB   H  N N 401 
VAL HG11 H  N N 402 
VAL HG12 H  N N 403 
VAL HG13 H  N N 404 
VAL HG21 H  N N 405 
VAL HG22 H  N N 406 
VAL HG23 H  N N 407 
VAL HXT  H  N N 408 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DDZ N   CA   sing N N 83  
DDZ CA  C    sing N N 84  
DDZ CA  CB   sing N N 85  
DDZ C   O    doub N N 86  
DDZ C   OXT  sing N N 87  
DDZ OG1 CB   sing N N 88  
DDZ OG2 CB   sing N N 89  
DDZ N   H    sing N N 90  
DDZ N   H2   sing N N 91  
DDZ CA  HA   sing N N 92  
DDZ CB  HB   sing N N 93  
DDZ OXT HXT  sing N N 94  
DDZ OG1 HG1  sing N N 95  
DDZ OG2 HG2  sing N N 96  
GLN N   CA   sing N N 97  
GLN N   H    sing N N 98  
GLN N   H2   sing N N 99  
GLN CA  C    sing N N 100 
GLN CA  CB   sing N N 101 
GLN CA  HA   sing N N 102 
GLN C   O    doub N N 103 
GLN C   OXT  sing N N 104 
GLN CB  CG   sing N N 105 
GLN CB  HB2  sing N N 106 
GLN CB  HB3  sing N N 107 
GLN CG  CD   sing N N 108 
GLN CG  HG2  sing N N 109 
GLN CG  HG3  sing N N 110 
GLN CD  OE1  doub N N 111 
GLN CD  NE2  sing N N 112 
GLN NE2 HE21 sing N N 113 
GLN NE2 HE22 sing N N 114 
GLN OXT HXT  sing N N 115 
GLU N   CA   sing N N 116 
GLU N   H    sing N N 117 
GLU N   H2   sing N N 118 
GLU CA  C    sing N N 119 
GLU CA  CB   sing N N 120 
GLU CA  HA   sing N N 121 
GLU C   O    doub N N 122 
GLU C   OXT  sing N N 123 
GLU CB  CG   sing N N 124 
GLU CB  HB2  sing N N 125 
GLU CB  HB3  sing N N 126 
GLU CG  CD   sing N N 127 
GLU CG  HG2  sing N N 128 
GLU CG  HG3  sing N N 129 
GLU CD  OE1  doub N N 130 
GLU CD  OE2  sing N N 131 
GLU OE2 HE2  sing N N 132 
GLU OXT HXT  sing N N 133 
GLY N   CA   sing N N 134 
GLY N   H    sing N N 135 
GLY N   H2   sing N N 136 
GLY CA  C    sing N N 137 
GLY CA  HA2  sing N N 138 
GLY CA  HA3  sing N N 139 
GLY C   O    doub N N 140 
GLY C   OXT  sing N N 141 
GLY OXT HXT  sing N N 142 
HIS N   CA   sing N N 143 
HIS N   H    sing N N 144 
HIS N   H2   sing N N 145 
HIS CA  C    sing N N 146 
HIS CA  CB   sing N N 147 
HIS CA  HA   sing N N 148 
HIS C   O    doub N N 149 
HIS C   OXT  sing N N 150 
HIS CB  CG   sing N N 151 
HIS CB  HB2  sing N N 152 
HIS CB  HB3  sing N N 153 
HIS CG  ND1  sing Y N 154 
HIS CG  CD2  doub Y N 155 
HIS ND1 CE1  doub Y N 156 
HIS ND1 HD1  sing N N 157 
HIS CD2 NE2  sing Y N 158 
HIS CD2 HD2  sing N N 159 
HIS CE1 NE2  sing Y N 160 
HIS CE1 HE1  sing N N 161 
HIS NE2 HE2  sing N N 162 
HIS OXT HXT  sing N N 163 
HOH O   H1   sing N N 164 
HOH O   H2   sing N N 165 
ILE N   CA   sing N N 166 
ILE N   H    sing N N 167 
ILE N   H2   sing N N 168 
ILE CA  C    sing N N 169 
ILE CA  CB   sing N N 170 
ILE CA  HA   sing N N 171 
ILE C   O    doub N N 172 
ILE C   OXT  sing N N 173 
ILE CB  CG1  sing N N 174 
ILE CB  CG2  sing N N 175 
ILE CB  HB   sing N N 176 
ILE CG1 CD1  sing N N 177 
ILE CG1 HG12 sing N N 178 
ILE CG1 HG13 sing N N 179 
ILE CG2 HG21 sing N N 180 
ILE CG2 HG22 sing N N 181 
ILE CG2 HG23 sing N N 182 
ILE CD1 HD11 sing N N 183 
ILE CD1 HD12 sing N N 184 
ILE CD1 HD13 sing N N 185 
ILE OXT HXT  sing N N 186 
LEU N   CA   sing N N 187 
LEU N   H    sing N N 188 
LEU N   H2   sing N N 189 
LEU CA  C    sing N N 190 
LEU CA  CB   sing N N 191 
LEU CA  HA   sing N N 192 
LEU C   O    doub N N 193 
LEU C   OXT  sing N N 194 
LEU CB  CG   sing N N 195 
LEU CB  HB2  sing N N 196 
LEU CB  HB3  sing N N 197 
LEU CG  CD1  sing N N 198 
LEU CG  CD2  sing N N 199 
LEU CG  HG   sing N N 200 
LEU CD1 HD11 sing N N 201 
LEU CD1 HD12 sing N N 202 
LEU CD1 HD13 sing N N 203 
LEU CD2 HD21 sing N N 204 
LEU CD2 HD22 sing N N 205 
LEU CD2 HD23 sing N N 206 
LEU OXT HXT  sing N N 207 
LYS N   CA   sing N N 208 
LYS N   H    sing N N 209 
LYS N   H2   sing N N 210 
LYS CA  C    sing N N 211 
LYS CA  CB   sing N N 212 
LYS CA  HA   sing N N 213 
LYS C   O    doub N N 214 
LYS C   OXT  sing N N 215 
LYS CB  CG   sing N N 216 
LYS CB  HB2  sing N N 217 
LYS CB  HB3  sing N N 218 
LYS CG  CD   sing N N 219 
LYS CG  HG2  sing N N 220 
LYS CG  HG3  sing N N 221 
LYS CD  CE   sing N N 222 
LYS CD  HD2  sing N N 223 
LYS CD  HD3  sing N N 224 
LYS CE  NZ   sing N N 225 
LYS CE  HE2  sing N N 226 
LYS CE  HE3  sing N N 227 
LYS NZ  HZ1  sing N N 228 
LYS NZ  HZ2  sing N N 229 
LYS NZ  HZ3  sing N N 230 
LYS OXT HXT  sing N N 231 
MET N   CA   sing N N 232 
MET N   H    sing N N 233 
MET N   H2   sing N N 234 
MET CA  C    sing N N 235 
MET CA  CB   sing N N 236 
MET CA  HA   sing N N 237 
MET C   O    doub N N 238 
MET C   OXT  sing N N 239 
MET CB  CG   sing N N 240 
MET CB  HB2  sing N N 241 
MET CB  HB3  sing N N 242 
MET CG  SD   sing N N 243 
MET CG  HG2  sing N N 244 
MET CG  HG3  sing N N 245 
MET SD  CE   sing N N 246 
MET CE  HE1  sing N N 247 
MET CE  HE2  sing N N 248 
MET CE  HE3  sing N N 249 
MET OXT HXT  sing N N 250 
PHE N   CA   sing N N 251 
PHE N   H    sing N N 252 
PHE N   H2   sing N N 253 
PHE CA  C    sing N N 254 
PHE CA  CB   sing N N 255 
PHE CA  HA   sing N N 256 
PHE C   O    doub N N 257 
PHE C   OXT  sing N N 258 
PHE CB  CG   sing N N 259 
PHE CB  HB2  sing N N 260 
PHE CB  HB3  sing N N 261 
PHE CG  CD1  doub Y N 262 
PHE CG  CD2  sing Y N 263 
PHE CD1 CE1  sing Y N 264 
PHE CD1 HD1  sing N N 265 
PHE CD2 CE2  doub Y N 266 
PHE CD2 HD2  sing N N 267 
PHE CE1 CZ   doub Y N 268 
PHE CE1 HE1  sing N N 269 
PHE CE2 CZ   sing Y N 270 
PHE CE2 HE2  sing N N 271 
PHE CZ  HZ   sing N N 272 
PHE OXT HXT  sing N N 273 
PRO N   CA   sing N N 274 
PRO N   CD   sing N N 275 
PRO N   H    sing N N 276 
PRO CA  C    sing N N 277 
PRO CA  CB   sing N N 278 
PRO CA  HA   sing N N 279 
PRO C   O    doub N N 280 
PRO C   OXT  sing N N 281 
PRO CB  CG   sing N N 282 
PRO CB  HB2  sing N N 283 
PRO CB  HB3  sing N N 284 
PRO CG  CD   sing N N 285 
PRO CG  HG2  sing N N 286 
PRO CG  HG3  sing N N 287 
PRO CD  HD2  sing N N 288 
PRO CD  HD3  sing N N 289 
PRO OXT HXT  sing N N 290 
SER N   CA   sing N N 291 
SER N   H    sing N N 292 
SER N   H2   sing N N 293 
SER CA  C    sing N N 294 
SER CA  CB   sing N N 295 
SER CA  HA   sing N N 296 
SER C   O    doub N N 297 
SER C   OXT  sing N N 298 
SER CB  OG   sing N N 299 
SER CB  HB2  sing N N 300 
SER CB  HB3  sing N N 301 
SER OG  HG   sing N N 302 
SER OXT HXT  sing N N 303 
THR N   CA   sing N N 304 
THR N   H    sing N N 305 
THR N   H2   sing N N 306 
THR CA  C    sing N N 307 
THR CA  CB   sing N N 308 
THR CA  HA   sing N N 309 
THR C   O    doub N N 310 
THR C   OXT  sing N N 311 
THR CB  OG1  sing N N 312 
THR CB  CG2  sing N N 313 
THR CB  HB   sing N N 314 
THR OG1 HG1  sing N N 315 
THR CG2 HG21 sing N N 316 
THR CG2 HG22 sing N N 317 
THR CG2 HG23 sing N N 318 
THR OXT HXT  sing N N 319 
TRP N   CA   sing N N 320 
TRP N   H    sing N N 321 
TRP N   H2   sing N N 322 
TRP CA  C    sing N N 323 
TRP CA  CB   sing N N 324 
TRP CA  HA   sing N N 325 
TRP C   O    doub N N 326 
TRP C   OXT  sing N N 327 
TRP CB  CG   sing N N 328 
TRP CB  HB2  sing N N 329 
TRP CB  HB3  sing N N 330 
TRP CG  CD1  doub Y N 331 
TRP CG  CD2  sing Y N 332 
TRP CD1 NE1  sing Y N 333 
TRP CD1 HD1  sing N N 334 
TRP CD2 CE2  doub Y N 335 
TRP CD2 CE3  sing Y N 336 
TRP NE1 CE2  sing Y N 337 
TRP NE1 HE1  sing N N 338 
TRP CE2 CZ2  sing Y N 339 
TRP CE3 CZ3  doub Y N 340 
TRP CE3 HE3  sing N N 341 
TRP CZ2 CH2  doub Y N 342 
TRP CZ2 HZ2  sing N N 343 
TRP CZ3 CH2  sing Y N 344 
TRP CZ3 HZ3  sing N N 345 
TRP CH2 HH2  sing N N 346 
TRP OXT HXT  sing N N 347 
TYR N   CA   sing N N 348 
TYR N   H    sing N N 349 
TYR N   H2   sing N N 350 
TYR CA  C    sing N N 351 
TYR CA  CB   sing N N 352 
TYR CA  HA   sing N N 353 
TYR C   O    doub N N 354 
TYR C   OXT  sing N N 355 
TYR CB  CG   sing N N 356 
TYR CB  HB2  sing N N 357 
TYR CB  HB3  sing N N 358 
TYR CG  CD1  doub Y N 359 
TYR CG  CD2  sing Y N 360 
TYR CD1 CE1  sing Y N 361 
TYR CD1 HD1  sing N N 362 
TYR CD2 CE2  doub Y N 363 
TYR CD2 HD2  sing N N 364 
TYR CE1 CZ   doub Y N 365 
TYR CE1 HE1  sing N N 366 
TYR CE2 CZ   sing Y N 367 
TYR CE2 HE2  sing N N 368 
TYR CZ  OH   sing N N 369 
TYR OH  HH   sing N N 370 
TYR OXT HXT  sing N N 371 
VAL N   CA   sing N N 372 
VAL N   H    sing N N 373 
VAL N   H2   sing N N 374 
VAL CA  C    sing N N 375 
VAL CA  CB   sing N N 376 
VAL CA  HA   sing N N 377 
VAL C   O    doub N N 378 
VAL C   OXT  sing N N 379 
VAL CB  CG1  sing N N 380 
VAL CB  CG2  sing N N 381 
VAL CB  HB   sing N N 382 
VAL CG1 HG11 sing N N 383 
VAL CG1 HG12 sing N N 384 
VAL CG1 HG13 sing N N 385 
VAL CG2 HG21 sing N N 386 
VAL CG2 HG22 sing N N 387 
VAL CG2 HG23 sing N N 388 
VAL OXT HXT  sing N N 389 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           'ANR- 22-CE11-0025-01' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9HH3 
_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]   0.013550 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002226 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005021 
_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]   0.013449 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
BR ? ? 25.79822 9.11301 ? ? 1.35700  25.34896 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CA ? ? 16.26893 3.65395 ? ? 3.58509  77.28589 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . THR A  1 15  ? -54.20200 -47.01600 -32.65600 1.000 67.68000  ? 46  THR A N   1 
ATOM   2     C  CA  . THR A  1 15  ? -54.10600 -47.35500 -31.24000 1.000 59.78000  ? 46  THR A CA  1 
ATOM   3     C  C   . THR A  1 15  ? -52.60000 -47.44000 -30.87000 1.000 60.81000  ? 46  THR A C   1 
ATOM   4     O  O   . THR A  1 15  ? -52.18500 -46.94600 -29.80000 1.000 54.21000  ? 46  THR A O   1 
ATOM   5     C  CB  . THR A  1 15  ? -54.89000 -48.69100 -30.90800 1.000 60.35000  ? 46  THR A CB  1 
ATOM   6     O  OG1 . THR A  1 15  ? -54.94900 -48.91700 -29.49000 1.000 62.93000  ? 46  THR A OG1 1 
ATOM   7     C  CG2 . THR A  1 15  ? -54.26000 -49.91500 -31.58400 1.000 56.41000  ? 46  THR A CG2 1 
ATOM   8     N  N   . ARG A  1 16  ? -51.78600 -48.03400 -31.75300 1.000 54.25000  ? 47  ARG A N   1 
ATOM   9     C  CA  . ARG A  1 16  ? -50.39300 -48.26400 -31.40400 1.000 48.99000  ? 47  ARG A CA  1 
ATOM   10    C  C   . ARG A  1 16  ? -49.69400 -46.92200 -31.19200 1.000 50.09000  ? 47  ARG A C   1 
ATOM   11    O  O   . ARG A  1 16  ? -50.04400 -45.92700 -31.83600 1.000 52.89000  ? 47  ARG A O   1 
ATOM   12    C  CB  . ARG A  1 16  ? -49.67000 -49.08800 -32.47000 1.000 45.57000  ? 47  ARG A CB  1 
ATOM   13    C  CG  . ARG A  1 16  ? -50.11900 -50.55000 -32.50300 1.000 53.05000  ? 47  ARG A CG  1 
ATOM   14    C  CD  . ARG A  1 16  ? -49.48500 -51.32900 -33.66200 1.000 49.47000  ? 47  ARG A CD  1 
ATOM   15    N  NE  . ARG A  1 16  ? -49.54800 -50.62800 -34.93500 1.000 42.97000  ? 47  ARG A NE  1 
ATOM   16    C  CZ  . ARG A  1 16  ? -48.90200 -51.02000 -36.02800 1.000 54.85000  ? 47  ARG A CZ  1 
ATOM   17    N  NH1 . ARG A  1 16  ? -48.07900 -52.05900 -36.01800 1.000 43.93000  ? 47  ARG A NH1 1 
ATOM   18    N  NH2 . ARG A  1 16  ? -49.07100 -50.34200 -37.16000 1.000 51.02000  ? 47  ARG A NH2 1 
ATOM   19    N  N   . PRO A  1 17  ? -48.76000 -46.83800 -30.25400 1.000 50.53000  ? 48  PRO A N   1 
ATOM   20    C  CA  . PRO A  1 17  ? -48.09900 -45.56200 -29.97500 1.000 46.40000  ? 48  PRO A CA  1 
ATOM   21    C  C   . PRO A  1 17  ? -46.96500 -45.28000 -30.94800 1.000 42.94000  ? 48  PRO A C   1 
ATOM   22    O  O   . PRO A  1 17  ? -46.43100 -46.17900 -31.61000 1.000 37.74000  ? 48  PRO A O   1 
ATOM   23    C  CB  . PRO A  1 17  ? -47.55700 -45.76700 -28.56500 1.000 41.42000  ? 48  PRO A CB  1 
ATOM   24    C  CG  . PRO A  1 17  ? -47.24300 -47.20400 -28.53200 1.000 47.57000  ? 48  PRO A CG  1 
ATOM   25    C  CD  . PRO A  1 17  ? -48.28200 -47.90700 -29.36500 1.000 47.59000  ? 48  PRO A CD  1 
ATOM   26    N  N   . ASN A  1 18  ? -46.66200 -43.98900 -31.07500 1.000 39.93000  ? 49  ASN A N   1 
ATOM   27    C  CA  . ASN A  1 18  ? -45.39700 -43.57400 -31.65600 1.000 46.09000  ? 49  ASN A CA  1 
ATOM   28    C  C   . ASN A  1 18  ? -44.25900 -43.83000 -30.66000 1.000 44.67000  ? 49  ASN A C   1 
ATOM   29    O  O   . ASN A  1 18  ? -44.45900 -43.87400 -29.44400 1.000 44.84000  ? 49  ASN A O   1 
ATOM   30    C  CB  . ASN A  1 18  ? -45.41600 -42.09400 -32.04200 1.000 46.13000  ? 49  ASN A CB  1 
ATOM   31    C  CG  . ASN A  1 18  ? -46.64400 -41.69200 -32.86200 1.000 49.93000  ? 49  ASN A CG  1 
ATOM   32    O  OD1 . ASN A  1 18  ? -46.84300 -42.15800 -33.98700 1.000 50.73000  ? 49  ASN A OD1 1 
ATOM   33    N  ND2 . ASN A  1 18  ? -47.41000 -40.74300 -32.34100 1.000 46.16000  ? 49  ASN A ND2 1 
ATOM   34    N  N   . ILE A  1 19  ? -43.04800 -43.98200 -31.18400 1.000 42.62000  ? 50  ILE A N   1 
ATOM   35    C  CA  . ILE A  1 19  ? -41.87500 -44.23000 -30.35400 1.000 43.70000  ? 50  ILE A CA  1 
ATOM   36    C  C   . ILE A  1 19  ? -40.75000 -43.27900 -30.73700 1.000 47.30000  ? 50  ILE A C   1 
ATOM   37    O  O   . ILE A  1 19  ? -40.23500 -43.34800 -31.85800 1.000 44.59000  ? 50  ILE A O   1 
ATOM   38    C  CB  . ILE A  1 19  ? -41.41000 -45.68500 -30.47700 1.000 44.05000  ? 50  ILE A CB  1 
ATOM   39    C  CG1 . ILE A  1 19  ? -42.51100 -46.60200 -29.94700 1.000 35.87000  ? 50  ILE A CG1 1 
ATOM   40    C  CG2 . ILE A  1 19  ? -40.08100 -45.88400 -29.77200 1.000 42.08000  ? 50  ILE A CG2 1 
ATOM   41    C  CD1 . ILE A  1 19  ? -42.33200 -48.03700 -30.28800 1.000 45.26000  ? 50  ILE A CD1 1 
ATOM   42    N  N   . LEU A  1 20  ? -40.32900 -42.43600 -29.78800 1.000 38.77000  ? 51  LEU A N   1 
ATOM   43    C  CA  . LEU A  1 20  ? -39.21900 -41.50200 -29.96900 1.000 41.82000  ? 51  LEU A CA  1 
ATOM   44    C  C   . LEU A  1 20  ? -38.09400 -41.85400 -28.99600 1.000 39.79000  ? 51  LEU A C   1 
ATOM   45    O  O   . LEU A  1 20  ? -38.27200 -41.77200 -27.77400 1.000 35.83000  ? 51  LEU A O   1 
ATOM   46    C  CB  . LEU A  1 20  ? -39.67200 -40.06600 -29.75500 1.000 37.70000  ? 51  LEU A CB  1 
ATOM   47    C  CG  . LEU A  1 20  ? -38.52100 -39.05900 -29.67700 1.000 43.21000  ? 51  LEU A CG  1 
ATOM   48    C  CD1 . LEU A  1 20  ? -37.69800 -39.01700 -30.98900 1.000 30.05000  ? 51  LEU A CD1 1 
ATOM   49    C  CD2 . LEU A  1 20  ? -39.05600 -37.66900 -29.28100 1.000 36.46000  ? 51  LEU A CD2 1 
ATOM   50    N  N   . VAL A  1 21  ? -36.95200 -42.28100 -29.53200 1.000 39.56000  ? 52  VAL A N   1 
ATOM   51    C  CA  . VAL A  1 21  ? -35.76900 -42.55500 -28.72700 1.000 41.27000  ? 52  VAL A CA  1 
ATOM   52    C  C   . VAL A  1 21  ? -34.83400 -41.36700 -28.84300 1.000 43.73000  ? 52  VAL A C   1 
ATOM   53    O  O   . VAL A  1 21  ? -34.33300 -41.07100 -29.93300 1.000 40.79000  ? 52  VAL A O   1 
ATOM   54    C  CB  . VAL A  1 21  ? -35.05200 -43.83500 -29.16600 1.000 43.07000  ? 52  VAL A CB  1 
ATOM   55    C  CG1 . VAL A  1 21  ? -33.83500 -44.07700 -28.23400 1.000 42.00000  ? 52  VAL A CG1 1 
ATOM   56    C  CG2 . VAL A  1 21  ? -35.99900 -44.99500 -29.12600 1.000 40.03000  ? 52  VAL A CG2 1 
ATOM   57    N  N   . VAL A  1 22  ? -34.62900 -40.66300 -27.73700 1.000 40.99000  ? 53  VAL A N   1 
ATOM   58    C  CA  . VAL A  1 22  ? -33.65800 -39.58300 -27.66800 1.000 32.17000  ? 53  VAL A CA  1 
ATOM   59    C  C   . VAL A  1 22  ? -32.41600 -40.13800 -26.97100 1.000 42.37000  ? 53  VAL A C   1 
ATOM   60    O  O   . VAL A  1 22  ? -32.42000 -40.39000 -25.76100 1.000 37.28000  ? 53  VAL A O   1 
ATOM   61    C  CB  . VAL A  1 22  ? -34.23700 -38.36600 -26.94700 1.000 39.43000  ? 53  VAL A CB  1 
ATOM   62    C  CG1 . VAL A  1 22  ? -33.25100 -37.21700 -26.95700 1.000 32.91000  ? 53  VAL A CG1 1 
ATOM   63    C  CG2 . VAL A  1 22  ? -35.61900 -37.98400 -27.57400 1.000 32.04000  ? 53  VAL A CG2 1 
ATOM   64    N  N   . LEU A  1 23  ? -31.36600 -40.35900 -27.75000 1.000 39.28000  ? 54  LEU A N   1 
ATOM   65    C  CA  . LEU A  1 23  ? -30.13300 -40.97300 -27.29700 1.000 36.57000  ? 54  LEU A CA  1 
ATOM   66    C  C   . LEU A  1 23  ? -29.05900 -39.89700 -27.34000 1.000 42.27000  ? 54  LEU A C   1 
ATOM   67    O  O   . LEU A  1 23  ? -28.74200 -39.36600 -28.41600 1.000 37.46000  ? 54  LEU A O   1 
ATOM   68    C  CB  . LEU A  1 23  ? -29.74100 -42.14900 -28.17600 1.000 31.13000  ? 54  LEU A CB  1 
ATOM   69    C  CG  . LEU A  1 23  ? -28.51400 -42.94600 -27.73400 1.000 40.16000  ? 54  LEU A CG  1 
ATOM   70    C  CD1 . LEU A  1 23  ? -28.75700 -43.68300 -26.37300 1.000 32.92000  ? 54  LEU A CD1 1 
ATOM   71    C  CD2 . LEU A  1 23  ? -28.06800 -43.93100 -28.84100 1.000 32.42000  ? 54  LEU A CD2 1 
ATOM   72    N  N   . CYS A  1 24  ? -28.56600 -39.52400 -26.17000 1.000 34.62000  ? 55  CYS A N   1 
ATOM   73    C  CA  . CYS A  1 24  ? -27.41600 -38.65300 -26.09200 1.000 34.67000  ? 55  CYS A CA  1 
ATOM   74    C  C   . CYS A  1 24  ? -26.15300 -39.49900 -26.08200 1.000 36.89000  ? 55  CYS A C   1 
ATOM   75    O  O   . CYS A  1 24  ? -26.18700 -40.72700 -25.91300 1.000 33.03000  ? 55  CYS A O   1 
ATOM   76    C  CB  . CYS A  1 24  ? -27.49100 -37.75800 -24.86300 1.000 38.94000  ? 55  CYS A CB  1 
ATOM   77    S  SG  . CYS A  1 24  ? -28.51900 -36.32900 -25.15500 1.000 46.99000  ? 55  CYS A SG  1 
ATOM   78    N  N   . ASP A  1 25  ? -25.02600 -38.82700 -26.27400 1.000 38.36000  ? 56  ASP A N   1 
ATOM   79    C  CA  . ASP A  1 25  ? -23.73200 -39.48200 -26.45300 1.000 39.58000  ? 56  ASP A CA  1 
ATOM   80    C  C   . ASP A  1 25  ? -22.77800 -39.01400 -25.35500 1.000 36.84000  ? 56  ASP A C   1 
ATOM   81    O  O   . ASP A  1 25  ? -22.40000 -37.84100 -25.32600 1.000 40.62000  ? 56  ASP A O   1 
ATOM   82    C  CB  . ASP A  1 25  ? -23.20400 -39.15400 -27.84300 1.000 38.44000  ? 56  ASP A CB  1 
ATOM   83    C  CG  . ASP A  1 25  ? -22.01500 -39.99400 -28.24100 1.000 45.17000  ? 56  ASP A CG  1 
ATOM   84    O  OD1 . ASP A  1 25  ? -21.52300 -40.82200 -27.42400 1.000 38.05000  ? 56  ASP A OD1 1 
ATOM   85    O  OD2 . ASP A  1 25  ? -21.55400 -39.79400 -29.39300 1.000 42.06000  ? 56  ASP A OD2 1 
ATOM   86    N  N   . ASP A  1 26  ? -22.40200 -39.91500 -24.44500 1.000 34.03000  ? 57  ASP A N   1 
ATOM   87    C  CA  . ASP A  1 26  ? -21.46600 -39.59900 -23.35600 1.000 37.83000  ? 57  ASP A CA  1 
ATOM   88    C  C   . ASP A  1 26  ? -22.05100 -38.62500 -22.31600 1.000 36.69000  ? 57  ASP A C   1 
ATOM   89    O  O   . ASP A  1 26  ? -21.31400 -37.84400 -21.69800 1.000 33.74000  ? 57  ASP A O   1 
ATOM   90    C  CB  . ASP A  1 26  ? -20.15600 -39.01200 -23.90900 1.000 36.50000  ? 57  ASP A CB  1 
ATOM   91    C  CG  . ASP A  1 26  ? -19.35100 -40.00900 -24.71000 1.000 44.29000  ? 57  ASP A CG  1 
ATOM   92    O  OD1 . ASP A  1 26  ? -19.78200 -41.18100 -24.85400 1.000 38.99000  ? 57  ASP A OD1 1 
ATOM   93    O  OD2 . ASP A  1 26  ? -18.26800 -39.60300 -25.19700 1.000 45.75000  ? 57  ASP A OD2 1 
ATOM   94    N  N   . LEU A  1 27  ? -23.35700 -38.64600 -22.08700 1.000 32.52000  ? 58  LEU A N   1 
ATOM   95    C  CA  . LEU A  1 27  ? -23.94500 -37.77100 -21.07400 1.000 40.81000  ? 58  LEU A CA  1 
ATOM   96    C  C   . LEU A  1 27  ? -23.66300 -38.31500 -19.66800 1.000 35.13000  ? 58  LEU A C   1 
ATOM   97    O  O   . LEU A  1 27  ? -23.92300 -39.49000 -19.39800 1.000 38.92000  ? 58  LEU A O   1 
ATOM   98    C  CB  . LEU A  1 27  ? -25.45500 -37.63800 -21.32500 1.000 34.80000  ? 58  LEU A CB  1 
ATOM   99    C  CG  . LEU A  1 27  ? -26.26200 -36.81900 -20.31800 1.000 35.43000  ? 58  LEU A CG  1 
ATOM   100   C  CD1 . LEU A  1 27  ? -26.10500 -35.31500 -20.52600 1.000 37.87000  ? 58  LEU A CD1 1 
ATOM   101   C  CD2 . LEU A  1 27  ? -27.71100 -37.21000 -20.37500 1.000 38.46000  ? 58  LEU A CD2 1 
ATOM   102   N  N   . GLY A  1 28  ? -23.09200 -37.47600 -18.79200 1.000 31.87000  ? 59  GLY A N   1 
ATOM   103   C  CA  . GLY A  1 28  ? -22.78900 -37.90800 -17.43400 1.000 29.00000  ? 59  GLY A CA  1 
ATOM   104   C  C   . GLY A  1 28  ? -24.02300 -38.08500 -16.55500 1.000 36.60000  ? 59  GLY A C   1 
ATOM   105   O  O   . GLY A  1 28  ? -25.05900 -37.45000 -16.73300 1.000 32.66000  ? 59  GLY A O   1 
ATOM   106   N  N   . TYR A  1 29  ? -23.88000 -38.94500 -15.54400 1.000 37.63000  ? 60  TYR A N   1 
ATOM   107   C  CA  . TYR A  1 29  ? -25.01200 -39.36800 -14.71900 1.000 37.34000  ? 60  TYR A CA  1 
ATOM   108   C  C   . TYR A  1 29  ? -25.67400 -38.20900 -13.98000 1.000 34.62000  ? 60  TYR A C   1 
ATOM   109   O  O   . TYR A  1 29  ? -26.86900 -38.25500 -13.69100 1.000 42.59000  ? 60  TYR A O   1 
ATOM   110   C  CB  . TYR A  1 29  ? -24.55000 -40.41700 -13.71300 1.000 37.11000  ? 60  TYR A CB  1 
ATOM   111   C  CG  . TYR A  1 29  ? -25.66800 -41.29100 -13.17400 1.000 40.28000  ? 60  TYR A CG  1 
ATOM   112   C  CD1 . TYR A  1 29  ? -26.44000 -42.07700 -14.03400 1.000 38.24000  ? 60  TYR A CD1 1 
ATOM   113   C  CD2 . TYR A  1 29  ? -25.92900 -41.35200 -11.80600 1.000 37.66000  ? 60  TYR A CD2 1 
ATOM   114   C  CE1 . TYR A  1 29  ? -27.44700 -42.90300 -13.54500 1.000 38.59000  ? 60  TYR A CE1 1 
ATOM   115   C  CE2 . TYR A  1 29  ? -26.91700 -42.17000 -11.30300 1.000 34.49000  ? 60  TYR A CE2 1 
ATOM   116   C  CZ  . TYR A  1 29  ? -27.68300 -42.93400 -12.17700 1.000 40.40000  ? 60  TYR A CZ  1 
ATOM   117   O  OH  . TYR A  1 29  ? -28.66800 -43.74800 -11.69800 1.000 41.21000  ? 60  TYR A OH  1 
ATOM   118   N  N   . ALA A  1 30  ? -24.92000 -37.18500 -13.65200 1.000 35.33000  ? 61  ALA A N   1 
ATOM   119   C  CA  . ALA A  1 30  ? -25.41600 -36.04000 -12.91300 1.000 41.48000  ? 61  ALA A CA  1 
ATOM   120   C  C   . ALA A  1 30  ? -25.56500 -34.82100 -13.81100 1.000 41.86000  ? 61  ALA A C   1 
ATOM   121   O  O   . ALA A  1 30  ? -25.47100 -33.69000 -13.34300 1.000 50.01000  ? 61  ALA A O   1 
ATOM   122   C  CB  . ALA A  1 30  ? -24.46900 -35.71900 -11.75500 1.000 35.41000  ? 61  ALA A CB  1 
ATOM   123   N  N   . ASP A  1 31  ? -25.75500 -35.02400 -15.10600 1.000 39.36000  ? 62  ASP A N   1 
ATOM   124   C  CA  . ASP A  1 31  ? -25.67900 -33.91400 -16.04700 1.000 38.56000  ? 62  ASP A CA  1 
ATOM   125   C  C   . ASP A  1 31  ? -27.03600 -33.56800 -16.64700 1.000 38.51000  ? 62  ASP A C   1 
ATOM   126   O  O   . ASP A  1 31  ? -27.10800 -32.82700 -17.64100 1.000 41.54000  ? 62  ASP A O   1 
ATOM   127   C  CB  . ASP A  1 31  ? -24.63300 -34.23000 -17.13000 1.000 33.09000  ? 62  ASP A CB  1 
ATOM   128   C  CG  . ASP A  1 31  ? -23.17600 -34.26400 -16.56500 1.000 41.43000  ? 62  ASP A CG  1 
ATOM   129   O  OD1 . ASP A  1 31  ? -22.93200 -33.68900 -15.48400 1.000 38.61000  ? 62  ASP A OD1 1 
ATOM   130   O  OD2 . ASP A  1 31  ? -22.26400 -34.82400 -17.21600 1.000 39.64000  ? 62  ASP A OD2 1 
ATOM   131   N  N   . VAL A  1 32  ? -28.11300 -34.07100 -16.06300 1.000 37.63000  ? 63  VAL A N   1 
ATOM   132   C  CA  . VAL A  1 32  ? -29.45800 -33.57300 -16.32900 1.000 35.85000  ? 63  VAL A CA  1 
ATOM   133   C  C   . VAL A  1 32  ? -30.14800 -33.24700 -15.00500 1.000 43.55000  ? 63  VAL A C   1 
ATOM   134   O  O   . VAL A  1 32  ? -29.89700 -33.88800 -13.97700 1.000 41.15000  ? 63  VAL A O   1 
ATOM   135   C  CB  . VAL A  1 32  ? -30.29200 -34.57800 -17.15100 1.000 35.46000  ? 63  VAL A CB  1 
ATOM   136   C  CG1 . VAL A  1 32  ? -29.85300 -34.55700 -18.62100 1.000 40.35000  ? 63  VAL A CG1 1 
ATOM   137   C  CG2 . VAL A  1 32  ? -30.16400 -35.98200 -16.59000 1.000 32.70000  ? 63  VAL A CG2 1 
ATOM   138   N  N   . GLY A  1 33  ? -31.03900 -32.24900 -15.04100 1.000 42.86000  ? 64  GLY A N   1 
ATOM   139   C  CA  . GLY A  1 33  ? -31.73000 -31.83600 -13.82600 1.000 39.36000  ? 64  GLY A CA  1 
ATOM   140   C  C   . GLY A  1 33  ? -32.41300 -32.98600 -13.11100 1.000 42.91000  ? 64  GLY A C   1 
ATOM   141   O  O   . GLY A  1 33  ? -32.23400 -33.18100 -11.90500 1.000 40.01000  ? 64  GLY A O   1 
ATOM   142   N  N   . PHE A  1 34  ? -33.18500 -33.78800 -13.85000 1.000 42.82000  ? 65  PHE A N   1 
ATOM   143   C  CA  . PHE A  1 34  ? -33.95300 -34.85000 -13.21100 1.000 41.97000  ? 65  PHE A CA  1 
ATOM   144   C  C   . PHE A  1 34  ? -33.07900 -35.93200 -12.59800 1.000 46.23000  ? 65  PHE A C   1 
ATOM   145   O  O   . PHE A  1 34  ? -33.58700 -36.78300 -11.85300 1.000 44.78000  ? 65  PHE A O   1 
ATOM   146   C  CB  . PHE A  1 34  ? -34.94700 -35.45200 -14.21200 1.000 44.76000  ? 65  PHE A CB  1 
ATOM   147   C  CG  . PHE A  1 34  ? -34.33400 -36.33500 -15.27900 1.000 42.82000  ? 65  PHE A CG  1 
ATOM   148   C  CD1 . PHE A  1 34  ? -34.05500 -37.67500 -15.02700 1.000 37.75000  ? 65  PHE A CD1 1 
ATOM   149   C  CD2 . PHE A  1 34  ? -34.11800 -35.84000 -16.56500 1.000 40.26000  ? 65  PHE A CD2 1 
ATOM   150   C  CE1 . PHE A  1 34  ? -33.51300 -38.49600 -16.02500 1.000 42.03000  ? 65  PHE A CE1 1 
ATOM   151   C  CE2 . PHE A  1 34  ? -33.58500 -36.65100 -17.56900 1.000 38.07000  ? 65  PHE A CE2 1 
ATOM   152   C  CZ  . PHE A  1 34  ? -33.28000 -37.97800 -17.30100 1.000 40.09000  ? 65  PHE A CZ  1 
ATOM   153   N  N   . ASN A  1 35  ? -31.78800 -35.94500 -12.89800 1.000 42.57000  ? 66  ASN A N   1 
ATOM   154   C  CA  . ASN A  1 35  ? -30.91400 -36.95500 -12.32600 1.000 42.88000  ? 66  ASN A CA  1 
ATOM   155   C  C   . ASN A  1 35  ? -29.89300 -36.34900 -11.37300 1.000 39.41000  ? 66  ASN A C   1 
ATOM   156   O  O   . ASN A  1 35  ? -28.86300 -36.97500 -11.09300 1.000 44.15000  ? 66  ASN A O   1 
ATOM   157   C  CB  . ASN A  1 35  ? -30.23200 -37.75300 -13.43800 1.000 39.52000  ? 66  ASN A CB  1 
ATOM   158   C  CG  . ASN A  1 35  ? -30.21900 -39.23100 -13.15900 1.000 49.67000  ? 66  ASN A CG  1 
ATOM   159   O  OD1 . ASN A  1 35  ? -31.23800 -39.81900 -12.77800 1.000 50.91000  ? 66  ASN A OD1 1 
ATOM   160   N  ND2 . ASN A  1 35  ? -29.03900 -39.84100 -13.28500 1.000 44.26000  ? 66  ASN A ND2 1 
ATOM   161   N  N   . GLY A  1 36  ? -30.13300 -35.12000 -10.90300 1.000 41.17000  ? 67  GLY A N   1 
ATOM   162   C  CA  . GLY A  1 36  ? -29.34100 -34.53700 -9.83300  1.000 42.33000  ? 67  GLY A CA  1 
ATOM   163   C  C   . GLY A  1 36  ? -28.43400 -33.38200 -10.21000 1.000 46.41000  ? 67  GLY A C   1 
ATOM   164   O  O   . GLY A  1 36  ? -27.69100 -32.90900 -9.35000  1.000 48.27000  ? 67  GLY A O   1 
ATOM   165   N  N   . SER A  1 37  ? -28.44400 -32.90900 -11.44900 1.000 47.97000  ? 68  SER A N   1 
ATOM   166   C  CA  . SER A  1 37  ? -27.52900 -31.83400 -11.82500 1.000 43.89000  ? 68  SER A CA  1 
ATOM   167   C  C   . SER A  1 37  ? -27.87500 -30.53700 -11.10100 1.000 45.43000  ? 68  SER A C   1 
ATOM   168   O  O   . SER A  1 37  ? -29.03800 -30.12600 -11.07100 1.000 47.98000  ? 68  SER A O   1 
ATOM   169   C  CB  . SER A  1 37  ? -27.57000 -31.61100 -13.34300 1.000 43.35000  ? 68  SER A CB  1 
ATOM   170   O  OG  . SER A  1 37  ? -26.67000 -30.58400 -13.73200 1.000 47.59000  ? 68  SER A OG  1 
ATOM   171   N  N   . THR A  1 38  ? -26.86500 -29.87600 -10.54200 1.000 46.18000  ? 69  THR A N   1 
ATOM   172   C  CA  . THR A  1 38  ? -27.05400 -28.57900 -9.89700  1.000 54.49000  ? 69  THR A CA  1 
ATOM   173   C  C   . THR A  1 38  ? -26.59800 -27.39300 -10.74200 1.000 55.15000  ? 69  THR A C   1 
ATOM   174   O  O   . THR A  1 38  ? -26.84400 -26.25000 -10.33700 1.000 53.25000  ? 69  THR A O   1 
ATOM   175   C  CB  . THR A  1 38  ? -26.33500 -28.51200 -8.54600  1.000 50.29000  ? 69  THR A CB  1 
ATOM   176   O  OG1 . THR A  1 38  ? -24.94400 -28.79500 -8.72500  1.000 60.79000  ? 69  THR A OG1 1 
ATOM   177   C  CG2 . THR A  1 38  ? -26.93100 -29.49500 -7.58400  1.000 52.26000  ? 69  THR A CG2 1 
ATOM   178   N  N   . ASP A  1 39  ? -25.84100 -27.61200 -11.82600 1.000 50.15000  ? 70  ASP A N   1 
ATOM   179   C  CA  . ASP A  1 39  ? -25.35500 -26.49200 -12.62300 1.000 46.87000  ? 70  ASP A CA  1 
ATOM   180   C  C   . ASP A  1 39  ? -25.81100 -26.49700 -14.07600 1.000 45.54000  ? 70  ASP A C   1 
ATOM   181   O  O   . ASP A  1 39  ? -25.82800 -25.42700 -14.69400 1.000 48.97000  ? 70  ASP A O   1 
ATOM   182   C  CB  . ASP A  1 39  ? -23.81800 -26.40800 -12.58900 1.000 42.09000  ? 70  ASP A CB  1 
ATOM   183   C  CG  . ASP A  1 39  ? -23.12500 -27.71700 -12.99900 1.000 49.37000  ? 70  ASP A CG  1 
ATOM   184   O  OD1 . ASP A  1 39  ? -23.77400 -28.77500 -13.07400 1.000 48.40000  ? 70  ASP A OD1 1 
ATOM   185   O  OD2 . ASP A  1 39  ? -21.90700 -27.67100 -13.26200 1.000 47.82000  ? 70  ASP A OD2 1 
ATOM   186   N  N   . ILE A  1 40  ? -26.18400 -27.64200 -14.63200 1.000 43.06000  ? 71  ILE A N   1 
ATOM   187   C  CA  . ILE A  1 40  ? -26.68000 -27.73600 -16.00200 1.000 40.84000  ? 71  ILE A CA  1 
ATOM   188   C  C   . ILE A  1 40  ? -28.20400 -27.71200 -15.97900 1.000 42.94000  ? 71  ILE A C   1 
ATOM   189   O  O   . ILE A  1 40  ? -28.83100 -28.56900 -15.34900 1.000 43.53000  ? 71  ILE A O   1 
ATOM   190   C  CB  . ILE A  1 40  ? -26.16800 -29.02100 -16.67700 1.000 43.60000  ? 71  ILE A CB  1 
ATOM   191   C  CG1 . ILE A  1 40  ? -24.62300 -29.07000 -16.68800 1.000 40.31000  ? 71  ILE A CG1 1 
ATOM   192   C  CG2 . ILE A  1 40  ? -26.77300 -29.18700 -18.07900 1.000 38.53000  ? 71  ILE A CG2 1 
ATOM   193   C  CD1 . ILE A  1 40  ? -24.06600 -30.35400 -17.34600 1.000 36.96000  ? 71  ILE A CD1 1 
ATOM   194   N  N   . LEU A  1 41  ? -28.80100 -26.79500 -16.73100 1.000 43.47000  ? 72  LEU A N   1 
ATOM   195   C  CA  . LEU A  1 41  ? -30.25000 -26.63400 -16.76200 1.000 39.37000  ? 72  LEU A CA  1 
ATOM   196   C  C   . LEU A  1 41  ? -30.85600 -27.44800 -17.89200 1.000 43.84000  ? 72  LEU A C   1 
ATOM   197   O  O   . LEU A  1 41  ? -30.43300 -27.32300 -19.03900 1.000 45.19000  ? 72  LEU A O   1 
ATOM   198   C  CB  . LEU A  1 41  ? -30.60600 -25.15700 -16.90300 1.000 42.02000  ? 72  LEU A CB  1 
ATOM   199   C  CG  . LEU A  1 41  ? -30.07200 -24.31700 -15.74600 1.000 50.25000  ? 72  LEU A CG  1 
ATOM   200   C  CD1 . LEU A  1 41  ? -30.20700 -22.83500 -16.01300 1.000 55.28000  ? 72  LEU A CD1 1 
ATOM   201   C  CD2 . LEU A  1 41  ? -30.88300 -24.68200 -14.50600 1.000 44.08000  ? 72  LEU A CD2 1 
ATOM   202   N  N   . THR A  1 42  ? -31.80900 -28.32600 -17.56300 1.000 41.85000  ? 73  THR A N   1 
ATOM   203   C  CA  . THR A  1 42  ? -32.54000 -29.09500 -18.57000 1.000 39.07000  ? 73  THR A CA  1 
ATOM   204   C  C   . THR A  1 42  ? -34.05600 -29.03500 -18.31800 1.000 40.31000  ? 73  THR A C   1 
ATOM   205   O  O   . THR A  1 42  ? -34.71500 -30.07200 -18.18500 1.000 39.03000  ? 73  THR A O   1 
ATOM   206   C  CB  . THR A  1 42  ? -32.05400 -30.54400 -18.57300 1.000 40.16000  ? 73  THR A CB  1 
ATOM   207   O  OG1 . THR A  1 42  ? -32.31600 -31.12600 -17.30200 1.000 41.52000  ? 73  THR A OG1 1 
ATOM   208   C  CG2 . THR A  1 42  ? -30.52000 -30.62400 -18.80300 1.000 40.65000  ? 73  THR A CG2 1 
ATOM   209   N  N   . PRO A  1 43  ? -34.65500 -27.83500 -18.31300 1.000 39.00000  ? 74  PRO A N   1 
ATOM   210   C  CA  . PRO A  1 43  ? -36.09200 -27.74000 -17.95000 1.000 40.59000  ? 74  PRO A CA  1 
ATOM   211   C  C   . PRO A  1 43  ? -37.02200 -28.58700 -18.80500 1.000 46.60000  ? 74  PRO A C   1 
ATOM   212   O  O   . PRO A  1 43  ? -37.94800 -29.22000 -18.27500 1.000 47.87000  ? 74  PRO A O   1 
ATOM   213   C  CB  . PRO A  1 43  ? -36.39700 -26.24500 -18.11000 1.000 37.56000  ? 74  PRO A CB  1 
ATOM   214   C  CG  . PRO A  1 43  ? -35.30100 -25.71800 -19.03900 1.000 44.57000  ? 74  PRO A CG  1 
ATOM   215   C  CD  . PRO A  1 43  ? -34.07400 -26.50600 -18.59600 1.000 40.33000  ? 74  PRO A CD  1 
ATOM   216   N  N   . GLU A  1 44  ? -36.80200 -28.63000 -20.11400 1.000 41.49000  ? 75  GLU A N   1 
ATOM   217   C  CA  . GLU A  1 44  ? -37.65000 -29.45200 -20.95600 1.000 37.00000  ? 75  GLU A CA  1 
ATOM   218   C  C   . GLU A  1 44  ? -37.51600 -30.93300 -20.61900 1.000 41.49000  ? 75  GLU A C   1 
ATOM   219   O  O   . GLU A  1 44  ? -38.51900 -31.63300 -20.45100 1.000 38.09000  ? 75  GLU A O   1 
ATOM   220   C  CB  . GLU A  1 44  ? -37.32100 -29.20300 -22.42600 1.000 44.55000  ? 75  GLU A CB  1 
ATOM   221   C  CG  . GLU A  1 44  ? -37.58300 -27.80100 -22.87300 1.000 45.20000  ? 75  GLU A CG  1 
ATOM   222   C  CD  . GLU A  1 44  ? -39.07900 -27.48200 -22.86700 1.000 54.88000  ? 75  GLU A CD  1 
ATOM   223   O  OE1 . GLU A  1 44  ? -39.89100 -28.40100 -23.12100 1.000 51.21000  ? 75  GLU A OE1 1 
ATOM   224   O  OE2 . GLU A  1 44  ? -39.44300 -26.30500 -22.68200 1.000 58.57000  ? 75  GLU A OE2 1 
ATOM   225   N  N   . LEU A  1 45  ? -36.28500 -31.44500 -20.55400 1.000 41.86000  ? 76  LEU A N   1 
ATOM   226   C  CA  . LEU A  1 45  ? -36.11100 -32.85000 -20.19400 1.000 42.84000  ? 76  LEU A CA  1 
ATOM   227   C  C   . LEU A  1 45  ? -36.70200 -33.14200 -18.80800 1.000 44.14000  ? 76  LEU A C   1 
ATOM   228   O  O   . LEU A  1 45  ? -37.31400 -34.19500 -18.59400 1.000 38.72000  ? 76  LEU A O   1 
ATOM   229   C  CB  . LEU A  1 45  ? -34.62500 -33.22000 -20.23900 1.000 38.12000  ? 76  LEU A CB  1 
ATOM   230   C  CG  . LEU A  1 45  ? -34.02700 -33.48300 -21.62300 1.000 44.42000  ? 76  LEU A CG  1 
ATOM   231   C  CD1 . LEU A  1 45  ? -32.51100 -33.48700 -21.52200 1.000 39.41000  ? 76  LEU A CD1 1 
ATOM   232   C  CD2 . LEU A  1 45  ? -34.55400 -34.78600 -22.23600 1.000 42.21000  ? 76  LEU A CD2 1 
ATOM   233   N  N   . ASP A  1 46  ? -36.51900 -32.22200 -17.85400 1.000 38.04000  ? 77  ASP A N   1 
ATOM   234   C  CA  . ASP A  1 46  ? -37.04600 -32.42900 -16.50700 1.000 40.39000  ? 77  ASP A CA  1 
ATOM   235   C  C   . ASP A  1 46  ? -38.57800 -32.49400 -16.51300 1.000 46.11000  ? 77  ASP A C   1 
ATOM   236   O  O   . ASP A  1 46  ? -39.17100 -33.37400 -15.87400 1.000 39.19000  ? 77  ASP A O   1 
ATOM   237   C  CB  . ASP A  1 46  ? -36.53500 -31.31700 -15.57600 1.000 37.14000  ? 77  ASP A CB  1 
ATOM   238   C  CG  . ASP A  1 46  ? -35.03600 -31.38500 -15.35700 1.000 41.08000  ? 77  ASP A CG  1 
ATOM   239   O  OD1 . ASP A  1 46  ? -34.40400 -32.36000 -15.83000 1.000 42.69000  ? 77  ASP A OD1 1 
ATOM   240   O  OD2 . ASP A  1 46  ? -34.46700 -30.44200 -14.75600 1.000 45.14000  ? 77  ASP A OD2 1 
ATOM   241   N  N   . ASN A  1 47  ? -39.23400 -31.60300 -17.26000 1.000 41.14000  ? 78  ASN A N   1 
ATOM   242   C  CA  . ASN A  1 47  ? -40.69600 -31.62400 -17.29300 1.000 49.49000  ? 78  ASN A CA  1 
ATOM   243   C  C   . ASN A  1 47  ? -41.22400 -32.95600 -17.82700 1.000 48.37000  ? 78  ASN A C   1 
ATOM   244   O  O   . ASN A  1 47  ? -42.16700 -33.53400 -17.26700 1.000 46.06000  ? 78  ASN A O   1 
ATOM   245   C  CB  . ASN A  1 47  ? -41.24200 -30.45100 -18.11100 1.000 45.71000  ? 78  ASN A CB  1 
ATOM   246   C  CG  . ASN A  1 47  ? -42.77500 -30.36500 -18.04100 1.000 52.19000  ? 78  ASN A CG  1 
ATOM   247   O  OD1 . ASN A  1 47  ? -43.48300 -30.94500 -18.85800 1.000 54.16000  ? 78  ASN A OD1 1 
ATOM   248   N  ND2 . ASN A  1 47  ? -43.28000 -29.65800 -17.03800 1.000 48.28000  ? 78  ASN A ND2 1 
ATOM   249   N  N   . LEU A  1 48  ? -40.64000 -33.45700 -18.91800 1.000 42.31000  ? 79  LEU A N   1 
ATOM   250   C  CA  . LEU A  1 48  ? -41.02700 -34.77900 -19.39800 1.000 38.09000  ? 79  LEU A CA  1 
ATOM   251   C  C   . LEU A  1 48  ? -40.80500 -35.83600 -18.31800 1.000 44.68000  ? 79  LEU A C   1 
ATOM   252   O  O   . LEU A  1 48  ? -41.66600 -36.69500 -18.09300 1.000 40.57000  ? 79  LEU A O   1 
ATOM   253   C  CB  . LEU A  1 48  ? -40.23400 -35.13600 -20.65500 1.000 40.33000  ? 79  LEU A CB  1 
ATOM   254   C  CG  . LEU A  1 48  ? -40.48000 -34.34300 -21.94600 1.000 46.16000  ? 79  LEU A CG  1 
ATOM   255   C  CD1 . LEU A  1 48  ? -39.59100 -34.87400 -23.07300 1.000 35.70000  ? 79  LEU A CD1 1 
ATOM   256   C  CD2 . LEU A  1 48  ? -41.94700 -34.42600 -22.36800 1.000 36.16000  ? 79  LEU A CD2 1 
ATOM   257   N  N   . ALA A  1 49  ? -39.63800 -35.79300 -17.64400 1.000 37.31000  ? 80  ALA A N   1 
ATOM   258   C  CA  . ALA A  1 49  ? -39.32100 -36.81500 -16.64800 1.000 42.46000  ? 80  ALA A CA  1 
ATOM   259   C  C   . ALA A  1 49  ? -40.28100 -36.74400 -15.46400 1.000 38.85000  ? 80  ALA A C   1 
ATOM   260   O  O   . ALA A  1 49  ? -40.74500 -37.77300 -14.97700 1.000 37.46000  ? 80  ALA A O   1 
ATOM   261   C  CB  . ALA A  1 49  ? -37.85900 -36.69500 -16.18000 1.000 35.91000  ? 80  ALA A CB  1 
ATOM   262   N  N   . GLN A  1 50  ? -40.58900 -35.53700 -14.99500 1.000 39.93000  ? 81  GLN A N   1 
ATOM   263   C  CA  . GLN A  1 50  ? -41.52400 -35.37800 -13.88500 1.000 44.13000  ? 81  GLN A CA  1 
ATOM   264   C  C   . GLN A  1 50  ? -42.90400 -35.90100 -14.23500 1.000 49.92000  ? 81  GLN A C   1 
ATOM   265   O  O   . GLN A  1 50  ? -43.62000 -36.38800 -13.35200 1.000 49.65000  ? 81  GLN A O   1 
ATOM   266   C  CB  . GLN A  1 50  ? -41.59000 -33.90600 -13.47400 1.000 40.24000  ? 81  GLN A CB  1 
ATOM   267   C  CG  . GLN A  1 50  ? -40.23400 -33.39700 -13.02300 1.000 45.66000  ? 81  GLN A CG  1 
ATOM   268   C  CD  . GLN A  1 50  ? -40.18400 -31.89800 -12.83200 1.000 57.33000  ? 81  GLN A CD  1 
ATOM   269   O  OE1 . GLN A  1 50  ? -41.16500 -31.19300 -13.09100 1.000 54.07000  ? 81  GLN A OE1 1 
ATOM   270   N  NE2 . GLN A  1 50  ? -39.01600 -31.39000 -12.40700 1.000 48.44000  ? 81  GLN A NE2 1 
ATOM   271   N  N   . ASN A  1 51  ? -43.27100 -35.84700 -15.51600 1.000 43.80000  ? 82  ASN A N   1 
ATOM   272   C  CA  . ASN A  1 51  ? -44.56000 -36.30700 -16.00800 1.000 45.98000  ? 82  ASN A CA  1 
ATOM   273   C  C   . ASN A  1 51  ? -44.52100 -37.72200 -16.54100 1.000 44.45000  ? 82  ASN A C   1 
ATOM   274   O  O   . ASN A  1 51  ? -45.46200 -38.13700 -17.21300 1.000 49.29000  ? 82  ASN A O   1 
ATOM   275   C  CB  . ASN A  1 51  ? -45.07600 -35.33200 -17.06000 1.000 47.52000  ? 82  ASN A CB  1 
ATOM   276   C  CG  . ASN A  1 51  ? -45.54000 -34.04100 -16.43700 1.000 49.03000  ? 82  ASN A CG  1 
ATOM   277   O  OD1 . ASN A  1 51  ? -46.39300 -34.05600 -15.55800 1.000 55.68000  ? 82  ASN A OD1 1 
ATOM   278   N  ND2 . ASN A  1 51  ? -44.88300 -32.94500 -16.77100 1.000 51.06000  ? 82  ASN A ND2 1 
ATOM   279   N  N   . GLY A  1 52  ? -43.49700 -38.48500 -16.21500 1.000 43.82000  ? 83  GLY A N   1 
ATOM   280   C  CA  . GLY A  1 52  ? -43.41500 -39.88000 -16.61400 1.000 41.31000  ? 83  GLY A CA  1 
ATOM   281   C  C   . GLY A  1 52  ? -42.68700 -40.66600 -15.54000 1.000 43.71000  ? 83  GLY A C   1 
ATOM   282   O  O   . GLY A  1 52  ? -42.76800 -40.33900 -14.35300 1.000 41.58000  ? 83  GLY A O   1 
ATOM   283   N  N   . SER A  1 53  ? -41.94200 -41.68300 -15.95300 1.000 38.88000  ? 84  SER A N   1 
ATOM   284   C  CA  . SER A  1 53  ? -41.24000 -42.54400 -15.02200 1.000 40.93000  ? 84  SER A CA  1 
ATOM   285   C  C   . SER A  1 53  ? -39.72300 -42.38300 -15.15400 1.000 45.21000  ? 84  SER A C   1 
ATOM   286   O  O   . SER A  1 53  ? -39.13700 -42.74700 -16.18400 1.000 41.33000  ? 84  SER A O   1 
ATOM   287   C  CB  . SER A  1 53  ? -41.66500 -43.98100 -15.27300 1.000 39.21000  ? 84  SER A CB  1 
ATOM   288   O  OG  . SER A  1 53  ? -40.86700 -44.87200 -14.56200 1.000 44.88000  ? 84  SER A OG  1 
ATOM   289   N  N   . ILE A  1 54  ? -39.08300 -41.93700 -14.07100 1.000 44.18000  ? 85  ILE A N   1 
ATOM   290   C  CA  . ILE A  1 54  ? -37.62900 -41.87200 -13.99400 1.000 43.12000  ? 85  ILE A CA  1 
ATOM   291   C  C   . ILE A  1 54  ? -37.08900 -43.22900 -13.57200 1.000 46.92000  ? 85  ILE A C   1 
ATOM   292   O  O   . ILE A  1 54  ? -37.64000 -43.87400 -12.67600 1.000 50.77000  ? 85  ILE A O   1 
ATOM   293   C  CB  . ILE A  1 54  ? -37.19100 -40.80200 -12.98900 1.000 41.72000  ? 85  ILE A CB  1 
ATOM   294   C  CG1 . ILE A  1 54  ? -37.58500 -39.42200 -13.48300 1.000 38.63000  ? 85  ILE A CG1 1 
ATOM   295   C  CG2 . ILE A  1 54  ? -35.69200 -40.90400 -12.70900 1.000 34.40000  ? 85  ILE A CG2 1 
ATOM   296   C  CD1 . ILE A  1 54  ? -37.38200 -38.33100 -12.44400 1.000 37.56000  ? 85  ILE A CD1 1 
ATOM   297   N  N   . PHE A  1 55  ? -36.02900 -43.68400 -14.24400 1.000 41.90000  ? 86  PHE A N   1 
ATOM   298   C  CA  . PHE A  1 55  ? -35.38100 -44.96200 -13.95400 1.000 41.67000  ? 86  PHE A CA  1 
ATOM   299   C  C   . PHE A  1 55  ? -34.07700 -44.68700 -13.21500 1.000 44.24000  ? 86  PHE A C   1 
ATOM   300   O  O   . PHE A  1 55  ? -33.14500 -44.11100 -13.79200 1.000 43.83000  ? 86  PHE A O   1 
ATOM   301   C  CB  . PHE A  1 55  ? -35.11100 -45.76300 -15.22200 1.000 43.40000  ? 86  PHE A CB  1 
ATOM   302   C  CG  . PHE A  1 55  ? -36.35000 -46.27600 -15.88000 1.000 38.16000  ? 86  PHE A CG  1 
ATOM   303   C  CD1 . PHE A  1 55  ? -37.16000 -45.43000 -16.61900 1.000 46.26000  ? 86  PHE A CD1 1 
ATOM   304   C  CD2 . PHE A  1 55  ? -36.73100 -47.59700 -15.72600 1.000 38.26000  ? 86  PHE A CD2 1 
ATOM   305   C  CE1 . PHE A  1 55  ? -38.33300 -45.88900 -17.22900 1.000 41.75000  ? 86  PHE A CE1 1 
ATOM   306   C  CE2 . PHE A  1 55  ? -37.90900 -48.07000 -16.33100 1.000 49.59000  ? 86  PHE A CE2 1 
ATOM   307   C  CZ  . PHE A  1 55  ? -38.70900 -47.20300 -17.08200 1.000 40.22000  ? 86  PHE A CZ  1 
ATOM   308   N  N   . THR A  1 56  ? -34.03800 -45.03800 -11.92100 1.000 43.17000  ? 87  THR A N   1 
ATOM   309   C  CA  . THR A  1 56  ? -32.89800 -44.75600 -11.05400 1.000 43.45000  ? 87  THR A CA  1 
ATOM   310   C  C   . THR A  1 56  ? -31.80900 -45.82300 -11.09700 1.000 36.90000  ? 87  THR A C   1 
ATOM   311   O  O   . THR A  1 56  ? -30.77100 -45.62300 -10.48900 1.000 40.18000  ? 87  THR A O   1 
ATOM   312   C  CB  . THR A  1 56  ? -33.36100 -44.58700 -9.60200  1.000 45.07000  ? 87  THR A CB  1 
ATOM   313   O  OG1 . THR A  1 56  ? -33.95800 -45.81600 -9.15400  1.000 41.89000  ? 87  THR A OG1 1 
ATOM   314   C  CG2 . THR A  1 56  ? -34.34400 -43.42100 -9.45700  1.000 41.79000  ? 87  THR A CG2 1 
ATOM   315   N  N   . SER A  1 57  ? -32.03300 -46.96200 -11.74400 1.000 39.49000  ? 88  SER A N   1 
ATOM   316   C  CA  . SER A  1 57  ? -30.99500 -47.96500 -11.95600 1.000 37.12000  ? 88  SER A CA  1 
ATOM   317   C  C   . SER A  1 57  ? -31.06600 -48.48400 -13.40200 1.000 39.57000  ? 88  SER A C   1 
ATOM   318   O  O   . SER A  1 57  ? -31.26700 -49.66800 -13.65900 1.000 37.58000  ? 88  SER A O   1 
ATOM   319   C  CB  . SER A  1 57  ? -31.08500 -49.13300 -10.96100 1.000 40.79000  ? 88  SER A CB  1 
ATOM   320   O  OG  . SER A  1 57  ? -30.40200 -48.89400 -9.71800  1.000 40.35000  ? 88  SER A OG  1 
ATOM   321   N  N   . ALA A  1 58  ? -30.82400 -47.58700 -14.36300 1.000 37.50000  ? 89  ALA A N   1 
ATOM   322   C  CA  . ALA A  1 58  ? -30.83300 -47.90700 -15.79000 1.000 37.38000  ? 89  ALA A CA  1 
ATOM   323   C  C   . ALA A  1 58  ? -29.41700 -48.18700 -16.29300 1.000 38.25000  ? 89  ALA A C   1 
ATOM   324   O  O   . ALA A  1 58  ? -28.47100 -47.47900 -15.94300 1.000 41.30000  ? 89  ALA A O   1 
ATOM   325   C  CB  . ALA A  1 58  ? -31.43600 -46.75000 -16.57500 1.000 30.68000  ? 89  ALA A CB  1 
ATOM   326   N  N   . TYR A  1 59  ? -29.26600 -49.21300 -17.11500 1.000 37.63000  ? 90  TYR A N   1 
ATOM   327   C  CA  . TYR A  1 59  ? -27.94200 -49.63100 -17.57000 1.000 31.36000  ? 90  TYR A CA  1 
ATOM   328   C  C   . TYR A  1 59  ? -27.93100 -49.79600 -19.07900 1.000 38.63000  ? 90  TYR A C   1 
ATOM   329   O  O   . TYR A  1 59  ? -28.89900 -50.30200 -19.65200 1.000 41.15000  ? 90  TYR A O   1 
ATOM   330   C  CB  . TYR A  1 59  ? -27.54700 -50.95700 -16.92900 1.000 32.57000  ? 90  TYR A CB  1 
ATOM   331   C  CG  . TYR A  1 59  ? -27.40200 -50.88500 -15.41400 1.000 41.42000  ? 90  TYR A CG  1 
ATOM   332   C  CD1 . TYR A  1 59  ? -26.21800 -50.39900 -14.83200 1.000 37.25000  ? 90  TYR A CD1 1 
ATOM   333   C  CD2 . TYR A  1 59  ? -28.41900 -51.34200 -14.56600 1.000 34.57000  ? 90  TYR A CD2 1 
ATOM   334   C  CE1 . TYR A  1 59  ? -26.05600 -50.34600 -13.44800 1.000 41.69000  ? 90  TYR A CE1 1 
ATOM   335   C  CE2 . TYR A  1 59  ? -28.27400 -51.28100 -13.17500 1.000 35.94000  ? 90  TYR A CE2 1 
ATOM   336   C  CZ  . TYR A  1 59  ? -27.08200 -50.78000 -12.62100 1.000 42.90000  ? 90  TYR A CZ  1 
ATOM   337   O  OH  . TYR A  1 59  ? -26.90100 -50.71000 -11.25400 1.000 40.16000  ? 90  TYR A OH  1 
ATOM   338   N  N   . VAL A  1 60  ? -26.82900 -49.39200 -19.72300 1.000 38.02000  ? 91  VAL A N   1 
ATOM   339   C  CA  . VAL A  1 60  ? -26.59500 -49.75100 -21.11700 1.000 34.94000  ? 91  VAL A CA  1 
ATOM   340   C  C   . VAL A  1 60  ? -25.77300 -51.03100 -21.13400 1.000 36.72000  ? 91  VAL A C   1 
ATOM   341   O  O   . VAL A  1 60  ? -25.16400 -51.40500 -20.13800 1.000 34.94000  ? 91  VAL A O   1 
ATOM   342   C  CB  . VAL A  1 60  ? -25.89400 -48.63300 -21.92700 1.000 34.92000  ? 91  VAL A CB  1 
ATOM   343   C  CG1 . VAL A  1 60  ? -26.78100 -47.44400 -22.07300 1.000 32.83000  ? 91  VAL A CG1 1 
ATOM   344   C  CG2 . VAL A  1 60  ? -24.55400 -48.20300 -21.26200 1.000 36.64000  ? 91  VAL A CG2 1 
ATOM   345   N  N   . ALA A  1 61  ? -25.73100 -51.70100 -22.28600 1.000 39.50000  ? 92  ALA A N   1 
ATOM   346   C  CA  . ALA A  1 61  ? -25.12400 -53.02800 -22.35900 1.000 34.86000  ? 92  ALA A CA  1 
ATOM   347   C  C   . ALA A  1 61  ? -23.60400 -52.99700 -22.53600 1.000 38.03000  ? 92  ALA A C   1 
ATOM   348   O  O   . ALA A  1 61  ? -22.97500 -54.06800 -22.54000 1.000 36.85000  ? 92  ALA A O   1 
ATOM   349   C  CB  . ALA A  1 61  ? -25.75000 -53.83800 -23.50700 1.000 37.80000  ? 92  ALA A CB  1 
ATOM   350   N  N   . HIS A  1 62  ? -22.99100 -51.81500 -22.66200 1.000 32.99000  ? 93  HIS A N   1 
ATOM   351   C  CA  . HIS A  1 62  ? -21.53500 -51.76000 -22.79800 1.000 38.13000  ? 93  HIS A CA  1 
ATOM   352   C  C   . HIS A  1 62  ? -21.09400 -50.36500 -22.41000 1.000 37.54000  ? 93  HIS A C   1 
ATOM   353   O  O   . HIS A  1 62  ? -21.81600 -49.40300 -22.70700 1.000 33.92000  ? 93  HIS A O   1 
ATOM   354   C  CB  . HIS A  1 62  ? -21.06500 -52.09900 -24.22400 1.000 34.35000  ? 93  HIS A CB  1 
ATOM   355   C  CG  . HIS A  1 62  ? -19.61100 -52.46800 -24.31000 1.000 38.67000  ? 93  HIS A CG  1 
ATOM   356   N  ND1 . HIS A  1 62  ? -19.13000 -53.69600 -23.90000 1.000 40.98000  ? 93  HIS A ND1 1 
ATOM   357   C  CD2 . HIS A  1 62  ? -18.53600 -51.78600 -24.78400 1.000 34.14000  ? 93  HIS A CD2 1 
ATOM   358   C  CE1 . HIS A  1 62  ? -17.81900 -53.74300 -24.08000 1.000 37.44000  ? 93  HIS A CE1 1 
ATOM   359   N  NE2 . HIS A  1 62  ? -17.43600 -52.59800 -24.62100 1.000 41.06000  ? 93  HIS A NE2 1 
ATOM   360   N  N   . PRO A  1 63  ? -19.92600 -50.20300 -21.76200 1.000 36.26000  ? 94  PRO A N   1 
ATOM   361   C  CA  . PRO A  1 63  ? -19.56000 -48.86600 -21.27800 1.000 33.35000  ? 94  PRO A CA  1 
ATOM   362   C  C   . PRO A  1 63  ? -18.96700 -47.93200 -22.32600 1.000 34.98000  ? 94  PRO A C   1 
ATOM   363   O  O   . PRO A  1 63  ? -18.44700 -46.89500 -21.92100 1.000 35.70000  ? 94  PRO A O   1 
ATOM   364   C  CB  . PRO A  1 63  ? -18.55300 -49.16300 -20.15200 1.000 36.90000  ? 94  PRO A CB  1 
ATOM   365   C  CG  . PRO A  1 63  ? -17.91500 -50.47100 -20.55700 1.000 37.34000  ? 94  PRO A CG  1 
ATOM   366   C  CD  . PRO A  1 63  ? -19.05500 -51.26100 -21.20500 1.000 36.70000  ? 94  PRO A CD  1 
ATOM   367   N  N   . PHE A  1 64  ? -19.08200 -48.20100 -23.63700 1.000 37.13000  ? 95  PHE A N   1 
ATOM   368   C  CA  . PHE A  1 64  ? -18.76700 -47.16400 -24.62100 1.000 37.60000  ? 95  PHE A CA  1 
ATOM   369   C  C   . PHE A  1 64  ? -19.53800 -47.34700 -25.93800 1.000 41.75000  ? 95  PHE A C   1 
ATOM   370   O  O   . PHE A  1 64  ? -20.10900 -48.40200 -26.20700 1.000 41.00000  ? 95  PHE A O   1 
ATOM   371   C  CB  . PHE A  1 64  ? -17.25000 -47.04300 -24.88300 1.000 34.59000  ? 95  PHE A CB  1 
ATOM   372   C  CG  . PHE A  1 64  ? -16.56000 -48.30400 -25.36000 1.000 35.65000  ? 95  PHE A CG  1 
ATOM   373   C  CD1 . PHE A  1 64  ? -16.67000 -48.71400 -26.68000 1.000 41.43000  ? 95  PHE A CD1 1 
ATOM   374   C  CD2 . PHE A  1 64  ? -15.68400 -48.99500 -24.52200 1.000 38.37000  ? 95  PHE A CD2 1 
ATOM   375   C  CE1 . PHE A  1 64  ? -15.98500 -49.84500 -27.14200 1.000 43.93000  ? 95  PHE A CE1 1 
ATOM   376   C  CE2 . PHE A  1 64  ? -14.98000 -50.13400 -24.97200 1.000 34.91000  ? 95  PHE A CE2 1 
ATOM   377   C  CZ  . PHE A  1 64  ? -15.14300 -50.55800 -26.28800 1.000 34.28000  ? 95  PHE A CZ  1 
ATOM   378   N  N   A CYS A  1 65  ? -19.47600 -46.29100 -26.76700 0.300 41.71000  ? 96  CYS A N   1 
ATOM   379   C  CA  A CYS A  1 65  ? -20.29600 -45.99600 -27.94600 0.300 40.03000  ? 96  CYS A CA  1 
ATOM   380   C  C   A CYS A  1 65  ? -20.74900 -47.18800 -28.78500 0.300 38.73000  ? 96  CYS A C   1 
ATOM   381   O  O   A CYS A  1 65  ? -21.89700 -47.62700 -28.67700 0.300 37.49000  ? 96  CYS A O   1 
ATOM   382   C  CB  A CYS A  1 65  ? -19.53900 -45.02700 -28.87300 0.300 42.38000  ? 96  CYS A CB  1 
ATOM   383   S  SG  A CYS A  1 65  ? -19.17500 -43.36900 -28.21500 0.300 43.77000  ? 96  CYS A SG  1 
HETATM 384   N  N   B DDZ A  1 65  ? -19.48300 -46.27700 -26.75200 0.700 41.78000  ? 96  DDZ A N   1 
HETATM 385   C  CA  B DDZ A  1 65  ? -20.23600 -45.90300 -27.99200 0.700 40.03000  ? 96  DDZ A CA  1 
HETATM 386   C  C   B DDZ A  1 65  ? -20.73300 -47.08300 -28.84800 0.700 38.66000  ? 96  DDZ A C   1 
HETATM 387   O  O   B DDZ A  1 65  ? -21.94600 -47.36000 -28.83000 0.700 36.79000  ? 96  DDZ A O   1 
HETATM 388   O  OG1 B DDZ A  1 65  ? -19.06300 -43.73700 -28.17800 0.700 44.35000  ? 96  DDZ A OG1 1 
HETATM 389   O  OG2 B DDZ A  1 65  ? -19.76800 -44.79400 -30.15700 0.700 43.05000  ? 96  DDZ A OG2 1 
HETATM 390   C  CB  B DDZ A  1 65  ? -19.31900 -44.98300 -28.82200 0.700 42.62000  ? 96  DDZ A CB  1 
ATOM   391   N  N   . GLY A  1 66  ? -19.87100 -47.67900 -29.65600 1.000 38.27000  ? 97  GLY A N   1 
ATOM   392   C  CA  . GLY A  1 66  ? -20.25600 -48.61600 -30.69600 1.000 38.54000  ? 97  GLY A CA  1 
ATOM   393   C  C   . GLY A  1 66  ? -20.99300 -49.86300 -30.24500 1.000 41.84000  ? 97  GLY A C   1 
ATOM   394   O  O   . GLY A  1 66  ? -22.03900 -50.22500 -30.79000 1.000 36.27000  ? 97  GLY A O   1 
ATOM   395   N  N   . PRO A  1 67  ? -20.41000 -50.58800 -29.28900 1.000 37.24000  ? 98  PRO A N   1 
ATOM   396   C  CA  . PRO A  1 67  ? -21.07900 -51.80500 -28.80800 1.000 36.06000  ? 98  PRO A CA  1 
ATOM   397   C  C   . PRO A  1 67  ? -22.38200 -51.51400 -28.10400 1.000 43.69000  ? 98  PRO A C   1 
ATOM   398   O  O   . PRO A  1 67  ? -23.35400 -52.27100 -28.25400 1.000 42.36000  ? 98  PRO A O   1 
ATOM   399   C  CB  . PRO A  1 67  ? -20.04200 -52.40900 -27.85100 1.000 38.99000  ? 98  PRO A CB  1 
ATOM   400   C  CG  . PRO A  1 67  ? -18.72300 -51.89700 -28.37600 1.000 35.40000  ? 98  PRO A CG  1 
ATOM   401   C  CD  . PRO A  1 67  ? -19.02800 -50.48300 -28.79500 1.000 37.03000  ? 98  PRO A CD  1 
ATOM   402   N  N   . SER A  1 68  ? -22.43600 -50.42600 -27.33600 1.000 38.81000  ? 99  SER A N   1 
ATOM   403   C  CA  . SER A  1 68  ? -23.69500 -50.06400 -26.70500 1.000 41.88000  ? 99  SER A CA  1 
ATOM   404   C  C   . SER A  1 68  ? -24.77100 -49.83100 -27.75500 1.000 37.63000  ? 99  SER A C   1 
ATOM   405   O  O   . SER A  1 68  ? -25.89000 -50.34700 -27.64400 1.000 41.64000  ? 99  SER A O   1 
ATOM   406   C  CB  . SER A  1 68  ? -23.50900 -48.82000 -25.85500 1.000 39.51000  ? 99  SER A CB  1 
ATOM   407   O  OG  . SER A  1 68  ? -24.76300 -48.36000 -25.41700 1.000 39.50000  ? 99  SER A OG  1 
ATOM   408   N  N   . ARG A  1 69  ? -24.43300 -49.08600 -28.80700 1.000 35.17000  ? 100 ARG A N   1 
ATOM   409   C  CA  . ARG A  1 69  ? -25.41000 -48.80700 -29.85000 1.000 39.04000  ? 100 ARG A CA  1 
ATOM   410   C  C   . ARG A  1 69  ? -25.78500 -50.07000 -30.61900 1.000 40.84000  ? 100 ARG A C   1 
ATOM   411   O  O   . ARG A  1 69  ? -26.97000 -50.33300 -30.83300 1.000 39.17000  ? 100 ARG A O   1 
ATOM   412   C  CB  . ARG A  1 69  ? -24.87100 -47.73700 -30.79000 1.000 39.12000  ? 100 ARG A CB  1 
ATOM   413   C  CG  . ARG A  1 69  ? -24.88100 -46.37900 -30.16200 1.000 37.76000  ? 100 ARG A CG  1 
ATOM   414   C  CD  . ARG A  1 69  ? -23.91800 -45.43900 -30.84600 1.000 40.18000  ? 100 ARG A CD  1 
ATOM   415   N  NE  . ARG A  1 69  ? -23.72900 -44.26600 -30.00700 1.000 40.23000  ? 100 ARG A NE  1 
ATOM   416   C  CZ  . ARG A  1 69  ? -24.52800 -43.21300 -29.99000 1.000 35.25000  ? 100 ARG A CZ  1 
ATOM   417   N  NH1 . ARG A  1 69  ? -25.52500 -43.08700 -30.85200 1.000 36.05000  ? 100 ARG A NH1 1 
ATOM   418   N  NH2 . ARG A  1 69  ? -24.33700 -42.27400 -29.07000 1.000 38.97000  ? 100 ARG A NH2 1 
ATOM   419   N  N   . SER A  1 70  ? -24.80000 -50.90100 -30.97300 1.000 41.23000  ? 101 SER A N   1 
ATOM   420   C  CA  . SER A  1 70  ? -25.11100 -52.21300 -31.54100 1.000 42.56000  ? 101 SER A CA  1 
ATOM   421   C  C   . SER A  1 70  ? -26.10100 -52.97900 -30.66800 1.000 41.76000  ? 101 SER A C   1 
ATOM   422   O  O   . SER A  1 70  ? -27.04500 -53.60000 -31.16900 1.000 47.75000  ? 101 SER A O   1 
ATOM   423   C  CB  . SER A  1 70  ? -23.82700 -53.01700 -31.71800 1.000 44.09000  ? 101 SER A CB  1 
ATOM   424   O  OG  . SER A  1 70  ? -24.12200 -54.38800 -31.84700 1.000 50.98000  ? 101 SER A OG  1 
ATOM   425   N  N   . ALA A  1 71  ? -25.91100 -52.93500 -29.35600 1.000 46.19000  ? 102 ALA A N   1 
ATOM   426   C  CA  . ALA A  1 71  ? -26.80300 -53.65800 -28.46000 1.000 43.43000  ? 102 ALA A CA  1 
ATOM   427   C  C   . ALA A  1 71  ? -28.21400 -53.07600 -28.48100 1.000 46.39000  ? 102 ALA A C   1 
ATOM   428   O  O   . ALA A  1 71  ? -29.19900 -53.81500 -28.39500 1.000 44.28000  ? 102 ALA A O   1 
ATOM   429   C  CB  . ALA A  1 71  ? -26.23200 -53.62600 -27.04700 1.000 34.99000  ? 102 ALA A CB  1 
ATOM   430   N  N   . ILE A  1 72  ? -28.32900 -51.74900 -28.53900 1.000 42.31000  ? 103 ILE A N   1 
ATOM   431   C  CA  . ILE A  1 72  ? -29.64200 -51.12500 -28.52100 1.000 41.03000  ? 103 ILE A CA  1 
ATOM   432   C  C   . ILE A  1 72  ? -30.45500 -51.55300 -29.73400 1.000 45.45000  ? 103 ILE A C   1 
ATOM   433   O  O   . ILE A  1 72  ? -31.63700 -51.89800 -29.61400 1.000 44.89000  ? 103 ILE A O   1 
ATOM   434   C  CB  . ILE A  1 72  ? -29.51300 -49.59300 -28.43000 1.000 42.71000  ? 103 ILE A CB  1 
ATOM   435   C  CG1 . ILE A  1 72  ? -29.16900 -49.18000 -27.00500 1.000 40.00000  ? 103 ILE A CG1 1 
ATOM   436   C  CG2 . ILE A  1 72  ? -30.78300 -48.91400 -28.91200 1.000 42.61000  ? 103 ILE A CG2 1 
ATOM   437   C  CD1 . ILE A  1 72  ? -28.66400 -47.77200 -26.90200 1.000 41.57000  ? 103 ILE A CD1 1 
ATOM   438   N  N   . LEU A  1 73  ? -29.84300 -51.55200 -30.91500 1.000 42.00000  ? 104 LEU A N   1 
ATOM   439   C  CA  . LEU A  1 73  ? -30.62000 -51.83500 -32.10800 1.000 43.32000  ? 104 LEU A CA  1 
ATOM   440   C  C   . LEU A  1 73  ? -30.79400 -53.33300 -32.33200 1.000 43.77000  ? 104 LEU A C   1 
ATOM   441   O  O   . LEU A  1 73  ? -31.83300 -53.73600 -32.84900 1.000 42.41000  ? 104 LEU A O   1 
ATOM   442   C  CB  . LEU A  1 73  ? -29.98400 -51.15200 -33.31800 1.000 42.98000  ? 104 LEU A CB  1 
ATOM   443   C  CG  . LEU A  1 73  ? -30.45700 -49.68800 -33.31000 1.000 45.25000  ? 104 LEU A CG  1 
ATOM   444   C  CD1 . LEU A  1 73  ? -29.55200 -48.79400 -34.08100 1.000 45.12000  ? 104 LEU A CD1 1 
ATOM   445   C  CD2 . LEU A  1 73  ? -31.89100 -49.52400 -33.82200 1.000 51.68000  ? 104 LEU A CD2 1 
ATOM   446   N  N   . THR A  1 74  ? -29.82800 -54.17100 -31.92000 1.000 40.10000  ? 105 THR A N   1 
ATOM   447   C  CA  . THR A  1 74  ? -29.95000 -55.62400 -32.06500 1.000 41.07000  ? 105 THR A CA  1 
ATOM   448   C  C   . THR A  1 74  ? -30.62100 -56.30500 -30.88200 1.000 46.31000  ? 105 THR A C   1 
ATOM   449   O  O   . THR A  1 74  ? -30.95900 -57.48900 -30.99400 1.000 41.38000  ? 105 THR A O   1 
ATOM   450   C  CB  . THR A  1 74  ? -28.59000 -56.32400 -32.24800 1.000 42.29000  ? 105 THR A CB  1 
ATOM   451   O  OG1 . THR A  1 74  ? -27.82000 -56.24000 -31.03200 1.000 51.31000  ? 105 THR A OG1 1 
ATOM   452   C  CG2 . THR A  1 74  ? -27.80000 -55.74400 -33.40300 1.000 38.73000  ? 105 THR A CG2 1 
ATOM   453   N  N   . GLY A  1 75  ? -30.72200 -55.63400 -29.72900 1.000 42.00000  ? 106 GLY A N   1 
ATOM   454   C  CA  . GLY A  1 75  ? -31.29600 -56.26200 -28.55600 1.000 35.96000  ? 106 GLY A CA  1 
ATOM   455   C  C   . GLY A  1 75  ? -30.43400 -57.34600 -27.95400 1.000 45.20000  ? 106 GLY A C   1 
ATOM   456   O  O   . GLY A  1 75  ? -30.92600 -58.13100 -27.13800 1.000 46.00000  ? 106 GLY A O   1 
ATOM   457   N  N   . ARG A  1 76  ? -29.15900 -57.41900 -28.33300 1.000 41.27000  ? 107 ARG A N   1 
ATOM   458   C  CA  . ARG A  1 76  ? -28.26100 -58.45200 -27.85100 1.000 40.36000  ? 107 ARG A CA  1 
ATOM   459   C  C   . ARG A  1 76  ? -26.97500 -57.83200 -27.32100 1.000 45.82000  ? 107 ARG A C   1 
ATOM   460   O  O   . ARG A  1 76  ? -26.53300 -56.77600 -27.78200 1.000 46.59000  ? 107 ARG A O   1 
ATOM   461   C  CB  . ARG A  1 76  ? -27.91000 -59.44300 -28.96000 1.000 46.64000  ? 107 ARG A CB  1 
ATOM   462   C  CG  . ARG A  1 76  ? -29.08200 -60.29200 -29.37900 1.000 47.43000  ? 107 ARG A CG  1 
ATOM   463   C  CD  . ARG A  1 76  ? -28.67800 -61.34500 -30.37600 1.000 49.50000  ? 107 ARG A CD  1 
ATOM   464   N  NE  . ARG A  1 76  ? -28.24500 -62.56600 -29.70600 1.000 47.79000  ? 107 ARG A NE  1 
ATOM   465   C  CZ  . ARG A  1 76  ? -27.57100 -63.54200 -30.30100 1.000 54.93000  ? 107 ARG A CZ  1 
ATOM   466   N  NH1 . ARG A  1 76  ? -27.26900 -63.48700 -31.59600 1.000 45.00000  ? 107 ARG A NH1 1 
ATOM   467   N  NH2 . ARG A  1 76  ? -27.23300 -64.62000 -29.59200 1.000 48.56000  ? 107 ARG A NH2 1 
ATOM   468   N  N   . TYR A  1 77  ? -26.38000 -58.50100 -26.34800 1.000 42.31000  ? 108 TYR A N   1 
ATOM   469   C  CA  . TYR A  1 77  ? -25.07100 -58.09700 -25.87400 1.000 45.24000  ? 108 TYR A CA  1 
ATOM   470   C  C   . TYR A  1 77  ? -24.08200 -58.10700 -27.04000 1.000 43.96000  ? 108 TYR A C   1 
ATOM   471   O  O   . TYR A  1 77  ? -24.15100 -58.99500 -27.89700 1.000 44.35000  ? 108 TYR A O   1 
ATOM   472   C  CB  . TYR A  1 77  ? -24.59800 -59.03700 -24.76100 1.000 47.48000  ? 108 TYR A CB  1 
ATOM   473   C  CG  . TYR A  1 77  ? -25.15400 -58.71800 -23.39400 1.000 43.09000  ? 108 TYR A CG  1 
ATOM   474   C  CD1 . TYR A  1 77  ? -24.68300 -57.61600 -22.67300 1.000 40.01000  ? 108 TYR A CD1 1 
ATOM   475   C  CD2 . TYR A  1 77  ? -26.10900 -59.53600 -22.79900 1.000 42.05000  ? 108 TYR A CD2 1 
ATOM   476   C  CE1 . TYR A  1 77  ? -25.16800 -57.31800 -21.41200 1.000 38.12000  ? 108 TYR A CE1 1 
ATOM   477   C  CE2 . TYR A  1 77  ? -26.59600 -59.25000 -21.52600 1.000 46.85000  ? 108 TYR A CE2 1 
ATOM   478   C  CZ  . TYR A  1 77  ? -26.12000 -58.13600 -20.83900 1.000 45.14000  ? 108 TYR A CZ  1 
ATOM   479   O  OH  . TYR A  1 77  ? -26.59900 -57.81800 -19.58900 1.000 43.68000  ? 108 TYR A OH  1 
ATOM   480   N  N   . PRO A  1 78  ? -23.19200 -57.11400 -27.14000 1.000 41.00000  ? 109 PRO A N   1 
ATOM   481   C  CA  . PRO A  1 78  ? -22.22100 -57.11400 -28.24900 1.000 44.73000  ? 109 PRO A CA  1 
ATOM   482   C  C   . PRO A  1 78  ? -21.26100 -58.28200 -28.21400 1.000 42.48000  ? 109 PRO A C   1 
ATOM   483   O  O   . PRO A  1 78  ? -20.69000 -58.62200 -29.26100 1.000 48.15000  ? 109 PRO A O   1 
ATOM   484   C  CB  . PRO A  1 78  ? -21.47800 -55.78300 -28.07300 1.000 42.00000  ? 109 PRO A CB  1 
ATOM   485   C  CG  . PRO A  1 78  ? -21.59100 -55.49900 -26.60800 1.000 38.90000  ? 109 PRO A CG  1 
ATOM   486   C  CD  . PRO A  1 78  ? -23.00300 -55.95600 -26.25900 1.000 42.80000  ? 109 PRO A CD  1 
ATOM   487   N  N   . HIS A  1 79  ? -21.07900 -58.92800 -27.05800 1.000 43.49000  ? 110 HIS A N   1 
ATOM   488   C  CA  . HIS A  1 79  ? -20.19200 -60.09100 -26.98900 1.000 49.50000  ? 110 HIS A CA  1 
ATOM   489   C  C   . HIS A  1 79  ? -20.78900 -61.29500 -27.69600 1.000 53.68000  ? 110 HIS A C   1 
ATOM   490   O  O   . HIS A  1 79  ? -20.07200 -62.26700 -27.96500 1.000 54.72000  ? 110 HIS A O   1 
ATOM   491   C  CB  . HIS A  1 79  ? -19.90200 -60.47500 -25.53900 1.000 44.66000  ? 110 HIS A CB  1 
ATOM   492   C  CG  . HIS A  1 79  ? -19.78100 -59.30100 -24.62100 1.000 47.55000  ? 110 HIS A CG  1 
ATOM   493   N  ND1 . HIS A  1 79  ? -20.87700 -58.58300 -24.18700 1.000 50.45000  ? 110 HIS A ND1 1 
ATOM   494   C  CD2 . HIS A  1 79  ? -18.69700 -58.70200 -24.07300 1.000 44.40000  ? 110 HIS A CD2 1 
ATOM   495   C  CE1 . HIS A  1 79  ? -20.47100 -57.59400 -23.40900 1.000 48.57000  ? 110 HIS A CE1 1 
ATOM   496   N  NE2 . HIS A  1 79  ? -19.15300 -57.64700 -23.32200 1.000 46.98000  ? 110 HIS A NE2 1 
ATOM   497   N  N   . LEU A  1 80  ? -22.08900 -61.25100 -27.98600 1.000 51.46000  ? 111 LEU A N   1 
ATOM   498   C  CA  . LEU A  1 80  ? -22.78000 -62.33400 -28.66500 1.000 54.83000  ? 111 LEU A CA  1 
ATOM   499   C  C   . LEU A  1 80  ? -22.90100 -62.11000 -30.16000 1.000 52.75000  ? 111 LEU A C   1 
ATOM   500   O  O   . LEU A  1 80  ? -23.10300 -63.07800 -30.89700 1.000 60.14000  ? 111 LEU A O   1 
ATOM   501   C  CB  . LEU A  1 80  ? -24.15700 -62.51700 -28.00900 1.000 59.13000  ? 111 LEU A CB  1 
ATOM   502   C  CG  . LEU A  1 80  ? -23.93900 -63.26100 -26.68100 1.000 59.87000  ? 111 LEU A CG  1 
ATOM   503   C  CD1 . LEU A  1 80  ? -25.03800 -63.02200 -25.71500 1.000 61.84000  ? 111 LEU A CD1 1 
ATOM   504   C  CD2 . LEU A  1 80  ? -23.92900 -64.75700 -27.01000 1.000 56.36000  ? 111 LEU A CD2 1 
ATOM   505   N  N   . THR A  1 81  ? -22.75900 -60.86400 -30.61200 1.000 51.93000  ? 112 THR A N   1 
ATOM   506   C  CA  . THR A  1 81  ? -22.81000 -60.48500 -32.01900 1.000 45.71000  ? 112 THR A CA  1 
ATOM   507   C  C   . THR A  1 81  ? -21.43900 -60.14100 -32.58900 1.000 53.35000  ? 112 THR A C   1 
ATOM   508   O  O   . THR A  1 81  ? -21.35000 -59.75800 -33.75900 1.000 49.66000  ? 112 THR A O   1 
ATOM   509   C  CB  . THR A  1 81  ? -23.77000 -59.30400 -32.20600 1.000 46.40000  ? 112 THR A CB  1 
ATOM   510   O  OG1 . THR A  1 81  ? -23.35100 -58.20200 -31.39300 1.000 49.49000  ? 112 THR A OG1 1 
ATOM   511   C  CG2 . THR A  1 81  ? -25.18800 -59.69700 -31.78800 1.000 53.76000  ? 112 THR A CG2 1 
ATOM   512   N  N   . GLY A  1 82  ? -20.38600 -60.17100 -31.76900 1.000 49.28000  ? 113 GLY A N   1 
ATOM   513   C  CA  . GLY A  1 82  ? -19.05000 -59.87600 -32.24700 1.000 47.57000  ? 113 GLY A CA  1 
ATOM   514   C  C   . GLY A  1 82  ? -18.68000 -58.41500 -32.36600 1.000 47.44000  ? 113 GLY A C   1 
ATOM   515   O  O   . GLY A  1 82  ? -17.70400 -58.09500 -33.05000 1.000 42.93000  ? 113 GLY A O   1 
ATOM   516   N  N   . THR A  1 83  ? -19.43000 -57.50800 -31.73600 1.000 46.62000  ? 114 THR A N   1 
ATOM   517   C  CA  . THR A  1 83  ? -19.28100 -56.07800 -31.98900 1.000 42.46000  ? 114 THR A CA  1 
ATOM   518   C  C   . THR A  1 83  ? -18.85900 -55.31800 -30.73100 1.000 43.66000  ? 114 THR A C   1 
ATOM   519   O  O   . THR A  1 83  ? -19.17100 -54.12900 -30.57400 1.000 41.18000  ? 114 THR A O   1 
ATOM   520   C  CB  . THR A  1 83  ? -20.58200 -55.51000 -32.56400 1.000 44.66000  ? 114 THR A CB  1 
ATOM   521   O  OG1 . THR A  1 83  ? -21.66900 -55.83200 -31.68800 1.000 47.57000  ? 114 THR A OG1 1 
ATOM   522   C  CG2 . THR A  1 83  ? -20.89800 -56.11400 -33.93200 1.000 43.63000  ? 114 THR A CG2 1 
ATOM   523   N  N   . ALA A  1 84  ? -18.07600 -55.96500 -29.86400 1.000 41.32000  ? 115 ALA A N   1 
ATOM   524   C  CA  . ALA A  1 84  ? -17.69000 -55.36200 -28.59100 1.000 41.02000  ? 115 ALA A CA  1 
ATOM   525   C  C   . ALA A  1 84  ? -16.47300 -54.44700 -28.68500 1.000 39.50000  ? 115 ALA A C   1 
ATOM   526   O  O   . ALA A  1 84  ? -16.02000 -53.96100 -27.64000 1.000 44.39000  ? 115 ALA A O   1 
ATOM   527   C  CB  . ALA A  1 84  ? -17.43000 -56.43100 -27.53100 1.000 38.40000  ? 115 ALA A CB  1 
ATOM   528   N  N   . TYR A  1 85  ? -15.91300 -54.21000 -29.87200 1.000 32.61000  ? 116 TYR A N   1 
ATOM   529   C  CA  . TYR A  1 85  ? -14.94900 -53.13200 -30.05300 1.000 36.83000  ? 116 TYR A CA  1 
ATOM   530   C  C   . TYR A  1 85  ? -15.53600 -52.06200 -30.96800 1.000 42.60000  ? 116 TYR A C   1 
ATOM   531   O  O   . TYR A  1 85  ? -16.36400 -52.35500 -31.84500 1.000 43.79000  ? 116 TYR A O   1 
ATOM   532   C  CB  . TYR A  1 85  ? -13.63300 -53.63300 -30.66100 1.000 41.46000  ? 116 TYR A CB  1 
ATOM   533   C  CG  . TYR A  1 85  ? -12.76700 -54.47500 -29.75400 1.000 41.22000  ? 116 TYR A CG  1 
ATOM   534   C  CD1 . TYR A  1 85  ? -11.78500 -53.89900 -28.94100 1.000 38.15000  ? 116 TYR A CD1 1 
ATOM   535   C  CD2 . TYR A  1 85  ? -12.90500 -55.85300 -29.73500 1.000 38.18000  ? 116 TYR A CD2 1 
ATOM   536   C  CE1 . TYR A  1 85  ? -10.98500 -54.68300 -28.13800 1.000 35.43000  ? 116 TYR A CE1 1 
ATOM   537   C  CE2 . TYR A  1 85  ? -12.11000 -56.64000 -28.93900 1.000 42.98000  ? 116 TYR A CE2 1 
ATOM   538   C  CZ  . TYR A  1 85  ? -11.14800 -56.06000 -28.14200 1.000 40.51000  ? 116 TYR A CZ  1 
ATOM   539   O  OH  . TYR A  1 85  ? -10.37300 -56.87400 -27.33200 1.000 42.57000  ? 116 TYR A OH  1 
ATOM   540   N  N   . ASN A  1 86  ? -15.08200 -50.82000 -30.78200 1.000 42.24000  ? 117 ASN A N   1 
ATOM   541   C  CA  . ASN A  1 86  ? -15.48000 -49.74100 -31.68200 1.000 41.12000  ? 117 ASN A CA  1 
ATOM   542   C  C   . ASN A  1 86  ? -14.92700 -49.97500 -33.07700 1.000 42.73000  ? 117 ASN A C   1 
ATOM   543   O  O   . ASN A  1 86  ? -13.82600 -50.50100 -33.25400 1.000 44.07000  ? 117 ASN A O   1 
ATOM   544   C  CB  . ASN A  1 86  ? -14.93000 -48.39300 -31.21800 1.000 44.66000  ? 117 ASN A CB  1 
ATOM   545   C  CG  . ASN A  1 86  ? -15.85400 -47.66600 -30.27800 1.000 43.44000  ? 117 ASN A CG  1 
ATOM   546   O  OD1 . ASN A  1 86  ? -17.01900 -48.02700 -30.11700 1.000 40.21000  ? 117 ASN A OD1 1 
ATOM   547   N  ND2 . ASN A  1 86  ? -15.33700 -46.61200 -29.65500 1.000 42.11000  ? 117 ASN A ND2 1 
ATOM   548   N  N   . LEU A  1 87  ? -15.67600 -49.53400 -34.07400 1.000 49.66000  ? 118 LEU A N   1 
ATOM   549   C  CA  . LEU A  1 87  ? -15.08900 -49.37100 -35.39300 1.000 47.94000  ? 118 LEU A CA  1 
ATOM   550   C  C   . LEU A  1 87  ? -14.10800 -48.21400 -35.35000 1.000 40.37000  ? 118 LEU A C   1 
ATOM   551   O  O   . LEU A  1 87  ? -14.39000 -47.16700 -34.76800 1.000 41.40000  ? 118 LEU A O   1 
ATOM   552   C  CB  . LEU A  1 87  ? -16.16900 -49.10500 -36.43700 1.000 39.55000  ? 118 LEU A CB  1 
ATOM   553   C  CG  . LEU A  1 87  ? -17.09300 -50.29900 -36.66800 1.000 46.14000  ? 118 LEU A CG  1 
ATOM   554   C  CD1 . LEU A  1 87  ? -18.36400 -49.83100 -37.37700 1.000 42.65000  ? 118 LEU A CD1 1 
ATOM   555   C  CD2 . LEU A  1 87  ? -16.40700 -51.42400 -37.44500 1.000 42.46000  ? 118 LEU A CD2 1 
ATOM   556   N  N   . PHE A  1 88  ? -12.93900 -48.41100 -35.94300 1.000 46.31000  ? 119 PHE A N   1 
ATOM   557   C  CA  . PHE A  1 88  ? -11.98300 -47.32200 -36.03400 1.000 42.51000  ? 119 PHE A CA  1 
ATOM   558   C  C   . PHE A  1 88  ? -12.54400 -46.20500 -36.89400 1.000 38.71000  ? 119 PHE A C   1 
ATOM   559   O  O   . PHE A  1 88  ? -13.35600 -46.43100 -37.79600 1.000 48.10000  ? 119 PHE A O   1 
ATOM   560   C  CB  . PHE A  1 88  ? -10.66000 -47.81700 -36.63100 1.000 47.69000  ? 119 PHE A CB  1 
ATOM   561   C  CG  . PHE A  1 88  ? -9.44600  -47.07500 -36.11500 1.000 40.89000  ? 119 PHE A CG  1 
ATOM   562   C  CD1 . PHE A  1 88  ? -8.92000  -47.36100 -34.85700 1.000 42.24000  ? 119 PHE A CD1 1 
ATOM   563   C  CD2 . PHE A  1 88  ? -8.83600  -46.10000 -36.88400 1.000 37.34000  ? 119 PHE A CD2 1 
ATOM   564   C  CE1 . PHE A  1 88  ? -7.79700  -46.67200 -34.38200 1.000 44.27000  ? 119 PHE A CE1 1 
ATOM   565   C  CE2 . PHE A  1 88  ? -7.71300  -45.41100 -36.42400 1.000 37.38000  ? 119 PHE A CE2 1 
ATOM   566   C  CZ  . PHE A  1 88  ? -7.19100  -45.70100 -35.16900 1.000 36.51000  ? 119 PHE A CZ  1 
ATOM   567   N  N   . HIS A  1 89  ? -12.08800 -44.98900 -36.63900 1.000 35.74000  ? 120 HIS A N   1 
ATOM   568   C  CA  . HIS A  1 89  ? -12.52400 -43.89800 -37.48900 1.000 40.93000  ? 120 HIS A CA  1 
ATOM   569   C  C   . HIS A  1 89  ? -12.10800 -44.16700 -38.94500 1.000 45.05000  ? 120 HIS A C   1 
ATOM   570   O  O   . HIS A  1 89  ? -11.10200 -44.83300 -39.22100 1.000 45.45000  ? 120 HIS A O   1 
ATOM   571   C  CB  . HIS A  1 89  ? -11.96300 -42.57300 -36.98000 1.000 41.37000  ? 120 HIS A CB  1 
ATOM   572   C  CG  . HIS A  1 89  ? -10.52000 -42.35300 -37.30000 1.000 44.46000  ? 120 HIS A CG  1 
ATOM   573   N  ND1 . HIS A  1 89  ? -10.09900 -41.80600 -38.49600 1.000 52.96000  ? 120 HIS A ND1 1 
ATOM   574   C  CD2 . HIS A  1 89  ? -9.39900  -42.55700 -36.56700 1.000 50.95000  ? 120 HIS A CD2 1 
ATOM   575   C  CE1 . HIS A  1 89  ? -8.78100  -41.71300 -38.49900 1.000 52.32000  ? 120 HIS A CE1 1 
ATOM   576   N  NE2 . HIS A  1 89  ? -8.33000  -42.15300 -37.33600 1.000 50.97000  ? 120 HIS A NE2 1 
ATOM   577   N  N   . ASN A  1 90  ? -12.92800 -43.68100 -39.88100 1.000 40.32000  ? 121 ASN A N   1 
ATOM   578   C  CA  . ASN A  1 90  ? -12.72800 -43.90100 -41.32000 1.000 48.34000  ? 121 ASN A CA  1 
ATOM   579   C  C   . ASN A  1 90  ? -12.66000 -45.38700 -41.66600 1.000 50.09000  ? 121 ASN A C   1 
ATOM   580   O  O   . ASN A  1 90  ? -11.86200 -45.80000 -42.50500 1.000 45.03000  ? 121 ASN A O   1 
ATOM   581   C  CB  . ASN A  1 90  ? -11.46000 -43.18700 -41.81200 1.000 42.59000  ? 121 ASN A CB  1 
ATOM   582   C  CG  . ASN A  1 90  ? -11.54300 -41.67500 -41.65300 1.000 46.73000  ? 121 ASN A CG  1 
ATOM   583   O  OD1 . ASN A  1 90  ? -11.42200 -41.14500 -40.53900 1.000 54.63000  ? 121 ASN A OD1 1 
ATOM   584   N  ND2 . ASN A  1 90  ? -11.72500 -40.97000 -42.76300 1.000 44.40000  ? 121 ASN A ND2 1 
ATOM   585   N  N   . SER A  1 91  ? -13.50100 -46.19700 -41.01800 1.000 45.30000  ? 122 SER A N   1 
ATOM   586   C  CA  . SER A  1 91  ? -13.48700 -47.63300 -41.26300 1.000 41.44000  ? 122 SER A CA  1 
ATOM   587   C  C   . SER A  1 91  ? -13.99700 -47.93100 -42.67800 1.000 43.10000  ? 122 SER A C   1 
ATOM   588   O  O   . SER A  1 91  ? -14.61000 -47.08900 -43.34500 1.000 46.63000  ? 122 SER A O   1 
ATOM   589   C  CB  . SER A  1 91  ? -14.29600 -48.37700 -40.19400 1.000 41.79000  ? 122 SER A CB  1 
ATOM   590   O  OG  . SER A  1 91  ? -15.67400 -48.00200 -40.21500 1.000 44.72000  ? 122 SER A OG  1 
ATOM   591   N  N   . SER A  1 92  ? -13.73800 -49.15700 -43.12300 1.000 49.85000  ? 123 SER A N   1 
ATOM   592   C  CA  . SER A  1 92  ? -13.90800 -49.51900 -44.52600 1.000 45.54000  ? 123 SER A CA  1 
ATOM   593   C  C   . SER A  1 92  ? -15.32900 -49.31100 -45.02200 1.000 48.72000  ? 123 SER A C   1 
ATOM   594   O  O   . SER A  1 92  ? -16.29500 -49.75500 -44.39800 1.000 50.48000  ? 123 SER A O   1 
ATOM   595   C  CB  . SER A  1 92  ? -13.52400 -50.97300 -44.71900 1.000 47.73000  ? 123 SER A CB  1 
ATOM   596   O  OG  . SER A  1 92  ? -13.90600 -51.38900 -45.99700 1.000 61.49000  ? 123 SER A OG  1 
ATOM   597   N  N   . GLU A  1 93  ? -15.43700 -48.73200 -46.21700 1.000 52.27000  ? 124 GLU A N   1 
ATOM   598   C  CA  . GLU A  1 93  ? -16.71200 -48.46200 -46.86200 1.000 49.58000  ? 124 GLU A CA  1 
ATOM   599   C  C   . GLU A  1 93  ? -17.05200 -49.47600 -47.93600 1.000 52.00000  ? 124 GLU A C   1 
ATOM   600   O  O   . GLU A  1 93  ? -18.00200 -49.26300 -48.69600 1.000 55.20000  ? 124 GLU A O   1 
ATOM   601   C  CB  . GLU A  1 93  ? -16.71400 -47.05300 -47.43400 1.000 43.59000  ? 124 GLU A CB  1 
ATOM   602   C  CG  . GLU A  1 93  ? -16.37100 -46.04100 -46.37400 1.000 52.24000  ? 124 GLU A CG  1 
ATOM   603   C  CD  . GLU A  1 93  ? -16.79700 -44.63900 -46.72600 1.000 60.78000  ? 124 GLU A CD  1 
ATOM   604   O  OE1 . GLU A  1 93  ? -17.63600 -44.49600 -47.64100 1.000 66.20000  ? 124 GLU A OE1 1 
ATOM   605   O  OE2 . GLU A  1 93  ? -16.33800 -43.68400 -46.05100 1.000 65.67000  ? 124 GLU A OE2 1 
ATOM   606   N  N   . ASP A  1 94  ? -16.29800 -50.56800 -48.01700 1.000 54.13000  ? 125 ASP A N   1 
ATOM   607   C  CA  . ASP A  1 94  ? -16.54600 -51.63400 -48.97400 1.000 55.84000  ? 125 ASP A CA  1 
ATOM   608   C  C   . ASP A  1 94  ? -17.23300 -52.78200 -48.25500 1.000 56.55000  ? 125 ASP A C   1 
ATOM   609   O  O   . ASP A  1 94  ? -16.72000 -53.28100 -47.24300 1.000 52.85000  ? 125 ASP A O   1 
ATOM   610   C  CB  . ASP A  1 94  ? -15.24000 -52.10900 -49.62300 1.000 57.05000  ? 125 ASP A CB  1 
ATOM   611   C  CG  . ASP A  1 94  ? -14.47400 -50.96700 -50.29000 1.000 69.05000  ? 125 ASP A CG  1 
ATOM   612   O  OD1 . ASP A  1 94  ? -14.99800 -49.82600 -50.32400 1.000 69.87000  ? 125 ASP A OD1 1 
ATOM   613   O  OD2 . ASP A  1 94  ? -13.34500 -51.19400 -50.77400 1.000 79.34000  ? 125 ASP A OD2 1 
ATOM   614   N  N   . ASP A  1 95  ? -18.38000 -53.21000 -48.80000 1.000 52.33000  ? 126 ASP A N   1 
ATOM   615   C  CA  . ASP A  1 95  ? -19.13700 -54.32000 -48.22100 1.000 54.26000  ? 126 ASP A CA  1 
ATOM   616   C  C   . ASP A  1 95  ? -18.25000 -55.54000 -48.01100 1.000 57.02000  ? 126 ASP A C   1 
ATOM   617   O  O   . ASP A  1 95  ? -18.52900 -56.37700 -47.14300 1.000 59.15000  ? 126 ASP A O   1 
ATOM   618   C  CB  . ASP A  1 95  ? -20.31500 -54.69800 -49.14200 1.000 50.75000  ? 126 ASP A CB  1 
ATOM   619   C  CG  . ASP A  1 95  ? -21.44800 -53.66200 -49.14600 1.000 58.93000  ? 126 ASP A CG  1 
ATOM   620   O  OD1 . ASP A  1 95  ? -21.39000 -52.66800 -48.39100 1.000 58.54000  ? 126 ASP A OD1 1 
ATOM   621   O  OD2 . ASP A  1 95  ? -22.40900 -53.83300 -49.93600 1.000 58.70000  ? 126 ASP A OD2 1 
ATOM   622   N  N   . LYS A  1 96  ? -17.19700 -55.66700 -48.82400 1.000 54.69000  ? 127 LYS A N   1 
ATOM   623   C  CA  . LYS A  1 96  ? -16.30500 -56.82100 -48.75700 1.000 61.75000  ? 127 LYS A CA  1 
ATOM   624   C  C   . LYS A  1 96  ? -15.58000 -56.90600 -47.41700 1.000 54.61000  ? 127 LYS A C   1 
ATOM   625   O  O   . LYS A  1 96  ? -15.36700 -58.00100 -46.89000 1.000 58.24000  ? 127 LYS A O   1 
ATOM   626   C  CB  . LYS A  1 96  ? -15.30400 -56.78000 -49.91900 1.000 61.88000  ? 127 LYS A CB  1 
ATOM   627   N  N   . ASP A  1 97  ? -15.17600 -55.76900 -46.85500 1.000 55.86000  ? 128 ASP A N   1 
ATOM   628   C  CA  . ASP A  1 97  ? -14.44300 -55.79100 -45.59200 1.000 54.28000  ? 128 ASP A CA  1 
ATOM   629   C  C   . ASP A  1 97  ? -15.29600 -56.06000 -44.35500 1.000 50.81000  ? 128 ASP A C   1 
ATOM   630   O  O   . ASP A  1 97  ? -14.71400 -56.31000 -43.29300 1.000 52.43000  ? 128 ASP A O   1 
ATOM   631   C  CB  . ASP A  1 97  ? -13.65700 -54.48300 -45.43000 1.000 50.17000  ? 128 ASP A CB  1 
ATOM   632   C  CG  . ASP A  1 97  ? -12.70200 -54.24200 -46.59100 1.000 52.75000  ? 128 ASP A CG  1 
ATOM   633   O  OD1 . ASP A  1 97  ? -12.09700 -55.23400 -47.03900 1.000 58.61000  ? 128 ASP A OD1 1 
ATOM   634   O  OD2 . ASP A  1 97  ? -12.50000 -53.08800 -47.02500 1.000 56.89000  ? 128 ASP A OD2 1 
ATOM   635   N  N   . ASN A  1 98  ? -16.63100 -56.03000 -44.46800 1.000 51.44000  ? 129 ASN A N   1 
ATOM   636   C  CA  . ASN A  1 98  ? -17.57900 -56.32500 -43.37500 1.000 51.03000  ? 129 ASN A CA  1 
ATOM   637   C  C   . ASN A  1 98  ? -17.27100 -55.58900 -42.07000 1.000 48.30000  ? 129 ASN A C   1 
ATOM   638   O  O   . ASN A  1 98  ? -17.34100 -56.15100 -40.98000 1.000 49.92000  ? 129 ASN A O   1 
ATOM   639   C  CB  . ASN A  1 98  ? -17.63300 -57.83300 -43.11400 1.000 52.26000  ? 129 ASN A CB  1 
ATOM   640   C  CG  . ASN A  1 98  ? -18.40000 -58.57400 -44.17700 1.000 56.21000  ? 129 ASN A CG  1 
ATOM   641   O  OD1 . ASN A  1 98  ? -19.47200 -58.14500 -44.59000 1.000 61.99000  ? 129 ASN A OD1 1 
ATOM   642   N  ND2 . ASN A  1 98  ? -17.85600 -59.68400 -44.63200 1.000 58.94000  ? 129 ASN A ND2 1 
ATOM   643   N  N   . MET A  1 99  ? -16.97900 -54.30100 -42.17800 1.000 49.54000  ? 130 MET A N   1 
ATOM   644   C  CA  . MET A  1 99  ? -16.74000 -53.46200 -41.00700 1.000 43.97000  ? 130 MET A CA  1 
ATOM   645   C  C   . MET A  1 99  ? -18.08300 -52.84400 -40.59000 1.000 46.65000  ? 130 MET A C   1 
ATOM   646   O  O   . MET A  1 99  ? -18.39300 -51.68200 -40.88600 1.000 43.09000  ? 130 MET A O   1 
ATOM   647   C  CB  . MET A  1 99  ? -15.66200 -52.42900 -41.30600 1.000 46.28000  ? 130 MET A CB  1 
ATOM   648   C  CG  . MET A  1 99  ? -14.20300 -52.98700 -41.32200 1.000 55.69000  ? 130 MET A CG  1 
ATOM   649   S  SD  . MET A  1 99  ? -13.69500 -53.88700 -39.81800 1.000 60.37000  ? 130 MET A SD  1 
ATOM   650   C  CE  . MET A  1 99  ? -12.12500 -54.58300 -40.31200 1.000 54.89000  ? 130 MET A CE  1 
ATOM   651   N  N   . GLY A  1 100 ? -18.92100 -53.67100 -39.95900 1.000 40.46000  ? 131 GLY A N   1 
ATOM   652   C  CA  . GLY A  1 100 ? -20.23100 -53.22800 -39.51500 1.000 42.54000  ? 131 GLY A CA  1 
ATOM   653   C  C   . GLY A  1 100 ? -20.94700 -54.34200 -38.78900 1.000 42.96000  ? 131 GLY A C   1 
ATOM   654   O  O   . GLY A  1 100 ? -20.54900 -55.50700 -38.84400 1.000 44.78000  ? 131 GLY A O   1 
ATOM   655   N  N   . VAL A  1 101 ? -22.02600 -53.96600 -38.10400 1.000 47.29000  ? 132 VAL A N   1 
ATOM   656   C  CA  . VAL A  1 101 ? -22.82200 -54.95900 -37.35700 1.000 47.32000  ? 132 VAL A CA  1 
ATOM   657   C  C   . VAL A  1 101 ? -23.37400 -56.00200 -38.32800 1.000 48.21000  ? 132 VAL A C   1 
ATOM   658   O  O   . VAL A  1 101 ? -23.86800 -55.63100 -39.41000 1.000 42.54000  ? 132 VAL A O   1 
ATOM   659   C  CB  . VAL A  1 101 ? -23.96700 -54.27500 -36.60300 1.000 43.89000  ? 132 VAL A CB  1 
ATOM   660   C  CG1 . VAL A  1 101 ? -24.78600 -55.31900 -35.83100 1.000 43.76000  ? 132 VAL A CG1 1 
ATOM   661   C  CG2 . VAL A  1 101 ? -23.42400 -53.18700 -35.69100 1.000 42.55000  ? 132 VAL A CG2 1 
ATOM   662   N  N   . PRO A  1 102 ? -23.26100 -57.29900 -38.03000 1.000 47.66000  ? 133 PRO A N   1 
ATOM   663   C  CA  . PRO A  1 102 ? -23.75500 -58.33800 -38.95600 1.000 53.71000  ? 133 PRO A CA  1 
ATOM   664   C  C   . PRO A  1 102 ? -25.15300 -58.04000 -39.47600 1.000 48.21000  ? 133 PRO A C   1 
ATOM   665   O  O   . PRO A  1 102 ? -26.06000 -57.70300 -38.71300 1.000 45.76000  ? 133 PRO A O   1 
ATOM   666   C  CB  . PRO A  1 102 ? -23.74900 -59.61300 -38.10100 1.000 53.63000  ? 133 PRO A CB  1 
ATOM   667   C  CG  . PRO A  1 102 ? -22.69500 -59.36600 -37.03600 1.000 50.01000  ? 133 PRO A CG  1 
ATOM   668   C  CD  . PRO A  1 102 ? -22.58100 -57.86300 -36.85000 1.000 44.63000  ? 133 PRO A CD  1 
ATOM   669   N  N   . VAL A  1 103 ? -25.32700 -58.15900 -40.79500 1.000 54.04000  ? 134 VAL A N   1 
ATOM   670   C  CA  . VAL A  1 103 ? -26.61600 -57.80300 -41.37900 1.000 53.17000  ? 134 VAL A CA  1 
ATOM   671   C  C   . VAL A  1 103 ? -27.68300 -58.83500 -41.05600 1.000 51.95000  ? 134 VAL A C   1 
ATOM   672   O  O   . VAL A  1 103 ? -28.87300 -58.55400 -41.21200 1.000 52.66000  ? 134 VAL A O   1 
ATOM   673   C  CB  . VAL A  1 103 ? -26.50100 -57.59100 -42.89800 1.000 51.11000  ? 134 VAL A CB  1 
ATOM   674   C  CG1 . VAL A  1 103 ? -25.48700 -56.48700 -43.20800 1.000 53.68000  ? 134 VAL A CG1 1 
ATOM   675   C  CG2 . VAL A  1 103 ? -26.13100 -58.87500 -43.58800 1.000 52.83000  ? 134 VAL A CG2 1 
ATOM   676   N  N   . GLU A  1 104 ? -27.29300 -60.04000 -40.64000 1.000 51.71000  ? 135 GLU A N   1 
ATOM   677   C  CA  . GLU A  1 104 ? -28.27800 -61.05400 -40.27900 1.000 55.85000  ? 135 GLU A CA  1 
ATOM   678   C  C   . GLU A  1 104 ? -28.95000 -60.76200 -38.94800 1.000 57.59000  ? 135 GLU A C   1 
ATOM   679   O  O   . GLU A  1 104 ? -30.00100 -61.34500 -38.66100 1.000 57.22000  ? 135 GLU A O   1 
ATOM   680   C  CB  . GLU A  1 104 ? -27.63000 -62.44200 -40.25100 1.000 58.63000  ? 135 GLU A CB  1 
ATOM   681   C  CG  . GLU A  1 104 ? -26.57200 -62.64000 -41.34700 1.000 67.12000  ? 135 GLU A CG  1 
ATOM   682   C  CD  . GLU A  1 104 ? -25.17500 -62.15500 -40.91800 1.000 70.16000  ? 135 GLU A CD  1 
ATOM   683   O  OE1 . GLU A  1 104 ? -24.68100 -62.63800 -39.87200 1.000 80.71000  ? 135 GLU A OE1 1 
ATOM   684   O  OE2 . GLU A  1 104 ? -24.57300 -61.29400 -41.60800 1.000 65.16000  ? 135 GLU A OE2 1 
ATOM   685   N  N   . GLU A  1 105 ? -28.33800 -59.92800 -38.10700 1.000 52.96000  ? 136 GLU A N   1 
ATOM   686   C  CA  . GLU A  1 105 ? -28.89200 -59.56300 -36.80200 1.000 58.44000  ? 136 GLU A CA  1 
ATOM   687   C  C   . GLU A  1 105 ? -29.90100 -58.42800 -36.99900 1.000 56.88000  ? 136 GLU A C   1 
ATOM   688   O  O   . GLU A  1 105 ? -29.53000 -57.25300 -37.06300 1.000 57.19000  ? 136 GLU A O   1 
ATOM   689   C  CB  . GLU A  1 105 ? -27.76600 -59.17200 -35.84600 1.000 47.86000  ? 136 GLU A CB  1 
ATOM   690   C  CG  . GLU A  1 105 ? -28.15900 -59.25900 -34.38800 1.000 55.08000  ? 136 GLU A CG  1 
ATOM   691   C  CD  . GLU A  1 105 ? -28.58300 -60.65200 -33.95400 1.000 49.76000  ? 136 GLU A CD  1 
ATOM   692   O  OE1 . GLU A  1 105 ? -27.70200 -61.52900 -33.81400 1.000 57.33000  ? 136 GLU A OE1 1 
ATOM   693   O  OE2 . GLU A  1 105 ? -29.79700 -60.88000 -33.77500 1.000 54.77000  ? 136 GLU A OE2 1 
ATOM   694   N  N   . THR A  1 106 ? -31.19100 -58.76300 -37.03800 1.000 50.11000  ? 137 THR A N   1 
ATOM   695   C  CA  . THR A  1 106 ? -32.19700 -57.79800 -37.46800 1.000 50.14000  ? 137 THR A CA  1 
ATOM   696   C  C   . THR A  1 106 ? -32.38900 -56.69100 -36.43200 1.000 45.44000  ? 137 THR A C   1 
ATOM   697   O  O   . THR A  1 106 ? -32.54700 -56.96200 -35.24100 1.000 45.40000  ? 137 THR A O   1 
ATOM   698   C  CB  . THR A  1 106 ? -33.52100 -58.51700 -37.74600 1.000 53.78000  ? 137 THR A CB  1 
ATOM   699   O  OG1 . THR A  1 106 ? -33.26500 -59.66400 -38.55800 1.000 52.75000  ? 137 THR A OG1 1 
ATOM   700   C  CG2 . THR A  1 106 ? -34.50200 -57.60300 -38.49500 1.000 42.44000  ? 137 THR A CG2 1 
ATOM   701   N  N   . TYR A  1 107 ? -32.32600 -55.43800 -36.88700 1.000 50.50000  ? 138 TYR A N   1 
ATOM   702   C  CA  . TYR A  1 107 ? -32.56800 -54.29000 -36.02000 1.000 43.42000  ? 138 TYR A CA  1 
ATOM   703   C  C   . TYR A  1 107 ? -34.05300 -54.14400 -35.69700 1.000 54.03000  ? 138 TYR A C   1 
ATOM   704   O  O   . TYR A  1 107 ? -34.93000 -54.46600 -36.50800 1.000 48.10000  ? 138 TYR A O   1 
ATOM   705   C  CB  . TYR A  1 107 ? -32.09700 -52.99900 -36.69200 1.000 46.21000  ? 138 TYR A CB  1 
ATOM   706   C  CG  . TYR A  1 107 ? -30.58600 -52.81500 -36.81800 1.000 44.97000  ? 138 TYR A CG  1 
ATOM   707   C  CD1 . TYR A  1 107 ? -29.70500 -53.79700 -36.40800 1.000 42.55000  ? 138 TYR A CD1 1 
ATOM   708   C  CD2 . TYR A  1 107 ? -30.05600 -51.65000 -37.37400 1.000 45.89000  ? 138 TYR A CD2 1 
ATOM   709   C  CE1 . TYR A  1 107 ? -28.33000 -53.62900 -36.53000 1.000 46.73000  ? 138 TYR A CE1 1 
ATOM   710   C  CE2 . TYR A  1 107 ? -28.66900 -51.47100 -37.51000 1.000 46.07000  ? 138 TYR A CE2 1 
ATOM   711   C  CZ  . TYR A  1 107 ? -27.82100 -52.46900 -37.09200 1.000 42.93000  ? 138 TYR A CZ  1 
ATOM   712   O  OH  . TYR A  1 107 ? -26.46200 -52.30700 -37.21700 1.000 45.11000  ? 138 TYR A OH  1 
ATOM   713   N  N   . MET A  1 108 ? -34.33500 -53.56600 -34.53000 1.000 49.95000  ? 139 MET A N   1 
ATOM   714   C  CA  . MET A  1 108 ? -35.72100 -53.28900 -34.19000 1.000 49.26000  ? 139 MET A CA  1 
ATOM   715   C  C   . MET A  1 108 ? -36.35100 -52.28200 -35.13900 1.000 49.94000  ? 139 MET A C   1 
ATOM   716   O  O   . MET A  1 108 ? -37.57900 -52.22200 -35.23500 1.000 52.64000  ? 139 MET A O   1 
ATOM   717   C  CB  . MET A  1 108 ? -35.81600 -52.76900 -32.77500 1.000 44.58000  ? 139 MET A CB  1 
ATOM   718   C  CG  . MET A  1 108 ? -35.07000 -51.49100 -32.55800 1.000 49.48000  ? 139 MET A CG  1 
ATOM   719   S  SD  . MET A  1 108 ? -35.43500 -50.95300 -30.89100 1.000 47.31000  ? 139 MET A SD  1 
ATOM   720   C  CE  . MET A  1 108 ? -34.20100 -49.68500 -30.58300 1.000 41.23000  ? 139 MET A CE  1 
ATOM   721   N  N   . SER A  1 109 ? -35.54600 -51.48800 -35.83700 1.000 47.92000  ? 140 SER A N   1 
ATOM   722   C  CA  . SER A  1 109 ? -36.10900 -50.57100 -36.82100 1.000 48.53000  ? 140 SER A CA  1 
ATOM   723   C  C   . SER A  1 109 ? -36.75700 -51.33100 -37.97400 1.000 46.98000  ? 140 SER A C   1 
ATOM   724   O  O   . SER A  1 109 ? -37.84100 -50.95700 -38.44400 1.000 46.35000  ? 140 SER A O   1 
ATOM   725   C  CB  . SER A  1 109 ? -35.02100 -49.63500 -37.35000 1.000 47.72000  ? 140 SER A CB  1 
ATOM   726   O  OG  . SER A  1 109 ? -33.83300 -50.35500 -37.65900 1.000 43.86000  ? 140 SER A OG  1 
ATOM   727   N  N   . LYS A  1 110 ? -36.09500 -52.38100 -38.46200 1.000 48.73000  ? 141 LYS A N   1 
ATOM   728   C  CA  . LYS A  1 110 ? -36.68400 -53.18800 -39.52600 1.000 48.34000  ? 141 LYS A CA  1 
ATOM   729   C  C   . LYS A  1 110 ? -37.95000 -53.89100 -39.04800 1.000 45.46000  ? 141 LYS A C   1 
ATOM   730   O  O   . LYS A  1 110 ? -38.96900 -53.89900 -39.75200 1.000 43.97000  ? 141 LYS A O   1 
ATOM   731   C  CB  . LYS A  1 110 ? -35.66800 -54.19700 -40.05200 1.000 47.51000  ? 141 LYS A CB  1 
ATOM   732   C  CG  . LYS A  1 110 ? -36.16000 -54.88300 -41.33800 1.000 48.82000  ? 141 LYS A CG  1 
ATOM   733   C  CD  . LYS A  1 110 ? -35.01600 -55.46600 -42.12200 1.000 53.19000  ? 141 LYS A CD  1 
ATOM   734   C  CE  . LYS A  1 110 ? -35.08700 -54.97900 -43.55500 1.000 63.45000  ? 141 LYS A CE  1 
ATOM   735   N  NZ  . LYS A  1 110 ? -36.46000 -55.13200 -44.12900 1.000 68.55000  ? 141 LYS A NZ  1 
ATOM   736   N  N   . VAL A  1 111 ? -37.90700 -54.47000 -37.84300 1.000 42.97000  ? 142 VAL A N   1 
ATOM   737   C  CA  . VAL A  1 111 ? -39.09900 -55.09800 -37.27400 1.000 48.27000  ? 142 VAL A CA  1 
ATOM   738   C  C   . VAL A  1 111 ? -40.23400 -54.08800 -37.19400 1.000 47.69000  ? 142 VAL A C   1 
ATOM   739   O  O   . VAL A  1 111 ? -41.37300 -54.36900 -37.58100 1.000 50.36000  ? 142 VAL A O   1 
ATOM   740   C  CB  . VAL A  1 111 ? -38.79700 -55.68900 -35.88900 1.000 48.23000  ? 142 VAL A CB  1 
ATOM   741   C  CG1 . VAL A  1 111 ? -40.06000 -56.25300 -35.31100 1.000 52.06000  ? 142 VAL A CG1 1 
ATOM   742   C  CG2 . VAL A  1 111 ? -37.72000 -56.74600 -35.97700 1.000 48.99000  ? 142 VAL A CG2 1 
ATOM   743   N  N   . LEU A  1 112 ? -39.94200 -52.89300 -36.69400 1.000 46.06000  ? 143 LEU A N   1 
ATOM   744   C  CA  . LEU A  1 112 ? -40.98900 -51.88100 -36.64200 1.000 48.23000  ? 143 LEU A CA  1 
ATOM   745   C  C   . LEU A  1 112 ? -41.38700 -51.43000 -38.03600 1.000 51.90000  ? 143 LEU A C   1 
ATOM   746   O  O   . LEU A  1 112 ? -42.57800 -51.19800 -38.29800 1.000 53.86000  ? 143 LEU A O   1 
ATOM   747   C  CB  . LEU A  1 112 ? -40.55400 -50.72200 -35.74700 1.000 51.29000  ? 143 LEU A CB  1 
ATOM   748   C  CG  . LEU A  1 112 ? -41.16000 -50.85800 -34.33600 1.000 54.61000  ? 143 LEU A CG  1 
ATOM   749   C  CD1 . LEU A  1 112 ? -40.86700 -52.18400 -33.64800 1.000 41.77000  ? 143 LEU A CD1 1 
ATOM   750   C  CD2 . LEU A  1 112 ? -40.72500 -49.69400 -33.46000 1.000 57.00000  ? 143 LEU A CD2 1 
ATOM   751   N  N   . GLN A  1 113 ? -40.42700 -51.38200 -38.95800 1.000 50.08000  ? 144 GLN A N   1 
ATOM   752   C  CA  . GLN A  1 113 ? -40.73800 -51.02300 -40.33800 1.000 48.56000  ? 144 GLN A CA  1 
ATOM   753   C  C   . GLN A  1 113 ? -41.72400 -52.01300 -40.94800 1.000 49.98000  ? 144 GLN A C   1 
ATOM   754   O  O   . GLN A  1 113 ? -42.73200 -51.62000 -41.55000 1.000 48.71000  ? 144 GLN A O   1 
ATOM   755   C  CB  . GLN A  1 113 ? -39.44800 -50.98500 -41.16800 1.000 44.76000  ? 144 GLN A CB  1 
ATOM   756   C  CG  . GLN A  1 113 ? -39.66900 -50.59200 -42.62700 1.000 52.45000  ? 144 GLN A CG  1 
ATOM   757   C  CD  . GLN A  1 113 ? -38.38700 -50.54300 -43.44200 1.000 46.47000  ? 144 GLN A CD  1 
ATOM   758   O  OE1 . GLN A  1 113 ? -37.70000 -51.55500 -43.62700 1.000 54.99000  ? 144 GLN A OE1 1 
ATOM   759   N  NE2 . GLN A  1 113 ? -38.05200 -49.35000 -43.92300 1.000 46.85000  ? 144 GLN A NE2 1 
ATOM   760   N  N   . ASN A  1 114 ? -41.43400 -53.30900 -40.80300 1.000 50.61000  ? 145 ASN A N   1 
ATOM   761   C  CA  . ASN A  1 114 ? -42.27100 -54.38900 -41.30500 1.000 51.00000  ? 145 ASN A CA  1 
ATOM   762   C  C   . ASN A  1 114 ? -43.63300 -54.45100 -40.63500 1.000 52.21000  ? 145 ASN A C   1 
ATOM   763   O  O   . ASN A  1 114 ? -44.48600 -55.21800 -41.09300 1.000 55.53000  ? 145 ASN A O   1 
ATOM   764   C  CB  . ASN A  1 114 ? -41.53400 -55.72800 -41.13200 1.000 49.04000  ? 145 ASN A CB  1 
ATOM   765   C  CG  . ASN A  1 114 ? -40.35800 -55.89100 -42.11600 1.000 58.53000  ? 145 ASN A CG  1 
ATOM   766   O  OD1 . ASN A  1 114 ? -40.30400 -55.21800 -43.14600 1.000 60.65000  ? 145 ASN A OD1 1 
ATOM   767   N  ND2 . ASN A  1 114 ? -39.40800 -56.76400 -41.78300 1.000 59.72000  ? 145 ASN A ND2 1 
ATOM   768   N  N   . ALA A  1 115 ? -43.84600 -53.71000 -39.54900 1.000 51.59000  ? 146 ALA A N   1 
ATOM   769   C  CA  . ALA A  1 115 ? -45.13300 -53.65800 -38.86600 1.000 53.65000  ? 146 ALA A CA  1 
ATOM   770   C  C   . ALA A  1 115 ? -45.90700 -52.37200 -39.15100 1.000 47.79000  ? 146 ALA A C   1 
ATOM   771   O  O   . ALA A  1 115 ? -46.82700 -52.03200 -38.40200 1.000 51.76000  ? 146 ALA A O   1 
ATOM   772   C  CB  . ALA A  1 115 ? -44.93500 -53.83900 -37.36000 1.000 49.31000  ? 146 ALA A CB  1 
ATOM   773   N  N   . GLY A  1 116 ? -45.52300 -51.62400 -40.18200 1.000 48.33000  ? 147 GLY A N   1 
ATOM   774   C  CA  . GLY A  1 116 ? -46.26500 -50.44600 -40.60400 1.000 42.57000  ? 147 GLY A CA  1 
ATOM   775   C  C   . GLY A  1 116 ? -45.84800 -49.13400 -39.98800 1.000 43.80000  ? 147 GLY A C   1 
ATOM   776   O  O   . GLY A  1 116 ? -46.54000 -48.12600 -40.17900 1.000 45.31000  ? 147 GLY A O   1 
ATOM   777   N  N   . TYR A  1 117 ? -44.71200 -49.09200 -39.30900 1.000 54.45000  ? 148 TYR A N   1 
ATOM   778   C  CA  . TYR A  1 117 ? -44.21500 -47.86000 -38.72500 1.000 47.63000  ? 148 TYR A CA  1 
ATOM   779   C  C   . TYR A  1 117 ? -43.42800 -47.09200 -39.78000 1.000 44.14000  ? 148 TYR A C   1 
ATOM   780   O  O   . TYR A  1 117 ? -42.75100 -47.68900 -40.62500 1.000 44.39000  ? 148 TYR A O   1 
ATOM   781   C  CB  . TYR A  1 117 ? -43.32800 -48.16300 -37.50700 1.000 45.53000  ? 148 TYR A CB  1 
ATOM   782   C  CG  . TYR A  1 117 ? -44.05800 -48.20500 -36.18000 1.000 49.82000  ? 148 TYR A CG  1 
ATOM   783   C  CD1 . TYR A  1 117 ? -44.93800 -49.23700 -35.87000 1.000 48.51000  ? 148 TYR A CD1 1 
ATOM   784   C  CD2 . TYR A  1 117 ? -43.86300 -47.20900 -35.23600 1.000 45.13000  ? 148 TYR A CD2 1 
ATOM   785   C  CE1 . TYR A  1 117 ? -45.61600 -49.26500 -34.64700 1.000 49.03000  ? 148 TYR A CE1 1 
ATOM   786   C  CE2 . TYR A  1 117 ? -44.53500 -47.22700 -34.01200 1.000 41.83000  ? 148 TYR A CE2 1 
ATOM   787   C  CZ  . TYR A  1 117 ? -45.40300 -48.25700 -33.72000 1.000 44.75000  ? 148 TYR A CZ  1 
ATOM   788   O  OH  . TYR A  1 117 ? -46.07100 -48.25100 -32.50900 1.000 40.88000  ? 148 TYR A OH  1 
ATOM   789   N  N   . TYR A  1 118 ? -43.54800 -45.76800 -39.74500 1.000 38.06000  ? 149 TYR A N   1 
ATOM   790   C  CA  . TYR A  1 118 ? -42.61700 -44.89900 -40.45100 1.000 43.24000  ? 149 TYR A CA  1 
ATOM   791   C  C   . TYR A  1 118 ? -41.33600 -44.78100 -39.61200 1.000 41.81000  ? 149 TYR A C   1 
ATOM   792   O  O   . TYR A  1 118 ? -41.39500 -44.36800 -38.45300 1.000 36.16000  ? 149 TYR A O   1 
ATOM   793   C  CB  . TYR A  1 118 ? -43.24600 -43.52700 -40.69900 1.000 39.30000  ? 149 TYR A CB  1 
ATOM   794   C  CG  . TYR A  1 118 ? -42.26400 -42.55000 -41.29200 1.000 42.74000  ? 149 TYR A CG  1 
ATOM   795   C  CD1 . TYR A  1 118 ? -41.87100 -42.66100 -42.62500 1.000 42.22000  ? 149 TYR A CD1 1 
ATOM   796   C  CD2 . TYR A  1 118 ? -41.70200 -41.53700 -40.52200 1.000 43.35000  ? 149 TYR A CD2 1 
ATOM   797   C  CE1 . TYR A  1 118 ? -40.95000 -41.78000 -43.18600 1.000 40.07000  ? 149 TYR A CE1 1 
ATOM   798   C  CE2 . TYR A  1 118 ? -40.76800 -40.65700 -41.06700 1.000 44.99000  ? 149 TYR A CE2 1 
ATOM   799   C  CZ  . TYR A  1 118 ? -40.39700 -40.78400 -42.39800 1.000 43.88000  ? 149 TYR A CZ  1 
ATOM   800   O  OH  . TYR A  1 118 ? -39.48000 -39.90900 -42.94400 1.000 47.31000  ? 149 TYR A OH  1 
ATOM   801   N  N   . THR A  1 119 ? -40.19300 -45.19400 -40.16200 1.000 42.68000  ? 150 THR A N   1 
ATOM   802   C  CA  . THR A  1 119 ? -38.95400 -45.25500 -39.39700 1.000 40.48000  ? 150 THR A CA  1 
ATOM   803   C  C   . THR A  1 119 ? -37.94900 -44.19700 -39.85200 1.000 43.68000  ? 150 THR A C   1 
ATOM   804   O  O   . THR A  1 119 ? -37.78200 -43.95600 -41.05100 1.000 47.31000  ? 150 THR A O   1 
ATOM   805   C  CB  . THR A  1 119 ? -38.32700 -46.63600 -39.49800 1.000 46.33000  ? 150 THR A CB  1 
ATOM   806   O  OG1 . THR A  1 119 ? -38.01600 -46.93300 -40.86800 1.000 43.43000  ? 150 THR A OG1 1 
ATOM   807   C  CG2 . THR A  1 119 ? -39.28900 -47.67600 -38.93400 1.000 40.41000  ? 150 THR A CG2 1 
ATOM   808   N  N   . SER A  1 120 ? -37.24200 -43.60300 -38.88800 1.000 43.71000  ? 151 SER A N   1 
ATOM   809   C  CA  . SER A  1 120 ? -36.32200 -42.50400 -39.15100 1.000 40.60000  ? 151 SER A CA  1 
ATOM   810   C  C   . SER A  1 120 ? -35.14200 -42.58700 -38.18500 1.000 46.44000  ? 151 SER A C   1 
ATOM   811   O  O   . SER A  1 120 ? -35.32100 -42.88100 -36.99700 1.000 43.53000  ? 151 SER A O   1 
ATOM   812   C  CB  . SER A  1 120 ? -37.04700 -41.15600 -39.02700 1.000 40.17000  ? 151 SER A CB  1 
ATOM   813   O  OG  . SER A  1 120 ? -36.17000 -40.09600 -38.68100 1.000 42.32000  ? 151 SER A OG  1 
ATOM   814   N  N   . ALA A  1 121 ? -33.93100 -42.39400 -38.71600 1.000 45.87000  ? 152 ALA A N   1 
ATOM   815   C  CA  . ALA A  1 121 ? -32.70400 -42.30000 -37.92300 1.000 40.98000  ? 152 ALA A CA  1 
ATOM   816   C  C   . ALA A  1 121 ? -32.07000 -40.93600 -38.16900 1.000 41.23000  ? 152 ALA A C   1 
ATOM   817   O  O   . ALA A  1 121 ? -32.06900 -40.44200 -39.30300 1.000 38.32000  ? 152 ALA A O   1 
ATOM   818   C  CB  . ALA A  1 121 ? -31.71200 -43.41500 -38.25600 1.000 39.31000  ? 152 ALA A CB  1 
ATOM   819   N  N   . ILE A  1 122 ? -31.61600 -40.29400 -37.09300 1.000 34.66000  ? 153 ILE A N   1 
ATOM   820   C  CA  . ILE A  1 122 ? -31.06400 -38.94600 -37.13100 1.000 38.45000  ? 153 ILE A CA  1 
ATOM   821   C  C   . ILE A  1 122 ? -29.79800 -38.89500 -36.28400 1.000 41.07000  ? 153 ILE A C   1 
ATOM   822   O  O   . ILE A  1 122 ? -29.74000 -39.47300 -35.19000 1.000 38.54000  ? 153 ILE A O   1 
ATOM   823   C  CB  . ILE A  1 122 ? -32.08200 -37.90400 -36.62500 1.000 39.43000  ? 153 ILE A CB  1 
ATOM   824   C  CG1 . ILE A  1 122 ? -33.35200 -37.96100 -37.44900 1.000 40.04000  ? 153 ILE A CG1 1 
ATOM   825   C  CG2 . ILE A  1 122 ? -31.51400 -36.48900 -36.68100 1.000 34.38000  ? 153 ILE A CG2 1 
ATOM   826   C  CD1 . ILE A  1 122 ? -34.48500 -37.27200 -36.78500 1.000 37.62000  ? 153 ILE A CD1 1 
ATOM   827   N  N   . GLY A  1 123 ? -28.79000 -38.20300 -36.77700 1.000 39.94000  ? 154 GLY A N   1 
ATOM   828   C  CA  . GLY A  1 123 ? -27.57900 -37.99000 -36.00300 1.000 32.96000  ? 154 GLY A CA  1 
ATOM   829   C  C   . GLY A  1 123 ? -26.57600 -39.09500 -36.25900 1.000 38.91000  ? 154 GLY A C   1 
ATOM   830   O  O   . GLY A  1 123 ? -26.36700 -39.49400 -37.40100 1.000 38.28000  ? 154 GLY A O   1 
ATOM   831   N  N   . LYS A  1 124 ? -26.00900 -39.62800 -35.17900 1.000 40.04000  ? 155 LYS A N   1 
ATOM   832   C  CA  . LYS A  1 124 ? -24.86700 -40.53500 -35.22200 1.000 40.93000  ? 155 LYS A CA  1 
ATOM   833   C  C   . LYS A  1 124 ? -25.28700 -41.96800 -35.53200 1.000 45.06000  ? 155 LYS A C   1 
ATOM   834   O  O   . LYS A  1 124 ? -26.31600 -42.45200 -35.04200 1.000 37.47000  ? 155 LYS A O   1 
ATOM   835   C  CB  . LYS A  1 124 ? -24.15000 -40.48200 -33.86800 1.000 36.75000  ? 155 LYS A CB  1 
ATOM   836   C  CG  . LYS A  1 124 ? -23.24500 -41.65300 -33.54700 1.000 40.26000  ? 155 LYS A CG  1 
ATOM   837   C  CD  . LYS A  1 124 ? -22.46000 -41.35000 -32.28700 1.000 40.39000  ? 155 LYS A CD  1 
ATOM   838   C  CE  . LYS A  1 124 ? -21.55300 -42.50600 -31.88600 1.000 38.43000  ? 155 LYS A CE  1 
ATOM   839   N  NZ  . LYS A  1 124 ? -20.64600 -41.99700 -30.84400 1.000 35.76000  ? 155 LYS A NZ  1 
ATOM   840   N  N   . TRP A  1 125 ? -24.46600 -42.65900 -36.32300 1.000 38.35000  ? 156 TRP A N   1 
ATOM   841   C  CA  . TRP A  1 125 ? -24.72400 -44.06500 -36.64100 1.000 40.59000  ? 156 TRP A CA  1 
ATOM   842   C  C   . TRP A  1 125 ? -23.67300 -44.95900 -35.98000 1.000 43.13000  ? 156 TRP A C   1 
ATOM   843   O  O   . TRP A  1 125 ? -23.92100 -45.51000 -34.89300 1.000 43.00000  ? 156 TRP A O   1 
ATOM   844   C  CB  . TRP A  1 125 ? -24.77500 -44.26300 -38.16900 1.000 38.60000  ? 156 TRP A CB  1 
ATOM   845   C  CG  . TRP A  1 125 ? -25.17900 -45.65000 -38.65000 1.000 41.35000  ? 156 TRP A CG  1 
ATOM   846   C  CD1 . TRP A  1 125 ? -24.43400 -46.50200 -39.42100 1.000 41.77000  ? 156 TRP A CD1 1 
ATOM   847   C  CD2 . TRP A  1 125 ? -26.42800 -46.32300 -38.41400 1.000 42.93000  ? 156 TRP A CD2 1 
ATOM   848   N  NE1 . TRP A  1 125 ? -25.12900 -47.66000 -39.65800 1.000 39.82000  ? 156 TRP A NE1 1 
ATOM   849   C  CE2 . TRP A  1 125 ? -26.35700 -47.57400 -39.06000 1.000 42.12000  ? 156 TRP A CE2 1 
ATOM   850   C  CE3 . TRP A  1 125 ? -27.59700 -45.98900 -37.71800 1.000 38.26000  ? 156 TRP A CE3 1 
ATOM   851   C  CZ2 . TRP A  1 125 ? -27.41200 -48.48900 -39.03300 1.000 45.07000  ? 156 TRP A CZ2 1 
ATOM   852   C  CZ3 . TRP A  1 125 ? -28.64200 -46.90100 -37.69500 1.000 37.00000  ? 156 TRP A CZ3 1 
ATOM   853   C  CH2 . TRP A  1 125 ? -28.54200 -48.13000 -38.34500 1.000 43.68000  ? 156 TRP A CH2 1 
ATOM   854   N  N   . HIS A  1 126 ? -22.49900 -45.10700 -36.61600 1.000 34.65000  ? 157 HIS A N   1 
ATOM   855   C  CA  . HIS A  1 126 ? -21.35800 -45.85400 -36.07400 1.000 36.96000  ? 157 HIS A CA  1 
ATOM   856   C  C   . HIS A  1 126 ? -21.58100 -47.36800 -36.01500 1.000 36.91000  ? 157 HIS A C   1 
ATOM   857   O  O   . HIS A  1 126 ? -20.96000 -48.07600 -35.19800 1.000 38.97000  ? 157 HIS A O   1 
ATOM   858   C  CB  . HIS A  1 126 ? -20.95900 -45.33900 -34.68600 1.000 39.21000  ? 157 HIS A CB  1 
ATOM   859   C  CG  . HIS A  1 126 ? -19.52000 -45.57100 -34.35100 1.000 37.92000  ? 157 HIS A CG  1 
ATOM   860   N  ND1 . HIS A  1 126 ? -19.01600 -45.42200 -33.07700 1.000 44.99000  ? 157 HIS A ND1 1 
ATOM   861   C  CD2 . HIS A  1 126 ? -18.47000 -45.90400 -35.13300 1.000 40.19000  ? 157 HIS A CD2 1 
ATOM   862   C  CE1 . HIS A  1 126 ? -17.71500 -45.66700 -33.08600 1.000 41.83000  ? 157 HIS A CE1 1 
ATOM   863   N  NE2 . HIS A  1 126 ? -17.35900 -45.96100 -34.32300 1.000 44.80000  ? 157 HIS A NE2 1 
ATOM   864   N  N   . LEU A  1 127 ? -22.46200 -47.89600 -36.84700 1.000 36.23000  ? 158 LEU A N   1 
ATOM   865   C  CA  . LEU A  1 127 ? -22.67700 -49.33500 -36.90400 1.000 39.15000  ? 158 LEU A CA  1 
ATOM   866   C  C   . LEU A  1 127 ? -22.22900 -49.90700 -38.24700 1.000 40.75000  ? 158 LEU A C   1 
ATOM   867   O  O   . LEU A  1 127 ? -22.65100 -51.00200 -38.62200 1.000 36.99000  ? 158 LEU A O   1 
ATOM   868   C  CB  . LEU A  1 127 ? -24.15000 -49.64200 -36.63400 1.000 39.03000  ? 158 LEU A CB  1 
ATOM   869   C  CG  . LEU A  1 127 ? -24.68300 -48.99000 -35.35300 1.000 40.61000  ? 158 LEU A CG  1 
ATOM   870   C  CD1 . LEU A  1 127 ? -26.19600 -49.18900 -35.20900 1.000 36.03000  ? 158 LEU A CD1 1 
ATOM   871   C  CD2 . LEU A  1 127 ? -23.94800 -49.54000 -34.14200 1.000 34.22000  ? 158 LEU A CD2 1 
ATOM   872   N  N   . GLY A  1 128 ? -21.38700 -49.17400 -38.98000 1.000 40.55000  ? 159 GLY A N   1 
ATOM   873   C  CA  . GLY A  1 128 ? -20.87500 -49.61500 -40.26500 1.000 39.32000  ? 159 GLY A CA  1 
ATOM   874   C  C   . GLY A  1 128 ? -21.05000 -48.55900 -41.34400 1.000 39.46000  ? 159 GLY A C   1 
ATOM   875   O  O   . GLY A  1 128 ? -22.13600 -47.99400 -41.50800 1.000 43.40000  ? 159 GLY A O   1 
ATOM   876   N  N   . ALA A  1 129 ? -19.97300 -48.25000 -42.05100 1.000 40.15000  ? 160 ALA A N   1 
ATOM   877   C  CA  . ALA A  1 129 ? -19.95000 -47.19700 -43.05100 1.000 44.66000  ? 160 ALA A CA  1 
ATOM   878   C  C   . ALA A  1 129 ? -20.01400 -47.72300 -44.48200 1.000 44.90000  ? 160 ALA A C   1 
ATOM   879   O  O   . ALA A  1 129 ? -19.91100 -46.92900 -45.41400 1.000 44.32000  ? 160 ALA A O   1 
ATOM   880   C  CB  . ALA A  1 129 ? -18.70400 -46.33400 -42.86200 1.000 41.01000  ? 160 ALA A CB  1 
ATOM   881   N  N   . ALA A  1 130 ? -20.07900 -49.06900 -44.67800 1.000 44.38000  ? 161 ALA A N   1 
ATOM   882   C  CA  . ALA A  1 130 ? -20.26300 -49.68700 -45.98500 1.000 49.83000  ? 161 ALA A CA  1 
ATOM   883   C  C   . ALA A  1 130 ? -21.75000 -49.81100 -46.29700 1.000 50.70000  ? 161 ALA A C   1 
ATOM   884   O  O   . ALA A  1 130 ? -22.57300 -49.93400 -45.37600 1.000 43.63000  ? 161 ALA A O   1 
ATOM   885   C  CB  . ALA A  1 130 ? -19.61400 -51.06800 -46.03300 1.000 42.88000  ? 161 ALA A CB  1 
ATOM   886   N  N   . PRO A  1 131 ? -22.09400 -49.82900 -47.59600 1.000 55.04000  ? 162 PRO A N   1 
ATOM   887   C  CA  . PRO A  1 131 ? -23.52100 -49.74900 -47.98000 1.000 45.42000  ? 162 PRO A CA  1 
ATOM   888   C  C   . PRO A  1 131 ? -24.41300 -50.80200 -47.35600 1.000 43.22000  ? 162 PRO A C   1 
ATOM   889   O  O   . PRO A  1 131 ? -25.54800 -50.47000 -47.00400 1.000 52.03000  ? 162 PRO A O   1 
ATOM   890   C  CB  . PRO A  1 131 ? -23.47700 -49.88000 -49.51300 1.000 47.51000  ? 162 PRO A CB  1 
ATOM   891   C  CG  . PRO A  1 131 ? -22.16900 -49.27700 -49.89000 1.000 52.63000  ? 162 PRO A CG  1 
ATOM   892   C  CD  . PRO A  1 131 ? -21.20300 -49.65400 -48.76200 1.000 53.41000  ? 162 PRO A CD  1 
ATOM   893   N  N   . LYS A  1 132 ? -23.96800 -52.05100 -47.21000 1.000 47.85000  ? 163 LYS A N   1 
ATOM   894   C  CA  . LYS A  1 132 ? -24.84100 -53.05700 -46.59400 1.000 50.95000  ? 163 LYS A CA  1 
ATOM   895   C  C   . LYS A  1 132 ? -25.15700 -52.75600 -45.12500 1.000 47.59000  ? 163 LYS A C   1 
ATOM   896   O  O   . LYS A  1 132 ? -26.04000 -53.39900 -44.55200 1.000 50.43000  ? 163 LYS A O   1 
ATOM   897   C  CB  . LYS A  1 132 ? -24.23000 -54.46400 -46.70800 1.000 48.92000  ? 163 LYS A CB  1 
ATOM   898   C  CG  . LYS A  1 132 ? -22.91800 -54.64300 -45.93500 1.000 57.63000  ? 163 LYS A CG  1 
ATOM   899   C  CD  . LYS A  1 132 ? -22.21000 -55.96800 -46.28200 1.000 56.03000  ? 163 LYS A CD  1 
ATOM   900   C  CE  . LYS A  1 132 ? -22.84100 -57.14500 -45.54200 1.000 63.42000  ? 163 LYS A CE  1 
ATOM   901   N  NZ  . LYS A  1 132 ? -21.98200 -58.37400 -45.53200 1.000 67.37000  ? 163 LYS A NZ  1 
ATOM   902   N  N   . PHE A  1 133 ? -24.43500 -51.84100 -44.48800 1.000 47.96000  ? 164 PHE A N   1 
ATOM   903   C  CA  . PHE A  1 133 ? -24.68800 -51.46700 -43.10200 1.000 43.87000  ? 164 PHE A CA  1 
ATOM   904   C  C   . PHE A  1 133 ? -25.44400 -50.15300 -42.97900 1.000 48.21000  ? 164 PHE A C   1 
ATOM   905   O  O   . PHE A  1 133 ? -25.71200 -49.70000 -41.85000 1.000 41.33000  ? 164 PHE A O   1 
ATOM   906   C  CB  . PHE A  1 133 ? -23.36200 -51.38000 -42.34400 1.000 45.76000  ? 164 PHE A CB  1 
ATOM   907   C  CG  . PHE A  1 133 ? -22.53900 -52.65900 -42.39100 1.000 46.75000  ? 164 PHE A CG  1 
ATOM   908   C  CD1 . PHE A  1 133 ? -23.05600 -53.85400 -41.90800 1.000 44.41000  ? 164 PHE A CD1 1 
ATOM   909   C  CD2 . PHE A  1 133 ? -21.26000 -52.66000 -42.91100 1.000 39.29000  ? 164 PHE A CD2 1 
ATOM   910   C  CE1 . PHE A  1 133 ? -22.31000 -55.02100 -41.93800 1.000 45.57000  ? 164 PHE A CE1 1 
ATOM   911   C  CE2 . PHE A  1 133 ? -20.51200 -53.83500 -42.93900 1.000 44.86000  ? 164 PHE A CE2 1 
ATOM   912   C  CZ  . PHE A  1 133 ? -21.03700 -55.01100 -42.44000 1.000 40.51000  ? 164 PHE A CZ  1 
ATOM   913   N  N   . HIS A  1 134 ? -25.83800 -49.56800 -44.11200 1.000 45.21000  ? 165 HIS A N   1 
ATOM   914   C  CA  . HIS A  1 134 ? -26.44500 -48.25400 -44.12600 1.000 44.01000  ? 165 HIS A CA  1 
ATOM   915   C  C   . HIS A  1 134 ? -27.81200 -48.28200 -43.43300 1.000 47.76000  ? 165 HIS A C   1 
ATOM   916   O  O   . HIS A  1 134 ? -28.54400 -49.27300 -43.51400 1.000 45.68000  ? 165 HIS A O   1 
ATOM   917   C  CB  . HIS A  1 134 ? -26.60400 -47.78200 -45.57200 1.000 44.81000  ? 165 HIS A CB  1 
ATOM   918   C  CG  . HIS A  1 134 ? -26.92800 -46.32500 -45.70200 1.000 40.86000  ? 165 HIS A CG  1 
ATOM   919   N  ND1 . HIS A  1 134 ? -28.20400 -45.82500 -45.54500 1.000 40.69000  ? 165 HIS A ND1 1 
ATOM   920   C  CD2 . HIS A  1 134 ? -26.13200 -45.25700 -45.94100 1.000 37.78000  ? 165 HIS A CD2 1 
ATOM   921   C  CE1 . HIS A  1 134 ? -28.17800 -44.50900 -45.67600 1.000 38.14000  ? 165 HIS A CE1 1 
ATOM   922   N  NE2 . HIS A  1 134 ? -26.93200 -44.14000 -45.91600 1.000 45.51000  ? 165 HIS A NE2 1 
ATOM   923   N  N   . PRO A  1 135 ? -28.17900 -47.20100 -42.73900 1.000 48.76000  ? 166 PRO A N   1 
ATOM   924   C  CA  . PRO A  1 135 ? -29.50800 -47.16100 -42.09500 1.000 41.28000  ? 166 PRO A CA  1 
ATOM   925   C  C   . PRO A  1 135 ? -30.67200 -47.46500 -43.03500 1.000 43.46000  ? 166 PRO A C   1 
ATOM   926   O  O   . PRO A  1 135 ? -31.64700 -48.11800 -42.61700 1.000 40.23000  ? 166 PRO A O   1 
ATOM   927   C  CB  . PRO A  1 135 ? -29.56200 -45.73600 -41.52800 1.000 39.75000  ? 166 PRO A CB  1 
ATOM   928   C  CG  . PRO A  1 135 ? -28.08300 -45.41700 -41.21800 1.000 42.63000  ? 166 PRO A CG  1 
ATOM   929   C  CD  . PRO A  1 135 ? -27.28100 -46.12200 -42.27100 1.000 42.31000  ? 166 PRO A CD  1 
ATOM   930   N  N   . ASN A  1 136 ? -30.61200 -47.00000 -44.28600 1.000 43.79000  ? 167 ASN A N   1 
ATOM   931   C  CA  . ASN A  1 136 ? -31.72500 -47.25000 -45.21300 1.000 47.34000  ? 167 ASN A CA  1 
ATOM   932   C  C   . ASN A  1 136 ? -31.84400 -48.72000 -45.58800 1.000 44.21000  ? 167 ASN A C   1 
ATOM   933   O  O   . ASN A  1 136 ? -32.91100 -49.15800 -46.01800 1.000 45.63000  ? 167 ASN A O   1 
ATOM   934   C  CB  . ASN A  1 136 ? -31.60100 -46.40700 -46.48000 1.000 36.22000  ? 167 ASN A CB  1 
ATOM   935   C  CG  . ASN A  1 136 ? -31.79800 -44.93200 -46.21400 1.000 41.89000  ? 167 ASN A CG  1 
ATOM   936   O  OD1 . ASN A  1 136 ? -31.10600 -44.10100 -46.79900 1.000 39.23000  ? 167 ASN A OD1 1 
ATOM   937   N  ND2 . ASN A  1 136 ? -32.72600 -44.59100 -45.28900 1.000 38.51000  ? 167 ASN A ND2 1 
ATOM   938   N  N   . LYS A  1 137 ? -30.78000 -49.49000 -45.45200 1.000 47.26000  ? 168 LYS A N   1 
ATOM   939   C  CA  . LYS A  1 137 ? -30.88200 -50.93100 -45.62100 1.000 49.92000  ? 168 LYS A CA  1 
ATOM   940   C  C   . LYS A  1 137 ? -31.16400 -51.65900 -44.30800 1.000 49.05000  ? 168 LYS A C   1 
ATOM   941   O  O   . LYS A  1 137 ? -31.35900 -52.87800 -44.32600 1.000 50.53000  ? 168 LYS A O   1 
ATOM   942   C  CB  . LYS A  1 137 ? -29.59500 -51.46900 -46.26600 1.000 46.22000  ? 168 LYS A CB  1 
ATOM   943   C  CG  . LYS A  1 137 ? -29.58300 -51.34800 -47.78700 1.000 56.01000  ? 168 LYS A CG  1 
ATOM   944   C  CD  . LYS A  1 137 ? -28.22700 -50.89700 -48.33900 1.000 62.70000  ? 168 LYS A CD  1 
ATOM   945   C  CE  . LYS A  1 137 ? -28.13400 -49.35300 -48.53700 1.000 64.52000  ? 168 LYS A CE  1 
ATOM   946   N  NZ  . LYS A  1 137 ? -26.75300 -48.80700 -48.91700 1.000 40.29000  ? 168 LYS A NZ  1 
ATOM   947   N  N   . ARG A  1 138 ? -31.19500 -50.95200 -43.16600 1.000 46.14000  ? 169 ARG A N   1 
ATOM   948   C  CA  . ARG A  1 138 ? -31.38100 -51.58600 -41.86200 1.000 43.64000  ? 169 ARG A CA  1 
ATOM   949   C  C   . ARG A  1 138 ? -32.71100 -51.19700 -41.23100 1.000 51.03000  ? 169 ARG A C   1 
ATOM   950   O  O   . ARG A  1 138 ? -32.81700 -51.12600 -40.00100 1.000 43.41000  ? 169 ARG A O   1 
ATOM   951   C  CB  . ARG A  1 138 ? -30.26100 -51.21600 -40.88400 1.000 41.90000  ? 169 ARG A CB  1 
ATOM   952   C  CG  . ARG A  1 138 ? -28.81700 -51.33900 -41.38500 1.000 46.17000  ? 169 ARG A CG  1 
ATOM   953   C  CD  . ARG A  1 138 ? -28.32800 -52.75900 -41.60800 1.000 44.49000  ? 169 ARG A CD  1 
ATOM   954   N  NE  . ARG A  1 138 ? -28.71700 -53.71500 -40.57700 1.000 39.72000  ? 169 ARG A NE  1 
ATOM   955   C  CZ  . ARG A  1 138 ? -27.88300 -54.48200 -39.89300 1.000 43.77000  ? 169 ARG A CZ  1 
ATOM   956   N  NH1 . ARG A  1 138 ? -26.57600 -54.33100 -39.97900 1.000 47.64000  ? 169 ARG A NH1 1 
ATOM   957   N  NH2 . ARG A  1 138 ? -28.37400 -55.46000 -39.14000 1.000 42.80000  ? 169 ARG A NH2 1 
ATOM   958   N  N   . GLY A  1 139 ? -33.72300 -50.91800 -42.05500 1.000 45.56000  ? 170 GLY A N   1 
ATOM   959   C  CA  . GLY A  1 139 ? -35.06900 -50.70100 -41.56900 1.000 44.80000  ? 170 GLY A CA  1 
ATOM   960   C  C   . GLY A  1 139 ? -35.48700 -49.25700 -41.40400 1.000 43.75000  ? 170 GLY A C   1 
ATOM   961   O  O   . GLY A  1 139 ? -36.58700 -49.00100 -40.90800 1.000 45.64000  ? 170 GLY A O   1 
ATOM   962   N  N   . PHE A  1 140 ? -34.66800 -48.30600 -41.81300 1.000 43.45000  ? 171 PHE A N   1 
ATOM   963   C  CA  . PHE A  1 140 ? -34.99000 -46.90400 -41.61800 1.000 43.48000  ? 171 PHE A CA  1 
ATOM   964   C  C   . PHE A  1 140 ? -35.43900 -46.31200 -42.94700 1.000 43.47000  ? 171 PHE A C   1 
ATOM   965   O  O   . PHE A  1 140 ? -34.65200 -46.25900 -43.89500 1.000 39.55000  ? 171 PHE A O   1 
ATOM   966   C  CB  . PHE A  1 140 ? -33.78800 -46.15300 -41.04300 1.000 43.56000  ? 171 PHE A CB  1 
ATOM   967   C  CG  . PHE A  1 140 ? -33.54800 -46.41900 -39.57000 1.000 39.08000  ? 171 PHE A CG  1 
ATOM   968   C  CD1 . PHE A  1 140 ? -34.34800 -45.82100 -38.60700 1.000 45.94000  ? 171 PHE A CD1 1 
ATOM   969   C  CD2 . PHE A  1 140 ? -32.57000 -47.29100 -39.15600 1.000 42.77000  ? 171 PHE A CD2 1 
ATOM   970   C  CE1 . PHE A  1 140 ? -34.14500 -46.07000 -37.25700 1.000 43.70000  ? 171 PHE A CE1 1 
ATOM   971   C  CE2 . PHE A  1 140 ? -32.35100 -47.54400 -37.80000 1.000 41.32000  ? 171 PHE A CE2 1 
ATOM   972   C  CZ  . PHE A  1 140 ? -33.13200 -46.92900 -36.85500 1.000 42.84000  ? 171 PHE A CZ  1 
ATOM   973   N  N   . ASP A  1 141 ? -36.70600 -45.87200 -43.01100 1.000 40.92000  ? 172 ASP A N   1 
ATOM   974   C  CA  . ASP A  1 141 ? -37.18700 -45.17700 -44.20300 1.000 45.07000  ? 172 ASP A CA  1 
ATOM   975   C  C   . ASP A  1 141 ? -36.35500 -43.94500 -44.48300 1.000 43.33000  ? 172 ASP A C   1 
ATOM   976   O  O   . ASP A  1 141 ? -36.11100 -43.60600 -45.64400 1.000 44.32000  ? 172 ASP A O   1 
ATOM   977   C  CB  . ASP A  1 141 ? -38.65600 -44.76800 -44.05700 1.000 42.28000  ? 172 ASP A CB  1 
ATOM   978   C  CG  . ASP A  1 141 ? -39.54700 -45.93200 -43.84100 1.000 45.59000  ? 172 ASP A CG  1 
ATOM   979   O  OD1 . ASP A  1 141 ? -39.23900 -47.01700 -44.38000 1.000 44.88000  ? 172 ASP A OD1 1 
ATOM   980   O  OD2 . ASP A  1 141 ? -40.53600 -45.78000 -43.09100 1.000 55.14000  ? 172 ASP A OD2 1 
ATOM   981   N  N   . ASP A  1 142 ? -35.96600 -43.22600 -43.43900 1.000 40.45000  ? 173 ASP A N   1 
ATOM   982   C  CA  . ASP A  1 142 ? -35.22600 -41.98500 -43.59400 1.000 44.09000  ? 173 ASP A CA  1 
ATOM   983   C  C   . ASP A  1 142 ? -33.99400 -42.00000 -42.69000 1.000 43.69000  ? 173 ASP A C   1 
ATOM   984   O  O   . ASP A  1 142 ? -34.02900 -42.58600 -41.60400 1.000 45.14000  ? 173 ASP A O   1 
ATOM   985   C  CB  . ASP A  1 142 ? -36.10900 -40.77100 -43.30500 1.000 39.25000  ? 173 ASP A CB  1 
ATOM   986   C  CG  . ASP A  1 142 ? -35.45800 -39.49400 -43.74600 1.000 43.46000  ? 173 ASP A CG  1 
ATOM   987   O  OD1 . ASP A  1 142 ? -34.50400 -39.05900 -43.06800 1.000 59.87000  ? 173 ASP A OD1 1 
ATOM   988   O  OD2 . ASP A  1 142 ? -35.82200 -38.95800 -44.79800 1.000 52.74000  ? 173 ASP A OD2 1 
ATOM   989   N  N   . PHE A  1 143 ? -32.88000 -41.45000 -43.18900 1.000 41.47000  ? 174 PHE A N   1 
ATOM   990   C  CA  . PHE A  1 143 ? -31.66200 -41.24500 -42.40200 1.000 38.08000  ? 174 PHE A CA  1 
ATOM   991   C  C   . PHE A  1 143 ? -31.13800 -39.84100 -42.66700 1.000 41.50000  ? 174 PHE A C   1 
ATOM   992   O  O   . PHE A  1 143 ? -30.99300 -39.43000 -43.82000 1.000 44.24000  ? 174 PHE A O   1 
ATOM   993   C  CB  . PHE A  1 143 ? -30.55800 -42.27600 -42.72200 1.000 38.29000  ? 174 PHE A CB  1 
ATOM   994   C  CG  . PHE A  1 143 ? -29.24900 -42.01900 -41.99600 1.000 39.90000  ? 174 PHE A CG  1 
ATOM   995   C  CD1 . PHE A  1 143 ? -29.21900 -41.87700 -40.61700 1.000 39.51000  ? 174 PHE A CD1 1 
ATOM   996   C  CD2 . PHE A  1 143 ? -28.06300 -41.86500 -42.70500 1.000 37.46000  ? 174 PHE A CD2 1 
ATOM   997   C  CE1 . PHE A  1 143 ? -28.02200 -41.61000 -39.94900 1.000 40.40000  ? 174 PHE A CE1 1 
ATOM   998   C  CE2 . PHE A  1 143 ? -26.86400 -41.59600 -42.06900 1.000 40.85000  ? 174 PHE A CE2 1 
ATOM   999   C  CZ  . PHE A  1 143 ? -26.82900 -41.46500 -40.66700 1.000 42.03000  ? 174 PHE A CZ  1 
ATOM   1000  N  N   . TYR A  1 144 ? -30.84700 -39.10300 -41.61000 1.000 39.77000  ? 175 TYR A N   1 
ATOM   1001  C  CA  . TYR A  1 144 ? -30.21600 -37.79900 -41.75400 1.000 43.47000  ? 175 TYR A CA  1 
ATOM   1002  C  C   . TYR A  1 144 ? -29.12200 -37.73400 -40.70500 1.000 40.25000  ? 175 TYR A C   1 
ATOM   1003  O  O   . TYR A  1 144 ? -29.43000 -37.62700 -39.51600 1.000 41.07000  ? 175 TYR A O   1 
ATOM   1004  C  CB  . TYR A  1 144 ? -31.21000 -36.65600 -41.57100 1.000 38.17000  ? 175 TYR A CB  1 
ATOM   1005  C  CG  . TYR A  1 144 ? -30.58100 -35.28700 -41.77100 1.000 42.13000  ? 175 TYR A CG  1 
ATOM   1006  C  CD1 . TYR A  1 144 ? -29.83100 -34.68000 -40.75700 1.000 34.54000  ? 175 TYR A CD1 1 
ATOM   1007  C  CD2 . TYR A  1 144 ? -30.74600 -34.59500 -42.96000 1.000 37.48000  ? 175 TYR A CD2 1 
ATOM   1008  C  CE1 . TYR A  1 144 ? -29.26100 -33.42800 -40.93300 1.000 38.01000  ? 175 TYR A CE1 1 
ATOM   1009  C  CE2 . TYR A  1 144 ? -30.19000 -33.34200 -43.14400 1.000 36.59000  ? 175 TYR A CE2 1 
ATOM   1010  C  CZ  . TYR A  1 144 ? -29.44100 -32.76500 -42.14100 1.000 43.47000  ? 175 TYR A CZ  1 
ATOM   1011  O  OH  . TYR A  1 144 ? -28.88600 -31.52100 -42.33900 1.000 41.13000  ? 175 TYR A OH  1 
ATOM   1012  N  N   . GLY A  1 145 ? -27.86400 -37.80900 -41.13300 1.000 41.78000  ? 176 GLY A N   1 
ATOM   1013  C  CA  . GLY A  1 145 ? -26.75800 -37.71800 -40.18200 1.000 37.24000  ? 176 GLY A CA  1 
ATOM   1014  C  C   . GLY A  1 145 ? -25.43100 -38.11900 -40.80000 1.000 42.74000  ? 176 GLY A C   1 
ATOM   1015  O  O   . GLY A  1 145 ? -25.16700 -37.83200 -41.97300 1.000 37.93000  ? 176 GLY A O   1 
ATOM   1016  N  N   . PHE A  1 146 ? -24.58500 -38.76300 -39.97200 1.000 43.94000  ? 177 PHE A N   1 
ATOM   1017  C  CA  . PHE A  1 146 ? -23.25000 -39.19900 -40.36400 1.000 34.25000  ? 177 PHE A CA  1 
ATOM   1018  C  C   . PHE A  1 146 ? -23.04500 -40.64500 -39.95100 1.000 40.08000  ? 177 PHE A C   1 
ATOM   1019  O  O   . PHE A  1 146 ? -23.61900 -41.11900 -38.96400 1.000 41.79000  ? 177 PHE A O   1 
ATOM   1020  C  CB  . PHE A  1 146 ? -22.13000 -38.33100 -39.74700 1.000 35.01000  ? 177 PHE A CB  1 
ATOM   1021  C  CG  . PHE A  1 146 ? -22.17300 -38.22500 -38.22300 1.000 38.73000  ? 177 PHE A CG  1 
ATOM   1022  C  CD1 . PHE A  1 146 ? -22.95500 -37.25400 -37.60700 1.000 35.64000  ? 177 PHE A CD1 1 
ATOM   1023  C  CD2 . PHE A  1 146 ? -21.41500 -39.07500 -37.42900 1.000 38.38000  ? 177 PHE A CD2 1 
ATOM   1024  C  CE1 . PHE A  1 146 ? -23.01500 -37.14500 -36.24000 1.000 35.79000  ? 177 PHE A CE1 1 
ATOM   1025  C  CE2 . PHE A  1 146 ? -21.44500 -38.97300 -36.04000 1.000 40.92000  ? 177 PHE A CE2 1 
ATOM   1026  C  CZ  . PHE A  1 146 ? -22.23600 -37.99600 -35.44100 1.000 42.30000  ? 177 PHE A CZ  1 
ATOM   1027  N  N   . LEU A  1 147 ? -22.17400 -41.33000 -40.68200 1.000 37.36000  ? 178 LEU A N   1 
ATOM   1028  C  CA  . LEU A  1 147 ? -22.06100 -42.77500 -40.54700 1.000 38.90000  ? 178 LEU A CA  1 
ATOM   1029  C  C   . LEU A  1 147 ? -21.09700 -43.22300 -39.46000 1.000 40.71000  ? 178 LEU A C   1 
ATOM   1030  O  O   . LEU A  1 147 ? -21.28500 -44.32200 -38.90900 1.000 42.86000  ? 178 LEU A O   1 
ATOM   1031  C  CB  . LEU A  1 147 ? -21.61500 -43.38000 -41.88200 1.000 43.27000  ? 178 LEU A CB  1 
ATOM   1032  C  CG  . LEU A  1 147 ? -22.66800 -43.23400 -42.97100 1.000 46.51000  ? 178 LEU A CG  1 
ATOM   1033  C  CD1 . LEU A  1 147 ? -22.20400 -43.87800 -44.26100 1.000 46.45000  ? 178 LEU A CD1 1 
ATOM   1034  C  CD2 . LEU A  1 147 ? -23.95900 -43.90000 -42.45900 1.000 45.46000  ? 178 LEU A CD2 1 
ATOM   1035  N  N   . GLY A  1 148 ? -20.12100 -42.39000 -39.09100 1.000 36.32000  ? 179 GLY A N   1 
ATOM   1036  C  CA  . GLY A  1 148 ? -19.10400 -42.75600 -38.12400 1.000 40.38000  ? 179 GLY A CA  1 
ATOM   1037  C  C   . GLY A  1 148 ? -19.46400 -42.39800 -36.69100 1.000 40.49000  ? 179 GLY A C   1 
ATOM   1038  O  O   . GLY A  1 148 ? -20.63200 -42.23500 -36.33300 1.000 43.29000  ? 179 GLY A O   1 
ATOM   1039  N  N   . GLY A  1 149 ? -18.43000 -42.23200 -35.87100 1.000 41.13000  ? 180 GLY A N   1 
ATOM   1040  C  CA  . GLY A  1 149 ? -18.57400 -42.15500 -34.43200 1.000 40.75000  ? 180 GLY A CA  1 
ATOM   1041  C  C   . GLY A  1 149 ? -18.69100 -40.78000 -33.83200 1.000 48.41000  ? 180 GLY A C   1 
ATOM   1042  O  O   . GLY A  1 149 ? -19.02700 -40.67500 -32.64900 1.000 41.93000  ? 180 GLY A O   1 
ATOM   1043  N  N   . GLY A  1 150 ? -18.42200 -39.73200 -34.60800 1.000 45.24000  ? 181 GLY A N   1 
ATOM   1044  C  CA  . GLY A  1 150 ? -18.50400 -38.37300 -34.10700 1.000 39.09000  ? 181 GLY A CA  1 
ATOM   1045  C  C   . GLY A  1 150 ? -18.44600 -37.39200 -35.25800 1.000 43.77000  ? 181 GLY A C   1 
ATOM   1046  O  O   . GLY A  1 150 ? -18.28000 -37.77000 -36.42400 1.000 37.67000  ? 181 GLY A O   1 
ATOM   1047  N  N   . HIS A  1 151 ? -18.59700 -36.11100 -34.91500 1.000 38.98000  ? 182 HIS A N   1 
ATOM   1048  C  CA  . HIS A  1 151 ? -18.62600 -35.07900 -35.93400 1.000 34.22000  ? 182 HIS A CA  1 
ATOM   1049  C  C   . HIS A  1 151 ? -18.47300 -33.71500 -35.28200 1.000 41.35000  ? 182 HIS A C   1 
ATOM   1050  O  O   . HIS A  1 151 ? -18.96100 -33.48900 -34.17300 1.000 41.91000  ? 182 HIS A O   1 
ATOM   1051  C  CB  . HIS A  1 151 ? -19.93900 -35.10800 -36.73300 1.000 34.92000  ? 182 HIS A CB  1 
ATOM   1052  C  CG  . HIS A  1 151 ? -19.78700 -34.56700 -38.11800 1.000 38.01000  ? 182 HIS A CG  1 
ATOM   1053  N  ND1 . HIS A  1 151 ? -19.66600 -33.21500 -38.37600 1.000 35.91000  ? 182 HIS A ND1 1 
ATOM   1054  C  CD2 . HIS A  1 151 ? -19.67100 -35.19500 -39.31400 1.000 36.76000  ? 182 HIS A CD2 1 
ATOM   1055  C  CE1 . HIS A  1 151 ? -19.50900 -33.03300 -39.67800 1.000 39.99000  ? 182 HIS A CE1 1 
ATOM   1056  N  NE2 . HIS A  1 151 ? -19.50100 -34.21700 -40.26700 1.000 40.89000  ? 182 HIS A NE2 1 
ATOM   1057  N  N   . ASP A  1 152 ? -17.79400 -32.81200 -35.98600 1.000 39.69000  ? 183 ASP A N   1 
ATOM   1058  C  CA  . ASP A  1 152 ? -17.75300 -31.41100 -35.60000 1.000 32.79000  ? 183 ASP A CA  1 
ATOM   1059  C  C   . ASP A  1 152 ? -19.13400 -30.76500 -35.73100 1.000 36.14000  ? 183 ASP A C   1 
ATOM   1060  O  O   . ASP A  1 152 ? -19.94700 -31.16600 -36.56800 1.000 37.81000  ? 183 ASP A O   1 
ATOM   1061  C  CB  . ASP A  1 152 ? -16.74700 -30.67000 -36.47100 1.000 40.07000  ? 183 ASP A CB  1 
ATOM   1062  C  CG  . ASP A  1 152 ? -15.29700 -31.01500 -36.12100 1.000 44.17000  ? 183 ASP A CG  1 
ATOM   1063  O  OD1 . ASP A  1 152 ? -15.08300 -31.90800 -35.28000 1.000 47.58000  ? 183 ASP A OD1 1 
ATOM   1064  O  OD2 . ASP A  1 152 ? -14.37400 -30.39600 -36.69200 1.000 51.08000  ? 183 ASP A OD2 1 
ATOM   1065  N  N   . TYR A  1 153 ? -19.37300 -29.69900 -34.94500 1.000 36.60000  ? 184 TYR A N   1 
ATOM   1066  C  CA  . TYR A  1 153 ? -20.73100 -29.18000 -34.74400 1.000 39.68000  ? 184 TYR A CA  1 
ATOM   1067  C  C   . TYR A  1 153 ? -21.11600 -27.99900 -35.63500 1.000 39.90000  ? 184 TYR A C   1 
ATOM   1068  O  O   . TYR A  1 153 ? -22.31300 -27.77100 -35.83900 1.000 38.05000  ? 184 TYR A O   1 
ATOM   1069  C  CB  . TYR A  1 153 ? -20.93500 -28.76500 -33.26100 1.000 41.95000  ? 184 TYR A CB  1 
ATOM   1070  C  CG  . TYR A  1 153 ? -21.06400 -29.95700 -32.29500 1.000 38.27000  ? 184 TYR A CG  1 
ATOM   1071  C  CD1 . TYR A  1 153 ? -19.93700 -30.62700 -31.85300 1.000 31.79000  ? 184 TYR A CD1 1 
ATOM   1072  C  CD2 . TYR A  1 153 ? -22.32000 -30.43800 -31.88700 1.000 37.03000  ? 184 TYR A CD2 1 
ATOM   1073  C  CE1 . TYR A  1 153 ? -20.02500 -31.73500 -31.01400 1.000 36.15000  ? 184 TYR A CE1 1 
ATOM   1074  C  CE2 . TYR A  1 153 ? -22.42600 -31.55700 -31.03300 1.000 32.92000  ? 184 TYR A CE2 1 
ATOM   1075  C  CZ  . TYR A  1 153 ? -21.26400 -32.19100 -30.59900 1.000 36.10000  ? 184 TYR A CZ  1 
ATOM   1076  O  OH  . TYR A  1 153 ? -21.31800 -33.29300 -29.76200 1.000 40.40000  ? 184 TYR A OH  1 
ATOM   1077  N  N   . PHE A  1 154 ? -20.16600 -27.25300 -36.19100 1.000 37.51000  ? 185 PHE A N   1 
ATOM   1078  C  CA  . PHE A  1 154 ? -20.51700 -26.03300 -36.91300 1.000 37.64000  ? 185 PHE A CA  1 
ATOM   1079  C  C   . PHE A  1 154 ? -20.24900 -26.20200 -38.40000 1.000 44.07000  ? 185 PHE A C   1 
ATOM   1080  O  O   . PHE A  1 154 ? -19.07400 -26.28600 -38.81000 1.000 44.39000  ? 185 PHE A O   1 
ATOM   1081  C  CB  . PHE A  1 154 ? -19.73300 -24.84000 -36.37400 1.000 38.79000  ? 185 PHE A CB  1 
ATOM   1082  C  CG  . PHE A  1 154 ? -20.25800 -24.30100 -35.07300 1.000 42.84000  ? 185 PHE A CG  1 
ATOM   1083  C  CD1 . PHE A  1 154 ? -21.43400 -23.54800 -35.03500 1.000 42.05000  ? 185 PHE A CD1 1 
ATOM   1084  C  CD2 . PHE A  1 154 ? -19.57300 -24.53800 -33.88900 1.000 36.84000  ? 185 PHE A CD2 1 
ATOM   1085  C  CE1 . PHE A  1 154 ? -21.91800 -23.03700 -33.81300 1.000 49.50000  ? 185 PHE A CE1 1 
ATOM   1086  C  CE2 . PHE A  1 154 ? -20.03900 -24.03000 -32.67700 1.000 39.85000  ? 185 PHE A CE2 1 
ATOM   1087  C  CZ  . PHE A  1 154 ? -21.22100 -23.28400 -32.63200 1.000 44.82000  ? 185 PHE A CZ  1 
ATOM   1088  N  N   . PRO A  1 155 ? -21.29300 -26.23900 -39.23500 1.000 43.71000  ? 186 PRO A N   1 
ATOM   1089  C  CA  . PRO A  1 155 ? -21.07700 -26.47700 -40.67200 1.000 44.43000  ? 186 PRO A CA  1 
ATOM   1090  C  C   . PRO A  1 155 ? -20.22300 -25.41800 -41.34800 1.000 45.76000  ? 186 PRO A C   1 
ATOM   1091  O  O   . PRO A  1 155 ? -19.42000 -25.75500 -42.22700 1.000 40.34000  ? 186 PRO A O   1 
ATOM   1092  C  CB  . PRO A  1 155 ? -22.51100 -26.47700 -41.24000 1.000 42.23000  ? 186 PRO A CB  1 
ATOM   1093  C  CG  . PRO A  1 155 ? -23.37900 -26.81000 -40.08500 1.000 47.06000  ? 186 PRO A CG  1 
ATOM   1094  C  CD  . PRO A  1 155 ? -22.72700 -26.10900 -38.91600 1.000 43.61000  ? 186 PRO A CD  1 
ATOM   1095  N  N   . SER A  1 156 ? -20.35300 -24.15000 -40.94800 1.000 40.56000  ? 187 SER A N   1 
ATOM   1096  C  CA  . SER A  1 156 ? -19.49200 -23.11900 -41.51700 1.000 44.60000  ? 187 SER A CA  1 
ATOM   1097  C  C   . SER A  1 156 ? -18.01700 -23.48400 -41.37600 1.000 47.91000  ? 187 SER A C   1 
ATOM   1098  O  O   . SER A  1 156 ? -17.20800 -23.16600 -42.25300 1.000 47.95000  ? 187 SER A O   1 
ATOM   1099  C  CB  . SER A  1 156 ? -19.78000 -21.75700 -40.86900 1.000 40.73000  ? 187 SER A CB  1 
ATOM   1100  O  OG  . SER A  1 156 ? -19.78000 -21.84900 -39.45600 1.000 50.39000  ? 187 SER A OG  1 
ATOM   1101  N  N   . GLU A  1 157 ? -17.64200 -24.12800 -40.26600 1.000 42.38000  ? 188 GLU A N   1 
ATOM   1102  C  CA  . GLU A  1 157 ? -16.24900 -24.49600 -40.02200 1.000 38.71000  ? 188 GLU A CA  1 
ATOM   1103  C  C   . GLU A  1 157 ? -15.84800 -25.82800 -40.64900 1.000 42.69000  ? 188 GLU A C   1 
ATOM   1104  O  O   . GLU A  1 157 ? -14.73900 -25.94200 -41.18400 1.000 43.39000  ? 188 GLU A O   1 
ATOM   1105  C  CB  . GLU A  1 157 ? -15.95300 -24.53200 -38.51700 1.000 39.55000  ? 188 GLU A CB  1 
ATOM   1106  C  CG  . GLU A  1 157 ? -16.23000 -23.21800 -37.82600 1.000 44.19000  ? 188 GLU A CG  1 
ATOM   1107  C  CD  . GLU A  1 157 ? -16.16900 -23.31500 -36.30600 1.000 62.46000  ? 188 GLU A CD  1 
ATOM   1108  O  OE1 . GLU A  1 157 ? -16.12900 -24.44900 -35.75600 1.000 54.05000  ? 188 GLU A OE1 1 
ATOM   1109  O  OE2 . GLU A  1 157 ? -16.13200 -22.23900 -35.66600 1.000 66.73000  ? 188 GLU A OE2 1 
ATOM   1110  N  N   . TYR A  1 158 ? -16.66900 -26.87400 -40.51600 1.000 37.09000  ? 189 TYR A N   1 
ATOM   1111  C  CA  . TYR A  1 158 ? -16.17500 -28.15000 -41.01900 1.000 40.70000  ? 189 TYR A CA  1 
ATOM   1112  C  C   . TYR A  1 158 ? -16.35600 -28.26700 -42.53500 1.000 41.36000  ? 189 TYR A C   1 
ATOM   1113  O  O   . TYR A  1 158 ? -15.57600 -28.97300 -43.17700 1.000 38.63000  ? 189 TYR A O   1 
ATOM   1114  C  CB  . TYR A  1 158 ? -16.81900 -29.34700 -40.29500 1.000 34.89000  ? 189 TYR A CB  1 
ATOM   1115  C  CG  . TYR A  1 158 ? -18.32500 -29.60600 -40.52800 1.000 39.75000  ? 189 TYR A CG  1 
ATOM   1116  C  CD1 . TYR A  1 158 ? -18.80200 -30.07500 -41.74700 1.000 35.64000  ? 189 TYR A CD1 1 
ATOM   1117  C  CD2 . TYR A  1 158 ? -19.24000 -29.47700 -39.47900 1.000 41.58000  ? 189 TYR A CD2 1 
ATOM   1118  C  CE1 . TYR A  1 158 ? -20.18200 -30.33700 -41.95100 1.000 37.39000  ? 189 TYR A CE1 1 
ATOM   1119  C  CE2 . TYR A  1 158 ? -20.60400 -29.74100 -39.65700 1.000 42.87000  ? 189 TYR A CE2 1 
ATOM   1120  C  CZ  . TYR A  1 158 ? -21.06700 -30.17100 -40.88900 1.000 42.71000  ? 189 TYR A CZ  1 
ATOM   1121  O  OH  . TYR A  1 158 ? -22.40700 -30.42700 -41.04000 1.000 41.40000  ? 189 TYR A OH  1 
ATOM   1122  N  N   . GLN A  1 159 ? -17.35000 -27.57800 -43.11500 1.000 39.47000  ? 190 GLN A N   1 
ATOM   1123  C  CA  . GLN A  1 159 ? -17.50700 -27.55300 -44.57500 1.000 41.21000  ? 190 GLN A CA  1 
ATOM   1124  C  C   . GLN A  1 159 ? -16.32600 -26.85300 -45.22500 1.000 43.40000  ? 190 GLN A C   1 
ATOM   1125  O  O   . GLN A  1 159 ? -15.76200 -27.34000 -46.21000 1.000 41.96000  ? 190 GLN A O   1 
ATOM   1126  C  CB  . GLN A  1 159 ? -18.81900 -26.85400 -44.97100 1.000 34.90000  ? 190 GLN A CB  1 
ATOM   1127  C  CG  . GLN A  1 159 ? -20.03700 -27.76000 -44.85900 1.000 38.22000  ? 190 GLN A CG  1 
ATOM   1128  C  CD  . GLN A  1 159 ? -21.35800 -27.03600 -44.77500 1.000 38.83000  ? 190 GLN A CD  1 
ATOM   1129  O  OE1 . GLN A  1 159 ? -21.42100 -25.81000 -44.66300 1.000 47.24000  ? 190 GLN A OE1 1 
ATOM   1130  N  NE2 . GLN A  1 159 ? -22.43600 -27.80200 -44.81300 1.000 37.92000  ? 190 GLN A NE2 1 
ATOM   1131  N  N   . LYS A  1 160 ? -15.92600 -25.71300 -44.66000 1.000 42.87000  ? 191 LYS A N   1 
ATOM   1132  C  CA  . LYS A  1 160 ? -14.74400 -25.01200 -45.13800 1.000 42.38000  ? 191 LYS A CA  1 
ATOM   1133  C  C   . LYS A  1 160 ? -13.50500 -25.90100 -45.08200 1.000 45.52000  ? 191 LYS A C   1 
ATOM   1134  O  O   . LYS A  1 160 ? -12.69900 -25.92300 -46.02100 1.000 43.37000  ? 191 LYS A O   1 
ATOM   1135  C  CB  . LYS A  1 160 ? -14.54100 -23.73100 -44.33800 1.000 48.74000  ? 191 LYS A CB  1 
ATOM   1136  C  CG  . LYS A  1 160 ? -13.19500 -23.09500 -44.56200 1.000 52.93000  ? 191 LYS A CG  1 
ATOM   1137  C  CD  . LYS A  1 160 ? -13.19000 -21.64300 -44.11500 1.000 57.40000  ? 191 LYS A CD  1 
ATOM   1138  C  CE  . LYS A  1 160 ? -11.88400 -20.96500 -44.50300 1.000 63.16000  ? 191 LYS A CE  1 
ATOM   1139  N  NZ  . LYS A  1 160 ? -11.90900 -19.53000 -44.12200 1.000 68.69000  ? 191 LYS A NZ  1 
ATOM   1140  N  N   . THR A  1 161 ? -13.29100 -26.58700 -43.95600 1.000 47.69000  ? 192 THR A N   1 
ATOM   1141  C  CA  . THR A  1 161 ? -12.14200 -27.48500 -43.86200 1.000 41.39000  ? 192 THR A CA  1 
ATOM   1142  C  C   . THR A  1 161 ? -12.24500 -28.64300 -44.85100 1.000 47.56000  ? 192 THR A C   1 
ATOM   1143  O  O   . THR A  1 161 ? -11.25800 -29.00600 -45.50300 1.000 44.55000  ? 192 THR A O   1 
ATOM   1144  C  CB  . THR A  1 161 ? -12.01600 -28.02600 -42.44400 1.000 47.81000  ? 192 THR A CB  1 
ATOM   1145  O  OG1 . THR A  1 161 ? -11.82400 -26.93300 -41.53800 1.000 50.79000  ? 192 THR A OG1 1 
ATOM   1146  C  CG2 . THR A  1 161 ? -10.85000 -28.98700 -42.35500 1.000 42.15000  ? 192 THR A CG2 1 
ATOM   1147  N  N   . TYR A  1 162 ? -13.43600 -29.23900 -44.97400 1.000 42.91000  ? 193 TYR A N   1 
ATOM   1148  C  CA  . TYR A  1 162 ? -13.57400 -30.39100 -45.85600 1.000 43.57000  ? 193 TYR A CA  1 
ATOM   1149  C  C   . TYR A  1 162 ? -13.28200 -29.99700 -47.29100 1.000 43.43000  ? 193 TYR A C   1 
ATOM   1150  O  O   . TYR A  1 162 ? -12.57000 -30.71100 -48.00000 1.000 44.92000  ? 193 TYR A O   1 
ATOM   1151  C  CB  . TYR A  1 162 ? -14.98200 -30.98700 -45.76500 1.000 40.34000  ? 193 TYR A CB  1 
ATOM   1152  C  CG  . TYR A  1 162 ? -15.18300 -32.12300 -46.74900 1.000 39.84000  ? 193 TYR A CG  1 
ATOM   1153  C  CD1 . TYR A  1 162 ? -14.62400 -33.36500 -46.52400 1.000 38.99000  ? 193 TYR A CD1 1 
ATOM   1154  C  CD2 . TYR A  1 162 ? -15.89700 -31.92800 -47.93200 1.000 44.83000  ? 193 TYR A CD2 1 
ATOM   1155  C  CE1 . TYR A  1 162 ? -14.78800 -34.40500 -47.42700 1.000 42.96000  ? 193 TYR A CE1 1 
ATOM   1156  C  CE2 . TYR A  1 162 ? -16.06400 -32.95500 -48.84900 1.000 37.12000  ? 193 TYR A CE2 1 
ATOM   1157  C  CZ  . TYR A  1 162 ? -15.51400 -34.19100 -48.59100 1.000 45.82000  ? 193 TYR A CZ  1 
ATOM   1158  O  OH  . TYR A  1 162 ? -15.68800 -35.22000 -49.49500 1.000 49.61000  ? 193 TYR A OH  1 
ATOM   1159  N  N   . LYS A  1 163 ? -13.81500 -28.85300 -47.72200 1.000 37.54000  ? 194 LYS A N   1 
ATOM   1160  C  CA  . LYS A  1 163 ? -13.58700 -28.38900 -49.08300 1.000 45.09000  ? 194 LYS A CA  1 
ATOM   1161  C  C   . LYS A  1 163 ? -12.11400 -28.10700 -49.33100 1.000 48.02000  ? 194 LYS A C   1 
ATOM   1162  O  O   . LYS A  1 163 ? -11.55200 -28.57200 -50.32600 1.000 45.62000  ? 194 LYS A O   1 
ATOM   1163  C  CB  . LYS A  1 163 ? -14.43100 -27.14900 -49.36100 1.000 42.73000  ? 194 LYS A CB  1 
ATOM   1164  C  CG  . LYS A  1 163 ? -15.89800 -27.49500 -49.64400 1.000 47.52000  ? 194 LYS A CG  1 
ATOM   1165  C  CD  . LYS A  1 163 ? -16.75800 -26.24400 -49.73000 1.000 51.46000  ? 194 LYS A CD  1 
ATOM   1166  C  CE  . LYS A  1 163 ? -18.18500 -26.54100 -49.32700 1.000 53.94000  ? 194 LYS A CE  1 
ATOM   1167  N  NZ  . LYS A  1 163 ? -19.14200 -25.59200 -49.95600 1.000 58.90000  ? 194 LYS A NZ  1 
ATOM   1168  N  N   . ALA A  1 164 ? -11.46700 -27.34600 -48.43600 1.000 41.97000  ? 195 ALA A N   1 
ATOM   1169  C  CA  . ALA A  1 164 ? -10.05800 -27.03400 -48.64900 1.000 42.74000  ? 195 ALA A CA  1 
ATOM   1170  C  C   . ALA A  1 164 ? -9.24700  -28.30900 -48.79200 1.000 45.32000  ? 195 ALA A C   1 
ATOM   1171  O  O   . ALA A  1 164 ? -8.42200  -28.43600 -49.70600 1.000 53.34000  ? 195 ALA A O   1 
ATOM   1172  C  CB  . ALA A  1 164 ? -9.50800  -26.15600 -47.51900 1.000 36.30000  ? 195 ALA A CB  1 
ATOM   1173  N  N   . GLN A  1 165 ? -9.48000  -29.27300 -47.90100 1.000 42.08000  ? 196 GLN A N   1 
ATOM   1174  C  CA  . GLN A  1 165 ? -8.70400  -30.50800 -47.92900 1.000 44.97000  ? 196 GLN A CA  1 
ATOM   1175  C  C   . GLN A  1 165 ? -9.08400  -31.40900 -49.09200 1.000 44.13000  ? 196 GLN A C   1 
ATOM   1176  O  O   . GLN A  1 165 ? -8.24300  -32.17400 -49.56500 1.000 43.70000  ? 196 GLN A O   1 
ATOM   1177  C  CB  . GLN A  1 165 ? -8.87300  -31.27400 -46.62500 1.000 39.01000  ? 196 GLN A CB  1 
ATOM   1178  C  CG  . GLN A  1 165 ? -8.29100  -30.58400 -45.40500 1.000 51.42000  ? 196 GLN A CG  1 
ATOM   1179  C  CD  . GLN A  1 165 ? -8.52900  -31.44000 -44.19500 1.000 61.47000  ? 196 GLN A CD  1 
ATOM   1180  O  OE1 . GLN A  1 165 ? -8.95400  -32.58300 -44.33900 1.000 58.55000  ? 196 GLN A OE1 1 
ATOM   1181  N  NE2 . GLN A  1 165 ? -8.27200  -30.90800 -43.00200 1.000 66.07000  ? 196 GLN A NE2 1 
ATOM   1182  N  N   . LYS A  1 166 ? -10.33500 -31.35400 -49.55600 1.000 45.82000  ? 197 LYS A N   1 
ATOM   1183  C  CA  . LYS A  1 166 ? -10.69300 -32.14600 -50.72800 1.000 49.20000  ? 197 LYS A CA  1 
ATOM   1184  C  C   . LYS A  1 166 ? -10.02800 -31.58400 -51.97400 1.000 52.71000  ? 197 LYS A C   1 
ATOM   1185  O  O   . LYS A  1 166 ? -9.53100  -32.33900 -52.81600 1.000 50.81000  ? 197 LYS A O   1 
ATOM   1186  C  CB  . LYS A  1 166 ? -12.20700 -32.18100 -50.91600 1.000 44.39000  ? 197 LYS A CB  1 
ATOM   1187  C  CG  . LYS A  1 166 ? -12.68600 -33.34000 -51.77000 1.000 55.27000  ? 197 LYS A CG  1 
ATOM   1188  C  CD  . LYS A  1 166 ? -12.27200 -34.64600 -51.10300 1.000 58.44000  ? 197 LYS A CD  1 
ATOM   1189  C  CE  . LYS A  1 166 ? -13.04800 -35.86200 -51.60700 1.000 67.63000  ? 197 LYS A CE  1 
ATOM   1190  N  NZ  . LYS A  1 166 ? -13.09200 -36.89200 -50.50900 1.000 68.51000  ? 197 LYS A NZ  1 
ATOM   1191  N  N   . LYS A  1 167 ? -9.96800  -30.25700 -52.07900 1.000 48.92000  ? 198 LYS A N   1 
ATOM   1192  C  CA  . LYS A  1 167 ? -9.32600  -29.62000 -53.22000 1.000 51.62000  ? 198 LYS A CA  1 
ATOM   1193  C  C   . LYS A  1 167 ? -7.81800  -29.82200 -53.21900 1.000 55.07000  ? 198 LYS A C   1 
ATOM   1194  O  O   . LYS A  1 167 ? -7.20100  -29.77600 -54.28800 1.000 54.33000  ? 198 LYS A O   1 
ATOM   1195  C  CB  . LYS A  1 167 ? -9.67200  -28.12700 -53.22800 1.000 52.17000  ? 198 LYS A CB  1 
ATOM   1196  C  CG  . LYS A  1 167 ? -8.72900  -27.22600 -54.00900 1.000 57.75000  ? 198 LYS A CG  1 
ATOM   1197  C  CD  . LYS A  1 167 ? -9.12400  -25.77200 -53.84800 1.000 52.81000  ? 198 LYS A CD  1 
ATOM   1198  C  CE  . LYS A  1 167 ? -9.56600  -25.16800 -55.17400 1.000 61.62000  ? 198 LYS A CE  1 
ATOM   1199  N  NZ  . LYS A  1 167 ? -9.49700  -23.66900 -55.14700 1.000 65.66000  ? 198 LYS A NZ  1 
ATOM   1200  N  N   . ALA A  1 168 ? -7.22200  -30.12000 -52.06900 1.000 50.59000  ? 199 ALA A N   1 
ATOM   1201  C  CA  . ALA A  1 168 ? -5.79200  -30.37400 -52.01700 1.000 47.30000  ? 199 ALA A CA  1 
ATOM   1202  C  C   . ALA A  1 168 ? -5.47600  -31.85200 -52.11900 1.000 43.61000  ? 199 ALA A C   1 
ATOM   1203  O  O   . ALA A  1 168 ? -4.32600  -32.24300 -51.93700 1.000 47.03000  ? 199 ALA A O   1 
ATOM   1204  C  CB  . ALA A  1 168 ? -5.20200  -29.79700 -50.72800 1.000 42.98000  ? 199 ALA A CB  1 
ATOM   1205  N  N   . GLY A  1 169 ? -6.46900  -32.67300 -52.45000 1.000 47.57000  ? 200 GLY A N   1 
ATOM   1206  C  CA  . GLY A  1 169 ? -6.27000  -34.10900 -52.55500 1.000 48.47000  ? 200 GLY A CA  1 
ATOM   1207  C  C   . GLY A  1 169 ? -5.70900  -34.76800 -51.31300 1.000 47.11000  ? 200 GLY A C   1 
ATOM   1208  O  O   . GLY A  1 169 ? -4.98600  -35.76400 -51.42200 1.000 47.92000  ? 200 GLY A O   1 
ATOM   1209  N  N   . ASN A  1 170 ? -6.05900  -34.26700 -50.13100 1.000 45.89000  ? 201 ASN A N   1 
ATOM   1210  C  CA  . ASN A  1 170 ? -5.67400  -34.89800 -48.87300 1.000 43.25000  ? 201 ASN A CA  1 
ATOM   1211  C  C   . ASN A  1 170 ? -6.26400  -36.29900 -48.82100 1.000 44.34000  ? 201 ASN A C   1 
ATOM   1212  O  O   . ASN A  1 170 ? -7.48700  -36.44800 -48.92800 1.000 48.28000  ? 201 ASN A O   1 
ATOM   1213  C  CB  . ASN A  1 170 ? -6.15500  -34.05100 -47.69200 1.000 42.33000  ? 201 ASN A CB  1 
ATOM   1214  C  CG  . ASN A  1 170 ? -5.77300  -34.63100 -46.31700 1.000 47.74000  ? 201 ASN A CG  1 
ATOM   1215  O  OD1 . ASN A  1 170 ? -5.58400  -35.85600 -46.12200 1.000 39.51000  ? 201 ASN A OD1 1 
ATOM   1216  N  ND2 . ASN A  1 170 ? -5.66800  -33.73400 -45.35000 1.000 43.77000  ? 201 ASN A ND2 1 
ATOM   1217  N  N   . PRO A  1 171 ? -5.44100  -37.34300 -48.70000 1.000 45.15000  ? 202 PRO A N   1 
ATOM   1218  C  CA  . PRO A  1 171 ? -5.95200  -38.71600 -48.66500 1.000 43.65000  ? 202 PRO A CA  1 
ATOM   1219  C  C   . PRO A  1 171 ? -6.40700  -39.17600 -47.28400 1.000 52.78000  ? 202 PRO A C   1 
ATOM   1220  O  O   . PRO A  1 171 ? -6.85600  -40.32000 -47.15300 1.000 51.22000  ? 202 PRO A O   1 
ATOM   1221  C  CB  . PRO A  1 171 ? -4.73800  -39.53200 -49.12700 1.000 42.04000  ? 202 PRO A CB  1 
ATOM   1222  C  CG  . PRO A  1 171 ? -3.57300  -38.76100 -48.59800 1.000 37.84000  ? 202 PRO A CG  1 
ATOM   1223  C  CD  . PRO A  1 171 ? -3.97500  -37.29800 -48.57200 1.000 41.76000  ? 202 PRO A CD  1 
ATOM   1224  N  N   . ASN A  1 172 ? -6.26100  -38.36700 -46.23400 1.000 43.90000  ? 203 ASN A N   1 
ATOM   1225  C  CA  . ASN A  1 172 ? -6.65700  -38.81100 -44.89700 1.000 54.77000  ? 203 ASN A CA  1 
ATOM   1226  C  C   . ASN A  1 172 ? -7.49500  -37.72700 -44.22500 1.000 48.58000  ? 203 ASN A C   1 
ATOM   1227  O  O   . ASN A  1 172 ? -7.17700  -37.23200 -43.14600 1.000 51.55000  ? 203 ASN A O   1 
ATOM   1228  C  CB  . ASN A  1 172 ? -5.42900  -39.15500 -44.04000 1.000 50.79000  ? 203 ASN A CB  1 
ATOM   1229  C  CG  . ASN A  1 172 ? -4.46200  -40.11000 -44.75000 1.000 63.82000  ? 203 ASN A CG  1 
ATOM   1230  O  OD1 . ASN A  1 172 ? -4.86500  -41.18200 -45.23000 1.000 64.93000  ? 203 ASN A OD1 1 
ATOM   1231  N  ND2 . ASN A  1 172 ? -3.17700  -39.72900 -44.80900 1.000 52.28000  ? 203 ASN A ND2 1 
ATOM   1232  N  N   . ILE A  1 173 ? -8.60100  -37.37200 -44.87200 1.000 47.16000  ? 204 ILE A N   1 
ATOM   1233  C  CA  . ILE A  1 173 ? -9.54000  -36.43200 -44.28300 1.000 47.35000  ? 204 ILE A CA  1 
ATOM   1234  C  C   . ILE A  1 173 ? -10.26400 -37.11300 -43.13100 1.000 45.45000  ? 204 ILE A C   1 
ATOM   1235  O  O   . ILE A  1 173 ? -10.74400 -38.24900 -43.26100 1.000 45.93000  ? 204 ILE A O   1 
ATOM   1236  C  CB  . ILE A  1 173 ? -10.52400 -35.93000 -45.34500 1.000 41.92000  ? 204 ILE A CB  1 
ATOM   1237  C  CG1 . ILE A  1 173 ? -9.74800  -35.29300 -46.51700 1.000 43.91000  ? 204 ILE A CG1 1 
ATOM   1238  C  CG2 . ILE A  1 173 ? -11.48600 -34.93400 -44.73100 1.000 39.78000  ? 204 ILE A CG2 1 
ATOM   1239  C  CD1 . ILE A  1 173 ? -10.65000 -34.72600 -47.61800 1.000 43.13000  ? 204 ILE A CD1 1 
ATOM   1240  N  N   . ARG A  1 174 ? -10.33300 -36.43500 -41.99200 1.000 42.81000  ? 205 ARG A N   1 
ATOM   1241  C  CA  . ARG A  1 174 ? -10.98800 -37.03600 -40.83500 1.000 48.58000  ? 205 ARG A CA  1 
ATOM   1242  C  C   . ARG A  1 174 ? -12.49400 -37.09900 -41.08200 1.000 41.49000  ? 205 ARG A C   1 
ATOM   1243  O  O   . ARG A  1 174 ? -13.08500 -36.13600 -41.57500 1.000 37.78000  ? 205 ARG A O   1 
ATOM   1244  C  CB  . ARG A  1 174 ? -10.66300 -36.23200 -39.56900 1.000 45.75000  ? 205 ARG A CB  1 
ATOM   1245  C  CG  . ARG A  1 174 ? -9.15800  -36.20200 -39.21400 1.000 51.02000  ? 205 ARG A CG  1 
ATOM   1246  C  CD  . ARG A  1 174 ? -8.85100  -35.31000 -37.97500 1.000 57.86000  ? 205 ARG A CD  1 
ATOM   1247  N  NE  . ARG A  1 174 ? -9.55100  -35.75800 -36.76800 1.000 59.29000  ? 205 ARG A NE  1 
ATOM   1248  C  CZ  . ARG A  1 174 ? -10.56900 -35.11600 -36.19500 1.000 61.19000  ? 205 ARG A CZ  1 
ATOM   1249  N  NH1 . ARG A  1 174 ? -10.97800 -33.93000 -36.63200 1.000 54.34000  ? 205 ARG A NH1 1 
ATOM   1250  N  NH2 . ARG A  1 174 ? -11.19200 -35.68000 -35.15300 1.000 52.86000  ? 205 ARG A NH2 1 
ATOM   1251  N  N   . ASP A  1 175 ? -13.12500 -38.23400 -40.74600 1.000 39.72000  ? 206 ASP A N   1 
ATOM   1252  C  CA  . ASP A  1 175 ? -14.56300 -38.30000 -41.02600 1.000 44.44000  ? 206 ASP A CA  1 
ATOM   1253  C  C   . ASP A  1 175 ? -15.35800 -37.33200 -40.16300 1.000 42.03000  ? 206 ASP A C   1 
ATOM   1254  O  O   . ASP A  1 175 ? -16.49800 -37.03300 -40.51600 1.000 42.40000  ? 206 ASP A O   1 
ATOM   1255  C  CB  . ASP A  1 175 ? -15.14500 -39.72500 -40.87700 1.000 40.83000  ? 206 ASP A CB  1 
ATOM   1256  C  CG  . ASP A  1 175 ? -14.88100 -40.34100 -39.52300 1.000 44.14000  ? 206 ASP A CG  1 
ATOM   1257  O  OD1 . ASP A  1 175 ? -14.42500 -39.60900 -38.62700 1.000 45.70000  ? 206 ASP A OD1 1 
ATOM   1258  O  OD2 . ASP A  1 175 ? -15.14900 -41.55100 -39.33900 1.000 42.21000  ? 206 ASP A OD2 1 
ATOM   1259  N  N   . TYR A  1 176 ? -14.76000 -36.76800 -39.10500 1.000 37.46000  ? 207 TYR A N   1 
ATOM   1260  C  CA  . TYR A  1 176 ? -15.43800 -35.73600 -38.32000 1.000 37.94000  ? 207 TYR A CA  1 
ATOM   1261  C  C   . TYR A  1 176 ? -15.78900 -34.49500 -39.12800 1.000 46.68000  ? 207 TYR A C   1 
ATOM   1262  O  O   . TYR A  1 176 ? -16.56600 -33.65800 -38.63200 1.000 40.89000  ? 207 TYR A O   1 
ATOM   1263  C  CB  . TYR A  1 176 ? -14.58400 -35.31200 -37.10700 1.000 37.94000  ? 207 TYR A CB  1 
ATOM   1264  C  CG  . TYR A  1 176 ? -14.84000 -36.14100 -35.86100 1.000 38.48000  ? 207 TYR A CG  1 
ATOM   1265  C  CD1 . TYR A  1 176 ? -14.77400 -37.53200 -35.89900 1.000 40.22000  ? 207 TYR A CD1 1 
ATOM   1266  C  CD2 . TYR A  1 176 ? -15.17600 -35.53700 -34.64600 1.000 44.53000  ? 207 TYR A CD2 1 
ATOM   1267  C  CE1 . TYR A  1 176 ? -15.00100 -38.30300 -34.76500 1.000 43.49000  ? 207 TYR A CE1 1 
ATOM   1268  C  CE2 . TYR A  1 176 ? -15.41700 -36.30800 -33.49400 1.000 43.29000  ? 207 TYR A CE2 1 
ATOM   1269  C  CZ  . TYR A  1 176 ? -15.32300 -37.68600 -33.56800 1.000 45.91000  ? 207 TYR A CZ  1 
ATOM   1270  O  OH  . TYR A  1 176 ? -15.56100 -38.46800 -32.46000 1.000 41.92000  ? 207 TYR A OH  1 
ATOM   1271  N  N   . VAL A  1 177 ? -15.24300 -34.33400 -40.33700 1.000 40.44000  ? 208 VAL A N   1 
ATOM   1272  C  CA  . VAL A  1 177 ? -15.57600 -33.18000 -41.15900 1.000 39.06000  ? 208 VAL A CA  1 
ATOM   1273  C  C   . VAL A  1 177 ? -16.24400 -33.55600 -42.47600 1.000 39.76000  ? 208 VAL A C   1 
ATOM   1274  O  O   . VAL A  1 177 ? -16.52300 -32.66000 -43.27500 1.000 40.85000  ? 208 VAL A O   1 
ATOM   1275  C  CB  . VAL A  1 177 ? -14.34300 -32.28500 -41.41800 1.000 37.97000  ? 208 VAL A CB  1 
ATOM   1276  C  CG1 . VAL A  1 177 ? -13.69800 -31.84900 -40.08000 1.000 35.56000  ? 208 VAL A CG1 1 
ATOM   1277  C  CG2 . VAL A  1 177 ? -13.33400 -32.95000 -42.34700 1.000 35.31000  ? 208 VAL A CG2 1 
ATOM   1278  N  N   . PHE A  1 178 ? -16.50000 -34.85000 -42.73500 1.000 38.44000  ? 209 PHE A N   1 
ATOM   1279  C  CA  . PHE A  1 178 ? -17.22400 -35.26100 -43.94300 1.000 43.76000  ? 209 PHE A CA  1 
ATOM   1280  C  C   . PHE A  1 178 ? -18.57800 -34.57300 -43.99000 1.000 40.42000  ? 209 PHE A C   1 
ATOM   1281  O  O   . PHE A  1 178 ? -19.21700 -34.37900 -42.95600 1.000 39.79000  ? 209 PHE A O   1 
ATOM   1282  C  CB  . PHE A  1 178 ? -17.50400 -36.76800 -43.99500 1.000 39.71000  ? 209 PHE A CB  1 
ATOM   1283  C  CG  . PHE A  1 178 ? -16.31300 -37.61300 -44.26100 1.000 41.89000  ? 209 PHE A CG  1 
ATOM   1284  C  CD1 . PHE A  1 178 ? -15.07100 -37.04900 -44.48300 1.000 39.99000  ? 209 PHE A CD1 1 
ATOM   1285  C  CD2 . PHE A  1 178 ? -16.42400 -38.99300 -44.21100 1.000 45.86000  ? 209 PHE A CD2 1 
ATOM   1286  C  CE1 . PHE A  1 178 ? -13.97400 -37.84600 -44.69800 1.000 40.09000  ? 209 PHE A CE1 1 
ATOM   1287  C  CE2 . PHE A  1 178 ? -15.32400 -39.80200 -44.42100 1.000 43.81000  ? 209 PHE A CE2 1 
ATOM   1288  C  CZ  . PHE A  1 178 ? -14.09900 -39.22600 -44.66300 1.000 43.91000  ? 209 PHE A CZ  1 
ATOM   1289  N  N   . PRO A  1 179 ? -19.06100 -34.25100 -45.17900 1.000 42.97000  ? 210 PRO A N   1 
ATOM   1290  C  CA  . PRO A  1 179 ? -20.44500 -33.77800 -45.30500 1.000 38.65000  ? 210 PRO A CA  1 
ATOM   1291  C  C   . PRO A  1 179 ? -21.40200 -34.79700 -44.71200 1.000 41.88000  ? 210 PRO A C   1 
ATOM   1292  O  O   . PRO A  1 179 ? -21.20800 -36.00800 -44.85400 1.000 41.39000  ? 210 PRO A O   1 
ATOM   1293  C  CB  . PRO A  1 179 ? -20.64300 -33.65800 -46.82300 1.000 37.34000  ? 210 PRO A CB  1 
ATOM   1294  C  CG  . PRO A  1 179 ? -19.24700 -33.52500 -47.39300 1.000 48.64000  ? 210 PRO A CG  1 
ATOM   1295  C  CD  . PRO A  1 179 ? -18.34900 -34.31300 -46.46600 1.000 46.33000  ? 210 PRO A CD  1 
ATOM   1296  N  N   . MET A  1 180 ? -22.43100 -34.30600 -44.02700 1.000 39.48000  ? 211 MET A N   1 
ATOM   1297  C  CA  . MET A  1 180 ? -23.46700 -35.23400 -43.60600 1.000 43.72000  ? 211 MET A CA  1 
ATOM   1298  C  C   . MET A  1 180 ? -24.34800 -35.55100 -44.80700 1.000 42.03000  ? 211 MET A C   1 
ATOM   1299  O  O   . MET A  1 180 ? -24.26400 -34.91300 -45.85900 1.000 40.50000  ? 211 MET A O   1 
ATOM   1300  C  CB  . MET A  1 180 ? -24.29500 -34.66900 -42.44800 1.000 43.33000  ? 211 MET A CB  1 
ATOM   1301  C  CG  . MET A  1 180 ? -23.45400 -34.34700 -41.19800 1.000 39.22000  ? 211 MET A CG  1 
ATOM   1302  S  SD  . MET A  1 180 ? -24.40600 -34.08900 -39.68500 1.000 40.10000  ? 211 MET A SD  1 
ATOM   1303  C  CE  . MET A  1 180 ? -25.38900 -32.65500 -40.08300 1.000 41.14000  ? 211 MET A CE  1 
ATOM   1304  N  N   . GLU A  1 181 ? -25.20700 -36.53700 -44.64100 1.000 39.80000  ? 212 GLU A N   1 
ATOM   1305  C  CA  . GLU A  1 181 ? -26.01100 -37.02700 -45.74000 1.000 43.45000  ? 212 GLU A CA  1 
ATOM   1306  C  C   . GLU A  1 181 ? -27.46900 -37.12000 -45.31700 1.000 43.79000  ? 212 GLU A C   1 
ATOM   1307  O  O   . GLU A  1 181 ? -27.79900 -37.27200 -44.13300 1.000 41.83000  ? 212 GLU A O   1 
ATOM   1308  C  CB  . GLU A  1 181 ? -25.54000 -38.40000 -46.20900 1.000 38.21000  ? 212 GLU A CB  1 
ATOM   1309  C  CG  . GLU A  1 181 ? -25.77500 -39.47500 -45.16000 1.000 44.93000  ? 212 GLU A CG  1 
ATOM   1310  C  CD  . GLU A  1 181 ? -25.66700 -40.87400 -45.71900 1.000 46.86000  ? 212 GLU A CD  1 
ATOM   1311  O  OE1 . GLU A  1 181 ? -24.52500 -41.34200 -45.92900 1.000 50.61000  ? 212 GLU A OE1 1 
ATOM   1312  O  OE2 . GLU A  1 181 ? -26.72900 -41.50100 -45.96000 1.000 49.35000  ? 212 GLU A OE2 1 
ATOM   1313  N  N   . HIS A  1 182 ? -28.32600 -37.05600 -46.32600 1.000 43.08000  ? 213 HIS A N   1 
ATOM   1314  C  CA  . HIS A  1 182 ? -29.76600 -37.29400 -46.22100 1.000 45.59000  ? 213 HIS A CA  1 
ATOM   1315  C  C   . HIS A  1 182 ? -30.09000 -38.40200 -47.21800 1.000 44.04000  ? 213 HIS A C   1 
ATOM   1316  O  O   . HIS A  1 182 ? -30.13600 -38.16400 -48.42800 1.000 46.73000  ? 213 HIS A O   1 
ATOM   1317  C  CB  . HIS A  1 182 ? -30.57200 -36.03100 -46.50800 1.000 46.41000  ? 213 HIS A CB  1 
ATOM   1318  C  CG  . HIS A  1 182 ? -32.05200 -36.20300 -46.33500 1.000 44.65000  ? 213 HIS A CG  1 
ATOM   1319  N  ND1 . HIS A  1 182 ? -32.96900 -35.37500 -46.94200 1.000 47.69000  ? 213 HIS A ND1 1 
ATOM   1320  C  CD2 . HIS A  1 182 ? -32.77300 -37.10700 -45.62600 1.000 47.51000  ? 213 HIS A CD2 1 
ATOM   1321  C  CE1 . HIS A  1 182 ? -34.19300 -35.76600 -46.62700 1.000 52.37000  ? 213 HIS A CE1 1 
ATOM   1322  N  NE2 . HIS A  1 182 ? -34.10500 -36.81900 -45.83500 1.000 48.73000  ? 213 HIS A NE2 1 
ATOM   1323  N  N   . ASN A  1 183 ? -30.20400 -39.62600 -46.71700 1.000 41.90000  ? 214 ASN A N   1 
ATOM   1324  C  CA  . ASN A  1 183 ? -30.50400 -40.79600 -47.54100 1.000 50.28000  ? 214 ASN A CA  1 
ATOM   1325  C  C   . ASN A  1 183 ? -29.51200 -40.93100 -48.68900 1.000 44.15000  ? 214 ASN A C   1 
ATOM   1326  O  O   . ASN A  1 183 ? -29.88900 -41.13100 -49.83800 1.000 42.85000  ? 214 ASN A O   1 
ATOM   1327  C  CB  . ASN A  1 183 ? -31.94100 -40.77400 -48.07300 1.000 40.56000  ? 214 ASN A CB  1 
ATOM   1328  C  CG  . ASN A  1 183 ? -32.96400 -40.90300 -46.97200 1.000 49.77000  ? 214 ASN A CG  1 
ATOM   1329  O  OD1 . ASN A  1 183 ? -32.81600 -41.72100 -46.04500 1.000 47.48000  ? 214 ASN A OD1 1 
ATOM   1330  N  ND2 . ASN A  1 183 ? -34.03700 -40.11900 -47.08100 1.000 48.10000  ? 214 ASN A ND2 1 
ATOM   1331  N  N   . GLY A  1 184 ? -28.23800 -40.75500 -48.40100 1.000 44.56000  ? 215 GLY A N   1 
ATOM   1332  C  CA  . GLY A  1 184 ? -27.22700 -40.96600 -49.41200 1.000 43.94000  ? 215 GLY A CA  1 
ATOM   1333  C  C   . GLY A  1 184 ? -26.86000 -39.74400 -50.22400 1.000 45.68000  ? 215 GLY A C   1 
ATOM   1334  O  O   . GLY A  1 184 ? -25.82700 -39.76000 -50.89700 1.000 56.56000  ? 215 GLY A O   1 
ATOM   1335  N  N   . LYS A  1 185 ? -27.66200 -38.68400 -50.17500 1.000 46.29000  ? 216 LYS A N   1 
ATOM   1336  C  CA  . LYS A  1 185 ? -27.38800 -37.42800 -50.86000 1.000 48.82000  ? 216 LYS A CA  1 
ATOM   1337  C  C   . LYS A  1 185 ? -26.80800 -36.42300 -49.87200 1.000 46.72000  ? 216 LYS A C   1 
ATOM   1338  O  O   . LYS A  1 185 ? -26.92100 -36.60800 -48.66200 1.000 46.51000  ? 216 LYS A O   1 
ATOM   1339  C  CB  . LYS A  1 185 ? -28.67200 -36.85800 -51.49000 1.000 36.31000  ? 216 LYS A CB  1 
ATOM   1340  C  CG  . LYS A  1 185 ? -29.27400 -37.70500 -52.60100 1.000 50.88000  ? 216 LYS A CG  1 
ATOM   1341  C  CD  . LYS A  1 185 ? -28.21200 -38.08700 -53.65000 1.000 60.66000  ? 216 LYS A CD  1 
ATOM   1342  C  CE  . LYS A  1 185 ? -27.47900 -36.86500 -54.28500 1.000 60.37000  ? 216 LYS A CE  1 
ATOM   1343  N  NZ  . LYS A  1 185 ? -25.96000 -37.03500 -54.37900 1.000 59.47000  ? 216 LYS A NZ  1 
ATOM   1344  N  N   . PRO A  1 186 ? -26.10000 -35.39400 -50.33700 1.000 51.14000  ? 217 PRO A N   1 
ATOM   1345  C  CA  . PRO A  1 186 ? -25.54900 -34.40000 -49.39600 1.000 43.12000  ? 217 PRO A CA  1 
ATOM   1346  C  C   . PRO A  1 186 ? -26.64500 -33.72600 -48.58300 1.000 48.81000  ? 217 PRO A C   1 
ATOM   1347  O  O   . PRO A  1 186 ? -27.71400 -33.39700 -49.10000 1.000 45.36000  ? 217 PRO A O   1 
ATOM   1348  C  CB  . PRO A  1 186 ? -24.81500 -33.40100 -50.31000 1.000 44.00000  ? 217 PRO A CB  1 
ATOM   1349  C  CG  . PRO A  1 186 ? -25.30200 -33.70800 -51.72500 1.000 48.35000  ? 217 PRO A CG  1 
ATOM   1350  C  CD  . PRO A  1 186 ? -25.60100 -35.18800 -51.71200 1.000 48.99000  ? 217 PRO A CD  1 
ATOM   1351  N  N   . ALA A  1 187 ? -26.37100 -33.53200 -47.28400 1.000 46.16000  ? 218 ALA A N   1 
ATOM   1352  C  CA  . ALA A  1 187 ? -27.35100 -32.92000 -46.38700 1.000 45.22000  ? 218 ALA A CA  1 
ATOM   1353  C  C   . ALA A  1 187 ? -27.39800 -31.40600 -46.52000 1.000 45.94000  ? 218 ALA A C   1 
ATOM   1354  O  O   . ALA A  1 187 ? -28.44000 -30.79800 -46.24400 1.000 45.60000  ? 218 ALA A O   1 
ATOM   1355  C  CB  . ALA A  1 187 ? -27.04400 -33.28600 -44.92700 1.000 45.13000  ? 218 ALA A CB  1 
ATOM   1356  N  N   . ASN A  1 188 ? -26.27500 -30.78700 -46.89800 1.000 47.02000  ? 219 ASN A N   1 
ATOM   1357  C  CA  . ASN A  1 188 ? -26.15000 -29.33100 -46.96900 1.000 45.25000  ? 219 ASN A CA  1 
ATOM   1358  C  C   . ASN A  1 188 ? -26.64400 -28.68600 -45.67300 1.000 48.18000  ? 219 ASN A C   1 
ATOM   1359  O  O   . ASN A  1 188 ? -27.54000 -27.83300 -45.67200 1.000 42.76000  ? 219 ASN A O   1 
ATOM   1360  C  CB  . ASN A  1 188 ? -26.89800 -28.77500 -48.17700 1.000 43.26000  ? 219 ASN A CB  1 
ATOM   1361  C  CG  . ASN A  1 188 ? -26.39600 -29.36200 -49.47800 1.000 48.64000  ? 219 ASN A CG  1 
ATOM   1362  O  OD1 . ASN A  1 188 ? -27.15100 -30.00400 -50.20900 1.000 52.91000  ? 219 ASN A OD1 1 
ATOM   1363  N  ND2 . ASN A  1 188 ? -25.11100 -29.19900 -49.74600 1.000 43.74000  ? 219 ASN A ND2 1 
ATOM   1364  N  N   . GLU A  1 189 ? -26.07600 -29.13600 -44.55100 1.000 46.16000  ? 220 GLU A N   1 
ATOM   1365  C  CA  . GLU A  1 189 ? -26.47700 -28.60200 -43.25700 1.000 40.81000  ? 220 GLU A CA  1 
ATOM   1366  C  C   . GLU A  1 189 ? -26.03600 -27.14700 -43.12700 1.000 44.60000  ? 220 GLU A C   1 
ATOM   1367  O  O   . GLU A  1 189 ? -24.93000 -26.77500 -43.53300 1.000 41.64000  ? 220 GLU A O   1 
ATOM   1368  C  CB  . GLU A  1 189 ? -25.87900 -29.44200 -42.12600 1.000 40.48000  ? 220 GLU A CB  1 
ATOM   1369  C  CG  . GLU A  1 189 ? -26.25400 -28.94700 -40.71900 1.000 40.40000  ? 220 GLU A CG  1 
ATOM   1370  C  CD  . GLU A  1 189 ? -27.75400 -28.89300 -40.51700 1.000 43.29000  ? 220 GLU A CD  1 
ATOM   1371  O  OE1 . GLU A  1 189 ? -28.40200 -29.96900 -40.53400 1.000 46.71000  ? 220 GLU A OE1 1 
ATOM   1372  O  OE2 . GLU A  1 189 ? -28.29500 -27.77000 -40.39800 1.000 48.96000  ? 220 GLU A OE2 1 
ATOM   1373  N  N   . THR A  1 190 ? -26.88200 -26.32700 -42.50700 1.000 47.33000  ? 221 THR A N   1 
ATOM   1374  C  CA  . THR A  1 190 ? -26.58500 -24.91100 -42.33700 1.000 47.69000  ? 221 THR A CA  1 
ATOM   1375  C  C   . THR A  1 190 ? -26.60300 -24.41200 -40.89300 1.000 51.50000  ? 221 THR A C   1 
ATOM   1376  O  O   . THR A  1 190 ? -26.44200 -23.20400 -40.67300 1.000 50.23000  ? 221 THR A O   1 
ATOM   1377  C  CB  . THR A  1 190 ? -27.58200 -24.07700 -43.14600 1.000 49.05000  ? 221 THR A CB  1 
ATOM   1378  O  OG1 . THR A  1 190 ? -28.90700 -24.39200 -42.69900 1.000 47.96000  ? 221 THR A OG1 1 
ATOM   1379  C  CG2 . THR A  1 190 ? -27.44300 -24.35200 -44.65000 1.000 47.69000  ? 221 THR A CG2 1 
ATOM   1380  N  N   . GLU A  1 191 ? -26.82800 -25.26700 -39.90500 1.000 47.68000  ? 222 GLU A N   1 
ATOM   1381  C  CA  . GLU A  1 191 ? -26.80100 -24.78100 -38.53200 1.000 49.05000  ? 222 GLU A CA  1 
ATOM   1382  C  C   . GLU A  1 191 ? -26.10000 -25.79300 -37.63500 1.000 44.10000  ? 222 GLU A C   1 
ATOM   1383  O  O   . GLU A  1 191 ? -25.87100 -26.94100 -38.01500 1.000 39.50000  ? 222 GLU A O   1 
ATOM   1384  C  CB  . GLU A  1 191 ? -28.21200 -24.42000 -38.02200 1.000 55.13000  ? 222 GLU A CB  1 
ATOM   1385  C  CG  . GLU A  1 191 ? -29.24600 -25.52600 -37.95000 1.000 49.59000  ? 222 GLU A CG  1 
ATOM   1386  C  CD  . GLU A  1 191 ? -30.64400 -24.98700 -37.58400 1.000 49.29000  ? 222 GLU A CD  1 
ATOM   1387  O  OE1 . GLU A  1 191 ? -30.73400 -23.85300 -37.08400 1.000 54.10000  ? 222 GLU A OE1 1 
ATOM   1388  O  OE2 . GLU A  1 191 ? -31.65100 -25.70700 -37.75800 1.000 54.35000  ? 222 GLU A OE2 1 
ATOM   1389  N  N   . TYR A  1 192 ? -25.70800 -25.31900 -36.45100 1.000 43.75000  ? 223 TYR A N   1 
ATOM   1390  C  CA  . TYR A  1 192 ? -25.25900 -26.14500 -35.33300 1.000 38.91000  ? 223 TYR A CA  1 
ATOM   1391  C  C   . TYR A  1 192 ? -25.99600 -27.47600 -35.35000 1.000 42.18000  ? 223 TYR A C   1 
ATOM   1392  O  O   . TYR A  1 192 ? -27.23200 -27.49700 -35.23500 1.000 38.77000  ? 223 TYR A O   1 
ATOM   1393  C  CB  . TYR A  1 192 ? -25.53200 -25.40100 -34.01400 1.000 45.07000  ? 223 TYR A CB  1 
ATOM   1394  C  CG  . TYR A  1 192 ? -24.96200 -26.01000 -32.73700 1.000 39.87000  ? 223 TYR A CG  1 
ATOM   1395  C  CD1 . TYR A  1 192 ? -23.60200 -26.15500 -32.57200 1.000 37.79000  ? 223 TYR A CD1 1 
ATOM   1396  C  CD2 . TYR A  1 192 ? -25.80000 -26.41900 -31.68700 1.000 37.08000  ? 223 TYR A CD2 1 
ATOM   1397  C  CE1 . TYR A  1 192 ? -23.06200 -26.67800 -31.40700 1.000 38.34000  ? 223 TYR A CE1 1 
ATOM   1398  C  CE2 . TYR A  1 192 ? -25.27200 -26.95800 -30.52100 1.000 37.37000  ? 223 TYR A CE2 1 
ATOM   1399  C  CZ  . TYR A  1 192 ? -23.89100 -27.07400 -30.39000 1.000 41.50000  ? 223 TYR A CZ  1 
ATOM   1400  O  OH  . TYR A  1 192 ? -23.30500 -27.59200 -29.26200 1.000 33.53000  ? 223 TYR A OH  1 
ATOM   1401  N  N   . ILE A  1 193 ? -25.26700 -28.58600 -35.52800 1.000 38.93000  ? 224 ILE A N   1 
ATOM   1402  C  CA  . ILE A  1 193 ? -25.93400 -29.81700 -35.95500 1.000 36.46000  ? 224 ILE A CA  1 
ATOM   1403  C  C   . ILE A  1 193 ? -26.91600 -30.33500 -34.91500 1.000 38.22000  ? 224 ILE A C   1 
ATOM   1404  O  O   . ILE A  1 193 ? -27.88800 -31.02000 -35.26600 1.000 43.42000  ? 224 ILE A O   1 
ATOM   1405  C  CB  . ILE A  1 193 ? -24.90900 -30.89100 -36.35200 1.000 40.05000  ? 224 ILE A CB  1 
ATOM   1406  C  CG1 . ILE A  1 193 ? -24.00700 -31.27900 -35.17600 1.000 37.82000  ? 224 ILE A CG1 1 
ATOM   1407  C  CG2 . ILE A  1 193 ? -24.14700 -30.47700 -37.59900 1.000 37.78000  ? 224 ILE A CG2 1 
ATOM   1408  C  CD1 . ILE A  1 193 ? -22.99300 -32.34700 -35.56400 1.000 34.99000  ? 224 ILE A CD1 1 
ATOM   1409  N  N   . THR A  1 194 ? -26.70800 -30.01600 -33.63500 1.000 32.67000  ? 225 THR A N   1 
ATOM   1410  C  CA  . THR A  1 194 ? -27.71900 -30.35400 -32.64800 1.000 36.13000  ? 225 THR A CA  1 
ATOM   1411  C  C   . THR A  1 194 ? -29.05100 -29.70700 -33.00700 1.000 36.58000  ? 225 THR A C   1 
ATOM   1412  O  O   . THR A  1 194 ? -30.09800 -30.36300 -32.98900 1.000 34.26000  ? 225 THR A O   1 
ATOM   1413  C  CB  . THR A  1 194 ? -27.28100 -29.90600 -31.25900 1.000 34.87000  ? 225 THR A CB  1 
ATOM   1414  O  OG1 . THR A  1 194 ? -26.12200 -30.65100 -30.85600 1.000 33.09000  ? 225 THR A OG1 1 
ATOM   1415  C  CG2 . THR A  1 194 ? -28.42200 -30.14500 -30.25700 1.000 30.53000  ? 225 THR A CG2 1 
ATOM   1416  N  N   . ASP A  1 195 ? -29.02200 -28.41900 -33.34900 1.000 33.01000  ? 226 ASP A N   1 
ATOM   1417  C  CA  . ASP A  1 195 ? -30.22900 -27.75900 -33.81700 1.000 40.94000  ? 226 ASP A CA  1 
ATOM   1418  C  C   . ASP A  1 195 ? -30.68900 -28.37200 -35.12500 1.000 41.47000  ? 226 ASP A C   1 
ATOM   1419  O  O   . ASP A  1 195 ? -31.89400 -28.55900 -35.34600 1.000 44.73000  ? 226 ASP A O   1 
ATOM   1420  C  CB  . ASP A  1 195 ? -29.97400 -26.26400 -34.01600 1.000 41.04000  ? 226 ASP A CB  1 
ATOM   1421  C  CG  . ASP A  1 195 ? -29.76800 -25.52400 -32.71700 1.000 47.83000  ? 226 ASP A CG  1 
ATOM   1422  O  OD1 . ASP A  1 195 ? -30.15000 -26.05600 -31.64500 1.000 54.07000  ? 226 ASP A OD1 1 
ATOM   1423  O  OD2 . ASP A  1 195 ? -29.22100 -24.40100 -32.76600 1.000 44.55000  ? 226 ASP A OD2 1 
ATOM   1424  N  N   . GLY A  1 196 ? -29.73500 -28.74200 -35.98300 1.000 41.72000  ? 227 GLY A N   1 
ATOM   1425  C  CA  . GLY A  1 196 ? -30.09900 -29.37100 -37.23700 1.000 38.98000  ? 227 GLY A CA  1 
ATOM   1426  C  C   . GLY A  1 196 ? -30.79600 -30.70000 -37.01400 1.000 42.89000  ? 227 GLY A C   1 
ATOM   1427  O  O   . GLY A  1 196 ? -31.76700 -31.02800 -37.69700 1.000 42.15000  ? 227 GLY A O   1 
ATOM   1428  N  N   . PHE A  1 197 ? -30.32300 -31.47400 -36.03700 1.000 39.83000  ? 228 PHE A N   1 
ATOM   1429  C  CA  . PHE A  1 197 ? -30.95700 -32.75400 -35.76200 1.000 39.37000  ? 228 PHE A CA  1 
ATOM   1430  C  C   . PHE A  1 197 ? -32.35500 -32.56800 -35.18400 1.000 42.03000  ? 228 PHE A C   1 
ATOM   1431  O  O   . PHE A  1 197 ? -33.27100 -33.33400 -35.49500 1.000 39.03000  ? 228 PHE A O   1 
ATOM   1432  C  CB  . PHE A  1 197 ? -30.07000 -33.56700 -34.82400 1.000 31.54000  ? 228 PHE A CB  1 
ATOM   1433  C  CG  . PHE A  1 197 ? -28.73200 -33.93000 -35.42700 1.000 38.45000  ? 228 PHE A CG  1 
ATOM   1434  C  CD1 . PHE A  1 197 ? -28.61500 -34.16400 -36.80600 1.000 38.71000  ? 228 PHE A CD1 1 
ATOM   1435  C  CD2 . PHE A  1 197 ? -27.59500 -34.03400 -34.62700 1.000 35.95000  ? 228 PHE A CD2 1 
ATOM   1436  C  CE1 . PHE A  1 197 ? -27.40100 -34.49600 -37.37400 1.000 40.76000  ? 228 PHE A CE1 1 
ATOM   1437  C  CE2 . PHE A  1 197 ? -26.37000 -34.36700 -35.18400 1.000 36.35000  ? 228 PHE A CE2 1 
ATOM   1438  C  CZ  . PHE A  1 197 ? -26.27600 -34.60800 -36.57800 1.000 33.85000  ? 228 PHE A CZ  1 
ATOM   1439  N  N   . SER A  1 198 ? -32.54800 -31.55800 -34.34400 1.000 41.63000  ? 229 SER A N   1 
ATOM   1440  C  CA  . SER A  1 198 ? -33.88600 -31.32400 -33.81900 1.000 41.51000  ? 229 SER A CA  1 
ATOM   1441  C  C   . SER A  1 198 ? -34.84100 -30.97400 -34.94800 1.000 36.61000  ? 229 SER A C   1 
ATOM   1442  O  O   . SER A  1 198 ? -35.95800 -31.50500 -35.01500 1.000 41.62000  ? 229 SER A O   1 
ATOM   1443  C  CB  . SER A  1 198 ? -33.86400 -30.21800 -32.76600 1.000 36.01000  ? 229 SER A CB  1 
ATOM   1444  O  OG  . SER A  1 198 ? -32.87800 -30.49800 -31.79400 1.000 46.33000  ? 229 SER A OG  1 
ATOM   1445  N  N   . ARG A  1 199 ? -34.40900 -30.09600 -35.85100 1.000 35.54000  ? 230 ARG A N   1 
ATOM   1446  C  CA  . ARG A  1 199 ? -35.26200 -29.70200 -36.97600 1.000 47.95000  ? 230 ARG A CA  1 
ATOM   1447  C  C   . ARG A  1 199 ? -35.68500 -30.91900 -37.79800 1.000 41.62000  ? 230 ARG A C   1 
ATOM   1448  O  O   . ARG A  1 199 ? -36.85500 -31.04600 -38.18100 1.000 41.04000  ? 230 ARG A O   1 
ATOM   1449  C  CB  . ARG A  1 199 ? -34.53000 -28.67100 -37.84700 1.000 48.50000  ? 230 ARG A CB  1 
ATOM   1450  C  CG  . ARG A  1 199 ? -35.19000 -28.33400 -39.19100 1.000 40.54000  ? 230 ARG A CG  1 
ATOM   1451  C  CD  . ARG A  1 199 ? -34.21000 -28.65600 -40.32800 1.000 44.15000  ? 230 ARG A CD  1 
ATOM   1452  N  NE  . ARG A  1 199 ? -32.99800 -27.86800 -40.17900 1.000 52.23000  ? 230 ARG A NE  1 
ATOM   1453  C  CZ  . ARG A  1 199 ? -31.76600 -28.27900 -40.44900 1.000 47.38000  ? 230 ARG A CZ  1 
ATOM   1454  N  NH1 . ARG A  1 199 ? -31.52100 -29.48400 -40.94200 1.000 39.91000  ? 230 ARG A NH1 1 
ATOM   1455  N  NH2 . ARG A  1 199 ? -30.74900 -27.46700 -40.18500 1.000 49.28000  ? 230 ARG A NH2 1 
ATOM   1456  N  N   . GLU A  1 200 ? -34.77100 -31.87200 -37.98700 1.000 39.72000  ? 231 GLU A N   1 
ATOM   1457  C  CA  . GLU A  1 200 ? -35.09800 -33.08600 -38.72900 1.000 39.04000  ? 231 GLU A CA  1 
ATOM   1458  C  C   . GLU A  1 200 ? -36.07500 -33.97900 -37.97100 1.000 41.77000  ? 231 GLU A C   1 
ATOM   1459  O  O   . GLU A  1 200 ? -36.88500 -34.68200 -38.58700 1.000 44.42000  ? 231 GLU A O   1 
ATOM   1460  C  CB  . GLU A  1 200 ? -33.82300 -33.87200 -39.01500 1.000 38.41000  ? 231 GLU A CB  1 
ATOM   1461  C  CG  . GLU A  1 200 ? -32.85900 -33.18000 -39.96600 1.000 39.76000  ? 231 GLU A CG  1 
ATOM   1462  C  CD  . GLU A  1 200 ? -33.50900 -32.83500 -41.29900 1.000 49.49000  ? 231 GLU A CD  1 
ATOM   1463  O  OE1 . GLU A  1 200 ? -34.19800 -33.73300 -41.85600 1.000 43.57000  ? 231 GLU A OE1 1 
ATOM   1464  O  OE2 . GLU A  1 200 ? -33.30600 -31.68600 -41.78300 1.000 45.26000  ? 231 GLU A OE2 1 
ATOM   1465  N  N   . ALA A  1 201 ? -35.97700 -34.02800 -36.64200 1.000 38.75000  ? 232 ALA A N   1 
ATOM   1466  C  CA  . ALA A  1 201 ? -36.94600 -34.81900 -35.89600 1.000 41.74000  ? 232 ALA A CA  1 
ATOM   1467  C  C   . ALA A  1 201 ? -38.34300 -34.23300 -36.06000 1.000 40.97000  ? 232 ALA A C   1 
ATOM   1468  O  O   . ALA A  1 201 ? -39.31400 -34.96400 -36.25900 1.000 40.84000  ? 232 ALA A O   1 
ATOM   1469  C  CB  . ALA A  1 201 ? -36.54700 -34.89300 -34.41900 1.000 32.14000  ? 232 ALA A CB  1 
ATOM   1470  N  N   . ILE A  1 202 ? -38.44300 -32.90400 -36.01000 1.000 43.42000  ? 233 ILE A N   1 
ATOM   1471  C  CA  . ILE A  1 202 ? -39.71300 -32.23100 -36.20900 1.000 40.82000  ? 233 ILE A CA  1 
ATOM   1472  C  C   . ILE A  1 202 ? -40.23600 -32.52900 -37.60600 1.000 47.27000  ? 233 ILE A C   1 
ATOM   1473  O  O   . ILE A  1 202 ? -41.40400 -32.90000 -37.78800 1.000 47.64000  ? 233 ILE A O   1 
ATOM   1474  C  CB  . ILE A  1 202 ? -39.54400 -30.71600 -35.97800 1.000 40.61000  ? 233 ILE A CB  1 
ATOM   1475  C  CG1 . ILE A  1 202 ? -39.34500 -30.41000 -34.49900 1.000 48.14000  ? 233 ILE A CG1 1 
ATOM   1476  C  CG2 . ILE A  1 202 ? -40.75400 -29.94800 -36.49600 1.000 44.38000  ? 233 ILE A CG2 1 
ATOM   1477  C  CD1 . ILE A  1 202 ? -38.80500 -29.00800 -34.24800 1.000 42.66000  ? 233 ILE A CD1 1 
ATOM   1478  N  N   . LYS A  1 203 ? -39.35500 -32.43700 -38.60700 1.000 47.76000  ? 234 LYS A N   1 
ATOM   1479  C  CA  . LYS A  1 203 ? -39.75300 -32.72400 -39.97500 1.000 44.42000  ? 234 LYS A CA  1 
ATOM   1480  C  C   . LYS A  1 203 ? -40.25100 -34.15400 -40.10900 1.000 41.14000  ? 234 LYS A C   1 
ATOM   1481  O  O   . LYS A  1 203 ? -41.26100 -34.40600 -40.77100 1.000 45.84000  ? 234 LYS A O   1 
ATOM   1482  C  CB  . LYS A  1 203 ? -38.59200 -32.45000 -40.92800 1.000 45.43000  ? 234 LYS A CB  1 
ATOM   1483  C  CG  . LYS A  1 203 ? -38.87600 -32.83200 -42.38300 1.000 52.14000  ? 234 LYS A CG  1 
ATOM   1484  C  CD  . LYS A  1 203 ? -37.71600 -32.43700 -43.31500 1.000 52.03000  ? 234 LYS A CD  1 
ATOM   1485  C  CE  . LYS A  1 203 ? -37.99900 -32.86400 -44.76500 1.000 58.23000  ? 234 LYS A CE  1 
ATOM   1486  N  NZ  . LYS A  1 203 ? -36.87600 -32.53000 -45.69600 1.000 68.58000  ? 234 LYS A NZ  1 
ATOM   1487  N  N   . ASN A  1 204 ? -39.56800 -35.10600 -39.48700 1.000 43.23000  ? 235 ASN A N   1 
ATOM   1488  C  CA  . ASN A  1 204 ? -40.02600 -36.48500 -39.61700 1.000 45.12000  ? 235 ASN A CA  1 
ATOM   1489  C  C   . ASN A  1 204 ? -41.31700 -36.74900 -38.83700 1.000 47.08000  ? 235 ASN A C   1 
ATOM   1490  O  O   . ASN A  1 204 ? -42.08100 -37.64000 -39.21500 1.000 39.73000  ? 235 ASN A O   1 
ATOM   1491  C  CB  . ASN A  1 204 ? -38.92500 -37.44400 -39.19500 1.000 43.82000  ? 235 ASN A CB  1 
ATOM   1492  C  CG  . ASN A  1 204 ? -37.86300 -37.59200 -40.26800 1.000 47.21000  ? 235 ASN A CG  1 
ATOM   1493  O  OD1 . ASN A  1 204 ? -37.98800 -38.41700 -41.17200 1.000 46.16000  ? 235 ASN A OD1 1 
ATOM   1494  N  ND2 . ASN A  1 204 ? -36.82400 -36.76700 -40.18600 1.000 35.95000  ? 235 ASN A ND2 1 
ATOM   1495  N  N   . ILE A  1 205 ? -41.57900 -36.00300 -37.75400 1.000 45.93000  ? 236 ILE A N   1 
ATOM   1496  C  CA  . ILE A  1 205 ? -42.84800 -36.16500 -37.04400 1.000 42.61000  ? 236 ILE A CA  1 
ATOM   1497  C  C   . ILE A  1 205 ? -44.01200 -35.73700 -37.93700 1.000 42.93000  ? 236 ILE A C   1 
ATOM   1498  O  O   . ILE A  1 205 ? -45.04400 -36.41800 -38.01100 1.000 43.86000  ? 236 ILE A O   1 
ATOM   1499  C  CB  . ILE A  1 205 ? -42.81300 -35.36400 -35.72300 1.000 42.97000  ? 236 ILE A CB  1 
ATOM   1500  C  CG1 . ILE A  1 205 ? -41.88200 -36.03200 -34.69900 1.000 40.10000  ? 236 ILE A CG1 1 
ATOM   1501  C  CG2 . ILE A  1 205 ? -44.19400 -35.18600 -35.15500 1.000 34.77000  ? 236 ILE A CG2 1 
ATOM   1502  C  CD1 . ILE A  1 205 ? -41.53300 -35.15200 -33.52000 1.000 37.56000  ? 236 ILE A CD1 1 
ATOM   1503  N  N   . LYS A  1 206 ? -43.84400 -34.62500 -38.66400 1.000 42.61000  ? 237 LYS A N   1 
ATOM   1504  C  CA  . LYS A  1 206 ? -44.87700 -34.16700 -39.58500 1.000 41.70000  ? 237 LYS A CA  1 
ATOM   1505  C  C   . LYS A  1 206 ? -45.05800 -35.12900 -40.75500 1.000 44.73000  ? 237 LYS A C   1 
ATOM   1506  O  O   . LYS A  1 206 ? -46.18500 -35.34800 -41.20100 1.000 50.23000  ? 237 LYS A O   1 
ATOM   1507  C  CB  . LYS A  1 206 ? -44.53300 -32.77400 -40.07700 1.000 34.89000  ? 237 LYS A CB  1 
ATOM   1508  C  CG  . LYS A  1 206 ? -44.69300 -31.74000 -39.02000 1.000 40.04000  ? 237 LYS A CG  1 
ATOM   1509  C  CD  . LYS A  1 206 ? -44.02300 -30.46800 -39.47200 1.000 42.15000  ? 237 LYS A CD  1 
ATOM   1510  C  CE  . LYS A  1 206 ? -44.44100 -29.27900 -38.65600 1.000 53.01000  ? 237 LYS A CE  1 
ATOM   1511  N  NZ  . LYS A  1 206 ? -43.48300 -28.14000 -38.86100 1.000 53.35000  ? 237 LYS A NZ  1 
ATOM   1512  N  N   . ILE A  1 207 ? -43.98300 -35.76600 -41.21600 1.000 49.99000  ? 238 ILE A N   1 
ATOM   1513  C  CA  . ILE A  1 207 ? -44.11200 -36.74200 -42.29700 1.000 48.15000  ? 238 ILE A CA  1 
ATOM   1514  C  C   . ILE A  1 207 ? -44.98200 -37.90900 -41.84200 1.000 47.78000  ? 238 ILE A C   1 
ATOM   1515  O  O   . ILE A  1 207 ? -45.93600 -38.30400 -42.52500 1.000 50.97000  ? 238 ILE A O   1 
ATOM   1516  C  CB  . ILE A  1 207 ? -42.71900 -37.19800 -42.78100 1.000 42.89000  ? 238 ILE A CB  1 
ATOM   1517  C  CG1 . ILE A  1 207 ? -42.02200 -36.03900 -43.51400 1.000 45.07000  ? 238 ILE A CG1 1 
ATOM   1518  C  CG2 . ILE A  1 207 ? -42.82500 -38.45600 -43.65000 1.000 41.13000  ? 238 ILE A CG2 1 
ATOM   1519  C  CD1 . ILE A  1 207 ? -40.51600 -36.26800 -43.87500 1.000 37.39000  ? 238 ILE A CD1 1 
ATOM   1520  N  N   . ALA A  1 208 ? -44.66600 -38.47200 -40.67300 1.000 46.62000  ? 239 ALA A N   1 
ATOM   1521  C  CA  . ALA A  1 208 ? -45.44800 -39.58100 -40.13500 1.000 41.98000  ? 239 ALA A CA  1 
ATOM   1522  C  C   . ALA A  1 208 ? -46.90500 -39.18700 -39.92400 1.000 42.55000  ? 239 ALA A C   1 
ATOM   1523  O  O   . ALA A  1 208 ? -47.81100 -39.99300 -40.14700 1.000 37.65000  ? 239 ALA A O   1 
ATOM   1524  C  CB  . ALA A  1 208 ? -44.84000 -40.03800 -38.81500 1.000 38.15000  ? 239 ALA A CB  1 
ATOM   1525  N  N   . ALA A  1 209 ? -47.14800 -37.95800 -39.46800 1.000 39.01000  ? 240 ALA A N   1 
ATOM   1526  C  CA  . ALA A  1 209 ? -48.52100 -37.51000 -39.31000 1.000 43.44000  ? 240 ALA A CA  1 
ATOM   1527  C  C   . ALA A  1 209 ? -49.23100 -37.46100 -40.66900 1.000 50.75000  ? 240 ALA A C   1 
ATOM   1528  O  O   . ALA A  1 209 ? -50.34000 -37.99000 -40.81600 1.000 47.56000  ? 240 ALA A O   1 
ATOM   1529  C  CB  . ALA A  1 209 ? -48.53700 -36.15200 -38.60900 1.000 36.17000  ? 240 ALA A CB  1 
ATOM   1530  N  N   . ALA A  1 210 ? -48.56400 -36.91800 -41.69700 1.000 45.07000  ? 241 ALA A N   1 
ATOM   1531  C  CA  . ALA A  1 210 ? -49.19500 -36.83900 -43.01100 1.000 44.76000  ? 241 ALA A CA  1 
ATOM   1532  C  C   . ALA A  1 210 ? -49.43800 -38.21900 -43.59300 1.000 45.82000  ? 241 ALA A C   1 
ATOM   1533  O  O   . ALA A  1 210 ? -50.45300 -38.43400 -44.26500 1.000 49.92000  ? 241 ALA A O   1 
ATOM   1534  C  CB  . ALA A  1 210 ? -48.34200 -36.00700 -43.97200 1.000 44.96000  ? 241 ALA A CB  1 
ATOM   1535  N  N   . LYS A  1 211 ? -48.54900 -39.17200 -43.32900 1.000 43.79000  ? 242 LYS A N   1 
ATOM   1536  C  CA  . LYS A  1 211 ? -48.79100 -40.52500 -43.80500 1.000 44.29000  ? 242 LYS A CA  1 
ATOM   1537  C  C   . LYS A  1 211 ? -49.83800 -41.24600 -42.96600 1.000 40.29000  ? 242 LYS A C   1 
ATOM   1538  O  O   . LYS A  1 211 ? -50.18000 -42.38400 -43.29100 1.000 41.55000  ? 242 LYS A O   1 
ATOM   1539  C  CB  . LYS A  1 211 ? -47.48500 -41.34700 -43.81200 1.000 46.18000  ? 242 LYS A CB  1 
ATOM   1540  C  CG  . LYS A  1 211 ? -46.37900 -40.81700 -44.73400 1.000 51.38000  ? 242 LYS A CG  1 
ATOM   1541  C  CD  . LYS A  1 211 ? -45.05600 -41.60600 -44.58300 1.000 49.50000  ? 242 LYS A CD  1 
ATOM   1542  C  CE  . LYS A  1 211 ? -44.94700 -42.79400 -45.52500 1.000 56.17000  ? 242 LYS A CE  1 
ATOM   1543  N  NZ  . LYS A  1 211 ? -44.06100 -42.47200 -46.68400 1.000 62.21000  ? 242 LYS A NZ  1 
ATOM   1544  N  N   . LYS A  1 212 ? -50.32400 -40.63400 -41.88400 1.000 42.06000  ? 243 LYS A N   1 
ATOM   1545  C  CA  . LYS A  1 212 ? -51.18900 -41.31500 -40.91000 1.000 46.95000  ? 243 LYS A CA  1 
ATOM   1546  C  C   . LYS A  1 212 ? -50.61400 -42.67100 -40.49200 1.000 43.75000  ? 243 LYS A C   1 
ATOM   1547  O  O   . LYS A  1 212 ? -51.28400 -43.70300 -40.52900 1.000 52.21000  ? 243 LYS A O   1 
ATOM   1548  C  CB  . LYS A  1 212 ? -52.61200 -41.47900 -41.45700 1.000 48.90000  ? 243 LYS A CB  1 
ATOM   1549  C  CG  . LYS A  1 212 ? -53.32400 -40.17700 -41.72500 1.000 53.44000  ? 243 LYS A CG  1 
ATOM   1550  C  CD  . LYS A  1 212 ? -54.77000 -40.39100 -42.23000 1.000 67.94000  ? 243 LYS A CD  1 
ATOM   1551  C  CE  . LYS A  1 212 ? -54.84700 -40.90300 -43.67900 1.000 62.00000  ? 243 LYS A CE  1 
ATOM   1552  N  NZ  . LYS A  1 212 ? -54.99000 -42.40100 -43.85000 1.000 56.45000  ? 243 LYS A NZ  1 
ATOM   1553  N  N   . GLN A  1 213 ? -49.34700 -42.65700 -40.09900 1.000 44.24000  ? 244 GLN A N   1 
ATOM   1554  C  CA  . GLN A  1 213 ? -48.57300 -43.82200 -39.71100 1.000 46.38000  ? 244 GLN A CA  1 
ATOM   1555  C  C   . GLN A  1 213 ? -47.94300 -43.57900 -38.34500 1.000 50.79000  ? 244 GLN A C   1 
ATOM   1556  O  O   . GLN A  1 213 ? -47.52100 -42.44800 -38.05000 1.000 48.09000  ? 244 GLN A O   1 
ATOM   1557  C  CB  . GLN A  1 213 ? -47.46000 -44.08900 -40.73800 1.000 47.47000  ? 244 GLN A CB  1 
ATOM   1558  C  CG  . GLN A  1 213 ? -47.54600 -45.38600 -41.50100 1.000 50.12000  ? 244 GLN A CG  1 
ATOM   1559  C  CD  . GLN A  1 213 ? -46.37800 -45.52400 -42.47900 1.000 54.80000  ? 244 GLN A CD  1 
ATOM   1560  O  OE1 . GLN A  1 213 ? -45.98200 -44.55400 -43.13600 1.000 50.15000  ? 244 GLN A OE1 1 
ATOM   1561  N  NE2 . GLN A  1 213 ? -45.80100 -46.71800 -42.54800 1.000 43.54000  ? 244 GLN A NE2 1 
ATOM   1562  N  N   . PRO A  1 214 ? -47.88600 -44.59000 -37.47500 1.000 45.98000  ? 245 PRO A N   1 
ATOM   1563  C  CA  . PRO A  1 214 ? -47.09800 -44.43100 -36.24800 1.000 46.44000  ? 245 PRO A CA  1 
ATOM   1564  C  C   . PRO A  1 214 ? -45.62700 -44.35900 -36.63000 1.000 49.88000  ? 245 PRO A C   1 
ATOM   1565  O  O   . PRO A  1 214 ? -45.18400 -45.03500 -37.56700 1.000 40.35000  ? 245 PRO A O   1 
ATOM   1566  C  CB  . PRO A  1 214 ? -47.41300 -45.69900 -35.44100 1.000 40.60000  ? 245 PRO A CB  1 
ATOM   1567  C  CG  . PRO A  1 214 ? -47.73100 -46.69200 -36.45600 1.000 51.58000  ? 245 PRO A CG  1 
ATOM   1568  C  CD  . PRO A  1 214 ? -48.45400 -45.94600 -37.58100 1.000 41.84000  ? 245 PRO A CD  1 
ATOM   1569  N  N   . PHE A  1 215 ? -44.87800 -43.50800 -35.93100 1.000 42.16000  ? 246 PHE A N   1 
ATOM   1570  C  CA  . PHE A  1 215 ? -43.46500 -43.33900 -36.22100 1.000 47.94000  ? 246 PHE A CA  1 
ATOM   1571  C  C   . PHE A  1 215 ? -42.58300 -44.00400 -35.17000 1.000 50.00000  ? 246 PHE A C   1 
ATOM   1572  O  O   . PHE A  1 215 ? -42.95900 -44.14800 -34.00000 1.000 51.40000  ? 246 PHE A O   1 
ATOM   1573  C  CB  . PHE A  1 215 ? -43.09000 -41.85200 -36.36300 1.000 45.75000  ? 246 PHE A CB  1 
ATOM   1574  C  CG  . PHE A  1 215 ? -43.19200 -41.03400 -35.08600 1.000 48.96000  ? 246 PHE A CG  1 
ATOM   1575  C  CD1 . PHE A  1 215 ? -42.27300 -41.17500 -34.04800 1.000 44.06000  ? 246 PHE A CD1 1 
ATOM   1576  C  CD2 . PHE A  1 215 ? -44.17900 -40.06300 -34.96200 1.000 42.76000  ? 246 PHE A CD2 1 
ATOM   1577  C  CE1 . PHE A  1 215 ? -42.36600 -40.38900 -32.89900 1.000 42.57000  ? 246 PHE A CE1 1 
ATOM   1578  C  CE2 . PHE A  1 215 ? -44.27500 -39.27000 -33.81900 1.000 46.89000  ? 246 PHE A CE2 1 
ATOM   1579  C  CZ  . PHE A  1 215 ? -43.37300 -39.43300 -32.78200 1.000 41.27000  ? 246 PHE A CZ  1 
ATOM   1580  N  N   . PHE A  1 216 ? -41.39400 -44.40400 -35.61800 1.000 46.31000  ? 247 PHE A N   1 
ATOM   1581  C  CA  . PHE A  1 216 ? -40.27500 -44.76200 -34.75800 1.000 41.60000  ? 247 PHE A CA  1 
ATOM   1582  C  C   . PHE A  1 216 ? -39.09300 -43.90500 -35.18800 1.000 42.74000  ? 247 PHE A C   1 
ATOM   1583  O  O   . PHE A  1 216 ? -38.56800 -44.09200 -36.29300 1.000 42.70000  ? 247 PHE A O   1 
ATOM   1584  C  CB  . PHE A  1 216 ? -39.92100 -46.23900 -34.86500 1.000 43.71000  ? 247 PHE A CB  1 
ATOM   1585  C  CG  . PHE A  1 216 ? -38.59300 -46.57500 -34.23300 1.000 48.11000  ? 247 PHE A CG  1 
ATOM   1586  C  CD1 . PHE A  1 216 ? -38.44000 -46.53000 -32.85700 1.000 44.33000  ? 247 PHE A CD1 1 
ATOM   1587  C  CD2 . PHE A  1 216 ? -37.49400 -46.89600 -35.01700 1.000 43.21000  ? 247 PHE A CD2 1 
ATOM   1588  C  CE1 . PHE A  1 216 ? -37.23500 -46.83300 -32.26600 1.000 43.40000  ? 247 PHE A CE1 1 
ATOM   1589  C  CE2 . PHE A  1 216 ? -36.27900 -47.18600 -34.44100 1.000 48.81000  ? 247 PHE A CE2 1 
ATOM   1590  C  CZ  . PHE A  1 216 ? -36.14400 -47.16300 -33.05600 1.000 46.53000  ? 247 PHE A CZ  1 
ATOM   1591  N  N   . ILE A  1 217 ? -38.68900 -42.96200 -34.33100 1.000 39.24000  ? 248 ILE A N   1 
ATOM   1592  C  CA  . ILE A  1 217 ? -37.59500 -42.02900 -34.60300 1.000 37.46000  ? 248 ILE A CA  1 
ATOM   1593  C  C   . ILE A  1 217 ? -36.43400 -42.34400 -33.66600 1.000 39.95000  ? 248 ILE A C   1 
ATOM   1594  O  O   . ILE A  1 217 ? -36.59400 -42.38600 -32.43600 1.000 38.31000  ? 248 ILE A O   1 
ATOM   1595  C  CB  . ILE A  1 217 ? -38.02600 -40.55900 -34.45900 1.000 40.79000  ? 248 ILE A CB  1 
ATOM   1596  C  CG1 . ILE A  1 217 ? -39.11900 -40.19100 -35.45600 1.000 41.79000  ? 248 ILE A CG1 1 
ATOM   1597  C  CG2 . ILE A  1 217 ? -36.83200 -39.64300 -34.65200 1.000 37.32000  ? 248 ILE A CG2 1 
ATOM   1598  C  CD1 . ILE A  1 217 ? -39.68700 -38.81800 -35.22700 1.000 43.69000  ? 248 ILE A CD1 1 
ATOM   1599  N  N   . TYR A  1 218 ? -35.27900 -42.61400 -34.25500 1.000 41.19000  ? 249 TYR A N   1 
ATOM   1600  C  CA  . TYR A  1 218 ? -34.04300 -42.89100 -33.52900 1.000 37.51000  ? 249 TYR A CA  1 
ATOM   1601  C  C   . TYR A  1 218 ? -33.21500 -41.62200 -33.60000 1.000 41.27000  ? 249 TYR A C   1 
ATOM   1602  O  O   . TYR A  1 218 ? -32.46100 -41.41300 -34.55400 1.000 39.33000  ? 249 TYR A O   1 
ATOM   1603  C  CB  . TYR A  1 218 ? -33.32600 -44.08700 -34.15200 1.000 36.79000  ? 249 TYR A CB  1 
ATOM   1604  C  CG  . TYR A  1 218 ? -32.00500 -44.47600 -33.52600 1.000 41.87000  ? 249 TYR A CG  1 
ATOM   1605  C  CD1 . TYR A  1 218 ? -31.96000 -45.07000 -32.27400 1.000 39.67000  ? 249 TYR A CD1 1 
ATOM   1606  C  CD2 . TYR A  1 218 ? -30.80600 -44.30900 -34.22000 1.000 39.47000  ? 249 TYR A CD2 1 
ATOM   1607  C  CE1 . TYR A  1 218 ? -30.75800 -45.45800 -31.70600 1.000 46.81000  ? 249 TYR A CE1 1 
ATOM   1608  C  CE2 . TYR A  1 218 ? -29.59500 -44.69800 -33.66400 1.000 40.40000  ? 249 TYR A CE2 1 
ATOM   1609  C  CZ  . TYR A  1 218 ? -29.58000 -45.27300 -32.40500 1.000 42.33000  ? 249 TYR A CZ  1 
ATOM   1610  O  OH  . TYR A  1 218 ? -28.39400 -45.66400 -31.82800 1.000 40.74000  ? 249 TYR A OH  1 
ATOM   1611  N  N   . LEU A  1 219 ? -33.36300 -40.76900 -32.58000 1.000 34.50000  ? 250 LEU A N   1 
ATOM   1612  C  CA  . LEU A  1 219 ? -32.72100 -39.45400 -32.53500 1.000 29.49000  ? 250 LEU A CA  1 
ATOM   1613  C  C   . LEU A  1 219 ? -31.40000 -39.57900 -31.76000 1.000 42.80000  ? 250 LEU A C   1 
ATOM   1614  O  O   . LEU A  1 219 ? -31.35000 -39.48700 -30.52200 1.000 34.77000  ? 250 LEU A O   1 
ATOM   1615  C  CB  . LEU A  1 219 ? -33.67600 -38.44300 -31.91200 1.000 34.27000  ? 250 LEU A CB  1 
ATOM   1616  C  CG  . LEU A  1 219 ? -33.23000 -37.00000 -31.65700 1.000 35.64000  ? 250 LEU A CG  1 
ATOM   1617  C  CD1 . LEU A  1 219 ? -32.52300 -36.39500 -32.86100 1.000 37.05000  ? 250 LEU A CD1 1 
ATOM   1618  C  CD2 . LEU A  1 219 ? -34.45800 -36.14900 -31.31900 1.000 36.78000  ? 250 LEU A CD2 1 
ATOM   1619  N  N   . ALA A  1 220 ? -30.31100 -39.80900 -32.50000 1.000 38.34000  ? 251 ALA A N   1 
ATOM   1620  C  CA  . ALA A  1 220 ? -28.99700 -40.07900 -31.90400 1.000 37.58000  ? 251 ALA A CA  1 
ATOM   1621  C  C   . ALA A  1 220 ? -28.12300 -38.83100 -31.97800 1.000 36.15000  ? 251 ALA A C   1 
ATOM   1622  O  O   . ALA A  1 220 ? -27.20300 -38.73300 -32.78700 1.000 41.41000  ? 251 ALA A O   1 
ATOM   1623  C  CB  . ALA A  1 220 ? -28.32300 -41.25500 -32.61300 1.000 33.17000  ? 251 ALA A CB  1 
ATOM   1624  N  N   . TYR A  1 221 ? -28.43700 -37.86600 -31.11700 1.000 34.12000  ? 252 TYR A N   1 
ATOM   1625  C  CA  . TYR A  1 221 ? -27.58800 -36.69700 -30.94000 1.000 36.49000  ? 252 TYR A CA  1 
ATOM   1626  C  C   . TYR A  1 221 ? -26.15300 -37.11800 -30.65700 1.000 36.54000  ? 252 TYR A C   1 
ATOM   1627  O  O   . TYR A  1 221 ? -25.90400 -38.05400 -29.89200 1.000 35.02000  ? 252 TYR A O   1 
ATOM   1628  C  CB  . TYR A  1 221 ? -28.08300 -35.86200 -29.76400 1.000 34.74000  ? 252 TYR A CB  1 
ATOM   1629  C  CG  . TYR A  1 221 ? -29.37800 -35.11100 -29.94600 1.000 37.14000  ? 252 TYR A CG  1 
ATOM   1630  C  CD1 . TYR A  1 221 ? -29.44100 -33.96300 -30.73600 1.000 36.26000  ? 252 TYR A CD1 1 
ATOM   1631  C  CD2 . TYR A  1 221 ? -30.52800 -35.51700 -29.28700 1.000 32.06000  ? 252 TYR A CD2 1 
ATOM   1632  C  CE1 . TYR A  1 221 ? -30.62400 -33.25500 -30.87500 1.000 35.38000  ? 252 TYR A CE1 1 
ATOM   1633  C  CE2 . TYR A  1 221 ? -31.70700 -34.81000 -29.41500 1.000 37.37000  ? 252 TYR A CE2 1 
ATOM   1634  C  CZ  . TYR A  1 221 ? -31.75600 -33.68300 -30.21100 1.000 38.71000  ? 252 TYR A CZ  1 
ATOM   1635  O  OH  . TYR A  1 221 ? -32.93800 -32.97500 -30.32400 1.000 41.39000  ? 252 TYR A OH  1 
ATOM   1636  N  N   . ASN A  1 222 ? -25.19600 -36.40900 -31.23900 1.000 35.00000  ? 253 ASN A N   1 
ATOM   1637  C  CA  . ASN A  1 222 ? -23.83200 -36.66700 -30.79400 1.000 36.80000  ? 253 ASN A CA  1 
ATOM   1638  C  C   . ASN A  1 222 ? -23.44300 -35.84500 -29.57800 1.000 32.94000  ? 253 ASN A C   1 
ATOM   1639  O  O   . ASN A  1 222 ? -22.50500 -36.22800 -28.88500 1.000 36.65000  ? 253 ASN A O   1 
ATOM   1640  C  CB  . ASN A  1 222 ? -22.82500 -36.46900 -31.93200 1.000 32.90000  ? 253 ASN A CB  1 
ATOM   1641  C  CG  . ASN A  1 222 ? -22.81100 -35.06100 -32.47400 1.000 40.87000  ? 253 ASN A CG  1 
ATOM   1642  O  OD1 . ASN A  1 222 ? -23.86200 -34.43400 -32.68100 1.000 32.38000  ? 253 ASN A OD1 1 
ATOM   1643  N  ND2 . ASN A  1 222 ? -21.60900 -34.54600 -32.71300 1.000 34.65000  ? 253 ASN A ND2 1 
ATOM   1644  N  N   . ALA A  1 223 ? -24.18800 -34.79100 -29.25300 1.000 33.57000  ? 254 ALA A N   1 
ATOM   1645  C  CA  . ALA A  1 223 ? -23.94700 -34.04500 -28.02500 1.000 31.61000  ? 254 ALA A CA  1 
ATOM   1646  C  C   . ALA A  1 223 ? -24.20400 -34.92600 -26.79900 1.000 35.41000  ? 254 ALA A C   1 
ATOM   1647  O  O   . ALA A  1 223 ? -25.12100 -35.76400 -26.80300 1.000 33.68000  ? 254 ALA A O   1 
ATOM   1648  C  CB  . ALA A  1 223 ? -24.84900 -32.81800 -27.96900 1.000 33.18000  ? 254 ALA A CB  1 
ATOM   1649  N  N   . PRO A  1 224 ? -23.42800 -34.72800 -25.70200 1.000 34.58000  ? 255 PRO A N   1 
ATOM   1650  C  CA  . PRO A  1 224 ? -22.30600 -33.80500 -25.52800 1.000 36.63000  ? 255 PRO A CA  1 
ATOM   1651  C  C   . PRO A  1 224 ? -20.90900 -34.42500 -25.73200 1.000 34.96000  ? 255 PRO A C   1 
ATOM   1652  O  O   . PRO A  1 224 ? -19.98400 -34.09100 -24.99000 1.000 33.64000  ? 255 PRO A O   1 
ATOM   1653  C  CB  . PRO A  1 224 ? -22.49200 -33.34700 -24.07800 1.000 35.37000  ? 255 PRO A CB  1 
ATOM   1654  C  CG  . PRO A  1 224 ? -22.97300 -34.59300 -23.38400 1.000 33.72000  ? 255 PRO A CG  1 
ATOM   1655  C  CD  . PRO A  1 224 ? -23.77800 -35.37000 -24.42100 1.000 38.05000  ? 255 PRO A CD  1 
ATOM   1656  N  N   . HIS A  1 225 ? -20.77200 -35.35000 -26.68100 1.000 27.61000  ? 256 HIS A N   1 
ATOM   1657  C  CA  . HIS A  1 225 ? -19.49600 -35.96300 -27.06900 1.000 35.20000  ? 256 HIS A CA  1 
ATOM   1658  C  C   . HIS A  1 225 ? -18.52600 -34.91700 -27.64400 1.000 35.32000  ? 256 HIS A C   1 
ATOM   1659  O  O   . HIS A  1 225 ? -18.94100 -33.91700 -28.24100 1.000 32.07000  ? 256 HIS A O   1 
ATOM   1660  C  CB  . HIS A  1 225 ? -19.82500 -37.03900 -28.09700 1.000 30.98000  ? 256 HIS A CB  1 
ATOM   1661  C  CG  . HIS A  1 225 ? -18.71900 -37.95800 -28.45500 1.000 35.35000  ? 256 HIS A CG  1 
ATOM   1662  N  ND1 . HIS A  1 225 ? -17.63800 -37.56500 -29.20800 1.000 38.62000  ? 256 HIS A ND1 1 
ATOM   1663  C  CD2 . HIS A  1 225 ? -18.59400 -39.29400 -28.28300 1.000 40.00000  ? 256 HIS A CD2 1 
ATOM   1664  C  CE1 . HIS A  1 225 ? -16.85700 -38.60900 -29.42100 1.000 42.98000  ? 256 HIS A CE1 1 
ATOM   1665  N  NE2 . HIS A  1 225 ? -17.41500 -39.67000 -28.87100 1.000 40.36000  ? 256 HIS A NE2 1 
ATOM   1666  N  N   . VAL A  1 226 ? -17.22100 -35.16300 -27.49600 1.000 33.89000  ? 257 VAL A N   1 
ATOM   1667  C  CA  . VAL A  1 226 ? -16.22200 -34.22900 -28.02000 1.000 32.35000  ? 257 VAL A CA  1 
ATOM   1668  C  C   . VAL A  1 226 ? -16.39200 -34.15000 -29.53800 1.000 36.11000  ? 257 VAL A C   1 
ATOM   1669  O  O   . VAL A  1 226 ? -16.95500 -35.07500 -30.14700 1.000 35.95000  ? 257 VAL A O   1 
ATOM   1670  C  CB  . VAL A  1 226 ? -14.78400 -34.61400 -27.59300 1.000 35.09000  ? 257 VAL A CB  1 
ATOM   1671  C  CG1 . VAL A  1 226 ? -14.58600 -34.32000 -26.11900 1.000 34.74000  ? 257 VAL A CG1 1 
ATOM   1672  C  CG2 . VAL A  1 226 ? -14.42700 -36.06800 -27.88300 1.000 31.48000  ? 257 VAL A CG2 1 
ATOM   1673  N  N   . PRO A  1 227 ? -15.96600 -33.05800 -30.19900 1.000 35.78000  ? 258 PRO A N   1 
ATOM   1674  C  CA  . PRO A  1 227 ? -15.31700 -31.85200 -29.66100 1.000 38.39000  ? 258 PRO A CA  1 
ATOM   1675  C  C   . PRO A  1 227 ? -16.30000 -30.98700 -28.89000 1.000 31.42000  ? 258 PRO A C   1 
ATOM   1676  O  O   . PRO A  1 227 ? -17.44500 -30.82400 -29.29900 1.000 38.72000  ? 258 PRO A O   1 
ATOM   1677  C  CB  . PRO A  1 227 ? -14.80900 -31.13500 -30.92800 1.000 33.03000  ? 258 PRO A CB  1 
ATOM   1678  C  CG  . PRO A  1 227 ? -15.84400 -31.52100 -31.97100 1.000 39.43000  ? 258 PRO A CG  1 
ATOM   1679  C  CD  . PRO A  1 227 ? -16.15000 -32.96400 -31.66200 1.000 36.60000  ? 258 PRO A CD  1 
ATOM   1680  N  N   . LEU A  1 228 ? -15.86700 -30.39800 -27.78300 1.000 36.81000  ? 259 LEU A N   1 
ATOM   1681  C  CA  . LEU A  1 228 ? -16.71300 -29.49600 -27.01100 1.000 33.09000  ? 259 LEU A CA  1 
ATOM   1682  C  C   . LEU A  1 228 ? -16.89800 -28.21400 -27.81400 1.000 34.04000  ? 259 LEU A C   1 
ATOM   1683  O  O   . LEU A  1 228 ? -15.98700 -27.39900 -27.93500 1.000 34.49000  ? 259 LEU A O   1 
ATOM   1684  C  CB  . LEU A  1 228 ? -16.07700 -29.26000 -25.65100 1.000 35.42000  ? 259 LEU A CB  1 
ATOM   1685  C  CG  . LEU A  1 228 ? -15.97100 -30.57300 -24.84800 1.000 39.09000  ? 259 LEU A CG  1 
ATOM   1686  C  CD1 . LEU A  1 228 ? -15.37300 -30.36100 -23.44300 1.000 39.21000  ? 259 LEU A CD1 1 
ATOM   1687  C  CD2 . LEU A  1 228 ? -17.34800 -31.27500 -24.75900 1.000 33.58000  ? 259 LEU A CD2 1 
ATOM   1688  N  N   . GLN A  1 229 ? -18.04800 -28.07600 -28.46600 1.000 33.66000  ? 260 GLN A N   1 
ATOM   1689  C  CA  . GLN A  1 229 ? -18.33300 -26.90200 -29.27500 1.000 32.38000  ? 260 GLN A CA  1 
ATOM   1690  C  C   . GLN A  1 229 ? -19.75000 -26.46800 -28.98900 1.000 39.04000  ? 260 GLN A C   1 
ATOM   1691  O  O   . GLN A  1 229 ? -20.66500 -27.29900 -29.01000 1.000 39.82000  ? 260 GLN A O   1 
ATOM   1692  C  CB  . GLN A  1 229 ? -18.13000 -27.19500 -30.77700 1.000 32.93000  ? 260 GLN A CB  1 
ATOM   1693  C  CG  . GLN A  1 229 ? -16.67700 -27.58000 -31.09000 1.000 41.48000  ? 260 GLN A CG  1 
ATOM   1694  C  CD  . GLN A  1 229 ? -16.41700 -28.03900 -32.51700 1.000 38.76000  ? 260 GLN A CD  1 
ATOM   1695  O  OE1 . GLN A  1 229 ? -17.33900 -28.25100 -33.28700 1.000 39.34000  ? 260 GLN A OE1 1 
ATOM   1696  N  NE2 . GLN A  1 229 ? -15.13100 -28.21300 -32.86200 1.000 39.49000  ? 260 GLN A NE2 1 
ATOM   1697  N  N   . ALA A  1 230 ? -19.93900 -25.17900 -28.71900 1.000 38.31000  ? 261 ALA A N   1 
ATOM   1698  C  CA  . ALA A  1 230 ? -21.25200 -24.71200 -28.33100 1.000 37.78000  ? 261 ALA A CA  1 
ATOM   1699  C  C   . ALA A  1 230 ? -21.52000 -23.35200 -28.92900 1.000 38.30000  ? 261 ALA A C   1 
ATOM   1700  O  O   . ALA A  1 230 ? -20.60300 -22.56300 -29.17300 1.000 43.13000  ? 261 ALA A O   1 
ATOM   1701  C  CB  . ALA A  1 230 ? -21.39800 -24.63500 -26.80400 1.000 33.79000  ? 261 ALA A CB  1 
ATOM   1702  N  N   . LYS A  1 231 ? -22.80500 -23.06200 -29.07900 1.000 32.28000  ? 262 LYS A N   1 
ATOM   1703  C  CA  . LYS A  1 231 ? -23.23400 -21.75200 -29.53700 1.000 40.80000  ? 262 LYS A CA  1 
ATOM   1704  C  C   . LYS A  1 231 ? -23.03700 -20.74100 -28.41700 1.000 43.31000  ? 262 LYS A C   1 
ATOM   1705  O  O   . LYS A  1 231 ? -23.29200 -21.03700 -27.24400 1.000 39.61000  ? 262 LYS A O   1 
ATOM   1706  C  CB  . LYS A  1 231 ? -24.71600 -21.77400 -29.93500 1.000 38.01000  ? 262 LYS A CB  1 
ATOM   1707  C  CG  . LYS A  1 231 ? -25.05900 -22.74000 -31.05400 1.000 43.21000  ? 262 LYS A CG  1 
ATOM   1708  C  CD  . LYS A  1 231 ? -26.56800 -22.95900 -31.19100 1.000 46.58000  ? 262 LYS A CD  1 
ATOM   1709  C  CE  . LYS A  1 231 ? -27.30300 -21.77600 -31.83200 1.000 44.49000  ? 262 LYS A CE  1 
ATOM   1710  N  NZ  . LYS A  1 231 ? -28.81900 -21.99300 -31.81000 1.000 44.91000  ? 262 LYS A NZ  1 
ATOM   1711  N  N   . ALA A  1 232 ? -22.61700 -19.53300 -28.79900 1.000 43.70000  ? 263 ALA A N   1 
ATOM   1712  C  CA  . ALA A  1 232 ? -22.35100 -18.47000 -27.83000 1.000 45.91000  ? 263 ALA A CA  1 
ATOM   1713  C  C   . ALA A  1 232 ? -23.58800 -18.12800 -27.01200 1.000 46.07000  ? 263 ALA A C   1 
ATOM   1714  O  O   . ALA A  1 232 ? -23.48900 -17.85500 -25.81200 1.000 50.68000  ? 263 ALA A O   1 
ATOM   1715  C  CB  . ALA A  1 232 ? -21.82800 -17.23200 -28.55300 1.000 47.13000  ? 263 ALA A CB  1 
ATOM   1716  N  N   . GLU A  1 233 ? -24.76000 -18.12700 -27.64700 1.000 48.79000  ? 264 GLU A N   1 
ATOM   1717  C  CA  . GLU A  1 233 ? -25.99100 -17.81300 -26.94200 1.000 45.87000  ? 264 GLU A CA  1 
ATOM   1718  C  C   . GLU A  1 233 ? -26.28400 -18.84800 -25.86600 1.000 53.23000  ? 264 GLU A C   1 
ATOM   1719  O  O   . GLU A  1 233 ? -26.81800 -18.50900 -24.80400 1.000 51.65000  ? 264 GLU A O   1 
ATOM   1720  C  CB  . GLU A  1 233 ? -27.14800 -17.72800 -27.95000 1.000 45.97000  ? 264 GLU A CB  1 
ATOM   1721  C  CG  . GLU A  1 233 ? -28.50700 -17.43400 -27.33700 1.000 58.66000  ? 264 GLU A CG  1 
ATOM   1722  C  CD  . GLU A  1 233 ? -29.38700 -16.54700 -28.22700 1.000 79.91000  ? 264 GLU A CD  1 
ATOM   1723  O  OE1 . GLU A  1 233 ? -29.39700 -16.74800 -29.46500 1.000 80.31000  ? 264 GLU A OE1 1 
ATOM   1724  O  OE2 . GLU A  1 233 ? -30.06600 -15.63800 -27.68800 1.000 81.45000  ? 264 GLU A OE2 1 
ATOM   1725  N  N   . ASP A  1 234 ? -25.91800 -20.10900 -26.11000 1.000 50.96000  ? 265 ASP A N   1 
ATOM   1726  C  CA  . ASP A  1 234 ? -26.09500 -21.14000 -25.10000 1.000 45.18000  ? 265 ASP A CA  1 
ATOM   1727  C  C   . ASP A  1 234 ? -25.02300 -21.03700 -24.02300 1.000 45.76000  ? 265 ASP A C   1 
ATOM   1728  O  O   . ASP A  1 234 ? -25.29500 -21.32200 -22.85200 1.000 44.65000  ? 265 ASP A O   1 
ATOM   1729  C  CB  . ASP A  1 234 ? -26.09700 -22.52500 -25.74300 1.000 47.00000  ? 265 ASP A CB  1 
ATOM   1730  C  CG  . ASP A  1 234 ? -27.33700 -22.77500 -26.59000 1.000 46.66000  ? 265 ASP A CG  1 
ATOM   1731  O  OD1 . ASP A  1 234 ? -28.40900 -22.26000 -26.22300 1.000 56.12000  ? 265 ASP A OD1 1 
ATOM   1732  O  OD2 . ASP A  1 234 ? -27.26400 -23.52300 -27.59400 1.000 53.00000  ? 265 ASP A OD2 1 
ATOM   1733  N  N   . VAL A  1 235 ? -23.78600 -20.70900 -24.40500 1.000 46.13000  ? 266 VAL A N   1 
ATOM   1734  C  CA  . VAL A  1 235 ? -22.72800 -20.52100 -23.41100 1.000 44.29000  ? 266 VAL A CA  1 
ATOM   1735  C  C   . VAL A  1 235 ? -23.09200 -19.39100 -22.45500 1.000 51.11000  ? 266 VAL A C   1 
ATOM   1736  O  O   . VAL A  1 235 ? -22.81500 -19.46800 -21.25200 1.000 49.20000  ? 266 VAL A O   1 
ATOM   1737  C  CB  . VAL A  1 235 ? -21.37300 -20.25900 -24.09900 1.000 41.54000  ? 266 VAL A CB  1 
ATOM   1738  C  CG1 . VAL A  1 235 ? -20.29700 -19.89800 -23.05600 1.000 47.05000  ? 266 VAL A CG1 1 
ATOM   1739  C  CG2 . VAL A  1 235 ? -20.92900 -21.46600 -24.87700 1.000 39.28000  ? 266 VAL A CG2 1 
ATOM   1740  N  N   . ALA A  1 236 ? -23.77200 -18.35700 -22.95700 1.000 52.68000  ? 267 ALA A N   1 
ATOM   1741  C  CA  . ALA A  1 236 ? -24.09200 -17.20300 -22.12900 1.000 52.33000  ? 267 ALA A CA  1 
ATOM   1742  C  C   . ALA A  1 236 ? -24.97500 -17.58100 -20.95200 1.000 51.28000  ? 267 ALA A C   1 
ATOM   1743  O  O   . ALA A  1 236 ? -24.91400 -16.93200 -19.90400 1.000 57.61000  ? 267 ALA A O   1 
ATOM   1744  C  CB  . ALA A  1 236 ? -24.78600 -16.13300 -22.97100 1.000 43.84000  ? 267 ALA A CB  1 
ATOM   1745  N  N   . LYS A  1 237 ? -25.79600 -18.62100 -21.10100 1.000 46.96000  ? 268 LYS A N   1 
ATOM   1746  C  CA  . LYS A  1 237 ? -26.67600 -19.06600 -20.02500 1.000 48.56000  ? 268 LYS A CA  1 
ATOM   1747  C  C   . LYS A  1 237 ? -25.93400 -19.77100 -18.90000 1.000 50.54000  ? 268 LYS A C   1 
ATOM   1748  O  O   . LYS A  1 237 ? -26.54300 -20.06000 -17.86600 1.000 52.07000  ? 268 LYS A O   1 
ATOM   1749  C  CB  . LYS A  1 237 ? -27.76900 -19.97900 -20.58900 1.000 42.52000  ? 268 LYS A CB  1 
ATOM   1750  C  CG  . LYS A  1 237 ? -28.65500 -19.24300 -21.57400 1.000 52.26000  ? 268 LYS A CG  1 
ATOM   1751  C  CD  . LYS A  1 237 ? -30.03800 -19.87000 -21.73300 1.000 57.06000  ? 268 LYS A CD  1 
ATOM   1752  C  CE  . LYS A  1 237 ? -30.95100 -18.93100 -22.51100 1.000 62.89000  ? 268 LYS A CE  1 
ATOM   1753  N  NZ  . LYS A  1 237 ? -31.18100 -17.66200 -21.75500 1.000 74.44000  ? 268 LYS A NZ  1 
ATOM   1754  N  N   . PHE A  1 238 ? -24.65200 -20.06000 -19.07700 1.000 45.68000  ? 269 PHE A N   1 
ATOM   1755  C  CA  . PHE A  1 238 ? -23.85900 -20.75200 -18.07300 1.000 51.50000  ? 269 PHE A CA  1 
ATOM   1756  C  C   . PHE A  1 238 ? -22.57400 -19.98900 -17.84100 1.000 44.71000  ? 269 PHE A C   1 
ATOM   1757  O  O   . PHE A  1 238 ? -21.52800 -20.58000 -17.59200 1.000 47.34000  ? 269 PHE A O   1 
ATOM   1758  C  CB  . PHE A  1 238 ? -23.58200 -22.19400 -18.49500 1.000 44.54000  ? 269 PHE A CB  1 
ATOM   1759  C  CG  . PHE A  1 238 ? -24.83000 -22.99100 -18.72600 1.000 46.06000  ? 269 PHE A CG  1 
ATOM   1760  C  CD1 . PHE A  1 238 ? -25.51000 -23.54900 -17.66800 1.000 40.17000  ? 269 PHE A CD1 1 
ATOM   1761  C  CD2 . PHE A  1 238 ? -25.36900 -23.10700 -20.00100 1.000 38.88000  ? 269 PHE A CD2 1 
ATOM   1762  C  CE1 . PHE A  1 238 ? -26.66500 -24.26200 -17.87600 1.000 42.71000  ? 269 PHE A CE1 1 
ATOM   1763  C  CE2 . PHE A  1 238 ? -26.53100 -23.81000 -20.21900 1.000 43.44000  ? 269 PHE A CE2 1 
ATOM   1764  C  CZ  . PHE A  1 238 ? -27.18800 -24.39300 -19.15900 1.000 45.86000  ? 269 PHE A CZ  1 
ATOM   1765  N  N   . ALA A  1 239 ? -22.64000 -18.66600 -17.95800 1.000 48.35000  ? 270 ALA A N   1 
ATOM   1766  C  CA  . ALA A  1 239 ? -21.43300 -17.86000 -17.82600 1.000 58.90000  ? 270 ALA A CA  1 
ATOM   1767  C  C   . ALA A  1 239 ? -20.84900 -17.89600 -16.41500 1.000 54.21000  ? 270 ALA A C   1 
ATOM   1768  O  O   . ALA A  1 239 ? -19.64400 -17.68600 -16.26800 1.000 50.64000  ? 270 ALA A O   1 
ATOM   1769  C  CB  . ALA A  1 239 ? -21.71600 -16.41600 -18.25200 1.000 58.97000  ? 270 ALA A CB  1 
ATOM   1770  N  N   . HIS A  1 240 ? -21.66100 -18.16000 -15.37800 1.000 54.19000  ? 271 HIS A N   1 
ATOM   1771  C  CA  . HIS A  1 240 ? -21.09400 -18.29800 -14.04000 1.000 53.86000  ? 271 HIS A CA  1 
ATOM   1772  C  C   . HIS A  1 240 ? -20.33100 -19.60100 -13.85300 1.000 59.63000  ? 271 HIS A C   1 
ATOM   1773  O  O   . HIS A  1 240 ? -19.69700 -19.75900 -12.80800 1.000 58.24000  ? 271 HIS A O   1 
ATOM   1774  C  CB  . HIS A  1 240 ? -22.17000 -18.21600 -12.94700 1.000 56.68000  ? 271 HIS A CB  1 
ATOM   1775  C  CG  . HIS A  1 240 ? -22.83300 -16.87500 -12.83300 1.000 67.33000  ? 271 HIS A CG  1 
ATOM   1776  N  ND1 . HIS A  1 240 ? -24.13000 -16.72300 -12.38300 1.000 74.20000  ? 271 HIS A ND1 1 
ATOM   1777  C  CD2 . HIS A  1 240 ? -22.38200 -15.62600 -13.10700 1.000 67.76000  ? 271 HIS A CD2 1 
ATOM   1778  C  CE1 . HIS A  1 240 ? -24.44900 -15.43900 -12.38800 1.000 72.87000  ? 271 HIS A CE1 1 
ATOM   1779  N  NE2 . HIS A  1 240 ? -23.40600 -14.75300 -12.82300 1.000 75.86000  ? 271 HIS A NE2 1 
ATOM   1780  N  N   . ILE A  1 241 ? -20.32300 -20.51900 -14.81900 1.000 54.12000  ? 272 ILE A N   1 
ATOM   1781  C  CA  . ILE A  1 241 ? -19.52900 -21.73500 -14.67100 1.000 49.01000  ? 272 ILE A CA  1 
ATOM   1782  C  C   . ILE A  1 241 ? -18.10700 -21.38300 -15.08000 1.000 49.80000  ? 272 ILE A C   1 
ATOM   1783  O  O   . ILE A  1 241 ? -17.87400 -20.94400 -16.21200 1.000 46.89000  ? 272 ILE A O   1 
ATOM   1784  C  CB  . ILE A  1 241 ? -20.08300 -22.88600 -15.52400 1.000 51.53000  ? 272 ILE A CB  1 
ATOM   1785  C  CG1 . ILE A  1 241 ? -21.50100 -23.23700 -15.10400 1.000 41.25000  ? 272 ILE A CG1 1 
ATOM   1786  C  CG2 . ILE A  1 241 ? -19.19900 -24.15200 -15.38400 1.000 46.14000  ? 272 ILE A CG2 1 
ATOM   1787  C  CD1 . ILE A  1 241 ? -22.05600 -24.41700 -15.89000 1.000 40.19000  ? 272 ILE A CD1 1 
ATOM   1788  N  N   . LYS A  1 242 ? -17.15900 -21.55200 -14.14500 1.000 44.02000  ? 273 LYS A N   1 
ATOM   1789  C  CA  . LYS A  1 242 ? -15.80300 -21.04000 -14.32500 1.000 48.58000  ? 273 LYS A CA  1 
ATOM   1790  C  C   . LYS A  1 242 ? -14.94700 -21.92000 -15.23200 1.000 46.50000  ? 273 LYS A C   1 
ATOM   1791  O  O   . LYS A  1 242 ? -14.14400 -21.40200 -16.01500 1.000 46.14000  ? 273 LYS A O   1 
ATOM   1792  C  CB  . LYS A  1 242 ? -15.12900 -20.86600 -12.95800 1.000 53.14000  ? 273 LYS A CB  1 
ATOM   1793  N  N   . ASP A  1 243 ? -15.04700 -23.23900 -15.09900 1.000 43.23000  ? 274 ASP A N   1 
ATOM   1794  C  CA  . ASP A  1 243 ? -14.24500 -24.13500 -15.92800 1.000 44.35000  ? 274 ASP A CA  1 
ATOM   1795  C  C   . ASP A  1 243 ? -14.74300 -24.09400 -17.36800 1.000 44.00000  ? 274 ASP A C   1 
ATOM   1796  O  O   . ASP A  1 243 ? -15.93100 -24.32300 -17.62800 1.000 44.70000  ? 274 ASP A O   1 
ATOM   1797  C  CB  . ASP A  1 243 ? -14.31200 -25.56700 -15.40300 1.000 42.50000  ? 274 ASP A CB  1 
ATOM   1798  C  CG  . ASP A  1 243 ? -13.46000 -26.52400 -16.23700 1.000 52.96000  ? 274 ASP A CG  1 
ATOM   1799  O  OD1 . ASP A  1 243 ? -12.21200 -26.39700 -16.18200 1.000 56.26000  ? 274 ASP A OD1 1 
ATOM   1800  O  OD2 . ASP A  1 243 ? -14.03900 -27.35000 -16.99700 1.000 48.88000  ? 274 ASP A OD2 1 
ATOM   1801  N  N   . LYS A  1 244 ? -13.83500 -23.81300 -18.30200 1.000 41.44000  ? 275 LYS A N   1 
ATOM   1802  C  CA  . LYS A  1 244 ? -14.25000 -23.62000 -19.68300 1.000 46.88000  ? 275 LYS A CA  1 
ATOM   1803  C  C   . LYS A  1 244 ? -14.88800 -24.88400 -20.24600 1.000 48.82000  ? 275 LYS A C   1 
ATOM   1804  O  O   . LYS A  1 244 ? -15.97500 -24.82700 -20.84800 1.000 40.19000  ? 275 LYS A O   1 
ATOM   1805  C  CB  . LYS A  1 244 ? -13.06100 -23.18200 -20.53700 1.000 46.03000  ? 275 LYS A CB  1 
ATOM   1806  N  N   . ASP A  1 245 ? -14.27900 -26.04400 -19.98100 1.000 41.73000  ? 276 ASP A N   1 
ATOM   1807  C  CA  . ASP A  1 245 ? -14.82700 -27.28500 -20.52100 1.000 42.24000  ? 276 ASP A CA  1 
ATOM   1808  C  C   . ASP A  1 245 ? -16.20300 -27.59500 -19.91700 1.000 43.68000  ? 276 ASP A C   1 
ATOM   1809  O  O   . ASP A  1 245 ? -17.14100 -27.95900 -20.63700 1.000 38.06000  ? 276 ASP A O   1 
ATOM   1810  C  CB  . ASP A  1 245 ? -13.85400 -28.43900 -20.26300 1.000 44.77000  ? 276 ASP A CB  1 
ATOM   1811  C  CG  . ASP A  1 245 ? -12.75400 -28.53700 -21.32500 1.000 55.56000  ? 276 ASP A CG  1 
ATOM   1812  O  OD1 . ASP A  1 245 ? -12.56200 -27.56900 -22.10100 1.000 53.03000  ? 276 ASP A OD1 1 
ATOM   1813  O  OD2 . ASP A  1 245 ? -12.07900 -29.58800 -21.39300 1.000 57.01000  ? 276 ASP A OD2 1 
ATOM   1814  N  N   . ARG A  1 246 ? -16.34900 -27.45400 -18.59600 1.000 45.16000  ? 277 ARG A N   1 
ATOM   1815  C  CA  . ARG A  1 246 ? -17.65500 -27.69600 -17.99900 1.000 43.36000  ? 277 ARG A CA  1 
ATOM   1816  C  C   . ARG A  1 246 ? -18.69300 -26.73600 -18.56800 1.000 38.03000  ? 277 ARG A C   1 
ATOM   1817  O  O   . ARG A  1 246 ? -19.82600 -27.13200 -18.86100 1.000 41.49000  ? 277 ARG A O   1 
ATOM   1818  C  CB  . ARG A  1 246 ? -17.56800 -27.58000 -16.47700 1.000 39.61000  ? 277 ARG A CB  1 
ATOM   1819  C  CG  . ARG A  1 246 ? -18.88900 -27.86900 -15.78200 1.000 41.05000  ? 277 ARG A CG  1 
ATOM   1820  C  CD  . ARG A  1 246 ? -19.31900 -29.32800 -15.93100 1.000 41.64000  ? 277 ARG A CD  1 
ATOM   1821  N  NE  . ARG A  1 246 ? -20.52200 -29.62300 -15.16400 1.000 33.28000  ? 277 ARG A NE  1 
ATOM   1822  C  CZ  . ARG A  1 246 ? -21.16600 -30.78200 -15.18900 1.000 38.79000  ? 277 ARG A CZ  1 
ATOM   1823  N  NH1 . ARG A  1 246 ? -20.74500 -31.79500 -15.93400 1.000 32.11000  ? 277 ARG A NH1 1 
ATOM   1824  N  NH2 . ARG A  1 246 ? -22.24500 -30.94100 -14.42400 1.000 39.21000  ? 277 ARG A NH2 1 
ATOM   1825  N  N   . ARG A  1 247 ? -18.30300 -25.48300 -18.78800 1.000 39.34000  ? 278 ARG A N   1 
ATOM   1826  C  CA  . ARG A  1 247 ? -19.24400 -24.49200 -19.29600 1.000 39.92000  ? 278 ARG A CA  1 
ATOM   1827  C  C   . ARG A  1 247 ? -19.71600 -24.82900 -20.71700 1.000 41.21000  ? 278 ARG A C   1 
ATOM   1828  O  O   . ARG A  1 247 ? -20.91700 -24.72900 -21.02300 1.000 37.14000  ? 278 ARG A O   1 
ATOM   1829  C  CB  . ARG A  1 247 ? -18.61400 -23.10400 -19.23200 1.000 41.58000  ? 278 ARG A CB  1 
ATOM   1830  C  CG  . ARG A  1 247 ? -19.55300 -22.02800 -19.72300 1.000 46.62000  ? 278 ARG A CG  1 
ATOM   1831  C  CD  . ARG A  1 247 ? -19.01500 -20.64700 -19.44100 1.000 48.61000  ? 278 ARG A CD  1 
ATOM   1832  N  NE  . ARG A  1 247 ? -17.74700 -20.41200 -20.11200 1.000 51.15000  ? 278 ARG A NE  1 
ATOM   1833  C  CZ  . ARG A  1 247 ? -16.58200 -20.30500 -19.49500 1.000 50.33000  ? 278 ARG A CZ  1 
ATOM   1834  N  NH1 . ARG A  1 247 ? -16.48900 -20.40500 -18.18100 1.000 49.42000  ? 278 ARG A NH1 1 
ATOM   1835  N  NH2 . ARG A  1 247 ? -15.48500 -20.07600 -20.21600 1.000 47.26000  ? 278 ARG A NH2 1 
ATOM   1836  N  N   . THR A  1 248 ? -18.78300 -25.19700 -21.61400 1.000 39.58000  ? 279 THR A N   1 
ATOM   1837  C  CA  . THR A  1 248 ? -19.17300 -25.54100 -22.98800 1.000 40.42000  ? 279 THR A CA  1 
ATOM   1838  C  C   . THR A  1 248 ? -20.05100 -26.77900 -23.00100 1.000 38.29000  ? 279 THR A C   1 
ATOM   1839  O  O   . THR A  1 248 ? -21.08400 -26.82600 -23.69200 1.000 36.47000  ? 279 THR A O   1 
ATOM   1840  C  CB  . THR A  1 248 ? -17.94000 -25.79800 -23.84700 1.000 41.12000  ? 279 THR A CB  1 
ATOM   1841  O  OG1 . THR A  1 248 ? -16.99800 -24.75900 -23.62600 1.000 38.65000  ? 279 THR A OG1 1 
ATOM   1842  C  CG2 . THR A  1 248 ? -18.32300 -25.81200 -25.31200 1.000 41.17000  ? 279 THR A CG2 1 
ATOM   1843  N  N   . TYR A  1 249 ? -19.65000 -27.78500 -22.21800 1.000 39.80000  ? 280 TYR A N   1 
ATOM   1844  C  CA  . TYR A  1 249 ? -20.42200 -29.02000 -22.07500 1.000 36.51000  ? 280 TYR A CA  1 
ATOM   1845  C  C   . TYR A  1 249 ? -21.83600 -28.71400 -21.60500 1.000 35.13000  ? 280 TYR A C   1 
ATOM   1846  O  O   . TYR A  1 249 ? -22.81500 -29.26800 -22.12600 1.000 37.94000  ? 280 TYR A O   1 
ATOM   1847  C  CB  . TYR A  1 249 ? -19.69900 -29.94400 -21.08400 1.000 33.60000  ? 280 TYR A CB  1 
ATOM   1848  C  CG  . TYR A  1 249 ? -20.36100 -31.25800 -20.79400 1.000 33.78000  ? 280 TYR A CG  1 
ATOM   1849  C  CD1 . TYR A  1 249 ? -21.40200 -31.34600 -19.85500 1.000 33.54000  ? 280 TYR A CD1 1 
ATOM   1850  C  CD2 . TYR A  1 249 ? -19.92500 -32.42900 -21.40400 1.000 33.00000  ? 280 TYR A CD2 1 
ATOM   1851  C  CE1 . TYR A  1 249 ? -22.01500 -32.55600 -19.57900 1.000 30.80000  ? 280 TYR A CE1 1 
ATOM   1852  C  CE2 . TYR A  1 249 ? -20.52300 -33.65200 -21.11100 1.000 33.59000  ? 280 TYR A CE2 1 
ATOM   1853  C  CZ  . TYR A  1 249 ? -21.56900 -33.69400 -20.19200 1.000 34.83000  ? 280 TYR A CZ  1 
ATOM   1854  O  OH  . TYR A  1 249 ? -22.16500 -34.87800 -19.87700 1.000 39.28000  ? 280 TYR A OH  1 
ATOM   1855  N  N   . ALA A  1 250 ? -21.96100 -27.83900 -20.60300 1.000 37.67000  ? 281 ALA A N   1 
ATOM   1856  C  CA  . ALA A  1 250 ? -23.28700 -27.44900 -20.14500 1.000 41.35000  ? 281 ALA A CA  1 
ATOM   1857  C  C   . ALA A  1 250 ? -24.08000 -26.83100 -21.28300 1.000 35.99000  ? 281 ALA A C   1 
ATOM   1858  O  O   . ALA A  1 250 ? -25.26100 -27.13400 -21.46300 1.000 34.29000  ? 281 ALA A O   1 
ATOM   1859  C  CB  . ALA A  1 250 ? -23.17500 -26.47400 -18.96000 1.000 34.87000  ? 281 ALA A CB  1 
ATOM   1860  N  N   . ALA A  1 251 ? -23.44100 -25.96200 -22.06800 1.000 36.65000  ? 282 ALA A N   1 
ATOM   1861  C  CA  . ALA A  1 251 ? -24.13400 -25.36100 -23.20400 1.000 37.64000  ? 282 ALA A CA  1 
ATOM   1862  C  C   . ALA A  1 251 ? -24.53600 -26.41100 -24.24600 1.000 39.77000  ? 282 ALA A C   1 
ATOM   1863  O  O   . ALA A  1 251 ? -25.57100 -26.25700 -24.90500 1.000 38.74000  ? 282 ALA A O   1 
ATOM   1864  C  CB  . ALA A  1 251 ? -23.27000 -24.26700 -23.83100 1.000 33.67000  ? 282 ALA A CB  1 
ATOM   1865  N  N   . MET A  1 252 ? -23.72000 -27.46100 -24.44100 1.000 39.20000  ? 283 MET A N   1 
ATOM   1866  C  CA  . MET A  1 252 ? -24.08000 -28.51200 -25.39800 1.000 35.45000  ? 283 MET A CA  1 
ATOM   1867  C  C   . MET A  1 252 ? -25.28700 -29.30100 -24.92400 1.000 38.29000  ? 283 MET A C   1 
ATOM   1868  O  O   . MET A  1 252 ? -26.19700 -29.59900 -25.71500 1.000 37.42000  ? 283 MET A O   1 
ATOM   1869  C  CB  . MET A  1 252 ? -22.90200 -29.46000 -25.63000 1.000 30.75000  ? 283 MET A CB  1 
ATOM   1870  C  CG  . MET A  1 252 ? -21.70800 -28.75600 -26.16200 1.000 35.13000  ? 283 MET A CG  1 
ATOM   1871  S  SD  . MET A  1 252 ? -20.29700 -29.84200 -26.20000 1.000 40.55000  ? 283 MET A SD  1 
ATOM   1872  C  CE  . MET A  1 252 ? -20.80700 -30.93300 -27.53400 1.000 37.43000  ? 283 MET A CE  1 
ATOM   1873  N  N   . VAL A  1 253 ? -25.30400 -29.67500 -23.64300 1.000 35.82000  ? 284 VAL A N   1 
ATOM   1874  C  CA  . VAL A  1 253 ? -26.47100 -30.38100 -23.12400 1.000 39.64000  ? 284 VAL A CA  1 
ATOM   1875  C  C   . VAL A  1 253 ? -27.69900 -29.49600 -23.24900 1.000 36.84000  ? 284 VAL A C   1 
ATOM   1876  O  O   . VAL A  1 253 ? -28.79000 -29.95900 -23.58500 1.000 39.51000  ? 284 VAL A O   1 
ATOM   1877  C  CB  . VAL A  1 253 ? -26.25100 -30.79800 -21.65800 1.000 38.87000  ? 284 VAL A CB  1 
ATOM   1878  C  CG1 . VAL A  1 253 ? -27.57000 -31.36800 -21.08600 1.000 37.95000  ? 284 VAL A CG1 1 
ATOM   1879  C  CG2 . VAL A  1 253 ? -25.13100 -31.79500 -21.54500 1.000 26.83000  ? 284 VAL A CG2 1 
ATOM   1880  N  N   . TYR A  1 254 ? -27.52700 -28.19600 -23.01000 1.000 39.80000  ? 285 TYR A N   1 
ATOM   1881  C  CA  . TYR A  1 254 ? -28.65600 -27.28500 -23.06700 1.000 42.22000  ? 285 TYR A CA  1 
ATOM   1882  C  C   . TYR A  1 254 ? -29.25400 -27.22700 -24.46700 1.000 44.66000  ? 285 TYR A C   1 
ATOM   1883  O  O   . TYR A  1 254 ? -30.47800 -27.29300 -24.62400 1.000 42.13000  ? 285 TYR A O   1 
ATOM   1884  C  CB  . TYR A  1 254 ? -28.21500 -25.90300 -22.58400 1.000 39.31000  ? 285 TYR A CB  1 
ATOM   1885  C  CG  . TYR A  1 254 ? -29.32700 -24.89200 -22.58900 1.000 45.62000  ? 285 TYR A CG  1 
ATOM   1886  C  CD1 . TYR A  1 254 ? -30.37700 -24.98700 -21.69100 1.000 44.88000  ? 285 TYR A CD1 1 
ATOM   1887  C  CD2 . TYR A  1 254 ? -29.30800 -23.81800 -23.46600 1.000 48.53000  ? 285 TYR A CD2 1 
ATOM   1888  C  CE1 . TYR A  1 254 ? -31.39300 -24.04900 -21.67600 1.000 52.54000  ? 285 TYR A CE1 1 
ATOM   1889  C  CE2 . TYR A  1 254 ? -30.32000 -22.87800 -23.46100 1.000 52.51000  ? 285 TYR A CE2 1 
ATOM   1890  C  CZ  . TYR A  1 254 ? -31.36100 -22.99600 -22.56100 1.000 57.03000  ? 285 TYR A CZ  1 
ATOM   1891  O  OH  . TYR A  1 254 ? -32.37700 -22.06600 -22.54500 1.000 64.97000  ? 285 TYR A OH  1 
ATOM   1892  N  N   . ALA A  1 255 ? -28.41000 -27.18800 -25.50100 1.000 41.99000  ? 286 ALA A N   1 
ATOM   1893  C  CA  . ALA A  1 255 ? -28.96400 -27.16300 -26.85100 1.000 44.26000  ? 286 ALA A CA  1 
ATOM   1894  C  C   . ALA A  1 255 ? -29.78700 -28.41600 -27.13800 1.000 39.58000  ? 286 ALA A C   1 
ATOM   1895  O  O   . ALA A  1 255 ? -30.76000 -28.34600 -27.89600 1.000 39.80000  ? 286 ALA A O   1 
ATOM   1896  C  CB  . ALA A  1 255 ? -27.86000 -26.97600 -27.89000 1.000 37.01000  ? 286 ALA A CB  1 
ATOM   1897  N  N   . VAL A  1 256 ? -29.43100 -29.56400 -26.54200 1.000 36.98000  ? 287 VAL A N   1 
ATOM   1898  C  CA  . VAL A  1 256 ? -30.28000 -30.74200 -26.69900 1.000 35.36000  ? 287 VAL A CA  1 
ATOM   1899  C  C   . VAL A  1 256 ? -31.62700 -30.50700 -26.03300 1.000 42.88000  ? 287 VAL A C   1 
ATOM   1900  O  O   . VAL A  1 256 ? -32.68200 -30.75200 -26.63400 1.000 46.40000  ? 287 VAL A O   1 
ATOM   1901  C  CB  . VAL A  1 256 ? -29.60000 -32.00000 -26.13100 1.000 37.60000  ? 287 VAL A CB  1 
ATOM   1902  C  CG1 . VAL A  1 256 ? -30.63400 -33.13500 -25.94500 1.000 35.60000  ? 287 VAL A CG1 1 
ATOM   1903  C  CG2 . VAL A  1 256 ? -28.51300 -32.47800 -27.06800 1.000 39.44000  ? 287 VAL A CG2 1 
ATOM   1904  N  N   . ASP A  1 257 ? -31.61000 -29.91000 -24.83800 1.000 44.97000  ? 288 ASP A N   1 
ATOM   1905  C  CA  . ASP A  1 257 ? -32.84500 -29.63500 -24.11100 1.000 45.01000  ? 288 ASP A CA  1 
ATOM   1906  C  C   . ASP A  1 257 ? -33.75600 -28.69500 -24.90400 1.000 41.40000  ? 288 ASP A C   1 
ATOM   1907  O  O   . ASP A  1 257 ? -34.95700 -28.96200 -25.05600 1.000 43.20000  ? 288 ASP A O   1 
ATOM   1908  C  CB  . ASP A  1 257 ? -32.49600 -29.06400 -22.72500 1.000 36.15000  ? 288 ASP A CB  1 
ATOM   1909  C  CG  . ASP A  1 257 ? -33.70200 -28.99900 -21.81100 1.000 44.53000  ? 288 ASP A CG  1 
ATOM   1910  O  OD1 . ASP A  1 257 ? -34.12000 -30.08100 -21.33200 1.000 45.33000  ? 288 ASP A OD1 1 
ATOM   1911  O  OD2 . ASP A  1 257 ? -34.24100 -27.88700 -21.58000 1.000 44.46000  ? 288 ASP A OD2 1 
ATOM   1912  N  N   . ARG A  1 258 ? -33.19000 -27.61100 -25.46500 1.000 40.75000  ? 289 ARG A N   1 
ATOM   1913  C  CA  . ARG A  1 258 ? -33.98500 -26.71500 -26.31500 1.000 43.51000  ? 289 ARG A CA  1 
ATOM   1914  C  C   . ARG A  1 258 ? -34.65400 -27.47200 -27.45300 1.000 43.24000  ? 289 ARG A C   1 
ATOM   1915  O  O   . ARG A  1 258 ? -35.82000 -27.21800 -27.78100 1.000 49.98000  ? 289 ARG A O   1 
ATOM   1916  C  CB  . ARG A  1 258 ? -33.11800 -25.59900 -26.90900 1.000 47.58000  ? 289 ARG A CB  1 
ATOM   1917  C  CG  . ARG A  1 258 ? -32.78900 -24.42700 -25.97800 1.000 51.38000  ? 289 ARG A CG  1 
ATOM   1918  C  CD  . ARG A  1 258 ? -32.15900 -23.21400 -26.73100 1.000 45.67000  ? 289 ARG A CD  1 
ATOM   1919  N  NE  . ARG A  1 258 ? -30.85900 -23.53100 -27.33200 1.000 52.16000  ? 289 ARG A NE  1 
ATOM   1920  C  CZ  . ARG A  1 258 ? -30.69300 -23.89500 -28.60000 1.000 50.90000  ? 289 ARG A CZ  1 
ATOM   1921  N  NH1 . ARG A  1 258 ? -31.72000 -23.98500 -29.43500 1.000 43.38000  ? 289 ARG A NH1 1 
ATOM   1922  N  NH2 . ARG A  1 258 ? -29.47500 -24.20700 -29.03100 1.000 48.71000  ? 289 ARG A NH2 1 
ATOM   1923  N  N   . GLY A  1 259 ? -33.92200 -28.38600 -28.09400 1.000 41.05000  ? 290 GLY A N   1 
ATOM   1924  C  CA  . GLY A  1 259 ? -34.51300 -29.12900 -29.19500 1.000 42.72000  ? 290 GLY A CA  1 
ATOM   1925  C  C   . GLY A  1 259 ? -35.59700 -30.08500 -28.73100 1.000 49.57000  ? 290 GLY A C   1 
ATOM   1926  O  O   . GLY A  1 259 ? -36.63100 -30.24500 -29.39400 1.000 44.97000  ? 290 GLY A O   1 
ATOM   1927  N  N   . VAL A  1 260 ? -35.40800 -30.68900 -27.55600 1.000 45.16000  ? 291 VAL A N   1 
ATOM   1928  C  CA  . VAL A  1 260 ? -36.46800 -31.53600 -27.03200 1.000 46.93000  ? 291 VAL A CA  1 
ATOM   1929  C  C   . VAL A  1 260 ? -37.73900 -30.71600 -26.80100 1.000 41.58000  ? 291 VAL A C   1 
ATOM   1930  O  O   . VAL A  1 260 ? -38.84300 -31.22300 -26.96600 1.000 39.98000  ? 291 VAL A O   1 
ATOM   1931  C  CB  . VAL A  1 260 ? -36.00200 -32.25800 -25.75800 1.000 40.07000  ? 291 VAL A CB  1 
ATOM   1932  C  CG1 . VAL A  1 260 ? -37.17700 -32.95200 -25.08500 1.000 44.70000  ? 291 VAL A CG1 1 
ATOM   1933  C  CG2 . VAL A  1 260 ? -34.94900 -33.28800 -26.11000 1.000 39.30000  ? 291 VAL A CG2 1 
ATOM   1934  N  N   . GLY A  1 261 ? -37.59900 -29.45400 -26.39000 1.000 45.36000  ? 292 GLY A N   1 
ATOM   1935  C  CA  . GLY A  1 261 ? -38.77000 -28.60900 -26.19500 1.000 42.24000  ? 292 GLY A CA  1 
ATOM   1936  C  C   . GLY A  1 261 ? -39.48400 -28.27400 -27.49300 1.000 47.77000  ? 292 GLY A C   1 
ATOM   1937  O  O   . GLY A  1 261 ? -40.71500 -28.21700 -27.54000 1.000 48.11000  ? 292 GLY A O   1 
ATOM   1938  N  N   . LYS A  1 262 ? -38.72000 -28.00200 -28.55400 1.000 47.93000  ? 293 LYS A N   1 
ATOM   1939  C  CA  . LYS A  1 262 ? -39.33600 -27.79500 -29.85900 1.000 48.97000  ? 293 LYS A CA  1 
ATOM   1940  C  C   . LYS A  1 262 ? -39.99300 -29.07600 -30.36800 1.000 46.67000  ? 293 LYS A C   1 
ATOM   1941  O  O   . LYS A  1 262 ? -41.09200 -29.02800 -30.93100 1.000 48.26000  ? 293 LYS A O   1 
ATOM   1942  C  CB  . LYS A  1 262 ? -38.29800 -27.24000 -30.84700 1.000 43.86000  ? 293 LYS A CB  1 
ATOM   1943  C  CG  . LYS A  1 262 ? -37.80000 -25.87700 -30.38300 1.000 52.80000  ? 293 LYS A CG  1 
ATOM   1944  C  CD  . LYS A  1 262 ? -36.63400 -25.26600 -31.15100 1.000 58.71000  ? 293 LYS A CD  1 
ATOM   1945  C  CE  . LYS A  1 262 ? -36.12100 -24.02800 -30.37200 1.000 65.87000  ? 293 LYS A CE  1 
ATOM   1946  N  NZ  . LYS A  1 262 ? -34.68200 -23.64300 -30.56900 1.000 58.75000  ? 293 LYS A NZ  1 
ATOM   1947  N  N   . ILE A  1 263 ? -39.36800 -30.23100 -30.13500 1.000 41.02000  ? 294 ILE A N   1 
ATOM   1948  C  CA  . ILE A  1 263 ? -39.99200 -31.48800 -30.53400 1.000 41.16000  ? 294 ILE A CA  1 
ATOM   1949  C  C   . ILE A  1 263 ? -41.30200 -31.67600 -29.79600 1.000 46.01000  ? 294 ILE A C   1 
ATOM   1950  O  O   . ILE A  1 263 ? -42.30300 -32.11600 -30.37300 1.000 44.76000  ? 294 ILE A O   1 
ATOM   1951  C  CB  . ILE A  1 263 ? -39.04000 -32.66300 -30.28100 1.000 37.71000  ? 294 ILE A CB  1 
ATOM   1952  C  CG1 . ILE A  1 263 ? -37.91800 -32.66800 -31.32100 1.000 39.23000  ? 294 ILE A CG1 1 
ATOM   1953  C  CG2 . ILE A  1 263 ? -39.80200 -33.98100 -30.29500 1.000 33.16000  ? 294 ILE A CG2 1 
ATOM   1954  C  CD1 . ILE A  1 263 ? -36.67000 -33.34300 -30.81800 1.000 35.83000  ? 294 ILE A CD1 1 
ATOM   1955  N  N   . VAL A  1 264 ? -41.31700 -31.33900 -28.50500 1.000 44.99000  ? 295 VAL A N   1 
ATOM   1956  C  CA  . VAL A  1 264 ? -42.52900 -31.48500 -27.71500 1.000 47.41000  ? 295 VAL A CA  1 
ATOM   1957  C  C   . VAL A  1 264 ? -43.63400 -30.58500 -28.26800 1.000 48.83000  ? 295 VAL A C   1 
ATOM   1958  O  O   . VAL A  1 264 ? -44.79200 -30.99900 -28.38600 1.000 46.20000  ? 295 VAL A O   1 
ATOM   1959  C  CB  . VAL A  1 264 ? -42.21600 -31.19400 -26.23500 1.000 48.29000  ? 295 VAL A CB  1 
ATOM   1960  C  CG1 . VAL A  1 264 ? -43.49400 -31.01500 -25.42600 1.000 45.08000  ? 295 VAL A CG1 1 
ATOM   1961  C  CG2 . VAL A  1 264 ? -41.38300 -32.31400 -25.65100 1.000 42.51000  ? 295 VAL A CG2 1 
ATOM   1962  N  N   . GLN A  1 265 ? -43.29600 -29.34200 -28.62400 1.000 51.39000  ? 296 GLN A N   1 
ATOM   1963  C  CA  . GLN A  1 265 ? -44.29000 -28.45600 -29.22800 1.000 52.79000  ? 296 GLN A CA  1 
ATOM   1964  C  C   . GLN A  1 265 ? -44.89400 -29.06000 -30.49400 1.000 54.88000  ? 296 GLN A C   1 
ATOM   1965  O  O   . GLN A  1 265 ? -46.10600 -28.96700 -30.72700 1.000 48.12000  ? 296 GLN A O   1 
ATOM   1966  C  CB  . GLN A  1 265 ? -43.66100 -27.10600 -29.54900 1.000 49.59000  ? 296 GLN A CB  1 
ATOM   1967  C  CG  . GLN A  1 265 ? -43.47200 -26.21800 -28.34800 1.000 57.22000  ? 296 GLN A CG  1 
ATOM   1968  C  CD  . GLN A  1 265 ? -43.41100 -24.74900 -28.73100 1.000 79.73000  ? 296 GLN A CD  1 
ATOM   1969  O  OE1 . GLN A  1 265 ? -43.24500 -24.40500 -29.91200 1.000 79.54000  ? 296 GLN A OE1 1 
ATOM   1970  N  NE2 . GLN A  1 265 ? -43.56000 -23.86700 -27.73400 1.000 79.76000  ? 296 GLN A NE2 1 
ATOM   1971  N  N   . THR A  1 266 ? -44.05900 -29.66600 -31.33400 1.000 51.43000  ? 297 THR A N   1 
ATOM   1972  C  CA  . THR A  1 266 ? -44.56800 -30.27600 -32.55100 1.000 49.60000  ? 297 THR A CA  1 
ATOM   1973  C  C   . THR A  1 266 ? -45.51200 -31.42100 -32.23200 1.000 49.71000  ? 297 THR A C   1 
ATOM   1974  O  O   . THR A  1 266 ? -46.58200 -31.54200 -32.84000 1.000 51.90000  ? 297 THR A O   1 
ATOM   1975  C  CB  . THR A  1 266 ? -43.40700 -30.74800 -33.41500 1.000 43.95000  ? 297 THR A CB  1 
ATOM   1976  O  OG1 . THR A  1 266 ? -42.60800 -29.61400 -33.79500 1.000 52.92000  ? 297 THR A OG1 1 
ATOM   1977  C  CG2 . THR A  1 266 ? -43.91000 -31.45600 -34.66300 1.000 44.67000  ? 297 THR A CG2 1 
ATOM   1978  N  N   . LEU A  1 267 ? -45.15100 -32.25200 -31.25800 1.000 48.44000  ? 298 LEU A N   1 
ATOM   1979  C  CA  . LEU A  1 267 ? -46.00200 -33.38200 -30.89700 1.000 48.12000  ? 298 LEU A CA  1 
ATOM   1980  C  C   . LEU A  1 267 ? -47.38600 -32.92200 -30.44600 1.000 49.01000  ? 298 LEU A C   1 
ATOM   1981  O  O   . LEU A  1 267 ? -48.37900 -33.62800 -30.65900 1.000 50.31000  ? 298 LEU A O   1 
ATOM   1982  C  CB  . LEU A  1 267 ? -45.31100 -34.21100 -29.81400 1.000 52.35000  ? 298 LEU A CB  1 
ATOM   1983  C  CG  . LEU A  1 267 ? -44.10800 -35.00900 -30.34600 1.000 51.34000  ? 298 LEU A CG  1 
ATOM   1984  C  CD1 . LEU A  1 267 ? -43.35800 -35.65500 -29.20200 1.000 39.98000  ? 298 LEU A CD1 1 
ATOM   1985  C  CD2 . LEU A  1 267 ? -44.52500 -36.05400 -31.39600 1.000 44.77000  ? 298 LEU A CD2 1 
ATOM   1986  N  N   . LYS A  1 268 ? -47.46900 -31.76200 -29.79700 1.000 52.71000  ? 299 LYS A N   1 
ATOM   1987  C  CA  . LYS A  1 268 ? -48.76200 -31.25900 -29.36300 1.000 52.38000  ? 299 LYS A CA  1 
ATOM   1988  C  C   . LYS A  1 268 ? -49.55400 -30.70500 -30.54100 1.000 56.39000  ? 299 LYS A C   1 
ATOM   1989  O  O   . LYS A  1 268 ? -50.75000 -30.99200 -30.67700 1.000 58.02000  ? 299 LYS A O   1 
ATOM   1990  C  CB  . LYS A  1 268 ? -48.56100 -30.19100 -28.28800 1.000 53.03000  ? 299 LYS A CB  1 
ATOM   1991  C  CG  . LYS A  1 268 ? -47.82300 -30.72600 -27.07100 1.000 56.57000  ? 299 LYS A CG  1 
ATOM   1992  C  CD  . LYS A  1 268 ? -47.53200 -29.66300 -26.01200 1.000 52.17000  ? 299 LYS A CD  1 
ATOM   1993  C  CE  . LYS A  1 268 ? -46.92900 -30.32600 -24.78300 1.000 51.49000  ? 299 LYS A CE  1 
ATOM   1994  N  NZ  . LYS A  1 268 ? -46.79500 -29.42900 -23.60500 1.000 57.84000  ? 299 LYS A NZ  1 
ATOM   1995  N  N   . GLU A  1 269 ? -48.89300 -29.97000 -31.44000 1.000 54.94000  ? 300 GLU A N   1 
ATOM   1996  C  CA  . GLU A  1 269 ? -49.59300 -29.43300 -32.60300 1.000 51.79000  ? 300 GLU A CA  1 
ATOM   1997  C  C   . GLU A  1 269 ? -50.13200 -30.55200 -33.48000 1.000 53.17000  ? 300 GLU A C   1 
ATOM   1998  O  O   . GLU A  1 269 ? -51.29500 -30.51500 -33.89400 1.000 58.53000  ? 300 GLU A O   1 
ATOM   1999  C  CB  . GLU A  1 269 ? -48.66900 -28.52000 -33.40400 1.000 55.19000  ? 300 GLU A CB  1 
ATOM   2000  C  CG  . GLU A  1 269 ? -48.41500 -27.17400 -32.74800 1.000 54.05000  ? 300 GLU A CG  1 
ATOM   2001  C  CD  . GLU A  1 269 ? -47.09600 -26.55900 -33.18600 1.000 67.77000  ? 300 GLU A CD  1 
ATOM   2002  O  OE1 . GLU A  1 269 ? -46.34000 -27.24800 -33.90800 1.000 70.87000  ? 300 GLU A OE1 1 
ATOM   2003  O  OE2 . GLU A  1 269 ? -46.81200 -25.39900 -32.80300 1.000 71.52000  ? 300 GLU A OE2 1 
ATOM   2004  N  N   . THR A  1 270 ? -49.33400 -31.58800 -33.72300 1.000 51.09000  ? 301 THR A N   1 
ATOM   2005  C  CA  . THR A  1 270 ? -49.85000 -32.72800 -34.46100 1.000 48.90000  ? 301 THR A CA  1 
ATOM   2006  C  C   . THR A  1 270 ? -50.73400 -33.61800 -33.59400 1.000 51.56000  ? 301 THR A C   1 
ATOM   2007  O  O   . THR A  1 270 ? -51.19300 -34.66000 -34.07200 1.000 56.45000  ? 301 THR A O   1 
ATOM   2008  C  CB  . THR A  1 270 ? -48.69700 -33.57000 -35.03100 1.000 59.42000  ? 301 THR A CB  1 
ATOM   2009  O  OG1 . THR A  1 270 ? -47.95500 -34.17400 -33.94900 1.000 55.46000  ? 301 THR A OG1 1 
ATOM   2010  C  CG2 . THR A  1 270 ? -47.75400 -32.70400 -35.90100 1.000 45.33000  ? 301 THR A CG2 1 
ATOM   2011  N  N   . LYS A  1 271 ? -51.02300 -33.20500 -32.35700 1.000 50.95000  ? 302 LYS A N   1 
ATOM   2012  C  CA  . LYS A  1 271 ? -51.84500 -33.99300 -31.43100 1.000 60.58000  ? 302 LYS A CA  1 
ATOM   2013  C  C   . LYS A  1 271 ? -51.32300 -35.43200 -31.27300 1.000 56.22000  ? 302 LYS A C   1 
ATOM   2014  O  O   . LYS A  1 271 ? -52.08700 -36.36300 -31.02900 1.000 53.09000  ? 302 LYS A O   1 
ATOM   2015  C  CB  . LYS A  1 271 ? -53.32500 -33.98300 -31.86100 1.000 57.08000  ? 302 LYS A CB  1 
ATOM   2016  N  N   . GLN A  1 272 ? -50.01000 -35.63300 -31.36900 1.000 55.04000  ? 303 GLN A N   1 
ATOM   2017  C  CA  . GLN A  1 272 ? -49.43500 -36.95300 -31.15300 1.000 51.45000  ? 303 GLN A CA  1 
ATOM   2018  C  C   . GLN A  1 272 ? -48.84300 -37.12900 -29.75500 1.000 49.50000  ? 303 GLN A C   1 
ATOM   2019  O  O   . GLN A  1 272 ? -48.40900 -38.23400 -29.42500 1.000 47.17000  ? 303 GLN A O   1 
ATOM   2020  C  CB  . GLN A  1 272 ? -48.34800 -37.22700 -32.19300 1.000 54.20000  ? 303 GLN A CB  1 
ATOM   2021  C  CG  . GLN A  1 272 ? -48.85300 -37.25600 -33.60700 1.000 54.64000  ? 303 GLN A CG  1 
ATOM   2022  C  CD  . GLN A  1 272 ? -49.98300 -38.24100 -33.77600 1.000 57.43000  ? 303 GLN A CD  1 
ATOM   2023  O  OE1 . GLN A  1 272 ? -49.88200 -39.41000 -33.38300 1.000 58.08000  ? 303 GLN A OE1 1 
ATOM   2024  N  NE2 . GLN A  1 272 ? -51.08100 -37.77300 -34.35300 1.000 67.61000  ? 303 GLN A NE2 1 
ATOM   2025  N  N   . PHE A  1 273 ? -48.86300 -36.08400 -28.91800 1.000 47.83000  ? 304 PHE A N   1 
ATOM   2026  C  CA  . PHE A  1 273 ? -48.09600 -36.07800 -27.66900 1.000 49.99000  ? 304 PHE A CA  1 
ATOM   2027  C  C   . PHE A  1 273 ? -48.54600 -37.18300 -26.71000 1.000 56.15000  ? 304 PHE A C   1 
ATOM   2028  O  O   . PHE A  1 273 ? -47.71400 -37.92900 -26.17300 1.000 56.40000  ? 304 PHE A O   1 
ATOM   2029  C  CB  . PHE A  1 273 ? -48.21200 -34.69800 -27.02100 1.000 51.42000  ? 304 PHE A CB  1 
ATOM   2030  C  CG  . PHE A  1 273 ? -47.33900 -34.49600 -25.79800 1.000 57.90000  ? 304 PHE A CG  1 
ATOM   2031  C  CD1 . PHE A  1 273 ? -45.95800 -34.54300 -25.89900 1.000 54.43000  ? 304 PHE A CD1 1 
ATOM   2032  C  CD2 . PHE A  1 273 ? -47.89900 -34.14900 -24.57100 1.000 57.90000  ? 304 PHE A CD2 1 
ATOM   2033  C  CE1 . PHE A  1 273 ? -45.14200 -34.32100 -24.78900 1.000 53.49000  ? 304 PHE A CE1 1 
ATOM   2034  C  CE2 . PHE A  1 273 ? -47.09900 -33.90700 -23.45700 1.000 56.14000  ? 304 PHE A CE2 1 
ATOM   2035  C  CZ  . PHE A  1 273 ? -45.71600 -33.99300 -23.56100 1.000 53.77000  ? 304 PHE A CZ  1 
ATOM   2036  N  N   . ASP A  1 274 ? -49.85600 -37.29300 -26.45600 1.000 52.83000  ? 305 ASP A N   1 
ATOM   2037  C  CA  . ASP A  1 274 ? -50.31100 -38.21700 -25.42000 1.000 52.87000  ? 305 ASP A CA  1 
ATOM   2038  C  C   . ASP A  1 274 ? -50.08000 -39.67500 -25.78000 1.000 47.82000  ? 305 ASP A C   1 
ATOM   2039  O  O   . ASP A  1 274 ? -49.88400 -40.48400 -24.87000 1.000 51.33000  ? 305 ASP A O   1 
ATOM   2040  C  CB  . ASP A  1 274 ? -51.78000 -37.98900 -25.07000 1.000 56.44000  ? 305 ASP A CB  1 
ATOM   2041  C  CG  . ASP A  1 274 ? -51.95200 -36.91400 -24.01100 1.000 71.06000  ? 305 ASP A CG  1 
ATOM   2042  O  OD1 . ASP A  1 274 ? -50.92800 -36.35700 -23.52200 1.000 58.42000  ? 305 ASP A OD1 1 
ATOM   2043  O  OD2 . ASP A  1 274 ? -53.11300 -36.67200 -23.62200 1.000 82.78000  ? 305 ASP A OD2 1 
ATOM   2044  N  N   . ASN A  1 275 ? -50.12000 -40.04700 -27.06500 1.000 40.19000  ? 306 ASN A N   1 
ATOM   2045  C  CA  . ASN A  1 275 ? -49.88800 -41.43700 -27.46800 1.000 45.02000  ? 306 ASN A CA  1 
ATOM   2046  C  C   . ASN A  1 275 ? -48.49900 -41.65400 -28.09100 1.000 46.92000  ? 306 ASN A C   1 
ATOM   2047  O  O   . ASN A  1 275 ? -48.31900 -42.51200 -28.96500 1.000 46.08000  ? 306 ASN A O   1 
ATOM   2048  C  CB  . ASN A  1 275 ? -50.98400 -41.93100 -28.42100 1.000 35.19000  ? 306 ASN A CB  1 
ATOM   2049  C  CG  . ASN A  1 275 ? -51.01700 -43.45600 -28.53300 1.000 39.64000  ? 306 ASN A CG  1 
ATOM   2050  O  OD1 . ASN A  1 275 ? -50.69200 -44.15800 -27.58000 1.000 40.16000  ? 306 ASN A OD1 1 
ATOM   2051  N  ND2 . ASN A  1 275 ? -51.41900 -43.96900 -29.69200 1.000 45.14000  ? 306 ASN A ND2 1 
ATOM   2052  N  N   . THR A  1 276 ? -47.50100 -40.91500 -27.62400 1.000 45.81000  ? 307 THR A N   1 
ATOM   2053  C  CA  . THR A  1 276 ? -46.10800 -41.14000 -27.98700 1.000 46.39000  ? 307 THR A CA  1 
ATOM   2054  C  C   . THR A  1 276 ? -45.34400 -41.59500 -26.75400 1.000 42.37000  ? 307 THR A C   1 
ATOM   2055  O  O   . THR A  1 276 ? -45.43900 -40.95600 -25.70500 1.000 38.42000  ? 307 THR A O   1 
ATOM   2056  C  CB  . THR A  1 276 ? -45.45900 -39.87000 -28.54900 1.000 46.99000  ? 307 THR A CB  1 
ATOM   2057  O  OG1 . THR A  1 276 ? -46.07200 -39.52500 -29.79000 1.000 46.58000  ? 307 THR A OG1 1 
ATOM   2058  C  CG2 . THR A  1 276 ? -43.93300 -40.07300 -28.76900 1.000 37.60000  ? 307 THR A CG2 1 
ATOM   2059  N  N   . LEU A  1 277 ? -44.62300 -42.71600 -26.86900 1.000 41.52000  ? 308 LEU A N   1 
ATOM   2060  C  CA  . LEU A  1 277 ? -43.66200 -43.11900 -25.84300 1.000 42.71000  ? 308 LEU A CA  1 
ATOM   2061  C  C   . LEU A  1 277 ? -42.31500 -42.47300 -26.15800 1.000 42.04000  ? 308 LEU A C   1 
ATOM   2062  O  O   . LEU A  1 277 ? -41.66400 -42.83500 -27.14100 1.000 41.63000  ? 308 LEU A O   1 
ATOM   2063  C  CB  . LEU A  1 277 ? -43.53400 -44.63800 -25.77600 1.000 36.31000  ? 308 LEU A CB  1 
ATOM   2064  C  CG  . LEU A  1 277 ? -42.32900 -45.16700 -25.00000 1.000 43.14000  ? 308 LEU A CG  1 
ATOM   2065  C  CD1 . LEU A  1 277 ? -42.39300 -44.76700 -23.53200 1.000 43.43000  ? 308 LEU A CD1 1 
ATOM   2066  C  CD2 . LEU A  1 277 ? -42.26500 -46.67000 -25.12800 1.000 41.74000  ? 308 LEU A CD2 1 
ATOM   2067  N  N   . ILE A  1 278 ? -41.89900 -41.52000 -25.32900 1.000 38.21000  ? 309 ILE A N   1 
ATOM   2068  C  CA  . ILE A  1 278 ? -40.58600 -40.89400 -25.43900 1.000 41.97000  ? 309 ILE A CA  1 
ATOM   2069  C  C   . ILE A  1 278 ? -39.65500 -41.58500 -24.44800 1.000 45.53000  ? 309 ILE A C   1 
ATOM   2070  O  O   . ILE A  1 278 ? -39.93600 -41.63000 -23.24200 1.000 42.29000  ? 309 ILE A O   1 
ATOM   2071  C  CB  . ILE A  1 278 ? -40.63900 -39.38800 -25.14700 1.000 44.06000  ? 309 ILE A CB  1 
ATOM   2072  C  CG1 . ILE A  1 278 ? -41.63200 -38.67700 -26.05600 1.000 40.55000  ? 309 ILE A CG1 1 
ATOM   2073  C  CG2 . ILE A  1 278 ? -39.24700 -38.77900 -25.29100 1.000 37.88000  ? 309 ILE A CG2 1 
ATOM   2074  C  CD1 . ILE A  1 278 ? -41.77800 -37.20900 -25.70900 1.000 39.35000  ? 309 ILE A CD1 1 
ATOM   2075  N  N   . VAL A  1 279 ? -38.55900 -42.13400 -24.95500 1.000 43.84000  ? 310 VAL A N   1 
ATOM   2076  C  CA  . VAL A  1 279 ? -37.51300 -42.75000 -24.13800 1.000 40.98000  ? 310 VAL A CA  1 
ATOM   2077  C  C   . VAL A  1 279 ? -36.27600 -41.88200 -24.26600 1.000 39.71000  ? 310 VAL A C   1 
ATOM   2078  O  O   . VAL A  1 279 ? -35.84400 -41.58400 -25.38200 1.000 41.45000  ? 310 VAL A O   1 
ATOM   2079  C  CB  . VAL A  1 279 ? -37.20900 -44.18700 -24.58500 1.000 44.29000  ? 310 VAL A CB  1 
ATOM   2080  C  CG1 . VAL A  1 279 ? -36.08900 -44.79500 -23.74000 1.000 35.25000  ? 310 VAL A CG1 1 
ATOM   2081  C  CG2 . VAL A  1 279 ? -38.49300 -45.03500 -24.57700 1.000 37.59000  ? 310 VAL A CG2 1 
ATOM   2082  N  N   . PHE A  1 280 ? -35.74600 -41.41700 -23.13900 1.000 40.48000  ? 311 PHE A N   1 
ATOM   2083  C  CA  . PHE A  1 280 ? -34.52200 -40.63100 -23.13800 1.000 40.59000  ? 311 PHE A CA  1 
ATOM   2084  C  C   . PHE A  1 280 ? -33.44700 -41.37400 -22.35500 1.000 41.35000  ? 311 PHE A C   1 
ATOM   2085  O  O   . PHE A  1 280 ? -33.69600 -41.82500 -21.23400 1.000 39.09000  ? 311 PHE A O   1 
ATOM   2086  C  CB  . PHE A  1 280 ? -34.76000 -39.24100 -22.53800 1.000 38.71000  ? 311 PHE A CB  1 
ATOM   2087  C  CG  . PHE A  1 280 ? -33.49300 -38.46600 -22.28300 1.000 41.10000  ? 311 PHE A CG  1 
ATOM   2088  C  CD1 . PHE A  1 280 ? -32.82100 -38.57300 -21.08000 1.000 42.18000  ? 311 PHE A CD1 1 
ATOM   2089  C  CD2 . PHE A  1 280 ? -32.98200 -37.62300 -23.24700 1.000 41.20000  ? 311 PHE A CD2 1 
ATOM   2090  C  CE1 . PHE A  1 280 ? -31.67300 -37.87100 -20.85300 1.000 36.21000  ? 311 PHE A CE1 1 
ATOM   2091  C  CE2 . PHE A  1 280 ? -31.83500 -36.89300 -23.01000 1.000 38.85000  ? 311 PHE A CE2 1 
ATOM   2092  C  CZ  . PHE A  1 280 ? -31.17500 -37.02500 -21.82600 1.000 37.17000  ? 311 PHE A CZ  1 
ATOM   2093  N  N   . LEU A  1 281 ? -32.24800 -41.47400 -22.92900 1.000 38.40000  ? 312 LEU A N   1 
ATOM   2094  C  CA  . LEU A  1 281 ? -31.14100 -42.10900 -22.23200 1.000 34.32000  ? 312 LEU A CA  1 
ATOM   2095  C  C   . LEU A  1 281 ? -29.81700 -41.68600 -22.87700 1.000 39.22000  ? 312 LEU A C   1 
ATOM   2096  O  O   . LEU A  1 281 ? -29.77800 -41.04900 -23.93300 1.000 31.53000  ? 312 LEU A O   1 
ATOM   2097  C  CB  . LEU A  1 281 ? -31.28000 -43.63500 -22.21300 1.000 36.77000  ? 312 LEU A CB  1 
ATOM   2098  C  CG  . LEU A  1 281 ? -30.93200 -44.40200 -23.48700 1.000 34.53000  ? 312 LEU A CG  1 
ATOM   2099  C  CD1 . LEU A  1 281 ? -30.62500 -45.84400 -23.16800 1.000 31.90000  ? 312 LEU A CD1 1 
ATOM   2100  C  CD2 . LEU A  1 281 ? -32.02700 -44.31200 -24.54200 1.000 37.48000  ? 312 LEU A CD2 1 
ATOM   2101  N  N   . SER A  1 282 ? -28.72500 -42.02400 -22.19800 1.000 35.52000  ? 313 SER A N   1 
ATOM   2102  C  CA  . SER A  1 282 ? -27.38200 -41.86600 -22.73200 1.000 34.77000  ? 313 SER A CA  1 
ATOM   2103  C  C   . SER A  1 282 ? -26.85000 -43.21100 -23.20100 1.000 38.04000  ? 313 SER A C   1 
ATOM   2104  O  O   . SER A  1 282 ? -27.24400 -44.26800 -22.68800 1.000 39.87000  ? 313 SER A O   1 
ATOM   2105  C  CB  . SER A  1 282 ? -26.45300 -41.28900 -21.67700 1.000 34.80000  ? 313 SER A CB  1 
ATOM   2106  O  OG  . SER A  1 282 ? -25.16000 -41.13300 -22.21100 1.000 39.16000  ? 313 SER A OG  1 
ATOM   2107  N  N   . ASP A  1 283 ? -25.94900 -43.18000 -24.18300 1.000 35.15000  ? 314 ASP A N   1 
ATOM   2108  C  CA  . ASP A  1 283 ? -25.44600 -44.46100 -24.67100 1.000 39.25000  ? 314 ASP A CA  1 
ATOM   2109  C  C   . ASP A  1 283 ? -24.39200 -45.07500 -23.75900 1.000 36.12000  ? 314 ASP A C   1 
ATOM   2110  O  O   . ASP A  1 283 ? -24.12000 -46.27800 -23.88100 1.000 38.19000  ? 314 ASP A O   1 
ATOM   2111  C  CB  . ASP A  1 283 ? -24.86200 -44.32900 -26.06600 1.000 40.98000  ? 314 ASP A CB  1 
ATOM   2112  C  CG  . ASP A  1 283 ? -23.57700 -43.54400 -26.08800 1.000 39.57000  ? 314 ASP A CG  1 
ATOM   2113  O  OD1 . ASP A  1 283 ? -23.35700 -42.66200 -25.21500 1.000 43.57000  ? 314 ASP A OD1 1 
ATOM   2114  O  OD2 . ASP A  1 283 ? -22.78200 -43.79700 -27.00700 1.000 41.96000  ? 314 ASP A OD2 1 
ATOM   2115  N  N   . ASN A  1 284 ? -23.80900 -44.29600 -22.84700 1.000 31.29000  ? 315 ASN A N   1 
ATOM   2116  C  CA  . ASN A  1 284 ? -22.85500 -44.80900 -21.86500 1.000 33.18000  ? 315 ASN A CA  1 
ATOM   2117  C  C   . ASN A  1 284 ? -22.58300 -43.69600 -20.86000 1.000 34.01000  ? 315 ASN A C   1 
ATOM   2118  O  O   . ASN A  1 284 ? -23.15900 -42.60900 -20.94000 1.000 36.47000  ? 315 ASN A O   1 
ATOM   2119  C  CB  . ASN A  1 284 ? -21.55200 -45.33200 -22.50400 1.000 35.40000  ? 315 ASN A CB  1 
ATOM   2120  C  CG  . ASN A  1 284 ? -20.90100 -44.31600 -23.44300 1.000 36.42000  ? 315 ASN A CG  1 
ATOM   2121  O  OD1 . ASN A  1 284 ? -20.84300 -44.52200 -24.65400 1.000 36.49000  ? 315 ASN A OD1 1 
ATOM   2122  N  ND2 . ASN A  1 284 ? -20.39800 -43.23300 -22.88700 1.000 35.79000  ? 315 ASN A ND2 1 
ATOM   2123  N  N   . GLY A  1 285 ? -21.73100 -43.98900 -19.88500 1.000 29.86000  ? 316 GLY A N   1 
ATOM   2124  C  CA  . GLY A  1 285 ? -21.40700 -43.00600 -18.86400 1.000 36.97000  ? 316 GLY A CA  1 
ATOM   2125  C  C   . GLY A  1 285 ? -20.63600 -41.81000 -19.40000 1.000 35.52000  ? 316 GLY A C   1 
ATOM   2126  O  O   . GLY A  1 285 ? -20.08300 -41.82300 -20.49700 1.000 35.24000  ? 316 GLY A O   1 
ATOM   2127  N  N   . GLY A  1 286 ? -20.64400 -40.72900 -18.62000 1.000 34.07000  ? 317 GLY A N   1 
ATOM   2128  C  CA  . GLY A  1 286 ? -19.92500 -39.53900 -19.01000 1.000 32.82000  ? 317 GLY A CA  1 
ATOM   2129  C  C   . GLY A  1 286 ? -18.42100 -39.73100 -18.91600 1.000 33.90000  ? 317 GLY A C   1 
ATOM   2130  O  O   . GLY A  1 286 ? -17.91700 -40.45300 -18.05700 1.000 32.95000  ? 317 GLY A O   1 
ATOM   2131  N  N   . ASN A  1 287 ? -17.68800 -39.06300 -19.81300 1.000 33.85000  ? 318 ASN A N   1 
ATOM   2132  C  CA  . ASN A  1 287 ? -16.21600 -39.04400 -19.76200 1.000 35.77000  ? 318 ASN A CA  1 
ATOM   2133  C  C   . ASN A  1 287 ? -15.80000 -37.87700 -18.86700 1.000 36.15000  ? 318 ASN A C   1 
ATOM   2134  O  O   . ASN A  1 287 ? -15.93400 -36.71500 -19.26600 1.000 35.79000  ? 318 ASN A O   1 
ATOM   2135  C  CB  . ASN A  1 287 ? -15.64100 -38.90000 -21.17100 1.000 27.31000  ? 318 ASN A CB  1 
ATOM   2136  C  CG  . ASN A  1 287 ? -14.10800 -39.01900 -21.21900 1.000 43.45000  ? 318 ASN A CG  1 
ATOM   2137  O  OD1 . ASN A  1 287 ? -13.39000 -38.65800 -20.26900 1.000 36.59000  ? 318 ASN A OD1 1 
ATOM   2138  N  ND2 . ASN A  1 287 ? -13.60400 -39.51600 -22.35100 1.000 36.46000  ? 318 ASN A ND2 1 
ATOM   2139  N  N   . PHE A  1 288 ? -15.27800 -38.16500 -17.66000 1.000 34.01000  ? 319 PHE A N   1 
ATOM   2140  C  CA  . PHE A  1 288 ? -15.05600 -37.01400 -16.79400 1.000 37.58000  ? 319 PHE A CA  1 
ATOM   2141  C  C   . PHE A  1 288 ? -13.79900 -36.22300 -17.16000 1.000 40.62000  ? 319 PHE A C   1 
ATOM   2142  O  O   . PHE A  1 288 ? -13.51400 -35.22000 -16.51000 1.000 38.05000  ? 319 PHE A O   1 
ATOM   2143  C  CB  . PHE A  1 288 ? -15.05400 -37.39800 -15.28900 1.000 34.27000  ? 319 PHE A CB  1 
ATOM   2144  C  CG  . PHE A  1 288 ? -14.13300 -38.53800 -14.87900 1.000 36.52000  ? 319 PHE A CG  1 
ATOM   2145  C  CD1 . PHE A  1 288 ? -12.88200 -38.72500 -15.44400 1.000 36.92000  ? 319 PHE A CD1 1 
ATOM   2146  C  CD2 . PHE A  1 288 ? -14.52500 -39.38500 -13.83800 1.000 37.43000  ? 319 PHE A CD2 1 
ATOM   2147  C  CE1 . PHE A  1 288 ? -12.04800 -39.75200 -15.03200 1.000 37.20000  ? 319 PHE A CE1 1 
ATOM   2148  C  CE2 . PHE A  1 288 ? -13.71000 -40.42400 -13.40500 1.000 38.85000  ? 319 PHE A CE2 1 
ATOM   2149  C  CZ  . PHE A  1 288 ? -12.45700 -40.61100 -14.00700 1.000 43.67000  ? 319 PHE A CZ  1 
ATOM   2150  N  N   . ASN A  1 289 ? -13.08600 -36.59700 -18.21500 1.000 34.10000  ? 320 ASN A N   1 
ATOM   2151  C  CA  . ASN A  1 289 ? -12.01200 -35.76300 -18.73700 1.000 37.91000  ? 320 ASN A CA  1 
ATOM   2152  C  C   . ASN A  1 289 ? -12.48800 -34.70600 -19.71400 1.000 36.94000  ? 320 ASN A C   1 
ATOM   2153  O  O   . ASN A  1 289 ? -11.69000 -33.84500 -20.10100 1.000 40.23000  ? 320 ASN A O   1 
ATOM   2154  C  CB  . ASN A  1 289 ? -10.96900 -36.63900 -19.41300 1.000 36.25000  ? 320 ASN A CB  1 
ATOM   2155  C  CG  . ASN A  1 289 ? -10.36300 -37.59000 -18.46200 1.000 38.92000  ? 320 ASN A CG  1 
ATOM   2156  O  OD1 . ASN A  1 289 ? -9.78500  -37.18900 -17.44100 1.000 40.00000  ? 320 ASN A OD1 1 
ATOM   2157  N  ND2 . ASN A  1 289 ? -10.54400 -38.87000 -18.72900 1.000 43.43000  ? 320 ASN A ND2 1 
ATOM   2158  N  N   . HIS A  1 290 ? -13.74100 -34.77200 -20.15500 1.000 35.22000  ? 321 HIS A N   1 
ATOM   2159  C  CA  . HIS A  1 290 ? -14.27700 -33.87000 -21.16700 1.000 33.39000  ? 321 HIS A CA  1 
ATOM   2160  C  C   . HIS A  1 290 ? -15.60800 -33.28600 -20.72600 1.000 40.47000  ? 321 HIS A C   1 
ATOM   2161  O  O   . HIS A  1 290 ? -16.58800 -33.27000 -21.47800 1.000 38.49000  ? 321 HIS A O   1 
ATOM   2162  C  CB  . HIS A  1 290 ? -14.41800 -34.60000 -22.49000 1.000 39.55000  ? 321 HIS A CB  1 
ATOM   2163  C  CG  . HIS A  1 290 ? -13.11200 -35.04700 -23.04500 1.000 40.61000  ? 321 HIS A CG  1 
ATOM   2164  N  ND1 . HIS A  1 290 ? -12.86200 -36.35000 -23.41100 1.000 49.79000  ? 321 HIS A ND1 1 
ATOM   2165  C  CD2 . HIS A  1 290 ? -11.96400 -34.36600 -23.25500 1.000 42.25000  ? 321 HIS A CD2 1 
ATOM   2166  C  CE1 . HIS A  1 290 ? -11.61100 -36.45400 -23.82200 1.000 47.97000  ? 321 HIS A CE1 1 
ATOM   2167  N  NE2 . HIS A  1 290 ? -11.04300 -35.26500 -23.73100 1.000 46.62000  ? 321 HIS A NE2 1 
ATOM   2168  N  N   . GLY A  1 291 ? -15.66300 -32.81300 -19.47700 1.000 33.96000  ? 322 GLY A N   1 
ATOM   2169  C  CA  . GLY A  1 291 ? -16.74500 -31.98700 -19.02400 1.000 30.69000  ? 322 GLY A CA  1 
ATOM   2170  C  C   . GLY A  1 291 ? -17.89100 -32.69200 -18.32000 1.000 37.73000  ? 322 GLY A C   1 
ATOM   2171  O  O   . GLY A  1 291 ? -18.78100 -32.00200 -17.82500 1.000 37.41000  ? 322 GLY A O   1 
ATOM   2172  N  N   . ALA A  1 292 ? -17.93000 -34.02900 -18.30100 1.000 33.96000  ? 323 ALA A N   1 
ATOM   2173  C  CA  . ALA A  1 292 ? -19.05200 -34.78300 -17.74800 1.000 35.84000  ? 323 ALA A CA  1 
ATOM   2174  C  C   . ALA A  1 292 ? -18.90600 -34.99600 -16.23600 1.000 38.86000  ? 323 ALA A C   1 
ATOM   2175  O  O   . ALA A  1 292 ? -17.80900 -34.94400 -15.68100 1.000 31.11000  ? 323 ALA A O   1 
ATOM   2176  C  CB  . ALA A  1 292 ? -19.19200 -36.14700 -18.42000 1.000 29.59000  ? 323 ALA A CB  1 
ATOM   2177  N  N   . ASN A  1 293 ? -20.04100 -35.25900 -15.57500 1.000 38.76000  ? 324 ASN A N   1 
ATOM   2178  C  CA  . ASN A  1 293 ? -20.05900 -35.51200 -14.13600 1.000 36.41000  ? 324 ASN A CA  1 
ATOM   2179  C  C   . ASN A  1 293 ? -20.97800 -36.69600 -13.88700 1.000 35.40000  ? 324 ASN A C   1 
ATOM   2180  O  O   . ASN A  1 293 ? -22.15800 -36.64600 -14.24200 1.000 39.88000  ? 324 ASN A O   1 
ATOM   2181  C  CB  . ASN A  1 293 ? -20.50300 -34.24800 -13.36800 1.000 36.43000  ? 324 ASN A CB  1 
ATOM   2182  C  CG  . ASN A  1 293 ? -20.37200 -34.38000 -11.82300 1.000 42.91000  ? 324 ASN A CG  1 
ATOM   2183  O  OD1 . ASN A  1 293 ? -20.35400 -35.47500 -11.24700 1.000 37.84000  ? 324 ASN A OD1 1 
ATOM   2184  N  ND2 . ASN A  1 293 ? -20.22300 -33.24100 -11.16900 1.000 44.06000  ? 324 ASN A ND2 1 
ATOM   2185  N  N   . ASN A  1 294 ? -20.43700 -37.75700 -13.28400 1.000 34.25000  ? 325 ASN A N   1 
ATOM   2186  C  CA  . ASN A  1 294 ? -21.17000 -38.98900 -13.02600 1.000 32.19000  ? 325 ASN A CA  1 
ATOM   2187  C  C   . ASN A  1 294 ? -21.61100 -39.13700 -11.55900 1.000 35.92000  ? 325 ASN A C   1 
ATOM   2188  O  O   . ASN A  1 294 ? -22.00400 -40.23100 -11.14700 1.000 35.99000  ? 325 ASN A O   1 
ATOM   2189  C  CB  . ASN A  1 294 ? -20.28200 -40.16200 -13.42200 1.000 36.58000  ? 325 ASN A CB  1 
ATOM   2190  C  CG  . ASN A  1 294 ? -20.01500 -40.21800 -14.92700 1.000 38.25000  ? 325 ASN A CG  1 
ATOM   2191  O  OD1 . ASN A  1 294 ? -20.90200 -39.95900 -15.76400 1.000 35.50000  ? 325 ASN A OD1 1 
ATOM   2192  N  ND2 . ASN A  1 294 ? -18.76800 -40.49300 -15.27300 1.000 34.77000  ? 325 ASN A ND2 1 
ATOM   2193  N  N   . TYR A  1 295 ? -21.54000 -38.07500 -10.76400 1.000 31.03000  ? 326 TYR A N   1 
ATOM   2194  C  CA  . TYR A  1 295 ? -21.89300 -38.18500 -9.36000  1.000 37.48000  ? 326 TYR A CA  1 
ATOM   2195  C  C   . TYR A  1 295 ? -23.31500 -38.74200 -9.20300  1.000 41.36000  ? 326 TYR A C   1 
ATOM   2196  O  O   . TYR A  1 295 ? -24.23700 -38.35100 -9.94200  1.000 36.57000  ? 326 TYR A O   1 
ATOM   2197  C  CB  . TYR A  1 295 ? -21.77100 -36.81900 -8.68300  1.000 40.83000  ? 326 TYR A CB  1 
ATOM   2198  C  CG  . TYR A  1 295 ? -22.11400 -36.84800 -7.21900  1.000 48.58000  ? 326 TYR A CG  1 
ATOM   2199  C  CD1 . TYR A  1 295 ? -23.44300 -36.72300 -6.80100  1.000 46.18000  ? 326 TYR A CD1 1 
ATOM   2200  C  CD2 . TYR A  1 295 ? -21.12600 -37.01800 -6.24600  1.000 42.68000  ? 326 TYR A CD2 1 
ATOM   2201  C  CE1 . TYR A  1 295 ? -23.77500 -36.75600 -5.45800  1.000 47.39000  ? 326 TYR A CE1 1 
ATOM   2202  C  CE2 . TYR A  1 295 ? -21.45200 -37.05000 -4.89700  1.000 47.47000  ? 326 TYR A CE2 1 
ATOM   2203  C  CZ  . TYR A  1 295 ? -22.77900 -36.91900 -4.51800  1.000 48.46000  ? 326 TYR A CZ  1 
ATOM   2204  O  OH  . TYR A  1 295 ? -23.12200 -36.95300 -3.20100  1.000 62.15000  ? 326 TYR A OH  1 
ATOM   2205  N  N   . PRO A  1 296 ? -23.53900 -39.62600 -8.24000  1.000 36.94000  ? 327 PRO A N   1 
ATOM   2206  C  CA  . PRO A  1 296 ? -22.57500 -40.10400 -7.22600  1.000 40.81000  ? 327 PRO A CA  1 
ATOM   2207  C  C   . PRO A  1 296 ? -21.81400 -41.36300 -7.63500  1.000 35.18000  ? 327 PRO A C   1 
ATOM   2208  O  O   . PRO A  1 296 ? -21.29200 -42.04000 -6.77100  1.000 35.48000  ? 327 PRO A O   1 
ATOM   2209  C  CB  . PRO A  1 296 ? -23.48800 -40.37700 -6.02500  1.000 37.89000  ? 327 PRO A CB  1 
ATOM   2210  C  CG  . PRO A  1 296 ? -24.79300 -40.91300 -6.69300  1.000 39.59000  ? 327 PRO A CG  1 
ATOM   2211  C  CD  . PRO A  1 296 ? -24.87000 -40.24200 -8.06400  1.000 34.91000  ? 327 PRO A CD  1 
ATOM   2212  N  N   . LEU A  1 297 ? -21.76100 -41.72900 -8.91800  1.000 34.12000  ? 328 LEU A N   1 
ATOM   2213  C  CA  . LEU A  1 297 ? -21.15100 -42.99000 -9.32000  1.000 33.82000  ? 328 LEU A CA  1 
ATOM   2214  C  C   . LEU A  1 297 ? -19.64300 -42.86600 -9.34600  1.000 32.47000  ? 328 LEU A C   1 
ATOM   2215  O  O   . LEU A  1 297 ? -19.08200 -41.77400 -9.46000  1.000 32.20000  ? 328 LEU A O   1 
ATOM   2216  C  CB  . LEU A  1 297 ? -21.62700 -43.44500 -10.71000 1.000 29.93000  ? 328 LEU A CB  1 
ATOM   2217  C  CG  . LEU A  1 297 ? -23.12500 -43.33600 -10.96200 1.000 33.31000  ? 328 LEU A CG  1 
ATOM   2218  C  CD1 . LEU A  1 297 ? -23.50300 -43.88000 -12.33400 1.000 36.45000  ? 328 LEU A CD1 1 
ATOM   2219  C  CD2 . LEU A  1 297 ? -23.81000 -44.12900 -9.83800  1.000 38.88000  ? 328 LEU A CD2 1 
ATOM   2220  N  N   . LYS A  1 298 ? -18.99000 -44.01300 -9.26300  1.000 31.10000  ? 329 LYS A N   1 
ATOM   2221  C  CA  . LYS A  1 298 ? -17.53900 -44.07700 -9.39200  1.000 38.52000  ? 329 LYS A CA  1 
ATOM   2222  C  C   . LYS A  1 298 ? -17.17300 -44.27700 -10.85900 1.000 36.74000  ? 329 LYS A C   1 
ATOM   2223  O  O   . LYS A  1 298 ? -17.85400 -45.00800 -11.58400 1.000 34.82000  ? 329 LYS A O   1 
ATOM   2224  C  CB  . LYS A  1 298 ? -16.96900 -45.21700 -8.54000  1.000 31.90000  ? 329 LYS A CB  1 
ATOM   2225  C  CG  . LYS A  1 298 ? -15.45900 -45.46200 -8.72700  1.000 42.67000  ? 329 LYS A CG  1 
ATOM   2226  C  CD  . LYS A  1 298 ? -14.98200 -46.61600 -7.88100  1.000 39.35000  ? 329 LYS A CD  1 
ATOM   2227  C  CE  . LYS A  1 298 ? -14.62000 -46.16200 -6.47200  1.000 37.86000  ? 329 LYS A CE  1 
ATOM   2228  N  NZ  . LYS A  1 298 ? -14.03900 -47.29200 -5.70300  1.000 42.40000  ? 329 LYS A NZ  1 
ATOM   2229  N  N   . GLY A  1 299 ? -16.09800 -43.62400 -11.29100 1.000 38.73000  ? 330 GLY A N   1 
ATOM   2230  C  CA  . GLY A  1 299 ? -15.55300 -43.89500 -12.60800 1.000 37.08000  ? 330 GLY A CA  1 
ATOM   2231  C  C   . GLY A  1 299 ? -16.13200 -43.06500 -13.74200 1.000 40.86000  ? 330 GLY A C   1 
ATOM   2232  O  O   . GLY A  1 299 ? -16.84100 -42.06500 -13.57200 1.000 36.11000  ? 330 GLY A O   1 
ATOM   2233  N  N   . THR A  1 300 ? -15.81100 -43.52800 -14.94500 1.000 36.37000  ? 331 THR A N   1 
ATOM   2234  C  CA  . THR A  1 300 ? -15.94300 -42.72200 -16.14700 1.000 35.44000  ? 331 THR A CA  1 
ATOM   2235  C  C   . THR A  1 300 ? -16.27800 -43.65300 -17.30300 1.000 35.64000  ? 331 THR A C   1 
ATOM   2236  O  O   . THR A  1 300 ? -16.13500 -44.87600 -17.19800 1.000 35.32000  ? 331 THR A O   1 
ATOM   2237  C  CB  . THR A  1 300 ? -14.63700 -41.94700 -16.41700 1.000 33.31000  ? 331 THR A CB  1 
ATOM   2238  O  OG1 . THR A  1 300 ? -14.78400 -41.02500 -17.50700 1.000 32.54000  ? 331 THR A OG1 1 
ATOM   2239  C  CG2 . THR A  1 300 ? -13.49000 -42.91600 -16.71800 1.000 31.81000  ? 331 THR A CG2 1 
ATOM   2240  N  N   . LYS A  1 301 ? -16.67700 -43.04800 -18.42700 1.000 35.69000  ? 332 LYS A N   1 
ATOM   2241  C  CA  . LYS A  1 301 ? -16.91800 -43.77500 -19.66900 1.000 36.80000  ? 332 LYS A CA  1 
ATOM   2242  C  C   . LYS A  1 301 ? -15.86000 -44.85100 -19.89400 1.000 37.15000  ? 332 LYS A C   1 
ATOM   2243  O  O   . LYS A  1 301 ? -14.66200 -44.59800 -19.75800 1.000 33.76000  ? 332 LYS A O   1 
ATOM   2244  C  CB  . LYS A  1 301 ? -16.90600 -42.79700 -20.84400 1.000 39.48000  ? 332 LYS A CB  1 
ATOM   2245  C  CG  . LYS A  1 301 ? -16.77500 -43.47600 -22.22400 1.000 35.80000  ? 332 LYS A CG  1 
ATOM   2246  C  CD  . LYS A  1 301 ? -16.83300 -42.45400 -23.33200 1.000 42.98000  ? 332 LYS A CD  1 
ATOM   2247  C  CE  . LYS A  1 301 ? -16.70200 -43.07400 -24.71600 1.000 38.30000  ? 332 LYS A CE  1 
ATOM   2248  N  NZ  . LYS A  1 301 ? -16.87300 -42.01800 -25.73300 1.000 35.87000  ? 332 LYS A NZ  1 
ATOM   2249  N  N   . GLY A  1 302 ? -16.31300 -46.07000 -20.17100 1.000 38.93000  ? 333 GLY A N   1 
ATOM   2250  C  CA  . GLY A  1 302 ? -15.43200 -47.18100 -20.44000 1.000 32.41000  ? 333 GLY A CA  1 
ATOM   2251  C  C   . GLY A  1 302 ? -15.19000 -48.11800 -19.27400 1.000 37.90000  ? 333 GLY A C   1 
ATOM   2252  O  O   . GLY A  1 302 ? -14.74100 -49.24600 -19.50700 1.000 36.58000  ? 333 GLY A O   1 
ATOM   2253  N  N   . ASP A  1 303 ? -15.51400 -47.71000 -18.03800 1.000 37.89000  ? 334 ASP A N   1 
ATOM   2254  C  CA  . ASP A  1 303 ? -15.25600 -48.51500 -16.84600 1.000 34.72000  ? 334 ASP A CA  1 
ATOM   2255  C  C   . ASP A  1 303 ? -16.40200 -49.50700 -16.62100 1.000 34.28000  ? 334 ASP A C   1 
ATOM   2256  O  O   . ASP A  1 303 ? -17.53200 -49.27700 -17.05600 1.000 35.31000  ? 334 ASP A O   1 
ATOM   2257  C  CB  . ASP A  1 303 ? -15.14200 -47.62900 -15.58800 1.000 38.56000  ? 334 ASP A CB  1 
ATOM   2258  C  CG  . ASP A  1 303 ? -13.92200 -46.70100 -15.60000 1.000 37.88000  ? 334 ASP A CG  1 
ATOM   2259  O  OD1 . ASP A  1 303 ? -12.94400 -46.96600 -16.32200 1.000 38.28000  ? 334 ASP A OD1 1 
ATOM   2260  O  OD2 . ASP A  1 303 ? -13.95300 -45.68100 -14.87900 1.000 33.92000  ? 334 ASP A OD2 1 
ATOM   2261  N  N   . THR A  1 304 ? -16.12500 -50.59900 -15.89100 1.000 34.78000  ? 335 THR A N   1 
ATOM   2262  C  CA  . THR A  1 304 ? -17.23300 -51.40400 -15.37900 1.000 35.66000  ? 335 THR A CA  1 
ATOM   2263  C  C   . THR A  1 304 ? -17.65900 -51.00700 -13.96700 1.000 39.96000  ? 335 THR A C   1 
ATOM   2264  O  O   . THR A  1 304 ? -18.53900 -51.66500 -13.40100 1.000 40.64000  ? 335 THR A O   1 
ATOM   2265  C  CB  . THR A  1 304 ? -16.92600 -52.90700 -15.40500 1.000 37.20000  ? 335 THR A CB  1 
ATOM   2266  O  OG1 . THR A  1 304 ? -15.69300 -53.18200 -14.73800 1.000 35.37000  ? 335 THR A OG1 1 
ATOM   2267  C  CG2 . THR A  1 304 ? -16.84300 -53.42200 -16.83000 1.000 39.39000  ? 335 THR A CG2 1 
ATOM   2268  N  N   . TRP A  1 305 ? -17.06900 -49.96100 -13.38200 1.000 33.75000  ? 336 TRP A N   1 
ATOM   2269  C  CA  . TRP A  1 305 ? -17.76700 -49.26500 -12.31200 1.000 36.01000  ? 336 TRP A CA  1 
ATOM   2270  C  C   . TRP A  1 305 ? -19.11300 -48.76500 -12.83000 1.000 35.65000  ? 336 TRP A C   1 
ATOM   2271  O  O   . TRP A  1 305 ? -19.32400 -48.60800 -14.04100 1.000 38.09000  ? 336 TRP A O   1 
ATOM   2272  C  CB  . TRP A  1 305 ? -16.98800 -48.04800 -11.82600 1.000 31.76000  ? 336 TRP A CB  1 
ATOM   2273  C  CG  . TRP A  1 305 ? -15.56300 -48.27500 -11.35300 1.000 39.18000  ? 336 TRP A CG  1 
ATOM   2274  C  CD1 . TRP A  1 305 ? -14.42700 -47.75000 -11.90400 1.000 32.78000  ? 336 TRP A CD1 1 
ATOM   2275  C  CD2 . TRP A  1 305 ? -15.14100 -49.03400 -10.21800 1.000 36.51000  ? 336 TRP A CD2 1 
ATOM   2276  N  NE1 . TRP A  1 305 ? -13.33800 -48.14500 -11.20200 1.000 39.88000  ? 336 TRP A NE1 1 
ATOM   2277  C  CE2 . TRP A  1 305 ? -13.73500 -48.93800 -10.15800 1.000 42.73000  ? 336 TRP A CE2 1 
ATOM   2278  C  CE3 . TRP A  1 305 ? -15.81200 -49.77900 -9.24300  1.000 36.28000  ? 336 TRP A CE3 1 
ATOM   2279  C  CZ2 . TRP A  1 305 ? -12.97200 -49.55900 -9.15100  1.000 42.92000  ? 336 TRP A CZ2 1 
ATOM   2280  C  CZ3 . TRP A  1 305 ? -15.06000 -50.41100 -8.24800  1.000 38.86000  ? 336 TRP A CZ3 1 
ATOM   2281  C  CH2 . TRP A  1 305 ? -13.64600 -50.29100 -8.20900  1.000 40.95000  ? 336 TRP A CH2 1 
ATOM   2282  N  N   . GLU A  1 306 ? -20.01600 -48.46400 -11.89700 1.000 37.58000  ? 337 GLU A N   1 
ATOM   2283  C  CA  . GLU A  1 306 ? -21.31700 -47.90300 -12.27500 1.000 34.86000  ? 337 GLU A CA  1 
ATOM   2284  C  C   . GLU A  1 306 ? -21.16300 -46.70400 -13.21000 1.000 34.54000  ? 337 GLU A C   1 
ATOM   2285  O  O   . GLU A  1 306 ? -21.97900 -46.51300 -14.11900 1.000 38.10000  ? 337 GLU A O   1 
ATOM   2286  C  CB  . GLU A  1 306 ? -22.10600 -47.49800 -11.02300 1.000 32.49000  ? 337 GLU A CB  1 
ATOM   2287  C  CG  . GLU A  1 306 ? -22.42900 -48.63800 -10.07700 1.000 36.56000  ? 337 GLU A CG  1 
ATOM   2288  C  CD  . GLU A  1 306 ? -23.40900 -49.63500 -10.66000 1.000 42.86000  ? 337 GLU A CD  1 
ATOM   2289  O  OE1 . GLU A  1 306 ? -24.63300 -49.40600 -10.53900 1.000 38.88000  ? 337 GLU A OE1 1 
ATOM   2290  O  OE2 . GLU A  1 306 ? -22.95000 -50.64500 -11.24400 1.000 45.07000  ? 337 GLU A OE2 1 
ATOM   2291  N  N   . GLY A  1 307 ? -20.11200 -45.89600 -13.01600 1.000 33.23000  ? 338 GLY A N   1 
ATOM   2292  C  CA  . GLY A  1 307 ? -19.93600 -44.68300 -13.80600 1.000 34.29000  ? 338 GLY A CA  1 
ATOM   2293  C  C   . GLY A  1 307 ? -19.78300 -44.91800 -15.29800 1.000 35.99000  ? 338 GLY A C   1 
ATOM   2294  O  O   . GLY A  1 307 ? -20.12600 -44.03100 -16.09300 1.000 36.32000  ? 338 GLY A O   1 
ATOM   2295  N  N   . GLY A  1 308 ? -19.31900 -46.10300 -15.69800 1.000 33.03000  ? 339 GLY A N   1 
ATOM   2296  C  CA  . GLY A  1 308 ? -19.18300 -46.43100 -17.10500 1.000 34.88000  ? 339 GLY A CA  1 
ATOM   2297  C  C   . GLY A  1 308 ? -20.49900 -46.74200 -17.81400 1.000 38.62000  ? 339 GLY A C   1 
ATOM   2298  O  O   . GLY A  1 308 ? -20.66200 -46.37200 -18.98200 1.000 35.11000  ? 339 GLY A O   1 
ATOM   2299  N  N   . TYR A  1 309 ? -21.45600 -47.43600 -17.16600 1.000 35.89000  ? 340 TYR A N   1 
ATOM   2300  C  CA  . TYR A  1 309 ? -22.60700 -47.88100 -17.95100 1.000 33.87000  ? 340 TYR A CA  1 
ATOM   2301  C  C   . TYR A  1 309 ? -23.97800 -47.72600 -17.28700 1.000 36.97000  ? 340 TYR A C   1 
ATOM   2302  O  O   . TYR A  1 309 ? -24.97000 -48.21500 -17.84500 1.000 44.77000  ? 340 TYR A O   1 
ATOM   2303  C  CB  . TYR A  1 309 ? -22.42300 -49.32200 -18.39400 1.000 32.87000  ? 340 TYR A CB  1 
ATOM   2304  C  CG  . TYR A  1 309 ? -22.33100 -50.34100 -17.29700 1.000 39.03000  ? 340 TYR A CG  1 
ATOM   2305  C  CD1 . TYR A  1 309 ? -21.19200 -50.44200 -16.50100 1.000 35.38000  ? 340 TYR A CD1 1 
ATOM   2306  C  CD2 . TYR A  1 309 ? -23.34800 -51.26800 -17.10700 1.000 38.38000  ? 340 TYR A CD2 1 
ATOM   2307  C  CE1 . TYR A  1 309 ? -21.09700 -51.40500 -15.52000 1.000 39.66000  ? 340 TYR A CE1 1 
ATOM   2308  C  CE2 . TYR A  1 309 ? -23.25700 -52.24300 -16.10800 1.000 35.66000  ? 340 TYR A CE2 1 
ATOM   2309  C  CZ  . TYR A  1 309 ? -22.12900 -52.30700 -15.32400 1.000 39.73000  ? 340 TYR A CZ  1 
ATOM   2310  O  OH  . TYR A  1 309 ? -22.02100 -53.27300 -14.33000 1.000 43.80000  ? 340 TYR A OH  1 
ATOM   2311  N  N   . ARG A  1 310 ? -24.07600 -47.05900 -16.14500 1.000 38.81000  ? 341 ARG A N   1 
ATOM   2312  C  CA  . ARG A  1 310 ? -25.34800 -46.68100 -15.55400 1.000 37.47000  ? 341 ARG A CA  1 
ATOM   2313  C  C   . ARG A  1 310 ? -25.67800 -45.26600 -16.01200 1.000 40.69000  ? 341 ARG A C   1 
ATOM   2314  O  O   . ARG A  1 310 ? -24.85700 -44.35500 -15.85600 1.000 34.63000  ? 341 ARG A O   1 
ATOM   2315  C  CB  . ARG A  1 310 ? -25.27400 -46.77700 -14.02900 1.000 39.72000  ? 341 ARG A CB  1 
ATOM   2316  C  CG  . ARG A  1 310 ? -26.61500 -46.62800 -13.27000 1.000 38.14000  ? 341 ARG A CG  1 
ATOM   2317  C  CD  . ARG A  1 310 ? -26.37800 -46.88900 -11.76600 1.000 37.78000  ? 341 ARG A CD  1 
ATOM   2318  N  NE  . ARG A  1 310 ? -27.50100 -46.49500 -10.93500 1.000 39.74000  ? 341 ARG A NE  1 
ATOM   2319  C  CZ  . ARG A  1 310 ? -27.71600 -46.94600 -9.70500  1.000 44.11000  ? 341 ARG A CZ  1 
ATOM   2320  N  NH1 . ARG A  1 310 ? -26.91500 -47.84200 -9.14100  1.000 44.24000  ? 341 ARG A NH1 1 
ATOM   2321  N  NH2 . ARG A  1 310 ? -28.74200 -46.46700 -9.01000  1.000 38.29000  ? 341 ARG A NH2 1 
ATOM   2322  N  N   . VAL A  1 311 ? -26.85400 -45.09300 -16.61500 1.000 38.57000  ? 342 VAL A N   1 
ATOM   2323  C  CA  . VAL A  1 311 ? -27.15800 -43.85800 -17.33400 1.000 33.51000  ? 342 VAL A CA  1 
ATOM   2324  C  C   . VAL A  1 311 ? -28.49700 -43.30800 -16.86900 1.000 38.62000  ? 342 VAL A C   1 
ATOM   2325  O  O   . VAL A  1 311 ? -29.36000 -44.04300 -16.36400 1.000 35.22000  ? 342 VAL A O   1 
ATOM   2326  C  CB  . VAL A  1 311 ? -27.15500 -44.07500 -18.86400 1.000 38.94000  ? 342 VAL A CB  1 
ATOM   2327  C  CG1 . VAL A  1 311 ? -25.75100 -44.52000 -19.33900 1.000 30.07000  ? 342 VAL A CG1 1 
ATOM   2328  C  CG2 . VAL A  1 311 ? -28.25700 -45.07100 -19.27700 1.000 27.43000  ? 342 VAL A CG2 1 
ATOM   2329  N  N   . PRO A  1 312 ? -28.71700 -42.01600 -17.06800 1.000 37.43000  ? 343 PRO A N   1 
ATOM   2330  C  CA  . PRO A  1 312 ? -30.05300 -41.46000 -16.84600 1.000 37.30000  ? 343 PRO A CA  1 
ATOM   2331  C  C   . PRO A  1 312 ? -31.02000 -42.01200 -17.87200 1.000 41.42000  ? 343 PRO A C   1 
ATOM   2332  O  O   . PRO A  1 312 ? -30.65200 -42.25100 -19.02500 1.000 41.39000  ? 343 PRO A O   1 
ATOM   2333  C  CB  . PRO A  1 312 ? -29.85300 -39.95100 -17.05400 1.000 37.54000  ? 343 PRO A CB  1 
ATOM   2334  C  CG  . PRO A  1 312 ? -28.32200 -39.73600 -17.06500 1.000 36.71000  ? 343 PRO A CG  1 
ATOM   2335  C  CD  . PRO A  1 312 ? -27.77700 -41.01100 -17.60100 1.000 35.36000  ? 343 PRO A CD  1 
ATOM   2336  N  N   . MET A  1 313 ? -32.28300 -42.17300 -17.46500 1.000 40.71000  ? 344 MET A N   1 
ATOM   2337  C  CA  . MET A  1 313 ? -33.29400 -42.65000 -18.39600 1.000 34.49000  ? 344 MET A CA  1 
ATOM   2338  C  C   . MET A  1 313 ? -34.69500 -42.37200 -17.87400 1.000 42.30000  ? 344 MET A C   1 
ATOM   2339  O  O   . MET A  1 313 ? -34.97000 -42.57400 -16.69300 1.000 43.63000  ? 344 MET A O   1 
ATOM   2340  C  CB  . MET A  1 313 ? -33.15400 -44.15000 -18.67500 1.000 38.80000  ? 344 MET A CB  1 
ATOM   2341  C  CG  . MET A  1 313 ? -34.20300 -44.63300 -19.69000 1.000 41.38000  ? 344 MET A CG  1 
ATOM   2342  S  SD  . MET A  1 313 ? -33.98200 -46.28800 -20.38400 1.000 47.09000  ? 344 MET A SD  1 
ATOM   2343  C  CE  . MET A  1 313 ? -34.53500 -47.26800 -18.97700 1.000 45.61000  ? 344 MET A CE  1 
ATOM   2344  N  N   . PHE A  1 314 ? -35.59300 -41.95100 -18.77100 1.000 44.23000  ? 345 PHE A N   1 
ATOM   2345  C  CA  . PHE A  1 314 ? -37.00700 -41.92100 -18.43400 1.000 47.35000  ? 345 PHE A CA  1 
ATOM   2346  C  C   . PHE A  1 314 ? -37.85100 -42.39200 -19.60600 1.000 43.91000  ? 345 PHE A C   1 
ATOM   2347  O  O   . PHE A  1 314 ? -37.44200 -42.29200 -20.76400 1.000 45.60000  ? 345 PHE A O   1 
ATOM   2348  C  CB  . PHE A  1 314 ? -37.45300 -40.53900 -17.94900 1.000 38.63000  ? 345 PHE A CB  1 
ATOM   2349  C  CG  . PHE A  1 314 ? -37.37900 -39.46000 -18.96800 1.000 40.36000  ? 345 PHE A CG  1 
ATOM   2350  C  CD1 . PHE A  1 314 ? -38.31300 -39.37300 -19.99600 1.000 35.94000  ? 345 PHE A CD1 1 
ATOM   2351  C  CD2 . PHE A  1 314 ? -36.42600 -38.45900 -18.84100 1.000 35.71000  ? 345 PHE A CD2 1 
ATOM   2352  C  CE1 . PHE A  1 314 ? -38.25900 -38.33900 -20.91400 1.000 37.37000  ? 345 PHE A CE1 1 
ATOM   2353  C  CE2 . PHE A  1 314 ? -36.38100 -37.41200 -19.74200 1.000 36.75000  ? 345 PHE A CE2 1 
ATOM   2354  C  CZ  . PHE A  1 314 ? -37.29900 -37.35900 -20.79800 1.000 37.98000  ? 345 PHE A CZ  1 
ATOM   2355  N  N   . PHE A  1 315 ? -39.02900 -42.92400 -19.26900 1.000 44.00000  ? 346 PHE A N   1 
ATOM   2356  C  CA  . PHE A  1 315 ? -40.13200 -43.19000 -20.18700 1.000 41.23000  ? 346 PHE A CA  1 
ATOM   2357  C  C   . PHE A  1 315 ? -41.19500 -42.12700 -19.95500 1.000 44.11000  ? 346 PHE A C   1 
ATOM   2358  O  O   . PHE A  1 315 ? -41.52900 -41.82000 -18.80700 1.000 47.98000  ? 346 PHE A O   1 
ATOM   2359  C  CB  . PHE A  1 315 ? -40.78100 -44.55700 -19.93100 1.000 40.84000  ? 346 PHE A CB  1 
ATOM   2360  C  CG  . PHE A  1 315 ? -39.99000 -45.73100 -20.41200 1.000 45.37000  ? 346 PHE A CG  1 
ATOM   2361  C  CD1 . PHE A  1 315 ? -38.63900 -45.61800 -20.72900 1.000 46.09000  ? 346 PHE A CD1 1 
ATOM   2362  C  CD2 . PHE A  1 315 ? -40.59900 -46.96800 -20.53000 1.000 42.83000  ? 346 PHE A CD2 1 
ATOM   2363  C  CE1 . PHE A  1 315 ? -37.92700 -46.72800 -21.17100 1.000 43.91000  ? 346 PHE A CE1 1 
ATOM   2364  C  CE2 . PHE A  1 315 ? -39.88000 -48.09200 -20.96400 1.000 41.69000  ? 346 PHE A CE2 1 
ATOM   2365  C  CZ  . PHE A  1 315 ? -38.55000 -47.96700 -21.28600 1.000 38.11000  ? 346 PHE A CZ  1 
ATOM   2366  N  N   . HIS A  1 316 ? -41.73900 -41.57200 -21.03300 1.000 44.41000  ? 347 HIS A N   1 
ATOM   2367  C  CA  . HIS A  1 316 ? -42.79600 -40.56800 -20.93100 1.000 44.93000  ? 347 HIS A CA  1 
ATOM   2368  C  C   . HIS A  1 316 ? -43.88300 -40.91000 -21.93500 1.000 46.44000  ? 347 HIS A C   1 
ATOM   2369  O  O   . HIS A  1 316 ? -43.62400 -40.91500 -23.14000 1.000 49.65000  ? 347 HIS A O   1 
ATOM   2370  C  CB  . HIS A  1 316 ? -42.25700 -39.16200 -21.18400 1.000 39.28000  ? 347 HIS A CB  1 
ATOM   2371  C  CG  . HIS A  1 316 ? -43.32000 -38.11400 -21.28800 1.000 44.75000  ? 347 HIS A CG  1 
ATOM   2372  N  ND1 . HIS A  1 316 ? -44.14800 -37.99300 -22.38300 1.000 46.49000  ? 347 HIS A ND1 1 
ATOM   2373  C  CD2 . HIS A  1 316 ? -43.67000 -37.11500 -20.44100 1.000 47.39000  ? 347 HIS A CD2 1 
ATOM   2374  C  CE1 . HIS A  1 316 ? -44.95800 -36.96200 -22.21100 1.000 46.06000  ? 347 HIS A CE1 1 
ATOM   2375  N  NE2 . HIS A  1 316 ? -44.69800 -36.41800 -21.03400 1.000 49.35000  ? 347 HIS A NE2 1 
ATOM   2376  N  N   . TRP A  1 317 ? -45.09600 -41.19900 -21.44400 1.000 44.74000  ? 348 TRP A N   1 
ATOM   2377  C  CA  . TRP A  1 317 ? -46.16500 -41.68500 -22.30700 1.000 40.98000  ? 348 TRP A CA  1 
ATOM   2378  C  C   . TRP A  1 317 ? -47.50200 -41.38000 -21.64300 1.000 41.86000  ? 348 TRP A C   1 
ATOM   2379  O  O   . TRP A  1 317 ? -48.08900 -42.25400 -20.99200 1.000 41.44000  ? 348 TRP A O   1 
ATOM   2380  C  CB  . TRP A  1 317 ? -45.99800 -43.18300 -22.51600 1.000 37.36000  ? 348 TRP A CB  1 
ATOM   2381  C  CG  . TRP A  1 317 ? -46.94400 -43.80300 -23.49000 1.000 46.23000  ? 348 TRP A CG  1 
ATOM   2382  C  CD1 . TRP A  1 317 ? -47.72500 -43.16600 -24.42800 1.000 39.34000  ? 348 TRP A CD1 1 
ATOM   2383  C  CD2 . TRP A  1 317 ? -47.23700 -45.19500 -23.60500 1.000 44.14000  ? 348 TRP A CD2 1 
ATOM   2384  N  NE1 . TRP A  1 317 ? -48.45200 -44.08900 -25.12600 1.000 40.53000  ? 348 TRP A NE1 1 
ATOM   2385  C  CE2 . TRP A  1 317 ? -48.18200 -45.33900 -24.63600 1.000 39.07000  ? 348 TRP A CE2 1 
ATOM   2386  C  CE3 . TRP A  1 317 ? -46.77600 -46.33700 -22.94300 1.000 41.77000  ? 348 TRP A CE3 1 
ATOM   2387  C  CZ2 . TRP A  1 317 ? -48.67300 -46.57000 -25.02200 1.000 45.53000  ? 348 TRP A CZ2 1 
ATOM   2388  C  CZ3 . TRP A  1 317 ? -47.26200 -47.56500 -23.33000 1.000 40.08000  ? 348 TRP A CZ3 1 
ATOM   2389  C  CH2 . TRP A  1 317 ? -48.20500 -47.67300 -24.35800 1.000 45.31000  ? 348 TRP A CH2 1 
ATOM   2390  N  N   . PRO A  1 318 ? -48.02500 -40.17500 -21.81100 1.000 40.08000  ? 349 PRO A N   1 
ATOM   2391  C  CA  . PRO A  1 318 ? -49.14700 -39.74500 -20.96300 1.000 44.21000  ? 349 PRO A CA  1 
ATOM   2392  C  C   . PRO A  1 318 ? -50.32800 -40.69500 -20.94600 1.000 48.40000  ? 349 PRO A C   1 
ATOM   2393  O  O   . PRO A  1 318 ? -50.92500 -40.87600 -19.87400 1.000 47.24000  ? 349 PRO A O   1 
ATOM   2394  C  CB  . PRO A  1 318 ? -49.50300 -38.37400 -21.54600 1.000 52.22000  ? 349 PRO A CB  1 
ATOM   2395  C  CG  . PRO A  1 318 ? -48.14000 -37.85900 -22.08000 1.000 44.94000  ? 349 PRO A CG  1 
ATOM   2396  C  CD  . PRO A  1 318 ? -47.50400 -39.08700 -22.66000 1.000 43.22000  ? 349 PRO A CD  1 
ATOM   2397  N  N   . LYS A  1 319 ? -50.62800 -41.37700 -22.06000 1.000 47.72000  ? 350 LYS A N   1 
ATOM   2398  C  CA  . LYS A  1 319 ? -51.80300 -42.24900 -22.10700 1.000 51.99000  ? 350 LYS A CA  1 
ATOM   2399  C  C   . LYS A  1 319 ? -51.74000 -43.37900 -21.08600 1.000 54.75000  ? 350 LYS A C   1 
ATOM   2400  O  O   . LYS A  1 319 ? -52.78700 -43.83500 -20.61100 1.000 52.48000  ? 350 LYS A O   1 
ATOM   2401  C  CB  . LYS A  1 319 ? -51.95500 -42.86600 -23.49800 1.000 49.96000  ? 350 LYS A CB  1 
ATOM   2402  C  CG  . LYS A  1 319 ? -53.22700 -43.69100 -23.67900 1.000 50.67000  ? 350 LYS A CG  1 
ATOM   2403  C  CD  . LYS A  1 319 ? -53.32500 -44.27600 -25.09100 1.000 51.00000  ? 350 LYS A CD  1 
ATOM   2404  C  CE  . LYS A  1 319 ? -52.46400 -45.52000 -25.24200 1.000 58.92000  ? 350 LYS A CE  1 
ATOM   2405  N  NZ  . LYS A  1 319 ? -52.40800 -46.09500 -26.62400 1.000 56.88000  ? 350 LYS A NZ  1 
ATOM   2406  N  N   . LYS A  1 320 ? -50.54300 -43.80400 -20.68400 1.000 46.46000  ? 351 LYS A N   1 
ATOM   2407  C  CA  . LYS A  1 320 ? -50.47300 -44.99100 -19.83700 1.000 49.15000  ? 351 LYS A CA  1 
ATOM   2408  C  C   . LYS A  1 320 ? -49.55300 -44.84600 -18.62600 1.000 50.29000  ? 351 LYS A C   1 
ATOM   2409  O  O   . LYS A  1 320 ? -49.83400 -45.43400 -17.58200 1.000 51.82000  ? 351 LYS A O   1 
ATOM   2410  C  CB  . LYS A  1 320 ? -50.03500 -46.21500 -20.65400 1.000 46.71000  ? 351 LYS A CB  1 
ATOM   2411  C  CG  . LYS A  1 320 ? -51.15500 -46.88600 -21.42600 1.000 55.76000  ? 351 LYS A CG  1 
ATOM   2412  C  CD  . LYS A  1 320 ? -50.85200 -48.35400 -21.75200 1.000 54.94000  ? 351 LYS A CD  1 
ATOM   2413  C  CE  . LYS A  1 320 ? -51.76100 -48.87300 -22.88700 1.000 59.35000  ? 351 LYS A CE  1 
ATOM   2414  N  NZ  . LYS A  1 320 ? -51.32300 -50.20800 -23.46000 1.000 62.54000  ? 351 LYS A NZ  1 
ATOM   2415  N  N   . ILE A  1 321 ? -48.46900 -44.07800 -18.73100 1.000 47.62000  ? 352 ILE A N   1 
ATOM   2416  C  CA  . ILE A  1 321 ? -47.48500 -43.98100 -17.65800 1.000 39.24000  ? 352 ILE A CA  1 
ATOM   2417  C  C   . ILE A  1 321 ? -47.84600 -42.81800 -16.74300 1.000 46.96000  ? 352 ILE A C   1 
ATOM   2418  O  O   . ILE A  1 321 ? -47.97300 -41.67400 -17.19200 1.000 45.34000  ? 352 ILE A O   1 
ATOM   2419  C  CB  . ILE A  1 321 ? -46.06900 -43.85000 -18.23100 1.000 39.92000  ? 352 ILE A CB  1 
ATOM   2420  C  CG1 . ILE A  1 321 ? -45.67300 -45.20500 -18.81300 1.000 43.50000  ? 352 ILE A CG1 1 
ATOM   2421  C  CG2 . ILE A  1 321 ? -45.05000 -43.39800 -17.14500 1.000 44.19000  ? 352 ILE A CG2 1 
ATOM   2422  C  CD1 . ILE A  1 321 ? -44.46200 -45.16100 -19.70700 1.000 46.19000  ? 352 ILE A CD1 1 
ATOM   2423  N  N   . LYS A  1 322 ? -47.98800 -43.11100 -15.45000 1.000 45.68000  ? 353 LYS A N   1 
ATOM   2424  C  CA  . LYS A  1 322 ? -48.40800 -42.10300 -14.48300 1.000 45.23000  ? 353 LYS A CA  1 
ATOM   2425  C  C   . LYS A  1 322 ? -47.32700 -41.05300 -14.25900 1.000 55.41000  ? 353 LYS A C   1 
ATOM   2426  O  O   . LYS A  1 322 ? -46.12600 -41.30300 -14.43700 1.000 48.59000  ? 353 LYS A O   1 
ATOM   2427  C  CB  . LYS A  1 322 ? -48.76300 -42.76500 -13.14700 1.000 53.65000  ? 353 LYS A CB  1 
ATOM   2428  N  N   . LYS A  1 323 ? -47.76200 -39.86900 -13.83900 1.000 49.27000  ? 354 LYS A N   1 
ATOM   2429  C  CA  . LYS A  1 323 ? -46.81400 -38.79700 -13.58900 1.000 52.01000  ? 354 LYS A CA  1 
ATOM   2430  C  C   . LYS A  1 323 ? -46.07000 -39.03700 -12.26600 1.000 49.97000  ? 354 LYS A C   1 
ATOM   2431  O  O   . LYS A  1 323 ? -46.52400 -39.78600 -11.40500 1.000 51.52000  ? 354 LYS A O   1 
ATOM   2432  C  CB  . LYS A  1 323 ? -47.55200 -37.45800 -13.59300 1.000 51.96000  ? 354 LYS A CB  1 
ATOM   2433  N  N   . ASP A  1 324 ? -44.89400 -38.40400 -12.12600 1.000 49.20000  ? 355 ASP A N   1 
ATOM   2434  C  CA  . ASP A  1 324 ? -44.07000 -38.46000 -10.90600 1.000 48.51000  ? 355 ASP A CA  1 
ATOM   2435  C  C   . ASP A  1 324 ? -43.67000 -39.87500 -10.49800 1.000 45.54000  ? 355 ASP A C   1 
ATOM   2436  O  O   . ASP A  1 324 ? -43.41400 -40.14900 -9.33000  1.000 47.80000  ? 355 ASP A O   1 
ATOM   2437  C  CB  . ASP A  1 324 ? -44.73700 -37.74400 -9.73300  1.000 56.24000  ? 355 ASP A CB  1 
ATOM   2438  C  CG  . ASP A  1 324 ? -44.70500 -36.24400 -9.89200  1.000 68.65000  ? 355 ASP A CG  1 
ATOM   2439  O  OD1 . ASP A  1 324 ? -43.63700 -35.64700 -9.59800  1.000 80.14000  ? 355 ASP A OD1 1 
ATOM   2440  O  OD2 . ASP A  1 324 ? -45.71100 -35.66100 -10.34300 1.000 64.91000  ? 355 ASP A OD2 1 
ATOM   2441  N  N   . GLN A  1 325 ? -43.58300 -40.79500 -11.43600 1.000 44.22000  ? 356 GLN A N   1 
ATOM   2442  C  CA  . GLN A  1 325 ? -43.15600 -42.13100 -11.07200 1.000 46.99000  ? 356 GLN A CA  1 
ATOM   2443  C  C   . GLN A  1 325 ? -41.62500 -42.21800 -11.01000 1.000 51.69000  ? 356 GLN A C   1 
ATOM   2444  O  O   . GLN A  1 325 ? -40.91300 -41.54000 -11.76500 1.000 41.83000  ? 356 GLN A O   1 
ATOM   2445  C  CB  . GLN A  1 325 ? -43.71600 -43.12700 -12.07600 1.000 45.86000  ? 356 GLN A CB  1 
ATOM   2446  C  CG  . GLN A  1 325 ? -43.17800 -44.52700 -11.94800 1.000 52.44000  ? 356 GLN A CG  1 
ATOM   2447  C  CD  . GLN A  1 325 ? -43.90700 -45.46500 -12.87800 1.000 58.32000  ? 356 GLN A CD  1 
ATOM   2448  O  OE1 . GLN A  1 325 ? -43.39100 -46.51800 -13.26700 1.000 57.84000  ? 356 GLN A OE1 1 
ATOM   2449  N  NE2 . GLN A  1 325 ? -45.13000 -45.08500 -13.24300 1.000 67.39000  ? 356 GLN A NE2 1 
ATOM   2450  N  N   . ARG A  1 326 ? -41.12900 -43.02300 -10.05800 1.000 46.87000  ? 357 ARG A N   1 
ATOM   2451  C  CA  . ARG A  1 326 ? -39.72200 -43.41000 -9.96400  1.000 42.08000  ? 357 ARG A CA  1 
ATOM   2452  C  C   . ARG A  1 326 ? -39.65000 -44.93300 -9.97500  1.000 41.57000  ? 357 ARG A C   1 
ATOM   2453  O  O   . ARG A  1 326 ? -40.17700 -45.58300 -9.07200  1.000 53.21000  ? 357 ARG A O   1 
ATOM   2454  C  CB  . ARG A  1 326 ? -39.05700 -42.85100 -8.69600  1.000 43.13000  ? 357 ARG A CB  1 
ATOM   2455  C  CG  . ARG A  1 326 ? -38.98900 -41.33700 -8.63000  1.000 45.33000  ? 357 ARG A CG  1 
ATOM   2456  C  CD  . ARG A  1 326 ? -38.26100 -40.83500 -7.38700  1.000 46.36000  ? 357 ARG A CD  1 
ATOM   2457  N  NE  . ARG A  1 326 ? -36.80900 -40.98100 -7.47300  1.000 56.79000  ? 357 ARG A NE  1 
ATOM   2458  C  CZ  . ARG A  1 326 ? -35.98900 -40.10200 -8.03700  1.000 52.75000  ? 357 ARG A CZ  1 
ATOM   2459  N  NH1 . ARG A  1 326 ? -36.44400 -39.00000 -8.61900  1.000 47.28000  ? 357 ARG A NH1 1 
ATOM   2460  N  NH2 . ARG A  1 326 ? -34.68200 -40.34700 -8.03800  1.000 50.91000  ? 357 ARG A NH2 1 
ATOM   2461  N  N   . PHE A  1 327 ? -39.00600 -45.50000 -10.98300 1.000 42.00000  ? 358 PHE A N   1 
ATOM   2462  C  CA  . PHE A  1 327 ? -38.83500 -46.94900 -11.11800 1.000 46.42000  ? 358 PHE A CA  1 
ATOM   2463  C  C   . PHE A  1 327 ? -37.42400 -47.31500 -10.64500 1.000 51.41000  ? 358 PHE A C   1 
ATOM   2464  O  O   . PHE A  1 327 ? -36.43300 -46.88900 -11.25500 1.000 45.28000  ? 358 PHE A O   1 
ATOM   2465  C  CB  . PHE A  1 327 ? -39.05500 -47.37600 -12.56600 1.000 45.53000  ? 358 PHE A CB  1 
ATOM   2466  C  CG  . PHE A  1 327 ? -39.19700 -48.85700 -12.75100 1.000 45.23000  ? 358 PHE A CG  1 
ATOM   2467  C  CD1 . PHE A  1 327 ? -40.42500 -49.48100 -12.58000 1.000 36.91000  ? 358 PHE A CD1 1 
ATOM   2468  C  CD2 . PHE A  1 327 ? -38.10600 -49.62600 -13.12200 1.000 48.32000  ? 358 PHE A CD2 1 
ATOM   2469  C  CE1 . PHE A  1 327 ? -40.55600 -50.84600 -12.74800 1.000 43.80000  ? 358 PHE A CE1 1 
ATOM   2470  C  CE2 . PHE A  1 327 ? -38.22500 -51.01300 -13.29600 1.000 46.90000  ? 358 PHE A CE2 1 
ATOM   2471  C  CZ  . PHE A  1 327 ? -39.45200 -51.61900 -13.11300 1.000 45.12000  ? 358 PHE A CZ  1 
ATOM   2472  N  N   . ASP A  1 328 ? -37.33600 -48.06100 -9.52900  1.000 52.35000  ? 359 ASP A N   1 
ATOM   2473  C  CA  . ASP A  1 328 ? -36.06900 -48.33000 -8.83700  1.000 47.55000  ? 359 ASP A CA  1 
ATOM   2474  C  C   . ASP A  1 328 ? -35.47500 -49.71600 -9.09000  1.000 46.15000  ? 359 ASP A C   1 
ATOM   2475  O  O   . ASP A  1 328 ? -34.33800 -49.96000 -8.66600  1.000 49.90000  ? 359 ASP A O   1 
ATOM   2476  C  CB  . ASP A  1 328 ? -36.22700 -48.17700 -7.30600  1.000 41.39000  ? 359 ASP A CB  1 
ATOM   2477  C  CG  . ASP A  1 328 ? -36.55400 -46.75000 -6.85900  1.000 52.44000  ? 359 ASP A CG  1 
ATOM   2478  O  OD1 . ASP A  1 328 ? -36.07300 -45.76900 -7.46100  1.000 52.29000  ? 359 ASP A OD1 1 
ATOM   2479  O  OD2 . ASP A  1 328 ? -37.25500 -46.60900 -5.83600  1.000 65.63000  ? 359 ASP A OD2 1 
ATOM   2480  N  N   . PHE A  1 329 ? -36.17400 -50.61300 -9.77900  1.000 42.79000  ? 360 PHE A N   1 
ATOM   2481  C  CA  . PHE A  1 329 ? -35.58100 -51.89900 -10.11200 1.000 42.78000  ? 360 PHE A CA  1 
ATOM   2482  C  C   . PHE A  1 329 ? -34.65100 -51.72500 -11.30800 1.000 48.37000  ? 360 PHE A C   1 
ATOM   2483  O  O   . PHE A  1 329 ? -34.87800 -50.85300 -12.14800 1.000 47.77000  ? 360 PHE A O   1 
ATOM   2484  C  CB  . PHE A  1 329 ? -36.64200 -52.94600 -10.44600 1.000 46.91000  ? 360 PHE A CB  1 
ATOM   2485  C  CG  . PHE A  1 329 ? -37.61600 -53.21200 -9.32300  1.000 57.08000  ? 360 PHE A CG  1 
ATOM   2486  C  CD1 . PHE A  1 329 ? -37.21000 -53.90400 -8.18100  1.000 56.41000  ? 360 PHE A CD1 1 
ATOM   2487  C  CD2 . PHE A  1 329 ? -38.92900 -52.76900 -9.40200  1.000 54.70000  ? 360 PHE A CD2 1 
ATOM   2488  C  CE1 . PHE A  1 329 ? -38.09300 -54.15000 -7.13100  1.000 54.57000  ? 360 PHE A CE1 1 
ATOM   2489  C  CE2 . PHE A  1 329 ? -39.82600 -53.01000 -8.35700  1.000 61.05000  ? 360 PHE A CE2 1 
ATOM   2490  C  CZ  . PHE A  1 329 ? -39.40300 -53.70500 -7.22000  1.000 59.70000  ? 360 PHE A CZ  1 
ATOM   2491  N  N   . PRO A  1 330 ? -33.56800 -52.49900 -11.37000 1.000 47.85000  ? 361 PRO A N   1 
ATOM   2492  C  CA  . PRO A  1 330 ? -32.62000 -52.35200 -12.48500 1.000 45.71000  ? 361 PRO A CA  1 
ATOM   2493  C  C   . PRO A  1 330 ? -33.22000 -52.73700 -13.82200 1.000 48.90000  ? 361 PRO A C   1 
ATOM   2494  O  O   . PRO A  1 330 ? -33.88000 -53.77000 -13.95500 1.000 50.92000  ? 361 PRO A O   1 
ATOM   2495  C  CB  . PRO A  1 330 ? -31.46200 -53.29200 -12.11000 1.000 45.20000  ? 361 PRO A CB  1 
ATOM   2496  C  CG  . PRO A  1 330 ? -31.99800 -54.16700 -11.00300 1.000 51.07000  ? 361 PRO A CG  1 
ATOM   2497  C  CD  . PRO A  1 330 ? -33.00100 -53.30300 -10.27600 1.000 46.71000  ? 361 PRO A CD  1 
ATOM   2498  N  N   . VAL A  1 331 ? -32.97100 -51.89300 -14.82500 1.000 45.01000  ? 362 VAL A N   1 
ATOM   2499  C  CA  . VAL A  1 331 ? -33.35200 -52.18600 -16.19600 1.000 43.57000  ? 362 VAL A CA  1 
ATOM   2500  C  C   . VAL A  1 331 ? -32.11800 -52.06100 -17.08400 1.000 43.46000  ? 362 VAL A C   1 
ATOM   2501  O  O   . VAL A  1 331 ? -31.09300 -51.47300 -16.71000 1.000 39.69000  ? 362 VAL A O   1 
ATOM   2502  C  CB  . VAL A  1 331 ? -34.47600 -51.25900 -16.72200 1.000 43.10000  ? 362 VAL A CB  1 
ATOM   2503  C  CG1 . VAL A  1 331 ? -35.73600 -51.42300 -15.90300 1.000 38.47000  ? 362 VAL A CG1 1 
ATOM   2504  C  CG2 . VAL A  1 331 ? -34.01500 -49.82100 -16.70000 1.000 33.01000  ? 362 VAL A CG2 1 
ATOM   2505  N  N   . SER A  1 332 ? -32.25800 -52.59600 -18.29200 1.000 41.76000  ? 363 SER A N   1 
ATOM   2506  C  CA  . SER A  1 332 ? -31.22700 -52.59100 -19.31300 1.000 38.98000  ? 363 SER A CA  1 
ATOM   2507  C  C   . SER A  1 332 ? -31.77400 -51.98400 -20.58800 1.000 39.20000  ? 363 SER A C   1 
ATOM   2508  O  O   . SER A  1 332 ? -32.93800 -52.18500 -20.93900 1.000 40.00000  ? 363 SER A O   1 
ATOM   2509  C  CB  . SER A  1 332 ? -30.73900 -53.99000 -19.62800 1.000 36.65000  ? 363 SER A CB  1 
ATOM   2510  O  OG  . SER A  1 332 ? -29.97000 -53.95700 -20.80100 1.000 43.55000  ? 363 SER A OG  1 
ATOM   2511  N  N   . SER A  1 333 ? -30.89200 -51.29300 -21.30500 1.000 37.74000  ? 364 SER A N   1 
ATOM   2512  C  CA  . SER A  1 333 ? -31.20000 -50.78700 -22.63400 1.000 31.28000  ? 364 SER A CA  1 
ATOM   2513  C  C   . SER A  1 333 ? -31.51800 -51.91500 -23.60300 1.000 36.39000  ? 364 SER A C   1 
ATOM   2514  O  O   . SER A  1 333 ? -32.16200 -51.67800 -24.63400 1.000 38.16000  ? 364 SER A O   1 
ATOM   2515  C  CB  . SER A  1 333 ? -30.02000 -49.95600 -23.12900 1.000 37.68000  ? 364 SER A CB  1 
ATOM   2516  O  OG  . SER A  1 333 ? -28.82800 -50.72800 -23.06100 1.000 36.91000  ? 364 SER A OG  1 
ATOM   2517  N  N   . LEU A  1 334 ? -31.07500 -53.13900 -23.29900 1.000 36.76000  ? 365 LEU A N   1 
ATOM   2518  C  CA  . LEU A  1 334 ? -31.50600 -54.29100 -24.07500 1.000 37.91000  ? 365 LEU A CA  1 
ATOM   2519  C  C   . LEU A  1 334 ? -33.00600 -54.51200 -23.96900 1.000 44.68000  ? 365 LEU A C   1 
ATOM   2520  O  O   . LEU A  1 334 ? -33.57400 -55.22800 -24.80300 1.000 39.13000  ? 365 LEU A O   1 
ATOM   2521  C  CB  . LEU A  1 334 ? -30.78000 -55.55400 -23.62600 1.000 39.43000  ? 365 LEU A CB  1 
ATOM   2522  C  CG  . LEU A  1 334 ? -29.27400 -55.57800 -23.83700 1.000 40.70000  ? 365 LEU A CG  1 
ATOM   2523  C  CD1 . LEU A  1 334 ? -28.57900 -56.53700 -22.87400 1.000 41.71000  ? 365 LEU A CD1 1 
ATOM   2524  C  CD2 . LEU A  1 334 ? -29.00900 -56.00500 -25.25600 1.000 43.93000  ? 365 LEU A CD2 1 
ATOM   2525  N  N   . ASP A  1 335 ? -33.66200 -53.90800 -22.97000 1.000 39.81000  ? 366 ASP A N   1 
ATOM   2526  C  CA  . ASP A  1 335 ? -35.09800 -54.10300 -22.82500 1.000 41.26000  ? 366 ASP A CA  1 
ATOM   2527  C  C   . ASP A  1 335 ? -35.89300 -53.31200 -23.85400 1.000 45.01000  ? 366 ASP A C   1 
ATOM   2528  O  O   . ASP A  1 335 ? -37.07900 -53.59300 -24.05100 1.000 44.70000  ? 366 ASP A O   1 
ATOM   2529  C  CB  . ASP A  1 335 ? -35.58700 -53.70800 -21.42300 1.000 33.86000  ? 366 ASP A CB  1 
ATOM   2530  C  CG  . ASP A  1 335 ? -34.96100 -54.54200 -20.30900 1.000 39.97000  ? 366 ASP A CG  1 
ATOM   2531  O  OD1 . ASP A  1 335 ? -34.58000 -55.71900 -20.54500 1.000 44.60000  ? 366 ASP A OD1 1 
ATOM   2532  O  OD2 . ASP A  1 335 ? -34.87300 -54.01300 -19.17400 1.000 38.78000  ? 366 ASP A OD2 1 
ATOM   2533  N  N   . LEU A  1 336 ? -35.28300 -52.32200 -24.50300 1.000 46.71000  ? 367 LEU A N   1 
ATOM   2534  C  CA  . LEU A  1 336 ? -36.05500 -51.48600 -25.41400 1.000 42.84000  ? 367 LEU A CA  1 
ATOM   2535  C  C   . LEU A  1 336 ? -36.52600 -52.27900 -26.63500 1.000 46.77000  ? 367 LEU A C   1 
ATOM   2536  O  O   . LEU A  1 336 ? -37.64500 -52.06800 -27.12300 1.000 45.22000  ? 367 LEU A O   1 
ATOM   2537  C  CB  . LEU A  1 336 ? -35.22000 -50.28000 -25.83300 1.000 40.96000  ? 367 LEU A CB  1 
ATOM   2538  C  CG  . LEU A  1 336 ? -34.68100 -49.41500 -24.69200 1.000 39.92000  ? 367 LEU A CG  1 
ATOM   2539  C  CD1 . LEU A  1 336 ? -33.75700 -48.36600 -25.26900 1.000 37.69000  ? 367 LEU A CD1 1 
ATOM   2540  C  CD2 . LEU A  1 336 ? -35.81300 -48.75500 -23.89200 1.000 42.71000  ? 367 LEU A CD2 1 
ATOM   2541  N  N   . TYR A  1 337 ? -35.68600 -53.19000 -27.15700 1.000 36.76000  ? 368 TYR A N   1 
ATOM   2542  C  CA  . TYR A  1 337 ? -36.08700 -53.95000 -28.34200 1.000 44.70000  ? 368 TYR A CA  1 
ATOM   2543  C  C   . TYR A  1 337 ? -37.37100 -54.75200 -28.11200 1.000 47.43000  ? 368 TYR A C   1 
ATOM   2544  O  O   . TYR A  1 337 ? -38.35100 -54.53300 -28.84700 1.000 48.60000  ? 368 TYR A O   1 
ATOM   2545  C  CB  . TYR A  1 337 ? -34.89500 -54.79700 -28.79500 1.000 47.61000  ? 368 TYR A CB  1 
ATOM   2546  C  CG  . TYR A  1 337 ? -34.94600 -55.47500 -30.16200 1.000 47.00000  ? 368 TYR A CG  1 
ATOM   2547  C  CD1 . TYR A  1 337 ? -36.06000 -56.19100 -30.59300 1.000 49.43000  ? 368 TYR A CD1 1 
ATOM   2548  C  CD2 . TYR A  1 337 ? -33.84000 -55.43400 -30.99600 1.000 47.34000  ? 368 TYR A CD2 1 
ATOM   2549  C  CE1 . TYR A  1 337 ? -36.06000 -56.83200 -31.81900 1.000 42.89000  ? 368 TYR A CE1 1 
ATOM   2550  C  CE2 . TYR A  1 337 ? -33.83000 -56.06900 -32.21800 1.000 47.66000  ? 368 TYR A CE2 1 
ATOM   2551  C  CZ  . TYR A  1 337 ? -34.94000 -56.76400 -32.62300 1.000 46.96000  ? 368 TYR A CZ  1 
ATOM   2552  O  OH  . TYR A  1 337 ? -34.92000 -57.38600 -33.84500 1.000 49.29000  ? 368 TYR A OH  1 
ATOM   2553  N  N   . PRO A  1 338 ? -37.45200 -55.67600 -27.14200 1.000 50.58000  ? 369 PRO A N   1 
ATOM   2554  C  CA  . PRO A  1 338 ? -38.72700 -56.39200 -26.93500 1.000 48.25000  ? 369 PRO A CA  1 
ATOM   2555  C  C   . PRO A  1 338 ? -39.83700 -55.50000 -26.39800 1.000 46.54000  ? 369 PRO A C   1 
ATOM   2556  O  O   . PRO A  1 338 ? -41.01700 -55.80300 -26.60000 1.000 45.84000  ? 369 PRO A O   1 
ATOM   2557  C  CB  . PRO A  1 338 ? -38.35500 -57.49400 -25.93400 1.000 47.11000  ? 369 PRO A CB  1 
ATOM   2558  C  CG  . PRO A  1 338 ? -37.17200 -56.90100 -25.18400 1.000 45.72000  ? 369 PRO A CG  1 
ATOM   2559  C  CD  . PRO A  1 338 ? -36.41000 -56.13300 -26.19200 1.000 44.24000  ? 369 PRO A CD  1 
ATOM   2560  N  N   . THR A  1 339 ? -39.51000 -54.42700 -25.68200 1.000 43.74000  ? 370 THR A N   1 
ATOM   2561  C  CA  . THR A  1 339 ? -40.56400 -53.51800 -25.25200 1.000 44.75000  ? 370 THR A CA  1 
ATOM   2562  C  C   . THR A  1 339 ? -41.17900 -52.78200 -26.43200 1.000 52.42000  ? 370 THR A C   1 
ATOM   2563  O  O   . THR A  1 339 ? -42.40800 -52.68400 -26.52500 1.000 52.65000  ? 370 THR A O   1 
ATOM   2564  C  CB  . THR A  1 339 ? -40.03100 -52.54300 -24.21500 1.000 46.30000  ? 370 THR A CB  1 
ATOM   2565  O  OG1 . THR A  1 339 ? -39.60400 -53.28900 -23.07500 1.000 47.11000  ? 370 THR A OG1 1 
ATOM   2566  C  CG2 . THR A  1 339 ? -41.07300 -51.52200 -23.82200 1.000 42.60000  ? 370 THR A CG2 1 
ATOM   2567  N  N   . PHE A  1 340 ? -40.35500 -52.30300 -27.37100 1.000 46.57000  ? 371 PHE A N   1 
ATOM   2568  C  CA  . PHE A  1 340 ? -40.91200 -51.55100 -28.48800 1.000 45.09000  ? 371 PHE A CA  1 
ATOM   2569  C  C   . PHE A  1 340 ? -41.71600 -52.45600 -29.41700 1.000 47.70000  ? 371 PHE A C   1 
ATOM   2570  O  O   . PHE A  1 340 ? -42.82600 -52.09800 -29.82500 1.000 44.27000  ? 371 PHE A O   1 
ATOM   2571  C  CB  . PHE A  1 340 ? -39.81400 -50.83500 -29.27200 1.000 41.36000  ? 371 PHE A CB  1 
ATOM   2572  C  CG  . PHE A  1 340 ? -39.17000 -49.69700 -28.53500 1.000 47.42000  ? 371 PHE A CG  1 
ATOM   2573  C  CD1 . PHE A  1 340 ? -39.76100 -49.15700 -27.39700 1.000 46.08000  ? 371 PHE A CD1 1 
ATOM   2574  C  CD2 . PHE A  1 340 ? -37.97200 -49.14900 -28.99600 1.000 43.20000  ? 371 PHE A CD2 1 
ATOM   2575  C  CE1 . PHE A  1 340 ? -39.15300 -48.10000 -26.72000 1.000 47.01000  ? 371 PHE A CE1 1 
ATOM   2576  C  CE2 . PHE A  1 340 ? -37.35400 -48.09100 -28.32000 1.000 43.57000  ? 371 PHE A CE2 1 
ATOM   2577  C  CZ  . PHE A  1 340 ? -37.93900 -47.56500 -27.18000 1.000 42.13000  ? 371 PHE A CZ  1 
ATOM   2578  N  N   . THR A  1 341 ? -41.16500 -53.62000 -29.77800 1.000 46.38000  ? 372 THR A N   1 
ATOM   2579  C  CA  . THR A  1 341 ? -41.88500 -54.52400 -30.66800 1.000 50.44000  ? 372 THR A CA  1 
ATOM   2580  C  C   . THR A  1 341 ? -43.16900 -55.02900 -30.01800 1.000 53.97000  ? 372 THR A C   1 
ATOM   2581  O  O   . THR A  1 341 ? -44.20800 -55.13000 -30.67900 1.000 45.90000  ? 372 THR A O   1 
ATOM   2582  C  CB  . THR A  1 341 ? -40.99800 -55.70000 -31.07200 1.000 48.86000  ? 372 THR A CB  1 
ATOM   2583  O  OG1 . THR A  1 341 ? -40.54600 -56.35800 -29.89200 1.000 50.17000  ? 372 THR A OG1 1 
ATOM   2584  C  CG2 . THR A  1 341 ? -39.79400 -55.23500 -31.86400 1.000 46.69000  ? 372 THR A CG2 1 
ATOM   2585  N  N   . GLY A  1 342 ? -43.12500 -55.30100 -28.71000 1.000 55.02000  ? 373 GLY A N   1 
ATOM   2586  C  CA  . GLY A  1 342 ? -44.35000 -55.61600 -27.99100 1.000 48.91000  ? 373 GLY A CA  1 
ATOM   2587  C  C   . GLY A  1 342 ? -45.38700 -54.52200 -28.14100 1.000 46.37000  ? 373 GLY A C   1 
ATOM   2588  O  O   . GLY A  1 342 ? -46.54900 -54.78600 -28.46200 1.000 51.41000  ? 373 GLY A O   1 
ATOM   2589  N  N   . LEU A  1 343 ? -44.98500 -53.27500 -27.89900 1.000 49.67000  ? 374 LEU A N   1 
ATOM   2590  C  CA  . LEU A  1 343 ? -45.90700 -52.16900 -28.11300 1.000 51.31000  ? 374 LEU A CA  1 
ATOM   2591  C  C   . LEU A  1 343 ? -46.32300 -52.06000 -29.56800 1.000 54.06000  ? 374 LEU A C   1 
ATOM   2592  O  O   . LEU A  1 343 ? -47.41300 -51.56400 -29.86400 1.000 55.54000  ? 374 LEU A O   1 
ATOM   2593  C  CB  . LEU A  1 343 ? -45.30100 -50.84400 -27.67000 1.000 47.80000  ? 374 LEU A CB  1 
ATOM   2594  C  CG  . LEU A  1 343 ? -45.08500 -50.57000 -26.18600 1.000 52.20000  ? 374 LEU A CG  1 
ATOM   2595  C  CD1 . LEU A  1 343 ? -44.35300 -49.24900 -26.09100 1.000 46.51000  ? 374 LEU A CD1 1 
ATOM   2596  C  CD2 . LEU A  1 343 ? -46.40100 -50.53400 -25.40500 1.000 46.66000  ? 374 LEU A CD2 1 
ATOM   2597  N  N   . ALA A  1 344 ? -45.45700 -52.44500 -30.49200 1.000 51.62000  ? 375 ALA A N   1 
ATOM   2598  C  CA  . ALA A  1 344 ? -45.83800 -52.32800 -31.88700 1.000 52.16000  ? 375 ALA A CA  1 
ATOM   2599  C  C   . ALA A  1 344 ? -46.70700 -53.48500 -32.33000 1.000 55.08000  ? 375 ALA A C   1 
ATOM   2600  O  O   . ALA A  1 344 ? -47.13300 -53.50000 -33.48700 1.000 50.78000  ? 375 ALA A O   1 
ATOM   2601  C  CB  . ALA A  1 344 ? -44.59500 -52.24000 -32.78400 1.000 44.42000  ? 375 ALA A CB  1 
ATOM   2602  N  N   . GLU A  1 345 ? -46.95300 -54.45700 -31.44400 1.000 57.76000  ? 376 GLU A N   1 
ATOM   2603  C  CA  . GLU A  1 345 ? -47.67100 -55.68600 -31.79200 1.000 63.69000  ? 376 GLU A CA  1 
ATOM   2604  C  C   . GLU A  1 345 ? -47.01800 -56.38400 -32.97200 1.000 55.86000  ? 376 GLU A C   1 
ATOM   2605  O  O   . GLU A  1 345 ? -47.68400 -57.03400 -33.77300 1.000 59.49000  ? 376 GLU A O   1 
ATOM   2606  C  CB  . GLU A  1 345 ? -49.15400 -55.41200 -32.06900 1.000 57.26000  ? 376 GLU A CB  1 
ATOM   2607  C  CG  . GLU A  1 345 ? -49.86100 -54.78800 -30.86800 1.000 63.14000  ? 376 GLU A CG  1 
ATOM   2608  C  CD  . GLU A  1 345 ? -51.23900 -54.24700 -31.20900 1.000 70.85000  ? 376 GLU A CD  1 
ATOM   2609  O  OE1 . GLU A  1 345 ? -51.80300 -54.65400 -32.24600 1.000 67.47000  ? 376 GLU A OE1 1 
ATOM   2610  O  OE2 . GLU A  1 345 ? -51.75400 -53.40000 -30.44500 1.000 76.16000  ? 376 GLU A OE2 1 
ATOM   2611  N  N   . ALA A  1 346 ? -45.70600 -56.25400 -33.08100 1.000 55.88000  ? 377 ALA A N   1 
ATOM   2612  C  CA  . ALA A  1 346 ? -44.97000 -56.82800 -34.19500 1.000 56.46000  ? 377 ALA A CA  1 
ATOM   2613  C  C   . ALA A  1 346 ? -44.55800 -58.25600 -33.87800 1.000 59.98000  ? 377 ALA A C   1 
ATOM   2614  O  O   . ALA A  1 346 ? -44.42700 -58.64100 -32.71400 1.000 71.27000  ? 377 ALA A O   1 
ATOM   2615  C  CB  . ALA A  1 346 ? -43.73000 -55.99600 -34.51800 1.000 57.11000  ? 377 ALA A CB  1 
ATOM   2616  N  N   . LYS A  1 347 ? -44.39700 -59.05400 -34.92500 1.000 58.12000  ? 378 LYS A N   1 
ATOM   2617  C  CA  . LYS A  1 347 ? -43.92000 -60.41700 -34.77600 1.000 61.94000  ? 378 LYS A CA  1 
ATOM   2618  C  C   . LYS A  1 347 ? -42.41300 -60.41600 -34.96600 1.000 63.36000  ? 378 LYS A C   1 
ATOM   2619  O  O   . LYS A  1 347 ? -41.88400 -59.73900 -35.85400 1.000 58.04000  ? 378 LYS A O   1 
ATOM   2620  C  CB  . LYS A  1 347 ? -44.58700 -61.35800 -35.78400 1.000 64.18000  ? 378 LYS A CB  1 
ATOM   2621  N  N   . LEU A  1 348 ? -41.73700 -61.16800 -34.14200 1.000 60.33000  ? 379 LEU A N   1 
ATOM   2622  C  CA  . LEU A  1 348 ? -40.30000 -61.17600 -34.26100 1.000 58.90000  ? 379 LEU A CA  1 
ATOM   2623  C  C   . LEU A  1 348 ? -39.87300 -62.03700 -35.44300 1.000 69.09000  ? 379 LEU A C   1 
ATOM   2624  O  O   . LEU A  1 348 ? -40.57300 -62.98200 -35.81500 1.000 71.66000  ? 379 LEU A O   1 
ATOM   2625  C  CB  . LEU A  1 348 ? -39.68500 -61.71500 -32.99600 1.000 59.48000  ? 379 LEU A CB  1 
ATOM   2626  C  CG  . LEU A  1 348 ? -39.79700 -60.72000 -31.85400 1.000 54.54000  ? 379 LEU A CG  1 
ATOM   2627  C  CD1 . LEU A  1 348 ? -38.99900 -61.26100 -30.68300 1.000 59.07000  ? 379 LEU A CD1 1 
ATOM   2628  C  CD2 . LEU A  1 348 ? -39.34900 -59.32500 -32.28700 1.000 53.26000  ? 379 LEU A CD2 1 
ATOM   2629  N  N   . PRO A  1 349 ? -38.73600 -61.72500 -36.06100 1.000 68.69000  ? 380 PRO A N   1 
ATOM   2630  C  CA  . PRO A  1 349 ? -38.22600 -62.59800 -37.12700 1.000 71.01000  ? 380 PRO A CA  1 
ATOM   2631  C  C   . PRO A  1 349 ? -38.02400 -64.01200 -36.60100 1.000 67.79000  ? 380 PRO A C   1 
ATOM   2632  O  O   . PRO A  1 349 ? -37.75200 -64.22700 -35.41700 1.000 66.90000  ? 380 PRO A O   1 
ATOM   2633  C  CB  . PRO A  1 349 ? -36.89000 -61.94700 -37.50900 1.000 65.67000  ? 380 PRO A CB  1 
ATOM   2634  C  CG  . PRO A  1 349 ? -37.05500 -60.50700 -37.10300 1.000 63.02000  ? 380 PRO A CG  1 
ATOM   2635  C  CD  . PRO A  1 349 ? -37.89900 -60.53100 -35.86200 1.000 55.37000  ? 380 PRO A CD  1 
ATOM   2636  N  N   . LYS A  1 350 ? -38.15200 -64.98500 -37.49500 1.000 67.77000  ? 381 LYS A N   1 
ATOM   2637  C  CA  . LYS A  1 350 ? -37.99200 -66.37400 -37.08300 1.000 70.80000  ? 381 LYS A CA  1 
ATOM   2638  C  C   . LYS A  1 350 ? -36.56600 -66.61800 -36.61200 1.000 69.10000  ? 381 LYS A C   1 
ATOM   2639  O  O   . LYS A  1 350 ? -35.61200 -66.44900 -37.38100 1.000 66.64000  ? 381 LYS A O   1 
ATOM   2640  C  CB  . LYS A  1 350 ? -38.34800 -67.31400 -38.23700 1.000 62.06000  ? 381 LYS A CB  1 
ATOM   2641  N  N   . GLY A  1 351 ? -36.42300 -66.99900 -35.34300 1.000 63.93000  ? 382 GLY A N   1 
ATOM   2642  C  CA  . GLY A  1 351 ? -35.12100 -67.29300 -34.77100 1.000 67.83000  ? 382 GLY A CA  1 
ATOM   2643  C  C   . GLY A  1 351 ? -34.38500 -66.12200 -34.14900 1.000 64.25000  ? 382 GLY A C   1 
ATOM   2644  O  O   . GLY A  1 351 ? -33.21600 -66.27600 -33.77700 1.000 59.66000  ? 382 GLY A O   1 
ATOM   2645  N  N   . LYS A  1 352 ? -35.04000 -64.98000 -33.97700 1.000 66.82000  ? 383 LYS A N   1 
ATOM   2646  C  CA  . LYS A  1 352 ? -34.37500 -63.79900 -33.44800 1.000 59.06000  ? 383 LYS A CA  1 
ATOM   2647  C  C   . LYS A  1 352 ? -34.10700 -63.97700 -31.96400 1.000 56.49000  ? 383 LYS A C   1 
ATOM   2648  O  O   . LYS A  1 352 ? -35.00000 -64.34500 -31.19800 1.000 58.05000  ? 383 LYS A O   1 
ATOM   2649  C  CB  . LYS A  1 352 ? -35.21700 -62.54900 -33.68600 1.000 53.70000  ? 383 LYS A CB  1 
ATOM   2650  C  CG  . LYS A  1 352 ? -34.70600 -61.33100 -32.93800 1.000 58.10000  ? 383 LYS A CG  1 
ATOM   2651  C  CD  . LYS A  1 352 ? -33.31300 -60.94200 -33.38100 1.000 51.95000  ? 383 LYS A CD  1 
ATOM   2652  C  CE  . LYS A  1 352 ? -32.89800 -59.67100 -32.70200 1.000 53.63000  ? 383 LYS A CE  1 
ATOM   2653  N  NZ  . LYS A  1 352 ? -31.78200 -59.01600 -33.42500 1.000 50.07000  ? 383 LYS A NZ  1 
ATOM   2654  N  N   . GLN A  1 353 ? -32.85500 -63.78500 -31.57600 1.000 59.46000  ? 384 GLN A N   1 
ATOM   2655  C  CA  . GLN A  1 353 ? -32.43100 -63.89500 -30.19000 1.000 56.68000  ? 384 GLN A CA  1 
ATOM   2656  C  C   . GLN A  1 353 ? -32.39300 -62.52600 -29.51700 1.000 53.83000  ? 384 GLN A C   1 
ATOM   2657  O  O   . GLN A  1 353 ? -31.93300 -61.54500 -30.11100 1.000 52.47000  ? 384 GLN A O   1 
ATOM   2658  C  CB  . GLN A  1 353 ? -31.04900 -64.53100 -30.14900 1.000 63.43000  ? 384 GLN A CB  1 
ATOM   2659  C  CG  . GLN A  1 353 ? -30.96300 -65.82600 -30.92600 1.000 60.02000  ? 384 GLN A CG  1 
ATOM   2660  C  CD  . GLN A  1 353 ? -31.16500 -67.01600 -30.02100 1.000 67.80000  ? 384 GLN A CD  1 
ATOM   2661  O  OE1 . GLN A  1 353 ? -32.19000 -67.12900 -29.34100 1.000 69.05000  ? 384 GLN A OE1 1 
ATOM   2662  N  NE2 . GLN A  1 353 ? -30.17000 -67.89500 -29.97500 1.000 69.45000  ? 384 GLN A NE2 1 
ATOM   2663  N  N   . LEU A  1 354 ? -32.88100 -62.46400 -28.28300 1.000 47.38000  ? 385 LEU A N   1 
ATOM   2664  C  CA  . LEU A  1 354 ? -32.93500 -61.22400 -27.51900 1.000 48.20000  ? 385 LEU A CA  1 
ATOM   2665  C  C   . LEU A  1 354 ? -32.40300 -61.48900 -26.11900 1.000 54.61000  ? 385 LEU A C   1 
ATOM   2666  O  O   . LEU A  1 354 ? -32.63500 -62.56100 -25.54900 1.000 54.60000  ? 385 LEU A O   1 
ATOM   2667  C  CB  . LEU A  1 354 ? -34.34800 -60.66500 -27.42300 1.000 47.46000  ? 385 LEU A CB  1 
ATOM   2668  C  CG  . LEU A  1 354 ? -34.96600 -60.09400 -28.70300 1.000 52.28000  ? 385 LEU A CG  1 
ATOM   2669  C  CD1 . LEU A  1 354 ? -36.31200 -59.41600 -28.41300 1.000 50.31000  ? 385 LEU A CD1 1 
ATOM   2670  C  CD2 . LEU A  1 354 ? -34.01400 -59.12700 -29.36400 1.000 45.56000  ? 385 LEU A CD2 1 
ATOM   2671  N  N   . ASP A  1 355 ? -31.66500 -60.52900 -25.57100 1.000 46.94000  ? 386 ASP A N   1 
ATOM   2672  C  CA  . ASP A  1 355 ? -31.13200 -60.71100 -24.23100 1.000 47.95000  ? 386 ASP A CA  1 
ATOM   2673  C  C   . ASP A  1 355 ? -31.90700 -59.92900 -23.19000 1.000 45.95000  ? 386 ASP A C   1 
ATOM   2674  O  O   . ASP A  1 355 ? -31.73300 -60.17400 -21.99500 1.000 53.97000  ? 386 ASP A O   1 
ATOM   2675  C  CB  . ASP A  1 355 ? -29.64900 -60.31100 -24.19400 1.000 43.51000  ? 386 ASP A CB  1 
ATOM   2676  C  CG  . ASP A  1 355 ? -28.78400 -61.26000 -24.98900 1.000 51.14000  ? 386 ASP A CG  1 
ATOM   2677  O  OD1 . ASP A  1 355 ? -29.09600 -62.47600 -24.98300 1.000 56.35000  ? 386 ASP A OD1 1 
ATOM   2678  O  OD2 . ASP A  1 355 ? -27.83100 -60.79000 -25.65700 1.000 50.28000  ? 386 ASP A OD2 1 
ATOM   2679  N  N   . GLY A  1 356 ? -32.77100 -59.01100 -23.61100 1.000 43.08000  ? 387 GLY A N   1 
ATOM   2680  C  CA  . GLY A  1 356 ? -33.59400 -58.25700 -22.69800 1.000 43.52000  ? 387 GLY A CA  1 
ATOM   2681  C  C   . GLY A  1 356 ? -35.03100 -58.75700 -22.69000 1.000 50.11000  ? 387 GLY A C   1 
ATOM   2682  O  O   . GLY A  1 356 ? -35.35700 -59.83300 -23.19700 1.000 48.80000  ? 387 GLY A O   1 
ATOM   2683  N  N   . LYS A  1 357 ? -35.89700 -57.95200 -22.08800 1.000 47.98000  ? 388 LYS A N   1 
ATOM   2684  C  CA  . LYS A  1 357 ? -37.28200 -58.33900 -21.89500 1.000 52.47000  ? 388 LYS A CA  1 
ATOM   2685  C  C   . LYS A  1 357 ? -38.16500 -57.10900 -22.00000 1.000 48.23000  ? 388 LYS A C   1 
ATOM   2686  O  O   . LYS A  1 357 ? -37.73800 -55.98000 -21.74000 1.000 45.68000  ? 388 LYS A O   1 
ATOM   2687  C  CB  . LYS A  1 357 ? -37.48200 -59.02500 -20.53800 1.000 51.18000  ? 388 LYS A CB  1 
ATOM   2688  C  CG  . LYS A  1 357 ? -36.93900 -58.20200 -19.39000 1.000 49.13000  ? 388 LYS A CG  1 
ATOM   2689  C  CD  . LYS A  1 357 ? -36.95100 -58.98000 -18.09200 1.000 51.53000  ? 388 LYS A CD  1 
ATOM   2690  C  CE  . LYS A  1 357 ? -36.17700 -60.26900 -18.22200 1.000 51.35000  ? 388 LYS A CE  1 
ATOM   2691  N  NZ  . LYS A  1 357 ? -35.95100 -60.82500 -16.85300 1.000 58.51000  ? 388 LYS A NZ  1 
ATOM   2692  N  N   . ASN A  1 358 ? -39.40600 -57.35300 -22.37200 1.000 49.76000  ? 389 ASN A N   1 
ATOM   2693  C  CA  . ASN A  1 358 ? -40.42500 -56.32000 -22.38200 1.000 47.17000  ? 389 ASN A CA  1 
ATOM   2694  C  C   . ASN A  1 358 ? -40.73800 -55.90500 -20.94600 1.000 44.83000  ? 389 ASN A C   1 
ATOM   2695  O  O   . ASN A  1 358 ? -41.11500 -56.74100 -20.12400 1.000 55.01000  ? 389 ASN A O   1 
ATOM   2696  C  CB  . ASN A  1 358 ? -41.65200 -56.87400 -23.11100 1.000 47.48000  ? 389 ASN A CB  1 
ATOM   2697  C  CG  . ASN A  1 358 ? -42.80800 -55.91900 -23.14600 1.000 45.96000  ? 389 ASN A CG  1 
ATOM   2698  O  OD1 . ASN A  1 358 ? -42.76000 -54.80500 -22.60300 1.000 47.35000  ? 389 ASN A OD1 1 
ATOM   2699  N  ND2 . ASN A  1 358 ? -43.87500 -56.34800 -23.81300 1.000 57.10000  ? 389 ASN A ND2 1 
ATOM   2700  N  N   . ILE A  1 359 ? -40.53500 -54.63000 -20.61900 1.000 43.58000  ? 390 ILE A N   1 
ATOM   2701  C  CA  . ILE A  1 359 ? -40.69600 -54.17000 -19.24600 1.000 42.00000  ? 390 ILE A CA  1 
ATOM   2702  C  C   . ILE A  1 359 ? -41.87300 -53.21600 -19.09000 1.000 49.02000  ? 390 ILE A C   1 
ATOM   2703  O  O   . ILE A  1 359 ? -42.06300 -52.64600 -18.00300 1.000 46.13000  ? 390 ILE A O   1 
ATOM   2704  C  CB  . ILE A  1 359 ? -39.40500 -53.51900 -18.72300 1.000 41.33000  ? 390 ILE A CB  1 
ATOM   2705  C  CG1 . ILE A  1 359 ? -39.14900 -52.20400 -19.44700 1.000 44.52000  ? 390 ILE A CG1 1 
ATOM   2706  C  CG2 . ILE A  1 359 ? -38.20100 -54.44000 -18.93900 1.000 43.32000  ? 390 ILE A CG2 1 
ATOM   2707  C  CD1 . ILE A  1 359 ? -38.00700 -51.40800 -18.83500 1.000 35.08000  ? 390 ILE A CD1 1 
ATOM   2708  N  N   . MET A  1 360 ? -42.66800 -53.01100 -20.14700 1.000 43.55000  ? 391 MET A N   1 
ATOM   2709  C  CA  . MET A  1 360 ? -43.73400 -52.01100 -20.06200 1.000 52.35000  ? 391 MET A CA  1 
ATOM   2710  C  C   . MET A  1 360 ? -44.77100 -52.39900 -19.00900 1.000 45.11000  ? 391 MET A C   1 
ATOM   2711  O  O   . MET A  1 360 ? -45.26700 -51.54400 -18.26800 1.000 48.10000  ? 391 MET A O   1 
ATOM   2712  C  CB  . MET A  1 360 ? -44.39300 -51.80100 -21.43000 1.000 46.13000  ? 391 MET A CB  1 
ATOM   2713  C  CG  . MET A  1 360 ? -45.31100 -50.58200 -21.48100 1.000 44.06000  ? 391 MET A CG  1 
ATOM   2714  S  SD  . MET A  1 360 ? -44.66300 -49.06200 -20.74300 1.000 49.76000  ? 391 MET A SD  1 
ATOM   2715  C  CE  . MET A  1 360 ? -43.77700 -48.37900 -22.14000 1.000 44.69000  ? 391 MET A CE  1 
ATOM   2716  N  N   . ASP A  1 361 ? -45.11400 -53.68000 -18.92700 1.000 38.80000  ? 392 ASP A N   1 
ATOM   2717  C  CA  . ASP A  1 361 ? -46.03800 -54.11700 -17.88500 1.000 51.70000  ? 392 ASP A CA  1 
ATOM   2718  C  C   . ASP A  1 361 ? -45.44700 -53.89400 -16.49400 1.000 52.65000  ? 392 ASP A C   1 
ATOM   2719  O  O   . ASP A  1 361 ? -46.10300 -53.31900 -15.61000 1.000 49.90000  ? 392 ASP A O   1 
ATOM   2720  C  CB  . ASP A  1 361 ? -46.37700 -55.59500 -18.08700 1.000 64.57000  ? 392 ASP A CB  1 
ATOM   2721  C  CG  . ASP A  1 361 ? -47.72100 -55.97600 -17.48700 1.000 75.94000  ? 392 ASP A CG  1 
ATOM   2722  O  OD1 . ASP A  1 361 ? -48.61700 -55.09900 -17.41400 1.000 69.95000  ? 392 ASP A OD1 1 
ATOM   2723  O  OD2 . ASP A  1 361 ? -47.86400 -57.14900 -17.05600 1.000 79.72000  ? 392 ASP A OD2 1 
ATOM   2724  N  N   . ASP A  1 362 ? -44.19200 -54.32700 -16.29500 1.000 50.74000  ? 393 ASP A N   1 
ATOM   2725  C  CA  . ASP A  1 362 ? -43.47300 -54.08200 -15.04000 1.000 42.06000  ? 393 ASP A CA  1 
ATOM   2726  C  C   . ASP A  1 362 ? -43.44100 -52.60400 -14.69600 1.000 45.05000  ? 393 ASP A C   1 
ATOM   2727  O  O   . ASP A  1 362 ? -43.61100 -52.23000 -13.53500 1.000 48.73000  ? 393 ASP A O   1 
ATOM   2728  C  CB  . ASP A  1 362 ? -42.05800 -54.65000 -15.14300 1.000 51.31000  ? 393 ASP A CB  1 
ATOM   2729  C  CG  . ASP A  1 362 ? -42.04900 -56.16800 -15.23100 1.000 54.98000  ? 393 ASP A CG  1 
ATOM   2730  O  OD1 . ASP A  1 362 ? -43.12200 -56.77000 -15.05300 1.000 59.62000  ? 393 ASP A OD1 1 
ATOM   2731  O  OD2 . ASP A  1 362 ? -40.99500 -56.76500 -15.54000 1.000 58.90000  ? 393 ASP A OD2 1 
ATOM   2732  N  N   . VAL A  1 363 ? -43.26700 -51.73900 -15.69200 1.000 41.72000  ? 394 VAL A N   1 
ATOM   2733  C  CA  . VAL A  1 363 ? -43.27100 -50.31400 -15.39400 1.000 47.07000  ? 394 VAL A CA  1 
ATOM   2734  C  C   . VAL A  1 363 ? -44.66300 -49.85800 -14.96100 1.000 53.79000  ? 394 VAL A C   1 
ATOM   2735  O  O   . VAL A  1 363 ? -44.80900 -49.03500 -14.04800 1.000 50.62000  ? 394 VAL A O   1 
ATOM   2736  C  CB  . VAL A  1 363 ? -42.77100 -49.51700 -16.60600 1.000 48.56000  ? 394 VAL A CB  1 
ATOM   2737  C  CG1 . VAL A  1 363 ? -43.01800 -48.04200 -16.40100 1.000 47.99000  ? 394 VAL A CG1 1 
ATOM   2738  C  CG2 . VAL A  1 363 ? -41.31000 -49.79700 -16.84100 1.000 43.98000  ? 394 VAL A CG2 1 
ATOM   2739  N  N   . LEU A  1 364 ? -45.70600 -50.36800 -15.61500 1.000 48.55000  ? 395 LEU A N   1 
ATOM   2740  C  CA  . LEU A  1 364 ? -47.04700 -49.90300 -15.28000 1.000 55.68000  ? 395 LEU A CA  1 
ATOM   2741  C  C   . LEU A  1 364 ? -47.52100 -50.45900 -13.94600 1.000 55.08000  ? 395 LEU A C   1 
ATOM   2742  O  O   . LEU A  1 364 ? -48.20900 -49.75600 -13.20600 1.000 54.46000  ? 395 LEU A O   1 
ATOM   2743  C  CB  . LEU A  1 364 ? -48.02500 -50.25100 -16.40200 1.000 52.84000  ? 395 LEU A CB  1 
ATOM   2744  C  CG  . LEU A  1 364 ? -47.80700 -49.50400 -17.72700 1.000 51.24000  ? 395 LEU A CG  1 
ATOM   2745  C  CD1 . LEU A  1 364 ? -48.63000 -50.15200 -18.83100 1.000 56.98000  ? 395 LEU A CD1 1 
ATOM   2746  C  CD2 . LEU A  1 364 ? -48.13900 -48.01500 -17.59400 1.000 42.29000  ? 395 LEU A CD2 1 
ATOM   2747  N  N   . LYS A  1 365 ? -47.08900 -51.66300 -13.57700 1.000 55.34000  ? 396 LYS A N   1 
ATOM   2748  C  CA  . LYS A  1 365 ? -47.47900 -52.25300 -12.30300 1.000 55.82000  ? 396 LYS A CA  1 
ATOM   2749  C  C   . LYS A  1 365 ? -46.39200 -52.15200 -11.23700 1.000 57.26000  ? 396 LYS A C   1 
ATOM   2750  O  O   . LYS A  1 365 ? -46.61200 -52.61500 -10.11900 1.000 59.36000  ? 396 LYS A O   1 
ATOM   2751  C  CB  . LYS A  1 365 ? -47.82800 -53.74000 -12.47400 1.000 56.95000  ? 396 LYS A CB  1 
ATOM   2752  C  CG  . LYS A  1 365 ? -48.52700 -54.13900 -13.75900 1.000 58.62000  ? 396 LYS A CG  1 
ATOM   2753  C  CD  . LYS A  1 365 ? -49.95100 -53.60300 -13.83000 1.000 68.69000  ? 396 LYS A CD  1 
ATOM   2754  C  CE  . LYS A  1 365 ? -50.76000 -54.33600 -14.89800 1.000 67.66000  ? 396 LYS A CE  1 
ATOM   2755  N  NZ  . LYS A  1 365 ? -51.96900 -53.55900 -15.27700 1.000 69.85000  ? 396 LYS A NZ  1 
ATOM   2756  N  N   . ASN A  1 366 ? -45.25200 -51.52200 -11.53100 1.000 57.90000  ? 397 ASN A N   1 
ATOM   2757  C  CA  . ASN A  1 366 ? -44.13600 -51.40000 -10.58800 1.000 52.33000  ? 397 ASN A CA  1 
ATOM   2758  C  C   . ASN A  1 366 ? -43.72000 -52.75400 -10.00600 1.000 54.02000  ? 397 ASN A C   1 
ATOM   2759  O  O   . ASN A  1 366 ? -43.67000 -52.95500 -8.79700  1.000 51.71000  ? 397 ASN A O   1 
ATOM   2760  C  CB  . ASN A  1 366 ? -44.47300 -50.40900 -9.47300  1.000 54.70000  ? 397 ASN A CB  1 
ATOM   2761  C  CG  . ASN A  1 366 ? -43.23400 -49.93800 -8.70200  1.000 57.20000  ? 397 ASN A CG  1 
ATOM   2762  O  OD1 . ASN A  1 366 ? -43.07800 -50.26400 -7.51800  1.000 53.40000  ? 397 ASN A OD1 1 
ATOM   2763  N  ND2 . ASN A  1 366 ? -42.35300 -49.17100 -9.36500  1.000 51.90000  ? 397 ASN A ND2 1 
ATOM   2764  N  N   . THR A  1 367 ? -43.34100 -53.66100 -10.89400 1.000 50.85000  ? 398 THR A N   1 
ATOM   2765  C  CA  . THR A  1 367 ? -42.83700 -54.97200 -10.50900 1.000 56.09000  ? 398 THR A CA  1 
ATOM   2766  C  C   . THR A  1 367 ? -41.41100 -55.12200 -11.03400 1.000 54.62000  ? 398 THR A C   1 
ATOM   2767  O  O   . THR A  1 367 ? -40.99300 -54.41300 -11.95600 1.000 51.19000  ? 398 THR A O   1 
ATOM   2768  C  CB  . THR A  1 367 ? -43.71400 -56.11100 -11.05100 1.000 57.21000  ? 398 THR A CB  1 
ATOM   2769  O  OG1 . THR A  1 367 ? -43.70300 -56.07400 -12.48300 1.000 56.01000  ? 398 THR A OG1 1 
ATOM   2770  C  CG2 . THR A  1 367 ? -45.15600 -55.98600 -10.53800 1.000 59.30000  ? 398 THR A CG2 1 
ATOM   2771  N  N   . GLU A  1 368 ? -40.66200 -56.04700 -10.41900 1.000 55.37000  ? 399 GLU A N   1 
ATOM   2772  C  CA  . GLU A  1 368 ? -39.23500 -56.24200 -10.67200 1.000 56.03000  ? 399 GLU A CA  1 
ATOM   2773  C  C   . GLU A  1 368 ? -38.96400 -57.08900 -11.91700 1.000 47.29000  ? 399 GLU A C   1 
ATOM   2774  O  O   . GLU A  1 368 ? -39.17400 -58.30800 -11.90900 1.000 47.43000  ? 399 GLU A O   1 
ATOM   2775  C  CB  . GLU A  1 368 ? -38.57200 -56.88000 -9.44700  1.000 52.84000  ? 399 GLU A CB  1 
ATOM   2776  C  CG  . GLU A  1 368 ? -37.05800 -56.99700 -9.56900  1.000 60.72000  ? 399 GLU A CG  1 
ATOM   2777  C  CD  . GLU A  1 368 ? -36.38300 -57.47300 -8.29200  1.000 62.63000  ? 399 GLU A CD  1 
ATOM   2778  O  OE1 . GLU A  1 368 ? -37.10900 -57.81700 -7.33400  1.000 64.99000  ? 399 GLU A OE1 1 
ATOM   2779  O  OE2 . GLU A  1 368 ? -35.12700 -57.50500 -8.26100  1.000 64.99000  ? 399 GLU A OE2 1 
ATOM   2780  N  N   . PRO A  1 369 ? -38.43500 -56.49600 -12.98800 1.000 42.21000  ? 400 PRO A N   1 
ATOM   2781  C  CA  . PRO A  1 369 ? -38.18200 -57.28800 -14.19700 1.000 45.98000  ? 400 PRO A CA  1 
ATOM   2782  C  C   . PRO A  1 369 ? -37.00400 -58.23900 -14.11300 1.000 49.77000  ? 400 PRO A C   1 
ATOM   2783  O  O   . PRO A  1 369 ? -36.97900 -59.21100 -14.88400 1.000 52.07000  ? 400 PRO A O   1 
ATOM   2784  C  CB  . PRO A  1 369 ? -37.96100 -56.21400 -15.27600 1.000 52.13000  ? 400 PRO A CB  1 
ATOM   2785  C  CG  . PRO A  1 369 ? -37.55800 -54.99200 -14.52800 1.000 45.63000  ? 400 PRO A CG  1 
ATOM   2786  C  CD  . PRO A  1 369 ? -38.29100 -55.04900 -13.23200 1.000 47.04000  ? 400 PRO A CD  1 
ATOM   2787  N  N   . TYR A  1 370 ? -36.02600 -58.01200 -13.23200 1.000 48.60000  ? 401 TYR A N   1 
ATOM   2788  C  CA  . TYR A  1 370 ? -34.82300 -58.84400 -13.19900 1.000 53.12000  ? 401 TYR A CA  1 
ATOM   2789  C  C   . TYR A  1 370 ? -34.63900 -59.54200 -11.85600 1.000 56.24000  ? 401 TYR A C   1 
ATOM   2790  O  O   . TYR A  1 370 ? -33.51800 -59.68200 -11.36200 1.000 51.95000  ? 401 TYR A O   1 
ATOM   2791  C  CB  . TYR A  1 370 ? -33.57400 -58.04700 -13.55900 1.000 47.16000  ? 401 TYR A CB  1 
ATOM   2792  C  CG  . TYR A  1 370 ? -33.42200 -57.80100 -15.04400 1.000 47.92000  ? 401 TYR A CG  1 
ATOM   2793  C  CD1 . TYR A  1 370 ? -34.00200 -56.68900 -15.64300 1.000 42.85000  ? 401 TYR A CD1 1 
ATOM   2794  C  CD2 . TYR A  1 370 ? -32.68200 -58.67300 -15.84300 1.000 49.25000  ? 401 TYR A CD2 1 
ATOM   2795  C  CE1 . TYR A  1 370 ? -33.86100 -56.45200 -17.00400 1.000 46.90000  ? 401 TYR A CE1 1 
ATOM   2796  C  CE2 . TYR A  1 370 ? -32.53400 -58.44200 -17.21100 1.000 42.54000  ? 401 TYR A CE2 1 
ATOM   2797  C  CZ  . TYR A  1 370 ? -33.12800 -57.32900 -17.77900 1.000 43.02000  ? 401 TYR A CZ  1 
ATOM   2798  O  OH  . TYR A  1 370 ? -33.00000 -57.08300 -19.12400 1.000 44.92000  ? 401 TYR A OH  1 
ATOM   2799  N  N   . LYS A  1 371 ? -35.74200 -59.95500 -11.23300 1.000 55.43000  ? 402 LYS A N   1 
ATOM   2800  C  CA  . LYS A  1 371 ? -35.64900 -60.70300 -9.98400  1.000 58.39000  ? 402 LYS A CA  1 
ATOM   2801  C  C   . LYS A  1 371 ? -34.85000 -61.97900 -10.20400 1.000 60.35000  ? 402 LYS A C   1 
ATOM   2802  O  O   . LYS A  1 371 ? -35.09500 -62.72900 -11.15700 1.000 53.55000  ? 402 LYS A O   1 
ATOM   2803  C  CB  . LYS A  1 371 ? -37.03700 -61.02800 -9.43500  1.000 62.75000  ? 402 LYS A CB  1 
ATOM   2804  C  CG  . LYS A  1 371 ? -37.00900 -61.80900 -8.13000  1.000 64.08000  ? 402 LYS A CG  1 
ATOM   2805  C  CD  . LYS A  1 371 ? -38.01000 -61.27200 -7.11900  1.000 69.80000  ? 402 LYS A CD  1 
ATOM   2806  C  CE  . LYS A  1 371 ? -37.54100 -61.54100 -5.67000  1.000 80.96000  ? 402 LYS A CE  1 
ATOM   2807  N  NZ  . LYS A  1 371 ? -36.27700 -60.81200 -5.27800  1.000 68.46000  ? 402 LYS A NZ  1 
ATOM   2808  N  N   . ASP A  1 372 ? -33.80700 -62.15200 -9.38900  1.000 57.78000  ? 403 ASP A N   1 
ATOM   2809  C  CA  . ASP A  1 372 ? -32.93500 -63.32100 -9.44100  1.000 57.59000  ? 403 ASP A CA  1 
ATOM   2810  C  C   . ASP A  1 372 ? -32.20900 -63.44900 -10.77400 1.000 54.90000  ? 403 ASP A C   1 
ATOM   2811  O  O   . ASP A  1 372 ? -31.71000 -64.52800 -11.10700 1.000 56.97000  ? 403 ASP A O   1 
ATOM   2812  C  CB  . ASP A  1 372 ? -33.71700 -64.60800 -9.14000  1.000 62.02000  ? 403 ASP A CB  1 
ATOM   2813  C  CG  . ASP A  1 372 ? -34.36100 -64.59800 -7.75300  1.000 67.91000  ? 403 ASP A CG  1 
ATOM   2814  O  OD1 . ASP A  1 372 ? -34.17200 -63.61500 -6.97800  1.000 66.06000  ? 403 ASP A OD1 1 
ATOM   2815  O  OD2 . ASP A  1 372 ? -35.05700 -65.59200 -7.43900  1.000 72.48000  ? 403 ASP A OD2 1 
ATOM   2816  N  N   . GLU A  1 373 ? -32.14100 -62.37400 -11.55500 1.000 54.93000  ? 404 GLU A N   1 
ATOM   2817  C  CA  . GLU A  1 373 ? -31.44900 -62.38200 -12.83600 1.000 53.13000  ? 404 GLU A CA  1 
ATOM   2818  C  C   . GLU A  1 373 ? -30.40400 -61.27600 -12.90700 1.000 55.26000  ? 404 GLU A C   1 
ATOM   2819  O  O   . GLU A  1 373 ? -30.42300 -60.30400 -12.14200 1.000 56.11000  ? 404 GLU A O   1 
ATOM   2820  C  CB  . GLU A  1 373 ? -32.44800 -62.23800 -13.99300 1.000 58.68000  ? 404 GLU A CB  1 
ATOM   2821  C  CG  . GLU A  1 373 ? -33.26600 -63.48700 -14.20500 1.000 64.50000  ? 404 GLU A CG  1 
ATOM   2822  C  CD  . GLU A  1 373 ? -34.43200 -63.28900 -15.15400 1.000 67.51000  ? 404 GLU A CD  1 
ATOM   2823  O  OE1 . GLU A  1 373 ? -35.28800 -62.42000 -14.86300 1.000 65.31000  ? 404 GLU A OE1 1 
ATOM   2824  O  OE2 . GLU A  1 373 ? -34.48800 -64.00500 -16.18500 1.000 74.22000  ? 404 GLU A OE2 1 
ATOM   2825  N  N   . MET A  1 374 ? -29.51600 -61.40900 -13.88100 1.000 56.50000  ? 405 MET A N   1 
ATOM   2826  C  CA  . MET A  1 374 ? -28.29500 -60.62400 -13.92800 1.000 53.08000  ? 405 MET A CA  1 
ATOM   2827  C  C   . MET A  1 374 ? -28.37800 -59.54300 -14.99200 1.000 50.39000  ? 405 MET A C   1 
ATOM   2828  O  O   . MET A  1 374 ? -28.97100 -59.74600 -16.05600 1.000 56.73000  ? 405 MET A O   1 
ATOM   2829  C  CB  . MET A  1 374 ? -27.09900 -61.52800 -14.21500 1.000 49.06000  ? 405 MET A CB  1 
ATOM   2830  C  CG  . MET A  1 374 ? -26.64400 -62.32800 -13.01200 1.000 54.33000  ? 405 MET A CG  1 
ATOM   2831  S  SD  . MET A  1 374 ? -25.70800 -61.31200 -11.83800 1.000 58.27000  ? 405 MET A SD  1 
ATOM   2832  C  CE  . MET A  1 374 ? -24.42300 -62.47900 -11.37200 1.000 53.24000  ? 405 MET A CE  1 
ATOM   2833  N  N   . ILE A  1 375 ? -27.78000 -58.39500 -14.69300 1.000 44.31000  ? 406 ILE A N   1 
ATOM   2834  C  CA  . ILE A  1 375 ? -27.47100 -57.37000 -15.68200 1.000 42.39000  ? 406 ILE A CA  1 
ATOM   2835  C  C   . ILE A  1 375 ? -25.94700 -57.24700 -15.71200 1.000 43.53000  ? 406 ILE A C   1 
ATOM   2836  O  O   . ILE A  1 375 ? -25.30800 -57.10400 -14.66300 1.000 44.09000  ? 406 ILE A O   1 
ATOM   2837  C  CB  . ILE A  1 375 ? -28.19100 -56.04700 -15.36900 1.000 41.34000  ? 406 ILE A CB  1 
ATOM   2838  C  CG1 . ILE A  1 375 ? -29.69000 -56.21300 -15.69600 1.000 48.55000  ? 406 ILE A CG1 1 
ATOM   2839  C  CG2 . ILE A  1 375 ? -27.59400 -54.88300 -16.14500 1.000 43.31000  ? 406 ILE A CG2 1 
ATOM   2840  C  CD1 . ILE A  1 375 ? -30.59200 -55.07300 -15.22900 1.000 41.90000  ? 406 ILE A CD1 1 
ATOM   2841  N  N   . TYR A  1 376 ? -25.36800 -57.41000 -16.89500 1.000 47.60000  ? 407 TYR A N   1 
ATOM   2842  C  CA  . TYR A  1 376 ? -23.94200 -57.64300 -17.06300 1.000 41.90000  ? 407 TYR A CA  1 
ATOM   2843  C  C   . TYR A  1 376 ? -23.21800 -56.50600 -17.76800 1.000 45.30000  ? 407 TYR A C   1 
ATOM   2844  O  O   . TYR A  1 376 ? -23.80300 -55.74000 -18.54200 1.000 42.93000  ? 407 TYR A O   1 
ATOM   2845  C  CB  . TYR A  1 376 ? -23.69200 -58.90000 -17.89300 1.000 41.34000  ? 407 TYR A CB  1 
ATOM   2846  C  CG  . TYR A  1 376 ? -24.09500 -60.19300 -17.26200 1.000 47.97000  ? 407 TYR A CG  1 
ATOM   2847  C  CD1 . TYR A  1 376 ? -23.49800 -60.61100 -16.07300 1.000 48.72000  ? 407 TYR A CD1 1 
ATOM   2848  C  CD2 . TYR A  1 376 ? -25.00000 -61.04500 -17.88700 1.000 49.37000  ? 407 TYR A CD2 1 
ATOM   2849  C  CE1 . TYR A  1 376 ? -23.82600 -61.81400 -15.49400 1.000 50.69000  ? 407 TYR A CE1 1 
ATOM   2850  C  CE2 . TYR A  1 376 ? -25.34000 -62.27300 -17.31300 1.000 47.60000  ? 407 TYR A CE2 1 
ATOM   2851  C  CZ  . TYR A  1 376 ? -24.73900 -62.64900 -16.11800 1.000 55.80000  ? 407 TYR A CZ  1 
ATOM   2852  O  OH  . TYR A  1 376 ? -25.05200 -63.84700 -15.50500 1.000 62.03000  ? 407 TYR A OH  1 
ATOM   2853  N  N   . SER A  1 377 ? -21.89700 -56.49400 -17.57100 1.000 44.06000  ? 408 SER A N   1 
ATOM   2854  C  CA  . SER A  1 377 ? -20.99800 -55.76400 -18.44900 1.000 41.47000  ? 408 SER A CA  1 
ATOM   2855  C  C   . SER A  1 377 ? -19.63200 -56.44100 -18.45300 1.000 46.58000  ? 408 SER A C   1 
ATOM   2856  O  O   . SER A  1 377 ? -19.12300 -56.85200 -17.40000 1.000 48.02000  ? 408 SER A O   1 
ATOM   2857  C  CB  . SER A  1 377 ? -20.83500 -54.30500 -18.03800 1.000 40.42000  ? 408 SER A CB  1 
ATOM   2858  O  OG  . SER A  1 377 ? -19.94600 -53.68400 -18.95900 1.000 45.44000  ? 408 SER A OG  1 
ATOM   2859  N  N   . LEU A  1 378 ? -19.03200 -56.54600 -19.63800 1.000 43.40000  ? 409 LEU A N   1 
ATOM   2860  C  CA  . LEU A  1 378 ? -17.65000 -57.00300 -19.75100 1.000 39.97000  ? 409 LEU A CA  1 
ATOM   2861  C  C   . LEU A  1 378 ? -16.93000 -56.15100 -20.78300 1.000 37.31000  ? 409 LEU A C   1 
ATOM   2862  O  O   . LEU A  1 378 ? -17.33800 -56.10100 -21.94300 1.000 37.86000  ? 409 LEU A O   1 
ATOM   2863  C  CB  . LEU A  1 378 ? -17.58200 -58.48400 -20.13000 1.000 39.58000  ? 409 LEU A CB  1 
ATOM   2864  C  CG  . LEU A  1 378 ? -16.16900 -59.08700 -20.17300 1.000 44.25000  ? 409 LEU A CG  1 
ATOM   2865  C  CD1 . LEU A  1 378 ? -16.19000 -60.53500 -19.70600 1.000 44.79000  ? 409 LEU A CD1 1 
ATOM   2866  C  CD2 . LEU A  1 378 ? -15.50800 -59.00000 -21.57900 1.000 34.33000  ? 409 LEU A CD2 1 
ATOM   2867  N  N   . ARG A  1 379 ? -15.84400 -55.49500 -20.38200 1.000 40.97000  ? 410 ARG A N   1 
ATOM   2868  C  CA  . ARG A  1 379 ? -15.13000 -54.60600 -21.28700 1.000 37.74000  ? 410 ARG A CA  1 
ATOM   2869  C  C   . ARG A  1 379 ? -13.71500 -55.13000 -21.48500 1.000 40.34000  ? 410 ARG A C   1 
ATOM   2870  O  O   . ARG A  1 379 ? -12.98100 -55.33800 -20.51100 1.000 37.22000  ? 410 ARG A O   1 
ATOM   2871  C  CB  . ARG A  1 379 ? -15.13000 -53.17600 -20.75400 1.000 32.97000  ? 410 ARG A CB  1 
ATOM   2872  C  CG  . ARG A  1 379 ? -14.48800 -52.21000 -21.72000 1.000 34.79000  ? 410 ARG A CG  1 
ATOM   2873  C  CD  . ARG A  1 379 ? -13.16100 -51.78600 -21.21800 1.000 33.86000  ? 410 ARG A CD  1 
ATOM   2874  N  NE  . ARG A  1 379 ? -12.30100 -51.26800 -22.26200 1.000 33.64000  ? 410 ARG A NE  1 
ATOM   2875  C  CZ  . ARG A  1 379 ? -12.23000 -49.99200 -22.60200 1.000 39.58000  ? 410 ARG A CZ  1 
ATOM   2876  N  NH1 . ARG A  1 379 ? -12.98200 -49.06900 -22.00700 1.000 35.37000  ? 410 ARG A NH1 1 
ATOM   2877  N  NH2 . ARG A  1 379 ? -11.37200 -49.62900 -23.54700 1.000 38.72000  ? 410 ARG A NH2 1 
ATOM   2878  N  N   . TYR A  1 380 ? -13.33600 -55.35300 -22.74500 1.000 40.41000  ? 411 TYR A N   1 
ATOM   2879  C  CA  . TYR A  1 380 ? -12.00500 -55.87900 -23.03200 1.000 35.14000  ? 411 TYR A CA  1 
ATOM   2880  C  C   . TYR A  1 380 ? -10.96100 -54.80400 -22.81400 1.000 41.57000  ? 411 TYR A C   1 
ATOM   2881  O  O   . TYR A  1 380 ? -11.09400 -53.69600 -23.34400 1.000 38.17000  ? 411 TYR A O   1 
ATOM   2882  C  CB  . TYR A  1 380 ? -11.91500 -56.38100 -24.47400 1.000 38.57000  ? 411 TYR A CB  1 
ATOM   2883  C  CG  . TYR A  1 380 ? -12.84900 -57.52400 -24.78400 1.000 46.77000  ? 411 TYR A CG  1 
ATOM   2884  C  CD1 . TYR A  1 380 ? -12.67000 -58.76800 -24.19100 1.000 47.30000  ? 411 TYR A CD1 1 
ATOM   2885  C  CD2 . TYR A  1 380 ? -13.92600 -57.35600 -25.64800 1.000 46.99000  ? 411 TYR A CD2 1 
ATOM   2886  C  CE1 . TYR A  1 380 ? -13.52600 -59.81300 -24.46400 1.000 48.22000  ? 411 TYR A CE1 1 
ATOM   2887  C  CE2 . TYR A  1 380 ? -14.78400 -58.40300 -25.93100 1.000 51.07000  ? 411 TYR A CE2 1 
ATOM   2888  C  CZ  . TYR A  1 380 ? -14.57600 -59.62600 -25.33400 1.000 45.16000  ? 411 TYR A CZ  1 
ATOM   2889  O  OH  . TYR A  1 380 ? -15.42100 -60.67300 -25.59900 1.000 48.69000  ? 411 TYR A OH  1 
ATOM   2890  N  N   . ARG A  1 381 ? -9.87300  -55.16000 -22.10700 1.000 37.21000  ? 412 ARG A N   1 
ATOM   2891  C  CA  . ARG A  1 381 ? -8.73200  -54.27200 -21.93800 1.000 38.04000  ? 412 ARG A CA  1 
ATOM   2892  C  C   . ARG A  1 381 ? -7.52400  -54.89900 -22.64500 1.000 43.95000  ? 412 ARG A C   1 
ATOM   2893  O  O   . ARG A  1 381 ? -7.63300  -55.94700 -23.29600 1.000 44.71000  ? 412 ARG A O   1 
ATOM   2894  C  CB  . ARG A  1 381 ? -8.44600  -54.01500 -20.44900 1.000 39.23000  ? 412 ARG A CB  1 
ATOM   2895  C  CG  . ARG A  1 381 ? -9.51100  -53.21100 -19.72400 1.000 40.76000  ? 412 ARG A CG  1 
ATOM   2896  C  CD  . ARG A  1 381 ? -9.36800  -51.71300 -20.06100 1.000 41.86000  ? 412 ARG A CD  1 
ATOM   2897  N  NE  . ARG A  1 381 ? -10.34800 -50.90200 -19.34800 1.000 43.37000  ? 412 ARG A NE  1 
ATOM   2898  C  CZ  . ARG A  1 381 ? -10.54700 -49.60900 -19.55600 1.000 44.52000  ? 412 ARG A CZ  1 
ATOM   2899  N  NH1 . ARG A  1 381 ? -9.85700  -48.94600 -20.47600 1.000 34.10000  ? 412 ARG A NH1 1 
ATOM   2900  N  NH2 . ARG A  1 381 ? -11.44500 -48.96200 -18.80600 1.000 36.58000  ? 412 ARG A NH2 1 
ATOM   2901  N  N   . GLU A  1 382 ? -6.35700  -54.27100 -22.49500 1.000 41.81000  ? 413 GLU A N   1 
ATOM   2902  C  CA  . GLU A  1 382 ? -5.13000  -54.74300 -23.14000 1.000 44.27000  ? 413 GLU A CA  1 
ATOM   2903  C  C   . GLU A  1 382 ? -4.50500  -55.85400 -22.29500 1.000 40.75000  ? 413 GLU A C   1 
ATOM   2904  O  O   . GLU A  1 382 ? -3.57400  -55.65200 -21.51700 1.000 42.25000  ? 413 GLU A O   1 
ATOM   2905  C  CB  . GLU A  1 382 ? -4.16400  -53.59000 -23.37000 1.000 41.41000  ? 413 GLU A CB  1 
ATOM   2906  C  CG  . GLU A  1 382 ? -4.81100  -52.41200 -24.05700 1.000 41.89000  ? 413 GLU A CG  1 
ATOM   2907  C  CD  . GLU A  1 382 ? -5.64000  -52.83200 -25.26400 1.000 54.02000  ? 413 GLU A CD  1 
ATOM   2908  O  OE1 . GLU A  1 382 ? -5.13700  -53.59500 -26.12900 1.000 50.89000  ? 413 GLU A OE1 1 
ATOM   2909  O  OE2 . GLU A  1 382 ? -6.79900  -52.36900 -25.36100 1.000 58.19000  ? 413 GLU A OE2 1 
ATOM   2910  N  N   . GLY A  1 383 ? -5.06000  -57.05300 -22.41800 1.000 42.53000  ? 414 GLY A N   1 
ATOM   2911  C  CA  . GLY A  1 383 ? -4.52100  -58.20100 -21.71500 1.000 36.26000  ? 414 GLY A CA  1 
ATOM   2912  C  C   . GLY A  1 383 ? -5.36800  -58.69600 -20.56800 1.000 39.26000  ? 414 GLY A C   1 
ATOM   2913  O  O   . GLY A  1 383 ? -5.02600  -59.71700 -19.96900 1.000 39.19000  ? 414 GLY A O   1 
ATOM   2914  N  N   . TYR A  1 384 ? -6.49100  -58.06300 -20.27200 1.000 39.28000  ? 415 TYR A N   1 
ATOM   2915  C  CA  . TYR A  1 384 ? -7.33200  -58.53700 -19.18100 1.000 40.32000  ? 415 TYR A CA  1 
ATOM   2916  C  C   . TYR A  1 384 ? -8.73000  -58.01100 -19.43900 1.000 35.34000  ? 415 TYR A C   1 
ATOM   2917  O  O   . TYR A  1 384 ? -8.94900  -57.26600 -20.39100 1.000 41.52000  ? 415 TYR A O   1 
ATOM   2918  C  CB  . TYR A  1 384 ? -6.78300  -58.09000 -17.82000 1.000 38.36000  ? 415 TYR A CB  1 
ATOM   2919  C  CG  . TYR A  1 384 ? -6.80400  -56.58800 -17.63200 1.000 34.65000  ? 415 TYR A CG  1 
ATOM   2920  C  CD1 . TYR A  1 384 ? -5.74900  -55.80200 -18.08400 1.000 40.87000  ? 415 TYR A CD1 1 
ATOM   2921  C  CD2 . TYR A  1 384 ? -7.88200  -55.94900 -17.01100 1.000 41.76000  ? 415 TYR A CD2 1 
ATOM   2922  C  CE1 . TYR A  1 384 ? -5.74700  -54.41500 -17.91800 1.000 39.92000  ? 415 TYR A CE1 1 
ATOM   2923  C  CE2 . TYR A  1 384 ? -7.89000  -54.56400 -16.83900 1.000 39.32000  ? 415 TYR A CE2 1 
ATOM   2924  C  CZ  . TYR A  1 384 ? -6.81800  -53.80800 -17.30900 1.000 39.83000  ? 415 TYR A CZ  1 
ATOM   2925  O  OH  . TYR A  1 384 ? -6.81100  -52.44700 -17.17400 1.000 39.05000  ? 415 TYR A OH  1 
ATOM   2926  N  N   . ASN A  1 385 ? -9.67200  -58.36600 -18.56700 1.000 36.53000  ? 416 ASN A N   1 
ATOM   2927  C  CA  . ASN A  1 385 ? -11.05000 -57.91800 -18.72100 1.000 39.38000  ? 416 ASN A CA  1 
ATOM   2928  C  C   . ASN A  1 385 ? -11.52900 -57.17600 -17.48900 1.000 42.67000  ? 416 ASN A C   1 
ATOM   2929  O  O   . ASN A  1 385 ? -11.25900 -57.59400 -16.35000 1.000 42.58000  ? 416 ASN A O   1 
ATOM   2930  C  CB  . ASN A  1 385 ? -11.99500 -59.09200 -18.98000 1.000 42.55000  ? 416 ASN A CB  1 
ATOM   2931  C  CG  . ASN A  1 385 ? -11.61600 -59.87300 -20.21300 1.000 42.18000  ? 416 ASN A CG  1 
ATOM   2932  O  OD1 . ASN A  1 385 ? -11.40700 -59.30700 -21.28500 1.000 37.57000  ? 416 ASN A OD1 1 
ATOM   2933  N  ND2 . ASN A  1 385 ? -11.45400 -61.17300 -20.04800 1.000 44.79000  ? 416 ASN A ND2 1 
ATOM   2934  N  N   . ASP A  1 386 ? -12.23800 -56.06900 -17.73800 1.000 37.45000  ? 417 ASP A N   1 
ATOM   2935  C  CA  . ASP A  1 386 ? -13.01200 -55.38400 -16.71800 1.000 39.00000  ? 417 ASP A CA  1 
ATOM   2936  C  C   . ASP A  1 386 ? -14.41100 -55.97700 -16.69700 1.000 42.78000  ? 417 ASP A C   1 
ATOM   2937  O  O   . ASP A  1 386 ? -15.02400 -56.16100 -17.75400 1.000 39.33000  ? 417 ASP A O   1 
ATOM   2938  C  CB  . ASP A  1 386 ? -13.08000 -53.87900 -16.99700 1.000 39.17000  ? 417 ASP A CB  1 
ATOM   2939  C  CG  . ASP A  1 386 ? -11.77500 -53.14300 -16.65400 1.000 40.04000  ? 417 ASP A CG  1 
ATOM   2940  O  OD1 . ASP A  1 386 ? -11.03400 -53.58500 -15.74700 1.000 39.84000  ? 417 ASP A OD1 1 
ATOM   2941  O  OD2 . ASP A  1 386 ? -11.51000 -52.10800 -17.28300 1.000 41.53000  ? 417 ASP A OD2 1 
ATOM   2942  N  N   . VAL A  1 387 ? -14.92200 -56.26900 -15.49500 1.000 44.11000  ? 418 VAL A N   1 
ATOM   2943  C  CA  . VAL A  1 387 ? -16.22100 -56.91500 -15.36400 1.000 41.27000  ? 418 VAL A CA  1 
ATOM   2944  C  C   . VAL A  1 387 ? -17.04800 -56.17800 -14.32700 1.000 42.38000  ? 418 VAL A C   1 
ATOM   2945  O  O   . VAL A  1 387 ? -16.52000 -55.59800 -13.37300 1.000 42.70000  ? 418 VAL A O   1 
ATOM   2946  C  CB  . VAL A  1 387 ? -16.12900 -58.41700 -14.99100 1.000 47.29000  ? 418 VAL A CB  1 
ATOM   2947  C  CG1 . VAL A  1 387 ? -17.52200 -59.05500 -14.98000 1.000 37.84000  ? 418 VAL A CG1 1 
ATOM   2948  C  CG2 . VAL A  1 387 ? -15.20900 -59.18200 -15.94800 1.000 41.43000  ? 418 VAL A CG2 1 
ATOM   2949  N  N   . GLY A  1 388 ? -18.35800 -56.18600 -14.55000 1.000 43.46000  ? 419 GLY A N   1 
ATOM   2950  C  CA  . GLY A  1 388 ? -19.37800 -55.79500 -13.59900 1.000 46.56000  ? 419 GLY A CA  1 
ATOM   2951  C  C   . GLY A  1 388 ? -20.63500 -56.63700 -13.80500 1.000 42.44000  ? 419 GLY A C   1 
ATOM   2952  O  O   . GLY A  1 388 ? -20.96300 -56.98800 -14.94500 1.000 42.52000  ? 419 GLY A O   1 
ATOM   2953  N  N   . ALA A  1 389 ? -21.32000 -57.00800 -12.71500 1.000 44.32000  ? 420 ALA A N   1 
ATOM   2954  C  CA  . ALA A  1 389 ? -22.51500 -57.84600 -12.79700 1.000 45.82000  ? 420 ALA A CA  1 
ATOM   2955  C  C   . ALA A  1 389 ? -23.41800 -57.54300 -11.61400 1.000 44.39000  ? 420 ALA A C   1 
ATOM   2956  O  O   . ALA A  1 389 ? -22.97000 -57.60500 -10.46500 1.000 48.89000  ? 420 ALA A O   1 
ATOM   2957  C  CB  . ALA A  1 389 ? -22.15500 -59.33200 -12.80100 1.000 43.15000  ? 420 ALA A CB  1 
ATOM   2958  N  N   . ARG A  1 390 ? -24.67700 -57.22200 -11.87300 1.000 40.36000  ? 421 ARG A N   1 
ATOM   2959  C  CA  . ARG A  1 390 ? -25.56400 -56.86100 -10.77500 1.000 45.57000  ? 421 ARG A CA  1 
ATOM   2960  C  C   . ARG A  1 390 ? -26.75500 -57.80900 -10.71700 1.000 44.43000  ? 421 ARG A C   1 
ATOM   2961  O  O   . ARG A  1 390 ? -27.33000 -58.16900 -11.74600 1.000 44.90000  ? 421 ARG A O   1 
ATOM   2962  C  CB  . ARG A  1 390 ? -26.05700 -55.41100 -10.90500 1.000 40.48000  ? 421 ARG A CB  1 
ATOM   2963  C  CG  . ARG A  1 390 ? -26.92300 -54.93900 -9.74400  1.000 41.76000  ? 421 ARG A CG  1 
ATOM   2964  C  CD  . ARG A  1 390 ? -27.63100 -53.60300 -10.04300 1.000 41.50000  ? 421 ARG A CD  1 
ATOM   2965  N  NE  . ARG A  1 390 ? -28.66900 -53.36100 -9.04900  1.000 39.89000  ? 421 ARG A NE  1 
ATOM   2966  C  CZ  . ARG A  1 390 ? -29.21900 -52.18600 -8.78800  1.000 45.47000  ? 421 ARG A CZ  1 
ATOM   2967  N  NH1 . ARG A  1 390 ? -28.86000 -51.09000 -9.44000  1.000 35.77000  ? 421 ARG A NH1 1 
ATOM   2968  N  NH2 . ARG A  1 390 ? -30.15300 -52.10800 -7.84300  1.000 39.81000  ? 421 ARG A NH2 1 
ATOM   2969  N  N   . MET A  1 391 ? -27.11700 -58.21200 -9.50500  1.000 47.36000  ? 422 MET A N   1 
ATOM   2970  C  CA  . MET A  1 391 ? -28.36800 -58.92500 -9.26600  1.000 46.06000  ? 422 MET A CA  1 
ATOM   2971  C  C   . MET A  1 391 ? -28.99300 -58.32900 -8.01700  1.000 48.61000  ? 422 MET A C   1 
ATOM   2972  O  O   . MET A  1 391 ? -28.44800 -58.45900 -6.91900  1.000 48.71000  ? 422 MET A O   1 
ATOM   2973  C  CB  . MET A  1 391 ? -28.16400 -60.42800 -9.09400  1.000 50.34000  ? 422 MET A CB  1 
ATOM   2974  C  CG  . MET A  1 391 ? -29.48300 -61.19500 -9.08100  1.000 49.27000  ? 422 MET A CG  1 
ATOM   2975  S  SD  . MET A  1 391 ? -29.37000 -62.95600 -8.75700  1.000 53.61000  ? 422 MET A SD  1 
ATOM   2976  C  CE  . MET A  1 391 ? -28.65300 -63.63200 -10.25300 1.000 48.38000  ? 422 MET A CE  1 
ATOM   2977  N  N   . GLY A  1 392 ? -30.13500 -57.69000 -8.17900  1.000 48.17000  ? 423 GLY A N   1 
ATOM   2978  C  CA  . GLY A  1 392 ? -30.81800 -57.10300 -7.04100  1.000 48.63000  ? 423 GLY A CA  1 
ATOM   2979  C  C   . GLY A  1 392 ? -30.09700 -55.94200 -6.39300  1.000 51.44000  ? 423 GLY A C   1 
ATOM   2980  O  O   . GLY A  1 392 ? -29.83500 -54.92300 -7.03900  1.000 57.64000  ? 423 GLY A O   1 
ATOM   2981  N  N   . ASP A  1 393 ? -29.77500 -56.07400 -5.11300  1.000 50.73000  ? 424 ASP A N   1 
ATOM   2982  C  CA  . ASP A  1 393 ? -29.04900 -55.03300 -4.41300  1.000 47.49000  ? 424 ASP A CA  1 
ATOM   2983  C  C   . ASP A  1 393 ? -27.54000 -55.24900 -4.49500  1.000 49.22000  ? 424 ASP A C   1 
ATOM   2984  O  O   . ASP A  1 393 ? -26.77600 -54.41200 -4.00200  1.000 42.23000  ? 424 ASP A O   1 
ATOM   2985  C  CB  . ASP A  1 393 ? -29.48100 -54.99100 -2.94400  1.000 48.15000  ? 424 ASP A CB  1 
ATOM   2986  C  CG  . ASP A  1 393 ? -30.97700 -54.73200 -2.76400  1.000 61.33000  ? 424 ASP A CG  1 
ATOM   2987  O  OD1 . ASP A  1 393 ? -31.57600 -53.90900 -3.50500  1.000 53.29000  ? 424 ASP A OD1 1 
ATOM   2988  O  OD2 . ASP A  1 393 ? -31.55800 -55.37800 -1.86400  1.000 60.15000  ? 424 ASP A OD2 1 
ATOM   2989  N  N   . TRP A  1 394 ? -27.10500 -56.33400 -5.13300  1.000 48.26000  ? 425 TRP A N   1 
ATOM   2990  C  CA  . TRP A  1 394 ? -25.72400 -56.78100 -5.09100  1.000 50.27000  ? 425 TRP A CA  1 
ATOM   2991  C  C   . TRP A  1 394 ? -25.05000 -56.66500 -6.45100  1.000 44.67000  ? 425 TRP A C   1 
ATOM   2992  O  O   . TRP A  1 394 ? -25.64800 -56.96600 -7.49000  1.000 46.75000  ? 425 TRP A O   1 
ATOM   2993  C  CB  . TRP A  1 394 ? -25.65300 -58.22100 -4.57400  1.000 54.65000  ? 425 TRP A CB  1 
ATOM   2994  C  CG  . TRP A  1 394 ? -26.17100 -58.28100 -3.17800  1.000 55.96000  ? 425 TRP A CG  1 
ATOM   2995  C  CD1 . TRP A  1 394 ? -27.44500 -58.57200 -2.79800  1.000 51.44000  ? 425 TRP A CD1 1 
ATOM   2996  C  CD2 . TRP A  1 394 ? -25.45200 -57.97200 -1.97400  1.000 52.96000  ? 425 TRP A CD2 1 
ATOM   2997  N  NE1 . TRP A  1 394 ? -27.56300 -58.48800 -1.42900  1.000 58.16000  ? 425 TRP A NE1 1 
ATOM   2998  C  CE2 . TRP A  1 394 ? -26.35600 -58.12300 -0.89800  1.000 49.02000  ? 425 TRP A CE2 1 
ATOM   2999  C  CE3 . TRP A  1 394 ? -24.13100 -57.59500 -1.70100  1.000 53.24000  ? 425 TRP A CE3 1 
ATOM   3000  C  CZ2 . TRP A  1 394 ? -25.98800 -57.90900 0.42600   1.000 49.75000  ? 425 TRP A CZ2 1 
ATOM   3001  C  CZ3 . TRP A  1 394 ? -23.76300 -57.37500 -0.39300  1.000 47.12000  ? 425 TRP A CZ3 1 
ATOM   3002  C  CH2 . TRP A  1 394 ? -24.69000 -57.53200 0.66200   1.000 53.02000  ? 425 TRP A CH2 1 
ATOM   3003  N  N   . LYS A  1 395 ? -23.80200 -56.20800 -6.42900  1.000 43.94000  ? 426 LYS A N   1 
ATOM   3004  C  CA  . LYS A  1 395 ? -22.99700 -56.09400 -7.63100  1.000 45.91000  ? 426 LYS A CA  1 
ATOM   3005  C  C   . LYS A  1 395 ? -21.58200 -56.59900 -7.37800  1.000 44.56000  ? 426 LYS A C   1 
ATOM   3006  O  O   . LYS A  1 395 ? -21.00000 -56.34300 -6.32200  1.000 44.12000  ? 426 LYS A O   1 
ATOM   3007  C  CB  . LYS A  1 395 ? -22.95400 -54.65000 -8.11600  1.000 41.69000  ? 426 LYS A CB  1 
ATOM   3008  C  CG  . LYS A  1 395 ? -22.19700 -54.50400 -9.41400  1.000 40.76000  ? 426 LYS A CG  1 
ATOM   3009  C  CD  . LYS A  1 395 ? -21.68300 -53.12300 -9.62000  1.000 35.75000  ? 426 LYS A CD  1 
ATOM   3010  C  CE  . LYS A  1 395 ? -20.91700 -53.04700 -10.94300 1.000 40.47000  ? 426 LYS A CE  1 
ATOM   3011  N  NZ  . LYS A  1 395 ? -20.70300 -51.62500 -11.36200 1.000 45.57000  ? 426 LYS A NZ  1 
ATOM   3012  N  N   . ILE A  1 396 ? -21.03000 -57.31300 -8.34300  1.000 41.41000  ? 427 ILE A N   1 
ATOM   3013  C  CA  . ILE A  1 396 ? -19.61300 -57.63200 -8.32300  1.000 40.43000  ? 427 ILE A CA  1 
ATOM   3014  C  C   . ILE A  1 396 ? -18.91700 -56.79700 -9.39400  1.000 44.89000  ? 427 ILE A C   1 
ATOM   3015  O  O   . ILE A  1 396 ? -19.47700 -56.51800 -10.46700 1.000 39.85000  ? 427 ILE A O   1 
ATOM   3016  C  CB  . ILE A  1 396 ? -19.34700 -59.13100 -8.54000  1.000 42.71000  ? 427 ILE A CB  1 
ATOM   3017  C  CG1 . ILE A  1 396 ? -20.01800 -59.62500 -9.81800  1.000 42.06000  ? 427 ILE A CG1 1 
ATOM   3018  C  CG2 . ILE A  1 396 ? -19.86900 -59.91400 -7.33100  1.000 49.54000  ? 427 ILE A CG2 1 
ATOM   3019  C  CD1 . ILE A  1 396 ? -19.57200 -61.03800 -10.23600 1.000 43.14000  ? 427 ILE A CD1 1 
ATOM   3020  N  N   . THR A  1 397 ? -17.66500 -56.43200 -9.10600  1.000 38.61000  ? 428 THR A N   1 
ATOM   3021  C  CA  . THR A  1 397 ? -16.88500 -55.54200 -9.95500  1.000 39.23000  ? 428 THR A CA  1 
ATOM   3022  C  C   . THR A  1 397 ? -15.44600 -56.03400 -9.96300  1.000 43.31000  ? 428 THR A C   1 
ATOM   3023  O  O   . THR A  1 397 ? -14.86900 -56.28600 -8.89500  1.000 44.56000  ? 428 THR A O   1 
ATOM   3024  C  CB  . THR A  1 397 ? -16.89900 -54.10100 -9.43400  1.000 37.78000  ? 428 THR A CB  1 
ATOM   3025  O  OG1 . THR A  1 397 ? -18.22700 -53.69800 -9.13700  1.000 45.08000  ? 428 THR A OG1 1 
ATOM   3026  C  CG2 . THR A  1 397 ? -16.36300 -53.15300 -10.48000 1.000 41.64000  ? 428 THR A CG2 1 
ATOM   3027  N  N   . ARG A  1 398 ? -14.86700 -56.15600 -11.15500 1.000 37.92000  ? 429 ARG A N   1 
ATOM   3028  C  CA  . ARG A  1 398 ? -13.41700 -56.26900 -11.29400 1.000 44.28000  ? 429 ARG A CA  1 
ATOM   3029  C  C   . ARG A  1 398 ? -12.92100 -55.18800 -12.24400 1.000 39.39000  ? 429 ARG A C   1 
ATOM   3030  O  O   . ARG A  1 398 ? -13.35800 -55.13000 -13.39700 1.000 37.89000  ? 429 ARG A O   1 
ATOM   3031  C  CB  . ARG A  1 398 ? -12.98200 -57.64600 -11.78900 1.000 38.93000  ? 429 ARG A CB  1 
ATOM   3032  C  CG  . ARG A  1 398 ? -11.52100 -57.92300 -11.43800 1.000 41.46000  ? 429 ARG A CG  1 
ATOM   3033  C  CD  . ARG A  1 398 ? -11.01600 -59.25500 -11.94400 1.000 37.85000  ? 429 ARG A CD  1 
ATOM   3034  N  NE  . ARG A  1 398 ? -9.59000  -59.39700 -11.68800 1.000 42.42000  ? 429 ARG A NE  1 
ATOM   3035  C  CZ  . ARG A  1 398 ? -8.87500  -60.44900 -12.06400 1.000 45.56000  ? 429 ARG A CZ  1 
ATOM   3036  N  NH1 . ARG A  1 398 ? -9.43500  -61.47600 -12.68600 1.000 38.73000  ? 429 ARG A NH1 1 
ATOM   3037  N  NH2 . ARG A  1 398 ? -7.57100  -60.47000 -11.81100 1.000 40.11000  ? 429 ARG A NH2 1 
ATOM   3038  N  N   . MET A  1 399 ? -12.01700 -54.33200 -11.75500 1.000 37.69000  ? 430 MET A N   1 
ATOM   3039  C  CA  . MET A  1 399 ? -11.45700 -53.24500 -12.54600 1.000 39.67000  ? 430 MET A CA  1 
ATOM   3040  C  C   . MET A  1 399 ? -9.93000  -53.31600 -12.52900 1.000 44.00000  ? 430 MET A C   1 
ATOM   3041  O  O   . MET A  1 399 ? -9.32100  -53.49200 -11.46900 1.000 36.48000  ? 430 MET A O   1 
ATOM   3042  C  CB  . MET A  1 399 ? -11.92900 -51.88200 -12.00100 1.000 34.39000  ? 430 MET A CB  1 
ATOM   3043  C  CG  . MET A  1 399 ? -13.29600 -51.44700 -12.56100 1.000 42.23000  ? 430 MET A CG  1 
ATOM   3044  S  SD  . MET A  1 399 ? -13.24500 -51.24600 -14.34800 1.000 39.28000  ? 430 MET A SD  1 
ATOM   3045  C  CE  . MET A  1 399 ? -12.20300 -49.77900 -14.47600 1.000 42.17000  ? 430 MET A CE  1 
ATOM   3046  N  N   . GLY A  1 400 ? -9.31900  -53.13300 -13.70000 1.000 38.02000  ? 431 GLY A N   1 
ATOM   3047  C  CA  . GLY A  1 400 ? -7.88200  -53.09700 -13.80000 1.000 37.64000  ? 431 GLY A CA  1 
ATOM   3048  C  C   . GLY A  1 400 ? -7.18700  -54.37500 -13.41000 1.000 43.25000  ? 431 GLY A C   1 
ATOM   3049  O  O   . GLY A  1 400 ? -5.97500  -54.35800 -13.15700 1.000 39.80000  ? 431 GLY A O   1 
ATOM   3050  N  N   . ASN A  1 401 ? -7.91800  -55.49000 -13.38300 1.000 38.39000  ? 432 ASN A N   1 
ATOM   3051  C  CA  . ASN A  1 401 ? -7.42800  -56.80700 -12.97300 1.000 42.15000  ? 432 ASN A CA  1 
ATOM   3052  C  C   . ASN A  1 401 ? -7.11000  -56.87400 -11.48400 1.000 38.24000  ? 432 ASN A C   1 
ATOM   3053  O  O   . ASN A  1 401 ? -6.47500  -57.81700 -11.03200 1.000 38.36000  ? 432 ASN A O   1 
ATOM   3054  C  CB  . ASN A  1 401 ? -6.20500  -57.24900 -13.80000 1.000 43.65000  ? 432 ASN A CB  1 
ATOM   3055  C  CG  . ASN A  1 401 ? -6.31500  -58.69400 -14.29200 1.000 48.93000  ? 432 ASN A CG  1 
ATOM   3056  O  OD1 . ASN A  1 401 ? -7.41800  -59.21000 -14.49300 1.000 43.11000  ? 432 ASN A OD1 1 
ATOM   3057  N  ND2 . ASN A  1 401 ? -5.16900  -59.34700 -14.49000 1.000 44.03000  ? 432 ASN A ND2 1 
ATOM   3058  N  N   . GLU A  1 402 ? -7.61500  -55.93100 -10.69200 1.000 41.37000  ? 433 GLU A N   1 
ATOM   3059  C  CA  . GLU A  1 402 ? -7.46500  -55.98700 -9.24400  1.000 43.55000  ? 433 GLU A CA  1 
ATOM   3060  C  C   . GLU A  1 402 ? -8.29600  -57.13800 -8.64500  1.000 39.68000  ? 433 GLU A C   1 
ATOM   3061  O  O   . GLU A  1 402 ? -9.02700  -57.82400 -9.35400  1.000 37.69000  ? 433 GLU A O   1 
ATOM   3062  C  CB  . GLU A  1 402 ? -7.87200  -54.64300 -8.63600  1.000 37.90000  ? 433 GLU A CB  1 
ATOM   3063  C  CG  . GLU A  1 402 ? -6.81000  -53.58100 -8.84000  1.000 36.58000  ? 433 GLU A CG  1 
ATOM   3064  C  CD  . GLU A  1 402 ? -5.54000  -53.92000 -8.09100  1.000 41.59000  ? 433 GLU A CD  1 
ATOM   3065  O  OE1 . GLU A  1 402 ? -5.58700  -53.99900 -6.84100  1.000 52.86000  ? 433 GLU A OE1 1 
ATOM   3066  O  OE2 . GLU A  1 402 ? -4.48700  -54.11400 -8.74700  1.000 44.33000  ? 433 GLU A OE2 1 
ATOM   3067  N  N   . PRO A  1 403 ? -8.16400  -57.40700 -7.34600  1.000 35.81000  ? 434 PRO A N   1 
ATOM   3068  C  CA  . PRO A  1 403 ? -9.05000  -58.40000 -6.71600  1.000 45.98000  ? 434 PRO A CA  1 
ATOM   3069  C  C   . PRO A  1 403 ? -10.53200 -58.05600 -6.89600  1.000 42.73000  ? 434 PRO A C   1 
ATOM   3070  O  O   . PRO A  1 403 ? -10.92100 -56.89200 -7.03700  1.000 41.02000  ? 434 PRO A O   1 
ATOM   3071  C  CB  . PRO A  1 403 ? -8.64300  -58.36400 -5.23800  1.000 40.27000  ? 434 PRO A CB  1 
ATOM   3072  C  CG  . PRO A  1 403 ? -7.20700  -57.85600 -5.23300  1.000 47.46000  ? 434 PRO A CG  1 
ATOM   3073  C  CD  . PRO A  1 403 ? -7.02400  -57.02700 -6.47700  1.000 44.85000  ? 434 PRO A CD  1 
ATOM   3074  N  N   . TRP A  1 404 ? -11.35900 -59.09500 -6.91300  1.000 37.37000  ? 435 TRP A N   1 
ATOM   3075  C  CA  . TRP A  1 404 ? -12.79800 -58.90400 -7.06700  1.000 39.37000  ? 435 TRP A CA  1 
ATOM   3076  C  C   . TRP A  1 404 ? -13.39700 -58.10900 -5.91600  1.000 37.45000  ? 435 TRP A C   1 
ATOM   3077  O  O   . TRP A  1 404 ? -13.02700 -58.27900 -4.75000  1.000 44.51000  ? 435 TRP A O   1 
ATOM   3078  C  CB  . TRP A  1 404 ? -13.50800 -60.25000 -7.16600  1.000 40.68000  ? 435 TRP A CB  1 
ATOM   3079  C  CG  . TRP A  1 404 ? -13.45200 -60.85000 -8.51300  1.000 38.56000  ? 435 TRP A CG  1 
ATOM   3080  C  CD1 . TRP A  1 404 ? -12.52700 -61.73300 -8.97800  1.000 34.76000  ? 435 TRP A CD1 1 
ATOM   3081  C  CD2 . TRP A  1 404 ? -14.35000 -60.58700 -9.60100  1.000 38.20000  ? 435 TRP A CD2 1 
ATOM   3082  N  NE1 . TRP A  1 404 ? -12.81200 -62.07400 -10.28600 1.000 43.32000  ? 435 TRP A NE1 1 
ATOM   3083  C  CE2 . TRP A  1 404 ? -13.92000 -61.37200 -10.69600 1.000 38.46000  ? 435 TRP A CE2 1 
ATOM   3084  C  CE3 . TRP A  1 404 ? -15.47200 -59.77000 -9.75300  1.000 39.16000  ? 435 TRP A CE3 1 
ATOM   3085  C  CZ2 . TRP A  1 404 ? -14.57000 -61.35800 -11.92700 1.000 39.82000  ? 435 TRP A CZ2 1 
ATOM   3086  C  CZ3 . TRP A  1 404 ? -16.14000 -59.76900 -10.97400 1.000 40.35000  ? 435 TRP A CZ3 1 
ATOM   3087  C  CH2 . TRP A  1 404 ? -15.69000 -60.56000 -12.04700 1.000 43.09000  ? 435 TRP A CH2 1 
ATOM   3088  N  N   . ARG A  1 405 ? -14.37900 -57.28300 -6.24500  1.000 41.98000  ? 436 ARG A N   1 
ATOM   3089  C  CA  . ARG A  1 405 ? -15.11200 -56.50100 -5.26500  1.000 41.83000  ? 436 ARG A CA  1 
ATOM   3090  C  C   . ARG A  1 405 ? -16.56800 -56.92600 -5.29000  1.000 45.77000  ? 436 ARG A C   1 
ATOM   3091  O  O   . ARG A  1 405 ? -17.11400 -57.29000 -6.34100  1.000 39.46000  ? 436 ARG A O   1 
ATOM   3092  C  CB  . ARG A  1 405 ? -15.02300 -54.99200 -5.53800  1.000 39.82000  ? 436 ARG A CB  1 
ATOM   3093  C  CG  . ARG A  1 405 ? -13.59700 -54.52100 -5.70500  1.000 41.75000  ? 436 ARG A CG  1 
ATOM   3094  C  CD  . ARG A  1 405 ? -13.51600 -53.08400 -6.19600  1.000 43.95000  ? 436 ARG A CD  1 
ATOM   3095  N  NE  . ARG A  1 405 ? -14.08100 -52.11900 -5.26200  1.000 45.35000  ? 436 ARG A NE  1 
ATOM   3096  C  CZ  . ARG A  1 405 ? -13.38900 -51.53200 -4.29500  1.000 48.95000  ? 436 ARG A CZ  1 
ATOM   3097  N  NH1 . ARG A  1 405 ? -12.12300 -51.85000 -4.06500  1.000 45.47000  ? 436 ARG A NH1 1 
ATOM   3098  N  NH2 . ARG A  1 405 ? -13.99000 -50.62600 -3.52300  1.000 44.52000  ? 436 ARG A NH2 1 
ATOM   3099  N  N   . LEU A  1 406 ? -17.17600 -56.88600 -4.10700  1.000 46.96000  ? 437 LEU A N   1 
ATOM   3100  C  CA  . LEU A  1 406 ? -18.59000 -57.15000 -3.91700  1.000 42.04000  ? 437 LEU A CA  1 
ATOM   3101  C  C   . LEU A  1 406 ? -19.20300 -55.93600 -3.24100  1.000 41.55000  ? 437 LEU A C   1 
ATOM   3102  O  O   . LEU A  1 406 ? -18.77000 -55.55200 -2.15200  1.000 44.63000  ? 437 LEU A O   1 
ATOM   3103  C  CB  . LEU A  1 406 ? -18.79100 -58.39900 -3.05400  1.000 40.89000  ? 437 LEU A CB  1 
ATOM   3104  C  CG  . LEU A  1 406 ? -20.22700 -58.71200 -2.64300  1.000 45.28000  ? 437 LEU A CG  1 
ATOM   3105  C  CD1 . LEU A  1 406 ? -21.01900 -59.17400 -3.87600  1.000 41.68000  ? 437 LEU A CD1 1 
ATOM   3106  C  CD2 . LEU A  1 406 ? -20.30800 -59.74500 -1.50500  1.000 44.57000  ? 437 LEU A CD2 1 
ATOM   3107  N  N   . HIS A  1 407 ? -20.24000 -55.36800 -3.85300  1.000 42.34000  ? 438 HIS A N   1 
ATOM   3108  C  CA  . HIS A  1 407 ? -20.90400 -54.20600 -3.28200  1.000 45.22000  ? 438 HIS A CA  1 
ATOM   3109  C  C   . HIS A  1 407 ? -22.40400 -54.40300 -3.13200  1.000 44.58000  ? 438 HIS A C   1 
ATOM   3110  O  O   . HIS A  1 407 ? -23.06100 -55.03800 -3.96500  1.000 42.37000  ? 438 HIS A O   1 
ATOM   3111  C  CB  . HIS A  1 407 ? -20.64800 -52.94600 -4.10700  1.000 37.64000  ? 438 HIS A CB  1 
ATOM   3112  C  CG  . HIS A  1 407 ? -19.19900 -52.60400 -4.19700  1.000 49.54000  ? 438 HIS A CG  1 
ATOM   3113  N  ND1 . HIS A  1 407 ? -18.51700 -52.02100 -3.15000  1.000 47.40000  ? 438 HIS A ND1 1 
ATOM   3114  C  CD2 . HIS A  1 407 ? -18.29100 -52.80100 -5.17900  1.000 41.65000  ? 438 HIS A CD2 1 
ATOM   3115  C  CE1 . HIS A  1 407 ? -17.25300 -51.86600 -3.48900  1.000 45.71000  ? 438 HIS A CE1 1 
ATOM   3116  N  NE2 . HIS A  1 407 ? -17.09000 -52.32900 -4.71300  1.000 41.47000  ? 438 HIS A NE2 1 
ATOM   3117  N  N   . ASN A  1 408 ? -22.92900 -53.83300 -2.05400  1.000 42.54000  ? 439 ASN A N   1 
ATOM   3118  C  CA  . ASN A  1 408 ? -24.35200 -53.57900 -1.91600  1.000 42.48000  ? 439 ASN A CA  1 
ATOM   3119  C  C   . ASN A  1 408 ? -24.55400 -52.20800 -2.54700  1.000 43.14000  ? 439 ASN A C   1 
ATOM   3120  O  O   . ASN A  1 408 ? -24.39800 -51.17700 -1.87500  1.000 38.37000  ? 439 ASN A O   1 
ATOM   3121  C  CB  . ASN A  1 408 ? -24.74600 -53.61100 -0.44000  1.000 39.20000  ? 439 ASN A CB  1 
ATOM   3122  C  CG  . ASN A  1 408 ? -26.25000 -53.49700 -0.22200  1.000 52.34000  ? 439 ASN A CG  1 
ATOM   3123  O  OD1 . ASN A  1 408 ? -26.89000 -52.52600 -0.64300  1.000 48.33000  ? 439 ASN A OD1 1 
ATOM   3124  N  ND2 . ASN A  1 408 ? -26.81500 -54.47600 0.47200   1.000 53.25000  ? 439 ASN A ND2 1 
ATOM   3125  N  N   . ILE A  1 409 ? -24.86900 -52.18300 -3.85900  1.000 41.04000  ? 440 ILE A N   1 
ATOM   3126  C  CA  . ILE A  1 409 ? -24.92900 -50.88900 -4.56200  1.000 40.92000  ? 440 ILE A CA  1 
ATOM   3127  C  C   . ILE A  1 409 ? -26.12100 -50.07800 -4.09200  1.000 45.39000  ? 440 ILE A C   1 
ATOM   3128  O  O   . ILE A  1 409 ? -26.19900 -48.88200 -4.38100  1.000 48.80000  ? 440 ILE A O   1 
ATOM   3129  C  CB  . ILE A  1 409 ? -24.94000 -50.95400 -6.11500  1.000 40.31000  ? 440 ILE A CB  1 
ATOM   3130  C  CG1 . ILE A  1 409 ? -25.56400 -52.23000 -6.63700  1.000 45.34000  ? 440 ILE A CG1 1 
ATOM   3131  C  CG2 . ILE A  1 409 ? -23.53600 -50.65200 -6.76000  1.000 38.08000  ? 440 ILE A CG2 1 
ATOM   3132  C  CD1 . ILE A  1 409 ? -27.00100 -52.32300 -6.32100  1.000 47.96000  ? 440 ILE A CD1 1 
ATOM   3133  N  N   . THR A  1 410 ? -27.09600 -50.70600 -3.43500  1.000 42.33000  ? 441 THR A N   1 
ATOM   3134  C  CA  . THR A  1 410 ? -28.19900 -49.91600 -2.91400  1.000 45.44000  ? 441 THR A CA  1 
ATOM   3135  C  C   . THR A  1 410 ? -27.76200 -49.13100 -1.69200  1.000 40.76000  ? 441 THR A C   1 
ATOM   3136  O  O   . THR A  1 410 ? -28.14300 -47.96800 -1.52100  1.000 46.42000  ? 441 THR A O   1 
ATOM   3137  C  CB  . THR A  1 410 ? -29.39800 -50.80900 -2.60000  1.000 50.55000  ? 441 THR A CB  1 
ATOM   3138  O  OG1 . THR A  1 410 ? -29.78800 -51.49300 -3.79800  1.000 49.16000  ? 441 THR A OG1 1 
ATOM   3139  C  CG2 . THR A  1 410 ? -30.57000 -49.96800 -2.10700  1.000 43.71000  ? 441 THR A CG2 1 
ATOM   3140  N  N   . GLN A  1 411 ? -26.90800 -49.71100 -0.87000  1.000 43.47000  ? 442 GLN A N   1 
ATOM   3141  C  CA  . GLN A  1 411 ? -26.41900 -48.99000 0.29700   1.000 45.12000  ? 442 GLN A CA  1 
ATOM   3142  C  C   . GLN A  1 411 ? -25.11400 -48.24400 0.02500   1.000 48.48000  ? 442 GLN A C   1 
ATOM   3143  O  O   . GLN A  1 411 ? -24.80400 -47.28300 0.74500   1.000 43.88000  ? 442 GLN A O   1 
ATOM   3144  C  CB  . GLN A  1 411 ? -26.22100 -49.97100 1.46600   1.000 48.42000  ? 442 GLN A CB  1 
ATOM   3145  C  CG  . GLN A  1 411 ? -27.12900 -49.71900 2.66700   1.000 57.50000  ? 442 GLN A CG  1 
ATOM   3146  C  CD  . GLN A  1 411 ? -28.60600 -49.88500 2.33100   1.000 66.54000  ? 442 GLN A CD  1 
ATOM   3147  O  OE1 . GLN A  1 411 ? -28.99900 -50.86500 1.69700   1.000 70.60000  ? 442 GLN A OE1 1 
ATOM   3148  N  NE2 . GLN A  1 411 ? -29.42900 -48.92100 2.74700   1.000 72.85000  ? 442 GLN A NE2 1 
ATOM   3149  N  N   . ASP A  1 412 ? -24.35700 -48.65500 -1.03100  1.000 44.11000  ? 443 ASP A N   1 
ATOM   3150  C  CA  . ASP A  1 412 ? -22.97800 -48.20300 -1.33100  1.000 45.64000  ? 443 ASP A CA  1 
ATOM   3151  C  C   . ASP A  1 412 ? -22.89900 -47.92500 -2.83500  1.000 43.22000  ? 443 ASP A C   1 
ATOM   3152  O  O   . ASP A  1 412 ? -22.24000 -48.63600 -3.60000  1.000 36.56000  ? 443 ASP A O   1 
ATOM   3153  C  CB  . ASP A  1 412 ? -21.97300 -49.27700 -0.91500  1.000 44.73000  ? 443 ASP A CB  1 
ATOM   3154  C  CG  . ASP A  1 412 ? -20.54900 -48.96800 -1.33200  1.000 45.54000  ? 443 ASP A CG  1 
ATOM   3155  O  OD1 . ASP A  1 412 ? -20.17200 -47.77400 -1.48700  1.000 47.51000  ? 443 ASP A OD1 1 
ATOM   3156  O  OD2 . ASP A  1 412 ? -19.83200 -49.96700 -1.57200  1.000 43.55000  ? 443 ASP A OD2 1 
ATOM   3157  N  N   . ILE A  1 413 ? -23.62800 -46.90000 -3.27800  1.000 38.64000  ? 444 ILE A N   1 
ATOM   3158  C  CA  . ILE A  1 413 ? -23.76400 -46.64600 -4.70800  1.000 41.45000  ? 444 ILE A CA  1 
ATOM   3159  C  C   . ILE A  1 413 ? -22.42600 -46.26700 -5.34600  1.000 42.93000  ? 444 ILE A C   1 
ATOM   3160  O  O   . ILE A  1 413 ? -22.19700 -46.54900 -6.52900  1.000 36.47000  ? 444 ILE A O   1 
ATOM   3161  C  CB  . ILE A  1 413 ? -24.84800 -45.57500 -4.92700  1.000 44.32000  ? 444 ILE A CB  1 
ATOM   3162  C  CG1 . ILE A  1 413 ? -25.24900 -45.50900 -6.41000  1.000 43.37000  ? 444 ILE A CG1 1 
ATOM   3163  C  CG2 . ILE A  1 413 ? -24.38900 -44.24000 -4.36000  1.000 33.66000  ? 444 ILE A CG2 1 
ATOM   3164  C  CD1 . ILE A  1 413 ? -26.56500 -44.79700 -6.64700  1.000 43.44000  ? 444 ILE A CD1 1 
ATOM   3165  N  N   . GLY A  1 414 ? -21.50800 -45.67200 -4.57300  1.000 42.62000  ? 445 GLY A N   1 
ATOM   3166  C  CA  . GLY A  1 414 ? -20.18800 -45.31100 -5.05000  1.000 43.62000  ? 445 GLY A CA  1 
ATOM   3167  C  C   . GLY A  1 414 ? -19.15400 -46.42700 -5.05100  1.000 44.81000  ? 445 GLY A C   1 
ATOM   3168  O  O   . GLY A  1 414 ? -17.98600 -46.17000 -5.36600  1.000 42.67000  ? 445 GLY A O   1 
ATOM   3169  N  N   . GLU A  1 415 ? -19.54600 -47.65000 -4.68600  1.000 42.06000  ? 446 GLU A N   1 
ATOM   3170  C  CA  . GLU A  1 415 ? -18.66100 -48.82300 -4.68500  1.000 46.26000  ? 446 GLU A CA  1 
ATOM   3171  C  C   . GLU A  1 415 ? -17.38900 -48.56500 -3.86800  1.000 42.93000  ? 446 GLU A C   1 
ATOM   3172  O  O   . GLU A  1 415 ? -16.26400 -48.87300 -4.27700  1.000 41.90000  ? 446 GLU A O   1 
ATOM   3173  C  CB  . GLU A  1 415 ? -18.33200 -49.25100 -6.11800  1.000 38.44000  ? 446 GLU A CB  1 
ATOM   3174  C  CG  . GLU A  1 415 ? -19.57700 -49.69400 -6.86600  1.000 41.33000  ? 446 GLU A CG  1 
ATOM   3175  C  CD  . GLU A  1 415 ? -19.33700 -49.87300 -8.36000  1.000 42.09000  ? 446 GLU A CD  1 
ATOM   3176  O  OE1 . GLU A  1 415 ? -19.27400 -48.83600 -9.05500  1.000 34.54000  ? 446 GLU A OE1 1 
ATOM   3177  O  OE2 . GLU A  1 415 ? -19.24500 -51.04000 -8.83400  1.000 40.62000  ? 446 GLU A OE2 1 
ATOM   3178  N  N   . LYS A  1 416 ? -17.57800 -48.02400 -2.66900  1.000 43.63000  ? 447 LYS A N   1 
ATOM   3179  C  CA  . LYS A  1 416 ? -16.44100 -47.72700 -1.81400  1.000 43.21000  ? 447 LYS A CA  1 
ATOM   3180  C  C   . LYS A  1 416 ? -16.09500 -48.84600 -0.83900  1.000 44.85000  ? 447 LYS A C   1 
ATOM   3181  O  O   . LYS A  1 416 ? -14.93000 -48.95000 -0.43900  1.000 43.79000  ? 447 LYS A O   1 
ATOM   3182  C  CB  . LYS A  1 416 ? -16.69300 -46.46000 -1.00200  1.000 41.99000  ? 447 LYS A CB  1 
ATOM   3183  C  CG  . LYS A  1 416 ? -16.71100 -45.17400 -1.76700  1.000 30.55000  ? 447 LYS A CG  1 
ATOM   3184  C  CD  . LYS A  1 416 ? -17.10600 -44.05600 -0.79100  1.000 41.92000  ? 447 LYS A CD  1 
ATOM   3185  C  CE  . LYS A  1 416 ? -16.82300 -42.67000 -1.34200  1.000 49.49000  ? 447 LYS A CE  1 
ATOM   3186  N  NZ  . LYS A  1 416 ? -17.64300 -42.53900 -2.57800  1.000 52.98000  ? 447 LYS A NZ  1 
ATOM   3187  N  N   . LYS A  1 417 ? -17.06800 -49.67300 -0.42700  1.000 41.43000  ? 448 LYS A N   1 
ATOM   3188  C  CA  . LYS A  1 417 ? -16.87700 -50.64300 0.65600   1.000 43.28000  ? 448 LYS A CA  1 
ATOM   3189  C  C   . LYS A  1 417 ? -16.95300 -52.06700 0.09900   1.000 48.26000  ? 448 LYS A C   1 
ATOM   3190  O  O   . LYS A  1 417 ? -18.04300 -52.58300 -0.16600  1.000 51.47000  ? 448 LYS A O   1 
ATOM   3191  C  CB  . LYS A  1 417 ? -17.91100 -50.41500 1.75500   1.000 42.93000  ? 448 LYS A CB  1 
ATOM   3192  N  N   . ASN A  1 418 ? -15.79400 -52.71200 -0.05300  1.000 40.15000  ? 449 ASN A N   1 
ATOM   3193  C  CA  . ASN A  1 418 ? -15.73200 -54.06900 -0.58300  1.000 42.37000  ? 449 ASN A CA  1 
ATOM   3194  C  C   . ASN A  1 418 ? -16.18900 -55.05900 0.49000   1.000 46.46000  ? 449 ASN A C   1 
ATOM   3195  O  O   . ASN A  1 418 ? -15.62000 -55.10500 1.57500   1.000 44.88000  ? 449 ASN A O   1 
ATOM   3196  C  CB  . ASN A  1 418 ? -14.31600 -54.37500 -1.05800  1.000 37.03000  ? 449 ASN A CB  1 
ATOM   3197  C  CG  . ASN A  1 418 ? -14.22600 -55.69000 -1.78600  1.000 46.64000  ? 449 ASN A CG  1 
ATOM   3198  O  OD1 . ASN A  1 418 ? -15.24900 -56.34800 -2.00900  1.000 45.88000  ? 449 ASN A OD1 1 
ATOM   3199  N  ND2 . ASN A  1 418 ? -13.00200 -56.08600 -2.17900  1.000 38.11000  ? 449 ASN A ND2 1 
ATOM   3200  N  N   . LEU A  1 419 ? -17.24600 -55.81200 0.21000   1.000 48.91000  ? 450 LEU A N   1 
ATOM   3201  C  CA  . LEU A  1 419 ? -17.76900 -56.79900 1.14900   1.000 40.66000  ? 450 LEU A CA  1 
ATOM   3202  C  C   . LEU A  1 419 ? -17.41600 -58.21900 0.72800   1.000 43.87000  ? 450 LEU A C   1 
ATOM   3203  O  O   . LEU A  1 419 ? -18.02500 -59.16800 1.22700   1.000 49.19000  ? 450 LEU A O   1 
ATOM   3204  C  CB  . LEU A  1 419 ? -19.29100 -56.65100 1.26000   1.000 45.14000  ? 450 LEU A CB  1 
ATOM   3205  C  CG  . LEU A  1 419 ? -19.84900 -55.27800 1.65200   1.000 45.44000  ? 450 LEU A CG  1 
ATOM   3206  C  CD1 . LEU A  1 419 ? -21.37500 -55.27700 1.60300   1.000 47.65000  ? 450 LEU A CD1 1 
ATOM   3207  C  CD2 . LEU A  1 419 ? -19.35600 -54.80100 3.01400   1.000 48.14000  ? 450 LEU A CD2 1 
ATOM   3208  N  N   . ALA A  1 420 ? -16.48500 -58.38400 -0.22000  1.000 47.84000  ? 451 ALA A N   1 
ATOM   3209  C  CA  . ALA A  1 420 ? -16.11800 -59.71700 -0.70200  1.000 52.08000  ? 451 ALA A CA  1 
ATOM   3210  C  C   . ALA A  1 420 ? -15.60400 -60.61900 0.41800   1.000 53.01000  ? 451 ALA A C   1 
ATOM   3211  O  O   . ALA A  1 420 ? -15.83700 -61.83300 0.38800   1.000 56.61000  ? 451 ALA A O   1 
ATOM   3212  C  CB  . ALA A  1 420 ? -15.08500 -59.61700 -1.81800  1.000 47.29000  ? 451 ALA A CB  1 
ATOM   3213  N  N   . GLY A  1 421 ? -14.88700 -60.06600 1.39700   1.000 53.46000  ? 452 GLY A N   1 
ATOM   3214  C  CA  . GLY A  1 421 ? -14.44200 -60.89000 2.51000   1.000 55.22000  ? 452 GLY A CA  1 
ATOM   3215  C  C   . GLY A  1 421 ? -15.59200 -61.27700 3.42700   1.000 56.89000  ? 452 GLY A C   1 
ATOM   3216  O  O   . GLY A  1 421 ? -15.63200 -62.38700 3.96000   1.000 59.82000  ? 452 GLY A O   1 
ATOM   3217  N  N   . ARG A  1 422 ? -16.54900 -60.37400 3.60900   1.000 55.27000  ? 453 ARG A N   1 
ATOM   3218  C  CA  . ARG A  1 422 ? -17.64100 -60.63500 4.53600   1.000 58.22000  ? 453 ARG A CA  1 
ATOM   3219  C  C   . ARG A  1 422 ? -18.63300 -61.65800 3.99300   1.000 56.58000  ? 453 ARG A C   1 
ATOM   3220  O  O   . ARG A  1 422 ? -19.18300 -62.44700 4.76700   1.000 62.51000  ? 453 ARG A O   1 
ATOM   3221  C  CB  . ARG A  1 422 ? -18.32100 -59.31700 4.88400   1.000 55.65000  ? 453 ARG A CB  1 
ATOM   3222  C  CG  . ARG A  1 422 ? -19.26800 -59.34600 6.05700   1.000 61.80000  ? 453 ARG A CG  1 
ATOM   3223  C  CD  . ARG A  1 422 ? -19.49200 -57.89900 6.42900   1.000 66.55000  ? 453 ARG A CD  1 
ATOM   3224  N  NE  . ARG A  1 422 ? -18.16300 -57.29800 6.54100   1.000 74.58000  ? 453 ARG A NE  1 
ATOM   3225  C  CZ  . ARG A  1 422 ? -17.89400 -55.99700 6.56800   1.000 75.72000  ? 453 ARG A CZ  1 
ATOM   3226  N  NH1 . ARG A  1 422 ? -18.85900 -55.09000 6.58400   1.000 72.03000  ? 453 ARG A NH1 1 
ATOM   3227  N  NH2 . ARG A  1 422 ? -16.62100 -55.59600 6.55700   1.000 75.30000  ? 453 ARG A NH2 1 
ATOM   3228  N  N   . TYR A  1 423 ? -18.88000 -61.67600 2.68800   1.000 57.01000  ? 454 TYR A N   1 
ATOM   3229  C  CA  . TYR A  1 423 ? -19.86000 -62.58600 2.09000   1.000 54.24000  ? 454 TYR A CA  1 
ATOM   3230  C  C   . TYR A  1 423 ? -19.26000 -63.36000 0.92800   1.000 53.34000  ? 454 TYR A C   1 
ATOM   3231  O  O   . TYR A  1 423 ? -19.69400 -63.22700 -0.21500  1.000 57.52000  ? 454 TYR A O   1 
ATOM   3232  C  CB  . TYR A  1 423 ? -21.09400 -61.82000 1.63700   1.000 52.28000  ? 454 TYR A CB  1 
ATOM   3233  C  CG  . TYR A  1 423 ? -21.70000 -60.99400 2.71700   1.000 55.88000  ? 454 TYR A CG  1 
ATOM   3234  C  CD1 . TYR A  1 423 ? -22.24700 -61.59700 3.84800   1.000 54.50000  ? 454 TYR A CD1 1 
ATOM   3235  C  CD2 . TYR A  1 423 ? -21.74200 -59.61800 2.61500   1.000 51.76000  ? 454 TYR A CD2 1 
ATOM   3236  C  CE1 . TYR A  1 423 ? -22.82400 -60.84100 4.85400   1.000 54.65000  ? 454 TYR A CE1 1 
ATOM   3237  C  CE2 . TYR A  1 423 ? -22.31900 -58.85100 3.61100   1.000 57.50000  ? 454 TYR A CE2 1 
ATOM   3238  C  CZ  . TYR A  1 423 ? -22.85600 -59.46600 4.73200   1.000 62.10000  ? 454 TYR A CZ  1 
ATOM   3239  O  OH  . TYR A  1 423 ? -23.41800 -58.69200 5.72700   1.000 62.13000  ? 454 TYR A OH  1 
ATOM   3240  N  N   . PRO A  1 424 ? -18.27000 -64.20800 1.19400   1.000 54.89000  ? 455 PRO A N   1 
ATOM   3241  C  CA  . PRO A  1 424 ? -17.62200 -64.92300 0.09300   1.000 51.60000  ? 455 PRO A CA  1 
ATOM   3242  C  C   . PRO A  1 424 ? -18.52800 -65.92800 -0.57200  1.000 58.84000  ? 455 PRO A C   1 
ATOM   3243  O  O   . PRO A  1 424 ? -18.27200 -66.29700 -1.72400  1.000 61.76000  ? 455 PRO A O   1 
ATOM   3244  C  CB  . PRO A  1 424 ? -16.42000 -65.59600 0.77400   1.000 51.60000  ? 455 PRO A CB  1 
ATOM   3245  C  CG  . PRO A  1 424 ? -16.87500 -65.80100 2.18700   1.000 54.18000  ? 455 PRO A CG  1 
ATOM   3246  C  CD  . PRO A  1 424 ? -17.70700 -64.57900 2.50700   1.000 54.26000  ? 455 PRO A CD  1 
ATOM   3247  N  N   . ASP A  1 425 ? -19.57800 -66.39700 0.10200   1.000 54.27000  ? 456 ASP A N   1 
ATOM   3248  C  CA  . ASP A  1 425 ? -20.50800 -67.28500 -0.58500  1.000 59.71000  ? 456 ASP A CA  1 
ATOM   3249  C  C   . ASP A  1 425 ? -21.24100 -66.55100 -1.70300  1.000 55.11000  ? 456 ASP A C   1 
ATOM   3250  O  O   . ASP A  1 425 ? -21.28800 -67.03000 -2.84000  1.000 58.31000  ? 456 ASP A O   1 
ATOM   3251  C  CB  . ASP A  1 425 ? -21.49400 -67.90800 0.40700   1.000 68.00000  ? 456 ASP A CB  1 
ATOM   3252  C  CG  . ASP A  1 425 ? -20.82300 -68.87300 1.37900   1.000 75.97000  ? 456 ASP A CG  1 
ATOM   3253  O  OD1 . ASP A  1 425 ? -19.67800 -69.31000 1.11000   1.000 68.27000  ? 456 ASP A OD1 1 
ATOM   3254  O  OD2 . ASP A  1 425 ? -21.45500 -69.21300 2.40500   1.000 81.52000  ? 456 ASP A OD2 1 
ATOM   3255  N  N   . ARG A  1 426 ? -21.82100 -65.38800 -1.40000  1.000 50.57000  ? 457 ARG A N   1 
ATOM   3256  C  CA  . ARG A  1 426 ? -22.51200 -64.62100 -2.43400  1.000 52.69000  ? 457 ARG A CA  1 
ATOM   3257  C  C   . ARG A  1 426 ? -21.56600 -64.24600 -3.56500  1.000 53.96000  ? 457 ARG A C   1 
ATOM   3258  O  O   . ARG A  1 426 ? -21.90400 -64.38700 -4.74400  1.000 56.01000  ? 457 ARG A O   1 
ATOM   3259  C  CB  . ARG A  1 426 ? -23.13100 -63.35800 -1.84300  1.000 56.66000  ? 457 ARG A CB  1 
ATOM   3260  C  CG  . ARG A  1 426 ? -23.99600 -62.59100 -2.82500  1.000 56.45000  ? 457 ARG A CG  1 
ATOM   3261  C  CD  . ARG A  1 426 ? -24.60300 -61.38900 -2.15400  1.000 54.96000  ? 457 ARG A CD  1 
ATOM   3262  N  NE  . ARG A  1 426 ? -25.50200 -61.79600 -1.08500  1.000 57.65000  ? 457 ARG A NE  1 
ATOM   3263  C  CZ  . ARG A  1 426 ? -26.74500 -62.20900 -1.27400  1.000 63.58000  ? 457 ARG A CZ  1 
ATOM   3264  N  NH1 . ARG A  1 426 ? -27.26000 -62.31400 -2.49000  1.000 62.17000  ? 457 ARG A NH1 1 
ATOM   3265  N  NH2 . ARG A  1 426 ? -27.48500 -62.54000 -0.21900  1.000 62.42000  ? 457 ARG A NH2 1 
ATOM   3266  N  N   . LEU A  1 427 ? -20.36400 -63.77000 -3.21800  1.000 53.08000  ? 458 LEU A N   1 
ATOM   3267  C  CA  . LEU A  1 427 ? -19.39800 -63.36800 -4.23400  1.000 53.30000  ? 458 LEU A CA  1 
ATOM   3268  C  C   . LEU A  1 427 ? -19.14900 -64.48600 -5.23000  1.000 52.24000  ? 458 LEU A C   1 
ATOM   3269  O  O   . LEU A  1 427 ? -19.21300 -64.27700 -6.44800  1.000 54.92000  ? 458 LEU A O   1 
ATOM   3270  C  CB  . LEU A  1 427 ? -18.08300 -62.94000 -3.57200  1.000 51.81000  ? 458 LEU A CB  1 
ATOM   3271  C  CG  . LEU A  1 427 ? -16.91900 -62.83000 -4.56500  1.000 43.79000  ? 458 LEU A CG  1 
ATOM   3272  C  CD1 . LEU A  1 427 ? -17.18300 -61.70700 -5.53400  1.000 52.70000  ? 458 LEU A CD1 1 
ATOM   3273  C  CD2 . LEU A  1 427 ? -15.57600 -62.62400 -3.85300  1.000 52.67000  ? 458 LEU A CD2 1 
ATOM   3274  N  N   . LYS A  1 428 ? -18.87600 -65.68800 -4.72200  1.000 58.37000  ? 459 LYS A N   1 
ATOM   3275  C  CA  . LYS A  1 428 ? -18.49800 -66.79400 -5.59000  1.000 59.28000  ? 459 LYS A CA  1 
ATOM   3276  C  C   . LYS A  1 428 ? -19.67500 -67.28000 -6.42900  1.000 57.86000  ? 459 LYS A C   1 
ATOM   3277  O  O   . LYS A  1 428 ? -19.47900 -67.72400 -7.56600  1.000 59.74000  ? 459 LYS A O   1 
ATOM   3278  C  CB  . LYS A  1 428 ? -17.94800 -67.95400 -4.75200  1.000 57.07000  ? 459 LYS A CB  1 
ATOM   3279  C  CG  . LYS A  1 428 ? -16.60900 -67.70900 -4.01800  1.000 66.06000  ? 459 LYS A CG  1 
ATOM   3280  C  CD  . LYS A  1 428 ? -15.38900 -67.90500 -4.91800  1.000 68.62000  ? 459 LYS A CD  1 
ATOM   3281  C  CE  . LYS A  1 428 ? -14.19600 -68.51100 -4.15800  1.000 60.72000  ? 459 LYS A CE  1 
ATOM   3282  N  NZ  . LYS A  1 428 ? -13.64400 -67.65000 -3.08100  1.000 64.07000  ? 459 LYS A NZ  1 
ATOM   3283  N  N   . GLU A  1 429 ? -20.90100 -67.20600 -5.90000  1.000 58.19000  ? 460 GLU A N   1 
ATOM   3284  C  CA  . GLU A  1 429 ? -22.05400 -67.60700 -6.70800  1.000 56.77000  ? 460 GLU A CA  1 
ATOM   3285  C  C   . GLU A  1 429 ? -22.32000 -66.59600 -7.82400  1.000 57.74000  ? 460 GLU A C   1 
ATOM   3286  O  O   . GLU A  1 429 ? -22.67700 -66.98300 -8.94300  1.000 60.19000  ? 460 GLU A O   1 
ATOM   3287  C  CB  . GLU A  1 429 ? -23.28800 -67.85200 -5.82000  1.000 57.29000  ? 460 GLU A CB  1 
ATOM   3288  C  CG  . GLU A  1 429 ? -24.13400 -66.64800 -5.44100  1.000 58.70000  ? 460 GLU A CG  1 
ATOM   3289  C  CD  . GLU A  1 429 ? -24.97000 -66.90200 -4.18600  1.000 71.14000  ? 460 GLU A CD  1 
ATOM   3290  O  OE1 . GLU A  1 429 ? -24.70200 -67.90700 -3.49300  1.000 78.44000  ? 460 GLU A OE1 1 
ATOM   3291  O  OE2 . GLU A  1 429 ? -25.89200 -66.10200 -3.88600  1.000 75.34000  ? 460 GLU A OE2 1 
ATOM   3292  N  N   . MET A  1 430 ? -22.13600 -65.29800 -7.55600  1.000 53.71000  ? 461 MET A N   1 
ATOM   3293  C  CA  . MET A  1 430 ? -22.31700 -64.32000 -8.62400  1.000 50.49000  ? 461 MET A CA  1 
ATOM   3294  C  C   . MET A  1 430 ? -21.23600 -64.46400 -9.69200  1.000 51.46000  ? 461 MET A C   1 
ATOM   3295  O  O   . MET A  1 430 ? -21.52000 -64.34200 -10.88800 1.000 53.95000  ? 461 MET A O   1 
ATOM   3296  C  CB  . MET A  1 430 ? -22.34200 -62.90400 -8.04600  1.000 45.29000  ? 461 MET A CB  1 
ATOM   3297  C  CG  . MET A  1 430 ? -23.60800 -62.63100 -7.24800  1.000 46.85000  ? 461 MET A CG  1 
ATOM   3298  S  SD  . MET A  1 430 ? -23.70600 -60.97800 -6.53400  1.000 52.01000  ? 461 MET A SD  1 
ATOM   3299  C  CE  . MET A  1 430 ? -24.17700 -60.02800 -7.99500  1.000 46.74000  ? 461 MET A CE  1 
ATOM   3300  N  N   . ILE A  1 431 ? -20.00400 -64.78200 -9.28800  1.000 53.78000  ? 462 ILE A N   1 
ATOM   3301  C  CA  . ILE A  1 431 ? -18.94300 -65.00700 -10.26700 1.000 52.35000  ? 462 ILE A CA  1 
ATOM   3302  C  C   . ILE A  1 431 ? -19.22300 -66.24600 -11.09800 1.000 54.54000  ? 462 ILE A C   1 
ATOM   3303  O  O   . ILE A  1 431 ? -18.98500 -66.26100 -12.31200 1.000 52.16000  ? 462 ILE A O   1 
ATOM   3304  C  CB  . ILE A  1 431 ? -17.57900 -65.08300 -9.56000  1.000 54.79000  ? 462 ILE A CB  1 
ATOM   3305  C  CG1 . ILE A  1 431 ? -17.14500 -63.66500 -9.19900  1.000 52.46000  ? 462 ILE A CG1 1 
ATOM   3306  C  CG2 . ILE A  1 431 ? -16.55600 -65.85500 -10.39800 1.000 54.35000  ? 462 ILE A CG2 1 
ATOM   3307  C  CD1 . ILE A  1 431 ? -15.86800 -63.56300 -8.51200  1.000 49.55000  ? 462 ILE A CD1 1 
ATOM   3308  N  N   . ALA A  1 432 ? -19.77200 -67.28700 -10.47300 1.000 55.59000  ? 463 ALA A N   1 
ATOM   3309  C  CA  . ALA A  1 432 ? -20.08100 -68.49700 -11.21800 1.000 57.13000  ? 463 ALA A CA  1 
ATOM   3310  C  C   . ALA A  1 432 ? -21.09500 -68.19600 -12.30800 1.000 54.81000  ? 463 ALA A C   1 
ATOM   3311  O  O   . ALA A  1 432 ? -20.93400 -68.61600 -13.46000 1.000 53.58000  ? 463 ALA A O   1 
ATOM   3312  C  CB  . ALA A  1 432 ? -20.59600 -69.58800 -10.27600 1.000 55.81000  ? 463 ALA A CB  1 
ATOM   3313  N  N   . LYS A  1 433 ? -22.15700 -67.46900 -11.96200 1.000 54.91000  ? 464 LYS A N   1 
ATOM   3314  C  CA  . LYS A  1 433 ? -23.16000 -67.16300 -12.97100 1.000 56.76000  ? 464 LYS A CA  1 
ATOM   3315  C  C   . LYS A  1 433 ? -22.57500 -66.27700 -14.06800 1.000 54.45000  ? 464 LYS A C   1 
ATOM   3316  O  O   . LYS A  1 433 ? -22.82200 -66.50700 -15.25400 1.000 57.93000  ? 464 LYS A O   1 
ATOM   3317  C  CB  . LYS A  1 433 ? -24.39400 -66.56100 -12.30300 1.000 54.26000  ? 464 LYS A CB  1 
ATOM   3318  C  CG  . LYS A  1 433 ? -25.59400 -66.70000 -13.17400 1.000 64.03000  ? 464 LYS A CG  1 
ATOM   3319  C  CD  . LYS A  1 433 ? -26.86500 -66.70400 -12.34600 1.000 67.35000  ? 464 LYS A CD  1 
ATOM   3320  C  CE  . LYS A  1 433 ? -28.06900 -66.91700 -13.25900 1.000 76.21000  ? 464 LYS A CE  1 
ATOM   3321  N  NZ  . LYS A  1 433 ? -28.02900 -68.27800 -13.92800 1.000 78.45000  ? 464 LYS A NZ  1 
ATOM   3322  N  N   . THR A  1 434 ? -21.76400 -65.28400 -13.69800 1.000 53.90000  ? 465 THR A N   1 
ATOM   3323  C  CA  . THR A  1 434 ? -21.14000 -64.42900 -14.70600 1.000 47.67000  ? 465 THR A CA  1 
ATOM   3324  C  C   . THR A  1 434 ? -20.20900 -65.21400 -15.62300 1.000 47.65000  ? 465 THR A C   1 
ATOM   3325  O  O   . THR A  1 434 ? -20.18900 -64.98700 -16.84000 1.000 49.57000  ? 465 THR A O   1 
ATOM   3326  C  CB  . THR A  1 434 ? -20.37500 -63.30600 -14.03000 1.000 45.29000  ? 465 THR A CB  1 
ATOM   3327  O  OG1 . THR A  1 434 ? -21.27300 -62.57400 -13.18700 1.000 47.12000  ? 465 THR A OG1 1 
ATOM   3328  C  CG2 . THR A  1 434 ? -19.78300 -62.38000 -15.08000 1.000 46.11000  ? 465 THR A CG2 1 
ATOM   3329  N  N   . GLN A  1 435 ? -19.42900 -66.14200 -15.06300 1.000 51.20000  ? 466 GLN A N   1 
ATOM   3330  C  CA  . GLN A  1 435 ? -18.55200 -66.96200 -15.89500 1.000 52.00000  ? 466 GLN A CA  1 
ATOM   3331  C  C   . GLN A  1 435 ? -19.34500 -67.79800 -16.89300 1.000 50.77000  ? 466 GLN A C   1 
ATOM   3332  O  O   . GLN A  1 435 ? -18.96800 -67.89500 -18.06800 1.000 53.78000  ? 466 GLN A O   1 
ATOM   3333  C  CB  . GLN A  1 435 ? -17.67600 -67.87800 -15.02500 1.000 48.09000  ? 466 GLN A CB  1 
ATOM   3334  C  CG  . GLN A  1 435 ? -16.70500 -68.70300 -15.87500 1.000 50.81000  ? 466 GLN A CG  1 
ATOM   3335  C  CD  . GLN A  1 435 ? -15.55100 -69.33300 -15.10200 1.000 60.07000  ? 466 GLN A CD  1 
ATOM   3336  O  OE1 . GLN A  1 435 ? -15.55600 -69.40000 -13.86600 1.000 58.27000  ? 466 GLN A OE1 1 
ATOM   3337  N  NE2 . GLN A  1 435 ? -14.55000 -69.80200 -15.83900 1.000 57.18000  ? 466 GLN A NE2 1 
ATOM   3338  N  N   . GLU A  1 436 ? -20.44400 -68.41500 -16.45000 1.000 51.18000  ? 467 GLU A N   1 
ATOM   3339  C  CA  . GLU A  1 436 ? -21.25400 -69.19100 -17.38700 1.000 57.40000  ? 467 GLU A CA  1 
ATOM   3340  C  C   . GLU A  1 436 ? -21.75800 -68.30900 -18.52300 1.000 54.26000  ? 467 GLU A C   1 
ATOM   3341  O  O   . GLU A  1 436 ? -21.76300 -68.72900 -19.68600 1.000 50.76000  ? 467 GLU A O   1 
ATOM   3342  C  CB  . GLU A  1 436 ? -22.40600 -69.88400 -16.66400 1.000 47.69000  ? 467 GLU A CB  1 
ATOM   3343  C  CG  . GLU A  1 436 ? -22.40100 -71.39600 -16.86200 1.000 63.47000  ? 467 GLU A CG  1 
ATOM   3344  C  CD  . GLU A  1 436 ? -22.66100 -71.82600 -18.31600 1.000 73.94000  ? 467 GLU A CD  1 
ATOM   3345  O  OE1 . GLU A  1 436 ? -23.71100 -71.44800 -18.88800 1.000 77.75000  ? 467 GLU A OE1 1 
ATOM   3346  O  OE2 . GLU A  1 436 ? -21.81400 -72.54900 -18.89200 1.000 79.00000  ? 467 GLU A OE2 1 
ATOM   3347  N  N   . TRP A  1 437 ? -22.16400 -67.07400 -18.20300 1.000 51.74000  ? 468 TRP A N   1 
ATOM   3348  C  CA  . TRP A  1 437 ? -22.54900 -66.11400 -19.23600 1.000 49.58000  ? 468 TRP A CA  1 
ATOM   3349  C  C   . TRP A  1 437 ? -21.45000 -65.94500 -20.28100 1.000 52.85000  ? 468 TRP A C   1 
ATOM   3350  O  O   . TRP A  1 437 ? -21.73700 -65.95000 -21.48400 1.000 55.92000  ? 468 TRP A O   1 
ATOM   3351  C  CB  . TRP A  1 437 ? -22.90600 -64.76900 -18.59700 1.000 50.71000  ? 468 TRP A CB  1 
ATOM   3352  C  CG  . TRP A  1 437 ? -23.13300 -63.63400 -19.57400 1.000 52.68000  ? 468 TRP A CG  1 
ATOM   3353  C  CD1 . TRP A  1 437 ? -24.07800 -63.55800 -20.55900 1.000 51.90000  ? 468 TRP A CD1 1 
ATOM   3354  C  CD2 . TRP A  1 437 ? -22.41200 -62.39000 -19.61700 1.000 54.00000  ? 468 TRP A CD2 1 
ATOM   3355  N  NE1 . TRP A  1 437 ? -23.97400 -62.35700 -21.23000 1.000 51.39000  ? 468 TRP A NE1 1 
ATOM   3356  C  CE2 . TRP A  1 437 ? -22.96800 -61.61800 -20.66000 1.000 48.92000  ? 468 TRP A CE2 1 
ATOM   3357  C  CE3 . TRP A  1 437 ? -21.34800 -61.85600 -18.87200 1.000 47.93000  ? 468 TRP A CE3 1 
ATOM   3358  C  CZ2 . TRP A  1 437 ? -22.48600 -60.35200 -20.98800 1.000 45.17000  ? 468 TRP A CZ2 1 
ATOM   3359  C  CZ3 . TRP A  1 437 ? -20.87400 -60.59900 -19.20100 1.000 44.66000  ? 468 TRP A CZ3 1 
ATOM   3360  C  CH2 . TRP A  1 437 ? -21.43800 -59.86400 -20.24600 1.000 46.84000  ? 468 TRP A CH2 1 
ATOM   3361  N  N   . THR A  1 438 ? -20.17600 -65.82000 -19.84900 1.000 52.20000  ? 469 THR A N   1 
ATOM   3362  C  CA  . THR A  1 438 ? -19.10400 -65.62200 -20.82600 1.000 53.77000  ? 469 THR A CA  1 
ATOM   3363  C  C   . THR A  1 438 ? -18.86300 -66.86000 -21.66900 1.000 51.62000  ? 469 THR A C   1 
ATOM   3364  O  O   . THR A  1 438 ? -18.25600 -66.75300 -22.73900 1.000 50.36000  ? 469 THR A O   1 
ATOM   3365  C  CB  . THR A  1 438 ? -17.76800 -65.21900 -20.15700 1.000 53.80000  ? 469 THR A CB  1 
ATOM   3366  O  OG1 . THR A  1 438 ? -17.26000 -66.29400 -19.34400 1.000 55.08000  ? 469 THR A OG1 1 
ATOM   3367  C  CG2 . THR A  1 438 ? -17.92000 -63.96200 -19.31000 1.000 45.88000  ? 469 THR A CG2 1 
ATOM   3368  N  N   . LYS A  1 439 ? -19.35300 -68.02200 -21.23600 1.000 48.57000  ? 470 LYS A N   1 
ATOM   3369  C  CA  . LYS A  1 439 ? -19.15800 -69.23000 -22.02400 1.000 51.13000  ? 470 LYS A CA  1 
ATOM   3370  C  C   . LYS A  1 439 ? -19.90600 -69.19100 -23.35500 1.000 57.53000  ? 470 LYS A C   1 
ATOM   3371  O  O   . LYS A  1 439 ? -19.53000 -69.92500 -24.27900 1.000 55.87000  ? 470 LYS A O   1 
ATOM   3372  C  CB  . LYS A  1 439 ? -19.54400 -70.45900 -21.19300 1.000 53.71000  ? 470 LYS A CB  1 
ATOM   3373  C  CG  . LYS A  1 439 ? -18.45800 -70.80900 -20.13600 1.000 56.51000  ? 470 LYS A CG  1 
ATOM   3374  C  CD  . LYS A  1 439 ? -18.71600 -72.11600 -19.39800 1.000 63.73000  ? 470 LYS A CD  1 
ATOM   3375  C  CE  . LYS A  1 439 ? -17.78300 -72.28400 -18.18300 1.000 66.78000  ? 470 LYS A CE  1 
ATOM   3376  N  NZ  . LYS A  1 439 ? -18.41300 -71.87300 -16.88000 1.000 64.08000  ? 470 LYS A NZ  1 
ATOM   3377  N  N   . SER A  1 440 ? -20.90600 -68.31900 -23.50300 1.000 53.39000  ? 471 SER A N   1 
ATOM   3378  C  CA  . SER A  1 440 ? -21.65500 -68.21700 -24.75700 1.000 54.90000  ? 471 SER A CA  1 
ATOM   3379  C  C   . SER A  1 440 ? -21.10400 -67.18100 -25.73500 1.000 55.60000  ? 471 SER A C   1 
ATOM   3380  O  O   . SER A  1 440 ? -21.70700 -66.99700 -26.79500 1.000 51.40000  ? 471 SER A O   1 
ATOM   3381  C  CB  . SER A  1 440 ? -23.11400 -67.86500 -24.48700 1.000 51.22000  ? 471 SER A CB  1 
ATOM   3382  O  OG  . SER A  1 440 ? -23.23600 -66.52900 -24.04400 1.000 62.14000  ? 471 SER A OG  1 
ATOM   3383  N  N   . PHE A  1 441 ? -19.99900 -66.50000 -25.41600 1.000 51.19000  ? 472 PHE A N   1 
ATOM   3384  C  CA  . PHE A  1 441 ? -19.53100 -65.38500 -26.23300 1.000 49.12000  ? 472 PHE A CA  1 
ATOM   3385  C  C   . PHE A  1 441 ? -18.99000 -65.89200 -27.56300 1.000 55.18000  ? 472 PHE A C   1 
ATOM   3386  O  O   . PHE A  1 441 ? -18.61800 -67.05700 -27.69900 1.000 60.83000  ? 472 PHE A O   1 
ATOM   3387  C  CB  . PHE A  1 441 ? -18.42900 -64.58800 -25.51800 1.000 41.99000  ? 472 PHE A CB  1 
ATOM   3388  C  CG  . PHE A  1 441 ? -18.91500 -63.76300 -24.35600 1.000 50.94000  ? 472 PHE A CG  1 
ATOM   3389  C  CD1 . PHE A  1 441 ? -20.23400 -63.81900 -23.93400 1.000 50.10000  ? 472 PHE A CD1 1 
ATOM   3390  C  CD2 . PHE A  1 441 ? -18.03900 -62.95200 -23.65600 1.000 55.07000  ? 472 PHE A CD2 1 
ATOM   3391  C  CE1 . PHE A  1 441 ? -20.67300 -63.06900 -22.84700 1.000 53.80000  ? 472 PHE A CE1 1 
ATOM   3392  C  CE2 . PHE A  1 441 ? -18.47500 -62.19600 -22.56500 1.000 46.92000  ? 472 PHE A CE2 1 
ATOM   3393  C  CZ  . PHE A  1 441 ? -19.79200 -62.25700 -22.16600 1.000 52.92000  ? 472 PHE A CZ  1 
ATOM   3394  N  N   . VAL A  1 442 ? -18.94800 -65.00000 -28.55200 1.000 52.64000  ? 473 VAL A N   1 
ATOM   3395  C  CA  . VAL A  1 442 ? -18.30600 -65.28100 -29.82700 1.000 48.94000  ? 473 VAL A CA  1 
ATOM   3396  C  C   . VAL A  1 442 ? -17.01900 -64.46100 -29.92800 1.000 57.33000  ? 473 VAL A C   1 
ATOM   3397  O  O   . VAL A  1 442 ? -16.76600 -63.54800 -29.14100 1.000 54.62000  ? 473 VAL A O   1 
ATOM   3398  C  CB  . VAL A  1 442 ? -19.22400 -64.99100 -31.02800 1.000 51.43000  ? 473 VAL A CB  1 
ATOM   3399  C  CG1 . VAL A  1 442 ? -20.57600 -65.72400 -30.88300 1.000 53.35000  ? 473 VAL A CG1 1 
ATOM   3400  C  CG2 . VAL A  1 442 ? -19.43200 -63.50600 -31.18300 1.000 52.32000  ? 473 VAL A CG2 1 
ATOM   3401  N  N   . LYS A  1 443 ? -16.21400 -64.78700 -30.92900 1.000 45.38000  ? 474 LYS A N   1 
ATOM   3402  C  CA  . LYS A  1 443 ? -15.01600 -64.02700 -31.20600 1.000 55.00000  ? 474 LYS A CA  1 
ATOM   3403  C  C   . LYS A  1 443 ? -15.38200 -62.66000 -31.78500 1.000 53.21000  ? 474 LYS A C   1 
ATOM   3404  O  O   . LYS A  1 443 ? -16.32800 -62.54900 -32.56900 1.000 57.56000  ? 474 LYS A O   1 
ATOM   3405  C  CB  . LYS A  1 443 ? -14.11000 -64.79000 -32.18200 1.000 51.55000  ? 474 LYS A CB  1 
ATOM   3406  N  N   . PRO A  1 444 ? -14.63700 -61.61400 -31.43700 1.000 53.39000  ? 475 PRO A N   1 
ATOM   3407  C  CA  . PRO A  1 444 ? -14.87200 -60.29800 -32.04000 1.000 49.24000  ? 475 PRO A CA  1 
ATOM   3408  C  C   . PRO A  1 444 ? -14.67300 -60.36500 -33.53900 1.000 47.58000  ? 475 PRO A C   1 
ATOM   3409  O  O   . PRO A  1 444 ? -13.72600 -60.98800 -34.01800 1.000 47.38000  ? 475 PRO A O   1 
ATOM   3410  C  CB  . PRO A  1 444 ? -13.79500 -59.41800 -31.39500 1.000 52.89000  ? 475 PRO A CB  1 
ATOM   3411  C  CG  . PRO A  1 444 ? -13.38900 -60.17200 -30.14600 1.000 54.60000  ? 475 PRO A CG  1 
ATOM   3412  C  CD  . PRO A  1 444 ? -13.46800 -61.61200 -30.54400 1.000 51.53000  ? 475 PRO A CD  1 
ATOM   3413  N  N   . LEU A  1 445 ? -15.58700 -59.73500 -34.27900 1.000 46.86000  ? 476 LEU A N   1 
ATOM   3414  C  CA  . LEU A  1 445 ? -15.42800 -59.59500 -35.72200 1.000 44.17000  ? 476 LEU A CA  1 
ATOM   3415  C  C   . LEU A  1 445 ? -14.30900 -58.64100 -36.08400 1.000 47.82000  ? 476 LEU A C   1 
ATOM   3416  O  O   . LEU A  1 445 ? -13.79400 -58.70000 -37.20100 1.000 48.86000  ? 476 LEU A O   1 
ATOM   3417  C  CB  . LEU A  1 445 ? -16.72600 -59.10800 -36.38000 1.000 41.18000  ? 476 LEU A CB  1 
ATOM   3418  C  CG  . LEU A  1 445 ? -17.93900 -60.03900 -36.29600 1.000 45.53000  ? 476 LEU A CG  1 
ATOM   3419  C  CD1 . LEU A  1 445 ? -19.13800 -59.37300 -36.90800 1.000 45.62000  ? 476 LEU A CD1 1 
ATOM   3420  C  CD2 . LEU A  1 445 ? -17.68600 -61.40100 -36.96100 1.000 42.96000  ? 476 LEU A CD2 1 
ATOM   3421  N  N   . TRP A  1 446 ? -13.97400 -57.72100 -35.18800 1.000 49.25000  ? 477 TRP A N   1 
ATOM   3422  C  CA  . TRP A  1 446 ? -12.84200 -56.83300 -35.35700 1.000 46.11000  ? 477 TRP A CA  1 
ATOM   3423  C  C   . TRP A  1 446 ? -12.38900 -56.43500 -33.96000 1.000 46.99000  ? 477 TRP A C   1 
ATOM   3424  O  O   . TRP A  1 446 ? -13.11000 -56.64100 -32.97900 1.000 48.56000  ? 477 TRP A O   1 
ATOM   3425  C  CB  . TRP A  1 446 ? -13.20200 -55.62600 -36.22400 1.000 41.18000  ? 477 TRP A CB  1 
ATOM   3426  C  CG  . TRP A  1 446 ? -14.33400 -54.82300 -35.67000 1.000 47.37000  ? 477 TRP A CG  1 
ATOM   3427  C  CD1 . TRP A  1 446 ? -14.25600 -53.83200 -34.72700 1.000 45.04000  ? 477 TRP A CD1 1 
ATOM   3428  C  CD2 . TRP A  1 446 ? -15.71700 -54.92500 -36.03200 1.000 48.24000  ? 477 TRP A CD2 1 
ATOM   3429  N  NE1 . TRP A  1 446 ? -15.49900 -53.34200 -34.45800 1.000 43.55000  ? 477 TRP A NE1 1 
ATOM   3430  C  CE2 . TRP A  1 446 ? -16.41700 -53.98700 -35.25300 1.000 49.22000  ? 477 TRP A CE2 1 
ATOM   3431  C  CE3 . TRP A  1 446 ? -16.43100 -55.72200 -36.93500 1.000 45.26000  ? 477 TRP A CE3 1 
ATOM   3432  C  CZ2 . TRP A  1 446 ? -17.80400 -53.82100 -35.34900 1.000 46.65000  ? 477 TRP A CZ2 1 
ATOM   3433  C  CZ3 . TRP A  1 446 ? -17.80300 -55.56800 -37.02000 1.000 49.78000  ? 477 TRP A CZ3 1 
ATOM   3434  C  CH2 . TRP A  1 446 ? -18.47700 -54.61800 -36.23300 1.000 50.33000  ? 477 TRP A CH2 1 
ATOM   3435  N  N   . VAL A  1 447 ? -11.16200 -55.93200 -33.86800 1.000 39.21000  ? 478 VAL A N   1 
ATOM   3436  C  CA  . VAL A  1 447 ? -10.64400 -55.41200 -32.60600 1.000 45.59000  ? 478 VAL A CA  1 
ATOM   3437  C  C   . VAL A  1 447 ? -10.30900 -53.94700 -32.84700 1.000 39.85000  ? 478 VAL A C   1 
ATOM   3438  O  O   . VAL A  1 447 ? -10.64200 -53.40700 -33.90700 1.000 42.84000  ? 478 VAL A O   1 
ATOM   3439  C  CB  . VAL A  1 447 ? -9.43000  -56.22200 -32.11100 1.000 47.40000  ? 478 VAL A CB  1 
ATOM   3440  C  CG1 . VAL A  1 447 ? -9.82600  -57.66100 -31.88400 1.000 43.87000  ? 478 VAL A CG1 1 
ATOM   3441  C  CG2 . VAL A  1 447 ? -8.29100  -56.14500 -33.11100 1.000 42.41000  ? 478 VAL A CG2 1 
ATOM   3442  N  N   . TYR A  1 448 ? -9.65900  -53.28300 -31.89200 1.000 38.78000  ? 479 TYR A N   1 
ATOM   3443  C  CA  . TYR A  1 448 ? -9.46800  -51.84100 -32.03300 1.000 44.51000  ? 479 TYR A CA  1 
ATOM   3444  C  C   . TYR A  1 448 ? -8.03800  -51.41600 -32.33600 1.000 41.95000  ? 479 TYR A C   1 
ATOM   3445  O  O   . TYR A  1 448 ? -7.83400  -50.49900 -33.13800 1.000 44.16000  ? 479 TYR A O   1 
ATOM   3446  C  CB  . TYR A  1 448 ? -9.94500  -51.10500 -30.77300 1.000 43.79000  ? 479 TYR A CB  1 
ATOM   3447  C  CG  . TYR A  1 448 ? -10.00600 -49.61400 -30.99100 1.000 41.48000  ? 479 TYR A CG  1 
ATOM   3448  C  CD1 . TYR A  1 448 ? -11.05700 -49.05500 -31.71900 1.000 43.98000  ? 479 TYR A CD1 1 
ATOM   3449  C  CD2 . TYR A  1 448 ? -9.04400  -48.77500 -30.48700 1.000 41.69000  ? 479 TYR A CD2 1 
ATOM   3450  C  CE1 . TYR A  1 448 ? -11.13800 -47.70600 -31.95300 1.000 41.64000  ? 479 TYR A CE1 1 
ATOM   3451  C  CE2 . TYR A  1 448 ? -9.12100  -47.40000 -30.69700 1.000 48.90000  ? 479 TYR A CE2 1 
ATOM   3452  C  CZ  . TYR A  1 448 ? -10.18500 -46.87500 -31.43100 1.000 46.96000  ? 479 TYR A CZ  1 
ATOM   3453  O  OH  . TYR A  1 448 ? -10.29500 -45.52500 -31.65400 1.000 48.95000  ? 479 TYR A OH  1 
ATOM   3454  N  N   . SER A  1 449 ? -7.03700  -52.05100 -31.73800 1.000 38.27000  ? 480 SER A N   1 
ATOM   3455  C  CA  . SER A  1 449 ? -5.65000  -51.65300 -31.94300 1.000 42.78000  ? 480 SER A CA  1 
ATOM   3456  C  C   . SER A  1 449 ? -4.81800  -52.84000 -32.41700 1.000 41.94000  ? 480 SER A C   1 
ATOM   3457  O  O   . SER A  1 449 ? -5.20100  -54.00100 -32.25300 1.000 46.11000  ? 480 SER A O   1 
ATOM   3458  C  CB  . SER A  1 449 ? -5.02200  -51.10800 -30.64900 1.000 32.53000  ? 480 SER A CB  1 
ATOM   3459  O  OG  . SER A  1 449 ? -4.84600  -52.20700 -29.76600 1.000 39.70000  ? 480 SER A OG  1 
ATOM   3460  N  N   . VAL A  1 450 ? -3.63400  -52.53300 -32.95600 1.000 43.45000  ? 481 VAL A N   1 
ATOM   3461  C  CA  . VAL A  1 450 ? -2.65800  -53.58100 -33.26300 1.000 40.22000  ? 481 VAL A CA  1 
ATOM   3462  C  C   . VAL A  1 450 ? -2.37600  -54.45100 -32.04400 1.000 42.56000  ? 481 VAL A C   1 
ATOM   3463  O  O   . VAL A  1 450 ? -2.27300  -55.68300 -32.14800 1.000 42.65000  ? 481 VAL A O   1 
ATOM   3464  C  CB  . VAL A  1 450 ? -1.36700  -52.95300 -33.81500 1.000 45.61000  ? 481 VAL A CB  1 
ATOM   3465  C  CG1 . VAL A  1 450 ? -0.25000  -54.00800 -33.87000 1.000 44.23000  ? 481 VAL A CG1 1 
ATOM   3466  C  CG2 . VAL A  1 450 ? -1.63600  -52.34900 -35.20800 1.000 39.18000  ? 481 VAL A CG2 1 
ATOM   3467  N  N   . LYS A  1 451 ? -2.20300  -53.82400 -30.87800 1.000 40.09000  ? 482 LYS A N   1 
ATOM   3468  C  CA  . LYS A  1 451 ? -2.00000  -54.58200 -29.64200 1.000 45.96000  ? 482 LYS A CA  1 
ATOM   3469  C  C   . LYS A  1 451 ? -3.12900  -55.58200 -29.40100 1.000 46.54000  ? 482 LYS A C   1 
ATOM   3470  O  O   . LYS A  1 451 ? -2.87400  -56.72000 -28.98200 1.000 47.62000  ? 482 LYS A O   1 
ATOM   3471  C  CB  . LYS A  1 451 ? -1.86800  -53.63000 -28.44800 1.000 42.23000  ? 482 LYS A CB  1 
ATOM   3472  C  CG  . LYS A  1 451 ? -1.76000  -54.36300 -27.12500 1.000 46.49000  ? 482 LYS A CG  1 
ATOM   3473  C  CD  . LYS A  1 451 ? -0.33900  -54.86700 -26.88600 1.000 51.00000  ? 482 LYS A CD  1 
ATOM   3474  C  CE  . LYS A  1 451 ? -0.22500  -55.59300 -25.54100 1.000 53.27000  ? 482 LYS A CE  1 
ATOM   3475  N  NZ  . LYS A  1 451 ? 1.17100   -55.98600 -25.18400 1.000 50.38000  ? 482 LYS A NZ  1 
ATOM   3476  N  N   . ASP A  1 452 ? -4.38200  -55.16200 -29.63300 1.000 41.26000  ? 483 ASP A N   1 
ATOM   3477  C  CA  . ASP A  1 452 ? -5.52800  -56.06400 -29.50100 1.000 41.85000  ? 483 ASP A CA  1 
ATOM   3478  C  C   . ASP A  1 452 ? -5.35400  -57.31000 -30.35200 1.000 45.92000  ? 483 ASP A C   1 
ATOM   3479  O  O   . ASP A  1 452 ? -5.54900  -58.43300 -29.87000 1.000 44.79000  ? 483 ASP A O   1 
ATOM   3480  C  CB  . ASP A  1 452 ? -6.82300  -55.36000 -29.92100 1.000 42.93000  ? 483 ASP A CB  1 
ATOM   3481  C  CG  . ASP A  1 452 ? -7.29900  -54.33500 -28.91500 1.000 47.33000  ? 483 ASP A CG  1 
ATOM   3482  O  OD1 . ASP A  1 452 ? -6.91100  -54.45100 -27.73800 1.000 53.06000  ? 483 ASP A OD1 1 
ATOM   3483  O  OD2 . ASP A  1 452 ? -8.02200  -53.39100 -29.31100 1.000 43.82000  ? 483 ASP A OD2 1 
ATOM   3484  N  N   . LYS A  1 453 ? -4.95900  -57.12500 -31.62000 1.000 44.25000  ? 484 LYS A N   1 
ATOM   3485  C  CA  . LYS A  1 453 ? -4.86500  -58.25200 -32.54400 1.000 49.14000  ? 484 LYS A CA  1 
ATOM   3486  C  C   . LYS A  1 453 ? -3.83400  -59.27400 -32.07500 1.000 49.97000  ? 484 LYS A C   1 
ATOM   3487  O  O   . LYS A  1 453 ? -4.13100  -60.47300 -31.98800 1.000 49.07000  ? 484 LYS A O   1 
ATOM   3488  C  CB  . LYS A  1 453 ? -4.51000  -57.74800 -33.94400 1.000 45.59000  ? 484 LYS A CB  1 
ATOM   3489  N  N   . GLU A  1 454 ? -2.64000  -58.80800 -31.70000 1.000 45.90000  ? 485 GLU A N   1 
ATOM   3490  C  CA  . GLU A  1 454 ? -1.59300  -59.72700 -31.25500 1.000 51.35000  ? 485 GLU A CA  1 
ATOM   3491  C  C   . GLU A  1 454 ? -2.07100  -60.55400 -30.06800 1.000 52.96000  ? 485 GLU A C   1 
ATOM   3492  O  O   . GLU A  1 454 ? -1.87900  -61.77700 -30.02700 1.000 52.90000  ? 485 GLU A O   1 
ATOM   3493  C  CB  . GLU A  1 454 ? -0.31200  -58.94700 -30.91000 1.000 45.81000  ? 485 GLU A CB  1 
ATOM   3494  C  CG  . GLU A  1 454 ? 0.13900   -58.01400 -32.04500 1.000 56.33000  ? 485 GLU A CG  1 
ATOM   3495  C  CD  . GLU A  1 454 ? 1.44100   -57.24300 -31.77300 1.000 63.25000  ? 485 GLU A CD  1 
ATOM   3496  O  OE1 . GLU A  1 454 ? 1.85200   -57.08500 -30.59400 1.000 56.79000  ? 485 GLU A OE1 1 
ATOM   3497  O  OE2 . GLU A  1 454 ? 2.05400   -56.79100 -32.76800 1.000 58.96000  ? 485 GLU A OE2 1 
ATOM   3498  N  N   . LEU A  1 455 ? -2.71000  -59.90100 -29.09400 1.000 51.75000  ? 486 LEU A N   1 
ATOM   3499  C  CA  . LEU A  1 455 ? -3.13600  -60.61700 -27.89800 1.000 56.19000  ? 486 LEU A CA  1 
ATOM   3500  C  C   . LEU A  1 455 ? -4.20500  -61.65800 -28.21700 1.000 52.51000  ? 486 LEU A C   1 
ATOM   3501  O  O   . LEU A  1 455 ? -4.25100  -62.72100 -27.58200 1.000 55.74000  ? 486 LEU A O   1 
ATOM   3502  C  CB  . LEU A  1 455 ? -3.65100  -59.64400 -26.83600 1.000 50.04000  ? 486 LEU A CB  1 
ATOM   3503  C  CG  . LEU A  1 455 ? -2.69600  -58.57400 -26.30500 1.000 55.81000  ? 486 LEU A CG  1 
ATOM   3504  C  CD1 . LEU A  1 455 ? -3.43400  -57.67100 -25.32000 1.000 47.47000  ? 486 LEU A CD1 1 
ATOM   3505  C  CD2 . LEU A  1 455 ? -1.44000  -59.15800 -25.69400 1.000 55.50000  ? 486 LEU A CD2 1 
ATOM   3506  N  N   . TRP A  1 456 ? -5.10900  -61.35300 -29.15100 1.000 50.42000  ? 487 TRP A N   1 
ATOM   3507  C  CA  . TRP A  1 456 ? -6.15500  -62.32000 -29.48100 1.000 53.72000  ? 487 TRP A CA  1 
ATOM   3508  C  C   . TRP A  1 456 ? -5.60800  -63.50100 -30.28200 1.000 50.14000  ? 487 TRP A C   1 
ATOM   3509  O  O   . TRP A  1 456 ? -6.03500  -64.64000 -30.07100 1.000 50.26000  ? 487 TRP A O   1 
ATOM   3510  C  CB  . TRP A  1 456 ? -7.29000  -61.65100 -30.25900 1.000 45.81000  ? 487 TRP A CB  1 
ATOM   3511  C  CG  . TRP A  1 456 ? -8.27300  -60.94000 -29.41500 1.000 51.63000  ? 487 TRP A CG  1 
ATOM   3512  C  CD1 . TRP A  1 456 ? -8.22400  -59.63800 -29.00300 1.000 49.46000  ? 487 TRP A CD1 1 
ATOM   3513  C  CD2 . TRP A  1 456 ? -9.45700  -61.50600 -28.82900 1.000 51.06000  ? 487 TRP A CD2 1 
ATOM   3514  N  NE1 . TRP A  1 456 ? -9.31500  -59.35300 -28.20700 1.000 47.45000  ? 487 TRP A NE1 1 
ATOM   3515  C  CE2 . TRP A  1 456 ? -10.09300 -60.48000 -28.09400 1.000 51.33000  ? 487 TRP A CE2 1 
ATOM   3516  C  CE3 . TRP A  1 456 ? -10.03800 -62.77900 -28.85600 1.000 46.32000  ? 487 TRP A CE3 1 
ATOM   3517  C  CZ2 . TRP A  1 456 ? -11.29900 -60.68600 -27.39900 1.000 48.83000  ? 487 TRP A CZ2 1 
ATOM   3518  C  CZ3 . TRP A  1 456 ? -11.22900 -62.98600 -28.16400 1.000 50.33000  ? 487 TRP A CZ3 1 
ATOM   3519  C  CH2 . TRP A  1 456 ? -11.84400 -61.94100 -27.44000 1.000 50.33000  ? 487 TRP A CH2 1 
ATOM   3520  N  N   . GLU A  1 457 ? -4.63500  -63.25300 -31.16500 1.000 46.17000  ? 488 GLU A N   1 
ATOM   3521  C  CA  . GLU A  1 457 ? -4.06800  -64.31800 -31.99100 1.000 55.76000  ? 488 GLU A CA  1 
ATOM   3522  C  C   . GLU A  1 457 ? -3.20200  -65.26200 -31.17200 1.000 59.25000  ? 488 GLU A C   1 
ATOM   3523  O  O   . GLU A  1 457 ? -3.14600  -66.46100 -31.46800 1.000 61.44000  ? 488 GLU A O   1 
ATOM   3524  C  CB  . GLU A  1 457 ? -3.23800  -63.72900 -33.12900 1.000 52.89000  ? 488 GLU A CB  1 
ATOM   3525  C  CG  . GLU A  1 457 ? -4.06100  -63.05500 -34.20800 1.000 63.41000  ? 488 GLU A CG  1 
ATOM   3526  C  CD  . GLU A  1 457 ? -3.21000  -62.22100 -35.16300 1.000 73.47000  ? 488 GLU A CD  1 
ATOM   3527  O  OE1 . GLU A  1 457 ? -2.07500  -61.84600 -34.78500 1.000 74.28000  ? 488 GLU A OE1 1 
ATOM   3528  O  OE2 . GLU A  1 457 ? -3.67800  -61.93900 -36.29100 1.000 76.92000  ? 488 GLU A OE2 1 
ATOM   3529  N  N   . SER A  1 458 ? -2.49300  -64.74100 -30.17500 1.000 56.68000  ? 489 SER A N   1 
ATOM   3530  C  CA  . SER A  1 458 ? -1.69200  -65.58100 -29.30100 1.000 55.87000  ? 489 SER A CA  1 
ATOM   3531  C  C   . SER A  1 458 ? -2.50600  -66.25500 -28.21000 1.000 55.76000  ? 489 SER A C   1 
ATOM   3532  O  O   . SER A  1 458 ? -1.97400  -67.13200 -27.52000 1.000 57.70000  ? 489 SER A O   1 
ATOM   3533  C  CB  . SER A  1 458 ? -0.59800  -64.75700 -28.64700 1.000 52.94000  ? 489 SER A CB  1 
ATOM   3534  O  OG  . SER A  1 458 ? -1.18100  -63.93300 -27.66600 1.000 57.71000  ? 489 SER A OG  1 
ATOM   3535  N  N   . GLY A  1 459 ? -3.76200  -65.86200 -28.01100 1.000 57.02000  ? 490 GLY A N   1 
ATOM   3536  C  CA  . GLY A  1 459 ? -4.55200  -66.41600 -26.93300 1.000 53.12000  ? 490 GLY A CA  1 
ATOM   3537  C  C   . GLY A  1 459 ? -4.40100  -65.70200 -25.60800 1.000 58.09000  ? 490 GLY A C   1 
ATOM   3538  O  O   . GLY A  1 459 ? -5.06500  -66.08900 -24.63300 1.000 54.64000  ? 490 GLY A O   1 
ATOM   3539  N  N   . GLN A  1 460 ? -3.49800  -64.71900 -25.52400 1.000 60.04000  ? 491 GLN A N   1 
ATOM   3540  C  CA  . GLN A  1 460 ? -3.39200  -63.89400 -24.32600 1.000 56.72000  ? 491 GLN A CA  1 
ATOM   3541  C  C   . GLN A  1 460 ? -4.74100  -63.27100 -23.98600 1.000 55.23000  ? 491 GLN A C   1 
ATOM   3542  O  O   . GLN A  1 460 ? -5.06800  -63.09300 -22.80800 1.000 49.86000  ? 491 GLN A O   1 
ATOM   3543  C  CB  . GLN A  1 460 ? -2.30600  -62.82700 -24.52600 1.000 59.79000  ? 491 GLN A CB  1 
ATOM   3544  C  CG  . GLN A  1 460 ? -0.90200  -63.43700 -24.62400 1.000 69.71000  ? 491 GLN A CG  1 
ATOM   3545  C  CD  . GLN A  1 460 ? 0.21100   -62.43000 -24.89500 1.000 67.39000  ? 491 GLN A CD  1 
ATOM   3546  O  OE1 . GLN A  1 460 ? 0.45100   -62.02600 -26.04100 1.000 61.88000  ? 491 GLN A OE1 1 
ATOM   3547  N  NE2 . GLN A  1 460 ? 0.92000   -62.04900 -23.84100 1.000 72.19000  ? 491 GLN A NE2 1 
ATOM   3548  N  N   . MET A  1 461 ? -5.55300  -62.96900 -25.00900 1.000 53.98000  ? 492 MET A N   1 
ATOM   3549  C  CA  . MET A  1 461 ? -6.95900  -62.62300 -24.85900 1.000 51.53000  ? 492 MET A CA  1 
ATOM   3550  C  C   . MET A  1 461 ? -7.79600  -63.76400 -25.41200 1.000 53.97000  ? 492 MET A C   1 
ATOM   3551  O  O   . MET A  1 461 ? -7.37100  -64.44000 -26.34600 1.000 52.93000  ? 492 MET A O   1 
ATOM   3552  C  CB  . MET A  1 461 ? -7.32600  -61.32700 -25.59900 1.000 50.54000  ? 492 MET A CB  1 
ATOM   3553  C  CG  . MET A  1 461 ? -6.76900  -60.05800 -24.97200 1.000 52.08000  ? 492 MET A CG  1 
ATOM   3554  S  SD  . MET A  1 461 ? -7.44600  -59.69900 -23.34200 1.000 50.19000  ? 492 MET A SD  1 
ATOM   3555  C  CE  . MET A  1 461 ? -8.99200  -58.86700 -23.74900 1.000 42.65000  ? 492 MET A CE  1 
ATOM   3556  N  N   . PRO A  1 462 ? -8.99400  -63.99800 -24.89100 1.000 57.79000  ? 493 PRO A N   1 
ATOM   3557  C  CA  . PRO A  1 462 ? -9.67800  -63.23500 -23.83900 1.000 51.73000  ? 493 PRO A CA  1 
ATOM   3558  C  C   . PRO A  1 462 ? -9.37000  -63.72800 -22.43000 1.000 53.61000  ? 493 PRO A C   1 
ATOM   3559  O  O   . PRO A  1 462 ? -9.48900  -62.96700 -21.46600 1.000 49.60000  ? 493 PRO A O   1 
ATOM   3560  C  CB  . PRO A  1 462 ? -11.15700 -63.40300 -24.21600 1.000 56.25000  ? 493 PRO A CB  1 
ATOM   3561  C  CG  . PRO A  1 462 ? -11.22500 -64.75300 -24.90400 1.000 53.18000  ? 493 PRO A CG  1 
ATOM   3562  C  CD  . PRO A  1 462 ? -9.89100  -64.96300 -25.56400 1.000 49.84000  ? 493 PRO A CD  1 
ATOM   3563  N  N   . ASN A  1 463 ? -8.98400  -64.99800 -22.32100 1.000 52.27000  ? 494 ASN A N   1 
ATOM   3564  C  CA  . ASN A  1 463 ? -8.66500  -65.68000 -21.06000 1.000 50.46000  ? 494 ASN A CA  1 
ATOM   3565  C  C   . ASN A  1 463 ? -9.69300  -65.37200 -19.97800 1.000 51.99000  ? 494 ASN A C   1 
ATOM   3566  O  O   . ASN A  1 463 ? -9.37600  -64.89300 -18.88200 1.000 51.29000  ? 494 ASN A O   1 
ATOM   3567  C  CB  . ASN A  1 463 ? -7.25500  -65.34400 -20.56300 1.000 49.37000  ? 494 ASN A CB  1 
ATOM   3568  C  CG  . ASN A  1 463 ? -6.77200  -66.32700 -19.50200 1.000 53.81000  ? 494 ASN A CG  1 
ATOM   3569  O  OD1 . ASN A  1 463 ? -7.57000  -67.08500 -18.93600 1.000 54.17000  ? 494 ASN A OD1 1 
ATOM   3570  N  ND2 . ASN A  1 463 ? -5.47000  -66.32800 -19.23200 1.000 45.73000  ? 494 ASN A ND2 1 
ATOM   3571  N  N   . TYR A  1 464 ? -10.93900 -65.72600 -20.29000 1.000 48.61000  ? 495 TYR A N   1 
ATOM   3572  C  CA  . TYR A  1 464 ? -12.00500 -65.58100 -19.31200 1.000 49.38000  ? 495 TYR A CA  1 
ATOM   3573  C  C   . TYR A  1 464 ? -11.69600 -66.39100 -18.06100 1.000 53.00000  ? 495 TYR A C   1 
ATOM   3574  O  O   . TYR A  1 464 ? -12.14100 -66.03700 -16.96300 1.000 52.83000  ? 495 TYR A O   1 
ATOM   3575  C  CB  . TYR A  1 464 ? -13.34000 -66.02000 -19.91900 1.000 49.86000  ? 495 TYR A CB  1 
ATOM   3576  C  CG  . TYR A  1 464 ? -13.75500 -65.25300 -21.15400 1.000 50.34000  ? 495 TYR A CG  1 
ATOM   3577  C  CD1 . TYR A  1 464 ? -13.99900 -63.88400 -21.09300 1.000 47.96000  ? 495 TYR A CD1 1 
ATOM   3578  C  CD2 . TYR A  1 464 ? -13.90700 -65.89300 -22.38100 1.000 46.75000  ? 495 TYR A CD2 1 
ATOM   3579  C  CE1 . TYR A  1 464 ? -14.38300 -63.17100 -22.21700 1.000 44.39000  ? 495 TYR A CE1 1 
ATOM   3580  C  CE2 . TYR A  1 464 ? -14.30000 -65.18800 -23.51600 1.000 45.37000  ? 495 TYR A CE2 1 
ATOM   3581  C  CZ  . TYR A  1 464 ? -14.53200 -63.82000 -23.42200 1.000 49.90000  ? 495 TYR A CZ  1 
ATOM   3582  O  OH  . TYR A  1 464 ? -14.91400 -63.08800 -24.52600 1.000 51.13000  ? 495 TYR A OH  1 
ATOM   3583  N  N   . GLU A  1 465 ? -10.93500 -67.46700 -18.21000 1.000 50.92000  ? 496 GLU A N   1 
ATOM   3584  C  CA  . GLU A  1 465 ? -10.65200 -68.35400 -17.05800 1.000 55.45000  ? 496 GLU A CA  1 
ATOM   3585  C  C   . GLU A  1 465 ? -9.90300  -67.56000 -15.98600 1.000 54.52000  ? 496 GLU A C   1 
ATOM   3586  O  O   . GLU A  1 465 ? -10.32100 -67.60100 -14.81900 1.000 54.71000  ? 496 GLU A O   1 
ATOM   3587  C  CB  . GLU A  1 465 ? -9.85100  -69.55900 -17.54000 1.000 58.52000  ? 496 GLU A CB  1 
ATOM   3588  C  CG  . GLU A  1 465 ? -10.42500 -70.20800 -18.79600 1.000 64.84000  ? 496 GLU A CG  1 
ATOM   3589  C  CD  . GLU A  1 465 ? -10.08000 -69.54400 -20.11900 1.000 65.28000  ? 496 GLU A CD  1 
ATOM   3590  O  OE1 . GLU A  1 465 ? -8.95000  -69.72200 -20.61600 1.000 68.80000  ? 496 GLU A OE1 1 
ATOM   3591  O  OE2 . GLU A  1 465 ? -10.95800 -68.83300 -20.64500 1.000 62.37000  ? 496 GLU A OE2 1 
ATOM   3592  N  N   . ALA A  1 466 ? -8.84400  -66.86100 -16.38400 1.000 52.20000  ? 497 ALA A N   1 
ATOM   3593  C  CA  . ALA A  1 466 ? -8.10500  -66.03200 -15.43700 1.000 54.99000  ? 497 ALA A CA  1 
ATOM   3594  C  C   . ALA A  1 466 ? -8.97000  -64.89900 -14.88700 1.000 46.96000  ? 497 ALA A C   1 
ATOM   3595  O  O   . ALA A  1 466 ? -8.84800  -64.53500 -13.71500 1.000 49.23000  ? 497 ALA A O   1 
ATOM   3596  C  CB  . ALA A  1 466 ? -6.84100  -65.47800 -16.11000 1.000 46.85000  ? 497 ALA A CB  1 
ATOM   3597  N  N   . THR A  1 467 ? -9.87200  -64.36500 -15.69600 1.000 43.52000  ? 498 THR A N   1 
ATOM   3598  C  CA  . THR A  1 467 ? -10.72000 -63.27800 -15.23600 1.000 45.32000  ? 498 THR A CA  1 
ATOM   3599  C  C   . THR A  1 467 ? -11.53200 -63.67200 -14.00500 1.000 47.84000  ? 498 THR A C   1 
ATOM   3600  O  O   . THR A  1 467 ? -11.75400 -62.84600 -13.11500 1.000 42.45000  ? 498 THR A O   1 
ATOM   3601  C  CB  . THR A  1 467 ? -11.63200 -62.86100 -16.38400 1.000 48.34000  ? 498 THR A CB  1 
ATOM   3602  O  OG1 . THR A  1 467 ? -10.85400 -62.17300 -17.37300 1.000 45.14000  ? 498 THR A OG1 1 
ATOM   3603  C  CG2 . THR A  1 467 ? -12.83000 -62.00700 -15.89900 1.000 45.78000  ? 498 THR A CG2 1 
ATOM   3604  N  N   . PHE A  1 468 ? -11.93100 -64.93400 -13.89400 1.000 44.20000  ? 499 PHE A N   1 
ATOM   3605  C  CA  . PHE A  1 468 ? -12.80600 -65.32500 -12.80500 1.000 43.81000  ? 499 PHE A CA  1 
ATOM   3606  C  C   . PHE A  1 468 ? -12.06900 -66.01600 -11.66600 1.000 54.10000  ? 499 PHE A C   1 
ATOM   3607  O  O   . PHE A  1 468 ? -12.72100 -66.61600 -10.80400 1.000 48.43000  ? 499 PHE A O   1 
ATOM   3608  C  CB  . PHE A  1 468 ? -13.94900 -66.19000 -13.34500 1.000 48.00000  ? 499 PHE A CB  1 
ATOM   3609  C  CG  . PHE A  1 468 ? -14.83200 -65.44900 -14.30200 1.000 42.11000  ? 499 PHE A CG  1 
ATOM   3610  C  CD1 . PHE A  1 468 ? -15.68800 -64.46000 -13.84800 1.000 47.01000  ? 499 PHE A CD1 1 
ATOM   3611  C  CD2 . PHE A  1 468 ? -14.76200 -65.69100 -15.65900 1.000 49.07000  ? 499 PHE A CD2 1 
ATOM   3612  C  CE1 . PHE A  1 468 ? -16.50300 -63.75000 -14.74800 1.000 46.58000  ? 499 PHE A CE1 1 
ATOM   3613  C  CE2 . PHE A  1 468 ? -15.54700 -64.97400 -16.56400 1.000 49.09000  ? 499 PHE A CE2 1 
ATOM   3614  C  CZ  . PHE A  1 468 ? -16.42100 -64.00200 -16.10200 1.000 45.47000  ? 499 PHE A CZ  1 
ATOM   3615  N  N   . GLU A  1 469 ? -10.73000 -65.96300 -11.65100 1.000 48.08000  ? 500 GLU A N   1 
ATOM   3616  C  CA  . GLU A  1 469 ? -9.98800  -66.30800 -10.44500 1.000 45.10000  ? 500 GLU A CA  1 
ATOM   3617  C  C   . GLU A  1 469 ? -10.41700 -65.40200 -9.29600  1.000 45.92000  ? 500 GLU A C   1 
ATOM   3618  O  O   . GLU A  1 469 ? -10.78200 -64.24600 -9.50300  1.000 47.20000  ? 500 GLU A O   1 
ATOM   3619  C  CB  . GLU A  1 469 ? -8.48900  -66.18200 -10.69800 1.000 47.03000  ? 500 GLU A CB  1 
ATOM   3620  C  CG  . GLU A  1 469 ? -7.94900  -67.22000 -11.67600 1.000 57.63000  ? 500 GLU A CG  1 
ATOM   3621  C  CD  . GLU A  1 469 ? -6.56200  -66.87700 -12.21200 1.000 59.37000  ? 500 GLU A CD  1 
ATOM   3622  O  OE1 . GLU A  1 469 ? -6.17400  -65.69400 -12.12700 1.000 55.26000  ? 500 GLU A OE1 1 
ATOM   3623  O  OE2 . GLU A  1 469 ? -5.85100  -67.80100 -12.68300 1.000 58.97000  ? 500 GLU A OE2 1 
ATOM   3624  N  N   . VAL A  1 470 ? -10.37200 -65.92900 -8.06900  1.000 45.86000  ? 501 VAL A N   1 
ATOM   3625  C  CA  . VAL A  1 470 ? -10.75700 -65.14600 -6.89400  1.000 48.41000  ? 501 VAL A CA  1 
ATOM   3626  C  C   . VAL A  1 470 ? -9.72900  -65.27600 -5.78100  1.000 50.05000  ? 501 VAL A C   1 
ATOM   3627  O  O   . VAL A  1 470 ? -9.13700  -64.28000 -5.35100  1.000 52.81000  ? 501 VAL A O   1 
ATOM   3628  C  CB  . VAL A  1 470 ? -12.13800 -65.54200 -6.35900  1.000 46.22000  ? 501 VAL A CB  1 
ATOM   3629  C  CG1 . VAL A  1 470 ? -12.47100 -64.69700 -5.15200  1.000 48.52000  ? 501 VAL A CG1 1 
ATOM   3630  C  CG2 . VAL A  1 470 ? -13.18300 -65.33800 -7.42600  1.000 50.43000  ? 501 VAL A CG2 1 
ATOM   3631  N  N   . ASP A  1 471 ? -9.51900  -66.50000 -5.29600  1.000 54.42000  ? 502 ASP A N   1 
ATOM   3632  C  CA  . ASP A  1 471 ? -8.70400  -66.67700 -4.10000  1.000 55.32000  ? 502 ASP A CA  1 
ATOM   3633  C  C   . ASP A  1 471 ? -7.25200  -66.28100 -4.33500  1.000 52.29000  ? 502 ASP A C   1 
ATOM   3634  O  O   . ASP A  1 471 ? -6.64400  -65.62900 -3.48000  1.000 46.96000  ? 502 ASP A O   1 
ATOM   3635  C  CB  . ASP A  1 471 ? -8.79200  -68.12100 -3.60200  1.000 53.68000  ? 502 ASP A CB  1 
ATOM   3636  C  CG  . ASP A  1 471 ? -10.16400 -68.46500 -3.03600  1.000 60.16000  ? 502 ASP A CG  1 
ATOM   3637  O  OD1 . ASP A  1 471 ? -10.89400 -67.53300 -2.63100  1.000 57.82000  ? 502 ASP A OD1 1 
ATOM   3638  O  OD2 . ASP A  1 471 ? -10.49700 -69.67000 -2.95700  1.000 68.76000  ? 502 ASP A OD2 1 
ATOM   3639  N  N   . LYS A  1 472 ? -6.68900  -66.62600 -5.49700  1.000 50.73000  ? 503 LYS A N   1 
ATOM   3640  C  CA  . LYS A  1 472 ? -5.28100  -66.32800 -5.71900  1.000 49.07000  ? 503 LYS A CA  1 
ATOM   3641  C  C   . LYS A  1 472 ? -4.99900  -64.82700 -5.75300  1.000 51.07000  ? 503 LYS A C   1 
ATOM   3642  O  O   . LYS A  1 472 ? -3.86000  -64.41500 -5.50900  1.000 52.74000  ? 503 LYS A O   1 
ATOM   3643  C  CB  . LYS A  1 472 ? -4.79700  -67.00200 -7.00100  1.000 44.76000  ? 503 LYS A CB  1 
ATOM   3644  C  CG  . LYS A  1 472 ? -5.36600  -66.43800 -8.26600  1.000 52.77000  ? 503 LYS A CG  1 
ATOM   3645  C  CD  . LYS A  1 472 ? -4.59500  -66.96600 -9.47900  1.000 52.35000  ? 503 LYS A CD  1 
ATOM   3646  C  CE  . LYS A  1 472 ? -4.71500  -68.46900 -9.61200  1.000 54.45000  ? 503 LYS A CE  1 
ATOM   3647  N  NZ  . LYS A  1 472 ? -4.03800  -68.93000 -10.84200 1.000 53.38000  ? 503 LYS A NZ  1 
ATOM   3648  N  N   . LEU A  1 473 ? -6.00900  -63.99600 -6.00000  1.000 48.08000  ? 504 LEU A N   1 
ATOM   3649  C  CA  . LEU A  1 473 ? -5.76300  -62.56400 -6.05600  1.000 46.66000  ? 504 LEU A CA  1 
ATOM   3650  C  C   . LEU A  1 473 ? -5.60300  -61.94300 -4.66700  1.000 45.55000  ? 504 LEU A C   1 
ATOM   3651  O  O   . LEU A  1 473 ? -5.04500  -60.85200 -4.56400  1.000 48.91000  ? 504 LEU A O   1 
ATOM   3652  C  CB  . LEU A  1 473 ? -6.88400  -61.85900 -6.82500  1.000 45.49000  ? 504 LEU A CB  1 
ATOM   3653  C  CG  . LEU A  1 473 ? -7.26700  -62.42500 -8.19500  1.000 48.18000  ? 504 LEU A CG  1 
ATOM   3654  C  CD1 . LEU A  1 473 ? -8.46100  -61.67300 -8.75400  1.000 44.36000  ? 504 LEU A CD1 1 
ATOM   3655  C  CD2 . LEU A  1 473 ? -6.07600  -62.33900 -9.14700  1.000 48.74000  ? 504 LEU A CD2 1 
ATOM   3656  N  N   . VAL A  1 474 ? -6.09500  -62.58900 -3.61100  1.000 42.96000  ? 505 VAL A N   1 
ATOM   3657  C  CA  . VAL A  1 474 ? -6.02300  -62.02800 -2.26900  1.000 42.72000  ? 505 VAL A CA  1 
ATOM   3658  C  C   . VAL A  1 474 ? -5.16000  -62.85300 -1.31300  1.000 49.63000  ? 505 VAL A C   1 
ATOM   3659  O  O   . VAL A  1 474 ? -4.80800  -62.35200 -0.23500  1.000 49.41000  ? 505 VAL A O   1 
ATOM   3660  C  CB  . VAL A  1 474 ? -7.42900  -61.82500 -1.66900  1.000 50.17000  ? 505 VAL A CB  1 
ATOM   3661  C  CG1 . VAL A  1 474 ? -8.07600  -60.58400 -2.27100  1.000 42.12000  ? 505 VAL A CG1 1 
ATOM   3662  C  CG2 . VAL A  1 474 ? -8.29800  -63.05900 -1.87300  1.000 49.05000  ? 505 VAL A CG2 1 
ATOM   3663  N  N   . ASP A  1 475 ? -4.85400  -64.11600 -1.61200  1.000 51.62000  ? 506 ASP A N   1 
ATOM   3664  C  CA  . ASP A  1 475 ? -4.10100  -64.96600 -0.69000  1.000 50.82000  ? 506 ASP A CA  1 
ATOM   3665  C  C   . ASP A  1 475 ? -2.61100  -64.64400 -0.68800  1.000 46.64000  ? 506 ASP A C   1 
ATOM   3666  O  O   . ASP A  1 475 ? -1.99900  -64.45500 -1.74100  1.000 47.34000  ? 506 ASP A O   1 
ATOM   3667  C  CB  . ASP A  1 475 ? -4.28400  -66.43900 -1.06100  1.000 50.53000  ? 506 ASP A CB  1 
ATOM   3668  C  CG  . ASP A  1 475 ? -5.66400  -66.94400 -0.76500  1.000 51.97000  ? 506 ASP A CG  1 
ATOM   3669  O  OD1 . ASP A  1 475 ? -6.31900  -66.39500 0.15200   1.000 50.43000  ? 506 ASP A OD1 1 
ATOM   3670  O  OD2 . ASP A  1 475 ? -6.10100  -67.87900 -1.46300  1.000 54.64000  ? 506 ASP A OD2 1 
ATOM   3671  N  N   . SER A  1 476 ? -2.02000  -64.64200 0.50000   1.000 50.00000  ? 507 SER A N   1 
ATOM   3672  C  CA  . SER A  1 476 ? -0.57800  -64.48300 0.55400   1.000 53.41000  ? 507 SER A CA  1 
ATOM   3673  C  C   . SER A  1 476 ? 0.11200   -65.81300 0.25800   1.000 52.76000  ? 507 SER A C   1 
ATOM   3674  O  O   . SER A  1 476 ? -0.31900  -66.85500 0.74900   1.000 52.76000  ? 507 SER A O   1 
ATOM   3675  C  CB  . SER A  1 476 ? -0.15200  -63.99100 1.92000   1.000 49.46000  ? 507 SER A CB  1 
ATOM   3676  O  OG  . SER A  1 476 ? 1.23400   -64.17500 2.06300   1.000 49.54000  ? 507 SER A OG  1 
ATOM   3677  N  N   . PRO A  1 477 ? 1.20800   -65.80200 -0.50300  1.000 53.02000  ? 508 PRO A N   1 
ATOM   3678  C  CA  . PRO A  1 477 ? 1.95500   -67.04000 -0.76400  1.000 49.73000  ? 508 PRO A CA  1 
ATOM   3679  C  C   . PRO A  1 477 ? 2.88600   -67.48800 0.35400   1.000 59.37000  ? 508 PRO A C   1 
ATOM   3680  O  O   . PRO A  1 477 ? 3.60800   -68.46800 0.15000   1.000 55.30000  ? 508 PRO A O   1 
ATOM   3681  C  CB  . PRO A  1 477 ? 2.76500   -66.69400 -2.02100  1.000 45.72000  ? 508 PRO A CB  1 
ATOM   3682  C  CG  . PRO A  1 477 ? 2.87200   -65.21500 -2.02400  1.000 53.29000  ? 508 PRO A CG  1 
ATOM   3683  C  CD  . PRO A  1 477 ? 1.71900   -64.64900 -1.26300  1.000 49.03000  ? 508 PRO A CD  1 
ATOM   3684  N  N   . TYR A  1 478 ? 2.87300   -66.84400 1.52900   1.000 48.03000  ? 509 TYR A N   1 
ATOM   3685  C  CA  . TYR A  1 478 ? 3.80600   -67.16400 2.59400   1.000 49.11000  ? 509 TYR A CA  1 
ATOM   3686  C  C   . TYR A  1 478 ? 3.12800   -67.59400 3.89200   1.000 60.14000  ? 509 TYR A C   1 
ATOM   3687  O  O   . TYR A  1 478 ? 1.90400   -67.56400 4.00600   1.000 62.61000  ? 509 TYR A O   1 
ATOM   3688  C  CB  . TYR A  1 478 ? 4.72500   -65.96500 2.86700   1.000 45.83000  ? 509 TYR A CB  1 
ATOM   3689  C  CG  . TYR A  1 478 ? 5.27500   -65.31300 1.60700   1.000 53.32000  ? 509 TYR A CG  1 
ATOM   3690  C  CD1 . TYR A  1 478 ? 6.29000   -65.92100 0.87700   1.000 55.63000  ? 509 TYR A CD1 1 
ATOM   3691  C  CD2 . TYR A  1 478 ? 4.80300   -64.09100 1.16100   1.000 47.76000  ? 509 TYR A CD2 1 
ATOM   3692  C  CE1 . TYR A  1 478 ? 6.80300   -65.34100 -0.27000  1.000 50.27000  ? 509 TYR A CE1 1 
ATOM   3693  C  CE2 . TYR A  1 478 ? 5.30900   -63.50900 0.01400   1.000 51.84000  ? 509 TYR A CE2 1 
ATOM   3694  C  CZ  . TYR A  1 478 ? 6.30400   -64.14000 -0.70100  1.000 52.31000  ? 509 TYR A CZ  1 
ATOM   3695  O  OH  . TYR A  1 478 ? 6.81700   -63.56700 -1.84800  1.000 48.34000  ? 509 TYR A OH  1 
ATOM   3696  N  N   . THR B  1 15  ? 25.78400  -24.76900 14.98800  1.000 59.16000  ? 46  THR B N   1 
ATOM   3697  C  CA  . THR B  1 15  ? 25.09600  -25.82800 15.71900  1.000 63.55000  ? 46  THR B CA  1 
ATOM   3698  C  C   . THR B  1 15  ? 24.04000  -26.58800 14.87200  1.000 65.13000  ? 46  THR B C   1 
ATOM   3699  O  O   . THR B  1 15  ? 23.09600  -26.00800 14.31500  1.000 57.00000  ? 46  THR B O   1 
ATOM   3700  C  CB  . THR B  1 15  ? 24.45100  -25.26700 17.00300  1.000 67.90000  ? 46  THR B CB  1 
ATOM   3701  O  OG1 . THR B  1 15  ? 23.84600  -26.34000 17.73600  1.000 76.79000  ? 46  THR B OG1 1 
ATOM   3702  C  CG2 . THR B  1 15  ? 23.44000  -24.15600 16.70500  1.000 67.15000  ? 46  THR B CG2 1 
ATOM   3703  N  N   . ARG B  1 16  ? 24.24700  -27.89900 14.77000  1.000 58.82000  ? 47  ARG B N   1 
ATOM   3704  C  CA  . ARG B  1 16  ? 23.46600  -28.71500 13.85700  1.000 53.07000  ? 47  ARG B CA  1 
ATOM   3705  C  C   . ARG B  1 16  ? 21.99300  -28.74000 14.27300  1.000 49.84000  ? 47  ARG B C   1 
ATOM   3706  O  O   . ARG B  1 16  ? 21.68700  -28.84300 15.46700  1.000 47.17000  ? 47  ARG B O   1 
ATOM   3707  C  CB  . ARG B  1 16  ? 24.03800  -30.13300 13.82100  1.000 50.47000  ? 47  ARG B CB  1 
ATOM   3708  C  CG  . ARG B  1 16  ? 25.39900  -30.24100 13.15000  1.000 49.25000  ? 47  ARG B CG  1 
ATOM   3709  C  CD  . ARG B  1 16  ? 25.96200  -31.66100 13.25300  1.000 50.24000  ? 47  ARG B CD  1 
ATOM   3710  N  NE  . ARG B  1 16  ? 25.94500  -32.25900 14.58300  1.000 48.99000  ? 47  ARG B NE  1 
ATOM   3711  C  CZ  . ARG B  1 16  ? 26.21400  -33.53900 14.82200  1.000 51.91000  ? 47  ARG B CZ  1 
ATOM   3712  N  NH1 . ARG B  1 16  ? 26.43100  -34.40100 13.83900  1.000 45.87000  ? 47  ARG B NH1 1 
ATOM   3713  N  NH2 . ARG B  1 16  ? 26.26500  -33.96900 16.07700  1.000 49.78000  ? 47  ARG B NH2 1 
ATOM   3714  N  N   . PRO B  1 17  ? 21.05600  -28.73500 13.32400  1.000 49.54000  ? 48  PRO B N   1 
ATOM   3715  C  CA  . PRO B  1 17  ? 19.63800  -28.66000 13.70200  1.000 47.73000  ? 48  PRO B CA  1 
ATOM   3716  C  C   . PRO B  1 17  ? 19.07200  -30.01100 14.10000  1.000 40.16000  ? 48  PRO B C   1 
ATOM   3717  O  O   . PRO B  1 17  ? 19.54000  -31.06600 13.66500  1.000 42.09000  ? 48  PRO B O   1 
ATOM   3718  C  CB  . PRO B  1 17  ? 18.96300  -28.16000 12.42100  1.000 45.34000  ? 48  PRO B CB  1 
ATOM   3719  C  CG  . PRO B  1 17  ? 19.82800  -28.81000 11.32800  1.000 48.62000  ? 48  PRO B CG  1 
ATOM   3720  C  CD  . PRO B  1 17  ? 21.23600  -28.81100 11.86400  1.000 42.46000  ? 48  PRO B CD  1 
ATOM   3721  N  N   . ASN B  1 18  ? 18.04600  -29.95100 14.94200  1.000 38.61000  ? 49  ASN B N   1 
ATOM   3722  C  CA  . ASN B  1 18  ? 17.16500  -31.09100 15.13100  1.000 43.62000  ? 49  ASN B CA  1 
ATOM   3723  C  C   . ASN B  1 18  ? 16.35200  -31.30200 13.86200  1.000 38.79000  ? 49  ASN B C   1 
ATOM   3724  O  O   . ASN B  1 18  ? 16.06900  -30.35700 13.12100  1.000 37.10000  ? 49  ASN B O   1 
ATOM   3725  C  CB  . ASN B  1 18  ? 16.18600  -30.85300 16.29000  1.000 45.92000  ? 49  ASN B CB  1 
ATOM   3726  C  CG  . ASN B  1 18  ? 16.87100  -30.39900 17.57800  1.000 46.73000  ? 49  ASN B CG  1 
ATOM   3727  O  OD1 . ASN B  1 18  ? 17.61900  -31.16700 18.18800  1.000 42.09000  ? 49  ASN B OD1 1 
ATOM   3728  N  ND2 . ASN B  1 18  ? 16.59800  -29.15800 18.00400  1.000 37.83000  ? 49  ASN B ND2 1 
ATOM   3729  N  N   . ILE B  1 19  ? 15.92800  -32.54200 13.64300  1.000 37.42000  ? 50  ILE B N   1 
ATOM   3730  C  CA  . ILE B  1 19  ? 15.11900  -32.88900 12.48500  1.000 33.45000  ? 50  ILE B CA  1 
ATOM   3731  C  C   . ILE B  1 19  ? 13.89200  -33.66300 12.96100  1.000 37.90000  ? 50  ILE B C   1 
ATOM   3732  O  O   . ILE B  1 19  ? 14.03000  -34.69800 13.62800  1.000 39.50000  ? 50  ILE B O   1 
ATOM   3733  C  CB  . ILE B  1 19  ? 15.91800  -33.70900 11.46400  1.000 41.12000  ? 50  ILE B CB  1 
ATOM   3734  C  CG1 . ILE B  1 19  ? 17.15600  -32.93100 10.98100  1.000 43.21000  ? 50  ILE B CG1 1 
ATOM   3735  C  CG2 . ILE B  1 19  ? 15.06500  -34.01300 10.24300  1.000 35.01000  ? 50  ILE B CG2 1 
ATOM   3736  C  CD1 . ILE B  1 19  ? 18.13400  -33.84200 10.22100  1.000 40.96000  ? 50  ILE B CD1 1 
ATOM   3737  N  N   . LEU B  1 20  ? 12.69500  -33.14000 12.65900  1.000 38.33000  ? 51  LEU B N   1 
ATOM   3738  C  CA  . LEU B  1 20  ? 11.42100  -33.78700 12.98700  1.000 35.90000  ? 51  LEU B CA  1 
ATOM   3739  C  C   . LEU B  1 20  ? 10.66200  -34.06800 11.68700  1.000 34.37000  ? 51  LEU B C   1 
ATOM   3740  O  O   . LEU B  1 20  ? 10.25900  -33.13800 10.97700  1.000 33.58000  ? 51  LEU B O   1 
ATOM   3741  C  CB  . LEU B  1 20  ? 10.57800  -32.92200 13.92800  1.000 36.06000  ? 51  LEU B CB  1 
ATOM   3742  C  CG  . LEU B  1 20  ? 9.13800   -33.40800 14.20700  1.000 39.00000  ? 51  LEU B CG  1 
ATOM   3743  C  CD1 . LEU B  1 20  ? 9.15200   -34.77700 14.89600  1.000 33.97000  ? 51  LEU B CD1 1 
ATOM   3744  C  CD2 . LEU B  1 20  ? 8.38500   -32.43500 15.06100  1.000 35.37000  ? 51  LEU B CD2 1 
ATOM   3745  N  N   . VAL B  1 21  ? 10.47800  -35.33800 11.36500  1.000 31.57000  ? 52  VAL B N   1 
ATOM   3746  C  CA  . VAL B  1 21  ? 9.67300   -35.74800 10.21600  1.000 40.34000  ? 52  VAL B CA  1 
ATOM   3747  C  C   . VAL B  1 21  ? 8.30900   -36.16500 10.72800  1.000 37.37000  ? 52  VAL B C   1 
ATOM   3748  O  O   . VAL B  1 21  ? 8.19300   -37.18200 11.42400  1.000 42.07000  ? 52  VAL B O   1 
ATOM   3749  C  CB  . VAL B  1 21  ? 10.31200  -36.90500 9.43600   1.000 41.07000  ? 52  VAL B CB  1 
ATOM   3750  C  CG1 . VAL B  1 21  ? 9.41900   -37.26500 8.25300   1.000 37.21000  ? 52  VAL B CG1 1 
ATOM   3751  C  CG2 . VAL B  1 21  ? 11.68800  -36.52300 8.95900   1.000 36.04000  ? 52  VAL B CG2 1 
ATOM   3752  N  N   . VAL B  1 22  ? 7.27100   -35.41200 10.37700  1.000 38.15000  ? 53  VAL B N   1 
ATOM   3753  C  CA  . VAL B  1 22  ? 5.89500   -35.80300 10.67000  1.000 31.49000  ? 53  VAL B CA  1 
ATOM   3754  C  C   . VAL B  1 22  ? 5.32000   -36.43800 9.41700   1.000 35.65000  ? 53  VAL B C   1 
ATOM   3755  O  O   . VAL B  1 22  ? 5.03500   -35.74200 8.44000   1.000 38.14000  ? 53  VAL B O   1 
ATOM   3756  C  CB  . VAL B  1 22  ? 5.03500   -34.61800 11.12400  1.000 34.77000  ? 53  VAL B CB  1 
ATOM   3757  C  CG1 . VAL B  1 22  ? 3.60600   -35.11100 11.42500  1.000 35.05000  ? 53  VAL B CG1 1 
ATOM   3758  C  CG2 . VAL B  1 22  ? 5.63200   -33.96000 12.34200  1.000 34.74000  ? 53  VAL B CG2 1 
ATOM   3759  N  N   . LEU B  1 23  ? 5.14200   -37.76000 9.44000   1.000 36.13000  ? 54  LEU B N   1 
ATOM   3760  C  CA  . LEU B  1 23  ? 4.68200   -38.53200 8.28200   1.000 37.50000  ? 54  LEU B CA  1 
ATOM   3761  C  C   . LEU B  1 23  ? 3.28400   -39.08400 8.56400   1.000 39.35000  ? 54  LEU B C   1 
ATOM   3762  O  O   . LEU B  1 23  ? 3.13000   -39.96900 9.41800   1.000 38.75000  ? 54  LEU B O   1 
ATOM   3763  C  CB  . LEU B  1 23  ? 5.66500   -39.67000 8.00100   1.000 36.78000  ? 54  LEU B CB  1 
ATOM   3764  C  CG  . LEU B  1 23  ? 5.32200   -40.54800 6.80500   1.000 43.61000  ? 54  LEU B CG  1 
ATOM   3765  C  CD1 . LEU B  1 23  ? 5.35600   -39.68900 5.51800   1.000 41.68000  ? 54  LEU B CD1 1 
ATOM   3766  C  CD2 . LEU B  1 23  ? 6.25300   -41.77400 6.70600   1.000 31.13000  ? 54  LEU B CD2 1 
ATOM   3767  N  N   . CYS B  1 24  ? 2.27500   -38.59600 7.83900   1.000 30.80000  ? 55  CYS B N   1 
ATOM   3768  C  CA  . CYS B  1 24  ? 0.93500   -39.16300 7.95300   1.000 41.90000  ? 55  CYS B CA  1 
ATOM   3769  C  C   . CYS B  1 24  ? 0.74600   -40.32500 6.97700   1.000 41.88000  ? 55  CYS B C   1 
ATOM   3770  O  O   . CYS B  1 24  ? 1.51000   -40.49800 6.02600   1.000 34.00000  ? 55  CYS B O   1 
ATOM   3771  C  CB  . CYS B  1 24  ? -0.12700  -38.10700 7.68600   1.000 36.93000  ? 55  CYS B CB  1 
ATOM   3772  S  SG  . CYS B  1 24  ? -0.36500  -37.00100 9.03900   1.000 44.93000  ? 55  CYS B SG  1 
ATOM   3773  N  N   . ASP B  1 25  ? -0.33600  -41.09100 7.17900   1.000 41.77000  ? 56  ASP B N   1 
ATOM   3774  C  CA  . ASP B  1 25  ? -0.56100  -42.33900 6.45100   1.000 38.08000  ? 56  ASP B CA  1 
ATOM   3775  C  C   . ASP B  1 25  ? -1.85100  -42.23800 5.62800   1.000 41.79000  ? 56  ASP B C   1 
ATOM   3776  O  O   . ASP B  1 25  ? -2.95200  -42.29500 6.18700   1.000 36.68000  ? 56  ASP B O   1 
ATOM   3777  C  CB  . ASP B  1 25  ? -0.63200  -43.50700 7.43900   1.000 34.93000  ? 56  ASP B CB  1 
ATOM   3778  C  CG  . ASP B  1 25  ? -0.49700  -44.87200 6.75300   1.000 42.40000  ? 56  ASP B CG  1 
ATOM   3779  O  OD1 . ASP B  1 25  ? -0.42100  -44.89100 5.51000   1.000 45.97000  ? 56  ASP B OD1 1 
ATOM   3780  O  OD2 . ASP B  1 25  ? -0.43200  -45.91600 7.44600   1.000 38.42000  ? 56  ASP B OD2 1 
ATOM   3781  N  N   . ASP B  1 26  ? -1.71400  -42.16300 4.30000   1.000 35.42000  ? 57  ASP B N   1 
ATOM   3782  C  CA  . ASP B  1 26  ? -2.84000  -42.05000 3.36400   1.000 36.54000  ? 57  ASP B CA  1 
ATOM   3783  C  C   . ASP B  1 26  ? -3.56900  -40.70100 3.45200   1.000 39.84000  ? 57  ASP B C   1 
ATOM   3784  O  O   . ASP B  1 26  ? -4.76500  -40.62000 3.17100   1.000 37.44000  ? 57  ASP B O   1 
ATOM   3785  C  CB  . ASP B  1 26  ? -3.86500  -43.17900 3.55100   1.000 36.81000  ? 57  ASP B CB  1 
ATOM   3786  C  CG  . ASP B  1 26  ? -3.29900  -44.54800 3.22700   1.000 44.08000  ? 57  ASP B CG  1 
ATOM   3787  O  OD1 . ASP B  1 26  ? -2.10000  -44.66700 2.90300   1.000 41.99000  ? 57  ASP B OD1 1 
ATOM   3788  O  OD2 . ASP B  1 26  ? -4.07200  -45.51900 3.27500   1.000 43.88000  ? 57  ASP B OD2 1 
ATOM   3789  N  N   . LEU B  1 27  ? -2.87200  -39.62600 3.79500   1.000 39.11000  ? 58  LEU B N   1 
ATOM   3790  C  CA  . LEU B  1 27  ? -3.49900  -38.31100 3.81100   1.000 32.02000  ? 58  LEU B CA  1 
ATOM   3791  C  C   . LEU B  1 27  ? -3.69100  -37.80900 2.38300   1.000 39.64000  ? 58  LEU B C   1 
ATOM   3792  O  O   . LEU B  1 27  ? -2.74200  -37.79600 1.58500   1.000 38.44000  ? 58  LEU B O   1 
ATOM   3793  C  CB  . LEU B  1 27  ? -2.63700  -37.34900 4.60400   1.000 29.90000  ? 58  LEU B CB  1 
ATOM   3794  C  CG  . LEU B  1 27  ? -3.09200  -35.89300 4.65600   1.000 39.51000  ? 58  LEU B CG  1 
ATOM   3795  C  CD1 . LEU B  1 27  ? -4.20400  -35.77200 5.67100   1.000 34.71000  ? 58  LEU B CD1 1 
ATOM   3796  C  CD2 . LEU B  1 27  ? -1.87400  -35.00100 5.01900   1.000 38.62000  ? 58  LEU B CD2 1 
ATOM   3797  N  N   . GLY B  1 28  ? -4.93100  -37.43300 2.05000   1.000 38.10000  ? 59  GLY B N   1 
ATOM   3798  C  CA  . GLY B  1 28  ? -5.23900  -36.98900 0.70300   1.000 35.03000  ? 59  GLY B CA  1 
ATOM   3799  C  C   . GLY B  1 28  ? -4.68200  -35.61000 0.39100   1.000 35.90000  ? 59  GLY B C   1 
ATOM   3800  O  O   . GLY B  1 28  ? -4.45800  -34.77500 1.26300   1.000 32.73000  ? 59  GLY B O   1 
ATOM   3801  N  N   . TYR B  1 29  ? -4.49100  -35.35700 -0.90300  1.000 36.25000  ? 60  TYR B N   1 
ATOM   3802  C  CA  . TYR B  1 29  ? -3.83300  -34.12800 -1.33500  1.000 37.87000  ? 60  TYR B CA  1 
ATOM   3803  C  C   . TYR B  1 29  ? -4.56600  -32.86900 -0.87200  1.000 37.37000  ? 60  TYR B C   1 
ATOM   3804  O  O   . TYR B  1 29  ? -3.93000  -31.84400 -0.61100  1.000 38.63000  ? 60  TYR B O   1 
ATOM   3805  C  CB  . TYR B  1 29  ? -3.75200  -34.09600 -2.86500  1.000 33.59000  ? 60  TYR B CB  1 
ATOM   3806  C  CG  . TYR B  1 29  ? -2.66700  -33.17000 -3.37000  1.000 36.54000  ? 60  TYR B CG  1 
ATOM   3807  C  CD1 . TYR B  1 29  ? -1.32700  -33.40700 -3.04700  1.000 33.66000  ? 60  TYR B CD1 1 
ATOM   3808  C  CD2 . TYR B  1 29  ? -2.96300  -32.07300 -4.15900  1.000 38.98000  ? 60  TYR B CD2 1 
ATOM   3809  C  CE1 . TYR B  1 29  ? -0.32100  -32.58500 -3.49500  1.000 32.85000  ? 60  TYR B CE1 1 
ATOM   3810  C  CE2 . TYR B  1 29  ? -1.94100  -31.23100 -4.63600  1.000 38.76000  ? 60  TYR B CE2 1 
ATOM   3811  C  CZ  . TYR B  1 29  ? -0.62200  -31.50500 -4.29600  1.000 38.18000  ? 60  TYR B CZ  1 
ATOM   3812  O  OH  . TYR B  1 29  ? 0.41300   -30.70500 -4.74600  1.000 41.59000  ? 60  TYR B OH  1 
ATOM   3813  N  N   . ALA B  1 30  ? -5.88800  -32.92300 -0.76500  1.000 36.21000  ? 61  ALA B N   1 
ATOM   3814  C  CA  . ALA B  1 30  ? -6.69400  -31.76900 -0.39500  1.000 42.58000  ? 61  ALA B CA  1 
ATOM   3815  C  C   . ALA B  1 30  ? -7.17500  -31.82300 1.05100   1.000 42.21000  ? 61  ALA B C   1 
ATOM   3816  O  O   . ALA B  1 30  ? -8.19000  -31.20200 1.37900   1.000 41.21000  ? 61  ALA B O   1 
ATOM   3817  C  CB  . ALA B  1 30  ? -7.91900  -31.67200 -1.30600  1.000 34.00000  ? 61  ALA B CB  1 
ATOM   3818  N  N   . ASP B  1 31  ? -6.47500  -32.53600 1.92800   1.000 37.22000  ? 62  ASP B N   1 
ATOM   3819  C  CA  . ASP B  1 31  ? -7.03100  -32.80900 3.24900   1.000 41.86000  ? 62  ASP B CA  1 
ATOM   3820  C  C   . ASP B  1 31  ? -6.30100  -32.08900 4.37900   1.000 40.20000  ? 62  ASP B C   1 
ATOM   3821  O  O   . ASP B  1 31  ? -6.50600  -32.41600 5.55500   1.000 39.89000  ? 62  ASP B O   1 
ATOM   3822  C  CB  . ASP B  1 31  ? -7.09800  -34.32200 3.45100   1.000 36.36000  ? 62  ASP B CB  1 
ATOM   3823  C  CG  . ASP B  1 31  ? -8.15900  -34.95400 2.54700   1.000 42.33000  ? 62  ASP B CG  1 
ATOM   3824  O  OD1 . ASP B  1 31  ? -9.07800  -34.21100 2.13500   1.000 38.24000  ? 62  ASP B OD1 1 
ATOM   3825  O  OD2 . ASP B  1 31  ? -8.09000  -36.16600 2.22800   1.000 44.75000  ? 62  ASP B OD2 1 
ATOM   3826  N  N   . VAL B  1 32  ? -5.48700  -31.08700 4.04900   1.000 37.22000  ? 63  VAL B N   1 
ATOM   3827  C  CA  . VAL B  1 32  ? -4.97300  -30.13600 5.02300   1.000 34.85000  ? 63  VAL B CA  1 
ATOM   3828  C  C   . VAL B  1 32  ? -5.25700  -28.73800 4.49100   1.000 43.01000  ? 63  VAL B C   1 
ATOM   3829  O  O   . VAL B  1 32  ? -5.20600  -28.50200 3.28100   1.000 40.58000  ? 63  VAL B O   1 
ATOM   3830  C  CB  . VAL B  1 32  ? -3.46000  -30.32600 5.27300   1.000 43.38000  ? 63  VAL B CB  1 
ATOM   3831  C  CG1 . VAL B  1 32  ? -3.21800  -31.57900 6.09000   1.000 39.88000  ? 63  VAL B CG1 1 
ATOM   3832  C  CG2 . VAL B  1 32  ? -2.66900  -30.34400 3.92400   1.000 39.69000  ? 63  VAL B CG2 1 
ATOM   3833  N  N   . GLY B  1 33  ? -5.51100  -27.79600 5.40900   1.000 42.93000  ? 64  GLY B N   1 
ATOM   3834  C  CA  . GLY B  1 33  ? -5.85900  -26.43600 5.00500   1.000 37.06000  ? 64  GLY B CA  1 
ATOM   3835  C  C   . GLY B  1 33  ? -4.86100  -25.80300 4.04900   1.000 42.95000  ? 64  GLY B C   1 
ATOM   3836  O  O   . GLY B  1 33  ? -5.23700  -25.27700 3.00100   1.000 44.11000  ? 64  GLY B O   1 
ATOM   3837  N  N   . PHE B  1 34  ? -3.57100  -25.86800 4.38100   1.000 38.75000  ? 65  PHE B N   1 
ATOM   3838  C  CA  . PHE B  1 34  ? -2.56500  -25.19100 3.56600   1.000 38.55000  ? 65  PHE B CA  1 
ATOM   3839  C  C   . PHE B  1 34  ? -2.46600  -25.74600 2.14800   1.000 47.05000  ? 65  PHE B C   1 
ATOM   3840  O  O   . PHE B  1 34  ? -1.79800  -25.13800 1.30800   1.000 45.78000  ? 65  PHE B O   1 
ATOM   3841  C  CB  . PHE B  1 34  ? -1.18900  -25.25900 4.25300   1.000 34.04000  ? 65  PHE B CB  1 
ATOM   3842  C  CG  . PHE B  1 34  ? -0.50300  -26.62400 4.19900   1.000 38.55000  ? 65  PHE B CG  1 
ATOM   3843  C  CD1 . PHE B  1 34  ? 0.24100   -27.01500 3.08200   1.000 36.27000  ? 65  PHE B CD1 1 
ATOM   3844  C  CD2 . PHE B  1 34  ? -0.56100  -27.49700 5.29200   1.000 36.51000  ? 65  PHE B CD2 1 
ATOM   3845  C  CE1 . PHE B  1 34  ? 0.90000   -28.25300 3.05000   1.000 33.35000  ? 65  PHE B CE1 1 
ATOM   3846  C  CE2 . PHE B  1 34  ? 0.07900   -28.74100 5.26500   1.000 35.87000  ? 65  PHE B CE2 1 
ATOM   3847  C  CZ  . PHE B  1 34  ? 0.82100   -29.11700 4.14000   1.000 37.45000  ? 65  PHE B CZ  1 
ATOM   3848  N  N   . ASN B  1 35  ? -3.08700  -26.88800 1.86800   1.000 42.52000  ? 66  ASN B N   1 
ATOM   3849  C  CA  . ASN B  1 35  ? -3.07200  -27.48400 0.54200   1.000 44.20000  ? 66  ASN B CA  1 
ATOM   3850  C  C   . ASN B  1 35  ? -4.44900  -27.50500 -0.10200  1.000 44.57000  ? 66  ASN B C   1 
ATOM   3851  O  O   . ASN B  1 35  ? -4.69100  -28.32800 -0.98100  1.000 41.07000  ? 66  ASN B O   1 
ATOM   3852  C  CB  . ASN B  1 35  ? -2.51400  -28.90300 0.58500   1.000 42.39000  ? 66  ASN B CB  1 
ATOM   3853  C  CG  . ASN B  1 35  ? -1.55300  -29.16900 -0.53500  1.000 43.73000  ? 66  ASN B CG  1 
ATOM   3854  O  OD1 . ASN B  1 35  ? -0.66500  -28.35500 -0.80800  1.000 40.22000  ? 66  ASN B OD1 1 
ATOM   3855  N  ND2 . ASN B  1 35  ? -1.74400  -30.30100 -1.22700  1.000 35.78000  ? 66  ASN B ND2 1 
ATOM   3856  N  N   . GLY B  1 36  ? -5.37300  -26.67900 0.37400   1.000 45.58000  ? 67  GLY B N   1 
ATOM   3857  C  CA  . GLY B  1 36  ? -6.64400  -26.45000 -0.28800  1.000 36.82000  ? 67  GLY B CA  1 
ATOM   3858  C  C   . GLY B  1 36  ? -7.88600  -26.97600 0.41100   1.000 43.19000  ? 67  GLY B C   1 
ATOM   3859  O  O   . GLY B  1 36  ? -8.98400  -26.77700 -0.11600  1.000 45.31000  ? 67  GLY B O   1 
ATOM   3860  N  N   . SER B  1 37  ? -7.78400  -27.60000 1.58800   1.000 42.64000  ? 68  SER B N   1 
ATOM   3861  C  CA  . SER B  1 37  ? -8.98100  -28.16500 2.20400   1.000 45.04000  ? 68  SER B CA  1 
ATOM   3862  C  C   . SER B  1 37  ? -9.97100  -27.08400 2.62900   1.000 49.90000  ? 68  SER B C   1 
ATOM   3863  O  O   . SER B  1 37  ? -9.59200  -26.07600 3.23000   1.000 48.49000  ? 68  SER B O   1 
ATOM   3864  C  CB  . SER B  1 37  ? -8.64200  -29.01800 3.41200   1.000 43.14000  ? 68  SER B CB  1 
ATOM   3865  O  OG  . SER B  1 37  ? -9.85900  -29.51400 3.93700   1.000 45.61000  ? 68  SER B OG  1 
ATOM   3866  N  N   . THR B  1 38  ? -11.24300 -27.30600 2.31400   1.000 47.56000  ? 69  THR B N   1 
ATOM   3867  C  CA  . THR B  1 38  ? -12.31400 -26.42900 2.74300   1.000 46.70000  ? 69  THR B CA  1 
ATOM   3868  C  C   . THR B  1 38  ? -13.07100 -26.97600 3.93500   1.000 50.97000  ? 69  THR B C   1 
ATOM   3869  O  O   . THR B  1 38  ? -13.79400 -26.21600 4.58600   1.000 57.15000  ? 69  THR B O   1 
ATOM   3870  C  CB  . THR B  1 38  ? -13.33400 -26.18900 1.61000   1.000 54.26000  ? 69  THR B CB  1 
ATOM   3871  O  OG1 . THR B  1 38  ? -13.86200 -27.44000 1.14500   1.000 57.40000  ? 69  THR B OG1 1 
ATOM   3872  C  CG2 . THR B  1 38  ? -12.70000 -25.43200 0.45400   1.000 45.90000  ? 69  THR B CG2 1 
ATOM   3873  N  N   . ASP B  1 39  ? -12.95000 -28.26500 4.23400   1.000 44.47000  ? 70  ASP B N   1 
ATOM   3874  C  CA  . ASP B  1 39  ? -13.74900 -28.83100 5.31000   1.000 49.50000  ? 70  ASP B CA  1 
ATOM   3875  C  C   . ASP B  1 39  ? -12.93600 -29.41200 6.45600   1.000 46.85000  ? 70  ASP B C   1 
ATOM   3876  O  O   . ASP B  1 39  ? -13.47800 -29.56600 7.55400   1.000 50.42000  ? 70  ASP B O   1 
ATOM   3877  C  CB  . ASP B  1 39  ? -14.73000 -29.89600 4.78000   1.000 50.11000  ? 70  ASP B CB  1 
ATOM   3878  C  CG  . ASP B  1 39  ? -14.06000 -31.03200 3.97900   1.000 46.81000  ? 70  ASP B CG  1 
ATOM   3879  O  OD1 . ASP B  1 39  ? -12.86800 -30.96200 3.58500   1.000 46.12000  ? 70  ASP B OD1 1 
ATOM   3880  O  OD2 . ASP B  1 39  ? -14.77600 -32.02800 3.76100   1.000 42.64000  ? 70  ASP B OD2 1 
ATOM   3881  N  N   . ILE B  1 40  ? -11.67500 -29.74100 6.24600   1.000 46.73000  ? 71  ILE B N   1 
ATOM   3882  C  CA  . ILE B  1 40  ? -10.81900 -30.22300 7.31500   1.000 43.12000  ? 71  ILE B CA  1 
ATOM   3883  C  C   . ILE B  1 40  ? -10.02400 -29.05000 7.85500   1.000 45.65000  ? 71  ILE B C   1 
ATOM   3884  O  O   . ILE B  1 40  ? -9.38200  -28.32300 7.09100   1.000 51.42000  ? 71  ILE B O   1 
ATOM   3885  C  CB  . ILE B  1 40  ? -9.91200  -31.35200 6.81600   1.000 44.57000  ? 71  ILE B CB  1 
ATOM   3886  C  CG1 . ILE B  1 40  ? -10.78500 -32.48200 6.27300   1.000 37.55000  ? 71  ILE B CG1 1 
ATOM   3887  C  CG2 . ILE B  1 40  ? -8.99300  -31.81400 7.91500   1.000 44.14000  ? 71  ILE B CG2 1 
ATOM   3888  C  CD1 . ILE B  1 40  ? -10.00200 -33.67600 5.81400   1.000 43.54000  ? 71  ILE B CD1 1 
ATOM   3889  N  N   . LEU B  1 41  ? -10.10600 -28.83400 9.16200   1.000 42.29000  ? 72  LEU B N   1 
ATOM   3890  C  CA  . LEU B  1 41  ? -9.40700  -27.74900 9.83800   1.000 48.98000  ? 72  LEU B CA  1 
ATOM   3891  C  C   . LEU B  1 41  ? -8.09000  -28.28100 10.40600  1.000 44.94000  ? 72  LEU B C   1 
ATOM   3892  O  O   . LEU B  1 41  ? -8.08700  -29.24300 11.17700  1.000 37.29000  ? 72  LEU B O   1 
ATOM   3893  C  CB  . LEU B  1 41  ? -10.28300 -27.16100 10.94500  1.000 47.77000  ? 72  LEU B CB  1 
ATOM   3894  C  CG  . LEU B  1 41  ? -11.65100 -26.62700 10.49000  1.000 50.73000  ? 72  LEU B CG  1 
ATOM   3895  C  CD1 . LEU B  1 41  ? -12.54900 -26.29300 11.67400  1.000 44.28000  ? 72  LEU B CD1 1 
ATOM   3896  C  CD2 . LEU B  1 41  ? -11.47200 -25.38400 9.61000   1.000 45.34000  ? 72  LEU B CD2 1 
ATOM   3897  N  N   . THR B  1 42  ? -6.97500  -27.68600 9.98500   1.000 37.78000  ? 73  THR B N   1 
ATOM   3898  C  CA  . THR B  1 42  ? -5.64800  -28.04500 10.48400  1.000 38.55000  ? 73  THR B CA  1 
ATOM   3899  C  C   . THR B  1 42  ? -4.87400  -26.78400 10.86400  1.000 43.15000  ? 73  THR B C   1 
ATOM   3900  O  O   . THR B  1 42  ? -3.79600  -26.51800 10.32000  1.000 44.15000  ? 73  THR B O   1 
ATOM   3901  C  CB  . THR B  1 42  ? -4.87700  -28.85200 9.43400   1.000 47.31000  ? 73  THR B CB  1 
ATOM   3902  O  OG1 . THR B  1 42  ? -4.73300  -28.08100 8.22700   1.000 43.33000  ? 73  THR B OG1 1 
ATOM   3903  C  CG2 . THR B  1 42  ? -5.60100  -30.17600 9.10000   1.000 38.77000  ? 73  THR B CG2 1 
ATOM   3904  N  N   . PRO B  1 43  ? -5.37700  -25.99900 11.83000  1.000 44.30000  ? 74  PRO B N   1 
ATOM   3905  C  CA  . PRO B  1 43  ? -4.71200  -24.72300 12.13900  1.000 39.59000  ? 74  PRO B CA  1 
ATOM   3906  C  C   . PRO B  1 43  ? -3.24800  -24.85600 12.54400  1.000 45.52000  ? 74  PRO B C   1 
ATOM   3907  O  O   . PRO B  1 43  ? -2.44000  -23.99800 12.16000  1.000 42.76000  ? 74  PRO B O   1 
ATOM   3908  C  CB  . PRO B  1 43  ? -5.58300  -24.13800 13.26400  1.000 43.99000  ? 74  PRO B CB  1 
ATOM   3909  C  CG  . PRO B  1 43  ? -6.26000  -25.29600 13.86600  1.000 46.33000  ? 74  PRO B CG  1 
ATOM   3910  C  CD  . PRO B  1 43  ? -6.56600  -26.19300 12.68300  1.000 44.73000  ? 74  PRO B CD  1 
ATOM   3911  N  N   . GLU B  1 44  ? -2.86200  -25.87300 13.31800  1.000 41.38000  ? 75  GLU B N   1 
ATOM   3912  C  CA  . GLU B  1 44  ? -1.45200  -25.95200 13.70000  1.000 39.28000  ? 75  GLU B CA  1 
ATOM   3913  C  C   . GLU B  1 44  ? -0.55600  -26.21400 12.48600  1.000 37.68000  ? 75  GLU B C   1 
ATOM   3914  O  O   . GLU B  1 44  ? 0.48300   -25.56600 12.31200  1.000 38.15000  ? 75  GLU B O   1 
ATOM   3915  C  CB  . GLU B  1 44  ? -1.23600  -27.02900 14.76200  1.000 42.48000  ? 75  GLU B CB  1 
ATOM   3916  C  CG  . GLU B  1 44  ? -2.07400  -26.86800 16.03600  1.000 46.38000  ? 75  GLU B CG  1 
ATOM   3917  C  CD  . GLU B  1 44  ? -1.73600  -25.61900 16.81000  1.000 52.52000  ? 75  GLU B CD  1 
ATOM   3918  O  OE1 . GLU B  1 44  ? -0.56100  -25.19700 16.78500  1.000 50.55000  ? 75  GLU B OE1 1 
ATOM   3919  O  OE2 . GLU B  1 44  ? -2.64400  -25.07600 17.47600  1.000 60.76000  ? 75  GLU B OE2 1 
ATOM   3920  N  N   . LEU B  1 45  ? -0.91800  -27.20200 11.66600  1.000 44.63000  ? 76  LEU B N   1 
ATOM   3921  C  CA  . LEU B  1 45  ? -0.16100  -27.50500 10.45400  1.000 39.78000  ? 76  LEU B CA  1 
ATOM   3922  C  C   . LEU B  1 45  ? -0.11100  -26.30200 9.52000   1.000 39.54000  ? 76  LEU B C   1 
ATOM   3923  O  O   . LEU B  1 45  ? 0.94500   -25.98600 8.95300   1.000 39.11000  ? 76  LEU B O   1 
ATOM   3924  C  CB  . LEU B  1 45  ? -0.79600  -28.71000 9.73900   1.000 36.89000  ? 76  LEU B CB  1 
ATOM   3925  C  CG  . LEU B  1 45  ? -0.46000  -30.07700 10.36700  1.000 39.00000  ? 76  LEU B CG  1 
ATOM   3926  C  CD1 . LEU B  1 45  ? -1.36000  -31.18900 9.88200   1.000 39.43000  ? 76  LEU B CD1 1 
ATOM   3927  C  CD2 . LEU B  1 45  ? 0.99800   -30.44000 10.12600  1.000 36.69000  ? 76  LEU B CD2 1 
ATOM   3928  N  N   . ASP B  1 46  ? -1.23200  -25.59200 9.37300   1.000 37.47000  ? 77  ASP B N   1 
ATOM   3929  C  CA  . ASP B  1 46  ? -1.23000  -24.43200 8.48700   1.000 42.92000  ? 77  ASP B CA  1 
ATOM   3930  C  C   . ASP B  1 46  ? -0.25400  -23.36700 8.97700   1.000 44.89000  ? 77  ASP B C   1 
ATOM   3931  O  O   . ASP B  1 46  ? 0.50700   -22.79500 8.19000   1.000 39.72000  ? 77  ASP B O   1 
ATOM   3932  C  CB  . ASP B  1 46  ? -2.64100  -23.85600 8.36900   1.000 39.31000  ? 77  ASP B CB  1 
ATOM   3933  C  CG  . ASP B  1 46  ? -3.60700  -24.77800 7.60400   1.000 45.53000  ? 77  ASP B CG  1 
ATOM   3934  O  OD1 . ASP B  1 46  ? -3.17500  -25.82600 7.04400   1.000 42.46000  ? 77  ASP B OD1 1 
ATOM   3935  O  OD2 . ASP B  1 46  ? -4.82700  -24.46800 7.61100   1.000 47.71000  ? 77  ASP B OD2 1 
ATOM   3936  N  N   . ASN B  1 47  ? -0.25500  -23.09300 10.28000  1.000 41.50000  ? 78  ASN B N   1 
ATOM   3937  C  CA  . ASN B  1 47  ? 0.64200   -22.08100 10.81500  1.000 44.18000  ? 78  ASN B CA  1 
ATOM   3938  C  C   . ASN B  1 47  ? 2.10700   -22.44000 10.56900  1.000 45.32000  ? 78  ASN B C   1 
ATOM   3939  O  O   . ASN B  1 47  ? 2.90400   -21.58000 10.17100  1.000 44.47000  ? 78  ASN B O   1 
ATOM   3940  C  CB  . ASN B  1 47  ? 0.36300   -21.87700 12.29800  1.000 48.88000  ? 78  ASN B CB  1 
ATOM   3941  C  CG  . ASN B  1 47  ? 1.25500   -20.84000 12.89300  1.000 48.39000  ? 78  ASN B CG  1 
ATOM   3942  O  OD1 . ASN B  1 47  ? 1.08000   -19.64300 12.66700  1.000 57.25000  ? 78  ASN B OD1 1 
ATOM   3943  N  ND2 . ASN B  1 47  ? 2.25800   -21.29400 13.62800  1.000 52.23000  ? 78  ASN B ND2 1 
ATOM   3944  N  N   . LEU B  1 48  ? 2.48500   -23.69900 10.80000  1.000 38.63000  ? 79  LEU B N   1 
ATOM   3945  C  CA  . LEU B  1 48  ? 3.84000   -24.13100 10.44500  1.000 39.22000  ? 79  LEU B CA  1 
ATOM   3946  C  C   . LEU B  1 48  ? 4.11500   -23.92000 8.95600   1.000 44.49000  ? 79  LEU B C   1 
ATOM   3947  O  O   . LEU B  1 48  ? 5.14900   -23.35400 8.57800   1.000 47.55000  ? 79  LEU B O   1 
ATOM   3948  C  CB  . LEU B  1 48  ? 4.03900   -25.60100 10.81100  1.000 38.43000  ? 79  LEU B CB  1 
ATOM   3949  C  CG  . LEU B  1 48  ? 4.02500   -25.90700 12.31600  1.000 36.91000  ? 79  LEU B CG  1 
ATOM   3950  C  CD1 . LEU B  1 48  ? 4.27700   -27.39100 12.56900  1.000 29.41000  ? 79  LEU B CD1 1 
ATOM   3951  C  CD2 . LEU B  1 48  ? 5.03600   -25.02200 13.03100  1.000 34.46000  ? 79  LEU B CD2 1 
ATOM   3952  N  N   . ALA B  1 49  ? 3.17400   -24.32300 8.09600   1.000 38.79000  ? 80  ALA B N   1 
ATOM   3953  C  CA  . ALA B  1 49  ? 3.40300   -24.21900 6.65700   1.000 44.73000  ? 80  ALA B CA  1 
ATOM   3954  C  C   . ALA B  1 49  ? 3.54600   -22.75800 6.21300   1.000 45.15000  ? 80  ALA B C   1 
ATOM   3955  O  O   . ALA B  1 49  ? 4.44500   -22.42800 5.43400   1.000 49.34000  ? 80  ALA B O   1 
ATOM   3956  C  CB  . ALA B  1 49  ? 2.27400   -24.92500 5.89400   1.000 33.55000  ? 80  ALA B CB  1 
ATOM   3957  N  N   . GLN B  1 50  ? 2.68800   -21.86800 6.71700   1.000 40.82000  ? 81  GLN B N   1 
ATOM   3958  C  CA  . GLN B  1 50  ? 2.77300   -20.45000 6.37600   1.000 40.95000  ? 81  GLN B CA  1 
ATOM   3959  C  C   . GLN B  1 50  ? 4.08300   -19.82100 6.85100   1.000 46.55000  ? 81  GLN B C   1 
ATOM   3960  O  O   . GLN B  1 50  ? 4.52100   -18.80700 6.29600   1.000 53.20000  ? 81  GLN B O   1 
ATOM   3961  C  CB  . GLN B  1 50  ? 1.56100   -19.71700 6.94200   1.000 44.48000  ? 81  GLN B CB  1 
ATOM   3962  C  CG  . GLN B  1 50  ? 0.24500   -20.31900 6.40200   1.000 51.27000  ? 81  GLN B CG  1 
ATOM   3963  C  CD  . GLN B  1 50  ? -0.99700  -19.77500 7.08200   1.000 54.41000  ? 81  GLN B CD  1 
ATOM   3964  O  OE1 . GLN B  1 50  ? -0.90900  -18.96100 8.00200   1.000 55.03000  ? 81  GLN B OE1 1 
ATOM   3965  N  NE2 . GLN B  1 50  ? -2.17200  -20.23800 6.63700   1.000 55.11000  ? 81  GLN B NE2 1 
ATOM   3966  N  N   . ASN B  1 51  ? 4.70100   -20.36800 7.89200   1.000 43.92000  ? 82  ASN B N   1 
ATOM   3967  C  CA  . ASN B  1 51  ? 5.97600   -19.85800 8.38100   1.000 48.82000  ? 82  ASN B CA  1 
ATOM   3968  C  C   . ASN B  1 51  ? 7.16100   -20.61500 7.82300   1.000 45.23000  ? 82  ASN B C   1 
ATOM   3969  O  O   . ASN B  1 51  ? 8.25600   -20.52000 8.37200   1.000 49.69000  ? 82  ASN B O   1 
ATOM   3970  C  CB  . ASN B  1 51  ? 6.00400   -19.85800 9.90900   1.000 41.95000  ? 82  ASN B CB  1 
ATOM   3971  C  CG  . ASN B  1 51  ? 5.09400   -18.79400 10.48100  1.000 51.11000  ? 82  ASN B CG  1 
ATOM   3972  O  OD1 . ASN B  1 51  ? 5.49000   -17.64300 10.60300  1.000 59.56000  ? 82  ASN B OD1 1 
ATOM   3973  N  ND2 . ASN B  1 51  ? 3.85400   -19.15200 10.76800  1.000 47.66000  ? 82  ASN B ND2 1 
ATOM   3974  N  N   . GLY B  1 52  ? 6.97300   -21.35500 6.75300   1.000 51.80000  ? 83  GLY B N   1 
ATOM   3975  C  CA  . GLY B  1 52  ? 8.05900   -22.07000 6.10500   1.000 45.99000  ? 83  GLY B CA  1 
ATOM   3976  C  C   . GLY B  1 52  ? 7.81200   -22.13500 4.61300   1.000 47.11000  ? 83  GLY B C   1 
ATOM   3977  O  O   . GLY B  1 52  ? 7.20500   -21.23300 4.02500   1.000 44.86000  ? 83  GLY B O   1 
ATOM   3978  N  N   . SER B  1 53  ? 8.26300   -23.22300 4.00100   1.000 44.65000  ? 84  SER B N   1 
ATOM   3979  C  CA  . SER B  1 53  ? 8.16400   -23.41000 2.56300   1.000 45.15000  ? 84  SER B CA  1 
ATOM   3980  C  C   . SER B  1 53  ? 7.17700   -24.54300 2.26700   1.000 44.21000  ? 84  SER B C   1 
ATOM   3981  O  O   . SER B  1 53  ? 7.35700   -25.67800 2.73200   1.000 43.11000  ? 84  SER B O   1 
ATOM   3982  C  CB  . SER B  1 53  ? 9.54700   -23.70400 1.98300   1.000 41.97000  ? 84  SER B CB  1 
ATOM   3983  O  OG  . SER B  1 53  ? 9.44900   -24.08900 0.62400   1.000 48.06000  ? 84  SER B OG  1 
ATOM   3984  N  N   . ILE B  1 54  ? 6.11700   -24.22400 1.53000   1.000 44.90000  ? 85  ILE B N   1 
ATOM   3985  C  CA  . ILE B  1 54  ? 5.15100   -25.21800 1.05300   1.000 35.16000  ? 85  ILE B CA  1 
ATOM   3986  C  C   . ILE B  1 54  ? 5.61700   -25.74900 -0.30300  1.000 42.56000  ? 85  ILE B C   1 
ATOM   3987  O  O   . ILE B  1 54  ? 6.01000   -24.97000 -1.18000  1.000 41.12000  ? 85  ILE B O   1 
ATOM   3988  C  CB  . ILE B  1 54  ? 3.75700   -24.59300 0.94300   1.000 40.61000  ? 85  ILE B CB  1 
ATOM   3989  C  CG1 . ILE B  1 54  ? 3.23800   -24.20000 2.33100   1.000 36.76000  ? 85  ILE B CG1 1 
ATOM   3990  C  CG2 . ILE B  1 54  ? 2.79700   -25.53200 0.16200   1.000 42.06000  ? 85  ILE B CG2 1 
ATOM   3991  C  CD1 . ILE B  1 54  ? 1.97800   -23.35800 2.25900   1.000 37.31000  ? 85  ILE B CD1 1 
ATOM   3992  N  N   . PHE B  1 55  ? 5.57100   -27.06700 -0.48600  1.000 36.80000  ? 86  PHE B N   1 
ATOM   3993  C  CA  . PHE B  1 55  ? 6.02900   -27.70700 -1.72300  1.000 38.84000  ? 86  PHE B CA  1 
ATOM   3994  C  C   . PHE B  1 55  ? 4.81300   -28.11000 -2.56000  1.000 38.80000  ? 86  PHE B C   1 
ATOM   3995  O  O   . PHE B  1 55  ? 4.08400   -29.04300 -2.20500  1.000 35.42000  ? 86  PHE B O   1 
ATOM   3996  C  CB  . PHE B  1 55  ? 6.90100   -28.91500 -1.41400  1.000 38.98000  ? 86  PHE B CB  1 
ATOM   3997  C  CG  . PHE B  1 55  ? 8.21000   -28.56800 -0.79600  1.000 39.94000  ? 86  PHE B CG  1 
ATOM   3998  C  CD1 . PHE B  1 55  ? 8.27800   -28.14300 0.52800   1.000 43.66000  ? 86  PHE B CD1 1 
ATOM   3999  C  CD2 . PHE B  1 55  ? 9.38100   -28.64300 -1.53500  1.000 40.69000  ? 86  PHE B CD2 1 
ATOM   4000  C  CE1 . PHE B  1 55  ? 9.49800   -27.80200 1.11300   1.000 38.61000  ? 86  PHE B CE1 1 
ATOM   4001  C  CE2 . PHE B  1 55  ? 10.61200  -28.31800 -0.94900  1.000 45.89000  ? 86  PHE B CE2 1 
ATOM   4002  C  CZ  . PHE B  1 55  ? 10.66300  -27.89800 0.37700   1.000 41.00000  ? 86  PHE B CZ  1 
ATOM   4003  N  N   . THR B  1 56  ? 4.59400   -27.39900 -3.67200  1.000 39.43000  ? 87  THR B N   1 
ATOM   4004  C  CA  . THR B  1 56  ? 3.40700   -27.61900 -4.49400  1.000 40.23000  ? 87  THR B CA  1 
ATOM   4005  C  C   . THR B  1 56  ? 3.55700   -28.76800 -5.48500  1.000 36.11000  ? 87  THR B C   1 
ATOM   4006  O  O   . THR B  1 56  ? 2.55400   -29.18100 -6.07200  1.000 34.24000  ? 87  THR B O   1 
ATOM   4007  C  CB  . THR B  1 56  ? 3.04400   -26.33100 -5.24700  1.000 40.78000  ? 87  THR B CB  1 
ATOM   4008  O  OG1 . THR B  1 56  ? 4.10900   -25.98400 -6.14100  1.000 43.51000  ? 87  THR B OG1 1 
ATOM   4009  C  CG2 . THR B  1 56  ? 2.80500   -25.17900 -4.25300  1.000 39.02000  ? 87  THR B CG2 1 
ATOM   4010  N  N   . SER B  1 57  ? 4.76200   -29.33600 -5.65300  1.000 37.07000  ? 88  SER B N   1 
ATOM   4011  C  CA  . SER B  1 57  ? 4.95400   -30.53400 -6.49800  1.000 37.85000  ? 88  SER B CA  1 
ATOM   4012  C  C   . SER B  1 57  ? 5.90200   -31.50500 -5.77200  1.000 39.91000  ? 88  SER B C   1 
ATOM   4013  O  O   . SER B  1 57  ? 7.02100   -31.76400 -6.22400  1.000 35.28000  ? 88  SER B O   1 
ATOM   4014  C  CB  . SER B  1 57  ? 5.50100   -30.16500 -7.88000  1.000 37.12000  ? 88  SER B CB  1 
ATOM   4015  O  OG  . SER B  1 57  ? 4.49200   -29.67900 -8.74100  1.000 39.05000  ? 88  SER B OG  1 
ATOM   4016  N  N   . ALA B  1 58  ? 5.45900   -32.04000 -4.62200  1.000 37.16000  ? 89  ALA B N   1 
ATOM   4017  C  CA  . ALA B  1 58  ? 6.23900   -33.01500 -3.85800  1.000 33.88000  ? 89  ALA B CA  1 
ATOM   4018  C  C   . ALA B  1 58  ? 5.76700   -34.42800 -4.18200  1.000 37.06000  ? 89  ALA B C   1 
ATOM   4019  O  O   . ALA B  1 58  ? 4.56000   -34.67900 -4.28700  1.000 34.99000  ? 89  ALA B O   1 
ATOM   4020  C  CB  . ALA B  1 58  ? 6.11600   -32.78100 -2.34500  1.000 28.17000  ? 89  ALA B CB  1 
ATOM   4021  N  N   . TYR B  1 59  ? 6.71500   -35.35700 -4.32600  1.000 32.16000  ? 90  TYR B N   1 
ATOM   4022  C  CA  . TYR B  1 59  ? 6.37800   -36.72300 -4.69500  1.000 30.12000  ? 90  TYR B CA  1 
ATOM   4023  C  C   . TYR B  1 59  ? 7.03800   -37.73000 -3.77300  1.000 34.54000  ? 90  TYR B C   1 
ATOM   4024  O  O   . TYR B  1 59  ? 8.20400   -37.57800 -3.40200  1.000 37.74000  ? 90  TYR B O   1 
ATOM   4025  C  CB  . TYR B  1 59  ? 6.80000   -37.03900 -6.12800  1.000 35.41000  ? 90  TYR B CB  1 
ATOM   4026  C  CG  . TYR B  1 59  ? 6.09800   -36.21400 -7.16500  1.000 34.25000  ? 90  TYR B CG  1 
ATOM   4027  C  CD1 . TYR B  1 59  ? 6.56900   -34.94800 -7.49500  1.000 35.89000  ? 90  TYR B CD1 1 
ATOM   4028  C  CD2 . TYR B  1 59  ? 4.96400   -36.69900 -7.83200  1.000 31.19000  ? 90  TYR B CD2 1 
ATOM   4029  C  CE1 . TYR B  1 59  ? 5.93600   -34.16800 -8.46700  1.000 32.87000  ? 90  TYR B CE1 1 
ATOM   4030  C  CE2 . TYR B  1 59  ? 4.31800   -35.91700 -8.79300  1.000 32.20000  ? 90  TYR B CE2 1 
ATOM   4031  C  CZ  . TYR B  1 59  ? 4.81900   -34.65100 -9.11300  1.000 34.46000  ? 90  TYR B CZ  1 
ATOM   4032  O  OH  . TYR B  1 59  ? 4.22600   -33.85400 -10.08400 1.000 36.24000  ? 90  TYR B OH  1 
ATOM   4033  N  N   . VAL B  1 60  ? 6.30500   -38.78600 -3.45300  1.000 31.48000  ? 91  VAL B N   1 
ATOM   4034  C  CA  . VAL B  1 60  ? 6.89600   -39.95000 -2.81900  1.000 29.03000  ? 91  VAL B CA  1 
ATOM   4035  C  C   . VAL B  1 60  ? 7.31300   -40.92300 -3.91800  1.000 32.87000  ? 91  VAL B C   1 
ATOM   4036  O  O   . VAL B  1 60  ? 6.93800   -40.77800 -5.07400  1.000 36.51000  ? 91  VAL B O   1 
ATOM   4037  C  CB  . VAL B  1 60  ? 5.92700   -40.60200 -1.80200  1.000 38.94000  ? 91  VAL B CB  1 
ATOM   4038  C  CG1 . VAL B  1 60  ? 5.71000   -39.67300 -0.59400  1.000 35.93000  ? 91  VAL B CG1 1 
ATOM   4039  C  CG2 . VAL B  1 60  ? 4.55600   -40.89700 -2.47100  1.000 34.25000  ? 91  VAL B CG2 1 
ATOM   4040  N  N   . ALA B  1 61  ? 8.15300   -41.88800 -3.57200  1.000 39.94000  ? 92  ALA B N   1 
ATOM   4041  C  CA  . ALA B  1 61  ? 8.77600   -42.77000 -4.55000  1.000 33.91000  ? 92  ALA B CA  1 
ATOM   4042  C  C   . ALA B  1 61  ? 7.92000   -43.97500 -4.91900  1.000 39.21000  ? 92  ALA B C   1 
ATOM   4043  O  O   . ALA B  1 61  ? 8.34600   -44.78200 -5.75400  1.000 39.60000  ? 92  ALA B O   1 
ATOM   4044  C  CB  . ALA B  1 61  ? 10.12100  -43.25600 -4.02000  1.000 35.61000  ? 92  ALA B CB  1 
ATOM   4045  N  N   . HIS B  1 62  ? 6.74100   -44.13600 -4.30700  1.000 34.45000  ? 93  HIS B N   1 
ATOM   4046  C  CA  . HIS B  1 62  ? 5.85400   -45.23000 -4.68000  1.000 34.89000  ? 93  HIS B CA  1 
ATOM   4047  C  C   . HIS B  1 62  ? 4.45900   -44.87500 -4.18700  1.000 39.47000  ? 93  HIS B C   1 
ATOM   4048  O  O   . HIS B  1 62  ? 4.33200   -44.22200 -3.13700  1.000 33.82000  ? 93  HIS B O   1 
ATOM   4049  C  CB  . HIS B  1 62  ? 6.33900   -46.57200 -4.10000  1.000 33.40000  ? 93  HIS B CB  1 
ATOM   4050  C  CG  . HIS B  1 62  ? 5.76800   -47.77900 -4.78100  1.000 35.66000  ? 93  HIS B CG  1 
ATOM   4051  N  ND1 . HIS B  1 62  ? 6.19000   -48.19600 -6.02700  1.000 35.34000  ? 93  HIS B ND1 1 
ATOM   4052  C  CD2 . HIS B  1 62  ? 4.85100   -48.69200 -4.36800  1.000 38.96000  ? 93  HIS B CD2 1 
ATOM   4053  C  CE1 . HIS B  1 62  ? 5.52900   -49.29300 -6.36700  1.000 39.40000  ? 93  HIS B CE1 1 
ATOM   4054  N  NE2 . HIS B  1 62  ? 4.71500   -49.61900 -5.37500  1.000 36.45000  ? 93  HIS B NE2 1 
ATOM   4055  N  N   . PRO B  1 63  ? 3.40300   -45.23700 -4.92000  1.000 36.62000  ? 94  PRO B N   1 
ATOM   4056  C  CA  . PRO B  1 63  ? 2.06000   -44.80400 -4.51100  1.000 33.67000  ? 94  PRO B CA  1 
ATOM   4057  C  C   . PRO B  1 63  ? 1.40200   -45.63200 -3.40600  1.000 41.30000  ? 94  PRO B C   1 
ATOM   4058  O  O   . PRO B  1 63  ? 0.17500   -45.54300 -3.30800  1.000 36.38000  ? 94  PRO B O   1 
ATOM   4059  C  CB  . PRO B  1 63  ? 1.25300   -44.88700 -5.82100  1.000 35.11000  ? 94  PRO B CB  1 
ATOM   4060  C  CG  . PRO B  1 63  ? 1.92800   -45.99000 -6.61900  1.000 35.08000  ? 94  PRO B CG  1 
ATOM   4061  C  CD  . PRO B  1 63  ? 3.42300   -45.80600 -6.28500  1.000 35.03000  ? 94  PRO B CD  1 
ATOM   4062  N  N   . PHE B  1 64  ? 2.11700   -46.45000 -2.60600  1.000 32.43000  ? 95  PHE B N   1 
ATOM   4063  C  CA  . PHE B  1 64  ? 1.48100   -47.00200 -1.40600  1.000 39.32000  ? 95  PHE B CA  1 
ATOM   4064  C  C   . PHE B  1 64  ? 2.53700   -47.35900 -0.35000  1.000 40.07000  ? 95  PHE B C   1 
ATOM   4065  O  O   . PHE B  1 64  ? 3.74000   -47.28200 -0.59900  1.000 38.98000  ? 95  PHE B O   1 
ATOM   4066  C  CB  . PHE B  1 64  ? 0.53600   -48.18200 -1.72800  1.000 32.16000  ? 95  PHE B CB  1 
ATOM   4067  C  CG  . PHE B  1 64  ? 1.20200   -49.35400 -2.39200  1.000 37.19000  ? 95  PHE B CG  1 
ATOM   4068  C  CD1 . PHE B  1 64  ? 1.91000   -50.28100 -1.63900  1.000 35.83000  ? 95  PHE B CD1 1 
ATOM   4069  C  CD2 . PHE B  1 64  ? 1.10700   -49.54500 -3.76600  1.000 39.70000  ? 95  PHE B CD2 1 
ATOM   4070  C  CE1 . PHE B  1 64  ? 2.52700   -51.37700 -2.23300  1.000 33.66000  ? 95  PHE B CE1 1 
ATOM   4071  C  CE2 . PHE B  1 64  ? 1.73300   -50.64200 -4.37900  1.000 42.20000  ? 95  PHE B CE2 1 
ATOM   4072  C  CZ  . PHE B  1 64  ? 2.44700   -51.55600 -3.60200  1.000 35.85000  ? 95  PHE B CZ  1 
ATOM   4073  N  N   A CYS B  1 65  ? 2.04900   -47.81800 0.80700   0.300 40.71000  ? 96  CYS B N   1 
ATOM   4074  C  CA  A CYS B  1 65  ? 2.69900   -47.72400 2.11200   0.300 39.64000  ? 96  CYS B CA  1 
ATOM   4075  C  C   A CYS B  1 65  ? 4.13100   -48.26300 2.18100   0.300 38.98000  ? 96  CYS B C   1 
ATOM   4076  O  O   A CYS B  1 65  ? 5.07800   -47.47300 2.22400   0.300 37.25000  ? 96  CYS B O   1 
ATOM   4077  C  CB  A CYS B  1 65  ? 1.80700   -48.42500 3.14800   0.300 42.27000  ? 96  CYS B CB  1 
ATOM   4078  S  SG  A CYS B  1 65  ? 0.08100   -47.79300 3.18500   0.300 42.41000  ? 96  CYS B SG  1 
HETATM 4079  N  N   B DDZ B  1 65  ? 2.02900   -47.80000 0.81500   0.700 41.00000  ? 96  DDZ B N   1 
HETATM 4080  C  CA  B DDZ B  1 65  ? 2.65200   -47.79100 2.17400   0.700 39.84000  ? 96  DDZ B CA  1 
HETATM 4081  C  C   B DDZ B  1 65  ? 4.10800   -48.27600 2.16000   0.700 38.53000  ? 96  DDZ B C   1 
HETATM 4082  O  O   B DDZ B  1 65  ? 5.01700   -47.42900 2.14800   0.700 36.77000  ? 96  DDZ B O   1 
HETATM 4083  O  OG1 B DDZ B  1 65  ? 2.57800   -48.93400 4.33400   0.700 45.72000  ? 96  DDZ B OG1 1 
HETATM 4084  O  OG2 B DDZ B  1 65  ? 0.56700   -48.07500 3.46100   0.700 43.67000  ? 96  DDZ B OG2 1 
HETATM 4085  C  CB  B DDZ B  1 65  ? 1.83200   -48.65700 3.15000   0.700 42.30000  ? 96  DDZ B CB  1 
ATOM   4086  N  N   . GLY B  1 66  ? 4.30500   -49.58700 2.20900   1.000 42.18000  ? 97  GLY B N   1 
ATOM   4087  C  CA  . GLY B  1 66  ? 5.60500   -50.19700 2.42300   1.000 44.05000  ? 97  GLY B CA  1 
ATOM   4088  C  C   . GLY B  1 66  ? 6.74900   -49.68400 1.56800   1.000 40.83000  ? 97  GLY B C   1 
ATOM   4089  O  O   . GLY B  1 66  ? 7.79300   -49.28500 2.08500   1.000 37.18000  ? 97  GLY B O   1 
ATOM   4090  N  N   . PRO B  1 67  ? 6.58600   -49.70100 0.24100   1.000 41.11000  ? 98  PRO B N   1 
ATOM   4091  C  CA  . PRO B  1 67  ? 7.67800   -49.20700 -0.62200  1.000 36.48000  ? 98  PRO B CA  1 
ATOM   4092  C  C   . PRO B  1 67  ? 7.97200   -47.73400 -0.44100  1.000 41.05000  ? 98  PRO B C   1 
ATOM   4093  O  O   . PRO B  1 67  ? 9.13900   -47.32400 -0.54100  1.000 42.20000  ? 98  PRO B O   1 
ATOM   4094  C  CB  . PRO B  1 67  ? 7.17600   -49.53000 -2.03400  1.000 35.03000  ? 98  PRO B CB  1 
ATOM   4095  C  CG  . PRO B  1 67  ? 6.30000   -50.75300 -1.82400  1.000 38.79000  ? 98  PRO B CG  1 
ATOM   4096  C  CD  . PRO B  1 67  ? 5.58400   -50.47000 -0.52000  1.000 35.73000  ? 98  PRO B CD  1 
ATOM   4097  N  N   . SER B  1 68  ? 6.94700   -46.91000 -0.20000  1.000 37.65000  ? 99  SER B N   1 
ATOM   4098  C  CA  . SER B  1 68  ? 7.21400   -45.49500 0.03800   1.000 37.10000  ? 99  SER B CA  1 
ATOM   4099  C  C   . SER B  1 68  ? 8.06300   -45.32100 1.29800   1.000 38.83000  ? 99  SER B C   1 
ATOM   4100  O  O   . SER B  1 68  ? 9.04900   -44.56900 1.29800   1.000 34.04000  ? 99  SER B O   1 
ATOM   4101  C  CB  . SER B  1 68  ? 5.90400   -44.70100 0.10000   1.000 37.74000  ? 99  SER B CB  1 
ATOM   4102  O  OG  . SER B  1 68  ? 6.11600   -43.34900 0.47000   1.000 37.22000  ? 99  SER B OG  1 
ATOM   4103  N  N   . ARG B  1 69  ? 7.72900   -46.05000 2.36300   1.000 36.84000  ? 100 ARG B N   1 
ATOM   4104  C  CA  . ARG B  1 69  ? 8.50300   -45.95100 3.59400   1.000 37.31000  ? 100 ARG B CA  1 
ATOM   4105  C  C   . ARG B  1 69  ? 9.90400   -46.53800 3.41600   1.000 42.22000  ? 100 ARG B C   1 
ATOM   4106  O  O   . ARG B  1 69  ? 10.89400  -45.95900 3.87900   1.000 36.20000  ? 100 ARG B O   1 
ATOM   4107  C  CB  . ARG B  1 69  ? 7.73100   -46.62300 4.71900   1.000 40.39000  ? 100 ARG B CB  1 
ATOM   4108  C  CG  . ARG B  1 69  ? 6.50600   -45.79200 5.08500   1.000 41.31000  ? 100 ARG B CG  1 
ATOM   4109  C  CD  . ARG B  1 69  ? 5.42100   -46.60000 5.75600   1.000 34.50000  ? 100 ARG B CD  1 
ATOM   4110  N  NE  . ARG B  1 69  ? 4.18100   -45.83300 5.77100   1.000 42.43000  ? 100 ARG B NE  1 
ATOM   4111  C  CZ  . ARG B  1 69  ? 3.84700   -44.95300 6.70200   1.000 38.42000  ? 100 ARG B CZ  1 
ATOM   4112  N  NH1 . ARG B  1 69  ? 4.58100   -44.78700 7.78600   1.000 34.98000  ? 100 ARG B NH1 1 
ATOM   4113  N  NH2 . ARG B  1 69  ? 2.74800   -44.22000 6.53800   1.000 38.77000  ? 100 ARG B NH2 1 
ATOM   4114  N  N   . SER B  1 70  ? 10.00900  -47.66500 2.71300   1.000 41.10000  ? 101 SER B N   1 
ATOM   4115  C  CA  . SER B  1 70  ? 11.31600  -48.19100 2.35200   1.000 40.60000  ? 101 SER B CA  1 
ATOM   4116  C  C   . SER B  1 70  ? 12.16900  -47.13800 1.64600   1.000 39.75000  ? 101 SER B C   1 
ATOM   4117  O  O   . SER B  1 70  ? 13.36200  -47.00800 1.92500   1.000 43.01000  ? 101 SER B O   1 
ATOM   4118  C  CB  . SER B  1 70  ? 11.14300  -49.43500 1.48400   1.000 40.17000  ? 101 SER B CB  1 
ATOM   4119  O  OG  . SER B  1 70  ? 12.33200  -49.74500 0.80900   1.000 47.89000  ? 101 SER B OG  1 
ATOM   4120  N  N   . ALA B  1 71  ? 11.57700  -46.37600 0.73200   1.000 40.91000  ? 102 ALA B N   1 
ATOM   4121  C  CA  . ALA B  1 71  ? 12.34000  -45.35000 0.02400   1.000 37.13000  ? 102 ALA B CA  1 
ATOM   4122  C  C   . ALA B  1 71  ? 12.74400  -44.19100 0.93000   1.000 43.94000  ? 102 ALA B C   1 
ATOM   4123  O  O   . ALA B  1 71  ? 13.85200  -43.65700 0.79600   1.000 40.05000  ? 102 ALA B O   1 
ATOM   4124  C  CB  . ALA B  1 71  ? 11.54300  -44.81900 -1.15300  1.000 39.33000  ? 102 ALA B CB  1 
ATOM   4125  N  N   . ILE B  1 72  ? 11.85100  -43.74900 1.82400   1.000 37.65000  ? 103 ILE B N   1 
ATOM   4126  C  CA  . ILE B  1 72  ? 12.18800  -42.61000 2.67200   1.000 40.90000  ? 103 ILE B CA  1 
ATOM   4127  C  C   . ILE B  1 72  ? 13.41100  -42.92400 3.52900   1.000 42.18000  ? 103 ILE B C   1 
ATOM   4128  O  O   . ILE B  1 72  ? 14.34300  -42.12200 3.61000   1.000 39.49000  ? 103 ILE B O   1 
ATOM   4129  C  CB  . ILE B  1 72  ? 10.99000  -42.18800 3.53900   1.000 44.34000  ? 103 ILE B CB  1 
ATOM   4130  C  CG1 . ILE B  1 72  ? 9.96000   -41.43300 2.69200   1.000 41.42000  ? 103 ILE B CG1 1 
ATOM   4131  C  CG2 . ILE B  1 72  ? 11.47100  -41.35100 4.73500   1.000 37.21000  ? 103 ILE B CG2 1 
ATOM   4132  C  CD1 . ILE B  1 72  ? 8.60100   -41.30500 3.34900   1.000 43.78000  ? 103 ILE B CD1 1 
ATOM   4133  N  N   . LEU B  1 73  ? 13.45100  -44.11500 4.13300   1.000 37.92000  ? 104 LEU B N   1 
ATOM   4134  C  CA  . LEU B  1 73  ? 14.51600  -44.45300 5.06300   1.000 39.12000  ? 104 LEU B CA  1 
ATOM   4135  C  C   . LEU B  1 73  ? 15.78900  -44.95600 4.37700   1.000 41.82000  ? 104 LEU B C   1 
ATOM   4136  O  O   . LEU B  1 73  ? 16.87300  -44.77700 4.93100   1.000 41.62000  ? 104 LEU B O   1 
ATOM   4137  C  CB  . LEU B  1 73  ? 14.01800  -45.48100 6.08700   1.000 37.93000  ? 104 LEU B CB  1 
ATOM   4138  C  CG  . LEU B  1 73  ? 13.34600  -44.78600 7.27500   1.000 44.95000  ? 104 LEU B CG  1 
ATOM   4139  C  CD1 . LEU B  1 73  ? 12.44800  -45.70600 8.02500   1.000 45.00000  ? 104 LEU B CD1 1 
ATOM   4140  C  CD2 . LEU B  1 73  ? 14.42000  -44.23200 8.23200   1.000 43.32000  ? 104 LEU B CD2 1 
ATOM   4141  N  N   . THR B  1 74  ? 15.69700  -45.62100 3.21800   1.000 38.47000  ? 105 THR B N   1 
ATOM   4142  C  CA  . THR B  1 74  ? 16.90100  -46.03600 2.50500   1.000 42.95000  ? 105 THR B CA  1 
ATOM   4143  C  C   . THR B  1 74  ? 17.41800  -44.98100 1.52200   1.000 44.17000  ? 105 THR B C   1 
ATOM   4144  O  O   . THR B  1 74  ? 18.58400  -45.03900 1.12200   1.000 40.03000  ? 105 THR B O   1 
ATOM   4145  C  CB  . THR B  1 74  ? 16.68300  -47.34400 1.71700   1.000 42.13000  ? 105 THR B CB  1 
ATOM   4146  O  OG1 . THR B  1 74  ? 15.78300  -47.11700 0.62400   1.000 44.69000  ? 105 THR B OG1 1 
ATOM   4147  C  CG2 . THR B  1 74  ? 16.19300  -48.50900 2.61100   1.000 38.60000  ? 105 THR B CG2 1 
ATOM   4148  N  N   . GLY B  1 75  ? 16.59600  -44.01600 1.13200   1.000 42.56000  ? 106 GLY B N   1 
ATOM   4149  C  CA  . GLY B  1 75  ? 17.00200  -43.05700 0.12000   1.000 38.60000  ? 106 GLY B CA  1 
ATOM   4150  C  C   . GLY B  1 75  ? 17.05900  -43.62200 -1.28500  1.000 45.20000  ? 106 GLY B C   1 
ATOM   4151  O  O   . GLY B  1 75  ? 17.52300  -42.93200 -2.20300  1.000 40.66000  ? 106 GLY B O   1 
ATOM   4152  N  N   . ARG B  1 76  ? 16.51200  -44.81900 -1.50000  1.000 34.96000  ? 107 ARG B N   1 
ATOM   4153  C  CA  . ARG B  1 76  ? 16.53000  -45.45800 -2.80500  1.000 39.98000  ? 107 ARG B CA  1 
ATOM   4154  C  C   . ARG B  1 76  ? 15.11600  -45.86100 -3.22300  1.000 41.23000  ? 107 ARG B C   1 
ATOM   4155  O  O   . ARG B  1 76  ? 14.26300  -46.17600 -2.38900  1.000 42.34000  ? 107 ARG B O   1 
ATOM   4156  C  CB  . ARG B  1 76  ? 17.42000  -46.68400 -2.77000  1.000 43.00000  ? 107 ARG B CB  1 
ATOM   4157  C  CG  . ARG B  1 76  ? 18.91700  -46.32700 -2.60600  1.000 52.14000  ? 107 ARG B CG  1 
ATOM   4158  C  CD  . ARG B  1 76  ? 19.77300  -47.56300 -2.63900  1.000 43.47000  ? 107 ARG B CD  1 
ATOM   4159  N  NE  . ARG B  1 76  ? 20.11800  -47.89200 -4.01300  1.000 54.67000  ? 107 ARG B NE  1 
ATOM   4160  C  CZ  . ARG B  1 76  ? 20.52800  -49.08800 -4.40900  1.000 52.24000  ? 107 ARG B CZ  1 
ATOM   4161  N  NH1 . ARG B  1 76  ? 20.68500  -50.08100 -3.54600  1.000 43.70000  ? 107 ARG B NH1 1 
ATOM   4162  N  NH2 . ARG B  1 76  ? 20.79300  -49.28600 -5.70200  1.000 43.28000  ? 107 ARG B NH2 1 
ATOM   4163  N  N   . TYR B  1 77  ? 14.88500  -45.85000 -4.52600  1.000 41.22000  ? 108 TYR B N   1 
ATOM   4164  C  CA  . TYR B  1 77  ? 13.64700  -46.37800 -5.07400  1.000 42.01000  ? 108 TYR B CA  1 
ATOM   4165  C  C   . TYR B  1 77  ? 13.47200  -47.82600 -4.62500  1.000 40.60000  ? 108 TYR B C   1 
ATOM   4166  O  O   . TYR B  1 77  ? 14.45900  -48.56000 -4.52700  1.000 46.74000  ? 108 TYR B O   1 
ATOM   4167  C  CB  . TYR B  1 77  ? 13.66900  -46.31100 -6.59700  1.000 36.27000  ? 108 TYR B CB  1 
ATOM   4168  C  CG  . TYR B  1 77  ? 13.31800  -44.96700 -7.16200  1.000 39.51000  ? 108 TYR B CG  1 
ATOM   4169  C  CD1 . TYR B  1 77  ? 11.99900  -44.51400 -7.12900  1.000 42.80000  ? 108 TYR B CD1 1 
ATOM   4170  C  CD2 . TYR B  1 77  ? 14.27300  -44.16500 -7.77900  1.000 35.48000  ? 108 TYR B CD2 1 
ATOM   4171  C  CE1 . TYR B  1 77  ? 11.64800  -43.28000 -7.66200  1.000 34.30000  ? 108 TYR B CE1 1 
ATOM   4172  C  CE2 . TYR B  1 77  ? 13.92900  -42.92500 -8.33400  1.000 41.70000  ? 108 TYR B CE2 1 
ATOM   4173  C  CZ  . TYR B  1 77  ? 12.60100  -42.48900 -8.26200  1.000 40.03000  ? 108 TYR B CZ  1 
ATOM   4174  O  OH  . TYR B  1 77  ? 12.20400  -41.27200 -8.79200  1.000 37.69000  ? 108 TYR B OH  1 
ATOM   4175  N  N   . PRO B  1 78  ? 12.25300  -48.25200 -4.27800  1.000 37.49000  ? 109 PRO B N   1 
ATOM   4176  C  CA  . PRO B  1 78  ? 12.06400  -49.64600 -3.84100  1.000 36.95000  ? 109 PRO B CA  1 
ATOM   4177  C  C   . PRO B  1 78  ? 12.36100  -50.66200 -4.92800  1.000 40.46000  ? 109 PRO B C   1 
ATOM   4178  O  O   . PRO B  1 78  ? 12.55900  -51.84100 -4.62400  1.000 42.93000  ? 109 PRO B O   1 
ATOM   4179  C  CB  . PRO B  1 78  ? 10.58500  -49.68700 -3.43400  1.000 38.19000  ? 109 PRO B CB  1 
ATOM   4180  C  CG  . PRO B  1 78  ? 9.96600   -48.62600 -4.30000  1.000 36.01000  ? 109 PRO B CG  1 
ATOM   4181  C  CD  . PRO B  1 78  ? 10.97600  -47.52400 -4.32700  1.000 41.64000  ? 109 PRO B CD  1 
ATOM   4182  N  N   . HIS B  1 79  ? 12.35300  -50.24500 -6.19300  1.000 39.36000  ? 110 HIS B N   1 
ATOM   4183  C  CA  . HIS B  1 79  ? 12.68600  -51.14300 -7.28600  1.000 43.49000  ? 110 HIS B CA  1 
ATOM   4184  C  C   . HIS B  1 79  ? 14.16500  -51.50100 -7.29500  1.000 48.90000  ? 110 HIS B C   1 
ATOM   4185  O  O   . HIS B  1 79  ? 14.55100  -52.45900 -7.96900  1.000 43.36000  ? 110 HIS B O   1 
ATOM   4186  C  CB  . HIS B  1 79  ? 12.30800  -50.49000 -8.60900  1.000 40.80000  ? 110 HIS B CB  1 
ATOM   4187  C  CG  . HIS B  1 79  ? 11.02600  -49.71200 -8.54300  1.000 50.65000  ? 110 HIS B CG  1 
ATOM   4188  N  ND1 . HIS B  1 79  ? 10.92700  -48.48600 -7.91900  1.000 41.92000  ? 110 HIS B ND1 1 
ATOM   4189  C  CD2 . HIS B  1 79  ? 9.78200   -50.00500 -8.99800  1.000 45.38000  ? 110 HIS B CD2 1 
ATOM   4190  C  CE1 . HIS B  1 79  ? 9.67900   -48.05300 -8.00400  1.000 45.00000  ? 110 HIS B CE1 1 
ATOM   4191  N  NE2 . HIS B  1 79  ? 8.96400   -48.95600 -8.65000  1.000 43.23000  ? 110 HIS B NE2 1 
ATOM   4192  N  N   . LEU B  1 80  ? 14.99800  -50.75300 -6.57000  1.000 43.99000  ? 111 LEU B N   1 
ATOM   4193  C  CA  . LEU B  1 80  ? 16.42400  -51.05100 -6.50100  1.000 49.13000  ? 111 LEU B CA  1 
ATOM   4194  C  C   . LEU B  1 80  ? 16.80400  -51.85600 -5.26900  1.000 48.68000  ? 111 LEU B C   1 
ATOM   4195  O  O   . LEU B  1 80  ? 17.84500  -52.50900 -5.28000  1.000 55.87000  ? 111 LEU B O   1 
ATOM   4196  C  CB  . LEU B  1 80  ? 17.22300  -49.74900 -6.53100  1.000 47.41000  ? 111 LEU B CB  1 
ATOM   4197  C  CG  . LEU B  1 80  ? 17.21300  -49.14200 -7.93000  1.000 56.01000  ? 111 LEU B CG  1 
ATOM   4198  C  CD1 . LEU B  1 80  ? 17.63000  -47.71000 -7.85600  1.000 56.50000  ? 111 LEU B CD1 1 
ATOM   4199  C  CD2 . LEU B  1 80  ? 18.17500  -49.88800 -8.81500  1.000 51.06000  ? 111 LEU B CD2 1 
ATOM   4200  N  N   . THR B  1 81  ? 15.96500  -51.85900 -4.23600  1.000 46.44000  ? 112 THR B N   1 
ATOM   4201  C  CA  . THR B  1 81  ? 16.21100  -52.58600 -3.00100  1.000 44.24000  ? 112 THR B CA  1 
ATOM   4202  C  C   . THR B  1 81  ? 15.38000  -53.85400 -2.88700  1.000 48.19000  ? 112 THR B C   1 
ATOM   4203  O  O   . THR B  1 81  ? 15.50000  -54.56000 -1.87800  1.000 49.18000  ? 112 THR B O   1 
ATOM   4204  C  CB  . THR B  1 81  ? 15.91400  -51.68700 -1.78300  1.000 47.77000  ? 112 THR B CB  1 
ATOM   4205  O  OG1 . THR B  1 81  ? 14.53400  -51.27200 -1.82100  1.000 48.96000  ? 112 THR B OG1 1 
ATOM   4206  C  CG2 . THR B  1 81  ? 16.79000  -50.45100 -1.80600  1.000 44.62000  ? 112 THR B CG2 1 
ATOM   4207  N  N   . GLY B  1 82  ? 14.49600  -54.12600 -3.85100  1.000 40.75000  ? 113 GLY B N   1 
ATOM   4208  C  CA  . GLY B  1 82  ? 13.66800  -55.31600 -3.80600  1.000 42.55000  ? 113 GLY B CA  1 
ATOM   4209  C  C   . GLY B  1 82  ? 12.41600  -55.21100 -2.95600  1.000 47.65000  ? 113 GLY B C   1 
ATOM   4210  O  O   . GLY B  1 82  ? 11.85300  -56.24200 -2.57600  1.000 43.89000  ? 113 GLY B O   1 
ATOM   4211  N  N   . THR B  1 83  ? 11.98500  -54.00000 -2.59700  1.000 43.19000  ? 114 THR B N   1 
ATOM   4212  C  CA  . THR B  1 83  ? 10.91300  -53.81700 -1.62600  1.000 47.38000  ? 114 THR B CA  1 
ATOM   4213  C  C   . THR B  1 83  ? 9.70900   -53.08700 -2.22200  1.000 43.06000  ? 114 THR B C   1 
ATOM   4214  O  O   . THR B  1 83  ? 9.03300   -52.32100 -1.52500  1.000 44.58000  ? 114 THR B O   1 
ATOM   4215  C  CB  . THR B  1 83  ? 11.42800  -53.06400 -0.40000  1.000 44.39000  ? 114 THR B CB  1 
ATOM   4216  O  OG1 . THR B  1 83  ? 12.01700  -51.84500 -0.83700  1.000 46.04000  ? 114 THR B OG1 1 
ATOM   4217  C  CG2 . THR B  1 83  ? 12.46800  -53.87400 0.33700   1.000 43.01000  ? 114 THR B CG2 1 
ATOM   4218  N  N   . ALA B  1 84  ? 9.42200   -53.31400 -3.50000  1.000 40.11000  ? 115 ALA B N   1 
ATOM   4219  C  CA  . ALA B  1 84  ? 8.34100   -52.61200 -4.18800  1.000 44.47000  ? 115 ALA B CA  1 
ATOM   4220  C  C   . ALA B  1 84  ? 6.96400   -53.26000 -4.00100  1.000 43.10000  ? 115 ALA B C   1 
ATOM   4221  O  O   . ALA B  1 84  ? 5.98800   -52.77900 -4.59600  1.000 41.22000  ? 115 ALA B O   1 
ATOM   4222  C  CB  . ALA B  1 84  ? 8.66300   -52.48300 -5.68900  1.000 40.81000  ? 115 ALA B CB  1 
ATOM   4223  N  N   . TYR B  1 85  ? 6.85500   -54.33400 -3.21000  1.000 37.50000  ? 116 TYR B N   1 
ATOM   4224  C  CA  . TYR B  1 85  ? 5.57000   -54.83900 -2.74500  1.000 40.93000  ? 116 TYR B CA  1 
ATOM   4225  C  C   . TYR B  1 85  ? 5.47200   -54.67000 -1.23800  1.000 43.95000  ? 116 TYR B C   1 
ATOM   4226  O  O   . TYR B  1 85  ? 6.48900   -54.68800 -0.53800  1.000 43.85000  ? 116 TYR B O   1 
ATOM   4227  C  CB  . TYR B  1 85  ? 5.36200   -56.32600 -3.07700  1.000 45.42000  ? 116 TYR B CB  1 
ATOM   4228  C  CG  . TYR B  1 85  ? 5.08200   -56.63400 -4.52300  1.000 46.48000  ? 116 TYR B CG  1 
ATOM   4229  C  CD1 . TYR B  1 85  ? 3.78000   -56.63200 -5.01600  1.000 41.20000  ? 116 TYR B CD1 1 
ATOM   4230  C  CD2 . TYR B  1 85  ? 6.12100   -56.94300 -5.39900  1.000 46.65000  ? 116 TYR B CD2 1 
ATOM   4231  C  CE1 . TYR B  1 85  ? 3.52600   -56.93100 -6.35000  1.000 48.41000  ? 116 TYR B CE1 1 
ATOM   4232  C  CE2 . TYR B  1 85  ? 5.87300   -57.23800 -6.72500  1.000 45.15000  ? 116 TYR B CE2 1 
ATOM   4233  C  CZ  . TYR B  1 85  ? 4.58500   -57.23300 -7.20000  1.000 44.72000  ? 116 TYR B CZ  1 
ATOM   4234  O  OH  . TYR B  1 85  ? 4.35900   -57.51900 -8.52600  1.000 36.96000  ? 116 TYR B OH  1 
ATOM   4235  N  N   . ASN B  1 86  ? 4.23600   -54.52800 -0.74300  1.000 37.53000  ? 117 ASN B N   1 
ATOM   4236  C  CA  . ASN B  1 86  ? 4.00800   -54.50700 0.68800   1.000 39.17000  ? 117 ASN B CA  1 
ATOM   4237  C  C   . ASN B  1 86  ? 4.27100   -55.88000 1.29900   1.000 45.26000  ? 117 ASN B C   1 
ATOM   4238  O  O   . ASN B  1 86  ? 3.96300   -56.92000 0.70800   1.000 40.61000  ? 117 ASN B O   1 
ATOM   4239  C  CB  . ASN B  1 86  ? 2.56700   -54.09900 1.00700   1.000 43.14000  ? 117 ASN B CB  1 
ATOM   4240  C  CG  . ASN B  1 86  ? 2.41000   -52.60100 1.17800   1.000 41.16000  ? 117 ASN B CG  1 
ATOM   4241  O  OD1 . ASN B  1 86  ? 3.39400   -51.88200 1.31500   1.000 47.13000  ? 117 ASN B OD1 1 
ATOM   4242  N  ND2 . ASN B  1 86  ? 1.17700   -52.12200 1.14600   1.000 43.37000  ? 117 ASN B ND2 1 
ATOM   4243  N  N   . LEU B  1 87  ? 4.78900   -55.87100 2.52500   1.000 41.62000  ? 118 LEU B N   1 
ATOM   4244  C  CA  . LEU B  1 87  ? 4.74900   -57.06500 3.35300   1.000 44.50000  ? 118 LEU B CA  1 
ATOM   4245  C  C   . LEU B  1 87  ? 3.30100   -57.35600 3.75300   1.000 44.52000  ? 118 LEU B C   1 
ATOM   4246  O  O   . LEU B  1 87  ? 2.55300   -56.44700 4.11900   1.000 36.00000  ? 118 LEU B O   1 
ATOM   4247  C  CB  . LEU B  1 87  ? 5.61000   -56.86500 4.60300   1.000 49.34000  ? 118 LEU B CB  1 
ATOM   4248  C  CG  . LEU B  1 87  ? 7.11600   -56.70600 4.38300   1.000 50.63000  ? 118 LEU B CG  1 
ATOM   4249  C  CD1 . LEU B  1 87  ? 7.74100   -56.12800 5.62500   1.000 41.54000  ? 118 LEU B CD1 1 
ATOM   4250  C  CD2 . LEU B  1 87  ? 7.77200   -58.02600 3.96800   1.000 44.88000  ? 118 LEU B CD2 1 
ATOM   4251  N  N   . PHE B  1 88  ? 2.90800   -58.62900 3.67300   1.000 46.90000  ? 119 PHE B N   1 
ATOM   4252  C  CA  . PHE B  1 88  ? 1.58300   -59.05200 4.11700   1.000 43.63000  ? 119 PHE B CA  1 
ATOM   4253  C  C   . PHE B  1 88  ? 1.44900   -58.85500 5.61400   1.000 42.91000  ? 119 PHE B C   1 
ATOM   4254  O  O   . PHE B  1 88  ? 2.43600   -58.89200 6.35100   1.000 49.32000  ? 119 PHE B O   1 
ATOM   4255  C  CB  . PHE B  1 88  ? 1.35700   -60.52300 3.76500   1.000 48.48000  ? 119 PHE B CB  1 
ATOM   4256  C  CG  . PHE B  1 88  ? -0.07800  -60.87400 3.44600   1.000 50.25000  ? 119 PHE B CG  1 
ATOM   4257  C  CD1 . PHE B  1 88  ? -0.63200  -60.52900 2.21300   1.000 50.82000  ? 119 PHE B CD1 1 
ATOM   4258  C  CD2 . PHE B  1 88  ? -0.84100  -61.63300 4.33600   1.000 44.91000  ? 119 PHE B CD2 1 
ATOM   4259  C  CE1 . PHE B  1 88  ? -1.96100  -60.87700 1.90000   1.000 49.47000  ? 119 PHE B CE1 1 
ATOM   4260  C  CE2 . PHE B  1 88  ? -2.16500  -61.98000 4.04100   1.000 46.78000  ? 119 PHE B CE2 1 
ATOM   4261  C  CZ  . PHE B  1 88  ? -2.72500  -61.60900 2.81700   1.000 46.19000  ? 119 PHE B CZ  1 
ATOM   4262  N  N   . HIS B  1 89  ? 0.21600   -58.65200 6.07200   1.000 43.84000  ? 120 HIS B N   1 
ATOM   4263  C  CA  . HIS B  1 89  ? -0.00700  -58.52100 7.50400   1.000 48.69000  ? 120 HIS B CA  1 
ATOM   4264  C  C   . HIS B  1 89  ? 0.45600   -59.78900 8.20900   1.000 46.29000  ? 120 HIS B C   1 
ATOM   4265  O  O   . HIS B  1 89  ? 0.46100   -60.88000 7.63400   1.000 40.80000  ? 120 HIS B O   1 
ATOM   4266  C  CB  . HIS B  1 89  ? -1.48900  -58.22100 7.81500   1.000 45.82000  ? 120 HIS B CB  1 
ATOM   4267  C  CG  . HIS B  1 89  ? -2.40800  -59.39500 7.63700   1.000 55.70000  ? 120 HIS B CG  1 
ATOM   4268  N  ND1 . HIS B  1 89  ? -2.60300  -60.35100 8.61400   1.000 53.78000  ? 120 HIS B ND1 1 
ATOM   4269  C  CD2 . HIS B  1 89  ? -3.20400  -59.75200 6.59800   1.000 50.75000  ? 120 HIS B CD2 1 
ATOM   4270  C  CE1 . HIS B  1 89  ? -3.46200  -61.25500 8.17700   1.000 50.21000  ? 120 HIS B CE1 1 
ATOM   4271  N  NE2 . HIS B  1 89  ? -3.84500  -60.91300 6.95900   1.000 57.54000  ? 120 HIS B NE2 1 
ATOM   4272  N  N   . ASN B  1 90  ? 0.93000   -59.61700 9.43900   1.000 47.69000  ? 121 ASN B N   1 
ATOM   4273  C  CA  . ASN B  1 90  ? 1.48300   -60.72500 10.21000  1.000 48.07000  ? 121 ASN B CA  1 
ATOM   4274  C  C   . ASN B  1 90  ? 2.60500   -61.41100 9.43000   1.000 49.70000  ? 121 ASN B C   1 
ATOM   4275  O  O   . ASN B  1 90  ? 2.70400   -62.64200 9.39000   1.000 48.73000  ? 121 ASN B O   1 
ATOM   4276  C  CB  . ASN B  1 90  ? 0.38300   -61.73100 10.59600  1.000 45.35000  ? 121 ASN B CB  1 
ATOM   4277  C  CG  . ASN B  1 90  ? -0.71300  -61.10300 11.44400  1.000 47.88000  ? 121 ASN B CG  1 
ATOM   4278  O  OD1 . ASN B  1 90  ? -1.59000  -60.42000 10.92900  1.000 51.85000  ? 121 ASN B OD1 1 
ATOM   4279  N  ND2 . ASN B  1 90  ? -0.63300  -61.28000 12.75100  1.000 48.61000  ? 121 ASN B ND2 1 
ATOM   4280  N  N   . SER B  1 91  ? 3.44300   -60.60800 8.77300   1.000 49.22000  ? 122 SER B N   1 
ATOM   4281  C  CA  . SER B  1 91  ? 4.57700   -61.18000 8.04900   1.000 52.26000  ? 122 SER B CA  1 
ATOM   4282  C  C   . SER B  1 91  ? 5.55500   -61.82200 9.03700   1.000 51.18000  ? 122 SER B C   1 
ATOM   4283  O  O   . SER B  1 91  ? 5.55300   -61.52300 10.23700  1.000 47.42000  ? 122 SER B O   1 
ATOM   4284  C  CB  . SER B  1 91  ? 5.29200   -60.10800 7.21200   1.000 47.72000  ? 122 SER B CB  1 
ATOM   4285  O  OG  . SER B  1 91  ? 5.81400   -59.05800 8.02500   1.000 45.34000  ? 122 SER B OG  1 
ATOM   4286  N  N   . SER B  1 92  ? 6.41300   -62.70300 8.50900   1.000 54.91000  ? 123 SER B N   1 
ATOM   4287  C  CA  . SER B  1 92  ? 7.24200   -63.56300 9.35900   1.000 56.08000  ? 123 SER B CA  1 
ATOM   4288  C  C   . SER B  1 92  ? 8.14900   -62.76800 10.28400  1.000 52.17000  ? 123 SER B C   1 
ATOM   4289  O  O   . SER B  1 92  ? 8.80700   -61.81700 9.86300   1.000 50.56000  ? 123 SER B O   1 
ATOM   4290  C  CB  . SER B  1 92  ? 8.11500   -64.48900 8.52400   1.000 54.87000  ? 123 SER B CB  1 
ATOM   4291  O  OG  . SER B  1 92  ? 9.03300   -65.13500 9.38400   1.000 56.84000  ? 123 SER B OG  1 
ATOM   4292  N  N   . GLU B  1 93  ? 8.23600   -63.22000 11.53500  1.000 52.62000  ? 124 GLU B N   1 
ATOM   4293  C  CA  . GLU B  1 93  ? 9.06000   -62.58600 12.55300  1.000 53.64000  ? 124 GLU B CA  1 
ATOM   4294  C  C   . GLU B  1 93  ? 10.36700  -63.33300 12.80700  1.000 60.88000  ? 124 GLU B C   1 
ATOM   4295  O  O   . GLU B  1 93  ? 11.09200  -62.99500 13.74600  1.000 61.08000  ? 124 GLU B O   1 
ATOM   4296  C  CB  . GLU B  1 93  ? 8.25500   -62.43700 13.85100  1.000 53.63000  ? 124 GLU B CB  1 
ATOM   4297  C  CG  . GLU B  1 93  ? 6.91500   -61.73100 13.61800  1.000 57.04000  ? 124 GLU B CG  1 
ATOM   4298  C  CD  . GLU B  1 93  ? 6.32600   -61.11200 14.87700  1.000 67.12000  ? 124 GLU B CD  1 
ATOM   4299  O  OE1 . GLU B  1 93  ? 7.07600   -60.96500 15.87000  1.000 75.06000  ? 124 GLU B OE1 1 
ATOM   4300  O  OE2 . GLU B  1 93  ? 5.14100   -60.69400 14.85300  1.000 59.35000  ? 124 GLU B OE2 1 
ATOM   4301  N  N   . ASP B  1 94  ? 10.70100  -64.31200 11.97300  1.000 61.56000  ? 125 ASP B N   1 
ATOM   4302  C  CA  . ASP B  1 94  ? 11.93000  -65.07800 12.11200  1.000 62.94000  ? 125 ASP B CA  1 
ATOM   4303  C  C   . ASP B  1 94  ? 12.96500  -64.53000 11.13900  1.000 63.31000  ? 125 ASP B C   1 
ATOM   4304  O  O   . ASP B  1 94  ? 12.67600  -64.38700 9.94400   1.000 58.93000  ? 125 ASP B O   1 
ATOM   4305  C  CB  . ASP B  1 94  ? 11.67900  -66.56600 11.84700  1.000 63.70000  ? 125 ASP B CB  1 
ATOM   4306  C  CG  . ASP B  1 94  ? 10.82800  -67.22400 12.93300  1.000 71.94000  ? 125 ASP B CG  1 
ATOM   4307  O  OD1 . ASP B  1 94  ? 11.16100  -67.08700 14.13000  1.000 80.40000  ? 125 ASP B OD1 1 
ATOM   4308  O  OD2 . ASP B  1 94  ? 9.81700   -67.87700 12.59500  1.000 80.34000  ? 125 ASP B OD2 1 
ATOM   4309  N  N   . ASP B  1 95  ? 14.16400  -64.21000 11.65800  1.000 53.51000  ? 126 ASP B N   1 
ATOM   4310  C  CA  . ASP B  1 95  ? 15.22200  -63.66100 10.81300  1.000 55.16000  ? 126 ASP B CA  1 
ATOM   4311  C  C   . ASP B  1 95  ? 15.54000  -64.55200 9.62000   1.000 59.87000  ? 126 ASP B C   1 
ATOM   4312  O  O   . ASP B  1 95  ? 15.88600  -64.04000 8.54900   1.000 56.20000  ? 126 ASP B O   1 
ATOM   4313  C  CB  . ASP B  1 95  ? 16.51400  -63.44200 11.61400  1.000 56.97000  ? 126 ASP B CB  1 
ATOM   4314  C  CG  . ASP B  1 95  ? 16.43300  -62.27200 12.58200  1.000 63.93000  ? 126 ASP B CG  1 
ATOM   4315  O  OD1 . ASP B  1 95  ? 15.37600  -61.59900 12.64100  1.000 64.21000  ? 126 ASP B OD1 1 
ATOM   4316  O  OD2 . ASP B  1 95  ? 17.46400  -61.98700 13.24800  1.000 58.12000  ? 126 ASP B OD2 1 
ATOM   4317  N  N   . LYS B  1 96  ? 15.39600  -65.87500 9.76400   1.000 60.45000  ? 127 LYS B N   1 
ATOM   4318  C  CA  . LYS B  1 96  ? 15.74400  -66.77300 8.66200   1.000 61.33000  ? 127 LYS B CA  1 
ATOM   4319  C  C   . LYS B  1 96  ? 14.92900  -66.42000 7.42500   1.000 62.20000  ? 127 LYS B C   1 
ATOM   4320  O  O   . LYS B  1 96  ? 15.44400  -66.43100 6.30100   1.000 62.79000  ? 127 LYS B O   1 
ATOM   4321  C  CB  . LYS B  1 96  ? 15.53700  -68.23400 9.07900   1.000 54.38000  ? 127 LYS B CB  1 
ATOM   4322  N  N   . ASP B  1 97  ? 13.65300  -66.10500 7.62000   1.000 60.00000  ? 128 ASP B N   1 
ATOM   4323  C  CA  . ASP B  1 97  ? 12.82700  -65.53500 6.57100   1.000 65.75000  ? 128 ASP B CA  1 
ATOM   4324  C  C   . ASP B  1 97  ? 13.24000  -64.07900 6.46300   1.000 66.96000  ? 128 ASP B C   1 
ATOM   4325  O  O   . ASP B  1 97  ? 13.28700  -63.37300 7.47300   1.000 68.60000  ? 128 ASP B O   1 
ATOM   4326  C  CB  . ASP B  1 97  ? 11.35000  -65.63100 6.94400   1.000 61.34000  ? 128 ASP B CB  1 
ATOM   4327  C  CG  . ASP B  1 97  ? 10.93600  -67.03600 7.31900   1.000 65.82000  ? 128 ASP B CG  1 
ATOM   4328  O  OD1 . ASP B  1 97  ? 11.32200  -67.99300 6.60400   1.000 66.96000  ? 128 ASP B OD1 1 
ATOM   4329  O  OD2 . ASP B  1 97  ? 10.25900  -67.18100 8.36200   1.000 64.65000  ? 128 ASP B OD2 1 
ATOM   4330  N  N   . ASN B  1 98  ? 13.57400  -63.62700 5.27200   1.000 62.74000  ? 129 ASN B N   1 
ATOM   4331  C  CA  . ASN B  1 98  ? 14.04300  -62.24900 5.14200   1.000 63.76000  ? 129 ASN B CA  1 
ATOM   4332  C  C   . ASN B  1 98  ? 12.89000  -61.32700 4.74000   1.000 54.81000  ? 129 ASN B C   1 
ATOM   4333  O  O   . ASN B  1 98  ? 12.91700  -60.64500 3.72100   1.000 55.89000  ? 129 ASN B O   1 
ATOM   4334  C  CB  . ASN B  1 98  ? 15.22200  -62.18300 4.17800   1.000 56.56000  ? 129 ASN B CB  1 
ATOM   4335  C  CG  . ASN B  1 98  ? 16.52800  -62.59400 4.84800   1.000 70.24000  ? 129 ASN B CG  1 
ATOM   4336  O  OD1 . ASN B  1 98  ? 17.11300  -61.83100 5.62800   1.000 64.94000  ? 129 ASN B OD1 1 
ATOM   4337  N  ND2 . ASN B  1 98  ? 16.98800  -63.80400 4.55100   1.000 65.62000  ? 129 ASN B ND2 1 
ATOM   4338  N  N   . MET B  1 99  ? 11.84600  -61.33700 5.56800   1.000 51.73000  ? 130 MET B N   1 
ATOM   4339  C  CA  . MET B  1 99  ? 10.65400  -60.52400 5.31900   1.000 50.92000  ? 130 MET B CA  1 
ATOM   4340  C  C   . MET B  1 99  ? 10.84200  -59.12200 5.90400   1.000 43.39000  ? 130 MET B C   1 
ATOM   4341  O  O   . MET B  1 99  ? 10.25800  -58.74800 6.91600   1.000 52.12000  ? 130 MET B O   1 
ATOM   4342  C  CB  . MET B  1 99  ? 9.43000   -61.21300 5.89600   1.000 49.45000  ? 130 MET B CB  1 
ATOM   4343  C  CG  . MET B  1 99  ? 8.96900   -62.41700 5.09300   1.000 55.36000  ? 130 MET B CG  1 
ATOM   4344  S  SD  . MET B  1 99  ? 8.76700   -62.07400 3.33400   1.000 60.49000  ? 130 MET B SD  1 
ATOM   4345  C  CE  . MET B  1 99  ? 8.44300   -63.69800 2.68600   1.000 61.89000  ? 130 MET B CE  1 
ATOM   4346  N  N   . GLY B  1 100 ? 11.70200  -58.35800 5.24500   1.000 48.16000  ? 131 GLY B N   1 
ATOM   4347  C  CA  . GLY B  1 100 ? 12.04100  -57.01200 5.68400   1.000 47.80000  ? 131 GLY B CA  1 
ATOM   4348  C  C   . GLY B  1 100 ? 13.03500  -56.38100 4.73100   1.000 45.17000  ? 131 GLY B C   1 
ATOM   4349  O  O   . GLY B  1 100 ? 13.62800  -57.04500 3.87200   1.000 47.44000  ? 131 GLY B O   1 
ATOM   4350  N  N   . VAL B  1 101 ? 13.19400  -55.07100 4.88400   1.000 39.70000  ? 132 VAL B N   1 
ATOM   4351  C  CA  . VAL B  1 101 ? 14.13400  -54.32900 4.03500   1.000 43.49000  ? 132 VAL B CA  1 
ATOM   4352  C  C   . VAL B  1 101 ? 15.56000  -54.82400 4.29100   1.000 44.33000  ? 132 VAL B C   1 
ATOM   4353  O  O   . VAL B  1 101 ? 15.98900  -54.89700 5.45800   1.000 49.30000  ? 132 VAL B O   1 
ATOM   4354  C  CB  . VAL B  1 101 ? 14.02200  -52.81700 4.30800   1.000 43.21000  ? 132 VAL B CB  1 
ATOM   4355  C  CG1 . VAL B  1 101 ? 14.96200  -52.05200 3.40100   1.000 44.92000  ? 132 VAL B CG1 1 
ATOM   4356  C  CG2 . VAL B  1 101 ? 12.56500  -52.33400 4.15400   1.000 37.96000  ? 132 VAL B CG2 1 
ATOM   4357  N  N   . PRO B  1 102 ? 16.33600  -55.15200 3.26300   1.000 43.31000  ? 133 PRO B N   1 
ATOM   4358  C  CA  . PRO B  1 102 ? 17.70100  -55.66100 3.48400   1.000 49.00000  ? 133 PRO B CA  1 
ATOM   4359  C  C   . PRO B  1 102 ? 18.49500  -54.83800 4.49200   1.000 47.81000  ? 133 PRO B C   1 
ATOM   4360  O  O   . PRO B  1 102 ? 18.59200  -53.61000 4.38900   1.000 46.52000  ? 133 PRO B O   1 
ATOM   4361  C  CB  . PRO B  1 102 ? 18.33500  -55.58800 2.09000   1.000 43.46000  ? 133 PRO B CB  1 
ATOM   4362  C  CG  . PRO B  1 102 ? 17.18800  -55.67000 1.13700   1.000 49.69000  ? 133 PRO B CG  1 
ATOM   4363  C  CD  . PRO B  1 102 ? 15.95400  -55.15000 1.83900   1.000 47.17000  ? 133 PRO B CD  1 
ATOM   4364  N  N   . VAL B  1 103 ? 19.11400  -55.53600 5.44700   1.000 48.18000  ? 134 VAL B N   1 
ATOM   4365  C  CA  . VAL B  1 103 ? 19.84100  -54.84500 6.51000   1.000 54.23000  ? 134 VAL B CA  1 
ATOM   4366  C  C   . VAL B  1 103 ? 21.10100  -54.17900 5.98900   1.000 51.86000  ? 134 VAL B C   1 
ATOM   4367  O  O   . VAL B  1 103 ? 21.61300  -53.25800 6.63000   1.000 55.37000  ? 134 VAL B O   1 
ATOM   4368  C  CB  . VAL B  1 103 ? 20.21300  -55.80800 7.65000   1.000 57.33000  ? 134 VAL B CB  1 
ATOM   4369  C  CG1 . VAL B  1 103 ? 18.95100  -56.25600 8.40700   1.000 52.68000  ? 134 VAL B CG1 1 
ATOM   4370  C  CG2 . VAL B  1 103 ? 20.99900  -56.99900 7.09900   1.000 50.72000  ? 134 VAL B CG2 1 
ATOM   4371  N  N   . GLU B  1 104 ? 21.59300  -54.59600 4.82500   1.000 49.49000  ? 135 GLU B N   1 
ATOM   4372  C  CA  . GLU B  1 104 ? 22.76600  -53.96300 4.24500   1.000 53.84000  ? 135 GLU B CA  1 
ATOM   4373  C  C   . GLU B  1 104 ? 22.46500  -52.56500 3.74500   1.000 55.80000  ? 135 GLU B C   1 
ATOM   4374  O  O   . GLU B  1 104 ? 23.39100  -51.76300 3.58500   1.000 53.52000  ? 135 GLU B O   1 
ATOM   4375  C  CB  . GLU B  1 104 ? 23.31000  -54.79900 3.08400   1.000 57.98000  ? 135 GLU B CB  1 
ATOM   4376  C  CG  . GLU B  1 104 ? 23.26000  -56.31500 3.28600   1.000 61.32000  ? 135 GLU B CG  1 
ATOM   4377  C  CD  . GLU B  1 104 ? 21.89900  -56.91000 2.93300   1.000 70.85000  ? 135 GLU B CD  1 
ATOM   4378  O  OE1 . GLU B  1 104 ? 21.49900  -56.82300 1.74200   1.000 73.75000  ? 135 GLU B OE1 1 
ATOM   4379  O  OE2 . GLU B  1 104 ? 21.22200  -57.44900 3.85000   1.000 71.37000  ? 135 GLU B OE2 1 
ATOM   4380  N  N   . GLU B  1 105 ? 21.19800  -52.25700 3.47600   1.000 53.19000  ? 136 GLU B N   1 
ATOM   4381  C  CA  . GLU B  1 105 ? 20.82200  -50.93300 2.99200   1.000 46.18000  ? 136 GLU B CA  1 
ATOM   4382  C  C   . GLU B  1 105 ? 20.68300  -50.00700 4.19600   1.000 50.16000  ? 136 GLU B C   1 
ATOM   4383  O  O   . GLU B  1 105 ? 19.64200  -49.97400 4.85600   1.000 58.35000  ? 136 GLU B O   1 
ATOM   4384  C  CB  . GLU B  1 105 ? 19.53000  -51.00800 2.18800   1.000 52.65000  ? 136 GLU B CB  1 
ATOM   4385  C  CG  . GLU B  1 105 ? 19.32700  -49.83500 1.24800   1.000 48.59000  ? 136 GLU B CG  1 
ATOM   4386  C  CD  . GLU B  1 105 ? 20.42200  -49.70300 0.19600   1.000 51.10000  ? 136 GLU B CD  1 
ATOM   4387  O  OE1 . GLU B  1 105 ? 20.45300  -50.52000 -0.74800  1.000 61.53000  ? 136 GLU B OE1 1 
ATOM   4388  O  OE2 . GLU B  1 105 ? 21.25200  -48.78300 0.30200   1.000 46.66000  ? 136 GLU B OE2 1 
ATOM   4389  N  N   . THR B  1 106 ? 21.70900  -49.20900 4.45400   1.000 47.33000  ? 137 THR B N   1 
ATOM   4390  C  CA  . THR B  1 106 ? 21.76200  -48.42100 5.68000   1.000 52.34000  ? 137 THR B CA  1 
ATOM   4391  C  C   . THR B  1 106 ? 20.76100  -47.26800 5.66000   1.000 48.26000  ? 137 THR B C   1 
ATOM   4392  O  O   . THR B  1 106 ? 20.79200  -46.42200 4.76000   1.000 47.17000  ? 137 THR B O   1 
ATOM   4393  C  CB  . THR B  1 106 ? 23.17600  -47.87900 5.88200   1.000 41.44000  ? 137 THR B CB  1 
ATOM   4394  O  OG1 . THR B  1 106 ? 24.10300  -48.95700 5.73900   1.000 49.29000  ? 137 THR B OG1 1 
ATOM   4395  C  CG2 . THR B  1 106 ? 23.31900  -47.24300 7.26500   1.000 37.53000  ? 137 THR B CG2 1 
ATOM   4396  N  N   . TYR B  1 107 ? 19.93300  -47.20500 6.70700   1.000 48.76000  ? 138 TYR B N   1 
ATOM   4397  C  CA  . TYR B  1 107 ? 18.93500  -46.15400 6.88500   1.000 46.89000  ? 138 TYR B CA  1 
ATOM   4398  C  C   . TYR B  1 107 ? 19.57800  -44.83300 7.28300   1.000 44.23000  ? 138 TYR B C   1 
ATOM   4399  O  O   . TYR B  1 107 ? 20.64100  -44.79400 7.90200   1.000 45.40000  ? 138 TYR B O   1 
ATOM   4400  C  CB  . TYR B  1 107 ? 17.93800  -46.53600 7.97400   1.000 44.30000  ? 138 TYR B CB  1 
ATOM   4401  C  CG  . TYR B  1 107 ? 16.96500  -47.65800 7.66600   1.000 44.38000  ? 138 TYR B CG  1 
ATOM   4402  C  CD1 . TYR B  1 107 ? 17.02400  -48.37400 6.47700   1.000 43.70000  ? 138 TYR B CD1 1 
ATOM   4403  C  CD2 . TYR B  1 107 ? 15.98800  -48.01200 8.60400   1.000 42.11000  ? 138 TYR B CD2 1 
ATOM   4404  C  CE1 . TYR B  1 107 ? 16.11800  -49.42200 6.22200   1.000 42.01000  ? 138 TYR B CE1 1 
ATOM   4405  C  CE2 . TYR B  1 107 ? 15.09600  -49.02100 8.36400   1.000 38.62000  ? 138 TYR B CE2 1 
ATOM   4406  C  CZ  . TYR B  1 107 ? 15.16700  -49.73100 7.18500   1.000 41.36000  ? 138 TYR B CZ  1 
ATOM   4407  O  OH  . TYR B  1 107 ? 14.26700  -50.73900 6.97400   1.000 43.51000  ? 138 TYR B OH  1 
ATOM   4408  N  N   . MET B  1 108 ? 18.90300  -43.73200 6.95800   1.000 44.67000  ? 139 MET B N   1 
ATOM   4409  C  CA  . MET B  1 108 ? 19.43900  -42.44300 7.38200   1.000 42.22000  ? 139 MET B CA  1 
ATOM   4410  C  C   . MET B  1 108 ? 19.40400  -42.27000 8.89900   1.000 45.91000  ? 139 MET B C   1 
ATOM   4411  O  O   . MET B  1 108 ? 20.17700  -41.47500 9.44000   1.000 47.09000  ? 139 MET B O   1 
ATOM   4412  C  CB  . MET B  1 108 ? 18.66800  -41.31600 6.70700   1.000 41.48000  ? 139 MET B CB  1 
ATOM   4413  C  CG  . MET B  1 108 ? 17.21400  -41.21300 7.13200   1.000 46.65000  ? 139 MET B CG  1 
ATOM   4414  S  SD  . MET B  1 108 ? 16.39300  -39.82300 6.31500   1.000 52.40000  ? 139 MET B SD  1 
ATOM   4415  C  CE  . MET B  1 108 ? 14.70200  -40.18700 6.73400   1.000 46.06000  ? 139 MET B CE  1 
ATOM   4416  N  N   . SER B  1 109 ? 18.53300  -43.00300 9.59900   1.000 47.01000  ? 140 SER B N   1 
ATOM   4417  C  CA  . SER B  1 109 ? 18.50800  -42.92200 11.05500  1.000 45.23000  ? 140 SER B CA  1 
ATOM   4418  C  C   . SER B  1 109 ? 19.80300  -43.44400 11.65300  1.000 43.19000  ? 140 SER B C   1 
ATOM   4419  O  O   . SER B  1 109 ? 20.27000  -42.92100 12.66600  1.000 39.62000  ? 140 SER B O   1 
ATOM   4420  C  CB  . SER B  1 109 ? 17.35100  -43.72900 11.62400  1.000 42.65000  ? 140 SER B CB  1 
ATOM   4421  O  OG  . SER B  1 109 ? 17.32200  -44.99200 10.99800  1.000 43.53000  ? 140 SER B OG  1 
ATOM   4422  N  N   . LYS B  1 110 ? 20.33000  -44.54400 11.11000  1.000 41.96000  ? 141 LYS B N   1 
ATOM   4423  C  CA  . LYS B  1 110 ? 21.61000  -45.04900 11.59200  1.000 50.24000  ? 141 LYS B CA  1 
ATOM   4424  C  C   . LYS B  1 110 ? 22.72300  -44.04700 11.31400  1.000 44.88000  ? 141 LYS B C   1 
ATOM   4425  O  O   . LYS B  1 110 ? 23.53600  -43.74800 12.19200  1.000 50.07000  ? 141 LYS B O   1 
ATOM   4426  C  CB  . LYS B  1 110 ? 21.92000  -46.40200 10.95000  1.000 47.23000  ? 141 LYS B CB  1 
ATOM   4427  C  CG  . LYS B  1 110 ? 23.20600  -47.02700 11.48500  1.000 50.04000  ? 141 LYS B CG  1 
ATOM   4428  C  CD  . LYS B  1 110 ? 23.25900  -48.51500 11.14500  1.000 60.58000  ? 141 LYS B CD  1 
ATOM   4429  C  CE  . LYS B  1 110 ? 22.74000  -49.39900 12.29900  1.000 60.88000  ? 141 LYS B CE  1 
ATOM   4430  N  NZ  . LYS B  1 110 ? 23.79000  -49.67400 13.33900  1.000 57.82000  ? 141 LYS B NZ  1 
ATOM   4431  N  N   . VAL B  1 111 ? 22.73900  -43.47900 10.10800  1.000 49.80000  ? 142 VAL B N   1 
ATOM   4432  C  CA  . VAL B  1 111 ? 23.71700  -42.45300 9.77300   1.000 45.63000  ? 142 VAL B CA  1 
ATOM   4433  C  C   . VAL B  1 111 ? 23.62000  -41.29800 10.75600  1.000 48.47000  ? 142 VAL B C   1 
ATOM   4434  O  O   . VAL B  1 111 ? 24.62900  -40.83100 11.28700  1.000 46.33000  ? 142 VAL B O   1 
ATOM   4435  C  CB  . VAL B  1 111 ? 23.51400  -41.97700 8.32200   1.000 42.08000  ? 142 VAL B CB  1 
ATOM   4436  C  CG1 . VAL B  1 111 ? 24.42900  -40.80800 7.99700   1.000 42.06000  ? 142 VAL B CG1 1 
ATOM   4437  C  CG2 . VAL B  1 111 ? 23.76800  -43.13500 7.36300   1.000 39.10000  ? 142 VAL B CG2 1 
ATOM   4438  N  N   . LEU B  1 112 ? 22.39900  -40.83200 11.03600  1.000 51.19000  ? 143 LEU B N   1 
ATOM   4439  C  CA  . LEU B  1 112 ? 22.28700  -39.72300 11.97200  1.000 49.50000  ? 143 LEU B CA  1 
ATOM   4440  C  C   . LEU B  1 112 ? 22.69100  -40.16200 13.36100  1.000 44.85000  ? 143 LEU B C   1 
ATOM   4441  O  O   . LEU B  1 112 ? 23.31700  -39.39800 14.09800  1.000 51.78000  ? 143 LEU B O   1 
ATOM   4442  C  CB  . LEU B  1 112 ? 20.87200  -39.17400 11.99200  1.000 41.56000  ? 143 LEU B CB  1 
ATOM   4443  C  CG  . LEU B  1 112 ? 20.60000  -38.54200 10.64300  1.000 46.41000  ? 143 LEU B CG  1 
ATOM   4444  C  CD1 . LEU B  1 112 ? 19.07400  -38.36800 10.41600  1.000 54.09000  ? 143 LEU B CD1 1 
ATOM   4445  C  CD2 . LEU B  1 112 ? 21.31200  -37.28100 10.55000  1.000 36.89000  ? 143 LEU B CD2 1 
ATOM   4446  N  N   . GLN B  1 113 ? 22.36700  -41.40300 13.71900  1.000 40.14000  ? 144 GLN B N   1 
ATOM   4447  C  CA  . GLN B  1 113 ? 22.74800  -41.92400 15.02500  1.000 45.25000  ? 144 GLN B CA  1 
ATOM   4448  C  C   . GLN B  1 113 ? 24.27100  -41.97700 15.17100  1.000 47.42000  ? 144 GLN B C   1 
ATOM   4449  O  O   . GLN B  1 113 ? 24.82000  -41.57300 16.20300  1.000 43.41000  ? 144 GLN B O   1 
ATOM   4450  C  CB  . GLN B  1 113 ? 22.13600  -43.30600 15.24700  1.000 41.74000  ? 144 GLN B CB  1 
ATOM   4451  C  CG  . GLN B  1 113 ? 22.44400  -43.88400 16.62300  1.000 37.80000  ? 144 GLN B CG  1 
ATOM   4452  C  CD  . GLN B  1 113 ? 21.85200  -45.24800 16.82400  1.000 39.90000  ? 144 GLN B CD  1 
ATOM   4453  O  OE1 . GLN B  1 113 ? 22.17900  -46.19200 16.11000  1.000 43.12000  ? 144 GLN B OE1 1 
ATOM   4454  N  NE2 . GLN B  1 113 ? 20.97200  -45.36700 17.80200  1.000 43.55000  ? 144 GLN B NE2 1 
ATOM   4455  N  N   . ASN B  1 114 ? 24.96800  -42.50300 14.15600  1.000 48.64000  ? 145 ASN B N   1 
ATOM   4456  C  CA  . ASN B  1 114 ? 26.42700  -42.54000 14.19600  1.000 48.25000  ? 145 ASN B CA  1 
ATOM   4457  C  C   . ASN B  1 114 ? 27.06800  -41.15200 14.19700  1.000 50.19000  ? 145 ASN B C   1 
ATOM   4458  O  O   . ASN B  1 114 ? 28.22900  -41.03500 14.61600  1.000 50.10000  ? 145 ASN B O   1 
ATOM   4459  C  CB  . ASN B  1 114 ? 26.94600  -43.38200 13.03600  1.000 43.11000  ? 145 ASN B CB  1 
ATOM   4460  C  CG  . ASN B  1 114 ? 26.63000  -44.86600 13.21800  1.000 56.53000  ? 145 ASN B CG  1 
ATOM   4461  O  OD1 . ASN B  1 114 ? 26.33900  -45.30900 14.32900  1.000 60.00000  ? 145 ASN B OD1 1 
ATOM   4462  N  ND2 . ASN B  1 114 ? 26.67700  -45.63400 12.13100  1.000 57.75000  ? 145 ASN B ND2 1 
ATOM   4463  N  N   . ALA B  1 115 ? 26.32000  -40.09200 13.87500  1.000 49.39000  ? 146 ALA B N   1 
ATOM   4464  C  CA  . ALA B  1 115 ? 26.83000  -38.72300 13.95000  1.000 46.13000  ? 146 ALA B CA  1 
ATOM   4465  C  C   . ALA B  1 115 ? 26.41400  -38.02100 15.24000  1.000 44.47000  ? 146 ALA B C   1 
ATOM   4466  O  O   . ALA B  1 115 ? 26.48700  -36.78700 15.32800  1.000 42.70000  ? 146 ALA B O   1 
ATOM   4467  C  CB  . ALA B  1 115 ? 26.37100  -37.90200 12.74600  1.000 43.15000  ? 146 ALA B CB  1 
ATOM   4468  N  N   . GLY B  1 116 ? 25.96400  -38.77700 16.23800  1.000 46.06000  ? 147 GLY B N   1 
ATOM   4469  C  CA  . GLY B  1 116 ? 25.69200  -38.20000 17.53700  1.000 40.38000  ? 147 GLY B CA  1 
ATOM   4470  C  C   . GLY B  1 116 ? 24.28200  -37.69100 17.74300  1.000 41.79000  ? 147 GLY B C   1 
ATOM   4471  O  O   . GLY B  1 116 ? 24.05200  -36.95000 18.69300  1.000 44.25000  ? 147 GLY B O   1 
ATOM   4472  N  N   . TYR B  1 117 ? 23.33000  -38.04600 16.88800  1.000 43.56000  ? 148 TYR B N   1 
ATOM   4473  C  CA  . TYR B  1 117 ? 21.95600  -37.59300 17.08400  1.000 43.94000  ? 148 TYR B CA  1 
ATOM   4474  C  C   . TYR B  1 117 ? 21.22100  -38.55800 18.01000  1.000 40.49000  ? 148 TYR B C   1 
ATOM   4475  O  O   . TYR B  1 117 ? 21.46300  -39.77100 17.99900  1.000 41.30000  ? 148 TYR B O   1 
ATOM   4476  C  CB  . TYR B  1 117 ? 21.23200  -37.48100 15.74400  1.000 42.86000  ? 148 TYR B CB  1 
ATOM   4477  C  CG  . TYR B  1 117 ? 21.35800  -36.14800 15.05600  1.000 40.86000  ? 148 TYR B CG  1 
ATOM   4478  C  CD1 . TYR B  1 117 ? 22.58300  -35.71100 14.55300  1.000 48.44000  ? 148 TYR B CD1 1 
ATOM   4479  C  CD2 . TYR B  1 117 ? 20.24600  -35.37000 14.82000  1.000 43.98000  ? 148 TYR B CD2 1 
ATOM   4480  C  CE1 . TYR B  1 117 ? 22.68700  -34.48800 13.87900  1.000 49.36000  ? 148 TYR B CE1 1 
ATOM   4481  C  CE2 . TYR B  1 117 ? 20.33600  -34.16100 14.14300  1.000 43.18000  ? 148 TYR B CE2 1 
ATOM   4482  C  CZ  . TYR B  1 117 ? 21.55000  -33.73100 13.67900  1.000 42.07000  ? 148 TYR B CZ  1 
ATOM   4483  O  OH  . TYR B  1 117 ? 21.60900  -32.53000 13.02300  1.000 44.13000  ? 148 TYR B OH  1 
ATOM   4484  N  N   . TYR B  1 118 ? 20.35200  -38.00800 18.83800  1.000 42.15000  ? 149 TYR B N   1 
ATOM   4485  C  CA  . TYR B  1 118 ? 19.38800  -38.81100 19.57500  1.000 45.81000  ? 149 TYR B CA  1 
ATOM   4486  C  C   . TYR B  1 118 ? 18.25000  -39.16100 18.62000  1.000 44.86000  ? 149 TYR B C   1 
ATOM   4487  O  O   . TYR B  1 118 ? 17.60700  -38.25700 18.07500  1.000 41.30000  ? 149 TYR B O   1 
ATOM   4488  C  CB  . TYR B  1 118 ? 18.87000  -38.02100 20.77000  1.000 45.33000  ? 149 TYR B CB  1 
ATOM   4489  C  CG  . TYR B  1 118 ? 17.77100  -38.72200 21.51700  1.000 47.34000  ? 149 TYR B CG  1 
ATOM   4490  C  CD1 . TYR B  1 118 ? 18.05400  -39.75300 22.39900  1.000 51.41000  ? 149 TYR B CD1 1 
ATOM   4491  C  CD2 . TYR B  1 118 ? 16.45100  -38.37700 21.31600  1.000 47.61000  ? 149 TYR B CD2 1 
ATOM   4492  C  CE1 . TYR B  1 118 ? 17.05700  -40.39700 23.07500  1.000 47.99000  ? 149 TYR B CE1 1 
ATOM   4493  C  CE2 . TYR B  1 118 ? 15.43800  -39.02600 21.97600  1.000 51.34000  ? 149 TYR B CE2 1 
ATOM   4494  C  CZ  . TYR B  1 118 ? 15.74400  -40.03400 22.85300  1.000 46.38000  ? 149 TYR B CZ  1 
ATOM   4495  O  OH  . TYR B  1 118 ? 14.73100  -40.67200 23.53000  1.000 42.23000  ? 149 TYR B OH  1 
ATOM   4496  N  N   . THR B  1 119 ? 18.04000  -40.45600 18.37000  1.000 39.64000  ? 150 THR B N   1 
ATOM   4497  C  CA  . THR B  1 119 ? 17.10700  -40.91200 17.35200  1.000 43.87000  ? 150 THR B CA  1 
ATOM   4498  C  C   . THR B  1 119 ? 15.88800  -41.59700 17.96400  1.000 45.63000  ? 150 THR B C   1 
ATOM   4499  O  O   . THR B  1 119 ? 16.00600  -42.40900 18.88800  1.000 44.61000  ? 150 THR B O   1 
ATOM   4500  C  CB  . THR B  1 119 ? 17.79600  -41.86200 16.37300  1.000 39.67000  ? 150 THR B CB  1 
ATOM   4501  O  OG1 . THR B  1 119 ? 18.32200  -42.98800 17.09000  1.000 43.92000  ? 150 THR B OG1 1 
ATOM   4502  C  CG2 . THR B  1 119 ? 18.93400  -41.13400 15.65000  1.000 41.71000  ? 150 THR B CG2 1 
ATOM   4503  N  N   . SER B  1 120 ? 14.72300  -41.31900 17.39500  1.000 42.21000  ? 151 SER B N   1 
ATOM   4504  C  CA  . SER B  1 120 ? 13.48600  -41.84400 17.95100  1.000 44.27000  ? 151 SER B CA  1 
ATOM   4505  C  C   . SER B  1 120 ? 12.51400  -42.07800 16.80800  1.000 41.88000  ? 151 SER B C   1 
ATOM   4506  O  O   . SER B  1 120 ? 12.29900  -41.18600 15.97500  1.000 41.86000  ? 151 SER B O   1 
ATOM   4507  C  CB  . SER B  1 120 ? 12.91300  -40.86300 18.98700  1.000 40.95000  ? 151 SER B CB  1 
ATOM   4508  O  OG  . SER B  1 120 ? 11.52800  -41.02200 19.17300  1.000 42.89000  ? 151 SER B OG  1 
ATOM   4509  N  N   . ALA B  1 121 ? 11.91400  -43.26700 16.80100  1.000 40.83000  ? 152 ALA B N   1 
ATOM   4510  C  CA  . ALA B  1 121 ? 10.88400  -43.66900 15.86300  1.000 38.17000  ? 152 ALA B CA  1 
ATOM   4511  C  C   . ALA B  1 121 ? 9.61200   -43.94700 16.65500  1.000 46.14000  ? 152 ALA B C   1 
ATOM   4512  O  O   . ALA B  1 121 ? 9.64600   -44.67100 17.65100  1.000 45.48000  ? 152 ALA B O   1 
ATOM   4513  C  CB  . ALA B  1 121 ? 11.30900  -44.91800 15.09000  1.000 36.20000  ? 152 ALA B CB  1 
ATOM   4514  N  N   . ILE B  1 122 ? 8.49700   -43.38600 16.20200  1.000 40.10000  ? 153 ILE B N   1 
ATOM   4515  C  CA  . ILE B  1 122 ? 7.21400   -43.46800 16.88800  1.000 38.06000  ? 153 ILE B CA  1 
ATOM   4516  C  C   . ILE B  1 122 ? 6.12500   -43.81800 15.87600  1.000 43.92000  ? 153 ILE B C   1 
ATOM   4517  O  O   . ILE B  1 122 ? 6.03300   -43.20000 14.80700  1.000 35.39000  ? 153 ILE B O   1 
ATOM   4518  C  CB  . ILE B  1 122 ? 6.87700   -42.13000 17.57800  1.000 36.29000  ? 153 ILE B CB  1 
ATOM   4519  C  CG1 . ILE B  1 122 ? 7.93900   -41.75800 18.60700  1.000 37.43000  ? 153 ILE B CG1 1 
ATOM   4520  C  CG2 . ILE B  1 122 ? 5.47000   -42.14500 18.16500  1.000 41.91000  ? 153 ILE B CG2 1 
ATOM   4521  C  CD1 . ILE B  1 122 ? 7.87900   -40.31500 19.02500  1.000 31.61000  ? 153 ILE B CD1 1 
ATOM   4522  N  N   . GLY B  1 123 ? 5.24900   -44.75500 16.25100  1.000 43.01000  ? 154 GLY B N   1 
ATOM   4523  C  CA  . GLY B  1 123 ? 4.10000   -45.09700 15.42300  1.000 37.28000  ? 154 GLY B CA  1 
ATOM   4524  C  C   . GLY B  1 123 ? 4.37400   -46.28300 14.50800  1.000 40.34000  ? 154 GLY B C   1 
ATOM   4525  O  O   . GLY B  1 123 ? 4.86100   -47.32000 14.95700  1.000 40.62000  ? 154 GLY B O   1 
ATOM   4526  N  N   . LYS B  1 124 ? 4.03300   -46.12800 13.23200  1.000 39.92000  ? 155 LYS B N   1 
ATOM   4527  C  CA  . LYS B  1 124 ? 4.01800   -47.22500 12.26200  1.000 40.49000  ? 155 LYS B CA  1 
ATOM   4528  C  C   . LYS B  1 124 ? 5.40700   -47.50700 11.69000  1.000 41.91000  ? 155 LYS B C   1 
ATOM   4529  O  O   . LYS B  1 124 ? 6.14900   -46.58400 11.36400  1.000 39.90000  ? 155 LYS B O   1 
ATOM   4530  C  CB  . LYS B  1 124 ? 3.06100   -46.87000 11.11900  1.000 34.66000  ? 155 LYS B CB  1 
ATOM   4531  C  CG  . LYS B  1 124 ? 3.18200   -47.70800 9.84800   1.000 43.17000  ? 155 LYS B CG  1 
ATOM   4532  C  CD  . LYS B  1 124 ? 2.04900   -47.34500 8.85900   1.000 40.51000  ? 155 LYS B CD  1 
ATOM   4533  C  CE  . LYS B  1 124 ? 2.12800   -48.10900 7.52700   1.000 39.20000  ? 155 LYS B CE  1 
ATOM   4534  N  NZ  . LYS B  1 124 ? 0.88000   -47.91700 6.67900   1.000 43.97000  ? 155 LYS B NZ  1 
ATOM   4535  N  N   . TRP B  1 125 ? 5.72600   -48.79100 11.50100  1.000 42.73000  ? 156 TRP B N   1 
ATOM   4536  C  CA  . TRP B  1 125 ? 6.99800   -49.20100 10.91300  1.000 45.06000  ? 156 TRP B CA  1 
ATOM   4537  C  C   . TRP B  1 125 ? 6.77700   -49.79100 9.52500   1.000 44.71000  ? 156 TRP B C   1 
ATOM   4538  O  O   . TRP B  1 125 ? 6.93500   -49.09000 8.51800   1.000 45.42000  ? 156 TRP B O   1 
ATOM   4539  C  CB  . TRP B  1 125 ? 7.70200   -50.18900 11.85100  1.000 44.61000  ? 156 TRP B CB  1 
ATOM   4540  C  CG  . TRP B  1 125 ? 9.10000   -50.59100 11.48800  1.000 44.29000  ? 156 TRP B CG  1 
ATOM   4541  C  CD1 . TRP B  1 125 ? 9.53200   -51.85700 11.23600  1.000 47.97000  ? 156 TRP B CD1 1 
ATOM   4542  C  CD2 . TRP B  1 125 ? 10.26500  -49.74900 11.40600  1.000 43.53000  ? 156 TRP B CD2 1 
ATOM   4543  N  NE1 . TRP B  1 125 ? 10.87900  -51.86200 10.98800  1.000 45.33000  ? 156 TRP B NE1 1 
ATOM   4544  C  CE2 . TRP B  1 125 ? 11.35400  -50.58000 11.07000  1.000 42.28000  ? 156 TRP B CE2 1 
ATOM   4545  C  CE3 . TRP B  1 125 ? 10.48500  -48.37800 11.54800  1.000 41.60000  ? 156 TRP B CE3 1 
ATOM   4546  C  CZ2 . TRP B  1 125 ? 12.64700  -50.08800 10.87800  1.000 41.97000  ? 156 TRP B CZ2 1 
ATOM   4547  C  CZ3 . TRP B  1 125 ? 11.78000  -47.88500 11.36600  1.000 43.02000  ? 156 TRP B CZ3 1 
ATOM   4548  C  CH2 . TRP B  1 125 ? 12.84200  -48.74200 11.03200  1.000 42.60000  ? 156 TRP B CH2 1 
ATOM   4549  N  N   . HIS B  1 126 ? 6.40300   -51.06900 9.46200   1.000 39.40000  ? 157 HIS B N   1 
ATOM   4550  C  CA  . HIS B  1 126 ? 6.09300   -51.77100 8.22400   1.000 44.79000  ? 157 HIS B CA  1 
ATOM   4551  C  C   . HIS B  1 126 ? 7.33000   -52.02900 7.37400   1.000 46.68000  ? 157 HIS B C   1 
ATOM   4552  O  O   . HIS B  1 126 ? 7.22400   -52.18900 6.14900   1.000 45.28000  ? 157 HIS B O   1 
ATOM   4553  C  CB  . HIS B  1 126 ? 5.03600   -51.02800 7.38600   1.000 38.59000  ? 157 HIS B CB  1 
ATOM   4554  C  CG  . HIS B  1 126 ? 4.25100   -51.92400 6.47300   1.000 48.34000  ? 157 HIS B CG  1 
ATOM   4555  N  ND1 . HIS B  1 126 ? 3.49900   -51.44500 5.41800   1.000 43.82000  ? 157 HIS B ND1 1 
ATOM   4556  C  CD2 . HIS B  1 126 ? 4.06400   -53.26900 6.48700   1.000 45.68000  ? 157 HIS B CD2 1 
ATOM   4557  C  CE1 . HIS B  1 126 ? 2.92300   -52.46000 4.79700   1.000 45.72000  ? 157 HIS B CE1 1 
ATOM   4558  N  NE2 . HIS B  1 126 ? 3.24500   -53.57700 5.42700   1.000 49.14000  ? 157 HIS B NE2 1 
ATOM   4559  N  N   . LEU B  1 127 ? 8.50900   -52.07300 7.98700   1.000 42.08000  ? 158 LEU B N   1 
ATOM   4560  C  CA  . LEU B  1 127 ? 9.72600   -52.39700 7.25500   1.000 49.33000  ? 158 LEU B CA  1 
ATOM   4561  C  C   . LEU B  1 127 ? 10.32100  -53.72900 7.69600   1.000 47.60000  ? 158 LEU B C   1 
ATOM   4562  O  O   . LEU B  1 127 ? 11.51000  -53.98100 7.48700   1.000 48.13000  ? 158 LEU B O   1 
ATOM   4563  C  CB  . LEU B  1 127 ? 10.74900  -51.26700 7.39000   1.000 42.78000  ? 158 LEU B CB  1 
ATOM   4564  C  CG  . LEU B  1 127 ? 10.16200  -49.90900 6.96000   1.000 45.65000  ? 158 LEU B CG  1 
ATOM   4565  C  CD1 . LEU B  1 127 ? 11.16400  -48.79100 7.19200   1.000 39.56000  ? 158 LEU B CD1 1 
ATOM   4566  C  CD2 . LEU B  1 127 ? 9.65100   -49.87800 5.51700   1.000 40.12000  ? 158 LEU B CD2 1 
ATOM   4567  N  N   . GLY B  1 128 ? 9.52600   -54.57400 8.32700   1.000 44.87000  ? 159 GLY B N   1 
ATOM   4568  C  CA  . GLY B  1 128 ? 10.02500  -55.86200 8.74800   1.000 45.39000  ? 159 GLY B CA  1 
ATOM   4569  C  C   . GLY B  1 128 ? 9.71900   -56.11600 10.20200  1.000 43.63000  ? 159 GLY B C   1 
ATOM   4570  O  O   . GLY B  1 128 ? 9.99900   -55.26300 11.04700  1.000 44.01000  ? 159 GLY B O   1 
ATOM   4571  N  N   . ALA B  1 129 ? 9.12600   -57.26600 10.50500  1.000 40.85000  ? 160 ALA B N   1 
ATOM   4572  C  CA  . ALA B  1 129 ? 8.71900   -57.59200 11.85800  1.000 49.92000  ? 160 ALA B CA  1 
ATOM   4573  C  C   . ALA B  1 129 ? 9.67600   -58.55700 12.57000  1.000 53.31000  ? 160 ALA B C   1 
ATOM   4574  O  O   . ALA B  1 129 ? 9.42400   -58.90700 13.72100  1.000 52.70000  ? 160 ALA B O   1 
ATOM   4575  C  CB  . ALA B  1 129 ? 7.29100   -58.16100 11.85600  1.000 50.26000  ? 160 ALA B CB  1 
ATOM   4576  N  N   . ALA B  1 130 ? 10.73300  -59.01600 11.91300  1.000 54.68000  ? 161 ALA B N   1 
ATOM   4577  C  CA  . ALA B  1 130 ? 11.73800  -59.87100 12.55100  1.000 54.96000  ? 161 ALA B CA  1 
ATOM   4578  C  C   . ALA B  1 130 ? 12.80300  -59.04300 13.26400  1.000 48.81000  ? 161 ALA B C   1 
ATOM   4579  O  O   . ALA B  1 130 ? 13.00700  -57.87100 12.94400  1.000 50.04000  ? 161 ALA B O   1 
ATOM   4580  C  CB  . ALA B  1 130 ? 12.40400  -60.77800 11.51600  1.000 50.95000  ? 161 ALA B CB  1 
ATOM   4581  N  N   . PRO B  1 131 ? 13.48300  -59.62900 14.26000  1.000 55.16000  ? 162 PRO B N   1 
ATOM   4582  C  CA  . PRO B  1 131 ? 14.42200  -58.83500 15.07200  1.000 48.75000  ? 162 PRO B CA  1 
ATOM   4583  C  C   . PRO B  1 131 ? 15.49600  -58.10200 14.28100  1.000 51.20000  ? 162 PRO B C   1 
ATOM   4584  O  O   . PRO B  1 131 ? 15.86900  -56.98200 14.65900  1.000 50.80000  ? 162 PRO B O   1 
ATOM   4585  C  CB  . PRO B  1 131 ? 15.03800  -59.88600 16.00300  1.000 52.43000  ? 162 PRO B CB  1 
ATOM   4586  C  CG  . PRO B  1 131 ? 13.96700  -60.89000 16.17500  1.000 60.53000  ? 162 PRO B CG  1 
ATOM   4587  C  CD  . PRO B  1 131 ? 13.25700  -60.96500 14.84600  1.000 58.62000  ? 162 PRO B CD  1 
ATOM   4588  N  N   . LYS B  1 132 ? 16.03600  -58.69400 13.21700  1.000 48.54000  ? 163 LYS B N   1 
ATOM   4589  C  CA  . LYS B  1 132 ? 17.08500  -57.98000 12.48900  1.000 54.54000  ? 163 LYS B CA  1 
ATOM   4590  C  C   . LYS B  1 132 ? 16.56900  -56.72600 11.78100  1.000 55.85000  ? 163 LYS B C   1 
ATOM   4591  O  O   . LYS B  1 132 ? 17.37900  -55.84400 11.45000  1.000 48.89000  ? 163 LYS B O   1 
ATOM   4592  C  CB  . LYS B  1 132 ? 17.77600  -58.90800 11.48400  1.000 47.51000  ? 163 LYS B CB  1 
ATOM   4593  C  CG  . LYS B  1 132 ? 16.88200  -59.42800 10.40500  1.000 55.29000  ? 163 LYS B CG  1 
ATOM   4594  C  CD  . LYS B  1 132 ? 17.60700  -59.56100 9.07300   1.000 56.55000  ? 163 LYS B CD  1 
ATOM   4595  C  CE  . LYS B  1 132 ? 17.81500  -61.00400 8.68200   1.000 57.47000  ? 163 LYS B CE  1 
ATOM   4596  N  NZ  . LYS B  1 132 ? 18.83400  -61.10200 7.59600   1.000 67.27000  ? 163 LYS B NZ  1 
ATOM   4597  N  N   . PHE B  1 133 ? 15.25000  -56.60400 11.58700  1.000 43.26000  ? 164 PHE B N   1 
ATOM   4598  C  CA  . PHE B  1 133 ? 14.64600  -55.44000 10.94700  1.000 42.93000  ? 164 PHE B CA  1 
ATOM   4599  C  C   . PHE B  1 133 ? 14.06200  -54.44400 11.94100  1.000 49.00000  ? 164 PHE B C   1 
ATOM   4600  O  O   . PHE B  1 133 ? 13.46100  -53.45700 11.51500  1.000 51.20000  ? 164 PHE B O   1 
ATOM   4601  C  CB  . PHE B  1 133 ? 13.54200  -55.86800 9.97400   1.000 46.36000  ? 164 PHE B CB  1 
ATOM   4602  C  CG  . PHE B  1 133 ? 13.99000  -56.84600 8.91100   1.000 50.31000  ? 164 PHE B CG  1 
ATOM   4603  C  CD1 . PHE B  1 133 ? 15.03500  -56.52900 8.03900   1.000 48.71000  ? 164 PHE B CD1 1 
ATOM   4604  C  CD2 . PHE B  1 133 ? 13.35300  -58.07600 8.77300   1.000 48.12000  ? 164 PHE B CD2 1 
ATOM   4605  C  CE1 . PHE B  1 133 ? 15.42800  -57.42900 7.05600   1.000 47.14000  ? 164 PHE B CE1 1 
ATOM   4606  C  CE2 . PHE B  1 133 ? 13.74100  -58.98500 7.79900   1.000 43.76000  ? 164 PHE B CE2 1 
ATOM   4607  C  CZ  . PHE B  1 133 ? 14.77200  -58.66400 6.93800   1.000 48.34000  ? 164 PHE B CZ  1 
ATOM   4608  N  N   . HIS B  1 134 ? 14.23400  -54.67200 13.24200  1.000 43.87000  ? 165 HIS B N   1 
ATOM   4609  C  CA  . HIS B  1 134 ? 13.61400  -53.84800 14.26500  1.000 49.06000  ? 165 HIS B CA  1 
ATOM   4610  C  C   . HIS B  1 134 ? 14.22700  -52.44300 14.27500  1.000 48.48000  ? 165 HIS B C   1 
ATOM   4611  O  O   . HIS B  1 134 ? 15.38500  -52.26700 13.88400  1.000 46.76000  ? 165 HIS B O   1 
ATOM   4612  C  CB  . HIS B  1 134 ? 13.78300  -54.52600 15.62700  1.000 43.15000  ? 165 HIS B CB  1 
ATOM   4613  C  CG  . HIS B  1 134 ? 13.00000  -53.89900 16.73200  1.000 39.66000  ? 165 HIS B CG  1 
ATOM   4614  N  ND1 . HIS B  1 134 ? 13.42400  -52.76000 17.38900  1.000 47.18000  ? 165 HIS B ND1 1 
ATOM   4615  C  CD2 . HIS B  1 134 ? 11.83900  -54.26500 17.32500  1.000 43.24000  ? 165 HIS B CD2 1 
ATOM   4616  C  CE1 . HIS B  1 134 ? 12.55000  -52.44300 18.32800  1.000 39.29000  ? 165 HIS B CE1 1 
ATOM   4617  N  NE2 . HIS B  1 134 ? 11.58400  -53.34800 18.31800  1.000 43.21000  ? 165 HIS B NE2 1 
ATOM   4618  N  N   . PRO B  1 135 ? 13.44500  -51.41600 14.65300  1.000 45.67000  ? 166 PRO B N   1 
ATOM   4619  C  CA  . PRO B  1 135 ? 13.99900  -50.04700 14.68100  1.000 46.23000  ? 166 PRO B CA  1 
ATOM   4620  C  C   . PRO B  1 135 ? 15.22600  -49.87900 15.56000  1.000 44.46000  ? 166 PRO B C   1 
ATOM   4621  O  O   . PRO B  1 135 ? 16.16800  -49.17900 15.16000  1.000 44.61000  ? 166 PRO B O   1 
ATOM   4622  C  CB  . PRO B  1 135 ? 12.82000  -49.19800 15.17500  1.000 40.04000  ? 166 PRO B CB  1 
ATOM   4623  C  CG  . PRO B  1 135 ? 11.60700  -49.95000 14.70200  1.000 45.12000  ? 166 PRO B CG  1 
ATOM   4624  C  CD  . PRO B  1 135 ? 11.97400  -51.41900 14.75200  1.000 48.20000  ? 166 PRO B CD  1 
ATOM   4625  N  N   . ASN B  1 136 ? 15.25900  -50.50800 16.74000  1.000 46.96000  ? 167 ASN B N   1 
ATOM   4626  C  CA  . ASN B  1 136 ? 16.41100  -50.34000 17.62500  1.000 45.62000  ? 167 ASN B CA  1 
ATOM   4627  C  C   . ASN B  1 136 ? 17.68700  -50.90200 16.99700  1.000 43.59000  ? 167 ASN B C   1 
ATOM   4628  O  O   . ASN B  1 136 ? 18.78300  -50.48000 17.37100  1.000 50.77000  ? 167 ASN B O   1 
ATOM   4629  C  CB  . ASN B  1 136 ? 16.13900  -50.98900 18.98800  1.000 40.11000  ? 167 ASN B CB  1 
ATOM   4630  C  CG  . ASN B  1 136 ? 15.11100  -50.21300 19.82900  1.000 49.19000  ? 167 ASN B CG  1 
ATOM   4631  O  OD1 . ASN B  1 136 ? 14.25500  -50.80300 20.48900  1.000 52.18000  ? 167 ASN B OD1 1 
ATOM   4632  N  ND2 . ASN B  1 136 ? 15.20500  -48.89000 19.81300  1.000 45.10000  ? 167 ASN B ND2 1 
ATOM   4633  N  N   . LYS B  1 137 ? 17.56600  -51.81500 16.02300  1.000 45.98000  ? 168 LYS B N   1 
ATOM   4634  C  CA  . LYS B  1 137 ? 18.69500  -52.29300 15.22900  1.000 47.37000  ? 168 LYS B CA  1 
ATOM   4635  C  C   . LYS B  1 137 ? 18.94600  -51.47800 13.96400  1.000 47.82000  ? 168 LYS B C   1 
ATOM   4636  O  O   . LYS B  1 137 ? 19.98700  -51.66700 13.32600  1.000 46.10000  ? 168 LYS B O   1 
ATOM   4637  C  CB  . LYS B  1 137 ? 18.46400  -53.74800 14.77600  1.000 42.45000  ? 168 LYS B CB  1 
ATOM   4638  C  CG  . LYS B  1 137 ? 18.46100  -54.77900 15.88000  1.000 50.99000  ? 168 LYS B CG  1 
ATOM   4639  C  CD  . LYS B  1 137 ? 19.64800  -54.58200 16.82500  1.000 58.53000  ? 168 LYS B CD  1 
ATOM   4640  C  CE  . LYS B  1 137 ? 19.94100  -55.85100 17.60600  1.000 64.30000  ? 168 LYS B CE  1 
ATOM   4641  N  NZ  . LYS B  1 137 ? 18.73500  -56.73300 17.59700  1.000 63.63000  ? 168 LYS B NZ  1 
ATOM   4642  N  N   . ARG B  1 138 ? 18.04800  -50.56500 13.58400  1.000 45.23000  ? 169 ARG B N   1 
ATOM   4643  C  CA  . ARG B  1 138 ? 18.19400  -49.83000 12.32800  1.000 43.38000  ? 169 ARG B CA  1 
ATOM   4644  C  C   . ARG B  1 138 ? 18.41400  -48.34800 12.57000  1.000 45.27000  ? 169 ARG B C   1 
ATOM   4645  O  O   . ARG B  1 138 ? 17.92300  -47.51600 11.79900  1.000 49.60000  ? 169 ARG B O   1 
ATOM   4646  C  CB  . ARG B  1 138 ? 16.97800  -49.98700 11.41200  1.000 45.40000  ? 169 ARG B CB  1 
ATOM   4647  C  CG  . ARG B  1 138 ? 16.42700  -51.37000 11.16000  1.000 46.61000  ? 169 ARG B CG  1 
ATOM   4648  C  CD  . ARG B  1 138 ? 17.27000  -52.25600 10.29200  1.000 48.60000  ? 169 ARG B CD  1 
ATOM   4649  N  NE  . ARG B  1 138 ? 17.82500  -51.62900 9.09900   1.000 47.74000  ? 169 ARG B NE  1 
ATOM   4650  C  CZ  . ARG B  1 138 ? 17.64400  -52.06400 7.85400   1.000 47.64000  ? 169 ARG B CZ  1 
ATOM   4651  N  NH1 . ARG B  1 138 ? 16.77600  -53.02900 7.56500   1.000 42.73000  ? 169 ARG B NH1 1 
ATOM   4652  N  NH2 . ARG B  1 138 ? 18.39800  -51.56100 6.88100   1.000 41.61000  ? 169 ARG B NH2 1 
ATOM   4653  N  N   . GLY B  1 139 ? 19.08400  -48.00000 13.66000  1.000 42.02000  ? 170 GLY B N   1 
ATOM   4654  C  CA  . GLY B  1 139 ? 19.50900  -46.64200 13.89400  1.000 41.66000  ? 170 GLY B CA  1 
ATOM   4655  C  C   . GLY B  1 139 ? 18.68200  -45.83200 14.86300  1.000 46.62000  ? 170 GLY B C   1 
ATOM   4656  O  O   . GLY B  1 139 ? 18.91400  -44.61900 14.97300  1.000 42.55000  ? 170 GLY B O   1 
ATOM   4657  N  N   . PHE B  1 140 ? 17.71500  -46.44300 15.55000  1.000 43.29000  ? 171 PHE B N   1 
ATOM   4658  C  CA  . PHE B  1 140 ? 16.82900  -45.71400 16.45100  1.000 45.59000  ? 171 PHE B CA  1 
ATOM   4659  C  C   . PHE B  1 140 ? 17.13400  -46.05500 17.90800  1.000 42.30000  ? 171 PHE B C   1 
ATOM   4660  O  O   . PHE B  1 140 ? 16.90100  -47.18800 18.33700  1.000 46.49000  ? 171 PHE B O   1 
ATOM   4661  C  CB  . PHE B  1 140 ? 15.36600  -46.02200 16.10400  1.000 42.57000  ? 171 PHE B CB  1 
ATOM   4662  C  CG  . PHE B  1 140 ? 14.90500  -45.38100 14.81600  1.000 38.92000  ? 171 PHE B CG  1 
ATOM   4663  C  CD1 . PHE B  1 140 ? 14.60100  -44.02600 14.75900  1.000 40.11000  ? 171 PHE B CD1 1 
ATOM   4664  C  CD2 . PHE B  1 140 ? 14.83500  -46.12100 13.65100  1.000 40.37000  ? 171 PHE B CD2 1 
ATOM   4665  C  CE1 . PHE B  1 140 ? 14.19000  -43.43100 13.56600  1.000 40.82000  ? 171 PHE B CE1 1 
ATOM   4666  C  CE2 . PHE B  1 140 ? 14.42100  -45.53700 12.45400  1.000 36.76000  ? 171 PHE B CE2 1 
ATOM   4667  C  CZ  . PHE B  1 140 ? 14.09300  -44.20500 12.41500  1.000 34.76000  ? 171 PHE B CZ  1 
ATOM   4668  N  N   . ASP B  1 141 ? 17.58300  -45.05800 18.68400  1.000 43.63000  ? 172 ASP B N   1 
ATOM   4669  C  CA  . ASP B  1 141 ? 17.77200  -45.26800 20.12400  1.000 48.07000  ? 172 ASP B CA  1 
ATOM   4670  C  C   . ASP B  1 141 ? 16.48000  -45.69900 20.79000  1.000 52.59000  ? 172 ASP B C   1 
ATOM   4671  O  O   . ASP B  1 141 ? 16.49300  -46.53600 21.69800  1.000 50.67000  ? 172 ASP B O   1 
ATOM   4672  C  CB  . ASP B  1 141 ? 18.25000  -43.99100 20.81900  1.000 43.19000  ? 172 ASP B CB  1 
ATOM   4673  C  CG  . ASP B  1 141 ? 19.55100  -43.48700 20.26800  1.000 47.12000  ? 172 ASP B CG  1 
ATOM   4674  O  OD1 . ASP B  1 141 ? 20.38100  -44.33100 19.87000  1.000 47.90000  ? 172 ASP B OD1 1 
ATOM   4675  O  OD2 . ASP B  1 141 ? 19.70400  -42.25100 20.16900  1.000 44.13000  ? 172 ASP B OD2 1 
ATOM   4676  N  N   . ASP B  1 142 ? 15.35700  -45.10600 20.36900  1.000 53.08000  ? 173 ASP B N   1 
ATOM   4677  C  CA  . ASP B  1 142 ? 14.05600  -45.29800 20.99100  1.000 47.18000  ? 173 ASP B CA  1 
ATOM   4678  C  C   . ASP B  1 142 ? 13.01800  -45.63400 19.92700  1.000 48.67000  ? 173 ASP B C   1 
ATOM   4679  O  O   . ASP B  1 142 ? 12.97800  -45.01000 18.85800  1.000 42.38000  ? 173 ASP B O   1 
ATOM   4680  C  CB  . ASP B  1 142 ? 13.64800  -44.02900 21.75400  1.000 44.63000  ? 173 ASP B CB  1 
ATOM   4681  C  CG  . ASP B  1 142 ? 12.50200  -44.27400 22.71400  1.000 55.28000  ? 173 ASP B CG  1 
ATOM   4682  O  OD1 . ASP B  1 142 ? 12.65800  -45.13100 23.61600  1.000 49.36000  ? 173 ASP B OD1 1 
ATOM   4683  O  OD2 . ASP B  1 142 ? 11.44900  -43.61200 22.57300  1.000 64.08000  ? 173 ASP B OD2 1 
ATOM   4684  N  N   . PHE B  1 143 ? 12.17600  -46.62000 20.22700  1.000 52.08000  ? 174 PHE B N   1 
ATOM   4685  C  CA  . PHE B  1 143 ? 11.04600  -46.97600 19.37700  1.000 43.65000  ? 174 PHE B CA  1 
ATOM   4686  C  C   . PHE B  1 143 ? 9.80500   -47.17800 20.23100  1.000 49.02000  ? 174 PHE B C   1 
ATOM   4687  O  O   . PHE B  1 143 ? 9.84700   -47.89600 21.23900  1.000 47.93000  ? 174 PHE B O   1 
ATOM   4688  C  CB  . PHE B  1 143 ? 11.31700  -48.23900 18.56600  1.000 43.45000  ? 174 PHE B CB  1 
ATOM   4689  C  CG  . PHE B  1 143 ? 10.13600  -48.67400 17.74500  1.000 46.71000  ? 174 PHE B CG  1 
ATOM   4690  C  CD1 . PHE B  1 143 ? 9.48400   -47.76000 16.91100  1.000 46.98000  ? 174 PHE B CD1 1 
ATOM   4691  C  CD2 . PHE B  1 143 ? 9.67800   -49.97900 17.78500  1.000 43.91000  ? 174 PHE B CD2 1 
ATOM   4692  C  CE1 . PHE B  1 143 ? 8.36900   -48.14100 16.14900  1.000 45.22000  ? 174 PHE B CE1 1 
ATOM   4693  C  CE2 . PHE B  1 143 ? 8.56100   -50.37000 17.02000  1.000 48.57000  ? 174 PHE B CE2 1 
ATOM   4694  C  CZ  . PHE B  1 143 ? 7.91200   -49.45300 16.20300  1.000 43.59000  ? 174 PHE B CZ  1 
ATOM   4695  N  N   . TYR B  1 144 ? 8.71200   -46.53300 19.83000  1.000 48.31000  ? 175 TYR B N   1 
ATOM   4696  C  CA  . TYR B  1 144 ? 7.40800   -46.69900 20.46700  1.000 46.25000  ? 175 TYR B CA  1 
ATOM   4697  C  C   . TYR B  1 144 ? 6.35600   -46.76800 19.36600  1.000 43.01000  ? 175 TYR B C   1 
ATOM   4698  O  O   . TYR B  1 144 ? 6.05500   -45.75800 18.72500  1.000 44.11000  ? 175 TYR B O   1 
ATOM   4699  C  CB  . TYR B  1 144 ? 7.12400   -45.56600 21.44000  1.000 43.89000  ? 175 TYR B CB  1 
ATOM   4700  C  CG  . TYR B  1 144 ? 5.83300   -45.68800 22.19400  1.000 47.45000  ? 175 TYR B CG  1 
ATOM   4701  C  CD1 . TYR B  1 144 ? 4.63300   -45.28500 21.63300  1.000 45.71000  ? 175 TYR B CD1 1 
ATOM   4702  C  CD2 . TYR B  1 144 ? 5.80800   -46.20300 23.46900  1.000 53.52000  ? 175 TYR B CD2 1 
ATOM   4703  C  CE1 . TYR B  1 144 ? 3.45100   -45.38600 22.32600  1.000 43.78000  ? 175 TYR B CE1 1 
ATOM   4704  C  CE2 . TYR B  1 144 ? 4.62100   -46.31200 24.17800  1.000 49.89000  ? 175 TYR B CE2 1 
ATOM   4705  C  CZ  . TYR B  1 144 ? 3.44400   -45.90200 23.60500  1.000 51.15000  ? 175 TYR B CZ  1 
ATOM   4706  O  OH  . TYR B  1 144 ? 2.25100   -46.01900 24.30900  1.000 48.90000  ? 175 TYR B OH  1 
ATOM   4707  N  N   . GLY B  1 145 ? 5.80200   -47.95200 19.14900  1.000 39.07000  ? 176 GLY B N   1 
ATOM   4708  C  CA  . GLY B  1 145 ? 4.80200   -48.15300 18.12900  1.000 38.33000  ? 176 GLY B CA  1 
ATOM   4709  C  C   . GLY B  1 145 ? 4.54200   -49.61200 17.83500  1.000 43.33000  ? 176 GLY B C   1 
ATOM   4710  O  O   . GLY B  1 145 ? 4.55300   -50.45300 18.74700  1.000 42.93000  ? 176 GLY B O   1 
ATOM   4711  N  N   . PHE B  1 146 ? 4.26500   -49.91400 16.56700  1.000 37.79000  ? 177 PHE B N   1 
ATOM   4712  C  CA  . PHE B  1 146 ? 3.92300   -51.26000 16.13100  1.000 39.17000  ? 177 PHE B CA  1 
ATOM   4713  C  C   . PHE B  1 146 ? 4.67500   -51.56100 14.85400  1.000 38.12000  ? 177 PHE B C   1 
ATOM   4714  O  O   . PHE B  1 146 ? 5.05700   -50.65900 14.11000  1.000 37.77000  ? 177 PHE B O   1 
ATOM   4715  C  CB  . PHE B  1 146 ? 2.40100   -51.43500 15.90800  1.000 41.87000  ? 177 PHE B CB  1 
ATOM   4716  C  CG  . PHE B  1 146 ? 1.80600   -50.43500 14.96300  1.000 42.78000  ? 177 PHE B CG  1 
ATOM   4717  C  CD1 . PHE B  1 146 ? 1.42200   -49.17900 15.41300  1.000 46.28000  ? 177 PHE B CD1 1 
ATOM   4718  C  CD2 . PHE B  1 146 ? 1.63100   -50.74700 13.62900  1.000 38.92000  ? 177 PHE B CD2 1 
ATOM   4719  C  CE1 . PHE B  1 146 ? 0.87300   -48.24600 14.53200  1.000 43.55000  ? 177 PHE B CE1 1 
ATOM   4720  C  CE2 . PHE B  1 146 ? 1.08500   -49.83300 12.75100  1.000 42.20000  ? 177 PHE B CE2 1 
ATOM   4721  C  CZ  . PHE B  1 146 ? 0.70300   -48.58100 13.19900  1.000 41.43000  ? 177 PHE B CZ  1 
ATOM   4722  N  N   . LEU B  1 147 ? 4.88000   -52.83800 14.60000  1.000 41.89000  ? 178 LEU B N   1 
ATOM   4723  C  CA  . LEU B  1 147 ? 5.81000   -53.23200 13.55800  1.000 42.05000  ? 178 LEU B CA  1 
ATOM   4724  C  C   . LEU B  1 147 ? 5.16100   -53.38000 12.19300  1.000 44.09000  ? 178 LEU B C   1 
ATOM   4725  O  O   . LEU B  1 147 ? 5.87100   -53.32600 11.17800  1.000 47.31000  ? 178 LEU B O   1 
ATOM   4726  C  CB  . LEU B  1 147 ? 6.48300   -54.55600 13.94000  1.000 45.16000  ? 178 LEU B CB  1 
ATOM   4727  C  CG  . LEU B  1 147 ? 7.36600   -54.48900 15.19300  1.000 46.03000  ? 178 LEU B CG  1 
ATOM   4728  C  CD1 . LEU B  1 147 ? 8.05800   -55.82300 15.44200  1.000 50.76000  ? 178 LEU B CD1 1 
ATOM   4729  C  CD2 . LEU B  1 147 ? 8.39000   -53.38200 15.09900  1.000 45.09000  ? 178 LEU B CD2 1 
ATOM   4730  N  N   . GLY B  1 148 ? 3.84600   -53.57600 12.14300  1.000 45.20000  ? 179 GLY B N   1 
ATOM   4731  C  CA  . GLY B  1 148 ? 3.14500   -53.87000 10.90700  1.000 48.94000  ? 179 GLY B CA  1 
ATOM   4732  C  C   . GLY B  1 148 ? 2.61700   -52.64100 10.19200  1.000 47.70000  ? 179 GLY B C   1 
ATOM   4733  O  O   . GLY B  1 148 ? 3.11700   -51.52700 10.35900  1.000 43.13000  ? 179 GLY B O   1 
ATOM   4734  N  N   . GLY B  1 149 ? 1.56800   -52.85700 9.38900   1.000 42.52000  ? 180 GLY B N   1 
ATOM   4735  C  CA  . GLY B  1 149 ? 1.09500   -51.84300 8.47000   1.000 39.04000  ? 180 GLY B CA  1 
ATOM   4736  C  C   . GLY B  1 149 ? -0.05800  -50.99100 8.96900   1.000 49.41000  ? 180 GLY B C   1 
ATOM   4737  O  O   . GLY B  1 149 ? -0.39600  -49.97800 8.34100   1.000 44.89000  ? 180 GLY B O   1 
ATOM   4738  N  N   . GLY B  1 150 ? -0.69700  -51.38500 10.06700  1.000 40.18000  ? 181 GLY B N   1 
ATOM   4739  C  CA  . GLY B  1 150 ? -1.79500  -50.57900 10.55800  1.000 36.89000  ? 181 GLY B CA  1 
ATOM   4740  C  C   . GLY B  1 150 ? -2.18800  -51.03800 11.93700  1.000 46.50000  ? 181 GLY B C   1 
ATOM   4741  O  O   . GLY B  1 150 ? -1.66600  -52.02800 12.45600  1.000 47.19000  ? 181 GLY B O   1 
ATOM   4742  N  N   . HIS B  1 151 ? -3.13700  -50.31600 12.52700  1.000 44.02000  ? 182 HIS B N   1 
ATOM   4743  C  CA  . HIS B  1 151 ? -3.51000  -50.65500 13.88900  1.000 40.44000  ? 182 HIS B CA  1 
ATOM   4744  C  C   . HIS B  1 151 ? -4.82200  -49.99800 14.26000  1.000 39.48000  ? 182 HIS B C   1 
ATOM   4745  O  O   . HIS B  1 151 ? -5.08400  -48.85900 13.86300  1.000 37.02000  ? 182 HIS B O   1 
ATOM   4746  C  CB  . HIS B  1 151 ? -2.41500  -50.21400 14.87600  1.000 40.33000  ? 182 HIS B CB  1 
ATOM   4747  C  CG  . HIS B  1 151 ? -2.40200  -51.02500 16.13700  1.000 46.29000  ? 182 HIS B CG  1 
ATOM   4748  N  ND1 . HIS B  1 151 ? -3.28600  -50.80600 17.17400  1.000 44.97000  ? 182 HIS B ND1 1 
ATOM   4749  C  CD2 . HIS B  1 151 ? -1.67100  -52.11100 16.48600  1.000 43.10000  ? 182 HIS B CD2 1 
ATOM   4750  C  CE1 . HIS B  1 151 ? -3.05700  -51.68500 18.13500  1.000 47.76000  ? 182 HIS B CE1 1 
ATOM   4751  N  NE2 . HIS B  1 151 ? -2.08700  -52.49000 17.74000  1.000 48.79000  ? 182 HIS B NE2 1 
ATOM   4752  N  N   . ASP B  1 152 ? -5.61600  -50.70300 15.06200  1.000 42.91000  ? 183 ASP B N   1 
ATOM   4753  C  CA  . ASP B  1 152 ? -6.79200  -50.08500 15.65900  1.000 45.92000  ? 183 ASP B CA  1 
ATOM   4754  C  C   . ASP B  1 152 ? -6.36400  -48.99000 16.62800  1.000 45.28000  ? 183 ASP B C   1 
ATOM   4755  O  O   . ASP B  1 152 ? -5.28100  -49.04900 17.22000  1.000 42.43000  ? 183 ASP B O   1 
ATOM   4756  C  CB  . ASP B  1 152 ? -7.63200  -51.14700 16.35500  1.000 49.16000  ? 183 ASP B CB  1 
ATOM   4757  C  CG  . ASP B  1 152 ? -8.39900  -52.00100 15.36600  1.000 56.25000  ? 183 ASP B CG  1 
ATOM   4758  O  OD1 . ASP B  1 152 ? -7.81000  -52.36800 14.33100  1.000 53.10000  ? 183 ASP B OD1 1 
ATOM   4759  O  OD2 . ASP B  1 152 ? -9.57100  -52.35200 15.64200  1.000 71.65000  ? 183 ASP B OD2 1 
ATOM   4760  N  N   . TYR B  1 153 ? -7.23800  -47.99300 16.80500  1.000 38.24000  ? 184 TYR B N   1 
ATOM   4761  C  CA  . TYR B  1 153 ? -6.83500  -46.74000 17.43200  1.000 39.85000  ? 184 TYR B CA  1 
ATOM   4762  C  C   . TYR B  1 153 ? -7.10200  -46.64100 18.93100  1.000 42.55000  ? 184 TYR B C   1 
ATOM   4763  O  O   . TYR B  1 153 ? -6.41000  -45.85700 19.59800  1.000 48.75000  ? 184 TYR B O   1 
ATOM   4764  C  CB  . TYR B  1 153 ? -7.54100  -45.56100 16.74300  1.000 40.51000  ? 184 TYR B CB  1 
ATOM   4765  C  CG  . TYR B  1 153 ? -6.97000  -45.24500 15.37400  1.000 41.40000  ? 184 TYR B CG  1 
ATOM   4766  C  CD1 . TYR B  1 153 ? -7.33000  -45.98600 14.25400  1.000 40.63000  ? 184 TYR B CD1 1 
ATOM   4767  C  CD2 . TYR B  1 153 ? -6.04000  -44.23400 15.21200  1.000 38.26000  ? 184 TYR B CD2 1 
ATOM   4768  C  CE1 . TYR B  1 153 ? -6.78900  -45.70300 12.99800  1.000 41.69000  ? 184 TYR B CE1 1 
ATOM   4769  C  CE2 . TYR B  1 153 ? -5.48900  -43.95200 13.97300  1.000 36.70000  ? 184 TYR B CE2 1 
ATOM   4770  C  CZ  . TYR B  1 153 ? -5.86200  -44.67900 12.87300  1.000 42.10000  ? 184 TYR B CZ  1 
ATOM   4771  O  OH  . TYR B  1 153 ? -5.31200  -44.36800 11.64300  1.000 40.42000  ? 184 TYR B OH  1 
ATOM   4772  N  N   . PHE B  1 154 ? -8.02800  -47.43600 19.48400  1.000 36.59000  ? 185 PHE B N   1 
ATOM   4773  C  CA  . PHE B  1 154 ? -8.47200  -47.31200 20.87400  1.000 45.98000  ? 185 PHE B CA  1 
ATOM   4774  C  C   . PHE B  1 154 ? -8.03800  -48.50800 21.71300  1.000 46.42000  ? 185 PHE B C   1 
ATOM   4775  O  O   . PHE B  1 154 ? -8.62600  -49.59800 21.58000  1.000 47.87000  ? 185 PHE B O   1 
ATOM   4776  C  CB  . PHE B  1 154 ? -9.99200  -47.17200 20.93700  1.000 38.74000  ? 185 PHE B CB  1 
ATOM   4777  C  CG  . PHE B  1 154 ? -10.48200 -45.81200 20.62200  1.000 39.85000  ? 185 PHE B CG  1 
ATOM   4778  C  CD1 . PHE B  1 154 ? -10.34300 -44.78600 21.54200  1.000 36.90000  ? 185 PHE B CD1 1 
ATOM   4779  C  CD2 . PHE B  1 154 ? -11.09300 -45.54500 19.40700  1.000 40.19000  ? 185 PHE B CD2 1 
ATOM   4780  C  CE1 . PHE B  1 154 ? -10.80800 -43.50500 21.24900  1.000 43.12000  ? 185 PHE B CE1 1 
ATOM   4781  C  CE2 . PHE B  1 154 ? -11.56900 -44.28400 19.10800  1.000 34.35000  ? 185 PHE B CE2 1 
ATOM   4782  C  CZ  . PHE B  1 154 ? -11.44000 -43.26800 20.00600  1.000 39.28000  ? 185 PHE B CZ  1 
ATOM   4783  N  N   . PRO B  1 155 ? -7.09000  -48.33200 22.63800  1.000 46.66000  ? 186 PRO B N   1 
ATOM   4784  C  CA  . PRO B  1 155 ? -6.60300  -49.48100 23.43000  1.000 44.50000  ? 186 PRO B CA  1 
ATOM   4785  C  C   . PRO B  1 155 ? -7.69300  -50.18900 24.22000  1.000 45.39000  ? 186 PRO B C   1 
ATOM   4786  O  O   . PRO B  1 155 ? -7.66000  -51.42100 24.34600  1.000 47.32000  ? 186 PRO B O   1 
ATOM   4787  C  CB  . PRO B  1 155 ? -5.59000  -48.83400 24.37600  1.000 43.73000  ? 186 PRO B CB  1 
ATOM   4788  C  CG  . PRO B  1 155 ? -5.19300  -47.55900 23.70000  1.000 52.27000  ? 186 PRO B CG  1 
ATOM   4789  C  CD  . PRO B  1 155 ? -6.45500  -47.07100 23.05000  1.000 45.84000  ? 186 PRO B CD  1 
ATOM   4790  N  N   . SER B  1 156 ? -8.67800  -49.45200 24.73100  1.000 42.02000  ? 187 SER B N   1 
ATOM   4791  C  CA  . SER B  1 156 ? -9.79600  -50.10500 25.41300  1.000 49.34000  ? 187 SER B CA  1 
ATOM   4792  C  C   . SER B  1 156 ? -10.46500 -51.14700 24.52100  1.000 53.44000  ? 187 SER B C   1 
ATOM   4793  O  O   . SER B  1 156 ? -10.87000 -52.20900 24.99800  1.000 61.99000  ? 187 SER B O   1 
ATOM   4794  C  CB  . SER B  1 156 ? -10.79600 -49.05800 25.91000  1.000 46.92000  ? 187 SER B CB  1 
ATOM   4795  O  OG  . SER B  1 156 ? -11.06800 -48.11700 24.89000  1.000 61.42000  ? 187 SER B OG  1 
ATOM   4796  N  N   . GLU B  1 157 ? -10.57200 -50.87800 23.21900  1.000 50.84000  ? 188 GLU B N   1 
ATOM   4797  C  CA  . GLU B  1 157 ? -11.20100 -51.85400 22.33200  1.000 46.63000  ? 188 GLU B CA  1 
ATOM   4798  C  C   . GLU B  1 157 ? -10.21900 -52.93500 21.87900  1.000 51.21000  ? 188 GLU B C   1 
ATOM   4799  O  O   . GLU B  1 157 ? -10.53800 -54.12800 21.94000  1.000 47.73000  ? 188 GLU B O   1 
ATOM   4800  C  CB  . GLU B  1 157 ? -11.82100 -51.14300 21.12200  1.000 49.15000  ? 188 GLU B CB  1 
ATOM   4801  C  CG  . GLU B  1 157 ? -12.84100 -50.06900 21.50600  1.000 52.12000  ? 188 GLU B CG  1 
ATOM   4802  C  CD  . GLU B  1 157 ? -13.31800 -49.22500 20.32100  1.000 66.99000  ? 188 GLU B CD  1 
ATOM   4803  O  OE1 . GLU B  1 157 ? -12.71500 -49.33300 19.22600  1.000 57.27000  ? 188 GLU B OE1 1 
ATOM   4804  O  OE2 . GLU B  1 157 ? -14.30500 -48.46000 20.48900  1.000 65.21000  ? 188 GLU B OE2 1 
ATOM   4805  N  N   . TYR B  1 158 ? -9.00800  -52.55900 21.44300  1.000 45.52000  ? 189 TYR B N   1 
ATOM   4806  C  CA  . TYR B  1 158 ? -8.19000  -53.59800 20.82300  1.000 47.67000  ? 189 TYR B CA  1 
ATOM   4807  C  C   . TYR B  1 158 ? -7.47200  -54.48700 21.85100  1.000 49.42000  ? 189 TYR B C   1 
ATOM   4808  O  O   . TYR B  1 158 ? -7.11200  -55.62500 21.52900  1.000 47.82000  ? 189 TYR B O   1 
ATOM   4809  C  CB  . TYR B  1 158 ? -7.19000  -52.99300 19.81800  1.000 45.03000  ? 189 TYR B CB  1 
ATOM   4810  C  CG  . TYR B  1 158 ? -6.03100  -52.16600 20.36900  1.000 48.40000  ? 189 TYR B CG  1 
ATOM   4811  C  CD1 . TYR B  1 158 ? -4.97700  -52.76800 21.06300  1.000 45.28000  ? 189 TYR B CD1 1 
ATOM   4812  C  CD2 . TYR B  1 158 ? -5.95700  -50.79500 20.13300  1.000 44.86000  ? 189 TYR B CD2 1 
ATOM   4813  C  CE1 . TYR B  1 158 ? -3.89300  -52.01100 21.53600  1.000 42.71000  ? 189 TYR B CE1 1 
ATOM   4814  C  CE2 . TYR B  1 158 ? -4.89800  -50.04400 20.58700  1.000 42.86000  ? 189 TYR B CE2 1 
ATOM   4815  C  CZ  . TYR B  1 158 ? -3.86500  -50.64800 21.29000  1.000 48.11000  ? 189 TYR B CZ  1 
ATOM   4816  O  OH  . TYR B  1 158 ? -2.81700  -49.86800 21.74700  1.000 43.83000  ? 189 TYR B OH  1 
ATOM   4817  N  N   . GLN B  1 159 ? -7.21400  -53.99700 23.06200  1.000 48.41000  ? 190 GLN B N   1 
ATOM   4818  C  CA  . GLN B  1 159 ? -6.63800  -54.88000 24.07700  1.000 58.44000  ? 190 GLN B CA  1 
ATOM   4819  C  C   . GLN B  1 159 ? -7.63500  -55.96300 24.48000  1.000 53.83000  ? 190 GLN B C   1 
ATOM   4820  O  O   . GLN B  1 159 ? -7.28800  -57.14900 24.54900  1.000 59.03000  ? 190 GLN B O   1 
ATOM   4821  C  CB  . GLN B  1 159 ? -6.17600  -54.06000 25.28300  1.000 51.16000  ? 190 GLN B CB  1 
ATOM   4822  C  CG  . GLN B  1 159 ? -4.83800  -53.35800 25.07000  1.000 49.17000  ? 190 GLN B CG  1 
ATOM   4823  C  CD  . GLN B  1 159 ? -4.64700  -52.18300 26.02100  1.000 49.03000  ? 190 GLN B CD  1 
ATOM   4824  O  OE1 . GLN B  1 159 ? -5.56100  -51.81700 26.75800  1.000 53.62000  ? 190 GLN B OE1 1 
ATOM   4825  N  NE2 . GLN B  1 159 ? -3.47200  -51.56500 25.98100  1.000 51.38000  ? 190 GLN B NE2 1 
ATOM   4826  N  N   . LYS B  1 160 ? -8.89000  -55.57200 24.70500  1.000 55.14000  ? 191 LYS B N   1 
ATOM   4827  C  CA  . LYS B  1 160 ? -9.94100  -56.54600 24.99100  1.000 59.53000  ? 191 LYS B CA  1 
ATOM   4828  C  C   . LYS B  1 160 ? -10.03200 -57.59900 23.91600  1.000 56.28000  ? 191 LYS B C   1 
ATOM   4829  O  O   . LYS B  1 160 ? -10.10500 -58.79600 24.21000  1.000 64.01000  ? 191 LYS B O   1 
ATOM   4830  C  CB  . LYS B  1 160 ? -11.30200 -55.86400 25.13200  1.000 62.13000  ? 191 LYS B CB  1 
ATOM   4831  C  CG  . LYS B  1 160 ? -12.47100 -56.83500 25.00400  1.000 60.13000  ? 191 LYS B CG  1 
ATOM   4832  C  CD  . LYS B  1 160 ? -13.71100 -56.21900 25.60400  1.000 69.91000  ? 191 LYS B CD  1 
ATOM   4833  C  CE  . LYS B  1 160 ? -13.92100 -54.79900 25.10000  1.000 76.50000  ? 191 LYS B CE  1 
ATOM   4834  N  NZ  . LYS B  1 160 ? -15.05800 -54.15000 25.83700  1.000 85.63000  ? 191 LYS B NZ  1 
ATOM   4835  N  N   . THR B  1 161 ? -10.06000 -57.16400 22.65600  1.000 58.86000  ? 192 THR B N   1 
ATOM   4836  C  CA  . THR B  1 161 ? -10.14800 -58.11600 21.56100  1.000 53.82000  ? 192 THR B CA  1 
ATOM   4837  C  C   . THR B  1 161 ? -8.95900  -59.05200 21.58000  1.000 55.32000  ? 192 THR B C   1 
ATOM   4838  O  O   . THR B  1 161 ? -9.11400  -60.26300 21.39400  1.000 58.81000  ? 192 THR B O   1 
ATOM   4839  C  CB  . THR B  1 161 ? -10.22600 -57.38100 20.22600  1.000 51.20000  ? 192 THR B CB  1 
ATOM   4840  O  OG1 . THR B  1 161 ? -11.37600 -56.53100 20.22500  1.000 50.42000  ? 192 THR B OG1 1 
ATOM   4841  C  CG2 . THR B  1 161 ? -10.34000 -58.37100 19.09700  1.000 38.71000  ? 192 THR B CG2 1 
ATOM   4842  N  N   . TYR B  1 162 ? -7.76700  -58.51100 21.85900  1.000 53.60000  ? 193 TYR B N   1 
ATOM   4843  C  CA  . TYR B  1 162 ? -6.56200  -59.33100 21.85500  1.000 58.58000  ? 193 TYR B CA  1 
ATOM   4844  C  C   . TYR B  1 162 ? -6.62300  -60.39900 22.94300  1.000 61.84000  ? 193 TYR B C   1 
ATOM   4845  O  O   . TYR B  1 162 ? -6.32900  -61.57400 22.68500  1.000 63.13000  ? 193 TYR B O   1 
ATOM   4846  C  CB  . TYR B  1 162 ? -5.31600  -58.45800 22.03200  1.000 54.43000  ? 193 TYR B CB  1 
ATOM   4847  C  CG  . TYR B  1 162 ? -4.04000  -59.27600 22.02000  1.000 49.92000  ? 193 TYR B CG  1 
ATOM   4848  C  CD1 . TYR B  1 162 ? -3.58000  -59.82500 20.83900  1.000 47.76000  ? 193 TYR B CD1 1 
ATOM   4849  C  CD2 . TYR B  1 162 ? -3.28200  -59.48000 23.17700  1.000 57.39000  ? 193 TYR B CD2 1 
ATOM   4850  C  CE1 . TYR B  1 162 ? -2.42500  -60.57200 20.79400  1.000 49.60000  ? 193 TYR B CE1 1 
ATOM   4851  C  CE2 . TYR B  1 162 ? -2.10100  -60.22600 23.13000  1.000 47.47000  ? 193 TYR B CE2 1 
ATOM   4852  C  CZ  . TYR B  1 162 ? -1.68900  -60.77000 21.93400  1.000 48.54000  ? 193 TYR B CZ  1 
ATOM   4853  O  OH  . TYR B  1 162 ? -0.53500  -61.51900 21.84700  1.000 60.56000  ? 193 TYR B OH  1 
ATOM   4854  N  N   . LYS B  1 163 ? -7.03100  -60.01500 24.16200  1.000 59.21000  ? 194 LYS B N   1 
ATOM   4855  C  CA  . LYS B  1 163 ? -7.14500  -60.99600 25.24300  1.000 62.05000  ? 194 LYS B CA  1 
ATOM   4856  C  C   . LYS B  1 163 ? -8.18400  -62.04900 24.89300  1.000 65.87000  ? 194 LYS B C   1 
ATOM   4857  O  O   . LYS B  1 163 ? -7.90200  -63.25000 24.92300  1.000 68.59000  ? 194 LYS B O   1 
ATOM   4858  C  CB  . LYS B  1 163 ? -7.50900  -60.31000 26.55900  1.000 59.92000  ? 194 LYS B CB  1 
ATOM   4859  N  N   . ALA B  1 164 ? -9.37800  -61.60600 24.49500  1.000 65.84000  ? 195 ALA B N   1 
ATOM   4860  C  CA  . ALA B  1 164 ? -10.43200 -62.53700 24.11100  1.000 67.08000  ? 195 ALA B CA  1 
ATOM   4861  C  C   . ALA B  1 164 ? -9.94600  -63.51100 23.04900  1.000 68.14000  ? 195 ALA B C   1 
ATOM   4862  O  O   . ALA B  1 164 ? -10.22600 -64.71200 23.12100  1.000 74.10000  ? 195 ALA B O   1 
ATOM   4863  C  CB  . ALA B  1 164 ? -11.66000 -61.77200 23.61300  1.000 69.01000  ? 195 ALA B CB  1 
ATOM   4864  N  N   . GLN B  1 165 ? -9.22600  -63.01200 22.04400  1.000 70.07000  ? 196 GLN B N   1 
ATOM   4865  C  CA  . GLN B  1 165 ? -8.76400  -63.89600 20.98400  1.000 70.07000  ? 196 GLN B CA  1 
ATOM   4866  C  C   . GLN B  1 165 ? -7.70000  -64.85300 21.50900  1.000 69.84000  ? 196 GLN B C   1 
ATOM   4867  O  O   . GLN B  1 165 ? -7.53700  -65.95100 20.96700  1.000 76.63000  ? 196 GLN B O   1 
ATOM   4868  C  CB  . GLN B  1 165 ? -8.25500  -63.07700 19.79500  1.000 69.25000  ? 196 GLN B CB  1 
ATOM   4869  C  CG  . GLN B  1 165 ? -9.35500  -62.29400 19.08000  1.000 66.67000  ? 196 GLN B CG  1 
ATOM   4870  C  CD  . GLN B  1 165 ? -10.51000 -63.19100 18.66200  1.000 77.27000  ? 196 GLN B CD  1 
ATOM   4871  O  OE1 . GLN B  1 165 ? -10.29600 -64.21100 17.99800  1.000 74.54000  ? 196 GLN B OE1 1 
ATOM   4872  N  NE2 . GLN B  1 165 ? -11.74300 -62.83000 19.06700  1.000 67.97000  ? 196 GLN B NE2 1 
ATOM   4873  N  N   . LYS B  1 166 ? -6.95600  -64.45400 22.54100  1.000 68.69000  ? 197 LYS B N   1 
ATOM   4874  C  CA  . LYS B  1 166 ? -6.08800  -65.41300 23.21700  1.000 75.64000  ? 197 LYS B CA  1 
ATOM   4875  C  C   . LYS B  1 166 ? -6.92000  -66.41300 24.01900  1.000 75.39000  ? 197 LYS B C   1 
ATOM   4876  O  O   . LYS B  1 166 ? -6.57700  -67.60000 24.08200  1.000 75.96000  ? 197 LYS B O   1 
ATOM   4877  C  CB  . LYS B  1 166 ? -5.09400  -64.69400 24.12700  1.000 74.78000  ? 197 LYS B CB  1 
ATOM   4878  N  N   . LYS B  1 167 ? -8.04400  -65.95800 24.59200  1.000 75.34000  ? 198 LYS B N   1 
ATOM   4879  C  CA  . LYS B  1 167 ? -8.91400  -66.82400 25.38200  1.000 77.33000  ? 198 LYS B CA  1 
ATOM   4880  C  C   . LYS B  1 167 ? -9.54200  -67.92800 24.54900  1.000 76.85000  ? 198 LYS B C   1 
ATOM   4881  O  O   . LYS B  1 167 ? -10.04100 -68.90500 25.11300  1.000 80.35000  ? 198 LYS B O   1 
ATOM   4882  C  CB  . LYS B  1 167 ? -10.02400 -66.00400 26.04900  1.000 74.25000  ? 198 LYS B CB  1 
ATOM   4883  N  N   . ALA B  1 168 ? -9.58500  -67.77100 23.23200  1.000 76.58000  ? 199 ALA B N   1 
ATOM   4884  C  CA  . ALA B  1 168 ? -9.98800  -68.84600 22.34100  1.000 78.25000  ? 199 ALA B CA  1 
ATOM   4885  C  C   . ALA B  1 168 ? -8.79800  -69.52500 21.66000  1.000 83.01000  ? 199 ALA B C   1 
ATOM   4886  O  O   . ALA B  1 168 ? -9.00300  -70.30600 20.72400  1.000 88.04000  ? 199 ALA B O   1 
ATOM   4887  C  CB  . ALA B  1 168 ? -10.97500 -68.32500 21.30000  1.000 80.04000  ? 199 ALA B CB  1 
ATOM   4888  N  N   . GLY B  1 169 ? -7.57300  -69.24500 22.09700  1.000 80.00000  ? 200 GLY B N   1 
ATOM   4889  C  CA  . GLY B  1 169 ? -6.39900  -69.84300 21.45600  1.000 81.67000  ? 200 GLY B CA  1 
ATOM   4890  C  C   . GLY B  1 169 ? -6.32000  -69.61500 19.96000  1.000 82.62000  ? 200 GLY B C   1 
ATOM   4891  O  O   . GLY B  1 169 ? -5.87100  -70.50400 19.22300  1.000 87.34000  ? 200 GLY B O   1 
ATOM   4892  N  N   . ASN B  1 170 ? -6.73200  -68.43300 19.49300  1.000 79.67000  ? 201 ASN B N   1 
ATOM   4893  C  CA  . ASN B  1 170 ? -6.69900  -68.07200 18.07200  1.000 76.11000  ? 201 ASN B CA  1 
ATOM   4894  C  C   . ASN B  1 170 ? -5.27400  -68.10700 17.53300  1.000 67.17000  ? 201 ASN B C   1 
ATOM   4895  O  O   . ASN B  1 170 ? -4.42000  -67.34600 18.00800  1.000 69.82000  ? 201 ASN B O   1 
ATOM   4896  C  CB  . ASN B  1 170 ? -7.29600  -66.67300 17.88800  1.000 73.00000  ? 201 ASN B CB  1 
ATOM   4897  C  CG  . ASN B  1 170 ? -7.43800  -66.25600 16.41900  1.000 67.30000  ? 201 ASN B CG  1 
ATOM   4898  O  OD1 . ASN B  1 170 ? -6.77100  -66.77000 15.51100  1.000 57.32000  ? 201 ASN B OD1 1 
ATOM   4899  N  ND2 . ASN B  1 170 ? -8.29500  -65.27200 16.19700  1.000 70.87000  ? 201 ASN B ND2 1 
ATOM   4900  N  N   . PRO B  1 171 ? -4.97900  -68.94000 16.53200  1.000 71.77000  ? 202 PRO B N   1 
ATOM   4901  C  CA  . PRO B  1 171 ? -3.60000  -69.03400 16.03400  1.000 70.43000  ? 202 PRO B CA  1 
ATOM   4902  C  C   . PRO B  1 171 ? -3.22400  -67.97400 15.00600  1.000 71.29000  ? 202 PRO B C   1 
ATOM   4903  O  O   . PRO B  1 171 ? -2.04100  -67.89300 14.64600  1.000 73.58000  ? 202 PRO B O   1 
ATOM   4904  C  CB  . PRO B  1 171 ? -3.56600  -70.43100 15.40500  1.000 67.88000  ? 202 PRO B CB  1 
ATOM   4905  C  CG  . PRO B  1 171 ? -4.97000  -70.62400 14.90000  1.000 66.27000  ? 202 PRO B CG  1 
ATOM   4906  C  CD  . PRO B  1 171 ? -5.89500  -69.84000 15.80800  1.000 68.61000  ? 202 PRO B CD  1 
ATOM   4907  N  N   . ASN B  1 172 ? -4.17700  -67.16400 14.52500  1.000 65.79000  ? 203 ASN B N   1 
ATOM   4908  C  CA  . ASN B  1 172 ? -3.91100  -66.12100 13.53100  1.000 60.92000  ? 203 ASN B CA  1 
ATOM   4909  C  C   . ASN B  1 172 ? -4.58400  -64.82500 13.96400  1.000 59.75000  ? 203 ASN B C   1 
ATOM   4910  O  O   . ASN B  1 172 ? -5.48100  -64.29500 13.31100  1.000 63.66000  ? 203 ASN B O   1 
ATOM   4911  C  CB  . ASN B  1 172 ? -4.35300  -66.49900 12.12000  1.000 56.56000  ? 203 ASN B CB  1 
ATOM   4912  C  CG  . ASN B  1 172 ? -3.76300  -67.80800 11.65800  1.000 66.30000  ? 203 ASN B CG  1 
ATOM   4913  O  OD1 . ASN B  1 172 ? -4.33300  -68.87000 11.88200  1.000 72.67000  ? 203 ASN B OD1 1 
ATOM   4914  N  ND2 . ASN B  1 172 ? -2.60500  -67.73800 11.00800  1.000 66.06000  ? 203 ASN B ND2 1 
ATOM   4915  N  N   . ILE B  1 173 ? -4.13300  -64.30700 15.09900  1.000 58.63000  ? 204 ILE B N   1 
ATOM   4916  C  CA  . ILE B  1 173 ? -4.60000  -63.00900 15.55000  1.000 62.03000  ? 204 ILE B CA  1 
ATOM   4917  C  C   . ILE B  1 173 ? -4.03800  -61.92700 14.63700  1.000 62.15000  ? 204 ILE B C   1 
ATOM   4918  O  O   . ILE B  1 173 ? -2.86800  -61.98100 14.22400  1.000 58.38000  ? 204 ILE B O   1 
ATOM   4919  C  CB  . ILE B  1 173 ? -4.20400  -62.78800 17.01500  1.000 52.41000  ? 204 ILE B CB  1 
ATOM   4920  C  CG1 . ILE B  1 173 ? -4.75500  -63.95200 17.83900  1.000 59.44000  ? 204 ILE B CG1 1 
ATOM   4921  C  CG2 . ILE B  1 173 ? -4.73600  -61.45500 17.51700  1.000 52.36000  ? 204 ILE B CG2 1 
ATOM   4922  C  CD1 . ILE B  1 173 ? -4.79500  -63.70500 19.31500  1.000 61.84000  ? 204 ILE B CD1 1 
ATOM   4923  N  N   . ARG B  1 174 ? -4.89600  -60.97500 14.26500  1.000 52.81000  ? 205 ARG B N   1 
ATOM   4924  C  CA  . ARG B  1 174 ? -4.49800  -59.89500 13.37300  1.000 53.65000  ? 205 ARG B CA  1 
ATOM   4925  C  C   . ARG B  1 174 ? -3.52900  -58.95400 14.07200  1.000 45.79000  ? 205 ARG B C   1 
ATOM   4926  O  O   . ARG B  1 174 ? -3.74700  -58.55400 15.22000  1.000 45.71000  ? 205 ARG B O   1 
ATOM   4927  C  CB  . ARG B  1 174 ? -5.72200  -59.09700 12.91300  1.000 50.88000  ? 205 ARG B CB  1 
ATOM   4928  C  CG  . ARG B  1 174 ? -6.78100  -59.88600 12.22100  1.000 53.54000  ? 205 ARG B CG  1 
ATOM   4929  C  CD  . ARG B  1 174 ? -7.83900  -58.95300 11.64100  1.000 60.81000  ? 205 ARG B CD  1 
ATOM   4930  N  NE  . ARG B  1 174 ? -8.40300  -58.03200 12.62700  1.000 62.19000  ? 205 ARG B NE  1 
ATOM   4931  C  CZ  . ARG B  1 174 ? -8.46500  -56.71400 12.46900  1.000 65.37000  ? 205 ARG B CZ  1 
ATOM   4932  N  NH1 . ARG B  1 174 ? -7.94900  -56.11900 11.40000  1.000 58.01000  ? 205 ARG B NH1 1 
ATOM   4933  N  NH2 . ARG B  1 174 ? -9.08000  -55.97500 13.39400  1.000 64.23000  ? 205 ARG B NH2 1 
ATOM   4934  N  N   . ASP B  1 175 ? -2.47700  -58.55600 13.35800  1.000 46.12000  ? 206 ASP B N   1 
ATOM   4935  C  CA  . ASP B  1 175 ? -1.52600  -57.65300 13.99000  1.000 43.41000  ? 206 ASP B CA  1 
ATOM   4936  C  C   . ASP B  1 175 ? -2.12200  -56.27100 14.26500  1.000 47.20000  ? 206 ASP B C   1 
ATOM   4937  O  O   . ASP B  1 175 ? -1.56500  -55.53300 15.09100  1.000 47.11000  ? 206 ASP B O   1 
ATOM   4938  C  CB  . ASP B  1 175 ? -0.26400  -57.54600 13.13300  1.000 46.79000  ? 206 ASP B CB  1 
ATOM   4939  C  CG  . ASP B  1 175 ? -0.54800  -57.14000 11.68900  1.000 48.20000  ? 206 ASP B CG  1 
ATOM   4940  O  OD1 . ASP B  1 175 ? -1.68100  -56.71600 11.35800  1.000 44.93000  ? 206 ASP B OD1 1 
ATOM   4941  O  OD2 . ASP B  1 175 ? 0.39600   -57.25200 10.87800  1.000 51.38000  ? 206 ASP B OD2 1 
ATOM   4942  N  N   . TYR B  1 176 ? -3.27200  -55.93400 13.66500  1.000 36.61000  ? 207 TYR B N   1 
ATOM   4943  C  CA  . TYR B  1 176 ? -3.94400  -54.68300 13.99400  1.000 38.79000  ? 207 TYR B CA  1 
ATOM   4944  C  C   . TYR B  1 176 ? -4.39000  -54.61300 15.44600  1.000 40.98000  ? 207 TYR B C   1 
ATOM   4945  O  O   . TYR B  1 176 ? -4.66900  -53.51700 15.94800  1.000 40.13000  ? 207 TYR B O   1 
ATOM   4946  C  CB  . TYR B  1 176 ? -5.17000  -54.48500 13.07500  1.000 44.76000  ? 207 TYR B CB  1 
ATOM   4947  C  CG  . TYR B  1 176 ? -4.85600  -53.77200 11.77000  1.000 46.53000  ? 207 TYR B CG  1 
ATOM   4948  C  CD1 . TYR B  1 176 ? -3.82400  -54.22500 10.93300  1.000 43.57000  ? 207 TYR B CD1 1 
ATOM   4949  C  CD2 . TYR B  1 176 ? -5.58200  -52.64700 11.37700  1.000 38.62000  ? 207 TYR B CD2 1 
ATOM   4950  C  CE1 . TYR B  1 176 ? -3.53400  -53.59400 9.74500   1.000 42.83000  ? 207 TYR B CE1 1 
ATOM   4951  C  CE2 . TYR B  1 176 ? -5.29800  -51.99700 10.18100  1.000 47.18000  ? 207 TYR B CE2 1 
ATOM   4952  C  CZ  . TYR B  1 176 ? -4.27400  -52.47600 9.37300   1.000 46.33000  ? 207 TYR B CZ  1 
ATOM   4953  O  OH  . TYR B  1 176 ? -3.97900  -51.83400 8.20500   1.000 40.26000  ? 207 TYR B OH  1 
ATOM   4954  N  N   . VAL B  1 177 ? -4.43500  -55.73600 16.15600  1.000 40.34000  ? 208 VAL B N   1 
ATOM   4955  C  CA  . VAL B  1 177 ? -4.84500  -55.69900 17.55400  1.000 44.41000  ? 208 VAL B CA  1 
ATOM   4956  C  C   . VAL B  1 177 ? -3.72000  -56.10500 18.50900  1.000 45.54000  ? 208 VAL B C   1 
ATOM   4957  O  O   . VAL B  1 177 ? -3.94600  -56.09400 19.72200  1.000 43.61000  ? 208 VAL B O   1 
ATOM   4958  C  CB  . VAL B  1 177 ? -6.10400  -56.56100 17.80400  1.000 48.70000  ? 208 VAL B CB  1 
ATOM   4959  C  CG1 . VAL B  1 177 ? -7.28600  -56.11800 16.89900  1.000 42.69000  ? 208 VAL B CG1 1 
ATOM   4960  C  CG2 . VAL B  1 177 ? -5.80400  -58.05000 17.63700  1.000 41.09000  ? 208 VAL B CG2 1 
ATOM   4961  N  N   . PHE B  1 178 ? -2.51200  -56.41600 18.00700  1.000 45.38000  ? 209 PHE B N   1 
ATOM   4962  C  CA  . PHE B  1 178 ? -1.36900  -56.73400 18.87800  1.000 47.04000  ? 209 PHE B CA  1 
ATOM   4963  C  C   . PHE B  1 178 ? -1.08000  -55.60100 19.85200  1.000 47.70000  ? 209 PHE B C   1 
ATOM   4964  O  O   . PHE B  1 178 ? -1.28200  -54.43200 19.53200  1.000 48.92000  ? 209 PHE B O   1 
ATOM   4965  C  CB  . PHE B  1 178 ? -0.07400  -56.96400 18.10600  1.000 37.93000  ? 209 PHE B CB  1 
ATOM   4966  C  CG  . PHE B  1 178 ? 0.00800   -58.26200 17.38600  1.000 46.57000  ? 209 PHE B CG  1 
ATOM   4967  C  CD1 . PHE B  1 178 ? -1.02700  -59.18900 17.43200  1.000 46.92000  ? 209 PHE B CD1 1 
ATOM   4968  C  CD2 . PHE B  1 178 ? 1.12800   -58.54900 16.62200  1.000 42.91000  ? 209 PHE B CD2 1 
ATOM   4969  C  CE1 . PHE B  1 178 ? -0.91800  -60.38700 16.73700  1.000 46.61000  ? 209 PHE B CE1 1 
ATOM   4970  C  CE2 . PHE B  1 178 ? 1.23800   -59.73100 15.92300  1.000 41.89000  ? 209 PHE B CE2 1 
ATOM   4971  C  CZ  . PHE B  1 178 ? 0.23300   -60.66100 15.99100  1.000 44.66000  ? 209 PHE B CZ  1 
ATOM   4972  N  N   . PRO B  1 179 ? -0.60200  -55.92800 21.04900  1.000 50.79000  ? 210 PRO B N   1 
ATOM   4973  C  CA  . PRO B  1 179 ? -0.03600  -54.89400 21.92300  1.000 54.53000  ? 210 PRO B CA  1 
ATOM   4974  C  C   . PRO B  1 179 ? 1.10700   -54.16600 21.22300  1.000 49.04000  ? 210 PRO B C   1 
ATOM   4975  O  O   . PRO B  1 179 ? 1.87100   -54.76300 20.46600  1.000 46.44000  ? 210 PRO B O   1 
ATOM   4976  C  CB  . PRO B  1 179 ? 0.47600   -55.68800 23.13500  1.000 44.48000  ? 210 PRO B CB  1 
ATOM   4977  C  CG  . PRO B  1 179 ? -0.29300  -56.94800 23.13100  1.000 56.10000  ? 210 PRO B CG  1 
ATOM   4978  C  CD  . PRO B  1 179 ? -0.58900  -57.25800 21.67000  1.000 54.31000  ? 210 PRO B CD  1 
ATOM   4979  N  N   . MET B  1 180 ? 1.17500   -52.85300 21.43700  1.000 48.84000  ? 211 MET B N   1 
ATOM   4980  C  CA  . MET B  1 180 ? 2.30100   -52.07000 20.96400  1.000 48.88000  ? 211 MET B CA  1 
ATOM   4981  C  C   . MET B  1 180 ? 3.49100   -52.21400 21.92400  1.000 53.86000  ? 211 MET B C   1 
ATOM   4982  O  O   . MET B  1 180 ? 3.37100   -52.70900 23.05300  1.000 56.59000  ? 211 MET B O   1 
ATOM   4983  C  CB  . MET B  1 180 ? 1.89400   -50.60100 20.78500  1.000 47.16000  ? 211 MET B CB  1 
ATOM   4984  C  CG  . MET B  1 180 ? 0.71700   -50.39000 19.79000  1.000 47.48000  ? 211 MET B CG  1 
ATOM   4985  S  SD  . MET B  1 180 ? 0.51400   -48.68600 19.14900  1.000 47.30000  ? 211 MET B SD  1 
ATOM   4986  C  CE  . MET B  1 180 ? 0.17700   -47.69000 20.60000  1.000 35.59000  ? 211 MET B CE  1 
ATOM   4987  N  N   . GLU B  1 181 ? 4.64500   -51.71600 21.49600  1.000 48.93000  ? 212 GLU B N   1 
ATOM   4988  C  CA  . GLU B  1 181 ? 5.88000   -51.92700 22.23100  1.000 55.19000  ? 212 GLU B CA  1 
ATOM   4989  C  C   . GLU B  1 181 ? 6.66300   -50.63600 22.39800  1.000 57.71000  ? 212 GLU B C   1 
ATOM   4990  O  O   . GLU B  1 181 ? 6.55200   -49.70200 21.59700  1.000 54.42000  ? 212 GLU B O   1 
ATOM   4991  C  CB  . GLU B  1 181 ? 6.77700   -52.94600 21.53000  1.000 48.95000  ? 212 GLU B CB  1 
ATOM   4992  C  CG  . GLU B  1 181 ? 7.26100   -52.45700 20.19900  1.000 51.30000  ? 212 GLU B CG  1 
ATOM   4993  C  CD  . GLU B  1 181 ? 8.41600   -53.25200 19.68400  1.000 55.29000  ? 212 GLU B CD  1 
ATOM   4994  O  OE1 . GLU B  1 181 ? 9.55900   -52.93200 20.07000  1.000 53.22000  ? 212 GLU B OE1 1 
ATOM   4995  O  OE2 . GLU B  1 181 ? 8.18100   -54.19000 18.89400  1.000 57.55000  ? 212 GLU B OE2 1 
ATOM   4996  N  N   . HIS B  1 182 ? 7.48300   -50.62300 23.45000  1.000 52.70000  ? 213 HIS B N   1 
ATOM   4997  C  CA  . HIS B  1 182 ? 8.46500   -49.57900 23.73000  1.000 44.57000  ? 213 HIS B CA  1 
ATOM   4998  C  C   . HIS B  1 182 ? 9.81500   -50.27200 23.86400  1.000 49.75000  ? 213 HIS B C   1 
ATOM   4999  O  O   . HIS B  1 182 ? 10.12400  -50.84800 24.90800  1.000 60.40000  ? 213 HIS B O   1 
ATOM   5000  C  CB  . HIS B  1 182 ? 8.12600   -48.79300 24.98200  1.000 47.85000  ? 213 HIS B CB  1 
ATOM   5001  C  CG  . HIS B  1 182 ? 9.07300   -47.66400 25.25000  1.000 53.47000  ? 213 HIS B CG  1 
ATOM   5002  N  ND1 . HIS B  1 182 ? 9.22000   -47.09200 26.49500  1.000 53.51000  ? 213 HIS B ND1 1 
ATOM   5003  C  CD2 . HIS B  1 182 ? 9.93200   -47.00700 24.43400  1.000 52.38000  ? 213 HIS B CD2 1 
ATOM   5004  C  CE1 . HIS B  1 182 ? 10.12200  -46.12600 26.43200  1.000 52.17000  ? 213 HIS B CE1 1 
ATOM   5005  N  NE2 . HIS B  1 182 ? 10.56700  -46.05300 25.19200  1.000 49.45000  ? 213 HIS B NE2 1 
ATOM   5006  N  N   . ASN B  1 183 ? 10.59100  -50.25800 22.78500  1.000 51.40000  ? 214 ASN B N   1 
ATOM   5007  C  CA  . ASN B  1 183 ? 11.91400  -50.87000 22.74400  1.000 52.06000  ? 214 ASN B CA  1 
ATOM   5008  C  C   . ASN B  1 183 ? 11.84800  -52.35100 23.10800  1.000 55.35000  ? 214 ASN B C   1 
ATOM   5009  O  O   . ASN B  1 183 ? 12.70700  -52.87400 23.81300  1.000 54.86000  ? 214 ASN B O   1 
ATOM   5010  C  CB  . ASN B  1 183 ? 12.88800  -50.12000 23.66200  1.000 50.68000  ? 214 ASN B CB  1 
ATOM   5011  C  CG  . ASN B  1 183 ? 13.14200  -48.68400 23.19800  1.000 50.92000  ? 214 ASN B CG  1 
ATOM   5012  O  OD1 . ASN B  1 183 ? 13.33800  -48.42300 22.01700  1.000 52.60000  ? 214 ASN B OD1 1 
ATOM   5013  N  ND2 . ASN B  1 183 ? 13.14700  -47.75800 24.13500  1.000 53.14000  ? 214 ASN B ND2 1 
ATOM   5014  N  N   . GLY B  1 184 ? 10.83300  -53.04600 22.59600  1.000 56.92000  ? 215 GLY B N   1 
ATOM   5015  C  CA  . GLY B  1 184 ? 10.69900  -54.47100 22.81300  1.000 54.18000  ? 215 GLY B CA  1 
ATOM   5016  C  C   . GLY B  1 184 ? 9.83400   -54.89400 23.98200  1.000 53.98000  ? 215 GLY B C   1 
ATOM   5017  O  O   . GLY B  1 184 ? 9.52500   -56.08200 24.09200  1.000 60.35000  ? 215 GLY B O   1 
ATOM   5018  N  N   . LYS B  1 185 ? 9.46400   -53.98400 24.87000  1.000 56.27000  ? 216 LYS B N   1 
ATOM   5019  C  CA  . LYS B  1 185 ? 8.62500   -54.24800 26.02400  1.000 50.72000  ? 216 LYS B CA  1 
ATOM   5020  C  C   . LYS B  1 185 ? 7.19100   -53.77100 25.79000  1.000 58.73000  ? 216 LYS B C   1 
ATOM   5021  O  O   . LYS B  1 185 ? 6.93900   -52.89800 24.95500  1.000 56.61000  ? 216 LYS B O   1 
ATOM   5022  C  CB  . LYS B  1 185 ? 9.22300   -53.55500 27.25100  1.000 56.57000  ? 216 LYS B CB  1 
ATOM   5023  C  CG  . LYS B  1 185 ? 10.68900  -53.94200 27.52700  1.000 59.89000  ? 216 LYS B CG  1 
ATOM   5024  C  CD  . LYS B  1 185 ? 11.16200  -53.36800 28.86500  1.000 71.29000  ? 216 LYS B CD  1 
ATOM   5025  C  CE  . LYS B  1 185 ? 12.53100  -53.93400 29.32800  1.000 78.97000  ? 216 LYS B CE  1 
ATOM   5026  N  NZ  . LYS B  1 185 ? 12.49200  -55.34700 29.83400  1.000 69.96000  ? 216 LYS B NZ  1 
ATOM   5027  N  N   . PRO B  1 186 ? 6.21700   -54.32600 26.51000  1.000 58.38000  ? 217 PRO B N   1 
ATOM   5028  C  CA  . PRO B  1 186 ? 4.82000   -53.91700 26.29600  1.000 57.53000  ? 217 PRO B CA  1 
ATOM   5029  C  C   . PRO B  1 186 ? 4.64100   -52.41600 26.48700  1.000 55.01000  ? 217 PRO B C   1 
ATOM   5030  O  O   . PRO B  1 186 ? 5.13000   -51.83500 27.45300  1.000 50.26000  ? 217 PRO B O   1 
ATOM   5031  C  CB  . PRO B  1 186 ? 4.05300   -54.71200 27.36100  1.000 55.79000  ? 217 PRO B CB  1 
ATOM   5032  C  CG  . PRO B  1 186 ? 4.91100   -55.94200 27.59400  1.000 54.55000  ? 217 PRO B CG  1 
ATOM   5033  C  CD  . PRO B  1 186 ? 6.33200   -55.47600 27.43400  1.000 55.62000  ? 217 PRO B CD  1 
ATOM   5034  N  N   . ALA B  1 187 ? 3.91900   -51.78200 25.55400  1.000 57.16000  ? 218 ALA B N   1 
ATOM   5035  C  CA  . ALA B  1 187 ? 3.73800   -50.33800 25.66200  1.000 48.85000  ? 218 ALA B CA  1 
ATOM   5036  C  C   . ALA B  1 187 ? 2.69200   -49.94900 26.69500  1.000 51.53000  ? 218 ALA B C   1 
ATOM   5037  O  O   . ALA B  1 187 ? 2.80700   -48.86700 27.28600  1.000 48.63000  ? 218 ALA B O   1 
ATOM   5038  C  CB  . ALA B  1 187 ? 3.36500   -49.74700 24.30200  1.000 52.81000  ? 218 ALA B CB  1 
ATOM   5039  N  N   . ASN B  1 188 ? 1.68400   -50.80500 26.92300  1.000 45.30000  ? 219 ASN B N   1 
ATOM   5040  C  CA  . ASN B  1 188 ? 0.57100   -50.51700 27.83500  1.000 45.44000  ? 219 ASN B CA  1 
ATOM   5041  C  C   . ASN B  1 188 ? -0.02600  -49.14200 27.53700  1.000 49.47000  ? 219 ASN B C   1 
ATOM   5042  O  O   . ASN B  1 188 ? -0.20300  -48.30000 28.42500  1.000 50.27000  ? 219 ASN B O   1 
ATOM   5043  C  CB  . ASN B  1 188 ? 0.99900   -50.60200 29.30700  1.000 46.29000  ? 219 ASN B CB  1 
ATOM   5044  C  CG  . ASN B  1 188 ? 1.49800   -51.97600 29.69100  1.000 49.39000  ? 219 ASN B CG  1 
ATOM   5045  O  OD1 . ASN B  1 188 ? 2.65400   -52.13400 30.08900  1.000 51.59000  ? 219 ASN B OD1 1 
ATOM   5046  N  ND2 . ASN B  1 188 ? 0.64700   -52.98400 29.53700  1.000 46.27000  ? 219 ASN B ND2 1 
ATOM   5047  N  N   . GLU B  1 189 ? -0.35100  -48.92100 26.26800  1.000 49.48000  ? 220 GLU B N   1 
ATOM   5048  C  CA  . GLU B  1 189 ? -0.96300  -47.66000 25.87600  1.000 51.21000  ? 220 GLU B CA  1 
ATOM   5049  C  C   . GLU B  1 189 ? -2.35100  -47.55500 26.50200  1.000 50.13000  ? 220 GLU B C   1 
ATOM   5050  O  O   . GLU B  1 189 ? -3.06900  -48.55300 26.63900  1.000 44.34000  ? 220 GLU B O   1 
ATOM   5051  C  CB  . GLU B  1 189 ? -1.05000  -47.55900 24.34400  1.000 53.50000  ? 220 GLU B CB  1 
ATOM   5052  C  CG  . GLU B  1 189 ? -1.70100  -46.28500 23.82000  1.000 50.54000  ? 220 GLU B CG  1 
ATOM   5053  C  CD  . GLU B  1 189 ? -1.02700  -45.00500 24.29500  1.000 50.64000  ? 220 GLU B CD  1 
ATOM   5054  O  OE1 . GLU B  1 189 ? 0.13300   -44.76500 23.91500  1.000 53.57000  ? 220 GLU B OE1 1 
ATOM   5055  O  OE2 . GLU B  1 189 ? -1.65000  -44.24300 25.07000  1.000 56.34000  ? 220 GLU B OE2 1 
ATOM   5056  N  N   . THR B  1 190 ? -2.72900  -46.33900 26.89100  1.000 47.36000  ? 221 THR B N   1 
ATOM   5057  C  CA  . THR B  1 190 ? -4.03500  -46.13200 27.48400  1.000 52.19000  ? 221 THR B CA  1 
ATOM   5058  C  C   . THR B  1 190 ? -4.88500  -45.09000 26.76800  1.000 56.20000  ? 221 THR B C   1 
ATOM   5059  O  O   . THR B  1 190 ? -6.03300  -44.86700 27.16500  1.000 57.35000  ? 221 THR B O   1 
ATOM   5060  C  CB  . THR B  1 190 ? -3.86700  -45.73100 28.94800  1.000 55.73000  ? 221 THR B CB  1 
ATOM   5061  O  OG1 . THR B  1 190 ? -3.08800  -44.52800 29.00600  1.000 57.47000  ? 221 THR B OG1 1 
ATOM   5062  C  CG2 . THR B  1 190 ? -3.14000  -46.83200 29.70900  1.000 58.22000  ? 221 THR B CG2 1 
ATOM   5063  N  N   . GLU B  1 191 ? -4.41200  -44.48900 25.69500  1.000 52.64000  ? 222 GLU B N   1 
ATOM   5064  C  CA  . GLU B  1 191 ? -5.25300  -43.49800 25.05100  1.000 52.76000  ? 222 GLU B CA  1 
ATOM   5065  C  C   . GLU B  1 191 ? -5.24600  -43.72700 23.55100  1.000 51.48000  ? 222 GLU B C   1 
ATOM   5066  O  O   . GLU B  1 191 ? -4.39200  -44.44300 23.01500  1.000 49.61000  ? 222 GLU B O   1 
ATOM   5067  C  CB  . GLU B  1 191 ? -4.82500  -42.06400 25.41400  1.000 51.61000  ? 222 GLU B CB  1 
ATOM   5068  C  CG  . GLU B  1 191 ? -3.45100  -41.65400 25.01400  1.000 51.25000  ? 222 GLU B CG  1 
ATOM   5069  C  CD  . GLU B  1 191 ? -3.09100  -40.27800 25.55000  1.000 55.27000  ? 222 GLU B CD  1 
ATOM   5070  O  OE1 . GLU B  1 191 ? -4.01800  -39.51900 25.89900  1.000 55.78000  ? 222 GLU B OE1 1 
ATOM   5071  O  OE2 . GLU B  1 191 ? -1.88000  -39.96000 25.64400  1.000 57.70000  ? 222 GLU B OE2 1 
ATOM   5072  N  N   . TYR B  1 192 ? -6.26200  -43.15700 22.90100  1.000 45.15000  ? 223 TYR B N   1 
ATOM   5073  C  CA  . TYR B  1 192 ? -6.32400  -43.02200 21.45300  1.000 41.85000  ? 223 TYR B CA  1 
ATOM   5074  C  C   . TYR B  1 192 ? -4.91600  -42.86500 20.88400  1.000 43.20000  ? 223 TYR B C   1 
ATOM   5075  O  O   . TYR B  1 192 ? -4.23300  -41.89900 21.24000  1.000 38.69000  ? 223 TYR B O   1 
ATOM   5076  C  CB  . TYR B  1 192 ? -7.15800  -41.79400 21.11200  1.000 44.69000  ? 223 TYR B CB  1 
ATOM   5077  C  CG  . TYR B  1 192 ? -7.48600  -41.60000 19.65700  1.000 42.39000  ? 223 TYR B CG  1 
ATOM   5078  C  CD1 . TYR B  1 192 ? -8.24200  -42.53800 18.95300  1.000 39.77000  ? 223 TYR B CD1 1 
ATOM   5079  C  CD2 . TYR B  1 192 ? -7.03100  -40.47900 18.98200  1.000 40.67000  ? 223 TYR B CD2 1 
ATOM   5080  C  CE1 . TYR B  1 192 ? -8.55400  -42.34400 17.60100  1.000 38.66000  ? 223 TYR B CE1 1 
ATOM   5081  C  CE2 . TYR B  1 192 ? -7.34300  -40.28000 17.64500  1.000 41.96000  ? 223 TYR B CE2 1 
ATOM   5082  C  CZ  . TYR B  1 192 ? -8.08900  -41.21700 16.96100  1.000 35.14000  ? 223 TYR B CZ  1 
ATOM   5083  O  OH  . TYR B  1 192 ? -8.38500  -40.99600 15.63700  1.000 40.63000  ? 223 TYR B OH  1 
ATOM   5084  N  N   . ILE B  1 193 ? -4.46200  -43.81000 20.04100  1.000 38.35000  ? 224 ILE B N   1 
ATOM   5085  C  CA  . ILE B  1 193 ? -3.02100  -43.93800 19.79200  1.000 41.56000  ? 224 ILE B CA  1 
ATOM   5086  C  C   . ILE B  1 193 ? -2.43800  -42.70500 19.09900  1.000 45.35000  ? 224 ILE B C   1 
ATOM   5087  O  O   . ILE B  1 193 ? -1.24400  -42.40400 19.27200  1.000 44.90000  ? 224 ILE B O   1 
ATOM   5088  C  CB  . ILE B  1 193 ? -2.67700  -45.22300 19.00000  1.000 39.91000  ? 224 ILE B CB  1 
ATOM   5089  C  CG1 . ILE B  1 193 ? -3.18900  -45.20000 17.57600  1.000 38.21000  ? 224 ILE B CG1 1 
ATOM   5090  C  CG2 . ILE B  1 193 ? -3.16700  -46.49100 19.71000  1.000 41.93000  ? 224 ILE B CG2 1 
ATOM   5091  C  CD1 . ILE B  1 193 ? -2.81000  -46.50000 16.86100  1.000 37.38000  ? 224 ILE B CD1 1 
ATOM   5092  N  N   . THR B  1 194 ? -3.24900  -41.96200 18.33600  1.000 36.77000  ? 225 THR B N   1 
ATOM   5093  C  CA  . THR B  1 194 ? -2.76500  -40.69600 17.79400  1.000 41.81000  ? 225 THR B CA  1 
ATOM   5094  C  C   . THR B  1 194 ? -2.31700  -39.77600 18.91900  1.000 44.59000  ? 225 THR B C   1 
ATOM   5095  O  O   . THR B  1 194 ? -1.23200  -39.18100 18.86200  1.000 40.54000  ? 225 THR B O   1 
ATOM   5096  C  CB  . THR B  1 194 ? -3.85000  -40.02800 16.93700  1.000 35.88000  ? 225 THR B CB  1 
ATOM   5097  O  OG1 . THR B  1 194 ? -4.11600  -40.84500 15.79900  1.000 40.15000  ? 225 THR B OG1 1 
ATOM   5098  C  CG2 . THR B  1 194 ? -3.38000  -38.68900 16.43700  1.000 36.63000  ? 225 THR B CG2 1 
ATOM   5099  N  N   . ASP B  1 195 ? -3.12200  -39.69500 19.98200  1.000 43.30000  ? 226 ASP B N   1 
ATOM   5100  C  CA  . ASP B  1 195 ? -2.73400  -38.90400 21.14400  1.000 45.07000  ? 226 ASP B CA  1 
ATOM   5101  C  C   . ASP B  1 195 ? -1.49700  -39.48600 21.82600  1.000 43.14000  ? 226 ASP B C   1 
ATOM   5102  O  O   . ASP B  1 195 ? -0.63000  -38.74200 22.31000  1.000 45.62000  ? 226 ASP B O   1 
ATOM   5103  C  CB  . ASP B  1 195 ? -3.90200  -38.83300 22.12200  1.000 46.42000  ? 226 ASP B CB  1 
ATOM   5104  C  CG  . ASP B  1 195 ? -5.07300  -37.98800 21.60400  1.000 47.35000  ? 226 ASP B CG  1 
ATOM   5105  O  OD1 . ASP B  1 195 ? -4.89500  -37.15400 20.69500  1.000 45.66000  ? 226 ASP B OD1 1 
ATOM   5106  O  OD2 . ASP B  1 195 ? -6.19400  -38.19100 22.10000  1.000 49.01000  ? 226 ASP B OD2 1 
ATOM   5107  N  N   . GLY B  1 196 ? -1.38800  -40.81300 21.86800  1.000 41.88000  ? 227 GLY B N   1 
ATOM   5108  C  CA  . GLY B  1 196 ? -0.21200  -41.41500 22.46900  1.000 44.86000  ? 227 GLY B CA  1 
ATOM   5109  C  C   . GLY B  1 196 ? 1.06000   -41.12800 21.69300  1.000 43.24000  ? 227 GLY B C   1 
ATOM   5110  O  O   . GLY B  1 196 ? 2.10400   -40.83000 22.28500  1.000 44.33000  ? 227 GLY B O   1 
ATOM   5111  N  N   . PHE B  1 197 ? 0.98800   -41.18600 20.35500  1.000 43.27000  ? 228 PHE B N   1 
ATOM   5112  C  CA  . PHE B  1 197 ? 2.18200   -40.92100 19.55900  1.000 41.92000  ? 228 PHE B CA  1 
ATOM   5113  C  C   . PHE B  1 197 ? 2.61500   -39.47200 19.73200  1.000 35.07000  ? 228 PHE B C   1 
ATOM   5114  O  O   . PHE B  1 197 ? 3.80800   -39.18300 19.86900  1.000 41.29000  ? 228 PHE B O   1 
ATOM   5115  C  CB  . PHE B  1 197 ? 1.92300   -41.25200 18.08800  1.000 37.65000  ? 228 PHE B CB  1 
ATOM   5116  C  CG  . PHE B  1 197 ? 1.60700   -42.72000 17.83400  1.000 34.16000  ? 228 PHE B CG  1 
ATOM   5117  C  CD1 . PHE B  1 197 ? 2.15600   -43.71200 18.61700  1.000 40.27000  ? 228 PHE B CD1 1 
ATOM   5118  C  CD2 . PHE B  1 197 ? 0.76300   -43.08700 16.80100  1.000 36.61000  ? 228 PHE B CD2 1 
ATOM   5119  C  CE1 . PHE B  1 197 ? 1.88400   -45.04300 18.38700  1.000 36.70000  ? 228 PHE B CE1 1 
ATOM   5120  C  CE2 . PHE B  1 197 ? 0.47000   -44.42100 16.56800  1.000 44.03000  ? 228 PHE B CE2 1 
ATOM   5121  C  CZ  . PHE B  1 197 ? 1.04500   -45.40400 17.37000  1.000 45.08000  ? 228 PHE B CZ  1 
ATOM   5122  N  N   . SER B  1 198 ? 1.65400   -38.56100 19.82000  1.000 37.05000  ? 229 SER B N   1 
ATOM   5123  C  CA  . SER B  1 198 ? 1.98500   -37.17700 20.13200  1.000 37.40000  ? 229 SER B CA  1 
ATOM   5124  C  C   . SER B  1 198 ? 2.63700   -37.09200 21.51500  1.000 42.50000  ? 229 SER B C   1 
ATOM   5125  O  O   . SER B  1 198 ? 3.64700   -36.40200 21.69700  1.000 37.86000  ? 229 SER B O   1 
ATOM   5126  C  CB  . SER B  1 198 ? 0.72600   -36.30900 20.08500  1.000 35.52000  ? 229 SER B CB  1 
ATOM   5127  O  OG  . SER B  1 198 ? -0.03200  -36.43900 18.87500  1.000 36.18000  ? 229 SER B OG  1 
ATOM   5128  N  N   . ARG B  1 199 ? 2.07900   -37.80800 22.49500  1.000 40.79000  ? 230 ARG B N   1 
ATOM   5129  C  CA  . ARG B  1 199 ? 2.63900   -37.79500 23.84400  1.000 45.49000  ? 230 ARG B CA  1 
ATOM   5130  C  C   . ARG B  1 199 ? 4.08100   -38.29800 23.83600  1.000 38.61000  ? 230 ARG B C   1 
ATOM   5131  O  O   . ARG B  1 199 ? 4.95400   -37.68900 24.45200  1.000 37.16000  ? 230 ARG B O   1 
ATOM   5132  C  CB  . ARG B  1 199 ? 1.77400   -38.65300 24.77600  1.000 40.92000  ? 230 ARG B CB  1 
ATOM   5133  C  CG  . ARG B  1 199 ? 2.31600   -38.82500 26.19900  1.000 40.24000  ? 230 ARG B CG  1 
ATOM   5134  C  CD  . ARG B  1 199 ? 1.70100   -40.03400 26.91400  1.000 39.58000  ? 230 ARG B CD  1 
ATOM   5135  N  NE  . ARG B  1 199 ? 2.12700   -41.29000 26.30300  1.000 43.40000  ? 230 ARG B NE  1 
ATOM   5136  C  CZ  . ARG B  1 199 ? 1.31500   -42.25500 25.88400  1.000 52.57000  ? 230 ARG B CZ  1 
ATOM   5137  N  NH1 . ARG B  1 199 ? -0.00900  -42.14500 25.97700  1.000 52.12000  ? 230 ARG B NH1 1 
ATOM   5138  N  NH2 . ARG B  1 199 ? 1.84100   -43.33900 25.30700  1.000 46.93000  ? 230 ARG B NH2 1 
ATOM   5139  N  N   . GLU B  1 200 ? 4.36200   -39.36100 23.07400  1.000 40.45000  ? 231 GLU B N   1 
ATOM   5140  C  CA  . GLU B  1 200 ? 5.72900   -39.88600 22.99400  1.000 38.25000  ? 231 GLU B CA  1 
ATOM   5141  C  C   . GLU B  1 200 ? 6.66800   -38.95700 22.22900  1.000 43.21000  ? 231 GLU B C   1 
ATOM   5142  O  O   . GLU B  1 200 ? 7.88000   -38.95900 22.47800  1.000 43.27000  ? 231 GLU B O   1 
ATOM   5143  C  CB  . GLU B  1 200 ? 5.73700   -41.26700 22.34600  1.000 39.61000  ? 231 GLU B CB  1 
ATOM   5144  C  CG  . GLU B  1 200 ? 5.10100   -42.34100 23.18700  1.000 47.73000  ? 231 GLU B CG  1 
ATOM   5145  C  CD  . GLU B  1 200 ? 5.74600   -42.44400 24.56200  1.000 51.95000  ? 231 GLU B CD  1 
ATOM   5146  O  OE1 . GLU B  1 200 ? 6.99900   -42.46500 24.62800  1.000 48.94000  ? 231 GLU B OE1 1 
ATOM   5147  O  OE2 . GLU B  1 200 ? 4.99900   -42.52100 25.56800  1.000 53.53000  ? 231 GLU B OE2 1 
ATOM   5148  N  N   . ALA B  1 201 ? 6.16200   -38.22300 21.23600  1.000 41.49000  ? 232 ALA B N   1 
ATOM   5149  C  CA  . ALA B  1 201 ? 7.03300   -37.26900 20.56300  1.000 42.12000  ? 232 ALA B CA  1 
ATOM   5150  C  C   . ALA B  1 201 ? 7.49500   -36.18800 21.52200  1.000 43.04000  ? 232 ALA B C   1 
ATOM   5151  O  O   . ALA B  1 201 ? 8.67900   -35.81500 21.53200  1.000 40.57000  ? 232 ALA B O   1 
ATOM   5152  C  CB  . ALA B  1 201 ? 6.32000   -36.64300 19.36900  1.000 43.82000  ? 232 ALA B CB  1 
ATOM   5153  N  N   . ILE B  1 202 ? 6.57000   -35.69300 22.34700  1.000 42.86000  ? 233 ILE B N   1 
ATOM   5154  C  CA  . ILE B  1 202 ? 6.87800   -34.65900 23.33200  1.000 41.05000  ? 233 ILE B CA  1 
ATOM   5155  C  C   . ILE B  1 202 ? 7.89000   -35.17000 24.34300  1.000 44.09000  ? 233 ILE B C   1 
ATOM   5156  O  O   . ILE B  1 202 ? 8.84700   -34.46900 24.69700  1.000 42.45000  ? 233 ILE B O   1 
ATOM   5157  C  CB  . ILE B  1 202 ? 5.58400   -34.17400 24.00800  1.000 41.50000  ? 233 ILE B CB  1 
ATOM   5158  C  CG1 . ILE B  1 202 ? 4.77800   -33.33900 23.00200  1.000 40.51000  ? 233 ILE B CG1 1 
ATOM   5159  C  CG2 . ILE B  1 202 ? 5.90800   -33.36400 25.27100  1.000 39.64000  ? 233 ILE B CG2 1 
ATOM   5160  C  CD1 . ILE B  1 202 ? 3.36900   -33.16500 23.36700  1.000 39.03000  ? 233 ILE B CD1 1 
ATOM   5161  N  N   . LYS B  1 203 ? 7.71200   -36.40900 24.79900  1.000 38.84000  ? 234 LYS B N   1 
ATOM   5162  C  CA  . LYS B  1 203 ? 8.64300   -36.97900 25.75800  1.000 45.71000  ? 234 LYS B CA  1 
ATOM   5163  C  C   . LYS B  1 203 ? 10.04900  -37.04900 25.17300  1.000 44.47000  ? 234 LYS B C   1 
ATOM   5164  O  O   . LYS B  1 203 ? 11.00800  -36.57900 25.79100  1.000 48.85000  ? 234 LYS B O   1 
ATOM   5165  C  CB  . LYS B  1 203 ? 8.15300   -38.36800 26.16600  1.000 44.83000  ? 234 LYS B CB  1 
ATOM   5166  C  CG  . LYS B  1 203 ? 9.06000   -39.09200 27.11700  1.000 44.56000  ? 234 LYS B CG  1 
ATOM   5167  C  CD  . LYS B  1 203 ? 8.47200   -40.44200 27.55100  1.000 48.86000  ? 234 LYS B CD  1 
ATOM   5168  C  CE  . LYS B  1 203 ? 9.42500   -41.14900 28.49900  1.000 51.87000  ? 234 LYS B CE  1 
ATOM   5169  N  NZ  . LYS B  1 203 ? 8.98200   -42.50000 28.95900  1.000 56.64000  ? 234 LYS B NZ  1 
ATOM   5170  N  N   . ASN B  1 204 ? 10.17500  -37.54500 23.93800  1.000 42.31000  ? 235 ASN B N   1 
ATOM   5171  C  CA  . ASN B  1 204 ? 11.49000  -37.68200 23.32300  1.000 44.60000  ? 235 ASN B CA  1 
ATOM   5172  C  C   . ASN B  1 204 ? 12.12500  -36.33200 23.01100  1.000 40.84000  ? 235 ASN B C   1 
ATOM   5173  O  O   . ASN B  1 204 ? 13.35600  -36.21900 23.01900  1.000 44.76000  ? 235 ASN B O   1 
ATOM   5174  C  CB  . ASN B  1 204 ? 11.40200  -38.51900 22.04900  1.000 38.15000  ? 235 ASN B CB  1 
ATOM   5175  C  CG  . ASN B  1 204 ? 11.31200  -40.00400 22.33800  1.000 44.82000  ? 235 ASN B CG  1 
ATOM   5176  O  OD1 . ASN B  1 204 ? 12.32300  -40.66300 22.49900  1.000 51.18000  ? 235 ASN B OD1 1 
ATOM   5177  N  ND2 . ASN B  1 204 ? 10.09600  -40.54000 22.39200  1.000 42.21000  ? 235 ASN B ND2 1 
ATOM   5178  N  N   . ILE B  1 205 ? 11.32800  -35.30400 22.74000  1.000 40.32000  ? 236 ILE B N   1 
ATOM   5179  C  CA  . ILE B  1 205 ? 11.90000  -33.96800 22.58600  1.000 43.50000  ? 236 ILE B CA  1 
ATOM   5180  C  C   . ILE B  1 205 ? 12.46300  -33.48800 23.91700  1.000 44.56000  ? 236 ILE B C   1 
ATOM   5181  O  O   . ILE B  1 205 ? 13.51200  -32.83300 23.96500  1.000 43.50000  ? 236 ILE B O   1 
ATOM   5182  C  CB  . ILE B  1 205 ? 10.86000  -32.96600 22.03900  1.000 42.55000  ? 236 ILE B CB  1 
ATOM   5183  C  CG1 . ILE B  1 205 ? 10.55200  -33.23800 20.57200  1.000 42.08000  ? 236 ILE B CG1 1 
ATOM   5184  C  CG2 . ILE B  1 205 ? 11.38000  -31.53300 22.18400  1.000 44.08000  ? 236 ILE B CG2 1 
ATOM   5185  C  CD1 . ILE B  1 205 ? 9.32000   -32.49500 20.05500  1.000 45.87000  ? 236 ILE B CD1 1 
ATOM   5186  N  N   . LYS B  1 206 ? 11.75800  -33.78000 25.01900  1.000 45.35000  ? 237 LYS B N   1 
ATOM   5187  C  CA  . LYS B  1 206 ? 12.25100  -33.36700 26.33200  1.000 45.32000  ? 237 LYS B CA  1 
ATOM   5188  C  C   . LYS B  1 206 ? 13.51000  -34.13200 26.72600  1.000 43.22000  ? 237 LYS B C   1 
ATOM   5189  O  O   . LYS B  1 206 ? 14.41300  -33.54700 27.32800  1.000 39.39000  ? 237 LYS B O   1 
ATOM   5190  C  CB  . LYS B  1 206 ? 11.16100  -33.54400 27.38100  1.000 38.49000  ? 237 LYS B CB  1 
ATOM   5191  C  CG  . LYS B  1 206 ? 10.05300  -32.53800 27.25200  1.000 43.64000  ? 237 LYS B CG  1 
ATOM   5192  C  CD  . LYS B  1 206 ? 8.88700   -32.97200 28.09200  1.000 44.59000  ? 237 LYS B CD  1 
ATOM   5193  C  CE  . LYS B  1 206 ? 7.91400   -31.86500 28.35800  1.000 51.20000  ? 237 LYS B CE  1 
ATOM   5194  N  NZ  . LYS B  1 206 ? 6.63800   -32.40700 28.91900  1.000 67.36000  ? 237 LYS B NZ  1 
ATOM   5195  N  N   . ILE B  1 207 ? 13.60600  -35.40900 26.33400  1.000 41.02000  ? 238 ILE B N   1 
ATOM   5196  C  CA  . ILE B  1 207 ? 14.79200  -36.21100 26.61700  1.000 39.83000  ? 238 ILE B CA  1 
ATOM   5197  C  C   . ILE B  1 207 ? 16.00700  -35.64100 25.88800  1.000 42.13000  ? 238 ILE B C   1 
ATOM   5198  O  O   . ILE B  1 207 ? 17.04800  -35.37300 26.49600  1.000 46.11000  ? 238 ILE B O   1 
ATOM   5199  C  CB  . ILE B  1 207 ? 14.54500  -37.68600 26.24500  1.000 42.64000  ? 238 ILE B CB  1 
ATOM   5200  C  CG1 . ILE B  1 207 ? 13.49900  -38.31800 27.17200  1.000 46.06000  ? 238 ILE B CG1 1 
ATOM   5201  C  CG2 . ILE B  1 207 ? 15.84300  -38.50700 26.35100  1.000 39.73000  ? 238 ILE B CG2 1 
ATOM   5202  C  CD1 . ILE B  1 207 ? 13.00700  -39.69600 26.70200  1.000 41.76000  ? 238 ILE B CD1 1 
ATOM   5203  N  N   . ALA B  1 208 ? 15.88700  -35.43700 24.57500  1.000 45.85000  ? 239 ALA B N   1 
ATOM   5204  C  CA  . ALA B  1 208 ? 17.00000  -34.88200 23.80600  1.000 45.03000  ? 239 ALA B CA  1 
ATOM   5205  C  C   . ALA B  1 208 ? 17.40600  -33.50200 24.31300  1.000 42.86000  ? 239 ALA B C   1 
ATOM   5206  O  O   . ALA B  1 208 ? 18.59700  -33.18100 24.36400  1.000 49.30000  ? 239 ALA B O   1 
ATOM   5207  C  CB  . ALA B  1 208 ? 16.63300  -34.81200 22.32500  1.000 47.13000  ? 239 ALA B CB  1 
ATOM   5208  N  N   . ALA B  1 209 ? 16.43400  -32.67700 24.69900  1.000 39.56000  ? 240 ALA B N   1 
ATOM   5209  C  CA  . ALA B  1 209 ? 16.74000  -31.36800 25.27200  1.000 42.19000  ? 240 ALA B CA  1 
ATOM   5210  C  C   . ALA B  1 209 ? 17.52100  -31.50300 26.57300  1.000 45.72000  ? 240 ALA B C   1 
ATOM   5211  O  O   . ALA B  1 209 ? 18.44400  -30.72500 26.83700  1.000 39.68000  ? 240 ALA B O   1 
ATOM   5212  C  CB  . ALA B  1 209 ? 15.45400  -30.57900 25.53700  1.000 41.87000  ? 240 ALA B CB  1 
ATOM   5213  N  N   . ALA B  1 210 ? 17.11800  -32.44000 27.42800  1.000 42.63000  ? 241 ALA B N   1 
ATOM   5214  C  CA  . ALA B  1 210 ? 17.83800  -32.61300 28.67400  1.000 46.52000  ? 241 ALA B CA  1 
ATOM   5215  C  C   . ALA B  1 210 ? 19.24600  -33.12600 28.40800  1.000 48.09000  ? 241 ALA B C   1 
ATOM   5216  O  O   . ALA B  1 210 ? 20.16500  -32.83600 29.17700  1.000 47.09000  ? 241 ALA B O   1 
ATOM   5217  C  CB  . ALA B  1 210 ? 17.06400  -33.55200 29.60100  1.000 44.00000  ? 241 ALA B CB  1 
ATOM   5218  N  N   . LYS B  1 211 ? 19.42200  -33.91600 27.34600  1.000 46.77000  ? 242 LYS B N   1 
ATOM   5219  C  CA  . LYS B  1 211 ? 20.73700  -34.41600 26.96900  1.000 45.61000  ? 242 LYS B CA  1 
ATOM   5220  C  C   . LYS B  1 211 ? 21.58400  -33.38300 26.23500  1.000 45.64000  ? 242 LYS B C   1 
ATOM   5221  O  O   . LYS B  1 211 ? 22.75600  -33.65700 25.95600  1.000 54.07000  ? 242 LYS B O   1 
ATOM   5222  C  CB  . LYS B  1 211 ? 20.58800  -35.66800 26.09800  1.000 49.08000  ? 242 LYS B CB  1 
ATOM   5223  C  CG  . LYS B  1 211 ? 19.91500  -36.82700 26.79300  1.000 50.77000  ? 242 LYS B CG  1 
ATOM   5224  C  CD  . LYS B  1 211 ? 19.71600  -38.00100 25.86800  1.000 43.95000  ? 242 LYS B CD  1 
ATOM   5225  C  CE  . LYS B  1 211 ? 20.97200  -38.87300 25.83300  1.000 55.58000  ? 242 LYS B CE  1 
ATOM   5226  N  NZ  . LYS B  1 211 ? 20.88300  -40.09900 26.70200  1.000 64.06000  ? 242 LYS B NZ  1 
ATOM   5227  N  N   . LYS B  1 212 ? 21.02600  -32.21800 25.90900  1.000 46.35000  ? 243 LYS B N   1 
ATOM   5228  C  CA  . LYS B  1 212 ? 21.69100  -31.23200 25.05200  1.000 51.08000  ? 243 LYS B CA  1 
ATOM   5229  C  C   . LYS B  1 212 ? 22.31200  -31.90100 23.81200  1.000 45.48000  ? 243 LYS B C   1 
ATOM   5230  O  O   . LYS B  1 212 ? 23.45900  -31.65400 23.44000  1.000 54.88000  ? 243 LYS B O   1 
ATOM   5231  C  CB  . LYS B  1 212 ? 22.72700  -30.43500 25.85300  1.000 51.27000  ? 243 LYS B CB  1 
ATOM   5232  N  N   . GLN B  1 213 ? 21.51700  -32.73800 23.15600  1.000 44.79000  ? 244 GLN B N   1 
ATOM   5233  C  CA  . GLN B  1 213 ? 21.86700  -33.52400 21.98200  1.000 50.61000  ? 244 GLN B CA  1 
ATOM   5234  C  C   . GLN B  1 213 ? 20.86900  -33.24300 20.86400  1.000 48.73000  ? 244 GLN B C   1 
ATOM   5235  O  O   . GLN B  1 213 ? 19.65800  -33.25300 21.10600  1.000 47.90000  ? 244 GLN B O   1 
ATOM   5236  C  CB  . GLN B  1 213 ? 21.83400  -35.02100 22.31700  1.000 45.52000  ? 244 GLN B CB  1 
ATOM   5237  C  CG  . GLN B  1 213 ? 22.52300  -35.92400 21.33600  1.000 36.31000  ? 244 GLN B CG  1 
ATOM   5238  C  CD  . GLN B  1 213 ? 22.43000  -37.36100 21.78700  1.000 45.61000  ? 244 GLN B CD  1 
ATOM   5239  O  OE1 . GLN B  1 213 ? 21.86400  -37.65400 22.84900  1.000 42.26000  ? 244 GLN B OE1 1 
ATOM   5240  N  NE2 . GLN B  1 213 ? 22.94800  -38.27500 20.97200  1.000 43.02000  ? 244 GLN B NE2 1 
ATOM   5241  N  N   . PRO B  1 214 ? 21.32600  -33.05500 19.62400  1.000 51.16000  ? 245 PRO B N   1 
ATOM   5242  C  CA  . PRO B  1 214 ? 20.37100  -32.89300 18.51800  1.000 43.72000  ? 245 PRO B CA  1 
ATOM   5243  C  C   . PRO B  1 214 ? 19.55100  -34.15500 18.32500  1.000 46.64000  ? 245 PRO B C   1 
ATOM   5244  O  O   . PRO B  1 214 ? 20.05600  -35.26800 18.48400  1.000 43.40000  ? 245 PRO B O   1 
ATOM   5245  C  CB  . PRO B  1 214 ? 21.26800  -32.61600 17.30600  1.000 49.05000  ? 245 PRO B CB  1 
ATOM   5246  C  CG  . PRO B  1 214 ? 22.63600  -33.20200 17.69100  1.000 49.99000  ? 245 PRO B CG  1 
ATOM   5247  C  CD  . PRO B  1 214 ? 22.73200  -32.96100 19.17200  1.000 42.88000  ? 245 PRO B CD  1 
ATOM   5248  N  N   . PHE B  1 215 ? 18.25900  -33.97100 18.03500  1.000 41.33000  ? 246 PHE B N   1 
ATOM   5249  C  CA  . PHE B  1 215 ? 17.37200  -35.10700 17.85500  1.000 41.68000  ? 246 PHE B CA  1 
ATOM   5250  C  C   . PHE B  1 215 ? 16.99500  -35.29800 16.39100  1.000 42.59000  ? 246 PHE B C   1 
ATOM   5251  O  O   . PHE B  1 215 ? 16.94100  -34.35300 15.59500  1.000 38.05000  ? 246 PHE B O   1 
ATOM   5252  C  CB  . PHE B  1 215 ? 16.10500  -34.99500 18.73200  1.000 41.03000  ? 246 PHE B CB  1 
ATOM   5253  C  CG  . PHE B  1 215 ? 15.11300  -33.90100 18.33000  1.000 41.52000  ? 246 PHE B CG  1 
ATOM   5254  C  CD1 . PHE B  1 215 ? 14.29700  -34.03700 17.20800  1.000 35.99000  ? 246 PHE B CD1 1 
ATOM   5255  C  CD2 . PHE B  1 215 ? 14.94700  -32.78100 19.13300  1.000 38.13000  ? 246 PHE B CD2 1 
ATOM   5256  C  CE1 . PHE B  1 215 ? 13.37500  -33.05400 16.86900  1.000 37.13000  ? 246 PHE B CE1 1 
ATOM   5257  C  CE2 . PHE B  1 215 ? 14.03700  -31.79800 18.80700  1.000 41.12000  ? 246 PHE B CE2 1 
ATOM   5258  C  CZ  . PHE B  1 215 ? 13.24200  -31.92900 17.67500  1.000 39.30000  ? 246 PHE B CZ  1 
ATOM   5259  N  N   . PHE B  1 216 ? 16.71400  -36.55000 16.06400  1.000 42.93000  ? 247 PHE B N   1 
ATOM   5260  C  CA  . PHE B  1 216 ? 16.04000  -36.93400 14.83600  1.000 37.78000  ? 247 PHE B CA  1 
ATOM   5261  C  C   . PHE B  1 216 ? 14.84400  -37.77800 15.24800  1.000 38.85000  ? 247 PHE B C   1 
ATOM   5262  O  O   . PHE B  1 216 ? 15.02900  -38.85100 15.82200  1.000 36.78000  ? 247 PHE B O   1 
ATOM   5263  C  CB  . PHE B  1 216 ? 16.95900  -37.72100 13.91600  1.000 33.31000  ? 247 PHE B CB  1 
ATOM   5264  C  CG  . PHE B  1 216 ? 16.23900  -38.38300 12.78300  1.000 39.61000  ? 247 PHE B CG  1 
ATOM   5265  C  CD1 . PHE B  1 216 ? 15.69300  -37.62200 11.75900  1.000 39.45000  ? 247 PHE B CD1 1 
ATOM   5266  C  CD2 . PHE B  1 216 ? 16.07400  -39.76100 12.75500  1.000 35.96000  ? 247 PHE B CD2 1 
ATOM   5267  C  CE1 . PHE B  1 216 ? 15.00000  -38.23800 10.68300  1.000 39.82000  ? 247 PHE B CE1 1 
ATOM   5268  C  CE2 . PHE B  1 216 ? 15.41000  -40.39400 11.69400  1.000 37.28000  ? 247 PHE B CE2 1 
ATOM   5269  C  CZ  . PHE B  1 216 ? 14.85600  -39.62800 10.65500  1.000 36.65000  ? 247 PHE B CZ  1 
ATOM   5270  N  N   . ILE B  1 217 ? 13.63000  -37.27000 15.03200  1.000 40.54000  ? 248 ILE B N   1 
ATOM   5271  C  CA  . ILE B  1 217 ? 12.39800  -37.98500 15.37900  1.000 39.55000  ? 248 ILE B CA  1 
ATOM   5272  C  C   . ILE B  1 217 ? 11.59600  -38.31300 14.11500  1.000 39.19000  ? 248 ILE B C   1 
ATOM   5273  O  O   . ILE B  1 217 ? 11.21900  -37.42100 13.34100  1.000 36.11000  ? 248 ILE B O   1 
ATOM   5274  C  CB  . ILE B  1 217 ? 11.55400  -37.20400 16.39300  1.000 40.16000  ? 248 ILE B CB  1 
ATOM   5275  C  CG1 . ILE B  1 217 ? 12.34300  -37.02100 17.70200  1.000 44.40000  ? 248 ILE B CG1 1 
ATOM   5276  C  CG2 . ILE B  1 217 ? 10.24100  -37.93400 16.65100  1.000 38.56000  ? 248 ILE B CG2 1 
ATOM   5277  C  CD1 . ILE B  1 217 ? 11.66500  -36.11200 18.70500  1.000 43.54000  ? 248 ILE B CD1 1 
ATOM   5278  N  N   . TYR B  1 218 ? 11.32100  -39.59900 13.92600  1.000 40.68000  ? 249 TYR B N   1 
ATOM   5279  C  CA  . TYR B  1 218 ? 10.51700  -40.12100 12.82100  1.000 34.57000  ? 249 TYR B CA  1 
ATOM   5280  C  C   . TYR B  1 218 ? 9.13000   -40.40500 13.38800  1.000 37.78000  ? 249 TYR B C   1 
ATOM   5281  O  O   . TYR B  1 218 ? 8.87600   -41.46500 13.95700  1.000 40.55000  ? 249 TYR B O   1 
ATOM   5282  C  CB  . TYR B  1 218 ? 11.20100  -41.36000 12.26100  1.000 34.46000  ? 249 TYR B CB  1 
ATOM   5283  C  CG  . TYR B  1 218 ? 10.54300  -42.07800 11.13200  1.000 36.68000  ? 249 TYR B CG  1 
ATOM   5284  C  CD1 . TYR B  1 218 ? 10.53000  -41.54500 9.83900   1.000 40.06000  ? 249 TYR B CD1 1 
ATOM   5285  C  CD2 . TYR B  1 218 ? 10.00800  -43.33400 11.32400  1.000 34.19000  ? 249 TYR B CD2 1 
ATOM   5286  C  CE1 . TYR B  1 218 ? 9.94200   -42.24000 8.78100   1.000 41.10000  ? 249 TYR B CE1 1 
ATOM   5287  C  CE2 . TYR B  1 218 ? 9.41600   -44.03000 10.28200  1.000 36.22000  ? 249 TYR B CE2 1 
ATOM   5288  C  CZ  . TYR B  1 218 ? 9.38900   -43.48100 9.01600   1.000 40.17000  ? 249 TYR B CZ  1 
ATOM   5289  O  OH  . TYR B  1 218 ? 8.80600   -44.18600 7.99300   1.000 39.92000  ? 249 TYR B OH  1 
ATOM   5290  N  N   . LEU B  1 219 ? 8.23600   -39.43000 13.27500  1.000 36.04000  ? 250 LEU B N   1 
ATOM   5291  C  CA  . LEU B  1 219 ? 6.89800   -39.53100 13.86800  1.000 36.63000  ? 250 LEU B CA  1 
ATOM   5292  C  C   . LEU B  1 219 ? 5.94700   -40.01700 12.78000  1.000 34.34000  ? 250 LEU B C   1 
ATOM   5293  O  O   . LEU B  1 219 ? 5.38700   -39.22000 12.03200  1.000 37.74000  ? 250 LEU B O   1 
ATOM   5294  C  CB  . LEU B  1 219 ? 6.46200   -38.18700 14.44900  1.000 31.29000  ? 250 LEU B CB  1 
ATOM   5295  C  CG  . LEU B  1 219 ? 5.02600   -38.05600 14.98200  1.000 34.34000  ? 250 LEU B CG  1 
ATOM   5296  C  CD1 . LEU B  1 219 ? 4.64700   -39.18500 15.93200  1.000 36.95000  ? 250 LEU B CD1 1 
ATOM   5297  C  CD2 . LEU B  1 219 ? 4.91100   -36.72000 15.66300  1.000 38.34000  ? 250 LEU B CD2 1 
ATOM   5298  N  N   . ALA B  1 220 ? 5.74800   -41.34200 12.71700  1.000 36.27000  ? 251 ALA B N   1 
ATOM   5299  C  CA  . ALA B  1 220 ? 4.99300   -42.00100 11.65400  1.000 37.12000  ? 251 ALA B CA  1 
ATOM   5300  C  C   . ALA B  1 220 ? 3.57800   -42.33400 12.14000  1.000 38.03000  ? 251 ALA B C   1 
ATOM   5301  O  O   . ALA B  1 220 ? 3.23900   -43.48700 12.41700  1.000 35.94000  ? 251 ALA B O   1 
ATOM   5302  C  CB  . ALA B  1 220 ? 5.73000   -43.26200 11.19700  1.000 32.15000  ? 251 ALA B CB  1 
ATOM   5303  N  N   . TYR B  1 221 ? 2.73400   -41.30800 12.21300  1.000 33.84000  ? 252 TYR B N   1 
ATOM   5304  C  CA  . TYR B  1 221 ? 1.31700   -41.52100 12.52100  1.000 41.08000  ? 252 TYR B CA  1 
ATOM   5305  C  C   . TYR B  1 221 ? 0.68200   -42.54000 11.58200  1.000 36.53000  ? 252 TYR B C   1 
ATOM   5306  O  O   . TYR B  1 221 ? 0.86400   -42.48000 10.36300  1.000 33.22000  ? 252 TYR B O   1 
ATOM   5307  C  CB  . TYR B  1 221 ? 0.53300   -40.21600 12.39500  1.000 33.52000  ? 252 TYR B CB  1 
ATOM   5308  C  CG  . TYR B  1 221 ? 0.80600   -39.16800 13.45600  1.000 41.39000  ? 252 TYR B CG  1 
ATOM   5309  C  CD1 . TYR B  1 221 ? 0.34100   -39.33000 14.75700  1.000 35.31000  ? 252 TYR B CD1 1 
ATOM   5310  C  CD2 . TYR B  1 221 ? 1.47800   -37.99300 13.13600  1.000 34.84000  ? 252 TYR B CD2 1 
ATOM   5311  C  CE1 . TYR B  1 221 ? 0.53200   -38.36300 15.70100  1.000 39.51000  ? 252 TYR B CE1 1 
ATOM   5312  C  CE2 . TYR B  1 221 ? 1.70000   -37.01000 14.09300  1.000 37.44000  ? 252 TYR B CE2 1 
ATOM   5313  C  CZ  . TYR B  1 221 ? 1.21800   -37.19900 15.37600  1.000 39.91000  ? 252 TYR B CZ  1 
ATOM   5314  O  OH  . TYR B  1 221 ? 1.41100   -36.23200 16.34200  1.000 36.67000  ? 252 TYR B OH  1 
ATOM   5315  N  N   . ASN B  1 222 ? -0.14900  -43.42700 12.14100  1.000 34.90000  ? 253 ASN B N   1 
ATOM   5316  C  CA  . ASN B  1 222 ? -0.94400  -44.25400 11.23700  1.000 40.02000  ? 253 ASN B CA  1 
ATOM   5317  C  C   . ASN B  1 222 ? -2.20600  -43.52700 10.76700  1.000 36.46000  ? 253 ASN B C   1 
ATOM   5318  O  O   . ASN B  1 222 ? -2.78400  -43.90800 9.75200   1.000 40.56000  ? 253 ASN B O   1 
ATOM   5319  C  CB  . ASN B  1 222 ? -1.28400  -45.60700 11.88300  1.000 36.20000  ? 253 ASN B CB  1 
ATOM   5320  C  CG  . ASN B  1 222 ? -2.16500  -45.48400 13.13300  1.000 37.56000  ? 253 ASN B CG  1 
ATOM   5321  O  OD1 . ASN B  1 222 ? -1.97400  -44.59900 13.96800  1.000 35.72000  ? 253 ASN B OD1 1 
ATOM   5322  N  ND2 . ASN B  1 222 ? -3.14400  -46.38400 13.25500  1.000 38.80000  ? 253 ASN B ND2 1 
ATOM   5323  N  N   . ALA B  1 223 ? -2.60700  -42.45500 11.43300  1.000 33.47000  ? 254 ALA B N   1 
ATOM   5324  C  CA  . ALA B  1 223 ? -3.73300  -41.66700 10.95200  1.000 39.79000  ? 254 ALA B CA  1 
ATOM   5325  C  C   . ALA B  1 223 ? -3.37400  -40.94500 9.64800   1.000 41.95000  ? 254 ALA B C   1 
ATOM   5326  O  O   . ALA B  1 223 ? -2.22000  -40.55100 9.44400   1.000 36.63000  ? 254 ALA B O   1 
ATOM   5327  C  CB  . ALA B  1 223 ? -4.15700  -40.65100 12.00700  1.000 30.82000  ? 254 ALA B CB  1 
ATOM   5328  N  N   . PRO B  1 224 ? -4.35300  -40.73800 8.74900   1.000 35.81000  ? 255 PRO B N   1 
ATOM   5329  C  CA  . PRO B  1 224 ? -5.76200  -41.18100 8.78700   1.000 34.74000  ? 255 PRO B CA  1 
ATOM   5330  C  C   . PRO B  1 224 ? -6.05100  -42.50100 8.05100   1.000 32.68000  ? 255 PRO B C   1 
ATOM   5331  O  O   . PRO B  1 224 ? -7.09100  -42.66500 7.38300   1.000 39.01000  ? 255 PRO B O   1 
ATOM   5332  C  CB  . PRO B  1 224 ? -6.48700  -40.00700 8.10900   1.000 33.65000  ? 255 PRO B CB  1 
ATOM   5333  C  CG  . PRO B  1 224 ? -5.51200  -39.54800 7.05500   1.000 36.72000  ? 255 PRO B CG  1 
ATOM   5334  C  CD  . PRO B  1 224 ? -4.10900  -39.81700 7.61900   1.000 31.54000  ? 255 PRO B CD  1 
ATOM   5335  N  N   . HIS B  1 225 ? -5.11400  -43.44300 8.12400   1.000 34.82000  ? 256 HIS B N   1 
ATOM   5336  C  CA  . HIS B  1 225 ? -5.28900  -44.77400 7.54600   1.000 40.12000  ? 256 HIS B CA  1 
ATOM   5337  C  C   . HIS B  1 225 ? -6.43200  -45.51700 8.24300   1.000 35.85000  ? 256 HIS B C   1 
ATOM   5338  O  O   . HIS B  1 225 ? -6.69000  -45.31500 9.43500   1.000 40.91000  ? 256 HIS B O   1 
ATOM   5339  C  CB  . HIS B  1 225 ? -3.96100  -45.54200 7.68000   1.000 39.31000  ? 256 HIS B CB  1 
ATOM   5340  C  CG  . HIS B  1 225 ? -3.89300  -46.85000 6.94800   1.000 42.80000  ? 256 HIS B CG  1 
ATOM   5341  N  ND1 . HIS B  1 225 ? -4.59600  -47.96700 7.34600   1.000 38.34000  ? 256 HIS B ND1 1 
ATOM   5342  C  CD2 . HIS B  1 225 ? -3.11400  -47.24800 5.91200   1.000 39.25000  ? 256 HIS B CD2 1 
ATOM   5343  C  CE1 . HIS B  1 225 ? -4.29200  -48.98300 6.55500   1.000 37.38000  ? 256 HIS B CE1 1 
ATOM   5344  N  NE2 . HIS B  1 225 ? -3.39400  -48.57300 5.68000   1.000 41.04000  ? 256 HIS B NE2 1 
ATOM   5345  N  N   . VAL B  1 226 ? -7.09200  -46.41400 7.50500   1.000 36.33000  ? 257 VAL B N   1 
ATOM   5346  C  CA  . VAL B  1 226 ? -8.18700  -47.21600 8.05400   1.000 35.49000  ? 257 VAL B CA  1 
ATOM   5347  C  C   . VAL B  1 226 ? -7.63900  -48.05400 9.21000   1.000 42.29000  ? 257 VAL B C   1 
ATOM   5348  O  O   . VAL B  1 226 ? -6.43000  -48.32700 9.25900   1.000 38.27000  ? 257 VAL B O   1 
ATOM   5349  C  CB  . VAL B  1 226 ? -8.83300  -48.12200 6.99100   1.000 46.30000  ? 257 VAL B CB  1 
ATOM   5350  C  CG1 . VAL B  1 226 ? -9.68900  -47.30500 5.96200   1.000 38.57000  ? 257 VAL B CG1 1 
ATOM   5351  C  CG2 . VAL B  1 226 ? -7.78200  -49.03600 6.32400   1.000 39.95000  ? 257 VAL B CG2 1 
ATOM   5352  N  N   . PRO B  1 227 ? -8.47100  -48.49500 10.15900  1.000 41.34000  ? 258 PRO B N   1 
ATOM   5353  C  CA  . PRO B  1 227 ? -9.92700  -48.30300 10.25900  1.000 40.67000  ? 258 PRO B CA  1 
ATOM   5354  C  C   . PRO B  1 227 ? -10.22700 -46.86300 10.58200  1.000 39.27000  ? 258 PRO B C   1 
ATOM   5355  O  O   . PRO B  1 227 ? -9.44100  -46.24500 11.29500  1.000 38.01000  ? 258 PRO B O   1 
ATOM   5356  C  CB  . PRO B  1 227 ? -10.32900 -49.25300 11.40200  1.000 41.47000  ? 258 PRO B CB  1 
ATOM   5357  C  CG  . PRO B  1 227 ? -9.06100  -49.26100 12.29900  1.000 40.93000  ? 258 PRO B CG  1 
ATOM   5358  C  CD  . PRO B  1 227 ? -7.93500  -49.27200 11.29600  1.000 38.47000  ? 258 PRO B CD  1 
ATOM   5359  N  N   . LEU B  1 228 ? -11.30100 -46.28800 10.03600  1.000 34.00000  ? 259 LEU B N   1 
ATOM   5360  C  CA  . LEU B  1 228 ? -11.68600 -44.92400 10.38700  1.000 37.72000  ? 259 LEU B CA  1 
ATOM   5361  C  C   . LEU B  1 228 ? -12.23700 -44.91500 11.82000  1.000 44.82000  ? 259 LEU B C   1 
ATOM   5362  O  O   . LEU B  1 228 ? -13.37400 -45.31800 12.07400  1.000 40.73000  ? 259 LEU B O   1 
ATOM   5363  C  CB  . LEU B  1 228 ? -12.70600 -44.39300 9.38900   1.000 39.96000  ? 259 LEU B CB  1 
ATOM   5364  C  CG  . LEU B  1 228 ? -12.18900 -44.30100 7.95200   1.000 41.85000  ? 259 LEU B CG  1 
ATOM   5365  C  CD1 . LEU B  1 228 ? -13.26800 -43.74300 7.01200   1.000 37.87000  ? 259 LEU B CD1 1 
ATOM   5366  C  CD2 . LEU B  1 228 ? -10.89400 -43.48000 7.87500   1.000 35.69000  ? 259 LEU B CD2 1 
ATOM   5367  N  N   . GLN B  1 229 ? -11.42500 -44.49700 12.77900  1.000 42.90000  ? 260 GLN B N   1 
ATOM   5368  C  CA  . GLN B  1 229 ? -11.85900 -44.42200 14.16700  1.000 40.56000  ? 260 GLN B CA  1 
ATOM   5369  C  C   . GLN B  1 229 ? -11.39900 -43.09800 14.75000  1.000 41.02000  ? 260 GLN B C   1 
ATOM   5370  O  O   . GLN B  1 229 ? -10.23000 -42.72000 14.59200  1.000 44.35000  ? 260 GLN B O   1 
ATOM   5371  C  CB  . GLN B  1 229 ? -11.31000 -45.60600 14.95100  1.000 38.94000  ? 260 GLN B CB  1 
ATOM   5372  C  CG  . GLN B  1 229 ? -11.80100 -46.91600 14.36800  1.000 40.39000  ? 260 GLN B CG  1 
ATOM   5373  C  CD  . GLN B  1 229 ? -11.12500 -48.11800 14.95300  1.000 43.37000  ? 260 GLN B CD  1 
ATOM   5374  O  OE1 . GLN B  1 229 ? -10.05500 -48.01100 15.54600  1.000 49.72000  ? 260 GLN B OE1 1 
ATOM   5375  N  NE2 . GLN B  1 229 ? -11.72700 -49.28400 14.76900  1.000 41.59000  ? 260 GLN B NE2 1 
ATOM   5376  N  N   . ALA B  1 230 ? -12.30800 -42.38200 15.40100  1.000 35.35000  ? 261 ALA B N   1 
ATOM   5377  C  CA  . ALA B  1 230 ? -11.98800 -41.04900 15.88200  1.000 39.19000  ? 261 ALA B CA  1 
ATOM   5378  C  C   . ALA B  1 230 ? -12.60600 -40.80900 17.25200  1.000 45.14000  ? 261 ALA B C   1 
ATOM   5379  O  O   . ALA B  1 230 ? -13.60700 -41.42700 17.62800  1.000 41.63000  ? 261 ALA B O   1 
ATOM   5380  C  CB  . ALA B  1 230 ? -12.46400 -39.97200 14.90300  1.000 35.76000  ? 261 ALA B CB  1 
ATOM   5381  N  N   . LYS B  1 231 ? -12.00600 -39.86100 17.97000  1.000 38.59000  ? 262 LYS B N   1 
ATOM   5382  C  CA  . LYS B  1 231 ? -12.50500 -39.44600 19.27500  1.000 43.98000  ? 262 LYS B CA  1 
ATOM   5383  C  C   . LYS B  1 231 ? -13.75300 -38.58200 19.13200  1.000 48.42000  ? 262 LYS B C   1 
ATOM   5384  O  O   . LYS B  1 231 ? -13.85400 -37.74500 18.22300  1.000 42.75000  ? 262 LYS B O   1 
ATOM   5385  C  CB  . LYS B  1 231 ? -11.44400 -38.65000 20.04100  1.000 39.61000  ? 262 LYS B CB  1 
ATOM   5386  C  CG  . LYS B  1 231 ? -10.23400 -39.44300 20.48800  1.000 45.47000  ? 262 LYS B CG  1 
ATOM   5387  C  CD  . LYS B  1 231 ? -9.11800  -38.54400 21.03800  1.000 43.39000  ? 262 LYS B CD  1 
ATOM   5388  C  CE  . LYS B  1 231 ? -9.54200  -37.72200 22.23900  1.000 49.06000  ? 262 LYS B CE  1 
ATOM   5389  N  NZ  . LYS B  1 231 ? -8.39900  -36.89400 22.72700  1.000 45.00000  ? 262 LYS B NZ  1 
ATOM   5390  N  N   . ALA B  1 232 ? -14.68600 -38.76600 20.07400  1.000 39.88000  ? 263 ALA B N   1 
ATOM   5391  C  CA  . ALA B  1 232 ? -15.94100 -38.02800 20.04100  1.000 43.69000  ? 263 ALA B CA  1 
ATOM   5392  C  C   . ALA B  1 232 ? -15.69600 -36.52600 20.06300  1.000 41.27000  ? 263 ALA B C   1 
ATOM   5393  O  O   . ALA B  1 232 ? -16.40700 -35.76800 19.39100  1.000 48.09000  ? 263 ALA B O   1 
ATOM   5394  C  CB  . ALA B  1 232 ? -16.84700 -38.46500 21.20000  1.000 36.33000  ? 263 ALA B CB  1 
ATOM   5395  N  N   . GLU B  1 233 ? -14.70200 -36.07100 20.83000  1.000 42.76000  ? 264 GLU B N   1 
ATOM   5396  C  CA  . GLU B  1 233 ? -14.41600 -34.64000 20.86400  1.000 45.92000  ? 264 GLU B CA  1 
ATOM   5397  C  C   . GLU B  1 233 ? -13.91800 -34.13600 19.51100  1.000 47.43000  ? 264 GLU B C   1 
ATOM   5398  O  O   . GLU B  1 233 ? -14.13500 -32.96800 19.16300  1.000 45.57000  ? 264 GLU B O   1 
ATOM   5399  C  CB  . GLU B  1 233 ? -13.39600 -34.31400 21.95300  1.000 47.96000  ? 264 GLU B CB  1 
ATOM   5400  C  CG  . GLU B  1 233 ? -13.69800 -34.92400 23.32700  1.000 57.01000  ? 264 GLU B CG  1 
ATOM   5401  C  CD  . GLU B  1 233 ? -13.15400 -36.35600 23.51300  1.000 57.26000  ? 264 GLU B CD  1 
ATOM   5402  O  OE1 . GLU B  1 233 ? -13.38500 -37.24900 22.65300  1.000 54.43000  ? 264 GLU B OE1 1 
ATOM   5403  O  OE2 . GLU B  1 233 ? -12.49100 -36.59300 24.54700  1.000 68.54000  ? 264 GLU B OE2 1 
ATOM   5404  N  N   . ASP B  1 234 ? -13.21900 -34.97800 18.75200  1.000 44.40000  ? 265 ASP B N   1 
ATOM   5405  C  CA  . ASP B  1 234 ? -12.77400 -34.53400 17.43600  1.000 48.55000  ? 265 ASP B CA  1 
ATOM   5406  C  C   . ASP B  1 234 ? -13.90900 -34.60000 16.41000  1.000 44.45000  ? 265 ASP B C   1 
ATOM   5407  O  O   . ASP B  1 234 ? -14.08600 -33.66800 15.61700  1.000 40.26000  ? 265 ASP B O   1 
ATOM   5408  C  CB  . ASP B  1 234 ? -11.56300 -35.35100 17.00700  1.000 38.74000  ? 265 ASP B CB  1 
ATOM   5409  C  CG  . ASP B  1 234 ? -10.34600 -35.06700 17.89400  1.000 44.10000  ? 265 ASP B CG  1 
ATOM   5410  O  OD1 . ASP B  1 234 ? -10.19800 -33.91200 18.35100  1.000 41.70000  ? 265 ASP B OD1 1 
ATOM   5411  O  OD2 . ASP B  1 234 ? -9.54000  -35.98900 18.14000  1.000 47.65000  ? 265 ASP B OD2 1 
ATOM   5412  N  N   . VAL B  1 235 ? -14.72400 -35.65600 16.44700  1.000 39.73000  ? 266 VAL B N   1 
ATOM   5413  C  CA  . VAL B  1 235 ? -15.84600 -35.73300 15.52100  1.000 43.61000  ? 266 VAL B CA  1 
ATOM   5414  C  C   . VAL B  1 235 ? -16.73500 -34.50300 15.65900  1.000 46.91000  ? 266 VAL B C   1 
ATOM   5415  O  O   . VAL B  1 235 ? -17.20400 -33.93500 14.66000  1.000 46.34000  ? 266 VAL B O   1 
ATOM   5416  C  CB  . VAL B  1 235 ? -16.65000 -37.02000 15.77100  1.000 45.43000  ? 266 VAL B CB  1 
ATOM   5417  C  CG1 . VAL B  1 235 ? -17.95800 -36.97200 14.97600  1.000 40.23000  ? 266 VAL B CG1 1 
ATOM   5418  C  CG2 . VAL B  1 235 ? -15.83600 -38.27400 15.42600  1.000 37.87000  ? 266 VAL B CG2 1 
ATOM   5419  N  N   . ALA B  1 236 ? -16.89500 -34.01500 16.88700  1.000 43.89000  ? 267 ALA B N   1 
ATOM   5420  C  CA  . ALA B  1 236 ? -17.81000 -32.90500 17.13700  1.000 49.21000  ? 267 ALA B CA  1 
ATOM   5421  C  C   . ALA B  1 236 ? -17.37700 -31.65300 16.40500  1.000 45.18000  ? 267 ALA B C   1 
ATOM   5422  O  O   . ALA B  1 236 ? -18.21000 -30.79700 16.09800  1.000 44.48000  ? 267 ALA B O   1 
ATOM   5423  C  CB  . ALA B  1 236 ? -17.90800 -32.61700 18.64200  1.000 51.77000  ? 267 ALA B CB  1 
ATOM   5424  N  N   . LYS B  1 237 ? -16.08300 -31.50600 16.13800  1.000 42.03000  ? 268 LYS B N   1 
ATOM   5425  C  CA  . LYS B  1 237 ? -15.68400 -30.33200 15.38200  1.000 46.69000  ? 268 LYS B CA  1 
ATOM   5426  C  C   . LYS B  1 237 ? -16.14800 -30.41500 13.93400  1.000 44.94000  ? 268 LYS B C   1 
ATOM   5427  O  O   . LYS B  1 237 ? -16.07200 -29.41200 13.22200  1.000 47.48000  ? 268 LYS B O   1 
ATOM   5428  C  CB  . LYS B  1 237 ? -14.15800 -30.15600 15.44900  1.000 46.56000  ? 268 LYS B CB  1 
ATOM   5429  N  N   . PHE B  1 238 ? -16.66400 -31.57000 13.49500  1.000 41.22000  ? 269 PHE B N   1 
ATOM   5430  C  CA  . PHE B  1 238 ? -17.09000 -31.74300 12.11200  1.000 43.70000  ? 269 PHE B CA  1 
ATOM   5431  C  C   . PHE B  1 238 ? -18.47700 -32.36200 12.06200  1.000 47.07000  ? 269 PHE B C   1 
ATOM   5432  O  O   . PHE B  1 238 ? -18.80100 -33.08900 11.12100  1.000 46.78000  ? 269 PHE B O   1 
ATOM   5433  C  CB  . PHE B  1 238 ? -16.09200 -32.61500 11.34900  1.000 38.60000  ? 269 PHE B CB  1 
ATOM   5434  C  CG  . PHE B  1 238 ? -14.68700 -32.11600 11.44600  1.000 44.94000  ? 269 PHE B CG  1 
ATOM   5435  C  CD1 . PHE B  1 238 ? -14.26100 -31.02900 10.69800  1.000 44.12000  ? 269 PHE B CD1 1 
ATOM   5436  C  CD2 . PHE B  1 238 ? -13.80400 -32.69900 12.34000  1.000 39.98000  ? 269 PHE B CD2 1 
ATOM   5437  C  CE1 . PHE B  1 238 ? -12.95600 -30.54800 10.81900  1.000 44.16000  ? 269 PHE B CE1 1 
ATOM   5438  C  CE2 . PHE B  1 238 ? -12.50900 -32.23000 12.47100  1.000 42.68000  ? 269 PHE B CE2 1 
ATOM   5439  C  CZ  . PHE B  1 238 ? -12.08200 -31.15700 11.70700  1.000 44.02000  ? 269 PHE B CZ  1 
ATOM   5440  N  N   . ALA B  1 239 ? -19.31400 -32.07500 13.06400  1.000 46.00000  ? 270 ALA B N   1 
ATOM   5441  C  CA  . ALA B  1 239 ? -20.61900 -32.72100 13.14000  1.000 47.96000  ? 270 ALA B CA  1 
ATOM   5442  C  C   . ALA B  1 239 ? -21.53000 -32.35000 11.96900  1.000 46.90000  ? 270 ALA B C   1 
ATOM   5443  O  O   . ALA B  1 239 ? -22.41900 -33.13000 11.63400  1.000 45.13000  ? 270 ALA B O   1 
ATOM   5444  C  CB  . ALA B  1 239 ? -21.28300 -32.38000 14.48000  1.000 45.51000  ? 270 ALA B CB  1 
ATOM   5445  N  N   . HIS B  1 240 ? -21.31100 -31.20100 11.32700  1.000 45.11000  ? 271 HIS B N   1 
ATOM   5446  C  CA  . HIS B  1 240 ? -22.07300 -30.79900 10.15300  1.000 50.86000  ? 271 HIS B CA  1 
ATOM   5447  C  C   . HIS B  1 240 ? -21.70900 -31.54300 8.86500   1.000 55.28000  ? 271 HIS B C   1 
ATOM   5448  O  O   . HIS B  1 240 ? -22.43200 -31.38000 7.87200   1.000 53.92000  ? 271 HIS B O   1 
ATOM   5449  C  CB  . HIS B  1 240 ? -21.86300 -29.32300 9.89600   1.000 57.68000  ? 271 HIS B CB  1 
ATOM   5450  C  CG  . HIS B  1 240 ? -20.45600 -29.00300 9.51200   1.000 62.37000  ? 271 HIS B CG  1 
ATOM   5451  N  ND1 . HIS B  1 240 ? -20.07300 -28.77100 8.20600   1.000 62.88000  ? 271 HIS B ND1 1 
ATOM   5452  C  CD2 . HIS B  1 240 ? -19.32800 -28.92200 10.25800  1.000 58.45000  ? 271 HIS B CD2 1 
ATOM   5453  C  CE1 . HIS B  1 240 ? -18.77300 -28.53700 8.16700   1.000 66.94000  ? 271 HIS B CE1 1 
ATOM   5454  N  NE2 . HIS B  1 240 ? -18.29600 -28.62000 9.40000   1.000 66.96000  ? 271 HIS B NE2 1 
ATOM   5455  N  N   . ILE B  1 241 ? -20.67600 -32.38500 8.85300   1.000 44.31000  ? 272 ILE B N   1 
ATOM   5456  C  CA  . ILE B  1 241 ? -20.34300 -33.13900 7.64600   1.000 45.27000  ? 272 ILE B CA  1 
ATOM   5457  C  C   . ILE B  1 241 ? -21.22700 -34.37500 7.61300   1.000 46.46000  ? 272 ILE B C   1 
ATOM   5458  O  O   . ILE B  1 241 ? -21.13400 -35.23500 8.49400   1.000 42.59000  ? 272 ILE B O   1 
ATOM   5459  C  CB  . ILE B  1 241 ? -18.85600 -33.53800 7.61500   1.000 48.17000  ? 272 ILE B CB  1 
ATOM   5460  C  CG1 . ILE B  1 241 ? -17.93300 -32.32500 7.54100   1.000 41.08000  ? 272 ILE B CG1 1 
ATOM   5461  C  CG2 . ILE B  1 241 ? -18.59300 -34.53000 6.48500   1.000 43.24000  ? 272 ILE B CG2 1 
ATOM   5462  C  CD1 . ILE B  1 241 ? -16.44200 -32.71000 7.47300   1.000 43.23000  ? 272 ILE B CD1 1 
ATOM   5463  N  N   . LYS B  1 242 ? -22.05000 -34.48900 6.56300   1.000 48.79000  ? 273 LYS B N   1 
ATOM   5464  C  CA  . LYS B  1 242 ? -23.09400 -35.50800 6.51400   1.000 48.71000  ? 273 LYS B CA  1 
ATOM   5465  C  C   . LYS B  1 242 ? -22.53100 -36.89200 6.21500   1.000 47.96000  ? 273 LYS B C   1 
ATOM   5466  O  O   . LYS B  1 242 ? -23.02700 -37.89100 6.74400   1.000 49.47000  ? 273 LYS B O   1 
ATOM   5467  C  CB  . LYS B  1 242 ? -24.15900 -35.12800 5.47500   1.000 54.75000  ? 273 LYS B CB  1 
ATOM   5468  N  N   . ASP B  1 243 ? -21.54600 -36.99700 5.33500   1.000 48.90000  ? 274 ASP B N   1 
ATOM   5469  C  CA  . ASP B  1 243 ? -20.99500 -38.31500 5.05600   1.000 49.48000  ? 274 ASP B CA  1 
ATOM   5470  C  C   . ASP B  1 243 ? -20.18300 -38.79600 6.25700   1.000 44.46000  ? 274 ASP B C   1 
ATOM   5471  O  O   . ASP B  1 243 ? -19.22600 -38.13700 6.66300   1.000 46.46000  ? 274 ASP B O   1 
ATOM   5472  C  CB  . ASP B  1 243 ? -20.12800 -38.28200 3.80900   1.000 46.82000  ? 274 ASP B CB  1 
ATOM   5473  C  CG  . ASP B  1 243 ? -19.63500 -39.64600 3.44700   1.000 50.27000  ? 274 ASP B CG  1 
ATOM   5474  O  OD1 . ASP B  1 243 ? -20.47700 -40.48500 3.07400   1.000 57.36000  ? 274 ASP B OD1 1 
ATOM   5475  O  OD2 . ASP B  1 243 ? -18.42500 -39.89700 3.55500   1.000 59.18000  ? 274 ASP B OD2 1 
ATOM   5476  N  N   . LYS B  1 244 ? -20.54600 -39.96800 6.79200   1.000 44.19000  ? 275 LYS B N   1 
ATOM   5477  C  CA  . LYS B  1 244 ? -19.94200 -40.46700 8.02200   1.000 46.79000  ? 275 LYS B CA  1 
ATOM   5478  C  C   . LYS B  1 244 ? -18.44100 -40.73000 7.86300   1.000 48.30000  ? 275 LYS B C   1 
ATOM   5479  O  O   . LYS B  1 244 ? -17.64200 -40.39500 8.75300   1.000 38.50000  ? 275 LYS B O   1 
ATOM   5480  C  CB  . LYS B  1 244 ? -20.66900 -41.73300 8.47700   1.000 45.50000  ? 275 LYS B CB  1 
ATOM   5481  C  CG  . LYS B  1 244 ? -19.93200 -42.50600 9.57400   1.000 49.72000  ? 275 LYS B CG  1 
ATOM   5482  C  CD  . LYS B  1 244 ? -20.91500 -43.13400 10.56700  1.000 60.46000  ? 275 LYS B CD  1 
ATOM   5483  C  CE  . LYS B  1 244 ? -20.70600 -44.63900 10.69600  1.000 67.20000  ? 275 LYS B CE  1 
ATOM   5484  N  NZ  . LYS B  1 244 ? -21.53900 -45.23700 11.78600  1.000 70.12000  ? 275 LYS B NZ  1 
ATOM   5485  N  N   . ASP B  1 245 ? -18.03700 -41.31600 6.73400   1.000 41.23000  ? 276 ASP B N   1 
ATOM   5486  C  CA  . ASP B  1 245 ? -16.62300 -41.60100 6.52500   1.000 49.29000  ? 276 ASP B CA  1 
ATOM   5487  C  C   . ASP B  1 245 ? -15.81100 -40.31100 6.46300   1.000 45.14000  ? 276 ASP B C   1 
ATOM   5488  O  O   . ASP B  1 245 ? -14.78200 -40.17300 7.13700   1.000 40.13000  ? 276 ASP B O   1 
ATOM   5489  C  CB  . ASP B  1 245 ? -16.45900 -42.39200 5.23500   1.000 47.97000  ? 276 ASP B CB  1 
ATOM   5490  C  CG  . ASP B  1 245 ? -16.64000 -43.86800 5.44400   1.000 56.99000  ? 276 ASP B CG  1 
ATOM   5491  O  OD1 . ASP B  1 245 ? -17.11600 -44.25100 6.53500   1.000 63.61000  ? 276 ASP B OD1 1 
ATOM   5492  O  OD2 . ASP B  1 245 ? -16.32600 -44.64600 4.51400   1.000 72.76000  ? 276 ASP B OD2 1 
ATOM   5493  N  N   . ARG B  1 246 ? -16.29000 -39.33000 5.69600   1.000 42.96000  ? 277 ARG B N   1 
ATOM   5494  C  CA  . ARG B  1 246 ? -15.59300 -38.05000 5.64700   1.000 40.81000  ? 277 ARG B CA  1 
ATOM   5495  C  C   . ARG B  1 246 ? -15.54700 -37.40800 7.02300   1.000 39.50000  ? 277 ARG B C   1 
ATOM   5496  O  O   . ARG B  1 246 ? -14.52200 -36.83600 7.41900   1.000 39.82000  ? 277 ARG B O   1 
ATOM   5497  C  CB  . ARG B  1 246 ? -16.28300 -37.11300 4.65600   1.000 37.69000  ? 277 ARG B CB  1 
ATOM   5498  C  CG  . ARG B  1 246 ? -15.58100 -35.77700 4.44400   1.000 32.66000  ? 277 ARG B CG  1 
ATOM   5499  C  CD  . ARG B  1 246 ? -14.21900 -35.98500 3.74900   1.000 28.03000  ? 277 ARG B CD  1 
ATOM   5500  N  NE  . ARG B  1 246 ? -13.63600 -34.70900 3.37600   1.000 32.04000  ? 277 ARG B NE  1 
ATOM   5501  C  CZ  . ARG B  1 246 ? -12.39700 -34.55800 2.93400   1.000 38.22000  ? 277 ARG B CZ  1 
ATOM   5502  N  NH1 . ARG B  1 246 ? -11.59600 -35.59800 2.75300   1.000 36.70000  ? 277 ARG B NH1 1 
ATOM   5503  N  NH2 . ARG B  1 246 ? -11.92700 -33.33100 2.74300   1.000 37.02000  ? 277 ARG B NH2 1 
ATOM   5504  N  N   . ARG B  1 247 ? -16.63600 -37.51500 7.78500   1.000 40.98000  ? 278 ARG B N   1 
ATOM   5505  C  CA  . ARG B  1 247 ? -16.64800 -36.87800 9.09600   1.000 38.93000  ? 278 ARG B CA  1 
ATOM   5506  C  C   . ARG B  1 247 ? -15.58900 -37.50700 9.99100   1.000 36.48000  ? 278 ARG B C   1 
ATOM   5507  O  O   . ARG B  1 247 ? -14.78400 -36.80600 10.61400  1.000 36.94000  ? 278 ARG B O   1 
ATOM   5508  C  CB  . ARG B  1 247 ? -18.04800 -36.97500 9.71200   1.000 40.63000  ? 278 ARG B CB  1 
ATOM   5509  C  CG  . ARG B  1 247 ? -18.16000 -36.32300 11.09300  1.000 42.07000  ? 278 ARG B CG  1 
ATOM   5510  C  CD  . ARG B  1 247 ? -19.59200 -36.25400 11.59700  1.000 40.07000  ? 278 ARG B CD  1 
ATOM   5511  N  NE  . ARG B  1 247 ? -20.18400 -37.58300 11.69600  1.000 41.48000  ? 278 ARG B NE  1 
ATOM   5512  C  CZ  . ARG B  1 247 ? -21.15500 -38.02700 10.90500  1.000 50.09000  ? 278 ARG B CZ  1 
ATOM   5513  N  NH1 . ARG B  1 247 ? -21.68200 -37.26400 9.95900   1.000 44.47000  ? 278 ARG B NH1 1 
ATOM   5514  N  NH2 . ARG B  1 247 ? -21.58800 -39.28100 11.04300  1.000 51.00000  ? 278 ARG B NH2 1 
ATOM   5515  N  N   . THR B  1 248 ? -15.54100 -38.84200 10.01800  1.000 36.66000  ? 279 THR B N   1 
ATOM   5516  C  CA  . THR B  1 248 ? -14.58100 -39.54700 10.85300  1.000 36.16000  ? 279 THR B CA  1 
ATOM   5517  C  C   . THR B  1 248 ? -13.14800 -39.29600 10.40100  1.000 42.10000  ? 279 THR B C   1 
ATOM   5518  O  O   . THR B  1 248 ? -12.25600 -39.07700 11.23000  1.000 36.35000  ? 279 THR B O   1 
ATOM   5519  C  CB  . THR B  1 248 ? -14.90100 -41.03500 10.85500  1.000 34.72000  ? 279 THR B CB  1 
ATOM   5520  O  OG1 . THR B  1 248 ? -16.28200 -41.19600 11.16500  1.000 45.73000  ? 279 THR B OG1 1 
ATOM   5521  C  CG2 . THR B  1 248 ? -14.08000 -41.75300 11.92000  1.000 40.48000  ? 279 THR B CG2 1 
ATOM   5522  N  N   . TYR B  1 249 ? -12.91100 -39.34400 9.09200   1.000 40.68000  ? 280 TYR B N   1 
ATOM   5523  C  CA  . TYR B  1 249 ? -11.59500 -39.03600 8.53600   1.000 37.13000  ? 280 TYR B CA  1 
ATOM   5524  C  C   . TYR B  1 249 ? -11.12800 -37.64100 8.93000   1.000 35.01000  ? 280 TYR B C   1 
ATOM   5525  O  O   . TYR B  1 249 ? -9.95600  -37.43700 9.28500   1.000 37.90000  ? 280 TYR B O   1 
ATOM   5526  C  CB  . TYR B  1 249 ? -11.67000 -39.19500 7.01400   1.000 34.58000  ? 280 TYR B CB  1 
ATOM   5527  C  CG  . TYR B  1 249 ? -10.43800 -38.83800 6.22800   1.000 34.83000  ? 280 TYR B CG  1 
ATOM   5528  C  CD1 . TYR B  1 249 ? -10.21000 -37.52200 5.82300   1.000 33.13000  ? 280 TYR B CD1 1 
ATOM   5529  C  CD2 . TYR B  1 249 ? -9.52800  -39.82200 5.84000   1.000 32.34000  ? 280 TYR B CD2 1 
ATOM   5530  C  CE1 . TYR B  1 249 ? -9.07400  -37.19300 5.07400   1.000 36.02000  ? 280 TYR B CE1 1 
ATOM   5531  C  CE2 . TYR B  1 249 ? -8.43000  -39.52200 5.09400   1.000 27.93000  ? 280 TYR B CE2 1 
ATOM   5532  C  CZ  . TYR B  1 249 ? -8.19600  -38.19800 4.71400   1.000 36.91000  ? 280 TYR B CZ  1 
ATOM   5533  O  OH  . TYR B  1 249 ? -7.09200  -37.88200 3.96000   1.000 35.93000  ? 280 TYR B OH  1 
ATOM   5534  N  N   . ALA B  1 250 ? -12.01300 -36.65000 8.81700   1.000 35.82000  ? 281 ALA B N   1 
ATOM   5535  C  CA  . ALA B  1 250 ? -11.64300 -35.30100 9.23400   1.000 36.50000  ? 281 ALA B CA  1 
ATOM   5536  C  C   . ALA B  1 250 ? -11.24800 -35.27500 10.70700  1.000 37.93000  ? 281 ALA B C   1 
ATOM   5537  O  O   . ALA B  1 250 ? -10.29900 -34.58400 11.09100  1.000 37.05000  ? 281 ALA B O   1 
ATOM   5538  C  CB  . ALA B  1 250 ? -12.80300 -34.32400 8.97100   1.000 31.51000  ? 281 ALA B CB  1 
ATOM   5539  N  N   . ALA B  1 251 ? -11.99000 -35.99700 11.55600  1.000 39.63000  ? 282 ALA B N   1 
ATOM   5540  C  CA  . ALA B  1 251 ? -11.65700 -35.99800 12.97300  1.000 38.56000  ? 282 ALA B CA  1 
ATOM   5541  C  C   . ALA B  1 251 ? -10.29200 -36.62500 13.19100  1.000 38.45000  ? 282 ALA B C   1 
ATOM   5542  O  O   . ALA B  1 251 ? -9.51900  -36.17100 14.04400  1.000 39.00000  ? 282 ALA B O   1 
ATOM   5543  C  CB  . ALA B  1 251 ? -12.73400 -36.71800 13.78500  1.000 32.86000  ? 282 ALA B CB  1 
ATOM   5544  N  N   . MET B  1 252 ? -9.95900  -37.64300 12.39600  1.000 38.38000  ? 283 MET B N   1 
ATOM   5545  C  CA  . MET B  1 252 ? -8.65800  -38.27600 12.53500  1.000 38.38000  ? 283 MET B CA  1 
ATOM   5546  C  C   . MET B  1 252 ? -7.52900  -37.31300 12.18700  1.000 40.94000  ? 283 MET B C   1 
ATOM   5547  O  O   . MET B  1 252 ? -6.53100  -37.22400 12.91700  1.000 39.13000  ? 283 MET B O   1 
ATOM   5548  C  CB  . MET B  1 252 ? -8.60700  -39.52700 11.66800  1.000 38.81000  ? 283 MET B CB  1 
ATOM   5549  C  CG  . MET B  1 252 ? -9.65100  -40.56200 12.05900  1.000 34.62000  ? 283 MET B CG  1 
ATOM   5550  S  SD  . MET B  1 252 ? -9.71200  -41.93300 10.90300  1.000 40.59000  ? 283 MET B SD  1 
ATOM   5551  C  CE  . MET B  1 252 ? -8.16000  -42.80100 11.16200  1.000 38.75000  ? 283 MET B CE  1 
ATOM   5552  N  N   . VAL B  1 253 ? -7.67900  -36.57300 11.08300  1.000 38.91000  ? 284 VAL B N   1 
ATOM   5553  C  CA  . VAL B  1 253 ? -6.66700  -35.60400 10.68100  1.000 31.92000  ? 284 VAL B CA  1 
ATOM   5554  C  C   . VAL B  1 253 ? -6.56000  -34.51600 11.73000  1.000 39.51000  ? 284 VAL B C   1 
ATOM   5555  O  O   . VAL B  1 253 ? -5.46900  -34.02100 12.03500  1.000 35.56000  ? 284 VAL B O   1 
ATOM   5556  C  CB  . VAL B  1 253 ? -7.00400  -35.02700 9.28800   1.000 37.32000  ? 284 VAL B CB  1 
ATOM   5557  C  CG1 . VAL B  1 253 ? -6.09100  -33.86200 8.93500   1.000 30.07000  ? 284 VAL B CG1 1 
ATOM   5558  C  CG2 . VAL B  1 253 ? -6.96300  -36.12400 8.21000   1.000 31.25000  ? 284 VAL B CG2 1 
ATOM   5559  N  N   . TYR B  1 254 ? -7.69900  -34.12700 12.30000  1.000 41.55000  ? 285 TYR B N   1 
ATOM   5560  C  CA  . TYR B  1 254 ? -7.70200  -33.07800 13.30900  1.000 36.23000  ? 285 TYR B CA  1 
ATOM   5561  C  C   . TYR B  1 254 ? -6.93100  -33.50100 14.55300  1.000 38.85000  ? 285 TYR B C   1 
ATOM   5562  O  O   . TYR B  1 254 ? -6.23500  -32.68100 15.16500  1.000 39.72000  ? 285 TYR B O   1 
ATOM   5563  C  CB  . TYR B  1 254 ? -9.13600  -32.71500 13.65000  1.000 41.21000  ? 285 TYR B CB  1 
ATOM   5564  C  CG  . TYR B  1 254 ? -9.24000  -31.59400 14.63800  1.000 43.19000  ? 285 TYR B CG  1 
ATOM   5565  C  CD1 . TYR B  1 254 ? -8.92600  -30.28900 14.27700  1.000 37.35000  ? 285 TYR B CD1 1 
ATOM   5566  C  CD2 . TYR B  1 254 ? -9.65100  -31.83900 15.93700  1.000 38.21000  ? 285 TYR B CD2 1 
ATOM   5567  C  CE1 . TYR B  1 254 ? -9.03200  -29.26000 15.18400  1.000 45.07000  ? 285 TYR B CE1 1 
ATOM   5568  C  CE2 . TYR B  1 254 ? -9.74800  -30.83500 16.84200  1.000 38.77000  ? 285 TYR B CE2 1 
ATOM   5569  C  CZ  . TYR B  1 254 ? -9.43900  -29.54700 16.48000  1.000 48.09000  ? 285 TYR B CZ  1 
ATOM   5570  O  OH  . TYR B  1 254 ? -9.54800  -28.56400 17.43600  1.000 49.65000  ? 285 TYR B OH  1 
ATOM   5571  N  N   . ALA B  1 255 ? -7.05700  -34.77100 14.95500  1.000 38.40000  ? 286 ALA B N   1 
ATOM   5572  C  CA  . ALA B  1 255 ? -6.30400  -35.25200 16.10500  1.000 39.18000  ? 286 ALA B CA  1 
ATOM   5573  C  C   . ALA B  1 255 ? -4.80300  -35.18000 15.84700  1.000 40.62000  ? 286 ALA B C   1 
ATOM   5574  O  O   . ALA B  1 255 ? -4.02500  -34.86100 16.75400  1.000 40.94000  ? 286 ALA B O   1 
ATOM   5575  C  CB  . ALA B  1 255 ? -6.72400  -36.68800 16.44800  1.000 39.30000  ? 286 ALA B CB  1 
ATOM   5576  N  N   . VAL B  1 256 ? -4.37800  -35.41800 14.60700  1.000 40.26000  ? 287 VAL B N   1 
ATOM   5577  C  CA  . VAL B  1 256 ? -2.95500  -35.26800 14.30400  1.000 44.78000  ? 287 VAL B CA  1 
ATOM   5578  C  C   . VAL B  1 256 ? -2.55300  -33.81500 14.46500  1.000 42.42000  ? 287 VAL B C   1 
ATOM   5579  O  O   . VAL B  1 256 ? -1.48900  -33.50600 15.02000  1.000 37.69000  ? 287 VAL B O   1 
ATOM   5580  C  CB  . VAL B  1 256 ? -2.63900  -35.78600 12.88500  1.000 39.38000  ? 287 VAL B CB  1 
ATOM   5581  C  CG1 . VAL B  1 256 ? -1.25100  -35.31300 12.43400  1.000 37.50000  ? 287 VAL B CG1 1 
ATOM   5582  C  CG2 . VAL B  1 256 ? -2.73700  -37.28300 12.84000  1.000 27.18000  ? 287 VAL B CG2 1 
ATOM   5583  N  N   . ASP B  1 257 ? -3.43000  -32.90400 14.01700  1.000 41.03000  ? 288 ASP B N   1 
ATOM   5584  C  CA  . ASP B  1 257 ? -3.16900  -31.47000 14.12500  1.000 45.53000  ? 288 ASP B CA  1 
ATOM   5585  C  C   . ASP B  1 257 ? -3.09600  -31.01800 15.58200  1.000 43.81000  ? 288 ASP B C   1 
ATOM   5586  O  O   . ASP B  1 257 ? -2.26900  -30.15700 15.92600  1.000 42.65000  ? 288 ASP B O   1 
ATOM   5587  C  CB  . ASP B  1 257 ? -4.22200  -30.65900 13.35600  1.000 30.40000  ? 288 ASP B CB  1 
ATOM   5588  C  CG  . ASP B  1 257 ? -3.82600  -29.21300 13.22400  1.000 41.81000  ? 288 ASP B CG  1 
ATOM   5589  O  OD1 . ASP B  1 257 ? -2.91800  -28.93100 12.41900  1.000 46.97000  ? 288 ASP B OD1 1 
ATOM   5590  O  OD2 . ASP B  1 257 ? -4.37700  -28.34800 13.92300  1.000 50.52000  ? 288 ASP B OD2 1 
ATOM   5591  N  N   . ARG B  1 258 ? -3.99700  -31.52800 16.43700  1.000 40.99000  ? 289 ARG B N   1 
ATOM   5592  C  CA  . ARG B  1 258 ? -3.92500  -31.18800 17.85700  1.000 41.54000  ? 289 ARG B CA  1 
ATOM   5593  C  C   . ARG B  1 258 ? -2.55800  -31.54400 18.42400  1.000 37.26000  ? 289 ARG B C   1 
ATOM   5594  O  O   . ARG B  1 258 ? -1.96700  -30.75900 19.16800  1.000 42.90000  ? 289 ARG B O   1 
ATOM   5595  C  CB  . ARG B  1 258 ? -5.01200  -31.91600 18.66100  1.000 39.70000  ? 289 ARG B CB  1 
ATOM   5596  C  CG  . ARG B  1 258 ? -6.44000  -31.35000 18.59200  1.000 47.29000  ? 289 ARG B CG  1 
ATOM   5597  C  CD  . ARG B  1 258 ? -7.36800  -32.00500 19.66300  1.000 37.98000  ? 289 ARG B CD  1 
ATOM   5598  N  NE  . ARG B  1 258 ? -7.61800  -33.43100 19.45200  1.000 40.52000  ? 289 ARG B NE  1 
ATOM   5599  C  CZ  . ARG B  1 258 ? -6.89800  -34.41300 19.98900  1.000 44.21000  ? 289 ARG B CZ  1 
ATOM   5600  N  NH1 . ARG B  1 258 ? -5.83700  -34.16200 20.74400  1.000 40.50000  ? 289 ARG B NH1 1 
ATOM   5601  N  NH2 . ARG B  1 258 ? -7.23200  -35.67700 19.74000  1.000 40.99000  ? 289 ARG B NH2 1 
ATOM   5602  N  N   . GLY B  1 259 ? -2.05100  -32.73500 18.08700  1.000 40.22000  ? 290 GLY B N   1 
ATOM   5603  C  CA  . GLY B  1 259 ? -0.76400  -33.17900 18.60500  1.000 43.67000  ? 290 GLY B CA  1 
ATOM   5604  C  C   . GLY B  1 259 ? 0.41400   -32.38400 18.07700  1.000 45.41000  ? 290 GLY B C   1 
ATOM   5605  O  O   . GLY B  1 259 ? 1.38600   -32.16700 18.79800  1.000 48.88000  ? 290 GLY B O   1 
ATOM   5606  N  N   . VAL B  1 260 ? 0.35400   -31.94800 16.81600  1.000 45.18000  ? 291 VAL B N   1 
ATOM   5607  C  CA  . VAL B  1 260 ? 1.41300   -31.09200 16.29600  1.000 41.17000  ? 291 VAL B CA  1 
ATOM   5608  C  C   . VAL B  1 260 ? 1.43300   -29.77100 17.05800  1.000 42.53000  ? 291 VAL B C   1 
ATOM   5609  O  O   . VAL B  1 260 ? 2.49800   -29.20200 17.32800  1.000 46.86000  ? 291 VAL B O   1 
ATOM   5610  C  CB  . VAL B  1 260 ? 1.23800   -30.88500 14.78300  1.000 40.76000  ? 291 VAL B CB  1 
ATOM   5611  C  CG1 . VAL B  1 260 ? 2.22700   -29.84500 14.27100  1.000 32.47000  ? 291 VAL B CG1 1 
ATOM   5612  C  CG2 . VAL B  1 260 ? 1.40900   -32.21000 14.05300  1.000 40.97000  ? 291 VAL B CG2 1 
ATOM   5613  N  N   . GLY B  1 261 ? 0.26200   -29.27000 17.43800  1.000 42.74000  ? 292 GLY B N   1 
ATOM   5614  C  CA  . GLY B  1 261 ? 0.23300   -28.05700 18.23600  1.000 41.70000  ? 292 GLY B CA  1 
ATOM   5615  C  C   . GLY B  1 261 ? 0.87100   -28.26400 19.59600  1.000 44.39000  ? 292 GLY B C   1 
ATOM   5616  O  O   . GLY B  1 261 ? 1.65300   -27.43000 20.06000  1.000 44.62000  ? 292 GLY B O   1 
ATOM   5617  N  N   . LYS B  1 262 ? 0.59700   -29.40500 20.22300  1.000 46.14000  ? 293 LYS B N   1 
ATOM   5618  C  CA  . LYS B  1 262 ? 1.25700   -29.70400 21.48300  1.000 46.61000  ? 293 LYS B CA  1 
ATOM   5619  C  C   . LYS B  1 262 ? 2.74300   -29.92300 21.26500  1.000 47.76000  ? 293 LYS B C   1 
ATOM   5620  O  O   . LYS B  1 262 ? 3.56400   -29.48700 22.08300  1.000 54.36000  ? 293 LYS B O   1 
ATOM   5621  C  CB  . LYS B  1 262 ? 0.63800   -30.93600 22.14300  1.000 45.90000  ? 293 LYS B CB  1 
ATOM   5622  C  CG  . LYS B  1 262 ? -0.85800  -30.86200 22.37100  1.000 47.98000  ? 293 LYS B CG  1 
ATOM   5623  C  CD  . LYS B  1 262 ? -1.33800  -29.79000 23.32300  1.000 61.14000  ? 293 LYS B CD  1 
ATOM   5624  C  CE  . LYS B  1 262 ? -0.98200  -30.11600 24.76800  1.000 74.55000  ? 293 LYS B CE  1 
ATOM   5625  N  NZ  . LYS B  1 262 ? -1.63700  -29.15200 25.71100  1.000 83.53000  ? 293 LYS B NZ  1 
ATOM   5626  N  N   . ILE B  1 263 ? 3.11800   -30.57900 20.16000  1.000 45.84000  ? 294 ILE B N   1 
ATOM   5627  C  CA  . ILE B  1 263 ? 4.54100   -30.77300 19.88800  1.000 46.49000  ? 294 ILE B CA  1 
ATOM   5628  C  C   . ILE B  1 263 ? 5.23500   -29.43000 19.73100  1.000 48.85000  ? 294 ILE B C   1 
ATOM   5629  O  O   . ILE B  1 263 ? 6.33000   -29.21300 20.27800  1.000 43.34000  ? 294 ILE B O   1 
ATOM   5630  C  CB  . ILE B  1 263 ? 4.75400   -31.67400 18.65800  1.000 45.08000  ? 294 ILE B CB  1 
ATOM   5631  C  CG1 . ILE B  1 263 ? 4.48500   -33.12800 19.04200  1.000 40.87000  ? 294 ILE B CG1 1 
ATOM   5632  C  CG2 . ILE B  1 263 ? 6.18700   -31.52600 18.14200  1.000 41.75000  ? 294 ILE B CG2 1 
ATOM   5633  C  CD1 . ILE B  1 263 ? 4.07500   -34.02800 17.91000  1.000 39.09000  ? 294 ILE B CD1 1 
ATOM   5634  N  N   . VAL B  1 264 ? 4.57900   -28.49100 19.03400  1.000 46.01000  ? 295 VAL B N   1 
ATOM   5635  C  CA  . VAL B  1 264 ? 5.15200   -27.16600 18.81600  1.000 40.63000  ? 295 VAL B CA  1 
ATOM   5636  C  C   . VAL B  1 264 ? 5.35900   -26.44900 20.15200  1.000 48.52000  ? 295 VAL B C   1 
ATOM   5637  O  O   . VAL B  1 264 ? 6.42200   -25.85800 20.40100  1.000 46.90000  ? 295 VAL B O   1 
ATOM   5638  C  CB  . VAL B  1 264 ? 4.25400   -26.35900 17.85300  1.000 43.11000  ? 295 VAL B CB  1 
ATOM   5639  C  CG1 . VAL B  1 264 ? 4.61600   -24.90000 17.84800  1.000 40.34000  ? 295 VAL B CG1 1 
ATOM   5640  C  CG2 . VAL B  1 264 ? 4.35700   -26.90400 16.41800  1.000 42.31000  ? 295 VAL B CG2 1 
ATOM   5641  N  N   . GLN B  1 265 ? 4.37300   -26.52000 21.05100  1.000 48.88000  ? 296 GLN B N   1 
ATOM   5642  C  CA  . GLN B  1 265 ? 4.53500   -25.86800 22.35000  1.000 51.26000  ? 296 GLN B CA  1 
ATOM   5643  C  C   . GLN B  1 265 ? 5.76400   -26.41200 23.07700  1.000 51.72000  ? 296 GLN B C   1 
ATOM   5644  O  O   . GLN B  1 265 ? 6.58000   -25.65000 23.60900  1.000 50.60000  ? 296 GLN B O   1 
ATOM   5645  C  CB  . GLN B  1 265 ? 3.27000   -26.05800 23.19000  1.000 53.91000  ? 296 GLN B CB  1 
ATOM   5646  C  CG  . GLN B  1 265 ? 2.99800   -24.94300 24.22400  1.000 62.02000  ? 296 GLN B CG  1 
ATOM   5647  C  CD  . GLN B  1 265 ? 2.71800   -23.56200 23.53800  1.000 80.36000  ? 296 GLN B CD  1 
ATOM   5648  O  OE1 . GLN B  1 265 ? 3.50100   -22.60900 23.65900  1.000 72.39000  ? 296 GLN B OE1 1 
ATOM   5649  N  NE2 . GLN B  1 265 ? 1.60800   -23.48200 22.79300  1.000 81.42000  ? 296 GLN B NE2 1 
ATOM   5650  N  N   . THR B  1 266 ? 5.94800   -27.72800 23.04900  1.000 46.89000  ? 297 THR B N   1 
ATOM   5651  C  CA  . THR B  1 266 ? 7.11200   -28.31600 23.69500  1.000 44.93000  ? 297 THR B CA  1 
ATOM   5652  C  C   . THR B  1 266 ? 8.40300   -27.82500 23.05300  1.000 50.85000  ? 297 THR B C   1 
ATOM   5653  O  O   . THR B  1 266 ? 9.39700   -27.58900 23.74500  1.000 51.48000  ? 297 THR B O   1 
ATOM   5654  C  CB  . THR B  1 266 ? 7.02900   -29.83700 23.63700  1.000 47.33000  ? 297 THR B CB  1 
ATOM   5655  O  OG1 . THR B  1 266 ? 5.83200   -30.27000 24.30200  1.000 52.48000  ? 297 THR B OG1 1 
ATOM   5656  C  CG2 . THR B  1 266 ? 8.23100   -30.45200 24.36700  1.000 47.66000  ? 297 THR B CG2 1 
ATOM   5657  N  N   . LEU B  1 267 ? 8.42700   -27.70800 21.72100  1.000 51.22000  ? 298 LEU B N   1 
ATOM   5658  C  CA  . LEU B  1 267 ? 9.63100   -27.20400 21.07300  1.000 47.68000  ? 298 LEU B CA  1 
ATOM   5659  C  C   . LEU B  1 267 ? 9.95800   -25.79300 21.54600  1.000 46.28000  ? 298 LEU B C   1 
ATOM   5660  O  O   . LEU B  1 267 ? 11.12900  -25.44300 21.73700  1.000 46.72000  ? 298 LEU B O   1 
ATOM   5661  C  CB  . LEU B  1 267 ? 9.47400   -27.24000 19.55500  1.000 41.84000  ? 298 LEU B CB  1 
ATOM   5662  C  CG  . LEU B  1 267 ? 9.54500   -28.62600 18.91000  1.000 41.34000  ? 298 LEU B CG  1 
ATOM   5663  C  CD1 . LEU B  1 267 ? 9.18200   -28.58200 17.41000  1.000 39.69000  ? 298 LEU B CD1 1 
ATOM   5664  C  CD2 . LEU B  1 267 ? 10.92800  -29.21300 19.11100  1.000 45.03000  ? 298 LEU B CD2 1 
ATOM   5665  N  N   . LYS B  1 268 ? 8.93700   -24.98000 21.78200  1.000 48.31000  ? 299 LYS B N   1 
ATOM   5666  C  CA  . LYS B  1 268 ? 9.20300   -23.61200 22.19800  1.000 47.48000  ? 299 LYS B CA  1 
ATOM   5667  C  C   . LYS B  1 268 ? 9.65600   -23.54500 23.65500  1.000 52.87000  ? 299 LYS B C   1 
ATOM   5668  O  O   . LYS B  1 268 ? 10.60500  -22.81500 23.98200  1.000 47.82000  ? 299 LYS B O   1 
ATOM   5669  C  CB  . LYS B  1 268 ? 7.95300   -22.76800 21.97900  1.000 50.02000  ? 299 LYS B CB  1 
ATOM   5670  C  CG  . LYS B  1 268 ? 7.59800   -22.54500 20.51800  1.000 48.73000  ? 299 LYS B CG  1 
ATOM   5671  C  CD  . LYS B  1 268 ? 6.37700   -21.68600 20.41900  1.000 45.79000  ? 299 LYS B CD  1 
ATOM   5672  C  CE  . LYS B  1 268 ? 6.17600   -21.19600 18.99200  1.000 57.72000  ? 299 LYS B CE  1 
ATOM   5673  N  NZ  . LYS B  1 268 ? 5.09500   -20.16800 18.91900  1.000 57.15000  ? 299 LYS B NZ  1 
ATOM   5674  N  N   . GLU B  1 269 ? 9.03300   -24.34700 24.52600  1.000 47.81000  ? 300 GLU B N   1 
ATOM   5675  C  CA  . GLU B  1 269 ? 9.42900   -24.34200 25.92800  1.000 55.31000  ? 300 GLU B CA  1 
ATOM   5676  C  C   . GLU B  1 269 ? 10.87300  -24.79000 26.08300  1.000 52.91000  ? 300 GLU B C   1 
ATOM   5677  O  O   . GLU B  1 269 ? 11.63300  -24.17700 26.83800  1.000 53.60000  ? 300 GLU B O   1 
ATOM   5678  C  CB  . GLU B  1 269 ? 8.49400   -25.22400 26.75400  1.000 48.58000  ? 300 GLU B CB  1 
ATOM   5679  C  CG  . GLU B  1 269 ? 7.02600   -24.86200 26.58900  1.000 63.33000  ? 300 GLU B CG  1 
ATOM   5680  C  CD  . GLU B  1 269 ? 6.24800   -24.94300 27.88600  1.000 70.82000  ? 300 GLU B CD  1 
ATOM   5681  O  OE1 . GLU B  1 269 ? 6.74800   -24.42500 28.91400  1.000 83.19000  ? 300 GLU B OE1 1 
ATOM   5682  O  OE2 . GLU B  1 269 ? 5.14100   -25.52500 27.87800  1.000 66.08000  ? 300 GLU B OE2 1 
ATOM   5683  N  N   . THR B  1 270 ? 11.27400  -25.84400 25.36400  1.000 47.15000  ? 301 THR B N   1 
ATOM   5684  C  CA  . THR B  1 270 ? 12.65600  -26.30000 25.37300  1.000 46.20000  ? 301 THR B CA  1 
ATOM   5685  C  C   . THR B  1 270 ? 13.56400  -25.48000 24.47600  1.000 46.70000  ? 301 THR B C   1 
ATOM   5686  O  O   . THR B  1 270 ? 14.71900  -25.87100 24.28100  1.000 50.92000  ? 301 THR B O   1 
ATOM   5687  C  CB  . THR B  1 270 ? 12.75200  -27.78000 24.98000  1.000 51.95000  ? 301 THR B CB  1 
ATOM   5688  O  OG1 . THR B  1 270 ? 12.27400  -27.97500 23.63800  1.000 54.97000  ? 301 THR B OG1 1 
ATOM   5689  C  CG2 . THR B  1 270 ? 11.98900  -28.64500 25.95000  1.000 48.64000  ? 301 THR B CG2 1 
ATOM   5690  N  N   . LYS B  1 271 ? 13.08300  -24.36900 23.92300  1.000 49.38000  ? 302 LYS B N   1 
ATOM   5691  C  CA  . LYS B  1 271 ? 13.90700  -23.51500 23.06300  1.000 50.11000  ? 302 LYS B CA  1 
ATOM   5692  C  C   . LYS B  1 271 ? 14.55400  -24.31400 21.92000  1.000 54.84000  ? 302 LYS B C   1 
ATOM   5693  O  O   . LYS B  1 271 ? 15.66400  -24.01800 21.47600  1.000 46.83000  ? 302 LYS B O   1 
ATOM   5694  C  CB  . LYS B  1 271 ? 14.97000  -22.76600 23.89800  1.000 47.65000  ? 302 LYS B CB  1 
ATOM   5695  N  N   . GLN B  1 272 ? 13.88000  -25.35600 21.42900  1.000 54.78000  ? 303 GLN B N   1 
ATOM   5696  C  CA  . GLN B  1 272 ? 14.39200  -26.07800 20.27200  1.000 49.44000  ? 303 GLN B CA  1 
ATOM   5697  C  C   . GLN B  1 272 ? 13.66200  -25.69800 18.98200  1.000 48.23000  ? 303 GLN B C   1 
ATOM   5698  O  O   . GLN B  1 272 ? 14.03700  -26.16800 17.90900  1.000 51.38000  ? 303 GLN B O   1 
ATOM   5699  C  CB  . GLN B  1 272 ? 14.32100  -27.58600 20.52400  1.000 48.02000  ? 303 GLN B CB  1 
ATOM   5700  C  CG  . GLN B  1 272 ? 15.20600  -28.03300 21.67800  1.000 48.45000  ? 303 GLN B CG  1 
ATOM   5701  C  CD  . GLN B  1 272 ? 16.68200  -27.63400 21.49300  1.000 61.48000  ? 303 GLN B CD  1 
ATOM   5702  O  OE1 . GLN B  1 272 ? 17.31000  -27.92400 20.46400  1.000 56.79000  ? 303 GLN B OE1 1 
ATOM   5703  N  NE2 . GLN B  1 272 ? 17.22200  -26.91900 22.47900  1.000 60.57000  ? 303 GLN B NE2 1 
ATOM   5704  N  N   . PHE B  1 273 ? 12.65300  -24.83500 19.06800  1.000 47.70000  ? 304 PHE B N   1 
ATOM   5705  C  CA  . PHE B  1 273 ? 11.78400  -24.54200 17.92900  1.000 49.60000  ? 304 PHE B CA  1 
ATOM   5706  C  C   . PHE B  1 273 ? 12.55300  -23.87700 16.78600  1.000 52.53000  ? 304 PHE B C   1 
ATOM   5707  O  O   . PHE B  1 273 ? 12.43000  -24.28000 15.62400  1.000 47.88000  ? 304 PHE B O   1 
ATOM   5708  C  CB  . PHE B  1 273 ? 10.62100  -23.66400 18.39400  1.000 50.96000  ? 304 PHE B CB  1 
ATOM   5709  C  CG  . PHE B  1 273 ? 9.55200   -23.41900 17.34400  1.000 50.55000  ? 304 PHE B CG  1 
ATOM   5710  C  CD1 . PHE B  1 273 ? 8.80100   -24.46800 16.83900  1.000 51.30000  ? 304 PHE B CD1 1 
ATOM   5711  C  CD2 . PHE B  1 273 ? 9.25000   -22.12600 16.93100  1.000 45.64000  ? 304 PHE B CD2 1 
ATOM   5712  C  CE1 . PHE B  1 273 ? 7.80100   -24.23800 15.89800  1.000 49.08000  ? 304 PHE B CE1 1 
ATOM   5713  C  CE2 . PHE B  1 273 ? 8.24900   -21.88200 16.00900  1.000 47.25000  ? 304 PHE B CE2 1 
ATOM   5714  C  CZ  . PHE B  1 273 ? 7.52100   -22.93700 15.48900  1.000 45.28000  ? 304 PHE B CZ  1 
ATOM   5715  N  N   . ASP B  1 274 ? 13.35000  -22.84800 17.09400  1.000 47.03000  ? 305 ASP B N   1 
ATOM   5716  C  CA  . ASP B  1 274 ? 13.94500  -22.03300 16.03600  1.000 55.59000  ? 305 ASP B CA  1 
ATOM   5717  C  C   . ASP B  1 274 ? 14.92700  -22.83300 15.17600  1.000 52.83000  ? 305 ASP B C   1 
ATOM   5718  O  O   . ASP B  1 274 ? 14.99000  -22.64200 13.95000  1.000 46.00000  ? 305 ASP B O   1 
ATOM   5719  C  CB  . ASP B  1 274 ? 14.64000  -20.82100 16.66500  1.000 53.11000  ? 305 ASP B CB  1 
ATOM   5720  C  CG  . ASP B  1 274 ? 15.42700  -19.98300 15.64900  1.000 63.69000  ? 305 ASP B CG  1 
ATOM   5721  O  OD1 . ASP B  1 274 ? 16.62600  -20.29500 15.40300  1.000 69.53000  ? 305 ASP B OD1 1 
ATOM   5722  O  OD2 . ASP B  1 274 ? 14.84900  -19.01100 15.09600  1.000 61.96000  ? 305 ASP B OD2 1 
ATOM   5723  N  N   . ASN B  1 275 ? 15.66700  -23.75500 15.78900  1.000 48.02000  ? 306 ASN B N   1 
ATOM   5724  C  CA  . ASN B  1 275 ? 16.66100  -24.57000 15.10300  1.000 48.94000  ? 306 ASN B CA  1 
ATOM   5725  C  C   . ASN B  1 275 ? 16.20900  -26.02300 14.93300  1.000 44.38000  ? 306 ASN B C   1 
ATOM   5726  O  O   . ASN B  1 275 ? 17.02800  -26.94900 14.96800  1.000 41.84000  ? 306 ASN B O   1 
ATOM   5727  C  CB  . ASN B  1 275 ? 18.01400  -24.50500 15.82300  1.000 46.80000  ? 306 ASN B CB  1 
ATOM   5728  C  CG  . ASN B  1 275 ? 19.15600  -24.95500 14.93800  1.000 47.79000  ? 306 ASN B CG  1 
ATOM   5729  O  OD1 . ASN B  1 275 ? 19.11900  -24.75800 13.72200  1.000 52.29000  ? 306 ASN B OD1 1 
ATOM   5730  N  ND2 . ASN B  1 275 ? 20.14700  -25.61500 15.52700  1.000 47.74000  ? 306 ASN B ND2 1 
ATOM   5731  N  N   . THR B  1 276 ? 14.91300  -26.25800 14.71800  1.000 46.47000  ? 307 THR B N   1 
ATOM   5732  C  CA  . THR B  1 276 ? 14.42700  -27.58200 14.33800  1.000 42.78000  ? 307 THR B CA  1 
ATOM   5733  C  C   . THR B  1 276 ? 13.90200  -27.52800 12.90900  1.000 37.34000  ? 307 THR B C   1 
ATOM   5734  O  O   . THR B  1 276 ? 13.11900  -26.63500 12.56300  1.000 38.28000  ? 307 THR B O   1 
ATOM   5735  C  CB  . THR B  1 276 ? 13.33800  -28.09700 15.29100  1.000 46.33000  ? 307 THR B CB  1 
ATOM   5736  O  OG1 . THR B  1 276 ? 13.88700  -28.31900 16.59500  1.000 43.67000  ? 307 THR B OG1 1 
ATOM   5737  C  CG2 . THR B  1 276 ? 12.77800  -29.42800 14.79500  1.000 38.17000  ? 307 THR B CG2 1 
ATOM   5738  N  N   . LEU B  1 277 ? 14.36400  -28.44800 12.06500  1.000 41.19000  ? 308 LEU B N   1 
ATOM   5739  C  CA  . LEU B  1 277 ? 13.78000  -28.60200 10.72800  1.000 40.75000  ? 308 LEU B CA  1 
ATOM   5740  C  C   . LEU B  1 277 ? 12.59600  -29.55100 10.86400  1.000 37.16000  ? 308 LEU B C   1 
ATOM   5741  O  O   . LEU B  1 277 ? 12.77500  -30.73700 11.15300  1.000 40.43000  ? 308 LEU B O   1 
ATOM   5742  C  CB  . LEU B  1 277 ? 14.79500  -29.13300 9.71000   1.000 41.72000  ? 308 LEU B CB  1 
ATOM   5743  C  CG  . LEU B  1 277 ? 14.22300  -29.58200 8.34000   1.000 44.12000  ? 308 LEU B CG  1 
ATOM   5744  C  CD1 . LEU B  1 277 ? 13.56900  -28.42300 7.58600   1.000 33.99000  ? 308 LEU B CD1 1 
ATOM   5745  C  CD2 . LEU B  1 277 ? 15.27700  -30.22100 7.42500   1.000 36.72000  ? 308 LEU B CD2 1 
ATOM   5746  N  N   . ILE B  1 278 ? 11.38700  -29.03200 10.70000  1.000 37.07000  ? 309 ILE B N   1 
ATOM   5747  C  CA  . ILE B  1 278 ? 10.19200  -29.86300 10.73900  1.000 36.34000  ? 309 ILE B CA  1 
ATOM   5748  C  C   . ILE B  1 278 ? 9.79000   -30.14800 9.31200   1.000 41.70000  ? 309 ILE B C   1 
ATOM   5749  O  O   . ILE B  1 278 ? 9.52900   -29.20700 8.54800   1.000 38.50000  ? 309 ILE B O   1 
ATOM   5750  C  CB  . ILE B  1 278 ? 9.04100   -29.19200 11.50100  1.000 41.42000  ? 309 ILE B CB  1 
ATOM   5751  C  CG1 . ILE B  1 278 ? 9.44500   -28.89200 12.95000  1.000 35.26000  ? 309 ILE B CG1 1 
ATOM   5752  C  CG2 . ILE B  1 278 ? 7.77500   -30.06900 11.42000  1.000 33.58000  ? 309 ILE B CG2 1 
ATOM   5753  C  CD1 . ILE B  1 278 ? 8.39000   -28.13100 13.71800  1.000 30.06000  ? 309 ILE B CD1 1 
ATOM   5754  N  N   . VAL B  1 279 ? 9.74200   -31.43400 8.95100   1.000 35.16000  ? 310 VAL B N   1 
ATOM   5755  C  CA  . VAL B  1 279 ? 9.26800   -31.84800 7.63500   1.000 37.37000  ? 310 VAL B CA  1 
ATOM   5756  C  C   . VAL B  1 279 ? 7.95500   -32.60100 7.81000   1.000 37.40000  ? 310 VAL B C   1 
ATOM   5757  O  O   . VAL B  1 279 ? 7.90600   -33.61800 8.51100   1.000 35.75000  ? 310 VAL B O   1 
ATOM   5758  C  CB  . VAL B  1 279 ? 10.29400  -32.72500 6.90100   1.000 41.16000  ? 310 VAL B CB  1 
ATOM   5759  C  CG1 . VAL B  1 279 ? 9.73500   -33.17600 5.51200   1.000 32.35000  ? 310 VAL B CG1 1 
ATOM   5760  C  CG2 . VAL B  1 279 ? 11.60100  -31.99800 6.74400   1.000 36.51000  ? 310 VAL B CG2 1 
ATOM   5761  N  N   . PHE B  1 280 ? 6.90400   -32.13200 7.14800   1.000 35.04000  ? 311 PHE B N   1 
ATOM   5762  C  CA  . PHE B  1 280 ? 5.60200   -32.77800 7.19100   1.000 31.34000  ? 311 PHE B CA  1 
ATOM   5763  C  C   . PHE B  1 280 ? 5.20900   -33.22500 5.79300   1.000 33.79000  ? 311 PHE B C   1 
ATOM   5764  O  O   . PHE B  1 280 ? 5.30500   -32.43600 4.84400   1.000 35.11000  ? 311 PHE B O   1 
ATOM   5765  C  CB  . PHE B  1 280 ? 4.54200   -31.83000 7.76900   1.000 33.85000  ? 311 PHE B CB  1 
ATOM   5766  C  CG  . PHE B  1 280 ? 3.14100   -32.29900 7.53700   1.000 34.77000  ? 311 PHE B CG  1 
ATOM   5767  C  CD1 . PHE B  1 280 ? 2.53400   -33.17900 8.41100   1.000 35.59000  ? 311 PHE B CD1 1 
ATOM   5768  C  CD2 . PHE B  1 280 ? 2.45300   -31.90600 6.40200   1.000 31.71000  ? 311 PHE B CD2 1 
ATOM   5769  C  CE1 . PHE B  1 280 ? 1.23200   -33.65400 8.16000   1.000 35.47000  ? 311 PHE B CE1 1 
ATOM   5770  C  CE2 . PHE B  1 280 ? 1.15900   -32.36200 6.15100   1.000 38.90000  ? 311 PHE B CE2 1 
ATOM   5771  C  CZ  . PHE B  1 280 ? 0.55000   -33.23200 7.03200   1.000 36.00000  ? 311 PHE B CZ  1 
ATOM   5772  N  N   . LEU B  1 281 ? 4.72900   -34.46400 5.66600   1.000 31.52000  ? 312 LEU B N   1 
ATOM   5773  C  CA  . LEU B  1 281 ? 4.28500   -34.97900 4.37300   1.000 35.28000  ? 312 LEU B CA  1 
ATOM   5774  C  C   . LEU B  1 281 ? 3.38600   -36.19100 4.59200   1.000 37.49000  ? 312 LEU B C   1 
ATOM   5775  O  O   . LEU B  1 281 ? 3.20000   -36.65400 5.71200   1.000 36.33000  ? 312 LEU B O   1 
ATOM   5776  C  CB  . LEU B  1 281 ? 5.46100   -35.33500 3.45600   1.000 34.63000  ? 312 LEU B CB  1 
ATOM   5777  C  CG  . LEU B  1 281 ? 6.21800   -36.63200 3.72400   1.000 40.68000  ? 312 LEU B CG  1 
ATOM   5778  C  CD1 . LEU B  1 281 ? 7.00400   -37.07400 2.47000   1.000 36.89000  ? 312 LEU B CD1 1 
ATOM   5779  C  CD2 . LEU B  1 281 ? 7.12400   -36.49700 4.91100   1.000 34.60000  ? 312 LEU B CD2 1 
ATOM   5780  N  N   . SER B  1 282 ? 2.77200   -36.65700 3.50500   1.000 37.64000  ? 313 SER B N   1 
ATOM   5781  C  CA  . SER B  1 282 ? 2.05700   -37.92400 3.48000   1.000 38.27000  ? 313 SER B CA  1 
ATOM   5782  C  C   . SER B  1 282 ? 2.88500   -39.00800 2.79100   1.000 39.76000  ? 313 SER B C   1 
ATOM   5783  O  O   . SER B  1 282 ? 3.72700   -38.71800 1.94000   1.000 31.46000  ? 313 SER B O   1 
ATOM   5784  C  CB  . SER B  1 282 ? 0.72700   -37.78400 2.75700   1.000 35.07000  ? 313 SER B CB  1 
ATOM   5785  O  OG  . SER B  1 282 ? 0.10000   -39.03200 2.80700   1.000 34.97000  ? 313 SER B OG  1 
ATOM   5786  N  N   . ASP B  1 283 ? 2.64700   -40.27300 3.16200   1.000 34.74000  ? 314 ASP B N   1 
ATOM   5787  C  CA  . ASP B  1 283 ? 3.47400   -41.31800 2.56800   1.000 34.12000  ? 314 ASP B CA  1 
ATOM   5788  C  C   . ASP B  1 283 ? 2.98900   -41.75000 1.19000   1.000 38.14000  ? 314 ASP B C   1 
ATOM   5789  O  O   . ASP B  1 283 ? 3.73400   -42.43300 0.47900   1.000 35.92000  ? 314 ASP B O   1 
ATOM   5790  C  CB  . ASP B  1 283 ? 3.56800   -42.54300 3.47900   1.000 38.78000  ? 314 ASP B CB  1 
ATOM   5791  C  CG  . ASP B  1 283 ? 2.25600   -43.33000 3.56400   1.000 43.13000  ? 314 ASP B CG  1 
ATOM   5792  O  OD1 . ASP B  1 283 ? 1.15400   -42.75200 3.41000   1.000 41.69000  ? 314 ASP B OD1 1 
ATOM   5793  O  OD2 . ASP B  1 283 ? 2.34100   -44.54700 3.80500   1.000 43.60000  ? 314 ASP B OD2 1 
ATOM   5794  N  N   . ASN B  1 284 ? 1.76200   -41.40200 0.81100   1.000 35.50000  ? 315 ASN B N   1 
ATOM   5795  C  CA  . ASN B  1 284 ? 1.24100   -41.68300 -0.51900  1.000 31.69000  ? 315 ASN B CA  1 
ATOM   5796  C  C   . ASN B  1 284 ? -0.06100  -40.89400 -0.63000  1.000 35.20000  ? 315 ASN B C   1 
ATOM   5797  O  O   . ASN B  1 284 ? -0.45200  -40.20600 0.31300   1.000 35.87000  ? 315 ASN B O   1 
ATOM   5798  C  CB  . ASN B  1 284 ? 1.05600   -43.18600 -0.74200  1.000 39.57000  ? 315 ASN B CB  1 
ATOM   5799  C  CG  . ASN B  1 284 ? 0.19200   -43.83400 0.32100   1.000 39.62000  ? 315 ASN B CG  1 
ATOM   5800  O  OD1 . ASN B  1 284 ? -1.01800  -43.53500 0.44900   1.000 40.84000  ? 315 ASN B OD1 1 
ATOM   5801  N  ND2 . ASN B  1 284 ? 0.78200   -44.75600 1.05800   1.000 33.29000  ? 315 ASN B ND2 1 
ATOM   5802  N  N   . GLY B  1 285 ? -0.69100  -40.93000 -1.80700  1.000 29.26000  ? 316 GLY B N   1 
ATOM   5803  C  CA  . GLY B  1 285 ? -1.92900  -40.19700 -2.00500  1.000 28.40000  ? 316 GLY B CA  1 
ATOM   5804  C  C   . GLY B  1 285 ? -3.06900  -40.78000 -1.19000  1.000 35.69000  ? 316 GLY B C   1 
ATOM   5805  O  O   . GLY B  1 285 ? -3.03200  -41.92700 -0.74700  1.000 37.28000  ? 316 GLY B O   1 
ATOM   5806  N  N   . GLY B  1 286 ? -4.10600  -39.97600 -0.98300  1.000 36.43000  ? 317 GLY B N   1 
ATOM   5807  C  CA  . GLY B  1 286 ? -5.25500  -40.44800 -0.22600  1.000 32.26000  ? 317 GLY B CA  1 
ATOM   5808  C  C   . GLY B  1 286 ? -6.03000  -41.52700 -0.96300  1.000 34.90000  ? 317 GLY B C   1 
ATOM   5809  O  O   . GLY B  1 286 ? -6.10700  -41.54900 -2.19400  1.000 32.35000  ? 317 GLY B O   1 
ATOM   5810  N  N   . ASN B  1 287 ? -6.61300  -42.44600 -0.18600  1.000 33.36000  ? 318 ASN B N   1 
ATOM   5811  C  CA  . ASN B  1 287 ? -7.52000  -43.46000 -0.71400  1.000 30.94000  ? 318 ASN B CA  1 
ATOM   5812  C  C   . ASN B  1 287 ? -8.90600  -42.83700 -0.74000  1.000 37.42000  ? 318 ASN B C   1 
ATOM   5813  O  O   . ASN B  1 287 ? -9.50400  -42.61700 0.31700   1.000 40.93000  ? 318 ASN B O   1 
ATOM   5814  C  CB  . ASN B  1 287 ? -7.51000  -44.72400 0.14300   1.000 32.27000  ? 318 ASN B CB  1 
ATOM   5815  C  CG  . ASN B  1 287 ? -8.36000  -45.85100 -0.45500  1.000 40.37000  ? 318 ASN B CG  1 
ATOM   5816  O  OD1 . ASN B  1 287 ? -9.36900  -45.60800 -1.15300  1.000 39.13000  ? 318 ASN B OD1 1 
ATOM   5817  N  ND2 . ASN B  1 287 ? -7.98300  -47.09100 -0.14900  1.000 32.99000  ? 318 ASN B ND2 1 
ATOM   5818  N  N   . PHE B  1 288 ? -9.42700  -42.53900 -1.94500  1.000 33.98000  ? 319 PHE B N   1 
ATOM   5819  C  CA  . PHE B  1 288 ? -10.70400 -41.83400 -1.94400  1.000 34.98000  ? 319 PHE B CA  1 
ATOM   5820  C  C   . PHE B  1 288 ? -11.90100 -42.75500 -1.70400  1.000 30.30000  ? 319 PHE B C   1 
ATOM   5821  O  O   . PHE B  1 288 ? -13.02600 -42.27300 -1.67500  1.000 31.09000  ? 319 PHE B O   1 
ATOM   5822  C  CB  . PHE B  1 288 ? -10.87000 -40.95700 -3.20600  1.000 36.79000  ? 319 PHE B CB  1 
ATOM   5823  C  CG  . PHE B  1 288 ? -10.86700 -41.68200 -4.56000  1.000 38.06000  ? 319 PHE B CG  1 
ATOM   5824  C  CD1 . PHE B  1 288 ? -11.18300 -43.02300 -4.70800  1.000 30.15000  ? 319 PHE B CD1 1 
ATOM   5825  C  CD2 . PHE B  1 288 ? -10.57500 -40.94000 -5.71500  1.000 38.96000  ? 319 PHE B CD2 1 
ATOM   5826  C  CE1 . PHE B  1 288 ? -11.20400 -43.61700 -5.97800  1.000 37.13000  ? 319 PHE B CE1 1 
ATOM   5827  C  CE2 . PHE B  1 288 ? -10.58700 -41.52200 -6.98800  1.000 38.40000  ? 319 PHE B CE2 1 
ATOM   5828  C  CZ  . PHE B  1 288 ? -10.89500 -42.86600 -7.12300  1.000 40.49000  ? 319 PHE B CZ  1 
ATOM   5829  N  N   . ASN B  1 289 ? -11.68100 -44.03900 -1.45700  1.000 34.12000  ? 320 ASN B N   1 
ATOM   5830  C  CA  . ASN B  1 289 ? -12.73000 -44.92600 -0.97100  1.000 38.42000  ? 320 ASN B CA  1 
ATOM   5831  C  C   . ASN B  1 289 ? -12.92700 -44.86600 0.54000   1.000 43.41000  ? 320 ASN B C   1 
ATOM   5832  O  O   . ASN B  1 289 ? -13.91600 -45.42300 1.02800   1.000 40.18000  ? 320 ASN B O   1 
ATOM   5833  C  CB  . ASN B  1 289 ? -12.41700 -46.37800 -1.35400  1.000 34.41000  ? 320 ASN B CB  1 
ATOM   5834  C  CG  . ASN B  1 289 ? -12.40400 -46.57700 -2.84500  1.000 44.71000  ? 320 ASN B CG  1 
ATOM   5835  O  OD1 . ASN B  1 289 ? -13.39900 -46.30500 -3.50800  1.000 42.32000  ? 320 ASN B OD1 1 
ATOM   5836  N  ND2 . ASN B  1 289 ? -11.26900 -46.99200 -3.39000  1.000 42.51000  ? 320 ASN B ND2 1 
ATOM   5837  N  N   . HIS B  1 290 ? -12.00600 -44.23700 1.28500   1.000 41.91000  ? 321 HIS B N   1 
ATOM   5838  C  CA  . HIS B  1 290 ? -11.99100 -44.24100 2.75400   1.000 35.46000  ? 321 HIS B CA  1 
ATOM   5839  C  C   . HIS B  1 290 ? -11.77900 -42.84600 3.30000   1.000 38.48000  ? 321 HIS B C   1 
ATOM   5840  O  O   . HIS B  1 290 ? -10.95500 -42.60300 4.18700   1.000 35.92000  ? 321 HIS B O   1 
ATOM   5841  C  CB  . HIS B  1 290 ? -10.94900 -45.23900 3.25400   1.000 32.76000  ? 321 HIS B CB  1 
ATOM   5842  C  CG  . HIS B  1 290 ? -11.30800 -46.64900 2.91300   1.000 40.42000  ? 321 HIS B CG  1 
ATOM   5843  N  ND1 . HIS B  1 290 ? -10.46200 -47.50400 2.24300   1.000 48.73000  ? 321 HIS B ND1 1 
ATOM   5844  C  CD2 . HIS B  1 290 ? -12.45700 -47.33900 3.11500   1.000 42.98000  ? 321 HIS B CD2 1 
ATOM   5845  C  CE1 . HIS B  1 290 ? -11.07000 -48.66400 2.05000   1.000 44.86000  ? 321 HIS B CE1 1 
ATOM   5846  N  NE2 . HIS B  1 290 ? -12.28200 -48.58800 2.56800   1.000 48.78000  ? 321 HIS B NE2 1 
ATOM   5847  N  N   . GLY B  1 291 ? -12.53700 -41.90300 2.75800   1.000 34.24000  ? 322 GLY B N   1 
ATOM   5848  C  CA  . GLY B  1 291 ? -12.66400 -40.58000 3.32100   1.000 33.48000  ? 322 GLY B CA  1 
ATOM   5849  C  C   . GLY B  1 291 ? -11.74800 -39.53400 2.73100   1.000 38.42000  ? 322 GLY B C   1 
ATOM   5850  O  O   . GLY B  1 291 ? -11.97700 -38.34300 2.96700   1.000 39.63000  ? 322 GLY B O   1 
ATOM   5851  N  N   . ALA B  1 292 ? -10.75500 -39.92200 1.93100   1.000 38.63000  ? 323 ALA B N   1 
ATOM   5852  C  CA  . ALA B  1 292 ? -9.77300  -38.94500 1.48600   1.000 34.67000  ? 323 ALA B CA  1 
ATOM   5853  C  C   . ALA B  1 292 ? -10.26400 -38.19700 0.24900   1.000 31.19000  ? 323 ALA B C   1 
ATOM   5854  O  O   . ALA B  1 292 ? -11.11000 -38.67700 -0.50300  1.000 38.60000  ? 323 ALA B O   1 
ATOM   5855  C  CB  . ALA B  1 292 ? -8.43500  -39.62200 1.18800   1.000 31.30000  ? 323 ALA B CB  1 
ATOM   5856  N  N   . ASN B  1 293 ? -9.69500  -37.01900 0.03100   1.000 36.03000  ? 324 ASN B N   1 
ATOM   5857  C  CA  . ASN B  1 293 ? -9.96300  -36.21500 -1.16100  1.000 36.81000  ? 324 ASN B CA  1 
ATOM   5858  C  C   . ASN B  1 293 ? -8.63500  -35.71000 -1.72100  1.000 34.61000  ? 324 ASN B C   1 
ATOM   5859  O  O   . ASN B  1 293 ? -7.89400  -35.01400 -1.02200  1.000 31.03000  ? 324 ASN B O   1 
ATOM   5860  C  CB  . ASN B  1 293 ? -10.90300 -35.05300 -0.83800  1.000 33.70000  ? 324 ASN B CB  1 
ATOM   5861  C  CG  . ASN B  1 293 ? -11.29300 -34.24300 -2.06900  1.000 41.39000  ? 324 ASN B CG  1 
ATOM   5862  O  OD1 . ASN B  1 293 ? -10.61400 -34.26300 -3.09000  1.000 43.66000  ? 324 ASN B OD1 1 
ATOM   5863  N  ND2 . ASN B  1 293 ? -12.39800 -33.52400 -1.96600  1.000 47.58000  ? 324 ASN B ND2 1 
ATOM   5864  N  N   . ASN B  1 294 ? -8.34800  -36.04000 -2.98200  1.000 34.91000  ? 325 ASN B N   1 
ATOM   5865  C  CA  . ASN B  1 294 ? -7.08800  -35.69100 -3.63300  1.000 35.71000  ? 325 ASN B CA  1 
ATOM   5866  C  C   . ASN B  1 294 ? -7.21800  -34.50700 -4.59800  1.000 41.52000  ? 325 ASN B C   1 
ATOM   5867  O  O   . ASN B  1 294 ? -6.31500  -34.29600 -5.42900  1.000 33.31000  ? 325 ASN B O   1 
ATOM   5868  C  CB  . ASN B  1 294 ? -6.50700  -36.90200 -4.36800  1.000 32.91000  ? 325 ASN B CB  1 
ATOM   5869  C  CG  . ASN B  1 294 ? -6.02400  -37.99300 -3.41000  1.000 37.05000  ? 325 ASN B CG  1 
ATOM   5870  O  OD1 . ASN B  1 294 ? -5.52300  -37.68700 -2.33700  1.000 36.98000  ? 325 ASN B OD1 1 
ATOM   5871  N  ND2 . ASN B  1 294 ? -6.15600  -39.26200 -3.80300  1.000 34.06000  ? 325 ASN B ND2 1 
ATOM   5872  N  N   . TYR B  1 295 ? -8.31200  -33.73300 -4.49400  1.000 39.84000  ? 326 TYR B N   1 
ATOM   5873  C  CA  . TYR B  1 295 ? -8.55500  -32.61700 -5.40100  1.000 34.92000  ? 326 TYR B CA  1 
ATOM   5874  C  C   . TYR B  1 295 ? -7.34100  -31.69100 -5.43200  1.000 39.96000  ? 326 TYR B C   1 
ATOM   5875  O  O   . TYR B  1 295 ? -6.73500  -31.44300 -4.38200  1.000 42.15000  ? 326 TYR B O   1 
ATOM   5876  C  CB  . TYR B  1 295 ? -9.77600  -31.82900 -4.93100  1.000 35.96000  ? 326 TYR B CB  1 
ATOM   5877  C  CG  . TYR B  1 295 ? -10.12900 -30.67100 -5.83600  1.000 40.13000  ? 326 TYR B CG  1 
ATOM   5878  C  CD1 . TYR B  1 295 ? -10.96600 -30.85200 -6.93400  1.000 39.24000  ? 326 TYR B CD1 1 
ATOM   5879  C  CD2 . TYR B  1 295 ? -9.60700  -29.40800 -5.60700  1.000 38.72000  ? 326 TYR B CD2 1 
ATOM   5880  C  CE1 . TYR B  1 295 ? -11.28100 -29.79200 -7.76800  1.000 43.17000  ? 326 TYR B CE1 1 
ATOM   5881  C  CE2 . TYR B  1 295 ? -9.91200  -28.35200 -6.42100  1.000 42.05000  ? 326 TYR B CE2 1 
ATOM   5882  C  CZ  . TYR B  1 295 ? -10.74800 -28.54600 -7.50100  1.000 48.88000  ? 326 TYR B CZ  1 
ATOM   5883  O  OH  . TYR B  1 295 ? -11.04100 -27.48900 -8.31200  1.000 53.43000  ? 326 TYR B OH  1 
ATOM   5884  N  N   . PRO B  1 296 ? -6.94400  -31.16900 -6.60000  1.000 38.36000  ? 327 PRO B N   1 
ATOM   5885  C  CA  . PRO B  1 296 ? -7.52700  -31.32500 -7.93900  1.000 37.06000  ? 327 PRO B CA  1 
ATOM   5886  C  C   . PRO B  1 296 ? -6.91900  -32.47000 -8.71900  1.000 35.05000  ? 327 PRO B C   1 
ATOM   5887  O  O   . PRO B  1 296 ? -7.05100  -32.50000 -9.92500  1.000 37.68000  ? 327 PRO B O   1 
ATOM   5888  C  CB  . PRO B  1 296 ? -7.17200  -29.99600 -8.61400  1.000 33.33000  ? 327 PRO B CB  1 
ATOM   5889  C  CG  . PRO B  1 296 ? -5.82000  -29.65200 -8.04000  1.000 33.68000  ? 327 PRO B CG  1 
ATOM   5890  C  CD  . PRO B  1 296 ? -5.78900  -30.24600 -6.63200  1.000 34.20000  ? 327 PRO B CD  1 
ATOM   5891  N  N   . LEU B  1 297 ? -6.22300  -33.39200 -8.06500  1.000 33.64000  ? 328 LEU B N   1 
ATOM   5892  C  CA  . LEU B  1 297 ? -5.51800  -34.46500 -8.74300  1.000 34.83000  ? 328 LEU B CA  1 
ATOM   5893  C  C   . LEU B  1 297 ? -6.47400  -35.56600 -9.12200  1.000 33.30000  ? 328 LEU B C   1 
ATOM   5894  O  O   . LEU B  1 297 ? -7.47800  -35.80300 -8.45900  1.000 38.38000  ? 328 LEU B O   1 
ATOM   5895  C  CB  . LEU B  1 297 ? -4.42700  -35.06500 -7.84300  1.000 27.99000  ? 328 LEU B CB  1 
ATOM   5896  C  CG  . LEU B  1 297 ? -3.57700  -34.02400 -7.14200  1.000 33.80000  ? 328 LEU B CG  1 
ATOM   5897  C  CD1 . LEU B  1 297 ? -2.48900  -34.70700 -6.26800  1.000 35.59000  ? 328 LEU B CD1 1 
ATOM   5898  C  CD2 . LEU B  1 297 ? -2.94300  -33.12100 -8.22500  1.000 33.72000  ? 328 LEU B CD2 1 
ATOM   5899  N  N   . LYS B  1 298 ? -6.07700  -36.32600 -10.12200 1.000 33.96000  ? 329 LYS B N   1 
ATOM   5900  C  CA  . LYS B  1 298 ? -6.83100  -37.47400 -10.56700 1.000 33.66000  ? 329 LYS B CA  1 
ATOM   5901  C  C   . LYS B  1 298 ? -6.36600  -38.70000 -9.79600  1.000 33.58000  ? 329 LYS B C   1 
ATOM   5902  O  O   . LYS B  1 298 ? -5.19500  -38.81100 -9.39900  1.000 32.95000  ? 329 LYS B O   1 
ATOM   5903  C  CB  . LYS B  1 298 ? -6.65900  -37.66100 -12.08400 1.000 32.23000  ? 329 LYS B CB  1 
ATOM   5904  C  CG  . LYS B  1 298 ? -7.31200  -38.91500 -12.64700 1.000 38.97000  ? 329 LYS B CG  1 
ATOM   5905  C  CD  . LYS B  1 298 ? -7.02700  -39.09000 -14.14600 1.000 38.93000  ? 329 LYS B CD  1 
ATOM   5906  C  CE  . LYS B  1 298 ? -8.00900  -38.36300 -15.01100 1.000 37.36000  ? 329 LYS B CE  1 
ATOM   5907  N  NZ  . LYS B  1 298 ? -7.72300  -38.62100 -16.43000 1.000 43.73000  ? 329 LYS B NZ  1 
ATOM   5908  N  N   . GLY B  1 299 ? -7.29600  -39.58900 -9.51800  1.000 33.98000  ? 330 GLY B N   1 
ATOM   5909  C  CA  . GLY B  1 299 ? -6.91700  -40.86900 -8.95800  1.000 32.34000  ? 330 GLY B CA  1 
ATOM   5910  C  C   . GLY B  1 299 ? -6.79000  -40.91000 -7.44400  1.000 40.63000  ? 330 GLY B C   1 
ATOM   5911  O  O   . GLY B  1 299 ? -7.11400  -39.97200 -6.69100  1.000 34.41000  ? 330 GLY B O   1 
ATOM   5912  N  N   . THR B  1 300 ? -6.23700  -42.03900 -7.00000  1.000 35.68000  ? 331 THR B N   1 
ATOM   5913  C  CA  . THR B  1 300 ? -6.32500  -42.46300 -5.61300  1.000 33.95000  ? 331 THR B CA  1 
ATOM   5914  C  C   . THR B  1 300 ? -5.05200  -43.22300 -5.23200  1.000 37.80000  ? 331 THR B C   1 
ATOM   5915  O  O   . THR B  1 300 ? -4.24000  -43.58700 -6.08400  1.000 34.31000  ? 331 THR B O   1 
ATOM   5916  C  CB  . THR B  1 300 ? -7.54700  -43.34700 -5.44100  1.000 36.48000  ? 331 THR B CB  1 
ATOM   5917  O  OG1 . THR B  1 300 ? -7.75900  -43.67200 -4.06400  1.000 29.42000  ? 331 THR B OG1 1 
ATOM   5918  C  CG2 . THR B  1 300 ? -7.35700  -44.62700 -6.27100  1.000 36.35000  ? 331 THR B CG2 1 
ATOM   5919  N  N   . LYS B  1 301 ? -4.90700  -43.48400 -3.93800  1.000 35.51000  ? 332 LYS B N   1 
ATOM   5920  C  CA  . LYS B  1 301 ? -3.80000  -44.27600 -3.42500  1.000 40.25000  ? 332 LYS B CA  1 
ATOM   5921  C  C   . LYS B  1 301 ? -3.55700  -45.48200 -4.31200  1.000 40.07000  ? 332 LYS B C   1 
ATOM   5922  O  O   . LYS B  1 301 ? -4.49500  -46.19700 -4.66600  1.000 35.19000  ? 332 LYS B O   1 
ATOM   5923  C  CB  . LYS B  1 301 ? -4.11900  -44.74500 -2.01100  1.000 36.43000  ? 332 LYS B CB  1 
ATOM   5924  C  CG  . LYS B  1 301 ? -3.20800  -45.84600 -1.49900  1.000 36.43000  ? 332 LYS B CG  1 
ATOM   5925  C  CD  . LYS B  1 301 ? -3.62700  -46.20900 -0.09400  1.000 39.19000  ? 332 LYS B CD  1 
ATOM   5926  C  CE  . LYS B  1 301 ? -2.81900  -47.35900 0.48800   1.000 42.08000  ? 332 LYS B CE  1 
ATOM   5927  N  NZ  . LYS B  1 301 ? -3.15000  -47.64600 1.91500   1.000 47.32000  ? 332 LYS B NZ  1 
ATOM   5928  N  N   . GLY B  1 302 ? -2.30400  -45.69000 -4.68600  1.000 31.08000  ? 333 GLY B N   1 
ATOM   5929  C  CA  . GLY B  1 302 ? -1.91900  -46.82300 -5.49500  1.000 31.36000  ? 333 GLY B CA  1 
ATOM   5930  C  C   . GLY B  1 302 ? -1.72500  -46.53300 -6.97300  1.000 32.36000  ? 333 GLY B C   1 
ATOM   5931  O  O   . GLY B  1 302 ? -1.11600  -47.35600 -7.66300  1.000 34.61000  ? 333 GLY B O   1 
ATOM   5932  N  N   . ASP B  1 303 ? -2.22000  -45.39700 -7.46900  1.000 33.35000  ? 334 ASP B N   1 
ATOM   5933  C  CA  . ASP B  1 303 ? -2.18900  -45.02500 -8.88000  1.000 39.34000  ? 334 ASP B CA  1 
ATOM   5934  C  C   . ASP B  1 303 ? -0.88600  -44.29700 -9.22000  1.000 36.64000  ? 334 ASP B C   1 
ATOM   5935  O  O   . ASP B  1 303 ? -0.28300  -43.64900 -8.36600  1.000 28.54000  ? 334 ASP B O   1 
ATOM   5936  C  CB  . ASP B  1 303 ? -3.33900  -44.08400 -9.26000  1.000 36.69000  ? 334 ASP B CB  1 
ATOM   5937  C  CG  . ASP B  1 303 ? -4.74200  -44.73400 -9.18700  1.000 42.53000  ? 334 ASP B CG  1 
ATOM   5938  O  OD1 . ASP B  1 303 ? -4.84900  -45.97600 -9.19600  1.000 42.11000  ? 334 ASP B OD1 1 
ATOM   5939  O  OD2 . ASP B  1 303 ? -5.74900  -43.97100 -9.19400  1.000 35.51000  ? 334 ASP B OD2 1 
ATOM   5940  N  N   . THR B  1 304 ? -0.51300  -44.33800 -10.50800 1.000 35.05000  ? 335 THR B N   1 
ATOM   5941  C  CA  . THR B  1 304 ? 0.52600   -43.45600 -11.03400 1.000 34.40000  ? 335 THR B CA  1 
ATOM   5942  C  C   . THR B  1 304 ? -0.03800  -42.19800 -11.66000 1.000 37.58000  ? 335 THR B C   1 
ATOM   5943  O  O   . THR B  1 304 ? 0.73900   -41.41100 -12.22600 1.000 34.16000  ? 335 THR B O   1 
ATOM   5944  C  CB  . THR B  1 304 ? 1.42700   -44.16000 -12.04900 1.000 35.07000  ? 335 THR B CB  1 
ATOM   5945  O  OG1 . THR B  1 304 ? 0.63100   -44.75600 -13.07700 1.000 35.11000  ? 335 THR B OG1 1 
ATOM   5946  C  CG2 . THR B  1 304 ? 2.23300   -45.25700 -11.32100 1.000 32.55000  ? 335 THR B CG2 1 
ATOM   5947  N  N   . TRP B  1 305 ? -1.35500  -41.98500 -11.57800 1.000 33.06000  ? 336 TRP B N   1 
ATOM   5948  C  CA  . TRP B  1 305 ? -1.84900  -40.62200 -11.66400 1.000 32.84000  ? 336 TRP B CA  1 
ATOM   5949  C  C   . TRP B  1 305 ? -1.24300  -39.80900 -10.51100 1.000 32.53000  ? 336 TRP B C   1 
ATOM   5950  O  O   . TRP B  1 305 ? -0.86000  -40.36100 -9.47200  1.000 32.00000  ? 336 TRP B O   1 
ATOM   5951  C  CB  . TRP B  1 305 ? -3.37700  -40.57800 -11.56900 1.000 36.20000  ? 336 TRP B CB  1 
ATOM   5952  C  CG  . TRP B  1 305 ? -4.19600  -41.40100 -12.53100 1.000 37.65000  ? 336 TRP B CG  1 
ATOM   5953  C  CD1 . TRP B  1 305 ? -5.03900  -42.42000 -12.20400 1.000 33.67000  ? 336 TRP B CD1 1 
ATOM   5954  C  CD2 . TRP B  1 305 ? -4.29800  -41.23600 -13.95200 1.000 36.67000  ? 336 TRP B CD2 1 
ATOM   5955  N  NE1 . TRP B  1 305 ? -5.65000  -42.91100 -13.32000 1.000 39.50000  ? 336 TRP B NE1 1 
ATOM   5956  C  CE2 . TRP B  1 305 ? -5.22200  -42.20500 -14.41500 1.000 40.98000  ? 336 TRP B CE2 1 
ATOM   5957  C  CE3 . TRP B  1 305 ? -3.69400  -40.37800 -14.87600 1.000 37.76000  ? 336 TRP B CE3 1 
ATOM   5958  C  CZ2 . TRP B  1 305 ? -5.56000  -42.35000 -15.77900 1.000 37.58000  ? 336 TRP B CZ2 1 
ATOM   5959  C  CZ3 . TRP B  1 305 ? -4.02300  -40.51300 -16.23800 1.000 34.59000  ? 336 TRP B CZ3 1 
ATOM   5960  C  CH2 . TRP B  1 305 ? -4.95300  -41.50200 -16.67100 1.000 43.02000  ? 336 TRP B CH2 1 
ATOM   5961  N  N   . GLU B  1 306 ? -1.21200  -38.47700 -10.67000 1.000 31.61000  ? 337 GLU B N   1 
ATOM   5962  C  CA  . GLU B  1 306 ? -0.66800  -37.62800 -9.61000  1.000 28.88000  ? 337 GLU B CA  1 
ATOM   5963  C  C   . GLU B  1 306 ? -1.31400  -37.96900 -8.27500  1.000 37.63000  ? 337 GLU B C   1 
ATOM   5964  O  O   . GLU B  1 306 ? -0.64500  -37.99400 -7.23800  1.000 33.61000  ? 337 GLU B O   1 
ATOM   5965  C  CB  . GLU B  1 306 ? -0.89600  -36.14200 -9.91200  1.000 33.67000  ? 337 GLU B CB  1 
ATOM   5966  C  CG  . GLU B  1 306 ? -0.24300  -35.60100 -11.18400 1.000 34.05000  ? 337 GLU B CG  1 
ATOM   5967  C  CD  . GLU B  1 306 ? 1.25900   -35.58400 -11.10700 1.000 39.93000  ? 337 GLU B CD  1 
ATOM   5968  O  OE1 . GLU B  1 306 ? 1.84400   -34.56600 -10.63200 1.000 41.02000  ? 337 GLU B OE1 1 
ATOM   5969  O  OE2 . GLU B  1 306 ? 1.85000   -36.62300 -11.48300 1.000 36.45000  ? 337 GLU B OE2 1 
ATOM   5970  N  N   . GLY B  1 307 ? -2.60800  -38.29700 -8.29200  1.000 34.09000  ? 338 GLY B N   1 
ATOM   5971  C  CA  . GLY B  1 307 ? -3.29500  -38.54700 -7.03700  1.000 37.11000  ? 338 GLY B CA  1 
ATOM   5972  C  C   . GLY B  1 307 ? -2.71700  -39.68500 -6.22200  1.000 36.15000  ? 338 GLY B C   1 
ATOM   5973  O  O   . GLY B  1 307 ? -2.93700  -39.73400 -5.00300  1.000 35.52000  ? 338 GLY B O   1 
ATOM   5974  N  N   . GLY B  1 308 ? -2.00400  -40.61000 -6.85600  1.000 31.51000  ? 339 GLY B N   1 
ATOM   5975  C  CA  . GLY B  1 308 ? -1.39200  -41.69700 -6.10600  1.000 34.04000  ? 339 GLY B CA  1 
ATOM   5976  C  C   . GLY B  1 308 ? -0.13800  -41.31600 -5.32300  1.000 37.67000  ? 339 GLY B C   1 
ATOM   5977  O  O   . GLY B  1 308 ? 0.09700   -41.84200 -4.22300  1.000 38.15000  ? 339 GLY B O   1 
ATOM   5978  N  N   . TYR B  1 309 ? 0.71800   -40.43800 -5.87400  1.000 29.84000  ? 340 TYR B N   1 
ATOM   5979  C  CA  . TYR B  1 309 ? 2.00400   -40.25200 -5.21700  1.000 34.48000  ? 340 TYR B CA  1 
ATOM   5980  C  C   . TYR B  1 309 ? 2.46400   -38.80000 -5.09800  1.000 33.20000  ? 340 TYR B C   1 
ATOM   5981  O  O   . TYR B  1 309 ? 3.58900   -38.55900 -4.63100  1.000 37.71000  ? 340 TYR B O   1 
ATOM   5982  C  CB  . TYR B  1 309 ? 3.07600   -41.11100 -5.91600  1.000 32.54000  ? 340 TYR B CB  1 
ATOM   5983  C  CG  . TYR B  1 309 ? 3.34500   -40.79100 -7.38400  1.000 37.62000  ? 340 TYR B CG  1 
ATOM   5984  C  CD1 . TYR B  1 309 ? 2.42200   -41.13500 -8.39500  1.000 37.26000  ? 340 TYR B CD1 1 
ATOM   5985  C  CD2 . TYR B  1 309 ? 4.57000   -40.22700 -7.77200  1.000 36.30000  ? 340 TYR B CD2 1 
ATOM   5986  C  CE1 . TYR B  1 309 ? 2.69100   -40.85100 -9.75000  1.000 38.15000  ? 340 TYR B CE1 1 
ATOM   5987  C  CE2 . TYR B  1 309 ? 4.85900   -39.96500 -9.09300  1.000 33.99000  ? 340 TYR B CE2 1 
ATOM   5988  C  CZ  . TYR B  1 309 ? 3.92900   -40.27800 -10.08000 1.000 38.75000  ? 340 TYR B CZ  1 
ATOM   5989  O  OH  . TYR B  1 309 ? 4.24600   -39.98300 -11.37500 1.000 35.29000  ? 340 TYR B OH  1 
ATOM   5990  N  N   . ARG B  1 310 ? 1.63800   -37.83000 -5.45400  1.000 31.70000  ? 341 ARG B N   1 
ATOM   5991  C  CA  . ARG B  1 310 ? 1.91200   -36.43300 -5.14600  1.000 33.54000  ? 341 ARG B CA  1 
ATOM   5992  C  C   . ARG B  1 310 ? 1.20300   -36.05300 -3.83800  1.000 31.82000  ? 341 ARG B C   1 
ATOM   5993  O  O   . ARG B  1 310 ? -0.01600  -36.24500 -3.70500  1.000 33.70000  ? 341 ARG B O   1 
ATOM   5994  C  CB  . ARG B  1 310 ? 1.45400   -35.56700 -6.31100  1.000 34.30000  ? 341 ARG B CB  1 
ATOM   5995  C  CG  . ARG B  1 310 ? 1.85200   -34.13200 -6.27600  1.000 37.15000  ? 341 ARG B CG  1 
ATOM   5996  C  CD  . ARG B  1 310 ? 1.37800   -33.45300 -7.59600  1.000 36.00000  ? 341 ARG B CD  1 
ATOM   5997  N  NE  . ARG B  1 310 ? 1.46800   -31.99700 -7.50600  1.000 41.28000  ? 341 ARG B NE  1 
ATOM   5998  C  CZ  . ARG B  1 310 ? 1.47900   -31.16900 -8.54300  1.000 36.23000  ? 341 ARG B CZ  1 
ATOM   5999  N  NH1 . ARG B  1 310 ? 1.42400   -31.61900 -9.78900  1.000 36.46000  ? 341 ARG B NH1 1 
ATOM   6000  N  NH2 . ARG B  1 310 ? 1.51300   -29.85700 -8.32100  1.000 33.73000  ? 341 ARG B NH2 1 
ATOM   6001  N  N   . VAL B  1 311 ? 1.95800   -35.51400 -2.88400  1.000 35.91000  ? 342 VAL B N   1 
ATOM   6002  C  CA  . VAL B  1 311 ? 1.50200   -35.40600 -1.49500  1.000 36.76000  ? 342 VAL B CA  1 
ATOM   6003  C  C   . VAL B  1 311 ? 1.69700   -33.97300 -1.00900  1.000 36.55000  ? 342 VAL B C   1 
ATOM   6004  O  O   . VAL B  1 311 ? 2.55100   -33.24000 -1.52500  1.000 31.50000  ? 342 VAL B O   1 
ATOM   6005  C  CB  . VAL B  1 311 ? 2.25500   -36.41100 -0.59200  1.000 35.67000  ? 342 VAL B CB  1 
ATOM   6006  C  CG1 . VAL B  1 311 ? 2.04200   -37.86300 -1.11200  1.000 28.12000  ? 342 VAL B CG1 1 
ATOM   6007  C  CG2 . VAL B  1 311 ? 3.75600   -36.08300 -0.55500  1.000 36.23000  ? 342 VAL B CG2 1 
ATOM   6008  N  N   . PRO B  1 312 ? 0.95200   -33.54500 0.01600   1.000 40.03000  ? 343 PRO B N   1 
ATOM   6009  C  CA  . PRO B  1 312 ? 1.27600   -32.26000 0.64800   1.000 35.44000  ? 343 PRO B CA  1 
ATOM   6010  C  C   . PRO B  1 312 ? 2.61100   -32.37900 1.35400   1.000 34.40000  ? 343 PRO B C   1 
ATOM   6011  O  O   . PRO B  1 312 ? 2.97500   -33.44900 1.84600   1.000 32.70000  ? 343 PRO B O   1 
ATOM   6012  C  CB  . PRO B  1 312 ? 0.14600   -32.04400 1.66700   1.000 33.52000  ? 343 PRO B CB  1 
ATOM   6013  C  CG  . PRO B  1 312 ? -0.91700  -33.09100 1.32300   1.000 36.58000  ? 343 PRO B CG  1 
ATOM   6014  C  CD  . PRO B  1 312 ? -0.13400  -34.23700 0.73200   1.000 37.01000  ? 343 PRO B CD  1 
ATOM   6015  N  N   . MET B  1 313 ? 3.34300   -31.26500 1.40200   1.000 32.82000  ? 344 MET B N   1 
ATOM   6016  C  CA  . MET B  1 313 ? 4.62100   -31.26300 2.10200   1.000 34.26000  ? 344 MET B CA  1 
ATOM   6017  C  C   . MET B  1 313 ? 5.06300   -29.83400 2.39400   1.000 39.06000  ? 344 MET B C   1 
ATOM   6018  O  O   . MET B  1 313 ? 4.88700   -28.93700 1.56600   1.000 35.95000  ? 344 MET B O   1 
ATOM   6019  C  CB  . MET B  1 313 ? 5.71600   -31.99800 1.31300   1.000 34.95000  ? 344 MET B CB  1 
ATOM   6020  C  CG  . MET B  1 313 ? 7.04400   -32.02700 2.05900   1.000 35.09000  ? 344 MET B CG  1 
ATOM   6021  S  SD  . MET B  1 313 ? 8.30500   -33.09000 1.36900   1.000 39.36000  ? 344 MET B SD  1 
ATOM   6022  C  CE  . MET B  1 313 ? 9.08500   -31.93000 0.24300   1.000 47.49000  ? 344 MET B CE  1 
ATOM   6023  N  N   . PHE B  1 314 ? 5.63500   -29.62900 3.58000   1.000 42.41000  ? 345 PHE B N   1 
ATOM   6024  C  CA  . PHE B  1 314 ? 6.29100   -28.36600 3.88000   1.000 42.87000  ? 345 PHE B CA  1 
ATOM   6025  C  C   . PHE B  1 314 ? 7.56200   -28.62400 4.66200   1.000 37.43000  ? 345 PHE B C   1 
ATOM   6026  O  O   . PHE B  1 314 ? 7.71600   -29.66400 5.30100   1.000 39.02000  ? 345 PHE B O   1 
ATOM   6027  C  CB  . PHE B  1 314 ? 5.38000   -27.37500 4.64500   1.000 34.22000  ? 345 PHE B CB  1 
ATOM   6028  C  CG  . PHE B  1 314 ? 4.98800   -27.81500 6.03200   1.000 35.82000  ? 345 PHE B CG  1 
ATOM   6029  C  CD1 . PHE B  1 314 ? 5.91200   -27.79300 7.08400   1.000 38.89000  ? 345 PHE B CD1 1 
ATOM   6030  C  CD2 . PHE B  1 314 ? 3.67600   -28.16100 6.31000   1.000 32.84000  ? 345 PHE B CD2 1 
ATOM   6031  C  CE1 . PHE B  1 314 ? 5.55700   -28.18900 8.35500   1.000 35.30000  ? 345 PHE B CE1 1 
ATOM   6032  C  CE2 . PHE B  1 314 ? 3.29500   -28.54600 7.59300   1.000 37.99000  ? 345 PHE B CE2 1 
ATOM   6033  C  CZ  . PHE B  1 314 ? 4.23100   -28.54700 8.62200   1.000 36.91000  ? 345 PHE B CZ  1 
ATOM   6034  N  N   . PHE B  1 315 ? 8.48700   -27.67600 4.55300   1.000 36.60000  ? 346 PHE B N   1 
ATOM   6035  C  CA  . PHE B  1 315 ? 9.65400   -27.56600 5.40800   1.000 36.62000  ? 346 PHE B CA  1 
ATOM   6036  C  C   . PHE B  1 315 ? 9.44600   -26.35900 6.33100   1.000 43.08000  ? 346 PHE B C   1 
ATOM   6037  O  O   . PHE B  1 315 ? 8.98500   -25.29000 5.88400   1.000 36.16000  ? 346 PHE B O   1 
ATOM   6038  C  CB  . PHE B  1 315 ? 10.94900  -27.36800 4.59000   1.000 41.03000  ? 346 PHE B CB  1 
ATOM   6039  C  CG  . PHE B  1 315 ? 11.48600  -28.61300 3.89800   1.000 40.26000  ? 346 PHE B CG  1 
ATOM   6040  C  CD1 . PHE B  1 315 ? 10.69300  -29.74200 3.68900   1.000 38.91000  ? 346 PHE B CD1 1 
ATOM   6041  C  CD2 . PHE B  1 315 ? 12.81800  -28.63200 3.43600   1.000 36.73000  ? 346 PHE B CD2 1 
ATOM   6042  C  CE1 . PHE B  1 315 ? 11.23200  -30.89400 3.03800   1.000 42.26000  ? 346 PHE B CE1 1 
ATOM   6043  C  CE2 . PHE B  1 315 ? 13.36100  -29.76100 2.79600   1.000 37.19000  ? 346 PHE B CE2 1 
ATOM   6044  C  CZ  . PHE B  1 315 ? 12.56700  -30.89800 2.59200   1.000 37.45000  ? 346 PHE B CZ  1 
ATOM   6045  N  N   . HIS B  1 316 ? 9.76300   -26.53000 7.61700   1.000 36.17000  ? 347 HIS B N   1 
ATOM   6046  C  CA  . HIS B  1 316 ? 9.67300   -25.43400 8.58300   1.000 37.03000  ? 347 HIS B CA  1 
ATOM   6047  C  C   . HIS B  1 316 ? 10.92400  -25.44300 9.45200   1.000 37.29000  ? 347 HIS B C   1 
ATOM   6048  O  O   . HIS B  1 316 ? 11.17700  -26.43100 10.14900  1.000 39.54000  ? 347 HIS B O   1 
ATOM   6049  C  CB  . HIS B  1 316 ? 8.42000   -25.55000 9.45700   1.000 38.01000  ? 347 HIS B CB  1 
ATOM   6050  C  CG  . HIS B  1 316 ? 8.39300   -24.57100 10.59200  1.000 45.44000  ? 347 HIS B CG  1 
ATOM   6051  N  ND1 . HIS B  1 316 ? 7.68000   -23.39000 10.54700  1.000 44.70000  ? 347 HIS B ND1 1 
ATOM   6052  C  CD2 . HIS B  1 316 ? 9.03800   -24.57300 11.78000  1.000 39.19000  ? 347 HIS B CD2 1 
ATOM   6053  C  CE1 . HIS B  1 316 ? 7.85200   -22.72900 11.67500  1.000 42.10000  ? 347 HIS B CE1 1 
ATOM   6054  N  NE2 . HIS B  1 316 ? 8.67300   -23.42500 12.44000  1.000 47.15000  ? 347 HIS B NE2 1 
ATOM   6055  N  N   . TRP B  1 317 ? 11.70600  -24.35300 9.39400   1.000 37.10000  ? 348 TRP B N   1 
ATOM   6056  C  CA  . TRP B  1 317 ? 13.01500  -24.20300 10.03600  1.000 40.58000  ? 348 TRP B CA  1 
ATOM   6057  C  C   . TRP B  1 317 ? 13.31700  -22.72300 10.21200  1.000 42.66000  ? 348 TRP B C   1 
ATOM   6058  O  O   . TRP B  1 317 ? 13.96800  -22.12800 9.34500   1.000 45.22000  ? 348 TRP B O   1 
ATOM   6059  C  CB  . TRP B  1 317 ? 14.11400  -24.83700 9.18900   1.000 37.61000  ? 348 TRP B CB  1 
ATOM   6060  C  CG  . TRP B  1 317 ? 15.47900  -24.87300 9.84300   1.000 44.07000  ? 348 TRP B CG  1 
ATOM   6061  C  CD1 . TRP B  1 317 ? 15.77600  -24.67000 11.16700  1.000 47.76000  ? 348 TRP B CD1 1 
ATOM   6062  C  CD2 . TRP B  1 317 ? 16.72800  -25.12900 9.19400   1.000 44.79000  ? 348 TRP B CD2 1 
ATOM   6063  N  NE1 . TRP B  1 317 ? 17.13200  -24.80500 11.37600  1.000 45.37000  ? 348 TRP B NE1 1 
ATOM   6064  C  CE2 . TRP B  1 317 ? 17.73500  -25.07800 10.17800  1.000 47.01000  ? 348 TRP B CE2 1 
ATOM   6065  C  CE3 . TRP B  1 317 ? 17.09200  -25.40200 7.87400   1.000 43.49000  ? 348 TRP B CE3 1 
ATOM   6066  C  CZ2 . TRP B  1 317 ? 19.07000  -25.29000 9.88200   1.000 47.39000  ? 348 TRP B CZ2 1 
ATOM   6067  C  CZ3 . TRP B  1 317 ? 18.41900  -25.61400 7.58600   1.000 49.59000  ? 348 TRP B CZ3 1 
ATOM   6068  C  CH2 . TRP B  1 317 ? 19.39200  -25.55000 8.58300   1.000 49.30000  ? 348 TRP B CH2 1 
ATOM   6069  N  N   . PRO B  1 318 ? 12.85500  -22.09400 11.29200  1.000 41.71000  ? 349 PRO B N   1 
ATOM   6070  C  CA  . PRO B  1 318 ? 12.91500  -20.62100 11.36200  1.000 43.59000  ? 349 PRO B CA  1 
ATOM   6071  C  C   . PRO B  1 318 ? 14.30800  -20.03300 11.17900  1.000 50.62000  ? 349 PRO B C   1 
ATOM   6072  O  O   . PRO B  1 318 ? 14.42300  -18.93500 10.61800  1.000 45.33000  ? 349 PRO B O   1 
ATOM   6073  C  CB  . PRO B  1 318 ? 12.33800  -20.31200 12.74700  1.000 40.74000  ? 349 PRO B CB  1 
ATOM   6074  C  CG  . PRO B  1 318 ? 11.40100  -21.48100 12.99700  1.000 43.50000  ? 349 PRO B CG  1 
ATOM   6075  C  CD  . PRO B  1 318 ? 12.11600  -22.67800 12.42200  1.000 38.56000  ? 349 PRO B CD  1 
ATOM   6076  N  N   . LYS B  1 319 ? 15.36500  -20.72500 11.62000  1.000 44.59000  ? 350 LYS B N   1 
ATOM   6077  C  CA  . LYS B  1 319 ? 16.71300  -20.17900 11.49800  1.000 44.95000  ? 350 LYS B CA  1 
ATOM   6078  C  C   . LYS B  1 319 ? 17.11900  -19.92000 10.05300  1.000 51.43000  ? 350 LYS B C   1 
ATOM   6079  O  O   . LYS B  1 319 ? 17.97700  -19.07000 9.80600   1.000 55.59000  ? 350 LYS B O   1 
ATOM   6080  C  CB  . LYS B  1 319 ? 17.73400  -21.14100 12.12100  1.000 46.35000  ? 350 LYS B CB  1 
ATOM   6081  C  CG  . LYS B  1 319 ? 19.13200  -20.54600 12.36700  1.000 51.36000  ? 350 LYS B CG  1 
ATOM   6082  C  CD  . LYS B  1 319 ? 20.14500  -21.63500 12.78600  1.000 55.46000  ? 350 LYS B CD  1 
ATOM   6083  C  CE  . LYS B  1 319 ? 20.78600  -22.31400 11.55700  1.000 60.52000  ? 350 LYS B CE  1 
ATOM   6084  N  NZ  . LYS B  1 319 ? 21.47400  -23.62900 11.84800  1.000 58.11000  ? 350 LYS B NZ  1 
ATOM   6085  N  N   . LYS B  1 320 ? 16.53200  -20.62000 9.09100   1.000 51.56000  ? 351 LYS B N   1 
ATOM   6086  C  CA  . LYS B  1 320 ? 17.02500  -20.51300 7.72100   1.000 49.72000  ? 351 LYS B CA  1 
ATOM   6087  C  C   . LYS B  1 320 ? 15.95300  -20.42000 6.64700   1.000 45.80000  ? 351 LYS B C   1 
ATOM   6088  O  O   . LYS B  1 320 ? 16.17900  -19.71700 5.66200   1.000 53.28000  ? 351 LYS B O   1 
ATOM   6089  C  CB  . LYS B  1 320 ? 17.93600  -21.69100 7.40200   1.000 51.47000  ? 351 LYS B CB  1 
ATOM   6090  C  CG  . LYS B  1 320 ? 19.26000  -21.61700 8.11500   1.000 51.45000  ? 351 LYS B CG  1 
ATOM   6091  C  CD  . LYS B  1 320 ? 20.40600  -21.64600 7.11400   1.000 55.92000  ? 351 LYS B CD  1 
ATOM   6092  C  CE  . LYS B  1 320 ? 21.69900  -22.17600 7.77000   1.000 60.08000  ? 351 LYS B CE  1 
ATOM   6093  N  NZ  . LYS B  1 320 ? 22.75700  -22.47500 6.76100   1.000 69.19000  ? 351 LYS B NZ  1 
ATOM   6094  N  N   . ILE B  1 321 ? 14.80000  -21.06200 6.78800   1.000 49.18000  ? 352 ILE B N   1 
ATOM   6095  C  CA  . ILE B  1 321 ? 13.78100  -21.05100 5.74300   1.000 47.14000  ? 352 ILE B CA  1 
ATOM   6096  C  C   . ILE B  1 321 ? 12.86400  -19.86300 6.00300   1.000 49.36000  ? 352 ILE B C   1 
ATOM   6097  O  O   . ILE B  1 321 ? 12.33400  -19.70200 7.10700   1.000 46.10000  ? 352 ILE B O   1 
ATOM   6098  C  CB  . ILE B  1 321 ? 13.01300  -22.38300 5.69200   1.000 42.59000  ? 352 ILE B CB  1 
ATOM   6099  C  CG1 . ILE B  1 321 ? 13.97600  -23.50600 5.28400   1.000 45.28000  ? 352 ILE B CG1 1 
ATOM   6100  C  CG2 . ILE B  1 321 ? 11.84100  -22.31600 4.72500   1.000 46.91000  ? 352 ILE B CG2 1 
ATOM   6101  C  CD1 . ILE B  1 321 ? 13.42500  -24.88200 5.39700   1.000 37.58000  ? 352 ILE B CD1 1 
ATOM   6102  N  N   . LYS B  1 322 ? 12.70800  -19.01300 4.99500   1.000 47.50000  ? 353 LYS B N   1 
ATOM   6103  C  CA  . LYS B  1 322 ? 11.90000  -17.81300 5.12000   1.000 52.56000  ? 353 LYS B CA  1 
ATOM   6104  C  C   . LYS B  1 322 ? 10.43300  -18.18900 5.24600   1.000 53.79000  ? 353 LYS B C   1 
ATOM   6105  O  O   . LYS B  1 322 ? 10.02100  -19.30700 4.92400   1.000 49.15000  ? 353 LYS B O   1 
ATOM   6106  C  CB  . LYS B  1 322 ? 12.10100  -16.88900 3.91100   1.000 48.88000  ? 353 LYS B CB  1 
ATOM   6107  N  N   . LYS B  1 323 ? 9.65800   -17.26700 5.79900   1.000 54.35000  ? 354 LYS B N   1 
ATOM   6108  C  CA  . LYS B  1 323 ? 8.23000   -17.49700 5.91700   1.000 51.82000  ? 354 LYS B CA  1 
ATOM   6109  C  C   . LYS B  1 323 ? 7.54000   -17.27300 4.57600   1.000 53.32000  ? 354 LYS B C   1 
ATOM   6110  O  O   . LYS B  1 323 ? 8.06200   -16.60500 3.68600   1.000 53.77000  ? 354 LYS B O   1 
ATOM   6111  C  CB  . LYS B  1 323 ? 7.61700   -16.56800 6.95600   1.000 54.91000  ? 354 LYS B CB  1 
ATOM   6112  C  CG  . LYS B  1 323 ? 8.25100   -16.64100 8.31500   1.000 52.85000  ? 354 LYS B CG  1 
ATOM   6113  C  CD  . LYS B  1 323 ? 7.64900   -15.56500 9.20300   1.000 62.40000  ? 354 LYS B CD  1 
ATOM   6114  C  CE  . LYS B  1 323 ? 7.99700   -15.77600 10.67500  1.000 57.17000  ? 354 LYS B CE  1 
ATOM   6115  N  NZ  . LYS B  1 323 ? 7.02000   -15.03900 11.54500  1.000 70.41000  ? 354 LYS B NZ  1 
ATOM   6116  N  N   . ASP B  1 324 ? 6.31500   -17.79800 4.46500   1.000 52.89000  ? 355 ASP B N   1 
ATOM   6117  C  CA  . ASP B  1 324 ? 5.44700   -17.57400 3.27500   1.000 51.94000  ? 355 ASP B CA  1 
ATOM   6118  C  C   . ASP B  1 324 ? 6.10900   -17.98800 1.96200   1.000 51.11000  ? 355 ASP B C   1 
ATOM   6119  O  O   . ASP B  1 324 ? 5.76100   -17.40800 0.92700   1.000 53.72000  ? 355 ASP B O   1 
ATOM   6120  C  CB  . ASP B  1 324 ? 4.94600   -16.14200 3.24300   1.000 58.12000  ? 355 ASP B CB  1 
ATOM   6121  C  CG  . ASP B  1 324 ? 4.43900   -15.60800 4.57300   1.000 65.12000  ? 355 ASP B CG  1 
ATOM   6122  O  OD1 . ASP B  1 324 ? 3.50500   -16.21500 5.12800   1.000 69.82000  ? 355 ASP B OD1 1 
ATOM   6123  O  OD2 . ASP B  1 324 ? 4.98600   -14.59300 5.04200   1.000 69.95000  ? 355 ASP B OD2 1 
ATOM   6124  N  N   . GLN B  1 325 ? 6.97000   -18.99300 1.99900   1.000 50.07000  ? 356 GLN B N   1 
ATOM   6125  C  CA  . GLN B  1 325 ? 7.58700   -19.45200 0.76200   1.000 46.42000  ? 356 GLN B CA  1 
ATOM   6126  C  C   . GLN B  1 325 ? 6.75400   -20.55000 0.09900   1.000 50.47000  ? 356 GLN B C   1 
ATOM   6127  O  O   . GLN B  1 325 ? 6.18100   -21.41400 0.77400   1.000 46.35000  ? 356 GLN B O   1 
ATOM   6128  C  CB  . GLN B  1 325 ? 8.99600   -19.96800 1.03900   1.000 50.34000  ? 356 GLN B CB  1 
ATOM   6129  C  CG  . GLN B  1 325 ? 9.72200   -20.53300 -0.18200  1.000 53.49000  ? 356 GLN B CG  1 
ATOM   6130  C  CD  . GLN B  1 325 ? 11.06000  -21.17800 0.17200   1.000 60.88000  ? 356 GLN B CD  1 
ATOM   6131  O  OE1 . GLN B  1 325 ? 11.59900  -21.98200 -0.59200  1.000 61.54000  ? 356 GLN B OE1 1 
ATOM   6132  N  NE2 . GLN B  1 325 ? 11.59400  -20.83800 1.34900   1.000 62.06000  ? 356 GLN B NE2 1 
ATOM   6133  N  N   . ARG B  1 326 ? 6.72700   -20.53200 -1.23000  1.000 49.43000  ? 357 ARG B N   1 
ATOM   6134  C  CA  . ARG B  1 326 ? 6.15100   -21.59700 -2.03600  1.000 45.06000  ? 357 ARG B CA  1 
ATOM   6135  C  C   . ARG B  1 326 ? 7.22500   -22.09800 -2.98900  1.000 45.47000  ? 357 ARG B C   1 
ATOM   6136  O  O   . ARG B  1 326 ? 7.76700   -21.32000 -3.77800  1.000 48.00000  ? 357 ARG B O   1 
ATOM   6137  C  CB  . ARG B  1 326 ? 4.93700   -21.09100 -2.80200  1.000 42.86000  ? 357 ARG B CB  1 
ATOM   6138  C  CG  . ARG B  1 326 ? 3.81100   -20.61200 -1.88900  1.000 50.62000  ? 357 ARG B CG  1 
ATOM   6139  C  CD  . ARG B  1 326 ? 2.57300   -20.17100 -2.67500  1.000 48.34000  ? 357 ARG B CD  1 
ATOM   6140  N  NE  . ARG B  1 326 ? 1.79700   -21.30300 -3.16200  1.000 52.18000  ? 357 ARG B NE  1 
ATOM   6141  C  CZ  . ARG B  1 326 ? 0.90200   -21.94800 -2.42300  1.000 50.51000  ? 357 ARG B CZ  1 
ATOM   6142  N  NH1 . ARG B  1 326 ? 0.70300   -21.63000 -1.15500  1.000 49.85000  ? 357 ARG B NH1 1 
ATOM   6143  N  NH2 . ARG B  1 326 ? 0.18700   -22.93000 -2.96900  1.000 48.62000  ? 357 ARG B NH2 1 
ATOM   6144  N  N   . PHE B  1 327 ? 7.56600   -23.37100 -2.88600  1.000 46.51000  ? 358 PHE B N   1 
ATOM   6145  C  CA  . PHE B  1 327 ? 8.57000   -23.99600 -3.74700  1.000 47.51000  ? 358 PHE B CA  1 
ATOM   6146  C  C   . PHE B  1 327 ? 7.84100   -24.81900 -4.80700  1.000 48.68000  ? 358 PHE B C   1 
ATOM   6147  O  O   . PHE B  1 327 ? 7.26300   -25.87200 -4.49900  1.000 44.98000  ? 358 PHE B O   1 
ATOM   6148  C  CB  . PHE B  1 327 ? 9.50300   -24.86400 -2.91000  1.000 41.47000  ? 358 PHE B CB  1 
ATOM   6149  C  CG  . PHE B  1 327 ? 10.74700  -25.28100 -3.61000  1.000 47.72000  ? 358 PHE B CG  1 
ATOM   6150  C  CD1 . PHE B  1 327 ? 11.87100  -24.47000 -3.59900  1.000 46.46000  ? 358 PHE B CD1 1 
ATOM   6151  C  CD2 . PHE B  1 327 ? 10.81300  -26.50100 -4.25800  1.000 44.24000  ? 358 PHE B CD2 1 
ATOM   6152  C  CE1 . PHE B  1 327 ? 13.03000  -24.86300 -4.22600  1.000 43.89000  ? 358 PHE B CE1 1 
ATOM   6153  C  CE2 . PHE B  1 327 ? 11.97500  -26.89800 -4.90000  1.000 42.65000  ? 358 PHE B CE2 1 
ATOM   6154  C  CZ  . PHE B  1 327 ? 13.08600  -26.07700 -4.87500  1.000 46.11000  ? 358 PHE B CZ  1 
ATOM   6155  N  N   . ASP B  1 328 ? 7.88900   -24.36400 -6.05900  1.000 45.79000  ? 359 ASP B N   1 
ATOM   6156  C  CA  . ASP B  1 328 ? 7.04300   -24.95400 -7.08800  1.000 42.31000  ? 359 ASP B CA  1 
ATOM   6157  C  C   . ASP B  1 328 ? 7.77300   -25.95500 -7.97100  1.000 45.46000  ? 359 ASP B C   1 
ATOM   6158  O  O   . ASP B  1 328 ? 7.12500   -26.61700 -8.78800  1.000 45.30000  ? 359 ASP B O   1 
ATOM   6159  C  CB  . ASP B  1 328 ? 6.41700   -23.85900 -7.96000  1.000 41.83000  ? 359 ASP B CB  1 
ATOM   6160  C  CG  . ASP B  1 328 ? 5.52400   -22.91800 -7.15600  1.000 46.65000  ? 359 ASP B CG  1 
ATOM   6161  O  OD1 . ASP B  1 328 ? 4.87100   -23.39000 -6.20500  1.000 46.77000  ? 359 ASP B OD1 1 
ATOM   6162  O  OD2 . ASP B  1 328 ? 5.44500   -21.71300 -7.48000  1.000 55.94000  ? 359 ASP B OD2 1 
ATOM   6163  N  N   . PHE B  1 329 ? 9.08400   -26.13900 -7.77800  1.000 38.56000  ? 360 PHE B N   1 
ATOM   6164  C  CA  . PHE B  1 329 ? 9.82700   -27.12000 -8.56000  1.000 40.48000  ? 360 PHE B CA  1 
ATOM   6165  C  C   . PHE B  1 329 ? 9.61800   -28.51900 -7.98100  1.000 43.68000  ? 360 PHE B C   1 
ATOM   6166  O  O   . PHE B  1 329 ? 9.53500   -28.67400 -6.76400  1.000 42.29000  ? 360 PHE B O   1 
ATOM   6167  C  CB  . PHE B  1 329 ? 11.32300  -26.77800 -8.57800  1.000 41.14000  ? 360 PHE B CB  1 
ATOM   6168  C  CG  . PHE B  1 329 ? 11.62600  -25.41100 -9.14600  1.000 46.46000  ? 360 PHE B CG  1 
ATOM   6169  C  CD1 . PHE B  1 329 ? 11.39500  -25.13200 -10.49200 1.000 48.48000  ? 360 PHE B CD1 1 
ATOM   6170  C  CD2 . PHE B  1 329 ? 12.12800  -24.40200 -8.34200  1.000 50.55000  ? 360 PHE B CD2 1 
ATOM   6171  C  CE1 . PHE B  1 329 ? 11.65800  -23.87300 -11.01900 1.000 45.63000  ? 360 PHE B CE1 1 
ATOM   6172  C  CE2 . PHE B  1 329 ? 12.40000  -23.13800 -8.86300  1.000 53.48000  ? 360 PHE B CE2 1 
ATOM   6173  C  CZ  . PHE B  1 329 ? 12.16200  -22.87900 -10.20600 1.000 56.66000  ? 360 PHE B CZ  1 
ATOM   6174  N  N   . PRO B  1 330 ? 9.56200   -29.54100 -8.83700  1.000 46.92000  ? 361 PRO B N   1 
ATOM   6175  C  CA  . PRO B  1 330 ? 9.33200   -30.92400 -8.38100  1.000 39.70000  ? 361 PRO B CA  1 
ATOM   6176  C  C   . PRO B  1 330 ? 10.45300  -31.44900 -7.50400  1.000 40.95000  ? 361 PRO B C   1 
ATOM   6177  O  O   . PRO B  1 330 ? 11.62700  -31.32900 -7.84600  1.000 44.00000  ? 361 PRO B O   1 
ATOM   6178  C  CB  . PRO B  1 330 ? 9.27000   -31.71300 -9.69400  1.000 34.82000  ? 361 PRO B CB  1 
ATOM   6179  C  CG  . PRO B  1 330 ? 8.87700   -30.70100 -10.68300 1.000 42.89000  ? 361 PRO B CG  1 
ATOM   6180  C  CD  . PRO B  1 330 ? 9.45800   -29.41400 -10.29700 1.000 39.32000  ? 361 PRO B CD  1 
ATOM   6181  N  N   . VAL B  1 331 ? 10.08100  -32.06900 -6.37700  1.000 38.98000  ? 362 VAL B N   1 
ATOM   6182  C  CA  . VAL B  1 331 ? 11.02900  -32.70800 -5.45900  1.000 38.09000  ? 362 VAL B CA  1 
ATOM   6183  C  C   . VAL B  1 331 ? 10.55600  -34.11800 -5.13900  1.000 36.44000  ? 362 VAL B C   1 
ATOM   6184  O  O   . VAL B  1 331 ? 9.42000   -34.50100 -5.41500  1.000 34.89000  ? 362 VAL B O   1 
ATOM   6185  C  CB  . VAL B  1 331 ? 11.22000  -31.91800 -4.14200  1.000 35.45000  ? 362 VAL B CB  1 
ATOM   6186  C  CG1 . VAL B  1 331 ? 11.78300  -30.52900 -4.43000  1.000 39.78000  ? 362 VAL B CG1 1 
ATOM   6187  C  CG2 . VAL B  1 331 ? 9.90900   -31.82600 -3.38200  1.000 30.13000  ? 362 VAL B CG2 1 
ATOM   6188  N  N   . SER B  1 332 ? 11.42900  -34.87700 -4.50300  1.000 37.75000  ? 363 SER B N   1 
ATOM   6189  C  CA  . SER B  1 332 ? 11.11700  -36.25200 -4.13700  1.000 35.03000  ? 363 SER B CA  1 
ATOM   6190  C  C   . SER B  1 332 ? 11.33700  -36.49100 -2.64900  1.000 33.20000  ? 363 SER B C   1 
ATOM   6191  O  O   . SER B  1 332 ? 12.23300  -35.91100 -2.04600  1.000 36.30000  ? 363 SER B O   1 
ATOM   6192  C  CB  . SER B  1 332 ? 11.96500  -37.22900 -4.90800  1.000 31.28000  ? 363 SER B CB  1 
ATOM   6193  O  OG  . SER B  1 332 ? 11.81900  -38.51000 -4.33500  1.000 44.00000  ? 363 SER B OG  1 
ATOM   6194  N  N   . SER B  1 333 ? 10.54000  -37.39400 -2.06600  1.000 33.31000  ? 364 SER B N   1 
ATOM   6195  C  CA  . SER B  1 333 ? 10.82800  -37.82500 -0.70500  1.000 34.59000  ? 364 SER B CA  1 
ATOM   6196  C  C   . SER B  1 333 ? 12.20900  -38.48200 -0.62300  1.000 36.34000  ? 364 SER B C   1 
ATOM   6197  O  O   . SER B  1 333 ? 12.76000  -38.61200 0.47800   1.000 34.26000  ? 364 SER B O   1 
ATOM   6198  C  CB  . SER B  1 333 ? 9.76600   -38.80600 -0.18200  1.000 33.90000  ? 364 SER B CB  1 
ATOM   6199  O  OG  . SER B  1 333 ? 9.66900   -39.98300 -0.98300  1.000 34.26000  ? 364 SER B OG  1 
ATOM   6200  N  N   . LEU B  1 334 ? 12.75300  -38.94500 -1.75500  1.000 35.06000  ? 365 LEU B N   1 
ATOM   6201  C  CA  . LEU B  1 334 ? 14.13100  -39.44800 -1.79200  1.000 34.08000  ? 365 LEU B CA  1 
ATOM   6202  C  C   . LEU B  1 334 ? 15.14300  -38.36000 -1.46000  1.000 37.77000  ? 365 LEU B C   1 
ATOM   6203  O  O   . LEU B  1 334 ? 16.31400  -38.66200 -1.19100  1.000 36.01000  ? 365 LEU B O   1 
ATOM   6204  C  CB  . LEU B  1 334 ? 14.43700  -40.02600 -3.17300  1.000 40.24000  ? 365 LEU B CB  1 
ATOM   6205  C  CG  . LEU B  1 334 ? 13.56900  -41.20100 -3.63800  1.000 41.94000  ? 365 LEU B CG  1 
ATOM   6206  C  CD1 . LEU B  1 334 ? 13.55100  -41.29100 -5.18500  1.000 34.52000  ? 365 LEU B CD1 1 
ATOM   6207  C  CD2 . LEU B  1 334 ? 14.09000  -42.47600 -2.98600  1.000 38.85000  ? 365 LEU B CD2 1 
ATOM   6208  N  N   . ASP B  1 335 ? 14.74000  -37.09700 -1.51200  1.000 36.40000  ? 366 ASP B N   1 
ATOM   6209  C  CA  . ASP B  1 335 ? 15.68300  -36.04000 -1.17100  1.000 41.01000  ? 366 ASP B CA  1 
ATOM   6210  C  C   . ASP B  1 335 ? 15.90100  -35.92200 0.33000   1.000 45.20000  ? 366 ASP B C   1 
ATOM   6211  O  O   . ASP B  1 335 ? 16.93800  -35.39100 0.75700   1.000 43.17000  ? 366 ASP B O   1 
ATOM   6212  C  CB  . ASP B  1 335 ? 15.18500  -34.72000 -1.73900  1.000 34.54000  ? 366 ASP B CB  1 
ATOM   6213  C  CG  . ASP B  1 335 ? 15.05500  -34.78300 -3.24600  1.000 41.24000  ? 366 ASP B CG  1 
ATOM   6214  O  OD1 . ASP B  1 335 ? 15.82000  -35.55400 -3.88500  1.000 39.47000  ? 366 ASP B OD1 1 
ATOM   6215  O  OD2 . ASP B  1 335 ? 14.17100  -34.10900 -3.78800  1.000 36.05000  ? 366 ASP B OD2 1 
ATOM   6216  N  N   . LEU B  1 336 ? 14.99500  -36.47500 1.14400   1.000 41.35000  ? 367 LEU B N   1 
ATOM   6217  C  CA  . LEU B  1 336 ? 15.12500  -36.26200 2.57800   1.000 39.87000  ? 367 LEU B CA  1 
ATOM   6218  C  C   . LEU B  1 336 ? 16.40600  -36.90300 3.11900   1.000 41.29000  ? 367 LEU B C   1 
ATOM   6219  O  O   . LEU B  1 336 ? 17.06200  -36.33000 3.99200   1.000 39.67000  ? 367 LEU B O   1 
ATOM   6220  C  CB  . LEU B  1 336 ? 13.90200  -36.80100 3.29700   1.000 37.90000  ? 367 LEU B CB  1 
ATOM   6221  C  CG  . LEU B  1 336 ? 12.56500  -36.22100 2.80500   1.000 37.84000  ? 367 LEU B CG  1 
ATOM   6222  C  CD1 . LEU B  1 336 ? 11.47900  -36.94700 3.51700   1.000 36.72000  ? 367 LEU B CD1 1 
ATOM   6223  C  CD2 . LEU B  1 336 ? 12.41700  -34.70500 2.97000   1.000 34.65000  ? 367 LEU B CD2 1 
ATOM   6224  N  N   . TYR B  1 337 ? 16.78200  -38.08300 2.60700   1.000 39.22000  ? 368 TYR B N   1 
ATOM   6225  C  CA  . TYR B  1 337 ? 17.98500  -38.76200 3.09400   1.000 40.25000  ? 368 TYR B CA  1 
ATOM   6226  C  C   . TYR B  1 337 ? 19.24200  -37.90400 2.91000   1.000 42.47000  ? 368 TYR B C   1 
ATOM   6227  O  O   . TYR B  1 337 ? 19.88300  -37.55400 3.91700   1.000 43.35000  ? 368 TYR B O   1 
ATOM   6228  C  CB  . TYR B  1 337 ? 18.08500  -40.14500 2.42600   1.000 34.21000  ? 368 TYR B CB  1 
ATOM   6229  C  CG  . TYR B  1 337 ? 19.10300  -41.13500 2.98300   1.000 42.37000  ? 368 TYR B CG  1 
ATOM   6230  C  CD1 . TYR B  1 337 ? 20.43900  -40.76800 3.24900   1.000 44.19000  ? 368 TYR B CD1 1 
ATOM   6231  C  CD2 . TYR B  1 337 ? 18.71200  -42.44600 3.27600   1.000 38.06000  ? 368 TYR B CD2 1 
ATOM   6232  C  CE1 . TYR B  1 337 ? 21.35400  -41.70000 3.76100   1.000 37.65000  ? 368 TYR B CE1 1 
ATOM   6233  C  CE2 . TYR B  1 337 ? 19.59300  -43.36600 3.80300   1.000 41.91000  ? 368 TYR B CE2 1 
ATOM   6234  C  CZ  . TYR B  1 337 ? 20.92300  -42.99500 4.03100   1.000 43.25000  ? 368 TYR B CZ  1 
ATOM   6235  O  OH  . TYR B  1 337 ? 21.77400  -43.93400 4.54000   1.000 39.77000  ? 368 TYR B OH  1 
ATOM   6236  N  N   . PRO B  1 338 ? 19.62800  -37.49700 1.69400   1.000 44.78000  ? 369 PRO B N   1 
ATOM   6237  C  CA  . PRO B  1 338 ? 20.84400  -36.66200 1.56900   1.000 43.60000  ? 369 PRO B CA  1 
ATOM   6238  C  C   . PRO B  1 338 ? 20.70400  -35.26800 2.17600   1.000 42.17000  ? 369 PRO B C   1 
ATOM   6239  O  O   . PRO B  1 338 ? 21.71200  -34.68100 2.58700   1.000 47.23000  ? 369 PRO B O   1 
ATOM   6240  C  CB  . PRO B  1 338 ? 21.07700  -36.60500 0.04800   1.000 38.45000  ? 369 PRO B CB  1 
ATOM   6241  C  CG  . PRO B  1 338 ? 19.65500  -36.80400 -0.53800  1.000 40.52000  ? 369 PRO B CG  1 
ATOM   6242  C  CD  . PRO B  1 338 ? 19.00400  -37.77900 0.38200   1.000 41.64000  ? 369 PRO B CD  1 
ATOM   6243  N  N   . THR B  1 339 ? 19.49600  -34.71300 2.25100   1.000 41.09000  ? 370 THR B N   1 
ATOM   6244  C  CA  . THR B  1 339 ? 19.31700  -33.41200 2.89000   1.000 37.33000  ? 370 THR B CA  1 
ATOM   6245  C  C   . THR B  1 339 ? 19.58900  -33.50200 4.38300   1.000 45.67000  ? 370 THR B C   1 
ATOM   6246  O  O   . THR B  1 339 ? 20.31500  -32.66800 4.95100   1.000 46.88000  ? 370 THR B O   1 
ATOM   6247  C  CB  . THR B  1 339 ? 17.88900  -32.92600 2.66200   1.000 43.44000  ? 370 THR B CB  1 
ATOM   6248  O  OG1 . THR B  1 339 ? 17.61300  -32.93200 1.26100   1.000 38.95000  ? 370 THR B OG1 1 
ATOM   6249  C  CG2 . THR B  1 339 ? 17.70500  -31.51700 3.19300   1.000 35.17000  ? 370 THR B CG2 1 
ATOM   6250  N  N   . PHE B  1 340 ? 19.06600  -34.54700 5.02400   1.000 42.51000  ? 371 PHE B N   1 
ATOM   6251  C  CA  . PHE B  1 340 ? 19.24300  -34.68600 6.46300   1.000 41.94000  ? 371 PHE B CA  1 
ATOM   6252  C  C   . PHE B  1 340 ? 20.69400  -35.01800 6.80400   1.000 44.70000  ? 371 PHE B C   1 
ATOM   6253  O  O   . PHE B  1 340 ? 21.24300  -34.47200 7.76000   1.000 41.27000  ? 371 PHE B O   1 
ATOM   6254  C  CB  . PHE B  1 340 ? 18.31000  -35.76400 7.02200   1.000 40.16000  ? 371 PHE B CB  1 
ATOM   6255  C  CG  . PHE B  1 340 ? 16.84600  -35.42900 6.90700   1.000 44.57000  ? 371 PHE B CG  1 
ATOM   6256  C  CD1 . PHE B  1 340 ? 16.43200  -34.14400 6.63100   1.000 40.44000  ? 371 PHE B CD1 1 
ATOM   6257  C  CD2 . PHE B  1 340 ? 15.88600  -36.42200 7.04000   1.000 41.81000  ? 371 PHE B CD2 1 
ATOM   6258  C  CE1 . PHE B  1 340 ? 15.08700  -33.84700 6.50500   1.000 41.23000  ? 371 PHE B CE1 1 
ATOM   6259  C  CE2 . PHE B  1 340 ? 14.54500  -36.13600 6.90700   1.000 37.88000  ? 371 PHE B CE2 1 
ATOM   6260  C  CZ  . PHE B  1 340 ? 14.14000  -34.84400 6.64300   1.000 40.16000  ? 371 PHE B CZ  1 
ATOM   6261  N  N   . THR B  1 341 ? 21.31500  -35.94500 6.06600   1.000 43.96000  ? 372 THR B N   1 
ATOM   6262  C  CA  . THR B  1 341 ? 22.70000  -36.28700 6.35800   1.000 48.03000  ? 372 THR B CA  1 
ATOM   6263  C  C   . THR B  1 341 ? 23.60800  -35.09800 6.11100   1.000 45.82000  ? 372 THR B C   1 
ATOM   6264  O  O   . THR B  1 341 ? 24.58800  -34.89800 6.83500   1.000 49.37000  ? 372 THR B O   1 
ATOM   6265  C  CB  . THR B  1 341 ? 23.16900  -37.48400 5.52600   1.000 44.87000  ? 372 THR B CB  1 
ATOM   6266  O  OG1 . THR B  1 341 ? 23.03300  -37.17900 4.14400   1.000 49.63000  ? 372 THR B OG1 1 
ATOM   6267  C  CG2 . THR B  1 341 ? 22.34700  -38.70900 5.83600   1.000 41.37000  ? 372 THR B CG2 1 
ATOM   6268  N  N   . GLY B  1 342 ? 23.30400  -34.30500 5.08700   1.000 44.28000  ? 373 GLY B N   1 
ATOM   6269  C  CA  . GLY B  1 342 ? 24.04200  -33.06600 4.88500   1.000 42.70000  ? 373 GLY B CA  1 
ATOM   6270  C  C   . GLY B  1 342 ? 23.94300  -32.11400 6.06600   1.000 46.68000  ? 373 GLY B C   1 
ATOM   6271  O  O   . GLY B  1 342 ? 24.95800  -31.69900 6.62500   1.000 47.66000  ? 373 GLY B O   1 
ATOM   6272  N  N   . LEU B  1 343 ? 22.71400  -31.80400 6.50000   1.000 46.65000  ? 374 LEU B N   1 
ATOM   6273  C  CA  . LEU B  1 343 ? 22.51400  -30.89000 7.62300   1.000 46.20000  ? 374 LEU B CA  1 
ATOM   6274  C  C   . LEU B  1 343 ? 23.15900  -31.42300 8.88300   1.000 46.28000  ? 374 LEU B C   1 
ATOM   6275  O  O   . LEU B  1 343 ? 23.55800  -30.64900 9.75500   1.000 44.48000  ? 374 LEU B O   1 
ATOM   6276  C  CB  . LEU B  1 343 ? 21.02900  -30.67100 7.88500   1.000 44.15000  ? 374 LEU B CB  1 
ATOM   6277  C  CG  . LEU B  1 343 ? 20.20900  -29.93200 6.83400   1.000 51.36000  ? 374 LEU B CG  1 
ATOM   6278  C  CD1 . LEU B  1 343 ? 18.74500  -30.04100 7.21800   1.000 49.75000  ? 374 LEU B CD1 1 
ATOM   6279  C  CD2 . LEU B  1 343 ? 20.62000  -28.47000 6.72300   1.000 50.90000  ? 374 LEU B CD2 1 
ATOM   6280  N  N   . ALA B  1 344 ? 23.23100  -32.73500 9.01100   1.000 43.14000  ? 375 ALA B N   1 
ATOM   6281  C  CA  . ALA B  1 344 ? 23.84700  -33.34100 10.16500  1.000 42.96000  ? 375 ALA B CA  1 
ATOM   6282  C  C   . ALA B  1 344 ? 25.36500  -33.38200 10.06400  1.000 53.76000  ? 375 ALA B C   1 
ATOM   6283  O  O   . ALA B  1 344 ? 26.01000  -33.85800 11.00900  1.000 45.23000  ? 375 ALA B O   1 
ATOM   6284  C  CB  . ALA B  1 344 ? 23.32500  -34.75100 10.33900  1.000 44.07000  ? 375 ALA B CB  1 
ATOM   6285  N  N   . GLU B  1 345 ? 25.94000  -32.92800 8.93800   1.000 42.93000  ? 376 GLU B N   1 
ATOM   6286  C  CA  . GLU B  1 345 ? 27.38200  -33.00500 8.71000   1.000 49.46000  ? 376 GLU B CA  1 
ATOM   6287  C  C   . GLU B  1 345 ? 27.88300  -34.42800 8.86500   1.000 56.41000  ? 376 GLU B C   1 
ATOM   6288  O  O   . GLU B  1 345 ? 29.00100  -34.66700 9.33200   1.000 67.35000  ? 376 GLU B O   1 
ATOM   6289  C  CB  . GLU B  1 345 ? 28.14100  -32.04600 9.63800   1.000 47.52000  ? 376 GLU B CB  1 
ATOM   6290  C  CG  . GLU B  1 345 ? 27.74900  -30.58600 9.40600   1.000 55.47000  ? 376 GLU B CG  1 
ATOM   6291  C  CD  . GLU B  1 345 ? 28.21600  -29.63900 10.50000  1.000 62.99000  ? 376 GLU B CD  1 
ATOM   6292  O  OE1 . GLU B  1 345 ? 29.10800  -30.01000 11.29700  1.000 61.87000  ? 376 GLU B OE1 1 
ATOM   6293  O  OE2 . GLU B  1 345 ? 27.69300  -28.50100 10.54400  1.000 70.26000  ? 376 GLU B OE2 1 
ATOM   6294  N  N   . ALA B  1 346 ? 27.03400  -35.37900 8.52000   1.000 45.70000  ? 377 ALA B N   1 
ATOM   6295  C  CA  . ALA B  1 346 ? 27.36700  -36.78100 8.66100   1.000 51.80000  ? 377 ALA B CA  1 
ATOM   6296  C  C   . ALA B  1 346 ? 28.03100  -37.28900 7.38800   1.000 56.63000  ? 377 ALA B C   1 
ATOM   6297  O  O   . ALA B  1 346 ? 27.83400  -36.74600 6.29900   1.000 65.99000  ? 377 ALA B O   1 
ATOM   6298  C  CB  . ALA B  1 346 ? 26.11300  -37.59800 8.98300   1.000 50.52000  ? 377 ALA B CB  1 
ATOM   6299  N  N   . LYS B  1 347 ? 28.87100  -38.30400 7.54300   1.000 63.30000  ? 378 LYS B N   1 
ATOM   6300  C  CA  . LYS B  1 347 ? 29.50700  -38.95400 6.40900   1.000 64.00000  ? 378 LYS B CA  1 
ATOM   6301  C  C   . LYS B  1 347 ? 28.70000  -40.18400 6.01500   1.000 59.56000  ? 378 LYS B C   1 
ATOM   6302  O  O   . LYS B  1 347 ? 28.29600  -40.97900 6.86900   1.000 61.38000  ? 378 LYS B O   1 
ATOM   6303  C  CB  . LYS B  1 347 ? 30.95200  -39.34800 6.72900   1.000 61.06000  ? 378 LYS B CB  1 
ATOM   6304  N  N   . LEU B  1 348 ? 28.52300  -40.36400 4.73500   1.000 57.01000  ? 379 LEU B N   1 
ATOM   6305  C  CA  . LEU B  1 348 ? 27.75400  -41.51000 4.29700   1.000 61.49000  ? 379 LEU B CA  1 
ATOM   6306  C  C   . LEU B  1 348 ? 28.59800  -42.78100 4.39500   1.000 57.16000  ? 379 LEU B C   1 
ATOM   6307  O  O   . LEU B  1 348 ? 29.82100  -42.72900 4.27400   1.000 56.76000  ? 379 LEU B O   1 
ATOM   6308  C  CB  . LEU B  1 348 ? 27.28800  -41.29500 2.86500   1.000 56.80000  ? 379 LEU B CB  1 
ATOM   6309  C  CG  . LEU B  1 348 ? 26.13800  -40.30300 2.77000   1.000 58.83000  ? 379 LEU B CG  1 
ATOM   6310  C  CD1 . LEU B  1 348 ? 25.67100  -40.13000 1.32800   1.000 55.34000  ? 379 LEU B CD1 1 
ATOM   6311  C  CD2 . LEU B  1 348 ? 25.01600  -40.83000 3.62400   1.000 52.59000  ? 379 LEU B CD2 1 
ATOM   6312  N  N   . PRO B  1 349 ? 27.97100  -43.93400 4.62500   1.000 60.22000  ? 380 PRO B N   1 
ATOM   6313  C  CA  . PRO B  1 349 ? 28.73200  -45.18500 4.62400   1.000 56.16000  ? 380 PRO B CA  1 
ATOM   6314  C  C   . PRO B  1 349 ? 29.40300  -45.37300 3.27200   1.000 62.65000  ? 380 PRO B C   1 
ATOM   6315  O  O   . PRO B  1 349 ? 28.88800  -44.95000 2.23400   1.000 58.51000  ? 380 PRO B O   1 
ATOM   6316  C  CB  . PRO B  1 349 ? 27.66200  -46.25700 4.85400   1.000 60.64000  ? 380 PRO B CB  1 
ATOM   6317  C  CG  . PRO B  1 349 ? 26.51100  -45.52500 5.47600   1.000 53.19000  ? 380 PRO B CG  1 
ATOM   6318  C  CD  . PRO B  1 349 ? 26.53400  -44.15900 4.85900   1.000 50.90000  ? 380 PRO B CD  1 
ATOM   6319  N  N   . LYS B  1 350 ? 30.54200  -46.05700 3.28900   1.000 65.13000  ? 381 LYS B N   1 
ATOM   6320  C  CA  . LYS B  1 350 ? 31.28100  -46.31300 2.06200   1.000 63.06000  ? 381 LYS B CA  1 
ATOM   6321  C  C   . LYS B  1 350 ? 30.44500  -47.16200 1.12600   1.000 61.28000  ? 381 LYS B C   1 
ATOM   6322  O  O   . LYS B  1 350 ? 29.98600  -48.24400 1.50200   1.000 53.61000  ? 381 LYS B O   1 
ATOM   6323  C  CB  . LYS B  1 350 ? 32.60300  -47.02000 2.36500   1.000 64.55000  ? 381 LYS B CB  1 
ATOM   6324  N  N   . GLY B  1 351 ? 30.19900  -46.64300 -0.07100  1.000 61.52000  ? 382 GLY B N   1 
ATOM   6325  C  CA  . GLY B  1 351 ? 29.46800  -47.38400 -1.07100  1.000 58.09000  ? 382 GLY B CA  1 
ATOM   6326  C  C   . GLY B  1 351 ? 27.96700  -47.21000 -1.03300  1.000 57.48000  ? 382 GLY B C   1 
ATOM   6327  O  O   . GLY B  1 351 ? 27.26200  -47.97500 -1.69100  1.000 49.12000  ? 382 GLY B O   1 
ATOM   6328  N  N   . LYS B  1 352 ? 27.45600  -46.25300 -0.26600  1.000 54.12000  ? 383 LYS B N   1 
ATOM   6329  C  CA  . LYS B  1 352 ? 26.01900  -46.05600 -0.15400  1.000 51.58000  ? 383 LYS B CA  1 
ATOM   6330  C  C   . LYS B  1 352 ? 25.50800  -45.36100 -1.40700  1.000 55.64000  ? 383 LYS B C   1 
ATOM   6331  O  O   . LYS B  1 352 ? 25.99600  -44.28800 -1.78500  1.000 52.48000  ? 383 LYS B O   1 
ATOM   6332  C  CB  . LYS B  1 352 ? 25.67700  -45.25100 1.09500   1.000 51.31000  ? 383 LYS B CB  1 
ATOM   6333  C  CG  . LYS B  1 352 ? 24.21000  -44.83300 1.20200   1.000 51.08000  ? 383 LYS B CG  1 
ATOM   6334  C  CD  . LYS B  1 352 ? 23.30400  -45.95100 1.66600   1.000 42.84000  ? 383 LYS B CD  1 
ATOM   6335  C  CE  . LYS B  1 352 ? 21.85900  -45.47500 1.64000   1.000 50.12000  ? 383 LYS B CE  1 
ATOM   6336  N  NZ  . LYS B  1 352 ? 20.94000  -46.53000 2.10600   1.000 53.18000  ? 383 LYS B NZ  1 
ATOM   6337  N  N   . GLN B  1 353 ? 24.55600  -45.98900 -2.07300  1.000 51.63000  ? 384 GLN B N   1 
ATOM   6338  C  CA  . GLN B  1 353 ? 23.94200  -45.40900 -3.25300  1.000 57.97000  ? 384 GLN B CA  1 
ATOM   6339  C  C   . GLN B  1 353 ? 22.63800  -44.71600 -2.86800  1.000 53.11000  ? 384 GLN B C   1 
ATOM   6340  O  O   . GLN B  1 353 ? 21.90200  -45.19400 -1.99700  1.000 47.78000  ? 384 GLN B O   1 
ATOM   6341  C  CB  . GLN B  1 353 ? 23.71700  -46.48400 -4.30800  1.000 64.19000  ? 384 GLN B CB  1 
ATOM   6342  C  CG  . GLN B  1 353 ? 25.03400  -47.11700 -4.78800  1.000 56.60000  ? 384 GLN B CG  1 
ATOM   6343  C  CD  . GLN B  1 353 ? 25.22300  -46.97400 -6.29900  1.000 77.57000  ? 384 GLN B CD  1 
ATOM   6344  O  OE1 . GLN B  1 353 ? 25.22400  -45.85600 -6.84100  1.000 74.70000  ? 384 GLN B OE1 1 
ATOM   6345  N  NE2 . GLN B  1 353 ? 25.37000  -48.11000 -6.98700  1.000 75.38000  ? 384 GLN B NE2 1 
ATOM   6346  N  N   . LEU B  1 354 ? 22.40100  -43.55300 -3.47600  1.000 49.29000  ? 385 LEU B N   1 
ATOM   6347  C  CA  . LEU B  1 354 ? 21.26100  -42.69600 -3.19100  1.000 47.46000  ? 385 LEU B CA  1 
ATOM   6348  C  C   . LEU B  1 354 ? 20.61900  -42.26400 -4.50100  1.000 51.14000  ? 385 LEU B C   1 
ATOM   6349  O  O   . LEU B  1 354 ? 21.32000  -41.99300 -5.48000  1.000 51.03000  ? 385 LEU B O   1 
ATOM   6350  C  CB  . LEU B  1 354 ? 21.70100  -41.46300 -2.40300  1.000 46.94000  ? 385 LEU B CB  1 
ATOM   6351  C  CG  . LEU B  1 354 ? 22.13700  -41.70000 -0.95800  1.000 49.46000  ? 385 LEU B CG  1 
ATOM   6352  C  CD1 . LEU B  1 354 ? 22.42500  -40.36700 -0.24600  1.000 46.46000  ? 385 LEU B CD1 1 
ATOM   6353  C  CD2 . LEU B  1 354 ? 21.10000  -42.51500 -0.18900  1.000 39.86000  ? 385 LEU B CD2 1 
ATOM   6354  N  N   . ASP B  1 355 ? 19.28400  -42.19800 -4.53100  1.000 48.15000  ? 386 ASP B N   1 
ATOM   6355  C  CA  . ASP B  1 355 ? 18.60200  -41.80100 -5.75700  1.000 43.12000  ? 386 ASP B CA  1 
ATOM   6356  C  C   . ASP B  1 355 ? 18.10800  -40.36400 -5.73400  1.000 40.91000  ? 386 ASP B C   1 
ATOM   6357  O  O   . ASP B  1 355 ? 17.75600  -39.83900 -6.78900  1.000 42.47000  ? 386 ASP B O   1 
ATOM   6358  C  CB  . ASP B  1 355 ? 17.43000  -42.74700 -6.05600  1.000 45.07000  ? 386 ASP B CB  1 
ATOM   6359  C  CG  . ASP B  1 355 ? 17.88600  -44.14300 -6.50500  1.000 49.23000  ? 386 ASP B CG  1 
ATOM   6360  O  OD1 . ASP B  1 355 ? 18.89900  -44.25100 -7.22800  1.000 56.48000  ? 386 ASP B OD1 1 
ATOM   6361  O  OD2 . ASP B  1 355 ? 17.23800  -45.14300 -6.12300  1.000 46.11000  ? 386 ASP B OD2 1 
ATOM   6362  N  N   . GLY B  1 356 ? 18.10700  -39.70100 -4.58300  1.000 43.30000  ? 387 GLY B N   1 
ATOM   6363  C  CA  . GLY B  1 356 ? 17.70600  -38.30800 -4.47900  1.000 41.73000  ? 387 GLY B CA  1 
ATOM   6364  C  C   . GLY B  1 356 ? 18.91100  -37.39800 -4.33100  1.000 44.34000  ? 387 GLY B C   1 
ATOM   6365  O  O   . GLY B  1 356 ? 20.04500  -37.76500 -4.65700  1.000 47.91000  ? 387 GLY B O   1 
ATOM   6366  N  N   . LYS B  1 357 ? 18.65300  -36.16900 -3.89300  1.000 43.56000  ? 388 LYS B N   1 
ATOM   6367  C  CA  . LYS B  1 357 ? 19.70900  -35.18800 -3.71300  1.000 45.11000  ? 388 LYS B CA  1 
ATOM   6368  C  C   . LYS B  1 357 ? 19.35000  -34.25900 -2.56000  1.000 46.40000  ? 388 LYS B C   1 
ATOM   6369  O  O   . LYS B  1 357 ? 18.18500  -34.13700 -2.17000  1.000 45.65000  ? 388 LYS B O   1 
ATOM   6370  C  CB  . LYS B  1 357 ? 19.94800  -34.39100 -4.98600  1.000 48.06000  ? 388 LYS B CB  1 
ATOM   6371  C  CG  . LYS B  1 357 ? 18.87600  -33.39600 -5.27400  1.000 42.11000  ? 388 LYS B CG  1 
ATOM   6372  C  CD  . LYS B  1 357 ? 19.01100  -32.94000 -6.70000  1.000 46.14000  ? 388 LYS B CD  1 
ATOM   6373  C  CE  . LYS B  1 357 ? 19.00800  -34.16800 -7.61700  1.000 49.77000  ? 388 LYS B CE  1 
ATOM   6374  N  NZ  . LYS B  1 357 ? 18.71600  -33.81700 -9.04600  1.000 52.66000  ? 388 LYS B NZ  1 
ATOM   6375  N  N   . ASN B  1 358 ? 20.38000  -33.62900 -2.00500  1.000 42.25000  ? 389 ASN B N   1 
ATOM   6376  C  CA  . ASN B  1 358 ? 20.23100  -32.57000 -1.00700  1.000 43.01000  ? 389 ASN B CA  1 
ATOM   6377  C  C   . ASN B  1 358 ? 19.64300  -31.31000 -1.62900  1.000 42.08000  ? 389 ASN B C   1 
ATOM   6378  O  O   . ASN B  1 358 ? 20.27900  -30.66800 -2.46500  1.000 44.84000  ? 389 ASN B O   1 
ATOM   6379  C  CB  . ASN B  1 358 ? 21.60100  -32.28400 -0.38500  1.000 42.88000  ? 389 ASN B CB  1 
ATOM   6380  C  CG  . ASN B  1 358 ? 21.60000  -31.10800 0.59300   1.000 50.30000  ? 389 ASN B CG  1 
ATOM   6381  O  OD1 . ASN B  1 358 ? 20.59600  -30.41900 0.80700   1.000 48.51000  ? 389 ASN B OD1 1 
ATOM   6382  N  ND2 . ASN B  1 358 ? 22.74700  -30.91100 1.23800   1.000 53.18000  ? 389 ASN B ND2 1 
ATOM   6383  N  N   . ILE B  1 359 ? 18.46600  -30.90100 -1.16600  1.000 43.73000  ? 390 ILE B N   1 
ATOM   6384  C  CA  . ILE B  1 359 ? 17.76700  -29.78600 -1.78500  1.000 44.85000  ? 390 ILE B CA  1 
ATOM   6385  C  C   . ILE B  1 359 ? 17.74500  -28.56000 -0.89100  1.000 39.87000  ? 390 ILE B C   1 
ATOM   6386  O  O   . ILE B  1 359 ? 17.16300  -27.53700 -1.27500  1.000 40.25000  ? 390 ILE B O   1 
ATOM   6387  C  CB  . ILE B  1 359 ? 16.33500  -30.17900 -2.20300  1.000 47.22000  ? 390 ILE B CB  1 
ATOM   6388  C  CG1 . ILE B  1 359 ? 15.45100  -30.45000 -0.96500  1.000 44.35000  ? 390 ILE B CG1 1 
ATOM   6389  C  CG2 . ILE B  1 359 ? 16.36800  -31.38000 -3.14500  1.000 42.04000  ? 390 ILE B CG2 1 
ATOM   6390  C  CD1 . ILE B  1 359 ? 13.95600  -30.62400 -1.28400  1.000 37.42000  ? 390 ILE B CD1 1 
ATOM   6391  N  N   . MET B  1 360 ? 18.43300  -28.59900 0.25100   1.000 40.26000  ? 391 MET B N   1 
ATOM   6392  C  CA  . MET B  1 360 ? 18.32800  -27.48900 1.20300   1.000 48.10000  ? 391 MET B CA  1 
ATOM   6393  C  C   . MET B  1 360 ? 18.82400  -26.18400 0.58800   1.000 46.23000  ? 391 MET B C   1 
ATOM   6394  O  O   . MET B  1 360 ? 18.15400  -25.14800 0.68500   1.000 50.10000  ? 391 MET B O   1 
ATOM   6395  C  CB  . MET B  1 360 ? 19.11000  -27.80300 2.48600   1.000 39.98000  ? 391 MET B CB  1 
ATOM   6396  C  CG  . MET B  1 360 ? 18.85400  -26.80100 3.59100   1.000 42.54000  ? 391 MET B CG  1 
ATOM   6397  S  SD  . MET B  1 360 ? 17.10100  -26.38300 3.75700   1.000 46.91000  ? 391 MET B SD  1 
ATOM   6398  C  CE  . MET B  1 360 ? 16.47200  -27.87600 4.56500   1.000 42.36000  ? 391 MET B CE  1 
ATOM   6399  N  N   . ASP B  1 361 ? 19.95700  -26.23600 -0.11200  1.000 47.04000  ? 392 ASP B N   1 
ATOM   6400  C  CA  . ASP B  1 361 ? 20.47100  -25.05700 -0.79900  1.000 52.87000  ? 392 ASP B CA  1 
ATOM   6401  C  C   . ASP B  1 361 ? 19.51900  -24.60800 -1.90400  1.000 50.00000  ? 392 ASP B C   1 
ATOM   6402  O  O   . ASP B  1 361 ? 19.23800  -23.41100 -2.03500  1.000 52.89000  ? 392 ASP B O   1 
ATOM   6403  C  CB  . ASP B  1 361 ? 21.87800  -25.35500 -1.34000  1.000 58.94000  ? 392 ASP B CB  1 
ATOM   6404  C  CG  . ASP B  1 361 ? 22.73500  -24.10500 -1.45800  1.000 73.07000  ? 392 ASP B CG  1 
ATOM   6405  O  OD1 . ASP B  1 361 ? 22.47500  -23.12900 -0.71100  1.000 70.87000  ? 392 ASP B OD1 1 
ATOM   6406  O  OD2 . ASP B  1 361 ? 23.69800  -24.11200 -2.26100  1.000 84.49000  ? 392 ASP B OD2 1 
ATOM   6407  N  N   . ASP B  1 362 ? 19.01100  -25.55600 -2.71000  1.000 51.44000  ? 393 ASP B N   1 
ATOM   6408  C  CA  . ASP B  1 362 ? 17.98600  -25.23600 -3.70700  1.000 46.77000  ? 393 ASP B CA  1 
ATOM   6409  C  C   . ASP B  1 362 ? 16.76700  -24.57000 -3.08300  1.000 48.22000  ? 393 ASP B C   1 
ATOM   6410  O  O   . ASP B  1 362 ? 16.13600  -23.70800 -3.70000  1.000 50.26000  ? 393 ASP B O   1 
ATOM   6411  C  CB  . ASP B  1 362 ? 17.52100  -26.49700 -4.44300  1.000 52.46000  ? 393 ASP B CB  1 
ATOM   6412  C  CG  . ASP B  1 362 ? 18.60500  -27.13900 -5.28900  1.000 55.73000  ? 393 ASP B CG  1 
ATOM   6413  O  OD1 . ASP B  1 362 ? 19.20400  -26.43200 -6.12600  1.000 59.39000  ? 393 ASP B OD1 1 
ATOM   6414  O  OD2 . ASP B  1 362 ? 18.82700  -28.36200 -5.13700  1.000 53.45000  ? 393 ASP B OD2 1 
ATOM   6415  N  N   . VAL B  1 363 ? 16.35800  -25.02600 -1.90000  1.000 53.32000  ? 394 VAL B N   1 
ATOM   6416  C  CA  . VAL B  1 363 ? 15.19300  -24.44400 -1.24400  1.000 50.46000  ? 394 VAL B CA  1 
ATOM   6417  C  C   . VAL B  1 363 ? 15.48600  -23.01700 -0.78200  1.000 53.82000  ? 394 VAL B C   1 
ATOM   6418  O  O   . VAL B  1 363 ? 14.64100  -22.12200 -0.90100  1.000 48.03000  ? 394 VAL B O   1 
ATOM   6419  C  CB  . VAL B  1 363 ? 14.76600  -25.34600 -0.07400  1.000 52.42000  ? 394 VAL B CB  1 
ATOM   6420  C  CG1 . VAL B  1 363 ? 13.73800  -24.64500 0.79700   1.000 55.28000  ? 394 VAL B CG1 1 
ATOM   6421  C  CG2 . VAL B  1 363 ? 14.24200  -26.64100 -0.59800  1.000 50.61000  ? 394 VAL B CG2 1 
ATOM   6422  N  N   . LEU B  1 364 ? 16.69100  -22.78000 -0.25200  1.000 53.95000  ? 395 LEU B N   1 
ATOM   6423  C  CA  . LEU B  1 364 ? 17.01100  -21.45100 0.26400   1.000 56.10000  ? 395 LEU B CA  1 
ATOM   6424  C  C   . LEU B  1 364 ? 17.16900  -20.42500 -0.85200  1.000 55.80000  ? 395 LEU B C   1 
ATOM   6425  O  O   . LEU B  1 364 ? 16.81300  -19.25500 -0.66300  1.000 57.00000  ? 395 LEU B O   1 
ATOM   6426  C  CB  . LEU B  1 364 ? 18.28500  -21.51500 1.11700   1.000 46.08000  ? 395 LEU B CB  1 
ATOM   6427  C  CG  . LEU B  1 364 ? 18.10400  -22.29200 2.42400   1.000 50.09000  ? 395 LEU B CG  1 
ATOM   6428  C  CD1 . LEU B  1 364 ? 19.41400  -22.60000 3.12100   1.000 51.23000  ? 395 LEU B CD1 1 
ATOM   6429  C  CD2 . LEU B  1 364 ? 17.16700  -21.54800 3.34900   1.000 46.57000  ? 395 LEU B CD2 1 
ATOM   6430  N  N   . LYS B  1 365 ? 17.64600  -20.83900 -2.03000  1.000 54.14000  ? 396 LYS B N   1 
ATOM   6431  C  CA  . LYS B  1 365 ? 17.85900  -19.91000 -3.13900  1.000 56.24000  ? 396 LYS B CA  1 
ATOM   6432  C  C   . LYS B  1 365 ? 16.82700  -20.03200 -4.25000  1.000 54.48000  ? 396 LYS B C   1 
ATOM   6433  O  O   . LYS B  1 365 ? 16.99000  -19.39100 -5.29000  1.000 62.51000  ? 396 LYS B O   1 
ATOM   6434  C  CB  . LYS B  1 365 ? 19.26100  -20.08200 -3.71200  1.000 57.60000  ? 396 LYS B CB  1 
ATOM   6435  C  CG  . LYS B  1 365 ? 20.35100  -19.74000 -2.70500  1.000 53.57000  ? 396 LYS B CG  1 
ATOM   6436  C  CD  . LYS B  1 365 ? 21.45200  -20.76800 -2.76000  1.000 61.99000  ? 396 LYS B CD  1 
ATOM   6437  C  CE  . LYS B  1 365 ? 22.73300  -20.24900 -2.14100  1.000 67.52000  ? 396 LYS B CE  1 
ATOM   6438  N  NZ  . LYS B  1 365 ? 23.88100  -21.15100 -2.49500  1.000 68.48000  ? 396 LYS B NZ  1 
ATOM   6439  N  N   . ASN B  1 366 ? 15.77500  -20.82800 -4.05800  1.000 54.12000  ? 397 ASN B N   1 
ATOM   6440  C  CA  . ASN B  1 366 ? 14.72700  -21.06000 -5.06000  1.000 56.00000  ? 397 ASN B CA  1 
ATOM   6441  C  C   . ASN B  1 366 ? 15.32200  -21.48500 -6.40400  1.000 56.62000  ? 397 ASN B C   1 
ATOM   6442  O  O   . ASN B  1 366 ? 15.08100  -20.87500 -7.44500  1.000 48.40000  ? 397 ASN B O   1 
ATOM   6443  C  CB  . ASN B  1 366 ? 13.83400  -19.83100 -5.23800  1.000 47.03000  ? 397 ASN B CB  1 
ATOM   6444  C  CG  . ASN B  1 366 ? 12.51400  -20.18500 -5.84700  1.000 56.58000  ? 397 ASN B CG  1 
ATOM   6445  O  OD1 . ASN B  1 366 ? 12.08000  -21.33700 -5.75600  1.000 55.40000  ? 397 ASN B OD1 1 
ATOM   6446  N  ND2 . ASN B  1 366 ? 11.86000  -19.21500 -6.47900  1.000 47.63000  ? 397 ASN B ND2 1 
ATOM   6447  N  N   . THR B  1 367 ? 16.04500  -22.60600 -6.36500  1.000 51.31000  ? 398 THR B N   1 
ATOM   6448  C  CA  . THR B  1 367 ? 16.69600  -23.19300 -7.52200  1.000 51.28000  ? 398 THR B CA  1 
ATOM   6449  C  C   . THR B  1 367 ? 16.13700  -24.58600 -7.78300  1.000 55.39000  ? 398 THR B C   1 
ATOM   6450  O  O   . THR B  1 367 ? 15.81900  -25.32700 -6.84600  1.000 53.93000  ? 398 THR B O   1 
ATOM   6451  C  CB  . THR B  1 367 ? 18.20300  -23.29700 -7.26500  1.000 56.39000  ? 398 THR B CB  1 
ATOM   6452  O  OG1 . THR B  1 367 ? 18.74300  -21.97800 -7.16200  1.000 66.04000  ? 398 THR B OG1 1 
ATOM   6453  C  CG2 . THR B  1 367 ? 18.91500  -24.06800 -8.37400  1.000 53.61000  ? 398 THR B CG2 1 
ATOM   6454  N  N   . GLU B  1 368 ? 16.13600  -24.97500 -9.06000  1.000 48.93000  ? 399 GLU B N   1 
ATOM   6455  C  CA  . GLU B  1 368 ? 15.50700  -26.19100 -9.54400  1.000 49.61000  ? 399 GLU B CA  1 
ATOM   6456  C  C   . GLU B  1 368 ? 16.39100  -27.41300 -9.31000  1.000 53.66000  ? 399 GLU B C   1 
ATOM   6457  O  O   . GLU B  1 368 ? 17.42200  -27.57100 -9.97300  1.000 58.96000  ? 399 GLU B O   1 
ATOM   6458  C  CB  . GLU B  1 368 ? 15.19900  -26.02300 -11.02700 1.000 52.72000  ? 399 GLU B CB  1 
ATOM   6459  C  CG  . GLU B  1 368 ? 14.42500  -27.16700 -11.61100 1.000 58.48000  ? 399 GLU B CG  1 
ATOM   6460  C  CD  . GLU B  1 368 ? 13.98600  -26.89800 -13.03400 1.000 57.58000  ? 399 GLU B CD  1 
ATOM   6461  O  OE1 . GLU B  1 368 ? 14.38000  -25.85000 -13.58500 1.000 62.28000  ? 399 GLU B OE1 1 
ATOM   6462  O  OE2 . GLU B  1 368 ? 13.25300  -27.73600 -13.59600 1.000 57.86000  ? 399 GLU B OE2 1 
ATOM   6463  N  N   . PRO B  1 369 ? 16.02100  -28.31500 -8.39600  1.000 49.77000  ? 400 PRO B N   1 
ATOM   6464  C  CA  . PRO B  1 369 ? 16.87700  -29.48800 -8.14500  1.000 43.50000  ? 400 PRO B CA  1 
ATOM   6465  C  C   . PRO B  1 369 ? 16.84200  -30.55200 -9.23000  1.000 43.97000  ? 400 PRO B C   1 
ATOM   6466  O  O   . PRO B  1 369 ? 17.80400  -31.31600 -9.33700  1.000 45.80000  ? 400 PRO B O   1 
ATOM   6467  C  CB  . PRO B  1 369 ? 16.33100  -30.04200 -6.81600  1.000 41.19000  ? 400 PRO B CB  1 
ATOM   6468  C  CG  . PRO B  1 369 ? 14.94500  -29.53500 -6.74100  1.000 44.29000  ? 400 PRO B CG  1 
ATOM   6469  C  CD  . PRO B  1 369 ? 14.94000  -28.19300 -7.40200  1.000 44.42000  ? 400 PRO B CD  1 
ATOM   6470  N  N   . TYR B  1 370 ? 15.78000  -30.64500 -10.02400 1.000 42.29000  ? 401 TYR B N   1 
ATOM   6471  C  CA  . TYR B  1 370 ? 15.62000  -31.72200 -11.00000 1.000 50.94000  ? 401 TYR B CA  1 
ATOM   6472  C  C   . TYR B  1 370 ? 15.52600  -31.17800 -12.41800 1.000 53.25000  ? 401 TYR B C   1 
ATOM   6473  O  O   . TYR B  1 370 ? 14.78600  -31.72700 -13.24300 1.000 54.67000  ? 401 TYR B O   1 
ATOM   6474  C  CB  . TYR B  1 370 ? 14.38400  -32.57400 -10.68600 1.000 44.19000  ? 401 TYR B CB  1 
ATOM   6475  C  CG  . TYR B  1 370 ? 14.62000  -33.52700 -9.53800  1.000 44.14000  ? 401 TYR B CG  1 
ATOM   6476  C  CD1 . TYR B  1 370 ? 15.11700  -34.80700 -9.76900  1.000 46.64000  ? 401 TYR B CD1 1 
ATOM   6477  C  CD2 . TYR B  1 370 ? 14.38600  -33.14000 -8.21800  1.000 42.03000  ? 401 TYR B CD2 1 
ATOM   6478  C  CE1 . TYR B  1 370 ? 15.36700  -35.68200 -8.72700  1.000 40.72000  ? 401 TYR B CE1 1 
ATOM   6479  C  CE2 . TYR B  1 370 ? 14.63300  -34.02000 -7.15200  1.000 38.76000  ? 401 TYR B CE2 1 
ATOM   6480  C  CZ  . TYR B  1 370 ? 15.12300  -35.28200 -7.42700  1.000 40.79000  ? 401 TYR B CZ  1 
ATOM   6481  O  OH  . TYR B  1 370 ? 15.36800  -36.16900 -6.42500  1.000 42.03000  ? 401 TYR B OH  1 
ATOM   6482  N  N   . LYS B  1 371 ? 16.22900  -30.07700 -12.70800 1.000 54.47000  ? 402 LYS B N   1 
ATOM   6483  C  CA  . LYS B  1 371 ? 16.18800  -29.52600 -14.06100 1.000 57.78000  ? 402 LYS B CA  1 
ATOM   6484  C  C   . LYS B  1 371 ? 16.70100  -30.56200 -15.02800 1.000 53.35000  ? 402 LYS B C   1 
ATOM   6485  O  O   . LYS B  1 371 ? 17.82600  -31.03500 -14.87600 1.000 51.61000  ? 402 LYS B O   1 
ATOM   6486  C  CB  . LYS B  1 371 ? 17.03300  -28.26100 -14.18100 1.000 62.65000  ? 402 LYS B CB  1 
ATOM   6487  C  CG  . LYS B  1 371 ? 16.88400  -27.56700 -15.55600 1.000 66.01000  ? 402 LYS B CG  1 
ATOM   6488  C  CD  . LYS B  1 371 ? 17.78100  -26.33500 -15.68400 1.000 62.28000  ? 402 LYS B CD  1 
ATOM   6489  C  CE  . LYS B  1 371 ? 17.16900  -25.30400 -16.61700 1.000 71.34000  ? 402 LYS B CE  1 
ATOM   6490  N  NZ  . LYS B  1 371 ? 17.40100  -23.90400 -16.14000 1.000 74.61000  ? 402 LYS B NZ  1 
ATOM   6491  N  N   . ASP B  1 372 ? 15.86900  -30.92300 -16.00700 1.000 51.58000  ? 403 ASP B N   1 
ATOM   6492  C  CA  . ASP B  1 372 ? 16.22600  -31.90800 -17.02300 1.000 55.84000  ? 403 ASP B CA  1 
ATOM   6493  C  C   . ASP B  1 372 ? 16.46300  -33.30200 -16.44700 1.000 53.20000  ? 403 ASP B C   1 
ATOM   6494  O  O   . ASP B  1 372 ? 17.14200  -34.12700 -17.07300 1.000 52.39000  ? 403 ASP B O   1 
ATOM   6495  C  CB  . ASP B  1 372 ? 17.43800  -31.43000 -17.83300 1.000 59.87000  ? 403 ASP B CB  1 
ATOM   6496  C  CG  . ASP B  1 372 ? 17.11300  -30.19900 -18.67300 1.000 61.63000  ? 403 ASP B CG  1 
ATOM   6497  O  OD1 . ASP B  1 372 ? 16.06200  -30.20500 -19.35600 1.000 64.24000  ? 403 ASP B OD1 1 
ATOM   6498  O  OD2 . ASP B  1 372 ? 17.86900  -29.21300 -18.62400 1.000 61.86000  ? 403 ASP B OD2 1 
ATOM   6499  N  N   . GLU B  1 373 ? 15.93900  -33.57600 -15.25100 1.000 53.24000  ? 404 GLU B N   1 
ATOM   6500  C  CA  . GLU B  1 373 ? 15.99900  -34.89400 -14.62100 1.000 50.19000  ? 404 GLU B CA  1 
ATOM   6501  C  C   . GLU B  1 373 ? 14.59400  -35.40200 -14.31300 1.000 54.31000  ? 404 GLU B C   1 
ATOM   6502  O  O   . GLU B  1 373 ? 13.62500  -34.63800 -14.23900 1.000 48.38000  ? 404 GLU B O   1 
ATOM   6503  C  CB  . GLU B  1 373 ? 16.79900  -34.86000 -13.31800 1.000 56.83000  ? 404 GLU B CB  1 
ATOM   6504  C  CG  . GLU B  1 373 ? 18.19700  -35.39000 -13.41900 1.000 66.77000  ? 404 GLU B CG  1 
ATOM   6505  C  CD  . GLU B  1 373 ? 19.15300  -34.27600 -13.67800 1.000 76.08000  ? 404 GLU B CD  1 
ATOM   6506  O  OE1 . GLU B  1 373 ? 18.79200  -33.45300 -14.55300 1.000 60.70000  ? 404 GLU B OE1 1 
ATOM   6507  O  OE2 . GLU B  1 373 ? 20.22100  -34.20800 -12.99600 1.000 72.17000  ? 404 GLU B OE2 1 
ATOM   6508  N  N   . MET B  1 374 ? 14.50600  -36.70200 -14.05300 1.000 52.40000  ? 405 MET B N   1 
ATOM   6509  C  CA  . MET B  1 374 ? 13.23200  -37.40000 -13.98400 1.000 45.91000  ? 405 MET B CA  1 
ATOM   6510  C  C   . MET B  1 374 ? 12.85300  -37.69300 -12.53700 1.000 47.28000  ? 405 MET B C   1 
ATOM   6511  O  O   . MET B  1 374 ? 13.71400  -37.96400 -11.69600 1.000 41.77000  ? 405 MET B O   1 
ATOM   6512  C  CB  . MET B  1 374 ? 13.28600  -38.72600 -14.75300 1.000 43.51000  ? 405 MET B CB  1 
ATOM   6513  C  CG  . MET B  1 374 ? 13.20000  -38.63100 -16.26700 1.000 48.48000  ? 405 MET B CG  1 
ATOM   6514  S  SD  . MET B  1 374 ? 11.53300  -38.31300 -16.93100 1.000 50.66000  ? 405 MET B SD  1 
ATOM   6515  C  CE  . MET B  1 374 ? 11.55900  -39.41200 -18.32400 1.000 46.29000  ? 405 MET B CE  1 
ATOM   6516  N  N   . ILE B  1 375 ? 11.55800  -37.61900 -12.24800 1.000 45.83000  ? 406 ILE B N   1 
ATOM   6517  C  CA  . ILE B  1 375 ? 10.97800  -38.19700 -11.04300 1.000 42.35000  ? 406 ILE B CA  1 
ATOM   6518  C  C   . ILE B  1 375 ? 9.97700   -39.24500 -11.51700 1.000 41.91000  ? 406 ILE B C   1 
ATOM   6519  O  O   . ILE B  1 375 ? 9.07300   -38.93400 -12.30200 1.000 41.43000  ? 406 ILE B O   1 
ATOM   6520  C  CB  . ILE B  1 375 ? 10.33300  -37.12900 -10.15400 1.000 38.23000  ? 406 ILE B CB  1 
ATOM   6521  C  CG1 . ILE B  1 375 ? 11.43800  -36.29600 -9.49800  1.000 44.07000  ? 406 ILE B CG1 1 
ATOM   6522  C  CG2 . ILE B  1 375 ? 9.47500   -37.79300 -9.09700  1.000 37.42000  ? 406 ILE B CG2 1 
ATOM   6523  C  CD1 . ILE B  1 375 ? 10.96500  -34.99400 -8.83500  1.000 43.87000  ? 406 ILE B CD1 1 
ATOM   6524  N  N   . TYR B  1 376 ? 10.16300  -40.47600 -11.06300 1.000 42.10000  ? 407 TYR B N   1 
ATOM   6525  C  CA  . TYR B  1 376 ? 9.53200   -41.66900 -11.59400 1.000 39.21000  ? 407 TYR B CA  1 
ATOM   6526  C  C   . TYR B  1 376 ? 8.55200   -42.26500 -10.59800 1.000 45.51000  ? 407 TYR B C   1 
ATOM   6527  O  O   . TYR B  1 376 ? 8.65200   -42.05600 -9.37800  1.000 43.63000  ? 407 TYR B O   1 
ATOM   6528  C  CB  . TYR B  1 376 ? 10.55600  -42.76500 -11.87500 1.000 43.50000  ? 407 TYR B CB  1 
ATOM   6529  C  CG  . TYR B  1 376 ? 11.61700  -42.46300 -12.90300 1.000 47.49000  ? 407 TYR B CG  1 
ATOM   6530  C  CD1 . TYR B  1 376 ? 11.28400  -42.17900 -14.21200 1.000 42.50000  ? 407 TYR B CD1 1 
ATOM   6531  C  CD2 . TYR B  1 376 ? 12.96100  -42.58200 -12.58100 1.000 48.20000  ? 407 TYR B CD2 1 
ATOM   6532  C  CE1 . TYR B  1 376 ? 12.25200  -41.94900 -15.16000 1.000 49.91000  ? 407 TYR B CE1 1 
ATOM   6533  C  CE2 . TYR B  1 376 ? 13.95100  -42.35900 -13.53600 1.000 49.79000  ? 407 TYR B CE2 1 
ATOM   6534  C  CZ  . TYR B  1 376 ? 13.57900  -42.04700 -14.82300 1.000 50.85000  ? 407 TYR B CZ  1 
ATOM   6535  O  OH  . TYR B  1 376 ? 14.53200  -41.80900 -15.78500 1.000 58.80000  ? 407 TYR B OH  1 
ATOM   6536  N  N   . SER B  1 377 ? 7.67900   -43.10400 -11.14100 1.000 35.16000  ? 408 SER B N   1 
ATOM   6537  C  CA  . SER B  1 377 ? 6.90200   -44.05000 -10.36300 1.000 41.83000  ? 408 SER B CA  1 
ATOM   6538  C  C   . SER B  1 377 ? 6.58600   -45.24900 -11.25600 1.000 41.09000  ? 408 SER B C   1 
ATOM   6539  O  O   . SER B  1 377 ? 6.18200   -45.08600 -12.40900 1.000 44.50000  ? 408 SER B O   1 
ATOM   6540  C  CB  . SER B  1 377 ? 5.59900   -43.40800 -9.84900  1.000 40.97000  ? 408 SER B CB  1 
ATOM   6541  O  OG  . SER B  1 377 ? 4.80400   -44.35600 -9.16200  1.000 38.94000  ? 408 SER B OG  1 
ATOM   6542  N  N   . LEU B  1 378 ? 6.73800   -46.44800 -10.71400 1.000 34.38000  ? 409 LEU B N   1 
ATOM   6543  C  CA  . LEU B  1 378 ? 6.29200   -47.64900 -11.41400 1.000 40.93000  ? 409 LEU B CA  1 
ATOM   6544  C  C   . LEU B  1 378 ? 5.63800   -48.56700 -10.39100 1.000 39.81000  ? 409 LEU B C   1 
ATOM   6545  O  O   . LEU B  1 378 ? 6.25900   -48.89700 -9.37000  1.000 35.58000  ? 409 LEU B O   1 
ATOM   6546  C  CB  . LEU B  1 378 ? 7.45100   -48.36200 -12.12300 1.000 36.40000  ? 409 LEU B CB  1 
ATOM   6547  C  CG  . LEU B  1 378 ? 7.04400   -49.55800 -12.97800 1.000 36.92000  ? 409 LEU B CG  1 
ATOM   6548  C  CD1 . LEU B  1 378 ? 8.00000   -49.69500 -14.15600 1.000 44.10000  ? 409 LEU B CD1 1 
ATOM   6549  C  CD2 . LEU B  1 378 ? 6.98000   -50.86700 -12.18200 1.000 34.92000  ? 409 LEU B CD2 1 
ATOM   6550  N  N   . ARG B  1 379 ? 4.37800   -48.94800 -10.64000 1.000 35.56000  ? 410 ARG B N   1 
ATOM   6551  C  CA  . ARG B  1 379 ? 3.61400   -49.77200 -9.70300  1.000 33.43000  ? 410 ARG B CA  1 
ATOM   6552  C  C   . ARG B  1 379 ? 3.20300   -51.06400 -10.38600 1.000 36.48000  ? 410 ARG B C   1 
ATOM   6553  O  O   . ARG B  1 379 ? 2.54200   -51.04100 -11.43000 1.000 39.40000  ? 410 ARG B O   1 
ATOM   6554  C  CB  . ARG B  1 379 ? 2.39100   -49.01700 -9.17700  1.000 37.82000  ? 410 ARG B CB  1 
ATOM   6555  C  CG  . ARG B  1 379 ? 1.57200   -49.78100 -8.15300  1.000 36.98000  ? 410 ARG B CG  1 
ATOM   6556  C  CD  . ARG B  1 379 ? 0.23000   -50.19900 -8.71700  1.000 35.14000  ? 410 ARG B CD  1 
ATOM   6557  N  NE  . ARG B  1 379 ? -0.31600  -51.32800 -7.97100  1.000 36.38000  ? 410 ARG B NE  1 
ATOM   6558  C  CZ  . ARG B  1 379 ? -1.12000  -51.22200 -6.92500  1.000 37.60000  ? 410 ARG B CZ  1 
ATOM   6559  N  NH1 . ARG B  1 379 ? -1.51300  -50.04000 -6.47100  1.000 38.28000  ? 410 ARG B NH1 1 
ATOM   6560  N  NH2 . ARG B  1 379 ? -1.50400  -52.32600 -6.29100  1.000 33.27000  ? 410 ARG B NH2 1 
ATOM   6561  N  N   . TYR B  1 380 ? 3.57800   -52.18200 -9.79700  1.000 37.26000  ? 411 TYR B N   1 
ATOM   6562  C  CA  . TYR B  1 380 ? 3.25100   -53.46700 -10.39200 1.000 35.85000  ? 411 TYR B CA  1 
ATOM   6563  C  C   . TYR B  1 380 ? 1.76900   -53.73800 -10.21000 1.000 42.71000  ? 411 TYR B C   1 
ATOM   6564  O  O   . TYR B  1 380 ? 1.20800   -53.51100 -9.13200  1.000 38.57000  ? 411 TYR B O   1 
ATOM   6565  C  CB  . TYR B  1 380 ? 4.07100   -54.57800 -9.72900  1.000 45.09000  ? 411 TYR B CB  1 
ATOM   6566  C  CG  . TYR B  1 380 ? 5.58300   -54.41200 -9.84200  1.000 47.81000  ? 411 TYR B CG  1 
ATOM   6567  C  CD1 . TYR B  1 380 ? 6.20600   -54.46900 -11.07300 1.000 42.58000  ? 411 TYR B CD1 1 
ATOM   6568  C  CD2 . TYR B  1 380 ? 6.37600   -54.22400 -8.71800  1.000 47.36000  ? 411 TYR B CD2 1 
ATOM   6569  C  CE1 . TYR B  1 380 ? 7.54300   -54.31800 -11.19400 1.000 41.45000  ? 411 TYR B CE1 1 
ATOM   6570  C  CE2 . TYR B  1 380 ? 7.75400   -54.08400 -8.83200  1.000 49.08000  ? 411 TYR B CE2 1 
ATOM   6571  C  CZ  . TYR B  1 380 ? 8.32200   -54.14400 -10.08400 1.000 45.10000  ? 411 TYR B CZ  1 
ATOM   6572  O  OH  . TYR B  1 380 ? 9.67600   -54.01200 -10.26400 1.000 49.31000  ? 411 TYR B OH  1 
ATOM   6573  N  N   . ARG B  1 381 ? 1.13600   -54.22700 -11.26300 1.000 41.99000  ? 412 ARG B N   1 
ATOM   6574  C  CA  . ARG B  1 381 ? -0.24600  -54.66900 -11.22100 1.000 36.64000  ? 412 ARG B CA  1 
ATOM   6575  C  C   . ARG B  1 381 ? -0.27400  -56.17200 -11.53200 1.000 48.69000  ? 412 ARG B C   1 
ATOM   6576  O  O   . ARG B  1 381 ? 0.77300   -56.82000 -11.68500 1.000 42.01000  ? 412 ARG B O   1 
ATOM   6577  C  CB  . ARG B  1 381 ? -1.09100  -53.86100 -12.19700 1.000 37.86000  ? 412 ARG B CB  1 
ATOM   6578  C  CG  . ARG B  1 381 ? -1.22100  -52.39700 -11.82500 1.000 40.02000  ? 412 ARG B CG  1 
ATOM   6579  C  CD  . ARG B  1 381 ? -2.26000  -52.22200 -10.73400 1.000 36.90000  ? 412 ARG B CD  1 
ATOM   6580  N  NE  . ARG B  1 381 ? -2.49300  -50.82100 -10.38900 1.000 39.45000  ? 412 ARG B NE  1 
ATOM   6581  C  CZ  . ARG B  1 381 ? -3.27500  -50.43400 -9.38600  1.000 42.02000  ? 412 ARG B CZ  1 
ATOM   6582  N  NH1 . ARG B  1 381 ? -3.86200  -51.31700 -8.58800  1.000 37.64000  ? 412 ARG B NH1 1 
ATOM   6583  N  NH2 . ARG B  1 381 ? -3.52500  -49.13600 -9.21600  1.000 30.76000  ? 412 ARG B NH2 1 
ATOM   6584  N  N   . GLU B  1 382 ? -1.47800  -56.73400 -11.64000 1.000 40.15000  ? 413 GLU B N   1 
ATOM   6585  C  CA  . GLU B  1 382 ? -1.61400  -58.17500 -11.85600 1.000 42.72000  ? 413 GLU B CA  1 
ATOM   6586  C  C   . GLU B  1 382 ? -1.46900  -58.44900 -13.34800 1.000 42.86000  ? 413 GLU B C   1 
ATOM   6587  O  O   . GLU B  1 382 ? -2.43600  -58.72100 -14.06000 1.000 43.17000  ? 413 GLU B O   1 
ATOM   6588  C  CB  . GLU B  1 382 ? -2.94700  -58.67900 -11.30900 1.000 46.64000  ? 413 GLU B CB  1 
ATOM   6589  C  CG  . GLU B  1 382 ? -3.22600  -58.20800 -9.86400  1.000 47.17000  ? 413 GLU B CG  1 
ATOM   6590  C  CD  . GLU B  1 382 ? -2.06200  -58.49600 -8.93000  1.000 53.34000  ? 413 GLU B CD  1 
ATOM   6591  O  OE1 . GLU B  1 382 ? -1.66800  -59.68500 -8.92400  1.000 53.25000  ? 413 GLU B OE1 1 
ATOM   6592  O  OE2 . GLU B  1 382 ? -1.53500  -57.55800 -8.23200  1.000 50.92000  ? 413 GLU B OE2 1 
ATOM   6593  N  N   . GLY B  1 383 ? -0.21500  -58.40700 -13.82600 1.000 47.29000  ? 414 GLY B N   1 
ATOM   6594  C  CA  . GLY B  1 383 ? 0.08300   -58.71900 -15.21200 1.000 39.49000  ? 414 GLY B CA  1 
ATOM   6595  C  C   . GLY B  1 383 ? 0.53700   -57.56400 -16.07600 1.000 45.16000  ? 414 GLY B C   1 
ATOM   6596  O  O   . GLY B  1 383 ? 0.67600   -57.74700 -17.29500 1.000 42.37000  ? 414 GLY B O   1 
ATOM   6597  N  N   . TYR B  1 384 ? 0.69800   -56.36800 -15.51800 1.000 40.51000  ? 415 TYR B N   1 
ATOM   6598  C  CA  . TYR B  1 384 ? 1.16100   -55.21000 -16.27500 1.000 33.69000  ? 415 TYR B CA  1 
ATOM   6599  C  C   . TYR B  1 384 ? 1.67100   -54.20900 -15.24800 1.000 40.15000  ? 415 TYR B C   1 
ATOM   6600  O  O   . TYR B  1 384 ? 1.66100   -54.48200 -14.04200 1.000 39.44000  ? 415 TYR B O   1 
ATOM   6601  C  CB  . TYR B  1 384 ? 0.04600   -54.65700 -17.18100 1.000 40.17000  ? 415 TYR B CB  1 
ATOM   6602  C  CG  . TYR B  1 384 ? -1.11800  -54.09200 -16.38500 1.000 41.43000  ? 415 TYR B CG  1 
ATOM   6603  C  CD1 . TYR B  1 384 ? -2.12600  -54.92400 -15.90400 1.000 39.00000  ? 415 TYR B CD1 1 
ATOM   6604  C  CD2 . TYR B  1 384 ? -1.20200  -52.73400 -16.10900 1.000 39.23000  ? 415 TYR B CD2 1 
ATOM   6605  C  CE1 . TYR B  1 384 ? -3.17900  -54.41800 -15.14700 1.000 40.79000  ? 415 TYR B CE1 1 
ATOM   6606  C  CE2 . TYR B  1 384 ? -2.26400  -52.21200 -15.36700 1.000 42.90000  ? 415 TYR B CE2 1 
ATOM   6607  C  CZ  . TYR B  1 384 ? -3.24400  -53.05900 -14.88300 1.000 39.87000  ? 415 TYR B CZ  1 
ATOM   6608  O  OH  . TYR B  1 384 ? -4.28000  -52.54000 -14.13600 1.000 37.56000  ? 415 TYR B OH  1 
ATOM   6609  N  N   . ASN B  1 385 ? 2.15800   -53.06400 -15.71800 1.000 35.78000  ? 416 ASN B N   1 
ATOM   6610  C  CA  . ASN B  1 385 ? 2.65600   -52.04600 -14.80700 1.000 37.93000  ? 416 ASN B CA  1 
ATOM   6611  C  C   . ASN B  1 385 ? 2.02600   -50.69600 -15.09900 1.000 37.64000  ? 416 ASN B C   1 
ATOM   6612  O  O   . ASN B  1 385 ? 1.89900   -50.29800 -16.26300 1.000 35.85000  ? 416 ASN B O   1 
ATOM   6613  C  CB  . ASN B  1 385 ? 4.18800   -51.93300 -14.89300 1.000 42.19000  ? 416 ASN B CB  1 
ATOM   6614  C  CG  . ASN B  1 385 ? 4.88300   -53.26000 -14.62400 1.000 45.01000  ? 416 ASN B CG  1 
ATOM   6615  O  OD1 . ASN B  1 385 ? 4.61500   -53.93200 -13.62300 1.000 44.72000  ? 416 ASN B OD1 1 
ATOM   6616  N  ND2 . ASN B  1 385 ? 5.72000   -53.68500 -15.57100 1.000 46.68000  ? 416 ASN B ND2 1 
ATOM   6617  N  N   . ASP B  1 386 ? 1.69000   -49.97300 -14.02500 1.000 38.28000  ? 417 ASP B N   1 
ATOM   6618  C  CA  . ASP B  1 386 ? 1.32300   -48.56700 -14.08500 1.000 36.71000  ? 417 ASP B CA  1 
ATOM   6619  C  C   . ASP B  1 386 ? 2.60500   -47.73400 -13.97500 1.000 36.52000  ? 417 ASP B C   1 
ATOM   6620  O  O   . ASP B  1 386 ? 3.47100   -48.03400 -13.15800 1.000 38.96000  ? 417 ASP B O   1 
ATOM   6621  C  CB  . ASP B  1 386 ? 0.36500   -48.21900 -12.93000 1.000 35.31000  ? 417 ASP B CB  1 
ATOM   6622  C  CG  . ASP B  1 386 ? -1.07400  -48.77900 -13.10400 1.000 38.94000  ? 417 ASP B CG  1 
ATOM   6623  O  OD1 . ASP B  1 386 ? -1.56100  -48.95600 -14.24700 1.000 40.16000  ? 417 ASP B OD1 1 
ATOM   6624  O  OD2 . ASP B  1 386 ? -1.73100  -49.03700 -12.05800 1.000 37.90000  ? 417 ASP B OD2 1 
ATOM   6625  N  N   . VAL B  1 387 ? 2.73100   -46.68600 -14.79400 1.000 38.41000  ? 418 VAL B N   1 
ATOM   6626  C  CA  . VAL B  1 387 ? 3.95800   -45.89500 -14.83300 1.000 38.27000  ? 418 VAL B CA  1 
ATOM   6627  C  C   . VAL B  1 387 ? 3.60500   -44.41900 -14.77400 1.000 38.61000  ? 418 VAL B C   1 
ATOM   6628  O  O   . VAL B  1 387 ? 2.57000   -43.99300 -15.28700 1.000 36.08000  ? 418 VAL B O   1 
ATOM   6629  C  CB  . VAL B  1 387 ? 4.82700   -46.18700 -16.09700 1.000 32.90000  ? 418 VAL B CB  1 
ATOM   6630  C  CG1 . VAL B  1 387 ? 6.12000   -45.39000 -16.06200 1.000 35.56000  ? 418 VAL B CG1 1 
ATOM   6631  C  CG2 . VAL B  1 387 ? 5.20400   -47.65900 -16.15600 1.000 34.66000  ? 418 VAL B CG2 1 
ATOM   6632  N  N   . GLY B  1 388 ? 4.48600   -43.63600 -14.15400 1.000 38.78000  ? 419 GLY B N   1 
ATOM   6633  C  CA  . GLY B  1 388 ? 4.43500   -42.18700 -14.24700 1.000 32.34000  ? 419 GLY B CA  1 
ATOM   6634  C  C   . GLY B  1 388 ? 5.83100   -41.60500 -14.19200 1.000 36.09000  ? 419 GLY B C   1 
ATOM   6635  O  O   . GLY B  1 388 ? 6.68500   -42.11400 -13.46000 1.000 38.03000  ? 419 GLY B O   1 
ATOM   6636  N  N   . ALA B  1 389 ? 6.09900   -40.55800 -14.97000 1.000 42.45000  ? 420 ALA B N   1 
ATOM   6637  C  CA  . ALA B  1 389 ? 7.43900   -39.97300 -14.98100 1.000 44.26000  ? 420 ALA B CA  1 
ATOM   6638  C  C   . ALA B  1 389 ? 7.33400   -38.49500 -15.32500 1.000 37.84000  ? 420 ALA B C   1 
ATOM   6639  O  O   . ALA B  1 389 ? 6.73100   -38.14700 -16.34000 1.000 37.51000  ? 420 ALA B O   1 
ATOM   6640  C  CB  . ALA B  1 389 ? 8.33600   -40.70600 -15.98400 1.000 34.60000  ? 420 ALA B CB  1 
ATOM   6641  N  N   . ARG B  1 390 ? 7.91400   -37.63100 -14.48600 1.000 40.57000  ? 421 ARG B N   1 
ATOM   6642  C  CA  . ARG B  1 390 ? 7.82900   -36.18700 -14.68000 1.000 40.16000  ? 421 ARG B CA  1 
ATOM   6643  C  C   . ARG B  1 390 ? 9.22000   -35.57900 -14.86800 1.000 44.42000  ? 421 ARG B C   1 
ATOM   6644  O  O   . ARG B  1 390 ? 10.17300  -35.93500 -14.16200 1.000 41.84000  ? 421 ARG B O   1 
ATOM   6645  C  CB  . ARG B  1 390 ? 7.15000   -35.50900 -13.48600 1.000 37.60000  ? 421 ARG B CB  1 
ATOM   6646  C  CG  . ARG B  1 390 ? 6.93300   -34.00200 -13.68500 1.000 38.20000  ? 421 ARG B CG  1 
ATOM   6647  C  CD  . ARG B  1 390 ? 6.48400   -33.26800 -12.41300 1.000 37.03000  ? 421 ARG B CD  1 
ATOM   6648  N  NE  . ARG B  1 390 ? 6.50200   -31.83300 -12.63100 1.000 32.03000  ? 421 ARG B NE  1 
ATOM   6649  C  CZ  . ARG B  1 390 ? 5.78300   -30.96200 -11.94100 1.000 42.14000  ? 421 ARG B CZ  1 
ATOM   6650  N  NH1 . ARG B  1 390 ? 4.97900   -31.35400 -10.96000 1.000 39.33000  ? 421 ARG B NH1 1 
ATOM   6651  N  NH2 . ARG B  1 390 ? 5.82800   -29.67200 -12.27900 1.000 41.65000  ? 421 ARG B NH2 1 
ATOM   6652  N  N   . MET B  1 391 ? 9.32200   -34.66500 -15.83400 1.000 45.89000  ? 422 MET B N   1 
ATOM   6653  C  CA  . MET B  1 391 ? 10.50200  -33.82500 -16.04100 1.000 43.53000  ? 422 MET B CA  1 
ATOM   6654  C  C   . MET B  1 391 ? 10.00600  -32.43100 -16.39300 1.000 49.09000  ? 422 MET B C   1 
ATOM   6655  O  O   . MET B  1 391 ? 9.27900   -32.25500 -17.38100 1.000 46.19000  ? 422 MET B O   1 
ATOM   6656  C  CB  . MET B  1 391 ? 11.41800  -34.38900 -17.13800 1.000 44.00000  ? 422 MET B CB  1 
ATOM   6657  C  CG  . MET B  1 391 ? 12.78000  -33.69000 -17.24600 1.000 50.93000  ? 422 MET B CG  1 
ATOM   6658  S  SD  . MET B  1 391 ? 13.84900  -34.47400 -18.49600 1.000 52.72000  ? 422 MET B SD  1 
ATOM   6659  C  CE  . MET B  1 391 ? 12.79400  -34.31800 -19.91700 1.000 55.00000  ? 422 MET B CE  1 
ATOM   6660  N  N   . GLY B  1 392 ? 10.32500  -31.47100 -15.55300 1.000 43.99000  ? 423 GLY B N   1 
ATOM   6661  C  CA  . GLY B  1 392 ? 9.86700   -30.11000 -15.78300 1.000 43.71000  ? 423 GLY B CA  1 
ATOM   6662  C  C   . GLY B  1 392 ? 8.35100   -30.01500 -15.69800 1.000 47.81000  ? 423 GLY B C   1 
ATOM   6663  O  O   . GLY B  1 392 ? 7.73300   -30.49800 -14.74400 1.000 42.61000  ? 423 GLY B O   1 
ATOM   6664  N  N   . ASP B  1 393 ? 7.73400   -29.47200 -16.75200 1.000 45.52000  ? 424 ASP B N   1 
ATOM   6665  C  CA  . ASP B  1 393 ? 6.29500   -29.30700 -16.83700 1.000 43.50000  ? 424 ASP B CA  1 
ATOM   6666  C  C   . ASP B  1 393 ? 5.59300   -30.49100 -17.48400 1.000 42.75000  ? 424 ASP B C   1 
ATOM   6667  O  O   . ASP B  1 393 ? 4.37900   -30.43000 -17.67000 1.000 44.74000  ? 424 ASP B O   1 
ATOM   6668  C  CB  . ASP B  1 393 ? 5.92600   -28.04500 -17.63200 1.000 44.46000  ? 424 ASP B CB  1 
ATOM   6669  C  CG  . ASP B  1 393 ? 6.44800   -26.77700 -17.00500 1.000 48.54000  ? 424 ASP B CG  1 
ATOM   6670  O  OD1 . ASP B  1 393 ? 6.47100   -26.66600 -15.76800 1.000 48.81000  ? 424 ASP B OD1 1 
ATOM   6671  O  OD2 . ASP B  1 393 ? 6.79500   -25.85400 -17.75300 1.000 58.83000  ? 424 ASP B OD2 1 
ATOM   6672  N  N   . TRP B  1 394 ? 6.32100   -31.53300 -17.87700 1.000 41.92000  ? 425 TRP B N   1 
ATOM   6673  C  CA  . TRP B  1 394 ? 5.76500   -32.61900 -18.67600 1.000 47.58000  ? 425 TRP B CA  1 
ATOM   6674  C  C   . TRP B  1 394 ? 5.71100   -33.90300 -17.86600 1.000 40.24000  ? 425 TRP B C   1 
ATOM   6675  O  O   . TRP B  1 394 ? 6.62500   -34.20100 -17.09700 1.000 41.91000  ? 425 TRP B O   1 
ATOM   6676  C  CB  . TRP B  1 394 ? 6.57800   -32.81900 -19.96300 1.000 44.23000  ? 425 TRP B CB  1 
ATOM   6677  C  CG  . TRP B  1 394 ? 6.44800   -31.57800 -20.81600 1.000 49.79000  ? 425 TRP B CG  1 
ATOM   6678  C  CD1 . TRP B  1 394 ? 7.28600   -30.49000 -20.82100 1.000 44.84000  ? 425 TRP B CD1 1 
ATOM   6679  C  CD2 . TRP B  1 394 ? 5.39900   -31.27600 -21.73500 1.000 46.22000  ? 425 TRP B CD2 1 
ATOM   6680  N  NE1 . TRP B  1 394 ? 6.81700   -29.53800 -21.67800 1.000 44.57000  ? 425 TRP B NE1 1 
ATOM   6681  C  CE2 . TRP B  1 394 ? 5.67000   -29.99900 -22.27000 1.000 49.48000  ? 425 TRP B CE2 1 
ATOM   6682  C  CE3 . TRP B  1 394 ? 4.25700   -31.96300 -22.17000 1.000 49.10000  ? 425 TRP B CE3 1 
ATOM   6683  C  CZ2 . TRP B  1 394 ? 4.84400   -29.39700 -23.21400 1.000 46.67000  ? 425 TRP B CZ2 1 
ATOM   6684  C  CZ3 . TRP B  1 394 ? 3.43700   -31.36400 -23.11100 1.000 47.59000  ? 425 TRP B CZ3 1 
ATOM   6685  C  CH2 . TRP B  1 394 ? 3.73300   -30.09500 -23.62200 1.000 46.65000  ? 425 TRP B CH2 1 
ATOM   6686  N  N   . LYS B  1 395 ? 4.61500   -34.64200 -18.01300 1.000 44.10000  ? 426 LYS B N   1 
ATOM   6687  C  CA  . LYS B  1 395 ? 4.48600   -35.92500 -17.35200 1.000 40.89000  ? 426 LYS B CA  1 
ATOM   6688  C  C   . LYS B  1 395 ? 3.93300   -36.95300 -18.32400 1.000 40.87000  ? 426 LYS B C   1 
ATOM   6689  O  O   . LYS B  1 395 ? 2.99400   -36.66800 -19.08200 1.000 39.43000  ? 426 LYS B O   1 
ATOM   6690  C  CB  . LYS B  1 395 ? 3.56900   -35.86400 -16.14600 1.000 38.99000  ? 426 LYS B CB  1 
ATOM   6691  C  CG  . LYS B  1 395 ? 3.63000   -37.19900 -15.38600 1.000 41.37000  ? 426 LYS B CG  1 
ATOM   6692  C  CD  . LYS B  1 395 ? 2.40700   -37.45600 -14.62300 1.000 37.31000  ? 426 LYS B CD  1 
ATOM   6693  C  CE  . LYS B  1 395 ? 2.46200   -38.78000 -13.87900 1.000 33.14000  ? 426 LYS B CE  1 
ATOM   6694  N  NZ  . LYS B  1 395 ? 1.26900   -38.75100 -12.98400 1.000 35.04000  ? 426 LYS B NZ  1 
ATOM   6695  N  N   . ILE B  1 396 ? 4.48700   -38.15700 -18.27200 1.000 34.88000  ? 427 ILE B N   1 
ATOM   6696  C  CA  . ILE B  1 396 ? 3.90700   -39.27000 -19.00300 1.000 38.80000  ? 427 ILE B CA  1 
ATOM   6697  C  C   . ILE B  1 396 ? 3.26000   -40.22900 -18.01800 1.000 36.33000  ? 427 ILE B C   1 
ATOM   6698  O  O   . ILE B  1 396 ? 3.74200   -40.43100 -16.89600 1.000 39.59000  ? 427 ILE B O   1 
ATOM   6699  C  CB  . ILE B  1 396 ? 4.95300   -40.00400 -19.86900 1.000 40.25000  ? 427 ILE B CB  1 
ATOM   6700  C  CG1 . ILE B  1 396 ? 6.13400   -40.44800 -19.03800 1.000 37.59000  ? 427 ILE B CG1 1 
ATOM   6701  C  CG2 . ILE B  1 396 ? 5.44900   -39.07300 -20.94300 1.000 42.08000  ? 427 ILE B CG2 1 
ATOM   6702  C  CD1 . ILE B  1 396 ? 7.08500   -41.42000 -19.79300 1.000 38.84000  ? 427 ILE B CD1 1 
ATOM   6703  N  N   . THR B  1 397 ? 2.17600   -40.85600 -18.46200 1.000 33.22000  ? 428 THR B N   1 
ATOM   6704  C  CA  . THR B  1 397 ? 1.40000   -41.73000 -17.59900 1.000 35.73000  ? 428 THR B CA  1 
ATOM   6705  C  C   . THR B  1 397 ? 0.89900   -42.91700 -18.40100 1.000 40.68000  ? 428 THR B C   1 
ATOM   6706  O  O   . THR B  1 397 ? 0.41300   -42.74600 -19.52600 1.000 43.55000  ? 428 THR B O   1 
ATOM   6707  C  CB  . THR B  1 397 ? 0.20100   -40.99600 -16.98100 1.000 36.56000  ? 428 THR B CB  1 
ATOM   6708  O  OG1 . THR B  1 397 ? 0.64000   -39.78100 -16.37100 1.000 36.03000  ? 428 THR B OG1 1 
ATOM   6709  C  CG2 . THR B  1 397 ? -0.41700  -41.85300 -15.91100 1.000 40.56000  ? 428 THR B CG2 1 
ATOM   6710  N  N   . ARG B  1 398 ? 1.03200   -44.11500 -17.82600 1.000 36.61000  ? 429 ARG B N   1 
ATOM   6711  C  CA  . ARG B  1 398 ? 0.27200   -45.27700 -18.26500 1.000 41.43000  ? 429 ARG B CA  1 
ATOM   6712  C  C   . ARG B  1 398 ? -0.45900  -45.86900 -17.06700 1.000 37.30000  ? 429 ARG B C   1 
ATOM   6713  O  O   . ARG B  1 398 ? 0.17400   -46.23800 -16.06600 1.000 36.42000  ? 429 ARG B O   1 
ATOM   6714  C  CB  . ARG B  1 398 ? 1.16000   -46.34000 -18.93500 1.000 42.24000  ? 429 ARG B CB  1 
ATOM   6715  C  CG  . ARG B  1 398 ? 0.33600   -47.24600 -19.86200 1.000 40.66000  ? 429 ARG B CG  1 
ATOM   6716  C  CD  . ARG B  1 398 ? 1.15000   -48.33800 -20.55700 1.000 43.03000  ? 429 ARG B CD  1 
ATOM   6717  N  NE  . ARG B  1 398 ? 0.28100   -49.22800 -21.32400 1.000 41.12000  ? 429 ARG B NE  1 
ATOM   6718  C  CZ  . ARG B  1 398 ? 0.69800   -50.30900 -21.98100 1.000 49.06000  ? 429 ARG B CZ  1 
ATOM   6719  N  NH1 . ARG B  1 398 ? 1.98400   -50.64100 -22.01700 1.000 42.09000  ? 429 ARG B NH1 1 
ATOM   6720  N  NH2 . ARG B  1 398 ? -0.19900  -51.09900 -22.58500 1.000 37.01000  ? 429 ARG B NH2 1 
ATOM   6721  N  N   . MET B  1 399 ? -1.78700  -45.94000 -17.17200 1.000 34.00000  ? 430 MET B N   1 
ATOM   6722  C  CA  . MET B  1 399 ? -2.66900  -46.51300 -16.16600 1.000 35.60000  ? 430 MET B CA  1 
ATOM   6723  C  C   . MET B  1 399 ? -3.57400  -47.58400 -16.79800 1.000 36.09000  ? 430 MET B C   1 
ATOM   6724  O  O   . MET B  1 399 ? -4.10200  -47.40100 -17.90200 1.000 37.33000  ? 430 MET B O   1 
ATOM   6725  C  CB  . MET B  1 399 ? -3.48700  -45.39700 -15.51200 1.000 36.77000  ? 430 MET B CB  1 
ATOM   6726  C  CG  . MET B  1 399 ? -2.75900  -44.71500 -14.33700 1.000 30.84000  ? 430 MET B CG  1 
ATOM   6727  S  SD  . MET B  1 399 ? -2.41900  -45.83900 -12.94700 1.000 35.71000  ? 430 MET B SD  1 
ATOM   6728  C  CE  . MET B  1 399 ? -4.09900  -46.09800 -12.37800 1.000 33.84000  ? 430 MET B CE  1 
ATOM   6729  N  N   . GLY B  1 400 ? -3.75000  -48.70400 -16.09200 1.000 33.72000  ? 431 GLY B N   1 
ATOM   6730  C  CA  . GLY B  1 400 ? -4.58500  -49.78700 -16.57600 1.000 30.28000  ? 431 GLY B CA  1 
ATOM   6731  C  C   . GLY B  1 400 ? -4.11900  -50.44400 -17.86900 1.000 39.95000  ? 431 GLY B C   1 
ATOM   6732  O  O   . GLY B  1 400 ? -4.94000  -51.04600 -18.57500 1.000 38.57000  ? 431 GLY B O   1 
ATOM   6733  N  N   . ASN B  1 401 ? -2.84200  -50.29200 -18.24000 1.000 35.84000  ? 432 ASN B N   1 
ATOM   6734  C  CA  . ASN B  1 401 ? -2.29700  -50.85000 -19.47400 1.000 37.74000  ? 432 ASN B CA  1 
ATOM   6735  C  C   . ASN B  1 401 ? -2.93400  -50.23100 -20.71700 1.000 40.04000  ? 432 ASN B C   1 
ATOM   6736  O  O   . ASN B  1 401 ? -2.90900  -50.82700 -21.78800 1.000 33.37000  ? 432 ASN B O   1 
ATOM   6737  C  CB  . ASN B  1 401 ? -2.43200  -52.37800 -19.51000 1.000 37.14000  ? 432 ASN B CB  1 
ATOM   6738  C  CG  . ASN B  1 401 ? -1.15900  -53.06700 -19.99800 1.000 48.14000  ? 432 ASN B CG  1 
ATOM   6739  O  OD1 . ASN B  1 401 ? -0.05200  -52.55600 -19.82300 1.000 45.60000  ? 432 ASN B OD1 1 
ATOM   6740  N  ND2 . ASN B  1 401 ? -1.31900  -54.23100 -20.61900 1.000 45.71000  ? 432 ASN B ND2 1 
ATOM   6741  N  N   . GLU B  1 402 ? -3.56700  -49.07100 -20.55300 1.000 35.74000  ? 433 GLU B N   1 
ATOM   6742  C  CA  . GLU B  1 402 ? -4.11200  -48.27200 -21.62500 1.000 33.92000  ? 433 GLU B CA  1 
ATOM   6743  C  C   . GLU B  1 402 ? -3.00400  -47.61100 -22.44800 1.000 31.27000  ? 433 GLU B C   1 
ATOM   6744  O  O   . GLU B  1 402 ? -1.83900  -47.66600 -22.08100 1.000 39.71000  ? 433 GLU B O   1 
ATOM   6745  C  CB  . GLU B  1 402 ? -5.03100  -47.20400 -21.02400 1.000 35.43000  ? 433 GLU B CB  1 
ATOM   6746  C  CG  . GLU B  1 402 ? -6.37500  -47.78100 -20.59900 1.000 34.97000  ? 433 GLU B CG  1 
ATOM   6747  C  CD  . GLU B  1 402 ? -7.15100  -48.25700 -21.79100 1.000 37.84000  ? 433 GLU B CD  1 
ATOM   6748  O  OE1 . GLU B  1 402 ? -7.48700  -47.40800 -22.66200 1.000 45.89000  ? 433 GLU B OE1 1 
ATOM   6749  O  OE2 . GLU B  1 402 ? -7.43100  -49.47900 -21.86100 1.000 45.20000  ? 433 GLU B OE2 1 
ATOM   6750  N  N   . PRO B  1 403 ? -3.33800  -46.94800 -23.55800 1.000 39.27000  ? 434 PRO B N   1 
ATOM   6751  C  CA  . PRO B  1 403 ? -2.31700  -46.17700 -24.27600 1.000 35.97000  ? 434 PRO B CA  1 
ATOM   6752  C  C   . PRO B  1 403 ? -1.61600  -45.17900 -23.35800 1.000 41.91000  ? 434 PRO B C   1 
ATOM   6753  O  O   . PRO B  1 403 ? -2.19700  -44.69800 -22.38500 1.000 38.67000  ? 434 PRO B O   1 
ATOM   6754  C  CB  . PRO B  1 403 ? -3.11500  -45.43900 -25.35500 1.000 34.84000  ? 434 PRO B CB  1 
ATOM   6755  C  CG  . PRO B  1 403 ? -4.36800  -46.25000 -25.56500 1.000 37.48000  ? 434 PRO B CG  1 
ATOM   6756  C  CD  . PRO B  1 403 ? -4.63300  -46.99200 -24.28600 1.000 38.64000  ? 434 PRO B CD  1 
ATOM   6757  N  N   . TRP B  1 404 ? -0.34900  -44.88400 -23.68500 1.000 32.60000  ? 435 TRP B N   1 
ATOM   6758  C  CA  . TRP B  1 404 ? 0.45300   -43.88500 -22.98500 1.000 42.06000  ? 435 TRP B CA  1 
ATOM   6759  C  C   . TRP B  1 404 ? -0.17700  -42.49900 -23.09500 1.000 38.46000  ? 435 TRP B C   1 
ATOM   6760  O  O   . TRP B  1 404 ? -0.80100  -42.16100 -24.09400 1.000 35.24000  ? 435 TRP B O   1 
ATOM   6761  C  CB  . TRP B  1 404 ? 1.87500   -43.82600 -23.57000 1.000 39.78000  ? 435 TRP B CB  1 
ATOM   6762  C  CG  . TRP B  1 404 ? 2.70200   -44.89600 -23.05500 1.000 40.06000  ? 435 TRP B CG  1 
ATOM   6763  C  CD1 . TRP B  1 404 ? 2.87500   -46.11800 -23.60300 1.000 39.14000  ? 435 TRP B CD1 1 
ATOM   6764  C  CD2 . TRP B  1 404 ? 3.44100   -44.89100 -21.82500 1.000 43.84000  ? 435 TRP B CD2 1 
ATOM   6765  N  NE1 . TRP B  1 404 ? 3.69000   -46.87700 -22.81200 1.000 39.73000  ? 435 TRP B NE1 1 
ATOM   6766  C  CE2 . TRP B  1 404 ? 4.06700   -46.14300 -21.71700 1.000 44.48000  ? 435 TRP B CE2 1 
ATOM   6767  C  CE3 . TRP B  1 404 ? 3.65400   -43.93700 -20.81700 1.000 39.93000  ? 435 TRP B CE3 1 
ATOM   6768  C  CZ2 . TRP B  1 404 ? 4.89900   -46.48000 -20.63600 1.000 41.20000  ? 435 TRP B CZ2 1 
ATOM   6769  C  CZ3 . TRP B  1 404 ? 4.47000   -44.26800 -19.75800 1.000 37.92000  ? 435 TRP B CZ3 1 
ATOM   6770  C  CH2 . TRP B  1 404 ? 5.08300   -45.53100 -19.66900 1.000 36.35000  ? 435 TRP B CH2 1 
ATOM   6771  N  N   . ARG B  1 405 ? -0.01700  -41.69300 -22.04300 1.000 34.12000  ? 436 ARG B N   1 
ATOM   6772  C  CA  . ARG B  1 405 ? -0.51200  -40.32400 -22.04400 1.000 36.38000  ? 436 ARG B CA  1 
ATOM   6773  C  C   . ARG B  1 405 ? 0.63200   -39.35700 -21.80200 1.000 38.49000  ? 436 ARG B C   1 
ATOM   6774  O  O   . ARG B  1 405 ? 1.54200   -39.64300 -21.01400 1.000 41.74000  ? 436 ARG B O   1 
ATOM   6775  C  CB  . ARG B  1 405 ? -1.58400  -40.13600 -20.98000 1.000 39.85000  ? 436 ARG B CB  1 
ATOM   6776  C  CG  . ARG B  1 405 ? -2.69800  -41.12900 -21.12000 1.000 41.27000  ? 436 ARG B CG  1 
ATOM   6777  C  CD  . ARG B  1 405 ? -3.61400  -41.15400 -19.90100 1.000 48.49000  ? 436 ARG B CD  1 
ATOM   6778  N  NE  . ARG B  1 405 ? -4.26900  -39.88400 -19.64900 1.000 42.20000  ? 436 ARG B NE  1 
ATOM   6779  C  CZ  . ARG B  1 405 ? -5.39600  -39.52900 -20.23900 1.000 47.42000  ? 436 ARG B CZ  1 
ATOM   6780  N  NH1 . ARG B  1 405 ? -5.93700  -40.27900 -21.19000 1.000 45.18000  ? 436 ARG B NH1 1 
ATOM   6781  N  NH2 . ARG B  1 405 ? -5.99600  -38.40500 -19.86600 1.000 40.53000  ? 436 ARG B NH2 1 
ATOM   6782  N  N   . LEU B  1 406 ? 0.56500   -38.20100 -22.45500 1.000 35.18000  ? 437 LEU B N   1 
ATOM   6783  C  CA  . LEU B  1 406 ? 1.50800   -37.12100 -22.21300 1.000 42.85000  ? 437 LEU B CA  1 
ATOM   6784  C  C   . LEU B  1 406 ? 0.72300   -35.91100 -21.73900 1.000 39.57000  ? 437 LEU B C   1 
ATOM   6785  O  O   . LEU B  1 406 ? -0.20200  -35.47300 -22.41900 1.000 41.64000  ? 437 LEU B O   1 
ATOM   6786  C  CB  . LEU B  1 406 ? 2.28100   -36.75900 -23.48500 1.000 41.07000  ? 437 LEU B CB  1 
ATOM   6787  C  CG  . LEU B  1 406 ? 3.16600   -35.52500 -23.33400 1.000 44.65000  ? 437 LEU B CG  1 
ATOM   6788  C  CD1 . LEU B  1 406 ? 4.33500   -35.87400 -22.42500 1.000 45.58000  ? 437 LEU B CD1 1 
ATOM   6789  C  CD2 . LEU B  1 406 ? 3.65800   -35.00300 -24.67300 1.000 43.71000  ? 437 LEU B CD2 1 
ATOM   6790  N  N   . HIS B  1 407 ? 1.09200   -35.35900 -20.59400 1.000 38.74000  ? 438 HIS B N   1 
ATOM   6791  C  CA  . HIS B  1 407 ? 0.38600   -34.18500 -20.10500 1.000 42.25000  ? 438 HIS B CA  1 
ATOM   6792  C  C   . HIS B  1 407 ? 1.37100   -33.07200 -19.79600 1.000 39.37000  ? 438 HIS B C   1 
ATOM   6793  O  O   . HIS B  1 407 ? 2.49000   -33.31300 -19.32100 1.000 45.78000  ? 438 HIS B O   1 
ATOM   6794  C  CB  . HIS B  1 407 ? -0.43500  -34.48600 -18.85100 1.000 37.00000  ? 438 HIS B CB  1 
ATOM   6795  C  CG  . HIS B  1 407 ? -1.41800  -35.59500 -19.03300 1.000 37.04000  ? 438 HIS B CG  1 
ATOM   6796  N  ND1 . HIS B  1 407 ? -2.61300  -35.43300 -19.69800 1.000 42.39000  ? 438 HIS B ND1 1 
ATOM   6797  C  CD2 . HIS B  1 407 ? -1.37700  -36.88900 -18.63900 1.000 40.71000  ? 438 HIS B CD2 1 
ATOM   6798  C  CE1 . HIS B  1 407 ? -3.26900  -36.57900 -19.70800 1.000 41.76000  ? 438 HIS B CE1 1 
ATOM   6799  N  NE2 . HIS B  1 407 ? -2.53800  -37.48100 -19.07700 1.000 45.43000  ? 438 HIS B NE2 1 
ATOM   6800  N  N   . ASN B  1 408 ? 0.93000   -31.84500 -20.02800 1.000 38.72000  ? 439 ASN B N   1 
ATOM   6801  C  CA  . ASN B  1 408 ? 1.61700   -30.69800 -19.44700 1.000 42.34000  ? 439 ASN B CA  1 
ATOM   6802  C  C   . ASN B  1 408 ? 1.04000   -30.57900 -18.05000 1.000 38.98000  ? 439 ASN B C   1 
ATOM   6803  O  O   . ASN B  1 408 ? -0.06000  -30.05400 -17.86500 1.000 42.02000  ? 439 ASN B O   1 
ATOM   6804  C  CB  . ASN B  1 408 ? 1.37800   -29.42200 -20.24000 1.000 40.65000  ? 439 ASN B CB  1 
ATOM   6805  C  CG  . ASN B  1 408 ? 2.20200   -28.26200 -19.72400 1.000 46.66000  ? 439 ASN B CG  1 
ATOM   6806  O  OD1 . ASN B  1 408 ? 2.12200   -27.88400 -18.54700 1.000 50.36000  ? 439 ASN B OD1 1 
ATOM   6807  N  ND2 . ASN B  1 408 ? 2.96700   -27.65900 -20.60800 1.000 52.37000  ? 439 ASN B ND2 1 
ATOM   6808  N  N   . ILE B  1 409 ? 1.74500   -31.14000 -17.06800 1.000 37.67000  ? 440 ILE B N   1 
ATOM   6809  C  CA  . ILE B  1 409 ? 1.16700   -31.25000 -15.73600 1.000 34.27000  ? 440 ILE B CA  1 
ATOM   6810  C  C   . ILE B  1 409 ? 1.00900   -29.87500 -15.10700 1.000 41.42000  ? 440 ILE B C   1 
ATOM   6811  O  O   . ILE B  1 409 ? 0.15200   -29.68700 -14.23800 1.000 44.89000  ? 440 ILE B O   1 
ATOM   6812  C  CB  . ILE B  1 409 ? 2.01500   -32.22500 -14.89500 1.000 40.45000  ? 440 ILE B CB  1 
ATOM   6813  C  CG1 . ILE B  1 409 ? 1.20400   -32.78200 -13.73200 1.000 42.48000  ? 440 ILE B CG1 1 
ATOM   6814  C  CG2 . ILE B  1 409 ? 3.28100   -31.53100 -14.34800 1.000 40.63000  ? 440 ILE B CG2 1 
ATOM   6815  C  CD1 . ILE B  1 409 ? 0.03200   -33.57200 -14.15700 1.000 39.52000  ? 440 ILE B CD1 1 
ATOM   6816  N  N   . THR B  1 410 ? 1.75100   -28.87700 -15.59400 1.000 42.36000  ? 441 THR B N   1 
ATOM   6817  C  CA  . THR B  1 410 ? 1.62200   -27.52400 -15.06500 1.000 34.92000  ? 441 THR B CA  1 
ATOM   6818  C  C   . THR B  1 410 ? 0.34900   -26.84800 -15.52800 1.000 37.17000  ? 441 THR B C   1 
ATOM   6819  O  O   . THR B  1 410 ? -0.23800  -26.07700 -14.76800 1.000 39.34000  ? 441 THR B O   1 
ATOM   6820  C  CB  . THR B  1 410 ? 2.85100   -26.68700 -15.44100 1.000 49.38000  ? 441 THR B CB  1 
ATOM   6821  O  OG1 . THR B  1 410 ? 4.03200   -27.28500 -14.87400 1.000 43.08000  ? 441 THR B OG1 1 
ATOM   6822  C  CG2 . THR B  1 410 ? 2.70900   -25.25700 -14.95000 1.000 43.43000  ? 441 THR B CG2 1 
ATOM   6823  N  N   . GLN B  1 411 ? -0.10900  -27.12500 -16.75400 1.000 43.13000  ? 442 GLN B N   1 
ATOM   6824  C  CA  . GLN B  1 411 ? -1.34400  -26.53100 -17.26100 1.000 43.45000  ? 442 GLN B CA  1 
ATOM   6825  C  C   . GLN B  1 411 ? -2.57200  -27.40700 -17.02700 1.000 43.47000  ? 442 GLN B C   1 
ATOM   6826  O  O   . GLN B  1 411 ? -3.69800  -26.89300 -17.04300 1.000 41.94000  ? 442 GLN B O   1 
ATOM   6827  C  CB  . GLN B  1 411 ? -1.23700  -26.30000 -18.77500 1.000 51.96000  ? 442 GLN B CB  1 
ATOM   6828  C  CG  . GLN B  1 411 ? -0.12700  -25.35500 -19.22400 1.000 57.68000  ? 442 GLN B CG  1 
ATOM   6829  C  CD  . GLN B  1 411 ? -0.35900  -23.92800 -18.78600 1.000 68.16000  ? 442 GLN B CD  1 
ATOM   6830  O  OE1 . GLN B  1 411 ? -1.50600  -23.48800 -18.62700 1.000 72.12000  ? 442 GLN B OE1 1 
ATOM   6831  N  NE2 . GLN B  1 411 ? 0.73100   -23.19100 -18.58000 1.000 67.71000  ? 442 GLN B NE2 1 
ATOM   6832  N  N   . ASP B  1 412 ? -2.37200  -28.71900 -16.82900 1.000 40.37000  ? 443 ASP B N   1 
ATOM   6833  C  CA  . ASP B  1 412 ? -3.42300  -29.74800 -16.82200 1.000 41.18000  ? 443 ASP B CA  1 
ATOM   6834  C  C   . ASP B  1 412 ? -3.12400  -30.65700 -15.62000 1.000 41.06000  ? 443 ASP B C   1 
ATOM   6835  O  O   . ASP B  1 412 ? -2.77800  -31.83200 -15.75500 1.000 36.17000  ? 443 ASP B O   1 
ATOM   6836  C  CB  . ASP B  1 412 ? -3.42500  -30.51600 -18.15700 1.000 37.89000  ? 443 ASP B CB  1 
ATOM   6837  C  CG  . ASP B  1 412 ? -4.39000  -31.69800 -18.18900 1.000 42.48000  ? 443 ASP B CG  1 
ATOM   6838  O  OD1 . ASP B  1 412 ? -5.39100  -31.70700 -17.42700 1.000 43.36000  ? 443 ASP B OD1 1 
ATOM   6839  O  OD2 . ASP B  1 412 ? -4.12200  -32.64500 -18.96900 1.000 39.48000  ? 443 ASP B OD2 1 
ATOM   6840  N  N   . ILE B  1 413 ? -3.24700  -30.08800 -14.41400 1.000 36.92000  ? 444 ILE B N   1 
ATOM   6841  C  CA  . ILE B  1 413 ? -2.85100  -30.78500 -13.19500 1.000 29.44000  ? 444 ILE B CA  1 
ATOM   6842  C  C   . ILE B  1 413 ? -3.69100  -32.03900 -12.98700 1.000 30.57000  ? 444 ILE B C   1 
ATOM   6843  O  O   . ILE B  1 413 ? -3.22600  -33.00400 -12.37400 1.000 31.77000  ? 444 ILE B O   1 
ATOM   6844  C  CB  . ILE B  1 413 ? -2.92200  -29.81400 -11.99900 1.000 31.76000  ? 444 ILE B CB  1 
ATOM   6845  C  CG1 . ILE B  1 413 ? -2.17300  -30.37900 -10.79100 1.000 35.05000  ? 444 ILE B CG1 1 
ATOM   6846  C  CG2 . ILE B  1 413 ? -4.38100  -29.43200 -11.70100 1.000 34.98000  ? 444 ILE B CG2 1 
ATOM   6847  C  CD1 . ILE B  1 413 ? -1.80900  -29.33000 -9.74000  1.000 36.23000  ? 444 ILE B CD1 1 
ATOM   6848  N  N   . GLY B  1 414 ? -4.92400  -32.06400 -13.52300 1.000 32.99000  ? 445 GLY B N   1 
ATOM   6849  C  CA  . GLY B  1 414 ? -5.80500  -33.21600 -13.46100 1.000 34.55000  ? 445 GLY B CA  1 
ATOM   6850  C  C   . GLY B  1 414 ? -5.60400  -34.28200 -14.52200 1.000 39.72000  ? 445 GLY B C   1 
ATOM   6851  O  O   . GLY B  1 414 ? -6.34900  -35.26800 -14.53200 1.000 39.71000  ? 445 GLY B O   1 
ATOM   6852  N  N   . GLU B  1 415 ? -4.62500  -34.12100 -15.41200 1.000 38.18000  ? 446 GLU B N   1 
ATOM   6853  C  CA  . GLU B  1 415 ? -4.31300  -35.12000 -16.43200 1.000 39.36000  ? 446 GLU B CA  1 
ATOM   6854  C  C   . GLU B  1 415 ? -5.53900  -35.45700 -17.27800 1.000 36.44000  ? 446 GLU B C   1 
ATOM   6855  O  O   . GLU B  1 415 ? -5.88700  -36.62000 -17.48500 1.000 32.68000  ? 446 GLU B O   1 
ATOM   6856  C  CB  . GLU B  1 415 ? -3.71300  -36.37900 -15.79200 1.000 38.20000  ? 446 GLU B CB  1 
ATOM   6857  C  CG  . GLU B  1 415 ? -2.37700  -36.09700 -15.15000 1.000 35.39000  ? 446 GLU B CG  1 
ATOM   6858  C  CD  . GLU B  1 415 ? -1.82500  -37.22400 -14.27900 1.000 40.53000  ? 446 GLU B CD  1 
ATOM   6859  O  OE1 . GLU B  1 415 ? -2.27200  -37.36100 -13.11000 1.000 40.24000  ? 446 GLU B OE1 1 
ATOM   6860  O  OE2 . GLU B  1 415 ? -0.87200  -37.92200 -14.72200 1.000 41.97000  ? 446 GLU B OE2 1 
ATOM   6861  N  N   . LYS B  1 416 ? -6.20700  -34.41400 -17.76600 1.000 40.16000  ? 447 LYS B N   1 
ATOM   6862  C  CA  . LYS B  1 416 ? -7.39700  -34.59200 -18.59200 1.000 40.23000  ? 447 LYS B CA  1 
ATOM   6863  C  C   . LYS B  1 416 ? -7.15900  -34.55900 -20.10300 1.000 35.47000  ? 447 LYS B C   1 
ATOM   6864  O  O   . LYS B  1 416 ? -7.95500  -35.14900 -20.83400 1.000 41.55000  ? 447 LYS B O   1 
ATOM   6865  C  CB  . LYS B  1 416 ? -8.45100  -33.55300 -18.23300 1.000 38.46000  ? 447 LYS B CB  1 
ATOM   6866  C  CG  . LYS B  1 416 ? -9.07700  -33.81200 -16.87800 1.000 39.34000  ? 447 LYS B CG  1 
ATOM   6867  C  CD  . LYS B  1 416 ? -10.08700 -32.71700 -16.52400 1.000 43.41000  ? 447 LYS B CD  1 
ATOM   6868  C  CE  . LYS B  1 416 ? -11.02100 -33.21800 -15.41500 1.000 44.97000  ? 447 LYS B CE  1 
ATOM   6869  N  NZ  . LYS B  1 416 ? -12.06200 -32.23400 -15.05000 1.000 46.59000  ? 447 LYS B NZ  1 
ATOM   6870  N  N   . LYS B  1 417 ? -6.12200  -33.87400 -20.60100 1.000 40.68000  ? 448 LYS B N   1 
ATOM   6871  C  CA  . LYS B  1 417 ? -5.90900  -33.66300 -22.04000 1.000 39.33000  ? 448 LYS B CA  1 
ATOM   6872  C  C   . LYS B  1 417 ? -4.65700  -34.42400 -22.48100 1.000 41.09000  ? 448 LYS B C   1 
ATOM   6873  O  O   . LYS B  1 417 ? -3.52800  -34.02500 -22.16200 1.000 41.53000  ? 448 LYS B O   1 
ATOM   6874  C  CB  . LYS B  1 417 ? -5.79300  -32.17300 -22.35900 1.000 43.87000  ? 448 LYS B CB  1 
ATOM   6875  N  N   . ASN B  1 418 ? -4.85700  -35.53700 -23.18000 1.000 41.61000  ? 449 ASN B N   1 
ATOM   6876  C  CA  . ASN B  1 418 ? -3.72700  -36.32400 -23.66300 1.000 44.34000  ? 449 ASN B CA  1 
ATOM   6877  C  C   . ASN B  1 418 ? -3.06000  -35.59900 -24.82400 1.000 47.84000  ? 449 ASN B C   1 
ATOM   6878  O  O   . ASN B  1 418 ? -3.71400  -35.29700 -25.82500 1.000 50.26000  ? 449 ASN B O   1 
ATOM   6879  C  CB  . ASN B  1 418 ? -4.16400  -37.71800 -24.11300 1.000 35.70000  ? 449 ASN B CB  1 
ATOM   6880  C  CG  . ASN B  1 418 ? -2.97000  -38.61800 -24.39100 1.000 44.17000  ? 449 ASN B CG  1 
ATOM   6881  O  OD1 . ASN B  1 418 ? -1.82200  -38.17000 -24.31700 1.000 43.00000  ? 449 ASN B OD1 1 
ATOM   6882  N  ND2 . ASN B  1 418 ? -3.22300  -39.89200 -24.64700 1.000 40.90000  ? 449 ASN B ND2 1 
ATOM   6883  N  N   . LEU B  1 419 ? -1.77400  -35.28800 -24.67900 1.000 43.73000  ? 450 LEU B N   1 
ATOM   6884  C  CA  . LEU B  1 419 ? -1.01300  -34.63100 -25.73300 1.000 46.27000  ? 450 LEU B CA  1 
ATOM   6885  C  C   . LEU B  1 419 ? -0.08100  -35.58100 -26.48300 1.000 44.12000  ? 450 LEU B C   1 
ATOM   6886  O  O   . LEU B  1 419 ? 0.73400   -35.12300 -27.28200 1.000 46.47000  ? 450 LEU B O   1 
ATOM   6887  C  CB  . LEU B  1 419 ? -0.20100  -33.46900 -25.15200 1.000 37.76000  ? 450 LEU B CB  1 
ATOM   6888  C  CG  . LEU B  1 419 ? -1.06300  -32.38500 -24.52100 1.000 40.98000  ? 450 LEU B CG  1 
ATOM   6889  C  CD1 . LEU B  1 419 ? -0.20100  -31.29800 -23.92100 1.000 41.16000  ? 450 LEU B CD1 1 
ATOM   6890  C  CD2 . LEU B  1 419 ? -1.99800  -31.81900 -25.59700 1.000 45.23000  ? 450 LEU B CD2 1 
ATOM   6891  N  N   . ALA B  1 420 ? -0.21800  -36.89200 -26.28400 1.000 41.43000  ? 451 ALA B N   1 
ATOM   6892  C  CA  . ALA B  1 420 ? 0.68300   -37.83000 -26.94300 1.000 38.99000  ? 451 ALA B CA  1 
ATOM   6893  C  C   . ALA B  1 420 ? 0.67400   -37.64600 -28.45800 1.000 50.69000  ? 451 ALA B C   1 
ATOM   6894  O  O   . ALA B  1 420 ? 1.72500   -37.71200 -29.10300 1.000 51.65000  ? 451 ALA B O   1 
ATOM   6895  C  CB  . ALA B  1 420 ? 0.28000   -39.25500 -26.58800 1.000 39.91000  ? 451 ALA B CB  1 
ATOM   6896  N  N   . GLY B  1 421 ? -0.49100  -37.35500 -29.03600 1.000 40.26000  ? 452 GLY B N   1 
ATOM   6897  C  CA  . GLY B  1 421 ? -0.56600  -37.20600 -30.48300 1.000 49.85000  ? 452 GLY B CA  1 
ATOM   6898  C  C   . GLY B  1 421 ? 0.07700   -35.93100 -30.99800 1.000 51.78000  ? 452 GLY B C   1 
ATOM   6899  O  O   . GLY B  1 421 ? 0.64900   -35.91500 -32.09100 1.000 50.58000  ? 452 GLY B O   1 
ATOM   6900  N  N   . ARG B  1 422 ? -0.04500  -34.83700 -30.24000 1.000 51.30000  ? 453 ARG B N   1 
ATOM   6901  C  CA  . ARG B  1 422 ? 0.50000   -33.55300 -30.67500 1.000 49.86000  ? 453 ARG B CA  1 
ATOM   6902  C  C   . ARG B  1 422 ? 2.03500   -33.50600 -30.55600 1.000 53.46000  ? 453 ARG B C   1 
ATOM   6903  O  O   . ARG B  1 422 ? 2.70000   -32.88300 -31.39200 1.000 49.98000  ? 453 ARG B O   1 
ATOM   6904  C  CB  . ARG B  1 422 ? -0.14700  -32.41700 -29.87400 1.000 44.81000  ? 453 ARG B CB  1 
ATOM   6905  C  CG  . ARG B  1 422 ? 0.13300   -31.02500 -30.42200 1.000 54.17000  ? 453 ARG B CG  1 
ATOM   6906  C  CD  . ARG B  1 422 ? -0.65400  -29.92700 -29.70600 1.000 65.59000  ? 453 ARG B CD  1 
ATOM   6907  N  NE  . ARG B  1 422 ? -2.08300  -30.21200 -29.62600 1.000 70.83000  ? 453 ARG B NE  1 
ATOM   6908  C  CZ  . ARG B  1 422 ? -2.93400  -29.57800 -28.82800 1.000 72.19000  ? 453 ARG B CZ  1 
ATOM   6909  N  NH1 . ARG B  1 422 ? -2.55200  -28.55400 -28.08100 1.000 69.02000  ? 453 ARG B NH1 1 
ATOM   6910  N  NH2 . ARG B  1 422 ? -4.20000  -29.98200 -28.77600 1.000 75.74000  ? 453 ARG B NH2 1 
ATOM   6911  N  N   . TYR B  1 423 ? 2.62300   -34.14300 -29.53300 1.000 44.74000  ? 454 TYR B N   1 
ATOM   6912  C  CA  . TYR B  1 423 ? 4.07900   -34.10500 -29.31300 1.000 42.26000  ? 454 TYR B CA  1 
ATOM   6913  C  C   . TYR B  1 423 ? 4.68000   -35.49000 -29.14700 1.000 41.52000  ? 454 TYR B C   1 
ATOM   6914  O  O   . TYR B  1 423 ? 5.28200   -35.79200 -28.10700 1.000 48.34000  ? 454 TYR B O   1 
ATOM   6915  C  CB  . TYR B  1 423 ? 4.41900   -33.26500 -28.08500 1.000 46.24000  ? 454 TYR B CB  1 
ATOM   6916  C  CG  . TYR B  1 423 ? 3.83900   -31.89400 -28.13100 1.000 50.72000  ? 454 TYR B CG  1 
ATOM   6917  C  CD1 . TYR B  1 423 ? 4.27200   -30.98700 -29.07900 1.000 51.36000  ? 454 TYR B CD1 1 
ATOM   6918  C  CD2 . TYR B  1 423 ? 2.82500   -31.51600 -27.26500 1.000 44.49000  ? 454 TYR B CD2 1 
ATOM   6919  C  CE1 . TYR B  1 423 ? 3.74100   -29.72800 -29.13900 1.000 56.03000  ? 454 TYR B CE1 1 
ATOM   6920  C  CE2 . TYR B  1 423 ? 2.27000   -30.24800 -27.32800 1.000 47.82000  ? 454 TYR B CE2 1 
ATOM   6921  C  CZ  . TYR B  1 423 ? 2.74100   -29.35900 -28.27000 1.000 55.96000  ? 454 TYR B CZ  1 
ATOM   6922  O  OH  . TYR B  1 423 ? 2.22700   -28.08800 -28.36400 1.000 62.25000  ? 454 TYR B OH  1 
ATOM   6923  N  N   . PRO B  1 424 ? 4.62200   -36.33300 -30.18400 1.000 43.70000  ? 455 PRO B N   1 
ATOM   6924  C  CA  . PRO B  1 424 ? 5.11500   -37.71900 -30.02600 1.000 40.84000  ? 455 PRO B CA  1 
ATOM   6925  C  C   . PRO B  1 424 ? 6.62200   -37.83000 -29.80700 1.000 49.84000  ? 455 PRO B C   1 
ATOM   6926  O  O   . PRO B  1 424 ? 7.07400   -38.84200 -29.25400 1.000 51.73000  ? 455 PRO B O   1 
ATOM   6927  C  CB  . PRO B  1 424 ? 4.70600   -38.38800 -31.34900 1.000 45.19000  ? 455 PRO B CB  1 
ATOM   6928  C  CG  . PRO B  1 424 ? 4.71200   -37.24500 -32.35100 1.000 47.12000  ? 455 PRO B CG  1 
ATOM   6929  C  CD  . PRO B  1 424 ? 4.17700   -36.05400 -31.56500 1.000 49.65000  ? 455 PRO B CD  1 
ATOM   6930  N  N   . ASP B  1 425 ? 7.41400   -36.84100 -30.22400 1.000 45.46000  ? 456 ASP B N   1 
ATOM   6931  C  CA  . ASP B  1 425 ? 8.84700   -36.88700 -29.93400 1.000 51.20000  ? 456 ASP B CA  1 
ATOM   6932  C  C   . ASP B  1 425 ? 9.09700   -36.80200 -28.43700 1.000 48.31000  ? 456 ASP B C   1 
ATOM   6933  O  O   . ASP B  1 425 ? 9.85900   -37.59900 -27.87000 1.000 48.55000  ? 456 ASP B O   1 
ATOM   6934  C  CB  . ASP B  1 425 ? 9.57200   -35.75700 -30.66600 1.000 53.31000  ? 456 ASP B CB  1 
ATOM   6935  C  CG  . ASP B  1 425 ? 9.55200   -35.93500 -32.18300 1.000 58.96000  ? 456 ASP B CG  1 
ATOM   6936  O  OD1 . ASP B  1 425 ? 9.31300   -37.06700 -32.65800 1.000 55.22000  ? 456 ASP B OD1 1 
ATOM   6937  O  OD2 . ASP B  1 425 ? 9.75800   -34.93200 -32.90000 1.000 70.19000  ? 456 ASP B OD2 1 
ATOM   6938  N  N   . ARG B  1 426 ? 8.46600   -35.83200 -27.77900 1.000 50.34000  ? 457 ARG B N   1 
ATOM   6939  C  CA  . ARG B  1 426 ? 8.62800   -35.72200 -26.33900 1.000 47.38000  ? 457 ARG B CA  1 
ATOM   6940  C  C   . ARG B  1 426 ? 8.20300   -37.01500 -25.66300 1.000 49.40000  ? 457 ARG B C   1 
ATOM   6941  O  O   . ARG B  1 426 ? 8.91300   -37.53500 -24.78900 1.000 47.90000  ? 457 ARG B O   1 
ATOM   6942  C  CB  . ARG B  1 426 ? 7.79700   -34.56900 -25.79900 1.000 46.54000  ? 457 ARG B CB  1 
ATOM   6943  C  CG  . ARG B  1 426 ? 8.10800   -34.27500 -24.34100 1.000 49.42000  ? 457 ARG B CG  1 
ATOM   6944  C  CD  . ARG B  1 426 ? 7.30600   -33.09300 -23.87700 1.000 52.88000  ? 457 ARG B CD  1 
ATOM   6945  N  NE  . ARG B  1 426 ? 7.85500   -31.86400 -24.43700 1.000 57.63000  ? 457 ARG B NE  1 
ATOM   6946  C  CZ  . ARG B  1 426 ? 8.93700   -31.24200 -23.99300 1.000 60.11000  ? 457 ARG B CZ  1 
ATOM   6947  N  NH1 . ARG B  1 426 ? 9.66000   -31.73300 -22.99700 1.000 51.66000  ? 457 ARG B NH1 1 
ATOM   6948  N  NH2 . ARG B  1 426 ? 9.31200   -30.10700 -24.57900 1.000 62.57000  ? 457 ARG B NH2 1 
ATOM   6949  N  N   . LEU B  1 427 ? 7.06000   -37.56500 -26.09300 1.000 43.61000  ? 458 LEU B N   1 
ATOM   6950  C  CA  . LEU B  1 427 ? 6.54500   -38.78900 -25.49600 1.000 44.63000  ? 458 LEU B CA  1 
ATOM   6951  C  C   . LEU B  1 427 ? 7.58000   -39.90000 -25.58000 1.000 45.92000  ? 458 LEU B C   1 
ATOM   6952  O  O   . LEU B  1 427 ? 7.86600   -40.56700 -24.58000 1.000 51.71000  ? 458 LEU B O   1 
ATOM   6953  C  CB  . LEU B  1 427 ? 5.21100   -39.19300 -26.15100 1.000 36.36000  ? 458 LEU B CB  1 
ATOM   6954  C  CG  . LEU B  1 427 ? 4.70000   -40.58600 -25.76200 1.000 43.34000  ? 458 LEU B CG  1 
ATOM   6955  C  CD1 . LEU B  1 427 ? 4.35200   -40.63000 -24.26300 1.000 45.55000  ? 458 LEU B CD1 1 
ATOM   6956  C  CD2 . LEU B  1 427 ? 3.47600   -40.94100 -26.55800 1.000 45.84000  ? 458 LEU B CD2 1 
ATOM   6957  N  N   . LYS B  1 428 ? 8.15800   -40.11500 -26.76700 1.000 47.02000  ? 459 LYS B N   1 
ATOM   6958  C  CA  . LYS B  1 428 ? 9.09600   -41.23100 -26.91300 1.000 46.21000  ? 459 LYS B CA  1 
ATOM   6959  C  C   . LYS B  1 428 ? 10.43200  -40.95400 -26.22400 1.000 42.62000  ? 459 LYS B C   1 
ATOM   6960  O  O   . LYS B  1 428 ? 11.05200  -41.88000 -25.68000 1.000 46.37000  ? 459 LYS B O   1 
ATOM   6961  C  CB  . LYS B  1 428 ? 9.26900   -41.56200 -28.39500 1.000 49.63000  ? 459 LYS B CB  1 
ATOM   6962  C  CG  . LYS B  1 428 ? 7.97100   -42.15400 -29.00300 1.000 55.41000  ? 459 LYS B CG  1 
ATOM   6963  C  CD  . LYS B  1 428 ? 7.89200   -42.06600 -30.52300 1.000 58.05000  ? 459 LYS B CD  1 
ATOM   6964  C  CE  . LYS B  1 428 ? 6.67300   -42.81600 -31.07700 1.000 58.97000  ? 459 LYS B CE  1 
ATOM   6965  N  NZ  . LYS B  1 428 ? 6.74600   -44.27500 -30.79700 1.000 56.21000  ? 459 LYS B NZ  1 
ATOM   6966  N  N   . GLU B  1 429 ? 10.86300  -39.69100 -26.15600 1.000 45.24000  ? 460 GLU B N   1 
ATOM   6967  C  CA  . GLU B  1 429 ? 12.07700  -39.41800 -25.39300 1.000 43.32000  ? 460 GLU B CA  1 
ATOM   6968  C  C   . GLU B  1 429 ? 11.85700  -39.70100 -23.91600 1.000 47.90000  ? 460 GLU B C   1 
ATOM   6969  O  O   . GLU B  1 429 ? 12.66900  -40.39200 -23.28600 1.000 50.81000  ? 460 GLU B O   1 
ATOM   6970  C  CB  . GLU B  1 429 ? 12.51700  -37.96500 -25.57900 1.000 50.82000  ? 460 GLU B CB  1 
ATOM   6971  N  N   . MET B  1 430 ? 10.71300  -39.27500 -23.37100 1.000 47.10000  ? 461 MET B N   1 
ATOM   6972  C  CA  . MET B  1 430 ? 10.44800  -39.55100 -21.96100 1.000 44.39000  ? 461 MET B CA  1 
ATOM   6973  C  C   . MET B  1 430 ? 10.25600  -41.04100 -21.73000 1.000 47.30000  ? 461 MET B C   1 
ATOM   6974  O  O   . MET B  1 430 ? 10.72200  -41.58500 -20.71800 1.000 44.64000  ? 461 MET B O   1 
ATOM   6975  C  CB  . MET B  1 430 ? 9.23600   -38.76400 -21.50200 1.000 42.21000  ? 461 MET B CB  1 
ATOM   6976  C  CG  . MET B  1 430 ? 9.55500   -37.30200 -21.47000 1.000 44.70000  ? 461 MET B CG  1 
ATOM   6977  S  SD  . MET B  1 430 ? 8.17100   -36.32100 -20.92100 1.000 46.11000  ? 461 MET B SD  1 
ATOM   6978  C  CE  . MET B  1 430 ? 8.41200   -36.46800 -19.13600 1.000 32.30000  ? 461 MET B CE  1 
ATOM   6979  N  N   . ILE B  1 431 ? 9.62800   -41.73600 -22.68100 1.000 42.52000  ? 462 ILE B N   1 
ATOM   6980  C  CA  . ILE B  1 431 ? 9.51800   -43.18400 -22.53500 1.000 46.27000  ? 462 ILE B CA  1 
ATOM   6981  C  C   . ILE B  1 431 ? 10.89800  -43.85000 -22.60900 1.000 47.25000  ? 462 ILE B C   1 
ATOM   6982  O  O   . ILE B  1 431 ? 11.19400  -44.78400 -21.84800 1.000 46.00000  ? 462 ILE B O   1 
ATOM   6983  C  CB  . ILE B  1 431 ? 8.52400   -43.73500 -23.57600 1.000 46.76000  ? 462 ILE B CB  1 
ATOM   6984  C  CG1 . ILE B  1 431 ? 7.11000   -43.33500 -23.13000 1.000 47.61000  ? 462 ILE B CG1 1 
ATOM   6985  C  CG2 . ILE B  1 431 ? 8.65500   -45.24200 -23.69600 1.000 43.64000  ? 462 ILE B CG2 1 
ATOM   6986  C  CD1 . ILE B  1 431 ? 5.99700   -43.74700 -23.99400 1.000 43.96000  ? 462 ILE B CD1 1 
ATOM   6987  N  N   . ALA B  1 432 ? 11.79400  -43.33800 -23.46100 1.000 51.24000  ? 463 ALA B N   1 
ATOM   6988  C  CA  . ALA B  1 432 ? 13.12300  -43.95800 -23.56700 1.000 52.91000  ? 463 ALA B CA  1 
ATOM   6989  C  C   . ALA B  1 432 ? 13.87900  -43.88800 -22.24400 1.000 43.35000  ? 463 ALA B C   1 
ATOM   6990  O  O   . ALA B  1 432 ? 14.43700  -44.89300 -21.77700 1.000 47.06000  ? 463 ALA B O   1 
ATOM   6991  C  CB  . ALA B  1 432 ? 13.94800  -43.30500 -24.67800 1.000 42.62000  ? 463 ALA B CB  1 
ATOM   6992  N  N   . LYS B  1 433 ? 13.90500  -42.70800 -21.62000 1.000 43.33000  ? 464 LYS B N   1 
ATOM   6993  C  CA  . LYS B  1 433 ? 14.62900  -42.55900 -20.35900 1.000 42.82000  ? 464 LYS B CA  1 
ATOM   6994  C  C   . LYS B  1 433 ? 14.03700  -43.44000 -19.26000 1.000 46.04000  ? 464 LYS B C   1 
ATOM   6995  O  O   . LYS B  1 433 ? 14.78100  -44.03800 -18.47000 1.000 45.41000  ? 464 LYS B O   1 
ATOM   6996  C  CB  . LYS B  1 433 ? 14.64300  -41.08900 -19.94400 1.000 47.39000  ? 464 LYS B CB  1 
ATOM   6997  C  CG  . LYS B  1 433 ? 15.22200  -40.19700 -21.03400 1.000 54.73000  ? 464 LYS B CG  1 
ATOM   6998  C  CD  . LYS B  1 433 ? 15.25300  -38.72400 -20.64600 1.000 61.99000  ? 464 LYS B CD  1 
ATOM   6999  C  CE  . LYS B  1 433 ? 15.83500  -37.87200 -21.77400 1.000 63.02000  ? 464 LYS B CE  1 
ATOM   7000  N  NZ  . LYS B  1 433 ? 15.63500  -36.40800 -21.53300 1.000 69.88000  ? 464 LYS B NZ  1 
ATOM   7001  N  N   . THR B  1 434 ? 12.69600  -43.50500 -19.18500 1.000 44.97000  ? 465 THR B N   1 
ATOM   7002  C  CA  . THR B  1 434 ? 12.01300  -44.30500 -18.17100 1.000 39.95000  ? 465 THR B CA  1 
ATOM   7003  C  C   . THR B  1 434 ? 12.32100  -45.78100 -18.34000 1.000 41.32000  ? 465 THR B C   1 
ATOM   7004  O  O   . THR B  1 434 ? 12.54400  -46.49300 -17.35400 1.000 42.29000  ? 465 THR B O   1 
ATOM   7005  C  CB  . THR B  1 434 ? 10.48800  -44.07100 -18.24500 1.000 43.70000  ? 465 THR B CB  1 
ATOM   7006  O  OG1 . THR B  1 434 ? 10.20200  -42.67600 -18.13500 1.000 37.17000  ? 465 THR B OG1 1 
ATOM   7007  C  CG2 . THR B  1 434 ? 9.78000   -44.76700 -17.09800 1.000 39.24000  ? 465 THR B CG2 1 
ATOM   7008  N  N   . GLN B  1 435 ? 12.32900  -46.26700 -19.58400 1.000 44.03000  ? 466 GLN B N   1 
ATOM   7009  C  CA  . GLN B  1 435 ? 12.69900  -47.66000 -19.81600 1.000 41.68000  ? 466 GLN B CA  1 
ATOM   7010  C  C   . GLN B  1 435 ? 14.12800  -47.94900 -19.34400 1.000 45.84000  ? 466 GLN B C   1 
ATOM   7011  O  O   . GLN B  1 435 ? 14.37500  -48.95400 -18.66200 1.000 42.30000  ? 466 GLN B O   1 
ATOM   7012  C  CB  . GLN B  1 435 ? 12.57700  -48.00100 -21.30100 1.000 39.03000  ? 466 GLN B CB  1 
ATOM   7013  C  CG  . GLN B  1 435 ? 12.86100  -49.48600 -21.57300 1.000 44.77000  ? 466 GLN B CG  1 
ATOM   7014  C  CD  . GLN B  1 435 ? 12.41700  -49.95100 -22.94400 1.000 57.64000  ? 466 GLN B CD  1 
ATOM   7015  O  OE1 . GLN B  1 435 ? 12.31700  -49.15800 -23.89900 1.000 53.49000  ? 466 GLN B OE1 1 
ATOM   7016  N  NE2 . GLN B  1 435 ? 12.15400  -51.25000 -23.05600 1.000 51.31000  ? 466 GLN B NE2 1 
ATOM   7017  N  N   . GLU B  1 436 ? 15.07600  -47.06200 -19.66500 1.000 44.29000  ? 467 GLU B N   1 
ATOM   7018  C  CA  . GLU B  1 436 ? 16.45400  -47.25400 -19.19600 1.000 46.97000  ? 467 GLU B CA  1 
ATOM   7019  C  C   . GLU B  1 436 ? 16.52300  -47.34900 -17.67400 1.000 47.12000  ? 467 GLU B C   1 
ATOM   7020  O  O   . GLU B  1 436 ? 17.27400  -48.16800 -17.12300 1.000 41.62000  ? 467 GLU B O   1 
ATOM   7021  C  CB  . GLU B  1 436 ? 17.35100  -46.11800 -19.69300 1.000 43.89000  ? 467 GLU B CB  1 
ATOM   7022  C  CG  . GLU B  1 436 ? 18.85800  -46.30000 -19.39100 1.000 51.43000  ? 467 GLU B CG  1 
ATOM   7023  C  CD  . GLU B  1 436 ? 19.46000  -47.60400 -19.94200 1.000 53.31000  ? 467 GLU B CD  1 
ATOM   7024  O  OE1 . GLU B  1 436 ? 19.06600  -48.05100 -21.04900 1.000 54.62000  ? 467 GLU B OE1 1 
ATOM   7025  O  OE2 . GLU B  1 436 ? 20.37800  -48.14800 -19.29200 1.000 60.40000  ? 467 GLU B OE2 1 
ATOM   7026  N  N   . TRP B  1 437 ? 15.74100  -46.52100 -16.97800 1.000 43.37000  ? 468 TRP B N   1 
ATOM   7027  C  CA  . TRP B  1 437 ? 15.69200  -46.59600 -15.52100 1.000 40.98000  ? 468 TRP B CA  1 
ATOM   7028  C  C   . TRP B  1 437 ? 15.36000  -48.00800 -15.03800 1.000 44.49000  ? 468 TRP B C   1 
ATOM   7029  O  O   . TRP B  1 437 ? 16.00500  -48.52500 -14.11700 1.000 48.35000  ? 468 TRP B O   1 
ATOM   7030  C  CB  . TRP B  1 437 ? 14.67600  -45.57100 -15.00600 1.000 46.93000  ? 468 TRP B CB  1 
ATOM   7031  C  CG  . TRP B  1 437 ? 14.37700  -45.60700 -13.51700 1.000 48.44000  ? 468 TRP B CG  1 
ATOM   7032  C  CD1 . TRP B  1 437 ? 15.26300  -45.41900 -12.48700 1.000 42.31000  ? 468 TRP B CD1 1 
ATOM   7033  C  CD2 . TRP B  1 437 ? 13.08500  -45.76600 -12.91000 1.000 46.24000  ? 468 TRP B CD2 1 
ATOM   7034  N  NE1 . TRP B  1 437 ? 14.60400  -45.49100 -11.27400 1.000 47.26000  ? 468 TRP B NE1 1 
ATOM   7035  C  CE2 . TRP B  1 437 ? 13.26600  -45.69300 -11.50900 1.000 46.59000  ? 468 TRP B CE2 1 
ATOM   7036  C  CE3 . TRP B  1 437 ? 11.79100  -45.96400 -13.41700 1.000 40.54000  ? 468 TRP B CE3 1 
ATOM   7037  C  CZ2 . TRP B  1 437 ? 12.20000  -45.82200 -10.61100 1.000 43.26000  ? 468 TRP B CZ2 1 
ATOM   7038  C  CZ3 . TRP B  1 437 ? 10.74500  -46.09800 -12.53000 1.000 40.43000  ? 468 TRP B CZ3 1 
ATOM   7039  C  CH2 . TRP B  1 437 ? 10.94800  -46.02700 -11.14300 1.000 44.00000  ? 468 TRP B CH2 1 
ATOM   7040  N  N   . THR B  1 438 ? 14.36900  -48.66000 -15.65300 1.000 45.82000  ? 469 THR B N   1 
ATOM   7041  C  CA  . THR B  1 438 ? 13.98700  -50.00400 -15.22100 1.000 42.94000  ? 469 THR B CA  1 
ATOM   7042  C  C   . THR B  1 438 ? 15.05600  -51.04800 -15.53100 1.000 46.41000  ? 469 THR B C   1 
ATOM   7043  O  O   . THR B  1 438 ? 14.96300  -52.17100 -15.02800 1.000 46.33000  ? 469 THR B O   1 
ATOM   7044  C  CB  . THR B  1 438 ? 12.63500  -50.41000 -15.82500 1.000 48.73000  ? 469 THR B CB  1 
ATOM   7045  O  OG1 . THR B  1 438 ? 12.79100  -50.80000 -17.19600 1.000 47.91000  ? 469 THR B OG1 1 
ATOM   7046  C  CG2 . THR B  1 438 ? 11.64200  -49.24600 -15.74000 1.000 45.43000  ? 469 THR B CG2 1 
ATOM   7047  N  N   . LYS B  1 439 ? 16.06300  -50.72400 -16.34500 1.000 44.20000  ? 470 LYS B N   1 
ATOM   7048  C  CA  . LYS B  1 439 ? 17.16400  -51.67000 -16.52900 1.000 48.92000  ? 470 LYS B CA  1 
ATOM   7049  C  C   . LYS B  1 439 ? 17.97600  -51.86400 -15.24600 1.000 50.50000  ? 470 LYS B C   1 
ATOM   7050  O  O   . LYS B  1 439 ? 18.68000  -52.86700 -15.10300 1.000 47.39000  ? 470 LYS B O   1 
ATOM   7051  C  CB  . LYS B  1 439 ? 18.10200  -51.18800 -17.64400 1.000 53.56000  ? 470 LYS B CB  1 
ATOM   7052  C  CG  . LYS B  1 439 ? 17.46400  -51.05200 -19.02200 1.000 45.95000  ? 470 LYS B CG  1 
ATOM   7053  C  CD  . LYS B  1 439 ? 17.12400  -52.42200 -19.58600 1.000 49.77000  ? 470 LYS B CD  1 
ATOM   7054  C  CE  . LYS B  1 439 ? 16.49700  -52.31600 -20.98400 1.000 60.61000  ? 470 LYS B CE  1 
ATOM   7055  N  NZ  . LYS B  1 439 ? 17.41300  -52.76800 -22.07500 1.000 71.15000  ? 470 LYS B NZ  1 
ATOM   7056  N  N   . SER B  1 440 ? 17.88400  -50.95000 -14.29100 1.000 48.67000  ? 471 SER B N   1 
ATOM   7057  C  CA  . SER B  1 440 ? 18.66300  -51.10800 -13.07300 1.000 47.23000  ? 471 SER B CA  1 
ATOM   7058  C  C   . SER B  1 440 ? 17.92500  -51.85200 -11.96800 1.000 50.01000  ? 471 SER B C   1 
ATOM   7059  O  O   . SER B  1 440 ? 18.52200  -52.12400 -10.92300 1.000 53.35000  ? 471 SER B O   1 
ATOM   7060  C  CB  . SER B  1 440 ? 19.09600  -49.73500 -12.58100 1.000 49.95000  ? 471 SER B CB  1 
ATOM   7061  O  OG  . SER B  1 440 ? 17.97000  -48.99600 -12.16100 1.000 55.54000  ? 471 SER B OG  1 
ATOM   7062  N  N   . PHE B  1 441 ? 16.68700  -52.26800 -12.20000 1.000 52.31000  ? 472 PHE B N   1 
ATOM   7063  C  CA  . PHE B  1 441 ? 15.86300  -52.82900 -11.14500 1.000 45.77000  ? 472 PHE B CA  1 
ATOM   7064  C  C   . PHE B  1 441 ? 16.40700  -54.18400 -10.69600 1.000 48.55000  ? 472 PHE B C   1 
ATOM   7065  O  O   . PHE B  1 441 ? 17.08100  -54.88200 -11.45000 1.000 55.88000  ? 472 PHE B O   1 
ATOM   7066  C  CB  . PHE B  1 441 ? 14.42100  -53.00800 -11.65000 1.000 43.80000  ? 472 PHE B CB  1 
ATOM   7067  C  CG  . PHE B  1 441 ? 13.64100  -51.71800 -11.80300 1.000 45.68000  ? 472 PHE B CG  1 
ATOM   7068  C  CD1 . PHE B  1 441 ? 14.23500  -50.48300 -11.59200 1.000 46.81000  ? 472 PHE B CD1 1 
ATOM   7069  C  CD2 . PHE B  1 441 ? 12.29100  -51.75100 -12.13400 1.000 47.19000  ? 472 PHE B CD2 1 
ATOM   7070  C  CE1 . PHE B  1 441 ? 13.50600  -49.29800 -11.72100 1.000 47.39000  ? 472 PHE B CE1 1 
ATOM   7071  C  CE2 . PHE B  1 441 ? 11.55200  -50.57800 -12.25700 1.000 46.80000  ? 472 PHE B CE2 1 
ATOM   7072  C  CZ  . PHE B  1 441 ? 12.16300  -49.34600 -12.05700 1.000 47.41000  ? 472 PHE B CZ  1 
ATOM   7073  N  N   . VAL B  1 442 ? 16.06800  -54.57600 -9.46800  1.000 47.61000  ? 473 VAL B N   1 
ATOM   7074  C  CA  . VAL B  1 442 ? 16.31500  -55.92700 -8.98600  1.000 45.10000  ? 473 VAL B CA  1 
ATOM   7075  C  C   . VAL B  1 442 ? 14.97800  -56.66800 -8.91900  1.000 53.46000  ? 473 VAL B C   1 
ATOM   7076  O  O   . VAL B  1 442 ? 13.90800  -56.08600 -9.06900  1.000 54.60000  ? 473 VAL B O   1 
ATOM   7077  C  CB  . VAL B  1 442 ? 17.04200  -55.96500 -7.61200  1.000 57.53000  ? 473 VAL B CB  1 
ATOM   7078  C  CG1 . VAL B  1 442 ? 18.38700  -55.21100 -7.62900  1.000 45.81000  ? 473 VAL B CG1 1 
ATOM   7079  C  CG2 . VAL B  1 442 ? 16.13500  -55.43300 -6.49600  1.000 53.75000  ? 473 VAL B CG2 1 
ATOM   7080  N  N   . LYS B  1 443 ? 15.05900  -57.97300 -8.72000  1.000 50.51000  ? 474 LYS B N   1 
ATOM   7081  C  CA  . LYS B  1 443 ? 13.87100  -58.77600 -8.51400  1.000 55.96000  ? 474 LYS B CA  1 
ATOM   7082  C  C   . LYS B  1 443 ? 13.26000  -58.48100 -7.14300  1.000 56.31000  ? 474 LYS B C   1 
ATOM   7083  O  O   . LYS B  1 443 ? 13.98400  -58.21500 -6.18100  1.000 53.29000  ? 474 LYS B O   1 
ATOM   7084  C  CB  . LYS B  1 443 ? 14.20900  -60.26600 -8.62400  1.000 49.59000  ? 474 LYS B CB  1 
ATOM   7085  N  N   . PRO B  1 444 ? 11.93500  -58.50100 -7.02900  1.000 50.98000  ? 475 PRO B N   1 
ATOM   7086  C  CA  . PRO B  1 444 ? 11.29700  -58.35300 -5.71800  1.000 48.01000  ? 475 PRO B CA  1 
ATOM   7087  C  C   . PRO B  1 444 ? 11.71800  -59.47500 -4.79500  1.000 50.37000  ? 475 PRO B C   1 
ATOM   7088  O  O   . PRO B  1 444 ? 11.77800  -60.63500 -5.20200  1.000 51.38000  ? 475 PRO B O   1 
ATOM   7089  C  CB  . PRO B  1 444 ? 9.80400   -58.43200 -6.04000  1.000 48.67000  ? 475 PRO B CB  1 
ATOM   7090  C  CG  . PRO B  1 444 ? 9.72700   -58.06600 -7.47700  1.000 53.51000  ? 475 PRO B CG  1 
ATOM   7091  C  CD  . PRO B  1 444 ? 10.94600  -58.65800 -8.10000  1.000 55.32000  ? 475 PRO B CD  1 
ATOM   7092  N  N   . LEU B  1 445 ? 12.05500  -59.10200 -3.55600  1.000 51.44000  ? 476 LEU B N   1 
ATOM   7093  C  CA  . LEU B  1 445 ? 12.39500  -60.06500 -2.51400  1.000 53.03000  ? 476 LEU B CA  1 
ATOM   7094  C  C   . LEU B  1 445 ? 11.16500  -60.80900 -2.01100  1.000 57.50000  ? 476 LEU B C   1 
ATOM   7095  O  O   . LEU B  1 445 ? 11.28000  -61.91400 -1.46700  1.000 58.07000  ? 476 LEU B O   1 
ATOM   7096  C  CB  . LEU B  1 445 ? 13.07800  -59.33700 -1.35700  1.000 49.52000  ? 476 LEU B CB  1 
ATOM   7097  C  CG  . LEU B  1 445 ? 14.36400  -58.63700 -1.75500  1.000 50.81000  ? 476 LEU B CG  1 
ATOM   7098  C  CD1 . LEU B  1 445 ? 14.91400  -57.86100 -0.57200  1.000 46.99000  ? 476 LEU B CD1 1 
ATOM   7099  C  CD2 . LEU B  1 445 ? 15.36900  -59.63800 -2.27000  1.000 53.29000  ? 476 LEU B CD2 1 
ATOM   7100  N  N   . TRP B  1 446 ? 9.99600   -60.19100 -2.13500  1.000 51.27000  ? 477 TRP B N   1 
ATOM   7101  C  CA  . TRP B  1 446 ? 8.71700   -60.81300 -1.84300  1.000 51.99000  ? 477 TRP B CA  1 
ATOM   7102  C  C   . TRP B  1 446 ? 7.69400   -60.12700 -2.73000  1.000 51.47000  ? 477 TRP B C   1 
ATOM   7103  O  O   . TRP B  1 446 ? 7.91100   -59.01300 -3.21900  1.000 47.99000  ? 477 TRP B O   1 
ATOM   7104  C  CB  . TRP B  1 446 ? 8.31600   -60.68600 -0.35700  1.000 53.04000  ? 477 TRP B CB  1 
ATOM   7105  C  CG  . TRP B  1 446 ? 8.25600   -59.25200 0.09700   1.000 51.31000  ? 477 TRP B CG  1 
ATOM   7106  C  CD1 . TRP B  1 446 ? 7.19700   -58.39000 -0.02000  1.000 50.53000  ? 477 TRP B CD1 1 
ATOM   7107  C  CD2 . TRP B  1 446 ? 9.31300   -58.50400 0.70600   1.000 50.46000  ? 477 TRP B CD2 1 
ATOM   7108  N  NE1 . TRP B  1 446 ? 7.53100   -57.15800 0.48100   1.000 47.69000  ? 477 TRP B NE1 1 
ATOM   7109  C  CE2 . TRP B  1 446 ? 8.82800   -57.20200 0.92800   1.000 52.68000  ? 477 TRP B CE2 1 
ATOM   7110  C  CE3 . TRP B  1 446 ? 10.62000  -58.81400 1.09800   1.000 51.62000  ? 477 TRP B CE3 1 
ATOM   7111  C  CZ2 . TRP B  1 446 ? 9.60100   -56.21500 1.52000   1.000 45.74000  ? 477 TRP B CZ2 1 
ATOM   7112  C  CZ3 . TRP B  1 446 ? 11.38500  -57.83200 1.68300   1.000 53.50000  ? 477 TRP B CZ3 1 
ATOM   7113  C  CH2 . TRP B  1 446 ? 10.87100  -56.54200 1.88700   1.000 48.71000  ? 477 TRP B CH2 1 
ATOM   7114  N  N   . VAL B  1 447 ? 6.57700   -60.81000 -2.94200  1.000 51.89000  ? 478 VAL B N   1 
ATOM   7115  C  CA  . VAL B  1 447 ? 5.46700   -60.23800 -3.68200  1.000 45.45000  ? 478 VAL B CA  1 
ATOM   7116  C  C   . VAL B  1 447 ? 4.28700   -60.24600 -2.72400  1.000 49.34000  ? 478 VAL B C   1 
ATOM   7117  O  O   . VAL B  1 447 ? 4.45600   -60.55000 -1.53600  1.000 51.46000  ? 478 VAL B O   1 
ATOM   7118  C  CB  . VAL B  1 447 ? 5.21400   -61.01600 -4.98400  1.000 52.19000  ? 478 VAL B CB  1 
ATOM   7119  C  CG1 . VAL B  1 447 ? 6.44900   -60.92300 -5.88200  1.000 43.16000  ? 478 VAL B CG1 1 
ATOM   7120  C  CG2 . VAL B  1 447 ? 4.86500   -62.47500 -4.68300  1.000 45.23000  ? 478 VAL B CG2 1 
ATOM   7121  N  N   . TYR B  1 448 ? 3.09000   -59.92000 -3.20300  1.000 44.23000  ? 479 TYR B N   1 
ATOM   7122  C  CA  . TYR B  1 448 ? 1.98800   -59.76500 -2.26900  1.000 43.45000  ? 479 TYR B CA  1 
ATOM   7123  C  C   . TYR B  1 448 ? 0.95700   -60.87800 -2.33600  1.000 45.72000  ? 479 TYR B C   1 
ATOM   7124  O  O   . TYR B  1 448 ? 0.46800   -61.30700 -1.29500  1.000 48.64000  ? 479 TYR B O   1 
ATOM   7125  C  CB  . TYR B  1 448 ? 1.28900   -58.41900 -2.48900  1.000 46.00000  ? 479 TYR B CB  1 
ATOM   7126  C  CG  . TYR B  1 448 ? 0.28400   -58.09800 -1.40300  1.000 47.38000  ? 479 TYR B CG  1 
ATOM   7127  C  CD1 . TYR B  1 448 ? 0.70700   -57.60500 -0.16500  1.000 42.77000  ? 479 TYR B CD1 1 
ATOM   7128  C  CD2 . TYR B  1 448 ? -1.08200  -58.27700 -1.61100  1.000 41.78000  ? 479 TYR B CD2 1 
ATOM   7129  C  CE1 . TYR B  1 448 ? -0.19000  -57.31100 0.83400   1.000 39.67000  ? 479 TYR B CE1 1 
ATOM   7130  C  CE2 . TYR B  1 448 ? -2.01200  -57.97200 -0.60200  1.000 45.44000  ? 479 TYR B CE2 1 
ATOM   7131  C  CZ  . TYR B  1 448 ? -1.54800  -57.49700 0.62000   1.000 48.58000  ? 479 TYR B CZ  1 
ATOM   7132  O  OH  . TYR B  1 448 ? -2.43100  -57.20000 1.63700   1.000 52.93000  ? 479 TYR B OH  1 
ATOM   7133  N  N   . SER B  1 449 ? 0.63400   -61.38400 -3.51900  1.000 41.93000  ? 480 SER B N   1 
ATOM   7134  C  CA  . SER B  1 449 ? -0.41400  -62.38500 -3.67500  1.000 44.65000  ? 480 SER B CA  1 
ATOM   7135  C  C   . SER B  1 449 ? 0.09500   -63.63400 -4.38900  1.000 46.25000  ? 480 SER B C   1 
ATOM   7136  O  O   . SER B  1 449 ? 1.08500   -63.59900 -5.13400  1.000 42.29000  ? 480 SER B O   1 
ATOM   7137  C  CB  . SER B  1 449 ? -1.59800  -61.81200 -4.47900  1.000 46.31000  ? 480 SER B CB  1 
ATOM   7138  O  OG  . SER B  1 449 ? -1.23800  -61.60600 -5.84700  1.000 43.51000  ? 480 SER B OG  1 
ATOM   7139  N  N   . VAL B  1 450 ? -0.65200  -64.73000 -4.21400  1.000 44.95000  ? 481 VAL B N   1 
ATOM   7140  C  CA  . VAL B  1 450 ? -0.37100  -65.95400 -4.96600  1.000 50.60000  ? 481 VAL B CA  1 
ATOM   7141  C  C   . VAL B  1 450 ? -0.31900  -65.65700 -6.45800  1.000 44.43000  ? 481 VAL B C   1 
ATOM   7142  O  O   . VAL B  1 450 ? 0.57400   -66.13300 -7.16500  1.000 49.49000  ? 481 VAL B O   1 
ATOM   7143  C  CB  . VAL B  1 450 ? -1.41400  -67.04900 -4.65400  1.000 51.13000  ? 481 VAL B CB  1 
ATOM   7144  C  CG1 . VAL B  1 450 ? -1.21000  -68.26200 -5.57300  1.000 42.81000  ? 481 VAL B CG1 1 
ATOM   7145  C  CG2 . VAL B  1 450 ? -1.32400  -67.47700 -3.20400  1.000 50.44000  ? 481 VAL B CG2 1 
ATOM   7146  N  N   . LYS B  1 451 ? -1.27700  -64.86600 -6.95800  1.000 47.40000  ? 482 LYS B N   1 
ATOM   7147  C  CA  . LYS B  1 451 ? -1.25100  -64.45000 -8.35800  1.000 48.52000  ? 482 LYS B CA  1 
ATOM   7148  C  C   . LYS B  1 451 ? 0.08100   -63.80500 -8.73400  1.000 48.33000  ? 482 LYS B C   1 
ATOM   7149  O  O   . LYS B  1 451 ? 0.64800   -64.10300 -9.79300  1.000 51.32000  ? 482 LYS B O   1 
ATOM   7150  C  CB  . LYS B  1 451 ? -2.38400  -63.46600 -8.62600  1.000 49.02000  ? 482 LYS B CB  1 
ATOM   7151  C  CG  . LYS B  1 451 ? -2.47900  -63.02900 -10.07400 1.000 51.47000  ? 482 LYS B CG  1 
ATOM   7152  C  CD  . LYS B  1 451 ? -3.03200  -64.14300 -10.93300 1.000 50.92000  ? 482 LYS B CD  1 
ATOM   7153  C  CE  . LYS B  1 451 ? -3.27600  -63.69300 -12.35700 1.000 47.43000  ? 482 LYS B CE  1 
ATOM   7154  N  NZ  . LYS B  1 451 ? -3.73800  -64.80600 -13.23600 1.000 52.30000  ? 482 LYS B NZ  1 
ATOM   7155  N  N   . ASP B  1 452 ? 0.58800   -62.91200 -7.88200  1.000 45.36000  ? 483 ASP B N   1 
ATOM   7156  C  CA  . ASP B  1 452 ? 1.87700   -62.27800 -8.14900  1.000 49.92000  ? 483 ASP B CA  1 
ATOM   7157  C  C   . ASP B  1 452 ? 2.96100   -63.32700 -8.34000  1.000 49.71000  ? 483 ASP B C   1 
ATOM   7158  O  O   . ASP B  1 452 ? 3.71400   -63.28900 -9.32300  1.000 45.45000  ? 483 ASP B O   1 
ATOM   7159  C  CB  . ASP B  1 452 ? 2.27500   -61.37000 -6.98500  1.000 45.92000  ? 483 ASP B CB  1 
ATOM   7160  C  CG  . ASP B  1 452 ? 1.39900   -60.14400 -6.84000  1.000 43.69000  ? 483 ASP B CG  1 
ATOM   7161  O  OD1 . ASP B  1 452 ? 0.72700   -59.71800 -7.80300  1.000 46.85000  ? 483 ASP B OD1 1 
ATOM   7162  O  OD2 . ASP B  1 452 ? 1.37000   -59.62500 -5.71000  1.000 48.43000  ? 483 ASP B OD2 1 
ATOM   7163  N  N   . LYS B  1 453 ? 3.02100   -64.30200 -7.42000  1.000 46.36000  ? 484 LYS B N   1 
ATOM   7164  C  CA  . LYS B  1 453 ? 4.08400   -65.29900 -7.46700  1.000 50.18000  ? 484 LYS B CA  1 
ATOM   7165  C  C   . LYS B  1 453 ? 4.01800   -66.09400 -8.75700  1.000 47.57000  ? 484 LYS B C   1 
ATOM   7166  O  O   . LYS B  1 453 ? 5.04900   -66.34200 -9.38400  1.000 51.46000  ? 484 LYS B O   1 
ATOM   7167  C  CB  . LYS B  1 453 ? 4.01300   -66.22800 -6.24900  1.000 51.14000  ? 484 LYS B CB  1 
ATOM   7168  N  N   . GLU B  1 454 ? 2.81600   -66.49200 -9.18000  1.000 47.56000  ? 485 GLU B N   1 
ATOM   7169  C  CA  . GLU B  1 454 ? 2.68800   -67.19600 -10.45400 1.000 50.69000  ? 485 GLU B CA  1 
ATOM   7170  C  C   . GLU B  1 454 ? 3.18300   -66.34500 -11.61600 1.000 50.11000  ? 485 GLU B C   1 
ATOM   7171  O  O   . GLU B  1 454 ? 3.91600   -66.83100 -12.48500 1.000 53.18000  ? 485 GLU B O   1 
ATOM   7172  C  CB  . GLU B  1 454 ? 1.24100   -67.62300 -10.69700 1.000 49.31000  ? 485 GLU B CB  1 
ATOM   7173  C  CG  . GLU B  1 454 ? 0.61800   -68.43700 -9.59600  1.000 45.15000  ? 485 GLU B CG  1 
ATOM   7174  C  CD  . GLU B  1 454 ? -0.81100  -68.85200 -9.91500  1.000 49.80000  ? 485 GLU B CD  1 
ATOM   7175  O  OE1 . GLU B  1 454 ? -1.45200  -68.21100 -10.78500 1.000 53.65000  ? 485 GLU B OE1 1 
ATOM   7176  O  OE2 . GLU B  1 454 ? -1.29200  -69.82200 -9.29200  1.000 57.60000  ? 485 GLU B OE2 1 
ATOM   7177  N  N   . LEU B  1 455 ? 2.76900   -65.07700 -11.67000 1.000 48.82000  ? 486 LEU B N   1 
ATOM   7178  C  CA  . LEU B  1 455 ? 3.11300   -64.25800 -12.83400 1.000 54.64000  ? 486 LEU B CA  1 
ATOM   7179  C  C   . LEU B  1 455 ? 4.61700   -64.02200 -12.93700 1.000 53.16000  ? 486 LEU B C   1 
ATOM   7180  O  O   . LEU B  1 455 ? 5.16600   -63.97400 -14.04200 1.000 55.70000  ? 486 LEU B O   1 
ATOM   7181  C  CB  . LEU B  1 455 ? 2.37100   -62.92100 -12.79800 1.000 53.19000  ? 486 LEU B CB  1 
ATOM   7182  C  CG  . LEU B  1 455 ? 0.84600   -62.92700 -12.84000 1.000 55.32000  ? 486 LEU B CG  1 
ATOM   7183  C  CD1 . LEU B  1 455 ? 0.28900   -61.51900 -12.63800 1.000 45.29000  ? 486 LEU B CD1 1 
ATOM   7184  C  CD2 . LEU B  1 455 ? 0.41700   -63.49400 -14.16500 1.000 49.07000  ? 486 LEU B CD2 1 
ATOM   7185  N  N   . TRP B  1 456 ? 5.29300   -63.82300 -11.80700 1.000 46.91000  ? 487 TRP B N   1 
ATOM   7186  C  CA  . TRP B  1 456 ? 6.73700   -63.63300 -11.86400 1.000 52.79000  ? 487 TRP B CA  1 
ATOM   7187  C  C   . TRP B  1 456 ? 7.44800   -64.94000 -12.18300 1.000 52.66000  ? 487 TRP B C   1 
ATOM   7188  O  O   . TRP B  1 456 ? 8.49200   -64.92800 -12.84200 1.000 61.85000  ? 487 TRP B O   1 
ATOM   7189  C  CB  . TRP B  1 456 ? 7.26300   -63.07600 -10.54000 1.000 49.92000  ? 487 TRP B CB  1 
ATOM   7190  C  CG  . TRP B  1 456 ? 7.03500   -61.61200 -10.35500 1.000 56.26000  ? 487 TRP B CG  1 
ATOM   7191  C  CD1 . TRP B  1 456 ? 5.91200   -61.02200 -9.84600  1.000 49.62000  ? 487 TRP B CD1 1 
ATOM   7192  C  CD2 . TRP B  1 456 ? 7.95400   -60.54600 -10.64500 1.000 55.84000  ? 487 TRP B CD2 1 
ATOM   7193  N  NE1 . TRP B  1 456 ? 6.06700   -59.65800 -9.81600  1.000 52.55000  ? 487 TRP B NE1 1 
ATOM   7194  C  CE2 . TRP B  1 456 ? 7.31200   -59.33600 -10.29100 1.000 51.69000  ? 487 TRP B CE2 1 
ATOM   7195  C  CE3 . TRP B  1 456 ? 9.25100   -60.49500 -11.16700 1.000 44.19000  ? 487 TRP B CE3 1 
ATOM   7196  C  CZ2 . TRP B  1 456 ? 7.92200   -58.08400 -10.45300 1.000 47.49000  ? 487 TRP B CZ2 1 
ATOM   7197  C  CZ3 . TRP B  1 456 ? 9.86400   -59.24700 -11.31900 1.000 47.85000  ? 487 TRP B CZ3 1 
ATOM   7198  C  CH2 . TRP B  1 456 ? 9.19400   -58.05900 -10.96500 1.000 49.18000  ? 487 TRP B CH2 1 
ATOM   7199  N  N   . GLU B  1 457 ? 6.90900   -66.07300 -11.72000 1.000 53.61000  ? 488 GLU B N   1 
ATOM   7200  C  CA  . GLU B  1 457 ? 7.55100   -67.35100 -12.01000 1.000 60.74000  ? 488 GLU B CA  1 
ATOM   7201  C  C   . GLU B  1 457 ? 7.38000   -67.73000 -13.47300 1.000 59.83000  ? 488 GLU B C   1 
ATOM   7202  O  O   . GLU B  1 457 ? 8.28900   -68.30600 -14.07700 1.000 59.05000  ? 488 GLU B O   1 
ATOM   7203  C  CB  . GLU B  1 457 ? 7.00000   -68.44700 -11.10200 1.000 60.67000  ? 488 GLU B CB  1 
ATOM   7204  C  CG  . GLU B  1 457 ? 7.43500   -68.29600 -9.66000  1.000 75.60000  ? 488 GLU B CG  1 
ATOM   7205  C  CD  . GLU B  1 457 ? 7.59700   -69.62900 -8.93000  1.000 95.50000  ? 488 GLU B CD  1 
ATOM   7206  O  OE1 . GLU B  1 457 ? 7.24200   -70.68800 -9.51500  1.000 98.80000  ? 488 GLU B OE1 1 
ATOM   7207  O  OE2 . GLU B  1 457 ? 8.08800   -69.60600 -7.77000  1.000 82.96000  ? 488 GLU B OE2 1 
ATOM   7208  N  N   . SER B  1 458 ? 6.23100   -67.40800 -14.06400 1.000 58.91000  ? 489 SER B N   1 
ATOM   7209  C  CA  . SER B  1 458 ? 6.00500   -67.69400 -15.47400 1.000 54.96000  ? 489 SER B CA  1 
ATOM   7210  C  C   . SER B  1 458 ? 6.64600   -66.67700 -16.40300 1.000 54.89000  ? 489 SER B C   1 
ATOM   7211  O  O   . SER B  1 458 ? 6.62600   -66.87800 -17.62000 1.000 59.18000  ? 489 SER B O   1 
ATOM   7212  C  CB  . SER B  1 458 ? 4.52100   -67.71800 -15.77300 1.000 59.96000  ? 489 SER B CB  1 
ATOM   7213  O  OG  . SER B  1 458 ? 4.04600   -66.38800 -15.75100 1.000 65.49000  ? 489 SER B OG  1 
ATOM   7214  N  N   . GLY B  1 459 ? 7.14800   -65.56600 -15.88200 1.000 55.62000  ? 490 GLY B N   1 
ATOM   7215  C  CA  . GLY B  1 459 ? 7.68000   -64.52500 -16.72900 1.000 52.61000  ? 490 GLY B CA  1 
ATOM   7216  C  C   . GLY B  1 459 ? 6.65300   -63.53900 -17.24500 1.000 57.70000  ? 490 GLY B C   1 
ATOM   7217  O  O   . GLY B  1 459 ? 7.03700   -62.55900 -17.90100 1.000 56.80000  ? 490 GLY B O   1 
ATOM   7218  N  N   . GLN B  1 460 ? 5.35800   -63.78600 -17.00700 1.000 54.19000  ? 491 GLN B N   1 
ATOM   7219  C  CA  . GLN B  1 460 ? 4.33700   -62.81100 -17.38900 1.000 59.44000  ? 491 GLN B CA  1 
ATOM   7220  C  C   . GLN B  1 460 ? 4.60400   -61.45000 -16.75100 1.000 53.85000  ? 491 GLN B C   1 
ATOM   7221  O  O   . GLN B  1 460 ? 4.33700   -60.40900 -17.35600 1.000 53.86000  ? 491 GLN B O   1 
ATOM   7222  C  CB  . GLN B  1 460 ? 2.94300   -63.34000 -17.01900 1.000 54.36000  ? 491 GLN B CB  1 
ATOM   7223  C  CG  . GLN B  1 460 ? 2.36900   -64.32000 -18.06900 1.000 61.53000  ? 491 GLN B CG  1 
ATOM   7224  C  CD  . GLN B  1 460 ? 1.76500   -65.60700 -17.47500 1.000 74.42000  ? 491 GLN B CD  1 
ATOM   7225  O  OE1 . GLN B  1 460 ? 1.50500   -65.70900 -16.27000 1.000 67.34000  ? 491 GLN B OE1 1 
ATOM   7226  N  NE2 . GLN B  1 460 ? 1.54500   -66.59800 -18.33600 1.000 85.19000  ? 491 GLN B NE2 1 
ATOM   7227  N  N   . MET B  1 461 ? 5.13900   -61.44100 -15.53900 1.000 52.65000  ? 492 MET B N   1 
ATOM   7228  C  CA  . MET B  1 461 ? 5.67400   -60.25400 -14.88900 1.000 50.49000  ? 492 MET B CA  1 
ATOM   7229  C  C   . MET B  1 461 ? 7.19000   -60.40500 -14.76800 1.000 51.92000  ? 492 MET B C   1 
ATOM   7230  O  O   . MET B  1 461 ? 7.67400   -61.51700 -14.52800 1.000 45.37000  ? 492 MET B O   1 
ATOM   7231  C  CB  . MET B  1 461 ? 5.07300   -60.07700 -13.48800 1.000 47.82000  ? 492 MET B CB  1 
ATOM   7232  C  CG  . MET B  1 461 ? 3.60400   -59.68200 -13.47100 1.000 50.44000  ? 492 MET B CG  1 
ATOM   7233  S  SD  . MET B  1 461 ? 3.36200   -58.05100 -14.17700 1.000 49.06000  ? 492 MET B SD  1 
ATOM   7234  C  CE  . MET B  1 461 ? 3.79100   -57.00800 -12.81500 1.000 39.31000  ? 492 MET B CE  1 
ATOM   7235  N  N   . PRO B  1 462 ? 7.96600   -59.30300 -14.85200 1.000 51.50000  ? 493 PRO B N   1 
ATOM   7236  C  CA  . PRO B  1 462 ? 7.54000   -57.89500 -14.96500 1.000 51.07000  ? 493 PRO B CA  1 
ATOM   7237  C  C   . PRO B  1 462 ? 7.26300   -57.38600 -16.36900 1.000 51.65000  ? 493 PRO B C   1 
ATOM   7238  O  O   . PRO B  1 462 ? 6.58500   -56.37500 -16.52500 1.000 48.46000  ? 493 PRO B O   1 
ATOM   7239  C  CB  . PRO B  1 462 ? 8.73800   -57.13500 -14.39000 1.000 46.70000  ? 493 PRO B CB  1 
ATOM   7240  C  CG  . PRO B  1 462 ? 9.92500   -58.00200 -14.71600 1.000 45.39000  ? 493 PRO B CG  1 
ATOM   7241  C  CD  . PRO B  1 462 ? 9.43200   -59.42500 -14.70700 1.000 46.93000  ? 493 PRO B CD  1 
ATOM   7242  N  N   . ASN B  1 463 ? 7.86400   -58.01500 -17.37400 1.000 51.84000  ? 494 ASN B N   1 
ATOM   7243  C  CA  . ASN B  1 463 ? 7.72000   -57.65900 -18.78600 1.000 47.69000  ? 494 ASN B CA  1 
ATOM   7244  C  C   . ASN B  1 463 ? 7.77900   -56.15000 -19.01000 1.000 49.66000  ? 494 ASN B C   1 
ATOM   7245  O  O   . ASN B  1 463 ? 6.84600   -55.52500 -19.52300 1.000 50.44000  ? 494 ASN B O   1 
ATOM   7246  C  CB  . ASN B  1 463 ? 6.43700   -58.23200 -19.38000 1.000 48.42000  ? 494 ASN B CB  1 
ATOM   7247  C  CG  . ASN B  1 463 ? 6.44400   -58.19600 -20.90200 1.000 48.70000  ? 494 ASN B CG  1 
ATOM   7248  O  OD1 . ASN B  1 463 ? 7.28700   -57.53000 -21.52100 1.000 47.29000  ? 494 ASN B OD1 1 
ATOM   7249  N  ND2 . ASN B  1 463 ? 5.46500   -58.85200 -21.51000 1.000 54.50000  ? 494 ASN B ND2 1 
ATOM   7250  N  N   . TYR B  1 464 ? 8.91400   -55.57000 -18.63400 1.000 47.92000  ? 495 TYR B N   1 
ATOM   7251  C  CA  . TYR B  1 464 ? 9.09500   -54.14600 -18.87300 1.000 49.12000  ? 495 TYR B CA  1 
ATOM   7252  C  C   . TYR B  1 464 ? 9.02300   -53.82000 -20.35400 1.000 46.73000  ? 495 TYR B C   1 
ATOM   7253  O  O   . TYR B  1 464 ? 8.60100   -52.71800 -20.72500 1.000 50.65000  ? 495 TYR B O   1 
ATOM   7254  C  CB  . TYR B  1 464 ? 10.42300  -53.66200 -18.27100 1.000 46.07000  ? 495 TYR B CB  1 
ATOM   7255  C  CG  . TYR B  1 464 ? 10.49400  -53.88400 -16.78100 1.000 48.42000  ? 495 TYR B CG  1 
ATOM   7256  C  CD1 . TYR B  1 464 ? 9.55700   -53.29600 -15.92600 1.000 46.14000  ? 495 TYR B CD1 1 
ATOM   7257  C  CD2 . TYR B  1 464 ? 11.48700  -54.66500 -16.21700 1.000 42.60000  ? 495 TYR B CD2 1 
ATOM   7258  C  CE1 . TYR B  1 464 ? 9.61000   -53.50200 -14.53600 1.000 39.99000  ? 495 TYR B CE1 1 
ATOM   7259  C  CE2 . TYR B  1 464 ? 11.54800  -54.86700 -14.83700 1.000 44.45000  ? 495 TYR B CE2 1 
ATOM   7260  C  CZ  . TYR B  1 464 ? 10.60200  -54.28400 -14.00100 1.000 43.69000  ? 495 TYR B CZ  1 
ATOM   7261  O  OH  . TYR B  1 464 ? 10.66100  -54.49100 -12.62800 1.000 43.18000  ? 495 TYR B OH  1 
ATOM   7262  N  N   . GLU B  1 465 ? 9.42300   -54.75500 -21.21700 1.000 50.62000  ? 496 GLU B N   1 
ATOM   7263  C  CA  . GLU B  1 465 ? 9.42700   -54.47500 -22.65200 1.000 50.19000  ? 496 GLU B CA  1 
ATOM   7264  C  C   . GLU B  1 465 ? 8.01500   -54.15600 -23.15400 1.000 47.09000  ? 496 GLU B C   1 
ATOM   7265  O  O   . GLU B  1 465 ? 7.80500   -53.18500 -23.89400 1.000 49.17000  ? 496 GLU B O   1 
ATOM   7266  C  CB  . GLU B  1 465 ? 10.02500  -55.67000 -23.39700 1.000 48.26000  ? 496 GLU B CB  1 
ATOM   7267  C  CG  . GLU B  1 465 ? 9.75900   -55.68800 -24.89400 1.000 63.11000  ? 496 GLU B CG  1 
ATOM   7268  C  CD  . GLU B  1 465 ? 10.85100  -54.99000 -25.69300 1.000 80.07000  ? 496 GLU B CD  1 
ATOM   7269  O  OE1 . GLU B  1 465 ? 11.34000  -53.92500 -25.23900 1.000 81.73000  ? 496 GLU B OE1 1 
ATOM   7270  O  OE2 . GLU B  1 465 ? 11.22300  -55.51600 -26.77100 1.000 85.00000  ? 496 GLU B OE2 1 
ATOM   7271  N  N   . ALA B  1 466 ? 7.02800   -54.96200 -22.74900 1.000 45.89000  ? 497 ALA B N   1 
ATOM   7272  C  CA  . ALA B  1 466 ? 5.65300   -54.68200 -23.15000 1.000 46.85000  ? 497 ALA B CA  1 
ATOM   7273  C  C   . ALA B  1 466 ? 5.17200   -53.36500 -22.55400 1.000 44.42000  ? 497 ALA B C   1 
ATOM   7274  O  O   . ALA B  1 466 ? 4.41400   -52.63200 -23.19900 1.000 43.26000  ? 497 ALA B O   1 
ATOM   7275  C  CB  . ALA B  1 466 ? 4.73500   -55.83300 -22.73400 1.000 39.69000  ? 497 ALA B CB  1 
ATOM   7276  N  N   . THR B  1 467 ? 5.64200   -53.02300 -21.34900 1.000 43.01000  ? 498 THR B N   1 
ATOM   7277  C  CA  . THR B  1 467 ? 5.20600   -51.78700 -20.72200 1.000 40.32000  ? 498 THR B CA  1 
ATOM   7278  C  C   . THR B  1 467 ? 5.54500   -50.56500 -21.56900 1.000 44.51000  ? 498 THR B C   1 
ATOM   7279  O  O   . THR B  1 467 ? 4.74500   -49.62300 -21.64700 1.000 39.44000  ? 498 THR B O   1 
ATOM   7280  C  CB  . THR B  1 467 ? 5.84700   -51.67700 -19.35100 1.000 42.71000  ? 498 THR B CB  1 
ATOM   7281  O  OG1 . THR B  1 467 ? 5.27800   -52.66000 -18.48700 1.000 44.63000  ? 498 THR B OG1 1 
ATOM   7282  C  CG2 . THR B  1 467 ? 5.63300   -50.30800 -18.75900 1.000 41.92000  ? 498 THR B CG2 1 
ATOM   7283  N  N   . PHE B  1 468 ? 6.68000   -50.57900 -22.26800 1.000 46.87000  ? 499 PHE B N   1 
ATOM   7284  C  CA  . PHE B  1 468 ? 7.12700   -49.38300 -22.97000 1.000 42.28000  ? 499 PHE B CA  1 
ATOM   7285  C  C   . PHE B  1 468 ? 6.80800   -49.40900 -24.46100 1.000 44.90000  ? 499 PHE B C   1 
ATOM   7286  O  O   . PHE B  1 468 ? 7.24000   -48.51000 -25.18600 1.000 46.12000  ? 499 PHE B O   1 
ATOM   7287  C  CB  . PHE B  1 468 ? 8.62000   -49.15900 -22.70200 1.000 43.06000  ? 499 PHE B CB  1 
ATOM   7288  C  CG  . PHE B  1 468 ? 8.91900   -48.85200 -21.24500 1.000 46.11000  ? 499 PHE B CG  1 
ATOM   7289  C  CD1 . PHE B  1 468 ? 8.59300   -47.61100 -20.69700 1.000 45.28000  ? 499 PHE B CD1 1 
ATOM   7290  C  CD2 . PHE B  1 468 ? 9.43400   -49.82200 -20.40600 1.000 40.46000  ? 499 PHE B CD2 1 
ATOM   7291  C  CE1 . PHE B  1 468 ? 8.84000   -47.33400 -19.33900 1.000 42.45000  ? 499 PHE B CE1 1 
ATOM   7292  C  CE2 . PHE B  1 468 ? 9.66400   -49.55500 -19.05400 1.000 46.10000  ? 499 PHE B CE2 1 
ATOM   7293  C  CZ  . PHE B  1 468 ? 9.36900   -48.30500 -18.52700 1.000 42.34000  ? 499 PHE B CZ  1 
ATOM   7294  N  N   . GLU B  1 469 ? 6.00100   -50.36800 -24.91700 1.000 48.20000  ? 500 GLU B N   1 
ATOM   7295  C  CA  . GLU B  1 469 ? 5.37600   -50.26800 -26.23800 1.000 49.49000  ? 500 GLU B CA  1 
ATOM   7296  C  C   . GLU B  1 469 ? 4.56100   -48.98000 -26.34500 1.000 47.95000  ? 500 GLU B C   1 
ATOM   7297  O  O   . GLU B  1 469 ? 4.00400   -48.49000 -25.36100 1.000 43.92000  ? 500 GLU B O   1 
ATOM   7298  C  CB  . GLU B  1 469 ? 4.44500   -51.46200 -26.49600 1.000 47.72000  ? 500 GLU B CB  1 
ATOM   7299  C  CG  . GLU B  1 469 ? 5.14600   -52.81200 -26.58500 1.000 45.04000  ? 500 GLU B CG  1 
ATOM   7300  C  CD  . GLU B  1 469 ? 4.20100   -54.00600 -26.49900 1.000 53.76000  ? 500 GLU B CD  1 
ATOM   7301  O  OE1 . GLU B  1 469 ? 3.03400   -53.84800 -26.08000 1.000 50.18000  ? 500 GLU B OE1 1 
ATOM   7302  O  OE2 . GLU B  1 469 ? 4.64400   -55.13000 -26.81800 1.000 54.01000  ? 500 GLU B OE2 1 
ATOM   7303  N  N   . VAL B  1 470 ? 4.47900   -48.42800 -27.55800 1.000 46.64000  ? 501 VAL B N   1 
ATOM   7304  C  CA  . VAL B  1 470 ? 3.73500   -47.18900 -27.76600 1.000 43.85000  ? 501 VAL B CA  1 
ATOM   7305  C  C   . VAL B  1 470 ? 2.78900   -47.23900 -28.96700 1.000 48.87000  ? 501 VAL B C   1 
ATOM   7306  O  O   . VAL B  1 470 ? 1.57600   -47.06100 -28.80100 1.000 48.99000  ? 501 VAL B O   1 
ATOM   7307  C  CB  . VAL B  1 470 ? 4.69400   -45.99200 -27.87900 1.000 46.23000  ? 501 VAL B CB  1 
ATOM   7308  C  CG1 . VAL B  1 470 ? 3.91100   -44.68600 -28.08700 1.000 43.01000  ? 501 VAL B CG1 1 
ATOM   7309  C  CG2 . VAL B  1 470 ? 5.52100   -45.89000 -26.61900 1.000 49.85000  ? 501 VAL B CG2 1 
ATOM   7310  N  N   . ASP B  1 471 ? 3.32600   -47.45900 -30.18100 1.000 46.81000  ? 502 ASP B N   1 
ATOM   7311  C  CA  . ASP B  1 471 ? 2.51800   -47.31000 -31.40000 1.000 47.34000  ? 502 ASP B CA  1 
ATOM   7312  C  C   . ASP B  1 471 ? 1.42200   -48.35900 -31.50500 1.000 41.86000  ? 502 ASP B C   1 
ATOM   7313  O  O   . ASP B  1 471 ? 0.29500   -48.04200 -31.89400 1.000 51.03000  ? 502 ASP B O   1 
ATOM   7314  C  CB  . ASP B  1 471 ? 3.41100   -47.39600 -32.64200 1.000 50.68000  ? 502 ASP B CB  1 
ATOM   7315  C  CG  . ASP B  1 471 ? 4.40200   -46.25700 -32.72200 1.000 57.49000  ? 502 ASP B CG  1 
ATOM   7316  O  OD1 . ASP B  1 471 ? 4.55200   -45.54200 -31.70700 1.000 69.74000  ? 502 ASP B OD1 1 
ATOM   7317  O  OD2 . ASP B  1 471 ? 5.06100   -46.10200 -33.76900 1.000 58.95000  ? 502 ASP B OD2 1 
ATOM   7318  N  N   . LYS B  1 472 ? 1.72400   -49.61000 -31.15900 1.000 43.96000  ? 503 LYS B N   1 
ATOM   7319  C  CA  . LYS B  1 472 ? 0.75300   -50.68700 -31.31800 1.000 44.31000  ? 503 LYS B CA  1 
ATOM   7320  C  C   . LYS B  1 472 ? -0.46800  -50.51400 -30.42000 1.000 49.37000  ? 503 LYS B C   1 
ATOM   7321  O  O   . LYS B  1 472 ? -1.50300  -51.13500 -30.68100 1.000 46.50000  ? 503 LYS B O   1 
ATOM   7322  C  CB  . LYS B  1 472 ? 1.41200   -52.03600 -31.04500 1.000 39.99000  ? 503 LYS B CB  1 
ATOM   7323  C  CG  . LYS B  1 472 ? 2.06500   -52.08200 -29.68700 1.000 54.02000  ? 503 LYS B CG  1 
ATOM   7324  C  CD  . LYS B  1 472 ? 2.39300   -53.51000 -29.27900 1.000 61.58000  ? 503 LYS B CD  1 
ATOM   7325  C  CE  . LYS B  1 472 ? 3.56700   -54.07900 -30.06200 1.000 56.53000  ? 503 LYS B CE  1 
ATOM   7326  N  NZ  . LYS B  1 472 ? 4.02100   -55.37500 -29.45600 1.000 49.96000  ? 503 LYS B NZ  1 
ATOM   7327  N  N   . LEU B  1 473 ? -0.36900  -49.71400 -29.35300 1.000 48.30000  ? 504 LEU B N   1 
ATOM   7328  C  CA  . LEU B  1 473 ? -1.52000  -49.50400 -28.49200 1.000 44.48000  ? 504 LEU B CA  1 
ATOM   7329  C  C   . LEU B  1 473 ? -2.52000  -48.56200 -29.15000 1.000 45.84000  ? 504 LEU B C   1 
ATOM   7330  O  O   . LEU B  1 473 ? -3.69400  -48.52900 -28.76200 1.000 44.83000  ? 504 LEU B O   1 
ATOM   7331  C  CB  . LEU B  1 473 ? -1.07600  -48.95400 -27.13900 1.000 41.98000  ? 504 LEU B CB  1 
ATOM   7332  C  CG  . LEU B  1 473 ? 0.07700   -49.73700 -26.50900 1.000 45.22000  ? 504 LEU B CG  1 
ATOM   7333  C  CD1 . LEU B  1 473 ? 0.59000   -49.06300 -25.24600 1.000 42.40000  ? 504 LEU B CD1 1 
ATOM   7334  C  CD2 . LEU B  1 473 ? -0.36600  -51.14900 -26.20100 1.000 42.61000  ? 504 LEU B CD2 1 
ATOM   7335  N  N   . VAL B  1 474 ? -2.06900  -47.80200 -30.13800 1.000 43.34000  ? 505 VAL B N   1 
ATOM   7336  C  CA  . VAL B  1 474 ? -2.87300  -46.76000 -30.75400 1.000 36.84000  ? 505 VAL B CA  1 
ATOM   7337  C  C   . VAL B  1 474 ? -3.11900  -47.01000 -32.23700 1.000 48.87000  ? 505 VAL B C   1 
ATOM   7338  O  O   . VAL B  1 474 ? -4.10800  -46.48900 -32.78400 1.000 44.44000  ? 505 VAL B O   1 
ATOM   7339  C  CB  . VAL B  1 474 ? -2.19100  -45.38800 -30.53800 1.000 48.58000  ? 505 VAL B CB  1 
ATOM   7340  C  CG1 . VAL B  1 474 ? -2.70900  -44.31400 -31.48800 1.000 57.14000  ? 505 VAL B CG1 1 
ATOM   7341  C  CG2 . VAL B  1 474 ? -2.34400  -44.94200 -29.08300 1.000 49.45000  ? 505 VAL B CG2 1 
ATOM   7342  N  N   . ASP B  1 475 ? -2.28000  -47.80400 -32.90500 1.000 45.54000  ? 506 ASP B N   1 
ATOM   7343  C  CA  . ASP B  1 475 ? -2.42000  -48.02900 -34.33500 1.000 46.68000  ? 506 ASP B CA  1 
ATOM   7344  C  C   . ASP B  1 475 ? -3.58900  -48.95700 -34.60400 1.000 41.51000  ? 506 ASP B C   1 
ATOM   7345  O  O   . ASP B  1 475 ? -3.82900  -49.90500 -33.84900 1.000 41.93000  ? 506 ASP B O   1 
ATOM   7346  C  CB  . ASP B  1 475 ? -1.15900  -48.67600 -34.91600 1.000 49.35000  ? 506 ASP B CB  1 
ATOM   7347  C  CG  . ASP B  1 475 ? 0.03500   -47.75300 -34.94300 1.000 49.26000  ? 506 ASP B CG  1 
ATOM   7348  O  OD1 . ASP B  1 475 ? -0.15100  -46.51300 -34.97500 1.000 56.36000  ? 506 ASP B OD1 1 
ATOM   7349  O  OD2 . ASP B  1 475 ? 1.16700   -48.28600 -34.98200 1.000 47.50000  ? 506 ASP B OD2 1 
ATOM   7350  N  N   . SER B  1 476 ? -4.33500  -48.66700 -35.66100 1.000 43.48000  ? 507 SER B N   1 
ATOM   7351  C  CA  . SER B  1 476 ? -5.32900  -49.65600 -36.08000 1.000 49.22000  ? 507 SER B CA  1 
ATOM   7352  C  C   . SER B  1 476 ? -4.67600  -50.74800 -36.93000 1.000 42.65000  ? 507 SER B C   1 
ATOM   7353  O  O   . SER B  1 476 ? -3.82000  -50.45200 -37.75600 1.000 46.20000  ? 507 SER B O   1 
ATOM   7354  C  CB  . SER B  1 476 ? -6.43500  -49.02000 -36.89800 1.000 39.42000  ? 507 SER B CB  1 
ATOM   7355  O  OG  . SER B  1 476 ? -7.16500  -50.06300 -37.53900 1.000 42.17000  ? 507 SER B OG  1 
ATOM   7356  N  N   . PRO B  1 477 ? -5.09300  -52.00700 -36.79900 1.000 49.44000  ? 508 PRO B N   1 
ATOM   7357  C  CA  . PRO B  1 477 ? -4.57600  -53.04100 -37.70800 1.000 43.28000  ? 508 PRO B CA  1 
ATOM   7358  C  C   . PRO B  1 477 ? -5.22700  -53.04400 -39.08400 1.000 51.65000  ? 508 PRO B C   1 
ATOM   7359  O  O   . PRO B  1 477 ? -4.86700  -53.88400 -39.91000 1.000 55.59000  ? 508 PRO B O   1 
ATOM   7360  C  CB  . PRO B  1 477 ? -4.88400  -54.34400 -36.96100 1.000 46.72000  ? 508 PRO B CB  1 
ATOM   7361  C  CG  . PRO B  1 477 ? -6.02100  -54.02700 -36.04400 1.000 46.04000  ? 508 PRO B CG  1 
ATOM   7362  C  CD  . PRO B  1 477 ? -5.99000  -52.54800 -35.75900 1.000 47.39000  ? 508 PRO B CD  1 
ATOM   7363  N  N   . TYR B  1 478 ? -6.11300  -52.10100 -39.38100 1.000 44.67000  ? 509 TYR B N   1 
ATOM   7364  C  CA  . TYR B  1 478 ? -6.79800  -52.05700 -40.65500 1.000 50.90000  ? 509 TYR B CA  1 
ATOM   7365  C  C   . TYR B  1 478 ? -6.46700  -50.69300 -41.26100 1.000 50.02000  ? 509 TYR B C   1 
ATOM   7366  O  O   . TYR B  1 478 ? -6.29200  -50.56600 -42.46700 1.000 53.07000  ? 509 TYR B O   1 
ATOM   7367  C  CB  . TYR B  1 478 ? -8.33300  -52.26600 -40.49400 1.000 47.88000  ? 509 TYR B CB  1 
ATOM   7368  C  CG  . TYR B  1 478 ? -8.69300  -53.33800 -39.47500 1.000 42.87000  ? 509 TYR B CG  1 
ATOM   7369  C  CD1 . TYR B  1 478 ? -8.56300  -54.69300 -39.75800 1.000 42.57000  ? 509 TYR B CD1 1 
ATOM   7370  C  CD2 . TYR B  1 478 ? -9.10900  -52.98000 -38.20800 1.000 42.83000  ? 509 TYR B CD2 1 
ATOM   7371  C  CE1 . TYR B  1 478 ? -8.85300  -55.66000 -38.78600 1.000 39.67000  ? 509 TYR B CE1 1 
ATOM   7372  C  CE2 . TYR B  1 478 ? -9.40000  -53.92400 -37.24100 1.000 41.32000  ? 509 TYR B CE2 1 
ATOM   7373  C  CZ  . TYR B  1 478 ? -9.27500  -55.25900 -37.52200 1.000 41.65000  ? 509 TYR B CZ  1 
ATOM   7374  O  OH  . TYR B  1 478 ? -9.57800  -56.16700 -36.51500 1.000 43.47000  ? 509 TYR B OH  1 
ATOM   7375  N  N   . THR C  1 15  ? 45.44600  -12.41100 -23.85400 1.000 77.26000  ? 46  THR C N   1 
ATOM   7376  C  CA  . THR C  1 15  ? 44.82700  -11.28500 -23.15300 1.000 78.68000  ? 46  THR C CA  1 
ATOM   7377  C  C   . THR C  1 15  ? 43.56500  -10.81000 -23.89900 1.000 77.47000  ? 46  THR C C   1 
ATOM   7378  O  O   . THR C  1 15  ? 43.57300  -10.66900 -25.13000 1.000 65.63000  ? 46  THR C O   1 
ATOM   7379  C  CB  . THR C  1 15  ? 45.82600  -10.11100 -22.97000 1.000 76.09000  ? 46  THR C CB  1 
ATOM   7380  O  OG1 . THR C  1 15  ? 46.44000  -10.19500 -21.67700 1.000 77.96000  ? 46  THR C OG1 1 
ATOM   7381  C  CG2 . THR C  1 15  ? 45.12800  -8.75400  -23.09700 1.000 79.22000  ? 46  THR C CG2 1 
ATOM   7382  N  N   . ARG C  1 16  ? 42.49800  -10.56900 -23.12800 1.000 74.71000  ? 47  ARG C N   1 
ATOM   7383  C  CA  . ARG C  1 16  ? 41.17200  -10.30300 -23.67500 1.000 65.42000  ? 47  ARG C CA  1 
ATOM   7384  C  C   . ARG C  1 16  ? 41.16500  -9.02800  -24.52000 1.000 62.70000  ? 47  ARG C C   1 
ATOM   7385  O  O   . ARG C  1 16  ? 41.87000  -8.06300  -24.20600 1.000 66.55000  ? 47  ARG C O   1 
ATOM   7386  C  CB  . ARG C  1 16  ? 40.15500  -10.18400 -22.54000 1.000 65.05000  ? 47  ARG C CB  1 
ATOM   7387  C  CG  . ARG C  1 16  ? 39.85100  -11.51000 -21.86100 1.000 68.04000  ? 47  ARG C CG  1 
ATOM   7388  C  CD  . ARG C  1 16  ? 38.99000  -11.41200 -20.59300 1.000 62.09000  ? 47  ARG C CD  1 
ATOM   7389  N  NE  . ARG C  1 16  ? 39.42400  -10.42500 -19.60800 1.000 71.40000  ? 47  ARG C NE  1 
ATOM   7390  C  CZ  . ARG C  1 16  ? 38.72900  -10.11200 -18.51900 1.000 69.98000  ? 47  ARG C CZ  1 
ATOM   7391  N  NH1 . ARG C  1 16  ? 37.54500  -10.64800 -18.27700 1.000 69.16000  ? 47  ARG C NH1 1 
ATOM   7392  N  NH2 . ARG C  1 16  ? 39.22600  -9.22400  -17.66000 1.000 73.34000  ? 47  ARG C NH2 1 
ATOM   7393  N  N   . PRO C  1 17  ? 40.35400  -8.98100  -25.57900 1.000 65.08000  ? 48  PRO C N   1 
ATOM   7394  C  CA  . PRO C  1 17  ? 40.34500  -7.80500  -26.45400 1.000 69.37000  ? 48  PRO C CA  1 
ATOM   7395  C  C   . PRO C  1 17  ? 39.53200  -6.66400  -25.86100 1.000 62.83000  ? 48  PRO C C   1 
ATOM   7396  O  O   . PRO C  1 17  ? 38.65100  -6.85700  -25.02100 1.000 65.40000  ? 48  PRO C O   1 
ATOM   7397  C  CB  . PRO C  1 17  ? 39.67300  -8.32600  -27.72700 1.000 65.20000  ? 48  PRO C CB  1 
ATOM   7398  C  CG  . PRO C  1 17  ? 38.69700  -9.32400  -27.21200 1.000 63.50000  ? 48  PRO C CG  1 
ATOM   7399  C  CD  . PRO C  1 17  ? 39.36300  -9.98200  -26.01900 1.000 65.65000  ? 48  PRO C CD  1 
ATOM   7400  N  N   . ASN C  1 18  ? 39.87100  -5.45300  -26.29700 1.000 62.05000  ? 49  ASN C N   1 
ATOM   7401  C  CA  . ASN C  1 18  ? 38.99700  -4.31200  -26.07200 1.000 65.15000  ? 49  ASN C CA  1 
ATOM   7402  C  C   . ASN C  1 18  ? 37.77400  -4.41400  -26.97300 1.000 58.46000  ? 49  ASN C C   1 
ATOM   7403  O  O   . ASN C  1 18  ? 37.80800  -5.05600  -28.02500 1.000 61.42000  ? 49  ASN C O   1 
ATOM   7404  C  CB  . ASN C  1 18  ? 39.72500  -3.00100  -26.36000 1.000 64.77000  ? 49  ASN C CB  1 
ATOM   7405  C  CG  . ASN C  1 18  ? 41.06900  -2.91300  -25.68400 1.000 65.47000  ? 49  ASN C CG  1 
ATOM   7406  O  OD1 . ASN C  1 18  ? 41.16600  -2.87900  -24.45400 1.000 65.62000  ? 49  ASN C OD1 1 
ATOM   7407  N  ND2 . ASN C  1 18  ? 42.12000  -2.84500  -26.48800 1.000 66.54000  ? 49  ASN C ND2 1 
ATOM   7408  N  N   . ILE C  1 19  ? 36.68300  -3.77700  -26.55500 1.000 61.67000  ? 50  ILE C N   1 
ATOM   7409  C  CA  . ILE C  1 19  ? 35.45800  -3.73600  -27.35100 1.000 63.82000  ? 50  ILE C CA  1 
ATOM   7410  C  C   . ILE C  1 19  ? 34.99100  -2.29200  -27.46900 1.000 62.27000  ? 50  ILE C C   1 
ATOM   7411  O  O   . ILE C  1 19  ? 34.63000  -1.66900  -26.46500 1.000 63.45000  ? 50  ILE C O   1 
ATOM   7412  C  CB  . ILE C  1 19  ? 34.33800  -4.61300  -26.76400 1.000 67.47000  ? 50  ILE C CB  1 
ATOM   7413  C  CG1 . ILE C  1 19  ? 34.73000  -6.09300  -26.76100 1.000 68.82000  ? 50  ILE C CG1 1 
ATOM   7414  C  CG2 . ILE C  1 19  ? 33.02400  -4.39800  -27.50800 1.000 60.62000  ? 50  ILE C CG2 1 
ATOM   7415  C  CD1 . ILE C  1 19  ? 33.80100  -6.94500  -25.91300 1.000 62.76000  ? 50  ILE C CD1 1 
ATOM   7416  N  N   . LEU C  1 20  ? 34.96800  -1.77600  -28.69800 1.000 62.45000  ? 51  LEU C N   1 
ATOM   7417  C  CA  . LEU C  1 20  ? 34.45200  -0.44400  -29.00500 1.000 58.46000  ? 51  LEU C CA  1 
ATOM   7418  C  C   . LEU C  1 20  ? 33.27100  -0.58900  -29.95300 1.000 58.27000  ? 51  LEU C C   1 
ATOM   7419  O  O   . LEU C  1 20  ? 33.45500  -0.90900  -31.13100 1.000 61.40000  ? 51  LEU C O   1 
ATOM   7420  C  CB  . LEU C  1 20  ? 35.53400  0.42100   -29.64300 1.000 55.49000  ? 51  LEU C CB  1 
ATOM   7421  C  CG  . LEU C  1 20  ? 35.04300  1.71500   -30.30000 1.000 57.40000  ? 51  LEU C CG  1 
ATOM   7422  C  CD1 . LEU C  1 20  ? 34.38700  2.65600   -29.31700 1.000 49.98000  ? 51  LEU C CD1 1 
ATOM   7423  C  CD2 . LEU C  1 20  ? 36.17300  2.39600   -31.05900 1.000 56.90000  ? 51  LEU C CD2 1 
ATOM   7424  N  N   . VAL C  1 21  ? 32.06500  -0.33600  -29.46500 1.000 55.62000  ? 52  VAL C N   1 
ATOM   7425  C  CA  . VAL C  1 21  ? 30.88800  -0.31100  -30.32400 1.000 54.65000  ? 52  VAL C CA  1 
ATOM   7426  C  C   . VAL C  1 21  ? 30.55200  1.15300   -30.58500 1.000 56.19000  ? 52  VAL C C   1 
ATOM   7427  O  O   . VAL C  1 21  ? 30.11800  1.87900   -29.68300 1.000 57.71000  ? 52  VAL C O   1 
ATOM   7428  C  CB  . VAL C  1 21  ? 29.70800  -1.07700  -29.71000 1.000 61.63000  ? 52  VAL C CB  1 
ATOM   7429  C  CG1 . VAL C  1 21  ? 29.75000  -0.99800  -28.21000 1.000 66.11000  ? 52  VAL C CG1 1 
ATOM   7430  C  CG2 . VAL C  1 21  ? 28.37100  -0.54900  -30.24200 1.000 55.04000  ? 52  VAL C CG2 1 
ATOM   7431  N  N   . VAL C  1 22  ? 30.74200  1.59100   -31.82200 1.000 59.65000  ? 53  VAL C N   1 
ATOM   7432  C  CA  . VAL C  1 22  ? 30.35600  2.92800   -32.24600 1.000 58.53000  ? 53  VAL C CA  1 
ATOM   7433  C  C   . VAL C  1 22  ? 28.99500  2.80300   -32.93000 1.000 58.02000  ? 53  VAL C C   1 
ATOM   7434  O  O   . VAL C  1 22  ? 28.85900  2.23200   -34.01900 1.000 54.73000  ? 53  VAL C O   1 
ATOM   7435  C  CB  . VAL C  1 22  ? 31.42900  3.57600   -33.13100 1.000 56.57000  ? 53  VAL C CB  1 
ATOM   7436  C  CG1 . VAL C  1 22  ? 32.10500  2.54700   -33.97700 1.000 64.51000  ? 53  VAL C CG1 1 
ATOM   7437  C  CG2 . VAL C  1 22  ? 30.83300  4.68700   -33.98200 1.000 61.44000  ? 53  VAL C CG2 1 
ATOM   7438  N  N   . LEU C  1 23  ? 27.98000  3.31700   -32.25200 1.000 57.92000  ? 54  LEU C N   1 
ATOM   7439  C  CA  . LEU C  1 23  ? 26.58600  3.16500   -32.62700 1.000 53.73000  ? 54  LEU C CA  1 
ATOM   7440  C  C   . LEU C  1 23  ? 26.06600  4.49600   -33.13900 1.000 61.08000  ? 54  LEU C C   1 
ATOM   7441  O  O   . LEU C  1 23  ? 25.99000  5.46700   -32.37500 1.000 58.52000  ? 54  LEU C O   1 
ATOM   7442  C  CB  . LEU C  1 23  ? 25.75900  2.71200   -31.42300 1.000 52.73000  ? 54  LEU C CB  1 
ATOM   7443  C  CG  . LEU C  1 23  ? 24.26000  2.51000   -31.68100 1.000 58.63000  ? 54  LEU C CG  1 
ATOM   7444  C  CD1 . LEU C  1 23  ? 24.01300  1.40000   -32.65900 1.000 51.67000  ? 54  LEU C CD1 1 
ATOM   7445  C  CD2 . LEU C  1 23  ? 23.53100  2.25200   -30.37700 1.000 58.92000  ? 54  LEU C CD2 1 
ATOM   7446  N  N   . CYS C  1 24  ? 25.70500  4.54000   -34.42000 1.000 55.97000  ? 55  CYS C N   1 
ATOM   7447  C  CA  . CYS C  1 24  ? 25.04200  5.72600   -34.93300 1.000 60.38000  ? 55  CYS C CA  1 
ATOM   7448  C  C   . CYS C  1 24  ? 23.53600  5.64500   -34.71400 1.000 58.37000  ? 55  CYS C C   1 
ATOM   7449  O  O   . CYS C  1 24  ? 22.98500  4.60900   -34.34400 1.000 59.16000  ? 55  CYS C O   1 
ATOM   7450  C  CB  . CYS C  1 24  ? 25.35200  5.93800   -36.40800 1.000 54.57000  ? 55  CYS C CB  1 
ATOM   7451  S  SG  . CYS C  1 24  ? 26.91700  6.74500   -36.58300 1.000 62.22000  ? 55  CYS C SG  1 
ATOM   7452  N  N   . ASP C  1 25  ? 22.88100  6.78800   -34.90300 1.000 59.47000  ? 56  ASP C N   1 
ATOM   7453  C  CA  . ASP C  1 25  ? 21.45800  6.96600   -34.63700 1.000 60.76000  ? 56  ASP C CA  1 
ATOM   7454  C  C   . ASP C  1 25  ? 20.80100  7.39000   -35.94400 1.000 57.25000  ? 56  ASP C C   1 
ATOM   7455  O  O   . ASP C  1 25  ? 21.12900  8.45200   -36.48000 1.000 55.52000  ? 56  ASP C O   1 
ATOM   7456  C  CB  . ASP C  1 25  ? 21.22800  7.99400   -33.52800 1.000 62.53000  ? 56  ASP C CB  1 
ATOM   7457  C  CG  . ASP C  1 25  ? 19.79500  8.00100   -33.03500 1.000 64.31000  ? 56  ASP C CG  1 
ATOM   7458  O  OD1 . ASP C  1 25  ? 18.97400  7.28500   -33.64400 1.000 66.86000  ? 56  ASP C OD1 1 
ATOM   7459  O  OD2 . ASP C  1 25  ? 19.49300  8.68200   -32.02500 1.000 63.98000  ? 56  ASP C OD2 1 
ATOM   7460  N  N   . ASP C  1 26  ? 19.94400  6.51700   -36.49400 1.000 56.73000  ? 57  ASP C N   1 
ATOM   7461  C  CA  . ASP C  1 26  ? 19.19900  6.76200   -37.74100 1.000 57.26000  ? 57  ASP C CA  1 
ATOM   7462  C  C   . ASP C  1 26  ? 20.10700  6.86800   -38.97000 1.000 55.96000  ? 57  ASP C C   1 
ATOM   7463  O  O   . ASP C  1 26  ? 19.80100  7.60800   -39.91300 1.000 54.69000  ? 57  ASP C O   1 
ATOM   7464  C  CB  . ASP C  1 26  ? 18.32400  8.01900   -37.65800 1.000 51.18000  ? 57  ASP C CB  1 
ATOM   7465  C  CG  . ASP C  1 26  ? 17.21500  7.90600   -36.63900 1.000 59.60000  ? 57  ASP C CG  1 
ATOM   7466  O  OD1 . ASP C  1 26  ? 17.12700  6.86700   -35.94200 1.000 56.53000  ? 57  ASP C OD1 1 
ATOM   7467  O  OD2 . ASP C  1 26  ? 16.42500  8.87400   -36.53900 1.000 60.45000  ? 57  ASP C OD2 1 
ATOM   7468  N  N   . LEU C  1 27  ? 21.23200  6.16000   -38.99800 1.000 57.66000  ? 58  LEU C N   1 
ATOM   7469  C  CA  . LEU C  1 27  ? 22.08800  6.19400   -40.18100 1.000 60.74000  ? 58  LEU C CA  1 
ATOM   7470  C  C   . LEU C  1 27  ? 21.48900  5.32900   -41.29300 1.000 59.75000  ? 58  LEU C C   1 
ATOM   7471  O  O   . LEU C  1 27  ? 21.12700  4.17000   -41.06100 1.000 61.83000  ? 58  LEU C O   1 
ATOM   7472  C  CB  . LEU C  1 27  ? 23.49300  5.72500   -39.83300 1.000 52.95000  ? 58  LEU C CB  1 
ATOM   7473  C  CG  . LEU C  1 27  ? 24.48700  5.68700   -40.99300 1.000 58.23000  ? 58  LEU C CG  1 
ATOM   7474  C  CD1 . LEU C  1 27  ? 25.00700  7.07700   -41.26300 1.000 58.73000  ? 58  LEU C CD1 1 
ATOM   7475  C  CD2 . LEU C  1 27  ? 25.63200  4.72800   -40.69300 1.000 55.99000  ? 58  LEU C CD2 1 
ATOM   7476  N  N   . GLY C  1 28  ? 21.35400  5.90500   -42.48900 1.000 58.32000  ? 59  GLY C N   1 
ATOM   7477  C  CA  . GLY C  1 28  ? 20.74300  5.18600   -43.59100 1.000 59.68000  ? 59  GLY C CA  1 
ATOM   7478  C  C   . GLY C  1 28  ? 21.62900  4.10300   -44.18400 1.000 61.97000  ? 59  GLY C C   1 
ATOM   7479  O  O   . GLY C  1 28  ? 22.85900  4.15100   -44.13200 1.000 59.97000  ? 59  GLY C O   1 
ATOM   7480  N  N   . TYR C  1 29  ? 20.96300  3.11900   -44.80500 1.000 64.43000  ? 60  TYR C N   1 
ATOM   7481  C  CA  . TYR C  1 29  ? 21.63800  1.92200   -45.30000 1.000 54.71000  ? 60  TYR C CA  1 
ATOM   7482  C  C   . TYR C  1 29  ? 22.67000  2.24700   -46.35800 1.000 57.53000  ? 60  TYR C C   1 
ATOM   7483  O  O   . TYR C  1 29  ? 23.67100  1.53500   -46.48500 1.000 59.41000  ? 60  TYR C O   1 
ATOM   7484  C  CB  . TYR C  1 29  ? 20.62700  0.94500   -45.88100 1.000 56.97000  ? 60  TYR C CB  1 
ATOM   7485  C  CG  . TYR C  1 29  ? 21.11700  -0.48000  -45.92000 1.000 57.78000  ? 60  TYR C CG  1 
ATOM   7486  C  CD1 . TYR C  1 29  ? 21.46700  -1.13900  -44.73900 1.000 56.94000  ? 60  TYR C CD1 1 
ATOM   7487  C  CD2 . TYR C  1 29  ? 21.19400  -1.18700  -47.11900 1.000 57.12000  ? 60  TYR C CD2 1 
ATOM   7488  C  CE1 . TYR C  1 29  ? 21.89200  -2.45100  -44.74500 1.000 54.87000  ? 60  TYR C CE1 1 
ATOM   7489  C  CE2 . TYR C  1 29  ? 21.62200  -2.51600  -47.13400 1.000 58.36000  ? 60  TYR C CE2 1 
ATOM   7490  C  CZ  . TYR C  1 29  ? 21.97200  -3.13300  -45.93800 1.000 54.86000  ? 60  TYR C CZ  1 
ATOM   7491  O  OH  . TYR C  1 29  ? 22.39200  -4.43200  -45.91700 1.000 55.85000  ? 60  TYR C OH  1 
ATOM   7492  N  N   . ALA C  1 30  ? 22.44200  3.29800   -47.13800 1.000 57.03000  ? 61  ALA C N   1 
ATOM   7493  C  CA  . ALA C  1 30  ? 23.36200  3.68300   -48.19700 1.000 56.30000  ? 61  ALA C CA  1 
ATOM   7494  C  C   . ALA C  1 30  ? 24.15100  4.93600   -47.83600 1.000 59.20000  ? 61  ALA C C   1 
ATOM   7495  O  O   . ALA C  1 30  ? 24.61800  5.65400   -48.71700 1.000 62.73000  ? 61  ALA C O   1 
ATOM   7496  C  CB  . ALA C  1 30  ? 22.60900  3.88700   -49.50700 1.000 56.56000  ? 61  ALA C CB  1 
ATOM   7497  N  N   . ASP C  1 31  ? 24.33600  5.20100   -46.54400 1.000 58.54000  ? 62  ASP C N   1 
ATOM   7498  C  CA  . ASP C  1 31  ? 24.90300  6.46500   -46.09900 1.000 60.99000  ? 62  ASP C CA  1 
ATOM   7499  C  C   . ASP C  1 31  ? 26.31200  6.31300   -45.53000 1.000 62.58000  ? 62  ASP C C   1 
ATOM   7500  O  O   . ASP C  1 31  ? 26.78400  7.20300   -44.81700 1.000 57.75000  ? 62  ASP C O   1 
ATOM   7501  C  CB  . ASP C  1 31  ? 23.98400  7.12100   -45.06900 1.000 59.21000  ? 62  ASP C CB  1 
ATOM   7502  C  CG  . ASP C  1 31  ? 22.65100  7.52400   -45.66300 1.000 61.08000  ? 62  ASP C CG  1 
ATOM   7503  O  OD1 . ASP C  1 31  ? 22.58200  7.65400   -46.90500 1.000 56.60000  ? 62  ASP C OD1 1 
ATOM   7504  O  OD2 . ASP C  1 31  ? 21.68400  7.72100   -44.88900 1.000 58.77000  ? 62  ASP C OD2 1 
ATOM   7505  N  N   . VAL C  1 32  ? 26.97500  5.18800   -45.79000 1.000 60.56000  ? 63  VAL C N   1 
ATOM   7506  C  CA  . VAL C  1 32  ? 28.41000  5.07100   -45.56400 1.000 63.65000  ? 63  VAL C CA  1 
ATOM   7507  C  C   . VAL C  1 32  ? 29.04400  4.53500   -46.83600 1.000 63.05000  ? 63  VAL C C   1 
ATOM   7508  O  O   . VAL C  1 32  ? 28.40700  3.80700   -47.60500 1.000 61.76000  ? 63  VAL C O   1 
ATOM   7509  C  CB  . VAL C  1 32  ? 28.77100  4.17900   -44.34900 1.000 62.28000  ? 63  VAL C CB  1 
ATOM   7510  C  CG1 . VAL C  1 32  ? 28.49800  4.92700   -43.05100 1.000 60.24000  ? 63  VAL C CG1 1 
ATOM   7511  C  CG2 . VAL C  1 32  ? 28.01500  2.85200   -44.39200 1.000 55.59000  ? 63  VAL C CG2 1 
ATOM   7512  N  N   . GLY C  1 33  ? 30.29800  4.94100   -47.07200 1.000 64.79000  ? 64  GLY C N   1 
ATOM   7513  C  CA  . GLY C  1 33  ? 30.99700  4.52000   -48.27600 1.000 56.94000  ? 64  GLY C CA  1 
ATOM   7514  C  C   . GLY C  1 33  ? 31.03800  3.01300   -48.43800 1.000 62.60000  ? 64  GLY C C   1 
ATOM   7515  O  O   . GLY C  1 33  ? 30.69900  2.48100   -49.49700 1.000 64.37000  ? 64  GLY C O   1 
ATOM   7516  N  N   . PHE C  1 34  ? 31.43700  2.29800   -47.38300 1.000 63.24000  ? 65  PHE C N   1 
ATOM   7517  C  CA  . PHE C  1 34  ? 31.58800  0.85400   -47.52100 1.000 63.38000  ? 65  PHE C CA  1 
ATOM   7518  C  C   . PHE C  1 34  ? 30.27500  0.14400   -47.81400 1.000 62.90000  ? 65  PHE C C   1 
ATOM   7519  O  O   . PHE C  1 34  ? 30.29800  -1.02400  -48.21600 1.000 64.48000  ? 65  PHE C O   1 
ATOM   7520  C  CB  . PHE C  1 34  ? 32.23800  0.26700   -46.26200 1.000 58.16000  ? 65  PHE C CB  1 
ATOM   7521  C  CG  . PHE C  1 34  ? 31.32900  0.18600   -45.06100 1.000 56.11000  ? 65  PHE C CG  1 
ATOM   7522  C  CD1 . PHE C  1 34  ? 30.48400  -0.89200  -44.87600 1.000 58.56000  ? 65  PHE C CD1 1 
ATOM   7523  C  CD2 . PHE C  1 34  ? 31.35900  1.16900   -44.09000 1.000 57.42000  ? 65  PHE C CD2 1 
ATOM   7524  C  CE1 . PHE C  1 34  ? 29.66800  -0.97500  -43.75400 1.000 55.78000  ? 65  PHE C CE1 1 
ATOM   7525  C  CE2 . PHE C  1 34  ? 30.54400  1.08400   -42.96400 1.000 58.09000  ? 65  PHE C CE2 1 
ATOM   7526  C  CZ  . PHE C  1 34  ? 29.69700  0.01600   -42.80500 1.000 54.16000  ? 65  PHE C CZ  1 
ATOM   7527  N  N   . ASN C  1 35  ? 29.13700  0.81400   -47.65800 1.000 61.92000  ? 66  ASN C N   1 
ATOM   7528  C  CA  . ASN C  1 35  ? 27.85000  0.20000   -47.94100 1.000 60.52000  ? 66  ASN C CA  1 
ATOM   7529  C  C   . ASN C  1 35  ? 27.17600  0.81300   -49.15600 1.000 64.65000  ? 66  ASN C C   1 
ATOM   7530  O  O   . ASN C  1 35  ? 25.97000  0.63100   -49.34200 1.000 63.74000  ? 66  ASN C O   1 
ATOM   7531  C  CB  . ASN C  1 35  ? 26.92600  0.30100   -46.72800 1.000 57.60000  ? 66  ASN C CB  1 
ATOM   7532  C  CG  . ASN C  1 35  ? 26.23200  -0.99300  -46.44700 1.000 61.62000  ? 66  ASN C CG  1 
ATOM   7533  O  OD1 . ASN C  1 35  ? 26.87300  -2.04800  -46.47100 1.000 62.34000  ? 66  ASN C OD1 1 
ATOM   7534  N  ND2 . ASN C  1 35  ? 24.91100  -0.94400  -46.21100 1.000 52.23000  ? 66  ASN C ND2 1 
ATOM   7535  N  N   . GLY C  1 36  ? 27.92900  1.53600   -49.98900 1.000 62.09000  ? 67  GLY C N   1 
ATOM   7536  C  CA  . GLY C  1 36  ? 27.42600  1.98500   -51.27200 1.000 61.50000  ? 67  GLY C CA  1 
ATOM   7537  C  C   . GLY C  1 36  ? 27.19800  3.47400   -51.41900 1.000 66.61000  ? 67  GLY C C   1 
ATOM   7538  O  O   . GLY C  1 36  ? 26.72900  3.89700   -52.48000 1.000 74.19000  ? 67  GLY C O   1 
ATOM   7539  N  N   . SER C  1 37  ? 27.52200  4.29300   -50.42100 1.000 69.78000  ? 68  SER C N   1 
ATOM   7540  C  CA  . SER C  1 37  ? 27.23100  5.71700   -50.54200 1.000 65.69000  ? 68  SER C CA  1 
ATOM   7541  C  C   . SER C  1 37  ? 28.04000  6.33000   -51.67200 1.000 74.11000  ? 68  SER C C   1 
ATOM   7542  O  O   . SER C  1 37  ? 29.25600  6.12700   -51.77300 1.000 71.21000  ? 68  SER C O   1 
ATOM   7543  C  CB  . SER C  1 37  ? 27.52300  6.45900   -49.24200 1.000 66.27000  ? 68  SER C CB  1 
ATOM   7544  O  OG  . SER C  1 37  ? 27.22700  7.83600   -49.40900 1.000 70.40000  ? 68  SER C OG  1 
ATOM   7545  N  N   . THR C  1 38  ? 27.35500  7.11300   -52.50200 1.000 75.23000  ? 69  THR C N   1 
ATOM   7546  C  CA  . THR C  1 38  ? 27.96900  7.77600   -53.64000 1.000 74.49000  ? 69  THR C CA  1 
ATOM   7547  C  C   . THR C  1 38  ? 28.28200  9.24500   -53.40000 1.000 70.47000  ? 69  THR C C   1 
ATOM   7548  O  O   . THR C  1 38  ? 29.15300  9.79400   -54.08200 1.000 71.81000  ? 69  THR C O   1 
ATOM   7549  C  CB  . THR C  1 38  ? 27.03400  7.65200   -54.84600 1.000 76.41000  ? 69  THR C CB  1 
ATOM   7550  O  OG1 . THR C  1 38  ? 25.75600  8.20300   -54.49900 1.000 75.78000  ? 69  THR C OG1 1 
ATOM   7551  C  CG2 . THR C  1 38  ? 26.85000  6.18700   -55.21700 1.000 69.54000  ? 69  THR C CG2 1 
ATOM   7552  N  N   . ASP C  1 39  ? 27.63400  9.87600   -52.42100 1.000 73.40000  ? 70  ASP C N   1 
ATOM   7553  C  CA  . ASP C  1 39  ? 27.78800  11.30000  -52.16700 1.000 73.58000  ? 70  ASP C CA  1 
ATOM   7554  C  C   . ASP C  1 39  ? 28.32100  11.61900  -50.78100 1.000 73.76000  ? 70  ASP C C   1 
ATOM   7555  O  O   . ASP C  1 39  ? 28.85400  12.71600  -50.58200 1.000 76.93000  ? 70  ASP C O   1 
ATOM   7556  C  CB  . ASP C  1 39  ? 26.44000  12.02500  -52.34400 1.000 74.33000  ? 70  ASP C CB  1 
ATOM   7557  C  CG  . ASP C  1 39  ? 25.32600  11.42500  -51.48400 1.000 74.24000  ? 70  ASP C CG  1 
ATOM   7558  O  OD1 . ASP C  1 39  ? 25.53200  10.32000  -50.92500 1.000 74.49000  ? 70  ASP C OD1 1 
ATOM   7559  O  OD2 . ASP C  1 39  ? 24.24700  12.06000  -51.36500 1.000 68.15000  ? 70  ASP C OD2 1 
ATOM   7560  N  N   . ILE C  1 40  ? 28.16500  10.71900  -49.81700 1.000 76.29000  ? 71  ILE C N   1 
ATOM   7561  C  CA  . ILE C  1 40  ? 28.69800  10.89500  -48.47500 1.000 67.36000  ? 71  ILE C CA  1 
ATOM   7562  C  C   . ILE C  1 40  ? 30.02200  10.16000  -48.40900 1.000 67.21000  ? 71  ILE C C   1 
ATOM   7563  O  O   . ILE C  1 40  ? 30.09200  8.96500   -48.71800 1.000 70.93000  ? 71  ILE C O   1 
ATOM   7564  C  CB  . ILE C  1 40  ? 27.72300  10.36500  -47.41700 1.000 68.49000  ? 71  ILE C CB  1 
ATOM   7565  C  CG1 . ILE C  1 40  ? 26.36500  11.04900  -47.57100 1.000 64.62000  ? 71  ILE C CG1 1 
ATOM   7566  C  CG2 . ILE C  1 40  ? 28.29000  10.58700  -46.01600 1.000 70.13000  ? 71  ILE C CG2 1 
ATOM   7567  C  CD1 . ILE C  1 40  ? 25.34900  10.58200  -46.56000 1.000 65.22000  ? 71  ILE C CD1 1 
ATOM   7568  N  N   . LEU C  1 41  ? 31.07600  10.87400  -48.03400 1.000 70.90000  ? 72  LEU C N   1 
ATOM   7569  C  CA  . LEU C  1 41  ? 32.41200  10.30500  -47.91900 1.000 68.55000  ? 72  LEU C CA  1 
ATOM   7570  C  C   . LEU C  1 41  ? 32.67000  9.93000   -46.46400 1.000 61.86000  ? 72  LEU C C   1 
ATOM   7571  O  O   . LEU C  1 41  ? 32.50800  10.76100  -45.56500 1.000 65.85000  ? 72  LEU C O   1 
ATOM   7572  C  CB  . LEU C  1 41  ? 33.47800  11.27000  -48.43900 1.000 68.54000  ? 72  LEU C CB  1 
ATOM   7573  C  CG  . LEU C  1 41  ? 33.39100  11.73300  -49.89800 1.000 68.46000  ? 72  LEU C CG  1 
ATOM   7574  C  CD1 . LEU C  1 41  ? 34.38100  12.85200  -50.18300 1.000 70.59000  ? 72  LEU C CD1 1 
ATOM   7575  C  CD2 . LEU C  1 41  ? 33.64900  10.58000  -50.85600 1.000 61.23000  ? 72  LEU C CD2 1 
ATOM   7576  N  N   . THR C  1 42  ? 33.01500  8.66600   -46.23400 1.000 63.56000  ? 73  THR C N   1 
ATOM   7577  C  CA  . THR C  1 42  ? 33.38100  8.16200   -44.90900 1.000 63.12000  ? 73  THR C CA  1 
ATOM   7578  C  C   . THR C  1 42  ? 34.69200  7.38400   -45.00700 1.000 69.77000  ? 73  THR C C   1 
ATOM   7579  O  O   . THR C  1 42  ? 34.74100  6.18000   -44.74400 1.000 68.65000  ? 73  THR C O   1 
ATOM   7580  C  CB  . THR C  1 42  ? 32.26500  7.29800   -44.31900 1.000 60.57000  ? 73  THR C CB  1 
ATOM   7581  O  OG1 . THR C  1 42  ? 31.94600  6.23800   -45.22600 1.000 68.07000  ? 73  THR C OG1 1 
ATOM   7582  C  CG2 . THR C  1 42  ? 31.02100  8.11600   -44.01300 1.000 63.38000  ? 73  THR C CG2 1 
ATOM   7583  N  N   . PRO C  1 43  ? 35.78500  8.05400   -45.38800 1.000 67.56000  ? 74  PRO C N   1 
ATOM   7584  C  CA  . PRO C  1 43  ? 37.03300  7.31700   -45.65600 1.000 72.41000  ? 74  PRO C CA  1 
ATOM   7585  C  C   . PRO C  1 43  ? 37.55800  6.51900   -44.46900 1.000 75.52000  ? 74  PRO C C   1 
ATOM   7586  O  O   . PRO C  1 43  ? 37.99600  5.37200   -44.64700 1.000 75.51000  ? 74  PRO C O   1 
ATOM   7587  C  CB  . PRO C  1 43  ? 38.00600  8.43200   -46.07000 1.000 71.89000  ? 74  PRO C CB  1 
ATOM   7588  C  CG  . PRO C  1 43  ? 37.43400  9.66900   -45.43600 1.000 73.11000  ? 74  PRO C CG  1 
ATOM   7589  C  CD  . PRO C  1 43  ? 35.96000  9.50600   -45.56000 1.000 65.44000  ? 74  PRO C CD  1 
ATOM   7590  N  N   . GLU C  1 44  ? 37.52900  7.08200   -43.26200 1.000 70.66000  ? 75  GLU C N   1 
ATOM   7591  C  CA  . GLU C  1 44  ? 38.03100  6.34200   -42.10600 1.000 73.54000  ? 75  GLU C CA  1 
ATOM   7592  C  C   . GLU C  1 44  ? 37.17200  5.11000   -41.81400 1.000 72.54000  ? 75  GLU C C   1 
ATOM   7593  O  O   . GLU C  1 44  ? 37.70200  4.00100   -41.66400 1.000 69.54000  ? 75  GLU C O   1 
ATOM   7594  C  CB  . GLU C  1 44  ? 38.12900  7.27300   -40.90100 1.000 70.05000  ? 75  GLU C CB  1 
ATOM   7595  C  CG  . GLU C  1 44  ? 39.04000  8.45100   -41.20100 1.000 75.50000  ? 75  GLU C CG  1 
ATOM   7596  C  CD  . GLU C  1 44  ? 40.48400  8.02500   -41.44000 1.000 79.14000  ? 75  GLU C CD  1 
ATOM   7597  O  OE1 . GLU C  1 44  ? 41.21800  7.85300   -40.45300 1.000 77.21000  ? 75  GLU C OE1 1 
ATOM   7598  O  OE2 . GLU C  1 44  ? 40.88500  7.84400   -42.61500 1.000 83.62000  ? 75  GLU C OE2 1 
ATOM   7599  N  N   . LEU C  1 45  ? 35.84200  5.27900   -41.73800 1.000 66.90000  ? 76  LEU C N   1 
ATOM   7600  C  CA  . LEU C  1 45  ? 34.96200  4.12300   -41.56600 1.000 64.99000  ? 76  LEU C CA  1 
ATOM   7601  C  C   . LEU C  1 45  ? 35.16800  3.11900   -42.68800 1.000 67.38000  ? 76  LEU C C   1 
ATOM   7602  O  O   . LEU C  1 45  ? 35.13600  1.90500   -42.45900 1.000 68.73000  ? 76  LEU C O   1 
ATOM   7603  C  CB  . LEU C  1 45  ? 33.48600  4.54000   -41.51700 1.000 63.97000  ? 76  LEU C CB  1 
ATOM   7604  C  CG  . LEU C  1 45  ? 32.89000  5.01400   -40.19000 1.000 65.48000  ? 76  LEU C CG  1 
ATOM   7605  C  CD1 . LEU C  1 45  ? 33.01400  3.93400   -39.15200 1.000 57.03000  ? 76  LEU C CD1 1 
ATOM   7606  C  CD2 . LEU C  1 45  ? 33.57300  6.24400   -39.69000 1.000 72.95000  ? 76  LEU C CD2 1 
ATOM   7607  N  N   . ASP C  1 46  ? 35.35800  3.60600   -43.91400 1.000 65.62000  ? 77  ASP C N   1 
ATOM   7608  C  CA  . ASP C  1 46  ? 35.59700  2.70300   -45.03100 1.000 66.50000  ? 77  ASP C CA  1 
ATOM   7609  C  C   . ASP C  1 46  ? 36.88300  1.91600   -44.81500 1.000 68.70000  ? 77  ASP C C   1 
ATOM   7610  O  O   . ASP C  1 46  ? 36.93900  0.71500   -45.09900 1.000 66.60000  ? 77  ASP C O   1 
ATOM   7611  C  CB  . ASP C  1 46  ? 35.65700  3.48800   -46.34400 1.000 71.15000  ? 77  ASP C CB  1 
ATOM   7612  C  CG  . ASP C  1 46  ? 34.31700  4.11500   -46.72200 1.000 67.68000  ? 77  ASP C CG  1 
ATOM   7613  O  OD1 . ASP C  1 46  ? 33.31200  3.88200   -46.01100 1.000 67.33000  ? 77  ASP C OD1 1 
ATOM   7614  O  OD2 . ASP C  1 46  ? 34.27100  4.85500   -47.73000 1.000 68.64000  ? 77  ASP C OD2 1 
ATOM   7615  N  N   . ASN C  1 47  ? 37.93200  2.58100   -44.32000 1.000 72.44000  ? 78  ASN C N   1 
ATOM   7616  C  CA  . ASN C  1 47  ? 39.19700  1.88800   -44.08400 1.000 71.28000  ? 78  ASN C CA  1 
ATOM   7617  C  C   . ASN C  1 47  ? 39.03100  0.75200   -43.08200 1.000 70.85000  ? 78  ASN C C   1 
ATOM   7618  O  O   . ASN C  1 47  ? 39.46100  -0.37700  -43.33700 1.000 74.32000  ? 78  ASN C O   1 
ATOM   7619  C  CB  . ASN C  1 47  ? 40.26700  2.86900   -43.60400 1.000 71.75000  ? 78  ASN C CB  1 
ATOM   7620  C  CG  . ASN C  1 47  ? 41.62600  2.19900   -43.41600 1.000 77.79000  ? 78  ASN C CG  1 
ATOM   7621  O  OD1 . ASN C  1 47  ? 42.19000  1.64700   -44.36000 1.000 81.17000  ? 78  ASN C OD1 1 
ATOM   7622  N  ND2 . ASN C  1 47  ? 42.15300  2.24300   -42.19300 1.000 71.75000  ? 78  ASN C ND2 1 
ATOM   7623  N  N   . LEU C  1 48  ? 38.35900  1.01600   -41.96100 1.000 65.30000  ? 79  LEU C N   1 
ATOM   7624  C  CA  . LEU C  1 48  ? 38.12000  -0.04000  -40.98200 1.000 64.41000  ? 79  LEU C CA  1 
ATOM   7625  C  C   . LEU C  1 48  ? 37.37000  -1.20600  -41.60900 1.000 62.11000  ? 79  LEU C C   1 
ATOM   7626  O  O   . LEU C  1 48  ? 37.72700  -2.37200  -41.40800 1.000 64.38000  ? 79  LEU C O   1 
ATOM   7627  C  CB  . LEU C  1 48  ? 37.34800  0.51600   -39.78300 1.000 62.14000  ? 79  LEU C CB  1 
ATOM   7628  C  CG  . LEU C  1 48  ? 38.11600  1.55000   -38.95300 1.000 65.09000  ? 79  LEU C CG  1 
ATOM   7629  C  CD1 . LEU C  1 48  ? 37.30600  2.00500   -37.75000 1.000 57.28000  ? 79  LEU C CD1 1 
ATOM   7630  C  CD2 . LEU C  1 48  ? 39.48200  1.01400   -38.52000 1.000 61.19000  ? 79  LEU C CD2 1 
ATOM   7631  N  N   . ALA C  1 49  ? 36.32800  -0.91100  -42.38100 1.000 67.16000  ? 80  ALA C N   1 
ATOM   7632  C  CA  . ALA C  1 49  ? 35.52200  -1.98000  -42.95800 1.000 67.05000  ? 80  ALA C CA  1 
ATOM   7633  C  C   . ALA C  1 49  ? 36.33500  -2.81000  -43.94300 1.000 71.93000  ? 80  ALA C C   1 
ATOM   7634  O  O   . ALA C  1 49  ? 36.33100  -4.04500  -43.88200 1.000 69.76000  ? 80  ALA C O   1 
ATOM   7635  C  CB  . ALA C  1 49  ? 34.28600  -1.39300  -43.64200 1.000 62.15000  ? 80  ALA C CB  1 
ATOM   7636  N  N   . GLN C  1 50  ? 37.08800  -2.14700  -44.82400 1.000 71.50000  ? 81  GLN C N   1 
ATOM   7637  C  CA  . GLN C  1 50  ? 37.88100  -2.88100  -45.80600 1.000 74.68000  ? 81  GLN C CA  1 
ATOM   7638  C  C   . GLN C  1 50  ? 38.91500  -3.77300  -45.13700 1.000 71.30000  ? 81  GLN C C   1 
ATOM   7639  O  O   . GLN C  1 50  ? 39.29200  -4.81000  -45.69100 1.000 75.75000  ? 81  GLN C O   1 
ATOM   7640  C  CB  . GLN C  1 50  ? 38.53900  -1.90700  -46.78300 1.000 72.26000  ? 81  GLN C CB  1 
ATOM   7641  C  CG  . GLN C  1 50  ? 37.49700  -1.04800  -47.47100 1.000 79.32000  ? 81  GLN C CG  1 
ATOM   7642  C  CD  . GLN C  1 50  ? 38.07100  0.05400   -48.32800 1.000 81.41000  ? 81  GLN C CD  1 
ATOM   7643  O  OE1 . GLN C  1 50  ? 38.96400  0.78700   -47.90400 1.000 84.06000  ? 81  GLN C OE1 1 
ATOM   7644  N  NE2 . GLN C  1 50  ? 37.50500  0.22700   -49.51900 1.000 85.54000  ? 81  GLN C NE2 1 
ATOM   7645  N  N   . ASN C  1 51  ? 39.37200  -3.40200  -43.94800 1.000 70.09000  ? 82  ASN C N   1 
ATOM   7646  C  CA  . ASN C  1 51  ? 40.33700  -4.20100  -43.20700 1.000 74.18000  ? 82  ASN C CA  1 
ATOM   7647  C  C   . ASN C  1 51  ? 39.67500  -5.15200  -42.21200 1.000 73.48000  ? 82  ASN C C   1 
ATOM   7648  O  O   . ASN C  1 51  ? 40.34900  -5.64900  -41.30200 1.000 72.37000  ? 82  ASN C O   1 
ATOM   7649  C  CB  . ASN C  1 51  ? 41.33300  -3.28600  -42.49700 1.000 72.13000  ? 82  ASN C CB  1 
ATOM   7650  C  CG  . ASN C  1 51  ? 42.26900  -2.59400  -43.46800 1.000 76.11000  ? 82  ASN C CG  1 
ATOM   7651  O  OD1 . ASN C  1 51  ? 42.87700  -3.24100  -44.31700 1.000 81.82000  ? 82  ASN C OD1 1 
ATOM   7652  N  ND2 . ASN C  1 51  ? 42.36600  -1.27500  -43.36900 1.000 77.55000  ? 82  ASN C ND2 1 
ATOM   7653  N  N   . GLY C  1 52  ? 38.38300  -5.41800  -42.36800 1.000 69.61000  ? 83  GLY C N   1 
ATOM   7654  C  CA  . GLY C  1 52  ? 37.66900  -6.34600  -41.50800 1.000 62.48000  ? 83  GLY C CA  1 
ATOM   7655  C  C   . GLY C  1 52  ? 36.58100  -7.06700  -42.27100 1.000 58.80000  ? 83  GLY C C   1 
ATOM   7656  O  O   . GLY C  1 52  ? 36.73700  -7.39700  -43.44900 1.000 63.65000  ? 83  GLY C O   1 
ATOM   7657  N  N   . SER C  1 53  ? 35.48400  -7.35500  -41.58300 1.000 59.42000  ? 84  SER C N   1 
ATOM   7658  C  CA  . SER C  1 53  ? 34.35700  -8.07000  -42.16200 1.000 61.45000  ? 84  SER C CA  1 
ATOM   7659  C  C   . SER C  1 53  ? 33.13400  -7.16100  -42.21700 1.000 60.31000  ? 84  SER C C   1 
ATOM   7660  O  O   . SER C  1 53  ? 32.70500  -6.63200  -41.18300 1.000 58.51000  ? 84  SER C O   1 
ATOM   7661  C  CB  . SER C  1 53  ? 34.04700  -9.32500  -41.36200 1.000 56.23000  ? 84  SER C CB  1 
ATOM   7662  O  OG  . SER C  1 53  ? 32.83500  -9.88900  -41.81100 1.000 62.08000  ? 84  SER C OG  1 
ATOM   7663  N  N   . ILE C  1 54  ? 32.58700  -6.97000  -43.43300 1.000 60.30000  ? 85  ILE C N   1 
ATOM   7664  C  CA  . ILE C  1 54  ? 31.33200  -6.25700  -43.67000 1.000 59.49000  ? 85  ILE C CA  1 
ATOM   7665  C  C   . ILE C  1 54  ? 30.17400  -7.23900  -43.58600 1.000 59.02000  ? 85  ILE C C   1 
ATOM   7666  O  O   . ILE C  1 54  ? 30.24700  -8.35200  -44.11300 1.000 67.02000  ? 85  ILE C O   1 
ATOM   7667  C  CB  . ILE C  1 54  ? 31.34500  -5.54600  -45.03900 1.000 60.80000  ? 85  ILE C CB  1 
ATOM   7668  C  CG1 . ILE C  1 54  ? 32.37200  -4.41300  -45.04500 1.000 58.65000  ? 85  ILE C CG1 1 
ATOM   7669  C  CG2 . ILE C  1 54  ? 29.93300  -5.05300  -45.41800 1.000 53.54000  ? 85  ILE C CG2 1 
ATOM   7670  C  CD1 . ILE C  1 54  ? 32.60800  -3.80300  -46.40900 1.000 61.73000  ? 85  ILE C CD1 1 
ATOM   7671  N  N   . PHE C  1 55  ? 29.10100  -6.83600  -42.92000 1.000 57.59000  ? 86  PHE C N   1 
ATOM   7672  C  CA  . PHE C  1 55  ? 27.92600  -7.67800  -42.74800 1.000 59.16000  ? 86  PHE C CA  1 
ATOM   7673  C  C   . PHE C  1 55  ? 26.83300  -7.15500  -43.68700 1.000 57.59000  ? 86  PHE C C   1 
ATOM   7674  O  O   . PHE C  1 55  ? 26.25700  -6.08900  -43.45200 1.000 53.35000  ? 86  PHE C O   1 
ATOM   7675  C  CB  . PHE C  1 55  ? 27.48000  -7.66800  -41.28400 1.000 55.95000  ? 86  PHE C CB  1 
ATOM   7676  C  CG  . PHE C  1 55  ? 28.48400  -8.30500  -40.33100 1.000 61.35000  ? 86  PHE C CG  1 
ATOM   7677  C  CD1 . PHE C  1 55  ? 29.67400  -7.65000  -40.01100 1.000 58.63000  ? 86  PHE C CD1 1 
ATOM   7678  C  CD2 . PHE C  1 55  ? 28.23100  -9.54100  -39.74400 1.000 61.72000  ? 86  PHE C CD2 1 
ATOM   7679  C  CE1 . PHE C  1 55  ? 30.60500  -8.21800  -39.13700 1.000 61.80000  ? 86  PHE C CE1 1 
ATOM   7680  C  CE2 . PHE C  1 55  ? 29.14600  -10.11500 -38.86200 1.000 57.43000  ? 86  PHE C CE2 1 
ATOM   7681  C  CZ  . PHE C  1 55  ? 30.33700  -9.45400  -38.55900 1.000 59.97000  ? 86  PHE C CZ  1 
ATOM   7682  N  N   . THR C  1 56  ? 26.55700  -7.89600  -44.75600 1.000 59.93000  ? 87  THR C N   1 
ATOM   7683  C  CA  . THR C  1 56  ? 25.60700  -7.42500  -45.75900 1.000 55.73000  ? 87  THR C CA  1 
ATOM   7684  C  C   . THR C  1 56  ? 24.16400  -7.73900  -45.40400 1.000 54.01000  ? 87  THR C C   1 
ATOM   7685  O  O   . THR C  1 56  ? 23.26300  -7.28500  -46.10700 1.000 59.38000  ? 87  THR C O   1 
ATOM   7686  C  CB  . THR C  1 56  ? 25.92800  -8.03200  -47.12100 1.000 58.51000  ? 87  THR C CB  1 
ATOM   7687  O  OG1 . THR C  1 56  ? 25.74400  -9.45100  -47.05400 1.000 63.39000  ? 87  THR C OG1 1 
ATOM   7688  C  CG2 . THR C  1 56  ? 27.36600  -7.72700  -47.50500 1.000 54.94000  ? 87  THR C CG2 1 
ATOM   7689  N  N   . SER C  1 57  ? 23.91600  -8.50600  -44.34300 1.000 56.39000  ? 88  SER C N   1 
ATOM   7690  C  CA  . SER C  1 57  ? 22.57100  -8.76600  -43.86600 1.000 52.72000  ? 88  SER C CA  1 
ATOM   7691  C  C   . SER C  1 57  ? 22.56900  -8.65000  -42.33100 1.000 63.94000  ? 88  SER C C   1 
ATOM   7692  O  O   . SER C  1 57  ? 22.43800  -9.62400  -41.59100 1.000 63.99000  ? 88  SER C O   1 
ATOM   7693  C  CB  . SER C  1 57  ? 22.07700  -10.13200 -44.34200 1.000 58.94000  ? 88  SER C CB  1 
ATOM   7694  O  OG  . SER C  1 57  ? 21.62400  -10.06800 -45.68900 1.000 59.32000  ? 88  SER C OG  1 
ATOM   7695  N  N   . ALA C  1 58  ? 22.79400  -7.43600  -41.83300 1.000 60.38000  ? 89  ALA C N   1 
ATOM   7696  C  CA  . ALA C  1 58  ? 22.75000  -7.14700  -40.40600 1.000 57.45000  ? 89  ALA C CA  1 
ATOM   7697  C  C   . ALA C  1 58  ? 21.41200  -6.51100  -40.01800 1.000 56.82000  ? 89  ALA C C   1 
ATOM   7698  O  O   . ALA C  1 58  ? 20.91000  -5.61300  -40.70100 1.000 56.78000  ? 89  ALA C O   1 
ATOM   7699  C  CB  . ALA C  1 58  ? 23.90900  -6.22900  -40.01600 1.000 54.36000  ? 89  ALA C CB  1 
ATOM   7700  N  N   . TYR C  1 59  ? 20.85200  -6.95200  -38.89900 1.000 55.98000  ? 90  TYR C N   1 
ATOM   7701  C  CA  . TYR C  1 59  ? 19.55600  -6.47300  -38.44700 1.000 56.37000  ? 90  TYR C CA  1 
ATOM   7702  C  C   . TYR C  1 59  ? 19.61800  -6.03400  -36.99000 1.000 63.76000  ? 90  TYR C C   1 
ATOM   7703  O  O   . TYR C  1 59  ? 20.33400  -6.62600  -36.17500 1.000 58.55000  ? 90  TYR C O   1 
ATOM   7704  C  CB  . TYR C  1 59  ? 18.48500  -7.54100  -38.59600 1.000 60.85000  ? 90  TYR C CB  1 
ATOM   7705  C  CG  . TYR C  1 59  ? 18.22000  -7.95900  -40.02200 1.000 65.77000  ? 90  TYR C CG  1 
ATOM   7706  C  CD1 . TYR C  1 59  ? 18.94900  -8.99200  -40.61500 1.000 62.54000  ? 90  TYR C CD1 1 
ATOM   7707  C  CD2 . TYR C  1 59  ? 17.23000  -7.33000  -40.77500 1.000 62.36000  ? 90  TYR C CD2 1 
ATOM   7708  C  CE1 . TYR C  1 59  ? 18.69300  -9.38700  -41.92200 1.000 65.83000  ? 90  TYR C CE1 1 
ATOM   7709  C  CE2 . TYR C  1 59  ? 16.96800  -7.71800  -42.08400 1.000 64.62000  ? 90  TYR C CE2 1 
ATOM   7710  C  CZ  . TYR C  1 59  ? 17.70300  -8.74700  -42.65300 1.000 63.84000  ? 90  TYR C CZ  1 
ATOM   7711  O  OH  . TYR C  1 59  ? 17.44900  -9.13700  -43.95000 1.000 64.55000  ? 90  TYR C OH  1 
ATOM   7712  N  N   . VAL C  1 60  ? 18.88800  -4.97200  -36.67100 1.000 61.62000  ? 91  VAL C N   1 
ATOM   7713  C  CA  . VAL C  1 60  ? 18.63300  -4.61800  -35.28200 1.000 56.24000  ? 91  VAL C CA  1 
ATOM   7714  C  C   . VAL C  1 60  ? 17.30100  -5.24100  -34.88700 1.000 57.54000  ? 91  VAL C C   1 
ATOM   7715  O  O   . VAL C  1 60  ? 16.49700  -5.64600  -35.73200 1.000 57.09000  ? 91  VAL C O   1 
ATOM   7716  C  CB  . VAL C  1 60  ? 18.64800  -3.08300  -35.03400 1.000 48.51000  ? 91  VAL C CB  1 
ATOM   7717  C  CG1 . VAL C  1 60  ? 20.05300  -2.50600  -35.29000 1.000 46.78000  ? 91  VAL C CG1 1 
ATOM   7718  C  CG2 . VAL C  1 60  ? 17.61600  -2.36400  -35.85300 1.000 40.41000  ? 91  VAL C CG2 1 
ATOM   7719  N  N   . ALA C  1 61  ? 17.05400  -5.31200  -33.58400 1.000 54.19000  ? 92  ALA C N   1 
ATOM   7720  C  CA  . ALA C  1 61  ? 15.90300  -6.03900  -33.07300 1.000 52.56000  ? 92  ALA C CA  1 
ATOM   7721  C  C   . ALA C  1 61  ? 14.61900  -5.22100  -33.08800 1.000 52.55000  ? 92  ALA C C   1 
ATOM   7722  O  O   . ALA C  1 61  ? 13.56700  -5.75000  -32.71200 1.000 60.75000  ? 92  ALA C O   1 
ATOM   7723  C  CB  . ALA C  1 61  ? 16.17900  -6.53900  -31.65400 1.000 53.93000  ? 92  ALA C CB  1 
ATOM   7724  N  N   . HIS C  1 62  ? 14.66000  -3.95800  -33.50700 1.000 51.71000  ? 93  HIS C N   1 
ATOM   7725  C  CA  . HIS C  1 62  ? 13.44300  -3.15900  -33.59500 1.000 51.63000  ? 93  HIS C CA  1 
ATOM   7726  C  C   . HIS C  1 62  ? 13.72200  -1.98300  -34.51800 1.000 50.03000  ? 93  HIS C C   1 
ATOM   7727  O  O   . HIS C  1 62  ? 14.86600  -1.51900  -34.58300 1.000 51.24000  ? 93  HIS C O   1 
ATOM   7728  C  CB  . HIS C  1 62  ? 12.99800  -2.66500  -32.20900 1.000 60.59000  ? 93  HIS C CB  1 
ATOM   7729  C  CG  . HIS C  1 62  ? 11.56800  -2.22800  -32.14400 1.000 57.15000  ? 93  HIS C CG  1 
ATOM   7730  N  ND1 . HIS C  1 62  ? 10.52300  -3.11500  -32.00900 1.000 62.56000  ? 93  HIS C ND1 1 
ATOM   7731  C  CD2 . HIS C  1 62  ? 11.01000  -0.99800  -32.23800 1.000 53.34000  ? 93  HIS C CD2 1 
ATOM   7732  C  CE1 . HIS C  1 62  ? 9.38200   -2.44800  -31.99100 1.000 59.72000  ? 93  HIS C CE1 1 
ATOM   7733  N  NE2 . HIS C  1 62  ? 9.65000   -1.16300  -32.13100 1.000 60.94000  ? 93  HIS C NE2 1 
ATOM   7734  N  N   . PRO C  1 63  ? 12.72300  -1.49700  -35.26100 1.000 56.67000  ? 94  PRO C N   1 
ATOM   7735  C  CA  . PRO C  1 63  ? 12.99600  -0.43100  -36.23800 1.000 57.95000  ? 94  PRO C CA  1 
ATOM   7736  C  C   . PRO C  1 63  ? 13.04100  0.99300   -35.69300 1.000 56.38000  ? 94  PRO C C   1 
ATOM   7737  O  O   . PRO C  1 63  ? 13.00000  1.91700   -36.50800 1.000 56.69000  ? 94  PRO C O   1 
ATOM   7738  C  CB  . PRO C  1 63  ? 11.82600  -0.56200  -37.22800 1.000 52.57000  ? 94  PRO C CB  1 
ATOM   7739  C  CG  . PRO C  1 63  ? 11.14000  -1.82900  -36.87800 1.000 55.64000  ? 94  PRO C CG  1 
ATOM   7740  C  CD  . PRO C  1 63  ? 11.36500  -2.03700  -35.43800 1.000 55.37000  ? 94  PRO C CD  1 
ATOM   7741  N  N   . PHE C  1 64  ? 13.13600  1.22300   -34.37900 1.000 60.76000  ? 95  PHE C N   1 
ATOM   7742  C  CA  . PHE C  1 64  ? 13.38900  2.58700   -33.90800 1.000 62.36000  ? 95  PHE C CA  1 
ATOM   7743  C  C   . PHE C  1 64  ? 14.11000  2.57900   -32.56100 1.000 62.98000  ? 95  PHE C C   1 
ATOM   7744  O  O   . PHE C  1 64  ? 14.25400  1.53700   -31.91900 1.000 59.47000  ? 95  PHE C O   1 
ATOM   7745  C  CB  . PHE C  1 64  ? 12.10200  3.44000   -33.87800 1.000 53.62000  ? 95  PHE C CB  1 
ATOM   7746  C  CG  . PHE C  1 64  ? 10.98100  2.88000   -33.04400 1.000 58.37000  ? 95  PHE C CG  1 
ATOM   7747  C  CD1 . PHE C  1 64  ? 10.97100  3.02900   -31.66700 1.000 63.95000  ? 95  PHE C CD1 1 
ATOM   7748  C  CD2 . PHE C  1 64  ? 9.89800   2.25900   -33.65100 1.000 63.48000  ? 95  PHE C CD2 1 
ATOM   7749  C  CE1 . PHE C  1 64  ? 9.91600   2.53400   -30.90600 1.000 63.19000  ? 95  PHE C CE1 1 
ATOM   7750  C  CE2 . PHE C  1 64  ? 8.84100   1.76200   -32.90300 1.000 59.53000  ? 95  PHE C CE2 1 
ATOM   7751  C  CZ  . PHE C  1 64  ? 8.84900   1.89700   -31.52900 1.000 59.26000  ? 95  PHE C CZ  1 
ATOM   7752  N  N   A CYS C  1 65  ? 14.52700  3.78500   -32.15000 0.300 62.11000  ? 96  CYS C N   1 
ATOM   7753  C  CA  A CYS C  1 65  ? 15.51600  4.07200   -31.11200 0.300 61.53000  ? 96  CYS C CA  1 
ATOM   7754  C  C   A CYS C  1 65  ? 15.43900  3.18600   -29.87500 0.300 60.07000  ? 96  CYS C C   1 
ATOM   7755  O  O   A CYS C  1 65  ? 16.19000  2.21400   -29.74400 0.300 59.76000  ? 96  CYS C O   1 
ATOM   7756  C  CB  A CYS C  1 65  ? 15.39100  5.53600   -30.66000 0.300 64.24000  ? 96  CYS C CB  1 
ATOM   7757  S  SG  A CYS C  1 65  ? 15.16800  6.78200   -31.96500 0.300 60.49000  ? 96  CYS C SG  1 
HETATM 7758  N  N   B DDZ C  1 65  ? 14.51600  3.77700   -32.12000 0.700 62.14000  ? 96  DDZ C N   1 
HETATM 7759  C  CA  B DDZ C  1 65  ? 15.61000  4.01700   -31.13300 0.700 61.50000  ? 96  DDZ C CA  1 
HETATM 7760  C  C   B DDZ C  1 65  ? 15.45900  3.18100   -29.85400 0.700 60.01000  ? 96  DDZ C C   1 
HETATM 7761  O  O   B DDZ C  1 65  ? 16.24800  2.22800   -29.68500 0.700 59.73000  ? 96  DDZ C O   1 
HETATM 7762  O  OG1 B DDZ C  1 65  ? 16.04400  6.30500   -31.89600 0.700 62.72000  ? 96  DDZ C OG1 1 
HETATM 7763  O  OG2 B DDZ C  1 65  ? 14.50900  5.96000   -30.15500 0.700 63.69000  ? 96  DDZ C OG2 1 
HETATM 7764  C  CB  B DDZ C  1 65  ? 15.70800  5.50500   -30.76600 0.700 64.84000  ? 96  DDZ C CB  1 
ATOM   7765  N  N   . GLY C  1 66  ? 14.54700  3.54300   -28.95700 1.000 63.51000  ? 97  GLY C N   1 
ATOM   7766  C  CA  . GLY C  1 66  ? 14.55200  3.01000   -27.61200 1.000 56.42000  ? 97  GLY C CA  1 
ATOM   7767  C  C   . GLY C  1 66  ? 14.58100  1.50400   -27.49300 1.000 59.40000  ? 97  GLY C C   1 
ATOM   7768  O  O   . GLY C  1 66  ? 15.47000  0.92800   -26.86100 1.000 65.80000  ? 97  GLY C O   1 
ATOM   7769  N  N   . PRO C  1 67  ? 13.61900  0.82900   -28.11100 1.000 64.50000  ? 98  PRO C N   1 
ATOM   7770  C  CA  . PRO C  1 67  ? 13.60000  -0.63800  -28.00100 1.000 62.04000  ? 98  PRO C CA  1 
ATOM   7771  C  C   . PRO C  1 67  ? 14.82700  -1.29300  -28.60400 1.000 61.41000  ? 98  PRO C C   1 
ATOM   7772  O  O   . PRO C  1 67  ? 15.34400  -2.27800  -28.05600 1.000 61.27000  ? 98  PRO C O   1 
ATOM   7773  C  CB  . PRO C  1 67  ? 12.31500  -1.01400  -28.74800 1.000 64.99000  ? 98  PRO C CB  1 
ATOM   7774  C  CG  . PRO C  1 67  ? 11.44200  0.20300   -28.58400 1.000 66.23000  ? 98  PRO C CG  1 
ATOM   7775  C  CD  . PRO C  1 67  ? 12.38400  1.35600   -28.71900 1.000 62.48000  ? 98  PRO C CD  1 
ATOM   7776  N  N   . SER C  1 68  ? 15.33100  -0.75000  -29.70900 1.000 56.59000  ? 99  SER C N   1 
ATOM   7777  C  CA  . SER C  1 68  ? 16.53800  -1.29900  -30.30400 1.000 55.48000  ? 99  SER C CA  1 
ATOM   7778  C  C   . SER C  1 68  ? 17.71200  -1.18000  -29.33300 1.000 58.00000  ? 99  SER C C   1 
ATOM   7779  O  O   . SER C  1 68  ? 18.45400  -2.14400  -29.10900 1.000 55.52000  ? 99  SER C O   1 
ATOM   7780  C  CB  . SER C  1 68  ? 16.80600  -0.58500  -31.63400 1.000 55.13000  ? 99  SER C CB  1 
ATOM   7781  O  OG  . SER C  1 68  ? 18.02400  -0.99200  -32.23100 1.000 56.29000  ? 99  SER C OG  1 
ATOM   7782  N  N   . ARG C  1 69  ? 17.86500  -0.00800  -28.70500 1.000 61.40000  ? 100 ARG C N   1 
ATOM   7783  C  CA  . ARG C  1 69  ? 18.95900  0.18800   -27.75700 1.000 57.47000  ? 100 ARG C CA  1 
ATOM   7784  C  C   . ARG C  1 69  ? 18.75900  -0.66200  -26.51600 1.000 57.31000  ? 100 ARG C C   1 
ATOM   7785  O  O   . ARG C  1 69  ? 19.72400  -1.20800  -25.96600 1.000 58.81000  ? 100 ARG C O   1 
ATOM   7786  C  CB  . ARG C  1 69  ? 19.08600  1.66600   -27.40300 1.000 58.27000  ? 100 ARG C CB  1 
ATOM   7787  C  CG  . ARG C  1 69  ? 19.63200  2.47900   -28.55100 1.000 57.81000  ? 100 ARG C CG  1 
ATOM   7788  C  CD  . ARG C  1 69  ? 19.30600  3.94800   -28.44400 1.000 60.72000  ? 100 ARG C CD  1 
ATOM   7789  N  NE  . ARG C  1 69  ? 19.62900  4.61300   -29.69800 1.000 58.14000  ? 100 ARG C NE  1 
ATOM   7790  C  CZ  . ARG C  1 69  ? 20.84300  5.03300   -30.01200 1.000 56.56000  ? 100 ARG C CZ  1 
ATOM   7791  N  NH1 . ARG C  1 69  ? 21.84100  4.95600   -29.14500 1.000 61.01000  ? 100 ARG C NH1 1 
ATOM   7792  N  NH2 . ARG C  1 69  ? 21.05900  5.54800   -31.21900 1.000 51.77000  ? 100 ARG C NH2 1 
ATOM   7793  N  N   . SER C  1 70  ? 17.51700  -0.76300  -26.04500 1.000 58.67000  ? 101 SER C N   1 
ATOM   7794  C  CA  . SER C  1 70  ? 17.20600  -1.73800  -25.00800 1.000 56.77000  ? 101 SER C CA  1 
ATOM   7795  C  C   . SER C  1 70  ? 17.66200  -3.13200  -25.42200 1.000 60.39000  ? 101 SER C C   1 
ATOM   7796  O  O   . SER C  1 70  ? 18.27100  -3.86000  -24.63100 1.000 65.49000  ? 101 SER C O   1 
ATOM   7797  C  CB  . SER C  1 70  ? 15.70400  -1.71600  -24.72200 1.000 58.65000  ? 101 SER C CB  1 
ATOM   7798  O  OG  . SER C  1 70  ? 15.29300  -2.89300  -24.06100 1.000 68.69000  ? 101 SER C OG  1 
ATOM   7799  N  N   . ALA C  1 71  ? 17.41300  -3.50400  -26.67900 1.000 61.74000  ? 102 ALA C N   1 
ATOM   7800  C  CA  . ALA C  1 71  ? 17.78700  -4.83600  -27.13700 1.000 59.63000  ? 102 ALA C CA  1 
ATOM   7801  C  C   . ALA C  1 71  ? 19.29400  -5.00100  -27.17200 1.000 56.30000  ? 102 ALA C C   1 
ATOM   7802  O  O   . ALA C  1 71  ? 19.82000  -6.06100  -26.80900 1.000 57.87000  ? 102 ALA C O   1 
ATOM   7803  C  CB  . ALA C  1 71  ? 17.18800  -5.10700  -28.51700 1.000 60.04000  ? 102 ALA C CB  1 
ATOM   7804  N  N   . ILE C  1 72  ? 20.01100  -3.97000  -27.60800 1.000 53.96000  ? 103 ILE C N   1 
ATOM   7805  C  CA  . ILE C  1 72  ? 21.46000  -4.10000  -27.67700 1.000 56.33000  ? 103 ILE C CA  1 
ATOM   7806  C  C   . ILE C  1 72  ? 22.02800  -4.37500  -26.29400 1.000 61.10000  ? 103 ILE C C   1 
ATOM   7807  O  O   . ILE C  1 72  ? 22.86200  -5.27400  -26.12200 1.000 54.75000  ? 103 ILE C O   1 
ATOM   7808  C  CB  . ILE C  1 72  ? 22.09600  -2.85700  -28.32100 1.000 55.60000  ? 103 ILE C CB  1 
ATOM   7809  C  CG1 . ILE C  1 72  ? 21.88600  -2.89400  -29.83400 1.000 53.23000  ? 103 ILE C CG1 1 
ATOM   7810  C  CG2 . ILE C  1 72  ? 23.56700  -2.78100  -27.98700 1.000 52.05000  ? 103 ILE C CG2 1 
ATOM   7811  C  CD1 . ILE C  1 72  ? 22.13600  -1.57500  -30.53600 1.000 56.63000  ? 103 ILE C CD1 1 
ATOM   7812  N  N   . LEU C  1 73  ? 21.55500  -3.63900  -25.27700 1.000 55.50000  ? 104 LEU C N   1 
ATOM   7813  C  CA  . LEU C  1 73  ? 22.17100  -3.76600  -23.96400 1.000 61.12000  ? 104 LEU C CA  1 
ATOM   7814  C  C   . LEU C  1 73  ? 21.61600  -4.92800  -23.15500 1.000 62.66000  ? 104 LEU C C   1 
ATOM   7815  O  O   . LEU C  1 73  ? 22.36800  -5.54800  -22.39500 1.000 66.00000  ? 104 LEU C O   1 
ATOM   7816  C  CB  . LEU C  1 73  ? 22.05400  -2.44900  -23.19500 1.000 62.25000  ? 104 LEU C CB  1 
ATOM   7817  C  CG  . LEU C  1 73  ? 23.23400  -1.52800  -23.54000 1.000 66.30000  ? 104 LEU C CG  1 
ATOM   7818  C  CD1 . LEU C  1 73  ? 22.95100  -0.06900  -23.27600 1.000 59.49000  ? 104 LEU C CD1 1 
ATOM   7819  C  CD2 . LEU C  1 73  ? 24.48100  -1.97200  -22.75600 1.000 67.67000  ? 104 LEU C CD2 1 
ATOM   7820  N  N   . THR C  1 74  ? 20.34500  -5.27800  -23.31700 1.000 61.92000  ? 105 THR C N   1 
ATOM   7821  C  CA  . THR C  1 74  ? 19.84100  -6.43200  -22.57900 1.000 70.28000  ? 105 THR C CA  1 
ATOM   7822  C  C   . THR C  1 74  ? 20.07600  -7.75600  -23.29300 1.000 67.48000  ? 105 THR C C   1 
ATOM   7823  O  O   . THR C  1 74  ? 20.06900  -8.80300  -22.63300 1.000 64.37000  ? 105 THR C O   1 
ATOM   7824  C  CB  . THR C  1 74  ? 18.34300  -6.29900  -22.30300 1.000 67.80000  ? 105 THR C CB  1 
ATOM   7825  O  OG1 . THR C  1 74  ? 17.64300  -6.36200  -23.54300 1.000 66.93000  ? 105 THR C OG1 1 
ATOM   7826  C  CG2 . THR C  1 74  ? 18.03200  -4.98500  -21.60600 1.000 66.36000  ? 105 THR C CG2 1 
ATOM   7827  N  N   . GLY C  1 75  ? 20.32700  -7.73300  -24.60500 1.000 67.97000  ? 106 GLY C N   1 
ATOM   7828  C  CA  . GLY C  1 75  ? 20.47400  -8.95600  -25.37700 1.000 68.91000  ? 106 GLY C CA  1 
ATOM   7829  C  C   . GLY C  1 75  ? 19.18400  -9.71500  -25.61300 1.000 67.81000  ? 106 GLY C C   1 
ATOM   7830  O  O   . GLY C  1 75  ? 19.22800  -10.87700 -26.03300 1.000 64.51000  ? 106 GLY C O   1 
ATOM   7831  N  N   . ARG C  1 76  ? 18.03800  -9.08400  -25.36600 1.000 64.51000  ? 107 ARG C N   1 
ATOM   7832  C  CA  . ARG C  1 76  ? 16.73600  -9.70700  -25.52100 1.000 66.73000  ? 107 ARG C CA  1 
ATOM   7833  C  C   . ARG C  1 76  ? 15.85500  -8.80700  -26.37300 1.000 64.76000  ? 107 ARG C C   1 
ATOM   7834  O  O   . ARG C  1 76  ? 15.99600  -7.58100  -26.35200 1.000 64.51000  ? 107 ARG C O   1 
ATOM   7835  C  CB  . ARG C  1 76  ? 16.03800  -9.95200  -24.17000 1.000 67.40000  ? 107 ARG C CB  1 
ATOM   7836  C  CG  . ARG C  1 76  ? 16.68900  -11.01000 -23.29700 1.000 72.85000  ? 107 ARG C CG  1 
ATOM   7837  C  CD  . ARG C  1 76  ? 15.85400  -11.26400 -22.04400 1.000 77.26000  ? 107 ARG C CD  1 
ATOM   7838  N  NE  . ARG C  1 76  ? 14.86900  -12.32700 -22.22900 1.000 77.07000  ? 107 ARG C NE  1 
ATOM   7839  C  CZ  . ARG C  1 76  ? 13.78300  -12.47300 -21.48200 1.000 81.77000  ? 107 ARG C CZ  1 
ATOM   7840  N  NH1 . ARG C  1 76  ? 13.52000  -11.64700 -20.48100 1.000 80.12000  ? 107 ARG C NH1 1 
ATOM   7841  N  NH2 . ARG C  1 76  ? 12.94100  -13.47300 -21.74300 1.000 83.56000  ? 107 ARG C NH2 1 
ATOM   7842  N  N   . TYR C  1 77  ? 14.93000  -9.42500  -27.10300 1.000 65.99000  ? 108 TYR C N   1 
ATOM   7843  C  CA  . TYR C  1 77  ? 13.95200  -8.65200  -27.85300 1.000 67.88000  ? 108 TYR C CA  1 
ATOM   7844  C  C   . TYR C  1 77  ? 13.19500  -7.73800  -26.90000 1.000 65.93000  ? 108 TYR C C   1 
ATOM   7845  O  O   . TYR C  1 77  ? 12.83800  -8.15900  -25.79200 1.000 65.61000  ? 108 TYR C O   1 
ATOM   7846  C  CB  . TYR C  1 77  ? 12.95700  -9.56300  -28.58300 1.000 68.50000  ? 108 TYR C CB  1 
ATOM   7847  C  CG  . TYR C  1 77  ? 13.48000  -10.11900 -29.88200 1.000 62.44000  ? 108 TYR C CG  1 
ATOM   7848  C  CD1 . TYR C  1 77  ? 13.57100  -9.32200  -31.01400 1.000 62.35000  ? 108 TYR C CD1 1 
ATOM   7849  C  CD2 . TYR C  1 77  ? 13.90500  -11.43700 -29.97000 1.000 63.97000  ? 108 TYR C CD2 1 
ATOM   7850  C  CE1 . TYR C  1 77  ? 14.05900  -9.82000  -32.20100 1.000 62.06000  ? 108 TYR C CE1 1 
ATOM   7851  C  CE2 . TYR C  1 77  ? 14.40300  -11.94300 -31.15200 1.000 67.96000  ? 108 TYR C CE2 1 
ATOM   7852  C  CZ  . TYR C  1 77  ? 14.47300  -11.13000 -32.26700 1.000 66.13000  ? 108 TYR C CZ  1 
ATOM   7853  O  OH  . TYR C  1 77  ? 14.96000  -11.62800 -33.45200 1.000 63.97000  ? 108 TYR C OH  1 
ATOM   7854  N  N   . PRO C  1 78  ? 12.92700  -6.49200  -27.29500 1.000 66.40000  ? 109 PRO C N   1 
ATOM   7855  C  CA  . PRO C  1 78  ? 12.18500  -5.59600  -26.39800 1.000 67.15000  ? 109 PRO C CA  1 
ATOM   7856  C  C   . PRO C  1 78  ? 10.78800  -6.08800  -26.07300 1.000 71.10000  ? 109 PRO C C   1 
ATOM   7857  O  O   . PRO C  1 78  ? 10.24500  -5.70300  -25.03200 1.000 70.61000  ? 109 PRO C O   1 
ATOM   7858  C  CB  . PRO C  1 78  ? 12.15000  -4.27600  -27.17900 1.000 63.37000  ? 109 PRO C CB  1 
ATOM   7859  C  CG  . PRO C  1 78  ? 12.27800  -4.70100  -28.61200 1.000 60.78000  ? 109 PRO C CG  1 
ATOM   7860  C  CD  . PRO C  1 78  ? 13.25000  -5.84300  -28.57700 1.000 59.92000  ? 109 PRO C CD  1 
ATOM   7861  N  N   . HIS C  1 79  ? 10.20400  -6.96000  -26.90200 1.000 68.72000  ? 110 HIS C N   1 
ATOM   7862  C  CA  . HIS C  1 79  ? 8.89200   -7.51700  -26.58500 1.000 69.92000  ? 110 HIS C CA  1 
ATOM   7863  C  C   . HIS C  1 79  ? 8.95700   -8.50000  -25.43100 1.000 72.16000  ? 110 HIS C C   1 
ATOM   7864  O  O   . HIS C  1 79  ? 7.90600   -8.86800  -24.89900 1.000 72.49000  ? 110 HIS C O   1 
ATOM   7865  C  CB  . HIS C  1 79  ? 8.25700   -8.20800  -27.80600 1.000 66.43000  ? 110 HIS C CB  1 
ATOM   7866  C  CG  . HIS C  1 79  ? 8.45900   -7.47400  -29.09500 1.000 62.95000  ? 110 HIS C CG  1 
ATOM   7867  N  ND1 . HIS C  1 79  ? 9.66700   -7.44400  -29.75600 1.000 61.90000  ? 110 HIS C ND1 1 
ATOM   7868  C  CD2 . HIS C  1 79  ? 7.60000   -6.74800  -29.84800 1.000 65.94000  ? 110 HIS C CD2 1 
ATOM   7869  C  CE1 . HIS C  1 79  ? 9.54800   -6.71600  -30.85100 1.000 62.34000  ? 110 HIS C CE1 1 
ATOM   7870  N  NE2 . HIS C  1 79  ? 8.30100   -6.29000  -30.93500 1.000 61.97000  ? 110 HIS C NE2 1 
ATOM   7871  N  N   . LEU C  1 80  ? 10.15000  -8.96400  -25.05700 1.000 72.51000  ? 111 LEU C N   1 
ATOM   7872  C  CA  . LEU C  1 80  ? 10.27300  -9.85700  -23.91400 1.000 76.63000  ? 111 LEU C CA  1 
ATOM   7873  C  C   . LEU C  1 80  ? 10.65200  -9.13000  -22.63000 1.000 79.01000  ? 111 LEU C C   1 
ATOM   7874  O  O   . LEU C  1 80  ? 10.46500  -9.68500  -21.54400 1.000 80.72000  ? 111 LEU C O   1 
ATOM   7875  C  CB  . LEU C  1 80  ? 11.27900  -10.98000 -24.19900 1.000 76.07000  ? 111 LEU C CB  1 
ATOM   7876  C  CG  . LEU C  1 80  ? 11.21200  -11.59000 -25.60600 1.000 76.55000  ? 111 LEU C CG  1 
ATOM   7877  C  CD1 . LEU C  1 80  ? 12.37500  -12.54500 -25.85200 1.000 76.09000  ? 111 LEU C CD1 1 
ATOM   7878  C  CD2 . LEU C  1 80  ? 9.87600   -12.24800 -25.88500 1.000 72.38000  ? 111 LEU C CD2 1 
ATOM   7879  N  N   . THR C  1 81  ? 11.16100  -7.90400  -22.72800 1.000 75.85000  ? 112 THR C N   1 
ATOM   7880  C  CA  . THR C  1 81  ? 11.52200  -7.10800  -21.56500 1.000 71.71000  ? 112 THR C CA  1 
ATOM   7881  C  C   . THR C  1 81  ? 10.49400  -6.03600  -21.24900 1.000 72.54000  ? 112 THR C C   1 
ATOM   7882  O  O   . THR C  1 81  ? 10.61900  -5.36800  -20.21800 1.000 70.60000  ? 112 THR C O   1 
ATOM   7883  C  CB  . THR C  1 81  ? 12.88400  -6.43700  -21.78000 1.000 74.39000  ? 112 THR C CB  1 
ATOM   7884  O  OG1 . THR C  1 81  ? 12.83400  -5.61000  -22.95600 1.000 64.52000  ? 112 THR C OG1 1 
ATOM   7885  C  CG2 . THR C  1 81  ? 13.99000  -7.49100  -21.90800 1.000 72.52000  ? 112 THR C CG2 1 
ATOM   7886  N  N   . GLY C  1 82  ? 9.47500   -5.88500  -22.09600 1.000 72.88000  ? 113 GLY C N   1 
ATOM   7887  C  CA  . GLY C  1 82  ? 8.43800   -4.89000  -21.91700 1.000 66.56000  ? 113 GLY C CA  1 
ATOM   7888  C  C   . GLY C  1 82  ? 8.76900   -3.51300  -22.43100 1.000 66.86000  ? 113 GLY C C   1 
ATOM   7889  O  O   . GLY C  1 82  ? 8.04500   -2.56300  -22.12500 1.000 69.70000  ? 113 GLY C O   1 
ATOM   7890  N  N   . THR C  1 83  ? 9.80400   -3.37600  -23.25100 1.000 63.74000  ? 114 THR C N   1 
ATOM   7891  C  CA  . THR C  1 83  ? 10.35900  -2.07600  -23.60000 1.000 67.00000  ? 114 THR C CA  1 
ATOM   7892  C  C   . THR C  1 83  ? 10.25200  -1.78300  -25.09200 1.000 68.83000  ? 114 THR C C   1 
ATOM   7893  O  O   . THR C  1 83  ? 11.13900  -1.16200  -25.68300 1.000 71.05000  ? 114 THR C O   1 
ATOM   7894  C  CB  . THR C  1 83  ? 11.81100  -1.99000  -23.13800 1.000 73.70000  ? 114 THR C CB  1 
ATOM   7895  O  OG1 . THR C  1 83  ? 12.54800  -3.09500  -23.68200 1.000 70.90000  ? 114 THR C OG1 1 
ATOM   7896  C  CG2 . THR C  1 83  ? 11.88900  -2.03200  -21.59700 1.000 64.03000  ? 114 THR C CG2 1 
ATOM   7897  N  N   . ALA C  1 84  ? 9.16300   -2.22900  -25.72100 1.000 72.58000  ? 115 ALA C N   1 
ATOM   7898  C  CA  . ALA C  1 84  ? 8.96100   -2.08800  -27.16400 1.000 69.42000  ? 115 ALA C CA  1 
ATOM   7899  C  C   . ALA C  1 84  ? 8.34400   -0.75600  -27.57000 1.000 67.84000  ? 115 ALA C C   1 
ATOM   7900  O  O   . ALA C  1 84  ? 8.08900   -0.54600  -28.75900 1.000 64.41000  ? 115 ALA C O   1 
ATOM   7901  C  CB  . ALA C  1 84  ? 8.08800   -3.22500  -27.69200 1.000 64.45000  ? 115 ALA C CB  1 
ATOM   7902  N  N   . TYR C  1 85  ? 8.09500   0.14400   -26.62900 1.000 69.62000  ? 116 TYR C N   1 
ATOM   7903  C  CA  . TYR C  1 85  ? 7.76100   1.52200   -26.94500 1.000 64.38000  ? 116 TYR C CA  1 
ATOM   7904  C  C   . TYR C  1 85  ? 8.87900   2.44200   -26.47100 1.000 68.19000  ? 116 TYR C C   1 
ATOM   7905  O  O   . TYR C  1 85  ? 9.61700   2.12800   -25.52900 1.000 68.96000  ? 116 TYR C O   1 
ATOM   7906  C  CB  . TYR C  1 85  ? 6.44400   1.94500   -26.29200 1.000 74.58000  ? 116 TYR C CB  1 
ATOM   7907  C  CG  . TYR C  1 85  ? 5.18300   1.34500   -26.89400 1.000 71.63000  ? 116 TYR C CG  1 
ATOM   7908  C  CD1 . TYR C  1 85  ? 4.65600   0.15500   -26.40300 1.000 72.58000  ? 116 TYR C CD1 1 
ATOM   7909  C  CD2 . TYR C  1 85  ? 4.50200   1.98800   -27.91800 1.000 67.13000  ? 116 TYR C CD2 1 
ATOM   7910  C  CE1 . TYR C  1 85  ? 3.48900   -0.39100  -26.92900 1.000 74.48000  ? 116 TYR C CE1 1 
ATOM   7911  C  CE2 . TYR C  1 85  ? 3.32500   1.44800   -28.45700 1.000 74.01000  ? 116 TYR C CE2 1 
ATOM   7912  C  CZ  . TYR C  1 85  ? 2.82600   0.25500   -27.95600 1.000 73.78000  ? 116 TYR C CZ  1 
ATOM   7913  O  OH  . TYR C  1 85  ? 1.66700   -0.30800  -28.47100 1.000 73.87000  ? 116 TYR C OH  1 
ATOM   7914  N  N   . ASN C  1 86  ? 9.00200   3.57900   -27.14100 1.000 64.50000  ? 117 ASN C N   1 
ATOM   7915  C  CA  . ASN C  1 86  ? 9.92300   4.61600   -26.70800 1.000 69.18000  ? 117 ASN C CA  1 
ATOM   7916  C  C   . ASN C  1 86  ? 9.47000   5.21600   -25.37500 1.000 74.90000  ? 117 ASN C C   1 
ATOM   7917  O  O   . ASN C  1 86  ? 8.27800   5.24400   -25.03700 1.000 72.52000  ? 117 ASN C O   1 
ATOM   7918  C  CB  . ASN C  1 86  ? 10.01900  5.73100   -27.76100 1.000 63.03000  ? 117 ASN C CB  1 
ATOM   7919  C  CG  . ASN C  1 86  ? 11.11200  5.49000   -28.78200 1.000 65.69000  ? 117 ASN C CG  1 
ATOM   7920  O  OD1 . ASN C  1 86  ? 11.98500  4.63200   -28.59500 1.000 65.61000  ? 117 ASN C OD1 1 
ATOM   7921  N  ND2 . ASN C  1 86  ? 11.07900  6.25300   -29.86900 1.000 65.38000  ? 117 ASN C ND2 1 
ATOM   7922  N  N   . LEU C  1 87  ? 10.44400  5.67000   -24.59800 1.000 76.40000  ? 118 LEU C N   1 
ATOM   7923  C  CA  . LEU C  1 87  ? 10.14400  6.59300   -23.51700 1.000 71.96000  ? 118 LEU C CA  1 
ATOM   7924  C  C   . LEU C  1 87  ? 9.70300   7.92200   -24.10600 1.000 66.02000  ? 118 LEU C C   1 
ATOM   7925  O  O   . LEU C  1 87  ? 10.28300  8.40400   -25.08400 1.000 67.99000  ? 118 LEU C O   1 
ATOM   7926  C  CB  . LEU C  1 87  ? 11.37600  6.80300   -22.63600 1.000 66.91000  ? 118 LEU C CB  1 
ATOM   7927  C  CG  . LEU C  1 87  ? 11.42500  5.99600   -21.34800 1.000 66.78000  ? 118 LEU C CG  1 
ATOM   7928  C  CD1 . LEU C  1 87  ? 10.03600  5.48800   -21.04400 1.000 74.24000  ? 118 LEU C CD1 1 
ATOM   7929  C  CD2 . LEU C  1 87  ? 12.41300  4.86000   -21.41500 1.000 71.96000  ? 118 LEU C CD2 1 
ATOM   7930  N  N   . PHE C  1 88  ? 8.64500   8.50200   -23.54600 1.000 65.57000  ? 119 PHE C N   1 
ATOM   7931  C  CA  . PHE C  1 88  ? 8.29800   9.84700   -23.97700 1.000 68.56000  ? 119 PHE C CA  1 
ATOM   7932  C  C   . PHE C  1 88  ? 9.42100   10.79300  -23.57000 1.000 68.24000  ? 119 PHE C C   1 
ATOM   7933  O  O   . PHE C  1 88  ? 10.14900  10.54300  -22.60200 1.000 73.43000  ? 119 PHE C O   1 
ATOM   7934  C  CB  . PHE C  1 88  ? 6.97200   10.30500  -23.36900 1.000 66.96000  ? 119 PHE C CB  1 
ATOM   7935  C  CG  . PHE C  1 88  ? 6.18100   11.22500  -24.26900 1.000 68.56000  ? 119 PHE C CG  1 
ATOM   7936  C  CD1 . PHE C  1 88  ? 5.40800   10.70900  -25.30400 1.000 68.92000  ? 119 PHE C CD1 1 
ATOM   7937  C  CD2 . PHE C  1 88  ? 6.24100   12.60100  -24.10700 1.000 66.77000  ? 119 PHE C CD2 1 
ATOM   7938  C  CE1 . PHE C  1 88  ? 4.68200   11.55200  -26.14600 1.000 69.92000  ? 119 PHE C CE1 1 
ATOM   7939  C  CE2 . PHE C  1 88  ? 5.52400   13.44700  -24.94100 1.000 73.36000  ? 119 PHE C CE2 1 
ATOM   7940  C  CZ  . PHE C  1 88  ? 4.74200   12.92100  -25.96300 1.000 72.16000  ? 119 PHE C CZ  1 
ATOM   7941  N  N   . HIS C  1 89  ? 9.58900   11.87600  -24.32300 1.000 64.18000  ? 120 HIS C N   1 
ATOM   7942  C  CA  . HIS C  1 89  ? 10.62500  12.81800  -23.94100 1.000 64.41000  ? 120 HIS C CA  1 
ATOM   7943  C  C   . HIS C  1 89  ? 10.32000  13.38500  -22.55300 1.000 71.89000  ? 120 HIS C C   1 
ATOM   7944  O  O   . HIS C  1 89  ? 9.16300   13.45900  -22.12500 1.000 64.74000  ? 120 HIS C O   1 
ATOM   7945  C  CB  . HIS C  1 89  ? 10.81500  13.89500  -25.02500 1.000 65.46000  ? 120 HIS C CB  1 
ATOM   7946  C  CG  . HIS C  1 89  ? 9.71600   14.91100  -25.12700 1.000 81.13000  ? 120 HIS C CG  1 
ATOM   7947  N  ND1 . HIS C  1 89  ? 9.74700   15.93100  -26.05900 1.000 85.54000  ? 120 HIS C ND1 1 
ATOM   7948  C  CD2 . HIS C  1 89  ? 8.55300   15.05900  -24.44900 1.000 79.17000  ? 120 HIS C CD2 1 
ATOM   7949  C  CE1 . HIS C  1 89  ? 8.65900   16.67000  -25.93700 1.000 82.76000  ? 120 HIS C CE1 1 
ATOM   7950  N  NE2 . HIS C  1 89  ? 7.91700   16.16100  -24.96800 1.000 82.29000  ? 120 HIS C NE2 1 
ATOM   7951  N  N   . ASN C  1 90  ? 11.38600  13.70300  -21.81600 1.000 67.46000  ? 121 ASN C N   1 
ATOM   7952  C  CA  . ASN C  1 90  ? 11.27400  14.15200  -20.43100 1.000 66.25000  ? 121 ASN C CA  1 
ATOM   7953  C  C   . ASN C  1 90  ? 10.55600  13.12000  -19.57000 1.000 66.70000  ? 121 ASN C C   1 
ATOM   7954  O  O   . ASN C  1 90  ? 9.73400   13.46000  -18.72500 1.000 75.12000  ? 121 ASN C O   1 
ATOM   7955  C  CB  . ASN C  1 90  ? 10.56400  15.50100  -20.35000 1.000 62.12000  ? 121 ASN C CB  1 
ATOM   7956  C  CG  . ASN C  1 90  ? 11.31800  16.59000  -21.06000 1.000 69.68000  ? 121 ASN C CG  1 
ATOM   7957  O  OD1 . ASN C  1 90  ? 11.30600  16.68300  -22.29100 1.000 66.34000  ? 121 ASN C OD1 1 
ATOM   7958  N  ND2 . ASN C  1 90  ? 11.99200  17.43100  -20.28200 1.000 77.99000  ? 121 ASN C ND2 1 
ATOM   7959  N  N   . SER C  1 91  ? 10.88000  11.84800  -19.76100 1.000 62.92000  ? 122 SER C N   1 
ATOM   7960  C  CA  . SER C  1 91  ? 10.20100  10.82700  -18.97900 1.000 73.42000  ? 122 SER C CA  1 
ATOM   7961  C  C   . SER C  1 91  ? 10.52400  10.98400  -17.49300 1.000 78.64000  ? 122 SER C C   1 
ATOM   7962  O  O   . SER C  1 91  ? 11.48100  11.66300  -17.10000 1.000 82.98000  ? 122 SER C O   1 
ATOM   7963  C  CB  . SER C  1 91  ? 10.59300  9.42600   -19.45900 1.000 75.29000  ? 122 SER C CB  1 
ATOM   7964  O  OG  . SER C  1 91  ? 11.61700  8.85500   -18.64400 1.000 80.41000  ? 122 SER C OG  1 
ATOM   7965  N  N   . SER C  1 92  ? 9.70700   10.33400  -16.66500 1.000 77.64000  ? 123 SER C N   1 
ATOM   7966  C  CA  . SER C  1 92  ? 9.78300   10.53000  -15.22400 1.000 82.20000  ? 123 SER C CA  1 
ATOM   7967  C  C   . SER C  1 92  ? 11.17900  10.21000  -14.71900 1.000 82.55000  ? 123 SER C C   1 
ATOM   7968  O  O   . SER C  1 92  ? 11.81400  9.24800   -15.16400 1.000 82.47000  ? 123 SER C O   1 
ATOM   7969  C  CB  . SER C  1 92  ? 8.76000   9.65200   -14.49500 1.000 84.69000  ? 123 SER C CB  1 
ATOM   7970  O  OG  . SER C  1 92  ? 8.98400   9.65600   -13.08800 1.000 84.73000  ? 123 SER C OG  1 
ATOM   7971  N  N   . GLU C  1 93  ? 11.66100  11.04400  -13.79900 1.000 79.40000  ? 124 GLU C N   1 
ATOM   7972  C  CA  . GLU C  1 93  ? 12.96800  10.85700  -13.19300 1.000 80.65000  ? 124 GLU C CA  1 
ATOM   7973  C  C   . GLU C  1 93  ? 12.88300  10.30500  -11.78100 1.000 74.20000  ? 124 GLU C C   1 
ATOM   7974  O  O   . GLU C  1 93  ? 13.90500  10.19900  -11.10300 1.000 73.90000  ? 124 GLU C O   1 
ATOM   7975  C  CB  . GLU C  1 93  ? 13.73500  12.17400  -13.21500 1.000 76.26000  ? 124 GLU C CB  1 
ATOM   7976  C  CG  . GLU C  1 93  ? 13.75900  12.77500  -14.59700 1.000 76.31000  ? 124 GLU C CG  1 
ATOM   7977  C  CD  . GLU C  1 93  ? 14.88400  13.74500  -14.76900 1.000 81.68000  ? 124 GLU C CD  1 
ATOM   7978  O  OE1 . GLU C  1 93  ? 15.81700  13.68300  -13.93800 1.000 85.71000  ? 124 GLU C OE1 1 
ATOM   7979  O  OE2 . GLU C  1 93  ? 14.85400  14.53800  -15.73900 1.000 80.90000  ? 124 GLU C OE2 1 
ATOM   7980  N  N   . ASP C  1 94  ? 11.69900  9.90800   -11.34400 1.000 76.01000  ? 125 ASP C N   1 
ATOM   7981  C  CA  . ASP C  1 94  ? 11.51600  9.34500   -10.02000 1.000 79.85000  ? 125 ASP C CA  1 
ATOM   7982  C  C   . ASP C  1 94  ? 11.46200  7.83200   -10.14700 1.000 78.68000  ? 125 ASP C C   1 
ATOM   7983  O  O   . ASP C  1 94  ? 10.69300  7.29700   -10.94800 1.000 83.62000  ? 125 ASP C O   1 
ATOM   7984  C  CB  . ASP C  1 94  ? 10.24100  9.88000   -9.36300  1.000 84.20000  ? 125 ASP C CB  1 
ATOM   7985  N  N   . ASP C  1 95  ? 12.28900  7.14800   -9.36000  1.000 75.16000  ? 126 ASP C N   1 
ATOM   7986  C  CA  . ASP C  1 95  ? 12.32300  5.69400   -9.38900  1.000 80.91000  ? 126 ASP C CA  1 
ATOM   7987  C  C   . ASP C  1 95  ? 10.94700  5.06700   -9.18800  1.000 87.49000  ? 126 ASP C C   1 
ATOM   7988  O  O   . ASP C  1 95  ? 10.72600  3.93500   -9.63100  1.000 90.75000  ? 126 ASP C O   1 
ATOM   7989  C  CB  . ASP C  1 95  ? 13.29200  5.18200   -8.32700  1.000 85.46000  ? 126 ASP C CB  1 
ATOM   7990  C  CG  . ASP C  1 95  ? 14.73700  5.47800   -8.67400  1.000 86.32000  ? 126 ASP C CG  1 
ATOM   7991  O  OD1 . ASP C  1 95  ? 14.96900  6.05800   -9.75700  1.000 86.56000  ? 126 ASP C OD1 1 
ATOM   7992  O  OD2 . ASP C  1 95  ? 15.63700  5.12100   -7.88000  1.000 82.85000  ? 126 ASP C OD2 1 
ATOM   7993  N  N   . LYS C  1 96  ? 10.01500  5.76900   -8.53400  1.000 89.00000  ? 127 LYS C N   1 
ATOM   7994  C  CA  . LYS C  1 96  ? 8.71600   5.16700   -8.24100  1.000 86.86000  ? 127 LYS C CA  1 
ATOM   7995  C  C   . LYS C  1 96  ? 7.98200   4.76600   -9.51500  1.000 85.22000  ? 127 LYS C C   1 
ATOM   7996  O  O   . LYS C  1 96  ? 7.47100   3.64600   -9.61200  1.000 86.17000  ? 127 LYS C O   1 
ATOM   7997  C  CB  . LYS C  1 96  ? 7.86300   6.13400   -7.41500  1.000 81.99000  ? 127 LYS C CB  1 
ATOM   7998  N  N   . ASP C  1 97  ? 7.90500   5.67000   -10.50000 1.000 88.71000  ? 128 ASP C N   1 
ATOM   7999  C  CA  . ASP C  1 97  ? 7.33900   5.35700   -11.82100 1.000 87.09000  ? 128 ASP C CA  1 
ATOM   8000  C  C   . ASP C  1 97  ? 8.41400   4.75300   -12.72800 1.000 89.24000  ? 128 ASP C C   1 
ATOM   8001  O  O   . ASP C  1 97  ? 8.97300   5.42000   -13.60300 1.000 91.82000  ? 128 ASP C O   1 
ATOM   8002  C  CB  . ASP C  1 97  ? 6.70200   6.58300   -12.47100 1.000 87.87000  ? 128 ASP C CB  1 
ATOM   8003  C  CG  . ASP C  1 97  ? 6.83100   7.82600   -11.64000 1.000 85.31000  ? 128 ASP C CG  1 
ATOM   8004  O  OD1 . ASP C  1 97  ? 7.94000   8.08800   -11.14200 1.000 86.35000  ? 128 ASP C OD1 1 
ATOM   8005  O  OD2 . ASP C  1 97  ? 5.82600   8.55700   -11.51900 1.000 84.93000  ? 128 ASP C OD2 1 
ATOM   8006  N  N   . ASN C  1 98  ? 8.72100   3.47300   -12.49200 1.000 87.07000  ? 129 ASN C N   1 
ATOM   8007  C  CA  . ASN C  1 98  ? 9.71300   2.69100   -13.23800 1.000 85.56000  ? 129 ASN C CA  1 
ATOM   8008  C  C   . ASN C  1 98  ? 9.75500   2.95300   -14.75200 1.000 84.14000  ? 129 ASN C C   1 
ATOM   8009  O  O   . ASN C  1 98  ? 9.55800   2.02500   -15.54400 1.000 81.18000  ? 129 ASN C O   1 
ATOM   8010  C  CB  . ASN C  1 98  ? 9.47600   1.19700   -12.98900 1.000 86.48000  ? 129 ASN C CB  1 
ATOM   8011  N  N   . MET C  1 99  ? 9.99700   4.20400   -15.16900 1.000 82.39000  ? 130 MET C N   1 
ATOM   8012  C  CA  . MET C  1 99  ? 10.07800  4.56700   -16.58800 1.000 73.79000  ? 130 MET C CA  1 
ATOM   8013  C  C   . MET C  1 99  ? 11.49900  4.34600   -17.11000 1.000 75.15000  ? 130 MET C C   1 
ATOM   8014  O  O   . MET C  1 99  ? 12.24000  5.28100   -17.41900 1.000 78.81000  ? 130 MET C O   1 
ATOM   8015  C  CB  . MET C  1 99  ? 9.66000   6.01600   -16.78700 1.000 70.72000  ? 130 MET C CB  1 
ATOM   8016  C  CG  . MET C  1 99  ? 8.17200   6.25600   -16.64400 1.000 82.39000  ? 130 MET C CG  1 
ATOM   8017  S  SD  . MET C  1 99  ? 7.19400   5.14000   -17.65700 1.000 78.96000  ? 130 MET C SD  1 
ATOM   8018  C  CE  . MET C  1 99  ? 5.54800   5.47300   -17.04800 1.000 81.46000  ? 130 MET C CE  1 
ATOM   8019  N  N   . GLY C  1 100 ? 11.85900  3.07400   -17.23400 1.000 71.77000  ? 131 GLY C N   1 
ATOM   8020  C  CA  . GLY C  1 100 ? 13.17800  2.69700   -17.71200 1.000 71.38000  ? 131 GLY C CA  1 
ATOM   8021  C  C   . GLY C  1 100 ? 13.28200  1.19000   -17.78100 1.000 69.38000  ? 131 GLY C C   1 
ATOM   8022  O  O   . GLY C  1 100 ? 12.47900  0.46200   -17.19000 1.000 71.84000  ? 131 GLY C O   1 
ATOM   8023  N  N   . VAL C  1 101 ? 14.32500  0.73100   -18.46700 1.000 70.81000  ? 132 VAL C N   1 
ATOM   8024  C  CA  . VAL C  1 101 ? 14.50000  -0.71000  -18.70100 1.000 69.62000  ? 132 VAL C CA  1 
ATOM   8025  C  C   . VAL C  1 101 ? 14.62300  -1.43900  -17.36300 1.000 73.92000  ? 132 VAL C C   1 
ATOM   8026  O  O   . VAL C  1 101 ? 15.47900  -1.07200  -16.53000 1.000 72.56000  ? 132 VAL C O   1 
ATOM   8027  C  CB  . VAL C  1 101 ? 15.74000  -0.96500  -19.58500 1.000 69.06000  ? 132 VAL C CB  1 
ATOM   8028  C  CG1 . VAL C  1 101 ? 15.92600  -2.45300  -19.84600 1.000 67.31000  ? 132 VAL C CG1 1 
ATOM   8029  C  CG2 . VAL C  1 101 ? 15.64400  -0.20500  -20.89900 1.000 62.99000  ? 132 VAL C CG2 1 
ATOM   8030  N  N   . PRO C  1 102 ? 13.83600  -2.49400  -17.13400 1.000 72.41000  ? 133 PRO C N   1 
ATOM   8031  C  CA  . PRO C  1 102 ? 13.86200  -3.20800  -15.84700 1.000 71.05000  ? 133 PRO C CA  1 
ATOM   8032  C  C   . PRO C  1 102 ? 15.26800  -3.50300  -15.34000 1.000 74.01000  ? 133 PRO C C   1 
ATOM   8033  O  O   . PRO C  1 102 ? 16.11300  -4.04000  -16.06400 1.000 75.04000  ? 133 PRO C O   1 
ATOM   8034  C  CB  . PRO C  1 102 ? 13.09800  -4.50200  -16.15400 1.000 71.79000  ? 133 PRO C CB  1 
ATOM   8035  C  CG  . PRO C  1 102 ? 12.18800  -4.15300  -17.27500 1.000 70.78000  ? 133 PRO C CG  1 
ATOM   8036  C  CD  . PRO C  1 102 ? 12.78900  -3.00200  -18.03900 1.000 68.48000  ? 133 PRO C CD  1 
ATOM   8037  N  N   . VAL C  1 103 ? 15.50700  -3.15700  -14.06900 1.000 72.36000  ? 134 VAL C N   1 
ATOM   8038  C  CA  . VAL C  1 103 ? 16.84200  -3.27100  -13.49200 1.000 65.75000  ? 134 VAL C CA  1 
ATOM   8039  C  C   . VAL C  1 103 ? 17.23600  -4.71200  -13.18400 1.000 70.07000  ? 134 VAL C C   1 
ATOM   8040  O  O   . VAL C  1 103 ? 18.43000  -4.98600  -13.00300 1.000 73.62000  ? 134 VAL C O   1 
ATOM   8041  C  CB  . VAL C  1 103 ? 16.97300  -2.36000  -12.25700 1.000 75.62000  ? 134 VAL C CB  1 
ATOM   8042  C  CG1 . VAL C  1 103 ? 16.03900  -1.15700  -12.38600 1.000 76.21000  ? 134 VAL C CG1 1 
ATOM   8043  C  CG2 . VAL C  1 103 ? 16.72600  -3.12300  -10.95800 1.000 66.55000  ? 134 VAL C CG2 1 
ATOM   8044  N  N   . GLU C  1 104 ? 16.28200  -5.64500  -13.10600 1.000 68.48000  ? 135 GLU C N   1 
ATOM   8045  C  CA  . GLU C  1 104 ? 16.66900  -7.04400  -12.93300 1.000 72.79000  ? 135 GLU C CA  1 
ATOM   8046  C  C   . GLU C  1 104 ? 17.29700  -7.62600  -14.19700 1.000 77.15000  ? 135 GLU C C   1 
ATOM   8047  O  O   . GLU C  1 104 ? 17.98500  -8.65000  -14.12100 1.000 80.46000  ? 135 GLU C O   1 
ATOM   8048  C  CB  . GLU C  1 104 ? 15.46800  -7.89400  -12.52300 1.000 70.58000  ? 135 GLU C CB  1 
ATOM   8049  N  N   . GLU C  1 105 ? 17.05600  -7.00700  -15.35200 1.000 73.61000  ? 136 GLU C N   1 
ATOM   8050  C  CA  . GLU C  1 105 ? 17.58600  -7.45300  -16.64000 1.000 72.36000  ? 136 GLU C CA  1 
ATOM   8051  C  C   . GLU C  1 105 ? 19.01600  -6.92900  -16.78200 1.000 72.13000  ? 136 GLU C C   1 
ATOM   8052  O  O   . GLU C  1 105 ? 19.23000  -5.75100  -17.07300 1.000 76.31000  ? 136 GLU C O   1 
ATOM   8053  C  CB  . GLU C  1 105 ? 16.68900  -6.95000  -17.76800 1.000 71.65000  ? 136 GLU C CB  1 
ATOM   8054  C  CG  . GLU C  1 105 ? 16.72500  -7.76200  -19.06600 1.000 75.47000  ? 136 GLU C CG  1 
ATOM   8055  C  CD  . GLU C  1 105 ? 16.26500  -9.20900  -18.87800 1.000 73.29000  ? 136 GLU C CD  1 
ATOM   8056  O  OE1 . GLU C  1 105 ? 15.04900  -9.42100  -18.66000 1.000 77.17000  ? 136 GLU C OE1 1 
ATOM   8057  O  OE2 . GLU C  1 105 ? 17.10800  -10.13000 -18.95700 1.000 69.75000  ? 136 GLU C OE2 1 
ATOM   8058  N  N   . THR C  1 106 ? 20.00500  -7.79600  -16.56700 1.000 71.66000  ? 137 THR C N   1 
ATOM   8059  C  CA  . THR C  1 106 ? 21.39900  -7.36200  -16.49600 1.000 73.78000  ? 137 THR C CA  1 
ATOM   8060  C  C   . THR C  1 106 ? 21.96100  -6.96600  -17.86500 1.000 71.42000  ? 137 THR C C   1 
ATOM   8061  O  O   . THR C  1 106 ? 21.91100  -7.74500  -18.82000 1.000 69.41000  ? 137 THR C O   1 
ATOM   8062  C  CB  . THR C  1 106 ? 22.25500  -8.47400  -15.89300 1.000 72.60000  ? 137 THR C CB  1 
ATOM   8063  O  OG1 . THR C  1 106 ? 21.63000  -8.97200  -14.70300 1.000 75.58000  ? 137 THR C OG1 1 
ATOM   8064  C  CG2 . THR C  1 106 ? 23.63000  -7.95400  -15.55800 1.000 70.52000  ? 137 THR C CG2 1 
ATOM   8065  N  N   . TYR C  1 107 ? 22.52300  -5.75800  -17.94400 1.000 68.64000  ? 138 TYR C N   1 
ATOM   8066  C  CA  . TYR C  1 107 ? 23.17400  -5.28200  -19.15700 1.000 65.22000  ? 138 TYR C CA  1 
ATOM   8067  C  C   . TYR C  1 107 ? 24.52000  -5.96400  -19.36600 1.000 69.98000  ? 138 TYR C C   1 
ATOM   8068  O  O   . TYR C  1 107 ? 25.19800  -6.35500  -18.41500 1.000 70.52000  ? 138 TYR C O   1 
ATOM   8069  C  CB  . TYR C  1 107 ? 23.42400  -3.77800  -19.10000 1.000 63.64000  ? 138 TYR C CB  1 
ATOM   8070  C  CG  . TYR C  1 107 ? 22.21400  -2.89300  -19.20900 1.000 64.00000  ? 138 TYR C CG  1 
ATOM   8071  C  CD1 . TYR C  1 107 ? 20.93100  -3.41100  -19.20000 1.000 66.28000  ? 138 TYR C CD1 1 
ATOM   8072  C  CD2 . TYR C  1 107 ? 22.36400  -1.52900  -19.38500 1.000 65.18000  ? 138 TYR C CD2 1 
ATOM   8073  C  CE1 . TYR C  1 107 ? 19.83200  -2.57800  -19.31800 1.000 65.73000  ? 138 TYR C CE1 1 
ATOM   8074  C  CE2 . TYR C  1 107 ? 21.27900  -0.69800  -19.51500 1.000 62.74000  ? 138 TYR C CE2 1 
ATOM   8075  C  CZ  . TYR C  1 107 ? 20.01800  -1.22300  -19.47800 1.000 60.73000  ? 138 TYR C CZ  1 
ATOM   8076  O  OH  . TYR C  1 107 ? 18.94200  -0.38000  -19.61100 1.000 65.27000  ? 138 TYR C OH  1 
ATOM   8077  N  N   . MET C  1 108 ? 24.93600  -6.05800  -20.63100 1.000 68.88000  ? 139 MET C N   1 
ATOM   8078  C  CA  . MET C  1 108 ? 26.25500  -6.61500  -20.90700 1.000 67.89000  ? 139 MET C CA  1 
ATOM   8079  C  C   . MET C  1 108 ? 27.38300  -5.74300  -20.36100 1.000 68.71000  ? 139 MET C C   1 
ATOM   8080  O  O   . MET C  1 108 ? 28.50800  -6.23600  -20.19500 1.000 68.97000  ? 139 MET C O   1 
ATOM   8081  C  CB  . MET C  1 108 ? 26.44300  -6.83100  -22.40900 1.000 66.54000  ? 139 MET C CB  1 
ATOM   8082  C  CG  . MET C  1 108 ? 26.36900  -5.57600  -23.25500 1.000 66.15000  ? 139 MET C CG  1 
ATOM   8083  S  SD  . MET C  1 108 ? 26.78100  -5.90800  -24.98900 1.000 67.14000  ? 139 MET C SD  1 
ATOM   8084  C  CE  . MET C  1 108 ? 26.19300  -4.42000  -25.77200 1.000 66.69000  ? 139 MET C CE  1 
ATOM   8085  N  N   . SER C  1 109 ? 27.12800  -4.45400  -20.11500 1.000 64.58000  ? 140 SER C N   1 
ATOM   8086  C  CA  . SER C  1 109 ? 28.14900  -3.61700  -19.49100 1.000 69.00000  ? 140 SER C CA  1 
ATOM   8087  C  C   . SER C  1 109 ? 28.41000  -4.04700  -18.05000 1.000 68.27000  ? 140 SER C C   1 
ATOM   8088  O  O   . SER C  1 109 ? 29.56700  -4.14700  -17.63000 1.000 66.89000  ? 140 SER C O   1 
ATOM   8089  C  CB  . SER C  1 109 ? 27.73800  -2.15000  -19.56700 1.000 68.37000  ? 140 SER C CB  1 
ATOM   8090  O  OG  . SER C  1 109 ? 26.36600  -2.00400  -19.24900 1.000 75.46000  ? 140 SER C OG  1 
ATOM   8091  N  N   . LYS C  1 110 ? 27.34900  -4.33700  -17.28600 1.000 67.99000  ? 141 LYS C N   1 
ATOM   8092  C  CA  . LYS C  1 110 ? 27.53800  -4.82700  -15.92300 1.000 67.59000  ? 141 LYS C CA  1 
ATOM   8093  C  C   . LYS C  1 110 ? 28.28200  -6.15900  -15.92200 1.000 73.01000  ? 141 LYS C C   1 
ATOM   8094  O  O   . LYS C  1 110 ? 29.17800  -6.37600  -15.09800 1.000 76.52000  ? 141 LYS C O   1 
ATOM   8095  C  CB  . LYS C  1 110 ? 26.18900  -4.95900  -15.21000 1.000 59.48000  ? 141 LYS C CB  1 
ATOM   8096  N  N   . VAL C  1 111 ? 27.91700  -7.07100  -16.82800 1.000 73.22000  ? 142 VAL C N   1 
ATOM   8097  C  CA  . VAL C  1 111 ? 28.64000  -8.33900  -16.93900 1.000 68.31000  ? 142 VAL C CA  1 
ATOM   8098  C  C   . VAL C  1 111 ? 30.10500  -8.08400  -17.26000 1.000 71.66000  ? 142 VAL C C   1 
ATOM   8099  O  O   . VAL C  1 111 ? 31.01100  -8.66000  -16.64500 1.000 73.71000  ? 142 VAL C O   1 
ATOM   8100  C  CB  . VAL C  1 111 ? 27.98400  -9.24000  -17.99700 1.000 65.37000  ? 142 VAL C CB  1 
ATOM   8101  C  CG1 . VAL C  1 111 ? 28.81000  -10.50200 -18.17600 1.000 63.19000  ? 142 VAL C CG1 1 
ATOM   8102  C  CG2 . VAL C  1 111 ? 26.54800  -9.54900  -17.60200 1.000 56.92000  ? 142 VAL C CG2 1 
ATOM   8103  N  N   . LEU C  1 112 ? 30.35600  -7.20300  -18.22400 1.000 68.33000  ? 143 LEU C N   1 
ATOM   8104  C  CA  . LEU C  1 112 ? 31.72600  -6.88800  -18.59000 1.000 68.26000  ? 143 LEU C CA  1 
ATOM   8105  C  C   . LEU C  1 112 ? 32.44900  -6.16600  -17.46400 1.000 70.57000  ? 143 LEU C C   1 
ATOM   8106  O  O   . LEU C  1 112 ? 33.65900  -6.35800  -17.27700 1.000 67.16000  ? 143 LEU C O   1 
ATOM   8107  C  CB  . LEU C  1 112 ? 31.72400  -6.03400  -19.84600 1.000 65.71000  ? 143 LEU C CB  1 
ATOM   8108  C  CG  . LEU C  1 112 ? 31.61400  -6.82900  -21.12800 1.000 70.75000  ? 143 LEU C CG  1 
ATOM   8109  C  CD1 . LEU C  1 112 ? 31.10400  -5.92100  -22.21800 1.000 72.64000  ? 143 LEU C CD1 1 
ATOM   8110  C  CD2 . LEU C  1 112 ? 32.97300  -7.34700  -21.47900 1.000 70.55000  ? 143 LEU C CD2 1 
ATOM   8111  N  N   . GLN C  1 113 ? 31.73100  -5.32300  -16.71500 1.000 68.88000  ? 144 GLN C N   1 
ATOM   8112  C  CA  . GLN C  1 113 ? 32.34300  -4.63600  -15.58300 1.000 70.88000  ? 144 GLN C CA  1 
ATOM   8113  C  C   . GLN C  1 113 ? 32.79300  -5.63800  -14.52900 1.000 72.83000  ? 144 GLN C C   1 
ATOM   8114  O  O   . GLN C  1 113 ? 33.95600  -5.63700  -14.10500 1.000 73.82000  ? 144 GLN C O   1 
ATOM   8115  C  CB  . GLN C  1 113 ? 31.35900  -3.61800  -15.00700 1.000 67.94000  ? 144 GLN C CB  1 
ATOM   8116  C  CG  . GLN C  1 113 ? 31.88300  -2.82900  -13.84000 1.000 70.12000  ? 144 GLN C CG  1 
ATOM   8117  C  CD  . GLN C  1 113 ? 30.88200  -1.81000  -13.32900 1.000 72.69000  ? 144 GLN C CD  1 
ATOM   8118  O  OE1 . GLN C  1 113 ? 29.77900  -2.15500  -12.89300 1.000 66.85000  ? 144 GLN C OE1 1 
ATOM   8119  N  NE2 . GLN C  1 113 ? 31.27000  -0.53800  -13.37100 1.000 75.64000  ? 144 GLN C NE2 1 
ATOM   8120  N  N   . ASN C  1 114 ? 31.89500  -6.54300  -14.13600 1.000 72.12000  ? 145 ASN C N   1 
ATOM   8121  C  CA  . ASN C  1 114 ? 32.23300  -7.60000  -13.18900 1.000 74.98000  ? 145 ASN C CA  1 
ATOM   8122  C  C   . ASN C  1 114 ? 33.28500  -8.57100  -13.72000 1.000 71.33000  ? 145 ASN C C   1 
ATOM   8123  O  O   . ASN C  1 114 ? 33.71400  -9.45400  -12.96800 1.000 71.42000  ? 145 ASN C O   1 
ATOM   8124  C  CB  . ASN C  1 114 ? 30.97000  -8.35500  -12.77000 1.000 69.42000  ? 145 ASN C CB  1 
ATOM   8125  C  CG  . ASN C  1 114 ? 30.06600  -7.51200  -11.89100 1.000 74.98000  ? 145 ASN C CG  1 
ATOM   8126  O  OD1 . ASN C  1 114 ? 30.50500  -6.51200  -11.32100 1.000 79.55000  ? 145 ASN C OD1 1 
ATOM   8127  N  ND2 . ASN C  1 114 ? 28.80300  -7.90600  -11.77600 1.000 71.60000  ? 145 ASN C ND2 1 
ATOM   8128  N  N   . ALA C  1 115 ? 33.67300  -8.47500  -14.99200 1.000 68.74000  ? 146 ALA C N   1 
ATOM   8129  C  CA  . ALA C  1 115 ? 34.73200  -9.31300  -15.53900 1.000 70.10000  ? 146 ALA C CA  1 
ATOM   8130  C  C   . ALA C  1 115 ? 36.05800  -8.57300  -15.65200 1.000 68.12000  ? 146 ALA C C   1 
ATOM   8131  O  O   . ALA C  1 115 ? 36.99500  -9.08000  -16.28000 1.000 64.18000  ? 146 ALA C O   1 
ATOM   8132  C  CB  . ALA C  1 115 ? 34.31800  -9.86900  -16.90300 1.000 72.98000  ? 146 ALA C CB  1 
ATOM   8133  N  N   . GLY C  1 116 ? 36.17400  -7.41300  -15.01900 1.000 70.88000  ? 147 GLY C N   1 
ATOM   8134  C  CA  . GLY C  1 116 ? 37.42700  -6.69600  -14.97900 1.000 69.13000  ? 147 GLY C CA  1 
ATOM   8135  C  C   . GLY C  1 116 ? 37.62500  -5.70600  -16.09800 1.000 67.97000  ? 147 GLY C C   1 
ATOM   8136  O  O   . GLY C  1 116 ? 38.75000  -5.23400  -16.29200 1.000 66.70000  ? 147 GLY C O   1 
ATOM   8137  N  N   . TYR C  1 117 ? 36.57600  -5.38500  -16.84500 1.000 66.51000  ? 148 TYR C N   1 
ATOM   8138  C  CA  . TYR C  1 117 ? 36.65600  -4.40200  -17.91200 1.000 65.36000  ? 148 TYR C CA  1 
ATOM   8139  C  C   . TYR C  1 117 ? 36.41300  -2.99600  -17.37000 1.000 64.69000  ? 148 TYR C C   1 
ATOM   8140  O  O   . TYR C  1 117 ? 35.57800  -2.79300  -16.48400 1.000 66.74000  ? 148 TYR C O   1 
ATOM   8141  C  CB  . TYR C  1 117 ? 35.62900  -4.71300  -19.00200 1.000 64.88000  ? 148 TYR C CB  1 
ATOM   8142  C  CG  . TYR C  1 117 ? 36.13600  -5.60700  -20.10700 1.000 66.14000  ? 148 TYR C CG  1 
ATOM   8143  C  CD1 . TYR C  1 117 ? 36.36400  -6.95800  -19.88800 1.000 66.31000  ? 148 TYR C CD1 1 
ATOM   8144  C  CD2 . TYR C  1 117 ? 36.39900  -5.09400  -21.37500 1.000 67.23000  ? 148 TYR C CD2 1 
ATOM   8145  C  CE1 . TYR C  1 117 ? 36.83400  -7.77900  -20.90400 1.000 68.77000  ? 148 TYR C CE1 1 
ATOM   8146  C  CE2 . TYR C  1 117 ? 36.87200  -5.90700  -22.39400 1.000 69.55000  ? 148 TYR C CE2 1 
ATOM   8147  C  CZ  . TYR C  1 117 ? 37.08600  -7.24800  -22.15000 1.000 70.60000  ? 148 TYR C CZ  1 
ATOM   8148  O  OH  . TYR C  1 117 ? 37.55200  -8.06200  -23.15600 1.000 65.34000  ? 148 TYR C OH  1 
ATOM   8149  N  N   . TYR C  1 118 ? 37.14900  -2.02500  -17.90700 1.000 61.99000  ? 149 TYR C N   1 
ATOM   8150  C  CA  . TYR C  1 118 ? 36.81400  -0.61800  -17.71300 1.000 69.71000  ? 149 TYR C CA  1 
ATOM   8151  C  C   . TYR C  1 118 ? 35.71600  -0.22100  -18.70100 1.000 62.15000  ? 149 TYR C C   1 
ATOM   8152  O  O   . TYR C  1 118 ? 35.93000  -0.24900  -19.91500 1.000 56.63000  ? 149 TYR C O   1 
ATOM   8153  C  CB  . TYR C  1 118 ? 38.06200  0.24900   -17.87700 1.000 67.73000  ? 149 TYR C CB  1 
ATOM   8154  C  CG  . TYR C  1 118 ? 37.77300  1.73000   -17.89000 1.000 67.12000  ? 149 TYR C CG  1 
ATOM   8155  C  CD1 . TYR C  1 118 ? 37.46200  2.42100   -16.72200 1.000 66.42000  ? 149 TYR C CD1 1 
ATOM   8156  C  CD2 . TYR C  1 118 ? 37.81800  2.43800   -19.07900 1.000 70.55000  ? 149 TYR C CD2 1 
ATOM   8157  C  CE1 . TYR C  1 118 ? 37.18900  3.79300   -16.75000 1.000 66.30000  ? 149 TYR C CE1 1 
ATOM   8158  C  CE2 . TYR C  1 118 ? 37.55100  3.79300   -19.12100 1.000 72.82000  ? 149 TYR C CE2 1 
ATOM   8159  C  CZ  . TYR C  1 118 ? 37.23600  4.46600   -17.96100 1.000 68.01000  ? 149 TYR C CZ  1 
ATOM   8160  O  OH  . TYR C  1 118 ? 36.97800  5.80900   -18.04200 1.000 66.15000  ? 149 TYR C OH  1 
ATOM   8161  N  N   . THR C  1 119 ? 34.55400  0.16400   -18.18300 1.000 60.75000  ? 150 THR C N   1 
ATOM   8162  C  CA  . THR C  1 119 ? 33.35900  0.37400   -18.99000 1.000 63.04000  ? 150 THR C CA  1 
ATOM   8163  C  C   . THR C  1 119 ? 33.02200  1.85600   -19.10000 1.000 66.14000  ? 150 THR C C   1 
ATOM   8164  O  O   . THR C  1 119 ? 33.12200  2.60400   -18.12400 1.000 70.97000  ? 150 THR C O   1 
ATOM   8165  C  CB  . THR C  1 119 ? 32.17000  -0.38100  -18.40100 1.000 65.58000  ? 150 THR C CB  1 
ATOM   8166  O  OG1 . THR C  1 119 ? 31.92700  0.07800   -17.06700 1.000 65.53000  ? 150 THR C OG1 1 
ATOM   8167  C  CG2 . THR C  1 119 ? 32.46500  -1.87300  -18.37400 1.000 65.80000  ? 150 THR C CG2 1 
ATOM   8168  N  N   . SER C  1 120 ? 32.59400  2.26400   -20.29100 1.000 66.03000  ? 151 SER C N   1 
ATOM   8169  C  CA  . SER C  1 120 ? 32.36100  3.66600   -20.61000 1.000 64.98000  ? 151 SER C CA  1 
ATOM   8170  C  C   . SER C  1 120 ? 31.20700  3.79900   -21.59800 1.000 61.94000  ? 151 SER C C   1 
ATOM   8171  O  O   . SER C  1 120 ? 31.18800  3.12500   -22.63300 1.000 64.03000  ? 151 SER C O   1 
ATOM   8172  C  CB  . SER C  1 120 ? 33.63400  4.27700   -21.19800 1.000 65.90000  ? 151 SER C CB  1 
ATOM   8173  O  OG  . SER C  1 120 ? 33.33800  5.37200   -22.04100 1.000 69.71000  ? 151 SER C OG  1 
ATOM   8174  N  N   . ALA C  1 121 ? 30.27100  4.69300   -21.29200 1.000 61.48000  ? 152 ALA C N   1 
ATOM   8175  C  CA  . ALA C  1 121 ? 29.15900  5.02100   -22.17900 1.000 62.00000  ? 152 ALA C CA  1 
ATOM   8176  C  C   . ALA C  1 121 ? 29.22700  6.49400   -22.53400 1.000 56.69000  ? 152 ALA C C   1 
ATOM   8177  O  O   . ALA C  1 121 ? 29.39500  7.34200   -21.65300 1.000 58.83000  ? 152 ALA C O   1 
ATOM   8178  C  CB  . ALA C  1 121 ? 27.80400  4.71000   -21.53800 1.000 61.66000  ? 152 ALA C CB  1 
ATOM   8179  N  N   . ILE C  1 122 ? 29.07900  6.79400   -23.81800 1.000 55.00000  ? 153 ILE C N   1 
ATOM   8180  C  CA  . ILE C  1 122 ? 29.19100  8.15200   -24.32700 1.000 57.60000  ? 153 ILE C CA  1 
ATOM   8181  C  C   . ILE C  1 122 ? 28.00500  8.43600   -25.24200 1.000 60.37000  ? 153 ILE C C   1 
ATOM   8182  O  O   . ILE C  1 122 ? 27.54900  7.55400   -25.97800 1.000 57.27000  ? 153 ILE C O   1 
ATOM   8183  C  CB  . ILE C  1 122 ? 30.52400  8.37600   -25.06600 1.000 55.24000  ? 153 ILE C CB  1 
ATOM   8184  C  CG1 . ILE C  1 122 ? 31.69500  8.10800   -24.12100 1.000 63.43000  ? 153 ILE C CG1 1 
ATOM   8185  C  CG2 . ILE C  1 122 ? 30.60800  9.79100   -25.61500 1.000 54.05000  ? 153 ILE C CG2 1 
ATOM   8186  C  CD1 . ILE C  1 122 ? 33.02200  7.91500   -24.83400 1.000 56.30000  ? 153 ILE C CD1 1 
ATOM   8187  N  N   . GLY C  1 123 ? 27.46400  9.64800   -25.13900 1.000 63.09000  ? 154 GLY C N   1 
ATOM   8188  C  CA  . GLY C  1 123 ? 26.43200  10.09900  -26.05900 1.000 60.26000  ? 154 GLY C CA  1 
ATOM   8189  C  C   . GLY C  1 123 ? 25.04700  9.78600   -25.53100 1.000 62.82000  ? 154 GLY C C   1 
ATOM   8190  O  O   . GLY C  1 123 ? 24.75900  10.00500  -24.35100 1.000 62.63000  ? 154 GLY C O   1 
ATOM   8191  N  N   . LYS C  1 124 ? 24.21300  9.21400   -26.39300 1.000 59.60000  ? 155 LYS C N   1 
ATOM   8192  C  CA  . LYS C  1 124 ? 22.79300  9.04900   -26.12300 1.000 57.76000  ? 155 LYS C CA  1 
ATOM   8193  C  C   . LYS C  1 124 ? 22.54100  7.86200   -25.20000 1.000 59.84000  ? 155 LYS C C   1 
ATOM   8194  O  O   . LYS C  1 124 ? 23.20600  6.83000   -25.29900 1.000 62.73000  ? 155 LYS C O   1 
ATOM   8195  C  CB  . LYS C  1 124 ? 22.05800  8.85700   -27.45400 1.000 65.20000  ? 155 LYS C CB  1 
ATOM   8196  C  CG  . LYS C  1 124 ? 20.65400  8.25600   -27.36900 1.000 69.63000  ? 155 LYS C CG  1 
ATOM   8197  C  CD  . LYS C  1 124 ? 19.98000  8.24700   -28.74200 1.000 57.75000  ? 155 LYS C CD  1 
ATOM   8198  C  CE  . LYS C  1 124 ? 18.60800  7.58300   -28.69600 1.000 58.07000  ? 155 LYS C CE  1 
ATOM   8199  N  NZ  . LYS C  1 124 ? 17.88600  7.76900   -29.99200 1.000 67.35000  ? 155 LYS C NZ  1 
ATOM   8200  N  N   . TRP C  1 125 ? 21.57100  8.02300   -24.29100 1.000 63.22000  ? 156 TRP C N   1 
ATOM   8201  C  CA  . TRP C  1 125 ? 21.16400  6.94200   -23.40200 1.000 60.63000  ? 156 TRP C CA  1 
ATOM   8202  C  C   . TRP C  1 125 ? 19.77800  6.45300   -23.78000 1.000 65.28000  ? 156 TRP C C   1 
ATOM   8203  O  O   . TRP C  1 125 ? 19.66700  5.44500   -24.51400 1.000 65.92000  ? 156 TRP C O   1 
ATOM   8204  C  CB  . TRP C  1 125 ? 21.20400  7.41900   -21.94500 1.000 60.08000  ? 156 TRP C CB  1 
ATOM   8205  C  CG  . TRP C  1 125 ? 20.90400  6.33100   -20.98100 1.000 64.51000  ? 156 TRP C CG  1 
ATOM   8206  C  CD1 . TRP C  1 125 ? 19.85500  6.28000   -20.10900 1.000 64.40000  ? 156 TRP C CD1 1 
ATOM   8207  C  CD2 . TRP C  1 125 ? 21.65800  5.12800   -20.77900 1.000 62.59000  ? 156 TRP C CD2 1 
ATOM   8208  N  NE1 . TRP C  1 125 ? 19.91100  5.12000   -19.37600 1.000 66.85000  ? 156 TRP C NE1 1 
ATOM   8209  C  CE2 . TRP C  1 125 ? 21.01000  4.39700   -19.76800 1.000 65.21000  ? 156 TRP C CE2 1 
ATOM   8210  C  CE3 . TRP C  1 125 ? 22.81900  4.60300   -21.35200 1.000 57.03000  ? 156 TRP C CE3 1 
ATOM   8211  C  CZ2 . TRP C  1 125 ? 21.48500  3.16800   -19.31600 1.000 61.94000  ? 156 TRP C CZ2 1 
ATOM   8212  C  CZ3 . TRP C  1 125 ? 23.28700  3.38800   -20.90700 1.000 57.21000  ? 156 TRP C CZ3 1 
ATOM   8213  C  CH2 . TRP C  1 125 ? 22.62100  2.68100   -19.89900 1.000 62.99000  ? 156 TRP C CH2 1 
ATOM   8214  N  N   . HIS C  1 126 ? 18.70000  7.07700   -23.31000 1.000 65.51000  ? 157 HIS C N   1 
ATOM   8215  C  CA  . HIS C  1 126 ? 17.30100  6.76800   -23.61300 1.000 62.09000  ? 157 HIS C CA  1 
ATOM   8216  C  C   . HIS C  1 126 ? 16.84400  5.43400   -23.03800 1.000 63.86000  ? 157 HIS C C   1 
ATOM   8217  O  O   . HIS C  1 126 ? 15.88500  4.84300   -23.53300 1.000 63.57000  ? 157 HIS C O   1 
ATOM   8218  C  CB  . HIS C  1 126 ? 16.99400  6.79700   -25.11000 1.000 60.35000  ? 157 HIS C CB  1 
ATOM   8219  C  CG  . HIS C  1 126 ? 15.55700  7.08900   -25.40700 1.000 65.35000  ? 157 HIS C CG  1 
ATOM   8220  N  ND1 . HIS C  1 126 ? 14.99800  6.91700   -26.65600 1.000 69.81000  ? 157 HIS C ND1 1 
ATOM   8221  C  CD2 . HIS C  1 126 ? 14.56200  7.54700   -24.60900 1.000 62.47000  ? 157 HIS C CD2 1 
ATOM   8222  C  CE1 . HIS C  1 126 ? 13.72000  7.25300   -26.61300 1.000 66.97000  ? 157 HIS C CE1 1 
ATOM   8223  N  NE2 . HIS C  1 126 ? 13.43100  7.64000   -25.38200 1.000 71.84000  ? 157 HIS C NE2 1 
ATOM   8224  N  N   . LEU C  1 127 ? 17.49200  4.95000   -21.98400 1.000 66.80000  ? 158 LEU C N   1 
ATOM   8225  C  CA  . LEU C  1 127 ? 17.09600  3.71100   -21.33400 1.000 63.83000  ? 158 LEU C CA  1 
ATOM   8226  C  C   . LEU C  1 127 ? 16.52900  3.95000   -19.94200 1.000 65.52000  ? 158 LEU C C   1 
ATOM   8227  O  O   . LEU C  1 127 ? 16.42200  3.00900   -19.14900 1.000 70.11000  ? 158 LEU C O   1 
ATOM   8228  C  CB  . LEU C  1 127 ? 18.28600  2.76200   -21.25900 1.000 62.36000  ? 158 LEU C CB  1 
ATOM   8229  C  CG  . LEU C  1 127 ? 18.93200  2.48800   -22.60800 1.000 62.77000  ? 158 LEU C CG  1 
ATOM   8230  C  CD1 . LEU C  1 127 ? 20.18500  1.70200   -22.36700 1.000 59.64000  ? 158 LEU C CD1 1 
ATOM   8231  C  CD2 . LEU C  1 127 ? 17.96900  1.71200   -23.51400 1.000 58.52000  ? 158 LEU C CD2 1 
ATOM   8232  N  N   . GLY C  1 128 ? 16.14800  5.18400   -19.63700 1.000 63.14000  ? 159 GLY C N   1 
ATOM   8233  C  CA  . GLY C  1 128 ? 15.55600  5.50300   -18.35100 1.000 72.86000  ? 159 GLY C CA  1 
ATOM   8234  C  C   . GLY C  1 128 ? 16.25100  6.67900   -17.69800 1.000 74.67000  ? 159 GLY C C   1 
ATOM   8235  O  O   . GLY C  1 128 ? 17.47000  6.64400   -17.49500 1.000 73.36000  ? 159 GLY C O   1 
ATOM   8236  N  N   . ALA C  1 129 ? 15.48300  7.70300   -17.32200 1.000 79.63000  ? 160 ALA C N   1 
ATOM   8237  C  CA  . ALA C  1 129 ? 16.03800  8.94200   -16.79300 1.000 80.25000  ? 160 ALA C CA  1 
ATOM   8238  C  C   . ALA C  1 129 ? 15.99700  9.01100   -15.27200 1.000 74.72000  ? 160 ALA C C   1 
ATOM   8239  O  O   . ALA C  1 129 ? 16.51600  9.96600   -14.69700 1.000 77.06000  ? 160 ALA C O   1 
ATOM   8240  C  CB  . ALA C  1 129 ? 15.29700  10.14400  -17.39200 1.000 67.46000  ? 160 ALA C CB  1 
ATOM   8241  N  N   . ALA C  1 130 ? 15.42200  8.02500   -14.61900 1.000 76.06000  ? 161 ALA C N   1 
ATOM   8242  C  CA  . ALA C  1 130 ? 15.44700  7.96800   -13.17100 1.000 75.20000  ? 161 ALA C CA  1 
ATOM   8243  C  C   . ALA C  1 130 ? 16.74300  7.29500   -12.70700 1.000 78.16000  ? 161 ALA C C   1 
ATOM   8244  O  O   . ALA C  1 130 ? 17.32100  6.47900   -13.43500 1.000 74.78000  ? 161 ALA C O   1 
ATOM   8245  C  CB  . ALA C  1 130 ? 14.23100  7.20500   -12.65200 1.000 75.05000  ? 161 ALA C CB  1 
ATOM   8246  N  N   . PRO C  1 131 ? 17.21600  7.62100   -11.49800 1.000 74.75000  ? 162 PRO C N   1 
ATOM   8247  C  CA  . PRO C  1 131 ? 18.56600  7.17800   -11.09300 1.000 74.19000  ? 162 PRO C CA  1 
ATOM   8248  C  C   . PRO C  1 131 ? 18.79900  5.68100   -11.16000 1.000 77.00000  ? 162 PRO C C   1 
ATOM   8249  O  O   . PRO C  1 131 ? 19.89600  5.25900   -11.54300 1.000 77.96000  ? 162 PRO C O   1 
ATOM   8250  C  CB  . PRO C  1 131 ? 18.68300  7.70500   -9.65800  1.000 71.37000  ? 162 PRO C CB  1 
ATOM   8251  C  CG  . PRO C  1 131 ? 17.83800  8.92600   -9.66000  1.000 73.11000  ? 162 PRO C CG  1 
ATOM   8252  C  CD  . PRO C  1 131 ? 16.66500  8.61900   -10.56700 1.000 72.35000  ? 162 PRO C CD  1 
ATOM   8253  N  N   . LYS C  1 132 ? 17.80500  4.85800   -10.82000 1.000 76.08000  ? 163 LYS C N   1 
ATOM   8254  C  CA  . LYS C  1 132 ? 18.02300  3.41700   -10.85800 1.000 71.71000  ? 163 LYS C CA  1 
ATOM   8255  C  C   . LYS C  1 132 ? 18.33100  2.92500   -12.26700 1.000 74.06000  ? 163 LYS C C   1 
ATOM   8256  O  O   . LYS C  1 132 ? 18.84200  1.81100   -12.42100 1.000 70.40000  ? 163 LYS C O   1 
ATOM   8257  C  CB  . LYS C  1 132 ? 16.80100  2.70100   -10.27100 1.000 72.91000  ? 163 LYS C CB  1 
ATOM   8258  C  CG  . LYS C  1 132 ? 15.50700  2.90700   -11.05200 1.000 75.22000  ? 163 LYS C CG  1 
ATOM   8259  C  CD  . LYS C  1 132 ? 14.27400  2.44300   -10.25600 1.000 79.60000  ? 163 LYS C CD  1 
ATOM   8260  C  CE  . LYS C  1 132 ? 14.04400  0.93800   -10.27000 1.000 67.50000  ? 163 LYS C CE  1 
ATOM   8261  N  NZ  . LYS C  1 132 ? 12.66400  0.61800   -9.81700  1.000 77.27000  ? 163 LYS C NZ  1 
ATOM   8262  N  N   . PHE C  1 133 ? 18.05600  3.73900   -13.28800 1.000 68.57000  ? 164 PHE C N   1 
ATOM   8263  C  CA  . PHE C  1 133 ? 18.35500  3.41000   -14.67500 1.000 68.83000  ? 164 PHE C CA  1 
ATOM   8264  C  C   . PHE C  1 133 ? 19.60300  4.11100   -15.19100 1.000 75.77000  ? 164 PHE C C   1 
ATOM   8265  O  O   . PHE C  1 133 ? 19.93700  3.96700   -16.37400 1.000 73.72000  ? 164 PHE C O   1 
ATOM   8266  C  CB  . PHE C  1 133 ? 17.17700  3.79100   -15.56900 1.000 73.42000  ? 164 PHE C CB  1 
ATOM   8267  C  CG  . PHE C  1 133 ? 15.87500  3.23700   -15.09900 1.000 71.08000  ? 164 PHE C CG  1 
ATOM   8268  C  CD1 . PHE C  1 133 ? 15.70600  1.87800   -14.93100 1.000 72.30000  ? 164 PHE C CD1 1 
ATOM   8269  C  CD2 . PHE C  1 133 ? 14.83000  4.08100   -14.80200 1.000 68.67000  ? 164 PHE C CD2 1 
ATOM   8270  C  CE1 . PHE C  1 133 ? 14.51300  1.36800   -14.48000 1.000 72.50000  ? 164 PHE C CE1 1 
ATOM   8271  C  CE2 . PHE C  1 133 ? 13.63300  3.58000   -14.35700 1.000 74.70000  ? 164 PHE C CE2 1 
ATOM   8272  C  CZ  . PHE C  1 133 ? 13.47400  2.21800   -14.19600 1.000 73.57000  ? 164 PHE C CZ  1 
ATOM   8273  N  N   . HIS C  1 134 ? 20.29200  4.86800   -14.34100 1.000 72.82000  ? 165 HIS C N   1 
ATOM   8274  C  CA  . HIS C  1 134 ? 21.41300  5.66800   -14.79900 1.000 70.36000  ? 165 HIS C CA  1 
ATOM   8275  C  C   . HIS C  1 134 ? 22.56300  4.75400   -15.22200 1.000 67.72000  ? 165 HIS C C   1 
ATOM   8276  O  O   . HIS C  1 134 ? 22.73700  3.66600   -14.66400 1.000 62.84000  ? 165 HIS C O   1 
ATOM   8277  C  CB  . HIS C  1 134 ? 21.86900  6.62300   -13.69500 1.000 72.65000  ? 165 HIS C CB  1 
ATOM   8278  C  CG  . HIS C  1 134 ? 22.82400  7.67700   -14.15900 1.000 70.37000  ? 165 HIS C CG  1 
ATOM   8279  N  ND1 . HIS C  1 134 ? 24.17600  7.44400   -14.31100 1.000 68.06000  ? 165 HIS C ND1 1 
ATOM   8280  C  CD2 . HIS C  1 134 ? 22.62100  8.96900   -14.51400 1.000 66.20000  ? 165 HIS C CD2 1 
ATOM   8281  C  CE1 . HIS C  1 134 ? 24.76400  8.54800   -14.74200 1.000 69.70000  ? 165 HIS C CE1 1 
ATOM   8282  N  NE2 . HIS C  1 134 ? 23.84300  9.48800   -14.87300 1.000 71.79000  ? 165 HIS C NE2 1 
ATOM   8283  N  N   . PRO C  1 135 ? 23.34900  5.16700   -16.22000 1.000 63.17000  ? 166 PRO C N   1 
ATOM   8284  C  CA  . PRO C  1 135 ? 24.47100  4.31900   -16.65500 1.000 64.42000  ? 166 PRO C CA  1 
ATOM   8285  C  C   . PRO C  1 135 ? 25.39100  3.88600   -15.52400 1.000 69.47000  ? 166 PRO C C   1 
ATOM   8286  O  O   . PRO C  1 135 ? 25.81500  2.72100   -15.49800 1.000 63.99000  ? 166 PRO C O   1 
ATOM   8287  C  CB  . PRO C  1 135 ? 25.19100  5.20600   -17.68100 1.000 64.19000  ? 166 PRO C CB  1 
ATOM   8288  C  CG  . PRO C  1 135 ? 24.10100  6.06500   -18.26100 1.000 58.18000  ? 166 PRO C CG  1 
ATOM   8289  C  CD  . PRO C  1 135 ? 23.10900  6.29500   -17.14300 1.000 59.66000  ? 166 PRO C CD  1 
ATOM   8290  N  N   . ASN C  1 136 ? 25.65900  4.76500   -14.55200 1.000 69.05000  ? 167 ASN C N   1 
ATOM   8291  C  CA  . ASN C  1 136 ? 26.61900  4.42400   -13.50600 1.000 68.26000  ? 167 ASN C CA  1 
ATOM   8292  C  C   . ASN C  1 136 ? 26.13200  3.27000   -12.64500 1.000 67.82000  ? 167 ASN C C   1 
ATOM   8293  O  O   . ASN C  1 136 ? 26.94800  2.51600   -12.10500 1.000 64.27000  ? 167 ASN C O   1 
ATOM   8294  C  CB  . ASN C  1 136 ? 26.89100  5.63900   -12.61300 1.000 71.27000  ? 167 ASN C CB  1 
ATOM   8295  C  CG  . ASN C  1 136 ? 27.63600  6.74300   -13.33200 1.000 70.25000  ? 167 ASN C CG  1 
ATOM   8296  O  OD1 . ASN C  1 136 ? 27.31900  7.92600   -13.17100 1.000 71.35000  ? 167 ASN C OD1 1 
ATOM   8297  N  ND2 . ASN C  1 136 ? 28.62400  6.36700   -14.14200 1.000 70.60000  ? 167 ASN C ND2 1 
ATOM   8298  N  N   . LYS C  1 137 ? 24.82000  3.07400   -12.55800 1.000 66.18000  ? 168 LYS C N   1 
ATOM   8299  C  CA  . LYS C  1 137 ? 24.25400  1.93800   -11.84300 1.000 71.36000  ? 168 LYS C CA  1 
ATOM   8300  C  C   . LYS C  1 137 ? 24.03800  0.71500   -12.73200 1.000 76.12000  ? 168 LYS C C   1 
ATOM   8301  O  O   . LYS C  1 137 ? 23.65900  -0.34800  -12.22200 1.000 70.27000  ? 168 LYS C O   1 
ATOM   8302  C  CB  . LYS C  1 137 ? 22.92100  2.35100   -11.19700 1.000 71.69000  ? 168 LYS C CB  1 
ATOM   8303  N  N   . ARG C  1 138 ? 24.26700  0.83500   -14.04300 1.000 70.90000  ? 169 ARG C N   1 
ATOM   8304  C  CA  . ARG C  1 138 ? 24.04700  -0.25700  -14.98300 1.000 70.89000  ? 169 ARG C CA  1 
ATOM   8305  C  C   . ARG C  1 138 ? 25.35100  -0.72300  -15.63000 1.000 70.86000  ? 169 ARG C C   1 
ATOM   8306  O  O   . ARG C  1 138 ? 25.36700  -1.13700  -16.79000 1.000 67.07000  ? 169 ARG C O   1 
ATOM   8307  C  CB  . ARG C  1 138 ? 23.01700  0.14800   -16.04100 1.000 68.72000  ? 169 ARG C CB  1 
ATOM   8308  C  CG  . ARG C  1 138 ? 21.74400  0.73700   -15.43800 1.000 70.52000  ? 169 ARG C CG  1 
ATOM   8309  C  CD  . ARG C  1 138 ? 20.48500  0.24600   -16.13000 1.000 72.29000  ? 169 ARG C CD  1 
ATOM   8310  N  NE  . ARG C  1 138 ? 20.29400  -1.19400  -15.99700 1.000 71.40000  ? 169 ARG C NE  1 
ATOM   8311  C  CZ  . ARG C  1 138 ? 19.11000  -1.79100  -16.04500 1.000 71.47000  ? 169 ARG C CZ  1 
ATOM   8312  N  NH1 . ARG C  1 138 ? 18.00300  -1.11200  -16.29800 1.000 65.09000  ? 169 ARG C NH1 1 
ATOM   8313  N  NH2 . ARG C  1 138 ? 19.04000  -3.10900  -15.89100 1.000 73.98000  ? 169 ARG C NH2 1 
ATOM   8314  N  N   . GLY C  1 139 ? 26.46000  -0.63400  -14.90300 1.000 69.32000  ? 170 GLY C N   1 
ATOM   8315  C  CA  . GLY C  1 139 ? 27.69900  -1.24500  -15.33200 1.000 64.03000  ? 170 GLY C CA  1 
ATOM   8316  C  C   . GLY C  1 139 ? 28.70500  -0.33900  -15.99900 1.000 66.21000  ? 170 GLY C C   1 
ATOM   8317  O  O   . GLY C  1 139 ? 29.73100  -0.83500  -16.48100 1.000 67.90000  ? 170 GLY C O   1 
ATOM   8318  N  N   . PHE C  1 140 ? 28.46700  0.96300   -16.04500 1.000 62.36000  ? 171 PHE C N   1 
ATOM   8319  C  CA  . PHE C  1 140 ? 29.37300  1.86700   -16.73500 1.000 61.89000  ? 171 PHE C CA  1 
ATOM   8320  C  C   . PHE C  1 140 ? 30.18100  2.64000   -15.70200 1.000 68.79000  ? 171 PHE C C   1 
ATOM   8321  O  O   . PHE C  1 140 ? 29.61800  3.41200   -14.91800 1.000 66.69000  ? 171 PHE C O   1 
ATOM   8322  C  CB  . PHE C  1 140 ? 28.60000  2.81200   -17.65500 1.000 65.01000  ? 171 PHE C CB  1 
ATOM   8323  C  CG  . PHE C  1 140 ? 28.06800  2.15100   -18.90200 1.000 63.48000  ? 171 PHE C CG  1 
ATOM   8324  C  CD1 . PHE C  1 140 ? 28.91500  1.84900   -19.95700 1.000 64.56000  ? 171 PHE C CD1 1 
ATOM   8325  C  CD2 . PHE C  1 140 ? 26.72300  1.82000   -19.01000 1.000 65.36000  ? 171 PHE C CD2 1 
ATOM   8326  C  CE1 . PHE C  1 140 ? 28.43900  1.24000   -21.10500 1.000 61.63000  ? 171 PHE C CE1 1 
ATOM   8327  C  CE2 . PHE C  1 140 ? 26.23400  1.21700   -20.15700 1.000 71.22000  ? 171 PHE C CE2 1 
ATOM   8328  C  CZ  . PHE C  1 140 ? 27.09600  0.92600   -21.20900 1.000 67.22000  ? 171 PHE C CZ  1 
ATOM   8329  N  N   . ASP C  1 141 ? 31.50100  2.42900   -15.70200 1.000 68.54000  ? 172 ASP C N   1 
ATOM   8330  C  CA  . ASP C  1 141 ? 32.35200  3.23000   -14.83600 1.000 65.11000  ? 172 ASP C CA  1 
ATOM   8331  C  C   . ASP C  1 141 ? 32.18800  4.70700   -15.15100 1.000 70.70000  ? 172 ASP C C   1 
ATOM   8332  O  O   . ASP C  1 141 ? 32.13300  5.53900   -14.23900 1.000 73.52000  ? 172 ASP C O   1 
ATOM   8333  C  CB  . ASP C  1 141 ? 33.82200  2.82700   -14.98400 1.000 66.63000  ? 172 ASP C CB  1 
ATOM   8334  C  CG  . ASP C  1 141 ? 34.08500  1.38500   -14.59600 1.000 69.02000  ? 172 ASP C CG  1 
ATOM   8335  O  OD1 . ASP C  1 141 ? 33.37200  0.86000   -13.71600 1.000 76.52000  ? 172 ASP C OD1 1 
ATOM   8336  O  OD2 . ASP C  1 141 ? 35.04100  0.79100   -15.13300 1.000 66.19000  ? 172 ASP C OD2 1 
ATOM   8337  N  N   . ASP C  1 142 ? 32.08200  5.05100   -16.43600 1.000 65.54000  ? 173 ASP C N   1 
ATOM   8338  C  CA  . ASP C  1 142 ? 32.02200  6.44000   -16.86100 1.000 67.14000  ? 173 ASP C CA  1 
ATOM   8339  C  C   . ASP C  1 142 ? 30.87400  6.66300   -17.83900 1.000 71.40000  ? 173 ASP C C   1 
ATOM   8340  O  O   . ASP C  1 142 ? 30.67300  5.88200   -18.77600 1.000 65.98000  ? 173 ASP C O   1 
ATOM   8341  C  CB  . ASP C  1 142 ? 33.33900  6.86000   -17.50600 1.000 68.32000  ? 173 ASP C CB  1 
ATOM   8342  C  CG  . ASP C  1 142 ? 33.46000  8.35300   -17.63700 1.000 75.16000  ? 173 ASP C CG  1 
ATOM   8343  O  OD1 . ASP C  1 142 ? 33.51000  9.00300   -16.57400 1.000 75.16000  ? 173 ASP C OD1 1 
ATOM   8344  O  OD2 . ASP C  1 142 ? 33.49600  8.87400   -18.77700 1.000 75.25000  ? 173 ASP C OD2 1 
ATOM   8345  N  N   . PHE C  1 143 ? 30.15800  7.76600   -17.65400 1.000 70.26000  ? 174 PHE C N   1 
ATOM   8346  C  CA  . PHE C  1 143 ? 29.11800  8.17000   -18.58900 1.000 69.61000  ? 174 PHE C CA  1 
ATOM   8347  C  C   . PHE C  1 143 ? 29.29600  9.63200   -18.95000 1.000 68.59000  ? 174 PHE C C   1 
ATOM   8348  O  O   . PHE C  1 143 ? 29.44600  10.48500  -18.06900 1.000 71.88000  ? 174 PHE C O   1 
ATOM   8349  C  CB  . PHE C  1 143 ? 27.70800  7.94500   -18.03000 1.000 66.09000  ? 174 PHE C CB  1 
ATOM   8350  C  CG  . PHE C  1 143 ? 26.63300  8.48700   -18.91200 1.000 64.01000  ? 174 PHE C CG  1 
ATOM   8351  C  CD1 . PHE C  1 143 ? 26.60500  8.16800   -20.26200 1.000 66.39000  ? 174 PHE C CD1 1 
ATOM   8352  C  CD2 . PHE C  1 143 ? 25.65100  9.31700   -18.40400 1.000 69.11000  ? 174 PHE C CD2 1 
ATOM   8353  C  CE1 . PHE C  1 143 ? 25.62700  8.67500   -21.09100 1.000 63.14000  ? 174 PHE C CE1 1 
ATOM   8354  C  CE2 . PHE C  1 143 ? 24.66000  9.82700   -19.23200 1.000 68.33000  ? 174 PHE C CE2 1 
ATOM   8355  C  CZ  . PHE C  1 143 ? 24.65100  9.50400   -20.57600 1.000 65.04000  ? 174 PHE C CZ  1 
ATOM   8356  N  N   . TYR C  1 144 ? 29.27800  9.91800   -20.24500 1.000 65.96000  ? 175 TYR C N   1 
ATOM   8357  C  CA  . TYR C  1 144 ? 29.32800  11.29200  -20.72200 1.000 69.85000  ? 175 TYR C CA  1 
ATOM   8358  C  C   . TYR C  1 144 ? 28.29300  11.43300  -21.83300 1.000 68.33000  ? 175 TYR C C   1 
ATOM   8359  O  O   . TYR C  1 144 ? 28.47900  10.91200  -22.93700 1.000 65.47000  ? 175 TYR C O   1 
ATOM   8360  C  CB  . TYR C  1 144 ? 30.73400  11.66100  -21.20000 1.000 65.29000  ? 175 TYR C CB  1 
ATOM   8361  C  CG  . TYR C  1 144 ? 30.87300  13.11300  -21.60000 1.000 71.53000  ? 175 TYR C CG  1 
ATOM   8362  C  CD1 . TYR C  1 144 ? 30.47100  13.55000  -22.85500 1.000 65.35000  ? 175 TYR C CD1 1 
ATOM   8363  C  CD2 . TYR C  1 144 ? 31.37700  14.05500  -20.70500 1.000 70.41000  ? 175 TYR C CD2 1 
ATOM   8364  C  CE1 . TYR C  1 144 ? 30.58600  14.87400  -23.22100 1.000 68.53000  ? 175 TYR C CE1 1 
ATOM   8365  C  CE2 . TYR C  1 144 ? 31.49300  15.38200  -21.06100 1.000 70.98000  ? 175 TYR C CE2 1 
ATOM   8366  C  CZ  . TYR C  1 144 ? 31.09000  15.78500  -22.32400 1.000 74.94000  ? 175 TYR C CZ  1 
ATOM   8367  O  OH  . TYR C  1 144 ? 31.19100  17.10100  -22.70300 1.000 76.52000  ? 175 TYR C OH  1 
ATOM   8368  N  N   . GLY C  1 145 ? 27.19600  12.12200  -21.53700 1.000 65.56000  ? 176 GLY C N   1 
ATOM   8369  C  CA  . GLY C  1 145 ? 26.17500  12.34400  -22.53600 1.000 66.45000  ? 176 GLY C CA  1 
ATOM   8370  C  C   . GLY C  1 145 ? 24.89000  12.86000  -21.93400 1.000 70.48000  ? 176 GLY C C   1 
ATOM   8371  O  O   . GLY C  1 145 ? 24.91900  13.64700  -20.98400 1.000 66.96000  ? 176 GLY C O   1 
ATOM   8372  N  N   . PHE C  1 146 ? 23.75800  12.42600  -22.49100 1.000 66.66000  ? 177 PHE C N   1 
ATOM   8373  C  CA  . PHE C  1 146 ? 22.43100  12.83600  -22.05800 1.000 65.04000  ? 177 PHE C CA  1 
ATOM   8374  C  C   . PHE C  1 146 ? 21.55000  11.60800  -21.88800 1.000 66.49000  ? 177 PHE C C   1 
ATOM   8375  O  O   . PHE C  1 146 ? 21.76800  10.57500  -22.52600 1.000 68.34000  ? 177 PHE C O   1 
ATOM   8376  C  CB  . PHE C  1 146 ? 21.80200  13.82900  -23.05200 1.000 61.28000  ? 177 PHE C CB  1 
ATOM   8377  C  CG  . PHE C  1 146 ? 21.80200  13.36400  -24.49400 1.000 65.74000  ? 177 PHE C CG  1 
ATOM   8378  C  CD1 . PHE C  1 146 ? 22.90300  13.60300  -25.31300 1.000 64.93000  ? 177 PHE C CD1 1 
ATOM   8379  C  CD2 . PHE C  1 146 ? 20.68800  12.73800  -25.04700 1.000 67.96000  ? 177 PHE C CD2 1 
ATOM   8380  C  CE1 . PHE C  1 146 ? 22.90700  13.20100  -26.65000 1.000 62.11000  ? 177 PHE C CE1 1 
ATOM   8381  C  CE2 . PHE C  1 146 ? 20.68300  12.33300  -26.38500 1.000 65.40000  ? 177 PHE C CE2 1 
ATOM   8382  C  CZ  . PHE C  1 146 ? 21.79300  12.56700  -27.18500 1.000 66.83000  ? 177 PHE C CZ  1 
ATOM   8383  N  N   . LEU C  1 147 ? 20.55000  11.72400  -21.02000 1.000 64.32000  ? 178 LEU C N   1 
ATOM   8384  C  CA  . LEU C  1 147 ? 19.79200  10.54800  -20.61400 1.000 65.27000  ? 178 LEU C CA  1 
ATOM   8385  C  C   . LEU C  1 147 ? 18.61600  10.22600  -21.53500 1.000 66.75000  ? 178 LEU C C   1 
ATOM   8386  O  O   . LEU C  1 147 ? 18.12600  9.08800   -21.50700 1.000 59.09000  ? 178 LEU C O   1 
ATOM   8387  C  CB  . LEU C  1 147 ? 19.28600  10.71100  -19.17900 1.000 59.79000  ? 178 LEU C CB  1 
ATOM   8388  C  CG  . LEU C  1 147 ? 20.33600  10.70000  -18.06700 1.000 75.88000  ? 178 LEU C CG  1 
ATOM   8389  C  CD1 . LEU C  1 147 ? 19.67800  10.79600  -16.68700 1.000 70.96000  ? 178 LEU C CD1 1 
ATOM   8390  C  CD2 . LEU C  1 147 ? 21.19000  9.43300   -18.16000 1.000 70.36000  ? 178 LEU C CD2 1 
ATOM   8391  N  N   . GLY C  1 148 ? 18.14900  11.19200  -22.33200 1.000 64.16000  ? 179 GLY C N   1 
ATOM   8392  C  CA  . GLY C  1 148 ? 16.97000  11.02600  -23.16100 1.000 67.77000  ? 179 GLY C CA  1 
ATOM   8393  C  C   . GLY C  1 148 ? 17.26500  10.53600  -24.56800 1.000 68.71000  ? 179 GLY C C   1 
ATOM   8394  O  O   . GLY C  1 148 ? 18.28200  9.88800   -24.83200 1.000 68.19000  ? 179 GLY C O   1 
ATOM   8395  N  N   . GLY C  1 149 ? 16.34500  10.86200  -25.48700 1.000 71.83000  ? 180 GLY C N   1 
ATOM   8396  C  CA  . GLY C  1 149 ? 16.34300  10.33300  -26.84200 1.000 65.51000  ? 180 GLY C CA  1 
ATOM   8397  C  C   . GLY C  1 149 ? 17.01000  11.18900  -27.90600 1.000 64.80000  ? 180 GLY C C   1 
ATOM   8398  O  O   . GLY C  1 149 ? 17.24100  10.72500  -29.02900 1.000 66.19000  ? 180 GLY C O   1 
ATOM   8399  N  N   . GLY C  1 150 ? 17.32100  12.43600  -27.58700 1.000 62.28000  ? 181 GLY C N   1 
ATOM   8400  C  CA  . GLY C  1 150 ? 17.97000  13.29000  -28.56900 1.000 64.64000  ? 181 GLY C CA  1 
ATOM   8401  C  C   . GLY C  1 150 ? 18.47400  14.54800  -27.90200 1.000 64.26000  ? 181 GLY C C   1 
ATOM   8402  O  O   . GLY C  1 150 ? 18.22000  14.78800  -26.71900 1.000 64.34000  ? 181 GLY C O   1 
ATOM   8403  N  N   . HIS C  1 151 ? 19.17600  15.36600  -28.68500 1.000 62.15000  ? 182 HIS C N   1 
ATOM   8404  C  CA  . HIS C  1 151 ? 19.77200  16.55900  -28.10500 1.000 62.76000  ? 182 HIS C CA  1 
ATOM   8405  C  C   . HIS C  1 151 ? 20.24000  17.49200  -29.20000 1.000 62.73000  ? 182 HIS C C   1 
ATOM   8406  O  O   . HIS C  1 151 ? 20.71300  17.04700  -30.24700 1.000 66.84000  ? 182 HIS C O   1 
ATOM   8407  C  CB  . HIS C  1 151 ? 20.95500  16.21100  -27.19400 1.000 69.32000  ? 182 HIS C CB  1 
ATOM   8408  C  CG  . HIS C  1 151 ? 21.21800  17.23900  -26.14200 1.000 62.71000  ? 182 HIS C CG  1 
ATOM   8409  N  ND1 . HIS C  1 151 ? 21.85500  18.43100  -26.41400 1.000 62.21000  ? 182 HIS C ND1 1 
ATOM   8410  C  CD2 . HIS C  1 151 ? 20.90700  17.26600  -24.82400 1.000 65.51000  ? 182 HIS C CD2 1 
ATOM   8411  C  CE1 . HIS C  1 151 ? 21.93100  19.14600  -25.30500 1.000 65.09000  ? 182 HIS C CE1 1 
ATOM   8412  N  NE2 . HIS C  1 151 ? 21.36500  18.46100  -24.32600 1.000 68.75000  ? 182 HIS C NE2 1 
ATOM   8413  N  N   . ASP C  1 152 ? 20.13400  18.79100  -28.93100 1.000 62.61000  ? 183 ASP C N   1 
ATOM   8414  C  CA  . ASP C  1 152 ? 20.71600  19.78100  -29.82400 1.000 63.55000  ? 183 ASP C CA  1 
ATOM   8415  C  C   . ASP C  1 152 ? 22.23400  19.65900  -29.83100 1.000 64.42000  ? 183 ASP C C   1 
ATOM   8416  O  O   . ASP C  1 152 ? 22.84600  19.21700  -28.85900 1.000 64.42000  ? 183 ASP C O   1 
ATOM   8417  C  CB  . ASP C  1 152 ? 20.28800  21.18200  -29.40200 1.000 67.81000  ? 183 ASP C CB  1 
ATOM   8418  C  CG  . ASP C  1 152 ? 18.83300  21.46800  -29.74600 1.000 70.94000  ? 183 ASP C CG  1 
ATOM   8419  O  OD1 . ASP C  1 152 ? 17.94200  21.17600  -28.91200 1.000 72.44000  ? 183 ASP C OD1 1 
ATOM   8420  O  OD2 . ASP C  1 152 ? 18.58300  21.96200  -30.86800 1.000 71.71000  ? 183 ASP C OD2 1 
ATOM   8421  N  N   . TYR C  1 153 ? 22.84200  20.08000  -30.93400 1.000 58.22000  ? 184 TYR C N   1 
ATOM   8422  C  CA  . TYR C  1 153 ? 24.23000  19.74000  -31.20600 1.000 61.42000  ? 184 TYR C CA  1 
ATOM   8423  C  C   . TYR C  1 153 ? 25.24400  20.80400  -30.79400 1.000 68.47000  ? 184 TYR C C   1 
ATOM   8424  O  O   . TYR C  1 153 ? 26.43300  20.47900  -30.68100 1.000 66.04000  ? 184 TYR C O   1 
ATOM   8425  C  CB  . TYR C  1 153 ? 24.39500  19.41600  -32.70000 1.000 61.74000  ? 184 TYR C CB  1 
ATOM   8426  C  CG  . TYR C  1 153 ? 23.84900  18.04300  -33.07100 1.000 67.18000  ? 184 TYR C CG  1 
ATOM   8427  C  CD1 . TYR C  1 153 ? 22.47800  17.82800  -33.23200 1.000 63.32000  ? 184 TYR C CD1 1 
ATOM   8428  C  CD2 . TYR C  1 153 ? 24.70600  16.96200  -33.25200 1.000 65.48000  ? 184 TYR C CD2 1 
ATOM   8429  C  CE1 . TYR C  1 153 ? 21.98800  16.57000  -33.56100 1.000 70.75000  ? 184 TYR C CE1 1 
ATOM   8430  C  CE2 . TYR C  1 153 ? 24.23000  15.70900  -33.58000 1.000 65.92000  ? 184 TYR C CE2 1 
ATOM   8431  C  CZ  . TYR C  1 153 ? 22.87500  15.51300  -33.74600 1.000 71.58000  ? 184 TYR C CZ  1 
ATOM   8432  O  OH  . TYR C  1 153 ? 22.40800  14.25300  -34.07200 1.000 61.02000  ? 184 TYR C OH  1 
ATOM   8433  N  N   . PHE C  1 154 ? 24.82700  22.05800  -30.59100 1.000 71.91000  ? 185 PHE C N   1 
ATOM   8434  C  CA  . PHE C  1 154 ? 25.75600  23.15500  -30.29700 1.000 70.83000  ? 185 PHE C CA  1 
ATOM   8435  C  C   . PHE C  1 154 ? 25.52800  23.66500  -28.88000 1.000 68.10000  ? 185 PHE C C   1 
ATOM   8436  O  O   . PHE C  1 154 ? 24.43600  24.17500  -28.58100 1.000 68.45000  ? 185 PHE C O   1 
ATOM   8437  C  CB  . PHE C  1 154 ? 25.60400  24.28900  -31.30600 1.000 64.63000  ? 185 PHE C CB  1 
ATOM   8438  C  CG  . PHE C  1 154 ? 26.21300  23.99200  -32.64900 1.000 62.40000  ? 185 PHE C CG  1 
ATOM   8439  C  CD1 . PHE C  1 154 ? 27.58400  23.99800  -32.82400 1.000 58.45000  ? 185 PHE C CD1 1 
ATOM   8440  C  CD2 . PHE C  1 154 ? 25.41200  23.73000  -33.74200 1.000 58.25000  ? 185 PHE C CD2 1 
ATOM   8441  C  CE1 . PHE C  1 154 ? 28.14000  23.74400  -34.06400 1.000 58.44000  ? 185 PHE C CE1 1 
ATOM   8442  C  CE2 . PHE C  1 154 ? 25.96800  23.47200  -34.97800 1.000 57.49000  ? 185 PHE C CE2 1 
ATOM   8443  C  CZ  . PHE C  1 154 ? 27.33400  23.49000  -35.14500 1.000 51.15000  ? 185 PHE C CZ  1 
ATOM   8444  N  N   . PRO C  1 155 ? 26.49800  23.51600  -27.96900 1.000 71.64000  ? 186 PRO C N   1 
ATOM   8445  C  CA  . PRO C  1 155 ? 26.26900  23.94600  -26.57500 1.000 68.54000  ? 186 PRO C CA  1 
ATOM   8446  C  C   . PRO C  1 155 ? 26.00100  25.43600  -26.42900 1.000 69.88000  ? 186 PRO C C   1 
ATOM   8447  O  O   . PRO C  1 155 ? 25.21800  25.84000  -25.55500 1.000 66.11000  ? 186 PRO C O   1 
ATOM   8448  C  CB  . PRO C  1 155 ? 27.57400  23.54000  -25.87200 1.000 69.44000  ? 186 PRO C CB  1 
ATOM   8449  C  CG  . PRO C  1 155 ? 28.16800  22.48500  -26.75000 1.000 68.42000  ? 186 PRO C CG  1 
ATOM   8450  C  CD  . PRO C  1 155 ? 27.84300  22.94400  -28.14600 1.000 69.45000  ? 186 PRO C CD  1 
ATOM   8451  N  N   . SER C  1 156 ? 26.63200  26.27100  -27.26000 1.000 65.66000  ? 187 SER C N   1 
ATOM   8452  C  CA  . SER C  1 156 ? 26.34700  27.70100  -27.21400 1.000 68.51000  ? 187 SER C CA  1 
ATOM   8453  C  C   . SER C  1 156 ? 24.85500  27.97900  -27.36300 1.000 69.85000  ? 187 SER C C   1 
ATOM   8454  O  O   . SER C  1 156 ? 24.29000  28.80200  -26.63000 1.000 66.43000  ? 187 SER C O   1 
ATOM   8455  C  CB  . SER C  1 156 ? 27.16500  28.41900  -28.28800 1.000 64.04000  ? 187 SER C CB  1 
ATOM   8456  O  OG  . SER C  1 156 ? 27.08900  27.74200  -29.52600 1.000 71.36000  ? 187 SER C OG  1 
ATOM   8457  N  N   . GLU C  1 157 ? 24.17800  27.22400  -28.22900 1.000 69.53000  ? 188 GLU C N   1 
ATOM   8458  C  CA  . GLU C  1 157 ? 22.77200  27.50000  -28.46900 1.000 60.73000  ? 188 GLU C CA  1 
ATOM   8459  C  C   . GLU C  1 157 ? 21.89500  26.89300  -27.38700 1.000 68.32000  ? 188 GLU C C   1 
ATOM   8460  O  O   . GLU C  1 157 ? 21.06000  27.59200  -26.80200 1.000 73.62000  ? 188 GLU C O   1 
ATOM   8461  C  CB  . GLU C  1 157 ? 22.35800  26.96400  -29.83400 1.000 71.93000  ? 188 GLU C CB  1 
ATOM   8462  C  CG  . GLU C  1 157 ? 23.20000  27.47100  -31.00100 1.000 74.24000  ? 188 GLU C CG  1 
ATOM   8463  C  CD  . GLU C  1 157 ? 22.86000  26.76700  -32.30000 1.000 74.81000  ? 188 GLU C CD  1 
ATOM   8464  O  OE1 . GLU C  1 157 ? 22.08600  25.78400  -32.26100 1.000 76.98000  ? 188 GLU C OE1 1 
ATOM   8465  O  OE2 . GLU C  1 157 ? 23.38100  27.17900  -33.35700 1.000 85.67000  ? 188 GLU C OE2 1 
ATOM   8466  N  N   . TYR C  1 158 ? 22.09400  25.62000  -27.05500 1.000 65.57000  ? 189 TYR C N   1 
ATOM   8467  C  CA  . TYR C  1 158 ? 21.12200  25.03300  -26.14300 1.000 71.69000  ? 189 TYR C CA  1 
ATOM   8468  C  C   . TYR C  1 158 ? 21.37500  25.43200  -24.69800 1.000 70.92000  ? 189 TYR C C   1 
ATOM   8469  O  O   . TYR C  1 158 ? 20.42100  25.49000  -23.91900 1.000 74.18000  ? 189 TYR C O   1 
ATOM   8470  C  CB  . TYR C  1 158 ? 21.05500  23.50600  -26.29600 1.000 73.97000  ? 189 TYR C CB  1 
ATOM   8471  C  CG  . TYR C  1 158 ? 22.29000  22.72100  -25.87300 1.000 73.40000  ? 189 TYR C CG  1 
ATOM   8472  C  CD1 . TYR C  1 158 ? 22.62400  22.55300  -24.52700 1.000 71.29000  ? 189 TYR C CD1 1 
ATOM   8473  C  CD2 . TYR C  1 158 ? 23.10600  22.12100  -26.83300 1.000 70.60000  ? 189 TYR C CD2 1 
ATOM   8474  C  CE1 . TYR C  1 158 ? 23.75200  21.82900  -24.15900 1.000 72.88000  ? 189 TYR C CE1 1 
ATOM   8475  C  CE2 . TYR C  1 158 ? 24.21800  21.39600  -26.47600 1.000 72.07000  ? 189 TYR C CE2 1 
ATOM   8476  C  CZ  . TYR C  1 158 ? 24.54600  21.26300  -25.14300 1.000 69.96000  ? 189 TYR C CZ  1 
ATOM   8477  O  OH  . TYR C  1 158 ? 25.65800  20.53800  -24.81100 1.000 65.41000  ? 189 TYR C OH  1 
ATOM   8478  N  N   . GLN C  1 159 ? 22.61800  25.75000  -24.31900 1.000 74.94000  ? 190 GLN C N   1 
ATOM   8479  C  CA  . GLN C  1 159 ? 22.83700  26.26300  -22.96800 1.000 76.59000  ? 190 GLN C CA  1 
ATOM   8480  C  C   . GLN C  1 159 ? 22.15300  27.61800  -22.80000 1.000 78.18000  ? 190 GLN C C   1 
ATOM   8481  O  O   . GLN C  1 159 ? 21.47500  27.86100  -21.79000 1.000 75.60000  ? 190 GLN C O   1 
ATOM   8482  C  CB  . GLN C  1 159 ? 24.33100  26.37200  -22.63700 1.000 75.32000  ? 190 GLN C CB  1 
ATOM   8483  C  CG  . GLN C  1 159 ? 25.02100  25.05600  -22.23800 1.000 75.38000  ? 190 GLN C CG  1 
ATOM   8484  C  CD  . GLN C  1 159 ? 26.55800  25.11000  -22.29600 1.000 71.54000  ? 190 GLN C CD  1 
ATOM   8485  O  OE1 . GLN C  1 159 ? 27.15800  26.10500  -22.71900 1.000 64.27000  ? 190 GLN C OE1 1 
ATOM   8486  N  NE2 . GLN C  1 159 ? 27.19400  24.01200  -21.89400 1.000 74.51000  ? 190 GLN C NE2 1 
ATOM   8487  N  N   . LYS C  1 160 ? 22.29800  28.51000  -23.79500 1.000 68.03000  ? 191 LYS C N   1 
ATOM   8488  C  CA  . LYS C  1 160 ? 21.59600  29.79200  -23.74600 1.000 75.08000  ? 191 LYS C CA  1 
ATOM   8489  C  C   . LYS C  1 160 ? 20.08500  29.58400  -23.62000 1.000 76.13000  ? 191 LYS C C   1 
ATOM   8490  O  O   . LYS C  1 160 ? 19.44100  30.14800  -22.72200 1.000 70.73000  ? 191 LYS C O   1 
ATOM   8491  C  CB  . LYS C  1 160 ? 21.93500  30.61900  -24.99100 1.000 76.48000  ? 191 LYS C CB  1 
ATOM   8492  C  CG  . LYS C  1 160 ? 21.04400  31.83600  -25.16200 1.000 78.92000  ? 191 LYS C CG  1 
ATOM   8493  C  CD  . LYS C  1 160 ? 21.57700  32.83200  -26.19600 1.000 83.04000  ? 191 LYS C CD  1 
ATOM   8494  C  CE  . LYS C  1 160 ? 21.98500  32.11200  -27.48100 1.000 85.57000  ? 191 LYS C CE  1 
ATOM   8495  N  NZ  . LYS C  1 160 ? 22.64800  32.98800  -28.50200 1.000 80.45000  ? 191 LYS C NZ  1 
ATOM   8496  N  N   . THR C  1 161 ? 19.50800  28.74400  -24.49400 1.000 74.75000  ? 192 THR C N   1 
ATOM   8497  C  CA  . THR C  1 161 ? 18.07400  28.47300  -24.42500 1.000 67.95000  ? 192 THR C CA  1 
ATOM   8498  C  C   . THR C  1 161 ? 17.69900  27.86900  -23.07500 1.000 71.98000  ? 192 THR C C   1 
ATOM   8499  O  O   . THR C  1 161 ? 16.65700  28.20600  -22.50100 1.000 73.73000  ? 192 THR C O   1 
ATOM   8500  C  CB  . THR C  1 161 ? 17.64100  27.54500  -25.56400 1.000 74.83000  ? 192 THR C CB  1 
ATOM   8501  O  OG1 . THR C  1 161 ? 17.93500  28.14700  -26.83600 1.000 69.95000  ? 192 THR C OG1 1 
ATOM   8502  C  CG2 . THR C  1 161 ? 16.13700  27.26200  -25.49000 1.000 67.67000  ? 192 THR C CG2 1 
ATOM   8503  N  N   . TYR C  1 162 ? 18.53200  26.96900  -22.55600 1.000 73.52000  ? 193 TYR C N   1 
ATOM   8504  C  CA  . TYR C  1 162 ? 18.22700  26.34300  -21.27500 1.000 73.12000  ? 193 TYR C CA  1 
ATOM   8505  C  C   . TYR C  1 162 ? 18.25500  27.35200  -20.13300 1.000 80.63000  ? 193 TYR C C   1 
ATOM   8506  O  O   . TYR C  1 162 ? 17.43800  27.26600  -19.20600 1.000 76.05000  ? 193 TYR C O   1 
ATOM   8507  C  CB  . TYR C  1 162 ? 19.19700  25.21000  -20.96600 1.000 67.68000  ? 193 TYR C CB  1 
ATOM   8508  C  CG  . TYR C  1 162 ? 18.90200  24.59700  -19.61700 1.000 67.62000  ? 193 TYR C CG  1 
ATOM   8509  C  CD1 . TYR C  1 162 ? 17.81900  23.75300  -19.45100 1.000 70.89000  ? 193 TYR C CD1 1 
ATOM   8510  C  CD2 . TYR C  1 162 ? 19.66800  24.89700  -18.50800 1.000 61.47000  ? 193 TYR C CD2 1 
ATOM   8511  C  CE1 . TYR C  1 162 ? 17.51800  23.19500  -18.22700 1.000 72.06000  ? 193 TYR C CE1 1 
ATOM   8512  C  CE2 . TYR C  1 162 ? 19.37000  24.34700  -17.26800 1.000 69.23000  ? 193 TYR C CE2 1 
ATOM   8513  C  CZ  . TYR C  1 162 ? 18.29000  23.49800  -17.13600 1.000 74.04000  ? 193 TYR C CZ  1 
ATOM   8514  O  OH  . TYR C  1 162 ? 17.97800  22.93100  -15.92200 1.000 73.45000  ? 193 TYR C OH  1 
ATOM   8515  N  N   . LYS C  1 163 ? 19.24500  28.25200  -20.13100 1.000 82.73000  ? 194 LYS C N   1 
ATOM   8516  C  CA  . LYS C  1 163 ? 19.34800  29.24800  -19.06600 1.000 81.90000  ? 194 LYS C CA  1 
ATOM   8517  C  C   . LYS C  1 163 ? 18.15900  30.20600  -19.07900 1.000 81.63000  ? 194 LYS C C   1 
ATOM   8518  O  O   . LYS C  1 163 ? 17.47700  30.37700  -18.06000 1.000 78.10000  ? 194 LYS C O   1 
ATOM   8519  C  CB  . LYS C  1 163 ? 20.66600  30.02100  -19.20000 1.000 78.92000  ? 194 LYS C CB  1 
ATOM   8520  N  N   . ALA C  1 164 ? 17.87300  30.81300  -20.23800 1.000 77.23000  ? 195 ALA C N   1 
ATOM   8521  C  CA  . ALA C  1 164 ? 16.77400  31.77000  -20.32300 1.000 77.92000  ? 195 ALA C CA  1 
ATOM   8522  C  C   . ALA C  1 164 ? 15.46900  31.16100  -19.82800 1.000 83.37000  ? 195 ALA C C   1 
ATOM   8523  O  O   . ALA C  1 164 ? 14.82200  31.69700  -18.91800 1.000 86.22000  ? 195 ALA C O   1 
ATOM   8524  C  CB  . ALA C  1 164 ? 16.62200  32.25900  -21.76900 1.000 67.95000  ? 195 ALA C CB  1 
ATOM   8525  N  N   . GLN C  1 165 ? 15.12300  29.97900  -20.34500 1.000 79.23000  ? 196 GLN C N   1 
ATOM   8526  C  CA  . GLN C  1 165 ? 13.84000  29.36200  -20.01800 1.000 79.82000  ? 196 GLN C CA  1 
ATOM   8527  C  C   . GLN C  1 165 ? 13.79200  28.86200  -18.57600 1.000 81.83000  ? 196 GLN C C   1 
ATOM   8528  O  O   . GLN C  1 165 ? 12.71000  28.81600  -17.97900 1.000 79.77000  ? 196 GLN C O   1 
ATOM   8529  C  CB  . GLN C  1 165 ? 13.55300  28.21700  -20.99800 1.000 76.72000  ? 196 GLN C CB  1 
ATOM   8530  N  N   . LYS C  1 166 ? 14.94200  28.48400  -17.99900 1.000 84.98000  ? 197 LYS C N   1 
ATOM   8531  C  CA  . LYS C  1 166 ? 14.96900  28.06800  -16.59700 1.000 83.49000  ? 197 LYS C CA  1 
ATOM   8532  C  C   . LYS C  1 166 ? 14.79300  29.25500  -15.65400 1.000 85.84000  ? 197 LYS C C   1 
ATOM   8533  O  O   . LYS C  1 166 ? 14.13900  29.13200  -14.61000 1.000 81.70000  ? 197 LYS C O   1 
ATOM   8534  C  CB  . LYS C  1 166 ? 16.26800  27.32200  -16.28400 1.000 73.77000  ? 197 LYS C CB  1 
ATOM   8535  N  N   . LYS C  1 167 ? 15.38700  30.40600  -15.98500 1.000 84.90000  ? 198 LYS C N   1 
ATOM   8536  C  CA  . LYS C  1 167 ? 15.20000  31.58300  -15.14200 1.000 84.93000  ? 198 LYS C CA  1 
ATOM   8537  C  C   . LYS C  1 167 ? 13.77500  32.11400  -15.23100 1.000 86.86000  ? 198 LYS C C   1 
ATOM   8538  O  O   . LYS C  1 167 ? 13.31100  32.77300  -14.29400 1.000 84.70000  ? 198 LYS C O   1 
ATOM   8539  C  CB  . LYS C  1 167 ? 16.20600  32.67900  -15.51200 1.000 77.85000  ? 198 LYS C CB  1 
ATOM   8540  N  N   . ALA C  1 168 ? 13.04400  31.76200  -16.29000 1.000 84.22000  ? 199 ALA C N   1 
ATOM   8541  C  CA  . ALA C  1 168 ? 11.65500  32.16200  -16.44800 1.000 79.23000  ? 199 ALA C CA  1 
ATOM   8542  C  C   . ALA C  1 168 ? 10.71300  31.14500  -15.83400 1.000 80.72000  ? 199 ALA C C   1 
ATOM   8543  O  O   . ALA C  1 168 ? 9.50300   31.20500  -16.07400 1.000 81.80000  ? 199 ALA C O   1 
ATOM   8544  C  CB  . ALA C  1 168 ? 11.31800  32.34800  -17.93000 1.000 69.61000  ? 199 ALA C CB  1 
ATOM   8545  N  N   . GLY C  1 169 ? 11.24600  30.22300  -15.04000 1.000 82.66000  ? 200 GLY C N   1 
ATOM   8546  C  CA  . GLY C  1 169 ? 10.41400  29.19600  -14.43800 1.000 81.16000  ? 200 GLY C CA  1 
ATOM   8547  C  C   . GLY C  1 169 ? 9.60400   28.42000  -15.44900 1.000 83.73000  ? 200 GLY C C   1 
ATOM   8548  O  O   . GLY C  1 169 ? 8.45200   28.06500  -15.17000 1.000 83.74000  ? 200 GLY C O   1 
ATOM   8549  N  N   . ASN C  1 170 ? 10.16300  28.17700  -16.63700 1.000 83.49000  ? 201 ASN C N   1 
ATOM   8550  C  CA  . ASN C  1 170 ? 9.48200   27.33800  -17.61200 1.000 77.91000  ? 201 ASN C CA  1 
ATOM   8551  C  C   . ASN C  1 170 ? 9.32000   25.97100  -16.96900 1.000 76.45000  ? 201 ASN C C   1 
ATOM   8552  O  O   . ASN C  1 170 ? 10.32500  25.33300  -16.63300 1.000 85.12000  ? 201 ASN C O   1 
ATOM   8553  C  CB  . ASN C  1 170 ? 10.27300  27.24200  -18.91600 1.000 75.99000  ? 201 ASN C CB  1 
ATOM   8554  C  CG  . ASN C  1 170 ? 9.54400   26.45300  -19.99400 1.000 77.44000  ? 201 ASN C CG  1 
ATOM   8555  O  OD1 . ASN C  1 170 ? 8.70100   25.60700  -19.70100 1.000 73.64000  ? 201 ASN C OD1 1 
ATOM   8556  N  ND2 . ASN C  1 170 ? 9.85400   26.74700  -21.25300 1.000 74.62000  ? 201 ASN C ND2 1 
ATOM   8557  N  N   . PRO C  1 171 ? 8.09500   25.49100  -16.75800 1.000 77.87000  ? 202 PRO C N   1 
ATOM   8558  C  CA  . PRO C  1 171 ? 7.92800   24.21700  -16.04800 1.000 80.12000  ? 202 PRO C CA  1 
ATOM   8559  C  C   . PRO C  1 171 ? 8.09200   22.99500  -16.93400 1.000 83.17000  ? 202 PRO C C   1 
ATOM   8560  O  O   . PRO C  1 171 ? 8.03200   21.86900  -16.42000 1.000 79.78000  ? 202 PRO C O   1 
ATOM   8561  C  CB  . PRO C  1 171 ? 6.50300   24.32400  -15.48800 1.000 75.92000  ? 202 PRO C CB  1 
ATOM   8562  C  CG  . PRO C  1 171 ? 5.77500   25.16600  -16.50600 1.000 77.46000  ? 202 PRO C CG  1 
ATOM   8563  C  CD  . PRO C  1 171 ? 6.80400   26.09800  -17.13700 1.000 78.08000  ? 202 PRO C CD  1 
ATOM   8564  N  N   . ASN C  1 172 ? 8.25700   23.18000  -18.24500 1.000 81.37000  ? 203 ASN C N   1 
ATOM   8565  C  CA  . ASN C  1 172 ? 8.40900   22.08200  -19.19000 1.000 77.22000  ? 203 ASN C CA  1 
ATOM   8566  C  C   . ASN C  1 172 ? 9.51500   22.39600  -20.20100 1.000 74.71000  ? 203 ASN C C   1 
ATOM   8567  O  O   . ASN C  1 172 ? 9.27100   22.56200  -21.39300 1.000 74.88000  ? 203 ASN C O   1 
ATOM   8568  C  CB  . ASN C  1 172 ? 7.08900   21.81000  -19.89400 1.000 69.96000  ? 203 ASN C CB  1 
ATOM   8569  C  CG  . ASN C  1 172 ? 5.94800   21.66700  -18.92800 1.000 80.17000  ? 203 ASN C CG  1 
ATOM   8570  O  OD1 . ASN C  1 172 ? 6.00500   20.85900  -17.99900 1.000 85.79000  ? 203 ASN C OD1 1 
ATOM   8571  N  ND2 . ASN C  1 172 ? 4.89800   22.45700  -19.13100 1.000 77.42000  ? 203 ASN C ND2 1 
ATOM   8572  N  N   . ILE C  1 173 ? 10.75100  22.53100  -19.72300 1.000 79.29000  ? 204 ILE C N   1 
ATOM   8573  C  CA  . ILE C  1 173 ? 11.87200  22.69600  -20.64200 1.000 81.67000  ? 204 ILE C CA  1 
ATOM   8574  C  C   . ILE C  1 173 ? 12.12300  21.36600  -21.34200 1.000 75.99000  ? 204 ILE C C   1 
ATOM   8575  O  O   . ILE C  1 173 ? 12.14100  20.30500  -20.70300 1.000 68.42000  ? 204 ILE C O   1 
ATOM   8576  C  CB  . ILE C  1 173 ? 13.12000  23.19200  -19.89700 1.000 80.61000  ? 204 ILE C CB  1 
ATOM   8577  N  N   . ARG C  1 174 ? 12.28400  21.41100  -22.66500 1.000 77.65000  ? 205 ARG C N   1 
ATOM   8578  C  CA  . ARG C  1 174 ? 12.48000  20.18900  -23.43600 1.000 74.31000  ? 205 ARG C CA  1 
ATOM   8579  C  C   . ARG C  1 174 ? 13.86400  19.61600  -23.15100 1.000 73.52000  ? 205 ARG C C   1 
ATOM   8580  O  O   . ARG C  1 174 ? 14.85500  20.34800  -23.09000 1.000 74.85000  ? 205 ARG C O   1 
ATOM   8581  C  CB  . ARG C  1 174 ? 12.28800  20.46600  -24.93100 1.000 64.45000  ? 205 ARG C CB  1 
ATOM   8582  N  N   . ASP C  1 175 ? 13.93300  18.29300  -22.97200 1.000 70.60000  ? 206 ASP C N   1 
ATOM   8583  C  CA  . ASP C  1 175 ? 15.21100  17.68600  -22.61300 1.000 69.00000  ? 206 ASP C CA  1 
ATOM   8584  C  C   . ASP C  1 175 ? 16.23800  17.74800  -23.73500 1.000 65.45000  ? 206 ASP C C   1 
ATOM   8585  O  O   . ASP C  1 175 ? 17.42000  17.50700  -23.47400 1.000 70.25000  ? 206 ASP C O   1 
ATOM   8586  C  CB  . ASP C  1 175 ? 15.02700  16.23500  -22.12800 1.000 71.78000  ? 206 ASP C CB  1 
ATOM   8587  C  CG  . ASP C  1 175 ? 14.30100  15.33600  -23.12900 1.000 63.66000  ? 206 ASP C CG  1 
ATOM   8588  O  OD1 . ASP C  1 175 ? 14.12000  15.72600  -24.30000 1.000 63.91000  ? 206 ASP C OD1 1 
ATOM   8589  O  OD2 . ASP C  1 175 ? 13.91000  14.22300  -22.71600 1.000 63.50000  ? 206 ASP C OD2 1 
ATOM   8590  N  N   . TYR C  1 176 ? 15.83200  18.07400  -24.96100 1.000 58.51000  ? 207 TYR C N   1 
ATOM   8591  C  CA  . TYR C  1 176 ? 16.81700  18.27900  -26.01200 1.000 64.85000  ? 207 TYR C CA  1 
ATOM   8592  C  C   . TYR C  1 176 ? 17.76000  19.43000  -25.72300 1.000 65.82000  ? 207 TYR C C   1 
ATOM   8593  O  O   . TYR C  1 176 ? 18.75400  19.58500  -26.44200 1.000 68.40000  ? 207 TYR C O   1 
ATOM   8594  C  CB  . TYR C  1 176 ? 16.13900  18.52700  -27.36300 1.000 64.94000  ? 207 TYR C CB  1 
ATOM   8595  C  CG  . TYR C  1 176 ? 15.86400  17.26200  -28.14000 1.000 63.11000  ? 207 TYR C CG  1 
ATOM   8596  C  CD1 . TYR C  1 176 ? 15.18600  16.20000  -27.54800 1.000 69.33000  ? 207 TYR C CD1 1 
ATOM   8597  C  CD2 . TYR C  1 176 ? 16.26500  17.13200  -29.46800 1.000 65.92000  ? 207 TYR C CD2 1 
ATOM   8598  C  CE1 . TYR C  1 176 ? 14.91700  15.03500  -28.25000 1.000 66.83000  ? 207 TYR C CE1 1 
ATOM   8599  C  CE2 . TYR C  1 176 ? 15.99900  15.96800  -30.18800 1.000 66.36000  ? 207 TYR C CE2 1 
ATOM   8600  C  CZ  . TYR C  1 176 ? 15.32100  14.92100  -29.56500 1.000 68.03000  ? 207 TYR C CZ  1 
ATOM   8601  O  OH  . TYR C  1 176 ? 15.05300  13.75200  -30.24100 1.000 72.08000  ? 207 TYR C OH  1 
ATOM   8602  N  N   . VAL C  1 177 ? 17.46700  20.26800  -24.73600 1.000 68.34000  ? 208 VAL C N   1 
ATOM   8603  C  CA  . VAL C  1 177 ? 18.35400  21.37500  -24.40700 1.000 76.34000  ? 208 VAL C CA  1 
ATOM   8604  C  C   . VAL C  1 177 ? 18.92700  21.27600  -23.00300 1.000 72.42000  ? 208 VAL C C   1 
ATOM   8605  O  O   . VAL C  1 177 ? 19.69500  22.15200  -22.60700 1.000 72.20000  ? 208 VAL C O   1 
ATOM   8606  C  CB  . VAL C  1 177 ? 17.66200  22.73900  -24.61100 1.000 76.34000  ? 208 VAL C CB  1 
ATOM   8607  C  CG1 . VAL C  1 177 ? 17.17100  22.87100  -26.05500 1.000 69.98000  ? 208 VAL C CG1 1 
ATOM   8608  C  CG2 . VAL C  1 177 ? 16.52600  22.92600  -23.61300 1.000 74.13000  ? 208 VAL C CG2 1 
ATOM   8609  N  N   . PHE C  1 178 ? 18.60200  20.22200  -22.25100 1.000 70.57000  ? 209 PHE C N   1 
ATOM   8610  C  CA  . PHE C  1 178 ? 19.18900  20.04700  -20.93500 1.000 65.17000  ? 209 PHE C CA  1 
ATOM   8611  C  C   . PHE C  1 178 ? 20.71000  20.02200  -21.04900 1.000 72.63000  ? 209 PHE C C   1 
ATOM   8612  O  O   . PHE C  1 178 ? 21.25800  19.55500  -22.05400 1.000 71.69000  ? 209 PHE C O   1 
ATOM   8613  C  CB  . PHE C  1 178 ? 18.72900  18.74400  -20.28500 1.000 67.29000  ? 209 PHE C CB  1 
ATOM   8614  C  CG  . PHE C  1 178 ? 17.30600  18.74500  -19.81800 1.000 65.63000  ? 209 PHE C CG  1 
ATOM   8615  C  CD1 . PHE C  1 178 ? 16.49300  19.84800  -20.00100 1.000 70.40000  ? 209 PHE C CD1 1 
ATOM   8616  C  CD2 . PHE C  1 178 ? 16.78900  17.63100  -19.16800 1.000 67.09000  ? 209 PHE C CD2 1 
ATOM   8617  C  CE1 . PHE C  1 178 ? 15.17800  19.83400  -19.56300 1.000 74.54000  ? 209 PHE C CE1 1 
ATOM   8618  C  CE2 . PHE C  1 178 ? 15.48500  17.60600  -18.72100 1.000 71.08000  ? 209 PHE C CE2 1 
ATOM   8619  C  CZ  . PHE C  1 178 ? 14.67200  18.70800  -18.91700 1.000 73.73000  ? 209 PHE C CZ  1 
ATOM   8620  N  N   . PRO C  1 179 ? 21.41400  20.55200  -20.05000 1.000 76.15000  ? 210 PRO C N   1 
ATOM   8621  C  CA  . PRO C  1 179 ? 22.86600  20.35100  -19.98500 1.000 70.93000  ? 210 PRO C CA  1 
ATOM   8622  C  C   . PRO C  1 179 ? 23.19500  18.86900  -19.89700 1.000 71.96000  ? 210 PRO C C   1 
ATOM   8623  O  O   . PRO C  1 179 ? 22.52600  18.10500  -19.19300 1.000 70.41000  ? 210 PRO C O   1 
ATOM   8624  C  CB  . PRO C  1 179 ? 23.27000  21.09400  -18.70800 1.000 67.28000  ? 210 PRO C CB  1 
ATOM   8625  C  CG  . PRO C  1 179 ? 22.00400  21.08800  -17.87000 1.000 73.00000  ? 210 PRO C CG  1 
ATOM   8626  C  CD  . PRO C  1 179 ? 20.90300  21.28300  -18.87700 1.000 73.42000  ? 210 PRO C CD  1 
ATOM   8627  N  N   . MET C  1 180 ? 24.25500  18.47200  -20.60000 1.000 73.24000  ? 211 MET C N   1 
ATOM   8628  C  CA  . MET C  1 180 ? 24.73700  17.10300  -20.50800 1.000 68.44000  ? 211 MET C CA  1 
ATOM   8629  C  C   . MET C  1 180 ? 25.45600  16.90100  -19.17800 1.000 72.69000  ? 211 MET C C   1 
ATOM   8630  O  O   . MET C  1 180 ? 25.74300  17.84800  -18.43700 1.000 72.74000  ? 211 MET C O   1 
ATOM   8631  C  CB  . MET C  1 180 ? 25.66500  16.77900  -21.68300 1.000 64.46000  ? 211 MET C CB  1 
ATOM   8632  C  CG  . MET C  1 180 ? 24.98400  16.90400  -23.04800 1.000 70.57000  ? 211 MET C CG  1 
ATOM   8633  S  SD  . MET C  1 180 ? 25.81500  16.19900  -24.50500 1.000 64.37000  ? 211 MET C SD  1 
ATOM   8634  C  CE  . MET C  1 180 ? 27.27400  17.23000  -24.60800 1.000 69.84000  ? 211 MET C CE  1 
ATOM   8635  N  N   . GLU C  1 181 ? 25.76000  15.64600  -18.88200 1.000 70.67000  ? 212 GLU C N   1 
ATOM   8636  C  CA  . GLU C  1 181 ? 26.33300  15.27700  -17.60400 1.000 68.79000  ? 212 GLU C CA  1 
ATOM   8637  C  C   . GLU C  1 181 ? 27.55400  14.39900  -17.81700 1.000 72.20000  ? 212 GLU C C   1 
ATOM   8638  O  O   . GLU C  1 181 ? 27.69500  13.72600  -18.84300 1.000 68.57000  ? 212 GLU C O   1 
ATOM   8639  C  CB  . GLU C  1 181 ? 25.30800  14.55900  -16.73400 1.000 72.59000  ? 212 GLU C CB  1 
ATOM   8640  C  CG  . GLU C  1 181 ? 24.85100  13.23000  -17.27900 1.000 69.49000  ? 212 GLU C CG  1 
ATOM   8641  C  CD  . GLU C  1 181 ? 24.15600  12.39500  -16.22700 1.000 75.31000  ? 212 GLU C CD  1 
ATOM   8642  O  OE1 . GLU C  1 181 ? 24.85700  11.64800  -15.50300 1.000 74.13000  ? 212 GLU C OE1 1 
ATOM   8643  O  OE2 . GLU C  1 181 ? 22.91300  12.49400  -16.11200 1.000 78.26000  ? 212 GLU C OE2 1 
ATOM   8644  N  N   . HIS C  1 182 ? 28.44300  14.42600  -16.82700 1.000 73.02000  ? 213 HIS C N   1 
ATOM   8645  C  CA  . HIS C  1 182 ? 29.62300  13.56900  -16.77400 1.000 73.18000  ? 213 HIS C CA  1 
ATOM   8646  C  C   . HIS C  1 182 ? 29.50100  12.86500  -15.42800 1.000 74.07000  ? 213 HIS C C   1 
ATOM   8647  O  O   . HIS C  1 182 ? 29.95000  13.38600  -14.40500 1.000 77.27000  ? 213 HIS C O   1 
ATOM   8648  C  CB  . HIS C  1 182 ? 30.89600  14.40900  -16.90800 1.000 64.43000  ? 213 HIS C CB  1 
ATOM   8649  C  CG  . HIS C  1 182 ? 32.16100  13.61900  -17.01600 1.000 76.07000  ? 213 HIS C CG  1 
ATOM   8650  N  ND1 . HIS C  1 182 ? 32.24800  12.28200  -16.69100 1.000 78.48000  ? 213 HIS C ND1 1 
ATOM   8651  C  CD2 . HIS C  1 182 ? 33.40000  13.98800  -17.42700 1.000 82.37000  ? 213 HIS C CD2 1 
ATOM   8652  C  CE1 . HIS C  1 182 ? 33.48600  11.86400  -16.89100 1.000 75.35000  ? 213 HIS C CE1 1 
ATOM   8653  N  NE2 . HIS C  1 182 ? 34.20500  12.87900  -17.33700 1.000 79.45000  ? 213 HIS C NE2 1 
ATOM   8654  N  N   . ASN C  1 183 ? 28.89300  11.68100  -15.43700 1.000 72.66000  ? 214 ASN C N   1 
ATOM   8655  C  CA  . ASN C  1 183 ? 28.67400  10.89600  -14.21900 1.000 80.87000  ? 214 ASN C CA  1 
ATOM   8656  C  C   . ASN C  1 183 ? 27.88700  11.69100  -13.16900 1.000 79.37000  ? 214 ASN C C   1 
ATOM   8657  O  O   . ASN C  1 183 ? 28.19600  11.65800  -11.97600 1.000 73.00000  ? 214 ASN C O   1 
ATOM   8658  C  CB  . ASN C  1 183 ? 30.00400  10.38300  -13.65600 1.000 73.51000  ? 214 ASN C CB  1 
ATOM   8659  C  CG  . ASN C  1 183 ? 30.67400  9.36000   -14.57700 1.000 73.87000  ? 214 ASN C CG  1 
ATOM   8660  O  OD1 . ASN C  1 183 ? 30.02900  8.43700   -15.08000 1.000 75.30000  ? 214 ASN C OD1 1 
ATOM   8661  N  ND2 . ASN C  1 183 ? 31.96800  9.53800   -14.81800 1.000 75.32000  ? 214 ASN C ND2 1 
ATOM   8662  N  N   . GLY C  1 184 ? 26.83300  12.37400  -13.62100 1.000 74.53000  ? 215 GLY C N   1 
ATOM   8663  C  CA  . GLY C  1 184 ? 25.95500  13.15600  -12.77000 1.000 72.74000  ? 215 GLY C CA  1 
ATOM   8664  C  C   . GLY C  1 184 ? 26.26800  14.64100  -12.68200 1.000 78.16000  ? 215 GLY C C   1 
ATOM   8665  O  O   . GLY C  1 184 ? 25.35400  15.47300  -12.74200 1.000 77.80000  ? 215 GLY C O   1 
ATOM   8666  N  N   . LYS C  1 185 ? 27.54100  15.00500  -12.58000 1.000 76.72000  ? 216 LYS C N   1 
ATOM   8667  C  CA  . LYS C  1 185 ? 27.86800  16.41600  -12.51900 1.000 77.35000  ? 216 LYS C CA  1 
ATOM   8668  C  C   . LYS C  1 185 ? 27.75200  17.02900  -13.91700 1.000 74.05000  ? 216 LYS C C   1 
ATOM   8669  O  O   . LYS C  1 185 ? 27.82700  16.31800  -14.92000 1.000 75.38000  ? 216 LYS C O   1 
ATOM   8670  C  CB  . LYS C  1 185 ? 29.27400  16.60700  -11.95500 1.000 65.11000  ? 216 LYS C CB  1 
ATOM   8671  N  N   . PRO C  1 186 ? 27.51800  18.34100  -14.00800 1.000 81.67000  ? 217 PRO C N   1 
ATOM   8672  C  CA  . PRO C  1 186 ? 27.37700  18.97100  -15.32800 1.000 69.72000  ? 217 PRO C CA  1 
ATOM   8673  C  C   . PRO C  1 186 ? 28.61000  18.74700  -16.18400 1.000 68.24000  ? 217 PRO C C   1 
ATOM   8674  O  O   . PRO C  1 186 ? 29.74000  18.85500  -15.71900 1.000 73.80000  ? 217 PRO C O   1 
ATOM   8675  C  CB  . PRO C  1 186 ? 27.17800  20.45700  -15.00000 1.000 75.30000  ? 217 PRO C CB  1 
ATOM   8676  C  CG  . PRO C  1 186 ? 27.59100  20.60900  -13.55100 1.000 78.28000  ? 217 PRO C CG  1 
ATOM   8677  C  CD  . PRO C  1 186 ? 27.23700  19.29700  -12.92000 1.000 82.72000  ? 217 PRO C CD  1 
ATOM   8678  N  N   . ALA C  1 187 ? 28.38000  18.44700  -17.45800 1.000 75.45000  ? 218 ALA C N   1 
ATOM   8679  C  CA  . ALA C  1 187 ? 29.49000  18.15200  -18.35500 1.000 71.86000  ? 218 ALA C CA  1 
ATOM   8680  C  C   . ALA C  1 187 ? 30.21800  19.40400  -18.81700 1.000 70.07000  ? 218 ALA C C   1 
ATOM   8681  O  O   . ALA C  1 187 ? 31.39400  19.32300  -19.19600 1.000 75.36000  ? 218 ALA C O   1 
ATOM   8682  C  CB  . ALA C  1 187 ? 28.98600  17.35800  -19.56200 1.000 76.20000  ? 218 ALA C CB  1 
ATOM   8683  N  N   . ASN C  1 188 ? 29.53500  20.54500  -18.85100 1.000 71.42000  ? 219 ASN C N   1 
ATOM   8684  C  CA  . ASN C  1 188 ? 30.10700  21.79800  -19.36200 1.000 73.38000  ? 219 ASN C CA  1 
ATOM   8685  C  C   . ASN C  1 188 ? 30.76100  21.59700  -20.72500 1.000 67.53000  ? 219 ASN C C   1 
ATOM   8686  O  O   . ASN C  1 188 ? 31.91700  21.95500  -20.94600 1.000 61.36000  ? 219 ASN C O   1 
ATOM   8687  C  CB  . ASN C  1 188 ? 31.10300  22.42400  -18.37600 1.000 66.51000  ? 219 ASN C CB  1 
ATOM   8688  C  CG  . ASN C  1 188 ? 30.45300  22.80700  -17.05100 1.000 73.70000  ? 219 ASN C CG  1 
ATOM   8689  O  OD1 . ASN C  1 188 ? 29.70100  23.77800  -16.98100 1.000 74.83000  ? 219 ASN C OD1 1 
ATOM   8690  N  ND2 . ASN C  1 188 ? 30.77800  22.07200  -15.98700 1.000 73.24000  ? 219 ASN C ND2 1 
ATOM   8691  N  N   . GLU C  1 189 ? 30.00100  21.01600  -21.64900 1.000 71.62000  ? 220 GLU C N   1 
ATOM   8692  C  CA  . GLU C  1 189 ? 30.49200  20.81900  -23.00500 1.000 67.52000  ? 220 GLU C CA  1 
ATOM   8693  C  C   . GLU C  1 189 ? 30.63800  22.16800  -23.70500 1.000 66.07000  ? 220 GLU C C   1 
ATOM   8694  O  O   . GLU C  1 189 ? 29.84800  23.09100  -23.47400 1.000 69.57000  ? 220 GLU C O   1 
ATOM   8695  C  CB  . GLU C  1 189 ? 29.54700  19.90600  -23.78200 1.000 66.45000  ? 220 GLU C CB  1 
ATOM   8696  C  CG  . GLU C  1 189 ? 29.97500  19.63500  -25.22200 1.000 69.22000  ? 220 GLU C CG  1 
ATOM   8697  C  CD  . GLU C  1 189 ? 31.39000  19.07600  -25.30100 1.000 70.61000  ? 220 GLU C CD  1 
ATOM   8698  O  OE1 . GLU C  1 189 ? 31.62700  17.97500  -24.76100 1.000 59.71000  ? 220 GLU C OE1 1 
ATOM   8699  O  OE2 . GLU C  1 189 ? 32.26200  19.72600  -25.91700 1.000 73.42000  ? 220 GLU C OE2 1 
ATOM   8700  N  N   . THR C  1 190 ? 31.66700  22.29500  -24.54800 1.000 65.53000  ? 221 THR C N   1 
ATOM   8701  C  CA  . THR C  1 190 ? 31.92300  23.55300  -25.23800 1.000 64.14000  ? 221 THR C CA  1 
ATOM   8702  C  C   . THR C  1 190 ? 32.07700  23.43500  -26.74800 1.000 62.65000  ? 221 THR C C   1 
ATOM   8703  O  O   . THR C  1 190 ? 32.38300  24.44000  -27.39700 1.000 70.44000  ? 221 THR C O   1 
ATOM   8704  C  CB  . THR C  1 190 ? 33.18300  24.23100  -24.66900 1.000 69.30000  ? 221 THR C CB  1 
ATOM   8705  O  OG1 . THR C  1 190 ? 34.32700  23.39100  -24.87000 1.000 74.18000  ? 221 THR C OG1 1 
ATOM   8706  C  CG2 . THR C  1 190 ? 33.01500  24.48200  -23.18600 1.000 67.47000  ? 221 THR C CG2 1 
ATOM   8707  N  N   . GLU C  1 191 ? 31.89800  22.25500  -27.33100 1.000 71.23000  ? 222 GLU C N   1 
ATOM   8708  C  CA  . GLU C  1 191 ? 32.04000  22.10200  -28.77400 1.000 70.60000  ? 222 GLU C CA  1 
ATOM   8709  C  C   . GLU C  1 191 ? 30.89900  21.24200  -29.30000 1.000 67.09000  ? 222 GLU C C   1 
ATOM   8710  O  O   . GLU C  1 191 ? 30.18000  20.60100  -28.52800 1.000 64.41000  ? 222 GLU C O   1 
ATOM   8711  C  CB  . GLU C  1 191 ? 33.40600  21.51500  -29.14400 1.000 71.98000  ? 222 GLU C CB  1 
ATOM   8712  C  CG  . GLU C  1 191 ? 33.67000  20.14900  -28.56000 1.000 74.04000  ? 222 GLU C CG  1 
ATOM   8713  C  CD  . GLU C  1 191 ? 35.08200  19.67000  -28.83300 1.000 76.66000  ? 222 GLU C CD  1 
ATOM   8714  O  OE1 . GLU C  1 191 ? 35.72000  20.21400  -29.76300 1.000 73.70000  ? 222 GLU C OE1 1 
ATOM   8715  O  OE2 . GLU C  1 191 ? 35.54900  18.75500  -28.11400 1.000 71.63000  ? 222 GLU C OE2 1 
ATOM   8716  N  N   . TYR C  1 192 ? 30.69100  21.31100  -30.62100 1.000 63.85000  ? 223 TYR C N   1 
ATOM   8717  C  CA  . TYR C  1 192 ? 29.82500  20.39500  -31.36200 1.000 65.71000  ? 223 TYR C CA  1 
ATOM   8718  C  C   . TYR C  1 192 ? 29.87900  18.98400  -30.79600 1.000 69.87000  ? 223 TYR C C   1 
ATOM   8719  O  O   . TYR C  1 192 ? 30.90200  18.29900  -30.92100 1.000 69.61000  ? 223 TYR C O   1 
ATOM   8720  C  CB  . TYR C  1 192 ? 30.24000  20.39000  -32.82900 1.000 69.59000  ? 223 TYR C CB  1 
ATOM   8721  C  CG  . TYR C  1 192 ? 29.33500  19.64700  -33.78100 1.000 70.15000  ? 223 TYR C CG  1 
ATOM   8722  C  CD1 . TYR C  1 192 ? 27.97200  19.96300  -33.87700 1.000 70.52000  ? 223 TYR C CD1 1 
ATOM   8723  C  CD2 . TYR C  1 192 ? 29.86200  18.72000  -34.67600 1.000 67.40000  ? 223 TYR C CD2 1 
ATOM   8724  C  CE1 . TYR C  1 192 ? 27.14400  19.31100  -34.78900 1.000 65.84000  ? 223 TYR C CE1 1 
ATOM   8725  C  CE2 . TYR C  1 192 ? 29.05100  18.07100  -35.59100 1.000 71.53000  ? 223 TYR C CE2 1 
ATOM   8726  C  CZ  . TYR C  1 192 ? 27.69400  18.37200  -35.63900 1.000 69.10000  ? 223 TYR C CZ  1 
ATOM   8727  O  OH  . TYR C  1 192 ? 26.89800  17.72900  -36.54500 1.000 71.72000  ? 223 TYR C OH  1 
ATOM   8728  N  N   . ILE C  1 193 ? 28.76100  18.52400  -30.23100 1.000 59.61000  ? 224 ILE C N   1 
ATOM   8729  C  CA  . ILE C  1 193 ? 28.81500  17.40400  -29.30100 1.000 61.93000  ? 224 ILE C CA  1 
ATOM   8730  C  C   . ILE C  1 193 ? 29.31000  16.13900  -29.98200 1.000 66.38000  ? 224 ILE C C   1 
ATOM   8731  O  O   . ILE C  1 193 ? 29.83000  15.23900  -29.31500 1.000 69.01000  ? 224 ILE C O   1 
ATOM   8732  C  CB  . ILE C  1 193 ? 27.44500  17.20300  -28.64300 1.000 66.49000  ? 224 ILE C CB  1 
ATOM   8733  C  CG1 . ILE C  1 193 ? 26.40900  16.74300  -29.67300 1.000 61.15000  ? 224 ILE C CG1 1 
ATOM   8734  C  CG2 . ILE C  1 193 ? 26.99600  18.49900  -28.01800 1.000 63.49000  ? 224 ILE C CG2 1 
ATOM   8735  C  CD1 . ILE C  1 193 ? 25.06300  16.48800  -29.05000 1.000 57.60000  ? 224 ILE C CD1 1 
ATOM   8736  N  N   . THR C  1 194 ? 29.14900  16.03500  -31.30300 1.000 64.97000  ? 225 THR C N   1 
ATOM   8737  C  CA  . THR C  1 194 ? 29.75600  14.92100  -32.02600 1.000 64.41000  ? 225 THR C CA  1 
ATOM   8738  C  C   . THR C  1 194 ? 31.26900  14.91900  -31.84700 1.000 68.12000  ? 225 THR C C   1 
ATOM   8739  O  O   . THR C  1 194 ? 31.86500  13.88400  -31.52500 1.000 69.94000  ? 225 THR C O   1 
ATOM   8740  C  CB  . THR C  1 194 ? 29.36800  14.98600  -33.50600 1.000 58.18000  ? 225 THR C CB  1 
ATOM   8741  O  OG1 . THR C  1 194 ? 27.96300  14.74800  -33.63400 1.000 58.66000  ? 225 THR C OG1 1 
ATOM   8742  C  CG2 . THR C  1 194 ? 30.11700  13.95400  -34.32200 1.000 57.18000  ? 225 THR C CG2 1 
ATOM   8743  N  N   . ASP C  1 195 ? 31.90600  16.08300  -32.01600 1.000 65.97000  ? 226 ASP C N   1 
ATOM   8744  C  CA  . ASP C  1 195 ? 33.34100  16.18100  -31.76300 1.000 66.95000  ? 226 ASP C CA  1 
ATOM   8745  C  C   . ASP C  1 195 ? 33.64700  16.00100  -30.27900 1.000 66.85000  ? 226 ASP C C   1 
ATOM   8746  O  O   . ASP C  1 195 ? 34.67300  15.41400  -29.91500 1.000 69.94000  ? 226 ASP C O   1 
ATOM   8747  C  CB  . ASP C  1 195 ? 33.88800  17.51200  -32.28800 1.000 65.52000  ? 226 ASP C CB  1 
ATOM   8748  C  CG  . ASP C  1 195 ? 33.85800  17.59300  -33.81400 1.000 69.03000  ? 226 ASP C CG  1 
ATOM   8749  O  OD1 . ASP C  1 195 ? 33.67100  16.54300  -34.46000 1.000 73.39000  ? 226 ASP C OD1 1 
ATOM   8750  O  OD2 . ASP C  1 195 ? 34.07300  18.68700  -34.37100 1.000 70.80000  ? 226 ASP C OD2 1 
ATOM   8751  N  N   . GLY C  1 196 ? 32.76700  16.49800  -29.41100 1.000 63.82000  ? 227 GLY C N   1 
ATOM   8752  C  CA  . GLY C  1 196 ? 32.94300  16.29100  -27.98400 1.000 62.71000  ? 227 GLY C CA  1 
ATOM   8753  C  C   . GLY C  1 196 ? 32.83300  14.83000  -27.58800 1.000 69.15000  ? 227 GLY C C   1 
ATOM   8754  O  O   . GLY C  1 196 ? 33.51300  14.37300  -26.66400 1.000 65.00000  ? 227 GLY C O   1 
ATOM   8755  N  N   . PHE C  1 197 ? 31.92100  14.09400  -28.23400 1.000 65.39000  ? 228 PHE C N   1 
ATOM   8756  C  CA  . PHE C  1 197 ? 31.79000  12.66700  -27.96800 1.000 62.23000  ? 228 PHE C CA  1 
ATOM   8757  C  C   . PHE C  1 197 ? 33.01700  11.89500  -28.44200 1.000 64.52000  ? 228 PHE C C   1 
ATOM   8758  O  O   . PHE C  1 197 ? 33.45300  10.94800  -27.77600 1.000 62.09000  ? 228 PHE C O   1 
ATOM   8759  C  CB  . PHE C  1 197 ? 30.52500  12.12300  -28.64100 1.000 64.14000  ? 228 PHE C CB  1 
ATOM   8760  C  CG  . PHE C  1 197 ? 29.24500  12.63300  -28.03600 1.000 63.47000  ? 228 PHE C CG  1 
ATOM   8761  C  CD1 . PHE C  1 197 ? 29.16400  12.89100  -26.67700 1.000 66.19000  ? 228 PHE C CD1 1 
ATOM   8762  C  CD2 . PHE C  1 197 ? 28.13000  12.85700  -28.81800 1.000 63.27000  ? 228 PHE C CD2 1 
ATOM   8763  C  CE1 . PHE C  1 197 ? 27.99800  13.35600  -26.10600 1.000 57.50000  ? 228 PHE C CE1 1 
ATOM   8764  C  CE2 . PHE C  1 197 ? 26.96000  13.32600  -28.25600 1.000 65.09000  ? 228 PHE C CE2 1 
ATOM   8765  C  CZ  . PHE C  1 197 ? 26.89300  13.57200  -26.89300 1.000 66.00000  ? 228 PHE C CZ  1 
ATOM   8766  N  N   . SER C  1 198 ? 33.58500  12.27700  -29.59100 1.000 61.20000  ? 229 SER C N   1 
ATOM   8767  C  CA  . SER C  1 198 ? 34.81300  11.63500  -30.05100 1.000 60.24000  ? 229 SER C CA  1 
ATOM   8768  C  C   . SER C  1 198 ? 35.96200  11.91300  -29.09000 1.000 65.75000  ? 229 SER C C   1 
ATOM   8769  O  O   . SER C  1 198 ? 36.72500  11.00800  -28.74000 1.000 66.27000  ? 229 SER C O   1 
ATOM   8770  C  CB  . SER C  1 198 ? 35.16900  12.11200  -31.45700 1.000 59.20000  ? 229 SER C CB  1 
ATOM   8771  O  OG  . SER C  1 198 ? 34.08000  11.95800  -32.34500 1.000 65.24000  ? 229 SER C OG  1 
ATOM   8772  N  N   . ARG C  1 199 ? 36.09100  13.16400  -28.64900 1.000 65.95000  ? 230 ARG C N   1 
ATOM   8773  C  CA  . ARG C  1 199 ? 37.14200  13.53100  -27.70800 1.000 65.71000  ? 230 ARG C CA  1 
ATOM   8774  C  C   . ARG C  1 199 ? 37.03800  12.71200  -26.42500 1.000 60.47000  ? 230 ARG C C   1 
ATOM   8775  O  O   . ARG C  1 199 ? 38.05100  12.25700  -25.88400 1.000 62.43000  ? 230 ARG C O   1 
ATOM   8776  C  CB  . ARG C  1 199 ? 37.01600  15.02300  -27.39500 1.000 68.51000  ? 230 ARG C CB  1 
ATOM   8777  C  CG  . ARG C  1 199 ? 37.90300  15.55300  -26.30000 1.000 62.85000  ? 230 ARG C CG  1 
ATOM   8778  C  CD  . ARG C  1 199 ? 37.31300  16.84600  -25.74600 1.000 66.83000  ? 230 ARG C CD  1 
ATOM   8779  N  NE  . ARG C  1 199 ? 36.07500  16.58900  -25.00700 1.000 73.07000  ? 230 ARG C NE  1 
ATOM   8780  C  CZ  . ARG C  1 199 ? 34.98200  17.34600  -25.05400 1.000 74.38000  ? 230 ARG C CZ  1 
ATOM   8781  N  NH1 . ARG C  1 199 ? 34.90800  18.40900  -25.84200 1.000 72.17000  ? 230 ARG C NH1 1 
ATOM   8782  N  NH2 . ARG C  1 199 ? 33.93700  17.03100  -24.28800 1.000 64.58000  ? 230 ARG C NH2 1 
ATOM   8783  N  N   . GLU C  1 200 ? 35.81100  12.49700  -25.93500 1.000 61.06000  ? 231 GLU C N   1 
ATOM   8784  C  CA  . GLU C  1 200 ? 35.62600  11.70500  -24.72400 1.000 64.67000  ? 231 GLU C CA  1 
ATOM   8785  C  C   . GLU C  1 200 ? 35.95000  10.23800  -24.96500 1.000 63.88000  ? 231 GLU C C   1 
ATOM   8786  O  O   . GLU C  1 200 ? 36.45700  9.56600   -24.06400 1.000 59.28000  ? 231 GLU C O   1 
ATOM   8787  C  CB  . GLU C  1 200 ? 34.19500  11.85200  -24.19300 1.000 62.15000  ? 231 GLU C CB  1 
ATOM   8788  C  CG  . GLU C  1 200 ? 33.88600  13.23700  -23.65600 1.000 68.40000  ? 231 GLU C CG  1 
ATOM   8789  C  CD  . GLU C  1 200 ? 34.82800  13.65900  -22.54400 1.000 73.26000  ? 231 GLU C CD  1 
ATOM   8790  O  OE1 . GLU C  1 200 ? 34.99300  12.88600  -21.56700 1.000 73.42000  ? 231 GLU C OE1 1 
ATOM   8791  O  OE2 . GLU C  1 200 ? 35.44600  14.74300  -22.67600 1.000 68.46000  ? 231 GLU C OE2 1 
ATOM   8792  N  N   . ALA C  1 201 ? 35.66800  9.72100   -26.16400 1.000 56.54000  ? 232 ALA C N   1 
ATOM   8793  C  CA  . ALA C  1 201 ? 36.07400  8.35700   -26.47200 1.000 62.07000  ? 232 ALA C CA  1 
ATOM   8794  C  C   . ALA C  1 201 ? 37.59100  8.23200   -26.43100 1.000 64.77000  ? 232 ALA C C   1 
ATOM   8795  O  O   . ALA C  1 201 ? 38.12600  7.25900   -25.88900 1.000 66.74000  ? 232 ALA C O   1 
ATOM   8796  C  CB  . ALA C  1 201 ? 35.52500  7.93400   -27.83700 1.000 55.00000  ? 232 ALA C CB  1 
ATOM   8797  N  N   . ILE C  1 202 ? 38.29600  9.23000   -26.96500 1.000 62.25000  ? 233 ILE C N   1 
ATOM   8798  C  CA  . ILE C  1 202 ? 39.75400  9.23100   -26.92500 1.000 64.49000  ? 233 ILE C CA  1 
ATOM   8799  C  C   . ILE C  1 202 ? 40.25200  9.25500   -25.48600 1.000 65.15000  ? 233 ILE C C   1 
ATOM   8800  O  O   . ILE C  1 202 ? 41.19100  8.53700   -25.12900 1.000 68.45000  ? 233 ILE C O   1 
ATOM   8801  C  CB  . ILE C  1 202 ? 40.31200  10.41500  -27.73700 1.000 68.17000  ? 233 ILE C CB  1 
ATOM   8802  C  CG1 . ILE C  1 202 ? 40.12200  10.16600  -29.23900 1.000 67.13000  ? 233 ILE C CG1 1 
ATOM   8803  C  CG2 . ILE C  1 202 ? 41.79800  10.63900  -27.41800 1.000 64.87000  ? 233 ILE C CG2 1 
ATOM   8804  C  CD1 . ILE C  1 202 ? 40.24600  11.41800  -30.10100 1.000 67.71000  ? 233 ILE C CD1 1 
ATOM   8805  N  N   . LYS C  1 203 ? 39.65100  10.09100  -24.64100 1.000 64.48000  ? 234 LYS C N   1 
ATOM   8806  C  CA  . LYS C  1 203 ? 40.08500  10.14300  -23.24900 1.000 61.04000  ? 234 LYS C CA  1 
ATOM   8807  C  C   . LYS C  1 203 ? 39.84200  8.81600   -22.53900 1.000 60.02000  ? 234 LYS C C   1 
ATOM   8808  O  O   . LYS C  1 203 ? 40.67700  8.36300   -21.75000 1.000 67.45000  ? 234 LYS C O   1 
ATOM   8809  C  CB  . LYS C  1 203 ? 39.40400  11.29700  -22.51300 1.000 59.66000  ? 234 LYS C CB  1 
ATOM   8810  C  CG  . LYS C  1 203 ? 39.75200  11.36400  -21.04400 1.000 61.93000  ? 234 LYS C CG  1 
ATOM   8811  C  CD  . LYS C  1 203 ? 39.20900  12.60900  -20.37500 1.000 63.37000  ? 234 LYS C CD  1 
ATOM   8812  C  CE  . LYS C  1 203 ? 38.09100  12.28500  -19.42700 1.000 69.24000  ? 234 LYS C CE  1 
ATOM   8813  N  NZ  . LYS C  1 203 ? 38.04900  13.27400  -18.31500 1.000 76.30000  ? 234 LYS C NZ  1 
ATOM   8814  N  N   . ASN C  1 204 ? 38.69100  8.19900   -22.76400 1.000 60.05000  ? 235 ASN C N   1 
ATOM   8815  C  CA  . ASN C  1 204 ? 38.41700  6.94300   -22.08400 1.000 62.99000  ? 235 ASN C CA  1 
ATOM   8816  C  C   . ASN C  1 204 ? 39.29600  5.81700   -22.62000 1.000 66.63000  ? 235 ASN C C   1 
ATOM   8817  O  O   . ASN C  1 204 ? 39.59900  4.87200   -21.88700 1.000 62.95000  ? 235 ASN C O   1 
ATOM   8818  C  CB  . ASN C  1 204 ? 36.93500  6.59700   -22.19500 1.000 60.96000  ? 235 ASN C CB  1 
ATOM   8819  C  CG  . ASN C  1 204 ? 36.07600  7.38700   -21.20700 1.000 65.78000  ? 235 ASN C CG  1 
ATOM   8820  O  OD1 . ASN C  1 204 ? 35.89400  6.98400   -20.05800 1.000 67.42000  ? 235 ASN C OD1 1 
ATOM   8821  N  ND2 . ASN C  1 204 ? 35.54700  8.51600   -21.65400 1.000 65.17000  ? 235 ASN C ND2 1 
ATOM   8822  N  N   . ILE C  1 205 ? 39.71300  5.89200   -23.88600 1.000 64.12000  ? 236 ILE C N   1 
ATOM   8823  C  CA  . ILE C  1 205 ? 40.67800  4.92100   -24.38900 1.000 63.76000  ? 236 ILE C CA  1 
ATOM   8824  C  C   . ILE C  1 205 ? 42.01700  5.10200   -23.68700 1.000 62.87000  ? 236 ILE C C   1 
ATOM   8825  O  O   . ILE C  1 205 ? 42.65600  4.12500   -23.28000 1.000 64.29000  ? 236 ILE C O   1 
ATOM   8826  C  CB  . ILE C  1 205 ? 40.81900  5.04100   -25.91800 1.000 63.05000  ? 236 ILE C CB  1 
ATOM   8827  C  CG1 . ILE C  1 205 ? 39.59200  4.47100   -26.61900 1.000 60.08000  ? 236 ILE C CG1 1 
ATOM   8828  C  CG2 . ILE C  1 205 ? 42.07600  4.34800   -26.40900 1.000 62.64000  ? 236 ILE C CG2 1 
ATOM   8829  C  CD1 . ILE C  1 205 ? 39.50200  4.81500   -28.08100 1.000 63.74000  ? 236 ILE C CD1 1 
ATOM   8830  N  N   . LYS C  1 206 ? 42.43900  6.35700   -23.49400 1.000 62.64000  ? 237 LYS C N   1 
ATOM   8831  C  CA  . LYS C  1 206 ? 43.68000  6.63100   -22.77400 1.000 64.79000  ? 237 LYS C CA  1 
ATOM   8832  C  C   . LYS C  1 206 ? 43.58100  6.26100   -21.29600 1.000 64.22000  ? 237 LYS C C   1 
ATOM   8833  O  O   . LYS C  1 206 ? 44.57900  5.82800   -20.71600 1.000 65.81000  ? 237 LYS C O   1 
ATOM   8834  C  CB  . LYS C  1 206 ? 44.09600  8.10100   -22.93900 1.000 60.86000  ? 237 LYS C CB  1 
ATOM   8835  C  CG  . LYS C  1 206 ? 44.65100  8.42800   -24.32900 1.000 58.98000  ? 237 LYS C CG  1 
ATOM   8836  C  CD  . LYS C  1 206 ? 44.77000  9.93200   -24.57200 1.000 62.96000  ? 237 LYS C CD  1 
ATOM   8837  C  CE  . LYS C  1 206 ? 45.71500  10.23500  -25.73300 1.000 66.96000  ? 237 LYS C CE  1 
ATOM   8838  N  NZ  . LYS C  1 206 ? 45.67200  11.63600  -26.25900 1.000 68.84000  ? 237 LYS C NZ  1 
ATOM   8839  N  N   . ILE C  1 207 ? 42.40500  6.39300   -20.67600 1.000 58.43000  ? 238 ILE C N   1 
ATOM   8840  C  CA  . ILE C  1 207 ? 42.26100  5.98800   -19.27500 1.000 64.59000  ? 238 ILE C CA  1 
ATOM   8841  C  C   . ILE C  1 207 ? 42.49300  4.48400   -19.11900 1.000 63.32000  ? 238 ILE C C   1 
ATOM   8842  O  O   . ILE C  1 207 ? 43.23300  4.03600   -18.23500 1.000 62.93000  ? 238 ILE C O   1 
ATOM   8843  C  CB  . ILE C  1 207 ? 40.88700  6.41500   -18.72100 1.000 67.13000  ? 238 ILE C CB  1 
ATOM   8844  C  CG1 . ILE C  1 207 ? 40.81100  7.93600   -18.55800 1.000 62.91000  ? 238 ILE C CG1 1 
ATOM   8845  C  CG2 . ILE C  1 207 ? 40.59000  5.74000   -17.39300 1.000 60.21000  ? 238 ILE C CG2 1 
ATOM   8846  C  CD1 . ILE C  1 207 ? 39.42400  8.44700   -18.21100 1.000 59.59000  ? 238 ILE C CD1 1 
ATOM   8847  N  N   . ALA C  1 208 ? 41.81700  3.68000   -19.93600 1.000 66.27000  ? 239 ALA C N   1 
ATOM   8848  C  CA  . ALA C  1 208 ? 41.98000  2.23200   -19.85400 1.000 64.74000  ? 239 ALA C CA  1 
ATOM   8849  C  C   . ALA C  1 208 ? 43.41300  1.80600   -20.14500 1.000 63.00000  ? 239 ALA C C   1 
ATOM   8850  O  O   . ALA C  1 208 ? 43.93600  0.88400   -19.50900 1.000 63.77000  ? 239 ALA C O   1 
ATOM   8851  C  CB  . ALA C  1 208 ? 41.01300  1.54600   -20.81600 1.000 63.72000  ? 239 ALA C CB  1 
ATOM   8852  N  N   . ALA C  1 209 ? 44.06900  2.46700   -21.09700 1.000 63.07000  ? 240 ALA C N   1 
ATOM   8853  C  CA  . ALA C  1 209 ? 45.45000  2.12000   -21.39600 1.000 63.31000  ? 240 ALA C CA  1 
ATOM   8854  C  C   . ALA C  1 209 ? 46.35000  2.36700   -20.18800 1.000 67.49000  ? 240 ALA C C   1 
ATOM   8855  O  O   . ALA C  1 209 ? 47.19300  1.52900   -19.84700 1.000 68.02000  ? 240 ALA C O   1 
ATOM   8856  C  CB  . ALA C  1 209 ? 45.93500  2.90500   -22.61600 1.000 60.70000  ? 240 ALA C CB  1 
ATOM   8857  N  N   . ALA C  1 210 ? 46.17900  3.50400   -19.51500 1.000 64.23000  ? 241 ALA C N   1 
ATOM   8858  C  CA  . ALA C  1 210 ? 47.00000  3.76400   -18.34100 1.000 63.46000  ? 241 ALA C CA  1 
ATOM   8859  C  C   . ALA C  1 210 ? 46.68900  2.77300   -17.22700 1.000 67.39000  ? 241 ALA C C   1 
ATOM   8860  O  O   . ALA C  1 210 ? 47.58100  2.41900   -16.44700 1.000 68.99000  ? 241 ALA C O   1 
ATOM   8861  C  CB  . ALA C  1 210 ? 46.80300  5.20000   -17.86300 1.000 62.04000  ? 241 ALA C CB  1 
ATOM   8862  N  N   . LYS C  1 211 ? 45.43300  2.32400   -17.12600 1.000 61.98000  ? 242 LYS C N   1 
ATOM   8863  C  CA  . LYS C  1 211 ? 45.08600  1.30900   -16.14400 1.000 62.90000  ? 242 LYS C CA  1 
ATOM   8864  C  C   . LYS C  1 211 ? 45.55900  -0.08000  -16.54700 1.000 64.31000  ? 242 LYS C C   1 
ATOM   8865  O  O   . LYS C  1 211 ? 45.44600  -1.00600  -15.74200 1.000 60.89000  ? 242 LYS C O   1 
ATOM   8866  C  CB  . LYS C  1 211 ? 43.57400  1.28600   -15.91300 1.000 65.53000  ? 242 LYS C CB  1 
ATOM   8867  C  CG  . LYS C  1 211 ? 43.00100  2.56300   -15.30600 1.000 65.74000  ? 242 LYS C CG  1 
ATOM   8868  C  CD  . LYS C  1 211 ? 41.48700  2.49900   -15.23400 1.000 64.44000  ? 242 LYS C CD  1 
ATOM   8869  C  CE  . LYS C  1 211 ? 40.93600  3.02800   -13.92400 1.000 59.09000  ? 242 LYS C CE  1 
ATOM   8870  N  NZ  . LYS C  1 211 ? 39.98100  2.04300   -13.33700 1.000 69.69000  ? 242 LYS C NZ  1 
ATOM   8871  N  N   . LYS C  1 212 ? 46.10800  -0.23800  -17.75400 1.000 67.45000  ? 243 LYS C N   1 
ATOM   8872  C  CA  . LYS C  1 212 ? 46.43500  -1.54900  -18.31200 1.000 67.47000  ? 243 LYS C CA  1 
ATOM   8873  C  C   . LYS C  1 212 ? 45.26600  -2.51500  -18.13100 1.000 64.87000  ? 243 LYS C C   1 
ATOM   8874  O  O   . LYS C  1 212 ? 45.41500  -3.63000  -17.63000 1.000 69.23000  ? 243 LYS C O   1 
ATOM   8875  C  CB  . LYS C  1 212 ? 47.71700  -2.10300  -17.68900 1.000 71.09000  ? 243 LYS C CB  1 
ATOM   8876  C  CG  . LYS C  1 212 ? 48.90600  -1.13500  -17.72300 1.000 72.18000  ? 243 LYS C CG  1 
ATOM   8877  C  CD  . LYS C  1 212 ? 50.23900  -1.89700  -17.68800 1.000 77.37000  ? 243 LYS C CD  1 
ATOM   8878  C  CE  . LYS C  1 212 ? 51.41300  -1.01300  -17.27700 1.000 78.32000  ? 243 LYS C CE  1 
ATOM   8879  N  NZ  . LYS C  1 212 ? 51.35300  -0.68400  -15.82700 1.000 78.36000  ? 243 LYS C NZ  1 
ATOM   8880  N  N   . GLN C  1 213 ? 44.08100  -2.05500  -18.53300 1.000 67.70000  ? 244 GLN C N   1 
ATOM   8881  C  CA  . GLN C  1 213 ? 42.81000  -2.74200  -18.39000 1.000 64.09000  ? 244 GLN C CA  1 
ATOM   8882  C  C   . GLN C  1 213 ? 42.10000  -2.81700  -19.73500 1.000 67.64000  ? 244 GLN C C   1 
ATOM   8883  O  O   . GLN C  1 213 ? 42.17000  -1.86700  -20.52600 1.000 71.71000  ? 244 GLN C O   1 
ATOM   8884  C  CB  . GLN C  1 213 ? 41.93700  -2.00300  -17.37100 1.000 63.12000  ? 244 GLN C CB  1 
ATOM   8885  C  CG  . GLN C  1 213 ? 40.80000  -2.80100  -16.80800 1.000 64.50000  ? 244 GLN C CG  1 
ATOM   8886  C  CD  . GLN C  1 213 ? 40.04800  -2.04800  -15.72700 1.000 69.71000  ? 244 GLN C CD  1 
ATOM   8887  O  OE1 . GLN C  1 213 ? 40.43800  -0.95200  -15.33200 1.000 74.34000  ? 244 GLN C OE1 1 
ATOM   8888  N  NE2 . GLN C  1 213 ? 38.96400  -2.63700  -15.24100 1.000 70.55000  ? 244 GLN C NE2 1 
ATOM   8889  N  N   . PRO C  1 214 ? 41.45600  -3.93900  -20.05500 1.000 67.60000  ? 245 PRO C N   1 
ATOM   8890  C  CA  . PRO C  1 214 ? 40.64500  -3.98800  -21.28200 1.000 64.38000  ? 245 PRO C CA  1 
ATOM   8891  C  C   . PRO C  1 214 ? 39.40200  -3.11900  -21.15400 1.000 65.23000  ? 245 PRO C C   1 
ATOM   8892  O  O   . PRO C  1 214 ? 38.70300  -3.15500  -20.13800 1.000 63.85000  ? 245 PRO C O   1 
ATOM   8893  C  CB  . PRO C  1 214 ? 40.29100  -5.47400  -21.40500 1.000 66.92000  ? 245 PRO C CB  1 
ATOM   8894  C  CG  . PRO C  1 214 ? 40.37800  -5.99200  -19.98800 1.000 63.94000  ? 245 PRO C CG  1 
ATOM   8895  C  CD  . PRO C  1 214 ? 41.49800  -5.23700  -19.36000 1.000 62.89000  ? 245 PRO C CD  1 
ATOM   8896  N  N   . PHE C  1 215 ? 39.09100  -2.37000  -22.21400 1.000 64.80000  ? 246 PHE C N   1 
ATOM   8897  C  CA  . PHE C  1 215 ? 37.97200  -1.43700  -22.16600 1.000 64.76000  ? 246 PHE C CA  1 
ATOM   8898  C  C   . PHE C  1 215 ? 36.77900  -1.95500  -22.94800 1.000 60.84000  ? 246 PHE C C   1 
ATOM   8899  O  O   . PHE C  1 215 ? 36.92400  -2.73200  -23.89400 1.000 62.28000  ? 246 PHE C O   1 
ATOM   8900  C  CB  . PHE C  1 215 ? 38.35200  -0.02700  -22.66900 1.000 60.18000  ? 246 PHE C CB  1 
ATOM   8901  C  CG  . PHE C  1 215 ? 38.66100  0.07600   -24.15000 1.000 57.82000  ? 246 PHE C CG  1 
ATOM   8902  C  CD1 . PHE C  1 215 ? 37.66700  0.00300   -25.10900 1.000 58.93000  ? 246 PHE C CD1 1 
ATOM   8903  C  CD2 . PHE C  1 215 ? 39.95000  0.33300   -24.57200 1.000 59.07000  ? 246 PHE C CD2 1 
ATOM   8904  C  CE1 . PHE C  1 215 ? 37.96500  0.14100   -26.46200 1.000 60.19000  ? 246 PHE C CE1 1 
ATOM   8905  C  CE2 . PHE C  1 215 ? 40.25500  0.47200   -25.92300 1.000 59.93000  ? 246 PHE C CE2 1 
ATOM   8906  C  CZ  . PHE C  1 215 ? 39.26300  0.37100   -26.86800 1.000 60.75000  ? 246 PHE C CZ  1 
ATOM   8907  N  N   . PHE C  1 216 ? 35.59800  -1.50700  -22.51900 1.000 58.15000  ? 247 PHE C N   1 
ATOM   8908  C  CA  . PHE C  1 216 ? 34.35500  -1.62100  -23.27600 1.000 61.76000  ? 247 PHE C CA  1 
ATOM   8909  C  C   . PHE C  1 216 ? 33.75400  -0.22800  -23.37400 1.000 64.04000  ? 247 PHE C C   1 
ATOM   8910  O  O   . PHE C  1 216 ? 33.31200  0.32600   -22.36200 1.000 63.25000  ? 247 PHE C O   1 
ATOM   8911  C  CB  . PHE C  1 216 ? 33.36800  -2.57200  -22.60500 1.000 63.42000  ? 247 PHE C CB  1 
ATOM   8912  C  CG  . PHE C  1 216 ? 31.97900  -2.50500  -23.18800 1.000 66.71000  ? 247 PHE C CG  1 
ATOM   8913  C  CD1 . PHE C  1 216 ? 31.72000  -3.00300  -24.45500 1.000 66.23000  ? 247 PHE C CD1 1 
ATOM   8914  C  CD2 . PHE C  1 216 ? 30.94200  -1.92100  -22.48100 1.000 63.43000  ? 247 PHE C CD2 1 
ATOM   8915  C  CE1 . PHE C  1 216 ? 30.44600  -2.94600  -24.99600 1.000 67.92000  ? 247 PHE C CE1 1 
ATOM   8916  C  CE2 . PHE C  1 216 ? 29.67300  -1.85100  -23.00900 1.000 67.01000  ? 247 PHE C CE2 1 
ATOM   8917  C  CZ  . PHE C  1 216 ? 29.41800  -2.36700  -24.27500 1.000 69.29000  ? 247 PHE C CZ  1 
ATOM   8918  N  N   . ILE C  1 217 ? 33.73900  0.34200   -24.57700 1.000 59.53000  ? 248 ILE C N   1 
ATOM   8919  C  CA  . ILE C  1 217 ? 33.23200  1.69500   -24.80300 1.000 61.04000  ? 248 ILE C CA  1 
ATOM   8920  C  C   . ILE C  1 217 ? 31.96900  1.64000   -25.64700 1.000 59.80000  ? 248 ILE C C   1 
ATOM   8921  O  O   . ILE C  1 217 ? 32.00400  1.23500   -26.81800 1.000 61.23000  ? 248 ILE C O   1 
ATOM   8922  C  CB  . ILE C  1 217 ? 34.27400  2.57900   -25.49400 1.000 63.23000  ? 248 ILE C CB  1 
ATOM   8923  C  CG1 . ILE C  1 217 ? 35.52100  2.67800   -24.63300 1.000 55.00000  ? 248 ILE C CG1 1 
ATOM   8924  C  CG2 . ILE C  1 217 ? 33.67300  3.95200   -25.77600 1.000 58.00000  ? 248 ILE C CG2 1 
ATOM   8925  C  CD1 . ILE C  1 217 ? 36.62900  3.32500   -25.33600 1.000 58.18000  ? 248 ILE C CD1 1 
ATOM   8926  N  N   . TYR C  1 218 ? 30.88000  2.13700   -25.08800 1.000 55.81000  ? 249 TYR C N   1 
ATOM   8927  C  CA  . TYR C  1 218 ? 29.59400  2.22600   -25.77600 1.000 56.51000  ? 249 TYR C CA  1 
ATOM   8928  C  C   . TYR C  1 218 ? 29.44700  3.67100   -26.25000 1.000 55.53000  ? 249 TYR C C   1 
ATOM   8929  O  O   . TYR C  1 218 ? 28.93700  4.53100   -25.53100 1.000 57.15000  ? 249 TYR C O   1 
ATOM   8930  C  CB  . TYR C  1 218 ? 28.47800  1.81300   -24.82400 1.000 53.69000  ? 249 TYR C CB  1 
ATOM   8931  C  CG  . TYR C  1 218 ? 27.08300  1.88100   -25.38200 1.000 54.09000  ? 249 TYR C CG  1 
ATOM   8932  C  CD1 . TYR C  1 218 ? 26.62700  0.93000   -26.28700 1.000 56.65000  ? 249 TYR C CD1 1 
ATOM   8933  C  CD2 . TYR C  1 218 ? 26.21300  2.89300   -24.99300 1.000 52.83000  ? 249 TYR C CD2 1 
ATOM   8934  C  CE1 . TYR C  1 218 ? 25.33900  0.97500   -26.77700 1.000 55.62000  ? 249 TYR C CE1 1 
ATOM   8935  C  CE2 . TYR C  1 218 ? 24.92900  2.95400   -25.48100 1.000 57.73000  ? 249 TYR C CE2 1 
ATOM   8936  C  CZ  . TYR C  1 218 ? 24.49600  1.99000   -26.37800 1.000 60.66000  ? 249 TYR C CZ  1 
ATOM   8937  O  OH  . TYR C  1 218 ? 23.21600  2.04800   -26.88300 1.000 62.58000  ? 249 TYR C OH  1 
ATOM   8938  N  N   . LEU C  1 219 ? 29.91300  3.93500   -27.47000 1.000 52.40000  ? 250 LEU C N   1 
ATOM   8939  C  CA  . LEU C  1 219 ? 29.97000  5.28400   -28.04100 1.000 49.93000  ? 250 LEU C CA  1 
ATOM   8940  C  C   . LEU C  1 219 ? 28.73700  5.48200   -28.90600 1.000 56.50000  ? 250 LEU C C   1 
ATOM   8941  O  O   . LEU C  1 219 ? 28.73700  5.17000   -30.10000 1.000 54.17000  ? 250 LEU C O   1 
ATOM   8942  C  CB  . LEU C  1 219 ? 31.25300  5.47300   -28.84100 1.000 49.67000  ? 250 LEU C CB  1 
ATOM   8943  C  CG  . LEU C  1 219 ? 31.39400  6.78200   -29.61900 1.000 60.07000  ? 250 LEU C CG  1 
ATOM   8944  C  CD1 . LEU C  1 219 ? 31.04000  7.97800   -28.73800 1.000 52.70000  ? 250 LEU C CD1 1 
ATOM   8945  C  CD2 . LEU C  1 219 ? 32.80000  6.90300   -30.24000 1.000 52.55000  ? 250 LEU C CD2 1 
ATOM   8946  N  N   . ALA C  1 220 ? 27.68600  6.04100   -28.29700 1.000 56.91000  ? 251 ALA C N   1 
ATOM   8947  C  CA  . ALA C  1 220 ? 26.37500  6.18600   -28.93500 1.000 51.05000  ? 251 ALA C CA  1 
ATOM   8948  C  C   . ALA C  1 220 ? 26.18600  7.61500   -29.43700 1.000 50.66000  ? 251 ALA C C   1 
ATOM   8949  O  O   . ALA C  1 220 ? 25.52200  8.44100   -28.80900 1.000 53.97000  ? 251 ALA C O   1 
ATOM   8950  C  CB  . ALA C  1 220 ? 25.25700  5.78800   -27.96900 1.000 60.01000  ? 251 ALA C CB  1 
ATOM   8951  N  N   . TYR C  1 221 ? 26.80000  7.90400   -30.58300 1.000 48.57000  ? 252 TYR C N   1 
ATOM   8952  C  CA  . TYR C  1 221 ? 26.55900  9.16300   -31.28000 1.000 56.03000  ? 252 TYR C CA  1 
ATOM   8953  C  C   . TYR C  1 221 ? 25.06200  9.38000   -31.49700 1.000 62.31000  ? 252 TYR C C   1 
ATOM   8954  O  O   . TYR C  1 221 ? 24.30600  8.42500   -31.71100 1.000 58.15000  ? 252 TYR C O   1 
ATOM   8955  C  CB  . TYR C  1 221 ? 27.25300  9.16700   -32.64100 1.000 49.43000  ? 252 TYR C CB  1 
ATOM   8956  C  CG  . TYR C  1 221 ? 28.75600  9.22100   -32.63600 1.000 54.72000  ? 252 TYR C CG  1 
ATOM   8957  C  CD1 . TYR C  1 221 ? 29.42400  10.37300  -32.26400 1.000 56.24000  ? 252 TYR C CD1 1 
ATOM   8958  C  CD2 . TYR C  1 221 ? 29.51600  8.14300   -33.09600 1.000 58.00000  ? 252 TYR C CD2 1 
ATOM   8959  C  CE1 . TYR C  1 221 ? 30.81200  10.43800  -32.29000 1.000 63.35000  ? 252 TYR C CE1 1 
ATOM   8960  C  CE2 . TYR C  1 221 ? 30.90300  8.20200   -33.13300 1.000 54.61000  ? 252 TYR C CE2 1 
ATOM   8961  C  CZ  . TYR C  1 221 ? 31.54200  9.35600   -32.72600 1.000 63.03000  ? 252 TYR C CZ  1 
ATOM   8962  O  OH  . TYR C  1 221 ? 32.91500  9.45300   -32.75300 1.000 59.40000  ? 252 TYR C OH  1 
ATOM   8963  N  N   . ASN C  1 222 ? 24.61600  10.63900  -31.38900 1.000 60.58000  ? 253 ASN C N   1 
ATOM   8964  C  CA  . ASN C  1 222 ? 23.26100  10.96300  -31.82900 1.000 61.55000  ? 253 ASN C CA  1 
ATOM   8965  C  C   . ASN C  1 222 ? 23.20400  11.33800  -33.30400 1.000 58.99000  ? 253 ASN C C   1 
ATOM   8966  O  O   . ASN C  1 222 ? 22.12100  11.32300  -33.89400 1.000 62.12000  ? 253 ASN C O   1 
ATOM   8967  C  CB  . ASN C  1 222 ? 22.64800  12.07800  -30.97300 1.000 64.40000  ? 253 ASN C CB  1 
ATOM   8968  C  CG  . ASN C  1 222 ? 23.35200  13.41800  -31.13000 1.000 66.49000  ? 253 ASN C CG  1 
ATOM   8969  O  OD1 . ASN C  1 222 ? 24.57100  13.50000  -31.22300 1.000 64.26000  ? 253 ASN C OD1 1 
ATOM   8970  N  ND2 . ASN C  1 222 ? 22.56600  14.48500  -31.12000 1.000 68.62000  ? 253 ASN C ND2 1 
ATOM   8971  N  N   . ALA C  1 223 ? 24.34000  11.63700  -33.92000 1.000 59.34000  ? 254 ALA C N   1 
ATOM   8972  C  CA  . ALA C  1 223 ? 24.36000  11.90300  -35.34500 1.000 54.71000  ? 254 ALA C CA  1 
ATOM   8973  C  C   . ALA C  1 223 ? 23.98600  10.64600  -36.13700 1.000 59.46000  ? 254 ALA C C   1 
ATOM   8974  O  O   . ALA C  1 223 ? 24.27000  9.52100   -35.71500 1.000 60.89000  ? 254 ALA C O   1 
ATOM   8975  C  CB  . ALA C  1 223 ? 25.74600  12.39200  -35.76400 1.000 46.57000  ? 254 ALA C CB  1 
ATOM   8976  N  N   . PRO C  1 224 ? 23.29300  10.80100  -37.26900 1.000 59.72000  ? 255 PRO C N   1 
ATOM   8977  C  CA  . PRO C  1 224 ? 22.69700  12.02600  -37.81300 1.000 58.56000  ? 255 PRO C CA  1 
ATOM   8978  C  C   . PRO C  1 224 ? 21.20500  12.17800  -37.48400 1.000 55.67000  ? 255 PRO C C   1 
ATOM   8979  O  O   . PRO C  1 224 ? 20.45700  12.67900  -38.29700 1.000 59.92000  ? 255 PRO C O   1 
ATOM   8980  C  CB  . PRO C  1 224 ? 22.94800  11.87100  -39.31300 1.000 61.03000  ? 255 PRO C CB  1 
ATOM   8981  C  CG  . PRO C  1 224 ? 22.83900  10.39000  -39.54000 1.000 59.77000  ? 255 PRO C CG  1 
ATOM   8982  C  CD  . PRO C  1 224 ? 23.30800  9.72200   -38.27200 1.000 58.69000  ? 255 PRO C CD  1 
ATOM   8983  N  N   . HIS C  1 225 ? 20.76400  11.75900  -36.30000 1.000 54.21000  ? 256 HIS C N   1 
ATOM   8984  C  CA  . HIS C  1 225 ? 19.39000  11.96100  -35.86300 1.000 54.36000  ? 256 HIS C CA  1 
ATOM   8985  C  C   . HIS C  1 225 ? 19.09000  13.45700  -35.76600 1.000 62.74000  ? 256 HIS C C   1 
ATOM   8986  O  O   . HIS C  1 225 ? 19.98900  14.27600  -35.56300 1.000 60.33000  ? 256 HIS C O   1 
ATOM   8987  C  CB  . HIS C  1 225 ? 19.19800  11.27000  -34.51200 1.000 59.99000  ? 256 HIS C CB  1 
ATOM   8988  C  CG  . HIS C  1 225 ? 17.78200  11.18500  -34.03700 1.000 64.89000  ? 256 HIS C CG  1 
ATOM   8989  N  ND1 . HIS C  1 225 ? 17.07500  12.28300  -33.59600 1.000 67.93000  ? 256 HIS C ND1 1 
ATOM   8990  C  CD2 . HIS C  1 225 ? 16.96600  10.11800  -33.86400 1.000 66.02000  ? 256 HIS C CD2 1 
ATOM   8991  C  CE1 . HIS C  1 225 ? 15.87600  11.89900  -33.19600 1.000 68.85000  ? 256 HIS C CE1 1 
ATOM   8992  N  NE2 . HIS C  1 225 ? 15.78300  10.59100  -33.35100 1.000 69.53000  ? 256 HIS C NE2 1 
ATOM   8993  N  N   . VAL C  1 226 ? 17.81900  13.81700  -35.94100 1.000 63.44000  ? 257 VAL C N   1 
ATOM   8994  C  CA  . VAL C  1 226 ? 17.39800  15.22000  -35.88300 1.000 61.88000  ? 257 VAL C CA  1 
ATOM   8995  C  C   . VAL C  1 226 ? 17.68600  15.79300  -34.50000 1.000 61.15000  ? 257 VAL C C   1 
ATOM   8996  O  O   . VAL C  1 226 ? 17.77900  15.02600  -33.52500 1.000 61.89000  ? 257 VAL C O   1 
ATOM   8997  C  CB  . VAL C  1 226 ? 15.90900  15.38900  -36.24300 1.000 59.94000  ? 257 VAL C CB  1 
ATOM   8998  C  CG1 . VAL C  1 226 ? 15.69500  15.20700  -37.74300 1.000 50.04000  ? 257 VAL C CG1 1 
ATOM   8999  C  CG2 . VAL C  1 226 ? 15.03000  14.45700  -35.40300 1.000 53.19000  ? 257 VAL C CG2 1 
ATOM   9000  N  N   . PRO C  1 227 ? 17.83500  17.13300  -34.35600 1.000 59.65000  ? 258 PRO C N   1 
ATOM   9001  C  CA  . PRO C  1 227 ? 17.73900  18.18600  -35.39000 1.000 60.03000  ? 258 PRO C CA  1 
ATOM   9002  C  C   . PRO C  1 227 ? 18.91600  18.14900  -36.35800 1.000 61.88000  ? 258 PRO C C   1 
ATOM   9003  O  O   . PRO C  1 227 ? 20.01400  17.84100  -35.93000 1.000 56.58000  ? 258 PRO C O   1 
ATOM   9004  C  CB  . PRO C  1 227 ? 17.73700  19.47800  -34.56500 1.000 57.96000  ? 258 PRO C CB  1 
ATOM   9005  C  CG  . PRO C  1 227 ? 18.58700  19.12900  -33.36100 1.000 59.59000  ? 258 PRO C CG  1 
ATOM   9006  C  CD  . PRO C  1 227 ? 18.18000  17.70800  -33.03700 1.000 60.74000  ? 258 PRO C CD  1 
ATOM   9007  N  N   . LEU C  1 228 ? 18.72500  18.40700  -37.65400 1.000 57.18000  ? 259 LEU C N   1 
ATOM   9008  C  CA  . LEU C  1 228 ? 19.84800  18.44800  -38.58600 1.000 54.46000  ? 259 LEU C CA  1 
ATOM   9009  C  C   . LEU C  1 228 ? 20.66200  19.70100  -38.31000 1.000 68.99000  ? 259 LEU C C   1 
ATOM   9010  O  O   . LEU C  1 228 ? 20.30700  20.79700  -38.75000 1.000 63.61000  ? 259 LEU C O   1 
ATOM   9011  C  CB  . LEU C  1 228 ? 19.36800  18.41600  -40.02800 1.000 52.15000  ? 259 LEU C CB  1 
ATOM   9012  C  CG  . LEU C  1 228 ? 18.63300  17.14400  -40.48400 1.000 64.82000  ? 259 LEU C CG  1 
ATOM   9013  C  CD1 . LEU C  1 228 ? 18.23100  17.22100  -41.95800 1.000 56.48000  ? 259 LEU C CD1 1 
ATOM   9014  C  CD2 . LEU C  1 228 ? 19.50000  15.90500  -40.24500 1.000 56.84000  ? 259 LEU C CD2 1 
ATOM   9015  N  N   . GLN C  1 229 ? 21.76500  19.54100  -37.57400 1.000 60.84000  ? 260 GLN C N   1 
ATOM   9016  C  CA  . GLN C  1 229 ? 22.66800  20.63900  -37.25400 1.000 61.49000  ? 260 GLN C CA  1 
ATOM   9017  C  C   . GLN C  1 229 ? 24.09000  20.16700  -37.53100 1.000 69.67000  ? 260 GLN C C   1 
ATOM   9018  O  O   . GLN C  1 229 ? 24.48900  19.08700  -37.07700 1.000 66.82000  ? 260 GLN C O   1 
ATOM   9019  C  CB  . GLN C  1 229 ? 22.52300  21.08700  -35.79600 1.000 57.34000  ? 260 GLN C CB  1 
ATOM   9020  C  CG  . GLN C  1 229 ? 21.14000  21.58800  -35.37000 1.000 62.48000  ? 260 GLN C CG  1 
ATOM   9021  C  CD  . GLN C  1 229 ? 21.07200  21.83600  -33.86000 1.000 69.56000  ? 260 GLN C CD  1 
ATOM   9022  O  OE1 . GLN C  1 229 ? 20.00400  22.06700  -33.29100 1.000 59.75000  ? 260 GLN C OE1 1 
ATOM   9023  N  NE2 . GLN C  1 229 ? 22.23100  21.79100  -33.20800 1.000 72.04000  ? 260 GLN C NE2 1 
ATOM   9024  N  N   . ALA C  1 230 ? 24.85600  20.96900  -38.27000 1.000 71.31000  ? 261 ALA C N   1 
ATOM   9025  C  CA  . ALA C  1 230 ? 26.18800  20.56700  -38.70400 1.000 66.02000  ? 261 ALA C CA  1 
ATOM   9026  C  C   . ALA C  1 230 ? 27.15900  21.73600  -38.57800 1.000 75.33000  ? 261 ALA C C   1 
ATOM   9027  O  O   . ALA C  1 230 ? 26.75900  22.90100  -38.48500 1.000 71.78000  ? 261 ALA C O   1 
ATOM   9028  C  CB  . ALA C  1 230 ? 26.17800  20.05200  -40.14600 1.000 53.62000  ? 261 ALA C CB  1 
ATOM   9029  N  N   . LYS C  1 231 ? 28.44800  21.39700  -38.50900 1.000 77.42000  ? 262 LYS C N   1 
ATOM   9030  C  CA  . LYS C  1 231 ? 29.51100  22.39300  -38.48700 1.000 72.37000  ? 262 LYS C CA  1 
ATOM   9031  C  C   . LYS C  1 231 ? 29.76200  22.93900  -39.88600 1.000 76.38000  ? 262 LYS C C   1 
ATOM   9032  O  O   . LYS C  1 231 ? 29.73700  22.19600  -40.87200 1.000 77.63000  ? 262 LYS C O   1 
ATOM   9033  C  CB  . LYS C  1 231 ? 30.80000  21.79300  -37.91800 1.000 78.54000  ? 262 LYS C CB  1 
ATOM   9034  N  N   . ALA C  1 232 ? 30.04300  24.24500  -39.95400 1.000 82.37000  ? 263 ALA C N   1 
ATOM   9035  C  CA  . ALA C  1 232 ? 30.24500  24.93400  -41.22800 1.000 78.59000  ? 263 ALA C CA  1 
ATOM   9036  C  C   . ALA C  1 232 ? 31.38100  24.32600  -42.04600 1.000 82.58000  ? 263 ALA C C   1 
ATOM   9037  O  O   . ALA C  1 232 ? 31.30800  24.26300  -43.28000 1.000 83.95000  ? 263 ALA C O   1 
ATOM   9038  C  CB  . ALA C  1 232 ? 30.51400  26.41400  -40.96100 1.000 77.56000  ? 263 ALA C CB  1 
ATOM   9039  N  N   . GLU C  1 233 ? 32.45900  23.92500  -41.37800 1.000 82.37000  ? 264 GLU C N   1 
ATOM   9040  C  CA  . GLU C  1 233 ? 33.60200  23.33100  -42.06300 1.000 86.17000  ? 264 GLU C CA  1 
ATOM   9041  C  C   . GLU C  1 233 ? 33.24800  21.99400  -42.69400 1.000 81.04000  ? 264 GLU C C   1 
ATOM   9042  O  O   . GLU C  1 233 ? 33.84900  21.61200  -43.70400 1.000 77.83000  ? 264 GLU C O   1 
ATOM   9043  C  CB  . GLU C  1 233 ? 34.77000  23.15000  -41.08800 1.000 88.00000  ? 264 GLU C CB  1 
ATOM   9044  C  CG  . GLU C  1 233 ? 35.18900  24.41600  -40.33600 1.000 95.89000  ? 264 GLU C CG  1 
ATOM   9045  C  CD  . GLU C  1 233 ? 34.17800  24.90400  -39.27900 1.000 97.34000  ? 264 GLU C CD  1 
ATOM   9046  O  OE1 . GLU C  1 233 ? 33.07400  24.31300  -39.15300 1.000 92.82000  ? 264 GLU C OE1 1 
ATOM   9047  O  OE2 . GLU C  1 233 ? 34.50100  25.90000  -38.57700 1.000 105.74000 ? 264 GLU C OE2 1 
ATOM   9048  N  N   . ASP C  1 234 ? 32.31400  21.25200  -42.08700 1.000 79.67000  ? 265 ASP C N   1 
ATOM   9049  C  CA  . ASP C  1 234 ? 31.88700  19.97400  -42.64800 1.000 79.47000  ? 265 ASP C CA  1 
ATOM   9050  C  C   . ASP C  1 234 ? 30.92700  20.17100  -43.81400 1.000 77.25000  ? 265 ASP C C   1 
ATOM   9051  O  O   . ASP C  1 234 ? 31.09800  19.56400  -44.87800 1.000 75.26000  ? 265 ASP C O   1 
ATOM   9052  C  CB  . ASP C  1 234 ? 31.21200  19.13200  -41.56400 1.000 76.42000  ? 265 ASP C CB  1 
ATOM   9053  C  CG  . ASP C  1 234 ? 32.17000  18.68300  -40.50100 1.000 75.89000  ? 265 ASP C CG  1 
ATOM   9054  O  OD1 . ASP C  1 234 ? 33.33400  18.38700  -40.84200 1.000 81.16000  ? 265 ASP C OD1 1 
ATOM   9055  O  OD2 . ASP C  1 234 ? 31.76500  18.64600  -39.32200 1.000 79.81000  ? 265 ASP C OD2 1 
ATOM   9056  N  N   . VAL C  1 235 ? 29.93800  21.05800  -43.64900 1.000 76.77000  ? 266 VAL C N   1 
ATOM   9057  C  CA  . VAL C  1 235 ? 29.00600  21.32500  -44.74400 1.000 80.84000  ? 266 VAL C CA  1 
ATOM   9058  C  C   . VAL C  1 235 ? 29.76700  21.81000  -45.96600 1.000 78.65000  ? 266 VAL C C   1 
ATOM   9059  O  O   . VAL C  1 235 ? 29.34300  21.58300  -47.10400 1.000 74.03000  ? 266 VAL C O   1 
ATOM   9060  C  CB  . VAL C  1 235 ? 27.89900  22.31100  -44.31200 1.000 79.54000  ? 266 VAL C CB  1 
ATOM   9061  C  CG1 . VAL C  1 235 ? 27.23500  21.83400  -43.03800 1.000 68.97000  ? 266 VAL C CG1 1 
ATOM   9062  C  CG2 . VAL C  1 235 ? 28.43700  23.71200  -44.13200 1.000 86.31000  ? 266 VAL C CG2 1 
ATOM   9063  N  N   . ALA C  1 236 ? 30.89900  22.48300  -45.74800 1.000 79.88000  ? 267 ALA C N   1 
ATOM   9064  C  CA  . ALA C  1 236 ? 31.69000  23.00100  -46.85300 1.000 78.38000  ? 267 ALA C CA  1 
ATOM   9065  C  C   . ALA C  1 236 ? 32.22000  21.88200  -47.73600 1.000 75.45000  ? 267 ALA C C   1 
ATOM   9066  O  O   . ALA C  1 236 ? 32.43900  22.08600  -48.93400 1.000 76.89000  ? 267 ALA C O   1 
ATOM   9067  C  CB  . ALA C  1 236 ? 32.84200  23.83800  -46.30200 1.000 87.30000  ? 267 ALA C CB  1 
ATOM   9068  N  N   . LYS C  1 237 ? 32.45700  20.70200  -47.16400 1.000 79.11000  ? 268 LYS C N   1 
ATOM   9069  C  CA  . LYS C  1 237 ? 32.90800  19.57300  -47.96800 1.000 77.93000  ? 268 LYS C CA  1 
ATOM   9070  C  C   . LYS C  1 237 ? 31.79700  18.98100  -48.82900 1.000 75.79000  ? 268 LYS C C   1 
ATOM   9071  O  O   . LYS C  1 237 ? 32.07800  18.10800  -49.65500 1.000 77.86000  ? 268 LYS C O   1 
ATOM   9072  C  CB  . LYS C  1 237 ? 33.50500  18.49500  -47.06600 1.000 79.05000  ? 268 LYS C CB  1 
ATOM   9073  N  N   . PHE C  1 238 ? 30.54700  19.42200  -48.65800 1.000 76.25000  ? 269 PHE C N   1 
ATOM   9074  C  CA  . PHE C  1 238 ? 29.43200  18.84600  -49.39900 1.000 79.89000  ? 269 PHE C CA  1 
ATOM   9075  C  C   . PHE C  1 238 ? 28.56100  19.92100  -50.04300 1.000 80.71000  ? 269 PHE C C   1 
ATOM   9076  O  O   . PHE C  1 238 ? 27.34300  19.75300  -50.16000 1.000 81.01000  ? 269 PHE C O   1 
ATOM   9077  C  CB  . PHE C  1 238 ? 28.57300  17.95000  -48.50300 1.000 78.49000  ? 269 PHE C CB  1 
ATOM   9078  C  CG  . PHE C  1 238 ? 29.33600  16.84800  -47.82200 1.000 75.62000  ? 269 PHE C CG  1 
ATOM   9079  C  CD1 . PHE C  1 238 ? 29.76600  15.74000  -48.53400 1.000 71.36000  ? 269 PHE C CD1 1 
ATOM   9080  C  CD2 . PHE C  1 238 ? 29.56300  16.89400  -46.45300 1.000 73.66000  ? 269 PHE C CD2 1 
ATOM   9081  C  CE1 . PHE C  1 238 ? 30.46500  14.72600  -47.90500 1.000 73.88000  ? 269 PHE C CE1 1 
ATOM   9082  C  CE2 . PHE C  1 238 ? 30.24700  15.87700  -45.81800 1.000 73.56000  ? 269 PHE C CE2 1 
ATOM   9083  C  CZ  . PHE C  1 238 ? 30.70000  14.79000  -46.54600 1.000 68.46000  ? 269 PHE C CZ  1 
ATOM   9084  N  N   . ALA C  1 239 ? 29.15600  21.04400  -50.44800 1.000 82.83000  ? 270 ALA C N   1 
ATOM   9085  C  CA  . ALA C  1 239 ? 28.36400  22.09900  -51.07500 1.000 83.92000  ? 270 ALA C CA  1 
ATOM   9086  C  C   . ALA C  1 239 ? 27.82000  21.67500  -52.43700 1.000 78.51000  ? 270 ALA C C   1 
ATOM   9087  O  O   . ALA C  1 239 ? 26.79900  22.21100  -52.87500 1.000 79.03000  ? 270 ALA C O   1 
ATOM   9088  C  CB  . ALA C  1 239 ? 29.19000  23.38200  -51.20900 1.000 86.54000  ? 270 ALA C CB  1 
ATOM   9089  N  N   . HIS C  1 240 ? 28.46400  20.70800  -53.10100 1.000 80.40000  ? 271 HIS C N   1 
ATOM   9090  C  CA  . HIS C  1 240 ? 27.99400  20.18400  -54.37900 1.000 70.22000  ? 271 HIS C CA  1 
ATOM   9091  C  C   . HIS C  1 240 ? 26.71800  19.36600  -54.24000 1.000 75.38000  ? 271 HIS C C   1 
ATOM   9092  O  O   . HIS C  1 240 ? 26.23700  18.83900  -55.24600 1.000 78.71000  ? 271 HIS C O   1 
ATOM   9093  C  CB  . HIS C  1 240 ? 29.08700  19.33500  -55.03000 1.000 69.27000  ? 271 HIS C CB  1 
ATOM   9094  N  N   . ILE C  1 241 ? 26.21500  19.17800  -53.02200 1.000 79.36000  ? 272 ILE C N   1 
ATOM   9095  C  CA  . ILE C  1 241 ? 24.92700  18.53300  -52.77900 1.000 79.09000  ? 272 ILE C CA  1 
ATOM   9096  C  C   . ILE C  1 241 ? 23.84800  19.61000  -52.76900 1.000 77.08000  ? 272 ILE C C   1 
ATOM   9097  O  O   . ILE C  1 241 ? 23.89400  20.53800  -51.95100 1.000 77.55000  ? 272 ILE C O   1 
ATOM   9098  C  CB  . ILE C  1 241 ? 24.93700  17.72800  -51.46700 1.000 74.50000  ? 272 ILE C CB  1 
ATOM   9099  C  CG1 . ILE C  1 241 ? 25.95300  16.58200  -51.56500 1.000 76.86000  ? 272 ILE C CG1 1 
ATOM   9100  C  CG2 . ILE C  1 241 ? 23.54600  17.18700  -51.14500 1.000 71.29000  ? 272 ILE C CG2 1 
ATOM   9101  C  CD1 . ILE C  1 241 ? 26.00700  15.68100  -50.34600 1.000 71.54000  ? 272 ILE C CD1 1 
ATOM   9102  N  N   . LYS C  1 242 ? 22.87100  19.48200  -53.67400 1.000 78.32000  ? 273 LYS C N   1 
ATOM   9103  C  CA  . LYS C  1 242 ? 21.89900  20.55100  -53.87500 1.000 72.92000  ? 273 LYS C CA  1 
ATOM   9104  C  C   . LYS C  1 242 ? 20.86200  20.60600  -52.75800 1.000 72.56000  ? 273 LYS C C   1 
ATOM   9105  O  O   . LYS C  1 242 ? 20.50300  21.69300  -52.29600 1.000 70.17000  ? 273 LYS C O   1 
ATOM   9106  C  CB  . LYS C  1 242 ? 21.21400  20.37700  -55.22700 1.000 67.32000  ? 273 LYS C CB  1 
ATOM   9107  N  N   . ASP C  1 243 ? 20.36600  19.46000  -52.30600 1.000 73.42000  ? 274 ASP C N   1 
ATOM   9108  C  CA  . ASP C  1 243 ? 19.35600  19.45900  -51.25400 1.000 68.96000  ? 274 ASP C CA  1 
ATOM   9109  C  C   . ASP C  1 243 ? 19.95600  19.82800  -49.89700 1.000 72.38000  ? 274 ASP C C   1 
ATOM   9110  O  O   . ASP C  1 243 ? 20.87800  19.16500  -49.41400 1.000 75.76000  ? 274 ASP C O   1 
ATOM   9111  C  CB  . ASP C  1 243 ? 18.67500  18.10000  -51.17700 1.000 69.22000  ? 274 ASP C CB  1 
ATOM   9112  C  CG  . ASP C  1 243 ? 17.58900  18.07400  -50.12600 1.000 76.51000  ? 274 ASP C CG  1 
ATOM   9113  O  OD1 . ASP C  1 243 ? 16.56600  18.77600  -50.30400 1.000 78.63000  ? 274 ASP C OD1 1 
ATOM   9114  O  OD2 . ASP C  1 243 ? 17.77700  17.37900  -49.10500 1.000 73.52000  ? 274 ASP C OD2 1 
ATOM   9115  N  N   . LYS C  1 244 ? 19.38500  20.84800  -49.25300 1.000 71.91000  ? 275 LYS C N   1 
ATOM   9116  C  CA  . LYS C  1 244 ? 19.93100  21.34000  -47.99100 1.000 73.85000  ? 275 LYS C CA  1 
ATOM   9117  C  C   . LYS C  1 244 ? 19.91900  20.26600  -46.90900 1.000 75.48000  ? 275 LYS C C   1 
ATOM   9118  O  O   . LYS C  1 244 ? 20.89100  20.12400  -46.15600 1.000 72.22000  ? 275 LYS C O   1 
ATOM   9119  C  CB  . LYS C  1 244 ? 19.14000  22.55900  -47.51600 1.000 72.21000  ? 275 LYS C CB  1 
ATOM   9120  C  CG  . LYS C  1 244 ? 19.43000  22.96800  -46.07100 1.000 79.02000  ? 275 LYS C CG  1 
ATOM   9121  C  CD  . LYS C  1 244 ? 18.41700  23.97800  -45.54000 1.000 85.73000  ? 275 LYS C CD  1 
ATOM   9122  C  CE  . LYS C  1 244 ? 17.00400  23.39100  -45.46500 1.000 87.50000  ? 275 LYS C CE  1 
ATOM   9123  N  NZ  . LYS C  1 244 ? 16.01900  24.36500  -44.88400 1.000 93.86000  ? 275 LYS C NZ  1 
ATOM   9124  N  N   . ASP C  1 245 ? 18.82500  19.51000  -46.80000 1.000 73.63000  ? 276 ASP C N   1 
ATOM   9125  C  CA  . ASP C  1 245 ? 18.75600  18.48700  -45.76200 1.000 70.09000  ? 276 ASP C CA  1 
ATOM   9126  C  C   . ASP C  1 245 ? 19.75200  17.36500  -46.02800 1.000 68.98000  ? 276 ASP C C   1 
ATOM   9127  O  O   . ASP C  1 245 ? 20.37500  16.84600  -45.09400 1.000 67.24000  ? 276 ASP C O   1 
ATOM   9128  C  CB  . ASP C  1 245 ? 17.33000  17.96100  -45.62000 1.000 76.11000  ? 276 ASP C CB  1 
ATOM   9129  C  CG  . ASP C  1 245 ? 16.49700  18.79700  -44.64100 1.000 82.90000  ? 276 ASP C CG  1 
ATOM   9130  O  OD1 . ASP C  1 245 ? 16.93000  19.92300  -44.29500 1.000 79.51000  ? 276 ASP C OD1 1 
ATOM   9131  O  OD2 . ASP C  1 245 ? 15.43100  18.31800  -44.19200 1.000 84.82000  ? 276 ASP C OD2 1 
ATOM   9132  N  N   . ARG C  1 246 ? 19.88800  16.94600  -47.28500 1.000 70.69000  ? 277 ARG C N   1 
ATOM   9133  C  CA  . ARG C  1 246 ? 20.89300  15.94300  -47.61300 1.000 65.84000  ? 277 ARG C CA  1 
ATOM   9134  C  C   . ARG C  1 246 ? 22.29700  16.45500  -47.30800 1.000 71.60000  ? 277 ARG C C   1 
ATOM   9135  O  O   . ARG C  1 246 ? 23.15700  15.69600  -46.84300 1.000 69.41000  ? 277 ARG C O   1 
ATOM   9136  C  CB  . ARG C  1 246 ? 20.76400  15.53100  -49.07700 1.000 63.02000  ? 277 ARG C CB  1 
ATOM   9137  C  CG  . ARG C  1 246 ? 21.73500  14.43900  -49.48800 1.000 65.03000  ? 277 ARG C CG  1 
ATOM   9138  C  CD  . ARG C  1 246 ? 21.43700  13.15400  -48.71800 1.000 63.27000  ? 277 ARG C CD  1 
ATOM   9139  N  NE  . ARG C  1 246 ? 22.21800  12.02100  -49.19800 1.000 59.30000  ? 277 ARG C NE  1 
ATOM   9140  C  CZ  . ARG C  1 246 ? 22.29400  10.85400  -48.57500 1.000 58.77000  ? 277 ARG C CZ  1 
ATOM   9141  N  NH1 . ARG C  1 246 ? 21.65400  10.63500  -47.43200 1.000 53.50000  ? 277 ARG C NH1 1 
ATOM   9142  N  NH2 . ARG C  1 246 ? 23.02900  9.88500   -49.10800 1.000 51.59000  ? 277 ARG C NH2 1 
ATOM   9143  N  N   . ARG C  1 247 ? 22.54800  17.74100  -47.57100 1.000 68.80000  ? 278 ARG C N   1 
ATOM   9144  C  CA  . ARG C  1 247 ? 23.86500  18.31300  -47.31300 1.000 69.74000  ? 278 ARG C CA  1 
ATOM   9145  C  C   . ARG C  1 247 ? 24.17800  18.32600  -45.81900 1.000 66.80000  ? 278 ARG C C   1 
ATOM   9146  O  O   . ARG C  1 247 ? 25.23300  17.84500  -45.39200 1.000 64.65000  ? 278 ARG C O   1 
ATOM   9147  C  CB  . ARG C  1 247 ? 23.94100  19.72200  -47.90600 1.000 69.85000  ? 278 ARG C CB  1 
ATOM   9148  C  CG  . ARG C  1 247 ? 25.26000  20.42800  -47.66200 1.000 75.75000  ? 278 ARG C CG  1 
ATOM   9149  C  CD  . ARG C  1 247 ? 25.34200  21.74800  -48.41000 1.000 78.00000  ? 278 ARG C CD  1 
ATOM   9150  N  NE  . ARG C  1 247 ? 24.26100  22.64300  -48.01200 1.000 76.80000  ? 278 ARG C NE  1 
ATOM   9151  C  CZ  . ARG C  1 247 ? 23.24500  22.97100  -48.79900 1.000 77.16000  ? 278 ARG C CZ  1 
ATOM   9152  N  NH1 . ARG C  1 247 ? 23.16300  22.52000  -50.04100 1.000 72.97000  ? 278 ARG C NH1 1 
ATOM   9153  N  NH2 . ARG C  1 247 ? 22.27100  23.74100  -48.31800 1.000 75.73000  ? 278 ARG C NH2 1 
ATOM   9154  N  N   . THR C  1 248 ? 23.24900  18.82500  -45.00300 1.000 65.72000  ? 279 THR C N   1 
ATOM   9155  C  CA  . THR C  1 248 ? 23.48900  18.87800  -43.56400 1.000 67.37000  ? 279 THR C CA  1 
ATOM   9156  C  C   . THR C  1 248 ? 23.67900  17.47900  -42.99700 1.000 67.78000  ? 279 THR C C   1 
ATOM   9157  O  O   . THR C  1 248 ? 24.55300  17.24900  -42.15100 1.000 65.01000  ? 279 THR C O   1 
ATOM   9158  C  CB  . THR C  1 248 ? 22.31600  19.56000  -42.85700 1.000 69.18000  ? 279 THR C CB  1 
ATOM   9159  O  OG1 . THR C  1 248 ? 21.97900  20.77300  -43.53600 1.000 71.36000  ? 279 THR C OG1 1 
ATOM   9160  C  CG2 . THR C  1 248 ? 22.65200  19.85900  -41.38000 1.000 68.24000  ? 279 THR C CG2 1 
ATOM   9161  N  N   . TYR C  1 249 ? 22.83200  16.54500  -43.43300 1.000 65.58000  ? 280 TYR C N   1 
ATOM   9162  C  CA  . TYR C  1 249 ? 22.93700  15.15700  -43.00800 1.000 64.85000  ? 280 TYR C CA  1 
ATOM   9163  C  C   . TYR C  1 249 ? 24.30100  14.58400  -43.35500 1.000 65.43000  ? 280 TYR C C   1 
ATOM   9164  O  O   . TYR C  1 249 ? 24.96300  13.97200  -42.51000 1.000 62.19000  ? 280 TYR C O   1 
ATOM   9165  C  CB  . TYR C  1 249 ? 21.81600  14.35400  -43.66500 1.000 63.15000  ? 280 TYR C CB  1 
ATOM   9166  C  CG  . TYR C  1 249 ? 21.77800  12.87800  -43.36000 1.000 54.52000  ? 280 TYR C CG  1 
ATOM   9167  C  CD1 . TYR C  1 249 ? 22.51700  11.97800  -44.10600 1.000 52.91000  ? 280 TYR C CD1 1 
ATOM   9168  C  CD2 . TYR C  1 249 ? 20.98900  12.39000  -42.33300 1.000 52.12000  ? 280 TYR C CD2 1 
ATOM   9169  C  CE1 . TYR C  1 249 ? 22.47100  10.63500  -43.84300 1.000 48.48000  ? 280 TYR C CE1 1 
ATOM   9170  C  CE2 . TYR C  1 249 ? 20.93000  11.05400  -42.06200 1.000 52.20000  ? 280 TYR C CE2 1 
ATOM   9171  C  CZ  . TYR C  1 249 ? 21.67800  10.17400  -42.82200 1.000 57.07000  ? 280 TYR C CZ  1 
ATOM   9172  O  OH  . TYR C  1 249 ? 21.63800  8.82100   -42.55900 1.000 61.83000  ? 280 TYR C OH  1 
ATOM   9173  N  N   . ALA C  1 250 ? 24.75400  14.81000  -44.58800 1.000 65.81000  ? 281 ALA C N   1 
ATOM   9174  C  CA  . ALA C  1 250 ? 26.06300  14.31600  -44.98900 1.000 64.57000  ? 281 ALA C CA  1 
ATOM   9175  C  C   . ALA C  1 250 ? 27.15600  14.88400  -44.09900 1.000 66.54000  ? 281 ALA C C   1 
ATOM   9176  O  O   . ALA C  1 250 ? 28.10100  14.17600  -43.74100 1.000 69.58000  ? 281 ALA C O   1 
ATOM   9177  C  CB  . ALA C  1 250 ? 26.32400  14.64800  -46.45700 1.000 63.43000  ? 281 ALA C CB  1 
ATOM   9178  N  N   . ALA C  1 251 ? 27.06000  16.17000  -43.75500 1.000 69.00000  ? 282 ALA C N   1 
ATOM   9179  C  CA  . ALA C  1 251 ? 28.04700  16.77600  -42.86900 1.000 68.56000  ? 282 ALA C CA  1 
ATOM   9180  C  C   . ALA C  1 251 ? 27.98900  16.17000  -41.47200 1.000 67.76000  ? 282 ALA C C   1 
ATOM   9181  O  O   . ALA C  1 251 ? 29.03200  15.98600  -40.83400 1.000 68.76000  ? 282 ALA C O   1 
ATOM   9182  C  CB  . ALA C  1 251 ? 27.84900  18.29000  -42.80200 1.000 69.96000  ? 282 ALA C CB  1 
ATOM   9183  N  N   . MET C  1 252 ? 26.78800  15.84300  -40.97800 1.000 63.69000  ? 283 MET C N   1 
ATOM   9184  C  CA  . MET C  1 252 ? 26.70300  15.23400  -39.65400 1.000 62.13000  ? 283 MET C CA  1 
ATOM   9185  C  C   . MET C  1 252 ? 27.38600  13.87500  -39.64900 1.000 67.36000  ? 283 MET C C   1 
ATOM   9186  O  O   . MET C  1 252 ? 28.11800  13.53700  -38.71000 1.000 66.23000  ? 283 MET C O   1 
ATOM   9187  C  CB  . MET C  1 252 ? 25.24700  15.09500  -39.20700 1.000 65.68000  ? 283 MET C CB  1 
ATOM   9188  C  CG  . MET C  1 252 ? 24.46100  16.38900  -39.15900 1.000 67.88000  ? 283 MET C CG  1 
ATOM   9189  S  SD  . MET C  1 252 ? 22.71200  16.12600  -38.77000 1.000 60.72000  ? 283 MET C SD  1 
ATOM   9190  C  CE  . MET C  1 252 ? 22.79300  15.68900  -37.03800 1.000 63.71000  ? 283 MET C CE  1 
ATOM   9191  N  N   . VAL C  1 253 ? 27.14100  13.08000  -40.69200 1.000 62.47000  ? 284 VAL C N   1 
ATOM   9192  C  CA  . VAL C  1 253 ? 27.78300  11.77700  -40.84000 1.000 67.83000  ? 284 VAL C CA  1 
ATOM   9193  C  C   . VAL C  1 253 ? 29.29100  11.92600  -41.00600 1.000 69.23000  ? 284 VAL C C   1 
ATOM   9194  O  O   . VAL C  1 253 ? 30.06900  11.14400  -40.45100 1.000 66.47000  ? 284 VAL C O   1 
ATOM   9195  C  CB  . VAL C  1 253 ? 27.14800  11.01900  -42.02100 1.000 62.99000  ? 284 VAL C CB  1 
ATOM   9196  C  CG1 . VAL C  1 253 ? 27.96800  9.78600   -42.38400 1.000 64.82000  ? 284 VAL C CG1 1 
ATOM   9197  C  CG2 . VAL C  1 253 ? 25.70100  10.62400  -41.67000 1.000 57.90000  ? 284 VAL C CG2 1 
ATOM   9198  N  N   . TYR C  1 254 ? 29.72600  12.94100  -41.75300 1.000 66.91000  ? 285 TYR C N   1 
ATOM   9199  C  CA  . TYR C  1 254 ? 31.15500  13.14300  -41.96900 1.000 68.41000  ? 285 TYR C CA  1 
ATOM   9200  C  C   . TYR C  1 254 ? 31.87300  13.42600  -40.65100 1.000 68.05000  ? 285 TYR C C   1 
ATOM   9201  O  O   . TYR C  1 254 ? 32.99400  12.95300  -40.42600 1.000 69.65000  ? 285 TYR C O   1 
ATOM   9202  C  CB  . TYR C  1 254 ? 31.36000  14.28700  -42.96400 1.000 70.92000  ? 285 TYR C CB  1 
ATOM   9203  C  CG  . TYR C  1 254 ? 32.80000  14.55100  -43.35100 1.000 74.87000  ? 285 TYR C CG  1 
ATOM   9204  C  CD1 . TYR C  1 254 ? 33.47900  13.69400  -44.20800 1.000 73.99000  ? 285 TYR C CD1 1 
ATOM   9205  C  CD2 . TYR C  1 254 ? 33.48500  15.65300  -42.84000 1.000 72.61000  ? 285 TYR C CD2 1 
ATOM   9206  C  CE1 . TYR C  1 254 ? 34.79400  13.93800  -44.56200 1.000 77.31000  ? 285 TYR C CE1 1 
ATOM   9207  C  CE2 . TYR C  1 254 ? 34.79900  15.90300  -43.17800 1.000 77.24000  ? 285 TYR C CE2 1 
ATOM   9208  C  CZ  . TYR C  1 254 ? 35.45100  15.04500  -44.03800 1.000 85.14000  ? 285 TYR C CZ  1 
ATOM   9209  O  OH  . TYR C  1 254 ? 36.76500  15.29600  -44.37400 1.000 89.64000  ? 285 TYR C OH  1 
ATOM   9210  N  N   . ALA C  1 255 ? 31.23600  14.19600  -39.76400 1.000 69.34000  ? 286 ALA C N   1 
ATOM   9211  C  CA  . ALA C  1 255 ? 31.82900  14.49000  -38.46300 1.000 67.72000  ? 286 ALA C CA  1 
ATOM   9212  C  C   . ALA C  1 255 ? 32.04500  13.22400  -37.64200 1.000 68.69000  ? 286 ALA C C   1 
ATOM   9213  O  O   . ALA C  1 255 ? 32.99400  13.15200  -36.85100 1.000 69.84000  ? 286 ALA C O   1 
ATOM   9214  C  CB  . ALA C  1 255 ? 30.95100  15.47900  -37.69700 1.000 68.97000  ? 286 ALA C CB  1 
ATOM   9215  N  N   . VAL C  1 256 ? 31.17400  12.22400  -37.80100 1.000 68.52000  ? 287 VAL C N   1 
ATOM   9216  C  CA  . VAL C  1 256 ? 31.39500  10.94800  -37.13000 1.000 64.70000  ? 287 VAL C CA  1 
ATOM   9217  C  C   . VAL C  1 256 ? 32.63200  10.26700  -37.69400 1.000 66.27000  ? 287 VAL C C   1 
ATOM   9218  O  O   . VAL C  1 256 ? 33.45600  9.72500   -36.94900 1.000 65.51000  ? 287 VAL C O   1 
ATOM   9219  C  CB  . VAL C  1 256 ? 30.15400  10.05000  -37.27300 1.000 65.81000  ? 287 VAL C CB  1 
ATOM   9220  C  CG1 . VAL C  1 256 ? 30.49500  8.61600   -36.84000 1.000 60.08000  ? 287 VAL C CG1 1 
ATOM   9221  C  CG2 . VAL C  1 256 ? 28.97400  10.62300  -36.48100 1.000 58.37000  ? 287 VAL C CG2 1 
ATOM   9222  N  N   . ASP C  1 257 ? 32.80200  10.32600  -39.01600 1.000 61.38000  ? 288 ASP C N   1 
ATOM   9223  C  CA  . ASP C  1 257 ? 33.97100  9.73600   -39.65300 1.000 66.48000  ? 288 ASP C CA  1 
ATOM   9224  C  C   . ASP C  1 257 ? 35.25800  10.38600  -39.15200 1.000 67.08000  ? 288 ASP C C   1 
ATOM   9225  O  O   . ASP C  1 257 ? 36.24100  9.69500   -38.86100 1.000 70.21000  ? 288 ASP C O   1 
ATOM   9226  C  CB  . ASP C  1 257 ? 33.84400  9.87100   -41.17300 1.000 65.94000  ? 288 ASP C CB  1 
ATOM   9227  C  CG  . ASP C  1 257 ? 34.91000  9.09200   -41.92500 1.000 69.11000  ? 288 ASP C CG  1 
ATOM   9228  O  OD1 . ASP C  1 257 ? 34.79900  7.85200   -42.02800 1.000 70.13000  ? 288 ASP C OD1 1 
ATOM   9229  O  OD2 . ASP C  1 257 ? 35.87300  9.71800   -42.40400 1.000 69.78000  ? 288 ASP C OD2 1 
ATOM   9230  N  N   . ARG C  1 258 ? 35.28100  11.72000  -39.07300 1.000 72.47000  ? 289 ARG C N   1 
ATOM   9231  C  CA  . ARG C  1 258 ? 36.44900  12.40300  -38.52100 1.000 70.34000  ? 289 ARG C CA  1 
ATOM   9232  C  C   . ARG C  1 258 ? 36.73900  11.94000  -37.10400 1.000 70.87000  ? 289 ARG C C   1 
ATOM   9233  O  O   . ARG C  1 258 ? 37.89400  11.68300  -36.75000 1.000 70.21000  ? 289 ARG C O   1 
ATOM   9234  C  CB  . ARG C  1 258 ? 36.26200  13.92200  -38.52700 1.000 65.75000  ? 289 ARG C CB  1 
ATOM   9235  C  CG  . ARG C  1 258 ? 36.53700  14.61700  -39.83900 1.000 78.23000  ? 289 ARG C CG  1 
ATOM   9236  C  CD  . ARG C  1 258 ? 36.60000  16.14000  -39.64000 1.000 73.94000  ? 289 ARG C CD  1 
ATOM   9237  N  NE  . ARG C  1 258 ? 35.31100  16.70300  -39.26100 1.000 73.61000  ? 289 ARG C NE  1 
ATOM   9238  C  CZ  . ARG C  1 258 ? 34.89900  16.91500  -38.01800 1.000 75.90000  ? 289 ARG C CZ  1 
ATOM   9239  N  NH1 . ARG C  1 258 ? 35.64700  16.59700  -36.97100 1.000 72.08000  ? 289 ARG C NH1 1 
ATOM   9240  N  NH2 . ARG C  1 258 ? 33.69700  17.44300  -37.81700 1.000 77.42000  ? 289 ARG C NH2 1 
ATOM   9241  N  N   . GLY C  1 259 ? 35.70100  11.82200  -36.27900 1.000 72.23000  ? 290 GLY C N   1 
ATOM   9242  C  CA  . GLY C  1 259 ? 35.91900  11.40400  -34.91100 1.000 65.32000  ? 290 GLY C CA  1 
ATOM   9243  C  C   . GLY C  1 259 ? 36.45700  9.99500   -34.83700 1.000 70.60000  ? 290 GLY C C   1 
ATOM   9244  O  O   . GLY C  1 259 ? 37.27400  9.68600   -33.96600 1.000 69.32000  ? 290 GLY C O   1 
ATOM   9245  N  N   . VAL C  1 260 ? 36.02000  9.12800   -35.75400 1.000 70.13000  ? 291 VAL C N   1 
ATOM   9246  C  CA  . VAL C  1 260 ? 36.54700  7.76900   -35.82700 1.000 72.70000  ? 291 VAL C CA  1 
ATOM   9247  C  C   . VAL C  1 260 ? 38.01400  7.77200   -36.22800 1.000 71.29000  ? 291 VAL C C   1 
ATOM   9248  O  O   . VAL C  1 260 ? 38.81600  6.99300   -35.69900 1.000 71.93000  ? 291 VAL C O   1 
ATOM   9249  C  CB  . VAL C  1 260 ? 35.69400  6.92200   -36.78700 1.000 68.82000  ? 291 VAL C CB  1 
ATOM   9250  C  CG1 . VAL C  1 260 ? 36.39000  5.60800   -37.08800 1.000 60.89000  ? 291 VAL C CG1 1 
ATOM   9251  C  CG2 . VAL C  1 260 ? 34.32300  6.67000   -36.15300 1.000 59.16000  ? 291 VAL C CG2 1 
ATOM   9252  N  N   . GLY C  1 261 ? 38.39600  8.66900   -37.13300 1.000 69.04000  ? 292 GLY C N   1 
ATOM   9253  C  CA  . GLY C  1 261 ? 39.78800  8.73600   -37.54900 1.000 67.50000  ? 292 GLY C CA  1 
ATOM   9254  C  C   . GLY C  1 261 ? 40.73500  9.08800   -36.42300 1.000 69.76000  ? 292 GLY C C   1 
ATOM   9255  O  O   . GLY C  1 261 ? 41.85600  8.57100   -36.35800 1.000 70.37000  ? 292 GLY C O   1 
ATOM   9256  N  N   . LYS C  1 262 ? 40.33000  10.00900  -35.55400 1.000 64.30000  ? 293 LYS C N   1 
ATOM   9257  C  CA  . LYS C  1 262 ? 41.17200  10.26900  -34.39600 1.000 72.84000  ? 293 LYS C CA  1 
ATOM   9258  C  C   . LYS C  1 262 ? 41.15600  9.10200   -33.41600 1.000 74.06000  ? 293 LYS C C   1 
ATOM   9259  O  O   . LYS C  1 262 ? 42.18600  8.77500   -32.82300 1.000 75.45000  ? 293 LYS C O   1 
ATOM   9260  C  CB  . LYS C  1 262 ? 40.79300  11.58900  -33.71200 1.000 71.28000  ? 293 LYS C CB  1 
ATOM   9261  C  CG  . LYS C  1 262 ? 40.93800  12.78000  -34.65000 1.000 70.06000  ? 293 LYS C CG  1 
ATOM   9262  C  CD  . LYS C  1 262 ? 42.41100  12.85100  -35.15200 1.000 90.71000  ? 293 LYS C CD  1 
ATOM   9263  C  CE  . LYS C  1 262 ? 43.48500  13.27600  -34.12600 1.000 82.25000  ? 293 LYS C CE  1 
ATOM   9264  N  NZ  . LYS C  1 262 ? 44.84100  13.44400  -34.77000 1.000 88.41000  ? 293 LYS C NZ  1 
ATOM   9265  N  N   . ILE C  1 263 ? 40.01000  8.44500   -33.25500 1.000 71.80000  ? 294 ILE C N   1 
ATOM   9266  C  CA  . ILE C  1 263 ? 39.92600  7.29200   -32.35800 1.000 69.49000  ? 294 ILE C CA  1 
ATOM   9267  C  C   . ILE C  1 263 ? 40.89800  6.20700   -32.80000 1.000 69.43000  ? 294 ILE C C   1 
ATOM   9268  O  O   . ILE C  1 263 ? 41.54100  5.55600   -31.96800 1.000 74.09000  ? 294 ILE C O   1 
ATOM   9269  C  CB  . ILE C  1 263 ? 38.47700  6.75600   -32.29300 1.000 63.56000  ? 294 ILE C CB  1 
ATOM   9270  C  CG1 . ILE C  1 263 ? 37.60700  7.67000   -31.43900 1.000 67.72000  ? 294 ILE C CG1 1 
ATOM   9271  C  CG2 . ILE C  1 263 ? 38.42800  5.33300   -31.75000 1.000 61.76000  ? 294 ILE C CG2 1 
ATOM   9272  C  CD1 . ILE C  1 263 ? 36.11500  7.63100   -31.82400 1.000 52.63000  ? 294 ILE C CD1 1 
ATOM   9273  N  N   . VAL C  1 264 ? 40.99600  5.96900   -34.10900 1.000 68.73000  ? 295 VAL C N   1 
ATOM   9274  C  CA  . VAL C  1 264 ? 41.93700  4.97400   -34.61100 1.000 68.64000  ? 295 VAL C CA  1 
ATOM   9275  C  C   . VAL C  1 264 ? 43.37300  5.42700   -34.36400 1.000 72.02000  ? 295 VAL C C   1 
ATOM   9276  O  O   . VAL C  1 264 ? 44.21900  4.64000   -33.91900 1.000 76.17000  ? 295 VAL C O   1 
ATOM   9277  C  CB  . VAL C  1 264 ? 41.66800  4.69800   -36.10000 1.000 67.02000  ? 295 VAL C CB  1 
ATOM   9278  C  CG1 . VAL C  1 264 ? 42.81900  3.92100   -36.72800 1.000 64.23000  ? 295 VAL C CG1 1 
ATOM   9279  C  CG2 . VAL C  1 264 ? 40.35000  3.96600   -36.27000 1.000 62.59000  ? 295 VAL C CG2 1 
ATOM   9280  N  N   . GLN C  1 265 ? 43.67300  6.69900   -34.64500 1.000 72.59000  ? 296 GLN C N   1 
ATOM   9281  C  CA  . GLN C  1 265 ? 45.01300  7.22100   -34.38800 1.000 77.08000  ? 296 GLN C CA  1 
ATOM   9282  C  C   . GLN C  1 265 ? 45.41300  7.06500   -32.92500 1.000 76.86000  ? 296 GLN C C   1 
ATOM   9283  O  O   . GLN C  1 265 ? 46.54600  6.66800   -32.62300 1.000 75.76000  ? 296 GLN C O   1 
ATOM   9284  C  CB  . GLN C  1 265 ? 45.10400  8.67900   -34.84200 1.000 79.47000  ? 296 GLN C CB  1 
ATOM   9285  C  CG  . GLN C  1 265 ? 46.51000  9.24300   -34.78400 1.000 89.03000  ? 296 GLN C CG  1 
ATOM   9286  C  CD  . GLN C  1 265 ? 47.50800  8.45400   -35.60400 1.000 91.60000  ? 296 GLN C CD  1 
ATOM   9287  O  OE1 . GLN C  1 265 ? 48.41000  7.80600   -35.04700 1.000 94.65000  ? 296 GLN C OE1 1 
ATOM   9288  N  NE2 . GLN C  1 265 ? 47.34800  8.48200   -36.92900 1.000 92.25000  ? 296 GLN C NE2 1 
ATOM   9289  N  N   . THR C  1 266 ? 44.50200  7.36800   -32.00400 1.000 73.83000  ? 297 THR C N   1 
ATOM   9290  C  CA  . THR C  1 266 ? 44.78600  7.15700   -30.59000 1.000 71.92000  ? 297 THR C CA  1 
ATOM   9291  C  C   . THR C  1 266 ? 44.99100  5.67800   -30.28300 1.000 72.98000  ? 297 THR C C   1 
ATOM   9292  O  O   . THR C  1 266 ? 45.88200  5.31700   -29.50400 1.000 74.09000  ? 297 THR C O   1 
ATOM   9293  C  CB  . THR C  1 266 ? 43.67100  7.76500   -29.74700 1.000 65.83000  ? 297 THR C CB  1 
ATOM   9294  O  OG1 . THR C  1 266 ? 43.68700  9.18600   -29.92400 1.000 69.57000  ? 297 THR C OG1 1 
ATOM   9295  C  CG2 . THR C  1 266 ? 43.83900  7.43500   -28.27700 1.000 68.80000  ? 297 THR C CG2 1 
ATOM   9296  N  N   . LEU C  1 267 ? 44.17900  4.80400   -30.88400 1.000 68.82000  ? 298 LEU C N   1 
ATOM   9297  C  CA  . LEU C  1 267 ? 44.34700  3.37200   -30.65300 1.000 74.87000  ? 298 LEU C CA  1 
ATOM   9298  C  C   . LEU C  1 267 ? 45.73700  2.90300   -31.07700 1.000 79.07000  ? 298 LEU C C   1 
ATOM   9299  O  O   . LEU C  1 267 ? 46.34500  2.05200   -30.41400 1.000 75.17000  ? 298 LEU C O   1 
ATOM   9300  C  CB  . LEU C  1 267 ? 43.26900  2.58700   -31.39800 1.000 68.24000  ? 298 LEU C CB  1 
ATOM   9301  C  CG  . LEU C  1 267 ? 41.87100  2.68900   -30.79600 1.000 68.77000  ? 298 LEU C CG  1 
ATOM   9302  C  CD1 . LEU C  1 267 ? 40.84600  2.03300   -31.71000 1.000 64.07000  ? 298 LEU C CD1 1 
ATOM   9303  C  CD2 . LEU C  1 267 ? 41.82500  2.09100   -29.40300 1.000 61.06000  ? 298 LEU C CD2 1 
ATOM   9304  N  N   . LYS C  1 268 ? 46.27000  3.47600   -32.15700 1.000 76.80000  ? 299 LYS C N   1 
ATOM   9305  C  CA  . LYS C  1 268 ? 47.59800  3.09800   -32.62900 1.000 70.41000  ? 299 LYS C CA  1 
ATOM   9306  C  C   . LYS C  1 268 ? 48.70100  3.69000   -31.75300 1.000 77.56000  ? 299 LYS C C   1 
ATOM   9307  O  O   . LYS C  1 268 ? 49.74300  3.05400   -31.56000 1.000 77.86000  ? 299 LYS C O   1 
ATOM   9308  C  CB  . LYS C  1 268 ? 47.76000  3.50700   -34.09400 1.000 75.58000  ? 299 LYS C CB  1 
ATOM   9309  C  CG  . LYS C  1 268 ? 46.91000  2.66500   -35.05100 1.000 70.56000  ? 299 LYS C CG  1 
ATOM   9310  C  CD  . LYS C  1 268 ? 46.97900  3.14900   -36.49200 1.000 74.58000  ? 299 LYS C CD  1 
ATOM   9311  C  CE  . LYS C  1 268 ? 46.04500  2.32400   -37.38200 1.000 77.43000  ? 299 LYS C CE  1 
ATOM   9312  N  NZ  . LYS C  1 268 ? 46.11200  2.68300   -38.82800 1.000 81.69000  ? 299 LYS C NZ  1 
ATOM   9313  N  N   . GLU C  1 269 ? 48.51900  4.92100   -31.25800 1.000 80.30000  ? 300 GLU C N   1 
ATOM   9314  C  CA  . GLU C  1 269 ? 49.49800  5.51300   -30.34500 1.000 74.63000  ? 300 GLU C CA  1 
ATOM   9315  C  C   . GLU C  1 269 ? 49.58200  4.74000   -29.03100 1.000 76.52000  ? 300 GLU C C   1 
ATOM   9316  O  O   . GLU C  1 269 ? 50.67800  4.49700   -28.51300 1.000 80.97000  ? 300 GLU C O   1 
ATOM   9317  C  CB  . GLU C  1 269 ? 49.14600  6.97300   -30.05700 1.000 76.23000  ? 300 GLU C CB  1 
ATOM   9318  C  CG  . GLU C  1 269 ? 49.40300  7.93900   -31.19500 1.000 83.01000  ? 300 GLU C CG  1 
ATOM   9319  C  CD  . GLU C  1 269 ? 48.67400  9.26300   -31.00400 1.000 91.07000  ? 300 GLU C CD  1 
ATOM   9320  O  OE1 . GLU C  1 269 ? 48.16300  9.51700   -29.88400 1.000 86.74000  ? 300 GLU C OE1 1 
ATOM   9321  O  OE2 . GLU C  1 269 ? 48.60400  10.04200  -31.98100 1.000 91.51000  ? 300 GLU C OE2 1 
ATOM   9322  N  N   . THR C  1 270 ? 48.43800  4.36900   -28.46200 1.000 72.59000  ? 301 THR C N   1 
ATOM   9323  C  CA  . THR C  1 270 ? 48.41000  3.57500   -27.24000 1.000 73.01000  ? 301 THR C CA  1 
ATOM   9324  C  C   . THR C  1 270 ? 48.62300  2.08000   -27.47100 1.000 73.80000  ? 301 THR C C   1 
ATOM   9325  O  O   . THR C  1 270 ? 48.41800  1.30500   -26.53100 1.000 73.70000  ? 301 THR C O   1 
ATOM   9326  C  CB  . THR C  1 270 ? 47.09000  3.79400   -26.50400 1.000 69.54000  ? 301 THR C CB  1 
ATOM   9327  O  OG1 . THR C  1 270 ? 46.01000  3.31000   -27.31500 1.000 74.59000  ? 301 THR C OG1 1 
ATOM   9328  C  CG2 . THR C  1 270 ? 46.89200  5.25300   -26.20500 1.000 66.24000  ? 301 THR C CG2 1 
ATOM   9329  N  N   . LYS C  1 271 ? 48.98000  1.66000   -28.68800 1.000 70.16000  ? 302 LYS C N   1 
ATOM   9330  C  CA  . LYS C  1 271 ? 49.21200  0.24500   -29.00500 1.000 73.27000  ? 302 LYS C CA  1 
ATOM   9331  C  C   . LYS C  1 271 ? 48.04600  -0.65500  -28.57100 1.000 75.76000  ? 302 LYS C C   1 
ATOM   9332  O  O   . LYS C  1 271 ? 48.23900  -1.81500  -28.20300 1.000 70.02000  ? 302 LYS C O   1 
ATOM   9333  C  CB  . LYS C  1 271 ? 50.53100  -0.24000  -28.39600 1.000 80.93000  ? 302 LYS C CB  1 
ATOM   9334  N  N   . GLN C  1 272 ? 46.82300  -0.12900  -28.59500 1.000 73.00000  ? 303 GLN C N   1 
ATOM   9335  C  CA  . GLN C  1 272 ? 45.63400  -0.92100  -28.32200 1.000 71.44000  ? 303 GLN C CA  1 
ATOM   9336  C  C   . GLN C  1 272 ? 44.90000  -1.32700  -29.59100 1.000 67.84000  ? 303 GLN C C   1 
ATOM   9337  O  O   . GLN C  1 272 ? 43.90300  -2.05400  -29.51100 1.000 62.77000  ? 303 GLN C O   1 
ATOM   9338  C  CB  . GLN C  1 272 ? 44.67600  -0.15100  -27.41000 1.000 73.05000  ? 303 GLN C CB  1 
ATOM   9339  C  CG  . GLN C  1 272 ? 45.20200  0.09200   -26.03600 1.000 67.52000  ? 303 GLN C CG  1 
ATOM   9340  C  CD  . GLN C  1 272 ? 45.61100  -1.20600  -25.38300 1.000 81.57000  ? 303 GLN C CD  1 
ATOM   9341  O  OE1 . GLN C  1 272 ? 44.84600  -2.17700  -25.36800 1.000 79.95000  ? 303 GLN C OE1 1 
ATOM   9342  N  NE2 . GLN C  1 272 ? 46.83000  -1.23900  -24.83900 1.000 80.96000  ? 303 GLN C NE2 1 
ATOM   9343  N  N   . PHE C  1 273 ? 45.37800  -0.87900  -30.75300 1.000 71.17000  ? 304 PHE C N   1 
ATOM   9344  C  CA  . PHE C  1 273 ? 44.62200  -1.02400  -31.99600 1.000 74.76000  ? 304 PHE C CA  1 
ATOM   9345  C  C   . PHE C  1 273 ? 44.41300  -2.47900  -32.37400 1.000 72.10000  ? 304 PHE C C   1 
ATOM   9346  O  O   . PHE C  1 273 ? 43.28300  -2.91300  -32.61800 1.000 68.51000  ? 304 PHE C O   1 
ATOM   9347  C  CB  . PHE C  1 273 ? 45.34100  -0.29000  -33.12600 1.000 73.59000  ? 304 PHE C CB  1 
ATOM   9348  C  CG  . PHE C  1 273 ? 44.60900  -0.32800  -34.43600 1.000 77.68000  ? 304 PHE C CG  1 
ATOM   9349  C  CD1 . PHE C  1 273 ? 43.37600  0.28500   -34.57800 1.000 74.94000  ? 304 PHE C CD1 1 
ATOM   9350  C  CD2 . PHE C  1 273 ? 45.16600  -0.96600  -35.53700 1.000 78.24000  ? 304 PHE C CD2 1 
ATOM   9351  C  CE1 . PHE C  1 273 ? 42.70200  0.25200   -35.79200 1.000 73.33000  ? 304 PHE C CE1 1 
ATOM   9352  C  CE2 . PHE C  1 273 ? 44.49700  -1.00300  -36.75300 1.000 76.03000  ? 304 PHE C CE2 1 
ATOM   9353  C  CZ  . PHE C  1 273 ? 43.26700  -0.39000  -36.88000 1.000 74.05000  ? 304 PHE C CZ  1 
ATOM   9354  N  N   . ASP C  1 274 ? 45.49600  -3.25300  -32.40400 1.000 76.29000  ? 305 ASP C N   1 
ATOM   9355  C  CA  . ASP C  1 274 ? 45.44400  -4.57800  -33.00400 1.000 70.85000  ? 305 ASP C CA  1 
ATOM   9356  C  C   . ASP C  1 274 ? 44.54200  -5.52400  -32.22600 1.000 66.53000  ? 305 ASP C C   1 
ATOM   9357  O  O   . ASP C  1 274 ? 43.92800  -6.40900  -32.83000 1.000 66.21000  ? 305 ASP C O   1 
ATOM   9358  C  CB  . ASP C  1 274 ? 46.86300  -5.13000  -33.11300 1.000 79.17000  ? 305 ASP C CB  1 
ATOM   9359  C  CG  . ASP C  1 274 ? 47.61400  -4.56200  -34.30400 1.000 85.16000  ? 305 ASP C CG  1 
ATOM   9360  O  OD1 . ASP C  1 274 ? 47.01300  -3.78700  -35.08900 1.000 84.19000  ? 305 ASP C OD1 1 
ATOM   9361  O  OD2 . ASP C  1 274 ? 48.81700  -4.86500  -34.44200 1.000 93.91000  ? 305 ASP C OD2 1 
ATOM   9362  N  N   . ASN C  1 275 ? 44.45600  -5.37100  -30.90000 1.000 67.24000  ? 306 ASN C N   1 
ATOM   9363  C  CA  . ASN C  1 275 ? 43.59400  -6.20700  -30.06700 1.000 64.36000  ? 306 ASN C CA  1 
ATOM   9364  C  C   . ASN C  1 275 ? 42.34900  -5.46500  -29.57600 1.000 67.85000  ? 306 ASN C C   1 
ATOM   9365  O  O   . ASN C  1 275 ? 41.86500  -5.69000  -28.46000 1.000 64.14000  ? 306 ASN C O   1 
ATOM   9366  C  CB  . ASN C  1 275 ? 44.34600  -6.77700  -28.87700 1.000 58.58000  ? 306 ASN C CB  1 
ATOM   9367  C  CG  . ASN C  1 275 ? 43.64000  -7.96800  -28.29300 1.000 61.44000  ? 306 ASN C CG  1 
ATOM   9368  O  OD1 . ASN C  1 275 ? 43.00800  -8.72100  -29.02500 1.000 65.05000  ? 306 ASN C OD1 1 
ATOM   9369  N  ND2 . ASN C  1 275 ? 43.68800  -8.11900  -26.97600 1.000 63.52000  ? 306 ASN C ND2 1 
ATOM   9370  N  N   . THR C  1 276 ? 41.81100  -4.57400  -30.40400 1.000 69.85000  ? 307 THR C N   1 
ATOM   9371  C  CA  . THR C  1 276 ? 40.51600  -3.95300  -30.15600 1.000 66.66000  ? 307 THR C CA  1 
ATOM   9372  C  C   . THR C  1 276 ? 39.53500  -4.44600  -31.21000 1.000 58.40000  ? 307 THR C C   1 
ATOM   9373  O  O   . THR C  1 276 ? 39.82300  -4.37500  -32.40800 1.000 58.19000  ? 307 THR C O   1 
ATOM   9374  C  CB  . THR C  1 276 ? 40.60600  -2.42200  -30.20600 1.000 61.79000  ? 307 THR C CB  1 
ATOM   9375  O  OG1 . THR C  1 276 ? 41.42800  -1.94600  -29.14000 1.000 66.92000  ? 307 THR C OG1 1 
ATOM   9376  C  CG2 . THR C  1 276 ? 39.23000  -1.80100  -30.06900 1.000 61.64000  ? 307 THR C CG2 1 
ATOM   9377  N  N   . LEU C  1 277 ? 38.40400  -4.97900  -30.76400 1.000 60.32000  ? 308 LEU C N   1 
ATOM   9378  C  CA  . LEU C  1 277 ? 37.28500  -5.28500  -31.64800 1.000 61.92000  ? 308 LEU C CA  1 
ATOM   9379  C  C   . LEU C  1 277 ? 36.41800  -4.03400  -31.75200 1.000 63.02000  ? 308 LEU C C   1 
ATOM   9380  O  O   . LEU C  1 277 ? 35.83200  -3.59200  -30.75300 1.000 57.09000  ? 308 LEU C O   1 
ATOM   9381  C  CB  . LEU C  1 277 ? 36.46200  -6.46100  -31.13400 1.000 58.38000  ? 308 LEU C CB  1 
ATOM   9382  C  CG  . LEU C  1 277 ? 35.10200  -6.54100  -31.84100 1.000 61.42000  ? 308 LEU C CG  1 
ATOM   9383  C  CD1 . LEU C  1 277 ? 35.23200  -6.84300  -33.33200 1.000 61.89000  ? 308 LEU C CD1 1 
ATOM   9384  C  CD2 . LEU C  1 277 ? 34.16100  -7.53400  -31.17400 1.000 63.06000  ? 308 LEU C CD2 1 
ATOM   9385  N  N   . ILE C  1 278 ? 36.37900  -3.44300  -32.94500 1.000 60.21000  ? 309 ILE C N   1 
ATOM   9386  C  CA  . ILE C  1 278 ? 35.54300  -2.28500  -33.24100 1.000 59.51000  ? 309 ILE C CA  1 
ATOM   9387  C  C   . ILE C  1 278 ? 34.30300  -2.77900  -33.96200 1.000 55.82000  ? 309 ILE C C   1 
ATOM   9388  O  O   . ILE C  1 278 ? 34.41100  -3.34100  -35.05700 1.000 58.84000  ? 309 ILE C O   1 
ATOM   9389  C  CB  . ILE C  1 278 ? 36.28700  -1.26800  -34.12100 1.000 59.09000  ? 309 ILE C CB  1 
ATOM   9390  C  CG1 . ILE C  1 278 ? 37.61600  -0.85100  -33.50700 1.000 52.85000  ? 309 ILE C CG1 1 
ATOM   9391  C  CG2 . ILE C  1 278 ? 35.43500  -0.03300  -34.32500 1.000 57.91000  ? 309 ILE C CG2 1 
ATOM   9392  C  CD1 . ILE C  1 278 ? 38.38200  0.08100   -34.41400 1.000 50.18000  ? 309 ILE C CD1 1 
ATOM   9393  N  N   . VAL C  1 279 ? 33.12500  -2.55200  -33.38300 1.000 54.72000  ? 310 VAL C N   1 
ATOM   9394  C  CA  . VAL C  1 279 ? 31.85300  -2.85400  -34.04000 1.000 59.75000  ? 310 VAL C CA  1 
ATOM   9395  C  C   . VAL C  1 279 ? 31.12400  -1.54400  -34.31500 1.000 61.91000  ? 310 VAL C C   1 
ATOM   9396  O  O   . VAL C  1 279 ? 30.79500  -0.79500  -33.38700 1.000 59.14000  ? 310 VAL C O   1 
ATOM   9397  C  CB  . VAL C  1 279 ? 30.98100  -3.79700  -33.20100 1.000 54.87000  ? 310 VAL C CB  1 
ATOM   9398  C  CG1 . VAL C  1 279 ? 29.66400  -4.02600  -33.89600 1.000 53.25000  ? 310 VAL C CG1 1 
ATOM   9399  C  CG2 . VAL C  1 279 ? 31.69200  -5.10100  -32.99500 1.000 57.03000  ? 310 VAL C CG2 1 
ATOM   9400  N  N   . PHE C  1 280 ? 30.82200  -1.29500  -35.58400 1.000 63.79000  ? 311 PHE C N   1 
ATOM   9401  C  CA  . PHE C  1 280 ? 30.12600  -0.09300  -36.02700 1.000 61.54000  ? 311 PHE C CA  1 
ATOM   9402  C  C   . PHE C  1 280 ? 28.78700  -0.49500  -36.62200 1.000 58.85000  ? 311 PHE C C   1 
ATOM   9403  O  O   . PHE C  1 280 ? 28.72600  -1.42500  -37.42900 1.000 57.35000  ? 311 PHE C O   1 
ATOM   9404  C  CB  . PHE C  1 280 ? 30.97100  0.66400   -37.06400 1.000 62.92000  ? 311 PHE C CB  1 
ATOM   9405  C  CG  . PHE C  1 280 ? 30.23400  1.77300   -37.78500 1.000 63.20000  ? 311 PHE C CG  1 
ATOM   9406  C  CD1 . PHE C  1 280 ? 29.51000  1.51700   -38.93900 1.000 60.21000  ? 311 PHE C CD1 1 
ATOM   9407  C  CD2 . PHE C  1 280 ? 30.29700  3.07600   -37.32700 1.000 62.48000  ? 311 PHE C CD2 1 
ATOM   9408  C  CE1 . PHE C  1 280 ? 28.85000  2.54200   -39.60900 1.000 61.55000  ? 311 PHE C CE1 1 
ATOM   9409  C  CE2 . PHE C  1 280 ? 29.63500  4.10400   -38.00300 1.000 64.03000  ? 311 PHE C CE2 1 
ATOM   9410  C  CZ  . PHE C  1 280 ? 28.91400  3.83200   -39.13800 1.000 53.33000  ? 311 PHE C CZ  1 
ATOM   9411  N  N   . LEU C  1 281 ? 27.72700  0.21500   -36.24700 1.000 53.33000  ? 312 LEU C N   1 
ATOM   9412  C  CA  . LEU C  1 281 ? 26.40200  -0.08300  -36.76600 1.000 52.04000  ? 312 LEU C CA  1 
ATOM   9413  C  C   . LEU C  1 281 ? 25.48700  1.11900   -36.55700 1.000 60.06000  ? 312 LEU C C   1 
ATOM   9414  O  O   . LEU C  1 281 ? 25.82800  2.07600   -35.85500 1.000 56.63000  ? 312 LEU C O   1 
ATOM   9415  C  CB  . LEU C  1 281 ? 25.82700  -1.34200  -36.10800 1.000 52.59000  ? 312 LEU C CB  1 
ATOM   9416  C  CG  . LEU C  1 281 ? 25.35200  -1.25900  -34.66000 1.000 54.30000  ? 312 LEU C CG  1 
ATOM   9417  C  CD1 . LEU C  1 281 ? 24.42700  -2.39800  -34.34400 1.000 44.18000  ? 312 LEU C CD1 1 
ATOM   9418  C  CD2 . LEU C  1 281 ? 26.53600  -1.25200  -33.66600 1.000 48.56000  ? 312 LEU C CD2 1 
ATOM   9419  N  N   . SER C  1 282 ? 24.31600  1.06100   -37.19400 1.000 55.54000  ? 313 SER C N   1 
ATOM   9420  C  CA  . SER C  1 282 ? 23.24500  2.01300   -36.93800 1.000 52.80000  ? 313 SER C CA  1 
ATOM   9421  C  C   . SER C  1 282 ? 22.20500  1.35800   -36.03500 1.000 59.17000  ? 313 SER C C   1 
ATOM   9422  O  O   . SER C  1 282 ? 22.06000  0.13100   -36.01100 1.000 58.58000  ? 313 SER C O   1 
ATOM   9423  C  CB  . SER C  1 282 ? 22.59500  2.49500   -38.23400 1.000 58.31000  ? 313 SER C CB  1 
ATOM   9424  O  OG  . SER C  1 282 ? 21.54900  3.40900   -37.95200 1.000 62.64000  ? 313 SER C OG  1 
ATOM   9425  N  N   . ASP C  1 283 ? 21.49200  2.18200   -35.27000 1.000 54.25000  ? 314 ASP C N   1 
ATOM   9426  C  CA  . ASP C  1 283 ? 20.55200  1.61400   -34.31900 1.000 51.70000  ? 314 ASP C CA  1 
ATOM   9427  C  C   . ASP C  1 283 ? 19.23100  1.22700   -34.95900 1.000 50.85000  ? 314 ASP C C   1 
ATOM   9428  O  O   . ASP C  1 283 ? 18.47500  0.45300   -34.35900 1.000 52.96000  ? 314 ASP C O   1 
ATOM   9429  C  CB  . ASP C  1 283 ? 20.30800  2.58700   -33.15800 1.000 52.81000  ? 314 ASP C CB  1 
ATOM   9430  C  CG  . ASP C  1 283 ? 19.50000  3.82100   -33.55500 1.000 57.94000  ? 314 ASP C CG  1 
ATOM   9431  O  OD1 . ASP C  1 283 ? 19.53100  4.26900   -34.72100 1.000 55.62000  ? 314 ASP C OD1 1 
ATOM   9432  O  OD2 . ASP C  1 283 ? 18.81200  4.35600   -32.66100 1.000 63.65000  ? 314 ASP C OD2 1 
ATOM   9433  N  N   . ASN C  1 284 ? 18.95100  1.74300   -36.15200 1.000 54.16000  ? 315 ASN C N   1 
ATOM   9434  C  CA  . ASN C  1 284 ? 17.76100  1.44000   -36.94400 1.000 54.34000  ? 315 ASN C CA  1 
ATOM   9435  C  C   . ASN C  1 284 ? 17.98100  2.08400   -38.30600 1.000 49.07000  ? 315 ASN C C   1 
ATOM   9436  O  O   . ASN C  1 284 ? 18.95200  2.81600   -38.51100 1.000 52.86000  ? 315 ASN C O   1 
ATOM   9437  C  CB  . ASN C  1 284 ? 16.46200  1.95700   -36.29900 1.000 58.81000  ? 315 ASN C CB  1 
ATOM   9438  C  CG  . ASN C  1 284 ? 16.51200  3.45500   -35.97700 1.000 54.90000  ? 315 ASN C CG  1 
ATOM   9439  O  OD1 . ASN C  1 284 ? 16.61500  4.27600   -36.87200 1.000 56.88000  ? 315 ASN C OD1 1 
ATOM   9440  N  ND2 . ASN C  1 284 ? 16.44000  3.80500   -34.68600 1.000 59.25000  ? 315 ASN C ND2 1 
ATOM   9441  N  N   . GLY C  1 285 ? 17.05100  1.84200   -39.22400 1.000 51.73000  ? 316 GLY C N   1 
ATOM   9442  C  CA  . GLY C  1 285 ? 17.17900  2.40400   -40.55300 1.000 52.34000  ? 316 GLY C CA  1 
ATOM   9443  C  C   . GLY C  1 285 ? 17.07400  3.91800   -40.55900 1.000 58.78000  ? 316 GLY C C   1 
ATOM   9444  O  O   . GLY C  1 285 ? 16.61400  4.55700   -39.60400 1.000 56.68000  ? 316 GLY C O   1 
ATOM   9445  N  N   . GLY C  1 286 ? 17.55700  4.51000   -41.64600 1.000 51.75000  ? 317 GLY C N   1 
ATOM   9446  C  CA  . GLY C  1 286 ? 17.45600  5.94500   -41.79500 1.000 55.75000  ? 317 GLY C CA  1 
ATOM   9447  C  C   . GLY C  1 286 ? 16.02400  6.40200   -42.02500 1.000 63.65000  ? 317 GLY C C   1 
ATOM   9448  O  O   . GLY C  1 286 ? 15.19200  5.69400   -42.60600 1.000 58.59000  ? 317 GLY C O   1 
ATOM   9449  N  N   . ASN C  1 287 ? 15.73000  7.61500   -41.55100 1.000 60.48000  ? 318 ASN C N   1 
ATOM   9450  C  CA  . ASN C  1 287 ? 14.46300  8.28600   -41.83700 1.000 53.85000  ? 318 ASN C CA  1 
ATOM   9451  C  C   . ASN C  1 287 ? 14.62500  9.06000   -43.13900 1.000 55.93000  ? 318 ASN C C   1 
ATOM   9452  O  O   . ASN C  1 287 ? 15.38800  10.03100  -43.19600 1.000 57.61000  ? 318 ASN C O   1 
ATOM   9453  C  CB  . ASN C  1 287 ? 14.06100  9.22200   -40.70000 1.000 56.98000  ? 318 ASN C CB  1 
ATOM   9454  C  CG  . ASN C  1 287 ? 12.67100  9.81800   -40.89700 1.000 58.80000  ? 318 ASN C CG  1 
ATOM   9455  O  OD1 . ASN C  1 287 ? 12.22000  10.00400  -42.02700 1.000 53.54000  ? 318 ASN C OD1 1 
ATOM   9456  N  ND2 . ASN C  1 287 ? 11.99700  10.13900  -39.79400 1.000 53.24000  ? 318 ASN C ND2 1 
ATOM   9457  N  N   . PHE C  1 288 ? 13.93900  8.62700   -44.19900 1.000 54.09000  ? 319 PHE C N   1 
ATOM   9458  C  CA  . PHE C  1 288 ? 14.15600  9.34200   -45.45100 1.000 57.39000  ? 319 PHE C CA  1 
ATOM   9459  C  C   . PHE C  1 288 ? 13.38200  10.65900  -45.51600 1.000 56.95000  ? 319 PHE C C   1 
ATOM   9460  O  O   . PHE C  1 288 ? 13.42000  11.33300  -46.55400 1.000 51.61000  ? 319 PHE C O   1 
ATOM   9461  C  CB  . PHE C  1 288 ? 13.86600  8.44800   -46.67700 1.000 59.32000  ? 319 PHE C CB  1 
ATOM   9462  C  CG  . PHE C  1 288 ? 12.48100  7.81700   -46.72600 1.000 61.06000  ? 319 PHE C CG  1 
ATOM   9463  C  CD1 . PHE C  1 288 ? 11.38500  8.38100   -46.09300 1.000 56.44000  ? 319 PHE C CD1 1 
ATOM   9464  C  CD2 . PHE C  1 288 ? 12.29400  6.63900   -47.44000 1.000 57.12000  ? 319 PHE C CD2 1 
ATOM   9465  C  CE1 . PHE C  1 288 ? 10.12800  7.78100   -46.17100 1.000 65.29000  ? 319 PHE C CE1 1 
ATOM   9466  C  CE2 . PHE C  1 288 ? 11.04400  6.03300   -47.52000 1.000 66.54000  ? 319 PHE C CE2 1 
ATOM   9467  C  CZ  . PHE C  1 288 ? 9.95600   6.60700   -46.88600 1.000 62.59000  ? 319 PHE C CZ  1 
ATOM   9468  N  N   . ASN C  1 289 ? 12.69200  11.04100  -44.43700 1.000 54.90000  ? 320 ASN C N   1 
ATOM   9469  C  CA  . ASN C  1 289 ? 12.14400  12.38600  -44.31100 1.000 60.33000  ? 320 ASN C CA  1 
ATOM   9470  C  C   . ASN C  1 289 ? 13.15600  13.37300  -43.76700 1.000 63.06000  ? 320 ASN C C   1 
ATOM   9471  O  O   . ASN C  1 289 ? 12.90100  14.58000  -43.80400 1.000 66.40000  ? 320 ASN C O   1 
ATOM   9472  C  CB  . ASN C  1 289 ? 10.91600  12.40300  -43.39100 1.000 58.52000  ? 320 ASN C CB  1 
ATOM   9473  C  CG  . ASN C  1 289 ? 9.79100   11.54700  -43.92300 1.000 60.20000  ? 320 ASN C CG  1 
ATOM   9474  O  OD1 . ASN C  1 289 ? 9.33300   11.74100  -45.04600 1.000 57.02000  ? 320 ASN C OD1 1 
ATOM   9475  N  ND2 . ASN C  1 289 ? 9.35200   10.57700  -43.12400 1.000 64.15000  ? 320 ASN C ND2 1 
ATOM   9476  N  N   . HIS C  1 290 ? 14.28300  12.89600  -43.25200 1.000 59.72000  ? 321 HIS C N   1 
ATOM   9477  C  CA  . HIS C  1 290 ? 15.25000  13.75300  -42.58600 1.000 56.25000  ? 321 HIS C CA  1 
ATOM   9478  C  C   . HIS C  1 290 ? 16.65700  13.46800  -43.09600 1.000 56.73000  ? 321 HIS C C   1 
ATOM   9479  O  O   . HIS C  1 290 ? 17.59500  13.27600  -42.32300 1.000 59.07000  ? 321 HIS C O   1 
ATOM   9480  C  CB  . HIS C  1 290 ? 15.14100  13.55400  -41.08100 1.000 56.25000  ? 321 HIS C CB  1 
ATOM   9481  C  CG  . HIS C  1 290 ? 13.79000  13.89600  -40.52400 1.000 64.67000  ? 321 HIS C CG  1 
ATOM   9482  N  ND1 . HIS C  1 290 ? 13.03100  14.94800  -40.99500 1.000 68.93000  ? 321 HIS C ND1 1 
ATOM   9483  C  CD2 . HIS C  1 290 ? 13.05300  13.31000  -39.54700 1.000 64.56000  ? 321 HIS C CD2 1 
ATOM   9484  C  CE1 . HIS C  1 290 ? 11.89100  15.00000  -40.32700 1.000 72.46000  ? 321 HIS C CE1 1 
ATOM   9485  N  NE2 . HIS C  1 290 ? 11.87900  14.01800  -39.44200 1.000 67.52000  ? 321 HIS C NE2 1 
ATOM   9486  N  N   . GLY C  1 291 ? 16.81600  13.39200  -44.41700 1.000 51.48000  ? 322 GLY C N   1 
ATOM   9487  C  CA  . GLY C  1 291 ? 18.12600  13.40300  -45.04200 1.000 52.08000  ? 322 GLY C CA  1 
ATOM   9488  C  C   . GLY C  1 291 ? 18.74100  12.05200  -45.34700 1.000 55.86000  ? 322 GLY C C   1 
ATOM   9489  O  O   . GLY C  1 291 ? 19.73800  12.00200  -46.08800 1.000 52.44000  ? 322 GLY C O   1 
ATOM   9490  N  N   . ALA C  1 292 ? 18.16700  10.96200  -44.84000 1.000 53.82000  ? 323 ALA C N   1 
ATOM   9491  C  CA  . ALA C  1 292 ? 18.73100  9.62600   -44.95900 1.000 54.19000  ? 323 ALA C CA  1 
ATOM   9492  C  C   . ALA C  1 292 ? 18.33400  8.95500   -46.27900 1.000 56.75000  ? 323 ALA C C   1 
ATOM   9493  O  O   . ALA C  1 292 ? 17.33900  9.31000   -46.91700 1.000 56.96000  ? 323 ALA C O   1 
ATOM   9494  C  CB  . ALA C  1 292 ? 18.28500  8.76200   -43.77900 1.000 58.61000  ? 323 ALA C CB  1 
ATOM   9495  N  N   . ASN C  1 293 ? 19.13600  7.96500   -46.67500 1.000 59.71000  ? 324 ASN C N   1 
ATOM   9496  C  CA  . ASN C  1 293 ? 18.94200  7.18400   -47.89600 1.000 59.25000  ? 324 ASN C CA  1 
ATOM   9497  C  C   . ASN C  1 293 ? 19.14200  5.71100   -47.56800 1.000 58.66000  ? 324 ASN C C   1 
ATOM   9498  O  O   . ASN C  1 293 ? 20.24000  5.31600   -47.16600 1.000 61.33000  ? 324 ASN C O   1 
ATOM   9499  C  CB  . ASN C  1 293 ? 19.94800  7.60600   -48.97000 1.000 57.55000  ? 324 ASN C CB  1 
ATOM   9500  C  CG  . ASN C  1 293 ? 19.71200  6.91900   -50.30500 1.000 62.58000  ? 324 ASN C CG  1 
ATOM   9501  O  OD1 . ASN C  1 293 ? 18.98700  5.93500   -50.39500 1.000 58.37000  ? 324 ASN C OD1 1 
ATOM   9502  N  ND2 . ASN C  1 293 ? 20.40700  7.38500   -51.33200 1.000 67.12000  ? 324 ASN C ND2 1 
ATOM   9503  N  N   . ASN C  1 294 ? 18.11000  4.89600   -47.79200 1.000 52.24000  ? 325 ASN C N   1 
ATOM   9504  C  CA  . ASN C  1 294 ? 18.13600  3.47500   -47.47000 1.000 50.93000  ? 325 ASN C CA  1 
ATOM   9505  C  C   . ASN C  1 294 ? 18.30100  2.56600   -48.69900 1.000 61.34000  ? 325 ASN C C   1 
ATOM   9506  O  O   . ASN C  1 294 ? 18.02500  1.36200   -48.60900 1.000 62.31000  ? 325 ASN C O   1 
ATOM   9507  C  CB  . ASN C  1 294 ? 16.87500  3.10200   -46.70400 1.000 45.57000  ? 325 ASN C CB  1 
ATOM   9508  C  CG  . ASN C  1 294 ? 16.81800  3.76000   -45.34700 1.000 56.86000  ? 325 ASN C CG  1 
ATOM   9509  O  OD1 . ASN C  1 294 ? 17.84800  3.96000   -44.69800 1.000 60.88000  ? 325 ASN C OD1 1 
ATOM   9510  N  ND2 . ASN C  1 294 ? 15.61700  4.09200   -44.89900 1.000 56.88000  ? 325 ASN C ND2 1 
ATOM   9511  N  N   . TYR C  1 295 ? 18.72400  3.11000   -49.83900 1.000 57.41000  ? 326 TYR C N   1 
ATOM   9512  C  CA  . TYR C  1 295 ? 18.89100  2.30000   -51.04400 1.000 59.09000  ? 326 TYR C CA  1 
ATOM   9513  C  C   . TYR C  1 295 ? 19.81500  1.11200   -50.76700 1.000 60.56000  ? 326 TYR C C   1 
ATOM   9514  O  O   . TYR C  1 295 ? 20.79200  1.24800   -50.02100 1.000 59.74000  ? 326 TYR C O   1 
ATOM   9515  C  CB  . TYR C  1 295 ? 19.46500  3.14700   -52.18500 1.000 59.40000  ? 326 TYR C CB  1 
ATOM   9516  C  CG  . TYR C  1 295 ? 19.65100  2.40600   -53.50400 1.000 59.99000  ? 326 TYR C CG  1 
ATOM   9517  C  CD1 . TYR C  1 295 ? 18.59100  2.24500   -54.40700 1.000 63.53000  ? 326 TYR C CD1 1 
ATOM   9518  C  CD2 . TYR C  1 295 ? 20.88700  1.86500   -53.84700 1.000 58.92000  ? 326 TYR C CD2 1 
ATOM   9519  C  CE1 . TYR C  1 295 ? 18.77000  1.55800   -55.62100 1.000 59.91000  ? 326 TYR C CE1 1 
ATOM   9520  C  CE2 . TYR C  1 295 ? 21.07000  1.19000   -55.04600 1.000 62.63000  ? 326 TYR C CE2 1 
ATOM   9521  C  CZ  . TYR C  1 295 ? 20.01800  1.03800   -55.92400 1.000 63.73000  ? 326 TYR C CZ  1 
ATOM   9522  O  OH  . TYR C  1 295 ? 20.23800  0.36700   -57.09800 1.000 64.71000  ? 326 TYR C OH  1 
ATOM   9523  N  N   . PRO C  1 296 ? 19.51900  -0.08200  -51.31700 1.000 63.62000  ? 327 PRO C N   1 
ATOM   9524  C  CA  . PRO C  1 296 ? 18.38100  -0.42600  -52.19200 1.000 55.05000  ? 327 PRO C CA  1 
ATOM   9525  C  C   . PRO C  1 296 ? 17.18500  -0.93400  -51.42600 1.000 55.63000  ? 327 PRO C C   1 
ATOM   9526  O  O   . PRO C  1 296 ? 16.30200  -1.54900  -52.00300 1.000 57.45000  ? 327 PRO C O   1 
ATOM   9527  C  CB  . PRO C  1 296 ? 18.96600  -1.51600  -53.09200 1.000 55.95000  ? 327 PRO C CB  1 
ATOM   9528  C  CG  . PRO C  1 296 ? 19.96600  -2.23500  -52.19600 1.000 55.15000  ? 327 PRO C CG  1 
ATOM   9529  C  CD  . PRO C  1 296 ? 20.47300  -1.20500  -51.19900 1.000 56.22000  ? 327 PRO C CD  1 
ATOM   9530  N  N   . LEU C  1 297 ? 17.12600  -0.70500  -50.12000 1.000 56.66000  ? 328 LEU C N   1 
ATOM   9531  C  CA  . LEU C  1 297 ? 16.02800  -1.26100  -49.35300 1.000 55.30000  ? 328 LEU C CA  1 
ATOM   9532  C  C   . LEU C  1 297 ? 14.77000  -0.43000  -49.57300 1.000 60.31000  ? 328 LEU C C   1 
ATOM   9533  O  O   . LEU C  1 297 ? 14.81800  0.71700   -50.03200 1.000 63.73000  ? 328 LEU C O   1 
ATOM   9534  C  CB  . LEU C  1 297 ? 16.36700  -1.31000  -47.86400 1.000 59.18000  ? 328 LEU C CB  1 
ATOM   9535  C  CG  . LEU C  1 297 ? 17.75200  -1.82400  -47.47800 1.000 62.10000  ? 328 LEU C CG  1 
ATOM   9536  C  CD1 . LEU C  1 297 ? 17.91100  -1.85800  -45.96200 1.000 60.65000  ? 328 LEU C CD1 1 
ATOM   9537  C  CD2 . LEU C  1 297 ? 17.97900  -3.19600  -48.08000 1.000 66.35000  ? 328 LEU C CD2 1 
ATOM   9538  N  N   . LYS C  1 298 ? 13.63000  -1.05100  -49.29600 1.000 59.50000  ? 329 LYS C N   1 
ATOM   9539  C  CA  . LYS C  1 298 ? 12.34500  -0.37600  -49.33600 1.000 59.69000  ? 329 LYS C CA  1 
ATOM   9540  C  C   . LYS C  1 298 ? 12.03800  0.19200   -47.95800 1.000 55.67000  ? 329 LYS C C   1 
ATOM   9541  O  O   . LYS C  1 298 ? 12.34400  -0.43000  -46.93900 1.000 57.45000  ? 329 LYS C O   1 
ATOM   9542  C  CB  . LYS C  1 298 ? 11.23500  -1.34500  -49.74400 1.000 50.77000  ? 329 LYS C CB  1 
ATOM   9543  C  CG  . LYS C  1 298 ? 9.83700   -0.75600  -49.65800 1.000 51.73000  ? 329 LYS C CG  1 
ATOM   9544  C  CD  . LYS C  1 298 ? 8.75100   -1.79500  -49.93800 1.000 55.63000  ? 329 LYS C CD  1 
ATOM   9545  C  CE  . LYS C  1 298 ? 8.44400   -1.95700  -51.41400 1.000 55.32000  ? 329 LYS C CE  1 
ATOM   9546  N  NZ  . LYS C  1 298 ? 7.25700   -2.84200  -51.61300 1.000 54.00000  ? 329 LYS C NZ  1 
ATOM   9547  N  N   . GLY C  1 299 ? 11.43400  1.36100   -47.92700 1.000 55.81000  ? 330 GLY C N   1 
ATOM   9548  C  CA  . GLY C  1 299 ? 10.92100  1.86800   -46.67400 1.000 57.53000  ? 330 GLY C CA  1 
ATOM   9549  C  C   . GLY C  1 299 ? 11.93500  2.66300   -45.87700 1.000 61.28000  ? 330 GLY C C   1 
ATOM   9550  O  O   . GLY C  1 299 ? 13.04400  3.00300   -46.32400 1.000 63.02000  ? 330 GLY C O   1 
ATOM   9551  N  N   . THR C  1 300 ? 11.53700  2.92400   -44.63300 1.000 56.89000  ? 331 THR C N   1 
ATOM   9552  C  CA  . THR C  1 300 ? 12.15800  3.95200   -43.81600 1.000 57.69000  ? 331 THR C CA  1 
ATOM   9553  C  C   . THR C  1 300 ? 12.09700  3.54600   -42.34800 1.000 59.26000  ? 331 THR C C   1 
ATOM   9554  O  O   . THR C  1 300 ? 11.46600  2.54600   -41.97900 1.000 54.96000  ? 331 THR C O   1 
ATOM   9555  C  CB  . THR C  1 300 ? 11.46000  5.29500   -44.05700 1.000 54.90000  ? 331 THR C CB  1 
ATOM   9556  O  OG1 . THR C  1 300 ? 12.13900  6.34600   -43.36600 1.000 56.65000  ? 331 THR C OG1 1 
ATOM   9557  C  CG2 . THR C  1 300 ? 10.02300  5.22200   -43.60300 1.000 54.19000  ? 331 THR C CG2 1 
ATOM   9558  N  N   . LYS C  1 301 ? 12.78700  4.33400   -41.51700 1.000 54.23000  ? 332 LYS C N   1 
ATOM   9559  C  CA  . LYS C  1 301 ? 12.77700  4.17100   -40.06800 1.000 53.64000  ? 332 LYS C CA  1 
ATOM   9560  C  C   . LYS C  1 301 ? 11.36800  3.91000   -39.54700 1.000 53.59000  ? 332 LYS C C   1 
ATOM   9561  O  O   . LYS C  1 301 ? 10.43300  4.65000   -39.84900 1.000 51.71000  ? 332 LYS C O   1 
ATOM   9562  C  CB  . LYS C  1 301 ? 13.36500  5.42400   -39.41000 1.000 57.49000  ? 332 LYS C CB  1 
ATOM   9563  C  CG  . LYS C  1 301 ? 13.13300  5.53200   -37.90800 1.000 55.11000  ? 332 LYS C CG  1 
ATOM   9564  C  CD  . LYS C  1 301 ? 13.81600  6.77500   -37.31700 1.000 56.17000  ? 332 LYS C CD  1 
ATOM   9565  C  CE  . LYS C  1 301 ? 13.52000  6.91400   -35.82400 1.000 62.92000  ? 332 LYS C CE  1 
ATOM   9566  N  NZ  . LYS C  1 301 ? 14.26600  7.99900   -35.12900 1.000 65.99000  ? 332 LYS C NZ  1 
ATOM   9567  N  N   . GLY C  1 302 ? 11.22400  2.84700   -38.75600 1.000 56.60000  ? 333 GLY C N   1 
ATOM   9568  C  CA  . GLY C  1 302 ? 9.94800   2.45500   -38.21000 1.000 51.20000  ? 333 GLY C CA  1 
ATOM   9569  C  C   . GLY C  1 302 ? 9.25300   1.34100   -38.96500 1.000 58.28000  ? 333 GLY C C   1 
ATOM   9570  O  O   . GLY C  1 302 ? 8.28600   0.76500   -38.44100 1.000 60.17000  ? 333 GLY C O   1 
ATOM   9571  N  N   . ASP C  1 303 ? 9.70000   1.02700   -40.17500 1.000 58.19000  ? 334 ASP C N   1 
ATOM   9572  C  CA  . ASP C  1 303 ? 9.04200   0.01500   -40.99100 1.000 57.03000  ? 334 ASP C CA  1 
ATOM   9573  C  C   . ASP C  1 303 ? 9.56100   -1.37700  -40.66400 1.000 58.30000  ? 334 ASP C C   1 
ATOM   9574  O  O   . ASP C  1 303 ? 10.66500  -1.54900  -40.14000 1.000 58.37000  ? 334 ASP C O   1 
ATOM   9575  C  CB  . ASP C  1 303 ? 9.25900   0.29000   -42.48100 1.000 54.86000  ? 334 ASP C CB  1 
ATOM   9576  C  CG  . ASP C  1 303 ? 8.55400   1.53400   -42.94700 1.000 55.05000  ? 334 ASP C CG  1 
ATOM   9577  O  OD1 . ASP C  1 303 ? 7.60600   1.94000   -42.23700 1.000 59.11000  ? 334 ASP C OD1 1 
ATOM   9578  O  OD2 . ASP C  1 303 ? 8.92700   2.09000   -44.01200 1.000 50.33000  ? 334 ASP C OD2 1 
ATOM   9579  N  N   . THR C  1 304 ? 8.73800   -2.38000  -40.96800 1.000 54.89000  ? 335 THR C N   1 
ATOM   9580  C  CA  . THR C  1 304 ? 9.22500   -3.75000  -41.03500 1.000 54.66000  ? 335 THR C CA  1 
ATOM   9581  C  C   . THR C  1 304 ? 9.62500   -4.16300  -42.45300 1.000 61.62000  ? 335 THR C C   1 
ATOM   9582  O  O   . THR C  1 304 ? 9.99500   -5.32500  -42.66300 1.000 55.70000  ? 335 THR C O   1 
ATOM   9583  C  CB  . THR C  1 304 ? 8.19100   -4.72000  -40.46900 1.000 56.21000  ? 335 THR C CB  1 
ATOM   9584  O  OG1 . THR C  1 304 ? 6.90800   -4.43500  -41.03600 1.000 59.86000  ? 335 THR C OG1 1 
ATOM   9585  C  CG2 . THR C  1 304 ? 8.12900   -4.62100  -38.96100 1.000 55.48000  ? 335 THR C CG2 1 
ATOM   9586  N  N   . TRP C  1 305 ? 9.55900   -3.24900  -43.42700 1.000 56.16000  ? 336 TRP C N   1 
ATOM   9587  C  CA  . TRP C  1 305 ? 10.37700  -3.40400  -44.61700 1.000 51.73000  ? 336 TRP C CA  1 
ATOM   9588  C  C   . TRP C  1 305 ? 11.85000  -3.43500  -44.20700 1.000 58.95000  ? 336 TRP C C   1 
ATOM   9589  O  O   . TRP C  1 305 ? 12.22100  -2.99800  -43.11500 1.000 55.83000  ? 336 TRP C O   1 
ATOM   9590  C  CB  . TRP C  1 305 ? 10.14700  -2.25900  -45.59700 1.000 50.68000  ? 336 TRP C CB  1 
ATOM   9591  C  CG  . TRP C  1 305 ? 8.73600   -2.03700  -46.08700 1.000 58.89000  ? 336 TRP C CG  1 
ATOM   9592  C  CD1 . TRP C  1 305 ? 7.96600   -0.92900  -45.88800 1.000 58.95000  ? 336 TRP C CD1 1 
ATOM   9593  C  CD2 . TRP C  1 305 ? 7.95200   -2.92300  -46.90600 1.000 54.61000  ? 336 TRP C CD2 1 
ATOM   9594  N  NE1 . TRP C  1 305 ? 6.75300   -1.07400  -46.51300 1.000 51.84000  ? 336 TRP C NE1 1 
ATOM   9595  C  CE2 . TRP C  1 305 ? 6.71600   -2.28900  -47.14100 1.000 53.82000  ? 336 TRP C CE2 1 
ATOM   9596  C  CE3 . TRP C  1 305 ? 8.17300   -4.19500  -47.44900 1.000 59.82000  ? 336 TRP C CE3 1 
ATOM   9597  C  CZ2 . TRP C  1 305 ? 5.70600   -2.87300  -47.90500 1.000 55.89000  ? 336 TRP C CZ2 1 
ATOM   9598  C  CZ3 . TRP C  1 305 ? 7.16400   -4.78200  -48.20500 1.000 63.23000  ? 336 TRP C CZ3 1 
ATOM   9599  C  CH2 . TRP C  1 305 ? 5.94600   -4.11700  -48.42600 1.000 61.04000  ? 336 TRP C CH2 1 
ATOM   9600  N  N   . GLU C  1 306 ? 12.70300  -3.95000  -45.09600 1.000 55.11000  ? 337 GLU C N   1 
ATOM   9601  C  CA  . GLU C  1 306 ? 14.13100  -3.97000  -44.78700 1.000 54.93000  ? 337 GLU C CA  1 
ATOM   9602  C  C   . GLU C  1 306 ? 14.64600  -2.59600  -44.37100 1.000 59.58000  ? 337 GLU C C   1 
ATOM   9603  O  O   . GLU C  1 306 ? 15.53000  -2.49700  -43.50800 1.000 57.37000  ? 337 GLU C O   1 
ATOM   9604  C  CB  . GLU C  1 306 ? 14.94900  -4.48500  -45.98000 1.000 54.11000  ? 337 GLU C CB  1 
ATOM   9605  C  CG  . GLU C  1 306 ? 14.65200  -5.93600  -46.39100 1.000 59.52000  ? 337 GLU C CG  1 
ATOM   9606  C  CD  . GLU C  1 306 ? 15.07100  -6.96900  -45.34600 1.000 56.69000  ? 337 GLU C CD  1 
ATOM   9607  O  OE1 . GLU C  1 306 ? 16.24200  -7.39500  -45.35700 1.000 56.39000  ? 337 GLU C OE1 1 
ATOM   9608  O  OE2 . GLU C  1 306 ? 14.22300  -7.36000  -44.51400 1.000 54.43000  ? 337 GLU C OE2 1 
ATOM   9609  N  N   . GLY C  1 307 ? 14.11000  -1.52800  -44.96800 1.000 57.14000  ? 338 GLY C N   1 
ATOM   9610  C  CA  . GLY C  1 307 ? 14.60700  -0.18600  -44.70400 1.000 54.71000  ? 338 GLY C CA  1 
ATOM   9611  C  C   . GLY C  1 307 ? 14.48700  0.25300   -43.26000 1.000 53.62000  ? 338 GLY C C   1 
ATOM   9612  O  O   . GLY C  1 307 ? 15.20900  1.15600   -42.84100 1.000 53.86000  ? 338 GLY C O   1 
ATOM   9613  N  N   . GLY C  1 308 ? 13.58700  -0.35800  -42.49200 1.000 52.86000  ? 339 GLY C N   1 
ATOM   9614  C  CA  . GLY C  1 308 ? 13.41100  -0.00400  -41.09700 1.000 52.92000  ? 339 GLY C CA  1 
ATOM   9615  C  C   . GLY C  1 308 ? 14.46700  -0.51100  -40.12800 1.000 59.32000  ? 339 GLY C C   1 
ATOM   9616  O  O   . GLY C  1 308 ? 14.85200  0.20300   -39.18900 1.000 54.16000  ? 339 GLY C O   1 
ATOM   9617  N  N   . TYR C  1 309 ? 14.94100  -1.74900  -40.31000 1.000 57.55000  ? 340 TYR C N   1 
ATOM   9618  C  CA  . TYR C  1 309 ? 15.80300  -2.33000  -39.28800 1.000 49.60000  ? 340 TYR C CA  1 
ATOM   9619  C  C   . TYR C  1 309 ? 17.00500  -3.07700  -39.85200 1.000 57.32000  ? 340 TYR C C   1 
ATOM   9620  O  O   . TYR C  1 309 ? 17.76600  -3.67100  -39.07000 1.000 53.45000  ? 340 TYR C O   1 
ATOM   9621  C  CB  . TYR C  1 309 ? 14.99200  -3.23900  -38.36900 1.000 50.23000  ? 340 TYR C CB  1 
ATOM   9622  C  CG  . TYR C  1 309 ? 14.33700  -4.43800  -39.03100 1.000 60.85000  ? 340 TYR C CG  1 
ATOM   9623  C  CD1 . TYR C  1 309 ? 13.22900  -4.28700  -39.86600 1.000 59.72000  ? 340 TYR C CD1 1 
ATOM   9624  C  CD2 . TYR C  1 309 ? 14.78200  -5.72600  -38.76300 1.000 55.97000  ? 340 TYR C CD2 1 
ATOM   9625  C  CE1 . TYR C  1 309 ? 12.62300  -5.38100  -40.44800 1.000 59.65000  ? 340 TYR C CE1 1 
ATOM   9626  C  CE2 . TYR C  1 309 ? 14.17600  -6.81800  -39.32800 1.000 61.09000  ? 340 TYR C CE2 1 
ATOM   9627  C  CZ  . TYR C  1 309 ? 13.10200  -6.64100  -40.17800 1.000 58.84000  ? 340 TYR C CZ  1 
ATOM   9628  O  OH  . TYR C  1 309 ? 12.51400  -7.74000  -40.74300 1.000 62.05000  ? 340 TYR C OH  1 
ATOM   9629  N  N   . ARG C  1 310 ? 17.24100  -3.01200  -41.16000 1.000 56.74000  ? 341 ARG C N   1 
ATOM   9630  C  CA  . ARG C  1 310 ? 18.46100  -3.53600  -41.76000 1.000 53.23000  ? 341 ARG C CA  1 
ATOM   9631  C  C   . ARG C  1 310 ? 19.48400  -2.40800  -41.86600 1.000 55.19000  ? 341 ARG C C   1 
ATOM   9632  O  O   . ARG C  1 310 ? 19.22500  -1.39400  -42.51800 1.000 57.45000  ? 341 ARG C O   1 
ATOM   9633  C  CB  . ARG C  1 310 ? 18.13900  -4.13400  -43.12900 1.000 53.97000  ? 341 ARG C CB  1 
ATOM   9634  C  CG  . ARG C  1 310 ? 19.24700  -4.91300  -43.74400 1.000 55.75000  ? 341 ARG C CG  1 
ATOM   9635  C  CD  . ARG C  1 310 ? 18.79100  -5.59300  -45.03000 1.000 55.82000  ? 341 ARG C CD  1 
ATOM   9636  N  NE  . ARG C  1 310 ? 19.93200  -6.13700  -45.75200 1.000 56.69000  ? 341 ARG C NE  1 
ATOM   9637  C  CZ  . ARG C  1 310 ? 19.85000  -7.08900  -46.67000 1.000 57.52000  ? 341 ARG C CZ  1 
ATOM   9638  N  NH1 . ARG C  1 310 ? 18.69100  -7.64200  -46.98800 1.000 48.71000  ? 341 ARG C NH1 1 
ATOM   9639  N  NH2 . ARG C  1 310 ? 20.96000  -7.49800  -47.27600 1.000 48.74000  ? 341 ARG C NH2 1 
ATOM   9640  N  N   . VAL C  1 311 ? 20.65600  -2.60500  -41.26800 1.000 54.65000  ? 342 VAL C N   1 
ATOM   9641  C  CA  . VAL C  1 311 ? 21.59600  -1.51300  -41.02100 1.000 54.24000  ? 342 VAL C CA  1 
ATOM   9642  C  C   . VAL C  1 311 ? 22.97200  -1.90800  -41.53800 1.000 58.16000  ? 342 VAL C C   1 
ATOM   9643  O  O   . VAL C  1 311 ? 23.29000  -3.10100  -41.66500 1.000 59.47000  ? 342 VAL C O   1 
ATOM   9644  C  CB  . VAL C  1 311 ? 21.67900  -1.17400  -39.51400 1.000 52.92000  ? 342 VAL C CB  1 
ATOM   9645  C  CG1 . VAL C  1 311 ? 20.30500  -0.80000  -38.96100 1.000 50.88000  ? 342 VAL C CG1 1 
ATOM   9646  C  CG2 . VAL C  1 311 ? 22.24900  -2.34600  -38.74600 1.000 47.35000  ? 342 VAL C CG2 1 
ATOM   9647  N  N   . PRO C  1 312 ? 23.82500  -0.93100  -41.82800 1.000 56.96000  ? 343 PRO C N   1 
ATOM   9648  C  CA  . PRO C  1 312 ? 25.23900  -1.25100  -42.05300 1.000 58.20000  ? 343 PRO C CA  1 
ATOM   9649  C  C   . PRO C  1 312 ? 25.90500  -1.68800  -40.75300 1.000 57.63000  ? 343 PRO C C   1 
ATOM   9650  O  O   . PRO C  1 312 ? 25.52000  -1.27000  -39.65600 1.000 50.44000  ? 343 PRO C O   1 
ATOM   9651  C  CB  . PRO C  1 312 ? 25.83200  0.06400   -42.58300 1.000 54.86000  ? 343 PRO C CB  1 
ATOM   9652  C  CG  . PRO C  1 312 ? 24.90500  1.13800   -42.06900 1.000 58.75000  ? 343 PRO C CG  1 
ATOM   9653  C  CD  . PRO C  1 312 ? 23.53100  0.49800   -42.04900 1.000 57.53000  ? 343 PRO C CD  1 
ATOM   9654  N  N   . MET C  1 313 ? 26.90300  -2.56200  -40.89200 1.000 57.34000  ? 344 MET C N   1 
ATOM   9655  C  CA  . MET C  1 313 ? 27.67100  -3.04900  -39.75600 1.000 51.14000  ? 344 MET C CA  1 
ATOM   9656  C  C   . MET C  1 313 ? 28.95600  -3.67900  -40.25500 1.000 55.55000  ? 344 MET C C   1 
ATOM   9657  O  O   . MET C  1 313 ? 28.95500  -4.36300  -41.27900 1.000 59.41000  ? 344 MET C O   1 
ATOM   9658  C  CB  . MET C  1 313 ? 26.90900  -4.09100  -38.92600 1.000 55.99000  ? 344 MET C CB  1 
ATOM   9659  C  CG  . MET C  1 313 ? 27.71200  -4.59800  -37.69800 1.000 52.40000  ? 344 MET C CG  1 
ATOM   9660  S  SD  . MET C  1 313 ? 26.76600  -5.60400  -36.52700 1.000 59.01000  ? 344 MET C SD  1 
ATOM   9661  C  CE  . MET C  1 313 ? 26.53000  -7.08800  -37.49200 1.000 64.72000  ? 344 MET C CE  1 
ATOM   9662  N  N   . PHE C  1 314 ? 30.04400  -3.44700  -39.52400 1.000 58.28000  ? 345 PHE C N   1 
ATOM   9663  C  CA  . PHE C  1 314 ? 31.28000  -4.18400  -39.72500 1.000 58.60000  ? 345 PHE C CA  1 
ATOM   9664  C  C   . PHE C  1 314 ? 31.89200  -4.52500  -38.37400 1.000 60.94000  ? 345 PHE C C   1 
ATOM   9665  O  O   . PHE C  1 314 ? 31.57600  -3.90300  -37.35600 1.000 57.22000  ? 345 PHE C O   1 
ATOM   9666  C  CB  . PHE C  1 314 ? 32.28300  -3.41700  -40.59700 1.000 53.17000  ? 345 PHE C CB  1 
ATOM   9667  C  CG  . PHE C  1 314 ? 32.83000  -2.15600  -39.97900 1.000 56.22000  ? 345 PHE C CG  1 
ATOM   9668  C  CD1 . PHE C  1 314 ? 33.76100  -2.20300  -38.94500 1.000 53.75000  ? 345 PHE C CD1 1 
ATOM   9669  C  CD2 . PHE C  1 314 ? 32.48300  -0.91700  -40.49700 1.000 55.64000  ? 345 PHE C CD2 1 
ATOM   9670  C  CE1 . PHE C  1 314 ? 34.30600  -1.03800  -38.39600 1.000 54.50000  ? 345 PHE C CE1 1 
ATOM   9671  C  CE2 . PHE C  1 314 ? 33.01700  0.25800   -39.95100 1.000 62.96000  ? 345 PHE C CE2 1 
ATOM   9672  C  CZ  . PHE C  1 314 ? 33.93300  0.19200   -38.89500 1.000 60.76000  ? 345 PHE C CZ  1 
ATOM   9673  N  N   . PHE C  1 315 ? 32.71700  -5.57900  -38.37800 1.000 63.23000  ? 346 PHE C N   1 
ATOM   9674  C  CA  . PHE C  1 315 ? 33.64600  -5.92300  -37.30500 1.000 49.97000  ? 346 PHE C CA  1 
ATOM   9675  C  C   . PHE C  1 315 ? 35.06600  -5.66500  -37.78700 1.000 58.23000  ? 346 PHE C C   1 
ATOM   9676  O  O   . PHE C  1 315 ? 35.41700  -6.03300  -38.91200 1.000 60.39000  ? 346 PHE C O   1 
ATOM   9677  C  CB  . PHE C  1 315 ? 33.55600  -7.40000  -36.91400 1.000 56.05000  ? 346 PHE C CB  1 
ATOM   9678  C  CG  . PHE C  1 315 ? 32.33400  -7.77000  -36.11300 1.000 55.01000  ? 346 PHE C CG  1 
ATOM   9679  C  CD1 . PHE C  1 315 ? 31.22800  -6.93800  -36.05800 1.000 55.51000  ? 346 PHE C CD1 1 
ATOM   9680  C  CD2 . PHE C  1 315 ? 32.29500  -8.98100  -35.42800 1.000 53.57000  ? 346 PHE C CD2 1 
ATOM   9681  C  CE1 . PHE C  1 315 ? 30.11100  -7.30000  -35.33300 1.000 57.53000  ? 346 PHE C CE1 1 
ATOM   9682  C  CE2 . PHE C  1 315 ? 31.18200  -9.34700  -34.70000 1.000 56.44000  ? 346 PHE C CE2 1 
ATOM   9683  C  CZ  . PHE C  1 315 ? 30.08900  -8.50900  -34.64900 1.000 58.20000  ? 346 PHE C CZ  1 
ATOM   9684  N  N   . HIS C  1 316 ? 35.89500  -5.05900  -36.94100 1.000 58.52000  ? 347 HIS C N   1 
ATOM   9685  C  CA  . HIS C  1 316 ? 37.29500  -4.81800  -37.27700 1.000 60.55000  ? 347 HIS C CA  1 
ATOM   9686  C  C   . HIS C  1 316 ? 38.17400  -5.19100  -36.09400 1.000 63.16000  ? 347 HIS C C   1 
ATOM   9687  O  O   . HIS C  1 316 ? 38.09700  -4.56000  -35.03400 1.000 56.74000  ? 347 HIS C O   1 
ATOM   9688  C  CB  . HIS C  1 316 ? 37.53300  -3.36500  -37.67800 1.000 59.23000  ? 347 HIS C CB  1 
ATOM   9689  C  CG  . HIS C  1 316 ? 38.98000  -3.00000  -37.81100 1.000 59.27000  ? 347 HIS C CG  1 
ATOM   9690  N  ND1 . HIS C  1 316 ? 39.63800  -2.99500  -39.02300 1.000 68.18000  ? 347 HIS C ND1 1 
ATOM   9691  C  CD2 . HIS C  1 316 ? 39.88100  -2.57600  -36.89400 1.000 61.69000  ? 347 HIS C CD2 1 
ATOM   9692  C  CE1 . HIS C  1 316 ? 40.88800  -2.60600  -38.84400 1.000 59.11000  ? 347 HIS C CE1 1 
ATOM   9693  N  NE2 . HIS C  1 316 ? 41.05800  -2.33900  -37.56300 1.000 60.59000  ? 347 HIS C NE2 1 
ATOM   9694  N  N   . TRP C  1 317 ? 39.03300  -6.18600  -36.29500 1.000 60.96000  ? 348 TRP C N   1 
ATOM   9695  C  CA  . TRP C  1 317 ? 39.84700  -6.75400  -35.23600 1.000 62.55000  ? 348 TRP C CA  1 
ATOM   9696  C  C   . TRP C  1 317 ? 41.07700  -7.39000  -35.86100 1.000 63.76000  ? 348 TRP C C   1 
ATOM   9697  O  O   . TRP C  1 317 ? 41.05400  -8.58100  -36.19200 1.000 64.27000  ? 348 TRP C O   1 
ATOM   9698  C  CB  . TRP C  1 317 ? 39.05400  -7.78600  -34.44500 1.000 62.61000  ? 348 TRP C CB  1 
ATOM   9699  C  CG  . TRP C  1 317 ? 39.77800  -8.32200  -33.26200 1.000 63.83000  ? 348 TRP C CG  1 
ATOM   9700  C  CD1 . TRP C  1 317 ? 40.93900  -7.83500  -32.70300 1.000 66.81000  ? 348 TRP C CD1 1 
ATOM   9701  C  CD2 . TRP C  1 317 ? 39.37600  -9.42000  -32.44700 1.000 64.24000  ? 348 TRP C CD2 1 
ATOM   9702  N  NE1 . TRP C  1 317 ? 41.28400  -8.58000  -31.60100 1.000 64.78000  ? 348 TRP C NE1 1 
ATOM   9703  C  CE2 . TRP C  1 317 ? 40.34200  -9.56000  -31.42300 1.000 67.70000  ? 348 TRP C CE2 1 
ATOM   9704  C  CE3 . TRP C  1 317 ? 38.30100  -10.30700 -32.48500 1.000 63.66000  ? 348 TRP C CE3 1 
ATOM   9705  C  CZ2 . TRP C  1 317 ? 40.25700  -10.55100 -30.45300 1.000 67.31000  ? 348 TRP C CZ2 1 
ATOM   9706  C  CZ3 . TRP C  1 317 ? 38.21700  -11.29100 -31.51500 1.000 69.38000  ? 348 TRP C CZ3 1 
ATOM   9707  C  CH2 . TRP C  1 317 ? 39.18900  -11.40600 -30.51600 1.000 62.71000  ? 348 TRP C CH2 1 
ATOM   9708  N  N   . PRO C  1 318 ? 42.14600  -6.62100  -36.07000 1.000 62.96000  ? 349 PRO C N   1 
ATOM   9709  C  CA  . PRO C  1 318 ? 43.28000  -7.13800  -36.85700 1.000 70.98000  ? 349 PRO C CA  1 
ATOM   9710  C  C   . PRO C  1 318 ? 43.85400  -8.44100  -36.32900 1.000 73.20000  ? 349 PRO C C   1 
ATOM   9711  O  O   . PRO C  1 318 ? 44.21300  -9.31200  -37.12900 1.000 73.96000  ? 349 PRO C O   1 
ATOM   9712  C  CB  . PRO C  1 318 ? 44.29900  -5.99500  -36.77500 1.000 65.53000  ? 349 PRO C CB  1 
ATOM   9713  C  CG  . PRO C  1 318 ? 43.44200  -4.76500  -36.61500 1.000 68.76000  ? 349 PRO C CG  1 
ATOM   9714  C  CD  . PRO C  1 318 ? 42.31600  -5.20300  -35.71000 1.000 65.85000  ? 349 PRO C CD  1 
ATOM   9715  N  N   . LYS C  1 319 ? 43.88800  -8.63400  -35.00700 1.000 70.56000  ? 350 LYS C N   1 
ATOM   9716  C  CA  . LYS C  1 319 ? 44.50700  -9.83300  -34.45700 1.000 69.17000  ? 350 LYS C CA  1 
ATOM   9717  C  C   . LYS C  1 319 ? 43.82300  -11.10900 -34.92000 1.000 69.35000  ? 350 LYS C C   1 
ATOM   9718  O  O   . LYS C  1 319 ? 44.47500  -12.15200 -34.98300 1.000 73.03000  ? 350 LYS C O   1 
ATOM   9719  C  CB  . LYS C  1 319 ? 44.50300  -9.78400  -32.92600 1.000 73.56000  ? 350 LYS C CB  1 
ATOM   9720  C  CG  . LYS C  1 319 ? 45.29200  -10.91300 -32.25700 1.000 69.27000  ? 350 LYS C CG  1 
ATOM   9721  C  CD  . LYS C  1 319 ? 45.05100  -10.96400 -30.75200 1.000 66.97000  ? 350 LYS C CD  1 
ATOM   9722  C  CE  . LYS C  1 319 ? 43.74700  -11.67900 -30.41000 1.000 75.49000  ? 350 LYS C CE  1 
ATOM   9723  N  NZ  . LYS C  1 319 ? 43.64100  -11.97700 -28.94200 1.000 75.30000  ? 350 LYS C NZ  1 
ATOM   9724  N  N   . LYS C  1 320 ? 42.55400  -11.05300 -35.29700 1.000 67.37000  ? 351 LYS C N   1 
ATOM   9725  C  CA  . LYS C  1 320 ? 41.85800  -12.29200 -35.62400 1.000 67.33000  ? 351 LYS C CA  1 
ATOM   9726  C  C   . LYS C  1 320 ? 41.00200  -12.24300 -36.88600 1.000 68.79000  ? 351 LYS C C   1 
ATOM   9727  O  O   . LYS C  1 320 ? 40.90800  -13.26900 -37.56500 1.000 68.84000  ? 351 LYS C O   1 
ATOM   9728  C  CB  . LYS C  1 320 ? 40.98900  -12.73100 -34.44400 1.000 69.41000  ? 351 LYS C CB  1 
ATOM   9729  C  CG  . LYS C  1 320 ? 41.80900  -13.10700 -33.22300 1.000 73.15000  ? 351 LYS C CG  1 
ATOM   9730  C  CD  . LYS C  1 320 ? 41.26300  -14.33700 -32.52900 1.000 68.16000  ? 351 LYS C CD  1 
ATOM   9731  C  CE  . LYS C  1 320 ? 42.29400  -14.91300 -31.56300 1.000 81.20000  ? 351 LYS C CE  1 
ATOM   9732  N  NZ  . LYS C  1 320 ? 43.50300  -15.42500 -32.27600 1.000 83.92000  ? 351 LYS C NZ  1 
ATOM   9733  N  N   . ILE C  1 321 ? 40.38500  -11.11700 -37.24400 1.000 73.68000  ? 352 ILE C N   1 
ATOM   9734  C  CA  . ILE C  1 321 ? 39.49000  -11.05700 -38.39800 1.000 67.14000  ? 352 ILE C CA  1 
ATOM   9735  C  C   . ILE C  1 321 ? 40.28500  -10.67500 -39.63900 1.000 64.18000  ? 352 ILE C C   1 
ATOM   9736  O  O   . ILE C  1 321 ? 40.98900  -9.66000  -39.64800 1.000 65.50000  ? 352 ILE C O   1 
ATOM   9737  C  CB  . ILE C  1 321 ? 38.33900  -10.07200 -38.15000 1.000 70.61000  ? 352 ILE C CB  1 
ATOM   9738  C  CG1 . ILE C  1 321 ? 37.56800  -10.50000 -36.89700 1.000 69.28000  ? 352 ILE C CG1 1 
ATOM   9739  C  CG2 . ILE C  1 321 ? 37.41600  -10.00600 -39.37100 1.000 71.25000  ? 352 ILE C CG2 1 
ATOM   9740  C  CD1 . ILE C  1 321 ? 36.24100  -9.82700  -36.72200 1.000 60.03000  ? 352 ILE C CD1 1 
ATOM   9741  N  N   . LYS C  1 322 ? 40.18900  -11.50300 -40.67900 1.000 72.50000  ? 353 LYS C N   1 
ATOM   9742  C  CA  . LYS C  1 322 ? 40.89400  -11.25400 -41.93200 1.000 69.64000  ? 353 LYS C CA  1 
ATOM   9743  C  C   . LYS C  1 322 ? 40.27700  -10.05700 -42.65100 1.000 75.37000  ? 353 LYS C C   1 
ATOM   9744  O  O   . LYS C  1 322 ? 39.07800  -9.78400  -42.53800 1.000 69.99000  ? 353 LYS C O   1 
ATOM   9745  C  CB  . LYS C  1 322 ? 40.81700  -12.49200 -42.83200 1.000 69.98000  ? 353 LYS C CB  1 
ATOM   9746  C  CG  . LYS C  1 322 ? 42.11700  -12.91900 -43.51100 1.000 72.01000  ? 353 LYS C CG  1 
ATOM   9747  C  CD  . LYS C  1 322 ? 41.96200  -14.32400 -44.12200 1.000 66.99000  ? 353 LYS C CD  1 
ATOM   9748  C  CE  . LYS C  1 322 ? 43.27100  -14.88400 -44.71900 1.000 73.30000  ? 353 LYS C CE  1 
ATOM   9749  N  NZ  . LYS C  1 322 ? 43.64100  -14.36100 -46.07800 1.000 76.01000  ? 353 LYS C NZ  1 
ATOM   9750  N  N   . LYS C  1 323 ? 41.10700  -9.36200  -43.42600 1.000 77.93000  ? 354 LYS C N   1 
ATOM   9751  C  CA  . LYS C  1 323 ? 40.69200  -8.18300  -44.17100 1.000 71.43000  ? 354 LYS C CA  1 
ATOM   9752  C  C   . LYS C  1 323 ? 39.89600  -8.57100  -45.41900 1.000 75.28000  ? 354 LYS C C   1 
ATOM   9753  O  O   . LYS C  1 323 ? 39.92100  -9.71700  -45.87400 1.000 74.57000  ? 354 LYS C O   1 
ATOM   9754  C  CB  . LYS C  1 323 ? 41.90800  -7.33500  -44.54900 1.000 72.44000  ? 354 LYS C CB  1 
ATOM   9755  C  CG  . LYS C  1 323 ? 43.20600  -8.11800  -44.61500 1.000 79.00000  ? 354 LYS C CG  1 
ATOM   9756  C  CD  . LYS C  1 323 ? 44.40700  -7.19600  -44.70300 1.000 74.57000  ? 354 LYS C CD  1 
ATOM   9757  C  CE  . LYS C  1 323 ? 44.44400  -6.21200  -43.54500 1.000 72.69000  ? 354 LYS C CE  1 
ATOM   9758  N  NZ  . LYS C  1 323 ? 45.69400  -5.39700  -43.58100 1.000 71.05000  ? 354 LYS C NZ  1 
ATOM   9759  N  N   . ASP C  1 324 ? 39.17100  -7.58400  -45.96000 1.000 75.24000  ? 355 ASP C N   1 
ATOM   9760  C  CA  . ASP C  1 324 ? 38.38400  -7.72600  -47.18900 1.000 72.74000  ? 355 ASP C CA  1 
ATOM   9761  C  C   . ASP C  1 324 ? 37.34500  -8.83400  -47.08500 1.000 69.84000  ? 355 ASP C C   1 
ATOM   9762  O  O   . ASP C  1 324 ? 36.93600  -9.40700  -48.09400 1.000 72.29000  ? 355 ASP C O   1 
ATOM   9763  C  CB  . ASP C  1 324 ? 39.27000  -7.94000  -48.41800 1.000 78.06000  ? 355 ASP C CB  1 
ATOM   9764  C  CG  . ASP C  1 324 ? 40.06300  -6.69500  -48.78800 1.000 90.71000  ? 355 ASP C CG  1 
ATOM   9765  O  OD1 . ASP C  1 324 ? 39.44000  -5.61100  -48.87500 1.000 91.25000  ? 355 ASP C OD1 1 
ATOM   9766  O  OD2 . ASP C  1 324 ? 41.29600  -6.79200  -49.00500 1.000 96.20000  ? 355 ASP C OD2 1 
ATOM   9767  N  N   . GLN C  1 325 ? 36.89800  -9.14400  -45.87300 1.000 63.95000  ? 356 GLN C N   1 
ATOM   9768  C  CA  . GLN C  1 325 ? 35.88300  -10.16600 -45.68900 1.000 65.55000  ? 356 GLN C CA  1 
ATOM   9769  C  C   . GLN C  1 325 ? 34.49400  -9.55900  -45.85600 1.000 69.29000  ? 356 GLN C C   1 
ATOM   9770  O  O   . GLN C  1 325 ? 34.25300  -8.41500  -45.45500 1.000 63.38000  ? 356 GLN C O   1 
ATOM   9771  C  CB  . GLN C  1 325 ? 36.01100  -10.81900 -44.30600 1.000 70.38000  ? 356 GLN C CB  1 
ATOM   9772  C  CG  . GLN C  1 325 ? 34.91400  -11.86500 -44.00300 1.000 73.81000  ? 356 GLN C CG  1 
ATOM   9773  C  CD  . GLN C  1 325 ? 34.91600  -12.35300 -42.54500 1.000 81.16000  ? 356 GLN C CD  1 
ATOM   9774  O  OE1 . GLN C  1 325 ? 33.92100  -12.91800 -42.05800 1.000 76.63000  ? 356 GLN C OE1 1 
ATOM   9775  N  NE2 . GLN C  1 325 ? 36.02700  -12.12600 -41.84500 1.000 71.34000  ? 356 GLN C NE2 1 
ATOM   9776  N  N   . ARG C  1 326 ? 33.58400  -10.33300 -46.45600 1.000 69.11000  ? 357 ARG C N   1 
ATOM   9777  C  CA  . ARG C  1 326 ? 32.16600  -10.00300 -46.51100 1.000 60.10000  ? 357 ARG C CA  1 
ATOM   9778  C  C   . ARG C  1 326 ? 31.37900  -11.17500 -45.94800 1.000 66.83000  ? 357 ARG C C   1 
ATOM   9779  O  O   . ARG C  1 326 ? 31.43100  -12.28400 -46.49400 1.000 65.09000  ? 357 ARG C O   1 
ATOM   9780  C  CB  . ARG C  1 326 ? 31.69300  -9.67700  -47.93500 1.000 65.19000  ? 357 ARG C CB  1 
ATOM   9781  C  CG  . ARG C  1 326 ? 32.34800  -8.44400  -48.52300 1.000 68.34000  ? 357 ARG C CG  1 
ATOM   9782  C  CD  . ARG C  1 326 ? 31.76700  -8.02500  -49.87900 1.000 71.65000  ? 357 ARG C CD  1 
ATOM   9783  N  NE  . ARG C  1 326 ? 31.78000  -6.56700  -49.94300 1.000 75.77000  ? 357 ARG C NE  1 
ATOM   9784  C  CZ  . ARG C  1 326 ? 30.71200  -5.79400  -49.80000 1.000 66.94000  ? 357 ARG C CZ  1 
ATOM   9785  N  NH1 . ARG C  1 326 ? 29.49800  -6.30600  -49.67200 1.000 70.71000  ? 357 ARG C NH1 1 
ATOM   9786  N  NH2 . ARG C  1 326 ? 30.87200  -4.47500  -49.73300 1.000 67.85000  ? 357 ARG C NH2 1 
ATOM   9787  N  N   . PHE C  1 327 ? 30.64900  -10.92600 -44.86900 1.000 60.89000  ? 358 PHE C N   1 
ATOM   9788  C  CA  . PHE C  1 327 ? 29.84600  -11.93900 -44.19500 1.000 61.43000  ? 358 PHE C CA  1 
ATOM   9789  C  C   . PHE C  1 327 ? 28.38400  -11.74500 -44.58500 1.000 63.03000  ? 358 PHE C C   1 
ATOM   9790  O  O   . PHE C  1 327 ? 27.76000  -10.75300 -44.19500 1.000 65.81000  ? 358 PHE C O   1 
ATOM   9791  C  CB  . PHE C  1 327 ? 30.03700  -11.84700 -42.68200 1.000 65.52000  ? 358 PHE C CB  1 
ATOM   9792  C  CG  . PHE C  1 327 ? 29.48500  -13.01600 -41.94000 1.000 64.93000  ? 358 PHE C CG  1 
ATOM   9793  C  CD1 . PHE C  1 327 ? 30.24700  -14.14800 -41.73900 1.000 67.70000  ? 358 PHE C CD1 1 
ATOM   9794  C  CD2 . PHE C  1 327 ? 28.18600  -12.99200 -41.46500 1.000 60.69000  ? 358 PHE C CD2 1 
ATOM   9795  C  CE1 . PHE C  1 327 ? 29.72900  -15.22700 -41.06500 1.000 68.89000  ? 358 PHE C CE1 1 
ATOM   9796  C  CE2 . PHE C  1 327 ? 27.66300  -14.07600 -40.79700 1.000 62.29000  ? 358 PHE C CE2 1 
ATOM   9797  C  CZ  . PHE C  1 327 ? 28.43200  -15.19100 -40.59800 1.000 64.27000  ? 358 PHE C CZ  1 
ATOM   9798  N  N   . ASP C  1 328 ? 27.83800  -12.69700 -45.34500 1.000 63.53000  ? 359 ASP C N   1 
ATOM   9799  C  CA  . ASP C  1 328 ? 26.53100  -12.55800 -45.97700 1.000 59.38000  ? 359 ASP C CA  1 
ATOM   9800  C  C   . ASP C  1 328 ? 25.42300  -13.29600 -45.24900 1.000 59.40000  ? 359 ASP C C   1 
ATOM   9801  O  O   . ASP C  1 328 ? 24.27500  -13.24800 -45.69500 1.000 64.39000  ? 359 ASP C O   1 
ATOM   9802  C  CB  . ASP C  1 328 ? 26.58600  -13.04800 -47.42400 1.000 53.13000  ? 359 ASP C CB  1 
ATOM   9803  C  CG  . ASP C  1 328 ? 27.56200  -12.25700 -48.25200 1.000 65.27000  ? 359 ASP C CG  1 
ATOM   9804  O  OD1 . ASP C  1 328 ? 27.67600  -11.04000 -47.98300 1.000 63.80000  ? 359 ASP C OD1 1 
ATOM   9805  O  OD2 . ASP C  1 328 ? 28.19500  -12.83700 -49.17100 1.000 62.50000  ? 359 ASP C OD2 1 
ATOM   9806  N  N   . PHE C  1 329 ? 25.72600  -13.98600 -44.18000 1.000 62.25000  ? 360 PHE C N   1 
ATOM   9807  C  CA  . PHE C  1 329 ? 24.64100  -14.63100 -43.46400 1.000 62.37000  ? 360 PHE C CA  1 
ATOM   9808  C  C   . PHE C  1 329 ? 23.94400  -13.62800 -42.55700 1.000 60.22000  ? 360 PHE C C   1 
ATOM   9809  O  O   . PHE C  1 329 ? 24.56700  -12.67000 -42.09100 1.000 61.69000  ? 360 PHE C O   1 
ATOM   9810  C  CB  . PHE C  1 329 ? 25.15700  -15.80000 -42.64000 1.000 68.97000  ? 360 PHE C CB  1 
ATOM   9811  C  CG  . PHE C  1 329 ? 25.83900  -16.84800 -43.45600 1.000 72.46000  ? 360 PHE C CG  1 
ATOM   9812  C  CD1 . PHE C  1 329 ? 27.18900  -16.74800 -43.75400 1.000 74.96000  ? 360 PHE C CD1 1 
ATOM   9813  C  CD2 . PHE C  1 329 ? 25.12700  -17.93000 -43.93700 1.000 73.48000  ? 360 PHE C CD2 1 
ATOM   9814  C  CE1 . PHE C  1 329 ? 27.81900  -17.71600 -44.51100 1.000 78.56000  ? 360 PHE C CE1 1 
ATOM   9815  C  CE2 . PHE C  1 329 ? 25.74800  -18.89700 -44.68500 1.000 78.14000  ? 360 PHE C CE2 1 
ATOM   9816  C  CZ  . PHE C  1 329 ? 27.09800  -18.79100 -44.97400 1.000 78.79000  ? 360 PHE C CZ  1 
ATOM   9817  N  N   . PRO C  1 330 ? 22.64100  -13.79700 -42.34400 1.000 57.38000  ? 361 PRO C N   1 
ATOM   9818  C  CA  . PRO C  1 330 ? 21.90800  -12.86400 -41.48300 1.000 60.73000  ? 361 PRO C CA  1 
ATOM   9819  C  C   . PRO C  1 330 ? 22.40200  -12.94800 -40.04800 1.000 67.41000  ? 361 PRO C C   1 
ATOM   9820  O  O   . PRO C  1 330 ? 22.49400  -14.03500 -39.47200 1.000 70.71000  ? 361 PRO C O   1 
ATOM   9821  C  CB  . PRO C  1 330 ? 20.45900  -13.34400 -41.59300 1.000 56.92000  ? 361 PRO C CB  1 
ATOM   9822  C  CG  . PRO C  1 330 ? 20.40500  -14.10700 -42.87900 1.000 62.97000  ? 361 PRO C CG  1 
ATOM   9823  C  CD  . PRO C  1 330 ? 21.74600  -14.74400 -43.02900 1.000 62.52000  ? 361 PRO C CD  1 
ATOM   9824  N  N   . VAL C  1 331 ? 22.69200  -11.78300 -39.46600 1.000 64.06000  ? 362 VAL C N   1 
ATOM   9825  C  CA  . VAL C  1 331 ? 23.06400  -11.65100 -38.06300 1.000 58.34000  ? 362 VAL C CA  1 
ATOM   9826  C  C   . VAL C  1 331 ? 22.16100  -10.59800 -37.42400 1.000 64.63000  ? 362 VAL C C   1 
ATOM   9827  O  O   . VAL C  1 331 ? 21.45900  -9.84800  -38.10800 1.000 66.73000  ? 362 VAL C O   1 
ATOM   9828  C  CB  . VAL C  1 331 ? 24.54800  -11.28900 -37.88500 1.000 62.93000  ? 362 VAL C CB  1 
ATOM   9829  C  CG1 . VAL C  1 331 ? 25.42900  -12.39200 -38.44100 1.000 63.71000  ? 362 VAL C CG1 1 
ATOM   9830  C  CG2 . VAL C  1 331 ? 24.85200  -9.99000  -38.59700 1.000 60.34000  ? 362 VAL C CG2 1 
ATOM   9831  N  N   . SER C  1 332 ? 22.17800  -10.55700 -36.09300 1.000 57.23000  ? 363 SER C N   1 
ATOM   9832  C  CA  . SER C  1 332 ? 21.32600  -9.66500  -35.31700 1.000 56.72000  ? 363 SER C CA  1 
ATOM   9833  C  C   . SER C  1 332 ? 22.13200  -8.82800  -34.32700 1.000 59.45000  ? 363 SER C C   1 
ATOM   9834  O  O   . SER C  1 332 ? 23.18800  -9.24600  -33.84300 1.000 53.89000  ? 363 SER C O   1 
ATOM   9835  C  CB  . SER C  1 332 ? 20.26600  -10.44000 -34.55200 1.000 56.02000  ? 363 SER C CB  1 
ATOM   9836  O  OG  . SER C  1 332 ? 19.60200  -9.58200  -33.63800 1.000 59.75000  ? 363 SER C OG  1 
ATOM   9837  N  N   . SER C  1 333 ? 21.61900  -7.63700  -34.01500 1.000 59.20000  ? 364 SER C N   1 
ATOM   9838  C  CA  . SER C  1 333 ? 22.24800  -6.86000  -32.94800 1.000 62.27000  ? 364 SER C CA  1 
ATOM   9839  C  C   . SER C  1 333 ? 22.18200  -7.58300  -31.60200 1.000 58.17000  ? 364 SER C C   1 
ATOM   9840  O  O   . SER C  1 333 ? 23.03400  -7.34600  -30.73800 1.000 60.53000  ? 364 SER C O   1 
ATOM   9841  C  CB  . SER C  1 333 ? 21.59000  -5.48400  -32.83800 1.000 52.58000  ? 364 SER C CB  1 
ATOM   9842  O  OG  . SER C  1 333 ? 20.19800  -5.63100  -32.62400 1.000 55.92000  ? 364 SER C OG  1 
ATOM   9843  N  N   . LEU C  1 334 ? 21.22400  -8.49700  -31.43000 1.000 54.50000  ? 365 LEU C N   1 
ATOM   9844  C  CA  . LEU C  1 334 ? 21.16300  -9.32800  -30.23800 1.000 57.67000  ? 365 LEU C CA  1 
ATOM   9845  C  C   . LEU C  1 334 ? 22.39000  -10.20800 -30.06100 1.000 62.36000  ? 365 LEU C C   1 
ATOM   9846  O  O   . LEU C  1 334 ? 22.60900  -10.73900 -28.96700 1.000 61.43000  ? 365 LEU C O   1 
ATOM   9847  C  CB  . LEU C  1 334 ? 19.93700  -10.21400 -30.30800 1.000 59.93000  ? 365 LEU C CB  1 
ATOM   9848  C  CG  . LEU C  1 334 ? 18.64200  -9.43900  -30.35400 1.000 59.41000  ? 365 LEU C CG  1 
ATOM   9849  C  CD1 . LEU C  1 334 ? 17.56700  -10.30700 -30.98300 1.000 54.73000  ? 365 LEU C CD1 1 
ATOM   9850  C  CD2 . LEU C  1 334 ? 18.29100  -9.02300  -28.93000 1.000 57.64000  ? 365 LEU C CD2 1 
ATOM   9851  N  N   . ASP C  1 335 ? 23.18100  -10.39100 -31.11300 1.000 63.29000  ? 366 ASP C N   1 
ATOM   9852  C  CA  . ASP C  1 335 ? 24.34000  -11.25900 -31.03500 1.000 61.56000  ? 366 ASP C CA  1 
ATOM   9853  C  C   . ASP C  1 335 ? 25.51400  -10.60900 -30.32300 1.000 63.71000  ? 366 ASP C C   1 
ATOM   9854  O  O   . ASP C  1 335 ? 26.43100  -11.32100 -29.89500 1.000 61.12000  ? 366 ASP C O   1 
ATOM   9855  C  CB  . ASP C  1 335 ? 24.73900  -11.68800 -32.44600 1.000 59.85000  ? 366 ASP C CB  1 
ATOM   9856  C  CG  . ASP C  1 335 ? 23.63200  -12.45900 -33.15000 1.000 66.30000  ? 366 ASP C CG  1 
ATOM   9857  O  OD1 . ASP C  1 335 ? 22.84400  -13.15000 -32.46200 1.000 67.72000  ? 366 ASP C OD1 1 
ATOM   9858  O  OD2 . ASP C  1 335 ? 23.51000  -12.32900 -34.38800 1.000 65.69000  ? 366 ASP C OD2 1 
ATOM   9859  N  N   . LEU C  1 336 ? 25.50900  -9.28200  -30.18800 1.000 64.95000  ? 367 LEU C N   1 
ATOM   9860  C  CA  . LEU C  1 336 ? 26.65400  -8.60700  -29.58700 1.000 57.84000  ? 367 LEU C CA  1 
ATOM   9861  C  C   . LEU C  1 336 ? 26.78600  -8.94800  -28.10800 1.000 61.28000  ? 367 LEU C C   1 
ATOM   9862  O  O   . LEU C  1 336 ? 27.90300  -9.15800  -27.61500 1.000 66.43000  ? 367 LEU C O   1 
ATOM   9863  C  CB  . LEU C  1 336 ? 26.52800  -7.10300  -29.78100 1.000 56.99000  ? 367 LEU C CB  1 
ATOM   9864  C  CG  . LEU C  1 336 ? 26.44800  -6.64800  -31.23300 1.000 57.85000  ? 367 LEU C CG  1 
ATOM   9865  C  CD1 . LEU C  1 336 ? 26.14900  -5.16100  -31.27600 1.000 55.51000  ? 367 LEU C CD1 1 
ATOM   9866  C  CD2 . LEU C  1 336 ? 27.75100  -6.97000  -31.97300 1.000 53.39000  ? 367 LEU C CD2 1 
ATOM   9867  N  N   . TYR C  1 337 ? 25.65700  -9.03600  -27.39200 1.000 61.49000  ? 368 TYR C N   1 
ATOM   9868  C  CA  . TYR C  1 337 ? 25.70400  -9.34300  -25.96200 1.000 64.52000  ? 368 TYR C CA  1 
ATOM   9869  C  C   . TYR C  1 337 ? 26.40100  -10.67400 -25.69700 1.000 63.68000  ? 368 TYR C C   1 
ATOM   9870  O  O   . TYR C  1 337 ? 27.45100  -10.67800 -25.02700 1.000 63.13000  ? 368 TYR C O   1 
ATOM   9871  C  CB  . TYR C  1 337 ? 24.27900  -9.27000  -25.39000 1.000 64.37000  ? 368 TYR C CB  1 
ATOM   9872  C  CG  . TYR C  1 337 ? 24.14800  -9.29200  -23.86800 1.000 67.73000  ? 368 TYR C CG  1 
ATOM   9873  C  CD1 . TYR C  1 337 ? 24.85900  -10.20200 -23.08900 1.000 65.55000  ? 368 TYR C CD1 1 
ATOM   9874  C  CD2 . TYR C  1 337 ? 23.28400  -8.41800  -23.21800 1.000 66.76000  ? 368 TYR C CD2 1 
ATOM   9875  C  CE1 . TYR C  1 337 ? 24.72500  -10.22900 -21.71000 1.000 69.33000  ? 368 TYR C CE1 1 
ATOM   9876  C  CE2 . TYR C  1 337 ? 23.14400  -8.44000  -21.84100 1.000 67.21000  ? 368 TYR C CE2 1 
ATOM   9877  C  CZ  . TYR C  1 337 ? 23.86900  -9.34300  -21.09300 1.000 69.94000  ? 368 TYR C CZ  1 
ATOM   9878  O  OH  . TYR C  1 337 ? 23.74000  -9.36400  -19.72300 1.000 71.79000  ? 368 TYR C OH  1 
ATOM   9879  N  N   . PRO C  1 338 ? 25.92600  -11.81600 -26.20900 1.000 61.65000  ? 369 PRO C N   1 
ATOM   9880  C  CA  . PRO C  1 338 ? 26.65900  -13.06800 -25.94600 1.000 62.64000  ? 369 PRO C CA  1 
ATOM   9881  C  C   . PRO C  1 338 ? 28.02300  -13.11400 -26.60500 1.000 62.68000  ? 369 PRO C C   1 
ATOM   9882  O  O   . PRO C  1 338 ? 28.92000  -13.78700 -26.08400 1.000 68.59000  ? 369 PRO C O   1 
ATOM   9883  C  CB  . PRO C  1 338 ? 25.72700  -14.14800 -26.50600 1.000 66.89000  ? 369 PRO C CB  1 
ATOM   9884  C  CG  . PRO C  1 338 ? 24.93800  -13.43000 -27.57200 1.000 64.50000  ? 369 PRO C CG  1 
ATOM   9885  C  CD  . PRO C  1 338 ? 24.71500  -12.05800 -27.01900 1.000 64.38000  ? 369 PRO C CD  1 
ATOM   9886  N  N   . THR C  1 339 ? 28.22100  -12.40800 -27.72200 1.000 63.26000  ? 370 THR C N   1 
ATOM   9887  C  CA  . THR C  1 339 ? 29.54600  -12.37100 -28.33600 1.000 63.37000  ? 370 THR C CA  1 
ATOM   9888  C  C   . THR C  1 339 ? 30.54900  -11.62300 -27.47000 1.000 65.01000  ? 370 THR C C   1 
ATOM   9889  O  O   . THR C  1 339 ? 31.71400  -12.02900 -27.36600 1.000 67.17000  ? 370 THR C O   1 
ATOM   9890  C  CB  . THR C  1 339 ? 29.48700  -11.72700 -29.71800 1.000 63.72000  ? 370 THR C CB  1 
ATOM   9891  O  OG1 . THR C  1 339 ? 28.57400  -12.45400 -30.54600 1.000 59.61000  ? 370 THR C OG1 1 
ATOM   9892  C  CG2 . THR C  1 339 ? 30.87100  -11.74000 -30.35700 1.000 63.72000  ? 370 THR C CG2 1 
ATOM   9893  N  N   . PHE C  1 340 ? 30.13900  -10.50800 -26.86200 1.000 65.98000  ? 371 PHE C N   1 
ATOM   9894  C  CA  . PHE C  1 340 ? 31.10500  -9.72800  -26.09700 1.000 65.31000  ? 371 PHE C CA  1 
ATOM   9895  C  C   . PHE C  1 340 ? 31.51400  -10.45900 -24.82700 1.000 69.84000  ? 371 PHE C C   1 
ATOM   9896  O  O   . PHE C  1 340 ? 32.71000  -10.63200 -24.55400 1.000 66.24000  ? 371 PHE C O   1 
ATOM   9897  C  CB  . PHE C  1 340 ? 30.53900  -8.34100  -25.78900 1.000 62.29000  ? 371 PHE C CB  1 
ATOM   9898  C  CG  . PHE C  1 340 ? 30.41400  -7.45800  -27.00800 1.000 67.95000  ? 371 PHE C CG  1 
ATOM   9899  C  CD1 . PHE C  1 340 ? 31.08100  -7.78300  -28.18700 1.000 67.06000  ? 371 PHE C CD1 1 
ATOM   9900  C  CD2 . PHE C  1 340 ? 29.64300  -6.30900  -26.98200 1.000 66.86000  ? 371 PHE C CD2 1 
ATOM   9901  C  CE1 . PHE C  1 340 ? 30.97600  -6.98200  -29.30700 1.000 64.21000  ? 371 PHE C CE1 1 
ATOM   9902  C  CE2 . PHE C  1 340 ? 29.53400  -5.50300  -28.10500 1.000 64.64000  ? 371 PHE C CE2 1 
ATOM   9903  C  CZ  . PHE C  1 340 ? 30.19500  -5.84000  -29.26600 1.000 61.28000  ? 371 PHE C CZ  1 
ATOM   9904  N  N   . THR C  1 341 ? 30.53100  -10.96000 -24.07700 1.000 70.03000  ? 372 THR C N   1 
ATOM   9905  C  CA  . THR C  1 341 ? 30.83500  -11.67700 -22.84600 1.000 71.03000  ? 372 THR C CA  1 
ATOM   9906  C  C   . THR C  1 341 ? 31.66100  -12.92700 -23.13200 1.000 74.18000  ? 372 THR C C   1 
ATOM   9907  O  O   . THR C  1 341 ? 32.57000  -13.26800 -22.36300 1.000 75.35000  ? 372 THR C O   1 
ATOM   9908  C  CB  . THR C  1 341 ? 29.53400  -12.02800 -22.12700 1.000 71.35000  ? 372 THR C CB  1 
ATOM   9909  O  OG1 . THR C  1 341 ? 28.70100  -12.80300 -23.00100 1.000 69.99000  ? 372 THR C OG1 1 
ATOM   9910  C  CG2 . THR C  1 341 ? 28.79700  -10.75600 -21.74800 1.000 63.42000  ? 372 THR C CG2 1 
ATOM   9911  N  N   . GLY C  1 342 ? 31.37700  -13.60700 -24.24800 1.000 70.19000  ? 373 GLY C N   1 
ATOM   9912  C  CA  . GLY C  1 342 ? 32.23600  -14.70000 -24.67700 1.000 63.44000  ? 373 GLY C CA  1 
ATOM   9913  C  C   . GLY C  1 342 ? 33.67300  -14.25800 -24.87100 1.000 68.40000  ? 373 GLY C C   1 
ATOM   9914  O  O   . GLY C  1 342 ? 34.60500  -14.89100 -24.37200 1.000 67.15000  ? 373 GLY C O   1 
ATOM   9915  N  N   . LEU C  1 343 ? 33.87500  -13.16900 -25.61300 1.000 68.56000  ? 374 LEU C N   1 
ATOM   9916  C  CA  . LEU C  1 343 ? 35.22800  -12.64900 -25.78000 1.000 67.29000  ? 374 LEU C CA  1 
ATOM   9917  C  C   . LEU C  1 343 ? 35.82200  -12.24400 -24.44200 1.000 70.60000  ? 374 LEU C C   1 
ATOM   9918  O  O   . LEU C  1 343 ? 37.03800  -12.33000 -24.24500 1.000 68.48000  ? 374 LEU C O   1 
ATOM   9919  C  CB  . LEU C  1 343 ? 35.22500  -11.45100 -26.72800 1.000 70.46000  ? 374 LEU C CB  1 
ATOM   9920  C  CG  . LEU C  1 343 ? 34.88400  -11.72100 -28.19200 1.000 69.33000  ? 374 LEU C CG  1 
ATOM   9921  C  CD1 . LEU C  1 343 ? 34.73900  -10.40800 -28.93800 1.000 66.92000  ? 374 LEU C CD1 1 
ATOM   9922  C  CD2 . LEU C  1 343 ? 35.94100  -12.59300 -28.84100 1.000 70.92000  ? 374 LEU C CD2 1 
ATOM   9923  N  N   . ALA C  1 344 ? 34.97800  -11.80700 -23.51500 1.000 72.71000  ? 375 ALA C N   1 
ATOM   9924  C  CA  . ALA C  1 344 ? 35.41600  -11.37800 -22.19900 1.000 72.92000  ? 375 ALA C CA  1 
ATOM   9925  C  C   . ALA C  1 344 ? 35.68300  -12.54000 -21.27000 1.000 76.66000  ? 375 ALA C C   1 
ATOM   9926  O  O   . ALA C  1 344 ? 36.09100  -12.30500 -20.12500 1.000 76.15000  ? 375 ALA C O   1 
ATOM   9927  C  CB  . ALA C  1 344 ? 34.35600  -10.48700 -21.55400 1.000 71.07000  ? 375 ALA C CB  1 
ATOM   9928  N  N   . GLU C  1 345 ? 35.42300  -13.77300 -21.72300 1.000 72.29000  ? 376 GLU C N   1 
ATOM   9929  C  CA  . GLU C  1 345 ? 35.52800  -14.95600 -20.87600 1.000 71.87000  ? 376 GLU C CA  1 
ATOM   9930  C  C   . GLU C  1 345 ? 34.72000  -14.74400 -19.60400 1.000 71.70000  ? 376 GLU C C   1 
ATOM   9931  O  O   . GLU C  1 345 ? 35.04800  -15.27000 -18.54000 1.000 75.90000  ? 376 GLU C O   1 
ATOM   9932  C  CB  . GLU C  1 345 ? 36.99200  -15.29000 -20.55500 1.000 68.60000  ? 376 GLU C CB  1 
ATOM   9933  C  CG  . GLU C  1 345 ? 37.86500  -15.55800 -21.77500 1.000 70.72000  ? 376 GLU C CG  1 
ATOM   9934  C  CD  . GLU C  1 345 ? 39.36000  -15.59800 -21.44600 1.000 78.82000  ? 376 GLU C CD  1 
ATOM   9935  O  OE1 . GLU C  1 345 ? 39.72300  -15.75700 -20.25600 1.000 71.86000  ? 376 GLU C OE1 1 
ATOM   9936  O  OE2 . GLU C  1 345 ? 40.17600  -15.47400 -22.38600 1.000 76.19000  ? 376 GLU C OE2 1 
ATOM   9937  N  N   . ALA C  1 346 ? 33.66900  -13.94200 -19.71100 1.000 70.96000  ? 377 ALA C N   1 
ATOM   9938  C  CA  . ALA C  1 346 ? 32.85000  -13.57300 -18.56900 1.000 79.17000  ? 377 ALA C CA  1 
ATOM   9939  C  C   . ALA C  1 346 ? 31.71700  -14.56600 -18.38100 1.000 83.59000  ? 377 ALA C C   1 
ATOM   9940  O  O   . ALA C  1 346 ? 31.28500  -15.23700 -19.32300 1.000 78.98000  ? 377 ALA C O   1 
ATOM   9941  C  CB  . ALA C  1 346 ? 32.27900  -12.16600 -18.73500 1.000 76.82000  ? 377 ALA C CB  1 
ATOM   9942  N  N   . LYS C  1 347 ? 31.24600  -14.66000 -17.14400 1.000 84.48000  ? 378 LYS C N   1 
ATOM   9943  C  CA  . LYS C  1 347 ? 30.12600  -15.52400 -16.80400 1.000 85.19000  ? 378 LYS C CA  1 
ATOM   9944  C  C   . LYS C  1 347 ? 28.82000  -14.74800 -16.87600 1.000 82.60000  ? 378 LYS C C   1 
ATOM   9945  O  O   . LYS C  1 347 ? 28.75100  -13.58600 -16.46500 1.000 83.80000  ? 378 LYS C O   1 
ATOM   9946  C  CB  . LYS C  1 347 ? 30.30800  -16.11200 -15.40000 1.000 89.26000  ? 378 LYS C CB  1 
ATOM   9947  N  N   . LEU C  1 348 ? 27.78600  -15.39100 -17.41800 1.000 81.01000  ? 379 LEU C N   1 
ATOM   9948  C  CA  . LEU C  1 348 ? 26.48900  -14.74000 -17.48000 1.000 79.69000  ? 379 LEU C CA  1 
ATOM   9949  C  C   . LEU C  1 348 ? 25.80100  -14.78600 -16.11700 1.000 83.25000  ? 379 LEU C C   1 
ATOM   9950  O  O   . LEU C  1 348 ? 26.04400  -15.69900 -15.32300 1.000 85.82000  ? 379 LEU C O   1 
ATOM   9951  C  CB  . LEU C  1 348 ? 25.59500  -15.39500 -18.52400 1.000 81.11000  ? 379 LEU C CB  1 
ATOM   9952  C  CG  . LEU C  1 348 ? 25.82800  -15.04700 -19.99400 1.000 77.47000  ? 379 LEU C CG  1 
ATOM   9953  C  CD1 . LEU C  1 348 ? 27.20500  -15.46800 -20.51600 1.000 76.79000  ? 379 LEU C CD1 1 
ATOM   9954  C  CD2 . LEU C  1 348 ? 24.70100  -15.65300 -20.82000 1.000 72.54000  ? 379 LEU C CD2 1 
ATOM   9955  N  N   . PRO C  1 349 ? 24.95400  -13.79900 -15.81900 1.000 86.64000  ? 380 PRO C N   1 
ATOM   9956  C  CA  . PRO C  1 349 ? 24.21600  -13.82100 -14.55000 1.000 89.17000  ? 380 PRO C CA  1 
ATOM   9957  C  C   . PRO C  1 349 ? 23.32000  -15.04500 -14.43800 1.000 89.01000  ? 380 PRO C C   1 
ATOM   9958  O  O   . PRO C  1 349 ? 22.78500  -15.54500 -15.43000 1.000 92.32000  ? 380 PRO C O   1 
ATOM   9959  C  CB  . PRO C  1 349 ? 23.37700  -12.53500 -14.61000 1.000 88.83000  ? 380 PRO C CB  1 
ATOM   9960  C  CG  . PRO C  1 349 ? 24.09200  -11.65100 -15.58900 1.000 81.92000  ? 380 PRO C CG  1 
ATOM   9961  C  CD  . PRO C  1 349 ? 24.65500  -12.59200 -16.61200 1.000 82.47000  ? 380 PRO C CD  1 
ATOM   9962  N  N   . LYS C  1 350 ? 23.12800  -15.50600 -13.20400 1.000 90.72000  ? 381 LYS C N   1 
ATOM   9963  C  CA  . LYS C  1 350 ? 22.22600  -16.62200 -12.96100 1.000 88.28000  ? 381 LYS C CA  1 
ATOM   9964  C  C   . LYS C  1 350 ? 20.80900  -16.18300 -13.30800 1.000 88.77000  ? 381 LYS C C   1 
ATOM   9965  O  O   . LYS C  1 350 ? 20.28200  -15.23500 -12.71600 1.000 90.96000  ? 381 LYS C O   1 
ATOM   9966  C  CB  . LYS C  1 350 ? 22.31900  -17.07800 -11.50900 1.000 89.05000  ? 381 LYS C CB  1 
ATOM   9967  N  N   . GLY C  1 351 ? 20.19700  -16.86800 -14.26900 1.000 92.23000  ? 382 GLY C N   1 
ATOM   9968  C  CA  . GLY C  1 351 ? 18.86100  -16.54800 -14.72900 1.000 91.80000  ? 382 GLY C CA  1 
ATOM   9969  C  C   . GLY C  1 351 ? 18.79400  -15.58000 -15.89000 1.000 86.92000  ? 382 GLY C C   1 
ATOM   9970  O  O   . GLY C  1 351 ? 17.70000  -15.09500 -16.21000 1.000 86.87000  ? 382 GLY C O   1 
ATOM   9971  N  N   . LYS C  1 352 ? 19.92800  -15.26000 -16.51200 1.000 85.85000  ? 383 LYS C N   1 
ATOM   9972  C  CA  . LYS C  1 352 ? 19.95200  -14.35200 -17.65400 1.000 84.23000  ? 383 LYS C CA  1 
ATOM   9973  C  C   . LYS C  1 352 ? 19.53900  -15.09400 -18.92600 1.000 79.55000  ? 383 LYS C C   1 
ATOM   9974  O  O   . LYS C  1 352 ? 20.18000  -16.08100 -19.31200 1.000 77.10000  ? 383 LYS C O   1 
ATOM   9975  C  CB  . LYS C  1 352 ? 21.34300  -13.74000 -17.81300 1.000 80.26000  ? 383 LYS C CB  1 
ATOM   9976  C  CG  . LYS C  1 352 ? 21.45900  -12.74800 -18.95400 1.000 73.35000  ? 383 LYS C CG  1 
ATOM   9977  C  CD  . LYS C  1 352 ? 20.47000  -11.62100 -18.78500 1.000 74.31000  ? 383 LYS C CD  1 
ATOM   9978  C  CE  . LYS C  1 352 ? 20.42600  -10.73800 -20.01600 1.000 73.63000  ? 383 LYS C CE  1 
ATOM   9979  N  NZ  . LYS C  1 352 ? 19.50600  -9.57100  -19.82100 1.000 69.21000  ? 383 LYS C NZ  1 
ATOM   9980  N  N   . GLN C  1 353 ? 18.47100  -14.63100 -19.57300 1.000 82.77000  ? 384 GLN C N   1 
ATOM   9981  C  CA  . GLN C  1 353 ? 18.03200  -15.17500 -20.85400 1.000 82.07000  ? 384 GLN C CA  1 
ATOM   9982  C  C   . GLN C  1 353 ? 18.52500  -14.28500 -21.99300 1.000 80.96000  ? 384 GLN C C   1 
ATOM   9983  O  O   . GLN C  1 353 ? 18.52600  -13.05400 -21.87500 1.000 77.64000  ? 384 GLN C O   1 
ATOM   9984  C  CB  . GLN C  1 353 ? 16.51100  -15.30900 -20.90700 1.000 78.34000  ? 384 GLN C CB  1 
ATOM   9985  C  CG  . GLN C  1 353 ? 15.97400  -16.50200 -20.12400 1.000 89.73000  ? 384 GLN C CG  1 
ATOM   9986  C  CD  . GLN C  1 353 ? 16.35500  -17.83500 -20.76000 1.000 97.32000  ? 384 GLN C CD  1 
ATOM   9987  O  OE1 . GLN C  1 353 ? 17.33700  -18.47000 -20.36000 1.000 99.42000  ? 384 GLN C OE1 1 
ATOM   9988  N  NE2 . GLN C  1 353 ? 15.58100  -18.26000 -21.76300 1.000 97.55000  ? 384 GLN C NE2 1 
ATOM   9989  N  N   . LEU C  1 354 ? 18.95800  -14.91200 -23.09400 1.000 80.35000  ? 385 LEU C N   1 
ATOM   9990  C  CA  . LEU C  1 354 ? 19.51200  -14.20700 -24.24900 1.000 73.78000  ? 385 LEU C CA  1 
ATOM   9991  C  C   . LEU C  1 354 ? 18.86800  -14.69800 -25.54100 1.000 75.24000  ? 385 LEU C C   1 
ATOM   9992  O  O   . LEU C  1 354 ? 18.60000  -15.89300 -25.70200 1.000 80.19000  ? 385 LEU C O   1 
ATOM   9993  C  CB  . LEU C  1 354 ? 21.03300  -14.39100 -24.35700 1.000 67.64000  ? 385 LEU C CB  1 
ATOM   9994  C  CG  . LEU C  1 354 ? 21.88600  -13.64400 -23.34200 1.000 67.28000  ? 385 LEU C CG  1 
ATOM   9995  C  CD1 . LEU C  1 354 ? 23.35700  -13.77200 -23.71300 1.000 69.48000  ? 385 LEU C CD1 1 
ATOM   9996  C  CD2 . LEU C  1 354 ? 21.46000  -12.18600 -23.28700 1.000 70.77000  ? 385 LEU C CD2 1 
ATOM   9997  N  N   . ASP C  1 355 ? 18.63300  -13.77100 -26.46800 1.000 72.22000  ? 386 ASP C N   1 
ATOM   9998  C  CA  . ASP C  1 355 ? 17.98600  -14.09400 -27.73300 1.000 74.01000  ? 386 ASP C CA  1 
ATOM   9999  C  C   . ASP C  1 355 ? 18.94300  -14.16400 -28.91300 1.000 71.97000  ? 386 ASP C C   1 
ATOM   10000 O  O   . ASP C  1 355 ? 18.52500  -14.56100 -30.00400 1.000 70.76000  ? 386 ASP C O   1 
ATOM   10001 C  CB  . ASP C  1 355 ? 16.88500  -13.08300 -28.01800 1.000 67.32000  ? 386 ASP C CB  1 
ATOM   10002 C  CG  . ASP C  1 355 ? 15.77800  -13.17800 -27.01300 1.000 74.61000  ? 386 ASP C CG  1 
ATOM   10003 O  OD1 . ASP C  1 355 ? 15.51300  -14.30200 -26.54000 1.000 75.40000  ? 386 ASP C OD1 1 
ATOM   10004 O  OD2 . ASP C  1 355 ? 15.18900  -12.13400 -26.68200 1.000 78.48000  ? 386 ASP C OD2 1 
ATOM   10005 N  N   . GLY C  1 356 ? 20.19400  -13.75100 -28.74000 1.000 70.56000  ? 387 GLY C N   1 
ATOM   10006 C  CA  . GLY C  1 356 ? 21.19300  -13.86800 -29.77000 1.000 62.39000  ? 387 GLY C CA  1 
ATOM   10007 C  C   . GLY C  1 356 ? 22.15400  -15.00500 -29.48500 1.000 68.35000  ? 387 GLY C C   1 
ATOM   10008 O  O   . GLY C  1 356 ? 21.95400  -15.82600 -28.58700 1.000 66.07000  ? 387 GLY C O   1 
ATOM   10009 N  N   . LYS C  1 357 ? 23.24700  -15.00700 -30.23700 1.000 63.10000  ? 388 LYS C N   1 
ATOM   10010 C  CA  . LYS C  1 357 ? 24.20300  -16.09400 -30.17900 1.000 64.97000  ? 388 LYS C CA  1 
ATOM   10011 C  C   . LYS C  1 357 ? 25.60700  -15.52800 -30.31300 1.000 69.80000  ? 388 LYS C C   1 
ATOM   10012 O  O   . LYS C  1 357 ? 25.82000  -14.50000 -30.96300 1.000 70.13000  ? 388 LYS C O   1 
ATOM   10013 C  CB  . LYS C  1 357 ? 23.94400  -17.10500 -31.30800 1.000 57.12000  ? 388 LYS C CB  1 
ATOM   10014 N  N   . ASN C  1 358 ? 26.56500  -16.20900 -29.69900 1.000 62.87000  ? 389 ASN C N   1 
ATOM   10015 C  CA  . ASN C  1 358 ? 27.95700  -15.86900 -29.92900 1.000 63.94000  ? 389 ASN C CA  1 
ATOM   10016 C  C   . ASN C  1 358 ? 28.28600  -16.28400 -31.35500 1.000 67.05000  ? 389 ASN C C   1 
ATOM   10017 O  O   . ASN C  1 358 ? 28.21100  -17.46900 -31.69300 1.000 67.88000  ? 389 ASN C O   1 
ATOM   10018 C  CB  . ASN C  1 358 ? 28.85600  -16.57500 -28.91600 1.000 60.54000  ? 389 ASN C CB  1 
ATOM   10019 C  CG  . ASN C  1 358 ? 30.33200  -16.28100 -29.12700 1.000 68.57000  ? 389 ASN C CG  1 
ATOM   10020 O  OD1 . ASN C  1 358 ? 30.71900  -15.52500 -30.01800 1.000 69.68000  ? 389 ASN C OD1 1 
ATOM   10021 N  ND2 . ASN C  1 358 ? 31.17000  -16.89800 -28.30600 1.000 77.25000  ? 389 ASN C ND2 1 
ATOM   10022 N  N   . ILE C  1 359 ? 28.60900  -15.30700 -32.20000 1.000 64.61000  ? 390 ILE C N   1 
ATOM   10023 C  CA  . ILE C  1 359 ? 28.82500  -15.53700 -33.62000 1.000 61.31000  ? 390 ILE C CA  1 
ATOM   10024 C  C   . ILE C  1 359 ? 30.28500  -15.34300 -34.00100 1.000 65.15000  ? 390 ILE C C   1 
ATOM   10025 O  O   . ILE C  1 359 ? 30.61600  -15.33700 -35.19400 1.000 61.31000  ? 390 ILE C O   1 
ATOM   10026 C  CB  . ILE C  1 359 ? 27.90900  -14.64800 -34.48300 1.000 65.51000  ? 390 ILE C CB  1 
ATOM   10027 C  CG1 . ILE C  1 359 ? 28.32600  -13.17700 -34.37500 1.000 58.84000  ? 390 ILE C CG1 1 
ATOM   10028 C  CG2 . ILE C  1 359 ? 26.46200  -14.80200 -34.05600 1.000 61.27000  ? 390 ILE C CG2 1 
ATOM   10029 C  CD1 . ILE C  1 359 ? 27.67100  -12.28300 -35.34200 1.000 58.69000  ? 390 ILE C CD1 1 
ATOM   10030 N  N   . MET C  1 360 ? 31.18000  -15.19400 -33.01700 1.000 67.66000  ? 391 MET C N   1 
ATOM   10031 C  CA  . MET C  1 360 ? 32.56400  -14.85700 -33.34400 1.000 67.70000  ? 391 MET C CA  1 
ATOM   10032 C  C   . MET C  1 360 ? 33.24000  -15.95300 -34.16400 1.000 74.71000  ? 391 MET C C   1 
ATOM   10033 O  O   . MET C  1 360 ? 33.96900  -15.66000 -35.12300 1.000 70.94000  ? 391 MET C O   1 
ATOM   10034 C  CB  . MET C  1 360 ? 33.35000  -14.57900 -32.07300 1.000 65.32000  ? 391 MET C CB  1 
ATOM   10035 C  CG  . MET C  1 360 ? 34.72000  -13.97400 -32.35000 1.000 69.74000  ? 391 MET C CG  1 
ATOM   10036 S  SD  . MET C  1 360 ? 34.60900  -12.69600 -33.62200 1.000 74.74000  ? 391 MET C SD  1 
ATOM   10037 C  CE  . MET C  1 360 ? 34.98800  -11.22900 -32.67000 1.000 64.24000  ? 391 MET C CE  1 
ATOM   10038 N  N   . ASP C  1 361 ? 33.03200  -17.22000 -33.79700 1.000 75.77000  ? 392 ASP C N   1 
ATOM   10039 C  CA  . ASP C  1 361 ? 33.60100  -18.30000 -34.59900 1.000 80.08000  ? 392 ASP C CA  1 
ATOM   10040 C  C   . ASP C  1 361 ? 32.98200  -18.33500 -35.99000 1.000 78.35000  ? 392 ASP C C   1 
ATOM   10041 O  O   . ASP C  1 361 ? 33.69600  -18.50500 -36.98900 1.000 73.90000  ? 392 ASP C O   1 
ATOM   10042 C  CB  . ASP C  1 361 ? 33.44100  -19.64300 -33.88700 1.000 85.04000  ? 392 ASP C CB  1 
ATOM   10043 C  CG  . ASP C  1 361 ? 34.74100  -20.11700 -33.25600 1.000 85.17000  ? 392 ASP C CG  1 
ATOM   10044 O  OD1 . ASP C  1 361 ? 35.77900  -19.46600 -33.49300 1.000 81.93000  ? 392 ASP C OD1 1 
ATOM   10045 O  OD2 . ASP C  1 361 ? 34.72300  -21.12800 -32.52100 1.000 96.79000  ? 392 ASP C OD2 1 
ATOM   10046 N  N   . ASP C  1 362 ? 31.65600  -18.18700 -36.06900 1.000 75.00000  ? 393 ASP C N   1 
ATOM   10047 C  CA  . ASP C  1 362 ? 30.99800  -18.11800 -37.36700 1.000 71.79000  ? 393 ASP C CA  1 
ATOM   10048 C  C   . ASP C  1 362 ? 31.62500  -17.04200 -38.23300 1.000 73.24000  ? 393 ASP C C   1 
ATOM   10049 O  O   . ASP C  1 362 ? 31.87200  -17.25800 -39.42300 1.000 79.66000  ? 393 ASP C O   1 
ATOM   10050 C  CB  . ASP C  1 362 ? 29.50900  -17.83800 -37.17600 1.000 68.04000  ? 393 ASP C CB  1 
ATOM   10051 C  CG  . ASP C  1 362 ? 28.82700  -18.91900 -36.38600 1.000 77.96000  ? 393 ASP C CG  1 
ATOM   10052 O  OD1 . ASP C  1 362 ? 29.51900  -19.89400 -36.04100 1.000 85.02000  ? 393 ASP C OD1 1 
ATOM   10053 O  OD2 . ASP C  1 362 ? 27.62000  -18.79400 -36.08100 1.000 75.44000  ? 393 ASP C OD2 1 
ATOM   10054 N  N   . VAL C  1 363 ? 31.94000  -15.89000 -37.64500 1.000 69.97000  ? 394 VAL C N   1 
ATOM   10055 C  CA  . VAL C  1 363 ? 32.54400  -14.81700 -38.42800 1.000 73.85000  ? 394 VAL C CA  1 
ATOM   10056 C  C   . VAL C  1 363 ? 33.94100  -15.20700 -38.88800 1.000 75.15000  ? 394 VAL C C   1 
ATOM   10057 O  O   . VAL C  1 363 ? 34.32400  -14.96000 -40.03900 1.000 73.34000  ? 394 VAL C O   1 
ATOM   10058 C  CB  . VAL C  1 363 ? 32.54900  -13.50600 -37.62000 1.000 67.96000  ? 394 VAL C CB  1 
ATOM   10059 C  CG1 . VAL C  1 363 ? 33.46400  -12.47500 -38.27000 1.000 65.59000  ? 394 VAL C CG1 1 
ATOM   10060 C  CG2 . VAL C  1 363 ? 31.12100  -12.96100 -37.50900 1.000 65.37000  ? 394 VAL C CG2 1 
ATOM   10061 N  N   . LEU C  1 364 ? 34.71800  -15.84100 -38.00900 1.000 75.75000  ? 395 LEU C N   1 
ATOM   10062 C  CA  . LEU C  1 364 ? 36.08000  -16.19900 -38.37700 1.000 76.15000  ? 395 LEU C CA  1 
ATOM   10063 C  C   . LEU C  1 364 ? 36.10600  -17.36400 -39.37000 1.000 77.80000  ? 395 LEU C C   1 
ATOM   10064 O  O   . LEU C  1 364 ? 36.98900  -17.41600 -40.23400 1.000 82.20000  ? 395 LEU C O   1 
ATOM   10065 C  CB  . LEU C  1 364 ? 36.88900  -16.50600 -37.10800 1.000 77.12000  ? 395 LEU C CB  1 
ATOM   10066 C  CG  . LEU C  1 364 ? 37.16600  -15.32600 -36.15600 1.000 75.51000  ? 395 LEU C CG  1 
ATOM   10067 C  CD1 . LEU C  1 364 ? 37.68000  -15.78500 -34.80200 1.000 66.59000  ? 395 LEU C CD1 1 
ATOM   10068 C  CD2 . LEU C  1 364 ? 38.15000  -14.32900 -36.75300 1.000 70.84000  ? 395 LEU C CD2 1 
ATOM   10069 N  N   . LYS C  1 365 ? 35.13100  -18.27200 -39.30500 1.000 75.60000  ? 396 LYS C N   1 
ATOM   10070 C  CA  . LYS C  1 365 ? 35.07900  -19.41400 -40.21500 1.000 80.68000  ? 396 LYS C CA  1 
ATOM   10071 C  C   . LYS C  1 365 ? 34.02300  -19.26200 -41.31500 1.000 86.58000  ? 396 LYS C C   1 
ATOM   10072 O  O   . LYS C  1 365 ? 33.83700  -20.18800 -42.11300 1.000 85.98000  ? 396 LYS C O   1 
ATOM   10073 C  CB  . LYS C  1 365 ? 34.82100  -20.70300 -39.42100 1.000 71.96000  ? 396 LYS C CB  1 
ATOM   10074 N  N   . ASN C  1 366 ? 33.34100  -18.11900 -41.37600 1.000 81.85000  ? 397 ASN C N   1 
ATOM   10075 C  CA  . ASN C  1 366 ? 32.32000  -17.80900 -42.38200 1.000 80.70000  ? 397 ASN C CA  1 
ATOM   10076 C  C   . ASN C  1 366 ? 31.26900  -18.92000 -42.50000 1.000 75.43000  ? 397 ASN C C   1 
ATOM   10077 O  O   . ASN C  1 366 ? 31.07800  -19.52300 -43.55200 1.000 77.08000  ? 397 ASN C O   1 
ATOM   10078 C  CB  . ASN C  1 366 ? 32.97800  -17.51700 -43.73200 1.000 81.44000  ? 397 ASN C CB  1 
ATOM   10079 C  CG  . ASN C  1 366 ? 32.12100  -16.63700 -44.60800 1.000 81.78000  ? 397 ASN C CG  1 
ATOM   10080 O  OD1 . ASN C  1 366 ? 31.08000  -17.06600 -45.11300 1.000 81.31000  ? 397 ASN C OD1 1 
ATOM   10081 N  ND2 . ASN C  1 366 ? 32.54100  -15.37700 -44.76900 1.000 72.44000  ? 397 ASN C ND2 1 
ATOM   10082 N  N   . THR C  1 367 ? 30.57500  -19.16800 -41.38900 1.000 79.35000  ? 398 THR C N   1 
ATOM   10083 C  CA  . THR C  1 367 ? 29.52500  -20.17400 -41.26900 1.000 73.95000  ? 398 THR C CA  1 
ATOM   10084 C  C   . THR C  1 367 ? 28.21900  -19.53000 -40.80300 1.000 76.81000  ? 398 THR C C   1 
ATOM   10085 O  O   . THR C  1 367 ? 28.21200  -18.41500 -40.28100 1.000 81.21000  ? 398 THR C O   1 
ATOM   10086 C  CB  . THR C  1 367 ? 29.94300  -21.28700 -40.30100 1.000 84.71000  ? 398 THR C CB  1 
ATOM   10087 O  OG1 . THR C  1 367 ? 29.97900  -20.77300 -38.96100 1.000 82.62000  ? 398 THR C OG1 1 
ATOM   10088 C  CG2 . THR C  1 367 ? 31.33400  -21.81400 -40.67500 1.000 79.73000  ? 398 THR C CG2 1 
ATOM   10089 N  N   . GLU C  1 368 ? 27.10000  -20.23800 -41.01500 1.000 74.55000  ? 399 GLU C N   1 
ATOM   10090 C  CA  . GLU C  1 368 ? 25.74200  -19.72700 -40.79800 1.000 79.97000  ? 399 GLU C CA  1 
ATOM   10091 C  C   . GLU C  1 368 ? 25.26100  -19.79900 -39.34900 1.000 81.87000  ? 399 GLU C C   1 
ATOM   10092 O  O   . GLU C  1 368 ? 25.03000  -20.89700 -38.82600 1.000 84.22000  ? 399 GLU C O   1 
ATOM   10093 C  CB  . GLU C  1 368 ? 24.76900  -20.49900 -41.69600 1.000 82.55000  ? 399 GLU C CB  1 
ATOM   10094 C  CG  . GLU C  1 368 ? 23.33800  -19.97500 -41.73500 1.000 83.93000  ? 399 GLU C CG  1 
ATOM   10095 C  CD  . GLU C  1 368 ? 22.50600  -20.67600 -42.80700 1.000 91.14000  ? 399 GLU C CD  1 
ATOM   10096 O  OE1 . GLU C  1 368 ? 23.02200  -21.63900 -43.41900 1.000 91.43000  ? 399 GLU C OE1 1 
ATOM   10097 O  OE2 . GLU C  1 368 ? 21.34800  -20.26300 -43.04600 1.000 90.22000  ? 399 GLU C OE2 1 
ATOM   10098 N  N   . PRO C  1 369 ? 25.10600  -18.65600 -38.66600 1.000 84.27000  ? 400 PRO C N   1 
ATOM   10099 C  CA  . PRO C  1 369 ? 24.58900  -18.68100 -37.28100 1.000 85.38000  ? 400 PRO C CA  1 
ATOM   10100 C  C   . PRO C  1 369 ? 23.08700  -18.90800 -37.14400 1.000 85.64000  ? 400 PRO C C   1 
ATOM   10101 O  O   . PRO C  1 369 ? 22.64500  -19.30100 -36.05300 1.000 77.36000  ? 400 PRO C O   1 
ATOM   10102 C  CB  . PRO C  1 369 ? 24.97900  -17.29300 -36.73200 1.000 79.43000  ? 400 PRO C CB  1 
ATOM   10103 C  CG  . PRO C  1 369 ? 25.11500  -16.43800 -37.93000 1.000 80.15000  ? 400 PRO C CG  1 
ATOM   10104 C  CD  . PRO C  1 369 ? 25.64900  -17.33300 -39.02200 1.000 83.46000  ? 400 PRO C CD  1 
ATOM   10105 N  N   . TYR C  1 370 ? 22.28300  -18.62900 -38.17600 1.000 86.30000  ? 401 TYR C N   1 
ATOM   10106 C  CA  . TYR C  1 370 ? 20.82700  -18.70700 -38.07300 1.000 85.79000  ? 401 TYR C CA  1 
ATOM   10107 C  C   . TYR C  1 370 ? 20.21400  -19.69900 -39.06100 1.000 87.23000  ? 401 TYR C C   1 
ATOM   10108 O  O   . TYR C  1 370 ? 19.08300  -19.50500 -39.50600 1.000 87.01000  ? 401 TYR C O   1 
ATOM   10109 C  CB  . TYR C  1 370 ? 20.19500  -17.32300 -38.24500 1.000 84.31000  ? 401 TYR C CB  1 
ATOM   10110 C  CG  . TYR C  1 370 ? 20.23800  -16.44900 -37.00100 1.000 83.53000  ? 401 TYR C CG  1 
ATOM   10111 C  CD1 . TYR C  1 370 ? 21.37000  -15.69500 -36.67600 1.000 78.10000  ? 401 TYR C CD1 1 
ATOM   10112 C  CD2 . TYR C  1 370 ? 19.13400  -16.37900 -36.15000 1.000 79.35000  ? 401 TYR C CD2 1 
ATOM   10113 C  CE1 . TYR C  1 370 ? 21.39700  -14.89600 -35.53200 1.000 77.71000  ? 401 TYR C CE1 1 
ATOM   10114 C  CE2 . TYR C  1 370 ? 19.14800  -15.59300 -35.01400 1.000 77.03000  ? 401 TYR C CE2 1 
ATOM   10115 C  CZ  . TYR C  1 370 ? 20.27800  -14.85200 -34.70400 1.000 84.10000  ? 401 TYR C CZ  1 
ATOM   10116 O  OH  . TYR C  1 370 ? 20.27200  -14.07500 -33.56200 1.000 75.22000  ? 401 TYR C OH  1 
ATOM   10117 N  N   . LYS C  1 371 ? 20.93500  -20.77200 -39.40000 1.000 91.69000  ? 402 LYS C N   1 
ATOM   10118 C  CA  . LYS C  1 371 ? 20.39000  -21.81100 -40.27500 1.000 87.21000  ? 402 LYS C CA  1 
ATOM   10119 C  C   . LYS C  1 371 ? 19.16900  -22.45600 -39.63800 1.000 87.41000  ? 402 LYS C C   1 
ATOM   10120 O  O   . LYS C  1 371 ? 19.24600  -22.96500 -38.51700 1.000 94.72000  ? 402 LYS C O   1 
ATOM   10121 C  CB  . LYS C  1 371 ? 21.44900  -22.87200 -40.57000 1.000 89.71000  ? 402 LYS C CB  1 
ATOM   10122 N  N   . ASP C  1 372 ? 18.04700  -22.43900 -40.35900 1.000 88.29000  ? 403 ASP C N   1 
ATOM   10123 C  CA  . ASP C  1 372 ? 16.76800  -22.97200 -39.89200 1.000 93.65000  ? 403 ASP C CA  1 
ATOM   10124 C  C   . ASP C  1 372 ? 16.23000  -22.20800 -38.68200 1.000 94.27000  ? 403 ASP C C   1 
ATOM   10125 O  O   . ASP C  1 372 ? 15.32100  -22.69200 -37.99200 1.000 97.31000  ? 403 ASP C O   1 
ATOM   10126 C  CB  . ASP C  1 372 ? 16.86900  -24.47200 -39.57200 1.000 92.51000  ? 403 ASP C CB  1 
ATOM   10127 N  N   . GLU C  1 373 ? 16.76500  -21.00900 -38.42700 1.000 93.02000  ? 404 GLU C N   1 
ATOM   10128 C  CA  . GLU C  1 373 ? 16.36200  -20.15200 -37.31600 1.000 92.58000  ? 404 GLU C CA  1 
ATOM   10129 C  C   . GLU C  1 373 ? 15.95600  -18.77600 -37.84100 1.000 91.30000  ? 404 GLU C C   1 
ATOM   10130 O  O   . GLU C  1 373 ? 16.23000  -18.42200 -38.99000 1.000 89.88000  ? 404 GLU C O   1 
ATOM   10131 C  CB  . GLU C  1 373 ? 17.49400  -20.03400 -36.27400 1.000 87.92000  ? 404 GLU C CB  1 
ATOM   10132 N  N   . MET C  1 374 ? 15.27000  -18.00500 -36.99800 1.000 86.03000  ? 405 MET C N   1 
ATOM   10133 C  CA  . MET C  1 374 ? 14.61900  -16.77000 -37.41800 1.000 79.38000  ? 405 MET C CA  1 
ATOM   10134 C  C   . MET C  1 374 ? 15.29000  -15.51400 -36.85600 1.000 76.66000  ? 405 MET C C   1 
ATOM   10135 O  O   . MET C  1 374 ? 15.93200  -15.54200 -35.80400 1.000 76.36000  ? 405 MET C O   1 
ATOM   10136 C  CB  . MET C  1 374 ? 13.14800  -16.77500 -37.01700 1.000 78.19000  ? 405 MET C CB  1 
ATOM   10137 C  CG  . MET C  1 374 ? 12.27200  -17.64400 -37.87700 1.000 84.35000  ? 405 MET C CG  1 
ATOM   10138 S  SD  . MET C  1 374 ? 11.80700  -16.95700 -39.47400 1.000 88.06000  ? 405 MET C SD  1 
ATOM   10139 C  CE  . MET C  1 374 ? 10.11900  -17.54100 -39.55700 1.000 76.20000  ? 405 MET C CE  1 
ATOM   10140 N  N   . ILE C  1 375 ? 15.20200  -14.42700 -37.62000 1.000 72.01000  ? 406 ILE C N   1 
ATOM   10141 C  CA  . ILE C  1 375 ? 15.42300  -13.06600 -37.13600 1.000 71.13000  ? 406 ILE C CA  1 
ATOM   10142 C  C   . ILE C  1 375 ? 14.11400  -12.30800 -37.29700 1.000 68.03000  ? 406 ILE C C   1 
ATOM   10143 O  O   . ILE C  1 375 ? 13.57400  -12.23900 -38.40500 1.000 66.31000  ? 406 ILE C O   1 
ATOM   10144 C  CB  . ILE C  1 375 ? 16.55100  -12.34800 -37.88700 1.000 73.31000  ? 406 ILE C CB  1 
ATOM   10145 C  CG1 . ILE C  1 375 ? 17.90400  -12.89700 -37.44600 1.000 70.90000  ? 406 ILE C CG1 1 
ATOM   10146 C  CG2 . ILE C  1 375 ? 16.43500  -10.84300 -37.67500 1.000 69.59000  ? 406 ILE C CG2 1 
ATOM   10147 C  CD1 . ILE C  1 375 ? 19.06800  -12.41100 -38.27200 1.000 73.76000  ? 406 ILE C CD1 1 
ATOM   10148 N  N   . TYR C  1 376 ? 13.61500  -11.72700 -36.20600 1.000 68.60000  ? 407 TYR C N   1 
ATOM   10149 C  CA  . TYR C  1 376 ? 12.25500  -11.20500 -36.13500 1.000 67.20000  ? 407 TYR C CA  1 
ATOM   10150 C  C   . TYR C  1 376 ? 12.21900  -9.68500  -36.06800 1.000 66.89000  ? 407 TYR C C   1 
ATOM   10151 O  O   . TYR C  1 376 ? 13.20300  -9.02300  -35.72800 1.000 69.73000  ? 407 TYR C O   1 
ATOM   10152 C  CB  . TYR C  1 376 ? 11.52600  -11.73500 -34.90400 1.000 70.76000  ? 407 TYR C CB  1 
ATOM   10153 C  CG  . TYR C  1 376 ? 11.28000  -13.20900 -34.92400 1.000 71.05000  ? 407 TYR C CG  1 
ATOM   10154 C  CD1 . TYR C  1 376 ? 10.45200  -13.77000 -35.87500 1.000 71.26000  ? 407 TYR C CD1 1 
ATOM   10155 C  CD2 . TYR C  1 376 ? 11.88400  -14.04800 -33.99900 1.000 74.77000  ? 407 TYR C CD2 1 
ATOM   10156 C  CE1 . TYR C  1 376 ? 10.21800  -15.12800 -35.91200 1.000 72.86000  ? 407 TYR C CE1 1 
ATOM   10157 C  CE2 . TYR C  1 376 ? 11.65100  -15.41900 -34.02300 1.000 77.17000  ? 407 TYR C CE2 1 
ATOM   10158 C  CZ  . TYR C  1 376 ? 10.80800  -15.94000 -34.98600 1.000 80.04000  ? 407 TYR C CZ  1 
ATOM   10159 O  OH  . TYR C  1 376 ? 10.55900  -17.28000 -35.04700 1.000 83.54000  ? 407 TYR C OH  1 
ATOM   10160 N  N   . SER C  1 377 ? 11.04200  -9.14900  -36.37500 1.000 60.09000  ? 408 SER C N   1 
ATOM   10161 C  CA  . SER C  1 377 ? 10.69500  -7.77300  -36.05900 1.000 59.10000  ? 408 SER C CA  1 
ATOM   10162 C  C   . SER C  1 377 ? 9.18400   -7.66900  -35.95100 1.000 61.58000  ? 408 SER C C   1 
ATOM   10163 O  O   . SER C  1 377 ? 8.47000   -8.17500  -36.81800 1.000 65.81000  ? 408 SER C O   1 
ATOM   10164 C  CB  . SER C  1 377 ? 11.20400  -6.81000  -37.12900 1.000 62.63000  ? 408 SER C CB  1 
ATOM   10165 O  OG  . SER C  1 377 ? 10.74200  -5.49200  -36.87400 1.000 60.17000  ? 408 SER C OG  1 
ATOM   10166 N  N   . LEU C  1 378 ? 8.70200   -7.00800  -34.90100 1.000 58.83000  ? 409 LEU C N   1 
ATOM   10167 C  CA  . LEU C  1 378 ? 7.28300   -6.70300  -34.76400 1.000 62.95000  ? 409 LEU C CA  1 
ATOM   10168 C  C   . LEU C  1 378 ? 7.16400   -5.31400  -34.17800 1.000 61.96000  ? 409 LEU C C   1 
ATOM   10169 O  O   . LEU C  1 378 ? 7.68600   -5.05500  -33.08800 1.000 60.43000  ? 409 LEU C O   1 
ATOM   10170 C  CB  . LEU C  1 378 ? 6.55400   -7.71700  -33.87900 1.000 63.04000  ? 409 LEU C CB  1 
ATOM   10171 C  CG  . LEU C  1 378 ? 5.03800   -7.50800  -33.79000 1.000 63.81000  ? 409 LEU C CG  1 
ATOM   10172 C  CD1 . LEU C  1 378 ? 4.33500   -8.84600  -33.64900 1.000 67.67000  ? 409 LEU C CD1 1 
ATOM   10173 C  CD2 . LEU C  1 378 ? 4.64900   -6.60100  -32.62400 1.000 62.04000  ? 409 LEU C CD2 1 
ATOM   10174 N  N   . ARG C  1 379 ? 6.46700   -4.43500  -34.88100 1.000 57.46000  ? 410 ARG C N   1 
ATOM   10175 C  CA  . ARG C  1 379 ? 6.33600   -3.05300  -34.46400 1.000 60.88000  ? 410 ARG C CA  1 
ATOM   10176 C  C   . ARG C  1 379 ? 4.87200   -2.73400  -34.22900 1.000 64.51000  ? 410 ARG C C   1 
ATOM   10177 O  O   . ARG C  1 379 ? 4.04500   -2.93800  -35.12000 1.000 67.95000  ? 410 ARG C O   1 
ATOM   10178 C  CB  . ARG C  1 379 ? 6.91800   -2.11600  -35.50700 1.000 62.17000  ? 410 ARG C CB  1 
ATOM   10179 C  CG  . ARG C  1 379 ? 6.90000   -0.67900  -35.08400 1.000 62.85000  ? 410 ARG C CG  1 
ATOM   10180 C  CD  . ARG C  1 379 ? 5.83400   0.03500   -35.84100 1.000 60.31000  ? 410 ARG C CD  1 
ATOM   10181 N  NE  . ARG C  1 379 ? 5.45200   1.29000   -35.21300 1.000 59.11000  ? 410 ARG C NE  1 
ATOM   10182 C  CZ  . ARG C  1 379 ? 6.00800   2.45600   -35.50700 1.000 59.82000  ? 410 ARG C CZ  1 
ATOM   10183 N  NH1 . ARG C  1 379 ? 6.99300   2.55200   -36.38700 1.000 60.95000  ? 410 ARG C NH1 1 
ATOM   10184 N  NH2 . ARG C  1 379 ? 5.54200   3.55700   -34.93400 1.000 63.80000  ? 410 ARG C NH2 1 
ATOM   10185 N  N   . TYR C  1 380 ? 4.55700   -2.23200  -33.03500 1.000 63.08000  ? 411 TYR C N   1 
ATOM   10186 C  CA  . TYR C  1 380 ? 3.18200   -1.87900  -32.71200 1.000 62.34000  ? 411 TYR C CA  1 
ATOM   10187 C  C   . TYR C  1 380 ? 2.76300   -0.62000  -33.46100 1.000 57.15000  ? 411 TYR C C   1 
ATOM   10188 O  O   . TYR C  1 380 ? 3.53300   0.33100   -33.58700 1.000 59.11000  ? 411 TYR C O   1 
ATOM   10189 C  CB  . TYR C  1 380 ? 3.02800   -1.67200  -31.21100 1.000 66.42000  ? 411 TYR C CB  1 
ATOM   10190 C  CG  . TYR C  1 380 ? 3.33800   -2.89500  -30.39000 1.000 62.27000  ? 411 TYR C CG  1 
ATOM   10191 C  CD1 . TYR C  1 380 ? 2.54900   -4.02900  -30.48100 1.000 69.81000  ? 411 TYR C CD1 1 
ATOM   10192 C  CD2 . TYR C  1 380 ? 4.38900   -2.90800  -29.49900 1.000 63.61000  ? 411 TYR C CD2 1 
ATOM   10193 C  CE1 . TYR C  1 380 ? 2.81200   -5.15100  -29.72700 1.000 64.86000  ? 411 TYR C CE1 1 
ATOM   10194 C  CE2 . TYR C  1 380 ? 4.65900   -4.02200  -28.73600 1.000 65.69000  ? 411 TYR C CE2 1 
ATOM   10195 C  CZ  . TYR C  1 380 ? 3.86500   -5.13900  -28.85200 1.000 66.83000  ? 411 TYR C CZ  1 
ATOM   10196 O  OH  . TYR C  1 380 ? 4.13100   -6.25700  -28.09500 1.000 76.57000  ? 411 TYR C OH  1 
ATOM   10197 N  N   . ARG C  1 381 ? 1.54900   -0.64200  -34.00700 1.000 64.63000  ? 412 ARG C N   1 
ATOM   10198 C  CA  . ARG C  1 381 ? 0.92000   0.49200   -34.67900 1.000 62.89000  ? 412 ARG C CA  1 
ATOM   10199 C  C   . ARG C  1 381 ? -0.38100  0.83400   -33.96200 1.000 61.87000  ? 412 ARG C C   1 
ATOM   10200 O  O   . ARG C  1 381 ? -0.73000  0.22400   -32.95100 1.000 68.37000  ? 412 ARG C O   1 
ATOM   10201 C  CB  . ARG C  1 381 ? 0.68900   0.16700   -36.15700 1.000 60.93000  ? 412 ARG C CB  1 
ATOM   10202 C  CG  . ARG C  1 381 ? 1.97100   0.03000   -36.93800 1.000 63.26000  ? 412 ARG C CG  1 
ATOM   10203 C  CD  . ARG C  1 381 ? 2.50500   1.37800   -37.42200 1.000 59.57000  ? 412 ARG C CD  1 
ATOM   10204 N  NE  . ARG C  1 381 ? 3.76100   1.19200   -38.14000 1.000 58.84000  ? 412 ARG C NE  1 
ATOM   10205 C  CZ  . ARG C  1 381 ? 4.51400   2.16600   -38.63200 1.000 61.47000  ? 412 ARG C CZ  1 
ATOM   10206 N  NH1 . ARG C  1 381 ? 4.15800   3.43600   -38.53800 1.000 59.09000  ? 412 ARG C NH1 1 
ATOM   10207 N  NH2 . ARG C  1 381 ? 5.66100   1.85600   -39.22800 1.000 67.15000  ? 412 ARG C NH2 1 
ATOM   10208 N  N   . GLU C  1 382 ? -1.13900  1.77300   -34.53400 1.000 65.89000  ? 413 GLU C N   1 
ATOM   10209 C  CA  . GLU C  1 382 ? -2.38900  2.23800   -33.92600 1.000 64.06000  ? 413 GLU C CA  1 
ATOM   10210 C  C   . GLU C  1 382 ? -3.51600  1.25400   -34.25700 1.000 67.61000  ? 413 GLU C C   1 
ATOM   10211 O  O   . GLU C  1 382 ? -4.38700  1.50400   -35.09800 1.000 57.77000  ? 413 GLU C O   1 
ATOM   10212 C  CB  . GLU C  1 382 ? -2.73400  3.63400   -34.42400 1.000 62.46000  ? 413 GLU C CB  1 
ATOM   10213 C  CG  . GLU C  1 382 ? -1.59000  4.60300   -34.39300 1.000 73.56000  ? 413 GLU C CG  1 
ATOM   10214 C  CD  . GLU C  1 382 ? -0.85300  4.57900   -33.07400 1.000 85.85000  ? 413 GLU C CD  1 
ATOM   10215 O  OE1 . GLU C  1 382 ? -1.51000  4.71300   -32.00900 1.000 85.80000  ? 413 GLU C OE1 1 
ATOM   10216 O  OE2 . GLU C  1 382 ? 0.38700   4.40200   -33.11500 1.000 76.72000  ? 413 GLU C OE2 1 
ATOM   10217 N  N   . GLY C  1 383 ? -3.48900  0.10700   -33.56800 1.000 66.30000  ? 414 GLY C N   1 
ATOM   10218 C  CA  . GLY C  1 383 ? -4.53500  -0.89400  -33.70100 1.000 67.63000  ? 414 GLY C CA  1 
ATOM   10219 C  C   . GLY C  1 383 ? -4.15300  -2.16300  -34.44200 1.000 68.36000  ? 414 GLY C C   1 
ATOM   10220 O  O   . GLY C  1 383 ? -4.99600  -3.06000  -34.55700 1.000 65.84000  ? 414 GLY C O   1 
ATOM   10221 N  N   . TYR C  1 384 ? -2.91300  -2.29200  -34.90800 1.000 62.23000  ? 415 TYR C N   1 
ATOM   10222 C  CA  . TYR C  1 384 ? -2.45400  -3.46600  -35.64600 1.000 65.39000  ? 415 TYR C CA  1 
ATOM   10223 C  C   . TYR C  1 384 ? -0.94100  -3.54000  -35.47000 1.000 66.91000  ? 415 TYR C C   1 
ATOM   10224 O  O   . TYR C  1 384 ? -0.33900  -2.69900  -34.79700 1.000 70.56000  ? 415 TYR C O   1 
ATOM   10225 C  CB  . TYR C  1 384 ? -2.86000  -3.40400  -37.13400 1.000 62.83000  ? 415 TYR C CB  1 
ATOM   10226 C  CG  . TYR C  1 384 ? -2.18500  -2.29300  -37.92200 1.000 59.90000  ? 415 TYR C CG  1 
ATOM   10227 C  CD1 . TYR C  1 384 ? -2.71500  -1.00200  -37.93600 1.000 54.74000  ? 415 TYR C CD1 1 
ATOM   10228 C  CD2 . TYR C  1 384 ? -1.02300  -2.53900  -38.65700 1.000 55.55000  ? 415 TYR C CD2 1 
ATOM   10229 C  CE1 . TYR C  1 384 ? -2.09900  0.02700   -38.64700 1.000 51.72000  ? 415 TYR C CE1 1 
ATOM   10230 C  CE2 . TYR C  1 384 ? -0.39800  -1.51900  -39.36900 1.000 52.56000  ? 415 TYR C CE2 1 
ATOM   10231 C  CZ  . TYR C  1 384 ? -0.93500  -0.23800  -39.35500 1.000 55.08000  ? 415 TYR C CZ  1 
ATOM   10232 O  OH  . TYR C  1 384 ? -0.31600  0.77400   -40.06500 1.000 58.89000  ? 415 TYR C OH  1 
ATOM   10233 N  N   . ASN C  1 385 ? -0.32900  -4.57600  -36.04100 1.000 67.35000  ? 416 ASN C N   1 
ATOM   10234 C  CA  . ASN C  1 385 ? 1.11200   -4.76200  -35.95500 1.000 62.54000  ? 416 ASN C CA  1 
ATOM   10235 C  C   . ASN C  1 385 ? 1.72500   -4.92800  -37.33800 1.000 64.28000  ? 416 ASN C C   1 
ATOM   10236 O  O   . ASN C  1 385 ? 1.13800   -5.57100  -38.21300 1.000 66.63000  ? 416 ASN C O   1 
ATOM   10237 C  CB  . ASN C  1 385 ? 1.45100   -5.96900  -35.08600 1.000 70.24000  ? 416 ASN C CB  1 
ATOM   10238 C  CG  . ASN C  1 385 ? 0.87700   -5.85300  -33.69100 1.000 73.34000  ? 416 ASN C CG  1 
ATOM   10239 O  OD1 . ASN C  1 385 ? 1.01500   -4.82100  -33.03000 1.000 70.76000  ? 416 ASN C OD1 1 
ATOM   10240 N  ND2 . ASN C  1 385 ? 0.21700   -6.90800  -33.24000 1.000 74.27000  ? 416 ASN C ND2 1 
ATOM   10241 N  N   . ASP C  1 386 ? 2.89100   -4.31200  -37.53400 1.000 60.34000  ? 417 ASP C N   1 
ATOM   10242 C  CA  . ASP C  1 386 ? 3.76100   -4.58100  -38.67100 1.000 63.37000  ? 417 ASP C CA  1 
ATOM   10243 C  C   . ASP C  1 386 ? 4.73500   -5.69600  -38.30800 1.000 64.27000  ? 417 ASP C C   1 
ATOM   10244 O  O   . ASP C  1 386 ? 5.24700   -5.73500  -37.18700 1.000 66.11000  ? 417 ASP C O   1 
ATOM   10245 C  CB  . ASP C  1 386 ? 4.54300   -3.33600  -39.07700 1.000 59.47000  ? 417 ASP C CB  1 
ATOM   10246 C  CG  . ASP C  1 386 ? 3.66700   -2.28400  -39.69500 1.000 62.13000  ? 417 ASP C CG  1 
ATOM   10247 O  OD1 . ASP C  1 386 ? 2.59900   -2.64400  -40.22500 1.000 64.70000  ? 417 ASP C OD1 1 
ATOM   10248 O  OD2 . ASP C  1 386 ? 4.06900   -1.10000  -39.70400 1.000 61.71000  ? 417 ASP C OD2 1 
ATOM   10249 N  N   . VAL C  1 387 ? 4.99200   -6.60700  -39.25400 1.000 60.81000  ? 418 VAL C N   1 
ATOM   10250 C  CA  . VAL C  1 387 ? 5.79700   -7.79200  -38.96700 1.000 56.34000  ? 418 VAL C CA  1 
ATOM   10251 C  C   . VAL C  1 387 ? 6.88800   -7.94900  -40.02000 1.000 57.76000  ? 418 VAL C C   1 
ATOM   10252 O  O   . VAL C  1 387 ? 6.72500   -7.56000  -41.18000 1.000 62.10000  ? 418 VAL C O   1 
ATOM   10253 C  CB  . VAL C  1 387 ? 4.92800   -9.07700  -38.89600 1.000 59.29000  ? 418 VAL C CB  1 
ATOM   10254 C  CG1 . VAL C  1 387 ? 5.76300   -10.29000 -38.49600 1.000 61.89000  ? 418 VAL C CG1 1 
ATOM   10255 C  CG2 . VAL C  1 387 ? 3.79300   -8.91000  -37.91600 1.000 59.14000  ? 418 VAL C CG2 1 
ATOM   10256 N  N   . GLY C  1 388 ? 8.01900   -8.50500  -39.59500 1.000 56.31000  ? 419 GLY C N   1 
ATOM   10257 C  CA  . GLY C  1 388 ? 9.06500   -8.95600  -40.49200 1.000 58.10000  ? 419 GLY C CA  1 
ATOM   10258 C  C   . GLY C  1 388 ? 9.76500   -10.17300 -39.91900 1.000 60.68000  ? 419 GLY C C   1 
ATOM   10259 O  O   . GLY C  1 388 ? 9.97100   -10.24700 -38.70300 1.000 65.87000  ? 419 GLY C O   1 
ATOM   10260 N  N   . ALA C  1 389 ? 10.09300  -11.15000 -40.77000 1.000 58.15000  ? 420 ALA C N   1 
ATOM   10261 C  CA  . ALA C  1 389 ? 10.74900  -12.38100 -40.34400 1.000 57.74000  ? 420 ALA C CA  1 
ATOM   10262 C  C   . ALA C  1 389 ? 11.51300  -12.96700 -41.52200 1.000 57.16000  ? 420 ALA C C   1 
ATOM   10263 O  O   . ALA C  1 389 ? 10.95000  -13.11800 -42.60800 1.000 64.39000  ? 420 ALA C O   1 
ATOM   10264 C  CB  . ALA C  1 389 ? 9.73200   -13.38900 -39.80300 1.000 64.11000  ? 420 ALA C CB  1 
ATOM   10265 N  N   . ARG C  1 390 ? 12.78700  -13.26800 -41.31700 1.000 56.67000  ? 421 ARG C N   1 
ATOM   10266 C  CA  . ARG C  1 390 ? 13.64900  -13.81400 -42.35500 1.000 64.92000  ? 421 ARG C CA  1 
ATOM   10267 C  C   . ARG C  1 390 ? 14.27000  -15.14300 -41.92900 1.000 72.16000  ? 421 ARG C C   1 
ATOM   10268 O  O   . ARG C  1 390 ? 14.72300  -15.29100 -40.78600 1.000 69.79000  ? 421 ARG C O   1 
ATOM   10269 C  CB  . ARG C  1 390 ? 14.74600  -12.81400 -42.72600 1.000 58.52000  ? 421 ARG C CB  1 
ATOM   10270 C  CG  . ARG C  1 390 ? 15.67100  -13.28000 -43.81400 1.000 60.11000  ? 421 ARG C CG  1 
ATOM   10271 C  CD  . ARG C  1 390 ? 16.84300  -12.34300 -43.96300 1.000 59.79000  ? 421 ARG C CD  1 
ATOM   10272 N  NE  . ARG C  1 390 ? 17.89900  -12.94200 -44.75600 1.000 59.02000  ? 421 ARG C NE  1 
ATOM   10273 C  CZ  . ARG C  1 390 ? 18.82000  -12.24900 -45.40100 1.000 63.09000  ? 421 ARG C CZ  1 
ATOM   10274 N  NH1 . ARG C  1 390 ? 18.81100  -10.92500 -45.39700 1.000 59.19000  ? 421 ARG C NH1 1 
ATOM   10275 N  NH2 . ARG C  1 390 ? 19.79100  -12.89600 -46.03900 1.000 58.16000  ? 421 ARG C NH2 1 
ATOM   10276 N  N   . MET C  1 391 ? 14.32700  -16.08600 -42.88100 1.000 69.41000  ? 422 MET C N   1 
ATOM   10277 C  CA  . MET C  1 391 ? 15.04200  -17.35700 -42.73900 1.000 69.01000  ? 422 MET C CA  1 
ATOM   10278 C  C   . MET C  1 391 ? 15.83900  -17.60100 -44.01300 1.000 66.70000  ? 422 MET C C   1 
ATOM   10279 O  O   . MET C  1 391 ? 15.25400  -17.81000 -45.07800 1.000 65.47000  ? 422 MET C O   1 
ATOM   10280 C  CB  . MET C  1 391 ? 14.07500  -18.52000 -42.52000 1.000 71.00000  ? 422 MET C CB  1 
ATOM   10281 C  CG  . MET C  1 391 ? 13.91900  -19.01200 -41.10500 1.000 84.39000  ? 422 MET C CG  1 
ATOM   10282 S  SD  . MET C  1 391 ? 12.76900  -20.41600 -40.98400 1.000 99.07000  ? 422 MET C SD  1 
ATOM   10283 C  CE  . MET C  1 391 ? 13.85400  -21.75800 -41.45900 1.000 81.00000  ? 422 MET C CE  1 
ATOM   10284 N  N   . GLY C  1 392 ? 17.15900  -17.58000 -43.91600 1.000 71.46000  ? 423 GLY C N   1 
ATOM   10285 C  CA  . GLY C  1 392 ? 17.95500  -17.85800 -45.10500 1.000 72.00000  ? 423 GLY C CA  1 
ATOM   10286 C  C   . GLY C  1 392 ? 17.73000  -16.80500 -46.17900 1.000 69.34000  ? 423 GLY C C   1 
ATOM   10287 O  O   . GLY C  1 392 ? 17.99100  -15.61300 -45.97800 1.000 68.62000  ? 423 GLY C O   1 
ATOM   10288 N  N   . ASP C  1 393 ? 17.22900  -17.24100 -47.33600 1.000 67.09000  ? 424 ASP C N   1 
ATOM   10289 C  CA  . ASP C  1 393 ? 16.92900  -16.34700 -48.44500 1.000 67.28000  ? 424 ASP C CA  1 
ATOM   10290 C  C   . ASP C  1 393 ? 15.49900  -15.81900 -48.43500 1.000 63.53000  ? 424 ASP C C   1 
ATOM   10291 O  O   . ASP C  1 393 ? 15.17100  -14.97600 -49.27800 1.000 60.14000  ? 424 ASP C O   1 
ATOM   10292 C  CB  . ASP C  1 393 ? 17.17900  -17.04600 -49.79100 1.000 67.82000  ? 424 ASP C CB  1 
ATOM   10293 C  CG  . ASP C  1 393 ? 18.63900  -17.39700 -50.02100 1.000 74.69000  ? 424 ASP C CG  1 
ATOM   10294 O  OD1 . ASP C  1 393 ? 19.51900  -16.58700 -49.66400 1.000 78.02000  ? 424 ASP C OD1 1 
ATOM   10295 O  OD2 . ASP C  1 393 ? 18.90900  -18.47300 -50.59200 1.000 81.65000  ? 424 ASP C OD2 1 
ATOM   10296 N  N   . TRP C  1 394 ? 14.66800  -16.24300 -47.48400 1.000 58.99000  ? 425 TRP C N   1 
ATOM   10297 C  CA  . TRP C  1 394 ? 13.23900  -15.96200 -47.49500 1.000 59.82000  ? 425 TRP C CA  1 
ATOM   10298 C  C   . TRP C  1 394 ? 12.84400  -15.01900 -46.36200 1.000 65.82000  ? 425 TRP C C   1 
ATOM   10299 O  O   . TRP C  1 394 ? 13.33300  -15.15100 -45.23500 1.000 59.99000  ? 425 TRP C O   1 
ATOM   10300 C  CB  . TRP C  1 394 ? 12.45800  -17.26500 -47.38900 1.000 66.72000  ? 425 TRP C CB  1 
ATOM   10301 C  CG  . TRP C  1 394 ? 12.70100  -18.14300 -48.56600 1.000 74.89000  ? 425 TRP C CG  1 
ATOM   10302 C  CD1 . TRP C  1 394 ? 13.62900  -19.13700 -48.67300 1.000 71.30000  ? 425 TRP C CD1 1 
ATOM   10303 C  CD2 . TRP C  1 394 ? 12.02500  -18.08500 -49.82700 1.000 73.36000  ? 425 TRP C CD2 1 
ATOM   10304 N  NE1 . TRP C  1 394 ? 13.56000  -19.71500 -49.91800 1.000 74.25000  ? 425 TRP C NE1 1 
ATOM   10305 C  CE2 . TRP C  1 394 ? 12.58600  -19.08500 -50.64700 1.000 72.44000  ? 425 TRP C CE2 1 
ATOM   10306 C  CE3 . TRP C  1 394 ? 10.99300  -17.28900 -50.33900 1.000 66.47000  ? 425 TRP C CE3 1 
ATOM   10307 C  CZ2 . TRP C  1 394 ? 12.15100  -19.31100 -51.94900 1.000 72.00000  ? 425 TRP C CZ2 1 
ATOM   10308 C  CZ3 . TRP C  1 394 ? 10.56100  -17.51800 -51.63200 1.000 68.42000  ? 425 TRP C CZ3 1 
ATOM   10309 C  CH2 . TRP C  1 394 ? 11.14000  -18.51800 -52.42200 1.000 72.74000  ? 425 TRP C CH2 1 
ATOM   10310 N  N   . LYS C  1 395 ? 11.96100  -14.05900 -46.67600 1.000 62.07000  ? 426 LYS C N   1 
ATOM   10311 C  CA  . LYS C  1 395 ? 11.43700  -13.10000 -45.71000 1.000 60.74000  ? 426 LYS C CA  1 
ATOM   10312 C  C   . LYS C  1 395 ? 9.94200   -12.89800 -45.90000 1.000 60.35000  ? 426 LYS C C   1 
ATOM   10313 O  O   . LYS C  1 395 ? 9.46900   -12.80200 -47.03400 1.000 61.94000  ? 426 LYS C O   1 
ATOM   10314 C  CB  . LYS C  1 395 ? 12.10800  -11.72600 -45.82200 1.000 59.21000  ? 426 LYS C CB  1 
ATOM   10315 C  CG  . LYS C  1 395 ? 11.64200  -10.77200 -44.73000 1.000 60.19000  ? 426 LYS C CG  1 
ATOM   10316 C  CD  . LYS C  1 395 ? 11.75900  -9.32500  -45.12500 1.000 62.62000  ? 426 LYS C CD  1 
ATOM   10317 C  CE  . LYS C  1 395 ? 11.26100  -8.42000  -43.99300 1.000 65.76000  ? 426 LYS C CE  1 
ATOM   10318 N  NZ  . LYS C  1 395 ? 11.60800  -6.98200  -44.22700 1.000 60.73000  ? 426 LYS C NZ  1 
ATOM   10319 N  N   . ILE C  1 396 ? 9.20600   -12.81100 -44.79000 1.000 64.14000  ? 427 ILE C N   1 
ATOM   10320 C  CA  . ILE C  1 396 ? 7.80200   -12.40800 -44.80500 1.000 57.52000  ? 427 ILE C CA  1 
ATOM   10321 C  C   . ILE C  1 396 ? 7.67000   -11.01900 -44.19000 1.000 58.89000  ? 427 ILE C C   1 
ATOM   10322 O  O   . ILE C  1 396 ? 8.48400   -10.58800 -43.36400 1.000 60.44000  ? 427 ILE C O   1 
ATOM   10323 C  CB  . ILE C  1 396 ? 6.86700   -13.40000 -44.08600 1.000 60.57000  ? 427 ILE C CB  1 
ATOM   10324 C  CG1 . ILE C  1 396 ? 7.35300   -13.69800 -42.65700 1.000 66.04000  ? 427 ILE C CG1 1 
ATOM   10325 C  CG2 . ILE C  1 396 ? 6.75700   -14.66900 -44.88500 1.000 68.05000  ? 427 ILE C CG2 1 
ATOM   10326 C  CD1 . ILE C  1 396 ? 6.33000   -14.46100 -41.80200 1.000 61.04000  ? 427 ILE C CD1 1 
ATOM   10327 N  N   . THR C  1 397 ? 6.65400   -10.30200 -44.64500 1.000 60.35000  ? 428 THR C N   1 
ATOM   10328 C  CA  . THR C  1 397 ? 6.40700   -8.91900  -44.27400 1.000 62.04000  ? 428 THR C CA  1 
ATOM   10329 C  C   . THR C  1 397 ? 4.91200   -8.68000  -44.23900 1.000 57.46000  ? 428 THR C C   1 
ATOM   10330 O  O   . THR C  1 397 ? 4.21200   -9.08300  -45.16800 1.000 60.04000  ? 428 THR C O   1 
ATOM   10331 C  CB  . THR C  1 397 ? 7.06100   -7.95900  -45.27700 1.000 61.01000  ? 428 THR C CB  1 
ATOM   10332 O  OG1 . THR C  1 397 ? 8.45700   -8.25300  -45.38500 1.000 64.92000  ? 428 THR C OG1 1 
ATOM   10333 C  CG2 . THR C  1 397 ? 6.84800   -6.50900  -44.88600 1.000 60.95000  ? 428 THR C CG2 1 
ATOM   10334 N  N   . ARG C  1 398 ? 4.43300   -8.03100  -43.17800 1.000 61.76000  ? 429 ARG C N   1 
ATOM   10335 C  CA  . ARG C  1 398 ? 3.11600   -7.39700  -43.16400 1.000 60.18000  ? 429 ARG C CA  1 
ATOM   10336 C  C   . ARG C  1 398 ? 3.30100   -5.94000  -42.76500 1.000 57.07000  ? 429 ARG C C   1 
ATOM   10337 O  O   . ARG C  1 398 ? 3.86100   -5.64700  -41.70900 1.000 63.46000  ? 429 ARG C O   1 
ATOM   10338 C  CB  . ARG C  1 398 ? 2.13200   -8.09800  -42.21800 1.000 61.74000  ? 429 ARG C CB  1 
ATOM   10339 C  CG  . ARG C  1 398 ? 0.68300   -7.78300  -42.55400 1.000 61.67000  ? 429 ARG C CG  1 
ATOM   10340 C  CD  . ARG C  1 398 ? -0.36400  -8.41600  -41.63500 1.000 63.55000  ? 429 ARG C CD  1 
ATOM   10341 N  NE  . ARG C  1 398 ? -1.69600  -7.95000  -42.02700 1.000 64.88000  ? 429 ARG C NE  1 
ATOM   10342 C  CZ  . ARG C  1 398 ? -2.83900  -8.26500  -41.42600 1.000 61.89000  ? 429 ARG C CZ  1 
ATOM   10343 N  NH1 . ARG C  1 398 ? -2.87800  -9.08800  -40.39300 1.000 64.67000  ? 429 ARG C NH1 1 
ATOM   10344 N  NH2 . ARG C  1 398 ? -3.97500  -7.74100  -41.87900 1.000 62.08000  ? 429 ARG C NH2 1 
ATOM   10345 N  N   . MET C  1 399 ? 2.86100   -5.04200  -43.62100 1.000 56.85000  ? 430 MET C N   1 
ATOM   10346 C  CA  . MET C  1 399 ? 2.93400   -3.61000  -43.40100 1.000 60.09000  ? 430 MET C CA  1 
ATOM   10347 C  C   . MET C  1 399 ? 1.53600   -3.04800  -43.56500 1.000 57.84000  ? 430 MET C C   1 
ATOM   10348 O  O   . MET C  1 399 ? 0.77200   -3.53600  -44.40200 1.000 55.06000  ? 430 MET C O   1 
ATOM   10349 C  CB  . MET C  1 399 ? 3.91200   -2.96000  -44.38100 1.000 52.13000  ? 430 MET C CB  1 
ATOM   10350 C  CG  . MET C  1 399 ? 5.34500   -2.96000  -43.87900 1.000 62.05000  ? 430 MET C CG  1 
ATOM   10351 S  SD  . MET C  1 399 ? 5.56800   -1.90200  -42.42300 1.000 60.86000  ? 430 MET C SD  1 
ATOM   10352 C  CE  . MET C  1 399 ? 5.52900   -0.29500  -43.18500 1.000 40.53000  ? 430 MET C CE  1 
ATOM   10353 N  N   . GLY C  1 400 ? 1.17300   -2.09100  -42.70700 1.000 57.09000  ? 431 GLY C N   1 
ATOM   10354 C  CA  . GLY C  1 400 ? -0.10700  -1.39600  -42.82400 1.000 55.39000  ? 431 GLY C CA  1 
ATOM   10355 C  C   . GLY C  1 400 ? -1.33800  -2.26800  -42.70200 1.000 53.58000  ? 431 GLY C C   1 
ATOM   10356 O  O   . GLY C  1 400 ? -2.42800  -1.84400  -43.08700 1.000 53.20000  ? 431 GLY C O   1 
ATOM   10357 N  N   . ASN C  1 401 ? -1.19200  -3.47400  -42.15300 1.000 58.74000  ? 432 ASN C N   1 
ATOM   10358 C  CA  . ASN C  1 401 ? -2.25100  -4.47200  -42.02000 1.000 59.43000  ? 432 ASN C CA  1 
ATOM   10359 C  C   . ASN C  1 401 ? -2.72800  -4.98600  -43.37500 1.000 58.19000  ? 432 ASN C C   1 
ATOM   10360 O  O   . ASN C  1 401 ? -3.78000  -5.62900  -43.46100 1.000 57.89000  ? 432 ASN C O   1 
ATOM   10361 C  CB  . ASN C  1 401 ? -3.43400  -3.94400  -41.19300 1.000 58.06000  ? 432 ASN C CB  1 
ATOM   10362 C  CG  . ASN C  1 401 ? -3.92000  -4.95700  -40.19000 1.000 58.42000  ? 432 ASN C CG  1 
ATOM   10363 O  OD1 . ASN C  1 401 ? -3.15100  -5.81000  -39.75400 1.000 56.74000  ? 432 ASN C OD1 1 
ATOM   10364 N  ND2 . ASN C  1 401 ? -5.19000  -4.86600  -39.80700 1.000 58.36000  ? 432 ASN C ND2 1 
ATOM   10365 N  N   . GLU C  1 402 ? -1.93300  -4.74500  -44.42000 1.000 55.49000  ? 433 GLU C N   1 
ATOM   10366 C  CA  . GLU C  1 402 ? -2.18700  -5.23900  -45.76300 1.000 57.47000  ? 433 GLU C CA  1 
ATOM   10367 C  C   . GLU C  1 402 ? -1.96300  -6.75300  -45.84800 1.000 58.03000  ? 433 GLU C C   1 
ATOM   10368 O  O   . GLU C  1 402 ? -1.49000  -7.37800  -44.89400 1.000 57.10000  ? 433 GLU C O   1 
ATOM   10369 C  CB  . GLU C  1 402 ? -1.29900  -4.47900  -46.75200 1.000 51.31000  ? 433 GLU C CB  1 
ATOM   10370 C  CG  . GLU C  1 402 ? -1.81100  -3.07600  -47.06800 1.000 55.86000  ? 433 GLU C CG  1 
ATOM   10371 C  CD  . GLU C  1 402 ? -3.11700  -3.08900  -47.88800 1.000 62.24000  ? 433 GLU C CD  1 
ATOM   10372 O  OE1 . GLU C  1 402 ? -3.09100  -3.59800  -49.03100 1.000 63.50000  ? 433 GLU C OE1 1 
ATOM   10373 O  OE2 . GLU C  1 402 ? -4.15500  -2.55700  -47.41500 1.000 56.91000  ? 433 GLU C OE2 1 
ATOM   10374 N  N   . PRO C  1 403 ? -2.31000  -7.37800  -46.98300 1.000 56.15000  ? 434 PRO C N   1 
ATOM   10375 C  CA  . PRO C  1 403 ? -2.03800  -8.81400  -47.14000 1.000 52.36000  ? 434 PRO C CA  1 
ATOM   10376 C  C   . PRO C  1 403 ? -0.57000  -9.14200  -46.95300 1.000 52.88000  ? 434 PRO C C   1 
ATOM   10377 O  O   . PRO C  1 403 ? 0.31600   -8.37600  -47.34100 1.000 52.19000  ? 434 PRO C O   1 
ATOM   10378 C  CB  . PRO C  1 403 ? -2.48600  -9.11100  -48.57600 1.000 53.60000  ? 434 PRO C CB  1 
ATOM   10379 C  CG  . PRO C  1 403 ? -3.46700  -8.07800  -48.90200 1.000 55.69000  ? 434 PRO C CG  1 
ATOM   10380 C  CD  . PRO C  1 403 ? -3.16900  -6.86100  -48.06400 1.000 56.13000  ? 434 PRO C CD  1 
ATOM   10381 N  N   . TRP C  1 404 ? -0.33000  -10.33200 -46.40600 1.000 47.80000  ? 435 TRP C N   1 
ATOM   10382 C  CA  . TRP C  1 404 ? 1.02200   -10.80200 -46.15600 1.000 57.56000  ? 435 TRP C CA  1 
ATOM   10383 C  C   . TRP C  1 404 ? 1.81400   -10.92600 -47.45300 1.000 58.84000  ? 435 TRP C C   1 
ATOM   10384 O  O   . TRP C  1 404 ? 1.28600   -11.29900 -48.50200 1.000 60.01000  ? 435 TRP C O   1 
ATOM   10385 C  CB  . TRP C  1 404 ? 0.98100   -12.16300 -45.45500 1.000 63.20000  ? 435 TRP C CB  1 
ATOM   10386 C  CG  . TRP C  1 404 ? 0.69600   -12.09500 -43.99200 1.000 68.76000  ? 435 TRP C CG  1 
ATOM   10387 C  CD1 . TRP C  1 404 ? -0.53100  -12.15700 -43.38800 1.000 70.15000  ? 435 TRP C CD1 1 
ATOM   10388 C  CD2 . TRP C  1 404 ? 1.65700   -11.96500 -42.93500 1.000 66.43000  ? 435 TRP C CD2 1 
ATOM   10389 N  NE1 . TRP C  1 404 ? -0.38900  -12.07100 -42.02100 1.000 69.72000  ? 435 TRP C NE1 1 
ATOM   10390 C  CE2 . TRP C  1 404 ? 0.94300   -11.95400 -41.72000 1.000 69.63000  ? 435 TRP C CE2 1 
ATOM   10391 C  CE3 . TRP C  1 404 ? 3.04700   -11.85100 -42.90000 1.000 66.64000  ? 435 TRP C CE3 1 
ATOM   10392 C  CZ2 . TRP C  1 404 ? 1.57700   -11.82800 -40.48700 1.000 68.98000  ? 435 TRP C CZ2 1 
ATOM   10393 C  CZ3 . TRP C  1 404 ? 3.67500   -11.73700 -41.67200 1.000 66.96000  ? 435 TRP C CZ3 1 
ATOM   10394 C  CH2 . TRP C  1 404 ? 2.94000   -11.72400 -40.48600 1.000 67.12000  ? 435 TRP C CH2 1 
ATOM   10395 N  N   . ARG C  1 405 ? 3.10400   -10.63600 -47.37200 1.000 58.02000  ? 436 ARG C N   1 
ATOM   10396 C  CA  . ARG C  1 405 ? 3.99700   -10.76400 -48.50900 1.000 57.94000  ? 436 ARG C CA  1 
ATOM   10397 C  C   . ARG C  1 405 ? 5.11500   -11.74900 -48.19600 1.000 66.78000  ? 436 ARG C C   1 
ATOM   10398 O  O   . ARG C  1 405 ? 5.61900   -11.80100 -47.06400 1.000 64.35000  ? 436 ARG C O   1 
ATOM   10399 C  CB  . ARG C  1 405 ? 4.57500   -9.39700  -48.89500 1.000 63.32000  ? 436 ARG C CB  1 
ATOM   10400 C  CG  . ARG C  1 405 ? 3.51900   -8.31600  -49.17100 1.000 62.53000  ? 436 ARG C CG  1 
ATOM   10401 C  CD  . ARG C  1 405 ? 4.14000   -6.91400  -49.23500 1.000 62.15000  ? 436 ARG C CD  1 
ATOM   10402 N  NE  . ARG C  1 405 ? 5.15100   -6.75400  -50.27400 1.000 61.96000  ? 436 ARG C NE  1 
ATOM   10403 C  CZ  . ARG C  1 405 ? 4.90900   -6.37000  -51.52000 1.000 61.22000  ? 436 ARG C CZ  1 
ATOM   10404 N  NH1 . ARG C  1 405 ? 3.67600   -6.16900  -51.95800 1.000 60.23000  ? 436 ARG C NH1 1 
ATOM   10405 N  NH2 . ARG C  1 405 ? 5.93300   -6.18400  -52.35000 1.000 57.85000  ? 436 ARG C NH2 1 
ATOM   10406 N  N   . LEU C  1 406 ? 5.51200   -12.51700 -49.21100 1.000 59.97000  ? 437 LEU C N   1 
ATOM   10407 C  CA  . LEU C  1 406 ? 6.65000   -13.42300 -49.13400 1.000 61.22000  ? 437 LEU C CA  1 
ATOM   10408 C  C   . LEU C  1 406 ? 7.64800   -13.02400 -50.20600 1.000 61.61000  ? 437 LEU C C   1 
ATOM   10409 O  O   . LEU C  1 406 ? 7.28200   -12.89700 -51.37700 1.000 63.79000  ? 437 LEU C O   1 
ATOM   10410 C  CB  . LEU C  1 406 ? 6.23300   -14.88800 -49.32300 1.000 61.32000  ? 437 LEU C CB  1 
ATOM   10411 C  CG  . LEU C  1 406 ? 7.39600   -15.88500 -49.53400 1.000 61.84000  ? 437 LEU C CG  1 
ATOM   10412 C  CD1 . LEU C  1 406 ? 8.26300   -16.08300 -48.30800 1.000 60.02000  ? 437 LEU C CD1 1 
ATOM   10413 C  CD2 . LEU C  1 406 ? 6.86700   -17.23200 -50.01000 1.000 71.47000  ? 437 LEU C CD2 1 
ATOM   10414 N  N   . HIS C  1 407 ? 8.89900   -12.81400 -49.80800 1.000 55.11000  ? 438 HIS C N   1 
ATOM   10415 C  CA  . HIS C  1 407 ? 9.93200   -12.40300 -50.74200 1.000 59.79000  ? 438 HIS C CA  1 
ATOM   10416 C  C   . HIS C  1 407 ? 11.13200  -13.33200 -50.65600 1.000 60.27000  ? 438 HIS C C   1 
ATOM   10417 O  O   . HIS C  1 407 ? 11.42800  -13.90100 -49.60000 1.000 59.24000  ? 438 HIS C O   1 
ATOM   10418 C  CB  . HIS C  1 407 ? 10.37700  -10.95900 -50.47900 1.000 56.09000  ? 438 HIS C CB  1 
ATOM   10419 C  CG  . HIS C  1 407 ? 9.25600   -9.97600  -50.54800 1.000 62.47000  ? 438 HIS C CG  1 
ATOM   10420 N  ND1 . HIS C  1 407 ? 8.73600   -9.52400  -51.74300 1.000 59.68000  ? 438 HIS C ND1 1 
ATOM   10421 C  CD2 . HIS C  1 407 ? 8.53200   -9.38100  -49.57000 1.000 60.55000  ? 438 HIS C CD2 1 
ATOM   10422 C  CE1 . HIS C  1 407 ? 7.74100   -8.69000  -51.49700 1.000 61.93000  ? 438 HIS C CE1 1 
ATOM   10423 N  NE2 . HIS C  1 407 ? 7.60100   -8.58200  -50.18600 1.000 65.80000  ? 438 HIS C NE2 1 
ATOM   10424 N  N   . ASN C  1 408 ? 11.79500  -13.52200 -51.79100 1.000 56.90000  ? 439 ASN C N   1 
ATOM   10425 C  CA  . ASN C  1 408 ? 13.15100  -14.06300 -51.78200 1.000 60.37000  ? 439 ASN C CA  1 
ATOM   10426 C  C   . ASN C  1 408 ? 14.07200  -12.85900 -51.65600 1.000 62.68000  ? 439 ASN C C   1 
ATOM   10427 O  O   . ASN C  1 408 ? 14.39200  -12.19100 -52.64700 1.000 60.24000  ? 439 ASN C O   1 
ATOM   10428 C  CB  . ASN C  1 408 ? 13.43400  -14.90800 -53.01700 1.000 62.78000  ? 439 ASN C CB  1 
ATOM   10429 C  CG  . ASN C  1 408 ? 14.78300  -15.59100 -52.95600 1.000 65.23000  ? 439 ASN C CG  1 
ATOM   10430 O  OD1 . ASN C  1 408 ? 15.83000  -14.94200 -52.93700 1.000 70.24000  ? 439 ASN C OD1 1 
ATOM   10431 N  ND2 . ASN C  1 408 ? 14.76200  -16.91400 -52.87000 1.000 66.31000  ? 439 ASN C ND2 1 
ATOM   10432 N  N   . ILE C  1 409 ? 14.48200  -12.57000 -50.41800 1.000 60.44000  ? 440 ILE C N   1 
ATOM   10433 C  CA  . ILE C  1 409 ? 15.20000  -11.33700 -50.14500 1.000 59.10000  ? 440 ILE C CA  1 
ATOM   10434 C  C   . ILE C  1 409 ? 16.56900  -11.34700 -50.79900 1.000 57.45000  ? 440 ILE C C   1 
ATOM   10435 O  O   . ILE C  1 409 ? 17.12600  -10.27800 -51.06600 1.000 63.30000  ? 440 ILE C O   1 
ATOM   10436 C  CB  . ILE C  1 409 ? 15.29300  -11.11500 -48.61600 1.000 62.62000  ? 440 ILE C CB  1 
ATOM   10437 C  CG1 . ILE C  1 409 ? 15.52300  -9.63800  -48.29100 1.000 59.45000  ? 440 ILE C CG1 1 
ATOM   10438 C  CG2 . ILE C  1 409 ? 16.39200  -11.97200 -47.98800 1.000 64.29000  ? 440 ILE C CG2 1 
ATOM   10439 C  CD1 . ILE C  1 409 ? 14.36300  -8.75200  -48.72100 1.000 53.84000  ? 440 ILE C CD1 1 
ATOM   10440 N  N   . THR C  1 410 ? 17.10400  -12.52700 -51.13100 1.000 64.60000  ? 441 THR C N   1 
ATOM   10441 C  CA  . THR C  1 410 ? 18.41900  -12.57400 -51.77100 1.000 71.50000  ? 441 THR C CA  1 
ATOM   10442 C  C   . THR C  1 410 ? 18.35500  -12.10200 -53.22100 1.000 67.31000  ? 441 THR C C   1 
ATOM   10443 O  O   . THR C  1 410 ? 19.27200  -11.42400 -53.70200 1.000 65.65000  ? 441 THR C O   1 
ATOM   10444 C  CB  . THR C  1 410 ? 18.99100  -13.99400 -51.69000 1.000 70.39000  ? 441 THR C CB  1 
ATOM   10445 O  OG1 . THR C  1 410 ? 19.08000  -14.39400 -50.31300 1.000 69.35000  ? 441 THR C OG1 1 
ATOM   10446 C  CG2 . THR C  1 410 ? 20.38800  -14.05800 -52.31500 1.000 63.95000  ? 441 THR C CG2 1 
ATOM   10447 N  N   . GLN C  1 411 ? 17.28400  -12.43800 -53.93000 1.000 63.93000  ? 442 GLN C N   1 
ATOM   10448 C  CA  . GLN C  1 411 ? 17.11300  -11.95800 -55.29500 1.000 69.94000  ? 442 GLN C CA  1 
ATOM   10449 C  C   . GLN C  1 411 ? 16.24600  -10.71700 -55.40400 1.000 68.93000  ? 442 GLN C C   1 
ATOM   10450 O  O   . GLN C  1 411 ? 16.28000  -10.05000 -56.44300 1.000 70.30000  ? 442 GLN C O   1 
ATOM   10451 C  CB  . GLN C  1 411 ? 16.58400  -13.07000 -56.20800 1.000 71.57000  ? 442 GLN C CB  1 
ATOM   10452 C  CG  . GLN C  1 411 ? 17.66500  -14.10400 -56.43400 1.000 75.66000  ? 442 GLN C CG  1 
ATOM   10453 C  CD  . GLN C  1 411 ? 18.84700  -13.48200 -57.19100 1.000 87.56000  ? 442 GLN C CD  1 
ATOM   10454 O  OE1 . GLN C  1 411 ? 18.67500  -12.54700 -57.98800 1.000 89.78000  ? 442 GLN C OE1 1 
ATOM   10455 N  NE2 . GLN C  1 411 ? 20.06100  -13.95700 -56.89200 1.000 90.02000  ? 442 GLN C NE2 1 
ATOM   10456 N  N   . ASP C  1 412 ? 15.48200  -10.39700 -54.36200 1.000 67.52000  ? 443 ASP C N   1 
ATOM   10457 C  CA  . ASP C  1 412 ? 14.48900  -9.33800  -54.39000 1.000 56.36000  ? 443 ASP C CA  1 
ATOM   10458 C  C   . ASP C  1 412 ? 14.70300  -8.49200  -53.12300 1.000 60.10000  ? 443 ASP C C   1 
ATOM   10459 O  O   . ASP C  1 412 ? 13.85700  -8.44500  -52.23200 1.000 52.85000  ? 443 ASP C O   1 
ATOM   10460 C  CB  . ASP C  1 412 ? 13.08100  -9.94300  -54.46700 1.000 56.58000  ? 443 ASP C CB  1 
ATOM   10461 C  CG  . ASP C  1 412 ? 11.97900  -8.90800  -54.39100 1.000 54.68000  ? 443 ASP C CG  1 
ATOM   10462 O  OD1 . ASP C  1 412 ? 12.25000  -7.73200  -54.71700 1.000 58.93000  ? 443 ASP C OD1 1 
ATOM   10463 O  OD2 . ASP C  1 412 ? 10.83700  -9.28300  -54.03000 1.000 56.37000  ? 443 ASP C OD2 1 
ATOM   10464 N  N   . ILE C  1 413 ? 15.86300  -7.82400  -53.05800 1.000 58.20000  ? 444 ILE C N   1 
ATOM   10465 C  CA  . ILE C  1 413 ? 16.24400  -7.08400  -51.85700 1.000 56.38000  ? 444 ILE C CA  1 
ATOM   10466 C  C   . ILE C  1 413 ? 15.28900  -5.92400  -51.60100 1.000 58.61000  ? 444 ILE C C   1 
ATOM   10467 O  O   . ILE C  1 413 ? 15.06600  -5.54100  -50.44500 1.000 61.71000  ? 444 ILE C O   1 
ATOM   10468 C  CB  . ILE C  1 413 ? 17.71000  -6.61100  -51.95500 1.000 54.45000  ? 444 ILE C CB  1 
ATOM   10469 C  CG1 . ILE C  1 413 ? 18.23000  -6.15500  -50.59300 1.000 57.34000  ? 444 ILE C CG1 1 
ATOM   10470 C  CG2 . ILE C  1 413 ? 17.88200  -5.49600  -52.98800 1.000 49.21000  ? 444 ILE C CG2 1 
ATOM   10471 C  CD1 . ILE C  1 413 ? 19.76300  -6.02400  -50.53100 1.000 49.37000  ? 444 ILE C CD1 1 
ATOM   10472 N  N   . GLY C  1 414 ? 14.66700  -5.38500  -52.65300 1.000 59.25000  ? 445 GLY C N   1 
ATOM   10473 C  CA  . GLY C  1 414 ? 13.71600  -4.29500  -52.51800 1.000 51.68000  ? 445 GLY C CA  1 
ATOM   10474 C  C   . GLY C  1 414 ? 12.30800  -4.68100  -52.13500 1.000 56.52000  ? 445 GLY C C   1 
ATOM   10475 O  O   . GLY C  1 414 ? 11.44900  -3.79500  -52.04700 1.000 54.67000  ? 445 GLY C O   1 
ATOM   10476 N  N   . GLU C  1 415 ? 12.03900  -5.96800  -51.89000 1.000 57.92000  ? 446 GLU C N   1 
ATOM   10477 C  CA  . GLU C  1 415 ? 10.70600  -6.43600  -51.48900 1.000 58.27000  ? 446 GLU C CA  1 
ATOM   10478 C  C   . GLU C  1 415 ? 9.62700   -5.97900  -52.48300 1.000 56.29000  ? 446 GLU C C   1 
ATOM   10479 O  O   . GLU C  1 415 ? 8.56700   -5.47900  -52.11400 1.000 54.34000  ? 446 GLU C O   1 
ATOM   10480 C  CB  . GLU C  1 415 ? 10.38700  -5.98200  -50.05400 1.000 55.00000  ? 446 GLU C CB  1 
ATOM   10481 C  CG  . GLU C  1 415 ? 11.28200  -6.62400  -48.99100 1.000 53.19000  ? 446 GLU C CG  1 
ATOM   10482 C  CD  . GLU C  1 415 ? 11.16500  -5.99800  -47.57500 1.000 61.39000  ? 446 GLU C CD  1 
ATOM   10483 O  OE1 . GLU C  1 415 ? 11.78200  -4.94200  -47.32300 1.000 58.53000  ? 446 GLU C OE1 1 
ATOM   10484 O  OE2 . GLU C  1 415 ? 10.47500  -6.57800  -46.70100 1.000 62.97000  ? 446 GLU C OE2 1 
ATOM   10485 N  N   . LYS C  1 416 ? 9.89800   -6.17800  -53.77300 1.000 61.25000  ? 447 LYS C N   1 
ATOM   10486 C  CA  . LYS C  1 416 ? 8.98700   -5.75700  -54.83000 1.000 58.01000  ? 447 LYS C CA  1 
ATOM   10487 C  C   . LYS C  1 416 ? 8.06400   -6.85500  -55.33100 1.000 61.89000  ? 447 LYS C C   1 
ATOM   10488 O  O   . LYS C  1 416 ? 6.96600   -6.55200  -55.81300 1.000 64.25000  ? 447 LYS C O   1 
ATOM   10489 C  CB  . LYS C  1 416 ? 9.77300   -5.21600  -56.02700 1.000 58.06000  ? 447 LYS C CB  1 
ATOM   10490 C  CG  . LYS C  1 416 ? 10.49300  -3.92200  -55.75600 1.000 59.71000  ? 447 LYS C CG  1 
ATOM   10491 C  CD  . LYS C  1 416 ? 11.39400  -3.56500  -56.92500 1.000 61.56000  ? 447 LYS C CD  1 
ATOM   10492 C  CE  . LYS C  1 416 ? 11.88000  -2.12800  -56.84400 1.000 66.12000  ? 447 LYS C CE  1 
ATOM   10493 N  NZ  . LYS C  1 416 ? 12.80800  -1.81200  -57.97600 1.000 83.55000  ? 447 LYS C NZ  1 
ATOM   10494 N  N   . LYS C  1 417 ? 8.47100   -8.11000  -55.24500 1.000 58.92000  ? 448 LYS C N   1 
ATOM   10495 C  CA  . LYS C  1 417 ? 7.76900   -9.20400  -55.90900 1.000 60.44000  ? 448 LYS C CA  1 
ATOM   10496 C  C   . LYS C  1 417 ? 7.15300   -10.12900 -54.86500 1.000 59.44000  ? 448 LYS C C   1 
ATOM   10497 O  O   . LYS C  1 417 ? 7.85200   -10.95300 -54.27200 1.000 60.08000  ? 448 LYS C O   1 
ATOM   10498 C  CB  . LYS C  1 417 ? 8.73800   -9.95300  -56.82300 1.000 57.86000  ? 448 LYS C CB  1 
ATOM   10499 C  CG  . LYS C  1 417 ? 8.07700   -10.77700 -57.93500 1.000 70.38000  ? 448 LYS C CG  1 
ATOM   10500 C  CD  . LYS C  1 417 ? 9.11300   -11.18700 -58.99300 1.000 78.22000  ? 448 LYS C CD  1 
ATOM   10501 C  CE  . LYS C  1 417 ? 9.12900   -12.69300 -59.24100 1.000 83.04000  ? 448 LYS C CE  1 
ATOM   10502 N  NZ  . LYS C  1 417 ? 7.95400   -13.15000 -60.05800 1.000 83.80000  ? 448 LYS C NZ  1 
ATOM   10503 N  N   . ASN C  1 418 ? 5.84000   -10.03100 -54.67300 1.000 57.51000  ? 449 ASN C N   1 
ATOM   10504 C  CA  . ASN C  1 418 ? 5.18000   -10.89400 -53.70300 1.000 59.39000  ? 449 ASN C CA  1 
ATOM   10505 C  C   . ASN C  1 418 ? 5.06900   -12.31300 -54.27300 1.000 63.10000  ? 449 ASN C C   1 
ATOM   10506 O  O   . ASN C  1 418 ? 4.47900   -12.51900 -55.33700 1.000 62.26000  ? 449 ASN C O   1 
ATOM   10507 C  CB  . ASN C  1 418 ? 3.80700   -10.33300 -53.34000 1.000 53.38000  ? 449 ASN C CB  1 
ATOM   10508 C  CG  . ASN C  1 418 ? 3.19700   -11.03000 -52.12700 1.000 62.30000  ? 449 ASN C CG  1 
ATOM   10509 O  OD1 . ASN C  1 418 ? 3.79700   -11.94300 -51.56200 1.000 61.27000  ? 449 ASN C OD1 1 
ATOM   10510 N  ND2 . ASN C  1 418 ? 2.01700   -10.58700 -51.70800 1.000 56.25000  ? 449 ASN C ND2 1 
ATOM   10511 N  N   . LEU C  1 419 ? 5.67300   -13.28400 -53.58300 1.000 63.15000  ? 450 LEU C N   1 
ATOM   10512 C  CA  . LEU C  1 419 ? 5.66200   -14.68700 -53.98900 1.000 61.22000  ? 450 LEU C CA  1 
ATOM   10513 C  C   . LEU C  1 419 ? 4.70800   -15.52800 -53.14900 1.000 64.91000  ? 450 LEU C C   1 
ATOM   10514 O  O   . LEU C  1 419 ? 4.82400   -16.75900 -53.14000 1.000 66.28000  ? 450 LEU C O   1 
ATOM   10515 C  CB  . LEU C  1 419 ? 7.07600   -15.27700 -53.91400 1.000 61.19000  ? 450 LEU C CB  1 
ATOM   10516 C  CG  . LEU C  1 419 ? 8.18700   -14.59700 -54.72800 1.000 57.15000  ? 450 LEU C CG  1 
ATOM   10517 C  CD1 . LEU C  1 419 ? 9.50600   -15.28400 -54.48600 1.000 64.52000  ? 450 LEU C CD1 1 
ATOM   10518 C  CD2 . LEU C  1 419 ? 7.87500   -14.50900 -56.23600 1.000 62.43000  ? 450 LEU C CD2 1 
ATOM   10519 N  N   . ALA C  1 420 ? 3.80000   -14.88400 -52.40700 1.000 66.42000  ? 451 ALA C N   1 
ATOM   10520 C  CA  . ALA C  1 420 ? 2.88100   -15.62200 -51.54300 1.000 68.33000  ? 451 ALA C CA  1 
ATOM   10521 C  C   . ALA C  1 420 ? 2.04500   -16.62400 -52.33200 1.000 69.53000  ? 451 ALA C C   1 
ATOM   10522 O  O   . ALA C  1 420 ? 1.79700   -17.74200 -51.86300 1.000 74.21000  ? 451 ALA C O   1 
ATOM   10523 C  CB  . ALA C  1 420 ? 1.97700   -14.64300 -50.78700 1.000 63.50000  ? 451 ALA C CB  1 
ATOM   10524 N  N   . GLY C  1 421 ? 1.62700   -16.26000 -53.54400 1.000 68.51000  ? 452 GLY C N   1 
ATOM   10525 C  CA  . GLY C  1 421 ? 0.84100   -17.18500 -54.34500 1.000 68.21000  ? 452 GLY C CA  1 
ATOM   10526 C  C   . GLY C  1 421 ? 1.66000   -18.35000 -54.86700 1.000 69.61000  ? 452 GLY C C   1 
ATOM   10527 O  O   . GLY C  1 421 ? 1.16200   -19.47400 -54.96700 1.000 71.83000  ? 452 GLY C O   1 
ATOM   10528 N  N   . ARG C  1 422 ? 2.93100   -18.10100 -55.19800 1.000 70.39000  ? 453 ARG C N   1 
ATOM   10529 C  CA  . ARG C  1 422 ? 3.76600   -19.13700 -55.79600 1.000 69.48000  ? 453 ARG C CA  1 
ATOM   10530 C  C   . ARG C  1 422 ? 4.16800   -20.20600 -54.78900 1.000 72.68000  ? 453 ARG C C   1 
ATOM   10531 O  O   . ARG C  1 422 ? 4.25400   -21.38700 -55.14000 1.000 74.51000  ? 453 ARG C O   1 
ATOM   10532 C  CB  . ARG C  1 422 ? 5.00700   -18.51500 -56.42900 1.000 73.37000  ? 453 ARG C CB  1 
ATOM   10533 C  CG  . ARG C  1 422 ? 5.80100   -19.49000 -57.28300 1.000 78.41000  ? 453 ARG C CG  1 
ATOM   10534 C  CD  . ARG C  1 422 ? 6.86800   -18.77800 -58.09900 1.000 85.34000  ? 453 ARG C CD  1 
ATOM   10535 N  NE  . ARG C  1 422 ? 6.29900   -17.65800 -58.84500 1.000 88.70000  ? 453 ARG C NE  1 
ATOM   10536 C  CZ  . ARG C  1 422 ? 7.01400   -16.70900 -59.43500 1.000 93.08000  ? 453 ARG C CZ  1 
ATOM   10537 N  NH1 . ARG C  1 422 ? 8.33700   -16.75500 -59.46000 1.000 91.53000  ? 453 ARG C NH1 1 
ATOM   10538 N  NH2 . ARG C  1 422 ? 6.38600   -15.69400 -60.02400 1.000 94.57000  ? 453 ARG C NH2 1 
ATOM   10539 N  N   . TYR C  1 423 ? 4.42200   -19.83100 -53.54200 1.000 75.22000  ? 454 TYR C N   1 
ATOM   10540 C  CA  . TYR C  1 423 ? 4.84500   -20.78800 -52.51700 1.000 67.66000  ? 454 TYR C CA  1 
ATOM   10541 C  C   . TYR C  1 423 ? 3.98300   -20.62700 -51.27300 1.000 73.50000  ? 454 TYR C C   1 
ATOM   10542 O  O   . TYR C  1 423 ? 4.48600   -20.29300 -50.19600 1.000 76.85000  ? 454 TYR C O   1 
ATOM   10543 C  CB  . TYR C  1 423 ? 6.31800   -20.60100 -52.17100 1.000 69.19000  ? 454 TYR C CB  1 
ATOM   10544 C  CG  . TYR C  1 423 ? 7.26700   -20.57700 -53.34600 1.000 76.60000  ? 454 TYR C CG  1 
ATOM   10545 C  CD1 . TYR C  1 423 ? 7.45100   -21.69800 -54.15900 1.000 75.42000  ? 454 TYR C CD1 1 
ATOM   10546 C  CD2 . TYR C  1 423 ? 7.98600   -19.43000 -53.64300 1.000 68.19000  ? 454 TYR C CD2 1 
ATOM   10547 C  CE1 . TYR C  1 423 ? 8.33100   -21.66900 -55.22900 1.000 64.51000  ? 454 TYR C CE1 1 
ATOM   10548 C  CE2 . TYR C  1 423 ? 8.86700   -19.39600 -54.70200 1.000 76.39000  ? 454 TYR C CE2 1 
ATOM   10549 C  CZ  . TYR C  1 423 ? 9.03400   -20.51200 -55.49200 1.000 76.26000  ? 454 TYR C CZ  1 
ATOM   10550 O  OH  . TYR C  1 423 ? 9.91400   -20.44300 -56.54100 1.000 85.93000  ? 454 TYR C OH  1 
ATOM   10551 N  N   . PRO C  1 424 ? 2.67600   -20.90000 -51.37400 1.000 77.91000  ? 455 PRO C N   1 
ATOM   10552 C  CA  . PRO C  1 424 ? 1.79600   -20.69000 -50.21000 1.000 73.17000  ? 455 PRO C CA  1 
ATOM   10553 C  C   . PRO C  1 424 ? 2.14000   -21.60500 -49.06300 1.000 76.94000  ? 455 PRO C C   1 
ATOM   10554 O  O   . PRO C  1 424 ? 1.75900   -21.33100 -47.91700 1.000 75.54000  ? 455 PRO C O   1 
ATOM   10555 C  CB  . PRO C  1 424 ? 0.40000   -20.99700 -50.76600 1.000 73.50000  ? 455 PRO C CB  1 
ATOM   10556 C  CG  . PRO C  1 424 ? 0.67300   -22.00000 -51.83800 1.000 75.47000  ? 455 PRO C CG  1 
ATOM   10557 C  CD  . PRO C  1 424 ? 1.96500   -21.56200 -52.48300 1.000 73.58000  ? 455 PRO C CD  1 
ATOM   10558 N  N   . ASP C  1 425 ? 2.84100   -22.69600 -49.35100 1.000 78.18000  ? 456 ASP C N   1 
ATOM   10559 C  CA  . ASP C  1 425 ? 3.33300   -23.56800 -48.29800 1.000 81.81000  ? 456 ASP C CA  1 
ATOM   10560 C  C   . ASP C  1 425 ? 4.31800   -22.82500 -47.39900 1.000 82.04000  ? 456 ASP C C   1 
ATOM   10561 O  O   . ASP C  1 425 ? 4.17700   -22.81300 -46.16900 1.000 80.17000  ? 456 ASP C O   1 
ATOM   10562 C  CB  . ASP C  1 425 ? 3.99900   -24.79500 -48.93800 1.000 81.32000  ? 456 ASP C CB  1 
ATOM   10563 C  CG  . ASP C  1 425 ? 4.92800   -24.42300 -50.13000 1.000 78.59000  ? 456 ASP C CG  1 
ATOM   10564 O  OD1 . ASP C  1 425 ? 4.54200   -23.58500 -50.97300 1.000 73.07000  ? 456 ASP C OD1 1 
ATOM   10565 O  OD2 . ASP C  1 425 ? 6.06200   -24.94500 -50.20900 1.000 77.90000  ? 456 ASP C OD2 1 
ATOM   10566 N  N   . ARG C  1 426 ? 5.31400   -22.18000 -48.00900 1.000 77.04000  ? 457 ARG C N   1 
ATOM   10567 C  CA  . ARG C  1 426 ? 6.34600   -21.48400 -47.25000 1.000 78.35000  ? 457 ARG C CA  1 
ATOM   10568 C  C   . ARG C  1 426 ? 5.76900   -20.36800 -46.38100 1.000 78.23000  ? 457 ARG C C   1 
ATOM   10569 O  O   . ARG C  1 426 ? 6.19100   -20.18700 -45.23200 1.000 78.66000  ? 457 ARG C O   1 
ATOM   10570 C  CB  . ARG C  1 426 ? 7.41500   -20.95000 -48.20000 1.000 72.86000  ? 457 ARG C CB  1 
ATOM   10571 C  CG  . ARG C  1 426 ? 8.57500   -20.35500 -47.46400 1.000 69.86000  ? 457 ARG C CG  1 
ATOM   10572 C  CD  . ARG C  1 426 ? 9.68000   -19.94800 -48.38700 1.000 74.28000  ? 457 ARG C CD  1 
ATOM   10573 N  NE  . ARG C  1 426 ? 10.90600  -20.64700 -48.02600 1.000 82.61000  ? 457 ARG C NE  1 
ATOM   10574 C  CZ  . ARG C  1 426 ? 11.34000  -21.75400 -48.61300 1.000 83.49000  ? 457 ARG C CZ  1 
ATOM   10575 N  NH1 . ARG C  1 426 ? 10.69800  -22.28800 -49.64400 1.000 79.36000  ? 457 ARG C NH1 1 
ATOM   10576 N  NH2 . ARG C  1 426 ? 12.43500  -22.35000 -48.14200 1.000 75.22000  ? 457 ARG C NH2 1 
ATOM   10577 N  N   . LEU C  1 427 ? 4.82200   -19.59600 -46.91900 1.000 76.87000  ? 458 LEU C N   1 
ATOM   10578 C  CA  . LEU C  1 427 ? 4.26400   -18.46900 -46.17600 1.000 79.43000  ? 458 LEU C CA  1 
ATOM   10579 C  C   . LEU C  1 427 ? 3.73200   -18.89700 -44.81200 1.000 79.20000  ? 458 LEU C C   1 
ATOM   10580 O  O   . LEU C  1 427 ? 4.12000   -18.33900 -43.78200 1.000 76.33000  ? 458 LEU C O   1 
ATOM   10581 C  CB  . LEU C  1 427 ? 3.15200   -17.80900 -46.99500 1.000 69.37000  ? 458 LEU C CB  1 
ATOM   10582 C  CG  . LEU C  1 427 ? 2.29000   -16.76400 -46.28400 1.000 68.88000  ? 458 LEU C CG  1 
ATOM   10583 C  CD1 . LEU C  1 427 ? 3.13200   -15.55500 -45.95200 1.000 71.90000  ? 458 LEU C CD1 1 
ATOM   10584 C  CD2 . LEU C  1 427 ? 1.10700   -16.35000 -47.14500 1.000 64.88000  ? 458 LEU C CD2 1 
ATOM   10585 N  N   . LYS C  1 428 ? 2.85900   -19.90600 -44.78200 1.000 77.82000  ? 459 LYS C N   1 
ATOM   10586 C  CA  . LYS C  1 428 ? 2.22800   -20.27800 -43.51900 1.000 74.99000  ? 459 LYS C CA  1 
ATOM   10587 C  C   . LYS C  1 428 ? 3.18600   -20.98400 -42.55900 1.000 72.50000  ? 459 LYS C C   1 
ATOM   10588 O  O   . LYS C  1 428 ? 2.97500   -20.93500 -41.34500 1.000 73.01000  ? 459 LYS C O   1 
ATOM   10589 C  CB  . LYS C  1 428 ? 0.97000   -21.10100 -43.77400 1.000 72.75000  ? 459 LYS C CB  1 
ATOM   10590 C  CG  . LYS C  1 428 ? -0.15100  -20.26300 -44.35900 1.000 72.45000  ? 459 LYS C CG  1 
ATOM   10591 C  CD  . LYS C  1 428 ? -1.22600  -21.11200 -44.99600 1.000 80.28000  ? 459 LYS C CD  1 
ATOM   10592 C  CE  . LYS C  1 428 ? -2.41300  -20.25700 -45.37400 1.000 78.75000  ? 459 LYS C CE  1 
ATOM   10593 N  NZ  . LYS C  1 428 ? -3.03100  -19.65900 -44.15700 1.000 82.83000  ? 459 LYS C NZ  1 
ATOM   10594 N  N   . GLU C  1 429 ? 4.21900   -21.66400 -43.06100 1.000 76.14000  ? 460 GLU C N   1 
ATOM   10595 C  CA  . GLU C  1 429 ? 5.20000   -22.24200 -42.14300 1.000 75.13000  ? 460 GLU C CA  1 
ATOM   10596 C  C   . GLU C  1 429 ? 5.97400   -21.14400 -41.42500 1.000 76.08000  ? 460 GLU C C   1 
ATOM   10597 O  O   . GLU C  1 429 ? 6.26400   -21.25900 -40.22800 1.000 76.22000  ? 460 GLU C O   1 
ATOM   10598 C  CB  . GLU C  1 429 ? 6.16100   -23.17000 -42.89200 1.000 74.21000  ? 460 GLU C CB  1 
ATOM   10599 N  N   . MET C  1 430 ? 6.32000   -20.07500 -42.14900 1.000 75.90000  ? 461 MET C N   1 
ATOM   10600 C  CA  . MET C  1 430 ? 6.99600   -18.93300 -41.54200 1.000 75.41000  ? 461 MET C CA  1 
ATOM   10601 C  C   . MET C  1 430 ? 6.07300   -18.15600 -40.61200 1.000 73.01000  ? 461 MET C C   1 
ATOM   10602 O  O   . MET C  1 430 ? 6.52000   -17.63100 -39.58700 1.000 73.58000  ? 461 MET C O   1 
ATOM   10603 C  CB  . MET C  1 430 ? 7.56900   -18.02500 -42.62600 1.000 66.50000  ? 461 MET C CB  1 
ATOM   10604 C  CG  . MET C  1 430 ? 8.76900   -18.62400 -43.28900 1.000 64.89000  ? 461 MET C CG  1 
ATOM   10605 S  SD  . MET C  1 430 ? 9.43100   -17.55300 -44.56200 1.000 72.94000  ? 461 MET C SD  1 
ATOM   10606 C  CE  . MET C  1 430 ? 10.93600  -17.00300 -43.73300 1.000 69.02000  ? 461 MET C CE  1 
ATOM   10607 N  N   . ILE C  1 431 ? 4.79200   -18.05000 -40.95300 1.000 66.29000  ? 462 ILE C N   1 
ATOM   10608 C  CA  . ILE C  1 431 ? 3.85900   -17.42300 -40.02700 1.000 67.34000  ? 462 ILE C CA  1 
ATOM   10609 C  C   . ILE C  1 431 ? 3.69300   -18.26300 -38.76500 1.000 74.61000  ? 462 ILE C C   1 
ATOM   10610 O  O   . ILE C  1 431 ? 3.49700   -17.72000 -37.66900 1.000 76.00000  ? 462 ILE C O   1 
ATOM   10611 C  CB  . ILE C  1 431 ? 2.52500   -17.15600 -40.74200 1.000 71.93000  ? 462 ILE C CB  1 
ATOM   10612 C  CG1 . ILE C  1 431 ? 2.71000   -15.97800 -41.70400 1.000 74.38000  ? 462 ILE C CG1 1 
ATOM   10613 C  CG2 . ILE C  1 431 ? 1.40200   -16.89400 -39.75100 1.000 66.28000  ? 462 ILE C CG2 1 
ATOM   10614 C  CD1 . ILE C  1 431 ? 1.48600   -15.60300 -42.51000 1.000 73.14000  ? 462 ILE C CD1 1 
ATOM   10615 N  N   . ALA C  1 432 ? 3.76900   -19.59200 -38.88900 1.000 71.57000  ? 463 ALA C N   1 
ATOM   10616 C  CA  . ALA C  1 432 ? 3.60800   -20.46100 -37.72900 1.000 74.05000  ? 463 ALA C CA  1 
ATOM   10617 C  C   . ALA C  1 432 ? 4.67900   -20.18600 -36.70100 1.000 79.88000  ? 463 ALA C C   1 
ATOM   10618 O  O   . ALA C  1 432 ? 4.39800   -20.01400 -35.50700 1.000 80.59000  ? 463 ALA C O   1 
ATOM   10619 C  CB  . ALA C  1 432 ? 3.71000   -21.92300 -38.15400 1.000 80.06000  ? 463 ALA C CB  1 
ATOM   10620 N  N   . LYS C  1 433 ? 5.93000   -20.17900 -37.15600 1.000 77.12000  ? 464 LYS C N   1 
ATOM   10621 C  CA  . LYS C  1 433 ? 7.04400   -19.93300 -36.25700 1.000 75.37000  ? 464 LYS C CA  1 
ATOM   10622 C  C   . LYS C  1 433 ? 7.00100   -18.54200 -35.64500 1.000 82.30000  ? 464 LYS C C   1 
ATOM   10623 O  O   . LYS C  1 433 ? 7.21900   -18.39700 -34.43900 1.000 82.45000  ? 464 LYS C O   1 
ATOM   10624 C  CB  . LYS C  1 433 ? 8.37300   -20.15400 -36.97100 1.000 76.49000  ? 464 LYS C CB  1 
ATOM   10625 C  CG  . LYS C  1 433 ? 9.59500   -19.87100 -36.05700 1.000 90.35000  ? 464 LYS C CG  1 
ATOM   10626 C  CD  . LYS C  1 433 ? 10.88500  -20.54800 -36.59200 1.000 90.82000  ? 464 LYS C CD  1 
ATOM   10627 C  CE  . LYS C  1 433 ? 12.10100  -20.27500 -35.64800 1.000 89.49000  ? 464 LYS C CE  1 
ATOM   10628 N  NZ  . LYS C  1 433 ? 11.94400  -20.65400 -34.21500 1.000 83.29000  ? 464 LYS C NZ  1 
ATOM   10629 N  N   . THR C  1 434 ? 6.73100   -17.50800 -36.44800 1.000 78.26000  ? 465 THR C N   1 
ATOM   10630 C  CA  . THR C  1 434 ? 6.66500   -16.14600 -35.91700 1.000 78.70000  ? 465 THR C CA  1 
ATOM   10631 C  C   . THR C  1 434 ? 5.55700   -16.00000 -34.87900 1.000 79.76000  ? 465 THR C C   1 
ATOM   10632 O  O   . THR C  1 434 ? 5.71500   -15.28800 -33.87600 1.000 76.65000  ? 465 THR C O   1 
ATOM   10633 C  CB  . THR C  1 434 ? 6.45800   -15.15400 -37.05700 1.000 74.23000  ? 465 THR C CB  1 
ATOM   10634 O  OG1 . THR C  1 434 ? 7.53200   -15.29300 -37.99500 1.000 77.87000  ? 465 THR C OG1 1 
ATOM   10635 C  CG2 . THR C  1 434 ? 6.41300   -13.73900 -36.53300 1.000 74.13000  ? 465 THR C CG2 1 
ATOM   10636 N  N   . GLN C  1 435 ? 4.41600   -16.64000 -35.11500 1.000 77.25000  ? 466 GLN C N   1 
ATOM   10637 C  CA  . GLN C  1 435 ? 3.35000   -16.58600 -34.12400 1.000 82.14000  ? 466 GLN C CA  1 
ATOM   10638 C  C   . GLN C  1 435 ? 3.79500   -17.23900 -32.81700 1.000 78.32000  ? 466 GLN C C   1 
ATOM   10639 O  O   . GLN C  1 435 ? 3.49100   -16.73800 -31.72800 1.000 79.58000  ? 466 GLN C O   1 
ATOM   10640 C  CB  . GLN C  1 435 ? 2.08600   -17.23300 -34.67900 1.000 76.81000  ? 466 GLN C CB  1 
ATOM   10641 C  CG  . GLN C  1 435 ? 0.89100   -17.04800 -33.79000 1.000 77.90000  ? 466 GLN C CG  1 
ATOM   10642 C  CD  . GLN C  1 435 ? -0.40000  -17.32600 -34.51500 1.000 83.66000  ? 466 GLN C CD  1 
ATOM   10643 O  OE1 . GLN C  1 435 ? -0.48400  -18.25900 -35.31600 1.000 81.55000  ? 466 GLN C OE1 1 
ATOM   10644 N  NE2 . GLN C  1 435 ? -1.41300  -16.50900 -34.25400 1.000 83.27000  ? 466 GLN C NE2 1 
ATOM   10645 N  N   . GLU C  1 436 ? 4.51500   -18.36100 -32.91000 1.000 76.44000  ? 467 GLU C N   1 
ATOM   10646 C  CA  . GLU C  1 436 ? 5.07600   -18.99600 -31.71900 1.000 80.41000  ? 467 GLU C CA  1 
ATOM   10647 C  C   . GLU C  1 436 ? 5.97500   -18.02900 -30.96100 1.000 80.75000  ? 467 GLU C C   1 
ATOM   10648 O  O   . GLU C  1 436 ? 5.94000   -17.97400 -29.72600 1.000 83.97000  ? 467 GLU C O   1 
ATOM   10649 C  CB  . GLU C  1 436 ? 5.84700   -20.25800 -32.12700 1.000 80.17000  ? 467 GLU C CB  1 
ATOM   10650 C  CG  . GLU C  1 436 ? 6.39700   -21.12400 -30.99500 1.000 85.28000  ? 467 GLU C CG  1 
ATOM   10651 C  CD  . GLU C  1 436 ? 5.34600   -21.57600 -29.99300 1.000 96.76000  ? 467 GLU C CD  1 
ATOM   10652 O  OE1 . GLU C  1 436 ? 4.20500   -21.89000 -30.40400 1.000 92.23000  ? 467 GLU C OE1 1 
ATOM   10653 O  OE2 . GLU C  1 436 ? 5.67400   -21.62500 -28.78500 1.000 102.14000 ? 467 GLU C OE2 1 
ATOM   10654 N  N   . TRP C  1 437 ? 6.78200   -17.25600 -31.69100 1.000 77.30000  ? 468 TRP C N   1 
ATOM   10655 C  CA  . TRP C  1 437 ? 7.62300   -16.22800 -31.08300 1.000 77.08000  ? 468 TRP C CA  1 
ATOM   10656 C  C   . TRP C  1 437 ? 6.79700   -15.24500 -30.25800 1.000 79.54000  ? 468 TRP C C   1 
ATOM   10657 O  O   . TRP C  1 437 ? 7.14900   -14.93300 -29.11400 1.000 78.68000  ? 468 TRP C O   1 
ATOM   10658 C  CB  . TRP C  1 437 ? 8.40400   -15.50900 -32.18500 1.000 77.10000  ? 468 TRP C CB  1 
ATOM   10659 C  CG  . TRP C  1 437 ? 9.21600   -14.32500 -31.76000 1.000 77.41000  ? 468 TRP C CG  1 
ATOM   10660 C  CD1 . TRP C  1 437 ? 10.25700  -14.31200 -30.87700 1.000 74.42000  ? 468 TRP C CD1 1 
ATOM   10661 C  CD2 . TRP C  1 437 ? 9.08700   -12.98400 -32.24600 1.000 74.08000  ? 468 TRP C CD2 1 
ATOM   10662 N  NE1 . TRP C  1 437 ? 10.77000  -13.04300 -30.76600 1.000 72.66000  ? 468 TRP C NE1 1 
ATOM   10663 C  CE2 . TRP C  1 437 ? 10.07200  -12.20700 -31.59600 1.000 72.26000  ? 468 TRP C CE2 1 
ATOM   10664 C  CE3 . TRP C  1 437 ? 8.22900   -12.36400 -33.15500 1.000 70.97000  ? 468 TRP C CE3 1 
ATOM   10665 C  CZ2 . TRP C  1 437 ? 10.22100  -10.84400 -31.82600 1.000 67.40000  ? 468 TRP C CZ2 1 
ATOM   10666 C  CZ3 . TRP C  1 437 ? 8.37800   -11.01200 -33.38700 1.000 71.13000  ? 468 TRP C CZ3 1 
ATOM   10667 C  CH2 . TRP C  1 437 ? 9.36500   -10.26300 -32.72200 1.000 72.38000  ? 468 TRP C CH2 1 
ATOM   10668 N  N   . THR C  1 438 ? 5.68000   -14.75600 -30.81500 1.000 80.89000  ? 469 THR C N   1 
ATOM   10669 C  CA  . THR C  1 438 ? 4.84500   -13.80100 -30.08800 1.000 76.12000  ? 469 THR C CA  1 
ATOM   10670 C  C   . THR C  1 438 ? 4.13200   -14.43900 -28.90600 1.000 79.40000  ? 469 THR C C   1 
ATOM   10671 O  O   . THR C  1 438 ? 3.61100   -13.70900 -28.05700 1.000 81.91000  ? 469 THR C O   1 
ATOM   10672 C  CB  . THR C  1 438 ? 3.80000   -13.14700 -31.00400 1.000 75.60000  ? 469 THR C CB  1 
ATOM   10673 O  OG1 . THR C  1 438 ? 2.82100   -14.11600 -31.39300 1.000 73.70000  ? 469 THR C OG1 1 
ATOM   10674 C  CG2 . THR C  1 438 ? 4.44900   -12.55700 -32.24200 1.000 74.09000  ? 469 THR C CG2 1 
ATOM   10675 N  N   . LYS C  1 439 ? 4.08100   -15.77300 -28.83500 1.000 79.77000  ? 470 LYS C N   1 
ATOM   10676 C  CA  . LYS C  1 439 ? 3.46900   -16.41600 -27.68200 1.000 82.11000  ? 470 LYS C CA  1 
ATOM   10677 C  C   . LYS C  1 439 ? 4.27500   -16.16700 -26.41300 1.000 85.32000  ? 470 LYS C C   1 
ATOM   10678 O  O   . LYS C  1 439 ? 3.73600   -16.29600 -25.30800 1.000 85.18000  ? 470 LYS C O   1 
ATOM   10679 C  CB  . LYS C  1 439 ? 3.31800   -17.91900 -27.93700 1.000 84.43000  ? 470 LYS C CB  1 
ATOM   10680 N  N   . SER C  1 440 ? 5.54200   -15.79300 -26.55200 1.000 80.71000  ? 471 SER C N   1 
ATOM   10681 C  CA  . SER C  1 440 ? 6.41400   -15.50000 -25.42900 1.000 78.33000  ? 471 SER C CA  1 
ATOM   10682 C  C   . SER C  1 440 ? 6.43000   -14.01600 -25.04900 1.000 78.98000  ? 471 SER C C   1 
ATOM   10683 O  O   . SER C  1 440 ? 7.15800   -13.63600 -24.12700 1.000 84.05000  ? 471 SER C O   1 
ATOM   10684 C  CB  . SER C  1 440 ? 7.83400   -16.00400 -25.74200 1.000 76.48000  ? 471 SER C CB  1 
ATOM   10685 O  OG  . SER C  1 440 ? 8.45400   -15.26500 -26.78500 1.000 76.56000  ? 471 SER C OG  1 
ATOM   10686 N  N   . PHE C  1 441 ? 5.64800   -13.17100 -25.71500 1.000 80.94000  ? 472 PHE C N   1 
ATOM   10687 C  CA  . PHE C  1 441 ? 5.73300   -11.73600 -25.47400 1.000 77.94000  ? 472 PHE C CA  1 
ATOM   10688 C  C   . PHE C  1 441 ? 5.16600   -11.36400 -24.10100 1.000 81.43000  ? 472 PHE C C   1 
ATOM   10689 O  O   . PHE C  1 441 ? 4.36700   -12.09500 -23.50900 1.000 83.02000  ? 472 PHE C O   1 
ATOM   10690 C  CB  . PHE C  1 441 ? 5.00200   -10.95600 -26.57500 1.000 73.92000  ? 472 PHE C CB  1 
ATOM   10691 C  CG  . PHE C  1 441 ? 5.75000   -10.90900 -27.88400 1.000 73.25000  ? 472 PHE C CG  1 
ATOM   10692 C  CD1 . PHE C  1 441 ? 6.92000   -11.63500 -28.06100 1.000 70.40000  ? 472 PHE C CD1 1 
ATOM   10693 C  CD2 . PHE C  1 441 ? 5.32000   -10.08200 -28.91000 1.000 75.68000  ? 472 PHE C CD2 1 
ATOM   10694 C  CE1 . PHE C  1 441 ? 7.62100   -11.57900 -29.24900 1.000 66.70000  ? 472 PHE C CE1 1 
ATOM   10695 C  CE2 . PHE C  1 441 ? 6.01600   -10.01500 -30.10300 1.000 69.14000  ? 472 PHE C CE2 1 
ATOM   10696 C  CZ  . PHE C  1 441 ? 7.17100   -10.76500 -30.26800 1.000 73.02000  ? 472 PHE C CZ  1 
ATOM   10697 N  N   . VAL C  1 442 ? 5.59800   -10.20800 -23.59800 1.000 80.63000  ? 473 VAL C N   1 
ATOM   10698 C  CA  . VAL C  1 442 ? 5.06300   -9.63100  -22.37000 1.000 81.11000  ? 473 VAL C CA  1 
ATOM   10699 C  C   . VAL C  1 442 ? 4.26000   -8.37700  -22.70400 1.000 72.10000  ? 473 VAL C C   1 
ATOM   10700 O  O   . VAL C  1 442 ? 4.34300   -7.82500  -23.80100 1.000 75.48000  ? 473 VAL C O   1 
ATOM   10701 C  CB  . VAL C  1 442 ? 6.17000   -9.29000  -21.34700 1.000 77.51000  ? 473 VAL C CB  1 
ATOM   10702 C  CG1 . VAL C  1 442 ? 7.07500   -10.48800 -21.08200 1.000 79.75000  ? 473 VAL C CG1 1 
ATOM   10703 C  CG2 . VAL C  1 442 ? 6.96900   -8.08300  -21.81300 1.000 74.97000  ? 473 VAL C CG2 1 
ATOM   10704 N  N   . LYS C  1 443 ? 3.51000   -7.90400  -21.71600 1.000 73.63000  ? 474 LYS C N   1 
ATOM   10705 C  CA  . LYS C  1 443 ? 2.81100   -6.63800  -21.85200 1.000 73.16000  ? 474 LYS C CA  1 
ATOM   10706 C  C   . LYS C  1 443 ? 3.81200   -5.48800  -21.78800 1.000 72.47000  ? 474 LYS C C   1 
ATOM   10707 O  O   . LYS C  1 443 ? 4.80400   -5.55700  -21.05800 1.000 76.60000  ? 474 LYS C O   1 
ATOM   10708 C  CB  . LYS C  1 443 ? 1.76200   -6.47600  -20.75300 1.000 66.88000  ? 474 LYS C CB  1 
ATOM   10709 N  N   . PRO C  1 444 ? 3.58300   -4.42100  -22.54300 1.000 74.56000  ? 475 PRO C N   1 
ATOM   10710 C  CA  . PRO C  1 444 ? 4.45000   -3.24900  -22.41700 1.000 75.23000  ? 475 PRO C CA  1 
ATOM   10711 C  C   . PRO C  1 444 ? 4.38900   -2.67900  -21.00700 1.000 77.30000  ? 475 PRO C C   1 
ATOM   10712 O  O   . PRO C  1 444 ? 3.31600   -2.58200  -20.40600 1.000 76.01000  ? 475 PRO C O   1 
ATOM   10713 C  CB  . PRO C  1 444 ? 3.86900   -2.26900  -23.44300 1.000 71.35000  ? 475 PRO C CB  1 
ATOM   10714 C  CG  . PRO C  1 444 ? 3.10900   -3.11900  -24.38800 1.000 73.48000  ? 475 PRO C CG  1 
ATOM   10715 C  CD  . PRO C  1 444 ? 2.52100   -4.19500  -23.53300 1.000 75.09000  ? 475 PRO C CD  1 
ATOM   10716 N  N   . LEU C  1 445 ? 5.56600   -2.33500  -20.46900 1.000 77.31000  ? 476 LEU C N   1 
ATOM   10717 C  CA  . LEU C  1 445 ? 5.64000   -1.61800  -19.19800 1.000 75.44000  ? 476 LEU C CA  1 
ATOM   10718 C  C   . LEU C  1 445 ? 5.12400   -0.19400  -19.32200 1.000 74.77000  ? 476 LEU C C   1 
ATOM   10719 O  O   . LEU C  1 445 ? 4.69800   0.38600   -18.31900 1.000 75.51000  ? 476 LEU C O   1 
ATOM   10720 C  CB  . LEU C  1 445 ? 7.07400   -1.59300  -18.67100 1.000 73.24000  ? 476 LEU C CB  1 
ATOM   10721 C  CG  . LEU C  1 445 ? 7.71300   -2.92300  -18.29200 1.000 69.43000  ? 476 LEU C CG  1 
ATOM   10722 C  CD1 . LEU C  1 445 ? 9.16700   -2.69100  -17.97700 1.000 76.06000  ? 476 LEU C CD1 1 
ATOM   10723 C  CD2 . LEU C  1 445 ? 7.00700   -3.49700  -17.07700 1.000 71.96000  ? 476 LEU C CD2 1 
ATOM   10724 N  N   . TRP C  1 446 ? 5.17100   0.38200   -20.52000 1.000 76.65000  ? 477 TRP C N   1 
ATOM   10725 C  CA  . TRP C  1 446 ? 4.55300   1.67000   -20.79600 1.000 74.66000  ? 477 TRP C CA  1 
ATOM   10726 C  C   . TRP C  1 446 ? 4.24100   1.70700   -22.28500 1.000 78.77000  ? 477 TRP C C   1 
ATOM   10727 O  O   . TRP C  1 446 ? 4.76100   0.89900   -23.06300 1.000 78.02000  ? 477 TRP C O   1 
ATOM   10728 C  CB  . TRP C  1 446 ? 5.46300   2.83500   -20.41800 1.000 72.23000  ? 477 TRP C CB  1 
ATOM   10729 C  CG  . TRP C  1 446 ? 6.72600   2.85300   -21.18900 1.000 70.14000  ? 477 TRP C CG  1 
ATOM   10730 C  CD1 . TRP C  1 446 ? 6.93200   3.43300   -22.40700 1.000 73.32000  ? 477 TRP C CD1 1 
ATOM   10731 C  CD2 . TRP C  1 446 ? 7.96200   2.24600   -20.81900 1.000 71.05000  ? 477 TRP C CD2 1 
ATOM   10732 N  NE1 . TRP C  1 446 ? 8.22900   3.23900   -22.80900 1.000 73.42000  ? 477 TRP C NE1 1 
ATOM   10733 C  CE2 . TRP C  1 446 ? 8.88000   2.50600   -21.85200 1.000 70.17000  ? 477 TRP C CE2 1 
ATOM   10734 C  CE3 . TRP C  1 446 ? 8.38600   1.51400   -19.71000 1.000 75.24000  ? 477 TRP C CE3 1 
ATOM   10735 C  CZ2 . TRP C  1 446 ? 10.19300  2.06900   -21.80300 1.000 71.82000  ? 477 TRP C CZ2 1 
ATOM   10736 C  CZ3 . TRP C  1 446 ? 9.69500   1.07800   -19.66600 1.000 72.14000  ? 477 TRP C CZ3 1 
ATOM   10737 C  CH2 . TRP C  1 446 ? 10.58200  1.35600   -20.70300 1.000 72.23000  ? 477 TRP C CH2 1 
ATOM   10738 N  N   . VAL C  1 447 ? 3.38000   2.64700   -22.67500 1.000 73.32000  ? 478 VAL C N   1 
ATOM   10739 C  CA  . VAL C  1 447 ? 3.09700   2.86200   -24.09100 1.000 74.95000  ? 478 VAL C CA  1 
ATOM   10740 C  C   . VAL C  1 447 ? 3.50700   4.28800   -24.42100 1.000 73.62000  ? 478 VAL C C   1 
ATOM   10741 O  O   . VAL C  1 447 ? 4.11200   4.96900   -23.59100 1.000 79.04000  ? 478 VAL C O   1 
ATOM   10742 C  CB  . VAL C  1 447 ? 1.61700   2.60500   -24.43200 1.000 75.41000  ? 478 VAL C CB  1 
ATOM   10743 C  CG1 . VAL C  1 447 ? 1.23000   1.17000   -24.09900 1.000 73.24000  ? 478 VAL C CG1 1 
ATOM   10744 C  CG2 . VAL C  1 447 ? 0.70900   3.60200   -23.72000 1.000 79.51000  ? 478 VAL C CG2 1 
ATOM   10745 N  N   . TYR C  1 448 ? 3.18800   4.75200   -25.62300 1.000 69.86000  ? 479 TYR C N   1 
ATOM   10746 C  CA  . TYR C  1 448 ? 3.64400   6.05300   -26.09000 1.000 67.57000  ? 479 TYR C CA  1 
ATOM   10747 C  C   . TYR C  1 448 ? 2.53300   7.08600   -26.18900 1.000 73.77000  ? 479 TYR C C   1 
ATOM   10748 O  O   . TYR C  1 448 ? 2.77700   8.25500   -25.90400 1.000 76.50000  ? 479 TYR C O   1 
ATOM   10749 C  CB  . TYR C  1 448 ? 4.32600   5.91900   -27.45600 1.000 65.58000  ? 479 TYR C CB  1 
ATOM   10750 C  CG  . TYR C  1 448 ? 5.05400   7.16100   -27.94600 1.000 60.94000  ? 479 TYR C CG  1 
ATOM   10751 C  CD1 . TYR C  1 448 ? 6.34900   7.46500   -27.52300 1.000 65.33000  ? 479 TYR C CD1 1 
ATOM   10752 C  CD2 . TYR C  1 448 ? 4.44100   8.03500   -28.82900 1.000 57.93000  ? 479 TYR C CD2 1 
ATOM   10753 C  CE1 . TYR C  1 448 ? 7.01700   8.61500   -27.99300 1.000 59.15000  ? 479 TYR C CE1 1 
ATOM   10754 C  CE2 . TYR C  1 448 ? 5.09100   9.17100   -29.29500 1.000 55.50000  ? 479 TYR C CE2 1 
ATOM   10755 C  CZ  . TYR C  1 448 ? 6.36900   9.46600   -28.87600 1.000 59.15000  ? 479 TYR C CZ  1 
ATOM   10756 O  OH  . TYR C  1 448 ? 6.98100   10.61300  -29.36100 1.000 56.48000  ? 479 TYR C OH  1 
ATOM   10757 N  N   . SER C  1 449 ? 1.32400   6.70800   -26.61200 1.000 78.64000  ? 480 SER C N   1 
ATOM   10758 C  CA  . SER C  1 449 ? 0.23500   7.66200   -26.79400 1.000 74.61000  ? 480 SER C CA  1 
ATOM   10759 C  C   . SER C  1 449 ? -1.00900  7.22700   -26.02000 1.000 76.83000  ? 480 SER C C   1 
ATOM   10760 O  O   . SER C  1 449 ? -1.16900  6.05600   -25.65500 1.000 76.55000  ? 480 SER C O   1 
ATOM   10761 C  CB  . SER C  1 449 ? -0.09500  7.83800   -28.28100 1.000 73.17000  ? 480 SER C CB  1 
ATOM   10762 O  OG  . SER C  1 449 ? -0.67500  6.65900   -28.80900 1.000 76.14000  ? 480 SER C OG  1 
ATOM   10763 N  N   . VAL C  1 450 ? -1.89600  8.19900   -25.77500 1.000 80.02000  ? 481 VAL C N   1 
ATOM   10764 C  CA  . VAL C  1 450 ? -3.18700  7.90800   -25.14700 1.000 80.83000  ? 481 VAL C CA  1 
ATOM   10765 C  C   . VAL C  1 450 ? -3.92700  6.83500   -25.92800 1.000 77.19000  ? 481 VAL C C   1 
ATOM   10766 O  O   . VAL C  1 450 ? -4.47800  5.89000   -25.34600 1.000 75.56000  ? 481 VAL C O   1 
ATOM   10767 C  CB  . VAL C  1 450 ? -4.03400  9.19100   -25.01800 1.000 80.49000  ? 481 VAL C CB  1 
ATOM   10768 C  CG1 . VAL C  1 450 ? -4.15400  9.61000   -23.55700 1.000 78.01000  ? 481 VAL C CG1 1 
ATOM   10769 C  CG2 . VAL C  1 450 ? -3.43800  10.31300  -25.84800 1.000 76.03000  ? 481 VAL C CG2 1 
ATOM   10770 N  N   . LYS C  1 451 ? -3.93300  6.95700   -27.26100 1.000 76.74000  ? 482 LYS C N   1 
ATOM   10771 C  CA  . LYS C  1 451 ? -4.53800  5.92800   -28.10400 1.000 76.15000  ? 482 LYS C CA  1 
ATOM   10772 C  C   . LYS C  1 451 ? -4.00000  4.54600   -27.75900 1.000 77.82000  ? 482 LYS C C   1 
ATOM   10773 O  O   . LYS C  1 451 ? -4.77900  3.60200   -27.58200 1.000 78.16000  ? 482 LYS C O   1 
ATOM   10774 C  CB  . LYS C  1 451 ? -4.28700  6.23600   -29.58300 1.000 72.74000  ? 482 LYS C CB  1 
ATOM   10775 C  CG  . LYS C  1 451 ? -4.95700  5.25800   -30.55000 1.000 76.06000  ? 482 LYS C CG  1 
ATOM   10776 C  CD  . LYS C  1 451 ? -6.25800  5.83300   -31.09100 1.000 78.50000  ? 482 LYS C CD  1 
ATOM   10777 C  CE  . LYS C  1 451 ? -7.37100  4.78000   -31.17100 1.000 75.13000  ? 482 LYS C CE  1 
ATOM   10778 N  NZ  . LYS C  1 451 ? -8.72900  5.42400   -31.10000 1.000 72.92000  ? 482 LYS C NZ  1 
ATOM   10779 N  N   . ASP C  1 452 ? -2.67700  4.42600   -27.57800 1.000 71.25000  ? 483 ASP C N   1 
ATOM   10780 C  CA  . ASP C  1 452 ? -2.09000  3.13800   -27.21500 1.000 74.98000  ? 483 ASP C CA  1 
ATOM   10781 C  C   . ASP C  1 452 ? -2.72500  2.58800   -25.94100 1.000 80.02000  ? 483 ASP C C   1 
ATOM   10782 O  O   . ASP C  1 452 ? -3.03500  1.39300   -25.85100 1.000 75.98000  ? 483 ASP C O   1 
ATOM   10783 C  CB  . ASP C  1 452 ? -0.57300  3.25700   -27.02700 1.000 76.47000  ? 483 ASP C CB  1 
ATOM   10784 C  CG  . ASP C  1 452 ? 0.17800   3.55500   -28.31400 1.000 76.28000  ? 483 ASP C CG  1 
ATOM   10785 O  OD1 . ASP C  1 452 ? -0.40000  3.40500   -29.40900 1.000 82.21000  ? 483 ASP C OD1 1 
ATOM   10786 O  OD2 . ASP C  1 452 ? 1.38300   3.88800   -28.22600 1.000 74.45000  ? 483 ASP C OD2 1 
ATOM   10787 N  N   . LYS C  1 453 ? -2.88900  3.44300   -24.92300 1.000 81.63000  ? 484 LYS C N   1 
ATOM   10788 C  CA  . LYS C  1 453 ? -3.43200  2.97000   -23.65200 1.000 82.26000  ? 484 LYS C CA  1 
ATOM   10789 C  C   . LYS C  1 453 ? -4.86500  2.48100   -23.82200 1.000 80.73000  ? 484 LYS C C   1 
ATOM   10790 O  O   . LYS C  1 453 ? -5.23100  1.41200   -23.31700 1.000 78.92000  ? 484 LYS C O   1 
ATOM   10791 C  CB  . LYS C  1 453 ? -3.35300  4.07300   -22.59200 1.000 80.94000  ? 484 LYS C CB  1 
ATOM   10792 N  N   . GLU C  1 454 ? -5.68800  3.24100   -24.54700 1.000 77.78000  ? 485 GLU C N   1 
ATOM   10793 C  CA  . GLU C  1 454 ? -7.06100  2.80700   -24.77900 1.000 79.66000  ? 485 GLU C CA  1 
ATOM   10794 C  C   . GLU C  1 454 ? -7.08300  1.45800   -25.48100 1.000 76.56000  ? 485 GLU C C   1 
ATOM   10795 O  O   . GLU C  1 454 ? -7.78800  0.53400   -25.06100 1.000 74.13000  ? 485 GLU C O   1 
ATOM   10796 C  CB  . GLU C  1 454 ? -7.80800  3.84800   -25.60700 1.000 72.58000  ? 485 GLU C CB  1 
ATOM   10797 C  CG  . GLU C  1 454 ? -7.71400  5.25500   -25.07100 1.000 75.18000  ? 485 GLU C CG  1 
ATOM   10798 C  CD  . GLU C  1 454 ? -8.53700  6.22400   -25.89700 1.000 84.56000  ? 485 GLU C CD  1 
ATOM   10799 O  OE1 . GLU C  1 454 ? -8.86500  5.86800   -27.05100 1.000 87.54000  ? 485 GLU C OE1 1 
ATOM   10800 O  OE2 . GLU C  1 454 ? -8.86000  7.33000   -25.39600 1.000 83.01000  ? 485 GLU C OE2 1 
ATOM   10801 N  N   . LEU C  1 455 ? -6.26700  1.31800   -26.52700 1.000 77.30000  ? 486 LEU C N   1 
ATOM   10802 C  CA  . LEU C  1 455 ? -6.29300  0.11000   -27.34200 1.000 77.32000  ? 486 LEU C CA  1 
ATOM   10803 C  C   . LEU C  1 455 ? -5.88400  -1.11500  -26.53500 1.000 82.06000  ? 486 LEU C C   1 
ATOM   10804 O  O   . LEU C  1 455 ? -6.49100  -2.18700  -26.66300 1.000 85.30000  ? 486 LEU C O   1 
ATOM   10805 C  CB  . LEU C  1 455 ? -5.35300  0.28400   -28.53400 1.000 73.34000  ? 486 LEU C CB  1 
ATOM   10806 C  CG  . LEU C  1 455 ? -5.62600  1.43400   -29.50300 1.000 78.81000  ? 486 LEU C CG  1 
ATOM   10807 C  CD1 . LEU C  1 455 ? -4.46700  1.56100   -30.47700 1.000 78.13000  ? 486 LEU C CD1 1 
ATOM   10808 C  CD2 . LEU C  1 455 ? -6.94100  1.24400   -30.25900 1.000 82.49000  ? 486 LEU C CD2 1 
ATOM   10809 N  N   . TRP C  1 456 ? -4.87300  -0.97100  -25.67700 1.000 76.73000  ? 487 TRP C N   1 
ATOM   10810 C  CA  . TRP C  1 456 ? -4.40100  -2.10800  -24.89900 1.000 76.53000  ? 487 TRP C CA  1 
ATOM   10811 C  C   . TRP C  1 456 ? -5.37000  -2.46900  -23.77500 1.000 79.90000  ? 487 TRP C C   1 
ATOM   10812 O  O   . TRP C  1 456 ? -5.49900  -3.64900  -23.42700 1.000 75.83000  ? 487 TRP C O   1 
ATOM   10813 C  CB  . TRP C  1 456 ? -3.01000  -1.79500  -24.35100 1.000 76.44000  ? 487 TRP C CB  1 
ATOM   10814 C  CG  . TRP C  1 456 ? -1.91300  -1.93000  -25.37400 1.000 72.58000  ? 487 TRP C CG  1 
ATOM   10815 C  CD1 . TRP C  1 456 ? -1.49700  -0.97500  -26.26400 1.000 71.19000  ? 487 TRP C CD1 1 
ATOM   10816 C  CD2 . TRP C  1 456 ? -1.07400  -3.06900  -25.58900 1.000 65.53000  ? 487 TRP C CD2 1 
ATOM   10817 N  NE1 . TRP C  1 456 ? -0.46200  -1.45600  -27.02700 1.000 69.22000  ? 487 TRP C NE1 1 
ATOM   10818 C  CE2 . TRP C  1 456 ? -0.18000  -2.73900  -26.63000 1.000 68.38000  ? 487 TRP C CE2 1 
ATOM   10819 C  CE3 . TRP C  1 456 ? -0.99600  -4.33800  -25.01100 1.000 68.00000  ? 487 TRP C CE3 1 
ATOM   10820 C  CZ2 . TRP C  1 456 ? 0.77500   -3.63600  -27.10500 1.000 64.55000  ? 487 TRP C CZ2 1 
ATOM   10821 C  CZ3 . TRP C  1 456 ? -0.04300  -5.23000  -25.48500 1.000 69.92000  ? 487 TRP C CZ3 1 
ATOM   10822 C  CH2 . TRP C  1 456 ? 0.82800   -4.87300  -26.52200 1.000 68.38000  ? 487 TRP C CH2 1 
ATOM   10823 N  N   . GLU C  1 457 ? -6.03700  -1.47100  -23.18200 1.000 80.51000  ? 488 GLU C N   1 
ATOM   10824 C  CA  . GLU C  1 457 ? -7.00300  -1.75100  -22.12200 1.000 80.37000  ? 488 GLU C CA  1 
ATOM   10825 C  C   . GLU C  1 457 ? -8.29100  -2.33500  -22.69100 1.000 85.83000  ? 488 GLU C C   1 
ATOM   10826 O  O   . GLU C  1 457 ? -8.88100  -3.25500  -22.10600 1.000 81.49000  ? 488 GLU C O   1 
ATOM   10827 C  CB  . GLU C  1 457 ? -7.29200  -0.47700  -21.32600 1.000 81.44000  ? 488 GLU C CB  1 
ATOM   10828 C  CG  . GLU C  1 457 ? -6.15500  -0.07100  -20.38400 1.000 88.50000  ? 488 GLU C CG  1 
ATOM   10829 C  CD  . GLU C  1 457 ? -6.29700  1.34900   -19.83900 1.000 95.64000  ? 488 GLU C CD  1 
ATOM   10830 O  OE1 . GLU C  1 457 ? -7.01100  2.16700   -20.47100 1.000 95.96000  ? 488 GLU C OE1 1 
ATOM   10831 O  OE2 . GLU C  1 457 ? -5.68600  1.64400   -18.78000 1.000 86.23000  ? 488 GLU C OE2 1 
ATOM   10832 N  N   . SER C  1 458 ? -8.71000  -1.85400  -23.86000 1.000 84.14000  ? 489 SER C N   1 
ATOM   10833 C  CA  . SER C  1 458 ? -9.92000  -2.35800  -24.48700 1.000 83.30000  ? 489 SER C CA  1 
ATOM   10834 C  C   . SER C  1 458 ? -9.71700  -3.70700  -25.15300 1.000 78.14000  ? 489 SER C C   1 
ATOM   10835 O  O   . SER C  1 458 ? -10.70100 -4.33000  -25.55300 1.000 84.71000  ? 489 SER C O   1 
ATOM   10836 C  CB  . SER C  1 458 ? -10.43300 -1.34600  -25.51300 1.000 83.02000  ? 489 SER C CB  1 
ATOM   10837 O  OG  . SER C  1 458 ? -9.58600  -1.31500  -26.64100 1.000 83.75000  ? 489 SER C OG  1 
ATOM   10838 N  N   . GLY C  1 459 ? -8.47800  -4.17700  -25.26600 1.000 82.11000  ? 490 GLY C N   1 
ATOM   10839 C  CA  . GLY C  1 459 ? -8.18400  -5.40000  -25.97600 1.000 82.89000  ? 490 GLY C CA  1 
ATOM   10840 C  C   . GLY C  1 459 ? -7.97900  -5.22400  -27.46700 1.000 83.52000  ? 490 GLY C C   1 
ATOM   10841 O  O   . GLY C  1 459 ? -7.59100  -6.19000  -28.13900 1.000 80.60000  ? 490 GLY C O   1 
ATOM   10842 N  N   . GLN C  1 460 ? -8.23300  -4.01800  -27.99900 1.000 81.86000  ? 491 GLN C N   1 
ATOM   10843 C  CA  . GLN C  1 460 ? -7.97600  -3.72800  -29.40500 1.000 78.91000  ? 491 GLN C CA  1 
ATOM   10844 C  C   . GLN C  1 460 ? -6.53200  -4.02000  -29.79500 1.000 82.08000  ? 491 GLN C C   1 
ATOM   10845 O  O   . GLN C  1 460 ? -6.27100  -4.40100  -30.94200 1.000 82.58000  ? 491 GLN C O   1 
ATOM   10846 C  CB  . GLN C  1 460 ? -8.34200  -2.27300  -29.70600 1.000 80.60000  ? 491 GLN C CB  1 
ATOM   10847 C  CG  . GLN C  1 460 ? -9.85200  -2.01700  -29.69100 1.000 84.49000  ? 491 GLN C CG  1 
ATOM   10848 C  CD  . GLN C  1 460 ? -10.23400 -0.54200  -29.62000 1.000 88.85000  ? 491 GLN C CD  1 
ATOM   10849 O  OE1 . GLN C  1 460 ? -9.98900  0.13400   -28.61300 1.000 86.82000  ? 491 GLN C OE1 1 
ATOM   10850 N  NE2 . GLN C  1 460 ? -10.85200 -0.04000  -30.68700 1.000 91.54000  ? 491 GLN C NE2 1 
ATOM   10851 N  N   . MET C  1 461 ? -5.57700  -3.82600  -28.86600 1.000 78.69000  ? 492 MET C N   1 
ATOM   10852 C  CA  . MET C  1 461 ? -4.18400  -4.25200  -28.95900 1.000 74.57000  ? 492 MET C CA  1 
ATOM   10853 C  C   . MET C  1 461 ? -3.86100  -5.33100  -27.92600 1.000 75.91000  ? 492 MET C C   1 
ATOM   10854 O  O   . MET C  1 461 ? -4.45800  -5.35800  -26.84600 1.000 74.91000  ? 492 MET C O   1 
ATOM   10855 C  CB  . MET C  1 461 ? -3.23600  -3.06300  -28.77000 1.000 72.21000  ? 492 MET C CB  1 
ATOM   10856 C  CG  . MET C  1 461 ? -3.19100  -2.12700  -29.96900 1.000 76.93000  ? 492 MET C CG  1 
ATOM   10857 S  SD  . MET C  1 461 ? -2.46300  -2.94700  -31.41300 1.000 78.77000  ? 492 MET C SD  1 
ATOM   10858 C  CE  . MET C  1 461 ? -0.72000  -2.80200  -31.06400 1.000 69.86000  ? 492 MET C CE  1 
ATOM   10859 N  N   . PRO C  1 462 ? -2.92000  -6.24300  -28.21900 1.000 70.29000  ? 493 PRO C N   1 
ATOM   10860 C  CA  . PRO C  1 462 ? -2.09700  -6.34500  -29.43300 1.000 74.61000  ? 493 PRO C CA  1 
ATOM   10861 C  C   . PRO C  1 462 ? -2.77100  -7.18300  -30.52000 1.000 80.67000  ? 493 PRO C C   1 
ATOM   10862 O  O   . PRO C  1 462 ? -2.52000  -6.99100  -31.70900 1.000 75.62000  ? 493 PRO C O   1 
ATOM   10863 C  CB  . PRO C  1 462 ? -0.81600  -7.01000  -28.91800 1.000 73.14000  ? 493 PRO C CB  1 
ATOM   10864 C  CG  . PRO C  1 462 ? -1.27600  -7.87700  -27.78700 1.000 70.46000  ? 493 PRO C CG  1 
ATOM   10865 C  CD  . PRO C  1 462 ? -2.48000  -7.19400  -27.18000 1.000 68.27000  ? 493 PRO C CD  1 
ATOM   10866 N  N   . ASN C  1 463 ? -3.65900  -8.09200  -30.11500 1.000 81.15000  ? 494 ASN C N   1 
ATOM   10867 C  CA  . ASN C  1 463 ? -4.38700  -8.98700  -31.01300 1.000 78.20000  ? 494 ASN C CA  1 
ATOM   10868 C  C   . ASN C  1 463 ? -3.45700  -9.64400  -32.03100 1.000 82.89000  ? 494 ASN C C   1 
ATOM   10869 O  O   . ASN C  1 463 ? -3.61000  -9.49700  -33.24900 1.000 82.02000  ? 494 ASN C O   1 
ATOM   10870 C  CB  . ASN C  1 463 ? -5.50800  -8.23000  -31.72100 1.000 74.13000  ? 494 ASN C CB  1 
ATOM   10871 C  CG  . ASN C  1 463 ? -6.50800  -9.15600  -32.36500 1.000 78.57000  ? 494 ASN C CG  1 
ATOM   10872 O  OD1 . ASN C  1 463 ? -6.24900  -10.35100 -32.52600 1.000 76.95000  ? 494 ASN C OD1 1 
ATOM   10873 N  ND2 . ASN C  1 463 ? -7.66300  -8.61500  -32.73200 1.000 75.62000  ? 494 ASN C ND2 1 
ATOM   10874 N  N   . TYR C  1 464 ? -2.49100  -10.40100 -31.50700 1.000 82.92000  ? 495 TYR C N   1 
ATOM   10875 C  CA  . TYR C  1 464 ? -1.55700  -11.09400 -32.38700 1.000 82.00000  ? 495 TYR C CA  1 
ATOM   10876 C  C   . TYR C  1 464 ? -2.25800  -12.06800 -33.32400 1.000 81.64000  ? 495 TYR C C   1 
ATOM   10877 O  O   . TYR C  1 464 ? -1.79400  -12.28500 -34.44700 1.000 80.50000  ? 495 TYR C O   1 
ATOM   10878 C  CB  . TYR C  1 464 ? -0.49700  -11.82000 -31.55500 1.000 82.45000  ? 495 TYR C CB  1 
ATOM   10879 C  CG  . TYR C  1 464 ? 0.27400   -10.90600 -30.63400 1.000 85.02000  ? 495 TYR C CG  1 
ATOM   10880 C  CD1 . TYR C  1 464 ? 1.00600   -9.83700  -31.13400 1.000 81.13000  ? 495 TYR C CD1 1 
ATOM   10881 C  CD2 . TYR C  1 464 ? 0.28800   -11.12900 -29.26000 1.000 85.21000  ? 495 TYR C CD2 1 
ATOM   10882 C  CE1 . TYR C  1 464 ? 1.71900   -9.00100  -30.29900 1.000 81.26000  ? 495 TYR C CE1 1 
ATOM   10883 C  CE2 . TYR C  1 464 ? 1.00500   -10.29300 -28.41400 1.000 79.43000  ? 495 TYR C CE2 1 
ATOM   10884 C  CZ  . TYR C  1 464 ? 1.71500   -9.23400  -28.93900 1.000 78.71000  ? 495 TYR C CZ  1 
ATOM   10885 O  OH  . TYR C  1 464 ? 2.42400   -8.40100  -28.10500 1.000 84.82000  ? 495 TYR C OH  1 
ATOM   10886 N  N   . GLU C  1 465 ? -3.37100  -12.65400 -32.89400 1.000 84.77000  ? 496 GLU C N   1 
ATOM   10887 C  CA  . GLU C  1 465 ? -4.04300  -13.64100 -33.73400 1.000 82.21000  ? 496 GLU C CA  1 
ATOM   10888 C  C   . GLU C  1 465 ? -4.56500  -13.02900 -35.03300 1.000 79.88000  ? 496 GLU C C   1 
ATOM   10889 O  O   . GLU C  1 465 ? -4.43700  -13.63500 -36.10600 1.000 80.31000  ? 496 GLU C O   1 
ATOM   10890 C  CB  . GLU C  1 465 ? -5.17100  -14.33700 -32.97100 1.000 84.76000  ? 496 GLU C CB  1 
ATOM   10891 C  CG  . GLU C  1 465 ? -5.70100  -15.56600 -33.71700 1.000 90.42000  ? 496 GLU C CG  1 
ATOM   10892 C  CD  . GLU C  1 465 ? -4.63700  -16.65300 -33.92200 1.000 98.09000  ? 496 GLU C CD  1 
ATOM   10893 O  OE1 . GLU C  1 465 ? -3.58600  -16.62400 -33.23000 1.000 92.32000  ? 496 GLU C OE1 1 
ATOM   10894 O  OE2 . GLU C  1 465 ? -4.86300  -17.54300 -34.78100 1.000 98.02000  ? 496 GLU C OE2 1 
ATOM   10895 N  N   . ALA C  1 466 ? -5.19600  -11.84900 -34.95700 1.000 76.26000  ? 497 ALA C N   1 
ATOM   10896 C  CA  . ALA C  1 466 ? -5.64900  -11.19300 -36.18600 1.000 76.54000  ? 497 ALA C CA  1 
ATOM   10897 C  C   . ALA C  1 466 ? -4.47200  -10.77500 -37.06600 1.000 79.90000  ? 497 ALA C C   1 
ATOM   10898 O  O   . ALA C  1 466 ? -4.57600  -10.79200 -38.30300 1.000 76.24000  ? 497 ALA C O   1 
ATOM   10899 C  CB  . ALA C  1 466 ? -6.51500  -9.97000  -35.85800 1.000 65.75000  ? 497 ALA C CB  1 
ATOM   10900 N  N   . THR C  1 467 ? -3.35600  -10.37600 -36.45000 1.000 70.27000  ? 498 THR C N   1 
ATOM   10901 C  CA  . THR C  1 467 ? -2.17600  -10.01200 -37.22300 1.000 75.65000  ? 498 THR C CA  1 
ATOM   10902 C  C   . THR C  1 467 ? -1.67700  -11.18900 -38.05200 1.000 75.52000  ? 498 THR C C   1 
ATOM   10903 O  O   . THR C  1 467 ? -1.15300  -10.99100 -39.15600 1.000 71.95000  ? 498 THR C O   1 
ATOM   10904 C  CB  . THR C  1 467 ? -1.10000  -9.45400  -36.28500 1.000 77.15000  ? 498 THR C CB  1 
ATOM   10905 O  OG1 . THR C  1 467 ? -1.48300  -8.13400  -35.88000 1.000 79.59000  ? 498 THR C OG1 1 
ATOM   10906 C  CG2 . THR C  1 467 ? 0.28300   -9.41700  -36.93800 1.000 67.95000  ? 498 THR C CG2 1 
ATOM   10907 N  N   . PHE C  1 468 ? -1.86700  -12.41700 -37.56700 1.000 74.81000  ? 499 PHE C N   1 
ATOM   10908 C  CA  . PHE C  1 468 ? -1.38400  -13.59900 -38.26800 1.000 75.33000  ? 499 PHE C CA  1 
ATOM   10909 C  C   . PHE C  1 468 ? -2.46900  -14.28700 -39.09400 1.000 72.40000  ? 499 PHE C C   1 
ATOM   10910 O  O   . PHE C  1 468 ? -2.26400  -15.41700 -39.54500 1.000 74.64000  ? 499 PHE C O   1 
ATOM   10911 C  CB  . PHE C  1 468 ? -0.76000  -14.59700 -37.29400 1.000 74.40000  ? 499 PHE C CB  1 
ATOM   10912 C  CG  . PHE C  1 468 ? 0.49500   -14.10100 -36.63000 1.000 81.96000  ? 499 PHE C CG  1 
ATOM   10913 C  CD1 . PHE C  1 468 ? 1.66100   -13.94100 -37.36200 1.000 77.74000  ? 499 PHE C CD1 1 
ATOM   10914 C  CD2 . PHE C  1 468 ? 0.53300   -13.86400 -35.26400 1.000 87.13000  ? 499 PHE C CD2 1 
ATOM   10915 C  CE1 . PHE C  1 468 ? 2.82900   -13.50800 -36.76100 1.000 78.96000  ? 499 PHE C CE1 1 
ATOM   10916 C  CE2 . PHE C  1 468 ? 1.70200   -13.43200 -34.65300 1.000 83.86000  ? 499 PHE C CE2 1 
ATOM   10917 C  CZ  . PHE C  1 468 ? 2.85200   -13.25700 -35.40400 1.000 83.32000  ? 499 PHE C CZ  1 
ATOM   10918 N  N   . GLU C  1 469 ? -3.61600  -13.64200 -39.29700 1.000 74.24000  ? 500 GLU C N   1 
ATOM   10919 C  CA  . GLU C  1 469 ? -4.53700  -14.07400 -40.34300 1.000 72.30000  ? 500 GLU C CA  1 
ATOM   10920 C  C   . GLU C  1 469 ? -3.82800  -14.06500 -41.69500 1.000 76.51000  ? 500 GLU C C   1 
ATOM   10921 O  O   . GLU C  1 469 ? -2.89100  -13.29300 -41.92100 1.000 76.38000  ? 500 GLU C O   1 
ATOM   10922 C  CB  . GLU C  1 469 ? -5.75000  -13.15800 -40.39200 1.000 64.82000  ? 500 GLU C CB  1 
ATOM   10923 C  CG  . GLU C  1 469 ? -6.65900  -13.24100 -39.19100 1.000 68.19000  ? 500 GLU C CG  1 
ATOM   10924 C  CD  . GLU C  1 469 ? -7.59100  -12.04400 -39.10600 1.000 74.44000  ? 500 GLU C CD  1 
ATOM   10925 O  OE1 . GLU C  1 469 ? -7.28700  -11.01900 -39.76200 1.000 75.13000  ? 500 GLU C OE1 1 
ATOM   10926 O  OE2 . GLU C  1 469 ? -8.61900  -12.12400 -38.39100 1.000 72.95000  ? 500 GLU C OE2 1 
ATOM   10927 N  N   . VAL C  1 470 ? -4.26700  -14.94300 -42.60400 1.000 69.70000  ? 501 VAL C N   1 
ATOM   10928 C  CA  . VAL C  1 470 ? -3.63600  -15.00800 -43.92000 1.000 70.39000  ? 501 VAL C CA  1 
ATOM   10929 C  C   . VAL C  1 470 ? -4.68900  -15.02100 -45.02200 1.000 68.61000  ? 501 VAL C C   1 
ATOM   10930 O  O   . VAL C  1 470 ? -4.73200  -14.12600 -45.87300 1.000 68.95000  ? 501 VAL C O   1 
ATOM   10931 C  CB  . VAL C  1 470 ? -2.73800  -16.25600 -44.05600 1.000 73.07000  ? 501 VAL C CB  1 
ATOM   10932 C  CG1 . VAL C  1 470 ? -1.97100  -16.23100 -45.37900 1.000 68.64000  ? 501 VAL C CG1 1 
ATOM   10933 C  CG2 . VAL C  1 470 ? -1.81900  -16.42100 -42.87300 1.000 76.04000  ? 501 VAL C CG2 1 
ATOM   10934 N  N   . ASP C  1 471 ? -5.52700  -16.06000 -45.02800 1.000 72.59000  ? 502 ASP C N   1 
ATOM   10935 C  CA  . ASP C  1 471 ? -6.44000  -16.28400 -46.14700 1.000 72.65000  ? 502 ASP C CA  1 
ATOM   10936 C  C   . ASP C  1 471 ? -7.52900  -15.22100 -46.20900 1.000 70.53000  ? 502 ASP C C   1 
ATOM   10937 O  O   . ASP C  1 471 ? -7.93500  -14.81200 -47.30100 1.000 70.03000  ? 502 ASP C O   1 
ATOM   10938 C  CB  . ASP C  1 471 ? -7.06100  -17.67600 -46.04800 1.000 74.68000  ? 502 ASP C CB  1 
ATOM   10939 C  CG  . ASP C  1 471 ? -6.02200  -18.78600 -46.12700 1.000 78.55000  ? 502 ASP C CG  1 
ATOM   10940 O  OD1 . ASP C  1 471 ? -5.41700  -19.09700 -45.08100 1.000 80.35000  ? 502 ASP C OD1 1 
ATOM   10941 O  OD2 . ASP C  1 471 ? -5.80100  -19.34700 -47.21900 1.000 84.98000  ? 502 ASP C OD2 1 
ATOM   10942 N  N   . LYS C  1 472 ? -8.02800  -14.77200 -45.05300 1.000 69.93000  ? 503 LYS C N   1 
ATOM   10943 C  CA  . LYS C  1 472 ? -9.14600  -13.82900 -45.04700 1.000 67.11000  ? 503 LYS C CA  1 
ATOM   10944 C  C   . LYS C  1 472 ? -8.79500  -12.50200 -45.70500 1.000 67.61000  ? 503 LYS C C   1 
ATOM   10945 O  O   . LYS C  1 472 ? -9.70500  -11.74100 -46.05000 1.000 67.60000  ? 503 LYS C O   1 
ATOM   10946 C  CB  . LYS C  1 472 ? -9.63300  -13.58300 -43.61400 1.000 68.11000  ? 503 LYS C CB  1 
ATOM   10947 N  N   . LEU C  1 473 ? -7.50000  -12.18900 -45.84300 1.000 69.97000  ? 504 LEU C N   1 
ATOM   10948 C  CA  . LEU C  1 473 ? -7.05900  -10.92000 -46.42200 1.000 69.85000  ? 504 LEU C CA  1 
ATOM   10949 C  C   . LEU C  1 473 ? -7.06900  -10.90100 -47.94900 1.000 70.42000  ? 504 LEU C C   1 
ATOM   10950 O  O   . LEU C  1 473 ? -7.15600  -9.81500  -48.53700 1.000 72.28000  ? 504 LEU C O   1 
ATOM   10951 C  CB  . LEU C  1 473 ? -5.65100  -10.58500 -45.91500 1.000 62.81000  ? 504 LEU C CB  1 
ATOM   10952 C  CG  . LEU C  1 473 ? -5.45400  -10.67100 -44.39700 1.000 61.98000  ? 504 LEU C CG  1 
ATOM   10953 C  CD1 . LEU C  1 473 ? -4.00100  -10.45400 -44.03200 1.000 62.85000  ? 504 LEU C CD1 1 
ATOM   10954 C  CD2 . LEU C  1 473 ? -6.31600  -9.64700  -43.70500 1.000 60.83000  ? 504 LEU C CD2 1 
ATOM   10955 N  N   . VAL C  1 474 ? -6.98100  -12.06200 -48.60300 1.000 74.16000  ? 505 VAL C N   1 
ATOM   10956 C  CA  . VAL C  1 474 ? -6.84900  -12.12800 -50.05500 1.000 69.56000  ? 505 VAL C CA  1 
ATOM   10957 C  C   . VAL C  1 474 ? -8.05300  -12.78000 -50.71800 1.000 76.99000  ? 505 VAL C C   1 
ATOM   10958 O  O   . VAL C  1 474 ? -8.28800  -12.53700 -51.91300 1.000 74.19000  ? 505 VAL C O   1 
ATOM   10959 C  CB  . VAL C  1 474 ? -5.55900  -12.87000 -50.46500 1.000 70.36000  ? 505 VAL C CB  1 
ATOM   10960 C  CG1 . VAL C  1 474 ? -4.34800  -11.97000 -50.28200 1.000 69.21000  ? 505 VAL C CG1 1 
ATOM   10961 C  CG2 . VAL C  1 474 ? -5.38900  -14.15100 -49.65500 1.000 72.39000  ? 505 VAL C CG2 1 
ATOM   10962 N  N   . ASP C  1 475 ? -8.82200  -13.58700 -49.99100 1.000 79.35000  ? 506 ASP C N   1 
ATOM   10963 C  CA  . ASP C  1 475 ? -9.96000  -14.26900 -50.57900 1.000 68.68000  ? 506 ASP C CA  1 
ATOM   10964 C  C   . ASP C  1 475 ? -11.09500 -13.27800 -50.74600 1.000 69.69000  ? 506 ASP C C   1 
ATOM   10965 O  O   . ASP C  1 475 ? -11.37600 -12.48300 -49.84600 1.000 73.04000  ? 506 ASP C O   1 
ATOM   10966 C  CB  . ASP C  1 475 ? -10.42800 -15.43100 -49.69800 1.000 69.04000  ? 506 ASP C CB  1 
ATOM   10967 C  CG  . ASP C  1 475 ? -9.41700  -16.55500 -49.62200 1.000 71.71000  ? 506 ASP C CG  1 
ATOM   10968 O  OD1 . ASP C  1 475 ? -8.58400  -16.68200 -50.54300 1.000 71.38000  ? 506 ASP C OD1 1 
ATOM   10969 O  OD2 . ASP C  1 475 ? -9.46600  -17.32600 -48.64400 1.000 73.00000  ? 506 ASP C OD2 1 
ATOM   10970 N  N   . SER C  1 476 ? -11.76500 -13.36000 -51.87100 1.000 67.37000  ? 507 SER C N   1 
ATOM   10971 C  CA  . SER C  1 476 ? -12.96600 -12.59200 -52.13300 1.000 70.16000  ? 507 SER C CA  1 
ATOM   10972 C  C   . SER C  1 476 ? -14.15000 -13.21500 -51.39800 1.000 73.21000  ? 507 SER C C   1 
ATOM   10973 O  O   . SER C  1 476 ? -14.18900 -14.43200 -51.18900 1.000 69.66000  ? 507 SER C O   1 
ATOM   10974 C  CB  . SER C  1 476 ? -13.26800 -12.56300 -53.62400 1.000 69.97000  ? 507 SER C CB  1 
ATOM   10975 O  OG  . SER C  1 476 ? -14.58200 -12.10400 -53.84100 1.000 64.24000  ? 507 SER C OG  1 
ATOM   10976 N  N   . PRO C  1 477 ? -15.10600 -12.40300 -50.94700 1.000 71.02000  ? 508 PRO C N   1 
ATOM   10977 C  CA  . PRO C  1 477 ? -16.31500 -12.96000 -50.33500 1.000 71.45000  ? 508 PRO C CA  1 
ATOM   10978 C  C   . PRO C  1 477 ? -17.33600 -13.50200 -51.32700 1.000 74.66000  ? 508 PRO C C   1 
ATOM   10979 O  O   . PRO C  1 477 ? -18.42500 -13.90100 -50.90000 1.000 74.13000  ? 508 PRO C O   1 
ATOM   10980 C  CB  . PRO C  1 477 ? -16.88700 -11.76100 -49.55400 1.000 67.56000  ? 508 PRO C CB  1 
ATOM   10981 C  CG  . PRO C  1 477 ? -16.34700 -10.56900 -50.20600 1.000 70.78000  ? 508 PRO C CG  1 
ATOM   10982 C  CD  . PRO C  1 477 ? -15.06900 -10.93100 -50.89200 1.000 67.83000  ? 508 PRO C CD  1 
ATOM   10983 N  N   . TYR C  1 478 ? -17.01300 -13.55900 -52.62400 1.000 77.04000  ? 509 TYR C N   1 
ATOM   10984 C  CA  . TYR C  1 478 ? -17.96900 -13.98400 -53.65400 1.000 78.25000  ? 509 TYR C CA  1 
ATOM   10985 C  C   . TYR C  1 478 ? -17.44700 -15.16700 -54.47800 1.000 72.97000  ? 509 TYR C C   1 
ATOM   10986 O  O   . TYR C  1 478 ? -18.03800 -16.24800 -54.48000 1.000 74.70000  ? 509 TYR C O   1 
ATOM   10987 C  CB  . TYR C  1 478 ? -18.29600 -12.80300 -54.57200 1.000 75.38000  ? 509 TYR C CB  1 
ATOM   10988 C  CG  . TYR C  1 478 ? -18.43700 -11.51500 -53.80400 1.000 75.57000  ? 509 TYR C CG  1 
ATOM   10989 C  CD1 . TYR C  1 478 ? -19.56300 -11.26500 -53.03400 1.000 75.50000  ? 509 TYR C CD1 1 
ATOM   10990 C  CD2 . TYR C  1 478 ? -17.43300 -10.55100 -53.83300 1.000 71.70000  ? 509 TYR C CD2 1 
ATOM   10991 C  CE1 . TYR C  1 478 ? -19.68800 -10.08900 -52.30800 1.000 76.73000  ? 509 TYR C CE1 1 
ATOM   10992 C  CE2 . TYR C  1 478 ? -17.55500 -9.36700  -53.11800 1.000 69.73000  ? 509 TYR C CE2 1 
ATOM   10993 C  CZ  . TYR C  1 478 ? -18.68200 -9.14300  -52.35100 1.000 74.71000  ? 509 TYR C CZ  1 
ATOM   10994 O  OH  . TYR C  1 478 ? -18.80900 -7.96900  -51.63100 1.000 75.08000  ? 509 TYR C OH  1 
ATOM   10995 N  N   . THR D  1 15  ? -30.53800 25.34600  -9.73300  1.000 85.46000  ? 46  THR D N   1 
ATOM   10996 C  CA  . THR D  1 15  ? -31.17300 24.05400  -9.45600  1.000 86.73000  ? 46  THR D CA  1 
ATOM   10997 C  C   . THR D  1 15  ? -30.44400 23.33300  -8.31000  1.000 83.25000  ? 46  THR D C   1 
ATOM   10998 O  O   . THR D  1 15  ? -29.22900 23.50900  -8.12600  1.000 81.25000  ? 46  THR D O   1 
ATOM   10999 C  CB  . THR D  1 15  ? -31.20900 23.14900  -10.72500 1.000 85.34000  ? 46  THR D CB  1 
ATOM   11000 O  OG1 . THR D  1 15  ? -31.98900 21.96800  -10.47100 1.000 81.00000  ? 46  THR D OG1 1 
ATOM   11001 C  CG2 . THR D  1 15  ? -29.79200 22.75100  -11.15500 1.000 81.16000  ? 46  THR D CG2 1 
ATOM   11002 N  N   . ARG D  1 16  ? -31.19100 22.51300  -7.56400  1.000 75.02000  ? 47  ARG D N   1 
ATOM   11003 C  CA  . ARG D  1 16  ? -30.68500 21.90700  -6.34000  1.000 74.72000  ? 47  ARG D CA  1 
ATOM   11004 C  C   . ARG D  1 16  ? -29.45300 21.05000  -6.63200  1.000 80.21000  ? 47  ARG D C   1 
ATOM   11005 O  O   . ARG D  1 16  ? -29.34500 20.44500  -7.70300  1.000 74.47000  ? 47  ARG D O   1 
ATOM   11006 C  CB  . ARG D  1 16  ? -31.76900 21.05400  -5.69500  1.000 71.56000  ? 47  ARG D CB  1 
ATOM   11007 C  CG  . ARG D  1 16  ? -32.86800 21.80700  -4.98300  1.000 70.61000  ? 47  ARG D CG  1 
ATOM   11008 C  CD  . ARG D  1 16  ? -34.05600 20.87400  -4.84900  1.000 72.74000  ? 47  ARG D CD  1 
ATOM   11009 N  NE  . ARG D  1 16  ? -34.32900 20.30500  -6.17100  1.000 66.86000  ? 47  ARG D NE  1 
ATOM   11010 C  CZ  . ARG D  1 16  ? -35.20300 19.34300  -6.44000  1.000 67.62000  ? 47  ARG D CZ  1 
ATOM   11011 N  NH1 . ARG D  1 16  ? -35.90300 18.74900  -5.48500  1.000 70.17000  ? 47  ARG D NH1 1 
ATOM   11012 N  NH2 . ARG D  1 16  ? -35.36000 18.95100  -7.70100  1.000 70.32000  ? 47  ARG D NH2 1 
ATOM   11013 N  N   . PRO D  1 17  ? -28.49900 21.01000  -5.70400  1.000 77.72000  ? 48  PRO D N   1 
ATOM   11014 C  CA  . PRO D  1 17  ? -27.25000 20.28000  -5.94000  1.000 79.36000  ? 48  PRO D CA  1 
ATOM   11015 C  C   . PRO D  1 17  ? -27.38700 18.79200  -5.65000  1.000 75.05000  ? 48  PRO D C   1 
ATOM   11016 O  O   . PRO D  1 17  ? -28.24000 18.34700  -4.87800  1.000 74.06000  ? 48  PRO D O   1 
ATOM   11017 C  CB  . PRO D  1 17  ? -26.28100 20.93400  -4.95000  1.000 76.30000  ? 48  PRO D CB  1 
ATOM   11018 C  CG  . PRO D  1 17  ? -27.17400 21.26500  -3.77400  1.000 73.78000  ? 48  PRO D CG  1 
ATOM   11019 C  CD  . PRO D  1 17  ? -28.52200 21.64700  -4.37500  1.000 73.77000  ? 48  PRO D CD  1 
ATOM   11020 N  N   . ASN D  1 18  ? -26.50200 18.02500  -6.27600  1.000 73.03000  ? 49  ASN D N   1 
ATOM   11021 C  CA  . ASN D  1 18  ? -26.29300 16.64000  -5.87600  1.000 72.38000  ? 49  ASN D CA  1 
ATOM   11022 C  C   . ASN D  1 18  ? -25.56700 16.56100  -4.53900  1.000 68.15000  ? 49  ASN D C   1 
ATOM   11023 O  O   . ASN D  1 18  ? -24.81200 17.45800  -4.16000  1.000 70.43000  ? 49  ASN D O   1 
ATOM   11024 C  CB  . ASN D  1 18  ? -25.48100 15.90800  -6.93000  1.000 70.02000  ? 49  ASN D CB  1 
ATOM   11025 C  CG  . ASN D  1 18  ? -26.00900 16.15100  -8.31600  1.000 70.98000  ? 49  ASN D CG  1 
ATOM   11026 O  OD1 . ASN D  1 18  ? -27.12400 15.74900  -8.65100  1.000 71.49000  ? 49  ASN D OD1 1 
ATOM   11027 N  ND2 . ASN D  1 18  ? -25.21700 16.82800  -9.13000  1.000 69.66000  ? 49  ASN D ND2 1 
ATOM   11028 N  N   . ILE D  1 19  ? -25.79300 15.46300  -3.82600  1.000 64.65000  ? 50  ILE D N   1 
ATOM   11029 C  CA  . ILE D  1 19  ? -25.15200 15.22200  -2.54100  1.000 65.53000  ? 50  ILE D CA  1 
ATOM   11030 C  C   . ILE D  1 19  ? -24.55700 13.82500  -2.57500  1.000 66.86000  ? 50  ILE D C   1 
ATOM   11031 O  O   . ILE D  1 19  ? -25.29100 12.84000  -2.70900  1.000 65.91000  ? 50  ILE D O   1 
ATOM   11032 C  CB  . ILE D  1 19  ? -26.13300 15.36800  -1.37000  1.000 63.88000  ? 50  ILE D CB  1 
ATOM   11033 C  CG1 . ILE D  1 19  ? -26.70200 16.78300  -1.34300  1.000 69.43000  ? 50  ILE D CG1 1 
ATOM   11034 C  CG2 . ILE D  1 19  ? -25.44300 15.07700  -0.05800  1.000 64.74000  ? 50  ILE D CG2 1 
ATOM   11035 C  CD1 . ILE D  1 19  ? -27.92700 16.92100  -0.47800  1.000 72.94000  ? 50  ILE D CD1 1 
ATOM   11036 N  N   . LEU D  1 20  ? -23.23700 13.74400  -2.44100  1.000 65.81000  ? 51  LEU D N   1 
ATOM   11037 C  CA  . LEU D  1 20  ? -22.48600 12.49400  -2.40400  1.000 61.91000  ? 51  LEU D CA  1 
ATOM   11038 C  C   . LEU D  1 20  ? -21.81300 12.39000  -1.04400  1.000 68.73000  ? 51  LEU D C   1 
ATOM   11039 O  O   . LEU D  1 20  ? -20.96400 13.22000  -0.69600  1.000 73.87000  ? 51  LEU D O   1 
ATOM   11040 C  CB  . LEU D  1 20  ? -21.46000 12.42600  -3.53700  1.000 61.99000  ? 51  LEU D CB  1 
ATOM   11041 C  CG  . LEU D  1 20  ? -20.42100 11.31200  -3.41700  1.000 65.53000  ? 51  LEU D CG  1 
ATOM   11042 C  CD1 . LEU D  1 20  ? -21.10400 9.95700   -3.33200  1.000 65.73000  ? 51  LEU D CD1 1 
ATOM   11043 C  CD2 . LEU D  1 20  ? -19.47900 11.33700  -4.62800  1.000 61.63000  ? 51  LEU D CD2 1 
ATOM   11044 N  N   . VAL D  1 21  ? -22.22200 11.40400  -0.26100  1.000 63.31000  ? 52  VAL D N   1 
ATOM   11045 C  CA  . VAL D  1 21  ? -21.61100 11.12000  1.02600   1.000 60.25000  ? 52  VAL D CA  1 
ATOM   11046 C  C   . VAL D  1 21  ? -20.66000 9.95300   0.81700   1.000 64.23000  ? 52  VAL D C   1 
ATOM   11047 O  O   . VAL D  1 21  ? -21.09800 8.83800   0.52000   1.000 64.14000  ? 52  VAL D O   1 
ATOM   11048 C  CB  . VAL D  1 21  ? -22.66700 10.77700  2.08400   1.000 64.20000  ? 52  VAL D CB  1 
ATOM   11049 C  CG1 . VAL D  1 21  ? -22.00500 10.53600  3.43100   1.000 62.25000  ? 52  VAL D CG1 1 
ATOM   11050 C  CG2 . VAL D  1 21  ? -23.74100 11.86100  2.15300   1.000 64.75000  ? 52  VAL D CG2 1 
ATOM   11051 N  N   . VAL D  1 22  ? -19.36100 10.19200  0.94800   1.000 62.87000  ? 53  VAL D N   1 
ATOM   11052 C  CA  . VAL D  1 22  ? -18.37500 9.12000   0.96500   1.000 57.41000  ? 53  VAL D CA  1 
ATOM   11053 C  C   . VAL D  1 22  ? -18.06100 8.85300   2.42100   1.000 60.43000  ? 53  VAL D C   1 
ATOM   11054 O  O   . VAL D  1 22  ? -17.41900 9.67600   3.08200   1.000 58.12000  ? 53  VAL D O   1 
ATOM   11055 C  CB  . VAL D  1 22  ? -17.11100 9.47600   0.18400   1.000 57.70000  ? 53  VAL D CB  1 
ATOM   11056 C  CG1 . VAL D  1 22  ? -16.14200 8.32300   0.27300   1.000 63.09000  ? 53  VAL D CG1 1 
ATOM   11057 C  CG2 . VAL D  1 22  ? -17.47100 9.74700   -1.26800  1.000 53.94000  ? 53  VAL D CG2 1 
ATOM   11058 N  N   . LEU D  1 23  ? -18.54600 7.72200   2.92400   1.000 60.13000  ? 54  LEU D N   1 
ATOM   11059 C  CA  . LEU D  1 23  ? -18.43200 7.35400   4.33100   1.000 59.68000  ? 54  LEU D CA  1 
ATOM   11060 C  C   . LEU D  1 23  ? -17.47600 6.17900   4.44000   1.000 58.92000  ? 54  LEU D C   1 
ATOM   11061 O  O   . LEU D  1 23  ? -17.78200 5.07900   3.96900   1.000 61.27000  ? 54  LEU D O   1 
ATOM   11062 C  CB  . LEU D  1 23  ? -19.79700 6.99900   4.91300   1.000 64.20000  ? 54  LEU D CB  1 
ATOM   11063 C  CG  . LEU D  1 23  ? -19.87700 6.60900   6.39200   1.000 59.97000  ? 54  LEU D CG  1 
ATOM   11064 C  CD1 . LEU D  1 23  ? -19.44600 7.75300   7.27200   1.000 60.46000  ? 54  LEU D CD1 1 
ATOM   11065 C  CD2 . LEU D  1 23  ? -21.30800 6.21100   6.73000   1.000 60.58000  ? 54  LEU D CD2 1 
ATOM   11066 N  N   . CYS D  1 24  ? -16.32600 6.41200   5.05700   1.000 65.91000  ? 55  CYS D N   1 
ATOM   11067 C  CA  . CYS D  1 24  ? -15.39800 5.33900   5.35000   1.000 53.55000  ? 55  CYS D CA  1 
ATOM   11068 C  C   . CYS D  1 24  ? -15.71600 4.73300   6.70500   1.000 56.67000  ? 55  CYS D C   1 
ATOM   11069 O  O   . CYS D  1 24  ? -16.44300 5.30800   7.52300   1.000 57.12000  ? 55  CYS D O   1 
ATOM   11070 C  CB  . CYS D  1 24  ? -13.97100 5.85000   5.30000   1.000 57.68000  ? 55  CYS D CB  1 
ATOM   11071 S  SG  . CYS D  1 24  ? -13.39400 5.99200   3.61500   1.000 67.38000  ? 55  CYS D SG  1 
ATOM   11072 N  N   . ASP D  1 25  ? -15.12900 3.56100   6.94600   1.000 58.36000  ? 56  ASP D N   1 
ATOM   11073 C  CA  . ASP D  1 25  ? -15.44100 2.72200   8.10000   1.000 56.57000  ? 56  ASP D CA  1 
ATOM   11074 C  C   . ASP D  1 25  ? -14.16700 2.49500   8.91400   1.000 59.21000  ? 56  ASP D C   1 
ATOM   11075 O  O   . ASP D  1 25  ? -13.26000 1.78200   8.46800   1.000 58.68000  ? 56  ASP D O   1 
ATOM   11076 C  CB  . ASP D  1 25  ? -16.04700 1.40600   7.61500   1.000 54.33000  ? 56  ASP D CB  1 
ATOM   11077 C  CG  . ASP D  1 25  ? -16.69600 0.62800   8.71200   1.000 59.00000  ? 56  ASP D CG  1 
ATOM   11078 O  OD1 . ASP D  1 25  ? -16.62300 1.08600   9.86800   1.000 58.53000  ? 56  ASP D OD1 1 
ATOM   11079 O  OD2 . ASP D  1 25  ? -17.26500 -0.44900  8.41900   1.000 57.76000  ? 56  ASP D OD2 1 
ATOM   11080 N  N   . ASP D  1 26  ? -14.10200 3.09100   10.11200  1.000 56.00000  ? 57  ASP D N   1 
ATOM   11081 C  CA  . ASP D  1 26  ? -12.93500 2.99000   11.00100  1.000 59.40000  ? 57  ASP D CA  1 
ATOM   11082 C  C   . ASP D  1 26  ? -11.68800 3.67400   10.41700  1.000 59.26000  ? 57  ASP D C   1 
ATOM   11083 O  O   . ASP D  1 26  ? -10.55800 3.24400   10.66700  1.000 59.14000  ? 57  ASP D O   1 
ATOM   11084 C  CB  . ASP D  1 26  ? -12.61100 1.53300   11.36900  1.000 56.67000  ? 57  ASP D CB  1 
ATOM   11085 C  CG  . ASP D  1 26  ? -13.68400 0.88700   12.22300  1.000 60.27000  ? 57  ASP D CG  1 
ATOM   11086 O  OD1 . ASP D  1 26  ? -14.69100 1.55600   12.51700  1.000 62.08000  ? 57  ASP D OD1 1 
ATOM   11087 O  OD2 . ASP D  1 26  ? -13.52500 -0.29500  12.60400  1.000 60.90000  ? 57  ASP D OD2 1 
ATOM   11088 N  N   . LEU D  1 27  ? -11.85800 4.74100   9.64200   1.000 56.61000  ? 58  LEU D N   1 
ATOM   11089 C  CA  . LEU D  1 27  ? -10.70900 5.49200   9.14200   1.000 61.10000  ? 58  LEU D CA  1 
ATOM   11090 C  C   . LEU D  1 27  ? -10.14800 6.34900   10.27000  1.000 59.32000  ? 58  LEU D C   1 
ATOM   11091 O  O   . LEU D  1 27  ? -10.87800 7.15200   10.85900  1.000 60.96000  ? 58  LEU D O   1 
ATOM   11092 C  CB  . LEU D  1 27  ? -11.10600 6.36200   7.95200   1.000 56.60000  ? 58  LEU D CB  1 
ATOM   11093 C  CG  . LEU D  1 27  ? -9.97800  7.25400   7.42600   1.000 56.32000  ? 58  LEU D CG  1 
ATOM   11094 C  CD1 . LEU D  1 27  ? -8.99600  6.50100   6.53400   1.000 49.29000  ? 58  LEU D CD1 1 
ATOM   11095 C  CD2 . LEU D  1 27  ? -10.53600 8.47000   6.71800   1.000 56.68000  ? 58  LEU D CD2 1 
ATOM   11096 N  N   . GLY D  1 28  ? -8.84400  6.20000   10.54900  1.000 67.13000  ? 59  GLY D N   1 
ATOM   11097 C  CA  . GLY D  1 28  ? -8.22400  6.89300   11.67000  1.000 59.30000  ? 59  GLY D CA  1 
ATOM   11098 C  C   . GLY D  1 28  ? -8.06400  8.38400   11.43600  1.000 58.07000  ? 59  GLY D C   1 
ATOM   11099 O  O   . GLY D  1 28  ? -8.06100  8.87300   10.30700  1.000 56.94000  ? 59  GLY D O   1 
ATOM   11100 N  N   . TYR D  1 29  ? -7.93800  9.12100   12.54500  1.000 59.20000  ? 60  TYR D N   1 
ATOM   11101 C  CA  . TYR D  1 29  ? -7.94400  10.58300  12.48400  1.000 60.62000  ? 60  TYR D CA  1 
ATOM   11102 C  C   . TYR D  1 29  ? -6.78900  11.14800  11.67000  1.000 60.94000  ? 60  TYR D C   1 
ATOM   11103 O  O   . TYR D  1 29  ? -6.93200  12.20700  11.04800  1.000 58.82000  ? 60  TYR D O   1 
ATOM   11104 C  CB  . TYR D  1 29  ? -7.88900  11.16300  13.88700  1.000 54.24000  ? 60  TYR D CB  1 
ATOM   11105 C  CG  . TYR D  1 29  ? -8.41500  12.57200  13.97000  1.000 63.61000  ? 60  TYR D CG  1 
ATOM   11106 C  CD1 . TYR D  1 29  ? -9.74100  12.86000  13.63500  1.000 55.02000  ? 60  TYR D CD1 1 
ATOM   11107 C  CD2 . TYR D  1 29  ? -7.59300  13.62100  14.39000  1.000 62.55000  ? 60  TYR D CD2 1 
ATOM   11108 C  CE1 . TYR D  1 29  ? -10.23900 14.15700  13.72500  1.000 58.96000  ? 60  TYR D CE1 1 
ATOM   11109 C  CE2 . TYR D  1 29  ? -8.08400  14.92800  14.48000  1.000 63.12000  ? 60  TYR D CE2 1 
ATOM   11110 C  CZ  . TYR D  1 29  ? -9.41000  15.19200  14.14500  1.000 61.63000  ? 60  TYR D CZ  1 
ATOM   11111 O  OH  . TYR D  1 29  ? -9.90500  16.48400  14.24400  1.000 55.07000  ? 60  TYR D OH  1 
ATOM   11112 N  N   . ALA D  1 30  ? -5.64100  10.47800  11.67800  1.000 58.46000  ? 61  ALA D N   1 
ATOM   11113 C  CA  . ALA D  1 30  ? -4.45100  10.92400  10.96800  1.000 60.43000  ? 61  ALA D CA  1 
ATOM   11114 C  C   . ALA D  1 30  ? -4.14700  10.05200  9.75800   1.000 60.07000  ? 61  ALA D C   1 
ATOM   11115 O  O   . ALA D  1 30  ? -2.98600  9.91600   9.36900   1.000 65.60000  ? 61  ALA D O   1 
ATOM   11116 C  CB  . ALA D  1 30  ? -3.25000  10.95200  11.90900  1.000 62.53000  ? 61  ALA D CB  1 
ATOM   11117 N  N   . ASP D  1 31  ? -5.16700  9.42200   9.17600   1.000 58.40000  ? 62  ASP D N   1 
ATOM   11118 C  CA  . ASP D  1 31  ? -4.95900  8.42100   8.13500   1.000 60.39000  ? 62  ASP D CA  1 
ATOM   11119 C  C   . ASP D  1 31  ? -5.39200  8.89000   6.74700   1.000 63.26000  ? 62  ASP D C   1 
ATOM   11120 O  O   . ASP D  1 31  ? -5.50000  8.06600   5.83200   1.000 65.87000  ? 62  ASP D O   1 
ATOM   11121 C  CB  . ASP D  1 31  ? -5.66400  7.11400   8.52000   1.000 63.84000  ? 62  ASP D CB  1 
ATOM   11122 C  CG  . ASP D  1 31  ? -4.98500  6.41200   9.70300   1.000 65.99000  ? 62  ASP D CG  1 
ATOM   11123 O  OD1 . ASP D  1 31  ? -3.78100  6.66300   9.93100   1.000 64.31000  ? 62  ASP D OD1 1 
ATOM   11124 O  OD2 . ASP D  1 31  ? -5.64500  5.62200   10.41400  1.000 64.47000  ? 62  ASP D OD2 1 
ATOM   11125 N  N   . VAL D  1 32  ? -5.63000  10.18800  6.56100   1.000 58.22000  ? 63  VAL D N   1 
ATOM   11126 C  CA  . VAL D  1 32  ? -5.67400  10.78700  5.23400   1.000 63.53000  ? 63  VAL D CA  1 
ATOM   11127 C  C   . VAL D  1 32  ? -4.72300  11.97400  5.25100   1.000 64.24000  ? 63  VAL D C   1 
ATOM   11128 O  O   . VAL D  1 32  ? -4.55900  12.64900  6.27500   1.000 61.70000  ? 63  VAL D O   1 
ATOM   11129 C  CB  . VAL D  1 32  ? -7.09300  11.22800  4.79200   1.000 62.88000  ? 63  VAL D CB  1 
ATOM   11130 C  CG1 . VAL D  1 32  ? -7.93800  10.01600  4.41300   1.000 57.80000  ? 63  VAL D CG1 1 
ATOM   11131 C  CG2 . VAL D  1 32  ? -7.76500  12.05000  5.88200   1.000 61.10000  ? 63  VAL D CG2 1 
ATOM   11132 N  N   . GLY D  1 33  ? -4.09000  12.22000  4.10400   1.000 61.04000  ? 64  GLY D N   1 
ATOM   11133 C  CA  . GLY D  1 33  ? -3.10800  13.29000  4.01800   1.000 65.40000  ? 64  GLY D CA  1 
ATOM   11134 C  C   . GLY D  1 33  ? -3.63900  14.63400  4.47900   1.000 70.55000  ? 64  GLY D C   1 
ATOM   11135 O  O   . GLY D  1 33  ? -3.01400  15.31200  5.29900   1.000 71.68000  ? 64  GLY D O   1 
ATOM   11136 N  N   . PHE D  1 34  ? -4.81700  15.03100  3.98200   1.000 61.09000  ? 65  PHE D N   1 
ATOM   11137 C  CA  . PHE D  1 34  ? -5.32500  16.35000  4.33300   1.000 63.16000  ? 65  PHE D CA  1 
ATOM   11138 C  C   . PHE D  1 34  ? -5.58300  16.47200  5.82000   1.000 64.43000  ? 65  PHE D C   1 
ATOM   11139 O  O   . PHE D  1 34  ? -5.84800  17.58100  6.30100   1.000 67.12000  ? 65  PHE D O   1 
ATOM   11140 C  CB  . PHE D  1 34  ? -6.60400  16.70800  3.54000   1.000 68.02000  ? 65  PHE D CB  1 
ATOM   11141 C  CG  . PHE D  1 34  ? -7.85200  15.97800  3.98400   1.000 57.85000  ? 65  PHE D CG  1 
ATOM   11142 C  CD1 . PHE D  1 34  ? -8.57500  16.40400  5.09400   1.000 57.55000  ? 65  PHE D CD1 1 
ATOM   11143 C  CD2 . PHE D  1 34  ? -8.34900  14.92300  3.23600   1.000 59.89000  ? 65  PHE D CD2 1 
ATOM   11144 C  CE1 . PHE D  1 34  ? -9.73400  15.74400  5.49000   1.000 68.16000  ? 65  PHE D CE1 1 
ATOM   11145 C  CE2 . PHE D  1 34  ? -9.51900  14.26100  3.61700   1.000 61.33000  ? 65  PHE D CE2 1 
ATOM   11146 C  CZ  . PHE D  1 34  ? -10.21200 14.66800  4.74100   1.000 62.59000  ? 65  PHE D CZ  1 
ATOM   11147 N  N   . ASN D  1 35  ? -5.53300  15.36300  6.55200   1.000 62.32000  ? 66  ASN D N   1 
ATOM   11148 C  CA  . ASN D  1 35  ? -5.66400  15.39200  7.99900   1.000 66.46000  ? 66  ASN D CA  1 
ATOM   11149 C  C   . ASN D  1 35  ? -4.35000  15.02300  8.69000   1.000 71.15000  ? 66  ASN D C   1 
ATOM   11150 O  O   . ASN D  1 35  ? -4.34300  14.73700  9.89200   1.000 70.53000  ? 66  ASN D O   1 
ATOM   11151 C  CB  . ASN D  1 35  ? -6.80600  14.47300  8.44400   1.000 64.41000  ? 66  ASN D CB  1 
ATOM   11152 C  CG  . ASN D  1 35  ? -7.71200  15.13500  9.46200   1.000 58.68000  ? 66  ASN D CG  1 
ATOM   11153 O  OD1 . ASN D  1 35  ? -8.06100  16.30400  9.30600   1.000 58.92000  ? 66  ASN D OD1 1 
ATOM   11154 N  ND2 . ASN D  1 35  ? -8.10500  14.39900  10.50200  1.000 56.28000  ? 66  ASN D ND2 1 
ATOM   11155 N  N   . GLY D  1 36  ? -3.23100  15.04000  7.95600   1.000 66.31000  ? 67  GLY D N   1 
ATOM   11156 C  CA  . GLY D  1 36  ? -1.91300  14.95600  8.56600   1.000 69.01000  ? 67  GLY D CA  1 
ATOM   11157 C  C   . GLY D  1 36  ? -1.13400  13.67000  8.36300   1.000 71.99000  ? 67  GLY D C   1 
ATOM   11158 O  O   . GLY D  1 36  ? -0.02500  13.56000  8.90100   1.000 81.03000  ? 67  GLY D O   1 
ATOM   11159 N  N   . SER D  1 37  ? -1.64800  12.70200  7.60700   1.000 71.07000  ? 68  SER D N   1 
ATOM   11160 C  CA  . SER D  1 37  ? -0.94300  11.43600  7.44700   1.000 71.30000  ? 68  SER D CA  1 
ATOM   11161 C  C   . SER D  1 37  ? 0.39600   11.63900  6.76100   1.000 71.87000  ? 68  SER D C   1 
ATOM   11162 O  O   . SER D  1 37  ? 0.49100   12.34400  5.75500   1.000 69.11000  ? 68  SER D O   1 
ATOM   11163 C  CB  . SER D  1 37  ? -1.76200  10.44200  6.62800   1.000 67.81000  ? 68  SER D CB  1 
ATOM   11164 O  OG  . SER D  1 37  ? -1.01800  9.24400   6.45700   1.000 68.49000  ? 68  SER D OG  1 
ATOM   11165 N  N   . THR D  1 38  ? 1.42900   10.97800  7.29900   1.000 71.44000  ? 69  THR D N   1 
ATOM   11166 C  CA  . THR D  1 38  ? 2.76500   11.04600  6.72200   1.000 77.34000  ? 69  THR D CA  1 
ATOM   11167 C  C   . THR D  1 38  ? 3.11700   9.84700   5.85200   1.000 74.72000  ? 69  THR D C   1 
ATOM   11168 O  O   . THR D  1 38  ? 4.05100   9.94800   5.05000   1.000 77.30000  ? 69  THR D O   1 
ATOM   11169 C  CB  . THR D  1 38  ? 3.83000   11.17000  7.82600   1.000 70.53000  ? 69  THR D CB  1 
ATOM   11170 O  OG1 . THR D  1 38  ? 3.72600   10.05500  8.71800   1.000 79.53000  ? 69  THR D OG1 1 
ATOM   11171 C  CG2 . THR D  1 38  ? 3.64700   12.46200  8.62100   1.000 68.52000  ? 69  THR D CG2 1 
ATOM   11172 N  N   . ASP D  1 39  ? 2.40600   8.72000   5.98400   1.000 68.82000  ? 70  ASP D N   1 
ATOM   11173 C  CA  . ASP D  1 39  ? 2.73600   7.51600   5.22600   1.000 68.60000  ? 70  ASP D CA  1 
ATOM   11174 C  C   . ASP D  1 39  ? 1.63100   7.01400   4.31000   1.000 72.26000  ? 70  ASP D C   1 
ATOM   11175 O  O   . ASP D  1 39  ? 1.93700   6.28700   3.35700   1.000 77.54000  ? 70  ASP D O   1 
ATOM   11176 C  CB  . ASP D  1 39  ? 3.15200   6.36700   6.15900   1.000 71.01000  ? 70  ASP D CB  1 
ATOM   11177 C  CG  . ASP D  1 39  ? 2.15400   6.12500   7.27800   1.000 76.28000  ? 70  ASP D CG  1 
ATOM   11178 O  OD1 . ASP D  1 39  ? 1.28700   6.99700   7.50300   1.000 78.50000  ? 70  ASP D OD1 1 
ATOM   11179 O  OD2 . ASP D  1 39  ? 2.22700   5.05700   7.92500   1.000 74.87000  ? 70  ASP D OD2 1 
ATOM   11180 N  N   . ILE D  1 40  ? 0.37600   7.37200   4.54800   1.000 66.57000  ? 71  ILE D N   1 
ATOM   11181 C  CA  . ILE D  1 40  ? -0.70300  6.97300   3.65100   1.000 71.57000  ? 71  ILE D CA  1 
ATOM   11182 C  C   . ILE D  1 40  ? -0.91400  8.07700   2.63000   1.000 70.91000  ? 71  ILE D C   1 
ATOM   11183 O  O   . ILE D  1 40  ? -1.06000  9.25200   2.98900   1.000 68.17000  ? 71  ILE D O   1 
ATOM   11184 C  CB  . ILE D  1 40  ? -1.99900  6.67000   4.41900   1.000 72.57000  ? 71  ILE D CB  1 
ATOM   11185 C  CG1 . ILE D  1 40  ? -1.78000  5.53500   5.42700   1.000 67.23000  ? 71  ILE D CG1 1 
ATOM   11186 C  CG2 . ILE D  1 40  ? -3.12200  6.34100   3.43400   1.000 68.02000  ? 71  ILE D CG2 1 
ATOM   11187 C  CD1 . ILE D  1 40  ? -3.01900  5.14700   6.20000   1.000 58.97000  ? 71  ILE D CD1 1 
ATOM   11188 N  N   . LEU D  1 41  ? -0.89400  7.69900   1.35400   1.000 68.62000  ? 72  LEU D N   1 
ATOM   11189 C  CA  . LEU D  1 41  ? -1.04300  8.62600   0.24100   1.000 72.61000  ? 72  LEU D CA  1 
ATOM   11190 C  C   . LEU D  1 41  ? -2.50600  8.64100   -0.20200  1.000 69.91000  ? 72  LEU D C   1 
ATOM   11191 O  O   . LEU D  1 41  ? -3.03100  7.61300   -0.64200  1.000 65.49000  ? 72  LEU D O   1 
ATOM   11192 C  CB  . LEU D  1 41  ? -0.15200  8.17900   -0.91400  1.000 72.40000  ? 72  LEU D CB  1 
ATOM   11193 C  CG  . LEU D  1 41  ? 1.30800   7.89800   -0.52600  1.000 76.23000  ? 72  LEU D CG  1 
ATOM   11194 C  CD1 . LEU D  1 41  ? 2.07000   7.26300   -1.70500  1.000 67.13000  ? 72  LEU D CD1 1 
ATOM   11195 C  CD2 . LEU D  1 41  ? 2.02800   9.12400   0.04600   1.000 70.53000  ? 72  LEU D CD2 1 
ATOM   11196 N  N   . THR D  1 42  ? -3.14900  9.80600   -0.11400  1.000 64.26000  ? 73  THR D N   1 
ATOM   11197 C  CA  . THR D  1 42  ? -4.53700  9.99000   -0.54800  1.000 67.45000  ? 73  THR D CA  1 
ATOM   11198 C  C   . THR D  1 42  ? -4.64300  11.23700  -1.41500  1.000 70.83000  ? 73  THR D C   1 
ATOM   11199 O  O   . THR D  1 42  ? -5.27200  12.23100  -1.03500  1.000 69.72000  ? 73  THR D O   1 
ATOM   11200 C  CB  . THR D  1 42  ? -5.48800  10.07000  0.64200   1.000 67.59000  ? 73  THR D CB  1 
ATOM   11201 O  OG1 . THR D  1 42  ? -5.08600  11.13400  1.52100   1.000 62.17000  ? 73  THR D OG1 1 
ATOM   11202 C  CG2 . THR D  1 42  ? -5.52700  8.73900   1.38400   1.000 68.66000  ? 73  THR D CG2 1 
ATOM   11203 N  N   . PRO D  1 43  ? -3.98900  11.23500  -2.57500  1.000 63.10000  ? 74  PRO D N   1 
ATOM   11204 C  CA  . PRO D  1 43  ? -3.93300  12.46900  -3.36700  1.000 67.59000  ? 74  PRO D CA  1 
ATOM   11205 C  C   . PRO D  1 43  ? -5.30300  12.96700  -3.81300  1.000 72.02000  ? 74  PRO D C   1 
ATOM   11206 O  O   . PRO D  1 43  ? -5.60500  14.15700  -3.63600  1.000 70.24000  ? 74  PRO D O   1 
ATOM   11207 C  CB  . PRO D  1 43  ? -3.02300  12.07000  -4.54200  1.000 62.25000  ? 74  PRO D CB  1 
ATOM   11208 C  CG  . PRO D  1 43  ? -3.16100  10.59400  -4.63100  1.000 63.62000  ? 74  PRO D CG  1 
ATOM   11209 C  CD  . PRO D  1 43  ? -3.25500  10.13600  -3.21600  1.000 63.90000  ? 74  PRO D CD  1 
ATOM   11210 N  N   . GLU D  1 44  ? -6.17500  12.07400  -4.29100  1.000 69.34000  ? 75  GLU D N   1 
ATOM   11211 C  CA  . GLU D  1 44  ? -7.48800  12.50300  -4.76300  1.000 67.58000  ? 75  GLU D CA  1 
ATOM   11212 C  C   . GLU D  1 44  ? -8.29400  13.14200  -3.64200  1.000 70.56000  ? 75  GLU D C   1 
ATOM   11213 O  O   . GLU D  1 44  ? -8.78800  14.26600  -3.78500  1.000 72.31000  ? 75  GLU D O   1 
ATOM   11214 C  CB  . GLU D  1 44  ? -8.25300  11.32000  -5.35800  1.000 64.84000  ? 75  GLU D CB  1 
ATOM   11215 C  CG  . GLU D  1 44  ? -7.61000  10.64900  -6.56600  1.000 64.57000  ? 75  GLU D CG  1 
ATOM   11216 C  CD  . GLU D  1 44  ? -7.61000  11.52400  -7.80900  1.000 76.67000  ? 75  GLU D CD  1 
ATOM   11217 O  OE1 . GLU D  1 44  ? -8.09300  12.67700  -7.73800  1.000 79.49000  ? 75  GLU D OE1 1 
ATOM   11218 O  OE2 . GLU D  1 44  ? -7.14600  11.04600  -8.87100  1.000 79.58000  ? 75  GLU D OE2 1 
ATOM   11219 N  N   . LEU D  1 45  ? -8.40300  12.45600  -2.50000  1.000 70.62000  ? 76  LEU D N   1 
ATOM   11220 C  CA  . LEU D  1 45  ? -9.13700  13.01400  -1.36800  1.000 65.65000  ? 76  LEU D CA  1 
ATOM   11221 C  C   . LEU D  1 45  ? -8.54600  14.34000  -0.92300  1.000 70.75000  ? 76  LEU D C   1 
ATOM   11222 O  O   . LEU D  1 45  ? -9.28400  15.28200  -0.60100  1.000 64.01000  ? 76  LEU D O   1 
ATOM   11223 C  CB  . LEU D  1 45  ? -9.13500  12.02300  -0.20900  1.000 69.00000  ? 76  LEU D CB  1 
ATOM   11224 C  CG  . LEU D  1 45  ? -10.17300 10.91000  -0.27500  1.000 70.46000  ? 76  LEU D CG  1 
ATOM   11225 C  CD1 . LEU D  1 45  ? -9.79700  9.81500   0.70700   1.000 68.79000  ? 76  LEU D CD1 1 
ATOM   11226 C  CD2 . LEU D  1 45  ? -11.54000 11.48700  0.05800   1.000 61.43000  ? 76  LEU D CD2 1 
ATOM   11227 N  N   . ASP D  1 46  ? -7.21100  14.43000  -0.89200  1.000 73.74000  ? 77  ASP D N   1 
ATOM   11228 C  CA  . ASP D  1 46  ? -6.56200  15.67600  -0.49600  1.000 75.11000  ? 77  ASP D CA  1 
ATOM   11229 C  C   . ASP D  1 46  ? -6.89900  16.79900  -1.46900  1.000 75.13000  ? 77  ASP D C   1 
ATOM   11230 O  O   . ASP D  1 46  ? -7.23200  17.91400  -1.05100  1.000 71.43000  ? 77  ASP D O   1 
ATOM   11231 C  CB  . ASP D  1 46  ? -5.04400  15.47800  -0.40400  1.000 72.53000  ? 77  ASP D CB  1 
ATOM   11232 C  CG  . ASP D  1 46  ? -4.62500  14.59700  0.77200   1.000 76.24000  ? 77  ASP D CG  1 
ATOM   11233 O  OD1 . ASP D  1 46  ? -5.49300  14.20800  1.58000   1.000 75.46000  ? 77  ASP D OD1 1 
ATOM   11234 O  OD2 . ASP D  1 46  ? -3.41100  14.31100  0.90000   1.000 82.25000  ? 77  ASP D OD2 1 
ATOM   11235 N  N   . ASN D  1 47  ? -6.86000  16.50500  -2.77100  1.000 72.92000  ? 78  ASN D N   1 
ATOM   11236 C  CA  . ASN D  1 47  ? -7.15500  17.51600  -3.77900  1.000 77.94000  ? 78  ASN D CA  1 
ATOM   11237 C  C   . ASN D  1 47  ? -8.56300  18.08500  -3.59400  1.000 75.64000  ? 78  ASN D C   1 
ATOM   11238 O  O   . ASN D  1 47  ? -8.76100  19.30800  -3.61400  1.000 73.79000  ? 78  ASN D O   1 
ATOM   11239 C  CB  . ASN D  1 47  ? -6.97000  16.89500  -5.16500  1.000 71.33000  ? 78  ASN D CB  1 
ATOM   11240 C  CG  . ASN D  1 47  ? -7.14000  17.89300  -6.27300  1.000 78.71000  ? 78  ASN D CG  1 
ATOM   11241 O  OD1 . ASN D  1 47  ? -7.16700  19.09900  -6.03000  1.000 80.29000  ? 78  ASN D OD1 1 
ATOM   11242 N  ND2 . ASN D  1 47  ? -7.21400  17.40400  -7.51100  1.000 82.77000  ? 78  ASN D ND2 1 
ATOM   11243 N  N   . LEU D  1 48  ? -9.55400  17.20900  -3.39200  1.000 66.77000  ? 79  LEU D N   1 
ATOM   11244 C  CA  . LEU D  1 48  ? -10.90800 17.67500  -3.09000  1.000 71.72000  ? 79  LEU D CA  1 
ATOM   11245 C  C   . LEU D  1 48  ? -10.94800 18.50700  -1.81400  1.000 71.60000  ? 79  LEU D C   1 
ATOM   11246 O  O   . LEU D  1 48  ? -11.62000 19.54500  -1.76500  1.000 63.57000  ? 79  LEU D O   1 
ATOM   11247 C  CB  . LEU D  1 48  ? -11.87900 16.49400  -2.98200  1.000 67.46000  ? 79  LEU D CB  1 
ATOM   11248 C  CG  . LEU D  1 48  ? -12.18400 15.77900  -4.29300  1.000 67.48000  ? 79  LEU D CG  1 
ATOM   11249 C  CD1 . LEU D  1 48  ? -13.20500 14.68700  -4.06000  1.000 71.48000  ? 79  LEU D CD1 1 
ATOM   11250 C  CD2 . LEU D  1 48  ? -12.69400 16.79500  -5.30900  1.000 65.59000  ? 79  LEU D CD2 1 
ATOM   11251 N  N   . ALA D  1 49  ? -10.26400 18.04900  -0.75900  1.000 70.06000  ? 80  ALA D N   1 
ATOM   11252 C  CA  . ALA D  1 49  ? -10.30300 18.76500  0.51300   1.000 68.71000  ? 80  ALA D CA  1 
ATOM   11253 C  C   . ALA D  1 49  ? -9.68900  20.15400  0.37600   1.000 72.36000  ? 80  ALA D C   1 
ATOM   11254 O  O   . ALA D  1 49  ? -10.17700 21.11800  0.98200   1.000 75.59000  ? 80  ALA D O   1 
ATOM   11255 C  CB  . ALA D  1 49  ? -9.59600  17.95700  1.60100   1.000 69.57000  ? 80  ALA D CB  1 
ATOM   11256 N  N   . GLN D  1 50  ? -8.59800  20.26900  -0.39300  1.000 74.50000  ? 81  GLN D N   1 
ATOM   11257 C  CA  . GLN D  1 50  ? -7.98800  21.57700  -0.63000  1.000 78.48000  ? 81  GLN D CA  1 
ATOM   11258 C  C   . GLN D  1 50  ? -8.95700  22.52100  -1.32200  1.000 80.59000  ? 81  GLN D C   1 
ATOM   11259 O  O   . GLN D  1 50  ? -8.92000  23.73600  -1.08600  1.000 77.50000  ? 81  GLN D O   1 
ATOM   11260 C  CB  . GLN D  1 50  ? -6.73900  21.43800  -1.50900  1.000 78.51000  ? 81  GLN D CB  1 
ATOM   11261 C  CG  . GLN D  1 50  ? -5.63500  20.53800  -0.97000  1.000 88.23000  ? 81  GLN D CG  1 
ATOM   11262 C  CD  . GLN D  1 50  ? -4.54800  20.26300  -2.00900  1.000 88.18000  ? 81  GLN D CD  1 
ATOM   11263 O  OE1 . GLN D  1 50  ? -3.94400  19.19100  -2.01500  1.000 86.21000  ? 81  GLN D OE1 1 
ATOM   11264 N  NE2 . GLN D  1 50  ? -4.31100  21.22300  -2.89700  1.000 90.99000  ? 81  GLN D NE2 1 
ATOM   11265 N  N   . ASN D  1 51  ? -9.86100  21.97600  -2.13700  1.000 75.55000  ? 82  ASN D N   1 
ATOM   11266 C  CA  . ASN D  1 51  ? -10.79900 22.78000  -2.89500  1.000 71.69000  ? 82  ASN D CA  1 
ATOM   11267 C  C   . ASN D  1 51  ? -12.11500 22.98100  -2.16500  1.000 71.78000  ? 82  ASN D C   1 
ATOM   11268 O  O   . ASN D  1 51  ? -13.09100 23.42100  -2.78000  1.000 78.99000  ? 82  ASN D O   1 
ATOM   11269 C  CB  . ASN D  1 51  ? -11.04800 22.12800  -4.25500  1.000 74.73000  ? 82  ASN D CB  1 
ATOM   11270 C  CG  . ASN D  1 51  ? -9.81600  22.14100  -5.14700  1.000 81.61000  ? 82  ASN D CG  1 
ATOM   11271 O  OD1 . ASN D  1 51  ? -8.80800  22.76100  -4.82000  1.000 79.02000  ? 82  ASN D OD1 1 
ATOM   11272 N  ND2 . ASN D  1 51  ? -9.89200  21.44000  -6.27900  1.000 87.10000  ? 82  ASN D ND2 1 
ATOM   11273 N  N   . GLY D  1 52  ? -12.16500 22.71500  -0.87300  1.000 69.63000  ? 83  GLY D N   1 
ATOM   11274 C  CA  . GLY D  1 52  ? -13.37600 22.92700  -0.09900  1.000 62.03000  ? 83  GLY D CA  1 
ATOM   11275 C  C   . GLY D  1 52  ? -13.04700 23.33900  1.30300   1.000 68.43000  ? 83  GLY D C   1 
ATOM   11276 O  O   . GLY D  1 52  ? -12.01400 23.96700  1.55200   1.000 69.06000  ? 83  GLY D O   1 
ATOM   11277 N  N   . SER D  1 53  ? -13.91300 22.96600  2.23700   1.000 65.28000  ? 84  SER D N   1 
ATOM   11278 C  CA  . SER D  1 53  ? -13.75500 23.32000  3.64000   1.000 68.87000  ? 84  SER D CA  1 
ATOM   11279 C  C   . SER D  1 53  ? -13.48000 22.06100  4.46300   1.000 69.97000  ? 84  SER D C   1 
ATOM   11280 O  O   . SER D  1 53  ? -14.29800 21.12700  4.47400   1.000 60.10000  ? 84  SER D O   1 
ATOM   11281 C  CB  . SER D  1 53  ? -14.99200 24.05200  4.15700   1.000 68.78000  ? 84  SER D CB  1 
ATOM   11282 O  OG  . SER D  1 53  ? -14.92000 24.21900  5.56600   1.000 73.63000  ? 84  SER D OG  1 
ATOM   11283 N  N   . ILE D  1 54  ? -12.29900 22.04900  5.15700   1.000 64.38000  ? 85  ILE D N   1 
ATOM   11284 C  CA  . ILE D  1 54  ? -11.87800 20.99200  6.07200   1.000 57.65000  ? 85  ILE D CA  1 
ATOM   11285 C  C   . ILE D  1 54  ? -12.36900 21.30400  7.47900   1.000 63.09000  ? 85  ILE D C   1 
ATOM   11286 O  O   . ILE D  1 54  ? -12.23100 22.43400  7.96200   1.000 65.21000  ? 85  ILE D O   1 
ATOM   11287 C  CB  . ILE D  1 54  ? -10.34700 20.84200  6.00700   1.000 64.62000  ? 85  ILE D CB  1 
ATOM   11288 C  CG1 . ILE D  1 54  ? -9.95300  20.31300  4.61800   1.000 63.89000  ? 85  ILE D CG1 1 
ATOM   11289 C  CG2 . ILE D  1 54  ? -9.82400  19.97600  7.13500   1.000 61.22000  ? 85  ILE D CG2 1 
ATOM   11290 C  CD1 . ILE D  1 54  ? -8.46700  20.32100  4.32900   1.000 65.48000  ? 85  ILE D CD1 1 
ATOM   11291 N  N   . PHE D  1 55  ? -12.92900 20.29900  8.15700   1.000 59.67000  ? 86  PHE D N   1 
ATOM   11292 C  CA  . PHE D  1 55  ? -13.53700 20.47200  9.48400   1.000 62.47000  ? 86  PHE D CA  1 
ATOM   11293 C  C   . PHE D  1 55  ? -12.64400 19.88800  10.57600  1.000 65.51000  ? 86  PHE D C   1 
ATOM   11294 O  O   . PHE D  1 55  ? -12.63700 18.67000  10.80600  1.000 59.77000  ? 86  PHE D O   1 
ATOM   11295 C  CB  . PHE D  1 55  ? -14.91800 19.81700  9.52100   1.000 61.68000  ? 86  PHE D CB  1 
ATOM   11296 C  CG  . PHE D  1 55  ? -15.94900 20.52500  8.69900   1.000 59.95000  ? 86  PHE D CG  1 
ATOM   11297 C  CD1 . PHE D  1 55  ? -15.89900 20.48400  7.30700   1.000 61.97000  ? 86  PHE D CD1 1 
ATOM   11298 C  CD2 . PHE D  1 55  ? -16.99200 21.19600  9.31500   1.000 59.55000  ? 86  PHE D CD2 1 
ATOM   11299 C  CE1 . PHE D  1 55  ? -16.85500 21.13100  6.53700   1.000 65.69000  ? 86  PHE D CE1 1 
ATOM   11300 C  CE2 . PHE D  1 55  ? -17.95500 21.84600  8.56000   1.000 67.23000  ? 86  PHE D CE2 1 
ATOM   11301 C  CZ  . PHE D  1 55  ? -17.88900 21.81500  7.16400   1.000 62.24000  ? 86  PHE D CZ  1 
ATOM   11302 N  N   . THR D  1 56  ? -11.98600 20.76500  11.32300  1.000 62.27000  ? 87  THR D N   1 
ATOM   11303 C  CA  . THR D  1 56  ? -10.98900 20.33600  12.28600  1.000 55.71000  ? 87  THR D CA  1 
ATOM   11304 C  C   . THR D  1 56  ? -11.58500 19.94600  13.63700  1.000 54.89000  ? 87  THR D C   1 
ATOM   11305 O  O   . THR D  1 56  ? -10.84700 19.42900  14.48000  1.000 60.16000  ? 87  THR D O   1 
ATOM   11306 C  CB  . THR D  1 56  ? -9.90200  21.42500  12.43200  1.000 55.96000  ? 87  THR D CB  1 
ATOM   11307 O  OG1 . THR D  1 56  ? -10.44800 22.62800  12.99200  1.000 51.48000  ? 87  THR D OG1 1 
ATOM   11308 C  CG2 . THR D  1 56  ? -9.31000  21.76100  11.05100  1.000 56.92000  ? 87  THR D CG2 1 
ATOM   11309 N  N   . SER D  1 57  ? -12.89000 20.14400  13.86400  1.000 54.89000  ? 88  SER D N   1 
ATOM   11310 C  CA  . SER D  1 57  ? -13.55600 19.63100  15.08200  1.000 57.80000  ? 88  SER D CA  1 
ATOM   11311 C  C   . SER D  1 57  ? -14.91200 18.98000  14.74000  1.000 66.50000  ? 88  SER D C   1 
ATOM   11312 O  O   . SER D  1 57  ? -15.96500 19.33400  15.27200  1.000 59.86000  ? 88  SER D O   1 
ATOM   11313 C  CB  . SER D  1 57  ? -13.73400 20.74300  16.11800  1.000 56.09000  ? 88  SER D CB  1 
ATOM   11314 O  OG  . SER D  1 57  ? -12.55900 20.96800  16.90600  1.000 53.51000  ? 88  SER D OG  1 
ATOM   11315 N  N   . ALA D  1 58  ? -14.87400 17.92800  13.91500  1.000 61.76000  ? 89  ALA D N   1 
ATOM   11316 C  CA  . ALA D  1 58  ? -16.06000 17.20400  13.47000  1.000 55.32000  ? 89  ALA D CA  1 
ATOM   11317 C  C   . ALA D  1 58  ? -16.29100 15.96000  14.31400  1.000 55.65000  ? 89  ALA D C   1 
ATOM   11318 O  O   . ALA D  1 58  ? -15.35200 15.21600  14.60000  1.000 58.30000  ? 89  ALA D O   1 
ATOM   11319 C  CB  . ALA D  1 58  ? -15.91700 16.79200  12.00700  1.000 55.97000  ? 89  ALA D CB  1 
ATOM   11320 N  N   . TYR D  1 59  ? -17.54900 15.71600  14.68300  1.000 54.06000  ? 90  TYR D N   1 
ATOM   11321 C  CA  . TYR D  1 59  ? -17.87900 14.60600  15.56400  1.000 57.80000  ? 90  TYR D CA  1 
ATOM   11322 C  C   . TYR D  1 59  ? -19.02700 13.77000  15.02200  1.000 63.80000  ? 90  TYR D C   1 
ATOM   11323 O  O   . TYR D  1 59  ? -20.02700 14.29500  14.52000  1.000 64.75000  ? 90  TYR D O   1 
ATOM   11324 C  CB  . TYR D  1 59  ? -18.26400 15.09500  16.94600  1.000 57.03000  ? 90  TYR D CB  1 
ATOM   11325 C  CG  . TYR D  1 59  ? -17.17200 15.83300  17.66300  1.000 62.33000  ? 90  TYR D CG  1 
ATOM   11326 C  CD1 . TYR D  1 59  ? -17.02100 17.20500  17.49300  1.000 64.00000  ? 90  TYR D CD1 1 
ATOM   11327 C  CD2 . TYR D  1 59  ? -16.29700 15.16900  18.52600  1.000 61.23000  ? 90  TYR D CD2 1 
ATOM   11328 C  CE1 . TYR D  1 59  ? -16.03300 17.90600  18.16000  1.000 63.31000  ? 90  TYR D CE1 1 
ATOM   11329 C  CE2 . TYR D  1 59  ? -15.30500 15.86200  19.20200  1.000 65.65000  ? 90  TYR D CE2 1 
ATOM   11330 C  CZ  . TYR D  1 59  ? -15.17900 17.23600  19.01000  1.000 64.49000  ? 90  TYR D CZ  1 
ATOM   11331 O  OH  . TYR D  1 59  ? -14.20400 17.95000  19.66000  1.000 56.52000  ? 90  TYR D OH  1 
ATOM   11332 N  N   . VAL D  1 60  ? -18.89800 12.47700  15.18100  1.000 57.52000  ? 91  VAL D N   1 
ATOM   11333 C  CA  . VAL D  1 60  ? -20.00900 11.58000  14.96500  1.000 55.83000  ? 91  VAL D CA  1 
ATOM   11334 C  C   . VAL D  1 60  ? -20.69700 11.37400  16.30900  1.000 60.87000  ? 91  VAL D C   1 
ATOM   11335 O  O   . VAL D  1 60  ? -20.14400 11.67000  17.37500  1.000 61.39000  ? 91  VAL D O   1 
ATOM   11336 C  CB  . VAL D  1 60  ? -19.52300 10.25900  14.34300  1.000 61.75000  ? 91  VAL D CB  1 
ATOM   11337 C  CG1 . VAL D  1 60  ? -18.92700 10.52600  12.95900  1.000 48.52000  ? 91  VAL D CG1 1 
ATOM   11338 C  CG2 . VAL D  1 60  ? -18.50700 9.58900   15.25100  1.000 56.79000  ? 91  VAL D CG2 1 
ATOM   11339 N  N   . ALA D  1 61  ? -21.92000 10.86900  16.26900  1.000 63.54000  ? 92  ALA D N   1 
ATOM   11340 C  CA  . ALA D  1 61  ? -22.76100 10.84600  17.45600  1.000 55.13000  ? 92  ALA D CA  1 
ATOM   11341 C  C   . ALA D  1 61  ? -22.51600 9.64600   18.34900  1.000 62.48000  ? 92  ALA D C   1 
ATOM   11342 O  O   . ALA D  1 61  ? -23.13500 9.55200   19.41400  1.000 67.20000  ? 92  ALA D O   1 
ATOM   11343 C  CB  . ALA D  1 61  ? -24.23700 10.88600  17.04800  1.000 65.96000  ? 92  ALA D CB  1 
ATOM   11344 N  N   . HIS D  1 62  ? -21.63300 8.73300   17.95300  1.000 63.67000  ? 93  HIS D N   1 
ATOM   11345 C  CA  . HIS D  1 62  ? -21.32800 7.57300   18.77500  1.000 58.93000  ? 93  HIS D CA  1 
ATOM   11346 C  C   . HIS D  1 62  ? -19.99400 7.02300   18.32500  1.000 61.04000  ? 93  HIS D C   1 
ATOM   11347 O  O   . HIS D  1 62  ? -19.67600 7.08300   17.13300  1.000 59.09000  ? 93  HIS D O   1 
ATOM   11348 C  CB  . HIS D  1 62  ? -22.40800 6.49800   18.64700  1.000 59.46000  ? 93  HIS D CB  1 
ATOM   11349 C  CG  . HIS D  1 62  ? -22.41400 5.50600   19.76100  1.000 60.19000  ? 93  HIS D CG  1 
ATOM   11350 N  ND1 . HIS D  1 62  ? -22.97900 5.77300   20.98800  1.000 60.15000  ? 93  HIS D ND1 1 
ATOM   11351 C  CD2 . HIS D  1 62  ? -21.92300 4.24600   19.83800  1.000 61.42000  ? 93  HIS D CD2 1 
ATOM   11352 C  CE1 . HIS D  1 62  ? -22.85100 4.71500   21.76900  1.000 57.30000  ? 93  HIS D CE1 1 
ATOM   11353 N  NE2 . HIS D  1 62  ? -22.20700 3.77700   21.09900  1.000 61.14000  ? 93  HIS D NE2 1 
ATOM   11354 N  N   . PRO D  1 63  ? -19.20700 6.48200   19.22900  1.000 60.38000  ? 94  PRO D N   1 
ATOM   11355 C  CA  . PRO D  1 63  ? -17.86600 6.03500   18.85500  1.000 59.03000  ? 94  PRO D CA  1 
ATOM   11356 C  C   . PRO D  1 63  ? -17.78900 4.66500   18.19100  1.000 58.49000  ? 94  PRO D C   1 
ATOM   11357 O  O   . PRO D  1 63  ? -16.69200 4.10000   18.17300  1.000 54.96000  ? 94  PRO D O   1 
ATOM   11358 C  CB  . PRO D  1 63  ? -17.12000 6.02000   20.19900  1.000 59.72000  ? 94  PRO D CB  1 
ATOM   11359 C  CG  . PRO D  1 63  ? -18.02100 6.69800   21.18000  1.000 65.70000  ? 94  PRO D CG  1 
ATOM   11360 C  CD  . PRO D  1 63  ? -19.39800 6.45200   20.68700  1.000 56.71000  ? 94  PRO D CD  1 
ATOM   11361 N  N   . PHE D  1 64  ? -18.87200 4.08300   17.66400  1.000 60.67000  ? 95  PHE D N   1 
ATOM   11362 C  CA  . PHE D  1 64  ? -18.66600 2.90000   16.83300  1.000 58.41000  ? 95  PHE D CA  1 
ATOM   11363 C  C   . PHE D  1 64  ? -19.80500 2.70400   15.81900  1.000 64.58000  ? 95  PHE D C   1 
ATOM   11364 O  O   . PHE D  1 64  ? -20.79700 3.44100   15.80600  1.000 59.87000  ? 95  PHE D O   1 
ATOM   11365 C  CB  . PHE D  1 64  ? -18.39000 1.66100   17.69900  1.000 54.31000  ? 95  PHE D CB  1 
ATOM   11366 C  CG  . PHE D  1 64  ? -19.45900 1.33300   18.69500  1.000 63.94000  ? 95  PHE D CG  1 
ATOM   11367 C  CD1 . PHE D  1 64  ? -20.62600 0.69000   18.29200  1.000 59.51000  ? 95  PHE D CD1 1 
ATOM   11368 C  CD2 . PHE D  1 64  ? -19.26100 1.57000   20.04900  1.000 59.42000  ? 95  PHE D CD2 1 
ATOM   11369 C  CE1 . PHE D  1 64  ? -21.59100 0.34600   19.21100  1.000 61.33000  ? 95  PHE D CE1 1 
ATOM   11370 C  CE2 . PHE D  1 64  ? -20.23400 1.22600   20.98100  1.000 57.02000  ? 95  PHE D CE2 1 
ATOM   11371 C  CZ  . PHE D  1 64  ? -21.39400 0.61300   20.56100  1.000 60.88000  ? 95  PHE D CZ  1 
ATOM   11372 N  N   A CYS D  1 65  ? -19.63800 1.67300   14.98100  0.300 62.70000  ? 96  CYS D N   1 
ATOM   11373 C  CA  A CYS D  1 65  ? -20.33100 1.47400   13.70800  0.300 61.20000  ? 96  CYS D CA  1 
ATOM   11374 C  C   A CYS D  1 65  ? -21.82900 1.76400   13.73700  0.300 60.58000  ? 96  CYS D C   1 
ATOM   11375 O  O   A CYS D  1 65  ? -22.27600 2.78300   13.20000  0.300 55.37000  ? 96  CYS D O   1 
ATOM   11376 C  CB  A CYS D  1 65  ? -20.09900 0.03700   13.21800  0.300 58.98000  ? 96  CYS D CB  1 
ATOM   11377 S  SG  A CYS D  1 65  ? -18.35400 -0.44100  13.01000  0.300 59.45000  ? 96  CYS D SG  1 
HETATM 11378 N  N   B DDZ D  1 65  ? -19.63100 1.66400   14.99100  0.700 62.81000  ? 96  DDZ D N   1 
HETATM 11379 C  CA  B DDZ D  1 65  ? -20.31500 1.41900   13.68600  0.700 61.26000  ? 96  DDZ D CA  1 
HETATM 11380 C  C   B DDZ D  1 65  ? -21.81300 1.74800   13.74000  0.700 60.64000  ? 96  DDZ D C   1 
HETATM 11381 O  O   B DDZ D  1 65  ? -22.20800 2.79200   13.17800  0.700 55.16000  ? 96  DDZ D O   1 
HETATM 11382 O  OG1 B DDZ D  1 65  ? -20.94700 -0.32400  12.11400  0.700 59.75000  ? 96  DDZ D OG1 1 
HETATM 11383 O  OG2 B DDZ D  1 65  ? -18.75500 -0.32400  12.97600  0.700 59.47000  ? 96  DDZ D OG2 1 
HETATM 11384 C  CB  B DDZ D  1 65  ? -20.12500 -0.03600  13.23900  0.700 58.91000  ? 96  DDZ D CB  1 
ATOM   11385 N  N   . GLY D  1 66  ? -22.60800 0.87200   14.34900  1.000 62.42000  ? 97  GLY D N   1 
ATOM   11386 C  CA  . GLY D  1 66  ? -24.05200 0.90500   14.23900  1.000 62.65000  ? 97  GLY D CA  1 
ATOM   11387 C  C   . GLY D  1 66  ? -24.77800 2.16800   14.66600  1.000 60.62000  ? 97  GLY D C   1 
ATOM   11388 O  O   . GLY D  1 66  ? -25.59400 2.72200   13.91400  1.000 53.88000  ? 97  GLY D O   1 
ATOM   11389 N  N   . PRO D  1 67  ? -24.54800 2.61200   15.90600  1.000 61.03000  ? 98  PRO D N   1 
ATOM   11390 C  CA  . PRO D  1 67  ? -25.23500 3.83100   16.36500  1.000 57.12000  ? 98  PRO D CA  1 
ATOM   11391 C  C   . PRO D  1 67  ? -24.83900 5.06100   15.57500  1.000 59.53000  ? 98  PRO D C   1 
ATOM   11392 O  O   . PRO D  1 67  ? -25.69400 5.90200   15.26500  1.000 61.00000  ? 98  PRO D O   1 
ATOM   11393 C  CB  . PRO D  1 67  ? -24.81900 3.92200   17.84000  1.000 64.61000  ? 98  PRO D CB  1 
ATOM   11394 C  CG  . PRO D  1 67  ? -24.55400 2.47800   18.23900  1.000 62.12000  ? 98  PRO D CG  1 
ATOM   11395 C  CD  . PRO D  1 67  ? -23.88400 1.90100   17.01600  1.000 59.60000  ? 98  PRO D CD  1 
ATOM   11396 N  N   . SER D  1 68  ? -23.57200 5.16600   15.18300  1.000 58.77000  ? 99  SER D N   1 
ATOM   11397 C  CA  . SER D  1 68  ? -23.16300 6.30900   14.37700  1.000 58.79000  ? 99  SER D CA  1 
ATOM   11398 C  C   . SER D  1 68  ? -23.91600 6.34900   13.05400  1.000 58.23000  ? 99  SER D C   1 
ATOM   11399 O  O   . SER D  1 68  ? -24.39100 7.40800   12.62900  1.000 61.60000  ? 99  SER D O   1 
ATOM   11400 C  CB  . SER D  1 68  ? -21.65600 6.27900   14.13700  1.000 56.66000  ? 99  SER D CB  1 
ATOM   11401 O  OG  . SER D  1 68  ? -21.29800 7.29000   13.20800  1.000 52.74000  ? 99  SER D OG  1 
ATOM   11402 N  N   . ARG D  1 69  ? -24.02000 5.20400   12.37300  1.000 59.65000  ? 100 ARG D N   1 
ATOM   11403 C  CA  . ARG D  1 69  ? -24.73300 5.19000   11.09800  1.000 60.61000  ? 100 ARG D CA  1 
ATOM   11404 C  C   . ARG D  1 69  ? -26.22900 5.39500   11.30300  1.000 57.11000  ? 100 ARG D C   1 
ATOM   11405 O  O   . ARG D  1 69  ? -26.87000 6.12100   10.53400  1.000 54.26000  ? 100 ARG D O   1 
ATOM   11406 C  CB  . ARG D  1 69  ? -24.44900 3.88900   10.33900  1.000 65.09000  ? 100 ARG D CB  1 
ATOM   11407 C  CG  . ARG D  1 69  ? -23.02600 3.81100   9.76900   1.000 61.54000  ? 100 ARG D CG  1 
ATOM   11408 C  CD  . ARG D  1 69  ? -22.59600 2.37700   9.45900   1.000 58.03000  ? 100 ARG D CD  1 
ATOM   11409 N  NE  . ARG D  1 69  ? -21.16200 2.31600   9.20700   1.000 59.94000  ? 100 ARG D NE  1 
ATOM   11410 C  CZ  . ARG D  1 69  ? -20.59300 2.57500   8.04100   1.000 53.95000  ? 100 ARG D CZ  1 
ATOM   11411 N  NH1 . ARG D  1 69  ? -21.31300 2.81400   6.96300   1.000 50.99000  ? 100 ARG D NH1 1 
ATOM   11412 N  NH2 . ARG D  1 69  ? -19.26600 2.61500   7.96200   1.000 57.55000  ? 100 ARG D NH2 1 
ATOM   11413 N  N   . SER D  1 70  ? -26.79900 4.76000   12.33300  1.000 55.08000  ? 101 SER D N   1 
ATOM   11414 C  CA  . SER D  1 70  ? -28.17800 5.05000   12.71700  1.000 53.40000  ? 101 SER D CA  1 
ATOM   11415 C  C   . SER D  1 70  ? -28.37900 6.54200   12.93700  1.000 59.48000  ? 101 SER D C   1 
ATOM   11416 O  O   . SER D  1 70  ? -29.34900 7.12800   12.44600  1.000 59.38000  ? 101 SER D O   1 
ATOM   11417 C  CB  . SER D  1 70  ? -28.53800 4.25600   13.97500  1.000 61.83000  ? 101 SER D CB  1 
ATOM   11418 O  OG  . SER D  1 70  ? -29.65300 4.79900   14.65800  1.000 65.43000  ? 101 SER D OG  1 
ATOM   11419 N  N   . ALA D  1 71  ? -27.42800 7.18100   13.62400  1.000 66.90000  ? 102 ALA D N   1 
ATOM   11420 C  CA  . ALA D  1 71  ? -27.51500 8.61300   13.90500  1.000 66.04000  ? 102 ALA D CA  1 
ATOM   11421 C  C   . ALA D  1 71  ? -27.43400 9.44400   12.62900  1.000 59.46000  ? 102 ALA D C   1 
ATOM   11422 O  O   . ALA D  1 71  ? -28.12000 10.46300  12.51100  1.000 58.49000  ? 102 ALA D O   1 
ATOM   11423 C  CB  . ALA D  1 71  ? -26.40400 9.02200   14.88100  1.000 61.62000  ? 102 ALA D CB  1 
ATOM   11424 N  N   . ILE D  1 72  ? -26.59300 9.03800   11.67200  1.000 59.53000  ? 103 ILE D N   1 
ATOM   11425 C  CA  . ILE D  1 72  ? -26.42600 9.81700   10.44000  1.000 61.29000  ? 103 ILE D CA  1 
ATOM   11426 C  C   . ILE D  1 72  ? -27.72900 9.88600   9.64800   1.000 62.78000  ? 103 ILE D C   1 
ATOM   11427 O  O   . ILE D  1 72  ? -28.14400 10.96000  9.19500   1.000 68.12000  ? 103 ILE D O   1 
ATOM   11428 C  CB  . ILE D  1 72  ? -25.30900 9.21900   9.57300   1.000 56.11000  ? 103 ILE D CB  1 
ATOM   11429 C  CG1 . ILE D  1 72  ? -23.95400 9.48900   10.21800  1.000 64.83000  ? 103 ILE D CG1 1 
ATOM   11430 C  CG2 . ILE D  1 72  ? -25.36200 9.85800   8.20300   1.000 56.27000  ? 103 ILE D CG2 1 
ATOM   11431 C  CD1 . ILE D  1 72  ? -22.84500 8.58600   9.72600   1.000 65.24000  ? 103 ILE D CD1 1 
ATOM   11432 N  N   . LEU D  1 73  ? -28.38400 8.74400   9.44300   1.000 57.63000  ? 104 LEU D N   1 
ATOM   11433 C  CA  . LEU D  1 73  ? -29.55100 8.75500   8.56800   1.000 65.19000  ? 104 LEU D CA  1 
ATOM   11434 C  C   . LEU D  1 73  ? -30.81800 9.16400   9.29900   1.000 62.00000  ? 104 LEU D C   1 
ATOM   11435 O  O   . LEU D  1 73  ? -31.70800 9.75800   8.68300   1.000 61.92000  ? 104 LEU D O   1 
ATOM   11436 C  CB  . LEU D  1 73  ? -29.75400 7.39200   7.87900   1.000 65.09000  ? 104 LEU D CB  1 
ATOM   11437 C  CG  . LEU D  1 73  ? -28.94300 7.14400   6.58800   1.000 60.20000  ? 104 LEU D CG  1 
ATOM   11438 C  CD1 . LEU D  1 73  ? -28.83900 5.67500   6.26900   1.000 60.23000  ? 104 LEU D CD1 1 
ATOM   11439 C  CD2 . LEU D  1 73  ? -29.49400 7.88600   5.39100   1.000 62.10000  ? 104 LEU D CD2 1 
ATOM   11440 N  N   . THR D  1 74  ? -30.91900 8.87900   10.59600  1.000 62.38000  ? 105 THR D N   1 
ATOM   11441 C  CA  . THR D  1 74  ? -32.08700 9.30600   11.35100  1.000 62.95000  ? 105 THR D CA  1 
ATOM   11442 C  C   . THR D  1 74  ? -31.96900 10.72900  11.87000  1.000 64.83000  ? 105 THR D C   1 
ATOM   11443 O  O   . THR D  1 74  ? -32.99700 11.34100  12.18200  1.000 59.39000  ? 105 THR D O   1 
ATOM   11444 C  CB  . THR D  1 74  ? -32.32100 8.39300   12.55400  1.000 66.81000  ? 105 THR D CB  1 
ATOM   11445 O  OG1 . THR D  1 74  ? -31.23800 8.56600   13.48400  1.000 67.97000  ? 105 THR D OG1 1 
ATOM   11446 C  CG2 . THR D  1 74  ? -32.43100 6.93000   12.12700  1.000 62.13000  ? 105 THR D CG2 1 
ATOM   11447 N  N   . GLY D  1 75  ? -30.75300 11.27000  11.96500  1.000 60.18000  ? 106 GLY D N   1 
ATOM   11448 C  CA  . GLY D  1 75  ? -30.58600 12.61500  12.48500  1.000 61.22000  ? 106 GLY D CA  1 
ATOM   11449 C  C   . GLY D  1 75  ? -30.82300 12.76800  13.96900  1.000 60.18000  ? 106 GLY D C   1 
ATOM   11450 O  O   . GLY D  1 75  ? -31.04300 13.88700  14.43500  1.000 58.83000  ? 106 GLY D O   1 
ATOM   11451 N  N   . ARG D  1 76  ? -30.83200 11.67000  14.71900  1.000 53.55000  ? 107 ARG D N   1 
ATOM   11452 C  CA  . ARG D  1 76  ? -31.08400 11.70600  16.15000  1.000 68.36000  ? 107 ARG D CA  1 
ATOM   11453 C  C   . ARG D  1 76  ? -30.00300 10.92400  16.89100  1.000 70.32000  ? 107 ARG D C   1 
ATOM   11454 O  O   . ARG D  1 76  ? -29.42900 9.97200   16.35600  1.000 70.46000  ? 107 ARG D O   1 
ATOM   11455 C  CB  . ARG D  1 76  ? -32.47000 11.13200  16.46900  1.000 65.52000  ? 107 ARG D CB  1 
ATOM   11456 C  CG  . ARG D  1 76  ? -33.64800 12.01200  16.01400  1.000 71.83000  ? 107 ARG D CG  1 
ATOM   11457 C  CD  . ARG D  1 76  ? -34.98400 11.37700  16.43100  1.000 66.82000  ? 107 ARG D CD  1 
ATOM   11458 N  NE  . ARG D  1 76  ? -35.40600 11.76900  17.77300  1.000 74.93000  ? 107 ARG D NE  1 
ATOM   11459 C  CZ  . ARG D  1 76  ? -36.26400 11.08300  18.52300  1.000 82.02000  ? 107 ARG D CZ  1 
ATOM   11460 N  NH1 . ARG D  1 76  ? -36.83900 9.97000   18.08300  1.000 75.34000  ? 107 ARG D NH1 1 
ATOM   11461 N  NH2 . ARG D  1 76  ? -36.54200 11.51300  19.75200  1.000 81.24000  ? 107 ARG D NH2 1 
ATOM   11462 N  N   . TYR D  1 77  ? -29.71400 11.33800  18.12300  1.000 68.68000  ? 108 TYR D N   1 
ATOM   11463 C  CA  . TYR D  1 77  ? -28.81000 10.55300  18.95000  1.000 68.29000  ? 108 TYR D CA  1 
ATOM   11464 C  C   . TYR D  1 77  ? -29.36500 9.14200   19.12800  1.000 66.76000  ? 108 TYR D C   1 
ATOM   11465 O  O   . TYR D  1 77  ? -30.56100 8.97100   19.38700  1.000 71.93000  ? 108 TYR D O   1 
ATOM   11466 C  CB  . TYR D  1 77  ? -28.59900 11.22400  20.31000  1.000 70.89000  ? 108 TYR D CB  1 
ATOM   11467 C  CG  . TYR D  1 77  ? -27.53000 12.31600  20.31500  1.000 72.96000  ? 108 TYR D CG  1 
ATOM   11468 C  CD1 . TYR D  1 77  ? -26.17600 11.99200  20.33000  1.000 68.23000  ? 108 TYR D CD1 1 
ATOM   11469 C  CD2 . TYR D  1 77  ? -27.87700 13.66500  20.27700  1.000 69.43000  ? 108 TYR D CD2 1 
ATOM   11470 C  CE1 . TYR D  1 77  ? -25.19500 12.98700  20.33000  1.000 72.10000  ? 108 TYR D CE1 1 
ATOM   11471 C  CE2 . TYR D  1 77  ? -26.91100 14.65900  20.27500  1.000 66.03000  ? 108 TYR D CE2 1 
ATOM   11472 C  CZ  . TYR D  1 77  ? -25.56900 14.31600  20.30400  1.000 73.06000  ? 108 TYR D CZ  1 
ATOM   11473 O  OH  . TYR D  1 77  ? -24.59700 15.29600  20.29300  1.000 68.44000  ? 108 TYR D OH  1 
ATOM   11474 N  N   . PRO D  1 78  ? -28.52600 8.11500   19.01900  1.000 66.81000  ? 109 PRO D N   1 
ATOM   11475 C  CA  . PRO D  1 78  ? -29.02500 6.74000   19.16600  1.000 70.06000  ? 109 PRO D CA  1 
ATOM   11476 C  C   . PRO D  1 78  ? -29.62600 6.44300   20.53200  1.000 69.74000  ? 109 PRO D C   1 
ATOM   11477 O  O   . PRO D  1 78  ? -30.27100 5.39500   20.68400  1.000 63.97000  ? 109 PRO D O   1 
ATOM   11478 C  CB  . PRO D  1 78  ? -27.77200 5.88600   18.89400  1.000 70.96000  ? 109 PRO D CB  1 
ATOM   11479 C  CG  . PRO D  1 78  ? -26.62300 6.79000   19.24700  1.000 64.09000  ? 109 PRO D CG  1 
ATOM   11480 C  CD  . PRO D  1 78  ? -27.07600 8.14700   18.75700  1.000 67.89000  ? 109 PRO D CD  1 
ATOM   11481 N  N   . HIS D  1 79  ? -29.35600 7.27500   21.54900  1.000 68.83000  ? 110 HIS D N   1 
ATOM   11482 C  CA  . HIS D  1 79  ? -29.99500 7.11200   22.85700  1.000 68.54000  ? 110 HIS D CA  1 
ATOM   11483 C  C   . HIS D  1 79  ? -31.45400 7.54900   22.82400  1.000 65.86000  ? 110 HIS D C   1 
ATOM   11484 O  O   . HIS D  1 79  ? -32.21600 7.23400   23.74600  1.000 70.29000  ? 110 HIS D O   1 
ATOM   11485 C  CB  . HIS D  1 79  ? -29.24600 7.90900   23.92000  1.000 65.48000  ? 110 HIS D CB  1 
ATOM   11486 C  CG  . HIS D  1 79  ? -27.76600 7.94400   23.70900  1.000 70.15000  ? 110 HIS D CG  1 
ATOM   11487 N  ND1 . HIS D  1 79  ? -27.17400 8.73400   22.74300  1.000 68.19000  ? 110 HIS D ND1 1 
ATOM   11488 C  CD2 . HIS D  1 79  ? -26.75900 7.27500   24.32200  1.000 67.14000  ? 110 HIS D CD2 1 
ATOM   11489 C  CE1 . HIS D  1 79  ? -25.86400 8.55700   22.78000  1.000 70.36000  ? 110 HIS D CE1 1 
ATOM   11490 N  NE2 . HIS D  1 79  ? -25.58600 7.68100   23.73100  1.000 65.66000  ? 110 HIS D NE2 1 
ATOM   11491 N  N   . LEU D  1 80  ? -31.84700 8.28500   21.78900  1.000 63.09000  ? 111 LEU D N   1 
ATOM   11492 C  CA  . LEU D  1 80  ? -33.22400 8.69700   21.59000  1.000 71.24000  ? 111 LEU D CA  1 
ATOM   11493 C  C   . LEU D  1 80  ? -33.98500 7.75200   20.67100  1.000 74.97000  ? 111 LEU D C   1 
ATOM   11494 O  O   . LEU D  1 80  ? -35.22000 7.75700   20.68300  1.000 70.95000  ? 111 LEU D O   1 
ATOM   11495 C  CB  . LEU D  1 80  ? -33.27600 10.11300  21.00000  1.000 68.63000  ? 111 LEU D CB  1 
ATOM   11496 C  CG  . LEU D  1 80  ? -33.60400 11.25200  21.96300  1.000 72.63000  ? 111 LEU D CG  1 
ATOM   11497 C  CD1 . LEU D  1 80  ? -32.70600 11.19600  23.19000  1.000 72.39000  ? 111 LEU D CD1 1 
ATOM   11498 C  CD2 . LEU D  1 80  ? -33.49700 12.59100  21.23700  1.000 76.22000  ? 111 LEU D CD2 1 
ATOM   11499 N  N   . THR D  1 81  ? -33.27500 6.94200   19.88700  1.000 68.95000  ? 112 THR D N   1 
ATOM   11500 C  CA  . THR D  1 81  ? -33.89300 6.00500   18.97100  1.000 65.08000  ? 112 THR D CA  1 
ATOM   11501 C  C   . THR D  1 81  ? -33.82200 4.56800   19.46100  1.000 69.01000  ? 112 THR D C   1 
ATOM   11502 O  O   . THR D  1 81  ? -34.40900 3.68500   18.82600  1.000 69.04000  ? 112 THR D O   1 
ATOM   11503 C  CB  . THR D  1 81  ? -33.21000 6.11400   17.61600  1.000 67.90000  ? 112 THR D CB  1 
ATOM   11504 O  OG1 . THR D  1 81  ? -31.82400 5.78500   17.77800  1.000 71.62000  ? 112 THR D OG1 1 
ATOM   11505 C  CG2 . THR D  1 81  ? -33.31500 7.54300   17.11200  1.000 61.81000  ? 112 THR D CG2 1 
ATOM   11506 N  N   . GLY D  1 82  ? -33.12900 4.31800   20.57100  1.000 63.41000  ? 113 GLY D N   1 
ATOM   11507 C  CA  . GLY D  1 82  ? -33.01100 2.97100   21.09200  1.000 64.46000  ? 113 GLY D CA  1 
ATOM   11508 C  C   . GLY D  1 82  ? -31.95100 2.12400   20.43300  1.000 64.81000  ? 113 GLY D C   1 
ATOM   11509 O  O   . GLY D  1 82  ? -31.95400 0.90300   20.61000  1.000 66.22000  ? 113 GLY D O   1 
ATOM   11510 N  N   . THR D  1 83  ? -31.03100 2.73500   19.69200  1.000 61.35000  ? 114 THR D N   1 
ATOM   11511 C  CA  . THR D  1 83  ? -30.09900 2.02100   18.83100  1.000 66.78000  ? 114 THR D CA  1 
ATOM   11512 C  C   . THR D  1 83  ? -28.65100 2.23100   19.26900  1.000 69.88000  ? 114 THR D C   1 
ATOM   11513 O  O   . THR D  1 83  ? -27.73100 2.30000   18.44800  1.000 67.97000  ? 114 THR D O   1 
ATOM   11514 C  CB  . THR D  1 83  ? -30.29200 2.45000   17.37900  1.000 63.74000  ? 114 THR D CB  1 
ATOM   11515 O  OG1 . THR D  1 83  ? -30.16600 3.87200   17.28000  1.000 67.65000  ? 114 THR D OG1 1 
ATOM   11516 C  CG2 . THR D  1 83  ? -31.67700 2.05400   16.90000  1.000 69.59000  ? 114 THR D CG2 1 
ATOM   11517 N  N   . ALA D  1 84  ? -28.42600 2.32800   20.57200  1.000 64.33000  ? 115 ALA D N   1 
ATOM   11518 C  CA  . ALA D  1 84  ? -27.09800 2.63400   21.07500  1.000 67.62000  ? 115 ALA D CA  1 
ATOM   11519 C  C   . ALA D  1 84  ? -26.21100 1.39700   21.22700  1.000 69.74000  ? 115 ALA D C   1 
ATOM   11520 O  O   . ALA D  1 84  ? -25.06400 1.53200   21.66500  1.000 65.95000  ? 115 ALA D O   1 
ATOM   11521 C  CB  . ALA D  1 84  ? -27.20700 3.38500   22.41000  1.000 60.47000  ? 115 ALA D CB  1 
ATOM   11522 N  N   . TYR D  1 85  ? -26.69700 0.20900   20.86700  1.000 66.85000  ? 116 TYR D N   1 
ATOM   11523 C  CA  . TYR D  1 85  ? -25.86500 -0.97700  20.72400  1.000 63.16000  ? 116 TYR D CA  1 
ATOM   11524 C  C   . TYR D  1 85  ? -25.81900 -1.42800  19.26900  1.000 61.99000  ? 116 TYR D C   1 
ATOM   11525 O  O   . TYR D  1 85  ? -26.75300 -1.18900  18.49800  1.000 70.78000  ? 116 TYR D O   1 
ATOM   11526 C  CB  . TYR D  1 85  ? -26.38100 -2.12900  21.58500  1.000 66.92000  ? 116 TYR D CB  1 
ATOM   11527 C  CG  . TYR D  1 85  ? -26.14100 -1.96400  23.06900  1.000 72.22000  ? 116 TYR D CG  1 
ATOM   11528 C  CD1 . TYR D  1 85  ? -24.97900 -2.44800  23.66100  1.000 66.89000  ? 116 TYR D CD1 1 
ATOM   11529 C  CD2 . TYR D  1 85  ? -27.08500 -1.34000  23.88500  1.000 71.36000  ? 116 TYR D CD2 1 
ATOM   11530 C  CE1 . TYR D  1 85  ? -24.76000 -2.31700  25.02800  1.000 70.79000  ? 116 TYR D CE1 1 
ATOM   11531 C  CE2 . TYR D  1 85  ? -26.87300 -1.19800  25.24800  1.000 68.24000  ? 116 TYR D CE2 1 
ATOM   11532 C  CZ  . TYR D  1 85  ? -25.70900 -1.69000  25.81500  1.000 71.49000  ? 116 TYR D CZ  1 
ATOM   11533 O  OH  . TYR D  1 85  ? -25.49300 -1.55600  27.16900  1.000 67.13000  ? 116 TYR D OH  1 
ATOM   11534 N  N   . ASN D  1 86  ? -24.72000 -2.08400  18.90100  1.000 60.24000  ? 117 ASN D N   1 
ATOM   11535 C  CA  . ASN D  1 86  ? -24.60700 -2.70800  17.59000  1.000 57.57000  ? 117 ASN D CA  1 
ATOM   11536 C  C   . ASN D  1 86  ? -25.56600 -3.88500  17.46600  1.000 65.97000  ? 117 ASN D C   1 
ATOM   11537 O  O   . ASN D  1 86  ? -25.83500 -4.60500  18.43500  1.000 61.52000  ? 117 ASN D O   1 
ATOM   11538 C  CB  . ASN D  1 86  ? -23.19200 -3.23300  17.34900  1.000 61.79000  ? 117 ASN D CB  1 
ATOM   11539 C  CG  . ASN D  1 86  ? -22.29000 -2.22800  16.65900  1.000 64.94000  ? 117 ASN D CG  1 
ATOM   11540 O  OD1 . ASN D  1 86  ? -22.74400 -1.22700  16.10100  1.000 61.79000  ? 117 ASN D OD1 1 
ATOM   11541 N  ND2 . ASN D  1 86  ? -20.99400 -2.49600  16.69900  1.000 63.87000  ? 117 ASN D ND2 1 
ATOM   11542 N  N   . LEU D  1 87  ? -26.05900 -4.09800  16.24700  1.000 65.86000  ? 118 LEU D N   1 
ATOM   11543 C  CA  . LEU D  1 87  ? -26.66200 -5.38000  15.90800  1.000 61.74000  ? 118 LEU D CA  1 
ATOM   11544 C  C   . LEU D  1 87  ? -25.57500 -6.44500  15.85100  1.000 59.87000  ? 118 LEU D C   1 
ATOM   11545 O  O   . LEU D  1 87  ? -24.50700 -6.22900  15.26400  1.000 58.57000  ? 118 LEU D O   1 
ATOM   11546 C  CB  . LEU D  1 87  ? -27.38200 -5.27400  14.57100  1.000 62.75000  ? 118 LEU D CB  1 
ATOM   11547 C  CG  . LEU D  1 87  ? -28.60600 -4.35700  14.62300  1.000 64.67000  ? 118 LEU D CG  1 
ATOM   11548 C  CD1 . LEU D  1 87  ? -28.97700 -3.90900  13.23500  1.000 58.03000  ? 118 LEU D CD1 1 
ATOM   11549 C  CD2 . LEU D  1 87  ? -29.78700 -5.06800  15.29700  1.000 65.00000  ? 118 LEU D CD2 1 
ATOM   11550 N  N   . PHE D  1 88  ? -25.84500 -7.59700  16.45700  1.000 58.87000  ? 119 PHE D N   1 
ATOM   11551 C  CA  . PHE D  1 88  ? -24.91500 -8.71800  16.40700  1.000 60.33000  ? 119 PHE D CA  1 
ATOM   11552 C  C   . PHE D  1 88  ? -24.77800 -9.22700  14.96700  1.000 62.14000  ? 119 PHE D C   1 
ATOM   11553 O  O   . PHE D  1 88  ? -25.65600 -9.01600  14.12500  1.000 62.13000  ? 119 PHE D O   1 
ATOM   11554 C  CB  . PHE D  1 88  ? -25.40400 -9.83000  17.33700  1.000 59.37000  ? 119 PHE D CB  1 
ATOM   11555 C  CG  . PHE D  1 88  ? -24.30500 -10.58700 18.02400  1.000 70.22000  ? 119 PHE D CG  1 
ATOM   11556 C  CD1 . PHE D  1 88  ? -23.67200 -10.04500 19.14900  1.000 68.02000  ? 119 PHE D CD1 1 
ATOM   11557 C  CD2 . PHE D  1 88  ? -23.92000 -11.85200 17.57800  1.000 63.28000  ? 119 PHE D CD2 1 
ATOM   11558 C  CE1 . PHE D  1 88  ? -22.66500 -10.74700 19.80800  1.000 65.56000  ? 119 PHE D CE1 1 
ATOM   11559 C  CE2 . PHE D  1 88  ? -22.91100 -12.56200 18.22500  1.000 66.41000  ? 119 PHE D CE2 1 
ATOM   11560 C  CZ  . PHE D  1 88  ? -22.27700 -12.00700 19.34500  1.000 70.61000  ? 119 PHE D CZ  1 
ATOM   11561 N  N   . HIS D  1 89  ? -23.64600 -9.86200  14.66500  1.000 63.51000  ? 120 HIS D N   1 
ATOM   11562 C  CA  . HIS D  1 89  ? -23.47400 -10.41300 13.32800  1.000 65.27000  ? 120 HIS D CA  1 
ATOM   11563 C  C   . HIS D  1 89  ? -24.54400 -11.46600 13.07600  1.000 69.55000  ? 120 HIS D C   1 
ATOM   11564 O  O   . HIS D  1 89  ? -24.99300 -12.15100 14.00000  1.000 65.89000  ? 120 HIS D O   1 
ATOM   11565 C  CB  . HIS D  1 89  ? -22.09400 -11.04200 13.15300  1.000 65.25000  ? 120 HIS D CB  1 
ATOM   11566 C  CG  . HIS D  1 89  ? -21.96800 -12.40400 13.75700  1.000 72.96000  ? 120 HIS D CG  1 
ATOM   11567 N  ND1 . HIS D  1 89  ? -22.06500 -12.63500 15.11300  1.000 73.80000  ? 120 HIS D ND1 1 
ATOM   11568 C  CD2 . HIS D  1 89  ? -21.76000 -13.61300 13.18300  1.000 72.01000  ? 120 HIS D CD2 1 
ATOM   11569 C  CE1 . HIS D  1 89  ? -21.91300 -13.92700 15.34900  1.000 73.19000  ? 120 HIS D CE1 1 
ATOM   11570 N  NE2 . HIS D  1 89  ? -21.73200 -14.54200 14.19400  1.000 74.68000  ? 120 HIS D NE2 1 
ATOM   11571 N  N   . ASN D  1 90  ? -24.97100 -11.57600 11.81500  1.000 68.74000  ? 121 ASN D N   1 
ATOM   11572 C  CA  . ASN D  1 90  ? -26.05400 -12.49200 11.45500  1.000 70.75000  ? 121 ASN D CA  1 
ATOM   11573 C  C   . ASN D  1 90  ? -27.28900 -12.23700 12.31300  1.000 69.33000  ? 121 ASN D C   1 
ATOM   11574 O  O   . ASN D  1 90  ? -27.88100 -13.16600 12.86500  1.000 65.73000  ? 121 ASN D O   1 
ATOM   11575 C  CB  . ASN D  1 90  ? -25.62900 -13.96600 11.54800  1.000 69.62000  ? 121 ASN D CB  1 
ATOM   11576 C  CG  . ASN D  1 90  ? -24.55100 -14.34100 10.54200  1.000 74.26000  ? 121 ASN D CG  1 
ATOM   11577 O  OD1 . ASN D  1 90  ? -23.36700 -14.06500 10.73400  1.000 74.18000  ? 121 ASN D OD1 1 
ATOM   11578 N  ND2 . ASN D  1 90  ? -24.97300 -14.95900 9.43600   1.000 77.32000  ? 121 ASN D ND2 1 
ATOM   11579 N  N   . SER D  1 91  ? -27.62000 -10.95700 12.49600  1.000 65.54000  ? 122 SER D N   1 
ATOM   11580 C  CA  . SER D  1 91  ? -28.80000 -10.55100 13.25400  1.000 70.37000  ? 122 SER D CA  1 
ATOM   11581 C  C   . SER D  1 91  ? -30.08400 -10.96300 12.52900  1.000 69.66000  ? 122 SER D C   1 
ATOM   11582 O  O   . SER D  1 91  ? -30.08100 -11.26900 11.33500  1.000 74.87000  ? 122 SER D O   1 
ATOM   11583 C  CB  . SER D  1 91  ? -28.78500 -9.04000  13.49400  1.000 67.45000  ? 122 SER D CB  1 
ATOM   11584 O  OG  . SER D  1 91  ? -28.80100 -8.32900  12.26800  1.000 67.40000  ? 122 SER D OG  1 
ATOM   11585 N  N   . SER D  1 92  ? -31.20000 -10.93100 13.26500  1.000 75.96000  ? 123 SER D N   1 
ATOM   11586 C  CA  . SER D  1 92  ? -32.46700 -11.47500 12.77400  1.000 77.86000  ? 123 SER D CA  1 
ATOM   11587 C  C   . SER D  1 92  ? -32.90900 -10.84000 11.45900  1.000 78.27000  ? 123 SER D C   1 
ATOM   11588 O  O   . SER D  1 92  ? -32.77600 -9.62900  11.25800  1.000 73.55000  ? 123 SER D O   1 
ATOM   11589 C  CB  . SER D  1 92  ? -33.57900 -11.27600 13.80200  1.000 79.25000  ? 123 SER D CB  1 
ATOM   11590 O  OG  . SER D  1 92  ? -34.83900 -11.58500 13.21400  1.000 81.49000  ? 123 SER D OG  1 
ATOM   11591 N  N   . GLU D  1 93  ? -33.43900 -11.67900 10.56200  1.000 83.10000  ? 124 GLU D N   1 
ATOM   11592 C  CA  . GLU D  1 93  ? -33.96000 -11.24400 9.27100   1.000 81.69000  ? 124 GLU D CA  1 
ATOM   11593 C  C   . GLU D  1 93  ? -35.48700 -11.24900 9.20100   1.000 78.86000  ? 124 GLU D C   1 
ATOM   11594 O  O   . GLU D  1 93  ? -36.04200 -11.02400 8.12300   1.000 84.19000  ? 124 GLU D O   1 
ATOM   11595 C  CB  . GLU D  1 93  ? -33.39100 -12.12700 8.15700   1.000 80.86000  ? 124 GLU D CB  1 
ATOM   11596 C  CG  . GLU D  1 93  ? -31.87600 -12.26800 8.17700   1.000 73.85000  ? 124 GLU D CG  1 
ATOM   11597 C  CD  . GLU D  1 93  ? -31.30300 -12.76600 6.85700   1.000 87.72000  ? 124 GLU D CD  1 
ATOM   11598 O  OE1 . GLU D  1 93  ? -31.98900 -12.65600 5.81700   1.000 87.42000  ? 124 GLU D OE1 1 
ATOM   11599 O  OE2 . GLU D  1 93  ? -30.17500 -13.30800 6.86900   1.000 90.30000  ? 124 GLU D OE2 1 
ATOM   11600 N  N   . ASP D  1 94  ? -36.18200 -11.48000 10.31200  1.000 85.75000  ? 125 ASP D N   1 
ATOM   11601 C  CA  . ASP D  1 94  ? -37.64300 -11.50400 10.33100  1.000 84.72000  ? 125 ASP D CA  1 
ATOM   11602 C  C   . ASP D  1 94  ? -38.19300 -10.19300 10.88500  1.000 82.48000  ? 125 ASP D C   1 
ATOM   11603 O  O   . ASP D  1 94  ? -37.75900 -9.74000  11.94700  1.000 85.83000  ? 125 ASP D O   1 
ATOM   11604 C  CB  . ASP D  1 94  ? -38.16300 -12.68200 11.16300  1.000 86.67000  ? 125 ASP D CB  1 
ATOM   11605 C  CG  . ASP D  1 94  ? -37.84000 -14.04000 10.53900  1.000 92.94000  ? 125 ASP D CG  1 
ATOM   11606 O  OD1 . ASP D  1 94  ? -37.29800 -14.09000 9.40800   1.000 91.75000  ? 125 ASP D OD1 1 
ATOM   11607 O  OD2 . ASP D  1 94  ? -38.13100 -15.06700 11.18900  1.000 95.83000  ? 125 ASP D OD2 1 
ATOM   11608 N  N   . ASP D  1 95  ? -39.14600 -9.58900  10.15900  1.000 81.87000  ? 126 ASP D N   1 
ATOM   11609 C  CA  . ASP D  1 95  ? -39.76100 -8.33200  10.59700  1.000 80.95000  ? 126 ASP D CA  1 
ATOM   11610 C  C   . ASP D  1 95  ? -40.31700 -8.42000  12.01000  1.000 84.42000  ? 126 ASP D C   1 
ATOM   11611 O  O   . ASP D  1 95  ? -40.40900 -7.40000  12.70300  1.000 84.36000  ? 126 ASP D O   1 
ATOM   11612 C  CB  . ASP D  1 95  ? -40.89800 -7.91800  9.65400   1.000 81.35000  ? 126 ASP D CB  1 
ATOM   11613 C  CG  . ASP D  1 95  ? -40.40600 -7.41100  8.31000   1.000 79.74000  ? 126 ASP D CG  1 
ATOM   11614 O  OD1 . ASP D  1 95  ? -39.17500 -7.31900  8.10900   1.000 84.11000  ? 126 ASP D OD1 1 
ATOM   11615 O  OD2 . ASP D  1 95  ? -41.25800 -7.10500  7.45000   1.000 74.01000  ? 126 ASP D OD2 1 
ATOM   11616 N  N   . LYS D  1 96  ? -40.72700 -9.61700  12.44200  1.000 85.48000  ? 127 LYS D N   1 
ATOM   11617 C  CA  . LYS D  1 96  ? -41.30500 -9.75900  13.77400  1.000 86.11000  ? 127 LYS D CA  1 
ATOM   11618 C  C   . LYS D  1 96  ? -40.28300 -9.38300  14.84200  1.000 88.40000  ? 127 LYS D C   1 
ATOM   11619 O  O   . LYS D  1 96  ? -40.58200 -8.62000  15.76900  1.000 84.64000  ? 127 LYS D O   1 
ATOM   11620 C  CB  . LYS D  1 96  ? -41.81800 -11.19100 13.96700  1.000 76.39000  ? 127 LYS D CB  1 
ATOM   11621 N  N   . ASP D  1 97  ? -39.05400 -9.87600  14.69200  1.000 89.04000  ? 128 ASP D N   1 
ATOM   11622 C  CA  . ASP D  1 97  ? -37.91900 -9.50600  15.53400  1.000 84.45000  ? 128 ASP D CA  1 
ATOM   11623 C  C   . ASP D  1 97  ? -37.42300 -8.14600  15.06300  1.000 83.31000  ? 128 ASP D C   1 
ATOM   11624 O  O   . ASP D  1 97  ? -36.67500 -8.04800  14.08700  1.000 86.77000  ? 128 ASP D O   1 
ATOM   11625 C  CB  . ASP D  1 97  ? -36.80600 -10.54500 15.43500  1.000 83.96000  ? 128 ASP D CB  1 
ATOM   11626 C  CG  . ASP D  1 97  ? -37.27900 -11.95000 15.72700  1.000 86.48000  ? 128 ASP D CG  1 
ATOM   11627 O  OD1 . ASP D  1 97  ? -38.06700 -12.12800 16.68000  1.000 93.13000  ? 128 ASP D OD1 1 
ATOM   11628 O  OD2 . ASP D  1 97  ? -36.84300 -12.87700 15.00800  1.000 84.84000  ? 128 ASP D OD2 1 
ATOM   11629 N  N   . ASN D  1 98  ? -37.85000 -7.08400  15.73600  1.000 74.68000  ? 129 ASN D N   1 
ATOM   11630 C  CA  . ASN D  1 98  ? -37.47200 -5.74100  15.32000  1.000 76.32000  ? 129 ASN D CA  1 
ATOM   11631 C  C   . ASN D  1 98  ? -35.98300 -5.44300  15.49300  1.000 78.17000  ? 129 ASN D C   1 
ATOM   11632 O  O   . ASN D  1 98  ? -35.61100 -4.45700  16.13800  1.000 75.28000  ? 129 ASN D O   1 
ATOM   11633 C  CB  . ASN D  1 98  ? -38.32700 -4.72200  16.06300  1.000 81.06000  ? 129 ASN D CB  1 
ATOM   11634 C  CG  . ASN D  1 98  ? -39.77800 -4.82200  15.67600  1.000 88.18000  ? 129 ASN D CG  1 
ATOM   11635 O  OD1 . ASN D  1 98  ? -40.20200 -4.27500  14.65100  1.000 88.72000  ? 129 ASN D OD1 1 
ATOM   11636 N  ND2 . ASN D  1 98  ? -40.54900 -5.55100  16.47400  1.000 91.76000  ? 129 ASN D ND2 1 
ATOM   11637 N  N   . MET D  1 99  ? -35.12700 -6.27700  14.89600  1.000 75.99000  ? 130 MET D N   1 
ATOM   11638 C  CA  . MET D  1 99  ? -33.67400 -6.09300  14.94300  1.000 74.22000  ? 130 MET D CA  1 
ATOM   11639 C  C   . MET D  1 99  ? -33.25400 -5.14000  13.82000  1.000 69.94000  ? 130 MET D C   1 
ATOM   11640 O  O   . MET D  1 99  ? -32.63200 -5.52300  12.82700  1.000 68.06000  ? 130 MET D O   1 
ATOM   11641 C  CB  . MET D  1 99  ? -32.96800 -7.43800  14.81500  1.000 68.84000  ? 130 MET D CB  1 
ATOM   11642 C  CG  . MET D  1 99  ? -33.01600 -8.32600  16.04600  1.000 72.25000  ? 130 MET D CG  1 
ATOM   11643 S  SD  . MET D  1 99  ? -32.43200 -7.50100  17.54400  1.000 85.16000  ? 130 MET D SD  1 
ATOM   11644 C  CE  . MET D  1 99  ? -32.89800 -8.70800  18.79800  1.000 77.76000  ? 130 MET D CE  1 
ATOM   11645 N  N   . GLY D  1 100 ? -33.60700 -3.87100  14.00500  1.000 64.76000  ? 131 GLY D N   1 
ATOM   11646 C  CA  . GLY D  1 100 ? -33.30500 -2.83800  13.02800  1.000 65.64000  ? 131 GLY D CA  1 
ATOM   11647 C  C   . GLY D  1 100 ? -33.77900 -1.49800  13.54900  1.000 67.79000  ? 131 GLY D C   1 
ATOM   11648 O  O   . GLY D  1 100 ? -34.51700 -1.41400  14.53700  1.000 70.43000  ? 131 GLY D O   1 
ATOM   11649 N  N   . VAL D  1 101 ? -33.31900 -0.44100  12.88300  1.000 68.11000  ? 132 VAL D N   1 
ATOM   11650 C  CA  . VAL D  1 101 ? -33.67400 0.92100   13.31300  1.000 68.33000  ? 132 VAL D CA  1 
ATOM   11651 C  C   . VAL D  1 101 ? -35.17600 1.12400   13.15700  1.000 69.53000  ? 132 VAL D C   1 
ATOM   11652 O  O   . VAL D  1 101 ? -35.72600 0.81900   12.08000  1.000 71.61000  ? 132 VAL D O   1 
ATOM   11653 C  CB  . VAL D  1 101 ? -32.89800 1.97300   12.50400  1.000 65.88000  ? 132 VAL D CB  1 
ATOM   11654 C  CG1 . VAL D  1 101 ? -33.23000 3.37600   12.99700  1.000 63.42000  ? 132 VAL D CG1 1 
ATOM   11655 C  CG2 . VAL D  1 101 ? -31.40000 1.72800   12.57200  1.000 66.12000  ? 132 VAL D CG2 1 
ATOM   11656 N  N   . PRO D  1 102 ? -35.88800 1.65000   14.18300  1.000 73.11000  ? 133 PRO D N   1 
ATOM   11657 C  CA  . PRO D  1 102 ? -37.34500 1.83600   14.07000  1.000 66.18000  ? 133 PRO D CA  1 
ATOM   11658 C  C   . PRO D  1 102 ? -37.76700 2.43800   12.74300  1.000 72.18000  ? 133 PRO D C   1 
ATOM   11659 O  O   . PRO D  1 102 ? -37.17700 3.42100   12.27200  1.000 66.14000  ? 133 PRO D O   1 
ATOM   11660 C  CB  . PRO D  1 102 ? -37.67100 2.78000   15.23000  1.000 67.04000  ? 133 PRO D CB  1 
ATOM   11661 C  CG  . PRO D  1 102 ? -36.59700 2.52300   16.24500  1.000 69.13000  ? 133 PRO D CG  1 
ATOM   11662 C  CD  . PRO D  1 102 ? -35.38000 2.00600   15.52100  1.000 67.05000  ? 133 PRO D CD  1 
ATOM   11663 N  N   . VAL D  1 103 ? -38.77800 1.82000   12.12400  1.000 72.06000  ? 134 VAL D N   1 
ATOM   11664 C  CA  . VAL D  1 103 ? -39.21600 2.23600   10.80000  1.000 68.65000  ? 134 VAL D CA  1 
ATOM   11665 C  C   . VAL D  1 103 ? -39.97900 3.55000   10.84500  1.000 67.39000  ? 134 VAL D C   1 
ATOM   11666 O  O   . VAL D  1 103 ? -40.02600 4.27100   9.83900   1.000 67.43000  ? 134 VAL D O   1 
ATOM   11667 C  CB  . VAL D  1 103 ? -40.03600 1.09300   10.18000  1.000 72.09000  ? 134 VAL D CB  1 
ATOM   11668 C  CG1 . VAL D  1 103 ? -41.09300 0.60900   11.16800  1.000 73.20000  ? 134 VAL D CG1 1 
ATOM   11669 C  CG2 . VAL D  1 103 ? -40.63100 1.50400   8.84600   1.000 77.38000  ? 134 VAL D CG2 1 
ATOM   11670 N  N   . GLU D  1 104 ? -40.51100 3.92300   12.01400  1.000 71.61000  ? 135 GLU D N   1 
ATOM   11671 C  CA  . GLU D  1 104 ? -41.19600 5.20600   12.13600  1.000 72.87000  ? 135 GLU D CA  1 
ATOM   11672 C  C   . GLU D  1 104 ? -40.22800 6.38100   12.08000  1.000 68.11000  ? 135 GLU D C   1 
ATOM   11673 O  O   . GLU D  1 104 ? -40.63000 7.48900   11.69600  1.000 67.30000  ? 135 GLU D O   1 
ATOM   11674 C  CB  . GLU D  1 104 ? -41.99400 5.24300   13.44200  1.000 69.39000  ? 135 GLU D CB  1 
ATOM   11675 N  N   . GLU D  1 105 ? -38.95600 6.15100   12.40400  1.000 75.13000  ? 136 GLU D N   1 
ATOM   11676 C  CA  . GLU D  1 105 ? -37.93500 7.19500   12.36900  1.000 74.63000  ? 136 GLU D CA  1 
ATOM   11677 C  C   . GLU D  1 105 ? -37.51200 7.37700   10.92600  1.000 70.33000  ? 136 GLU D C   1 
ATOM   11678 O  O   . GLU D  1 105 ? -36.70300 6.61300   10.39600  1.000 74.32000  ? 136 GLU D O   1 
ATOM   11679 C  CB  . GLU D  1 105 ? -36.75700 6.82700   13.26400  1.000 72.14000  ? 136 GLU D CB  1 
ATOM   11680 C  CG  . GLU D  1 105 ? -35.81900 7.98600   13.61100  1.000 72.26000  ? 136 GLU D CG  1 
ATOM   11681 C  CD  . GLU D  1 105 ? -36.51200 9.16400   14.26900  1.000 66.21000  ? 136 GLU D CD  1 
ATOM   11682 O  OE1 . GLU D  1 105 ? -36.95500 9.01400   15.42700  1.000 71.76000  ? 136 GLU D OE1 1 
ATOM   11683 O  OE2 . GLU D  1 105 ? -36.54700 10.25200  13.64600  1.000 63.11000  ? 136 GLU D OE2 1 
ATOM   11684 N  N   . THR D  1 106 ? -38.05500 8.40300   10.29000  1.000 66.51000  ? 137 THR D N   1 
ATOM   11685 C  CA  . THR D  1 106 ? -37.89600 8.55200   8.85300   1.000 70.90000  ? 137 THR D CA  1 
ATOM   11686 C  C   . THR D  1 106 ? -36.46400 8.96200   8.53100   1.000 68.49000  ? 137 THR D C   1 
ATOM   11687 O  O   . THR D  1 106 ? -35.94800 9.93800   9.08500   1.000 69.51000  ? 137 THR D O   1 
ATOM   11688 C  CB  . THR D  1 106 ? -38.91400 9.57200   8.34300   1.000 70.43000  ? 137 THR D CB  1 
ATOM   11689 O  OG1 . THR D  1 106 ? -40.19400 9.24900   8.90400   1.000 75.70000  ? 137 THR D OG1 1 
ATOM   11690 C  CG2 . THR D  1 106 ? -39.02700 9.55100   6.81700   1.000 59.69000  ? 137 THR D CG2 1 
ATOM   11691 N  N   . TYR D  1 107 ? -35.81700 8.19500   7.64900   1.000 67.72000  ? 138 TYR D N   1 
ATOM   11692 C  CA  . TYR D  1 107 ? -34.45600 8.50000   7.21700   1.000 67.06000  ? 138 TYR D CA  1 
ATOM   11693 C  C   . TYR D  1 107 ? -34.44900 9.70200   6.29000   1.000 62.68000  ? 138 TYR D C   1 
ATOM   11694 O  O   . TYR D  1 107 ? -35.42900 9.97900   5.59900   1.000 64.44000  ? 138 TYR D O   1 
ATOM   11695 C  CB  . TYR D  1 107 ? -33.82400 7.32200   6.47700   1.000 62.32000  ? 138 TYR D CB  1 
ATOM   11696 C  CG  . TYR D  1 107 ? -33.48100 6.13900   7.32700   1.000 62.19000  ? 138 TYR D CG  1 
ATOM   11697 C  CD1 . TYR D  1 107 ? -33.82900 6.09800   8.65700   1.000 61.99000  ? 138 TYR D CD1 1 
ATOM   11698 C  CD2 . TYR D  1 107 ? -32.78800 5.06300   6.79500   1.000 61.15000  ? 138 TYR D CD2 1 
ATOM   11699 C  CE1 . TYR D  1 107 ? -33.53000 5.02100   9.43200   1.000 60.58000  ? 138 TYR D CE1 1 
ATOM   11700 C  CE2 . TYR D  1 107 ? -32.46700 3.98300   7.57000   1.000 56.88000  ? 138 TYR D CE2 1 
ATOM   11701 C  CZ  . TYR D  1 107 ? -32.85300 3.96300   8.88900   1.000 59.87000  ? 138 TYR D CZ  1 
ATOM   11702 O  OH  . TYR D  1 107 ? -32.55300 2.88400   9.69100   1.000 62.48000  ? 138 TYR D OH  1 
ATOM   11703 N  N   . MET D  1 108 ? -33.32300 10.41300  6.27000   1.000 63.51000  ? 139 MET D N   1 
ATOM   11704 C  CA  . MET D  1 108 ? -33.19500 11.54100  5.35800   1.000 63.07000  ? 139 MET D CA  1 
ATOM   11705 C  C   . MET D  1 108 ? -33.18800 11.09300  3.91000   1.000 60.50000  ? 139 MET D C   1 
ATOM   11706 O  O   . MET D  1 108 ? -33.44100 11.91200  3.02700   1.000 67.27000  ? 139 MET D O   1 
ATOM   11707 C  CB  . MET D  1 108 ? -31.92700 12.35200  5.64500   1.000 68.83000  ? 139 MET D CB  1 
ATOM   11708 C  CG  . MET D  1 108 ? -30.61700 11.58800  5.44900   1.000 66.04000  ? 139 MET D CG  1 
ATOM   11709 S  SD  . MET D  1 108 ? -29.14500 12.62700  5.64400   1.000 76.29000  ? 139 MET D SD  1 
ATOM   11710 C  CE  . MET D  1 108 ? -27.85300 11.40200  5.76900   1.000 72.33000  ? 139 MET D CE  1 
ATOM   11711 N  N   . SER D  1 109 ? -32.87900 9.82300   3.64300   1.000 65.15000  ? 140 SER D N   1 
ATOM   11712 C  CA  . SER D  1 109 ? -32.94200 9.32400   2.27000   1.000 67.00000  ? 140 SER D CA  1 
ATOM   11713 C  C   . SER D  1 109 ? -34.37100 9.34400   1.74000   1.000 69.69000  ? 140 SER D C   1 
ATOM   11714 O  O   . SER D  1 109 ? -34.61200 9.77500   0.60300   1.000 63.22000  ? 140 SER D O   1 
ATOM   11715 C  CB  . SER D  1 109 ? -32.36500 7.90800   2.19700   1.000 63.74000  ? 140 SER D CB  1 
ATOM   11716 O  OG  . SER D  1 109 ? -32.81900 7.12200   3.29000   1.000 67.33000  ? 140 SER D OG  1 
ATOM   11717 N  N   . LYS D  1 110 ? -35.33700 8.91000   2.56300   1.000 66.06000  ? 141 LYS D N   1 
ATOM   11718 C  CA  . LYS D  1 110 ? -36.73400 8.93300   2.13900   1.000 70.34000  ? 141 LYS D CA  1 
ATOM   11719 C  C   . LYS D  1 110 ? -37.19700 10.35700  1.88000   1.000 71.44000  ? 141 LYS D C   1 
ATOM   11720 O  O   . LYS D  1 110 ? -37.84000 10.63200  0.85700   1.000 74.66000  ? 141 LYS D O   1 
ATOM   11721 C  CB  . LYS D  1 110 ? -37.62300 8.26200   3.19000   1.000 74.54000  ? 141 LYS D CB  1 
ATOM   11722 N  N   . VAL D  1 111 ? -36.83000 11.28200  2.77500   1.000 70.95000  ? 142 VAL D N   1 
ATOM   11723 C  CA  . VAL D  1 111 ? -37.21000 12.68700  2.62600   1.000 74.50000  ? 142 VAL D CA  1 
ATOM   11724 C  C   . VAL D  1 111 ? -36.72600 13.23300  1.28900   1.000 66.42000  ? 142 VAL D C   1 
ATOM   11725 O  O   . VAL D  1 111 ? -37.47400 13.89500  0.55800   1.000 63.48000  ? 142 VAL D O   1 
ATOM   11726 C  CB  . VAL D  1 111 ? -36.66600 13.51800  3.80500   1.000 65.90000  ? 142 VAL D CB  1 
ATOM   11727 C  CG1 . VAL D  1 111 ? -36.96900 14.98500  3.59800   1.000 66.60000  ? 142 VAL D CG1 1 
ATOM   11728 C  CG2 . VAL D  1 111 ? -37.27300 13.04100  5.10600   1.000 66.70000  ? 142 VAL D CG2 1 
ATOM   11729 N  N   . LEU D  1 112 ? -35.46700 12.95900  0.94700   1.000 67.08000  ? 143 LEU D N   1 
ATOM   11730 C  CA  . LEU D  1 112 ? -34.94300 13.43200  -0.33000  1.000 69.45000  ? 143 LEU D CA  1 
ATOM   11731 C  C   . LEU D  1 112 ? -35.61300 12.71800  -1.48600  1.000 66.27000  ? 143 LEU D C   1 
ATOM   11732 O  O   . LEU D  1 112 ? -35.84000 13.31600  -2.54500  1.000 68.84000  ? 143 LEU D O   1 
ATOM   11733 C  CB  . LEU D  1 112 ? -33.43000 13.23500  -0.39900  1.000 74.34000  ? 143 LEU D CB  1 
ATOM   11734 C  CG  . LEU D  1 112 ? -32.53600 14.32600  0.18600   1.000 64.94000  ? 143 LEU D CG  1 
ATOM   11735 C  CD1 . LEU D  1 112 ? -32.86000 14.52200  1.63200   1.000 63.13000  ? 143 LEU D CD1 1 
ATOM   11736 C  CD2 . LEU D  1 112 ? -31.07400 13.93800  0.02200   1.000 68.40000  ? 143 LEU D CD2 1 
ATOM   11737 N  N   . GLN D  1 113 ? -35.92500 11.43300  -1.30300  1.000 65.56000  ? 144 GLN D N   1 
ATOM   11738 C  CA  . GLN D  1 113 ? -36.61900 10.69200  -2.34800  1.000 70.50000  ? 144 GLN D CA  1 
ATOM   11739 C  C   . GLN D  1 113 ? -37.99900 11.28500  -2.58600  1.000 68.44000  ? 144 GLN D C   1 
ATOM   11740 O  O   . GLN D  1 113 ? -38.35900 11.61400  -3.72300  1.000 66.82000  ? 144 GLN D O   1 
ATOM   11741 C  CB  . GLN D  1 113 ? -36.72100 9.21600   -1.97300  1.000 69.24000  ? 144 GLN D CB  1 
ATOM   11742 C  CG  . GLN D  1 113 ? -37.35600 8.38300   -3.04900  1.000 69.85000  ? 144 GLN D CG  1 
ATOM   11743 C  CD  . GLN D  1 113 ? -37.47500 6.93500   -2.66500  1.000 68.54000  ? 144 GLN D CD  1 
ATOM   11744 O  OE1 . GLN D  1 113 ? -38.17700 6.58300   -1.70900  1.000 71.66000  ? 144 GLN D OE1 1 
ATOM   11745 N  NE2 . GLN D  1 113 ? -36.77600 6.08000   -3.39800  1.000 66.33000  ? 144 GLN D NE2 1 
ATOM   11746 N  N   . ASN D  1 114 ? -38.76500 11.48300  -1.50600  1.000 66.99000  ? 145 ASN D N   1 
ATOM   11747 C  CA  . ASN D  1 114 ? -40.08600 12.09300  -1.61200  1.000 64.32000  ? 145 ASN D CA  1 
ATOM   11748 C  C   . ASN D  1 114 ? -40.02800 13.51900  -2.10700  1.000 61.95000  ? 145 ASN D C   1 
ATOM   11749 O  O   . ASN D  1 114 ? -41.07200 14.08200  -2.44300  1.000 63.46000  ? 145 ASN D O   1 
ATOM   11750 C  CB  . ASN D  1 114 ? -40.78100 12.09000  -0.26200  1.000 68.80000  ? 145 ASN D CB  1 
ATOM   11751 C  CG  . ASN D  1 114 ? -41.13700 10.70600  0.19100   1.000 77.87000  ? 145 ASN D CG  1 
ATOM   11752 O  OD1 . ASN D  1 114 ? -41.17000 9.76600   -0.61400  1.000 78.94000  ? 145 ASN D OD1 1 
ATOM   11753 N  ND2 . ASN D  1 114 ? -41.41500 10.56100  1.48400   1.000 77.32000  ? 145 ASN D ND2 1 
ATOM   11754 N  N   . ALA D  1 115 ? -38.84300 14.11900  -2.13400  1.000 65.54000  ? 146 ALA D N   1 
ATOM   11755 C  CA  . ALA D  1 115 ? -38.64000 15.45700  -2.65500  1.000 62.31000  ? 146 ALA D CA  1 
ATOM   11756 C  C   . ALA D  1 115 ? -38.02100 15.43800  -4.04300  1.000 64.67000  ? 146 ALA D C   1 
ATOM   11757 O  O   . ALA D  1 115 ? -37.48600 16.45500  -4.49300  1.000 66.56000  ? 146 ALA D O   1 
ATOM   11758 C  CB  . ALA D  1 115 ? -37.78200 16.27200  -1.69100  1.000 66.76000  ? 146 ALA D CB  1 
ATOM   11759 N  N   . GLY D  1 116 ? -38.04500 14.28900  -4.70900  1.000 66.62000  ? 147 GLY D N   1 
ATOM   11760 C  CA  . GLY D  1 116 ? -37.62800 14.20900  -6.09000  1.000 59.88000  ? 147 GLY D CA  1 
ATOM   11761 C  C   . GLY D  1 116 ? -36.17400 13.89400  -6.34200  1.000 68.82000  ? 147 GLY D C   1 
ATOM   11762 O  O   . GLY D  1 116 ? -35.71800 14.06200  -7.48200  1.000 66.18000  ? 147 GLY D O   1 
ATOM   11763 N  N   . TYR D  1 117 ? -35.42300 13.45000  -5.33400  1.000 65.81000  ? 148 TYR D N   1 
ATOM   11764 C  CA  . TYR D  1 117 ? -34.03500 13.08200  -5.56600  1.000 70.51000  ? 148 TYR D CA  1 
ATOM   11765 C  C   . TYR D  1 117 ? -33.95600 11.62800  -6.00500  1.000 67.27000  ? 148 TYR D C   1 
ATOM   11766 O  O   . TYR D  1 117 ? -34.69200 10.77300  -5.50000  1.000 64.37000  ? 148 TYR D O   1 
ATOM   11767 C  CB  . TYR D  1 117 ? -33.18000 13.29400  -4.31300  1.000 71.96000  ? 148 TYR D CB  1 
ATOM   11768 C  CG  . TYR D  1 117 ? -32.56300 14.66700  -4.20700  1.000 71.58000  ? 148 TYR D CG  1 
ATOM   11769 C  CD1 . TYR D  1 117 ? -33.34600 15.77600  -3.93400  1.000 73.64000  ? 148 TYR D CD1 1 
ATOM   11770 C  CD2 . TYR D  1 117 ? -31.19800 14.85900  -4.38300  1.000 77.49000  ? 148 TYR D CD2 1 
ATOM   11771 C  CE1 . TYR D  1 117 ? -32.79200 17.04500  -3.83900  1.000 75.86000  ? 148 TYR D CE1 1 
ATOM   11772 C  CE2 . TYR D  1 117 ? -30.63000 16.12800  -4.28900  1.000 75.84000  ? 148 TYR D CE2 1 
ATOM   11773 C  CZ  . TYR D  1 117 ? -31.43600 17.21800  -4.01300  1.000 72.51000  ? 148 TYR D CZ  1 
ATOM   11774 O  OH  . TYR D  1 117 ? -30.90600 18.48300  -3.91100  1.000 68.61000  ? 148 TYR D OH  1 
ATOM   11775 N  N   . TYR D  1 118 ? -33.03500 11.35200  -6.92900  1.000 64.40000  ? 149 TYR D N   1 
ATOM   11776 C  CA  . TYR D  1 118 ? -32.64300 9.97900   -7.22900  1.000 68.94000  ? 149 TYR D CA  1 
ATOM   11777 C  C   . TYR D  1 118 ? -31.70100 9.47600   -6.13600  1.000 66.06000  ? 149 TYR D C   1 
ATOM   11778 O  O   . TYR D  1 118 ? -30.59500 9.99700   -5.98400  1.000 65.83000  ? 149 TYR D O   1 
ATOM   11779 C  CB  . TYR D  1 118 ? -31.95900 9.90600   -8.59100  1.000 63.47000  ? 149 TYR D CB  1 
ATOM   11780 C  CG  . TYR D  1 118 ? -31.38500 8.54500   -8.85800  1.000 65.45000  ? 149 TYR D CG  1 
ATOM   11781 C  CD1 . TYR D  1 118 ? -32.20900 7.47800   -9.19700  1.000 72.35000  ? 149 TYR D CD1 1 
ATOM   11782 C  CD2 . TYR D  1 118 ? -30.02500 8.31300   -8.75300  1.000 65.28000  ? 149 TYR D CD2 1 
ATOM   11783 C  CE1 . TYR D  1 118 ? -31.68700 6.21500   -9.42800  1.000 69.83000  ? 149 TYR D CE1 1 
ATOM   11784 C  CE2 . TYR D  1 118 ? -29.49400 7.05600   -8.98300  1.000 64.52000  ? 149 TYR D CE2 1 
ATOM   11785 C  CZ  . TYR D  1 118 ? -30.32700 6.01300   -9.31800  1.000 69.58000  ? 149 TYR D CZ  1 
ATOM   11786 O  OH  . TYR D  1 118 ? -29.80000 4.76300   -9.55200  1.000 70.07000  ? 149 TYR D OH  1 
ATOM   11787 N  N   . THR D  1 119 ? -32.12700 8.45600   -5.39100  1.000 59.11000  ? 150 THR D N   1 
ATOM   11788 C  CA  . THR D  1 119 ? -31.41900 8.00200   -4.20200  1.000 67.38000  ? 150 THR D CA  1 
ATOM   11789 C  C   . THR D  1 119 ? -30.77400 6.63700   -4.42100  1.000 69.63000  ? 150 THR D C   1 
ATOM   11790 O  O   . THR D  1 119 ? -31.35600 5.75300   -5.06000  1.000 68.12000  ? 150 THR D O   1 
ATOM   11791 C  CB  . THR D  1 119 ? -32.36500 7.94900   -3.00200  1.000 68.38000  ? 150 THR D CB  1 
ATOM   11792 O  OG1 . THR D  1 119 ? -33.44200 7.04500   -3.26600  1.000 62.71000  ? 150 THR D OG1 1 
ATOM   11793 C  CG2 . THR D  1 119 ? -32.93600 9.33300   -2.71700  1.000 66.37000  ? 150 THR D CG2 1 
ATOM   11794 N  N   . SER D  1 120 ? -29.56100 6.47800   -3.89200  1.000 64.02000  ? 151 SER D N   1 
ATOM   11795 C  CA  . SER D  1 120 ? -28.77400 5.26500   -4.07600  1.000 62.83000  ? 151 SER D CA  1 
ATOM   11796 C  C   . SER D  1 120 ? -27.89600 5.03800   -2.86100  1.000 60.30000  ? 151 SER D C   1 
ATOM   11797 O  O   . SER D  1 120 ? -27.23900 5.97200   -2.40100  1.000 63.31000  ? 151 SER D O   1 
ATOM   11798 C  CB  . SER D  1 120 ? -27.88900 5.34600   -5.31500  1.000 66.98000  ? 151 SER D CB  1 
ATOM   11799 O  OG  . SER D  1 120 ? -26.75900 4.49900   -5.15000  1.000 69.42000  ? 151 SER D OG  1 
ATOM   11800 N  N   . ALA D  1 121 ? -27.87600 3.80000   -2.37000  1.000 58.27000  ? 152 ALA D N   1 
ATOM   11801 C  CA  . ALA D  1 121 ? -27.01600 3.36800   -1.27900  1.000 60.59000  ? 152 ALA D CA  1 
ATOM   11802 C  C   . ALA D  1 121 ? -26.10800 2.25700   -1.78200  1.000 61.82000  ? 152 ALA D C   1 
ATOM   11803 O  O   . ALA D  1 121 ? -26.57200 1.32200   -2.43600  1.000 63.88000  ? 152 ALA D O   1 
ATOM   11804 C  CB  . ALA D  1 121 ? -27.82700 2.88600   -0.07300  1.000 57.45000  ? 152 ALA D CB  1 
ATOM   11805 N  N   . ILE D  1 122 ? -24.82300 2.35600   -1.45600  1.000 63.18000  ? 153 ILE D N   1 
ATOM   11806 C  CA  . ILE D  1 122 ? -23.79800 1.43900   -1.92700  1.000 58.49000  ? 153 ILE D CA  1 
ATOM   11807 C  C   . ILE D  1 122 ? -22.93400 1.00700   -0.74600  1.000 59.50000  ? 153 ILE D C   1 
ATOM   11808 O  O   . ILE D  1 122 ? -22.57800 1.83200   0.10000   1.000 57.52000  ? 153 ILE D O   1 
ATOM   11809 C  CB  . ILE D  1 122 ? -22.92400 2.10800   -2.99800  1.000 56.73000  ? 153 ILE D CB  1 
ATOM   11810 C  CG1 . ILE D  1 122 ? -23.79600 2.58100   -4.16500  1.000 60.68000  ? 153 ILE D CG1 1 
ATOM   11811 C  CG2 . ILE D  1 122 ? -21.80000 1.15200   -3.42300  1.000 58.97000  ? 153 ILE D CG2 1 
ATOM   11812 C  CD1 . ILE D  1 122 ? -23.12000 3.59400   -5.06100  1.000 61.35000  ? 153 ILE D CD1 1 
ATOM   11813 N  N   . GLY D  1 123 ? -22.60500 -0.28300  -0.68400  1.000 57.29000  ? 154 GLY D N   1 
ATOM   11814 C  CA  . GLY D  1 123 ? -21.66500 -0.78100  0.30900   1.000 55.46000  ? 154 GLY D CA  1 
ATOM   11815 C  C   . GLY D  1 123 ? -22.35800 -1.24700  1.57700   1.000 62.56000  ? 154 GLY D C   1 
ATOM   11816 O  O   . GLY D  1 123 ? -23.33800 -1.99200  1.51700   1.000 64.13000  ? 154 GLY D O   1 
ATOM   11817 N  N   . LYS D  1 124 ? -21.84500 -0.80000  2.72600   1.000 53.99000  ? 155 LYS D N   1 
ATOM   11818 C  CA  . LYS D  1 124 ? -22.25600 -1.30600  4.03400   1.000 60.82000  ? 155 LYS D CA  1 
ATOM   11819 C  C   . LYS D  1 124 ? -23.55800 -0.65300  4.49100   1.000 56.83000  ? 155 LYS D C   1 
ATOM   11820 O  O   . LYS D  1 124 ? -23.78100 0.53600   4.26500   1.000 61.40000  ? 155 LYS D O   1 
ATOM   11821 C  CB  . LYS D  1 124 ? -21.14100 -1.04800  5.06000   1.000 58.38000  ? 155 LYS D CB  1 
ATOM   11822 C  CG  . LYS D  1 124 ? -21.52800 -1.12700  6.54700   1.000 57.52000  ? 155 LYS D CG  1 
ATOM   11823 C  CD  . LYS D  1 124 ? -20.28500 -0.97700  7.44000   1.000 55.57000  ? 155 LYS D CD  1 
ATOM   11824 C  CE  . LYS D  1 124 ? -20.63900 -0.98000  8.93300   1.000 56.48000  ? 155 LYS D CE  1 
ATOM   11825 N  NZ  . LYS D  1 124 ? -19.42700 -1.06900  9.81600   1.000 55.04000  ? 155 LYS D NZ  1 
ATOM   11826 N  N   . TRP D  1 125 ? -24.42000 -1.44400  5.13700   1.000 55.72000  ? 156 TRP D N   1 
ATOM   11827 C  CA  . TRP D  1 125 ? -25.69900 -0.96700  5.66500   1.000 60.45000  ? 156 TRP D CA  1 
ATOM   11828 C  C   . TRP D  1 125 ? -25.69600 -0.95600  7.19100   1.000 61.81000  ? 156 TRP D C   1 
ATOM   11829 O  O   . TRP D  1 125 ? -25.50000 0.09200   7.82000   1.000 64.16000  ? 156 TRP D O   1 
ATOM   11830 C  CB  . TRP D  1 125 ? -26.83900 -1.84400  5.13400   1.000 63.65000  ? 156 TRP D CB  1 
ATOM   11831 C  CG  . TRP D  1 125 ? -28.22900 -1.37800  5.47300   1.000 63.45000  ? 156 TRP D CG  1 
ATOM   11832 C  CD1 . TRP D  1 125 ? -29.17700 -2.06800  6.18400   1.000 63.98000  ? 156 TRP D CD1 1 
ATOM   11833 C  CD2 . TRP D  1 125 ? -28.83200 -0.12600  5.11100   1.000 58.24000  ? 156 TRP D CD2 1 
ATOM   11834 N  NE1 . TRP D  1 125 ? -30.33100 -1.32100  6.28300   1.000 60.16000  ? 156 TRP D NE1 1 
ATOM   11835 C  CE2 . TRP D  1 125 ? -30.14200 -0.12500  5.63700   1.000 56.97000  ? 156 TRP D CE2 1 
ATOM   11836 C  CE3 . TRP D  1 125 ? -28.39000 0.99400   4.40300   1.000 56.44000  ? 156 TRP D CE3 1 
ATOM   11837 C  CZ2 . TRP D  1 125 ? -31.01000 0.94800   5.47100   1.000 54.33000  ? 156 TRP D CZ2 1 
ATOM   11838 C  CZ3 . TRP D  1 125 ? -29.25700 2.05800   4.23800   1.000 57.75000  ? 156 TRP D CZ3 1 
ATOM   11839 C  CH2 . TRP D  1 125 ? -30.55100 2.02600   4.76700   1.000 54.37000  ? 156 TRP D CH2 1 
ATOM   11840 N  N   . HIS D  1 126 ? -25.94700 -2.11900  7.78400   1.000 58.40000  ? 157 HIS D N   1 
ATOM   11841 C  CA  . HIS D  1 126 ? -25.89900 -2.34900  9.22500   1.000 61.38000  ? 157 HIS D CA  1 
ATOM   11842 C  C   . HIS D  1 126 ? -27.01100 -1.63500  9.98400   1.000 60.39000  ? 157 HIS D C   1 
ATOM   11843 O  O   . HIS D  1 126 ? -26.88700 -1.41000  11.18800  1.000 57.16000  ? 157 HIS D O   1 
ATOM   11844 C  CB  . HIS D  1 126 ? -24.54100 -1.96200  9.82100   1.000 52.28000  ? 157 HIS D CB  1 
ATOM   11845 C  CG  . HIS D  1 126 ? -24.22100 -2.71500  11.06600  1.000 55.31000  ? 157 HIS D CG  1 
ATOM   11846 N  ND1 . HIS D  1 126 ? -23.18300 -2.37400  11.90500  1.000 60.52000  ? 157 HIS D ND1 1 
ATOM   11847 C  CD2 . HIS D  1 126 ? -24.82100 -3.79400  11.62500  1.000 57.53000  ? 157 HIS D CD2 1 
ATOM   11848 C  CE1 . HIS D  1 126 ? -23.14800 -3.22000  12.92100  1.000 62.17000  ? 157 HIS D CE1 1 
ATOM   11849 N  NE2 . HIS D  1 126 ? -24.13300 -4.09000  12.77600  1.000 59.85000  ? 157 HIS D NE2 1 
ATOM   11850 N  N   . LEU D  1 127 ? -28.11200 -1.30900  9.31100   1.000 54.14000  ? 158 LEU D N   1 
ATOM   11851 C  CA  . LEU D  1 127 ? -29.26400 -0.66600  9.93400   1.000 63.22000  ? 158 LEU D CA  1 
ATOM   11852 C  C   . LEU D  1 127 ? -30.47700 -1.59500  9.99700   1.000 65.92000  ? 158 LEU D C   1 
ATOM   11853 O  O   . LEU D  1 127 ? -31.60700 -1.13000  10.18500  1.000 63.90000  ? 158 LEU D O   1 
ATOM   11854 C  CB  . LEU D  1 127 ? -29.60500 0.62500   9.19000   1.000 53.41000  ? 158 LEU D CB  1 
ATOM   11855 C  CG  . LEU D  1 127 ? -28.40800 1.58400   9.11800   1.000 63.23000  ? 158 LEU D CG  1 
ATOM   11856 C  CD1 . LEU D  1 127 ? -28.68200 2.76500   8.21000   1.000 58.06000  ? 158 LEU D CD1 1 
ATOM   11857 C  CD2 . LEU D  1 127 ? -28.04000 2.08800   10.51700  1.000 52.58000  ? 158 LEU D CD2 1 
ATOM   11858 N  N   . GLY D  1 128 ? -30.25800 -2.90300  9.88700   1.000 64.63000  ? 159 GLY D N   1 
ATOM   11859 C  CA  . GLY D  1 128 ? -31.35600 -3.84800  9.92700   1.000 67.01000  ? 159 GLY D CA  1 
ATOM   11860 C  C   . GLY D  1 128 ? -31.29700 -4.85900  8.80200   1.000 68.93000  ? 159 GLY D C   1 
ATOM   11861 O  O   . GLY D  1 128 ? -31.09700 -4.49800  7.63600   1.000 62.41000  ? 159 GLY D O   1 
ATOM   11862 N  N   . ALA D  1 129 ? -31.42400 -6.13900  9.15000   1.000 68.25000  ? 160 ALA D N   1 
ATOM   11863 C  CA  . ALA D  1 129 ? -31.31700 -7.22300  8.18300   1.000 71.35000  ? 160 ALA D CA  1 
ATOM   11864 C  C   . ALA D  1 129 ? -32.67100 -7.77600  7.72800   1.000 72.37000  ? 160 ALA D C   1 
ATOM   11865 O  O   . ALA D  1 129 ? -32.69500 -8.69800  6.91300   1.000 71.59000  ? 160 ALA D O   1 
ATOM   11866 C  CB  . ALA D  1 129 ? -30.46000 -8.35700  8.76200   1.000 71.62000  ? 160 ALA D CB  1 
ATOM   11867 N  N   . ALA D  1 130 ? -33.86800 -7.24400  8.29600   1.000 70.94000  ? 161 ALA D N   1 
ATOM   11868 C  CA  . ALA D  1 130 ? -35.22100 -7.61700  7.89500   1.000 69.69000  ? 161 ALA D CA  1 
ATOM   11869 C  C   . ALA D  1 130 ? -35.74500 -6.72900  6.76400   1.000 73.34000  ? 161 ALA D C   1 
ATOM   11870 O  O   . ALA D  1 130 ? -35.31000 -5.58000  6.61700   1.000 71.37000  ? 161 ALA D O   1 
ATOM   11871 C  CB  . ALA D  1 130 ? -36.16800 -7.53500  9.08700   1.000 70.87000  ? 161 ALA D CB  1 
ATOM   11872 N  N   . PRO D  1 131 ? -36.68800 -7.24300  5.95600   1.000 76.03000  ? 162 PRO D N   1 
ATOM   11873 C  CA  . PRO D  1 131 ? -37.15900 -6.46400  4.79100   1.000 73.66000  ? 162 PRO D CA  1 
ATOM   11874 C  C   . PRO D  1 131 ? -37.68300 -5.07900  5.13500   1.000 69.89000  ? 162 PRO D C   1 
ATOM   11875 O  O   . PRO D  1 131 ? -37.45900 -4.14000  4.36100   1.000 69.25000  ? 162 PRO D O   1 
ATOM   11876 C  CB  . PRO D  1 131 ? -38.26600 -7.35500  4.20500   1.000 66.54000  ? 162 PRO D CB  1 
ATOM   11877 C  CG  . PRO D  1 131 ? -37.83200 -8.74100  4.54100   1.000 69.05000  ? 162 PRO D CG  1 
ATOM   11878 C  CD  . PRO D  1 131 ? -37.16700 -8.64100  5.91100   1.000 74.09000  ? 162 PRO D CD  1 
ATOM   11879 N  N   . LYS D  1 132 ? -38.39100 -4.91800  6.25900   1.000 68.95000  ? 163 LYS D N   1 
ATOM   11880 C  CA  . LYS D  1 132 ? -38.89900 -3.59200  6.61200   1.000 72.80000  ? 163 LYS D CA  1 
ATOM   11881 C  C   . LYS D  1 132 ? -37.78300 -2.60100  6.92600   1.000 70.37000  ? 163 LYS D C   1 
ATOM   11882 O  O   . LYS D  1 132 ? -38.02400 -1.39000  6.87800   1.000 68.67000  ? 163 LYS D O   1 
ATOM   11883 C  CB  . LYS D  1 132 ? -39.84400 -3.66700  7.81200   1.000 72.42000  ? 163 LYS D CB  1 
ATOM   11884 C  CG  . LYS D  1 132 ? -39.16200 -4.13900  9.08500   1.000 73.78000  ? 163 LYS D CG  1 
ATOM   11885 C  CD  . LYS D  1 132 ? -40.15100 -4.42100  10.21900  1.000 77.57000  ? 163 LYS D CD  1 
ATOM   11886 C  CE  . LYS D  1 132 ? -40.58800 -3.13600  10.92500  1.000 74.64000  ? 163 LYS D CE  1 
ATOM   11887 N  NZ  . LYS D  1 132 ? -41.21000 -3.42100  12.26300  1.000 70.77000  ? 163 LYS D NZ  1 
ATOM   11888 N  N   . PHE D  1 133 ? -36.57100 -3.08400  7.21500   1.000 70.92000  ? 164 PHE D N   1 
ATOM   11889 C  CA  . PHE D  1 133 ? -35.40900 -2.23600  7.46200   1.000 66.35000  ? 164 PHE D CA  1 
ATOM   11890 C  C   . PHE D  1 133 ? -34.51200 -2.13500  6.24400   1.000 66.83000  ? 164 PHE D C   1 
ATOM   11891 O  O   . PHE D  1 133 ? -33.42300 -1.56500  6.34400   1.000 62.96000  ? 164 PHE D O   1 
ATOM   11892 C  CB  . PHE D  1 133 ? -34.56900 -2.75800  8.63200   1.000 65.19000  ? 164 PHE D CB  1 
ATOM   11893 C  CG  . PHE D  1 133 ? -35.33200 -2.94600  9.89700   1.000 64.44000  ? 164 PHE D CG  1 
ATOM   11894 C  CD1 . PHE D  1 133 ? -36.01500 -1.89400  10.47400  1.000 64.27000  ? 164 PHE D CD1 1 
ATOM   11895 C  CD2 . PHE D  1 133 ? -35.34900 -4.18100  10.52700  1.000 67.92000  ? 164 PHE D CD2 1 
ATOM   11896 C  CE1 . PHE D  1 133 ? -36.72000 -2.07400  11.65000  1.000 67.81000  ? 164 PHE D CE1 1 
ATOM   11897 C  CE2 . PHE D  1 133 ? -36.05000 -4.37100  11.70200  1.000 69.12000  ? 164 PHE D CE2 1 
ATOM   11898 C  CZ  . PHE D  1 133 ? -36.73700 -3.31700  12.26600  1.000 68.49000  ? 164 PHE D CZ  1 
ATOM   11899 N  N   . HIS D  1 134 ? -34.92600 -2.72100  5.12000   1.000 70.11000  ? 165 HIS D N   1 
ATOM   11900 C  CA  . HIS D  1 134 ? -34.09900 -2.77300  3.92500   1.000 63.78000  ? 165 HIS D CA  1 
ATOM   11901 C  C   . HIS D  1 134 ? -33.95300 -1.38100  3.31100   1.000 57.43000  ? 165 HIS D C   1 
ATOM   11902 O  O   . HIS D  1 134 ? -34.88200 -0.57300  3.36500   1.000 57.49000  ? 165 HIS D O   1 
ATOM   11903 C  CB  . HIS D  1 134 ? -34.71500 -3.73300  2.90400   1.000 60.07000  ? 165 HIS D CB  1 
ATOM   11904 C  CG  . HIS D  1 134 ? -33.81400 -4.06000  1.75700   1.000 52.45000  ? 165 HIS D CG  1 
ATOM   11905 N  ND1 . HIS D  1 134 ? -33.66800 -3.23000  0.66800   1.000 52.61000  ? 165 HIS D ND1 1 
ATOM   11906 C  CD2 . HIS D  1 134 ? -32.98600 -5.11100  1.54300   1.000 56.63000  ? 165 HIS D CD2 1 
ATOM   11907 C  CE1 . HIS D  1 134 ? -32.79800 -3.76000  -0.17400  1.000 56.76000  ? 165 HIS D CE1 1 
ATOM   11908 N  NE2 . HIS D  1 134 ? -32.37200 -4.90300  0.33100   1.000 55.66000  ? 165 HIS D NE2 1 
ATOM   11909 N  N   . PRO D  1 135 ? -32.80400 -1.09000  2.68900   1.000 58.20000  ? 166 PRO D N   1 
ATOM   11910 C  CA  . PRO D  1 135 ? -32.63400 0.22300   2.04500   1.000 60.63000  ? 166 PRO D CA  1 
ATOM   11911 C  C   . PRO D  1 135 ? -33.73500 0.58900   1.06100   1.000 58.34000  ? 166 PRO D C   1 
ATOM   11912 O  O   . PRO D  1 135 ? -34.15300 1.75000   1.02900   1.000 63.81000  ? 166 PRO D O   1 
ATOM   11913 C  CB  . PRO D  1 135 ? -31.28100 0.08000   1.33100   1.000 58.20000  ? 166 PRO D CB  1 
ATOM   11914 C  CG  . PRO D  1 135 ? -30.54100 -0.89400  2.13800   1.000 56.69000  ? 166 PRO D CG  1 
ATOM   11915 C  CD  . PRO D  1 135 ? -31.54400 -1.85700  2.71000   1.000 56.60000  ? 166 PRO D CD  1 
ATOM   11916 N  N   . ASN D  1 136 ? -34.23000 -0.36300  0.26400   1.000 59.02000  ? 167 ASN D N   1 
ATOM   11917 C  CA  . ASN D  1 136 ? -35.22500 -0.02200  -0.75600  1.000 63.41000  ? 167 ASN D CA  1 
ATOM   11918 C  C   . ASN D  1 136 ? -36.54700 0.42300   -0.16000  1.000 54.90000  ? 167 ASN D C   1 
ATOM   11919 O  O   . ASN D  1 136 ? -37.30800 1.13000   -0.82500  1.000 65.97000  ? 167 ASN D O   1 
ATOM   11920 C  CB  . ASN D  1 136 ? -35.44700 -1.20800  -1.69400  1.000 62.56000  ? 167 ASN D CB  1 
ATOM   11921 C  CG  . ASN D  1 136 ? -34.26900 -1.44600  -2.62000  1.000 62.34000  ? 167 ASN D CG  1 
ATOM   11922 O  OD1 . ASN D  1 136 ? -33.82200 -2.57900  -2.79100  1.000 60.31000  ? 167 ASN D OD1 1 
ATOM   11923 N  ND2 . ASN D  1 136 ? -33.80800 -0.38700  -3.28000  1.000 63.64000  ? 167 ASN D ND2 1 
ATOM   11924 N  N   . LYS D  1 137 ? -36.84100 0.02800   1.06200   1.000 58.48000  ? 168 LYS D N   1 
ATOM   11925 C  CA  . LYS D  1 137 ? -38.02000 0.51900   1.75200   1.000 63.82000  ? 168 LYS D CA  1 
ATOM   11926 C  C   . LYS D  1 137 ? -37.72200 1.72400   2.62800   1.000 67.61000  ? 168 LYS D C   1 
ATOM   11927 O  O   . LYS D  1 137 ? -38.63900 2.23800   3.27500   1.000 74.98000  ? 168 LYS D O   1 
ATOM   11928 C  CB  . LYS D  1 137 ? -38.66400 -0.61300  2.55800   1.000 67.16000  ? 168 LYS D CB  1 
ATOM   11929 C  CG  . LYS D  1 137 ? -39.55900 -1.49500  1.67500   1.000 72.66000  ? 168 LYS D CG  1 
ATOM   11930 C  CD  . LYS D  1 137 ? -40.05900 -2.73700  2.38400   1.000 78.61000  ? 168 LYS D CD  1 
ATOM   11931 C  CE  . LYS D  1 137 ? -40.93800 -3.56500  1.46100   1.000 79.47000  ? 168 LYS D CE  1 
ATOM   11932 N  NZ  . LYS D  1 137 ? -41.35600 -4.86600  2.07600   1.000 85.44000  ? 168 LYS D NZ  1 
ATOM   11933 N  N   . ARG D  1 138 ? -36.45800 2.14800   2.70400   1.000 65.63000  ? 169 ARG D N   1 
ATOM   11934 C  CA  . ARG D  1 138 ? -36.04600 3.29300   3.50900   1.000 67.82000  ? 169 ARG D CA  1 
ATOM   11935 C  C   . ARG D  1 138 ? -35.53200 4.44600   2.64400   1.000 66.01000  ? 169 ARG D C   1 
ATOM   11936 O  O   . ARG D  1 138 ? -34.60500 5.15900   3.03600   1.000 64.48000  ? 169 ARG D O   1 
ATOM   11937 C  CB  . ARG D  1 138 ? -34.99900 2.88900   4.55000   1.000 59.02000  ? 169 ARG D CB  1 
ATOM   11938 C  CG  . ARG D  1 138 ? -35.42300 1.68600   5.37400   1.000 68.20000  ? 169 ARG D CG  1 
ATOM   11939 C  CD  . ARG D  1 138 ? -35.11300 1.85300   6.86400   1.000 71.47000  ? 169 ARG D CD  1 
ATOM   11940 N  NE  . ARG D  1 138 ? -35.85800 2.95400   7.46900   1.000 64.48000  ? 169 ARG D NE  1 
ATOM   11941 C  CZ  . ARG D  1 138 ? -36.15900 3.03100   8.75800   1.000 67.20000  ? 169 ARG D CZ  1 
ATOM   11942 N  NH1 . ARG D  1 138 ? -35.71100 2.13700   9.62800   1.000 67.44000  ? 169 ARG D NH1 1 
ATOM   11943 N  NH2 . ARG D  1 138 ? -36.89600 4.05000   9.19100   1.000 69.35000  ? 169 ARG D NH2 1 
ATOM   11944 N  N   . GLY D  1 139 ? -36.08400 4.60600   1.44700   1.000 63.52000  ? 170 GLY D N   1 
ATOM   11945 C  CA  . GLY D  1 139 ? -35.84700 5.79300   0.65400   1.000 63.07000  ? 170 GLY D CA  1 
ATOM   11946 C  C   . GLY D  1 139 ? -34.80900 5.69700   -0.43700  1.000 62.88000  ? 170 GLY D C   1 
ATOM   11947 O  O   . GLY D  1 139 ? -34.52200 6.71600   -1.07500  1.000 60.90000  ? 170 GLY D O   1 
ATOM   11948 N  N   . PHE D  1 140 ? -34.24600 4.51800   -0.68600  1.000 62.73000  ? 171 PHE D N   1 
ATOM   11949 C  CA  . PHE D  1 140 ? -33.19600 4.35300   -1.68500  1.000 64.15000  ? 171 PHE D CA  1 
ATOM   11950 C  C   . PHE D  1 140 ? -33.76600 3.64400   -2.90900  1.000 66.52000  ? 171 PHE D C   1 
ATOM   11951 O  O   . PHE D  1 140 ? -34.24100 2.50700   -2.80300  1.000 65.07000  ? 171 PHE D O   1 
ATOM   11952 C  CB  . PHE D  1 140 ? -32.01600 3.57000   -1.11700  1.000 60.68000  ? 171 PHE D CB  1 
ATOM   11953 C  CG  . PHE D  1 140 ? -31.17200 4.35200   -0.14200  1.000 62.61000  ? 171 PHE D CG  1 
ATOM   11954 C  CD1 . PHE D  1 140 ? -30.30700 5.33800   -0.58900  1.000 58.98000  ? 171 PHE D CD1 1 
ATOM   11955 C  CD2 . PHE D  1 140 ? -31.20800 4.06400   1.21100   1.000 60.39000  ? 171 PHE D CD2 1 
ATOM   11956 C  CE1 . PHE D  1 140 ? -29.52300 6.04700   0.29700   1.000 61.69000  ? 171 PHE D CE1 1 
ATOM   11957 C  CE2 . PHE D  1 140 ? -30.41900 4.76600   2.10400   1.000 63.85000  ? 171 PHE D CE2 1 
ATOM   11958 C  CZ  . PHE D  1 140 ? -29.57800 5.76100   1.64700   1.000 58.47000  ? 171 PHE D CZ  1 
ATOM   11959 N  N   . ASP D  1 141 ? -33.74200 4.32600   -4.06100  1.000 62.02000  ? 172 ASP D N   1 
ATOM   11960 C  CA  . ASP D  1 141 ? -34.16100 3.68600   -5.30900  1.000 67.76000  ? 172 ASP D CA  1 
ATOM   11961 C  C   . ASP D  1 141 ? -33.29900 2.47400   -5.62700  1.000 68.26000  ? 172 ASP D C   1 
ATOM   11962 O  O   . ASP D  1 141 ? -33.80000 1.45300   -6.11000  1.000 72.97000  ? 172 ASP D O   1 
ATOM   11963 C  CB  . ASP D  1 141 ? -34.10700 4.67200   -6.47600  1.000 66.09000  ? 172 ASP D CB  1 
ATOM   11964 C  CG  . ASP D  1 141 ? -35.00900 5.87200   -6.27200  1.000 66.58000  ? 172 ASP D CG  1 
ATOM   11965 O  OD1 . ASP D  1 141 ? -36.06600 5.71900   -5.62100  1.000 65.06000  ? 172 ASP D OD1 1 
ATOM   11966 O  OD2 . ASP D  1 141 ? -34.65700 6.96600   -6.76900  1.000 69.96000  ? 172 ASP D OD2 1 
ATOM   11967 N  N   . ASP D  1 142 ? -32.00000 2.57400   -5.37300  1.000 64.95000  ? 173 ASP D N   1 
ATOM   11968 C  CA  . ASP D  1 142 ? -31.03600 1.54300   -5.72300  1.000 65.62000  ? 173 ASP D CA  1 
ATOM   11969 C  C   . ASP D  1 142 ? -30.19500 1.22600   -4.50500  1.000 64.38000  ? 173 ASP D C   1 
ATOM   11970 O  O   . ASP D  1 142 ? -29.80300 2.13400   -3.77200  1.000 67.65000  ? 173 ASP D O   1 
ATOM   11971 C  CB  . ASP D  1 142 ? -30.12900 2.00300   -6.88000  1.000 63.90000  ? 173 ASP D CB  1 
ATOM   11972 C  CG  . ASP D  1 142 ? -29.28800 0.87700   -7.45900  1.000 72.29000  ? 173 ASP D CG  1 
ATOM   11973 O  OD1 . ASP D  1 142 ? -28.25100 0.53700   -6.83800  1.000 75.27000  ? 173 ASP D OD1 1 
ATOM   11974 O  OD2 . ASP D  1 142 ? -29.65900 0.33000   -8.52900  1.000 69.40000  ? 173 ASP D OD2 1 
ATOM   11975 N  N   . PHE D  1 143 ? -29.93800 -0.06100  -4.28200  1.000 64.16000  ? 174 PHE D N   1 
ATOM   11976 C  CA  . PHE D  1 143 ? -29.00800 -0.50100  -3.25200  1.000 61.37000  ? 174 PHE D CA  1 
ATOM   11977 C  C   . PHE D  1 143 ? -28.07400 -1.53800  -3.84900  1.000 68.77000  ? 174 PHE D C   1 
ATOM   11978 O  O   . PHE D  1 143 ? -28.52500 -2.48000  -4.51200  1.000 65.10000  ? 174 PHE D O   1 
ATOM   11979 C  CB  . PHE D  1 143 ? -29.70300 -1.08300  -2.02700  1.000 60.15000  ? 174 PHE D CB  1 
ATOM   11980 C  CG  . PHE D  1 143 ? -28.74500 -1.66300  -1.02400  1.000 64.43000  ? 174 PHE D CG  1 
ATOM   11981 C  CD1 . PHE D  1 143 ? -27.66500 -0.91500  -0.56500  1.000 62.30000  ? 174 PHE D CD1 1 
ATOM   11982 C  CD2 . PHE D  1 143 ? -28.90600 -2.96300  -0.55200  1.000 62.97000  ? 174 PHE D CD2 1 
ATOM   11983 C  CE1 . PHE D  1 143 ? -26.76400 -1.44800  0.35100   1.000 63.30000  ? 174 PHE D CE1 1 
ATOM   11984 C  CE2 . PHE D  1 143 ? -28.00900 -3.51000  0.36700   1.000 63.40000  ? 174 PHE D CE2 1 
ATOM   11985 C  CZ  . PHE D  1 143 ? -26.93500 -2.75000  0.82200   1.000 63.31000  ? 174 PHE D CZ  1 
ATOM   11986 N  N   . TYR D  1 144 ? -26.77500 -1.35100  -3.62000  1.000 65.01000  ? 175 TYR D N   1 
ATOM   11987 C  CA  . TYR D  1 144 ? -25.76100 -2.31700  -4.02600  1.000 62.19000  ? 175 TYR D CA  1 
ATOM   11988 C  C   . TYR D  1 144 ? -24.79500 -2.48200  -2.86100  1.000 62.03000  ? 175 TYR D C   1 
ATOM   11989 O  O   . TYR D  1 144 ? -23.98400 -1.59000  -2.59500  1.000 62.45000  ? 175 TYR D O   1 
ATOM   11990 C  CB  . TYR D  1 144 ? -25.02700 -1.85700  -5.28500  1.000 59.53000  ? 175 TYR D CB  1 
ATOM   11991 C  CG  . TYR D  1 144 ? -24.02200 -2.86300  -5.82800  1.000 67.75000  ? 175 TYR D CG  1 
ATOM   11992 C  CD1 . TYR D  1 144 ? -22.76200 -3.00400  -5.25100  1.000 63.46000  ? 175 TYR D CD1 1 
ATOM   11993 C  CD2 . TYR D  1 144 ? -24.31600 -3.63900  -6.94200  1.000 66.92000  ? 175 TYR D CD2 1 
ATOM   11994 C  CE1 . TYR D  1 144 ? -21.84100 -3.90600  -5.74800  1.000 67.37000  ? 175 TYR D CE1 1 
ATOM   11995 C  CE2 . TYR D  1 144 ? -23.39600 -4.54100  -7.45300  1.000 62.83000  ? 175 TYR D CE2 1 
ATOM   11996 C  CZ  . TYR D  1 144 ? -22.16100 -4.67100  -6.85400  1.000 71.44000  ? 175 TYR D CZ  1 
ATOM   11997 O  OH  . TYR D  1 144 ? -21.23800 -5.57100  -7.34800  1.000 75.28000  ? 175 TYR D OH  1 
ATOM   11998 N  N   . GLY D  1 145 ? -24.87200 -3.61900  -2.17500  1.000 65.90000  ? 176 GLY D N   1 
ATOM   11999 C  CA  . GLY D  1 145 ? -23.95600 -3.88800  -1.07500  1.000 57.08000  ? 176 GLY D CA  1 
ATOM   12000 C  C   . GLY D  1 145 ? -24.42100 -5.06700  -0.24500  1.000 62.73000  ? 176 GLY D C   1 
ATOM   12001 O  O   . GLY D  1 145 ? -25.01100 -6.02300  -0.77100  1.000 57.55000  ? 176 GLY D O   1 
ATOM   12002 N  N   . PHE D  1 146 ? -24.14800 -4.98200  1.06800   1.000 52.12000  ? 177 PHE D N   1 
ATOM   12003 C  CA  . PHE D  1 146 ? -24.47500 -6.02900  2.02300   1.000 49.50000  ? 177 PHE D CA  1 
ATOM   12004 C  C   . PHE D  1 146 ? -25.13900 -5.40900  3.24400   1.000 57.24000  ? 177 PHE D C   1 
ATOM   12005 O  O   . PHE D  1 146 ? -24.89400 -4.24900  3.58900   1.000 56.36000  ? 177 PHE D O   1 
ATOM   12006 C  CB  . PHE D  1 146 ? -23.23900 -6.80900  2.47700   1.000 56.95000  ? 177 PHE D CB  1 
ATOM   12007 C  CG  . PHE D  1 146 ? -22.18500 -5.95000  3.11000   1.000 56.56000  ? 177 PHE D CG  1 
ATOM   12008 C  CD1 . PHE D  1 146 ? -22.23800 -5.66400  4.46600   1.000 58.33000  ? 177 PHE D CD1 1 
ATOM   12009 C  CD2 . PHE D  1 146 ? -21.14800 -5.43200  2.36400   1.000 54.72000  ? 177 PHE D CD2 1 
ATOM   12010 C  CE1 . PHE D  1 146 ? -21.29600 -4.87700  5.05200   1.000 56.67000  ? 177 PHE D CE1 1 
ATOM   12011 C  CE2 . PHE D  1 146 ? -20.19900 -4.64700  2.95200   1.000 53.32000  ? 177 PHE D CE2 1 
ATOM   12012 C  CZ  . PHE D  1 146 ? -20.27200 -4.37000  4.29400   1.000 59.71000  ? 177 PHE D CZ  1 
ATOM   12013 N  N   . LEU D  1 147 ? -25.94100 -6.21600  3.93600   1.000 57.40000  ? 178 LEU D N   1 
ATOM   12014 C  CA  . LEU D  1 147 ? -26.82800 -5.69300  4.96900   1.000 59.73000  ? 178 LEU D CA  1 
ATOM   12015 C  C   . LEU D  1 147 ? -26.21600 -5.61600  6.35800   1.000 58.55000  ? 178 LEU D C   1 
ATOM   12016 O  O   . LEU D  1 147 ? -26.75800 -4.89300  7.20600   1.000 62.06000  ? 178 LEU D O   1 
ATOM   12017 C  CB  . LEU D  1 147 ? -28.09800 -6.53400  5.05500   1.000 53.88000  ? 178 LEU D CB  1 
ATOM   12018 C  CG  . LEU D  1 147 ? -29.01500 -6.44300  3.84800   1.000 63.12000  ? 178 LEU D CG  1 
ATOM   12019 C  CD1 . LEU D  1 147 ? -30.27600 -7.25000  4.12000   1.000 53.07000  ? 178 LEU D CD1 1 
ATOM   12020 C  CD2 . LEU D  1 147 ? -29.34500 -4.97900  3.52400   1.000 60.49000  ? 178 LEU D CD2 1 
ATOM   12021 N  N   . GLY D  1 148 ? -25.14600 -6.36000  6.63100   1.000 59.35000  ? 179 GLY D N   1 
ATOM   12022 C  CA  . GLY D  1 148 ? -24.56600 -6.43900  7.95800   1.000 58.91000  ? 179 GLY D CA  1 
ATOM   12023 C  C   . GLY D  1 148 ? -23.46200 -5.43500  8.21700   1.000 62.83000  ? 179 GLY D C   1 
ATOM   12024 O  O   . GLY D  1 148 ? -23.38200 -4.37100  7.59300   1.000 61.61000  ? 179 GLY D O   1 
ATOM   12025 N  N   . GLY D  1 149 ? -22.58700 -5.79200  9.16100   1.000 61.78000  ? 180 GLY D N   1 
ATOM   12026 C  CA  . GLY D  1 149 ? -21.58600 -4.86800  9.65800   1.000 60.61000  ? 180 GLY D CA  1 
ATOM   12027 C  C   . GLY D  1 149 ? -20.22800 -4.93500  8.99900   1.000 64.24000  ? 180 GLY D C   1 
ATOM   12028 O  O   . GLY D  1 149 ? -19.41100 -4.02900  9.20800   1.000 67.07000  ? 180 GLY D O   1 
ATOM   12029 N  N   . GLY D  1 150 ? -19.96400 -5.96800  8.20300   1.000 59.69000  ? 181 GLY D N   1 
ATOM   12030 C  CA  . GLY D  1 150 ? -18.68400 -6.10200  7.52800   1.000 55.15000  ? 181 GLY D CA  1 
ATOM   12031 C  C   . GLY D  1 150 ? -18.76700 -7.16100  6.45000   1.000 60.53000  ? 181 GLY D C   1 
ATOM   12032 O  O   . GLY D  1 150 ? -19.81100 -7.79000  6.24700   1.000 63.35000  ? 181 GLY D O   1 
ATOM   12033 N  N   . HIS D  1 151 ? -17.65600 -7.31400  5.72400   1.000 58.59000  ? 182 HIS D N   1 
ATOM   12034 C  CA  . HIS D  1 151 ? -17.56200 -8.26200  4.61800   1.000 56.87000  ? 182 HIS D CA  1 
ATOM   12035 C  C   . HIS D  1 151 ? -16.11000 -8.44200  4.18500   1.000 57.50000  ? 182 HIS D C   1 
ATOM   12036 O  O   . HIS D  1 151 ? -15.32500 -7.49200  4.19900   1.000 56.31000  ? 182 HIS D O   1 
ATOM   12037 C  CB  . HIS D  1 151 ? -18.39900 -7.80000  3.42800   1.000 57.61000  ? 182 HIS D CB  1 
ATOM   12038 C  CG  . HIS D  1 151 ? -18.82600 -8.91300  2.53400   1.000 61.77000  ? 182 HIS D CG  1 
ATOM   12039 N  ND1 . HIS D  1 151 ? -17.96400 -9.52300  1.64700   1.000 58.89000  ? 182 HIS D ND1 1 
ATOM   12040 C  CD2 . HIS D  1 151 ? -20.02800 -9.51400  2.37200   1.000 62.56000  ? 182 HIS D CD2 1 
ATOM   12041 C  CE1 . HIS D  1 151 ? -18.61600 -10.46400 0.98800   1.000 62.64000  ? 182 HIS D CE1 1 
ATOM   12042 N  NE2 . HIS D  1 151 ? -19.87000 -10.47700 1.40700   1.000 61.58000  ? 182 HIS D NE2 1 
ATOM   12043 N  N   . ASP D  1 152 ? -15.77100 -9.66400  3.77300   1.000 57.39000  ? 183 ASP D N   1 
ATOM   12044 C  CA  . ASP D  1 152 ? -14.48000 -9.90000  3.13700   1.000 61.38000  ? 183 ASP D CA  1 
ATOM   12045 C  C   . ASP D  1 152 ? -14.40900 -9.17800  1.79600   1.000 56.30000  ? 183 ASP D C   1 
ATOM   12046 O  O   . ASP D  1 152 ? -15.42700 -8.87100  1.17500   1.000 55.21000  ? 183 ASP D O   1 
ATOM   12047 C  CB  . ASP D  1 152 ? -14.22100 -11.39500 2.94100   1.000 67.15000  ? 183 ASP D CB  1 
ATOM   12048 C  CG  . ASP D  1 152 ? -13.84300 -12.10100 4.23800   1.000 66.90000  ? 183 ASP D CG  1 
ATOM   12049 O  OD1 . ASP D  1 152 ? -14.51600 -11.88600 5.26400   1.000 67.52000  ? 183 ASP D OD1 1 
ATOM   12050 O  OD2 . ASP D  1 152 ? -12.85700 -12.86200 4.23200   1.000 75.10000  ? 183 ASP D OD2 1 
ATOM   12051 N  N   . TYR D  1 153 ? -13.18100 -8.90400  1.35500   1.000 59.06000  ? 184 TYR D N   1 
ATOM   12052 C  CA  . TYR D  1 153 ? -12.93500 -7.97200  0.25900   1.000 63.11000  ? 184 TYR D CA  1 
ATOM   12053 C  C   . TYR D  1 153 ? -12.77900 -8.61000  -1.12200  1.000 63.83000  ? 184 TYR D C   1 
ATOM   12054 O  O   . TYR D  1 153 ? -12.83800 -7.88600  -2.12100  1.000 60.95000  ? 184 TYR D O   1 
ATOM   12055 C  CB  . TYR D  1 153 ? -11.68500 -7.13700  0.54900   1.000 57.20000  ? 184 TYR D CB  1 
ATOM   12056 C  CG  . TYR D  1 153 ? -11.92200 -6.06900  1.57600   1.000 59.92000  ? 184 TYR D CG  1 
ATOM   12057 C  CD1 . TYR D  1 153 ? -11.92800 -6.37300  2.92600   1.000 57.93000  ? 184 TYR D CD1 1 
ATOM   12058 C  CD2 . TYR D  1 153 ? -12.15600 -4.74700  1.19700   1.000 61.48000  ? 184 TYR D CD2 1 
ATOM   12059 C  CE1 . TYR D  1 153 ? -12.15500 -5.39700  3.87800   1.000 62.00000  ? 184 TYR D CE1 1 
ATOM   12060 C  CE2 . TYR D  1 153 ? -12.38500 -3.75100  2.15200   1.000 59.47000  ? 184 TYR D CE2 1 
ATOM   12061 C  CZ  . TYR D  1 153 ? -12.38500 -4.08800  3.49000   1.000 63.15000  ? 184 TYR D CZ  1 
ATOM   12062 O  OH  . TYR D  1 153 ? -12.59500 -3.12800  4.46400   1.000 64.18000  ? 184 TYR D OH  1 
ATOM   12063 N  N   . PHE D  1 154 ? -12.50900 -9.90100  -1.22200  1.000 64.16000  ? 185 PHE D N   1 
ATOM   12064 C  CA  . PHE D  1 154 ? -12.27900 -10.51800 -2.52800  1.000 58.81000  ? 185 PHE D CA  1 
ATOM   12065 C  C   . PHE D  1 154 ? -13.36600 -11.53100 -2.83700  1.000 64.67000  ? 185 PHE D C   1 
ATOM   12066 O  O   . PHE D  1 154 ? -13.40400 -12.59900 -2.19800  1.000 67.54000  ? 185 PHE D O   1 
ATOM   12067 C  CB  . PHE D  1 154 ? -10.91100 -11.19300 -2.56400  1.000 58.71000  ? 185 PHE D CB  1 
ATOM   12068 C  CG  . PHE D  1 154 ? -9.75900  -10.24100 -2.72400  1.000 63.67000  ? 185 PHE D CG  1 
ATOM   12069 C  CD1 . PHE D  1 154 ? -9.47000  -9.67400  -3.95700  1.000 57.61000  ? 185 PHE D CD1 1 
ATOM   12070 C  CD2 . PHE D  1 154 ? -8.96100  -9.90400  -1.62800  1.000 57.35000  ? 185 PHE D CD2 1 
ATOM   12071 C  CE1 . PHE D  1 154 ? -8.39600  -8.79900  -4.09900  1.000 59.43000  ? 185 PHE D CE1 1 
ATOM   12072 C  CE2 . PHE D  1 154 ? -7.89100  -9.02900  -1.76400  1.000 58.84000  ? 185 PHE D CE2 1 
ATOM   12073 C  CZ  . PHE D  1 154 ? -7.60700  -8.47500  -2.99800  1.000 62.23000  ? 185 PHE D CZ  1 
ATOM   12074 N  N   . PRO D  1 155 ? -14.25600 -11.26000 -3.79400  1.000 65.06000  ? 186 PRO D N   1 
ATOM   12075 C  CA  . PRO D  1 155 ? -15.29000 -12.24900 -4.14300  1.000 59.69000  ? 186 PRO D CA  1 
ATOM   12076 C  C   . PRO D  1 155 ? -14.66900 -13.52800 -4.64700  1.000 64.61000  ? 186 PRO D C   1 
ATOM   12077 O  O   . PRO D  1 155 ? -15.25500 -14.61300 -4.53400  1.000 57.70000  ? 186 PRO D O   1 
ATOM   12078 C  CB  . PRO D  1 155 ? -16.11200 -11.53400 -5.22000  1.000 68.14000  ? 186 PRO D CB  1 
ATOM   12079 C  CG  . PRO D  1 155 ? -15.13800 -10.59200 -5.85100  1.000 68.85000  ? 186 PRO D CG  1 
ATOM   12080 C  CD  . PRO D  1 155 ? -14.19900 -10.14900 -4.75500  1.000 63.97000  ? 186 PRO D CD  1 
ATOM   12081 N  N   . SER D  1 156 ? -13.48300 -13.39500 -5.23400  1.000 64.92000  ? 187 SER D N   1 
ATOM   12082 C  CA  . SER D  1 156 ? -12.69200 -14.53800 -5.65100  1.000 64.54000  ? 187 SER D CA  1 
ATOM   12083 C  C   . SER D  1 156 ? -12.53100 -15.55100 -4.51300  1.000 68.71000  ? 187 SER D C   1 
ATOM   12084 O  O   . SER D  1 156 ? -12.66800 -16.76100 -4.72300  1.000 71.59000  ? 187 SER D O   1 
ATOM   12085 C  CB  . SER D  1 156 ? -11.34400 -13.98900 -6.13200  1.000 70.62000  ? 187 SER D CB  1 
ATOM   12086 O  OG  . SER D  1 156 ? -11.40000 -12.54000 -6.23500  1.000 66.45000  ? 187 SER D OG  1 
ATOM   12087 N  N   . GLU D  1 157 ? -12.29100 -15.07200 -3.29000  1.000 68.42000  ? 188 GLU D N   1 
ATOM   12088 C  CA  . GLU D  1 157 ? -12.11200 -15.91800 -2.10800  1.000 62.67000  ? 188 GLU D CA  1 
ATOM   12089 C  C   . GLU D  1 157 ? -13.40900 -16.21100 -1.35500  1.000 60.29000  ? 188 GLU D C   1 
ATOM   12090 O  O   . GLU D  1 157 ? -13.64000 -17.35600 -0.95900  1.000 62.21000  ? 188 GLU D O   1 
ATOM   12091 C  CB  . GLU D  1 157 ? -11.07400 -15.29000 -1.16800  1.000 64.53000  ? 188 GLU D CB  1 
ATOM   12092 C  CG  . GLU D  1 157 ? -9.74200  -15.05200 -1.85600  1.000 61.05000  ? 188 GLU D CG  1 
ATOM   12093 C  CD  . GLU D  1 157 ? -8.75900  -14.23800 -1.03600  1.000 72.49000  ? 188 GLU D CD  1 
ATOM   12094 O  OE1 . GLU D  1 157 ? -9.14200  -13.69500 0.01900   1.000 74.63000  ? 188 GLU D OE1 1 
ATOM   12095 O  OE2 . GLU D  1 157 ? -7.59300  -14.12200 -1.46800  1.000 85.57000  ? 188 GLU D OE2 1 
ATOM   12096 N  N   . TYR D  1 158 ? -14.25100 -15.20400 -1.10800  1.000 62.66000  ? 189 TYR D N   1 
ATOM   12097 C  CA  . TYR D  1 158 ? -15.39800 -15.44500 -0.23400  1.000 59.55000  ? 189 TYR D CA  1 
ATOM   12098 C  C   . TYR D  1 158 ? -16.54500 -16.15800 -0.93900  1.000 59.33000  ? 189 TYR D C   1 
ATOM   12099 O  O   . TYR D  1 158 ? -17.36500 -16.79400 -0.26100  1.000 58.45000  ? 189 TYR D O   1 
ATOM   12100 C  CB  . TYR D  1 158 ? -15.90000 -14.14300 0.42200   1.000 55.89000  ? 189 TYR D CB  1 
ATOM   12101 C  CG  . TYR D  1 158 ? -16.52800 -13.10100 -0.49200  1.000 63.30000  ? 189 TYR D CG  1 
ATOM   12102 C  CD1 . TYR D  1 158 ? -17.77600 -13.31900 -1.07800  1.000 61.78000  ? 189 TYR D CD1 1 
ATOM   12103 C  CD2 . TYR D  1 158 ? -15.90800 -11.86500 -0.71200  1.000 61.05000  ? 189 TYR D CD2 1 
ATOM   12104 C  CE1 . TYR D  1 158 ? -18.36700 -12.37500 -1.90000  1.000 61.10000  ? 189 TYR D CE1 1 
ATOM   12105 C  CE2 . TYR D  1 158 ? -16.50400 -10.90100 -1.51800  1.000 59.98000  ? 189 TYR D CE2 1 
ATOM   12106 C  CZ  . TYR D  1 158 ? -17.73600 -11.17300 -2.11800  1.000 62.52000  ? 189 TYR D CZ  1 
ATOM   12107 O  OH  . TYR D  1 158 ? -18.35400 -10.25800 -2.94100  1.000 60.27000  ? 189 TYR D OH  1 
ATOM   12108 N  N   . GLN D  1 159 ? -16.65000 -16.04500 -2.26800  1.000 64.07000  ? 190 GLN D N   1 
ATOM   12109 C  CA  . GLN D  1 159 ? -17.64700 -16.83900 -2.98600  1.000 61.07000  ? 190 GLN D CA  1 
ATOM   12110 C  C   . GLN D  1 159 ? -17.31400 -18.32600 -2.89200  1.000 58.25000  ? 190 GLN D C   1 
ATOM   12111 O  O   . GLN D  1 159 ? -18.19100 -19.15300 -2.60300  1.000 55.25000  ? 190 GLN D O   1 
ATOM   12112 C  CB  . GLN D  1 159 ? -17.75300 -16.38600 -4.45200  1.000 58.61000  ? 190 GLN D CB  1 
ATOM   12113 C  CG  . GLN D  1 159 ? -18.56600 -15.10800 -4.63700  1.000 61.24000  ? 190 GLN D CG  1 
ATOM   12114 C  CD  . GLN D  1 159 ? -18.37300 -14.43300 -5.99500  1.000 58.27000  ? 190 GLN D CD  1 
ATOM   12115 O  OE1 . GLN D  1 159 ? -17.55600 -14.85500 -6.80900  1.000 57.62000  ? 190 GLN D OE1 1 
ATOM   12116 N  NE2 . GLN D  1 159 ? -19.12400 -13.35900 -6.22900  1.000 61.75000  ? 190 GLN D NE2 1 
ATOM   12117 N  N   . LYS D  1 160 ? -16.03400 -18.67400 -3.08600  1.000 62.77000  ? 191 LYS D N   1 
ATOM   12118 C  CA  . LYS D  1 160 ? -15.59000 -20.05900 -2.93400  1.000 62.03000  ? 191 LYS D CA  1 
ATOM   12119 C  C   . LYS D  1 160 ? -15.93600 -20.60500 -1.55100  1.000 64.69000  ? 191 LYS D C   1 
ATOM   12120 O  O   . LYS D  1 160 ? -16.56100 -21.66500 -1.42400  1.000 62.70000  ? 191 LYS D O   1 
ATOM   12121 C  CB  . LYS D  1 160 ? -14.08400 -20.15200 -3.19600  1.000 60.67000  ? 191 LYS D CB  1 
ATOM   12122 C  CG  . LYS D  1 160 ? -13.48500 -21.46800 -2.75300  1.000 67.82000  ? 191 LYS D CG  1 
ATOM   12123 C  CD  . LYS D  1 160 ? -12.10700 -21.71000 -3.34300  1.000 72.80000  ? 191 LYS D CD  1 
ATOM   12124 C  CE  . LYS D  1 160 ? -11.56000 -23.09700 -2.94100  1.000 74.55000  ? 191 LYS D CE  1 
ATOM   12125 N  NZ  . LYS D  1 160 ? -12.52600 -24.23100 -3.18000  1.000 66.51000  ? 191 LYS D NZ  1 
ATOM   12126 N  N   . THR D  1 161 ? -15.57900 -19.85700 -0.50200  1.000 61.12000  ? 192 THR D N   1 
ATOM   12127 C  CA  . THR D  1 161 ? -15.91100 -20.27000 0.85900   1.000 58.50000  ? 192 THR D CA  1 
ATOM   12128 C  C   . THR D  1 161 ? -17.41900 -20.38800 1.07000   1.000 60.88000  ? 192 THR D C   1 
ATOM   12129 O  O   . THR D  1 161 ? -17.88700 -21.33100 1.72100   1.000 58.51000  ? 192 THR D O   1 
ATOM   12130 C  CB  . THR D  1 161 ? -15.31700 -19.27900 1.86200   1.000 56.17000  ? 192 THR D CB  1 
ATOM   12131 O  OG1 . THR D  1 161 ? -13.88800 -19.28500 1.76400   1.000 57.54000  ? 192 THR D OG1 1 
ATOM   12132 C  CG2 . THR D  1 161 ? -15.75500 -19.60400 3.27300   1.000 56.45000  ? 192 THR D CG2 1 
ATOM   12133 N  N   . TYR D  1 162 ? -18.19600 -19.44000 0.54500   1.000 57.17000  ? 193 TYR D N   1 
ATOM   12134 C  CA  . TYR D  1 162 ? -19.64000 -19.48300 0.76500   1.000 58.85000  ? 193 TYR D CA  1 
ATOM   12135 C  C   . TYR D  1 162 ? -20.28700 -20.67000 0.06100   1.000 65.50000  ? 193 TYR D C   1 
ATOM   12136 O  O   . TYR D  1 162 ? -21.14800 -21.35100 0.63600   1.000 67.59000  ? 193 TYR D O   1 
ATOM   12137 C  CB  . TYR D  1 162 ? -20.29700 -18.18200 0.30600   1.000 56.04000  ? 193 TYR D CB  1 
ATOM   12138 C  CG  . TYR D  1 162 ? -21.81400 -18.22100 0.42900   1.000 61.80000  ? 193 TYR D CG  1 
ATOM   12139 C  CD1 . TYR D  1 162 ? -22.44400 -18.07600 1.65800   1.000 59.45000  ? 193 TYR D CD1 1 
ATOM   12140 C  CD2 . TYR D  1 162 ? -22.61200 -18.45800 -0.68800  1.000 60.00000  ? 193 TYR D CD2 1 
ATOM   12141 C  CE1 . TYR D  1 162 ? -23.82600 -18.12300 1.76100   1.000 53.17000  ? 193 TYR D CE1 1 
ATOM   12142 C  CE2 . TYR D  1 162 ? -23.98300 -18.51800 -0.58500  1.000 54.73000  ? 193 TYR D CE2 1 
ATOM   12143 C  CZ  . TYR D  1 162 ? -24.58000 -18.35800 0.63400   1.000 51.48000  ? 193 TYR D CZ  1 
ATOM   12144 O  OH  . TYR D  1 162 ? -25.94800 -18.41000 0.70900   1.000 69.38000  ? 193 TYR D OH  1 
ATOM   12145 N  N   . LYS D  1 163 ? -19.92300 -20.90900 -1.20100  1.000 65.60000  ? 194 LYS D N   1 
ATOM   12146 C  CA  . LYS D  1 163 ? -20.52100 -22.02400 -1.93400  1.000 67.12000  ? 194 LYS D CA  1 
ATOM   12147 C  C   . LYS D  1 163 ? -20.16000 -23.34900 -1.27100  1.000 63.25000  ? 194 LYS D C   1 
ATOM   12148 O  O   . LYS D  1 163 ? -21.03000 -24.19100 -1.01800  1.000 61.51000  ? 194 LYS D O   1 
ATOM   12149 C  CB  . LYS D  1 163 ? -20.08400 -21.99100 -3.40400  1.000 62.92000  ? 194 LYS D CB  1 
ATOM   12150 N  N   . ALA D  1 164 ? -18.87300 -23.54300 -0.97200  1.000 66.65000  ? 195 ALA D N   1 
ATOM   12151 C  CA  . ALA D  1 164 ? -18.43500 -24.76200 -0.29400  1.000 67.29000  ? 195 ALA D CA  1 
ATOM   12152 C  C   . ALA D  1 164 ? -19.18100 -24.96800 1.02100   1.000 66.76000  ? 195 ALA D C   1 
ATOM   12153 O  O   . ALA D  1 164 ? -19.62600 -26.08100 1.32500   1.000 73.67000  ? 195 ALA D O   1 
ATOM   12154 C  CB  . ALA D  1 164 ? -16.92400 -24.73300 -0.07100  1.000 51.64000  ? 195 ALA D CB  1 
ATOM   12155 N  N   . GLN D  1 165 ? -19.32100 -23.91200 1.82400   1.000 68.82000  ? 196 GLN D N   1 
ATOM   12156 C  CA  . GLN D  1 165 ? -19.96900 -24.08400 3.12200   1.000 71.92000  ? 196 GLN D CA  1 
ATOM   12157 C  C   . GLN D  1 165 ? -21.47700 -24.27900 3.01500   1.000 66.04000  ? 196 GLN D C   1 
ATOM   12158 O  O   . GLN D  1 165 ? -22.05400 -24.98400 3.84700   1.000 72.56000  ? 196 GLN D O   1 
ATOM   12159 C  CB  . GLN D  1 165 ? -19.65500 -22.90300 4.04100   1.000 71.26000  ? 196 GLN D CB  1 
ATOM   12160 C  CG  . GLN D  1 165 ? -18.24300 -22.94000 4.59500   1.000 63.77000  ? 196 GLN D CG  1 
ATOM   12161 C  CD  . GLN D  1 165 ? -17.97800 -21.85300 5.62800   1.000 81.31000  ? 196 GLN D CD  1 
ATOM   12162 O  OE1 . GLN D  1 165 ? -16.85000 -21.69900 6.10600   1.000 82.70000  ? 196 GLN D OE1 1 
ATOM   12163 N  NE2 . GLN D  1 165 ? -19.01600 -21.09600 5.98000   1.000 84.06000  ? 196 GLN D NE2 1 
ATOM   12164 N  N   . LYS D  1 166 ? -22.13700 -23.69200 2.00900   1.000 71.07000  ? 197 LYS D N   1 
ATOM   12165 C  CA  . LYS D  1 166 ? -23.57600 -23.93300 1.86300   1.000 72.46000  ? 197 LYS D CA  1 
ATOM   12166 C  C   . LYS D  1 166 ? -23.84800 -25.36400 1.40900   1.000 73.70000  ? 197 LYS D C   1 
ATOM   12167 O  O   . LYS D  1 166 ? -24.78700 -26.01100 1.89000   1.000 69.91000  ? 197 LYS D O   1 
ATOM   12168 C  CB  . LYS D  1 166 ? -24.19500 -22.93400 0.88000   1.000 67.62000  ? 197 LYS D CB  1 
ATOM   12169 N  N   . LYS D  1 167 ? -23.00400 -25.88400 0.51200   1.000 72.71000  ? 198 LYS D N   1 
ATOM   12170 C  CA  . LYS D  1 167 ? -23.13800 -27.25000 0.02500   1.000 72.22000  ? 198 LYS D CA  1 
ATOM   12171 C  C   . LYS D  1 167 ? -22.83600 -28.28600 1.10400   1.000 73.40000  ? 198 LYS D C   1 
ATOM   12172 O  O   . LYS D  1 167 ? -23.31400 -29.42300 1.01400   1.000 73.91000  ? 198 LYS D O   1 
ATOM   12173 C  CB  . LYS D  1 167 ? -22.20400 -27.44300 -1.17000  1.000 71.78000  ? 198 LYS D CB  1 
ATOM   12174 C  CG  . LYS D  1 167 ? -22.33200 -28.76300 -1.90800  1.000 73.06000  ? 198 LYS D CG  1 
ATOM   12175 C  CD  . LYS D  1 167 ? -21.06400 -29.02700 -2.69300  1.000 72.71000  ? 198 LYS D CD  1 
ATOM   12176 C  CE  . LYS D  1 167 ? -21.31700 -29.78700 -3.98500  1.000 77.05000  ? 198 LYS D CE  1 
ATOM   12177 N  NZ  . LYS D  1 167 ? -20.02000 -30.00200 -4.70300  1.000 77.23000  ? 198 LYS D NZ  1 
ATOM   12178 N  N   . ALA D  1 168 ? -22.11400 -27.90500 2.15200   1.000 72.26000  ? 199 ALA D N   1 
ATOM   12179 C  CA  . ALA D  1 168 ? -21.82400 -28.80600 3.25700   1.000 68.25000  ? 199 ALA D CA  1 
ATOM   12180 C  C   . ALA D  1 168 ? -22.82500 -28.66300 4.39400   1.000 66.67000  ? 199 ALA D C   1 
ATOM   12181 O  O   . ALA D  1 168 ? -22.58200 -29.18800 5.48500   1.000 66.07000  ? 199 ALA D O   1 
ATOM   12182 C  CB  . ALA D  1 168 ? -20.39900 -28.58000 3.76900   1.000 55.31000  ? 199 ALA D CB  1 
ATOM   12183 N  N   . GLY D  1 169 ? -23.95100 -27.99000 4.15100   1.000 69.60000  ? 200 GLY D N   1 
ATOM   12184 C  CA  . GLY D  1 169 ? -24.97500 -27.77800 5.16700   1.000 68.35000  ? 200 GLY D CA  1 
ATOM   12185 C  C   . GLY D  1 169 ? -24.50400 -27.08300 6.42600   1.000 78.36000  ? 200 GLY D C   1 
ATOM   12186 O  O   . GLY D  1 169 ? -24.93600 -27.44000 7.53000   1.000 85.07000  ? 200 GLY D O   1 
ATOM   12187 N  N   . ASN D  1 170 ? -23.59700 -26.13200 6.29300   1.000 77.15000  ? 201 ASN D N   1 
ATOM   12188 C  CA  . ASN D  1 170 ? -23.16200 -25.32400 7.42700   1.000 81.25000  ? 201 ASN D CA  1 
ATOM   12189 C  C   . ASN D  1 170 ? -24.32200 -24.47600 7.94300   1.000 84.10000  ? 201 ASN D C   1 
ATOM   12190 O  O   . ASN D  1 170 ? -24.88900 -23.69000 7.17300   1.000 81.21000  ? 201 ASN D O   1 
ATOM   12191 C  CB  . ASN D  1 170 ? -21.98700 -24.44600 7.00700   1.000 81.99000  ? 201 ASN D CB  1 
ATOM   12192 C  CG  . ASN D  1 170 ? -21.37700 -23.68400 8.16100   1.000 83.30000  ? 201 ASN D CG  1 
ATOM   12193 O  OD1 . ASN D  1 170 ? -22.01800 -23.44000 9.18800   1.000 83.01000  ? 201 ASN D OD1 1 
ATOM   12194 N  ND2 . ASN D  1 170 ? -20.12200 -23.29600 7.99400   1.000 82.85000  ? 201 ASN D ND2 1 
ATOM   12195 N  N   . PRO D  1 171 ? -24.73200 -24.62000 9.20900   1.000 89.78000  ? 202 PRO D N   1 
ATOM   12196 C  CA  . PRO D  1 171 ? -25.84200 -23.81300 9.73300   1.000 83.88000  ? 202 PRO D CA  1 
ATOM   12197 C  C   . PRO D  1 171 ? -25.43200 -22.45000 10.27400  1.000 86.05000  ? 202 PRO D C   1 
ATOM   12198 O  O   . PRO D  1 171 ? -26.32000 -21.65900 10.62800  1.000 85.40000  ? 202 PRO D O   1 
ATOM   12199 C  CB  . PRO D  1 171 ? -26.38400 -24.69100 10.86700  1.000 86.91000  ? 202 PRO D CB  1 
ATOM   12200 C  CG  . PRO D  1 171 ? -25.13600 -25.39200 11.39700  1.000 88.25000  ? 202 PRO D CG  1 
ATOM   12201 C  CD  . PRO D  1 171 ? -24.18400 -25.54300 10.22600  1.000 82.72000  ? 202 PRO D CD  1 
ATOM   12202 N  N   . ASN D  1 172 ? -24.12700 -22.15400 10.34100  1.000 87.38000  ? 203 ASN D N   1 
ATOM   12203 C  CA  . ASN D  1 172 ? -23.60900 -20.90900 10.91700  1.000 87.91000  ? 203 ASN D CA  1 
ATOM   12204 C  C   . ASN D  1 172 ? -22.57800 -20.27500 9.97700   1.000 82.42000  ? 203 ASN D C   1 
ATOM   12205 O  O   . ASN D  1 172 ? -21.40700 -20.10800 10.31100  1.000 77.87000  ? 203 ASN D O   1 
ATOM   12206 C  CB  . ASN D  1 172 ? -22.98600 -21.18000 12.28300  1.000 90.37000  ? 203 ASN D CB  1 
ATOM   12207 C  CG  . ASN D  1 172 ? -23.90000 -21.97500 13.18500  1.000 92.01000  ? 203 ASN D CG  1 
ATOM   12208 O  OD1 . ASN D  1 172 ? -25.04400 -21.58600 13.42300  1.000 92.88000  ? 203 ASN D OD1 1 
ATOM   12209 N  ND2 . ASN D  1 172 ? -23.41200 -23.11300 13.67000  1.000 92.00000  ? 203 ASN D ND2 1 
ATOM   12210 N  N   . ILE D  1 173 ? -23.03100 -19.91500 8.77800   1.000 83.63000  ? 204 ILE D N   1 
ATOM   12211 C  CA  . ILE D  1 173 ? -22.18600 -19.19000 7.83800   1.000 80.95000  ? 204 ILE D CA  1 
ATOM   12212 C  C   . ILE D  1 173 ? -22.01800 -17.75200 8.31000   1.000 71.32000  ? 204 ILE D C   1 
ATOM   12213 O  O   . ILE D  1 173 ? -22.99800 -17.07900 8.65800   1.000 71.12000  ? 204 ILE D O   1 
ATOM   12214 C  CB  . ILE D  1 173 ? -22.79100 -19.22600 6.42400   1.000 79.83000  ? 204 ILE D CB  1 
ATOM   12215 C  CG1 . ILE D  1 173 ? -23.75100 -20.41800 6.26100   1.000 84.47000  ? 204 ILE D CG1 1 
ATOM   12216 C  CG2 . ILE D  1 173 ? -21.68500 -19.22700 5.37100   1.000 67.34000  ? 204 ILE D CG2 1 
ATOM   12217 C  CD1 . ILE D  1 173 ? -25.22600 -20.07200 6.48200   1.000 75.91000  ? 204 ILE D CD1 1 
ATOM   12218 N  N   . ARG D  1 174 ? -20.77900 -17.26600 8.30100   1.000 71.51000  ? 205 ARG D N   1 
ATOM   12219 C  CA  . ARG D  1 174 ? -20.50900 -15.88600 8.69100   1.000 73.73000  ? 205 ARG D CA  1 
ATOM   12220 C  C   . ARG D  1 174 ? -21.05800 -14.93700 7.63200   1.000 69.42000  ? 205 ARG D C   1 
ATOM   12221 O  O   . ARG D  1 174 ? -20.94500 -15.19800 6.42900   1.000 67.70000  ? 205 ARG D O   1 
ATOM   12222 C  CB  . ARG D  1 174 ? -19.00200 -15.66700 8.85900   1.000 70.63000  ? 205 ARG D CB  1 
ATOM   12223 C  CG  . ARG D  1 174 ? -18.39400 -16.34500 10.08000  1.000 67.88000  ? 205 ARG D CG  1 
ATOM   12224 C  CD  . ARG D  1 174 ? -16.85900 -16.33900 10.06600  1.000 75.01000  ? 205 ARG D CD  1 
ATOM   12225 N  NE  . ARG D  1 174 ? -16.26600 -15.01500 9.89300   1.000 72.53000  ? 205 ARG D NE  1 
ATOM   12226 C  CZ  . ARG D  1 174 ? -15.56900 -14.64100 8.82600   1.000 81.91000  ? 205 ARG D CZ  1 
ATOM   12227 N  NH1 . ARG D  1 174 ? -15.35200 -15.46900 7.81300   1.000 78.04000  ? 205 ARG D NH1 1 
ATOM   12228 N  NH2 . ARG D  1 174 ? -15.07000 -13.40500 8.77400   1.000 80.13000  ? 205 ARG D NH2 1 
ATOM   12229 N  N   . ASP D  1 175 ? -21.70200 -13.85000 8.07000   1.000 67.38000  ? 206 ASP D N   1 
ATOM   12230 C  CA  . ASP D  1 175 ? -22.22400 -12.93300 7.06000   1.000 66.21000  ? 206 ASP D CA  1 
ATOM   12231 C  C   . ASP D  1 175 ? -21.12100 -12.14800 6.34800   1.000 61.64000  ? 206 ASP D C   1 
ATOM   12232 O  O   . ASP D  1 175 ? -21.37500 -11.58800 5.27900   1.000 61.21000  ? 206 ASP D O   1 
ATOM   12233 C  CB  . ASP D  1 175 ? -23.31300 -11.99900 7.63600   1.000 66.86000  ? 206 ASP D CB  1 
ATOM   12234 C  CG  . ASP D  1 175 ? -22.88200 -11.21200 8.87900   1.000 73.45000  ? 206 ASP D CG  1 
ATOM   12235 O  OD1 . ASP D  1 175 ? -21.68200 -11.18100 9.24600   1.000 64.72000  ? 206 ASP D OD1 1 
ATOM   12236 O  OD2 . ASP D  1 175 ? -23.79900 -10.60200 9.48900   1.000 72.49000  ? 206 ASP D OD2 1 
ATOM   12237 N  N   . TYR D  1 176 ? -19.89400 -12.13200 6.86500   1.000 56.16000  ? 207 TYR D N   1 
ATOM   12238 C  CA  . TYR D  1 176 ? -18.81700 -11.52700 6.08800   1.000 62.51000  ? 207 TYR D CA  1 
ATOM   12239 C  C   . TYR D  1 176 ? -18.57700 -12.23400 4.75300   1.000 64.01000  ? 207 TYR D C   1 
ATOM   12240 O  O   . TYR D  1 176 ? -17.83500 -11.70100 3.91800   1.000 59.09000  ? 207 TYR D O   1 
ATOM   12241 C  CB  . TYR D  1 176 ? -17.51300 -11.52300 6.88300   1.000 67.84000  ? 207 TYR D CB  1 
ATOM   12242 C  CG  . TYR D  1 176 ? -17.33500 -10.32200 7.78200   1.000 65.95000  ? 207 TYR D CG  1 
ATOM   12243 C  CD1 . TYR D  1 176 ? -18.32500 -9.96100  8.69900   1.000 64.45000  ? 207 TYR D CD1 1 
ATOM   12244 C  CD2 . TYR D  1 176 ? -16.17500 -9.55700  7.72900   1.000 59.22000  ? 207 TYR D CD2 1 
ATOM   12245 C  CE1 . TYR D  1 176 ? -18.16200 -8.86600  9.53700   1.000 62.49000  ? 207 TYR D CE1 1 
ATOM   12246 C  CE2 . TYR D  1 176 ? -16.00300 -8.45800  8.56100   1.000 60.26000  ? 207 TYR D CE2 1 
ATOM   12247 C  CZ  . TYR D  1 176 ? -16.99500 -8.12300  9.46400   1.000 61.59000  ? 207 TYR D CZ  1 
ATOM   12248 O  OH  . TYR D  1 176 ? -16.82400 -7.03600  10.28400  1.000 65.77000  ? 207 TYR D OH  1 
ATOM   12249 N  N   . VAL D  1 177 ? -19.15800 -13.41700 4.53100   1.000 64.76000  ? 208 VAL D N   1 
ATOM   12250 C  CA  . VAL D  1 177 ? -18.98800 -14.12900 3.27000   1.000 65.51000  ? 208 VAL D CA  1 
ATOM   12251 C  C   . VAL D  1 177 ? -20.29200 -14.31900 2.49900   1.000 60.11000  ? 208 VAL D C   1 
ATOM   12252 O  O   . VAL D  1 177 ? -20.27400 -14.97300 1.45600   1.000 61.35000  ? 208 VAL D O   1 
ATOM   12253 C  CB  . VAL D  1 177 ? -18.28000 -15.49000 3.46400   1.000 57.94000  ? 208 VAL D CB  1 
ATOM   12254 C  CG1 . VAL D  1 177 ? -16.91400 -15.31600 4.12800   1.000 60.30000  ? 208 VAL D CG1 1 
ATOM   12255 C  CG2 . VAL D  1 177 ? -19.13100 -16.45500 4.25500   1.000 61.11000  ? 208 VAL D CG2 1 
ATOM   12256 N  N   . PHE D  1 178 ? -21.42900 -13.80600 2.98100   1.000 57.63000  ? 209 PHE D N   1 
ATOM   12257 C  CA  . PHE D  1 178 ? -22.65200 -13.90500 2.17700   1.000 61.95000  ? 209 PHE D CA  1 
ATOM   12258 C  C   . PHE D  1 178 ? -22.46600 -13.18100 0.84000   1.000 61.64000  ? 209 PHE D C   1 
ATOM   12259 O  O   . PHE D  1 178 ? -21.81100 -12.14000 0.77400   1.000 63.49000  ? 209 PHE D O   1 
ATOM   12260 C  CB  . PHE D  1 178 ? -23.87300 -13.29200 2.86700   1.000 56.70000  ? 209 PHE D CB  1 
ATOM   12261 C  CG  . PHE D  1 178 ? -24.36900 -14.05700 4.05800   1.000 64.44000  ? 209 PHE D CG  1 
ATOM   12262 C  CD1 . PHE D  1 178 ? -23.71200 -15.19300 4.50800   1.000 64.99000  ? 209 PHE D CD1 1 
ATOM   12263 C  CD2 . PHE D  1 178 ? -25.51700 -13.63700 4.72300   1.000 56.34000  ? 209 PHE D CD2 1 
ATOM   12264 C  CE1 . PHE D  1 178 ? -24.18200 -15.87900 5.61600   1.000 70.16000  ? 209 PHE D CE1 1 
ATOM   12265 C  CE2 . PHE D  1 178 ? -25.99500 -14.31700 5.81600   1.000 62.57000  ? 209 PHE D CE2 1 
ATOM   12266 C  CZ  . PHE D  1 178 ? -25.33000 -15.44000 6.27000   1.000 69.75000  ? 209 PHE D CZ  1 
ATOM   12267 N  N   . PRO D  1 179 ? -23.06900 -13.67900 -0.23300  1.000 65.15000  ? 210 PRO D N   1 
ATOM   12268 C  CA  . PRO D  1 179 ? -23.10200 -12.89500 -1.47000  1.000 63.74000  ? 210 PRO D CA  1 
ATOM   12269 C  C   . PRO D  1 179 ? -23.76900 -11.54500 -1.23900  1.000 64.67000  ? 210 PRO D C   1 
ATOM   12270 O  O   . PRO D  1 179 ? -24.77100 -11.43800 -0.53100  1.000 58.95000  ? 210 PRO D O   1 
ATOM   12271 C  CB  . PRO D  1 179 ? -23.91900 -13.77500 -2.42200  1.000 65.90000  ? 210 PRO D CB  1 
ATOM   12272 C  CG  . PRO D  1 179 ? -24.75800 -14.63200 -1.50900  1.000 64.38000  ? 210 PRO D CG  1 
ATOM   12273 C  CD  . PRO D  1 179 ? -23.83200 -14.93100 -0.36000  1.000 63.12000  ? 210 PRO D CD  1 
ATOM   12274 N  N   . MET D  1 180 ? -23.21300 -10.51300 -1.86800  1.000 63.99000  ? 211 MET D N   1 
ATOM   12275 C  CA  . MET D  1 180 ? -23.79700 -9.18400  -1.81500  1.000 65.62000  ? 211 MET D CA  1 
ATOM   12276 C  C   . MET D  1 180 ? -25.03100 -9.12200  -2.71600  1.000 69.35000  ? 211 MET D C   1 
ATOM   12277 O  O   . MET D  1 180 ? -25.35700 -10.07100 -3.43700  1.000 70.71000  ? 211 MET D O   1 
ATOM   12278 C  CB  . MET D  1 180 ? -22.76200 -8.13300  -2.21800  1.000 65.15000  ? 211 MET D CB  1 
ATOM   12279 C  CG  . MET D  1 180 ? -21.51900 -8.11000  -1.32600  1.000 59.70000  ? 211 MET D CG  1 
ATOM   12280 S  SD  . MET D  1 180 ? -20.51300 -6.62300  -1.52200  1.000 60.33000  ? 211 MET D SD  1 
ATOM   12281 C  CE  . MET D  1 180 ? -20.02300 -6.78300  -3.24400  1.000 61.56000  ? 211 MET D CE  1 
ATOM   12282 N  N   . GLU D  1 181 ? -25.75200 -8.00800  -2.65100  1.000 63.47000  ? 212 GLU D N   1 
ATOM   12283 C  CA  . GLU D  1 181 ? -27.01000 -7.91400  -3.36700  1.000 56.97000  ? 212 GLU D CA  1 
ATOM   12284 C  C   . GLU D  1 181 ? -27.09900 -6.61200  -4.14600  1.000 62.76000  ? 212 GLU D C   1 
ATOM   12285 O  O   . GLU D  1 181 ? -26.42400 -5.62500  -3.84400  1.000 60.98000  ? 212 GLU D O   1 
ATOM   12286 C  CB  . GLU D  1 181 ? -28.20700 -8.01400  -2.42700  1.000 61.33000  ? 212 GLU D CB  1 
ATOM   12287 C  CG  . GLU D  1 181 ? -28.35600 -6.83400  -1.50200  1.000 64.06000  ? 212 GLU D CG  1 
ATOM   12288 C  CD  . GLU D  1 181 ? -29.72000 -6.77500  -0.83900  1.000 60.89000  ? 212 GLU D CD  1 
ATOM   12289 O  OE1 . GLU D  1 181 ? -29.92000 -7.48000  0.18000   1.000 56.51000  ? 212 GLU D OE1 1 
ATOM   12290 O  OE2 . GLU D  1 181 ? -30.58400 -6.02000  -1.33400  1.000 56.72000  ? 212 GLU D OE2 1 
ATOM   12291 N  N   . HIS D  1 182 ? -27.93900 -6.65000  -5.18000  1.000 67.93000  ? 213 HIS D N   1 
ATOM   12292 C  CA  . HIS D  1 182 ? -28.34300 -5.48600  -5.96500  1.000 61.95000  ? 213 HIS D CA  1 
ATOM   12293 C  C   . HIS D  1 182 ? -29.87000 -5.45700  -5.97200  1.000 63.38000  ? 213 HIS D C   1 
ATOM   12294 O  O   . HIS D  1 182 ? -30.49600 -6.13100  -6.79200  1.000 69.52000  ? 213 HIS D O   1 
ATOM   12295 C  CB  . HIS D  1 182 ? -27.78400 -5.55100  -7.38300  1.000 63.36000  ? 213 HIS D CB  1 
ATOM   12296 C  CG  . HIS D  1 182 ? -28.11500 -4.35600  -8.22200  1.000 66.12000  ? 213 HIS D CG  1 
ATOM   12297 N  ND1 . HIS D  1 182 ? -28.12000 -4.39500  -9.60100  1.000 66.33000  ? 213 HIS D ND1 1 
ATOM   12298 C  CD2 . HIS D  1 182 ? -28.45500 -3.09100  -7.87800  1.000 62.85000  ? 213 HIS D CD2 1 
ATOM   12299 C  CE1 . HIS D  1 182 ? -28.44300 -3.20200  -10.06900 1.000 71.17000  ? 213 HIS D CE1 1 
ATOM   12300 N  NE2 . HIS D  1 182 ? -28.64800 -2.39200  -9.04400  1.000 65.82000  ? 213 HIS D NE2 1 
ATOM   12301 N  N   . ASN D  1 183 ? -30.46000 -4.68400  -5.05800  1.000 63.37000  ? 214 ASN D N   1 
ATOM   12302 C  CA  . ASN D  1 183 ? -31.91400 -4.55600  -4.92800  1.000 66.26000  ? 214 ASN D CA  1 
ATOM   12303 C  C   . ASN D  1 183 ? -32.59200 -5.91200  -4.75000  1.000 65.79000  ? 214 ASN D C   1 
ATOM   12304 O  O   . ASN D  1 183 ? -33.67500 -6.15600  -5.28100  1.000 64.12000  ? 214 ASN D O   1 
ATOM   12305 C  CB  . ASN D  1 183 ? -32.51900 -3.80500  -6.11800  1.000 61.94000  ? 214 ASN D CB  1 
ATOM   12306 C  CG  . ASN D  1 183 ? -32.15500 -2.32700  -6.12900  1.000 67.01000  ? 214 ASN D CG  1 
ATOM   12307 O  OD1 . ASN D  1 183 ? -32.22900 -1.65300  -5.10000  1.000 65.33000  ? 214 ASN D OD1 1 
ATOM   12308 N  ND2 . ASN D  1 183 ? -31.79400 -1.80700  -7.30000  1.000 61.29000  ? 214 ASN D ND2 1 
ATOM   12309 N  N   . GLY D  1 184 ? -31.97400 -6.78200  -3.96200  1.000 66.23000  ? 215 GLY D N   1 
ATOM   12310 C  CA  . GLY D  1 184 ? -32.53400 -8.08800  -3.69900  1.000 66.25000  ? 215 GLY D CA  1 
ATOM   12311 C  C   . GLY D  1 184 ? -32.09900 -9.18200  -4.65200  1.000 68.74000  ? 215 GLY D C   1 
ATOM   12312 O  O   . GLY D  1 184 ? -32.73500 -10.23900 -4.67500  1.000 76.92000  ? 215 GLY D O   1 
ATOM   12313 N  N   . LYS D  1 185 ? -31.06300 -8.96300  -5.45500  1.000 65.61000  ? 216 LYS D N   1 
ATOM   12314 C  CA  . LYS D  1 185 ? -30.59200 -9.93000  -6.43300  1.000 69.40000  ? 216 LYS D CA  1 
ATOM   12315 C  C   . LYS D  1 185 ? -29.10900 -10.21100 -6.25300  1.000 71.98000  ? 216 LYS D C   1 
ATOM   12316 O  O   . LYS D  1 185 ? -28.36300 -9.36200  -5.75300  1.000 68.75000  ? 216 LYS D O   1 
ATOM   12317 C  CB  . LYS D  1 185 ? -30.89500 -9.43000  -7.85400  1.000 68.39000  ? 216 LYS D CB  1 
ATOM   12318 C  CG  . LYS D  1 185 ? -32.39700 -9.28300  -8.09300  1.000 64.88000  ? 216 LYS D CG  1 
ATOM   12319 C  CD  . LYS D  1 185 ? -32.77700 -9.49400  -9.55600  1.000 67.12000  ? 216 LYS D CD  1 
ATOM   12320 C  CE  . LYS D  1 185 ? -34.29200 -9.42900  -9.73800  1.000 75.10000  ? 216 LYS D CE  1 
ATOM   12321 N  NZ  . LYS D  1 185 ? -35.02000 -10.41800 -8.87600  1.000 63.34000  ? 216 LYS D NZ  1 
ATOM   12322 N  N   . PRO D  1 186 ? -28.63100 -11.37500 -6.73200  1.000 73.63000  ? 217 PRO D N   1 
ATOM   12323 C  CA  . PRO D  1 186 ? -27.27600 -11.85600 -6.39400  1.000 72.17000  ? 217 PRO D CA  1 
ATOM   12324 C  C   . PRO D  1 186 ? -26.03500 -10.99800 -6.64800  1.000 77.20000  ? 217 PRO D C   1 
ATOM   12325 O  O   . PRO D  1 186 ? -24.93800 -11.46800 -6.31800  1.000 84.35000  ? 217 PRO D O   1 
ATOM   12326 C  CB  . PRO D  1 186 ? -27.17500 -13.14900 -7.21200  1.000 73.14000  ? 217 PRO D CB  1 
ATOM   12327 C  CG  . PRO D  1 186 ? -28.56900 -13.63800 -7.29300  1.000 74.82000  ? 217 PRO D CG  1 
ATOM   12328 C  CD  . PRO D  1 186 ? -29.43900 -12.42100 -7.38300  1.000 76.32000  ? 217 PRO D CD  1 
ATOM   12329 N  N   . ALA D  1 187 ? -26.13600 -9.79800  -7.21800  1.000 66.12000  ? 218 ALA D N   1 
ATOM   12330 C  CA  . ALA D  1 187 ? -24.96400 -8.92700  -7.38100  1.000 70.55000  ? 218 ALA D CA  1 
ATOM   12331 C  C   . ALA D  1 187 ? -23.79900 -9.49800  -8.19200  1.000 70.38000  ? 218 ALA D C   1 
ATOM   12332 O  O   . ALA D  1 187 ? -23.27100 -8.80000  -9.06500  1.000 63.01000  ? 218 ALA D O   1 
ATOM   12333 C  CB  . ALA D  1 187 ? -24.42400 -8.51300  -6.00800  1.000 60.66000  ? 218 ALA D CB  1 
ATOM   12334 N  N   . ASN D  1 188 ? -23.37400 -10.73400 -7.89500  1.000 67.47000  ? 219 ASN D N   1 
ATOM   12335 C  CA  . ASN D  1 188 ? -22.31000 -11.44800 -8.62000  1.000 66.37000  ? 219 ASN D CA  1 
ATOM   12336 C  C   . ASN D  1 188 ? -21.05800 -10.59600 -8.82000  1.000 66.49000  ? 219 ASN D C   1 
ATOM   12337 O  O   . ASN D  1 188 ? -20.58600 -10.38400 -9.93800  1.000 73.87000  ? 219 ASN D O   1 
ATOM   12338 C  CB  . ASN D  1 188 ? -22.82800 -11.97200 -9.96600  1.000 64.21000  ? 219 ASN D CB  1 
ATOM   12339 C  CG  . ASN D  1 188 ? -23.94600 -12.97500 -9.80400  1.000 64.06000  ? 219 ASN D CG  1 
ATOM   12340 O  OD1 . ASN D  1 188 ? -23.71100 -14.12100 -9.43100  1.000 68.61000  ? 219 ASN D OD1 1 
ATOM   12341 N  ND2 . ASN D  1 188 ? -25.17300 -12.54300 -10.05500 1.000 63.11000  ? 219 ASN D ND2 1 
ATOM   12342 N  N   . GLU D  1 189 ? -20.51700 -10.11000 -7.71200  1.000 66.15000  ? 220 GLU D N   1 
ATOM   12343 C  CA  . GLU D  1 189 ? -19.33400 -9.27000  -7.78000  1.000 67.30000  ? 220 GLU D CA  1 
ATOM   12344 C  C   . GLU D  1 189 ? -18.13500 -10.06200 -8.29800  1.000 72.09000  ? 220 GLU D C   1 
ATOM   12345 O  O   . GLU D  1 189 ? -18.00500 -11.26800 -8.06200  1.000 69.23000  ? 220 GLU D O   1 
ATOM   12346 C  CB  . GLU D  1 189 ? -19.03000 -8.67900  -6.40400  1.000 64.94000  ? 220 GLU D CB  1 
ATOM   12347 C  CG  . GLU D  1 189 ? -17.78700 -7.81300  -6.37200  1.000 68.84000  ? 220 GLU D CG  1 
ATOM   12348 C  CD  . GLU D  1 189 ? -17.83500 -6.69200  -7.39600  1.000 70.87000  ? 220 GLU D CD  1 
ATOM   12349 O  OE1 . GLU D  1 189 ? -18.70800 -5.80500  -7.27800  1.000 65.35000  ? 220 GLU D OE1 1 
ATOM   12350 O  OE2 . GLU D  1 189 ? -16.99800 -6.70400  -8.32100  1.000 74.03000  ? 220 GLU D OE2 1 
ATOM   12351 N  N   . THR D  1 190 ? -17.27600 -9.37300  -9.06400  1.000 66.29000  ? 221 THR D N   1 
ATOM   12352 C  CA  . THR D  1 190 ? -16.07500 -9.97900  -9.63000  1.000 70.29000  ? 221 THR D CA  1 
ATOM   12353 C  C   . THR D  1 190 ? -14.81000 -9.19000  -9.29200  1.000 70.56000  ? 221 THR D C   1 
ATOM   12354 O  O   . THR D  1 190 ? -13.73500 -9.52900  -9.78900  1.000 67.43000  ? 221 THR D O   1 
ATOM   12355 C  CB  . THR D  1 190 ? -16.18400 -10.11500 -11.15600 1.000 67.98000  ? 221 THR D CB  1 
ATOM   12356 O  OG1 . THR D  1 190 ? -16.24900 -8.81400  -11.74900 1.000 67.88000  ? 221 THR D OG1 1 
ATOM   12357 C  CG2 . THR D  1 190 ? -17.45700 -10.85800 -11.52100 1.000 60.83000  ? 221 THR D CG2 1 
ATOM   12358 N  N   . GLU D  1 191 ? -14.89800 -8.16000  -8.45700  1.000 67.99000  ? 222 GLU D N   1 
ATOM   12359 C  CA  . GLU D  1 191 ? -13.75000 -7.32400  -8.15900  1.000 67.04000  ? 222 GLU D CA  1 
ATOM   12360 C  C   . GLU D  1 191 ? -13.61200 -7.12000  -6.66300  1.000 62.47000  ? 222 GLU D C   1 
ATOM   12361 O  O   . GLU D  1 191 ? -14.58200 -7.22800  -5.91200  1.000 62.58000  ? 222 GLU D O   1 
ATOM   12362 C  CB  . GLU D  1 191 ? -13.89900 -5.92400  -8.76800  1.000 66.79000  ? 222 GLU D CB  1 
ATOM   12363 C  CG  . GLU D  1 191 ? -13.58200 -5.75400  -10.22300 1.000 72.47000  ? 222 GLU D CG  1 
ATOM   12364 C  CD  . GLU D  1 191 ? -13.46600 -4.27100  -10.58000 1.000 78.11000  ? 222 GLU D CD  1 
ATOM   12365 O  OE1 . GLU D  1 191 ? -14.51900 -3.61000  -10.72800 1.000 78.08000  ? 222 GLU D OE1 1 
ATOM   12366 O  OE2 . GLU D  1 191 ? -12.32200 -3.76000  -10.67700 1.000 72.92000  ? 222 GLU D OE2 1 
ATOM   12367 N  N   . TYR D  1 192 ? -12.38400 -6.80600  -6.25000  1.000 62.22000  ? 223 TYR D N   1 
ATOM   12368 C  CA  . TYR D  1 192 ? -12.09800 -6.23100  -4.94200  1.000 60.51000  ? 223 TYR D CA  1 
ATOM   12369 C  C   . TYR D  1 192 ? -13.20200 -5.24800  -4.57800  1.000 61.09000  ? 223 TYR D C   1 
ATOM   12370 O  O   . TYR D  1 192 ? -13.37200 -4.22200  -5.24600  1.000 66.00000  ? 223 TYR D O   1 
ATOM   12371 C  CB  . TYR D  1 192 ? -10.74300 -5.53200  -5.00700  1.000 63.38000  ? 223 TYR D CB  1 
ATOM   12372 C  CG  . TYR D  1 192 ? -10.18000 -5.02100  -3.70400  1.000 60.80000  ? 223 TYR D CG  1 
ATOM   12373 C  CD1 . TYR D  1 192 ? -9.92600  -5.87500  -2.64100  1.000 63.06000  ? 223 TYR D CD1 1 
ATOM   12374 C  CD2 . TYR D  1 192 ? -9.86800  -3.67800  -3.55600  1.000 61.17000  ? 223 TYR D CD2 1 
ATOM   12375 C  CE1 . TYR D  1 192 ? -9.39100  -5.39000  -1.45700  1.000 60.78000  ? 223 TYR D CE1 1 
ATOM   12376 C  CE2 . TYR D  1 192 ? -9.33000  -3.18800  -2.39000  1.000 61.24000  ? 223 TYR D CE2 1 
ATOM   12377 C  CZ  . TYR D  1 192 ? -9.09200  -4.04100  -1.34800  1.000 61.46000  ? 223 TYR D CZ  1 
ATOM   12378 O  OH  . TYR D  1 192 ? -8.56300  -3.52300  -0.19500  1.000 62.55000  ? 223 TYR D OH  1 
ATOM   12379 N  N   . ILE D  1 193 ? -13.96700 -5.55300  -3.52400  1.000 61.88000  ? 224 ILE D N   1 
ATOM   12380 C  CA  . ILE D  1 193 ? -15.28600 -4.93000  -3.39500  1.000 62.93000  ? 224 ILE D CA  1 
ATOM   12381 C  C   . ILE D  1 193 ? -15.17900 -3.41500  -3.26000  1.000 62.60000  ? 224 ILE D C   1 
ATOM   12382 O  O   . ILE D  1 193 ? -16.11500 -2.69000  -3.62400  1.000 64.54000  ? 224 ILE D O   1 
ATOM   12383 C  CB  . ILE D  1 193 ? -16.08500 -5.54200  -2.22200  1.000 61.29000  ? 224 ILE D CB  1 
ATOM   12384 C  CG1 . ILE D  1 193 ? -15.46100 -5.19900  -0.86500  1.000 55.64000  ? 224 ILE D CG1 1 
ATOM   12385 C  CG2 . ILE D  1 193 ? -16.21800 -7.05400  -2.40600  1.000 53.87000  ? 224 ILE D CG2 1 
ATOM   12386 C  CD1 . ILE D  1 193 ? -16.27500 -5.72800  0.29500   1.000 53.71000  ? 224 ILE D CD1 1 
ATOM   12387 N  N   . THR D  1 194 ? -14.05300 -2.91100  -2.74700  1.000 53.89000  ? 225 THR D N   1 
ATOM   12388 C  CA  . THR D  1 194 ? -13.81500 -1.47200  -2.76500  1.000 58.69000  ? 225 THR D CA  1 
ATOM   12389 C  C   . THR D  1 194 ? -13.84000 -0.93400  -4.19100  1.000 58.61000  ? 225 THR D C   1 
ATOM   12390 O  O   . THR D  1 194 ? -14.39000 0.14300   -4.44400  1.000 53.98000  ? 225 THR D O   1 
ATOM   12391 C  CB  . THR D  1 194 ? -12.47400 -1.13800  -2.10600  1.000 57.56000  ? 225 THR D CB  1 
ATOM   12392 O  OG1 . THR D  1 194 ? -12.52700 -1.49800  -0.72900  1.000 58.13000  ? 225 THR D OG1 1 
ATOM   12393 C  CG2 . THR D  1 194 ? -12.20600 0.35400   -2.19300  1.000 53.27000  ? 225 THR D CG2 1 
ATOM   12394 N  N   . ASP D  1 195 ? -13.20200 -1.64400  -5.12500  1.000 55.07000  ? 226 ASP D N   1 
ATOM   12395 C  CA  . ASP D  1 195 ? -13.27200 -1.24200  -6.52500  1.000 59.84000  ? 226 ASP D CA  1 
ATOM   12396 C  C   . ASP D  1 195 ? -14.68600 -1.39900  -7.08200  1.000 65.56000  ? 226 ASP D C   1 
ATOM   12397 O  O   . ASP D  1 195 ? -15.14500 -0.55700  -7.86300  1.000 65.95000  ? 226 ASP D O   1 
ATOM   12398 C  CB  . ASP D  1 195 ? -12.26600 -2.04100  -7.35000  1.000 57.64000  ? 226 ASP D CB  1 
ATOM   12399 C  CG  . ASP D  1 195 ? -10.82900 -1.66000  -7.03500  1.000 62.88000  ? 226 ASP D CG  1 
ATOM   12400 O  OD1 . ASP D  1 195 ? -10.61300 -0.58500  -6.43000  1.000 69.62000  ? 226 ASP D OD1 1 
ATOM   12401 O  OD2 . ASP D  1 195 ? -9.91200  -2.41600  -7.41400  1.000 66.22000  ? 226 ASP D OD2 1 
ATOM   12402 N  N   . GLY D  1 196 ? -15.40000 -2.45400  -6.67200  1.000 70.05000  ? 227 GLY D N   1 
ATOM   12403 C  CA  . GLY D  1 196 ? -16.77400 -2.63300  -7.12300  1.000 61.19000  ? 227 GLY D CA  1 
ATOM   12404 C  C   . GLY D  1 196 ? -17.70600 -1.54700  -6.62000  1.000 63.12000  ? 227 GLY D C   1 
ATOM   12405 O  O   . GLY D  1 196 ? -18.59800 -1.09500  -7.34600  1.000 63.54000  ? 227 GLY D O   1 
ATOM   12406 N  N   . PHE D  1 197 ? -17.52300 -1.11800  -5.36800  1.000 61.20000  ? 228 PHE D N   1 
ATOM   12407 C  CA  . PHE D  1 197 ? -18.34800 -0.04200  -4.83200  1.000 59.42000  ? 228 PHE D CA  1 
ATOM   12408 C  C   . PHE D  1 197 ? -18.08000 1.27200   -5.56000  1.000 64.42000  ? 228 PHE D C   1 
ATOM   12409 O  O   . PHE D  1 197 ? -18.99800 2.08000   -5.74400  1.000 60.19000  ? 228 PHE D O   1 
ATOM   12410 C  CB  . PHE D  1 197 ? -18.10900 0.09900   -3.33100  1.000 59.80000  ? 228 PHE D CB  1 
ATOM   12411 C  CG  . PHE D  1 197 ? -18.60600 -1.07400  -2.52300  1.000 59.71000  ? 228 PHE D CG  1 
ATOM   12412 C  CD1 . PHE D  1 197 ? -19.74200 -1.75900  -2.90500  1.000 58.67000  ? 228 PHE D CD1 1 
ATOM   12413 C  CD2 . PHE D  1 197 ? -17.92200 -1.50000  -1.38700  1.000 60.66000  ? 228 PHE D CD2 1 
ATOM   12414 C  CE1 . PHE D  1 197 ? -20.20200 -2.83800  -2.16400  1.000 59.43000  ? 228 PHE D CE1 1 
ATOM   12415 C  CE2 . PHE D  1 197 ? -18.37400 -2.58200  -0.64200  1.000 58.07000  ? 228 PHE D CE2 1 
ATOM   12416 C  CZ  . PHE D  1 197 ? -19.51300 -3.25000  -1.02900  1.000 57.69000  ? 228 PHE D CZ  1 
ATOM   12417 N  N   . SER D  1 198 ? -16.82400 1.51400   -5.96000  1.000 61.40000  ? 229 SER D N   1 
ATOM   12418 C  CA  . SER D  1 198 ? -16.51200 2.68600   -6.77700  1.000 61.85000  ? 229 SER D CA  1 
ATOM   12419 C  C   . SER D  1 198 ? -17.19800 2.60200   -8.12600  1.000 65.48000  ? 229 SER D C   1 
ATOM   12420 O  O   . SER D  1 198 ? -17.81300 3.56900   -8.59100  1.000 66.68000  ? 229 SER D O   1 
ATOM   12421 C  CB  . SER D  1 198 ? -14.99900 2.82200   -6.97900  1.000 61.72000  ? 229 SER D CB  1 
ATOM   12422 O  OG  . SER D  1 198 ? -14.29900 2.85300   -5.75300  1.000 56.35000  ? 229 SER D OG  1 
ATOM   12423 N  N   . ARG D  1 199 ? -17.10600 1.44500   -8.76800  1.000 64.51000  ? 230 ARG D N   1 
ATOM   12424 C  CA  . ARG D  1 199 ? -17.73600 1.26700   -10.06700 1.000 62.85000  ? 230 ARG D CA  1 
ATOM   12425 C  C   . ARG D  1 199 ? -19.25400 1.45600   -9.99500  1.000 66.37000  ? 230 ARG D C   1 
ATOM   12426 O  O   . ARG D  1 199 ? -19.85200 2.04400   -10.90300 1.000 66.63000  ? 230 ARG D O   1 
ATOM   12427 C  CB  . ARG D  1 199 ? -17.30000 -0.08600  -10.63400 1.000 65.65000  ? 230 ARG D CB  1 
ATOM   12428 C  CG  . ARG D  1 199 ? -18.04300 -0.63100  -11.82000 1.000 59.28000  ? 230 ARG D CG  1 
ATOM   12429 C  CD  . ARG D  1 199 ? -17.52500 -2.04200  -12.06300 1.000 74.98000  ? 230 ARG D CD  1 
ATOM   12430 N  NE  . ARG D  1 199 ? -17.73300 -2.90400  -10.90500 1.000 79.98000  ? 230 ARG D NE  1 
ATOM   12431 C  CZ  . ARG D  1 199 ? -18.87000 -3.51800  -10.62500 1.000 72.63000  ? 230 ARG D CZ  1 
ATOM   12432 N  NH1 . ARG D  1 199 ? -19.91900 -3.41900  -11.42300 1.000 71.09000  ? 230 ARG D NH1 1 
ATOM   12433 N  NH2 . ARG D  1 199 ? -18.95600 -4.24300  -9.51500  1.000 67.05000  ? 230 ARG D NH2 1 
ATOM   12434 N  N   . GLU D  1 200 ? -19.89700 1.00200   -8.91400  1.000 64.32000  ? 231 GLU D N   1 
ATOM   12435 C  CA  . GLU D  1 200 ? -21.34000 1.20300   -8.80600  1.000 63.61000  ? 231 GLU D CA  1 
ATOM   12436 C  C   . GLU D  1 200 ? -21.69300 2.67200   -8.58700  1.000 65.64000  ? 231 GLU D C   1 
ATOM   12437 O  O   . GLU D  1 200 ? -22.69700 3.16200   -9.11600  1.000 65.00000  ? 231 GLU D O   1 
ATOM   12438 C  CB  . GLU D  1 200 ? -21.91000 0.34000   -7.68600  1.000 63.15000  ? 231 GLU D CB  1 
ATOM   12439 C  CG  . GLU D  1 200 ? -21.88600 -1.13300  -8.02200  1.000 72.47000  ? 231 GLU D CG  1 
ATOM   12440 C  CD  . GLU D  1 200 ? -22.64800 -1.46000  -9.29200  1.000 69.55000  ? 231 GLU D CD  1 
ATOM   12441 O  OE1 . GLU D  1 200 ? -23.80700 -1.00300  -9.42000  1.000 73.08000  ? 231 GLU D OE1 1 
ATOM   12442 O  OE2 . GLU D  1 200 ? -22.09500 -2.17300  -10.15900 1.000 69.68000  ? 231 GLU D OE2 1 
ATOM   12443 N  N   . ALA D  1 201 ? -20.87200 3.40100   -7.83700  1.000 62.65000  ? 232 ALA D N   1 
ATOM   12444 C  CA  . ALA D  1 201 ? -21.11500 4.82700   -7.69000  1.000 60.88000  ? 232 ALA D CA  1 
ATOM   12445 C  C   . ALA D  1 201 ? -21.00500 5.53600   -9.03500  1.000 63.04000  ? 232 ALA D C   1 
ATOM   12446 O  O   . ALA D  1 201 ? -21.79100 6.44200   -9.33200  1.000 62.32000  ? 232 ALA D O   1 
ATOM   12447 C  CB  . ALA D  1 201 ? -20.15400 5.42100   -6.66600  1.000 57.95000  ? 232 ALA D CB  1 
ATOM   12448 N  N   . ILE D  1 202 ? -20.03500 5.14100   -9.86000  1.000 62.59000  ? 233 ILE D N   1 
ATOM   12449 C  CA  . ILE D  1 202 ? -19.92400 5.71400   -11.19700 1.000 64.25000  ? 233 ILE D CA  1 
ATOM   12450 C  C   . ILE D  1 202 ? -21.17800 5.42100   -12.01100 1.000 63.68000  ? 233 ILE D C   1 
ATOM   12451 O  O   . ILE D  1 202 ? -21.71200 6.30200   -12.70000 1.000 63.63000  ? 233 ILE D O   1 
ATOM   12452 C  CB  . ILE D  1 202 ? -18.66700 5.17900   -11.90700 1.000 61.44000  ? 233 ILE D CB  1 
ATOM   12453 C  CG1 . ILE D  1 202 ? -17.40800 5.82000   -11.32600 1.000 65.22000  ? 233 ILE D CG1 1 
ATOM   12454 C  CG2 . ILE D  1 202 ? -18.78400 5.39200   -13.41800 1.000 58.33000  ? 233 ILE D CG2 1 
ATOM   12455 C  CD1 . ILE D  1 202 ? -16.11600 5.09300   -11.67900 1.000 63.83000  ? 233 ILE D CD1 1 
ATOM   12456 N  N   . LYS D  1 203 ? -21.66900 4.18300   -11.94500 1.000 60.96000  ? 234 LYS D N   1 
ATOM   12457 C  CA  . LYS D  1 203 ? -22.87200 3.82900   -12.69100 1.000 66.38000  ? 234 LYS D CA  1 
ATOM   12458 C  C   . LYS D  1 203 ? -24.05300 4.68200   -12.25200 1.000 62.99000  ? 234 LYS D C   1 
ATOM   12459 O  O   . LYS D  1 203 ? -24.78700 5.21900   -13.08500 1.000 65.07000  ? 234 LYS D O   1 
ATOM   12460 C  CB  . LYS D  1 203 ? -23.18800 2.33800   -12.51100 1.000 67.93000  ? 234 LYS D CB  1 
ATOM   12461 C  CG  . LYS D  1 203 ? -24.50900 1.88200   -13.13400 1.000 62.78000  ? 234 LYS D CG  1 
ATOM   12462 C  CD  . LYS D  1 203 ? -24.72800 0.37700   -13.00700 1.000 63.43000  ? 234 LYS D CD  1 
ATOM   12463 C  CE  . LYS D  1 203 ? -26.07500 -0.04600  -13.59700 1.000 64.17000  ? 234 LYS D CE  1 
ATOM   12464 N  NZ  . LYS D  1 203 ? -26.35600 -1.52000  -13.49100 1.000 70.72000  ? 234 LYS D NZ  1 
ATOM   12465 N  N   . ASN D  1 204 ? -24.23100 4.84800   -10.94100 1.000 63.34000  ? 235 ASN D N   1 
ATOM   12466 C  CA  . ASN D  1 204 ? -25.37100 5.60900   -10.45100 1.000 63.56000  ? 235 ASN D CA  1 
ATOM   12467 C  C   . ASN D  1 204 ? -25.24500 7.09500   -10.76600 1.000 63.32000  ? 235 ASN D C   1 
ATOM   12468 O  O   . ASN D  1 204 ? -26.26600 7.77300   -10.90300 1.000 61.92000  ? 235 ASN D O   1 
ATOM   12469 C  CB  . ASN D  1 204 ? -25.54800 5.38200   -8.94900  1.000 66.97000  ? 235 ASN D CB  1 
ATOM   12470 C  CG  . ASN D  1 204 ? -26.27700 4.08500   -8.62900  1.000 63.94000  ? 235 ASN D CG  1 
ATOM   12471 O  OD1 . ASN D  1 204 ? -27.50300 4.04900   -8.53400  1.000 58.68000  ? 235 ASN D OD1 1 
ATOM   12472 N  ND2 . ASN D  1 204 ? -25.52300 3.01000   -8.48500  1.000 71.54000  ? 235 ASN D ND2 1 
ATOM   12473 N  N   . ILE D  1 205 ? -24.02000 7.62200   -10.88500 1.000 61.99000  ? 236 ILE D N   1 
ATOM   12474 C  CA  . ILE D  1 205 ? -23.86000 9.01600   -11.30100 1.000 65.70000  ? 236 ILE D CA  1 
ATOM   12475 C  C   . ILE D  1 205 ? -24.32800 9.19400   -12.73800 1.000 63.37000  ? 236 ILE D C   1 
ATOM   12476 O  O   . ILE D  1 205 ? -24.94500 10.20600  -13.09100 1.000 66.42000  ? 236 ILE D O   1 
ATOM   12477 C  CB  . ILE D  1 205 ? -22.41000 9.49200   -11.10600 1.000 70.24000  ? 236 ILE D CB  1 
ATOM   12478 C  CG1 . ILE D  1 205 ? -22.11200 9.67100   -9.61600  1.000 67.06000  ? 236 ILE D CG1 1 
ATOM   12479 C  CG2 . ILE D  1 205 ? -22.17700 10.81600  -11.82600 1.000 64.94000  ? 236 ILE D CG2 1 
ATOM   12480 C  CD1 . ILE D  1 205 ? -20.64900 9.83800   -9.31800  1.000 65.32000  ? 236 ILE D CD1 1 
ATOM   12481 N  N   . LYS D  1 206 ? -24.02900 8.22200   -13.59000 1.000 65.01000  ? 237 LYS D N   1 
ATOM   12482 C  CA  . LYS D  1 206 ? -24.54200 8.24700   -14.94700 1.000 62.44000  ? 237 LYS D CA  1 
ATOM   12483 C  C   . LYS D  1 206 ? -26.05600 8.03700   -14.97700 1.000 67.02000  ? 237 LYS D C   1 
ATOM   12484 O  O   . LYS D  1 206 ? -26.74100 8.55900   -15.86800 1.000 62.57000  ? 237 LYS D O   1 
ATOM   12485 C  CB  . LYS D  1 206 ? -23.80100 7.19800   -15.75600 1.000 60.81000  ? 237 LYS D CB  1 
ATOM   12486 C  CG  . LYS D  1 206 ? -22.36100 7.61000   -16.01200 1.000 62.55000  ? 237 LYS D CG  1 
ATOM   12487 C  CD  . LYS D  1 206 ? -21.60300 6.41500   -16.54400 1.000 66.63000  ? 237 LYS D CD  1 
ATOM   12488 C  CE  . LYS D  1 206 ? -20.61600 6.79700   -17.64100 1.000 75.69000  ? 237 LYS D CE  1 
ATOM   12489 N  NZ  . LYS D  1 206 ? -19.69400 5.66600   -17.94500 1.000 80.12000  ? 237 LYS D NZ  1 
ATOM   12490 N  N   . ILE D  1 207 ? -26.59600 7.28900   -14.01100 1.000 65.47000  ? 238 ILE D N   1 
ATOM   12491 C  CA  . ILE D  1 207 ? -28.03800 7.06400   -13.96700 1.000 63.02000  ? 238 ILE D CA  1 
ATOM   12492 C  C   . ILE D  1 207 ? -28.75300 8.38300   -13.74400 1.000 64.47000  ? 238 ILE D C   1 
ATOM   12493 O  O   . ILE D  1 207 ? -29.57800 8.81000   -14.55600 1.000 69.41000  ? 238 ILE D O   1 
ATOM   12494 C  CB  . ILE D  1 207 ? -28.40000 6.07100   -12.85200 1.000 67.76000  ? 238 ILE D CB  1 
ATOM   12495 C  CG1 . ILE D  1 207 ? -27.80800 4.69500   -13.12500 1.000 65.95000  ? 238 ILE D CG1 1 
ATOM   12496 C  CG2 . ILE D  1 207 ? -29.90500 5.94300   -12.75500 1.000 63.70000  ? 238 ILE D CG2 1 
ATOM   12497 C  CD1 . ILE D  1 207 ? -27.85800 4.31800   -14.52900 1.000 66.80000  ? 238 ILE D CD1 1 
ATOM   12498 N  N   . ALA D  1 208 ? -28.40800 9.06500   -12.65200 1.000 65.26000  ? 239 ALA D N   1 
ATOM   12499 C  CA  . ALA D  1 208 ? -29.00000 10.36600  -12.36400 1.000 68.59000  ? 239 ALA D CA  1 
ATOM   12500 C  C   . ALA D  1 208 ? -28.70800 11.35500  -13.48100 1.000 69.82000  ? 239 ALA D C   1 
ATOM   12501 O  O   . ALA D  1 208 ? -29.54000 12.22000  -13.78700 1.000 69.09000  ? 239 ALA D O   1 
ATOM   12502 C  CB  . ALA D  1 208 ? -28.49000 10.89700  -11.02700 1.000 64.74000  ? 239 ALA D CB  1 
ATOM   12503 N  N   . ALA D  1 209 ? -27.52500 11.24700  -14.09400 1.000 68.28000  ? 240 ALA D N   1 
ATOM   12504 C  CA  . ALA D  1 209 ? -27.20000 12.11200  -15.21900 1.000 61.21000  ? 240 ALA D CA  1 
ATOM   12505 C  C   . ALA D  1 209 ? -28.17200 11.89300  -16.36600 1.000 68.06000  ? 240 ALA D C   1 
ATOM   12506 O  O   . ALA D  1 209 ? -28.65400 12.85800  -16.97100 1.000 71.66000  ? 240 ALA D O   1 
ATOM   12507 C  CB  . ALA D  1 209 ? -25.76700 11.86300  -15.68300 1.000 63.91000  ? 240 ALA D CB  1 
ATOM   12508 N  N   . ALA D  1 210 ? -28.48100 10.63000  -16.67200 1.000 68.28000  ? 241 ALA D N   1 
ATOM   12509 C  CA  . ALA D  1 210 ? -29.40600 10.34100  -17.76200 1.000 60.85000  ? 241 ALA D CA  1 
ATOM   12510 C  C   . ALA D  1 210 ? -30.82100 10.79400  -17.43600 1.000 62.87000  ? 241 ALA D C   1 
ATOM   12511 O  O   . ALA D  1 210 ? -31.53500 11.30400  -18.31000 1.000 63.18000  ? 241 ALA D O   1 
ATOM   12512 C  CB  . ALA D  1 210 ? -29.40000 8.84600   -18.06600 1.000 60.38000  ? 241 ALA D CB  1 
ATOM   12513 N  N   . LYS D  1 211 ? -31.23200 10.66000  -16.18200 1.000 61.97000  ? 242 LYS D N   1 
ATOM   12514 C  CA  . LYS D  1 211 ? -32.57400 11.06600  -15.80200 1.000 60.92000  ? 242 LYS D CA  1 
ATOM   12515 C  C   . LYS D  1 211 ? -32.72700 12.57500  -15.65600 1.000 66.55000  ? 242 LYS D C   1 
ATOM   12516 O  O   . LYS D  1 211 ? -33.85200 13.03800  -15.44300 1.000 70.75000  ? 242 LYS D O   1 
ATOM   12517 C  CB  . LYS D  1 211 ? -32.97200 10.37600  -14.49800 1.000 59.15000  ? 242 LYS D CB  1 
ATOM   12518 C  CG  . LYS D  1 211 ? -32.99800 8.85800   -14.59200 1.000 54.38000  ? 242 LYS D CG  1 
ATOM   12519 C  CD  . LYS D  1 211 ? -33.32500 8.22300   -13.24100 1.000 55.96000  ? 242 LYS D CD  1 
ATOM   12520 C  CE  . LYS D  1 211 ? -34.83400 8.09900   -13.06600 1.000 65.37000  ? 242 LYS D CE  1 
ATOM   12521 N  NZ  . LYS D  1 211 ? -35.31700 8.06500   -11.65500 1.000 65.93000  ? 242 LYS D NZ  1 
ATOM   12522 N  N   . LYS D  1 212 ? -31.64000 13.34500  -15.78600 1.000 70.92000  ? 243 LYS D N   1 
ATOM   12523 C  CA  . LYS D  1 212 ? -31.62600 14.77500  -15.45900 1.000 68.54000  ? 243 LYS D CA  1 
ATOM   12524 C  C   . LYS D  1 212 ? -32.28300 15.00600  -14.10200 1.000 67.83000  ? 243 LYS D C   1 
ATOM   12525 O  O   . LYS D  1 212 ? -33.15900 15.85500  -13.93400 1.000 72.80000  ? 243 LYS D O   1 
ATOM   12526 C  CB  . LYS D  1 212 ? -32.30100 15.61600  -16.54600 1.000 67.54000  ? 243 LYS D CB  1 
ATOM   12527 C  CG  . LYS D  1 212 ? -31.77400 15.38100  -17.95200 1.000 66.83000  ? 243 LYS D CG  1 
ATOM   12528 C  CD  . LYS D  1 212 ? -30.31700 15.79100  -18.09600 1.000 76.36000  ? 243 LYS D CD  1 
ATOM   12529 C  CE  . LYS D  1 212 ? -30.07700 17.24600  -17.68200 1.000 81.96000  ? 243 LYS D CE  1 
ATOM   12530 N  NZ  . LYS D  1 212 ? -28.67400 17.68100  -17.97600 1.000 74.80000  ? 243 LYS D NZ  1 
ATOM   12531 N  N   . GLN D  1 213 ? -31.84500 14.22400  -13.12600 1.000 65.38000  ? 244 GLN D N   1 
ATOM   12532 C  CA  . GLN D  1 213 ? -32.38500 14.23400  -11.78500 1.000 70.13000  ? 244 GLN D CA  1 
ATOM   12533 C  C   . GLN D  1 213 ? -31.25500 14.43100  -10.78200 1.000 69.12000  ? 244 GLN D C   1 
ATOM   12534 O  O   . GLN D  1 213 ? -30.15400 13.90300  -10.96900 1.000 70.20000  ? 244 GLN D O   1 
ATOM   12535 C  CB  . GLN D  1 213 ? -33.12800 12.91600  -11.53800 1.000 63.33000  ? 244 GLN D CB  1 
ATOM   12536 C  CG  . GLN D  1 213 ? -34.10500 12.88900  -10.39300 1.000 65.25000  ? 244 GLN D CG  1 
ATOM   12537 C  CD  . GLN D  1 213 ? -34.88200 11.59000  -10.40000 1.000 68.95000  ? 244 GLN D CD  1 
ATOM   12538 O  OE1 . GLN D  1 213 ? -35.45900 11.16900  -9.39500  1.000 68.72000  ? 244 GLN D OE1 1 
ATOM   12539 N  NE2 . GLN D  1 213 ? -34.91400 10.95200  -11.56100 1.000 70.02000  ? 244 GLN D NE2 1 
ATOM   12540 N  N   . PRO D  1 214 ? -31.47400 15.21700  -9.73600  1.000 69.94000  ? 245 PRO D N   1 
ATOM   12541 C  CA  . PRO D  1 214 ? -30.45300 15.32100  -8.68700  1.000 73.07000  ? 245 PRO D CA  1 
ATOM   12542 C  C   . PRO D  1 214 ? -30.31500 13.99600  -7.95200  1.000 74.89000  ? 245 PRO D C   1 
ATOM   12543 O  O   . PRO D  1 214 ? -31.31000 13.33000  -7.64800  1.000 72.37000  ? 245 PRO D O   1 
ATOM   12544 C  CB  . PRO D  1 214 ? -30.99400 16.42700  -7.76900  1.000 74.33000  ? 245 PRO D CB  1 
ATOM   12545 C  CG  . PRO D  1 214 ? -32.49100 16.39100  -7.98900  1.000 74.28000  ? 245 PRO D CG  1 
ATOM   12546 C  CD  . PRO D  1 214 ? -32.65800 16.05200  -9.45300  1.000 73.39000  ? 245 PRO D CD  1 
ATOM   12547 N  N   . PHE D  1 215 ? -29.07000 13.61500  -7.65800  1.000 70.69000  ? 246 PHE D N   1 
ATOM   12548 C  CA  . PHE D  1 215 ? -28.82000 12.34900  -6.98900  1.000 69.38000  ? 246 PHE D CA  1 
ATOM   12549 C  C   . PHE D  1 215 ? -28.45000 12.56200  -5.53000  1.000 67.94000  ? 246 PHE D C   1 
ATOM   12550 O  O   . PHE D  1 215 ? -27.94300 13.61400  -5.13100  1.000 70.67000  ? 246 PHE D O   1 
ATOM   12551 C  CB  . PHE D  1 215 ? -27.72800 11.51400  -7.68300  1.000 67.16000  ? 246 PHE D CB  1 
ATOM   12552 C  CG  . PHE D  1 215 ? -26.33000 12.07900  -7.59100  1.000 66.76000  ? 246 PHE D CG  1 
ATOM   12553 C  CD1 . PHE D  1 215 ? -25.62700 12.07400  -6.39700  1.000 63.79000  ? 246 PHE D CD1 1 
ATOM   12554 C  CD2 . PHE D  1 215 ? -25.68900 12.51600  -8.72700  1.000 64.19000  ? 246 PHE D CD2 1 
ATOM   12555 C  CE1 . PHE D  1 215 ? -24.34500 12.56600  -6.32900  1.000 70.15000  ? 246 PHE D CE1 1 
ATOM   12556 C  CE2 . PHE D  1 215 ? -24.40400 12.99500  -8.67000  1.000 67.75000  ? 246 PHE D CE2 1 
ATOM   12557 C  CZ  . PHE D  1 215 ? -23.72800 13.02000  -7.46900  1.000 64.93000  ? 246 PHE D CZ  1 
ATOM   12558 N  N   . PHE D  1 216 ? -28.72900 11.54800  -4.73100  1.000 65.14000  ? 247 PHE D N   1 
ATOM   12559 C  CA  . PHE D  1 216 ? -28.17000 11.44100  -3.39500  1.000 67.66000  ? 247 PHE D CA  1 
ATOM   12560 C  C   . PHE D  1 216 ? -27.55000 10.05600  -3.29500  1.000 68.46000  ? 247 PHE D C   1 
ATOM   12561 O  O   . PHE D  1 216 ? -28.27800 9.06000   -3.26500  1.000 67.60000  ? 247 PHE D O   1 
ATOM   12562 C  CB  . PHE D  1 216 ? -29.24000 11.66400  -2.33600  1.000 65.34000  ? 247 PHE D CB  1 
ATOM   12563 C  CG  . PHE D  1 216 ? -28.79800 11.30400  -0.96900  1.000 65.01000  ? 247 PHE D CG  1 
ATOM   12564 C  CD1 . PHE D  1 216 ? -27.82300 12.05500  -0.32800  1.000 70.06000  ? 247 PHE D CD1 1 
ATOM   12565 C  CD2 . PHE D  1 216 ? -29.35900 10.23300  -0.30400  1.000 64.44000  ? 247 PHE D CD2 1 
ATOM   12566 C  CE1 . PHE D  1 216 ? -27.40500 11.73400  0.95500   1.000 63.67000  ? 247 PHE D CE1 1 
ATOM   12567 C  CE2 . PHE D  1 216 ? -28.94300 9.90300   0.98100   1.000 69.46000  ? 247 PHE D CE2 1 
ATOM   12568 C  CZ  . PHE D  1 216 ? -27.96500 10.65900  1.61100   1.000 62.00000  ? 247 PHE D CZ  1 
ATOM   12569 N  N   . ILE D  1 217 ? -26.21700 9.99000   -3.24100  1.000 65.03000  ? 248 ILE D N   1 
ATOM   12570 C  CA  . ILE D  1 217 ? -25.47900 8.72800   -3.23200  1.000 58.32000  ? 248 ILE D CA  1 
ATOM   12571 C  C   . ILE D  1 217 ? -24.85800 8.55700   -1.85500  1.000 63.41000  ? 248 ILE D C   1 
ATOM   12572 O  O   . ILE D  1 217 ? -24.01800 9.36300   -1.43900  1.000 65.44000  ? 248 ILE D O   1 
ATOM   12573 C  CB  . ILE D  1 217 ? -24.37400 8.69600   -4.29900  1.000 65.83000  ? 248 ILE D CB  1 
ATOM   12574 C  CG1 . ILE D  1 217 ? -24.91900 8.88800   -5.71500  1.000 63.59000  ? 248 ILE D CG1 1 
ATOM   12575 C  CG2 . ILE D  1 217 ? -23.58900 7.39800   -4.19500  1.000 62.71000  ? 248 ILE D CG2 1 
ATOM   12576 C  CD1 . ILE D  1 217 ? -26.31900 8.38600   -5.94100  1.000 68.01000  ? 248 ILE D CD1 1 
ATOM   12577 N  N   . TYR D  1 218 ? -25.23300 7.48500   -1.17100  1.000 62.49000  ? 249 TYR D N   1 
ATOM   12578 C  CA  . TYR D  1 218 ? -24.71000 7.14900   0.15000   1.000 60.96000  ? 249 TYR D CA  1 
ATOM   12579 C  C   . TYR D  1 218 ? -23.67600 6.04500   -0.05300  1.000 61.56000  ? 249 TYR D C   1 
ATOM   12580 O  O   . TYR D  1 218 ? -24.00500 4.85800   -0.07500  1.000 61.39000  ? 249 TYR D O   1 
ATOM   12581 C  CB  . TYR D  1 218 ? -25.85200 6.71900   1.05700   1.000 55.07000  ? 249 TYR D CB  1 
ATOM   12582 C  CG  . TYR D  1 218 ? -25.46700 6.35200   2.46700   1.000 61.83000  ? 249 TYR D CG  1 
ATOM   12583 C  CD1 . TYR D  1 218 ? -25.12200 7.33400   3.39800   1.000 61.09000  ? 249 TYR D CD1 1 
ATOM   12584 C  CD2 . TYR D  1 218 ? -25.47400 5.02600   2.88100   1.000 56.34000  ? 249 TYR D CD2 1 
ATOM   12585 C  CE1 . TYR D  1 218 ? -24.79000 7.00100   4.69500   1.000 51.96000  ? 249 TYR D CE1 1 
ATOM   12586 C  CE2 . TYR D  1 218 ? -25.14300 4.68100   4.17100   1.000 63.87000  ? 249 TYR D CE2 1 
ATOM   12587 C  CZ  . TYR D  1 218 ? -24.80000 5.67100   5.07900   1.000 64.30000  ? 249 TYR D CZ  1 
ATOM   12588 O  OH  . TYR D  1 218 ? -24.47200 5.31300   6.36900   1.000 56.88000  ? 249 TYR D OH  1 
ATOM   12589 N  N   . LEU D  1 219 ? -22.41500 6.44500   -0.21100  1.000 59.23000  ? 250 LEU D N   1 
ATOM   12590 C  CA  . LEU D  1 219 ? -21.31600 5.53200   -0.54200  1.000 58.91000  ? 250 LEU D CA  1 
ATOM   12591 C  C   . LEU D  1 219 ? -20.61900 5.12400   0.75000   1.000 58.06000  ? 250 LEU D C   1 
ATOM   12592 O  O   . LEU D  1 219 ? -19.73000 5.81700   1.25000   1.000 58.56000  ? 250 LEU D O   1 
ATOM   12593 C  CB  . LEU D  1 219 ? -20.35800 6.18300   -1.52900  1.000 56.17000  ? 250 LEU D CB  1 
ATOM   12594 C  CG  . LEU D  1 219 ? -19.08600 5.42500   -1.90900  1.000 62.67000  ? 250 LEU D CG  1 
ATOM   12595 C  CD1 . LEU D  1 219 ? -19.39500 3.98000   -2.27200  1.000 58.32000  ? 250 LEU D CD1 1 
ATOM   12596 C  CD2 . LEU D  1 219 ? -18.37700 6.14400   -3.06300  1.000 55.57000  ? 250 LEU D CD2 1 
ATOM   12597 N  N   . ALA D  1 220 ? -21.04200 3.98000   1.29200   1.000 59.02000  ? 251 ALA D N   1 
ATOM   12598 C  CA  . ALA D  1 220 ? -20.58500 3.48500   2.59300   1.000 57.17000  ? 251 ALA D CA  1 
ATOM   12599 C  C   . ALA D  1 220 ? -19.54200 2.38500   2.40300   1.000 54.02000  ? 251 ALA D C   1 
ATOM   12600 O  O   . ALA D  1 220 ? -19.81600 1.20100   2.57300   1.000 57.41000  ? 251 ALA D O   1 
ATOM   12601 C  CB  . ALA D  1 220 ? -21.77300 2.98000   3.40900   1.000 56.53000  ? 251 ALA D CB  1 
ATOM   12602 N  N   . TYR D  1 221 ? -18.32400 2.79200   2.05000   1.000 57.64000  ? 252 TYR D N   1 
ATOM   12603 C  CA  . TYR D  1 221 ? -17.21100 1.85200   1.99500   1.000 61.57000  ? 252 TYR D CA  1 
ATOM   12604 C  C   . TYR D  1 221 ? -17.08100 1.09000   3.30000   1.000 57.89000  ? 252 TYR D C   1 
ATOM   12605 O  O   . TYR D  1 221 ? -17.23900 1.65700   4.38300   1.000 55.58000  ? 252 TYR D O   1 
ATOM   12606 C  CB  . TYR D  1 221 ? -15.88500 2.57300   1.72600   1.000 55.91000  ? 252 TYR D CB  1 
ATOM   12607 C  CG  . TYR D  1 221 ? -15.71800 3.09200   0.32800   1.000 60.17000  ? 252 TYR D CG  1 
ATOM   12608 C  CD1 . TYR D  1 221 ? -15.47300 2.23100   -0.72600  1.000 55.96000  ? 252 TYR D CD1 1 
ATOM   12609 C  CD2 . TYR D  1 221 ? -15.78400 4.44700   0.06600   1.000 62.30000  ? 252 TYR D CD2 1 
ATOM   12610 C  CE1 . TYR D  1 221 ? -15.30700 2.70400   -2.00500  1.000 56.14000  ? 252 TYR D CE1 1 
ATOM   12611 C  CE2 . TYR D  1 221 ? -15.62300 4.93300   -1.20600  1.000 60.75000  ? 252 TYR D CE2 1 
ATOM   12612 C  CZ  . TYR D  1 221 ? -15.39100 4.06000   -2.24500  1.000 57.59000  ? 252 TYR D CZ  1 
ATOM   12613 O  OH  . TYR D  1 221 ? -15.21500 4.56200   -3.51600  1.000 60.59000  ? 252 TYR D OH  1 
ATOM   12614 N  N   . ASN D  1 222 ? -16.77400 -0.20100  3.19600   1.000 54.82000  ? 253 ASN D N   1 
ATOM   12615 C  CA  . ASN D  1 222 ? -16.35000 -0.88300  4.40900   1.000 57.77000  ? 253 ASN D CA  1 
ATOM   12616 C  C   . ASN D  1 222 ? -14.86100 -0.68300  4.67500   1.000 57.07000  ? 253 ASN D C   1 
ATOM   12617 O  O   . ASN D  1 222 ? -14.41200 -0.93700  5.79600   1.000 52.64000  ? 253 ASN D O   1 
ATOM   12618 C  CB  . ASN D  1 222 ? -16.69800 -2.37600  4.37200   1.000 53.82000  ? 253 ASN D CB  1 
ATOM   12619 C  CG  . ASN D  1 222 ? -16.00500 -3.12800  3.24000   1.000 61.84000  ? 253 ASN D CG  1 
ATOM   12620 O  OD1 . ASN D  1 222 ? -15.94700 -2.65900  2.10300   1.000 61.06000  ? 253 ASN D OD1 1 
ATOM   12621 N  ND2 . ASN D  1 222 ? -15.44900 -4.29300  3.56100   1.000 59.62000  ? 253 ASN D ND2 1 
ATOM   12622 N  N   . ALA D  1 223 ? -14.09700 -0.21100  3.68900   1.000 50.10000  ? 254 ALA D N   1 
ATOM   12623 C  CA  . ALA D  1 223 ? -12.69800 0.12200   3.92900   1.000 57.21000  ? 254 ALA D CA  1 
ATOM   12624 C  C   . ALA D  1 223 ? -12.57900 1.32300   4.87500   1.000 61.63000  ? 254 ALA D C   1 
ATOM   12625 O  O   . ALA D  1 223 ? -13.41600 2.23400   4.84500   1.000 58.13000  ? 254 ALA D O   1 
ATOM   12626 C  CB  . ALA D  1 223 ? -12.00100 0.42700   2.61000   1.000 51.33000  ? 254 ALA D CB  1 
ATOM   12627 N  N   . PRO D  1 224 ? -11.54400 1.35500   5.74100   1.000 54.78000  ? 255 PRO D N   1 
ATOM   12628 C  CA  . PRO D  1 224 ? -10.51300 0.33900   6.00000   1.000 56.35000  ? 255 PRO D CA  1 
ATOM   12629 C  C   . PRO D  1 224 ? -10.78800 -0.58600  7.19800   1.000 53.02000  ? 255 PRO D C   1 
ATOM   12630 O  O   . PRO D  1 224 ? -9.88200  -0.99400  7.88600   1.000 56.96000  ? 255 PRO D O   1 
ATOM   12631 C  CB  . PRO D  1 224 ? -9.27600  1.19800   6.24900   1.000 56.98000  ? 255 PRO D CB  1 
ATOM   12632 C  CG  . PRO D  1 224 ? -9.82200  2.41400   6.94900   1.000 56.97000  ? 255 PRO D CG  1 
ATOM   12633 C  CD  . PRO D  1 224 ? -11.21600 2.63000   6.40700   1.000 53.91000  ? 255 PRO D CD  1 
ATOM   12634 N  N   . HIS D  1 225 ? -12.04200 -0.94300  7.43300   1.000 56.66000  ? 256 HIS D N   1 
ATOM   12635 C  CA  . HIS D  1 225 ? -12.44600 -1.88400  8.47000   1.000 55.26000  ? 256 HIS D CA  1 
ATOM   12636 C  C   . HIS D  1 225 ? -11.84400 -3.27100  8.21000   1.000 59.85000  ? 256 HIS D C   1 
ATOM   12637 O  O   . HIS D  1 225 ? -11.47800 -3.62300  7.08000   1.000 59.26000  ? 256 HIS D O   1 
ATOM   12638 C  CB  . HIS D  1 225 ? -13.97500 -1.93300  8.49600   1.000 50.63000  ? 256 HIS D CB  1 
ATOM   12639 C  CG  . HIS D  1 225 ? -14.57700 -2.63500  9.66700   1.000 59.21000  ? 256 HIS D CG  1 
ATOM   12640 N  ND1 . HIS D  1 225 ? -14.50300 -4.00000  9.84300   1.000 59.67000  ? 256 HIS D ND1 1 
ATOM   12641 C  CD2 . HIS D  1 225 ? -15.35900 -2.16800  10.67000  1.000 59.97000  ? 256 HIS D CD2 1 
ATOM   12642 C  CE1 . HIS D  1 225 ? -15.17200 -4.33800  10.93200  1.000 64.19000  ? 256 HIS D CE1 1 
ATOM   12643 N  NE2 . HIS D  1 225 ? -15.69700 -3.24400  11.45600  1.000 63.25000  ? 256 HIS D NE2 1 
ATOM   12644 N  N   . VAL D  1 226 ? -11.68900 -4.04300  9.28300   1.000 60.12000  ? 257 VAL D N   1 
ATOM   12645 C  CA  . VAL D  1 226 ? -11.19200 -5.41300  9.17800   1.000 60.32000  ? 257 VAL D CA  1 
ATOM   12646 C  C   . VAL D  1 226 ? -12.18200 -6.23200  8.35000   1.000 58.03000  ? 257 VAL D C   1 
ATOM   12647 O  O   . VAL D  1 226 ? -13.36700 -5.87800  8.28000   1.000 56.50000  ? 257 VAL D O   1 
ATOM   12648 C  CB  . VAL D  1 226 ? -10.97900 -6.04000  10.56400  1.000 57.45000  ? 257 VAL D CB  1 
ATOM   12649 C  CG1 . VAL D  1 226 ? -9.76200  -5.43500  11.23500  1.000 57.22000  ? 257 VAL D CG1 1 
ATOM   12650 C  CG2 . VAL D  1 226 ? -12.23600 -5.88800  11.41600  1.000 55.32000  ? 257 VAL D CG2 1 
ATOM   12651 N  N   . PRO D  1 227 ? -11.75600 -7.32700  7.70700   1.000 59.99000  ? 258 PRO D N   1 
ATOM   12652 C  CA  . PRO D  1 227 ? -10.39200 -7.89000  7.67200   1.000 62.09000  ? 258 PRO D CA  1 
ATOM   12653 C  C   . PRO D  1 227 ? -9.43700  -7.04300  6.83600   1.000 62.24000  ? 258 PRO D C   1 
ATOM   12654 O  O   . PRO D  1 227 ? -9.82100  -6.53100  5.77600   1.000 56.95000  ? 258 PRO D O   1 
ATOM   12655 C  CB  . PRO D  1 227 ? -10.61100 -9.26900  7.04500   1.000 59.22000  ? 258 PRO D CB  1 
ATOM   12656 C  CG  . PRO D  1 227 ? -11.78400 -9.03200  6.10900   1.000 54.79000  ? 258 PRO D CG  1 
ATOM   12657 C  CD  . PRO D  1 227 ? -12.68800 -8.11200  6.87700   1.000 54.64000  ? 258 PRO D CD  1 
ATOM   12658 N  N   . LEU D  1 228 ? -8.18700  -6.88200  7.26700   1.000 54.46000  ? 259 LEU D N   1 
ATOM   12659 C  CA  . LEU D  1 228 ? -7.22300  -6.13500  6.46700   1.000 53.75000  ? 259 LEU D CA  1 
ATOM   12660 C  C   . LEU D  1 228 ? -6.85800  -6.97500  5.24700   1.000 59.81000  ? 259 LEU D C   1 
ATOM   12661 O  O   . LEU D  1 228 ? -6.01700  -7.87300  5.32200   1.000 54.82000  ? 259 LEU D O   1 
ATOM   12662 C  CB  . LEU D  1 228 ? -5.99400  -5.79400  7.29800   1.000 53.84000  ? 259 LEU D CB  1 
ATOM   12663 C  CG  . LEU D  1 228 ? -6.30600  -4.92500  8.51700   1.000 57.85000  ? 259 LEU D CG  1 
ATOM   12664 C  CD1 . LEU D  1 228 ? -5.03900  -4.56700  9.27600   1.000 53.61000  ? 259 LEU D CD1 1 
ATOM   12665 C  CD2 . LEU D  1 228 ? -7.12100  -3.68000  8.15400   1.000 58.50000  ? 259 LEU D CD2 1 
ATOM   12666 N  N   . GLN D  1 229 ? -7.49700  -6.68500  4.11200   1.000 62.40000  ? 260 GLN D N   1 
ATOM   12667 C  CA  . GLN D  1 229 ? -7.25100  -7.37900  2.85000   1.000 60.42000  ? 260 GLN D CA  1 
ATOM   12668 C  C   . GLN D  1 229 ? -7.10400  -6.33900  1.75500   1.000 58.72000  ? 260 GLN D C   1 
ATOM   12669 O  O   . GLN D  1 229 ? -7.94800  -5.44400  1.63400   1.000 60.10000  ? 260 GLN D O   1 
ATOM   12670 C  CB  . GLN D  1 229 ? -8.39200  -8.34200  2.50600   1.000 59.42000  ? 260 GLN D CB  1 
ATOM   12671 C  CG  . GLN D  1 229 ? -8.61800  -9.42400  3.54500   1.000 66.05000  ? 260 GLN D CG  1 
ATOM   12672 C  CD  . GLN D  1 229 ? -9.85100  -10.25700 3.25600   1.000 62.95000  ? 260 GLN D CD  1 
ATOM   12673 O  OE1 . GLN D  1 229 ? -10.68000 -9.89900  2.41300   1.000 61.76000  ? 260 GLN D OE1 1 
ATOM   12674 N  NE2 . GLN D  1 229 ? -9.98200  -11.37500 3.95900   1.000 58.58000  ? 260 GLN D NE2 1 
ATOM   12675 N  N   . ALA D  1 230 ? -6.04100  -6.44500  0.96700   1.000 56.85000  ? 261 ALA D N   1 
ATOM   12676 C  CA  . ALA D  1 230 ? -5.75600  -5.42400  -0.03000  1.000 60.72000  ? 261 ALA D CA  1 
ATOM   12677 C  C   . ALA D  1 230 ? -5.20400  -6.05100  -1.30200  1.000 65.86000  ? 261 ALA D C   1 
ATOM   12678 O  O   . ALA D  1 230 ? -4.62700  -7.13900  -1.28900  1.000 65.56000  ? 261 ALA D O   1 
ATOM   12679 C  CB  . ALA D  1 230 ? -4.77200  -4.37400  0.50000   1.000 62.48000  ? 261 ALA D CB  1 
ATOM   12680 N  N   . LYS D  1 231 ? -5.34000  -5.30500  -2.39600  1.000 74.50000  ? 262 LYS D N   1 
ATOM   12681 C  CA  . LYS D  1 231 ? -4.83100  -5.73900  -3.68900  1.000 71.08000  ? 262 LYS D CA  1 
ATOM   12682 C  C   . LYS D  1 231 ? -3.31400  -5.65100  -3.71100  1.000 65.99000  ? 262 LYS D C   1 
ATOM   12683 O  O   . LYS D  1 231 ? -2.71900  -4.72600  -3.14900  1.000 68.26000  ? 262 LYS D O   1 
ATOM   12684 C  CB  . LYS D  1 231 ? -5.41200  -4.87100  -4.81300  1.000 68.35000  ? 262 LYS D CB  1 
ATOM   12685 C  CG  . LYS D  1 231 ? -6.84800  -5.17900  -5.20400  1.000 71.28000  ? 262 LYS D CG  1 
ATOM   12686 C  CD  . LYS D  1 231 ? -7.46900  -4.03200  -5.99100  1.000 72.60000  ? 262 LYS D CD  1 
ATOM   12687 C  CE  . LYS D  1 231 ? -6.66400  -3.66100  -7.23100  1.000 78.16000  ? 262 LYS D CE  1 
ATOM   12688 N  NZ  . LYS D  1 231 ? -6.87300  -4.62200  -8.34900  1.000 76.56000  ? 262 LYS D NZ  1 
ATOM   12689 N  N   . ALA D  1 232 ? -2.69100  -6.62200  -4.38000  1.000 66.37000  ? 263 ALA D N   1 
ATOM   12690 C  CA  . ALA D  1 232 ? -1.23300  -6.67300  -4.42500  1.000 71.31000  ? 263 ALA D CA  1 
ATOM   12691 C  C   . ALA D  1 232 ? -0.63700  -5.40500  -5.01900  1.000 72.56000  ? 263 ALA D C   1 
ATOM   12692 O  O   . ALA D  1 232 ? 0.37000   -4.89100  -4.51400  1.000 78.83000  ? 263 ALA D O   1 
ATOM   12693 C  CB  . ALA D  1 232 ? -0.77900  -7.89200  -5.22800  1.000 76.52000  ? 263 ALA D CB  1 
ATOM   12694 N  N   . GLU D  1 233 ? -1.24900  -4.87500  -6.08100  1.000 78.91000  ? 264 GLU D N   1 
ATOM   12695 C  CA  . GLU D  1 233 ? -0.70600  -3.67900  -6.71800  1.000 75.41000  ? 264 GLU D CA  1 
ATOM   12696 C  C   . GLU D  1 233 ? -0.75800  -2.48500  -5.77900  1.000 75.91000  ? 264 GLU D C   1 
ATOM   12697 O  O   . GLU D  1 233 ? 0.12600   -1.61900  -5.81600  1.000 78.86000  ? 264 GLU D O   1 
ATOM   12698 C  CB  . GLU D  1 233 ? -1.46100  -3.38100  -8.01600  1.000 76.95000  ? 264 GLU D CB  1 
ATOM   12699 N  N   . ASP D  1 234 ? -1.75800  -2.44200  -4.90100  1.000 71.80000  ? 265 ASP D N   1 
ATOM   12700 C  CA  . ASP D  1 234 ? -1.84700  -1.35000  -3.94300  1.000 70.34000  ? 265 ASP D CA  1 
ATOM   12701 C  C   . ASP D  1 234 ? -0.80900  -1.51400  -2.82900  1.000 76.86000  ? 265 ASP D C   1 
ATOM   12702 O  O   . ASP D  1 234 ? -0.19600  -0.52800  -2.39200  1.000 73.53000  ? 265 ASP D O   1 
ATOM   12703 C  CB  . ASP D  1 234 ? -3.27900  -1.26700  -3.41000  1.000 71.97000  ? 265 ASP D CB  1 
ATOM   12704 C  CG  . ASP D  1 234 ? -4.28500  -0.78500  -4.48200  1.000 70.80000  ? 265 ASP D CG  1 
ATOM   12705 O  OD1 . ASP D  1 234 ? -3.92800  0.08600   -5.30900  1.000 65.41000  ? 265 ASP D OD1 1 
ATOM   12706 O  OD2 . ASP D  1 234 ? -5.43000  -1.28700  -4.50700  1.000 69.84000  ? 265 ASP D OD2 1 
ATOM   12707 N  N   . VAL D  1 235 ? -0.58200  -2.74900  -2.37100  1.000 75.09000  ? 266 VAL D N   1 
ATOM   12708 C  CA  . VAL D  1 235 ? 0.45200   -2.99100  -1.36900  1.000 73.12000  ? 266 VAL D CA  1 
ATOM   12709 C  C   . VAL D  1 235 ? 1.80800   -2.51500  -1.87100  1.000 76.73000  ? 266 VAL D C   1 
ATOM   12710 O  O   . VAL D  1 235 ? 2.62800   -2.01000  -1.08900  1.000 72.29000  ? 266 VAL D O   1 
ATOM   12711 C  CB  . VAL D  1 235 ? 0.48000   -4.48700  -0.99500  1.000 74.87000  ? 266 VAL D CB  1 
ATOM   12712 C  CG1 . VAL D  1 235 ? 1.60600   -4.78300  -0.00600  1.000 63.67000  ? 266 VAL D CG1 1 
ATOM   12713 C  CG2 . VAL D  1 235 ? -0.86300  -4.90400  -0.42200  1.000 71.05000  ? 266 VAL D CG2 1 
ATOM   12714 N  N   . ALA D  1 236 ? 2.05200   -2.62200  -3.18200  1.000 78.77000  ? 267 ALA D N   1 
ATOM   12715 C  CA  . ALA D  1 236 ? 3.36100   -2.26000  -3.71800  1.000 77.45000  ? 267 ALA D CA  1 
ATOM   12716 C  C   . ALA D  1 236 ? 3.67400   -0.78200  -3.52000  1.000 77.06000  ? 267 ALA D C   1 
ATOM   12717 O  O   . ALA D  1 236 ? 4.84100   -0.41800  -3.35200  1.000 77.64000  ? 267 ALA D O   1 
ATOM   12718 C  CB  . ALA D  1 236 ? 3.44400   -2.62400  -5.19900  1.000 73.89000  ? 267 ALA D CB  1 
ATOM   12719 N  N   . LYS D  1 237 ? 2.65400   0.07800   -3.50000  1.000 78.81000  ? 268 LYS D N   1 
ATOM   12720 C  CA  . LYS D  1 237 ? 2.88800   1.50400   -3.30400  1.000 74.03000  ? 268 LYS D CA  1 
ATOM   12721 C  C   . LYS D  1 237 ? 3.28800   1.84800   -1.87600  1.000 77.44000  ? 268 LYS D C   1 
ATOM   12722 O  O   . LYS D  1 237 ? 3.68000   2.99500   -1.61700  1.000 76.16000  ? 268 LYS D O   1 
ATOM   12723 C  CB  . LYS D  1 237 ? 1.64300   2.30100   -3.69800  1.000 77.67000  ? 268 LYS D CB  1 
ATOM   12724 N  N   . PHE D  1 238 ? 3.22200   0.89000   -0.95400  1.000 75.30000  ? 269 PHE D N   1 
ATOM   12725 C  CA  . PHE D  1 238 ? 3.54200   1.15200   0.44400   1.000 81.26000  ? 269 PHE D CA  1 
ATOM   12726 C  C   . PHE D  1 238 ? 4.54300   0.13700   0.98800   1.000 79.55000  ? 269 PHE D C   1 
ATOM   12727 O  O   . PHE D  1 238 ? 4.51200   -0.21600  2.17500   1.000 76.23000  ? 269 PHE D O   1 
ATOM   12728 C  CB  . PHE D  1 238 ? 2.26300   1.20700   1.28000   1.000 75.15000  ? 269 PHE D CB  1 
ATOM   12729 C  CG  . PHE D  1 238 ? 1.33000   2.30300   0.85400   1.000 73.65000  ? 269 PHE D CG  1 
ATOM   12730 C  CD1 . PHE D  1 238 ? 1.57200   3.61500   1.24000   1.000 71.98000  ? 269 PHE D CD1 1 
ATOM   12731 C  CD2 . PHE D  1 238 ? 0.25300   2.04000   0.02400   1.000 75.80000  ? 269 PHE D CD2 1 
ATOM   12732 C  CE1 . PHE D  1 238 ? 0.73900   4.63800   0.84500   1.000 75.36000  ? 269 PHE D CE1 1 
ATOM   12733 C  CE2 . PHE D  1 238 ? -0.59500  3.06600   -0.38400  1.000 73.54000  ? 269 PHE D CE2 1 
ATOM   12734 C  CZ  . PHE D  1 238 ? -0.35000  4.36800   0.02800   1.000 71.62000  ? 269 PHE D CZ  1 
ATOM   12735 N  N   . ALA D  1 239 ? 5.46200   -0.30900  0.12400   1.000 74.63000  ? 270 ALA D N   1 
ATOM   12736 C  CA  . ALA D  1 239 ? 6.43300   -1.31900  0.52100   1.000 78.89000  ? 270 ALA D CA  1 
ATOM   12737 C  C   . ALA D  1 239 ? 7.40400   -0.80700  1.58400   1.000 74.41000  ? 270 ALA D C   1 
ATOM   12738 O  O   . ALA D  1 239 ? 7.90600   -1.60300  2.38000   1.000 78.17000  ? 270 ALA D O   1 
ATOM   12739 C  CB  . ALA D  1 239 ? 7.19200   -1.80700  -0.71000  1.000 80.18000  ? 270 ALA D CB  1 
ATOM   12740 N  N   . HIS D  1 240 ? 7.64200   0.50700   1.65400   1.000 70.32000  ? 271 HIS D N   1 
ATOM   12741 C  CA  . HIS D  1 240 ? 8.52900   1.05300   2.68100   1.000 73.11000  ? 271 HIS D CA  1 
ATOM   12742 C  C   . HIS D  1 240 ? 7.93100   1.02600   4.08800   1.000 75.88000  ? 271 HIS D C   1 
ATOM   12743 O  O   . HIS D  1 240 ? 8.60700   1.43700   5.03800   1.000 73.73000  ? 271 HIS D O   1 
ATOM   12744 C  CB  . HIS D  1 240 ? 8.92600   2.48900   2.32700   1.000 73.43000  ? 271 HIS D CB  1 
ATOM   12745 N  N   . ILE D  1 241 ? 6.68900   0.59100   4.25400   1.000 74.95000  ? 272 ILE D N   1 
ATOM   12746 C  CA  . ILE D  1 241 ? 6.07500   0.47500   5.57200   1.000 76.39000  ? 272 ILE D CA  1 
ATOM   12747 C  C   . ILE D  1 241 ? 6.40900   -0.90100  6.13900   1.000 77.57000  ? 272 ILE D C   1 
ATOM   12748 O  O   . ILE D  1 241 ? 6.09000   -1.92600  5.52000   1.000 75.61000  ? 272 ILE D O   1 
ATOM   12749 C  CB  . ILE D  1 241 ? 4.55500   0.68600   5.49600   1.000 76.42000  ? 272 ILE D CB  1 
ATOM   12750 C  CG1 . ILE D  1 241 ? 4.23700   2.09300   4.97500   1.000 73.94000  ? 272 ILE D CG1 1 
ATOM   12751 C  CG2 . ILE D  1 241 ? 3.91600   0.44500   6.86700   1.000 69.03000  ? 272 ILE D CG2 1 
ATOM   12752 C  CD1 . ILE D  1 241 ? 2.74100   2.41000   4.88000   1.000 72.25000  ? 272 ILE D CD1 1 
ATOM   12753 N  N   . LYS D  1 242 ? 7.05300   -0.92400  7.31400   1.000 70.50000  ? 273 LYS D N   1 
ATOM   12754 C  CA  . LYS D  1 242 ? 7.56600   -2.17900  7.85900   1.000 74.44000  ? 273 LYS D CA  1 
ATOM   12755 C  C   . LYS D  1 242 ? 6.46200   -3.05000  8.46200   1.000 71.95000  ? 273 LYS D C   1 
ATOM   12756 O  O   . LYS D  1 242 ? 6.46100   -4.27000  8.26600   1.000 71.61000  ? 273 LYS D O   1 
ATOM   12757 C  CB  . LYS D  1 242 ? 8.64700   -1.89300  8.90700   1.000 70.90000  ? 273 LYS D CB  1 
ATOM   12758 N  N   . ASP D  1 243 ? 5.51500   -2.46000  9.18900   1.000 72.00000  ? 274 ASP D N   1 
ATOM   12759 C  CA  . ASP D  1 243 ? 4.46600   -3.26100  9.81200   1.000 66.36000  ? 274 ASP D CA  1 
ATOM   12760 C  C   . ASP D  1 243 ? 3.52100   -3.80400  8.75300   1.000 70.14000  ? 274 ASP D C   1 
ATOM   12761 O  O   . ASP D  1 243 ? 3.02600   -3.06000  7.90200   1.000 71.80000  ? 274 ASP D O   1 
ATOM   12762 C  CB  . ASP D  1 243 ? 3.69300   -2.45000  10.85900  1.000 68.70000  ? 274 ASP D CB  1 
ATOM   12763 C  CG  . ASP D  1 243 ? 2.61500   -3.28600  11.58700  1.000 79.59000  ? 274 ASP D CG  1 
ATOM   12764 O  OD1 . ASP D  1 243 ? 2.55500   -4.52000  11.39800  1.000 81.89000  ? 274 ASP D OD1 1 
ATOM   12765 O  OD2 . ASP D  1 243 ? 1.81300   -2.70800  12.35500  1.000 78.16000  ? 274 ASP D OD2 1 
ATOM   12766 N  N   . LYS D  1 244 ? 3.31800   -5.11900  8.77800   1.000 70.79000  ? 275 LYS D N   1 
ATOM   12767 C  CA  . LYS D  1 244 ? 2.44800   -5.74800  7.79500   1.000 69.72000  ? 275 LYS D CA  1 
ATOM   12768 C  C   . LYS D  1 244 ? 1.02500   -5.20700  7.90200   1.000 70.37000  ? 275 LYS D C   1 
ATOM   12769 O  O   . LYS D  1 244 ? 0.34700   -5.01200  6.88600   1.000 71.64000  ? 275 LYS D O   1 
ATOM   12770 C  CB  . LYS D  1 244 ? 2.47700   -7.26700  7.96900   1.000 68.50000  ? 275 LYS D CB  1 
ATOM   12771 C  CG  . LYS D  1 244 ? 1.67400   -8.02700  6.93600   1.000 76.64000  ? 275 LYS D CG  1 
ATOM   12772 C  CD  . LYS D  1 244 ? 1.68200   -9.52600  7.20000   1.000 81.65000  ? 275 LYS D CD  1 
ATOM   12773 C  CE  . LYS D  1 244 ? 0.61800   -10.23100 6.33600   1.000 72.96000  ? 275 LYS D CE  1 
ATOM   12774 N  NZ  . LYS D  1 244 ? 0.51200   -11.71900 6.58800   1.000 84.87000  ? 275 LYS D NZ  1 
ATOM   12775 N  N   . ASP D  1 245 ? 0.54100   -4.99100  9.12700   1.000 70.57000  ? 276 ASP D N   1 
ATOM   12776 C  CA  . ASP D  1 245 ? -0.82200  -4.49700  9.30200   1.000 67.81000  ? 276 ASP D CA  1 
ATOM   12777 C  C   . ASP D  1 245 ? -0.96400  -3.05200  8.82300   1.000 65.90000  ? 276 ASP D C   1 
ATOM   12778 O  O   . ASP D  1 245 ? -1.90900  -2.72700  8.09300   1.000 64.85000  ? 276 ASP D O   1 
ATOM   12779 C  CB  . ASP D  1 245 ? -1.25400  -4.64000  10.76000  1.000 68.69000  ? 276 ASP D CB  1 
ATOM   12780 C  CG  . ASP D  1 245 ? -1.83500  -6.01800  11.06700  1.000 74.74000  ? 276 ASP D CG  1 
ATOM   12781 O  OD1 . ASP D  1 245 ? -1.66500  -6.94400  10.23800  1.000 76.21000  ? 276 ASP D OD1 1 
ATOM   12782 O  OD2 . ASP D  1 245 ? -2.46300  -6.17600  12.13700  1.000 76.36000  ? 276 ASP D OD2 1 
ATOM   12783 N  N   . ARG D  1 246 ? -0.02700  -2.17200  9.20300   1.000 63.86000  ? 277 ARG D N   1 
ATOM   12784 C  CA  . ARG D  1 246 ? -0.08600  -0.79400  8.71600   1.000 62.52000  ? 277 ARG D CA  1 
ATOM   12785 C  C   . ARG D  1 246 ? 0.00600   -0.76200  7.19800   1.000 66.09000  ? 277 ARG D C   1 
ATOM   12786 O  O   . ARG D  1 246 ? -0.69500  0.01800   6.54400   1.000 62.32000  ? 277 ARG D O   1 
ATOM   12787 C  CB  . ARG D  1 246 ? 1.03300   0.06300   9.31700   1.000 66.96000  ? 277 ARG D CB  1 
ATOM   12788 C  CG  . ARG D  1 246 ? 1.00200   1.57100   8.91500   1.000 60.07000  ? 277 ARG D CG  1 
ATOM   12789 C  CD  . ARG D  1 246 ? -0.17800  2.36300   9.51900   1.000 66.88000  ? 277 ARG D CD  1 
ATOM   12790 N  NE  . ARG D  1 246 ? -0.10100  3.80200   9.24600   1.000 70.16000  ? 277 ARG D NE  1 
ATOM   12791 C  CZ  . ARG D  1 246 ? -1.04600  4.69100   9.54800   1.000 64.04000  ? 277 ARG D CZ  1 
ATOM   12792 N  NH1 . ARG D  1 246 ? -2.15500  4.34400   10.17700  1.000 60.97000  ? 277 ARG D NH1 1 
ATOM   12793 N  NH2 . ARG D  1 246 ? -0.87900  5.96200   9.20100   1.000 66.53000  ? 277 ARG D NH2 1 
ATOM   12794 N  N   . ARG D  1 247 ? 0.83800   -1.63100  6.62100   1.000 65.44000  ? 278 ARG D N   1 
ATOM   12795 C  CA  . ARG D  1 247 ? 1.00300   -1.63900  5.17400   1.000 67.17000  ? 278 ARG D CA  1 
ATOM   12796 C  C   . ARG D  1 247 ? -0.30700  -1.98400  4.48800   1.000 65.45000  ? 278 ARG D C   1 
ATOM   12797 O  O   . ARG D  1 247 ? -0.72800  -1.30300  3.54800   1.000 68.02000  ? 278 ARG D O   1 
ATOM   12798 C  CB  . ARG D  1 247 ? 2.08500   -2.63600  4.77000   1.000 66.85000  ? 278 ARG D CB  1 
ATOM   12799 C  CG  . ARG D  1 247 ? 2.30800   -2.73900  3.27800   1.000 67.29000  ? 278 ARG D CG  1 
ATOM   12800 C  CD  . ARG D  1 247 ? 3.49800   -3.63300  2.93900   1.000 72.16000  ? 278 ARG D CD  1 
ATOM   12801 N  NE  . ARG D  1 247 ? 4.49200   -3.66700  4.00600   1.000 73.72000  ? 278 ARG D NE  1 
ATOM   12802 C  CZ  . ARG D  1 247 ? 4.76800   -4.73700  4.73900   1.000 68.49000  ? 278 ARG D CZ  1 
ATOM   12803 N  NH1 . ARG D  1 247 ? 4.14500   -5.88900  4.54700   1.000 59.67000  ? 278 ARG D NH1 1 
ATOM   12804 N  NH2 . ARG D  1 247 ? 5.68200   -4.64500  5.70200   1.000 77.88000  ? 278 ARG D NH2 1 
ATOM   12805 N  N   . THR D  1 248 ? -0.97800  -3.03200  4.95800   1.000 64.30000  ? 279 THR D N   1 
ATOM   12806 C  CA  . THR D  1 248 ? -2.22900  -3.43300  4.32800   1.000 64.85000  ? 279 THR D CA  1 
ATOM   12807 C  C   . THR D  1 248 ? -3.28000  -2.34400  4.46600   1.000 62.25000  ? 279 THR D C   1 
ATOM   12808 O  O   . THR D  1 248 ? -3.95600  -1.99200  3.49500   1.000 66.51000  ? 279 THR D O   1 
ATOM   12809 C  CB  . THR D  1 248 ? -2.71600  -4.73500  4.95100   1.000 63.74000  ? 279 THR D CB  1 
ATOM   12810 O  OG1 . THR D  1 248 ? -1.62400  -5.65600  4.99200   1.000 67.72000  ? 279 THR D OG1 1 
ATOM   12811 C  CG2 . THR D  1 248 ? -3.86000  -5.32600  4.13800   1.000 55.89000  ? 279 THR D CG2 1 
ATOM   12812 N  N   . TYR D  1 249 ? -3.40200  -1.78000  5.66900   1.000 59.18000  ? 280 TYR D N   1 
ATOM   12813 C  CA  . TYR D  1 249 ? -4.34300  -0.69900  5.92700   1.000 56.47000  ? 280 TYR D CA  1 
ATOM   12814 C  C   . TYR D  1 249 ? -4.08600  0.47000   4.99000   1.000 62.39000  ? 280 TYR D C   1 
ATOM   12815 O  O   . TYR D  1 249 ? -5.01800  1.02300   4.39600   1.000 62.21000  ? 280 TYR D O   1 
ATOM   12816 C  CB  . TYR D  1 249 ? -4.21100  -0.28000  7.39000   1.000 59.63000  ? 280 TYR D CB  1 
ATOM   12817 C  CG  . TYR D  1 249 ? -5.09500  0.83600   7.86800   1.000 54.92000  ? 280 TYR D CG  1 
ATOM   12818 C  CD1 . TYR D  1 249 ? -4.72700  2.16500   7.69900   1.000 53.16000  ? 280 TYR D CD1 1 
ATOM   12819 C  CD2 . TYR D  1 249 ? -6.28000  0.56100   8.53900   1.000 57.17000  ? 280 TYR D CD2 1 
ATOM   12820 C  CE1 . TYR D  1 249 ? -5.53000  3.19200   8.15100   1.000 55.34000  ? 280 TYR D CE1 1 
ATOM   12821 C  CE2 . TYR D  1 249 ? -7.09000  1.57900   9.00000   1.000 53.57000  ? 280 TYR D CE2 1 
ATOM   12822 C  CZ  . TYR D  1 249 ? -6.71000  2.89300   8.79800   1.000 57.28000  ? 280 TYR D CZ  1 
ATOM   12823 O  OH  . TYR D  1 249 ? -7.51100  3.91100   9.25500   1.000 57.36000  ? 280 TYR D OH  1 
ATOM   12824 N  N   . ALA D  1 250 ? -2.81500  0.84500   4.82800   1.000 65.22000  ? 281 ALA D N   1 
ATOM   12825 C  CA  . ALA D  1 250 ? -2.46900  1.91500   3.90000   1.000 66.85000  ? 281 ALA D CA  1 
ATOM   12826 C  C   . ALA D  1 250 ? -2.92400  1.58100   2.48400   1.000 63.18000  ? 281 ALA D C   1 
ATOM   12827 O  O   . ALA D  1 250 ? -3.49400  2.43300   1.79200   1.000 64.32000  ? 281 ALA D O   1 
ATOM   12828 C  CB  . ALA D  1 250 ? -0.96400  2.18000   3.93900   1.000 67.05000  ? 281 ALA D CB  1 
ATOM   12829 N  N   . ALA D  1 251 ? -2.71900  0.33700   2.04800   1.000 58.71000  ? 282 ALA D N   1 
ATOM   12830 C  CA  . ALA D  1 251 ? -3.18100  -0.05000  0.72200   1.000 60.35000  ? 282 ALA D CA  1 
ATOM   12831 C  C   . ALA D  1 251 ? -4.70200  0.02400   0.62900   1.000 60.28000  ? 282 ALA D C   1 
ATOM   12832 O  O   . ALA D  1 251 ? -5.25200  0.46000   -0.39000  1.000 62.01000  ? 282 ALA D O   1 
ATOM   12833 C  CB  . ALA D  1 251 ? -2.69200  -1.45600  0.38200   1.000 61.82000  ? 282 ALA D CB  1 
ATOM   12834 N  N   . MET D  1 252 ? -5.39900  -0.35100  1.70000   1.000 55.50000  ? 283 MET D N   1 
ATOM   12835 C  CA  . MET D  1 252 ? -6.85400  -0.29100  1.68000   1.000 56.44000  ? 283 MET D CA  1 
ATOM   12836 C  C   . MET D  1 252 ? -7.35600  1.14500   1.56300   1.000 58.07000  ? 283 MET D C   1 
ATOM   12837 O  O   . MET D  1 252 ? -8.27200  1.43200   0.78100   1.000 58.71000  ? 283 MET D O   1 
ATOM   12838 C  CB  . MET D  1 252 ? -7.41800  -0.94800  2.93700   1.000 58.66000  ? 283 MET D CB  1 
ATOM   12839 C  CG  . MET D  1 252 ? -7.00100  -2.37900  3.13000   1.000 58.42000  ? 283 MET D CG  1 
ATOM   12840 S  SD  . MET D  1 252 ? -7.58500  -3.02900  4.70900   1.000 58.78000  ? 283 MET D SD  1 
ATOM   12841 C  CE  . MET D  1 252 ? -9.34000  -3.22300  4.41100   1.000 51.52000  ? 283 MET D CE  1 
ATOM   12842 N  N   . VAL D  1 253 ? -6.77900  2.06400   2.33900   1.000 60.99000  ? 284 VAL D N   1 
ATOM   12843 C  CA  . VAL D  1 253 ? -7.19800  3.45700   2.23600   1.000 62.35000  ? 284 VAL D CA  1 
ATOM   12844 C  C   . VAL D  1 253 ? -6.86900  3.99200   0.85200   1.000 60.03000  ? 284 VAL D C   1 
ATOM   12845 O  O   . VAL D  1 253 ? -7.63100  4.77300   0.27500   1.000 63.70000  ? 284 VAL D O   1 
ATOM   12846 C  CB  . VAL D  1 253 ? -6.55900  4.30800   3.34900   1.000 61.82000  ? 284 VAL D CB  1 
ATOM   12847 C  CG1 . VAL D  1 253 ? -6.89200  5.78400   3.14700   1.000 56.94000  ? 284 VAL D CG1 1 
ATOM   12848 C  CG2 . VAL D  1 253 ? -7.01500  3.83400   4.70700   1.000 58.16000  ? 284 VAL D CG2 1 
ATOM   12849 N  N   . TYR D  1 254 ? -5.73600  3.56200   0.29200   1.000 63.90000  ? 285 TYR D N   1 
ATOM   12850 C  CA  . TYR D  1 254 ? -5.33100  4.02300   -1.03400  1.000 63.14000  ? 285 TYR D CA  1 
ATOM   12851 C  C   . TYR D  1 254 ? -6.32800  3.59900   -2.09800  1.000 66.35000  ? 285 TYR D C   1 
ATOM   12852 O  O   . TYR D  1 254 ? -6.61000  4.35700   -3.03200  1.000 67.71000  ? 285 TYR D O   1 
ATOM   12853 C  CB  . TYR D  1 254 ? -3.95400  3.47100   -1.39000  1.000 66.41000  ? 285 TYR D CB  1 
ATOM   12854 C  CG  . TYR D  1 254 ? -3.41100  3.95200   -2.71500  1.000 63.51000  ? 285 TYR D CG  1 
ATOM   12855 C  CD1 . TYR D  1 254 ? -2.93900  5.24800   -2.86000  1.000 59.54000  ? 285 TYR D CD1 1 
ATOM   12856 C  CD2 . TYR D  1 254 ? -3.39900  3.11500   -3.82800  1.000 66.87000  ? 285 TYR D CD2 1 
ATOM   12857 C  CE1 . TYR D  1 254 ? -2.44300  5.69400   -4.07300  1.000 66.09000  ? 285 TYR D CE1 1 
ATOM   12858 C  CE2 . TYR D  1 254 ? -2.90800  3.54500   -5.04100  1.000 62.91000  ? 285 TYR D CE2 1 
ATOM   12859 C  CZ  . TYR D  1 254 ? -2.43000  4.83900   -5.16200  1.000 69.73000  ? 285 TYR D CZ  1 
ATOM   12860 O  OH  . TYR D  1 254 ? -1.93300  5.28200   -6.37200  1.000 70.51000  ? 285 TYR D OH  1 
ATOM   12861 N  N   . ALA D  1 255 ? -6.85000  2.37700   -1.99000  1.000 65.54000  ? 286 ALA D N   1 
ATOM   12862 C  CA  . ALA D  1 255 ? -7.80500  1.90800   -2.98200  1.000 63.86000  ? 286 ALA D CA  1 
ATOM   12863 C  C   . ALA D  1 255 ? -9.05700  2.77900   -2.99800  1.000 64.31000  ? 286 ALA D C   1 
ATOM   12864 O  O   . ALA D  1 255 ? -9.64100  3.01400   -4.06000  1.000 60.56000  ? 286 ALA D O   1 
ATOM   12865 C  CB  . ALA D  1 255 ? -8.15300  0.44500   -2.71300  1.000 62.73000  ? 286 ALA D CB  1 
ATOM   12866 N  N   . VAL D  1 256 ? -9.47100  3.28000   -1.82700  1.000 65.44000  ? 287 VAL D N   1 
ATOM   12867 C  CA  . VAL D  1 256 ? -10.59500 4.21000   -1.75400  1.000 62.79000  ? 287 VAL D CA  1 
ATOM   12868 C  C   . VAL D  1 256 ? -10.22900 5.52500   -2.42700  1.000 63.66000  ? 287 VAL D C   1 
ATOM   12869 O  O   . VAL D  1 256 ? -11.08100 6.17900   -3.04000  1.000 63.96000  ? 287 VAL D O   1 
ATOM   12870 C  CB  . VAL D  1 256 ? -11.04200 4.40100   -0.29600  1.000 64.16000  ? 287 VAL D CB  1 
ATOM   12871 C  CG1 . VAL D  1 256 ? -12.00000 5.58700   -0.16300  1.000 65.22000  ? 287 VAL D CG1 1 
ATOM   12872 C  CG2 . VAL D  1 256 ? -11.70400 3.13100   0.20100   1.000 62.17000  ? 287 VAL D CG2 1 
ATOM   12873 N  N   . ASP D  1 257 ? -8.96700  5.94200   -2.31100  1.000 65.85000  ? 288 ASP D N   1 
ATOM   12874 C  CA  . ASP D  1 257 ? -8.51900  7.15300   -2.99000  1.000 65.38000  ? 288 ASP D CA  1 
ATOM   12875 C  C   . ASP D  1 257 ? -8.63900  7.03300   -4.50000  1.000 64.59000  ? 288 ASP D C   1 
ATOM   12876 O  O   . ASP D  1 257 ? -9.12900  7.95300   -5.16100  1.000 66.89000  ? 288 ASP D O   1 
ATOM   12877 C  CB  . ASP D  1 257 ? -7.07300  7.46600   -2.63300  1.000 63.84000  ? 288 ASP D CB  1 
ATOM   12878 C  CG  . ASP D  1 257 ? -6.62200  8.78200   -3.21000  1.000 67.09000  ? 288 ASP D CG  1 
ATOM   12879 O  OD1 . ASP D  1 257 ? -7.00700  9.82600   -2.64600  1.000 71.50000  ? 288 ASP D OD1 1 
ATOM   12880 O  OD2 . ASP D  1 257 ? -5.92300  8.76400   -4.25200  1.000 67.19000  ? 288 ASP D OD2 1 
ATOM   12881 N  N   . ARG D  1 258 ? -8.16300  5.92500   -5.07500  1.000 64.49000  ? 289 ARG D N   1 
ATOM   12882 C  CA  . ARG D  1 258 ? -8.31900  5.75800   -6.51500  1.000 63.27000  ? 289 ARG D CA  1 
ATOM   12883 C  C   . ARG D  1 258 ? -9.78700  5.80200   -6.90800  1.000 71.15000  ? 289 ARG D C   1 
ATOM   12884 O  O   . ARG D  1 258 ? -10.14800 6.40500   -7.92500  1.000 74.12000  ? 289 ARG D O   1 
ATOM   12885 C  CB  . ARG D  1 258 ? -7.66300  4.47000   -7.01700  1.000 67.61000  ? 289 ARG D CB  1 
ATOM   12886 C  CG  . ARG D  1 258 ? -6.95500  3.61600   -5.99600  1.000 72.18000  ? 289 ARG D CG  1 
ATOM   12887 C  CD  . ARG D  1 258 ? -6.08700  2.56300   -6.69700  1.000 69.75000  ? 289 ARG D CD  1 
ATOM   12888 N  NE  . ARG D  1 258 ? -6.87900  1.63100   -7.48900  1.000 77.73000  ? 289 ARG D NE  1 
ATOM   12889 C  CZ  . ARG D  1 258 ? -7.41200  0.50300   -7.03400  1.000 79.66000  ? 289 ARG D CZ  1 
ATOM   12890 N  NH1 . ARG D  1 258 ? -7.24000  0.11000   -5.78200  1.000 66.85000  ? 289 ARG D NH1 1 
ATOM   12891 N  NH2 . ARG D  1 258 ? -8.14300  -0.24700  -7.85800  1.000 82.17000  ? 289 ARG D NH2 1 
ATOM   12892 N  N   . GLY D  1 259 ? -10.64900 5.16400   -6.11600  1.000 70.64000  ? 290 GLY D N   1 
ATOM   12893 C  CA  . GLY D  1 259 ? -12.06100 5.15600   -6.44900  1.000 70.62000  ? 290 GLY D CA  1 
ATOM   12894 C  C   . GLY D  1 259 ? -12.68100 6.53400   -6.38000  1.000 66.77000  ? 290 GLY D C   1 
ATOM   12895 O  O   . GLY D  1 259 ? -13.56500 6.85900   -7.17400  1.000 71.76000  ? 290 GLY D O   1 
ATOM   12896 N  N   . VAL D  1 260 ? -12.22900 7.36500   -5.44100  1.000 66.02000  ? 291 VAL D N   1 
ATOM   12897 C  CA  . VAL D  1 260 ? -12.70500 8.74300   -5.40300  1.000 67.47000  ? 291 VAL D CA  1 
ATOM   12898 C  C   . VAL D  1 260 ? -12.26500 9.47600   -6.66200  1.000 71.82000  ? 291 VAL D C   1 
ATOM   12899 O  O   . VAL D  1 260 ? -13.01200 10.29200  -7.21600  1.000 70.85000  ? 291 VAL D O   1 
ATOM   12900 C  CB  . VAL D  1 260 ? -12.21900 9.44700   -4.12200  1.000 65.10000  ? 291 VAL D CB  1 
ATOM   12901 C  CG1 . VAL D  1 260 ? -12.52300 10.94400  -4.16500  1.000 63.16000  ? 291 VAL D CG1 1 
ATOM   12902 C  CG2 . VAL D  1 260 ? -12.86400 8.81100   -2.91500  1.000 62.87000  ? 291 VAL D CG2 1 
ATOM   12903 N  N   . GLY D  1 261 ? -11.05900 9.17400   -7.15300  1.000 68.59000  ? 292 GLY D N   1 
ATOM   12904 C  CA  . GLY D  1 261 ? -10.58900 9.80000   -8.37800  1.000 66.40000  ? 292 GLY D CA  1 
ATOM   12905 C  C   . GLY D  1 261 ? -11.38900 9.40200   -9.60500  1.000 71.81000  ? 292 GLY D C   1 
ATOM   12906 O  O   . GLY D  1 261 ? -11.76400 10.25700  -10.41400 1.000 68.28000  ? 292 GLY D O   1 
ATOM   12907 N  N   . LYS D  1 262 ? -11.70000 8.11000   -9.74100  1.000 67.69000  ? 293 LYS D N   1 
ATOM   12908 C  CA  . LYS D  1 262 ? -12.53200 7.67900   -10.85800 1.000 73.48000  ? 293 LYS D CA  1 
ATOM   12909 C  C   . LYS D  1 262 ? -13.93500 8.26900   -10.75300 1.000 71.01000  ? 293 LYS D C   1 
ATOM   12910 O  O   . LYS D  1 262 ? -14.55000 8.61400   -11.76700 1.000 74.75000  ? 293 LYS D O   1 
ATOM   12911 C  CB  . LYS D  1 262 ? -12.58100 6.15100   -10.92500 1.000 70.82000  ? 293 LYS D CB  1 
ATOM   12912 C  CG  . LYS D  1 262 ? -11.22900 5.50700   -11.13300 1.000 74.05000  ? 293 LYS D CG  1 
ATOM   12913 C  CD  . LYS D  1 262 ? -10.65700 5.91200   -12.48800 1.000 76.00000  ? 293 LYS D CD  1 
ATOM   12914 C  CE  . LYS D  1 262 ? -9.15500  5.66500   -12.58800 1.000 80.36000  ? 293 LYS D CE  1 
ATOM   12915 N  NZ  . LYS D  1 262 ? -8.82400  4.25700   -12.93900 1.000 88.54000  ? 293 LYS D NZ  1 
ATOM   12916 N  N   . ILE D  1 263 ? -14.46200 8.38800   -9.53700  1.000 70.91000  ? 294 ILE D N   1 
ATOM   12917 C  CA  . ILE D  1 263 ? -15.75500 9.03500   -9.35900  1.000 68.64000  ? 294 ILE D CA  1 
ATOM   12918 C  C   . ILE D  1 263 ? -15.69100 10.48500  -9.82600  1.000 69.87000  ? 294 ILE D C   1 
ATOM   12919 O  O   . ILE D  1 263 ? -16.63100 10.99800  -10.44000 1.000 67.79000  ? 294 ILE D O   1 
ATOM   12920 C  CB  . ILE D  1 263 ? -16.21100 8.91800   -7.89400  1.000 66.32000  ? 294 ILE D CB  1 
ATOM   12921 C  CG1 . ILE D  1 263 ? -16.71800 7.50100   -7.61500  1.000 66.29000  ? 294 ILE D CG1 1 
ATOM   12922 C  CG2 . ILE D  1 263 ? -17.29700 9.93400   -7.57600  1.000 72.75000  ? 294 ILE D CG2 1 
ATOM   12923 C  CD1 . ILE D  1 263 ? -16.66800 7.11300   -6.15800  1.000 60.04000  ? 294 ILE D CD1 1 
ATOM   12924 N  N   . VAL D  1 264 ? -14.58500 11.17100  -9.54000  1.000 73.59000  ? 295 VAL D N   1 
ATOM   12925 C  CA  . VAL D  1 264 ? -14.46000 12.57200  -9.93500  1.000 72.19000  ? 295 VAL D CA  1 
ATOM   12926 C  C   . VAL D  1 264 ? -14.46900 12.70800  -11.45200 1.000 76.91000  ? 295 VAL D C   1 
ATOM   12927 O  O   . VAL D  1 264 ? -15.18800 13.54700  -12.00900 1.000 76.93000  ? 295 VAL D O   1 
ATOM   12928 C  CB  . VAL D  1 264 ? -13.19500 13.19300  -9.32000  1.000 71.62000  ? 295 VAL D CB  1 
ATOM   12929 C  CG1 . VAL D  1 264 ? -12.86500 14.50000  -10.01900 1.000 75.26000  ? 295 VAL D CG1 1 
ATOM   12930 C  CG2 . VAL D  1 264 ? -13.42400 13.45900  -7.85100  1.000 72.44000  ? 295 VAL D CG2 1 
ATOM   12931 N  N   . GLN D  1 265 ? -13.70400 11.86400  -12.14800 1.000 74.92000  ? 296 GLN D N   1 
ATOM   12932 C  CA  . GLN D  1 265 ? -13.69100 11.94400  -13.60200 1.000 73.97000  ? 296 GLN D CA  1 
ATOM   12933 C  C   . GLN D  1 265 ? -15.10700 11.82900  -14.15400 1.000 79.48000  ? 296 GLN D C   1 
ATOM   12934 O  O   . GLN D  1 265 ? -15.49800 12.58600  -15.05100 1.000 84.63000  ? 296 GLN D O   1 
ATOM   12935 C  CB  . GLN D  1 265 ? -12.76900 10.86500  -14.18200 1.000 73.93000  ? 296 GLN D CB  1 
ATOM   12936 C  CG  . GLN D  1 265 ? -13.34200 10.09000  -15.38400 1.000 85.53000  ? 296 GLN D CG  1 
ATOM   12937 C  CD  . GLN D  1 265 ? -13.37300 10.89400  -16.69000 1.000 91.90000  ? 296 GLN D CD  1 
ATOM   12938 O  OE1 . GLN D  1 265 ? -14.44600 11.20100  -17.23000 1.000 88.49000  ? 296 GLN D OE1 1 
ATOM   12939 N  NE2 . GLN D  1 265 ? -12.19300 11.21400  -17.21300 1.000 93.02000  ? 296 GLN D NE2 1 
ATOM   12940 N  N   . THR D  1 266 ? -15.90800 10.92100  -13.59700 1.000 80.02000  ? 297 THR D N   1 
ATOM   12941 C  CA  . THR D  1 266 ? -17.28900 10.78600  -14.05000 1.000 77.29000  ? 297 THR D CA  1 
ATOM   12942 C  C   . THR D  1 266 ? -18.09600 12.05100  -13.76500 1.000 74.50000  ? 297 THR D C   1 
ATOM   12943 O  O   . THR D  1 266 ? -18.80200 12.56000  -14.64200 1.000 75.88000  ? 297 THR D O   1 
ATOM   12944 C  CB  . THR D  1 266 ? -17.92800 9.56300   -13.38600 1.000 75.66000  ? 297 THR D CB  1 
ATOM   12945 O  OG1 . THR D  1 266 ? -17.21700 8.38500   -13.78900 1.000 81.41000  ? 297 THR D OG1 1 
ATOM   12946 C  CG2 . THR D  1 266 ? -19.38400 9.41800   -13.80000 1.000 73.54000  ? 297 THR D CG2 1 
ATOM   12947 N  N   . LEU D  1 267 ? -17.97100 12.60000  -12.55500 1.000 76.24000  ? 298 LEU D N   1 
ATOM   12948 C  CA  . LEU D  1 267 ? -18.72100 13.80500  -12.21400 1.000 72.82000  ? 298 LEU D CA  1 
ATOM   12949 C  C   . LEU D  1 267 ? -18.34800 14.96300  -13.12700 1.000 76.41000  ? 298 LEU D C   1 
ATOM   12950 O  O   . LEU D  1 267 ? -19.20500 15.77500  -13.50000 1.000 73.31000  ? 298 LEU D O   1 
ATOM   12951 C  CB  . LEU D  1 267 ? -18.47200 14.17800  -10.75600 1.000 70.90000  ? 298 LEU D CB  1 
ATOM   12952 C  CG  . LEU D  1 267 ? -19.14600 13.30600  -9.70900  1.000 69.44000  ? 298 LEU D CG  1 
ATOM   12953 C  CD1 . LEU D  1 267 ? -18.61200 13.66700  -8.35100  1.000 58.99000  ? 298 LEU D CD1 1 
ATOM   12954 C  CD2 . LEU D  1 267 ? -20.63700 13.53300  -9.75300  1.000 70.70000  ? 298 LEU D CD2 1 
ATOM   12955 N  N   . LYS D  1 268 ? -17.07300 15.05600  -13.50300 1.000 78.07000  ? 299 LYS D N   1 
ATOM   12956 C  CA  . LYS D  1 268 ? -16.65900 16.12800  -14.39600 1.000 79.32000  ? 299 LYS D CA  1 
ATOM   12957 C  C   . LYS D  1 268 ? -17.10800 15.84500  -15.82600 1.000 78.03000  ? 299 LYS D C   1 
ATOM   12958 O  O   . LYS D  1 268 ? -17.55200 16.76100  -16.52800 1.000 78.61000  ? 299 LYS D O   1 
ATOM   12959 C  CB  . LYS D  1 268 ? -15.14100 16.32600  -14.32000 1.000 75.30000  ? 299 LYS D CB  1 
ATOM   12960 N  N   . GLU D  1 269 ? -17.03700 14.57900  -16.25700 1.000 76.75000  ? 300 GLU D N   1 
ATOM   12961 C  CA  . GLU D  1 269 ? -17.45900 14.23100  -17.61300 1.000 77.27000  ? 300 GLU D CA  1 
ATOM   12962 C  C   . GLU D  1 269 ? -18.94300 14.51200  -17.82500 1.000 72.72000  ? 300 GLU D C   1 
ATOM   12963 O  O   . GLU D  1 269 ? -19.33400 15.03500  -18.87300 1.000 77.22000  ? 300 GLU D O   1 
ATOM   12964 C  CB  . GLU D  1 269 ? -17.14400 12.76200  -17.90600 1.000 77.50000  ? 300 GLU D CB  1 
ATOM   12965 N  N   . THR D  1 270 ? -19.78600 14.17200  -16.84800 1.000 70.46000  ? 301 THR D N   1 
ATOM   12966 C  CA  . THR D  1 270 ? -21.21400 14.46700  -16.90300 1.000 69.80000  ? 301 THR D CA  1 
ATOM   12967 C  C   . THR D  1 270 ? -21.53600 15.91100  -16.53100 1.000 75.32000  ? 301 THR D C   1 
ATOM   12968 O  O   . THR D  1 270 ? -22.71000 16.21400  -16.28800 1.000 75.55000  ? 301 THR D O   1 
ATOM   12969 C  CB  . THR D  1 270 ? -22.00100 13.54800  -15.97100 1.000 70.89000  ? 301 THR D CB  1 
ATOM   12970 O  OG1 . THR D  1 270 ? -21.69900 13.87900  -14.61400 1.000 75.50000  ? 301 THR D OG1 1 
ATOM   12971 C  CG2 . THR D  1 270 ? -21.62400 12.09900  -16.21600 1.000 68.98000  ? 301 THR D CG2 1 
ATOM   12972 N  N   . LYS D  1 271 ? -20.52900 16.78200  -16.42100 1.000 75.37000  ? 302 LYS D N   1 
ATOM   12973 C  CA  . LYS D  1 271 ? -20.72400 18.18500  -16.04100 1.000 73.21000  ? 302 LYS D CA  1 
ATOM   12974 C  C   . LYS D  1 271 ? -21.52000 18.29900  -14.74500 1.000 77.19000  ? 302 LYS D C   1 
ATOM   12975 O  O   . LYS D  1 271 ? -22.27700 19.24900  -14.53700 1.000 76.20000  ? 302 LYS D O   1 
ATOM   12976 C  CB  . LYS D  1 271 ? -21.40100 18.97400  -17.16300 1.000 74.17000  ? 302 LYS D CB  1 
ATOM   12977 N  N   . GLN D  1 272 ? -21.34900 17.32500  -13.85500 1.000 78.79000  ? 303 GLN D N   1 
ATOM   12978 C  CA  . GLN D  1 272 ? -22.03100 17.32900  -12.57300 1.000 74.42000  ? 303 GLN D CA  1 
ATOM   12979 C  C   . GLN D  1 272 ? -21.14200 17.77100  -11.41900 1.000 71.42000  ? 303 GLN D C   1 
ATOM   12980 O  O   . GLN D  1 272 ? -21.63600 17.91800  -10.29400 1.000 69.98000  ? 303 GLN D O   1 
ATOM   12981 C  CB  . GLN D  1 272 ? -22.60600 15.93300  -12.30900 1.000 72.77000  ? 303 GLN D CB  1 
ATOM   12982 C  CG  . GLN D  1 272 ? -24.05400 15.93700  -11.83200 1.000 72.43000  ? 303 GLN D CG  1 
ATOM   12983 C  CD  . GLN D  1 272 ? -24.97100 16.76100  -12.72600 1.000 83.56000  ? 303 GLN D CD  1 
ATOM   12984 O  OE1 . GLN D  1 272 ? -24.78700 16.80900  -13.94800 1.000 84.64000  ? 303 GLN D OE1 1 
ATOM   12985 N  NE2 . GLN D  1 272 ? -25.96800 17.41700  -12.11900 1.000 74.93000  ? 303 GLN D NE2 1 
ATOM   12986 N  N   . PHE D  1 273 ? -19.85600 18.02300  -11.68400 1.000 75.67000  ? 304 PHE D N   1 
ATOM   12987 C  CA  . PHE D  1 273 ? -18.88400 18.26100  -10.61800 1.000 74.23000  ? 304 PHE D CA  1 
ATOM   12988 C  C   . PHE D  1 273 ? -19.20100 19.52400  -9.82600  1.000 75.66000  ? 304 PHE D C   1 
ATOM   12989 O  O   . PHE D  1 273 ? -19.29800 19.48700  -8.59100  1.000 77.99000  ? 304 PHE D O   1 
ATOM   12990 C  CB  . PHE D  1 273 ? -17.47800 18.35900  -11.21800 1.000 79.18000  ? 304 PHE D CB  1 
ATOM   12991 C  CG  . PHE D  1 273 ? -16.37700 18.43400  -10.19200 1.000 77.61000  ? 304 PHE D CG  1 
ATOM   12992 C  CD1 . PHE D  1 273 ? -16.08000 17.34900  -9.38800  1.000 80.60000  ? 304 PHE D CD1 1 
ATOM   12993 C  CD2 . PHE D  1 273 ? -15.64400 19.59800  -10.02700 1.000 83.74000  ? 304 PHE D CD2 1 
ATOM   12994 C  CE1 . PHE D  1 273 ? -15.05400 17.41600  -8.45100  1.000 81.88000  ? 304 PHE D CE1 1 
ATOM   12995 C  CE2 . PHE D  1 273 ? -14.61300 19.67400  -9.08300  1.000 81.87000  ? 304 PHE D CE2 1 
ATOM   12996 C  CZ  . PHE D  1 273 ? -14.32000 18.58100  -8.30300  1.000 78.96000  ? 304 PHE D CZ  1 
ATOM   12997 N  N   . ASP D  1 274 ? -19.37900 20.64800  -10.52000 1.000 78.71000  ? 305 ASP D N   1 
ATOM   12998 C  CA  . ASP D  1 274 ? -19.41200 21.93000  -9.83300  1.000 75.08000  ? 305 ASP D CA  1 
ATOM   12999 C  C   . ASP D  1 274 ? -20.61900 22.07300  -8.91900  1.000 76.99000  ? 305 ASP D C   1 
ATOM   13000 O  O   . ASP D  1 274 ? -20.50500 22.68700  -7.84600  1.000 73.86000  ? 305 ASP D O   1 
ATOM   13001 C  CB  . ASP D  1 274 ? -19.36000 23.06400  -10.85600 1.000 82.82000  ? 305 ASP D CB  1 
ATOM   13002 C  CG  . ASP D  1 274 ? -19.49300 24.42600  -10.21300 1.000 90.37000  ? 305 ASP D CG  1 
ATOM   13003 O  OD1 . ASP D  1 274 ? -20.64300 24.91100  -10.05600 1.000 85.17000  ? 305 ASP D OD1 1 
ATOM   13004 O  OD2 . ASP D  1 274 ? -18.43900 25.01400  -9.84700  1.000 90.10000  ? 305 ASP D OD2 1 
ATOM   13005 N  N   . ASN D  1 275 ? -21.75600 21.48800  -9.28700  1.000 75.03000  ? 306 ASN D N   1 
ATOM   13006 C  CA  . ASN D  1 275 ? -22.95700 21.56100  -8.46000  1.000 72.13000  ? 306 ASN D CA  1 
ATOM   13007 C  C   . ASN D  1 275 ? -23.24400 20.24600  -7.73100  1.000 72.86000  ? 306 ASN D C   1 
ATOM   13008 O  O   . ASN D  1 275 ? -24.39900 19.87100  -7.52600  1.000 74.38000  ? 306 ASN D O   1 
ATOM   13009 C  CB  . ASN D  1 275 ? -24.17500 22.00900  -9.27200  1.000 67.28000  ? 306 ASN D CB  1 
ATOM   13010 C  CG  . ASN D  1 275 ? -25.31000 22.49100  -8.38100  1.000 78.14000  ? 306 ASN D CG  1 
ATOM   13011 O  OD1 . ASN D  1 275 ? -25.06600 23.03700  -7.30500  1.000 74.87000  ? 306 ASN D OD1 1 
ATOM   13012 N  ND2 . ASN D  1 275 ? -26.56700 22.25800  -8.81100  1.000 73.80000  ? 306 ASN D ND2 1 
ATOM   13013 N  N   . THR D  1 276 ? -22.19200 19.53200  -7.33500  1.000 77.71000  ? 307 THR D N   1 
ATOM   13014 C  CA  . THR D  1 276 ? -22.30100 18.37900  -6.44800  1.000 71.40000  ? 307 THR D CA  1 
ATOM   13015 C  C   . THR D  1 276 ? -21.59200 18.70000  -5.13400  1.000 67.64000  ? 307 THR D C   1 
ATOM   13016 O  O   . THR D  1 276 ? -20.41900 19.08500  -5.13800  1.000 70.43000  ? 307 THR D O   1 
ATOM   13017 C  CB  . THR D  1 276 ? -21.70400 17.13600  -7.11000  1.000 69.69000  ? 307 THR D CB  1 
ATOM   13018 O  OG1 . THR D  1 276 ? -22.46600 16.81300  -8.28400  1.000 70.82000  ? 307 THR D OG1 1 
ATOM   13019 C  CG2 . THR D  1 276 ? -21.73500 15.95600  -6.14800  1.000 66.26000  ? 307 THR D CG2 1 
ATOM   13020 N  N   . LEU D  1 277 ? -22.30800 18.55800  -4.01400  1.000 63.19000  ? 308 LEU D N   1 
ATOM   13021 C  CA  . LEU D  1 277 ? -21.72500 18.66100  -2.67400  1.000 65.68000  ? 308 LEU D CA  1 
ATOM   13022 C  C   . LEU D  1 277 ? -21.23800 17.28500  -2.20500  1.000 67.03000  ? 308 LEU D C   1 
ATOM   13023 O  O   . LEU D  1 277 ? -22.04300 16.37900  -1.96200  1.000 65.08000  ? 308 LEU D O   1 
ATOM   13024 C  CB  . LEU D  1 277 ? -22.73900 19.23200  -1.68900  1.000 58.60000  ? 308 LEU D CB  1 
ATOM   13025 C  CG  . LEU D  1 277 ? -22.32700 19.07200  -0.22800  1.000 66.21000  ? 308 LEU D CG  1 
ATOM   13026 C  CD1 . LEU D  1 277 ? -21.08000 19.90500  0.05200   1.000 68.83000  ? 308 LEU D CD1 1 
ATOM   13027 C  CD2 . LEU D  1 277 ? -23.45100 19.42100  0.72800   1.000 57.16000  ? 308 LEU D CD2 1 
ATOM   13028 N  N   . ILE D  1 278 ? -19.92700 17.13000  -2.06300  1.000 67.43000  ? 309 ILE D N   1 
ATOM   13029 C  CA  . ILE D  1 278 ? -19.32600 15.89500  -1.56900  1.000 63.99000  ? 309 ILE D CA  1 
ATOM   13030 C  C   . ILE D  1 278 ? -18.98400 16.07700  -0.09900  1.000 59.24000  ? 309 ILE D C   1 
ATOM   13031 O  O   . ILE D  1 278 ? -18.23600 16.99000  0.25800   1.000 63.23000  ? 309 ILE D O   1 
ATOM   13032 C  CB  . ILE D  1 278 ? -18.07600 15.52300  -2.37900  1.000 62.87000  ? 309 ILE D CB  1 
ATOM   13033 C  CG1 . ILE D  1 278 ? -18.42100 15.41000  -3.86700  1.000 58.68000  ? 309 ILE D CG1 1 
ATOM   13034 C  CG2 . ILE D  1 278 ? -17.48300 14.22700  -1.86600  1.000 61.62000  ? 309 ILE D CG2 1 
ATOM   13035 C  CD1 . ILE D  1 278 ? -17.21800 15.12600  -4.74400  1.000 58.14000  ? 309 ILE D CD1 1 
ATOM   13036 N  N   . VAL D  1 279 ? -19.52600 15.22100  0.76100   1.000 59.93000  ? 310 VAL D N   1 
ATOM   13037 C  CA  . VAL D  1 279 ? -19.17900 15.19800  2.18300   1.000 60.66000  ? 310 VAL D CA  1 
ATOM   13038 C  C   . VAL D  1 279 ? -18.40300 13.91700  2.44500   1.000 60.23000  ? 310 VAL D C   1 
ATOM   13039 O  O   . VAL D  1 279 ? -18.89300 12.82100  2.14700   1.000 61.09000  ? 310 VAL D O   1 
ATOM   13040 C  CB  . VAL D  1 279 ? -20.41400 15.27200  3.09600   1.000 61.57000  ? 310 VAL D CB  1 
ATOM   13041 C  CG1 . VAL D  1 279 ? -19.98100 15.16500  4.56900   1.000 57.16000  ? 310 VAL D CG1 1 
ATOM   13042 C  CG2 . VAL D  1 279 ? -21.20500 16.54500  2.85600   1.000 52.41000  ? 310 VAL D CG2 1 
ATOM   13043 N  N   . PHE D  1 280 ? -17.19400 14.04500  2.99300   1.000 61.95000  ? 311 PHE D N   1 
ATOM   13044 C  CA  . PHE D  1 280 ? -16.35400 12.89300  3.29700   1.000 59.04000  ? 311 PHE D CA  1 
ATOM   13045 C  C   . PHE D  1 280 ? -16.13000 12.81800  4.80000   1.000 60.48000  ? 311 PHE D C   1 
ATOM   13046 O  O   . PHE D  1 280 ? -15.87700 13.83500  5.44700   1.000 65.84000  ? 311 PHE D O   1 
ATOM   13047 C  CB  . PHE D  1 280 ? -15.02900 12.97000  2.54400   1.000 56.58000  ? 311 PHE D CB  1 
ATOM   13048 C  CG  . PHE D  1 280 ? -14.01400 11.95000  2.97400   1.000 62.81000  ? 311 PHE D CG  1 
ATOM   13049 C  CD1 . PHE D  1 280 ? -13.99400 10.69200  2.39200   1.000 61.96000  ? 311 PHE D CD1 1 
ATOM   13050 C  CD2 . PHE D  1 280 ? -13.04800 12.26100  3.93400   1.000 64.90000  ? 311 PHE D CD2 1 
ATOM   13051 C  CE1 . PHE D  1 280 ? -13.03400 9.74800   2.77000   1.000 65.16000  ? 311 PHE D CE1 1 
ATOM   13052 C  CE2 . PHE D  1 280 ? -12.08800 11.32600  4.32300   1.000 62.14000  ? 311 PHE D CE2 1 
ATOM   13053 C  CZ  . PHE D  1 280 ? -12.08100 10.06500  3.73600   1.000 65.10000  ? 311 PHE D CZ  1 
ATOM   13054 N  N   . LEU D  1 281 ? -16.26400 11.62400  5.35700   1.000 55.87000  ? 312 LEU D N   1 
ATOM   13055 C  CA  . LEU D  1 281 ? -16.07100 11.43300  6.78400   1.000 59.43000  ? 312 LEU D CA  1 
ATOM   13056 C  C   . LEU D  1 281 ? -15.86400 9.95100   7.06100   1.000 60.73000  ? 312 LEU D C   1 
ATOM   13057 O  O   . LEU D  1 281 ? -16.02800 9.09700   6.18200   1.000 59.54000  ? 312 LEU D O   1 
ATOM   13058 C  CB  . LEU D  1 281 ? -17.25300 12.00200  7.58100   1.000 52.94000  ? 312 LEU D CB  1 
ATOM   13059 C  CG  . LEU D  1 281 ? -18.58800 11.25000  7.54000   1.000 55.46000  ? 312 LEU D CG  1 
ATOM   13060 C  CD1 . LEU D  1 281 ? -19.49300 11.61800  8.71000   1.000 60.25000  ? 312 LEU D CD1 1 
ATOM   13061 C  CD2 . LEU D  1 281 ? -19.32300 11.50200  6.23800   1.000 58.11000  ? 312 LEU D CD2 1 
ATOM   13062 N  N   . SER D  1 282 ? -15.46900 9.67200   8.29400   1.000 51.91000  ? 313 SER D N   1 
ATOM   13063 C  CA  . SER D  1 282 ? -15.42500 8.34100   8.87500   1.000 54.98000  ? 313 SER D CA  1 
ATOM   13064 C  C   . SER D  1 282 ? -16.62600 8.17700   9.79200   1.000 59.70000  ? 313 SER D C   1 
ATOM   13065 O  O   . SER D  1 282 ? -17.13400 9.15700   10.34600  1.000 60.74000  ? 313 SER D O   1 
ATOM   13066 C  CB  . SER D  1 282 ? -14.13100 8.14800   9.67900   1.000 61.26000  ? 313 SER D CB  1 
ATOM   13067 O  OG  . SER D  1 282 ? -14.06400 6.88800   10.33500  1.000 62.54000  ? 313 SER D OG  1 
ATOM   13068 N  N   . ASP D  1 283 ? -17.08200 6.93500   9.96400   1.000 55.38000  ? 314 ASP D N   1 
ATOM   13069 C  CA  . ASP D  1 283 ? -18.22800 6.74600   10.84300  1.000 55.04000  ? 314 ASP D CA  1 
ATOM   13070 C  C   . ASP D  1 283 ? -17.82000 6.75000   12.31300  1.000 57.59000  ? 314 ASP D C   1 
ATOM   13071 O  O   . ASP D  1 283 ? -18.68000 6.91600   13.18200  1.000 56.87000  ? 314 ASP D O   1 
ATOM   13072 C  CB  . ASP D  1 283 ? -18.98300 5.46100   10.47900  1.000 56.88000  ? 314 ASP D CB  1 
ATOM   13073 C  CG  . ASP D  1 283 ? -18.21800 4.18400   10.83000  1.000 60.70000  ? 314 ASP D CG  1 
ATOM   13074 O  OD1 . ASP D  1 283 ? -16.96200 4.19100   10.88000  1.000 59.29000  ? 314 ASP D OD1 1 
ATOM   13075 O  OD2 . ASP D  1 283 ? -18.89900 3.15000   11.03100  1.000 63.50000  ? 314 ASP D OD2 1 
ATOM   13076 N  N   . ASN D  1 284 ? -16.53100 6.60100   12.60600  1.000 61.32000  ? 315 ASN D N   1 
ATOM   13077 C  CA  . ASN D  1 284 ? -16.00000 6.70700   13.96100  1.000 52.84000  ? 315 ASN D CA  1 
ATOM   13078 C  C   . ASN D  1 284 ? -14.47800 6.73700   13.85200  1.000 59.57000  ? 315 ASN D C   1 
ATOM   13079 O  O   . ASN D  1 284 ? -13.90900 6.63700   12.75700  1.000 55.74000  ? 315 ASN D O   1 
ATOM   13080 C  CB  . ASN D  1 284 ? -16.51000 5.58000   14.87800  1.000 56.43000  ? 315 ASN D CB  1 
ATOM   13081 C  CG  . ASN D  1 284 ? -16.30600 4.17400   14.28800  1.000 61.18000  ? 315 ASN D CG  1 
ATOM   13082 O  OD1 . ASN D  1 284 ? -17.26800 3.52300   13.84000  1.000 55.96000  ? 315 ASN D OD1 1 
ATOM   13083 N  ND2 . ASN D  1 284 ? -15.06200 3.69000   14.31400  1.000 53.21000  ? 315 ASN D ND2 1 
ATOM   13084 N  N   . GLY D  1 285 ? -13.81800 6.90100   15.00200  1.000 52.15000  ? 316 GLY D N   1 
ATOM   13085 C  CA  . GLY D  1 285 ? -12.37800 6.95600   15.00900  1.000 58.18000  ? 316 GLY D CA  1 
ATOM   13086 C  C   . GLY D  1 285 ? -11.75700 5.63800   14.59300  1.000 64.02000  ? 316 GLY D C   1 
ATOM   13087 O  O   . GLY D  1 285 ? -12.40000 4.58700   14.57100  1.000 61.20000  ? 316 GLY D O   1 
ATOM   13088 N  N   . GLY D  1 286 ? -10.47800 5.69800   14.23700  1.000 61.23000  ? 317 GLY D N   1 
ATOM   13089 C  CA  . GLY D  1 286 ? -9.77000  4.48700   13.87500  1.000 62.10000  ? 317 GLY D CA  1 
ATOM   13090 C  C   . GLY D  1 286 ? -9.58700  3.55100   15.06000  1.000 60.81000  ? 317 GLY D C   1 
ATOM   13091 O  O   . GLY D  1 286 ? -9.57200  3.96200   16.22600  1.000 58.66000  ? 317 GLY D O   1 
ATOM   13092 N  N   . ASN D  1 287 ? -9.54000  2.25400   14.75500  1.000 57.64000  ? 318 ASN D N   1 
ATOM   13093 C  CA  . ASN D  1 287 ? -9.15300  1.22900   15.72400  1.000 52.54000  ? 318 ASN D CA  1 
ATOM   13094 C  C   . ASN D  1 287 ? -7.64400  1.08900   15.61300  1.000 52.33000  ? 318 ASN D C   1 
ATOM   13095 O  O   . ASN D  1 287 ? -7.14800  0.57700   14.60600  1.000 56.30000  ? 318 ASN D O   1 
ATOM   13096 C  CB  . ASN D  1 287 ? -9.86100  -0.09000  15.41800  1.000 55.55000  ? 318 ASN D CB  1 
ATOM   13097 C  CG  . ASN D  1 287 ? -9.62300  -1.15500  16.46700  1.000 56.08000  ? 318 ASN D CG  1 
ATOM   13098 O  OD1 . ASN D  1 287 ? -8.56500  -1.22500  17.08500  1.000 54.15000  ? 318 ASN D OD1 1 
ATOM   13099 N  ND2 . ASN D  1 287 ? -10.63700 -1.98500  16.69400  1.000 59.00000  ? 318 ASN D ND2 1 
ATOM   13100 N  N   . PHE D  1 288 ? -6.90300  1.56300   16.62200  1.000 53.51000  ? 319 PHE D N   1 
ATOM   13101 C  CA  . PHE D  1 288 ? -5.45300  1.52000   16.46400  1.000 57.84000  ? 319 PHE D CA  1 
ATOM   13102 C  C   . PHE D  1 288 ? -4.87000  0.13300   16.73500  1.000 55.54000  ? 319 PHE D C   1 
ATOM   13103 O  O   . PHE D  1 288 ? -3.65000  -0.04800  16.63700  1.000 49.96000  ? 319 PHE D O   1 
ATOM   13104 C  CB  . PHE D  1 288 ? -4.76300  2.61000   17.31000  1.000 53.87000  ? 319 PHE D CB  1 
ATOM   13105 C  CG  . PHE D  1 288 ? -5.02400  2.55500   18.79700  1.000 58.65000  ? 319 PHE D CG  1 
ATOM   13106 C  CD1 . PHE D  1 288 ? -5.49200  1.41000   19.43100  1.000 55.59000  ? 319 PHE D CD1 1 
ATOM   13107 C  CD2 . PHE D  1 288 ? -4.76200  3.67900   19.57200  1.000 54.46000  ? 319 PHE D CD2 1 
ATOM   13108 C  CE1 . PHE D  1 288 ? -5.69400  1.38700   20.80000  1.000 51.55000  ? 319 PHE D CE1 1 
ATOM   13109 C  CE2 . PHE D  1 288 ? -4.97300  3.66300   20.94300  1.000 57.91000  ? 319 PHE D CE2 1 
ATOM   13110 C  CZ  . PHE D  1 288 ? -5.43400  2.51800   21.55700  1.000 52.38000  ? 319 PHE D CZ  1 
ATOM   13111 N  N   . ASN D  1 289 ? -5.71900  -0.85200  17.01800  1.000 51.67000  ? 320 ASN D N   1 
ATOM   13112 C  CA  . ASN D  1 289 ? -5.28600  -2.23900  17.03200  1.000 57.43000  ? 320 ASN D CA  1 
ATOM   13113 C  C   . ASN D  1 289 ? -5.28600  -2.86800  15.64000  1.000 57.74000  ? 320 ASN D C   1 
ATOM   13114 O  O   . ASN D  1 289 ? -4.73300  -3.95800  15.47500  1.000 53.38000  ? 320 ASN D O   1 
ATOM   13115 C  CB  . ASN D  1 289 ? -6.17000  -3.06500  17.97200  1.000 55.94000  ? 320 ASN D CB  1 
ATOM   13116 C  CG  . ASN D  1 289 ? -6.07600  -2.61200  19.42300  1.000 59.69000  ? 320 ASN D CG  1 
ATOM   13117 O  OD1 . ASN D  1 289 ? -7.09000  -2.53200  20.12500  1.000 54.61000  ? 320 ASN D OD1 1 
ATOM   13118 N  ND2 . ASN D  1 289 ? -4.85400  -2.31300  19.88200  1.000 52.60000  ? 320 ASN D ND2 1 
ATOM   13119 N  N   . HIS D  1 290 ? -5.87500  -2.21500  14.63500  1.000 57.77000  ? 321 HIS D N   1 
ATOM   13120 C  CA  . HIS D  1 290 ? -6.00700  -2.80000  13.30300  1.000 52.48000  ? 321 HIS D CA  1 
ATOM   13121 C  C   . HIS D  1 290 ? -5.53400  -1.83400  12.22900  1.000 57.15000  ? 321 HIS D C   1 
ATOM   13122 O  O   . HIS D  1 290 ? -6.17000  -1.66500  11.18700  1.000 51.08000  ? 321 HIS D O   1 
ATOM   13123 C  CB  . HIS D  1 290 ? -7.44100  -3.22100  13.03200  1.000 56.81000  ? 321 HIS D CB  1 
ATOM   13124 C  CG  . HIS D  1 290 ? -7.92800  -4.31300  13.92800  1.000 57.99000  ? 321 HIS D CG  1 
ATOM   13125 N  ND1 . HIS D  1 290 ? -9.22200  -4.36800  14.40200  1.000 65.18000  ? 321 HIS D ND1 1 
ATOM   13126 C  CD2 . HIS D  1 290 ? -7.30200  -5.40900  14.41600  1.000 60.09000  ? 321 HIS D CD2 1 
ATOM   13127 C  CE1 . HIS D  1 290 ? -9.36600  -5.44100  15.15900  1.000 65.01000  ? 321 HIS D CE1 1 
ATOM   13128 N  NE2 . HIS D  1 290 ? -8.21400  -6.08800  15.18700  1.000 60.72000  ? 321 HIS D NE2 1 
ATOM   13129 N  N   . GLY D  1 291 ? -4.37100  -1.21700  12.44400  1.000 51.53000  ? 322 GLY D N   1 
ATOM   13130 C  CA  . GLY D  1 291 ? -3.71700  -0.44900  11.40500  1.000 49.65000  ? 322 GLY D CA  1 
ATOM   13131 C  C   . GLY D  1 291 ? -3.98700  1.04400   11.41700  1.000 54.20000  ? 322 GLY D C   1 
ATOM   13132 O  O   . GLY D  1 291 ? -3.33400  1.76800   10.66300  1.000 61.97000  ? 322 GLY D O   1 
ATOM   13133 N  N   . ALA D  1 292 ? -4.92600  1.52800   12.23000  1.000 53.75000  ? 323 ALA D N   1 
ATOM   13134 C  CA  . ALA D  1 292 ? -5.32600  2.93000   12.21500  1.000 56.40000  ? 323 ALA D CA  1 
ATOM   13135 C  C   . ALA D  1 292 ? -4.43400  3.78600   13.11700  1.000 60.96000  ? 323 ALA D C   1 
ATOM   13136 O  O   . ALA D  1 292 ? -3.85600  3.30500   14.09300  1.000 53.98000  ? 323 ALA D O   1 
ATOM   13137 C  CB  . ALA D  1 292 ? -6.78100  3.07000   12.66600  1.000 49.92000  ? 323 ALA D CB  1 
ATOM   13138 N  N   . ASN D  1 293 ? -4.39300  5.08700   12.81800  1.000 59.23000  ? 324 ASN D N   1 
ATOM   13139 C  CA  . ASN D  1 293 ? -3.62800  6.06300   13.59100  1.000 57.79000  ? 324 ASN D CA  1 
ATOM   13140 C  C   . ASN D  1 293 ? -4.50600  7.28500   13.84700  1.000 56.31000  ? 324 ASN D C   1 
ATOM   13141 O  O   . ASN D  1 293 ? -4.95900  7.93200   12.90100  1.000 60.75000  ? 324 ASN D O   1 
ATOM   13142 C  CB  . ASN D  1 293 ? -2.35200  6.45700   12.83900  1.000 59.37000  ? 324 ASN D CB  1 
ATOM   13143 C  CG  . ASN D  1 293 ? -1.40800  7.32100   13.67400  1.000 64.88000  ? 324 ASN D CG  1 
ATOM   13144 O  OD1 . ASN D  1 293 ? -1.79700  7.93600   14.66700  1.000 61.73000  ? 324 ASN D OD1 1 
ATOM   13145 N  ND2 . ASN D  1 293 ? -0.14400  7.34400   13.27400  1.000 69.64000  ? 324 ASN D ND2 1 
ATOM   13146 N  N   . ASN D  1 294 ? -4.73500  7.61400   15.11800  1.000 53.20000  ? 325 ASN D N   1 
ATOM   13147 C  CA  . ASN D  1 294 ? -5.62500  8.71400   15.47800  1.000 58.72000  ? 325 ASN D CA  1 
ATOM   13148 C  C   . ASN D  1 294 ? -4.88700  9.97900   15.90700  1.000 62.82000  ? 325 ASN D C   1 
ATOM   13149 O  O   . ASN D  1 294 ? -5.50600  10.87000  16.51200  1.000 57.30000  ? 325 ASN D O   1 
ATOM   13150 C  CB  . ASN D  1 294 ? -6.59400  8.28800   16.57900  1.000 51.71000  ? 325 ASN D CB  1 
ATOM   13151 C  CG  . ASN D  1 294 ? -7.59000  7.27400   16.09200  1.000 53.87000  ? 325 ASN D CG  1 
ATOM   13152 O  OD1 . ASN D  1 294 ? -7.96600  7.30000   14.92600  1.000 55.98000  ? 325 ASN D OD1 1 
ATOM   13153 N  ND2 . ASN D  1 294 ? -8.08400  6.42700   16.99300  1.000 58.90000  ? 325 ASN D ND2 1 
ATOM   13154 N  N   . TYR D  1 295 ? -3.59500  10.07600  15.59600  1.000 64.35000  ? 326 TYR D N   1 
ATOM   13155 C  CA  . TYR D  1 295 ? -2.79600  11.21200  16.02000  1.000 62.55000  ? 326 TYR D CA  1 
ATOM   13156 C  C   . TYR D  1 295 ? -3.45800  12.51600  15.57800  1.000 61.22000  ? 326 TYR D C   1 
ATOM   13157 O  O   . TYR D  1 295 ? -3.93700  12.61300  14.44300  1.000 63.23000  ? 326 TYR D O   1 
ATOM   13158 C  CB  . TYR D  1 295 ? -1.39200  11.12400  15.41700  1.000 63.89000  ? 326 TYR D CB  1 
ATOM   13159 C  CG  . TYR D  1 295 ? -0.48300  12.22300  15.90600  1.000 63.37000  ? 326 TYR D CG  1 
ATOM   13160 C  CD1 . TYR D  1 295 ? 0.21600   12.07600  17.09800  1.000 59.40000  ? 326 TYR D CD1 1 
ATOM   13161 C  CD2 . TYR D  1 295 ? -0.34700  13.41500  15.20100  1.000 66.58000  ? 326 TYR D CD2 1 
ATOM   13162 C  CE1 . TYR D  1 295 ? 1.05000   13.08200  17.57000  1.000 70.44000  ? 326 TYR D CE1 1 
ATOM   13163 C  CE2 . TYR D  1 295 ? 0.48300   14.42800  15.65900  1.000 68.59000  ? 326 TYR D CE2 1 
ATOM   13164 C  CZ  . TYR D  1 295 ? 1.18000   14.25400  16.84300  1.000 71.13000  ? 326 TYR D CZ  1 
ATOM   13165 O  OH  . TYR D  1 295 ? 2.00400   15.24800  17.30700  1.000 70.91000  ? 326 TYR D OH  1 
ATOM   13166 N  N   . PRO D  1 296 ? -3.48600  13.53700  16.42800  1.000 60.51000  ? 327 PRO D N   1 
ATOM   13167 C  CA  . PRO D  1 296 ? -2.93800  13.58100  17.78000  1.000 54.99000  ? 327 PRO D CA  1 
ATOM   13168 C  C   . PRO D  1 296 ? -3.99300  13.23200  18.81900  1.000 59.61000  ? 327 PRO D C   1 
ATOM   13169 O  O   . PRO D  1 296 ? -3.84400  13.58500  19.98200  1.000 58.06000  ? 327 PRO D O   1 
ATOM   13170 C  CB  . PRO D  1 296 ? -2.48500  15.03700  17.90500  1.000 57.71000  ? 327 PRO D CB  1 
ATOM   13171 C  CG  . PRO D  1 296 ? -3.54700  15.80200  17.11600  1.000 61.34000  ? 327 PRO D CG  1 
ATOM   13172 C  CD  . PRO D  1 296 ? -4.03700  14.84700  16.02900  1.000 61.32000  ? 327 PRO D CD  1 
ATOM   13173 N  N   . LEU D  1 297 ? -5.10200  12.59500  18.46400  1.000 57.65000  ? 328 LEU D N   1 
ATOM   13174 C  CA  . LEU D  1 297 ? -6.10100  12.41300  19.50000  1.000 58.80000  ? 328 LEU D CA  1 
ATOM   13175 C  C   . LEU D  1 297 ? -5.72300  11.24900  20.41500  1.000 57.61000  ? 328 LEU D C   1 
ATOM   13176 O  O   . LEU D  1 297 ? -4.94900  10.36000  20.05600  1.000 55.83000  ? 328 LEU D O   1 
ATOM   13177 C  CB  . LEU D  1 297 ? -7.48700  12.20700  18.88700  1.000 55.14000  ? 328 LEU D CB  1 
ATOM   13178 C  CG  . LEU D  1 297 ? -7.91700  13.17200  17.76900  1.000 59.54000  ? 328 LEU D CG  1 
ATOM   13179 C  CD1 . LEU D  1 297 ? -9.34400  12.86100  17.29400  1.000 60.89000  ? 328 LEU D CD1 1 
ATOM   13180 C  CD2 . LEU D  1 297 ? -7.81400  14.63600  18.18900  1.000 56.91000  ? 328 LEU D CD2 1 
ATOM   13181 N  N   . LYS D  1 298 ? -6.27600  11.27900  21.62100  1.000 59.17000  ? 329 LYS D N   1 
ATOM   13182 C  CA  . LYS D  1 298 ? -6.10800  10.19700  22.57600  1.000 57.56000  ? 329 LYS D CA  1 
ATOM   13183 C  C   . LYS D  1 298 ? -7.20500  9.16800   22.33800  1.000 61.59000  ? 329 LYS D C   1 
ATOM   13184 O  O   . LYS D  1 298 ? -8.35300  9.52500   22.05000  1.000 57.36000  ? 329 LYS D O   1 
ATOM   13185 C  CB  . LYS D  1 298 ? -6.18600  10.72100  24.01100  1.000 51.81000  ? 329 LYS D CB  1 
ATOM   13186 C  CG  . LYS D  1 298 ? -6.20400  9.63400   25.06200  1.000 59.30000  ? 329 LYS D CG  1 
ATOM   13187 C  CD  . LYS D  1 298 ? -6.40200  10.17600  26.47600  1.000 65.44000  ? 329 LYS D CD  1 
ATOM   13188 C  CE  . LYS D  1 298 ? -5.08900  10.57700  27.13600  1.000 58.70000  ? 329 LYS D CE  1 
ATOM   13189 N  NZ  . LYS D  1 298 ? -5.31400  10.92400  28.56400  1.000 60.00000  ? 329 LYS D NZ  1 
ATOM   13190 N  N   . GLY D  1 299 ? -6.84400  7.89600   22.46700  1.000 55.47000  ? 330 GLY D N   1 
ATOM   13191 C  CA  . GLY D  1 299 ? -7.80400  6.81300   22.41300  1.000 57.50000  ? 330 GLY D CA  1 
ATOM   13192 C  C   . GLY D  1 299 ? -8.03000  6.26500   21.01900  1.000 57.11000  ? 330 GLY D C   1 
ATOM   13193 O  O   . GLY D  1 299 ? -7.29800  6.52800   20.05700  1.000 56.21000  ? 330 GLY D O   1 
ATOM   13194 N  N   . THR D  1 300 ? -9.07400  5.45000   20.92900  1.000 53.84000  ? 331 THR D N   1 
ATOM   13195 C  CA  . THR D  1 300 ? -9.28600  4.58600   19.77600  1.000 59.55000  ? 331 THR D CA  1 
ATOM   13196 C  C   . THR D  1 300 ? -10.79100 4.40000   19.59100  1.000 55.07000  ? 331 THR D C   1 
ATOM   13197 O  O   . THR D  1 300 ? -11.58800 4.83000   20.42700  1.000 57.15000  ? 331 THR D O   1 
ATOM   13198 C  CB  . THR D  1 300 ? -8.52400  3.25900   19.96100  1.000 55.00000  ? 331 THR D CB  1 
ATOM   13199 O  OG1 . THR D  1 300 ? -8.61300  2.45300   18.77300  1.000 54.45000  ? 331 THR D OG1 1 
ATOM   13200 C  CG2 . THR D  1 300 ? -9.04200  2.49300   21.18900  1.000 50.87000  ? 331 THR D CG2 1 
ATOM   13201 N  N   . LYS D  1 301 ? -11.17300 3.77600   18.47200  1.000 55.47000  ? 332 LYS D N   1 
ATOM   13202 C  CA  . LYS D  1 301 ? -12.57800 3.48600   18.17200  1.000 55.22000  ? 332 LYS D CA  1 
ATOM   13203 C  C   . LYS D  1 301 ? -13.32200 2.98000   19.39600  1.000 52.85000  ? 332 LYS D C   1 
ATOM   13204 O  O   . LYS D  1 301 ? -12.86200 2.06600   20.08500  1.000 51.20000  ? 332 LYS D O   1 
ATOM   13205 C  CB  . LYS D  1 301 ? -12.66200 2.44300   17.06000  1.000 53.19000  ? 332 LYS D CB  1 
ATOM   13206 C  CG  . LYS D  1 301 ? -14.01500 1.79900   16.90300  1.000 57.62000  ? 332 LYS D CG  1 
ATOM   13207 C  CD  . LYS D  1 301 ? -13.97900 0.80000   15.75300  1.000 62.26000  ? 332 LYS D CD  1 
ATOM   13208 C  CE  . LYS D  1 301 ? -15.29400 0.06600   15.60300  1.000 52.74000  ? 332 LYS D CE  1 
ATOM   13209 N  NZ  . LYS D  1 301 ? -15.27800 -0.83000  14.40400  1.000 62.24000  ? 332 LYS D NZ  1 
ATOM   13210 N  N   . GLY D  1 302 ? -14.47000 3.58600   19.67500  1.000 49.82000  ? 333 GLY D N   1 
ATOM   13211 C  CA  . GLY D  1 302 ? -15.25400 3.18800   20.82100  1.000 49.58000  ? 333 GLY D CA  1 
ATOM   13212 C  C   . GLY D  1 302 ? -15.09700 4.06500   22.05000  1.000 59.69000  ? 333 GLY D C   1 
ATOM   13213 O  O   . GLY D  1 302 ? -15.89400 3.91800   22.99200  1.000 58.03000  ? 333 GLY D O   1 
ATOM   13214 N  N   . ASP D  1 303 ? -14.09400 4.95000   22.08500  1.000 50.74000  ? 334 ASP D N   1 
ATOM   13215 C  CA  . ASP D  1 303 ? -13.83100 5.77100   23.26600  1.000 60.18000  ? 334 ASP D CA  1 
ATOM   13216 C  C   . ASP D  1 303 ? -14.61500 7.08500   23.26400  1.000 56.85000  ? 334 ASP D C   1 
ATOM   13217 O  O   . ASP D  1 303 ? -14.94100 7.63700   22.20800  1.000 53.12000  ? 334 ASP D O   1 
ATOM   13218 C  CB  . ASP D  1 303 ? -12.34100 6.09400   23.37100  1.000 58.44000  ? 334 ASP D CB  1 
ATOM   13219 C  CG  . ASP D  1 303 ? -11.51300 4.88400   23.66800  1.000 58.95000  ? 334 ASP D CG  1 
ATOM   13220 O  OD1 . ASP D  1 303 ? -12.08900 3.90700   24.20100  1.000 58.51000  ? 334 ASP D OD1 1 
ATOM   13221 O  OD2 . ASP D  1 303 ? -10.30100 4.90900   23.34600  1.000 55.80000  ? 334 ASP D OD2 1 
ATOM   13222 N  N   . THR D  1 304 ? -14.83900 7.62700   24.46900  1.000 55.02000  ? 335 THR D N   1 
ATOM   13223 C  CA  . THR D  1 304 ? -15.29200 9.00800   24.58700  1.000 59.01000  ? 335 THR D CA  1 
ATOM   13224 C  C   . THR D  1 304 ? -14.12900 9.98500   24.70900  1.000 62.47000  ? 335 THR D C   1 
ATOM   13225 O  O   . THR D  1 304 ? -14.36800 11.18400  24.87000  1.000 64.25000  ? 335 THR D O   1 
ATOM   13226 C  CB  . THR D  1 304 ? -16.28800 9.19900   25.76100  1.000 60.22000  ? 335 THR D CB  1 
ATOM   13227 O  OG1 . THR D  1 304 ? -15.82100 8.57400   26.96500  1.000 61.36000  ? 335 THR D OG1 1 
ATOM   13228 C  CG2 . THR D  1 304 ? -17.69700 8.70500   25.42000  1.000 59.90000  ? 335 THR D CG2 1 
ATOM   13229 N  N   . TRP D  1 305 ? -12.88100 9.51200   24.62400  1.000 60.89000  ? 336 TRP D N   1 
ATOM   13230 C  CA  . TRP D  1 305 ? -11.79700 10.39500  24.21200  1.000 57.86000  ? 336 TRP D CA  1 
ATOM   13231 C  C   . TRP D  1 305 ? -12.07700 10.87900  22.78700  1.000 60.61000  ? 336 TRP D C   1 
ATOM   13232 O  O   . TRP D  1 305 ? -12.88200 10.29900  22.06000  1.000 61.96000  ? 336 TRP D O   1 
ATOM   13233 C  CB  . TRP D  1 305 ? -10.43100 9.69300   24.27400  1.000 55.15000  ? 336 TRP D CB  1 
ATOM   13234 C  CG  . TRP D  1 305 ? -10.00900 9.04900   25.59400  1.000 57.91000  ? 336 TRP D CG  1 
ATOM   13235 C  CD1 . TRP D  1 305 ? -9.78000  7.72100   25.80900  1.000 63.45000  ? 336 TRP D CD1 1 
ATOM   13236 C  CD2 . TRP D  1 305 ? -9.72700  9.70300   26.84400  1.000 61.70000  ? 336 TRP D CD2 1 
ATOM   13237 N  NE1 . TRP D  1 305 ? -9.39700  7.50000   27.11200  1.000 60.29000  ? 336 TRP D NE1 1 
ATOM   13238 C  CE2 . TRP D  1 305 ? -9.35600  8.70000   27.76700  1.000 66.02000  ? 336 TRP D CE2 1 
ATOM   13239 C  CE3 . TRP D  1 305 ? -9.76200  11.03300  27.27300  1.000 63.56000  ? 336 TRP D CE3 1 
ATOM   13240 C  CZ2 . TRP D  1 305 ? -9.02400  8.98600   29.08900  1.000 65.12000  ? 336 TRP D CZ2 1 
ATOM   13241 C  CZ3 . TRP D  1 305 ? -9.43400  11.31500  28.58100  1.000 60.25000  ? 336 TRP D CZ3 1 
ATOM   13242 C  CH2 . TRP D  1 305 ? -9.07100  10.29500  29.47700  1.000 67.13000  ? 336 TRP D CH2 1 
ATOM   13243 N  N   . GLU D  1 306 ? -11.39900 11.95600  22.38400  1.000 56.98000  ? 337 GLU D N   1 
ATOM   13244 C  CA  . GLU D  1 306 ? -11.56700 12.47100  21.02700  1.000 58.92000  ? 337 GLU D CA  1 
ATOM   13245 C  C   . GLU D  1 306 ? -11.37400 11.38600  19.97000  1.000 58.54000  ? 337 GLU D C   1 
ATOM   13246 O  O   . GLU D  1 306 ? -12.04400 11.39300  18.93500  1.000 52.97000  ? 337 GLU D O   1 
ATOM   13247 C  CB  . GLU D  1 306 ? -10.59000 13.62100  20.77300  1.000 58.95000  ? 337 GLU D CB  1 
ATOM   13248 C  CG  . GLU D  1 306 ? -10.79900 14.84300  21.66000  1.000 63.57000  ? 337 GLU D CG  1 
ATOM   13249 C  CD  . GLU D  1 306 ? -12.11600 15.54000  21.36300  1.000 64.19000  ? 337 GLU D CD  1 
ATOM   13250 O  OE1 . GLU D  1 306 ? -12.13800 16.38100  20.42800  1.000 55.28000  ? 337 GLU D OE1 1 
ATOM   13251 O  OE2 . GLU D  1 306 ? -13.12100 15.23400  22.06700  1.000 59.56000  ? 337 GLU D OE2 1 
ATOM   13252 N  N   . GLY D  1 307 ? -10.44700 10.45900  20.20400  1.000 59.24000  ? 338 GLY D N   1 
ATOM   13253 C  CA  . GLY D  1 307 ? -10.14600 9.44300   19.21400  1.000 53.24000  ? 338 GLY D CA  1 
ATOM   13254 C  C   . GLY D  1 307 ? -11.32100 8.54800   18.87200  1.000 61.25000  ? 338 GLY D C   1 
ATOM   13255 O  O   . GLY D  1 307 ? -11.35700 7.98600   17.77300  1.000 59.50000  ? 338 GLY D O   1 
ATOM   13256 N  N   . GLY D  1 308 ? -12.30700 8.43700   19.76800  1.000 60.42000  ? 339 GLY D N   1 
ATOM   13257 C  CA  . GLY D  1 308 ? -13.43500 7.56800   19.49000  1.000 58.01000  ? 339 GLY D CA  1 
ATOM   13258 C  C   . GLY D  1 308 ? -14.40900 8.13400   18.47400  1.000 63.35000  ? 339 GLY D C   1 
ATOM   13259 O  O   . GLY D  1 308 ? -14.88300 7.41200   17.58900  1.000 61.23000  ? 339 GLY D O   1 
ATOM   13260 N  N   . TYR D  1 309 ? -14.70000 9.43700   18.55500  1.000 61.92000  ? 340 TYR D N   1 
ATOM   13261 C  CA  . TYR D  1 309 ? -15.78700 9.97100   17.74200  1.000 58.72000  ? 340 TYR D CA  1 
ATOM   13262 C  C   . TYR D  1 309 ? -15.46300 11.29900  17.07100  1.000 58.82000  ? 340 TYR D C   1 
ATOM   13263 O  O   . TYR D  1 309 ? -16.35400 11.90500  16.47800  1.000 56.38000  ? 340 TYR D O   1 
ATOM   13264 C  CB  . TYR D  1 309 ? -17.07400 10.10400  18.57200  1.000 57.31000  ? 340 TYR D CB  1 
ATOM   13265 C  CG  . TYR D  1 309 ? -17.00500 11.04800  19.76000  1.000 65.68000  ? 340 TYR D CG  1 
ATOM   13266 C  CD1 . TYR D  1 309 ? -16.31000 10.69600  20.91500  1.000 62.31000  ? 340 TYR D CD1 1 
ATOM   13267 C  CD2 . TYR D  1 309 ? -17.66800 12.27700  19.73800  1.000 66.62000  ? 340 TYR D CD2 1 
ATOM   13268 C  CE1 . TYR D  1 309 ? -16.25700 11.55100  22.01200  1.000 70.58000  ? 340 TYR D CE1 1 
ATOM   13269 C  CE2 . TYR D  1 309 ? -17.62600 13.13400  20.82500  1.000 65.61000  ? 340 TYR D CE2 1 
ATOM   13270 C  CZ  . TYR D  1 309 ? -16.91500 12.76900  21.95800  1.000 71.02000  ? 340 TYR D CZ  1 
ATOM   13271 O  OH  . TYR D  1 309 ? -16.86400 13.61800  23.04000  1.000 65.83000  ? 340 TYR D OH  1 
ATOM   13272 N  N   . ARG D  1 310 ? -14.23200 11.77400  17.14600  1.000 61.25000  ? 341 ARG D N   1 
ATOM   13273 C  CA  . ARG D  1 310 ? -13.78500 12.90400  16.35000  1.000 59.21000  ? 341 ARG D CA  1 
ATOM   13274 C  C   . ARG D  1 310 ? -13.10600 12.36800  15.10000  1.000 54.64000  ? 341 ARG D C   1 
ATOM   13275 O  O   . ARG D  1 310 ? -12.17100 11.57000  15.20100  1.000 57.08000  ? 341 ARG D O   1 
ATOM   13276 C  CB  . ARG D  1 310 ? -12.82300 13.77500  17.15000  1.000 56.16000  ? 341 ARG D CB  1 
ATOM   13277 C  CG  . ARG D  1 310 ? -12.46700 15.06500  16.49900  1.000 52.76000  ? 341 ARG D CG  1 
ATOM   13278 C  CD  . ARG D  1 310 ? -11.61800 15.84500  17.43300  1.000 56.47000  ? 341 ARG D CD  1 
ATOM   13279 N  NE  . ARG D  1 310 ? -11.01400 17.00800  16.80600  1.000 57.85000  ? 341 ARG D NE  1 
ATOM   13280 C  CZ  . ARG D  1 310 ? -10.55900 18.03100  17.50600  1.000 56.15000  ? 341 ARG D CZ  1 
ATOM   13281 N  NH1 . ARG D  1 310 ? -10.65300 18.04800  18.82400  1.000 52.19000  ? 341 ARG D NH1 1 
ATOM   13282 N  NH2 . ARG D  1 310 ? -10.00700 19.06100  16.86800  1.000 50.43000  ? 341 ARG D NH2 1 
ATOM   13283 N  N   . VAL D  1 311 ? -13.57300 12.80300  13.93500  1.000 56.90000  ? 342 VAL D N   1 
ATOM   13284 C  CA  . VAL D  1 311 ? -13.24100 12.16000  12.66100  1.000 49.78000  ? 342 VAL D CA  1 
ATOM   13285 C  C   . VAL D  1 311 ? -12.79100 13.21900  11.66700  1.000 51.03000  ? 342 VAL D C   1 
ATOM   13286 O  O   . VAL D  1 311 ? -13.06400 14.41600  11.84400  1.000 58.17000  ? 342 VAL D O   1 
ATOM   13287 C  CB  . VAL D  1 311 ? -14.45100 11.37800  12.09900  1.000 60.86000  ? 342 VAL D CB  1 
ATOM   13288 C  CG1 . VAL D  1 311 ? -14.90300 10.32500  13.09400  1.000 54.78000  ? 342 VAL D CG1 1 
ATOM   13289 C  CG2 . VAL D  1 311 ? -15.59800 12.34500  11.78100  1.000 53.94000  ? 342 VAL D CG2 1 
ATOM   13290 N  N   . PRO D  1 312 ? -12.09900 12.81800  10.60300  1.000 58.65000  ? 343 PRO D N   1 
ATOM   13291 C  CA  . PRO D  1 312 ? -11.86100 13.75500  9.49500   1.000 57.79000  ? 343 PRO D CA  1 
ATOM   13292 C  C   . PRO D  1 312 ? -13.15600 14.04000  8.74300   1.000 61.19000  ? 343 PRO D C   1 
ATOM   13293 O  O   . PRO D  1 312 ? -14.08800 13.23100  8.74800   1.000 58.73000  ? 343 PRO D O   1 
ATOM   13294 C  CB  . PRO D  1 312 ? -10.84900 13.02100  8.60900   1.000 53.36000  ? 343 PRO D CB  1 
ATOM   13295 C  CG  . PRO D  1 312 ? -11.09600 11.58800  8.90000   1.000 58.89000  ? 343 PRO D CG  1 
ATOM   13296 C  CD  . PRO D  1 312 ? -11.50500 11.49600  10.34000  1.000 55.46000  ? 343 PRO D CD  1 
ATOM   13297 N  N   . MET D  1 313 ? -13.22900 15.22900  8.14100   1.000 63.83000  ? 344 MET D N   1 
ATOM   13298 C  CA  . MET D  1 313 ? -14.37200 15.60700  7.31700   1.000 64.16000  ? 344 MET D CA  1 
ATOM   13299 C  C   . MET D  1 313 ? -14.04400 16.80700  6.44400   1.000 61.21000  ? 344 MET D C   1 
ATOM   13300 O  O   . MET D  1 313 ? -13.46000 17.78000  6.92800   1.000 58.79000  ? 344 MET D O   1 
ATOM   13301 C  CB  . MET D  1 313 ? -15.60900 15.97200  8.14500   1.000 61.29000  ? 344 MET D CB  1 
ATOM   13302 C  CG  . MET D  1 313 ? -16.77600 16.39600  7.24000   1.000 61.25000  ? 344 MET D CG  1 
ATOM   13303 S  SD  . MET D  1 313 ? -18.32100 16.62000  8.10900   1.000 65.44000  ? 344 MET D SD  1 
ATOM   13304 C  CE  . MET D  1 313 ? -18.52000 15.02600  8.85000   1.000 61.62000  ? 344 MET D CE  1 
ATOM   13305 N  N   . PHE D  1 314 ? -14.50800 16.77300  5.18800   1.000 58.74000  ? 345 PHE D N   1 
ATOM   13306 C  CA  . PHE D  1 314 ? -14.49000 17.96300  4.35200   1.000 57.92000  ? 345 PHE D CA  1 
ATOM   13307 C  C   . PHE D  1 314 ? -15.80600 18.08300  3.59000   1.000 66.88000  ? 345 PHE D C   1 
ATOM   13308 O  O   . PHE D  1 314 ? -16.50200 17.09000  3.35500   1.000 58.22000  ? 345 PHE D O   1 
ATOM   13309 C  CB  . PHE D  1 314 ? -13.29100 17.97800  3.37600   1.000 60.08000  ? 345 PHE D CB  1 
ATOM   13310 C  CG  . PHE D  1 314 ? -13.34000 16.94400  2.27500   1.000 64.28000  ? 345 PHE D CG  1 
ATOM   13311 C  CD1 . PHE D  1 314 ? -14.19500 17.09100  1.18500   1.000 63.74000  ? 345 PHE D CD1 1 
ATOM   13312 C  CD2 . PHE D  1 314 ? -12.48400 15.85300  2.29500   1.000 65.29000  ? 345 PHE D CD2 1 
ATOM   13313 C  CE1 . PHE D  1 314 ? -14.22500 16.14500  0.16600   1.000 63.90000  ? 345 PHE D CE1 1 
ATOM   13314 C  CE2 . PHE D  1 314 ? -12.50000 14.90700  1.25800   1.000 63.37000  ? 345 PHE D CE2 1 
ATOM   13315 C  CZ  . PHE D  1 314 ? -13.37400 15.05300  0.20100   1.000 64.31000  ? 345 PHE D CZ  1 
ATOM   13316 N  N   . PHE D  1 315 ? -16.14700 19.32800  3.23900   1.000 69.57000  ? 346 PHE D N   1 
ATOM   13317 C  CA  . PHE D  1 315 ? -17.19300 19.65400  2.27700   1.000 65.21000  ? 346 PHE D CA  1 
ATOM   13318 C  C   . PHE D  1 315 ? -16.53800 20.16700  1.00500   1.000 61.78000  ? 346 PHE D C   1 
ATOM   13319 O  O   . PHE D  1 315 ? -15.66500 21.03700  1.06300   1.000 65.39000  ? 346 PHE D O   1 
ATOM   13320 C  CB  . PHE D  1 315 ? -18.14300 20.72900  2.80600   1.000 62.59000  ? 346 PHE D CB  1 
ATOM   13321 C  CG  . PHE D  1 315 ? -19.12900 20.24300  3.82800   1.000 64.73000  ? 346 PHE D CG  1 
ATOM   13322 C  CD1 . PHE D  1 315 ? -18.94900 19.04000  4.48800   1.000 61.93000  ? 346 PHE D CD1 1 
ATOM   13323 C  CD2 . PHE D  1 315 ? -20.24700 21.01400  4.13600   1.000 58.93000  ? 346 PHE D CD2 1 
ATOM   13324 C  CE1 . PHE D  1 315 ? -19.86900 18.61200  5.44600   1.000 57.17000  ? 346 PHE D CE1 1 
ATOM   13325 C  CE2 . PHE D  1 315 ? -21.16200 20.60100  5.07900   1.000 54.54000  ? 346 PHE D CE2 1 
ATOM   13326 C  CZ  . PHE D  1 315 ? -20.97300 19.39800  5.74200   1.000 59.90000  ? 346 PHE D CZ  1 
ATOM   13327 N  N   . HIS D  1 316 ? -16.98600 19.66300  -0.13700  1.000 59.38000  ? 347 HIS D N   1 
ATOM   13328 C  CA  . HIS D  1 316 ? -16.48800 20.10700  -1.43200  1.000 64.66000  ? 347 HIS D CA  1 
ATOM   13329 C  C   . HIS D  1 316 ? -17.67200 20.32800  -2.35600  1.000 71.25000  ? 347 HIS D C   1 
ATOM   13330 O  O   . HIS D  1 316 ? -18.36800 19.37400  -2.72000  1.000 70.98000  ? 347 HIS D O   1 
ATOM   13331 C  CB  . HIS D  1 316 ? -15.52500 19.09800  -2.05000  1.000 59.87000  ? 347 HIS D CB  1 
ATOM   13332 C  CG  . HIS D  1 316 ? -15.18400 19.40100  -3.47400  1.000 65.38000  ? 347 HIS D CG  1 
ATOM   13333 N  ND1 . HIS D  1 316 ? -14.02400 20.04600  -3.84100  1.000 67.45000  ? 347 HIS D ND1 1 
ATOM   13334 C  CD2 . HIS D  1 316 ? -15.87300 19.18600  -4.62000  1.000 71.65000  ? 347 HIS D CD2 1 
ATOM   13335 C  CE1 . HIS D  1 316 ? -13.99500 20.18200  -5.15500  1.000 76.06000  ? 347 HIS D CE1 1 
ATOM   13336 N  NE2 . HIS D  1 316 ? -15.11100 19.67600  -5.65000  1.000 73.91000  ? 347 HIS D NE2 1 
ATOM   13337 N  N   . TRP D  1 317 ? -17.87100 21.57200  -2.75800  1.000 74.48000  ? 348 TRP D N   1 
ATOM   13338 C  CA  . TRP D  1 317 ? -18.99700 22.03200  -3.55100  1.000 68.16000  ? 348 TRP D CA  1 
ATOM   13339 C  C   . TRP D  1 317 ? -18.59400 23.31600  -4.25000  1.000 73.13000  ? 348 TRP D C   1 
ATOM   13340 O  O   . TRP D  1 317 ? -18.80800 24.40100  -3.69800  1.000 76.37000  ? 348 TRP D O   1 
ATOM   13341 C  CB  . TRP D  1 317 ? -20.22100 22.27900  -2.67900  1.000 70.59000  ? 348 TRP D CB  1 
ATOM   13342 C  CG  . TRP D  1 317 ? -21.41900 22.70900  -3.47900  1.000 73.75000  ? 348 TRP D CG  1 
ATOM   13343 C  CD1 . TRP D  1 317 ? -21.56900 22.65500  -4.83800  1.000 69.90000  ? 348 TRP D CD1 1 
ATOM   13344 C  CD2 . TRP D  1 317 ? -22.62900 23.25500  -2.96400  1.000 69.27000  ? 348 TRP D CD2 1 
ATOM   13345 N  NE1 . TRP D  1 317 ? -22.80000 23.13700  -5.19200  1.000 74.83000  ? 348 TRP D NE1 1 
ATOM   13346 C  CE2 . TRP D  1 317 ? -23.47300 23.50700  -4.05800  1.000 71.40000  ? 348 TRP D CE2 1 
ATOM   13347 C  CE3 . TRP D  1 317 ? -23.08500 23.54600  -1.68000  1.000 71.88000  ? 348 TRP D CE3 1 
ATOM   13348 C  CZ2 . TRP D  1 317 ? -24.74900 24.03800  -3.90500  1.000 71.46000  ? 348 TRP D CZ2 1 
ATOM   13349 C  CZ3 . TRP D  1 317 ? -24.34600 24.07800  -1.53000  1.000 67.30000  ? 348 TRP D CZ3 1 
ATOM   13350 C  CH2 . TRP D  1 317 ? -25.16400 24.31800  -2.63400  1.000 69.26000  ? 348 TRP D CH2 1 
ATOM   13351 N  N   . PRO D  1 318 ? -17.99100 23.23800  -5.43400  1.000 69.70000  ? 349 PRO D N   1 
ATOM   13352 C  CA  . PRO D  1 318 ? -17.39400 24.44700  -6.02900  1.000 70.73000  ? 349 PRO D CA  1 
ATOM   13353 C  C   . PRO D  1 318 ? -18.35700 25.63300  -6.16300  1.000 76.73000  ? 349 PRO D C   1 
ATOM   13354 O  O   . PRO D  1 318 ? -17.95100 26.79400  -5.99900  1.000 73.46000  ? 349 PRO D O   1 
ATOM   13355 C  CB  . PRO D  1 318 ? -16.89200 23.92500  -7.38100  1.000 72.72000  ? 349 PRO D CB  1 
ATOM   13356 C  CG  . PRO D  1 318 ? -16.57400 22.47600  -7.12000  1.000 70.69000  ? 349 PRO D CG  1 
ATOM   13357 C  CD  . PRO D  1 318 ? -17.67700 22.02000  -6.20300  1.000 70.66000  ? 349 PRO D CD  1 
ATOM   13358 N  N   . LYS D  1 319 ? -19.63800 25.36500  -6.42800  1.000 74.89000  ? 350 LYS D N   1 
ATOM   13359 C  CA  . LYS D  1 319 ? -20.63000 26.42500  -6.62300  1.000 77.26000  ? 350 LYS D CA  1 
ATOM   13360 C  C   . LYS D  1 319 ? -20.84700 27.29500  -5.38400  1.000 75.24000  ? 350 LYS D C   1 
ATOM   13361 O  O   . LYS D  1 319 ? -21.38200 28.40200  -5.50100  1.000 79.29000  ? 350 LYS D O   1 
ATOM   13362 C  CB  . LYS D  1 319 ? -21.96800 25.81500  -7.05800  1.000 74.90000  ? 350 LYS D CB  1 
ATOM   13363 N  N   . LYS D  1 320 ? -20.51400 26.80500  -4.20400  1.000 72.06000  ? 351 LYS D N   1 
ATOM   13364 C  CA  . LYS D  1 320 ? -20.81100 27.52200  -2.96700  1.000 72.62000  ? 351 LYS D CA  1 
ATOM   13365 C  C   . LYS D  1 320 ? -19.68000 27.49300  -1.94300  1.000 79.99000  ? 351 LYS D C   1 
ATOM   13366 O  O   . LYS D  1 320 ? -19.60400 28.40900  -1.11300  1.000 69.94000  ? 351 LYS D O   1 
ATOM   13367 C  CB  . LYS D  1 320 ? -22.08800 26.96800  -2.32200  1.000 79.16000  ? 351 LYS D CB  1 
ATOM   13368 N  N   . ILE D  1 321 ? -18.84600 26.45200  -1.93100  1.000 81.09000  ? 352 ILE D N   1 
ATOM   13369 C  CA  . ILE D  1 321 ? -17.77000 26.29400  -0.96100  1.000 79.88000  ? 352 ILE D CA  1 
ATOM   13370 C  C   . ILE D  1 321 ? -16.50200 26.93200  -1.51200  1.000 75.98000  ? 352 ILE D C   1 
ATOM   13371 O  O   . ILE D  1 321 ? -16.04800 26.58800  -2.61100  1.000 70.65000  ? 352 ILE D O   1 
ATOM   13372 C  CB  . ILE D  1 321 ? -17.53200 24.81100  -0.63700  1.000 78.94000  ? 352 ILE D CB  1 
ATOM   13373 N  N   . LYS D  1 322 ? -15.94200 27.87200  -0.74700  1.000 76.21000  ? 353 LYS D N   1 
ATOM   13374 C  CA  . LYS D  1 322 ? -14.67700 28.49900  -1.10600  1.000 73.66000  ? 353 LYS D CA  1 
ATOM   13375 C  C   . LYS D  1 322 ? -13.52400 27.51500  -0.90900  1.000 76.13000  ? 353 LYS D C   1 
ATOM   13376 O  O   . LYS D  1 322 ? -13.57600 26.61600  -0.06100  1.000 72.28000  ? 353 LYS D O   1 
ATOM   13377 C  CB  . LYS D  1 322 ? -14.44600 29.75100  -0.25900  1.000 68.11000  ? 353 LYS D CB  1 
ATOM   13378 N  N   . LYS D  1 323 ? -12.45800 27.71000  -1.67400  1.000 77.74000  ? 354 LYS D N   1 
ATOM   13379 C  CA  . LYS D  1 323 ? -11.31600 26.81700  -1.56400  1.000 76.84000  ? 354 LYS D CA  1 
ATOM   13380 C  C   . LYS D  1 323 ? -10.49000 27.11000  -0.30700  1.000 77.31000  ? 354 LYS D C   1 
ATOM   13381 O  O   . LYS D  1 323 ? -10.62800 28.15300  0.34600   1.000 72.09000  ? 354 LYS D O   1 
ATOM   13382 C  CB  . LYS D  1 323 ? -10.42800 26.92200  -2.80600  1.000 76.32000  ? 354 LYS D CB  1 
ATOM   13383 C  CG  . LYS D  1 323 ? -11.16700 26.68800  -4.11600  1.000 73.64000  ? 354 LYS D CG  1 
ATOM   13384 C  CD  . LYS D  1 323 ? -10.17000 26.44300  -5.23800  1.000 79.34000  ? 354 LYS D CD  1 
ATOM   13385 C  CE  . LYS D  1 323 ? -10.86100 26.10300  -6.55700  1.000 85.74000  ? 354 LYS D CE  1 
ATOM   13386 N  NZ  . LYS D  1 323 ? -9.86700  25.78300  -7.63400  1.000 81.77000  ? 354 LYS D NZ  1 
ATOM   13387 N  N   . ASP D  1 324 ? -9.66900  26.12600  0.06400   1.000 69.45000  ? 355 ASP D N   1 
ATOM   13388 C  CA  . ASP D  1 324 ? -8.67000  26.27900  1.11200   1.000 69.80000  ? 355 ASP D CA  1 
ATOM   13389 C  C   . ASP D  1 324 ? -9.28800  26.73100  2.42600   1.000 71.85000  ? 355 ASP D C   1 
ATOM   13390 O  O   . ASP D  1 324 ? -8.62200  27.36200  3.24900   1.000 75.37000  ? 355 ASP D O   1 
ATOM   13391 C  CB  . ASP D  1 324 ? -7.58100  27.26300  0.68600   1.000 78.51000  ? 355 ASP D CB  1 
ATOM   13392 C  CG  . ASP D  1 324 ? -6.79500  26.77500  -0.51000  1.000 87.77000  ? 355 ASP D CG  1 
ATOM   13393 O  OD1 . ASP D  1 324 ? -6.85000  25.56100  -0.80200  1.000 87.89000  ? 355 ASP D OD1 1 
ATOM   13394 O  OD2 . ASP D  1 324 ? -6.13300  27.61200  -1.16700  1.000 95.18000  ? 355 ASP D OD2 1 
ATOM   13395 N  N   . GLN D  1 325 ? -10.55700 26.41400  2.63700   1.000 69.24000  ? 356 GLN D N   1 
ATOM   13396 C  CA  . GLN D  1 325 ? -11.23400 26.84000  3.85100   1.000 74.76000  ? 356 GLN D CA  1 
ATOM   13397 C  C   . GLN D  1 325 ? -10.91200 25.89800  5.00700   1.000 69.88000  ? 356 GLN D C   1 
ATOM   13398 O  O   . GLN D  1 325 ? -10.73500 24.68900  4.82800   1.000 70.26000  ? 356 GLN D O   1 
ATOM   13399 C  CB  . GLN D  1 325 ? -12.75100 26.91200  3.62900   1.000 68.13000  ? 356 GLN D CB  1 
ATOM   13400 N  N   . ARG D  1 326 ? -10.83100 26.46700  6.20300   1.000 55.57000  ? 357 ARG D N   1 
ATOM   13401 C  CA  . ARG D  1 326 ? -10.66000 25.69400  7.41800   1.000 61.85000  ? 357 ARG D CA  1 
ATOM   13402 C  C   . ARG D  1 326 ? -11.79100 26.05100  8.36900   1.000 64.41000  ? 357 ARG D C   1 
ATOM   13403 O  O   . ARG D  1 326 ? -11.90000 27.20200  8.80600   1.000 66.76000  ? 357 ARG D O   1 
ATOM   13404 C  CB  . ARG D  1 326 ? -9.29900  25.99600  8.04600   1.000 71.56000  ? 357 ARG D CB  1 
ATOM   13405 C  CG  . ARG D  1 326 ? -8.68200  24.84800  8.78600   1.000 66.28000  ? 357 ARG D CG  1 
ATOM   13406 C  CD  . ARG D  1 326 ? -7.16600  25.04900  8.92100   1.000 77.21000  ? 357 ARG D CD  1 
ATOM   13407 N  NE  . ARG D  1 326 ? -6.54200  23.85400  9.47700   1.000 76.57000  ? 357 ARG D NE  1 
ATOM   13408 C  CZ  . ARG D  1 326 ? -6.09000  22.83800  8.75400   1.000 77.16000  ? 357 ARG D CZ  1 
ATOM   13409 N  NH1 . ARG D  1 326 ? -6.18800  22.83000  7.43100   1.000 70.91000  ? 357 ARG D NH1 1 
ATOM   13410 N  NH2 . ARG D  1 326 ? -5.56600  21.78600  9.37400   1.000 76.18000  ? 357 ARG D NH2 1 
ATOM   13411 N  N   . PHE D  1 327 ? -12.63200 25.07400  8.68800   1.000 61.35000  ? 358 PHE D N   1 
ATOM   13412 C  CA  . PHE D  1 327 ? -13.76700 25.29900  9.57500   1.000 65.58000  ? 358 PHE D CA  1 
ATOM   13413 C  C   . PHE D  1 327 ? -13.44900 24.68800  10.93400  1.000 66.72000  ? 358 PHE D C   1 
ATOM   13414 O  O   . PHE D  1 327 ? -13.42600 23.46100  11.08400  1.000 69.18000  ? 358 PHE D O   1 
ATOM   13415 C  CB  . PHE D  1 327 ? -15.04900 24.71900  8.97800   1.000 66.26000  ? 358 PHE D CB  1 
ATOM   13416 C  CG  . PHE D  1 327 ? -16.29700 25.23200  9.63900   1.000 66.60000  ? 358 PHE D CG  1 
ATOM   13417 C  CD1 . PHE D  1 327 ? -16.89100 26.39700  9.19900   1.000 61.38000  ? 358 PHE D CD1 1 
ATOM   13418 C  CD2 . PHE D  1 327 ? -16.85000 24.57100  10.72600  1.000 67.50000  ? 358 PHE D CD2 1 
ATOM   13419 C  CE1 . PHE D  1 327 ? -18.01800 26.88400  9.80700   1.000 67.43000  ? 358 PHE D CE1 1 
ATOM   13420 C  CE2 . PHE D  1 327 ? -17.98600 25.05700  11.34300  1.000 70.66000  ? 358 PHE D CE2 1 
ATOM   13421 C  CZ  . PHE D  1 327 ? -18.57400 26.21800  10.87800  1.000 68.15000  ? 358 PHE D CZ  1 
ATOM   13422 N  N   . ASP D  1 328 ? -13.23200 25.54300  11.92600  1.000 58.71000  ? 359 ASP D N   1 
ATOM   13423 C  CA  . ASP D  1 328 ? -12.72300 25.11700  13.21700  1.000 62.40000  ? 359 ASP D CA  1 
ATOM   13424 C  C   . ASP D  1 328 ? -13.79300 25.04600  14.28900  1.000 68.68000  ? 359 ASP D C   1 
ATOM   13425 O  O   . ASP D  1 328 ? -13.50000 24.61600  15.41000  1.000 68.56000  ? 359 ASP D O   1 
ATOM   13426 C  CB  . ASP D  1 328 ? -11.58600 26.04800  13.65100  1.000 68.07000  ? 359 ASP D CB  1 
ATOM   13427 C  CG  . ASP D  1 328 ? -10.39200 25.97000  12.71000  1.000 65.12000  ? 359 ASP D CG  1 
ATOM   13428 O  OD1 . ASP D  1 328 ? -10.06700 24.84600  12.26800  1.000 70.66000  ? 359 ASP D OD1 1 
ATOM   13429 O  OD2 . ASP D  1 328 ? -9.82500  27.02600  12.35600  1.000 67.08000  ? 359 ASP D OD2 1 
ATOM   13430 N  N   . PHE D  1 329 ? -15.01000 25.40800  13.97600  1.000 70.44000  ? 360 PHE D N   1 
ATOM   13431 C  CA  . PHE D  1 329 ? -16.03700 25.28400  15.00100  1.000 69.30000  ? 360 PHE D CA  1 
ATOM   13432 C  C   . PHE D  1 329 ? -16.53500 23.83800  15.04700  1.000 62.92000  ? 360 PHE D C   1 
ATOM   13433 O  O   . PHE D  1 329 ? -16.60500 23.17400  14.01000  1.000 65.05000  ? 360 PHE D O   1 
ATOM   13434 C  CB  . PHE D  1 329 ? -17.19300 26.24200  14.69800  1.000 72.97000  ? 360 PHE D CB  1 
ATOM   13435 C  CG  . PHE D  1 329 ? -16.74600 27.67400  14.51600  1.000 76.60000  ? 360 PHE D CG  1 
ATOM   13436 C  CD1 . PHE D  1 329 ? -16.61400 28.52600  15.60000  1.000 79.14000  ? 360 PHE D CD1 1 
ATOM   13437 C  CD2 . PHE D  1 329 ? -16.40400 28.14900  13.25200  1.000 78.95000  ? 360 PHE D CD2 1 
ATOM   13438 C  CE1 . PHE D  1 329 ? -16.17900 29.83000  15.42600  1.000 78.41000  ? 360 PHE D CE1 1 
ATOM   13439 C  CE2 . PHE D  1 329 ? -15.96300 29.45200  13.07600  1.000 79.68000  ? 360 PHE D CE2 1 
ATOM   13440 C  CZ  . PHE D  1 329 ? -15.85600 30.29200  14.16500  1.000 75.96000  ? 360 PHE D CZ  1 
ATOM   13441 N  N   . PRO D  1 330 ? -16.85000 23.32100  16.23100  1.000 63.19000  ? 361 PRO D N   1 
ATOM   13442 C  CA  . PRO D  1 330 ? -17.32200 21.92900  16.33400  1.000 66.20000  ? 361 PRO D CA  1 
ATOM   13443 C  C   . PRO D  1 330 ? -18.66800 21.71800  15.64900  1.000 68.70000  ? 361 PRO D C   1 
ATOM   13444 O  O   . PRO D  1 330 ? -19.60200 22.50500  15.82000  1.000 68.49000  ? 361 PRO D O   1 
ATOM   13445 C  CB  . PRO D  1 330 ? -17.40800 21.68900  17.85000  1.000 68.60000  ? 361 PRO D CB  1 
ATOM   13446 C  CG  . PRO D  1 330 ? -17.29500 23.07700  18.49200  1.000 61.86000  ? 361 PRO D CG  1 
ATOM   13447 C  CD  . PRO D  1 330 ? -16.44200 23.86300  17.53900  1.000 67.10000  ? 361 PRO D CD  1 
ATOM   13448 N  N   . VAL D  1 331 ? -18.74800 20.64500  14.85700  1.000 66.99000  ? 362 VAL D N   1 
ATOM   13449 C  CA  . VAL D  1 331 ? -19.96300 20.23500  14.16500  1.000 66.17000  ? 362 VAL D CA  1 
ATOM   13450 C  C   . VAL D  1 331 ? -20.22900 18.77600  14.50900  1.000 67.81000  ? 362 VAL D C   1 
ATOM   13451 O  O   . VAL D  1 331 ? -19.36700 18.06100  15.02200  1.000 61.49000  ? 362 VAL D O   1 
ATOM   13452 C  CB  . VAL D  1 331 ? -19.86700 20.39900  12.63200  1.000 64.18000  ? 362 VAL D CB  1 
ATOM   13453 C  CG1 . VAL D  1 331 ? -19.59600 21.84500  12.24800  1.000 63.52000  ? 362 VAL D CG1 1 
ATOM   13454 C  CG2 . VAL D  1 331 ? -18.80500 19.47200  12.06200  1.000 63.73000  ? 362 VAL D CG2 1 
ATOM   13455 N  N   . SER D  1 332 ? -21.43500 18.32700  14.19400  1.000 64.59000  ? 363 SER D N   1 
ATOM   13456 C  CA  . SER D  1 332 ? -21.81800 16.95700  14.48200  1.000 66.03000  ? 363 SER D CA  1 
ATOM   13457 C  C   . SER D  1 332 ? -22.30200 16.30600  13.19500  1.000 62.29000  ? 363 SER D C   1 
ATOM   13458 O  O   . SER D  1 332 ? -22.83000 16.98000  12.31000  1.000 63.95000  ? 363 SER D O   1 
ATOM   13459 C  CB  . SER D  1 332 ? -22.89400 16.90000  15.56500  1.000 60.08000  ? 363 SER D CB  1 
ATOM   13460 O  OG  . SER D  1 332 ? -23.34700 15.57700  15.73100  1.000 63.10000  ? 363 SER D OG  1 
ATOM   13461 N  N   . SER D  1 333 ? -22.10200 14.99000  13.07300  1.000 63.12000  ? 364 SER D N   1 
ATOM   13462 C  CA  . SER D  1 333 ? -22.68600 14.30400  11.92200  1.000 65.40000  ? 364 SER D CA  1 
ATOM   13463 C  C   . SER D  1 333 ? -24.21000 14.41000  11.92900  1.000 62.60000  ? 364 SER D C   1 
ATOM   13464 O  O   . SER D  1 333 ? -24.83100 14.35000  10.86000  1.000 58.45000  ? 364 SER D O   1 
ATOM   13465 C  CB  . SER D  1 333 ? -22.24400 12.83600  11.87600  1.000 51.68000  ? 364 SER D CB  1 
ATOM   13466 O  OG  . SER D  1 333 ? -22.58300 12.16000  13.07400  1.000 60.77000  ? 364 SER D OG  1 
ATOM   13467 N  N   . LEU D  1 334 ? -24.80500 14.65800  13.10100  1.000 58.25000  ? 365 LEU D N   1 
ATOM   13468 C  CA  . LEU D  1 334 ? -26.23000 14.94000  13.21700  1.000 56.28000  ? 365 LEU D CA  1 
ATOM   13469 C  C   . LEU D  1 334 ? -26.65400 16.14900  12.39400  1.000 66.28000  ? 365 LEU D C   1 
ATOM   13470 O  O   . LEU D  1 334 ? -27.85700 16.33700  12.16600  1.000 66.77000  ? 365 LEU D O   1 
ATOM   13471 C  CB  . LEU D  1 334 ? -26.57400 15.16500  14.68900  1.000 62.79000  ? 365 LEU D CB  1 
ATOM   13472 C  CG  . LEU D  1 334 ? -26.33400 13.93200  15.55800  1.000 64.04000  ? 365 LEU D CG  1 
ATOM   13473 C  CD1 . LEU D  1 334 ? -26.06700 14.29900  17.00600  1.000 61.78000  ? 365 LEU D CD1 1 
ATOM   13474 C  CD2 . LEU D  1 334 ? -27.54600 13.01000  15.46900  1.000 60.18000  ? 365 LEU D CD2 1 
ATOM   13475 N  N   . ASP D  1 335 ? -25.70000 16.97800  11.95100  1.000 65.69000  ? 366 ASP D N   1 
ATOM   13476 C  CA  . ASP D  1 335 ? -26.03200 18.14300  11.13600  1.000 67.43000  ? 366 ASP D CA  1 
ATOM   13477 C  C   . ASP D  1 335 ? -26.32600 17.78600  9.68500   1.000 63.06000  ? 366 ASP D C   1 
ATOM   13478 O  O   . ASP D  1 335 ? -26.88600 18.61300  8.96000   1.000 64.79000  ? 366 ASP D O   1 
ATOM   13479 C  CB  . ASP D  1 335 ? -24.90500 19.18400  11.18100  1.000 64.35000  ? 366 ASP D CB  1 
ATOM   13480 C  CG  . ASP D  1 335 ? -24.63100 19.70400  12.59700  1.000 70.18000  ? 366 ASP D CG  1 
ATOM   13481 O  OD1 . ASP D  1 335 ? -25.55400 19.69100  13.44500  1.000 68.71000  ? 366 ASP D OD1 1 
ATOM   13482 O  OD2 . ASP D  1 335 ? -23.49100 20.15300  12.85300  1.000 71.76000  ? 366 ASP D OD2 1 
ATOM   13483 N  N   . LEU D  1 336 ? -25.94900 16.58900  9.23700   1.000 66.10000  ? 367 LEU D N   1 
ATOM   13484 C  CA  . LEU D  1 336 ? -26.11000 16.24900  7.82300   1.000 70.76000  ? 367 LEU D CA  1 
ATOM   13485 C  C   . LEU D  1 336 ? -27.58100 16.14900  7.42300   1.000 65.48000  ? 367 LEU D C   1 
ATOM   13486 O  O   . LEU D  1 336 ? -27.96000 16.54200  6.31000   1.000 59.16000  ? 367 LEU D O   1 
ATOM   13487 C  CB  . LEU D  1 336 ? -25.38600 14.93900  7.52400   1.000 66.50000  ? 367 LEU D CB  1 
ATOM   13488 C  CG  . LEU D  1 336 ? -23.88800 14.96900  7.82100   1.000 65.79000  ? 367 LEU D CG  1 
ATOM   13489 C  CD1 . LEU D  1 336 ? -23.31400 13.57200  7.68900   1.000 60.95000  ? 367 LEU D CD1 1 
ATOM   13490 C  CD2 . LEU D  1 336 ? -23.18600 15.93000  6.86400   1.000 61.72000  ? 367 LEU D CD2 1 
ATOM   13491 N  N   . TYR D  1 337 ? -28.41500 15.60100  8.30300   1.000 65.34000  ? 368 TYR D N   1 
ATOM   13492 C  CA  . TYR D  1 337 ? -29.82900 15.43200  7.97800   1.000 65.88000  ? 368 TYR D CA  1 
ATOM   13493 C  C   . TYR D  1 337 ? -30.47400 16.77900  7.66600   1.000 69.73000  ? 368 TYR D C   1 
ATOM   13494 O  O   . TYR D  1 337 ? -30.93300 16.97400  6.52400   1.000 67.48000  ? 368 TYR D O   1 
ATOM   13495 C  CB  . TYR D  1 337 ? -30.50000 14.66100  9.12300   1.000 63.14000  ? 368 TYR D CB  1 
ATOM   13496 C  CG  . TYR D  1 337 ? -31.87500 14.05500  8.87200   1.000 72.51000  ? 368 TYR D CG  1 
ATOM   13497 C  CD1 . TYR D  1 337 ? -32.89500 14.75800  8.22200   1.000 73.11000  ? 368 TYR D CD1 1 
ATOM   13498 C  CD2 . TYR D  1 337 ? -32.16700 12.77800  9.35100   1.000 72.09000  ? 368 TYR D CD2 1 
ATOM   13499 C  CE1 . TYR D  1 337 ? -34.16800 14.17400  8.03100   1.000 70.10000  ? 368 TYR D CE1 1 
ATOM   13500 C  CE2 . TYR D  1 337 ? -33.41800 12.19800  9.17000   1.000 70.56000  ? 368 TYR D CE2 1 
ATOM   13501 C  CZ  . TYR D  1 337 ? -34.41200 12.89100  8.51100   1.000 72.07000  ? 368 TYR D CZ  1 
ATOM   13502 O  OH  . TYR D  1 337 ? -35.63400 12.27500  8.34700   1.000 72.92000  ? 368 TYR D OH  1 
ATOM   13503 N  N   . PRO D  1 338 ? -30.49400 17.76300  8.58300   1.000 65.99000  ? 369 PRO D N   1 
ATOM   13504 C  CA  . PRO D  1 338 ? -31.11200 19.05200  8.23200   1.000 65.93000  ? 369 PRO D CA  1 
ATOM   13505 C  C   . PRO D  1 338 ? -30.34700 19.84600  7.18800   1.000 65.27000  ? 369 PRO D C   1 
ATOM   13506 O  O   . PRO D  1 338 ? -30.96900 20.62000  6.45800   1.000 65.37000  ? 369 PRO D O   1 
ATOM   13507 C  CB  . PRO D  1 338 ? -31.18100 19.79000  9.58000   1.000 64.53000  ? 369 PRO D CB  1 
ATOM   13508 C  CG  . PRO D  1 338 ? -30.09700 19.21600  10.37400  1.000 65.76000  ? 369 PRO D CG  1 
ATOM   13509 C  CD  . PRO D  1 338 ? -30.05700 17.76400  9.99700   1.000 71.81000  ? 369 PRO D CD  1 
ATOM   13510 N  N   . THR D  1 339 ? -29.03000 19.67900  7.06500   1.000 68.18000  ? 370 THR D N   1 
ATOM   13511 C  CA  . THR D  1 339 ? -28.32200 20.39900  6.01000   1.000 65.85000  ? 370 THR D CA  1 
ATOM   13512 C  C   . THR D  1 339 ? -28.77200 19.92500  4.63600   1.000 68.73000  ? 370 THR D C   1 
ATOM   13513 O  O   . THR D  1 339 ? -28.91100 20.73200  3.71000   1.000 66.20000  ? 370 THR D O   1 
ATOM   13514 C  CB  . THR D  1 339 ? -26.80900 20.23000  6.15600   1.000 62.42000  ? 370 THR D CB  1 
ATOM   13515 O  OG1 . THR D  1 339 ? -26.39700 20.69300  7.44600   1.000 70.75000  ? 370 THR D OG1 1 
ATOM   13516 C  CG2 . THR D  1 339 ? -26.07700 21.03200  5.09300   1.000 58.58000  ? 370 THR D CG2 1 
ATOM   13517 N  N   . PHE D  1 340 ? -28.98000 18.61300  4.48300   1.000 70.51000  ? 371 PHE D N   1 
ATOM   13518 C  CA  . PHE D  1 340 ? -29.35300 18.05400  3.18600   1.000 67.38000  ? 371 PHE D CA  1 
ATOM   13519 C  C   . PHE D  1 340 ? -30.79000 18.41600  2.81200   1.000 67.51000  ? 371 PHE D C   1 
ATOM   13520 O  O   . PHE D  1 340 ? -31.06800 18.81700  1.67500   1.000 61.55000  ? 371 PHE D O   1 
ATOM   13521 C  CB  . PHE D  1 340 ? -29.14500 16.53700  3.20000   1.000 66.61000  ? 371 PHE D CB  1 
ATOM   13522 C  CG  . PHE D  1 340 ? -27.69000 16.12100  3.31600   1.000 71.49000  ? 371 PHE D CG  1 
ATOM   13523 C  CD1 . PHE D  1 340 ? -26.67000 17.03000  3.06600   1.000 69.15000  ? 371 PHE D CD1 1 
ATOM   13524 C  CD2 . PHE D  1 340 ? -27.34800 14.82600  3.70400   1.000 69.91000  ? 371 PHE D CD2 1 
ATOM   13525 C  CE1 . PHE D  1 340 ? -25.33500 16.65900  3.18100   1.000 68.96000  ? 371 PHE D CE1 1 
ATOM   13526 C  CE2 . PHE D  1 340 ? -26.01300 14.44600  3.83600   1.000 65.36000  ? 371 PHE D CE2 1 
ATOM   13527 C  CZ  . PHE D  1 340 ? -25.00500 15.36400  3.56700   1.000 69.50000  ? 371 PHE D CZ  1 
ATOM   13528 N  N   . THR D  1 341 ? -31.72800 18.26000  3.74800   1.000 67.35000  ? 372 THR D N   1 
ATOM   13529 C  CA  . THR D  1 341 ? -33.10100 18.63800  3.43900   1.000 63.90000  ? 372 THR D CA  1 
ATOM   13530 C  C   . THR D  1 341 ? -33.20500 20.14100  3.19100   1.000 70.29000  ? 372 THR D C   1 
ATOM   13531 O  O   . THR D  1 341 ? -33.97100 20.58500  2.32500   1.000 68.10000  ? 372 THR D O   1 
ATOM   13532 C  CB  . THR D  1 341 ? -34.04600 18.19200  4.55200   1.000 67.19000  ? 372 THR D CB  1 
ATOM   13533 O  OG1 . THR D  1 341 ? -33.64200 18.75800  5.79900   1.000 63.07000  ? 372 THR D OG1 1 
ATOM   13534 C  CG2 . THR D  1 341 ? -34.04500 16.67800  4.66900   1.000 66.33000  ? 372 THR D CG2 1 
ATOM   13535 N  N   . GLY D  1 342 ? -32.42400 20.93900  3.92400   1.000 67.14000  ? 373 GLY D N   1 
ATOM   13536 C  CA  . GLY D  1 342 ? -32.33800 22.35900  3.61200   1.000 66.08000  ? 373 GLY D CA  1 
ATOM   13537 C  C   . GLY D  1 342 ? -31.88800 22.61100  2.18300   1.000 64.16000  ? 373 GLY D C   1 
ATOM   13538 O  O   . GLY D  1 342 ? -32.51400 23.37500  1.44300   1.000 65.67000  ? 373 GLY D O   1 
ATOM   13539 N  N   . LEU D  1 343 ? -30.79400 21.97000  1.77400   1.000 61.10000  ? 374 LEU D N   1 
ATOM   13540 C  CA  . LEU D  1 343 ? -30.32600 22.11900  0.40100   1.000 62.11000  ? 374 LEU D CA  1 
ATOM   13541 C  C   . LEU D  1 343 ? -31.35000 21.62000  -0.59700  1.000 66.65000  ? 374 LEU D C   1 
ATOM   13542 O  O   . LEU D  1 343 ? -31.48500 22.18100  -1.69100  1.000 68.29000  ? 374 LEU D O   1 
ATOM   13543 C  CB  . LEU D  1 343 ? -29.03000 21.33700  0.21700   1.000 67.19000  ? 374 LEU D CB  1 
ATOM   13544 C  CG  . LEU D  1 343 ? -27.78500 21.87000  0.88700   1.000 62.31000  ? 374 LEU D CG  1 
ATOM   13545 C  CD1 . LEU D  1 343 ? -26.70800 20.82400  0.83000   1.000 63.70000  ? 374 LEU D CD1 1 
ATOM   13546 C  CD2 . LEU D  1 343 ? -27.36000 23.07900  0.07000   1.000 67.28000  ? 374 LEU D CD2 1 
ATOM   13547 N  N   . ALA D  1 344 ? -32.08100 20.57400  -0.23300  1.000 70.32000  ? 375 ALA D N   1 
ATOM   13548 C  CA  . ALA D  1 344 ? -33.06200 19.97400  -1.12200  1.000 71.30000  ? 375 ALA D CA  1 
ATOM   13549 C  C   . ALA D  1 344 ? -34.40200 20.70000  -1.11800  1.000 69.52000  ? 375 ALA D C   1 
ATOM   13550 O  O   . ALA D  1 344 ? -35.28600 20.32600  -1.89100  1.000 69.06000  ? 375 ALA D O   1 
ATOM   13551 C  CB  . ALA D  1 344 ? -33.25500 18.50200  -0.74600  1.000 63.72000  ? 375 ALA D CB  1 
ATOM   13552 N  N   . GLU D  1 345 ? -34.57800 21.71700  -0.27700  1.000 66.24000  ? 376 GLU D N   1 
ATOM   13553 C  CA  . GLU D  1 345 ? -35.87100 22.38600  -0.14300  1.000 69.78000  ? 376 GLU D CA  1 
ATOM   13554 C  C   . GLU D  1 345 ? -36.97300 21.38000  0.17200   1.000 68.05000  ? 376 GLU D C   1 
ATOM   13555 O  O   . GLU D  1 345 ? -38.12500 21.53900  -0.24300  1.000 71.50000  ? 376 GLU D O   1 
ATOM   13556 C  CB  . GLU D  1 345 ? -36.22200 23.18500  -1.40600  1.000 67.27000  ? 376 GLU D CB  1 
ATOM   13557 C  CG  . GLU D  1 345 ? -35.19300 24.23600  -1.79400  1.000 71.81000  ? 376 GLU D CG  1 
ATOM   13558 C  CD  . GLU D  1 345 ? -35.44200 24.83600  -3.17800  1.000 82.60000  ? 376 GLU D CD  1 
ATOM   13559 O  OE1 . GLU D  1 345 ? -36.58000 24.73000  -3.69500  1.000 81.79000  ? 376 GLU D OE1 1 
ATOM   13560 O  OE2 . GLU D  1 345 ? -34.49200 25.41100  -3.75300  1.000 87.09000  ? 376 GLU D OE2 1 
ATOM   13561 N  N   . ALA D  1 346 ? -36.62700 20.31500  0.88000   1.000 59.68000  ? 377 ALA D N   1 
ATOM   13562 C  CA  . ALA D  1 346 ? -37.60700 19.29000  1.19600   1.000 66.62000  ? 377 ALA D CA  1 
ATOM   13563 C  C   . ALA D  1 346 ? -38.32900 19.64700  2.48700   1.000 75.21000  ? 377 ALA D C   1 
ATOM   13564 O  O   . ALA D  1 346 ? -37.76000 20.26300  3.39300   1.000 75.74000  ? 377 ALA D O   1 
ATOM   13565 C  CB  . ALA D  1 346 ? -36.94100 17.92400  1.34000   1.000 65.58000  ? 377 ALA D CB  1 
ATOM   13566 N  N   . LYS D  1 347 ? -39.58000 19.22700  2.58200   1.000 71.23000  ? 378 LYS D N   1 
ATOM   13567 C  CA  . LYS D  1 347 ? -40.36100 19.49200  3.77500   1.000 76.35000  ? 378 LYS D CA  1 
ATOM   13568 C  C   . LYS D  1 347 ? -40.23300 18.31900  4.73300   1.000 78.95000  ? 378 LYS D C   1 
ATOM   13569 O  O   . LYS D  1 347 ? -40.24500 17.15700  4.31900   1.000 82.14000  ? 378 LYS D O   1 
ATOM   13570 C  CB  . LYS D  1 347 ? -41.83000 19.74200  3.41700   1.000 81.19000  ? 378 LYS D CB  1 
ATOM   13571 N  N   . LEU D  1 348 ? -40.08300 18.62500  5.99500   1.000 77.64000  ? 379 LEU D N   1 
ATOM   13572 C  CA  . LEU D  1 348 ? -39.94400 17.55200  6.95800   1.000 74.76000  ? 379 LEU D CA  1 
ATOM   13573 C  C   . LEU D  1 348 ? -41.30900 16.94700  7.30400   1.000 79.03000  ? 379 LEU D C   1 
ATOM   13574 O  O   . LEU D  1 348 ? -42.32000 17.65100  7.33200   1.000 81.26000  ? 379 LEU D O   1 
ATOM   13575 C  CB  . LEU D  1 348 ? -39.26100 18.07400  8.22200   1.000 76.81000  ? 379 LEU D CB  1 
ATOM   13576 C  CG  . LEU D  1 348 ? -37.73600 18.31400  8.26000   1.000 74.49000  ? 379 LEU D CG  1 
ATOM   13577 C  CD1 . LEU D  1 348 ? -37.20300 19.36500  7.26200   1.000 70.38000  ? 379 LEU D CD1 1 
ATOM   13578 C  CD2 . LEU D  1 348 ? -37.36800 18.71800  9.67000   1.000 64.08000  ? 379 LEU D CD2 1 
ATOM   13579 N  N   . PRO D  1 349 ? -41.35400 15.64200  7.58200   1.000 83.81000  ? 380 PRO D N   1 
ATOM   13580 C  CA  . PRO D  1 349 ? -42.60300 15.00300  8.02200   1.000 84.28000  ? 380 PRO D CA  1 
ATOM   13581 C  C   . PRO D  1 349 ? -43.13200 15.58200  9.32900   1.000 86.31000  ? 380 PRO D C   1 
ATOM   13582 O  O   . PRO D  1 349 ? -42.39600 16.15800  10.13300  1.000 88.82000  ? 380 PRO D O   1 
ATOM   13583 C  CB  . PRO D  1 349 ? -42.20900 13.53000  8.19600   1.000 78.72000  ? 380 PRO D CB  1 
ATOM   13584 C  CG  . PRO D  1 349 ? -41.01600 13.35800  7.31300   1.000 80.27000  ? 380 PRO D CG  1 
ATOM   13585 C  CD  . PRO D  1 349 ? -40.27100 14.66000  7.39300   1.000 79.76000  ? 380 PRO D CD  1 
ATOM   13586 N  N   . LYS D  1 350 ? -44.44200 15.42900  9.52700   1.000 87.29000  ? 381 LYS D N   1 
ATOM   13587 C  CA  . LYS D  1 350 ? -45.07900 15.87100  10.76300  1.000 87.00000  ? 381 LYS D CA  1 
ATOM   13588 C  C   . LYS D  1 350 ? -44.52400 15.08500  11.94400  1.000 85.87000  ? 381 LYS D C   1 
ATOM   13589 O  O   . LYS D  1 350 ? -44.60800 13.85300  11.97900  1.000 87.84000  ? 381 LYS D O   1 
ATOM   13590 C  CB  . LYS D  1 350 ? -46.59400 15.68800  10.67800  1.000 80.32000  ? 381 LYS D CB  1 
ATOM   13591 N  N   . GLY D  1 351 ? -43.94400 15.79400  12.90600  1.000 76.74000  ? 382 GLY D N   1 
ATOM   13592 C  CA  . GLY D  1 351 ? -43.38900 15.13900  14.06400  1.000 75.03000  ? 382 GLY D CA  1 
ATOM   13593 C  C   . GLY D  1 351 ? -41.94200 14.73500  13.91900  1.000 79.12000  ? 382 GLY D C   1 
ATOM   13594 O  O   . GLY D  1 351 ? -41.44000 13.97800  14.76100  1.000 73.43000  ? 382 GLY D O   1 
ATOM   13595 N  N   . LYS D  1 352 ? -41.25300 15.20000  12.87900  1.000 73.29000  ? 383 LYS D N   1 
ATOM   13596 C  CA  . LYS D  1 352 ? -39.87400 14.78900  12.68000  1.000 73.72000  ? 383 LYS D CA  1 
ATOM   13597 C  C   . LYS D  1 352 ? -39.00600 15.52300  13.69500  1.000 74.56000  ? 383 LYS D C   1 
ATOM   13598 O  O   . LYS D  1 352 ? -38.87400 16.75100  13.63700  1.000 76.31000  ? 383 LYS D O   1 
ATOM   13599 C  CB  . LYS D  1 352 ? -39.44600 15.09600  11.24900  1.000 69.97000  ? 383 LYS D CB  1 
ATOM   13600 N  N   . GLN D  1 353 ? -38.38500 14.77000  14.60300  1.000 69.06000  ? 384 GLN D N   1 
ATOM   13601 C  CA  . GLN D  1 353 ? -37.51500 15.33400  15.62700  1.000 74.41000  ? 384 GLN D CA  1 
ATOM   13602 C  C   . GLN D  1 353 ? -36.06100 15.21900  15.19400  1.000 76.44000  ? 384 GLN D C   1 
ATOM   13603 O  O   . GLN D  1 353 ? -35.62500 14.17000  14.71100  1.000 76.65000  ? 384 GLN D O   1 
ATOM   13604 C  CB  . GLN D  1 353 ? -37.71300 14.62300  16.96800  1.000 67.15000  ? 384 GLN D CB  1 
ATOM   13605 N  N   . LEU D  1 354 ? -35.30700 16.29300  15.39500  1.000 72.97000  ? 385 LEU D N   1 
ATOM   13606 C  CA  . LEU D  1 354 ? -33.91700 16.34000  14.97100  1.000 73.69000  ? 385 LEU D CA  1 
ATOM   13607 C  C   . LEU D  1 354 ? -33.03100 16.89900  16.08500  1.000 72.01000  ? 385 LEU D C   1 
ATOM   13608 O  O   . LEU D  1 354 ? -33.39500 17.86300  16.76900  1.000 65.84000  ? 385 LEU D O   1 
ATOM   13609 C  CB  . LEU D  1 354 ? -33.78100 17.17900  13.67900  1.000 68.19000  ? 385 LEU D CB  1 
ATOM   13610 C  CG  . LEU D  1 354 ? -34.35500 16.54400  12.40500  1.000 67.29000  ? 385 LEU D CG  1 
ATOM   13611 C  CD1 . LEU D  1 354 ? -33.99500 17.33600  11.15200  1.000 61.78000  ? 385 LEU D CD1 1 
ATOM   13612 C  CD2 . LEU D  1 354 ? -33.89500 15.10000  12.26100  1.000 68.03000  ? 385 LEU D CD2 1 
ATOM   13613 N  N   . ASP D  1 355 ? -31.84900 16.30500  16.24700  1.000 71.32000  ? 386 ASP D N   1 
ATOM   13614 C  CA  . ASP D  1 355 ? -30.90400 16.73900  17.26600  1.000 62.77000  ? 386 ASP D CA  1 
ATOM   13615 C  C   . ASP D  1 355 ? -29.77800 17.60200  16.71500  1.000 62.11000  ? 386 ASP D C   1 
ATOM   13616 O  O   . ASP D  1 355 ? -29.09900 18.26600  17.50000  1.000 67.68000  ? 386 ASP D O   1 
ATOM   13617 C  CB  . ASP D  1 355 ? -30.30500 15.52400  17.98500  1.000 64.98000  ? 386 ASP D CB  1 
ATOM   13618 C  CG  . ASP D  1 355 ? -31.29000 14.84600  18.91600  1.000 69.96000  ? 386 ASP D CG  1 
ATOM   13619 O  OD1 . ASP D  1 355 ? -32.09400 15.57100  19.54200  1.000 70.30000  ? 386 ASP D OD1 1 
ATOM   13620 O  OD2 . ASP D  1 355 ? -31.26000 13.59700  19.02900  1.000 71.84000  ? 386 ASP D OD2 1 
ATOM   13621 N  N   . GLY D  1 356 ? -29.60100 17.65600  15.39600  1.000 57.85000  ? 387 GLY D N   1 
ATOM   13622 C  CA  . GLY D  1 356 ? -28.59900 18.49700  14.78200  1.000 58.08000  ? 387 GLY D CA  1 
ATOM   13623 C  C   . GLY D  1 356 ? -29.20700 19.74700  14.17100  1.000 63.40000  ? 387 GLY D C   1 
ATOM   13624 O  O   . GLY D  1 356 ? -30.36300 20.09800  14.41100  1.000 65.02000  ? 387 GLY D O   1 
ATOM   13625 N  N   . LYS D  1 357 ? -28.40900 20.42300  13.34900  1.000 62.59000  ? 388 LYS D N   1 
ATOM   13626 C  CA  . LYS D  1 357 ? -28.81200 21.70500  12.79100  1.000 63.43000  ? 388 LYS D CA  1 
ATOM   13627 C  C   . LYS D  1 357 ? -28.28200 21.83100  11.37400  1.000 66.13000  ? 388 LYS D C   1 
ATOM   13628 O  O   . LYS D  1 357 ? -27.29600 21.19600  11.00000  1.000 66.19000  ? 388 LYS D O   1 
ATOM   13629 C  CB  . LYS D  1 357 ? -28.28900 22.91900  13.59600  1.000 67.25000  ? 388 LYS D CB  1 
ATOM   13630 C  CG  . LYS D  1 357 ? -27.97000 22.71900  15.08000  1.000 68.82000  ? 388 LYS D CG  1 
ATOM   13631 C  CD  . LYS D  1 357 ? -27.44400 24.03200  15.68400  1.000 74.77000  ? 388 LYS D CD  1 
ATOM   13632 C  CE  . LYS D  1 357 ? -26.81000 23.84700  17.06900  1.000 78.12000  ? 388 LYS D CE  1 
ATOM   13633 N  NZ  . LYS D  1 357 ? -27.74500 23.39300  18.14500  1.000 80.02000  ? 388 LYS D NZ  1 
ATOM   13634 N  N   . ASN D  1 358 ? -28.96500 22.65600  10.58600  1.000 64.52000  ? 389 ASN D N   1 
ATOM   13635 C  CA  . ASN D  1 358 ? -28.48400 23.02800  9.26300   1.000 66.31000  ? 389 ASN D CA  1 
ATOM   13636 C  C   . ASN D  1 358 ? -27.27600 23.94000  9.41900   1.000 69.35000  ? 389 ASN D C   1 
ATOM   13637 O  O   . ASN D  1 358 ? -27.38900 25.05000  9.94700   1.000 76.07000  ? 389 ASN D O   1 
ATOM   13638 C  CB  . ASN D  1 358 ? -29.60600 23.72000  8.48200   1.000 61.06000  ? 389 ASN D CB  1 
ATOM   13639 C  CG  . ASN D  1 358 ? -29.18700 24.16900  7.09300   1.000 65.64000  ? 389 ASN D CG  1 
ATOM   13640 O  OD1 . ASN D  1 358 ? -28.04100 23.99400  6.67300   1.000 72.10000  ? 389 ASN D OD1 1 
ATOM   13641 N  ND2 . ASN D  1 358 ? -30.14200 24.72500  6.35000   1.000 76.95000  ? 389 ASN D ND2 1 
ATOM   13642 N  N   . ILE D  1 359 ? -26.11900 23.48900  8.95200   1.000 69.98000  ? 390 ILE D N   1 
ATOM   13643 C  CA  . ILE D  1 359 ? -24.88700 24.24100  9.14700   1.000 73.59000  ? 390 ILE D CA  1 
ATOM   13644 C  C   . ILE D  1 359 ? -24.36200 24.81100  7.84300   1.000 72.11000  ? 390 ILE D C   1 
ATOM   13645 O  O   . ILE D  1 359 ? -23.22800 25.28900  7.80400   1.000 73.44000  ? 390 ILE D O   1 
ATOM   13646 C  CB  . ILE D  1 359 ? -23.80800 23.39800  9.84400   1.000 65.88000  ? 390 ILE D CB  1 
ATOM   13647 C  CG1 . ILE D  1 359 ? -23.34000 22.26400  8.93000   1.000 65.43000  ? 390 ILE D CG1 1 
ATOM   13648 C  CG2 . ILE D  1 359 ? -24.31700 22.87100  11.18200  1.000 69.48000  ? 390 ILE D CG2 1 
ATOM   13649 C  CD1 . ILE D  1 359 ? -22.14800 21.52900  9.45500   1.000 63.82000  ? 390 ILE D CD1 1 
ATOM   13650 N  N   . MET D  1 360 ? -25.13600 24.73800  6.75800   1.000 63.27000  ? 391 MET D N   1 
ATOM   13651 C  CA  . MET D  1 360 ? -24.58200 25.17900  5.48500   1.000 69.39000  ? 391 MET D CA  1 
ATOM   13652 C  C   . MET D  1 360 ? -24.27300 26.66500  5.51000   1.000 77.45000  ? 391 MET D C   1 
ATOM   13653 O  O   . MET D  1 360 ? -23.17500 27.07800  5.11600   1.000 73.91000  ? 391 MET D O   1 
ATOM   13654 C  CB  . MET D  1 360 ? -25.52800 24.87300  4.32700   1.000 68.30000  ? 391 MET D CB  1 
ATOM   13655 C  CG  . MET D  1 360 ? -24.85800 25.08800  2.97900   1.000 69.07000  ? 391 MET D CG  1 
ATOM   13656 S  SD  . MET D  1 360 ? -23.20500 24.34700  2.99300   1.000 77.18000  ? 391 MET D SD  1 
ATOM   13657 C  CE  . MET D  1 360 ? -22.60600 24.71200  1.35200   1.000 69.83000  ? 391 MET D CE  1 
ATOM   13658 N  N   . ASP D  1 361 ? -25.19600 27.47300  6.04300   1.000 78.34000  ? 392 ASP D N   1 
ATOM   13659 C  CA  . ASP D  1 361 ? -24.97000 28.91400  6.09600   1.000 79.71000  ? 392 ASP D CA  1 
ATOM   13660 C  C   . ASP D  1 361 ? -23.75900 29.24500  6.94900   1.000 79.08000  ? 392 ASP D C   1 
ATOM   13661 O  O   . ASP D  1 361 ? -22.88200 30.01200  6.53300   1.000 76.73000  ? 392 ASP D O   1 
ATOM   13662 C  CB  . ASP D  1 361 ? -26.20400 29.62700  6.64700   1.000 80.41000  ? 392 ASP D CB  1 
ATOM   13663 C  CG  . ASP D  1 361 ? -26.26400 31.08000  6.22400   1.000 92.02000  ? 392 ASP D CG  1 
ATOM   13664 O  OD1 . ASP D  1 361 ? -25.72600 31.40700  5.14300   1.000 93.48000  ? 392 ASP D OD1 1 
ATOM   13665 O  OD2 . ASP D  1 361 ? -26.80300 31.90400  6.99400   1.000 95.86000  ? 392 ASP D OD2 1 
ATOM   13666 N  N   . ASP D  1 362 ? -23.68300 28.64000  8.13700   1.000 75.62000  ? 393 ASP D N   1 
ATOM   13667 C  CA  . ASP D  1 362 ? -22.52900 28.81500  9.00500   1.000 72.10000  ? 393 ASP D CA  1 
ATOM   13668 C  C   . ASP D  1 362 ? -21.24000 28.49100  8.26800   1.000 71.85000  ? 393 ASP D C   1 
ATOM   13669 O  O   . ASP D  1 362 ? -20.23900 29.19100  8.42500   1.000 74.20000  ? 393 ASP D O   1 
ATOM   13670 C  CB  . ASP D  1 362 ? -22.69300 27.93900  10.23900  1.000 75.08000  ? 393 ASP D CB  1 
ATOM   13671 C  CG  . ASP D  1 362 ? -23.92500 28.30700  11.03900  1.000 80.27000  ? 393 ASP D CG  1 
ATOM   13672 O  OD1 . ASP D  1 362 ? -25.04700 28.16100  10.49300  1.000 86.16000  ? 393 ASP D OD1 1 
ATOM   13673 O  OD2 . ASP D  1 362 ? -23.78200 28.74400  12.20100  1.000 79.48000  ? 393 ASP D OD2 1 
ATOM   13674 N  N   . VAL D  1 363 ? -21.25700 27.46100  7.41900   1.000 75.61000  ? 394 VAL D N   1 
ATOM   13675 C  CA  . VAL D  1 363 ? -20.06100 27.12300  6.65200   1.000 74.16000  ? 394 VAL D CA  1 
ATOM   13676 C  C   . VAL D  1 363 ? -19.72000 28.25500  5.69300   1.000 68.56000  ? 394 VAL D C   1 
ATOM   13677 O  O   . VAL D  1 363 ? -18.54800 28.59000  5.49900   1.000 63.98000  ? 394 VAL D O   1 
ATOM   13678 C  CB  . VAL D  1 363 ? -20.25600 25.78700  5.90600   1.000 73.54000  ? 394 VAL D CB  1 
ATOM   13679 C  CG1 . VAL D  1 363 ? -19.16500 25.58200  4.86900   1.000 66.76000  ? 394 VAL D CG1 1 
ATOM   13680 C  CG2 . VAL D  1 363 ? -20.28500 24.62100  6.88900   1.000 70.67000  ? 394 VAL D CG2 1 
ATOM   13681 N  N   . LEU D  1 364 ? -20.73600 28.85500  5.07100   1.000 74.60000  ? 395 LEU D N   1 
ATOM   13682 C  CA  . LEU D  1 364 ? -20.48200 29.94100  4.12900   1.000 76.65000  ? 395 LEU D CA  1 
ATOM   13683 C  C   . LEU D  1 364 ? -20.09900 31.23800  4.82700   1.000 71.82000  ? 395 LEU D C   1 
ATOM   13684 O  O   . LEU D  1 364 ? -19.37700 32.05400  4.24600   1.000 73.43000  ? 395 LEU D O   1 
ATOM   13685 C  CB  . LEU D  1 364 ? -21.69400 30.17800  3.23000   1.000 71.37000  ? 395 LEU D CB  1 
ATOM   13686 C  CG  . LEU D  1 364 ? -22.04100 29.13900  2.16900   1.000 74.26000  ? 395 LEU D CG  1 
ATOM   13687 C  CD1 . LEU D  1 364 ? -20.87600 28.18000  1.92900   1.000 66.21000  ? 395 LEU D CD1 1 
ATOM   13688 C  CD2 . LEU D  1 364 ? -23.33400 28.41500  2.49800   1.000 74.67000  ? 395 LEU D CD2 1 
ATOM   13689 N  N   . LYS D  1 365 ? -20.59500 31.46400  6.04500   1.000 75.04000  ? 396 LYS D N   1 
ATOM   13690 C  CA  . LYS D  1 365 ? -20.31900 32.69200  6.78300   1.000 79.60000  ? 396 LYS D CA  1 
ATOM   13691 C  C   . LYS D  1 365 ? -19.35800 32.51300  7.96700   1.000 77.07000  ? 396 LYS D C   1 
ATOM   13692 O  O   . LYS D  1 365 ? -19.12400 33.47200  8.70800   1.000 76.70000  ? 396 LYS D O   1 
ATOM   13693 C  CB  . LYS D  1 365 ? -21.64300 33.32000  7.22900   1.000 75.51000  ? 396 LYS D CB  1 
ATOM   13694 C  CG  . LYS D  1 365 ? -22.30500 34.10200  6.09200   1.000 79.41000  ? 396 LYS D CG  1 
ATOM   13695 C  CD  . LYS D  1 365 ? -23.83100 34.13400  6.17300   1.000 84.44000  ? 396 LYS D CD  1 
ATOM   13696 C  CE  . LYS D  1 365 ? -24.43600 34.69000  4.87600   1.000 86.84000  ? 396 LYS D CE  1 
ATOM   13697 N  NZ  . LYS D  1 365 ? -25.92600 34.62100  4.84700   1.000 84.83000  ? 396 LYS D NZ  1 
ATOM   13698 N  N   . ASN D  1 366 ? -18.79000 31.32700  8.15900   1.000 75.32000  ? 397 ASN D N   1 
ATOM   13699 C  CA  . ASN D  1 366 ? -17.83300 31.06200  9.23600   1.000 70.24000  ? 397 ASN D CA  1 
ATOM   13700 C  C   . ASN D  1 366 ? -18.34600 31.51900  10.60300  1.000 74.19000  ? 397 ASN D C   1 
ATOM   13701 O  O   . ASN D  1 366 ? -17.77800 32.40400  11.24200  1.000 80.46000  ? 397 ASN D O   1 
ATOM   13702 C  CB  . ASN D  1 366 ? -16.47800 31.69800  8.93300   1.000 70.28000  ? 397 ASN D CB  1 
ATOM   13703 C  CG  . ASN D  1 366 ? -15.35800 31.05400  9.72800   1.000 78.04000  ? 397 ASN D CG  1 
ATOM   13704 O  OD1 . ASN D  1 366 ? -14.92100 29.94500  9.41400   1.000 76.23000  ? 397 ASN D OD1 1 
ATOM   13705 N  ND2 . ASN D  1 366 ? -14.90200 31.73400  10.77800  1.000 77.76000  ? 397 ASN D ND2 1 
ATOM   13706 N  N   . THR D  1 367 ? -19.45200 30.91600  11.03400  1.000 72.14000  ? 398 THR D N   1 
ATOM   13707 C  CA  . THR D  1 367 ? -20.05800 31.19300  12.32900  1.000 73.17000  ? 398 THR D CA  1 
ATOM   13708 C  C   . THR D  1 367 ? -20.19800 29.90500  13.13000  1.000 74.05000  ? 398 THR D C   1 
ATOM   13709 O  O   . THR D  1 367 ? -20.28400 28.81300  12.56400  1.000 75.18000  ? 398 THR D O   1 
ATOM   13710 C  CB  . THR D  1 367 ? -21.44600 31.83800  12.16300  1.000 85.24000  ? 398 THR D CB  1 
ATOM   13711 O  OG1 . THR D  1 367 ? -22.46500 30.85100  12.38500  1.000 85.37000  ? 398 THR D OG1 1 
ATOM   13712 C  CG2 . THR D  1 367 ? -21.61200 32.41300  10.74700  1.000 76.98000  ? 398 THR D CG2 1 
ATOM   13713 N  N   . GLU D  1 368 ? -20.24800 30.03900  14.46300  1.000 78.71000  ? 399 GLU D N   1 
ATOM   13714 C  CA  . GLU D  1 368 ? -20.32400 28.86000  15.32800  1.000 81.97000  ? 399 GLU D CA  1 
ATOM   13715 C  C   . GLU D  1 368 ? -21.76400 28.38300  15.44400  1.000 79.35000  ? 399 GLU D C   1 
ATOM   13716 O  O   . GLU D  1 368 ? -22.59500 29.07200  16.04900  1.000 76.27000  ? 399 GLU D O   1 
ATOM   13717 C  CB  . GLU D  1 368 ? -19.79100 29.10000  16.74400  1.000 75.06000  ? 399 GLU D CB  1 
ATOM   13718 C  CG  . GLU D  1 368 ? -19.02700 30.38100  16.97500  1.000 88.49000  ? 399 GLU D CG  1 
ATOM   13719 C  CD  . GLU D  1 368 ? -18.68800 30.58300  18.44100  1.000 88.70000  ? 399 GLU D CD  1 
ATOM   13720 O  OE1 . GLU D  1 368 ? -18.99000 29.67500  19.25200  1.000 82.36000  ? 399 GLU D OE1 1 
ATOM   13721 O  OE2 . GLU D  1 368 ? -18.08900 31.63200  18.76900  1.000 91.12000  ? 399 GLU D OE2 1 
ATOM   13722 N  N   . PRO D  1 369 ? -22.10100 27.21200  14.89800  1.000 77.26000  ? 400 PRO D N   1 
ATOM   13723 C  CA  . PRO D  1 369 ? -23.47400 26.72000  15.05500  1.000 78.31000  ? 400 PRO D CA  1 
ATOM   13724 C  C   . PRO D  1 369 ? -23.79200 26.26200  16.46400  1.000 78.26000  ? 400 PRO D C   1 
ATOM   13725 O  O   . PRO D  1 369 ? -24.97200 26.26100  16.83700  1.000 76.31000  ? 400 PRO D O   1 
ATOM   13726 C  CB  . PRO D  1 369 ? -23.55100 25.55900  14.05400  1.000 78.66000  ? 400 PRO D CB  1 
ATOM   13727 C  CG  . PRO D  1 369 ? -22.13300 25.13000  13.86000  1.000 73.17000  ? 400 PRO D CG  1 
ATOM   13728 C  CD  . PRO D  1 369 ? -21.32100 26.38000  13.96400  1.000 73.86000  ? 400 PRO D CD  1 
ATOM   13729 N  N   . TYR D  1 370 ? -22.79500 25.91700  17.27700  1.000 74.97000  ? 401 TYR D N   1 
ATOM   13730 C  CA  . TYR D  1 370 ? -23.08100 25.33200  18.57900  1.000 74.75000  ? 401 TYR D CA  1 
ATOM   13731 C  C   . TYR D  1 370 ? -22.55500 26.19100  19.72700  1.000 77.41000  ? 401 TYR D C   1 
ATOM   13732 O  O   . TYR D  1 370 ? -22.22600 25.66900  20.79500  1.000 75.37000  ? 401 TYR D O   1 
ATOM   13733 C  CB  . TYR D  1 370 ? -22.48800 23.92700  18.66900  1.000 78.52000  ? 401 TYR D CB  1 
ATOM   13734 C  CG  . TYR D  1 370 ? -23.21900 22.85000  17.89200  1.000 74.37000  ? 401 TYR D CG  1 
ATOM   13735 C  CD1 . TYR D  1 370 ? -22.87800 22.57800  16.57200  1.000 66.63000  ? 401 TYR D CD1 1 
ATOM   13736 C  CD2 . TYR D  1 370 ? -24.21400 22.07700  18.49000  1.000 77.50000  ? 401 TYR D CD2 1 
ATOM   13737 C  CE1 . TYR D  1 370 ? -23.51700 21.58200  15.85500  1.000 72.48000  ? 401 TYR D CE1 1 
ATOM   13738 C  CE2 . TYR D  1 370 ? -24.86800 21.07200  17.77700  1.000 73.96000  ? 401 TYR D CE2 1 
ATOM   13739 C  CZ  . TYR D  1 370 ? -24.51100 20.82900  16.45700  1.000 74.39000  ? 401 TYR D CZ  1 
ATOM   13740 O  OH  . TYR D  1 370 ? -25.14800 19.83600  15.73100  1.000 71.56000  ? 401 TYR D OH  1 
ATOM   13741 N  N   . LYS D  1 371 ? -22.48800 27.50800  19.53200  1.000 80.60000  ? 402 LYS D N   1 
ATOM   13742 C  CA  . LYS D  1 371 ? -22.12800 28.39700  20.62800  1.000 77.94000  ? 402 LYS D CA  1 
ATOM   13743 C  C   . LYS D  1 371 ? -23.15700 28.24000  21.73500  1.000 75.62000  ? 402 LYS D C   1 
ATOM   13744 O  O   . LYS D  1 371 ? -24.36000 28.31400  21.48800  1.000 75.77000  ? 402 LYS D O   1 
ATOM   13745 C  CB  . LYS D  1 371 ? -22.05800 29.84700  20.15700  1.000 76.07000  ? 402 LYS D CB  1 
ATOM   13746 N  N   . ASP D  1 372 ? -22.67500 27.95800  22.94400  1.000 77.90000  ? 403 ASP D N   1 
ATOM   13747 C  CA  . ASP D  1 372 ? -23.46000 27.70900  24.15300  1.000 79.30000  ? 403 ASP D CA  1 
ATOM   13748 C  C   . ASP D  1 372 ? -24.31200 26.45300  24.05800  1.000 82.00000  ? 403 ASP D C   1 
ATOM   13749 O  O   . ASP D  1 372 ? -25.21000 26.25600  24.89200  1.000 78.54000  ? 403 ASP D O   1 
ATOM   13750 C  CB  . ASP D  1 372 ? -24.36700 28.88900  24.51400  1.000 79.61000  ? 403 ASP D CB  1 
ATOM   13751 C  CG  . ASP D  1 372 ? -23.59800 30.15800  24.73000  1.000 79.91000  ? 403 ASP D CG  1 
ATOM   13752 O  OD1 . ASP D  1 372 ? -22.60400 30.12100  25.48200  1.000 85.42000  ? 403 ASP D OD1 1 
ATOM   13753 O  OD2 . ASP D  1 372 ? -23.98000 31.18700  24.13300  1.000 85.40000  ? 403 ASP D OD2 1 
ATOM   13754 N  N   . GLU D  1 373 ? -24.04700 25.58400  23.08500  1.000 81.60000  ? 404 GLU D N   1 
ATOM   13755 C  CA  . GLU D  1 373 ? -24.72900 24.30500  22.97900  1.000 80.88000  ? 404 GLU D CA  1 
ATOM   13756 C  C   . GLU D  1 373 ? -23.69900 23.18200  22.94100  1.000 81.48000  ? 404 GLU D C   1 
ATOM   13757 O  O   . GLU D  1 373 ? -22.52800 23.38900  22.60500  1.000 79.41000  ? 404 GLU D O   1 
ATOM   13758 C  CB  . GLU D  1 373 ? -25.63600 24.25700  21.73900  1.000 81.01000  ? 404 GLU D CB  1 
ATOM   13759 C  CG  . GLU D  1 373 ? -26.94600 25.02600  21.90700  1.000 78.81000  ? 404 GLU D CG  1 
ATOM   13760 C  CD  . GLU D  1 373 ? -27.48500 25.55400  20.59200  1.000 80.40000  ? 404 GLU D CD  1 
ATOM   13761 O  OE1 . GLU D  1 373 ? -26.86900 26.47900  20.01400  1.000 79.12000  ? 404 GLU D OE1 1 
ATOM   13762 O  OE2 . GLU D  1 373 ? -28.52400 25.03900  20.13300  1.000 94.07000  ? 404 GLU D OE2 1 
ATOM   13763 N  N   . MET D  1 374 ? -24.17500 21.97100  23.22300  1.000 81.33000  ? 405 MET D N   1 
ATOM   13764 C  CA  . MET D  1 374 ? -23.32600 20.82500  23.50500  1.000 75.38000  ? 405 MET D CA  1 
ATOM   13765 C  C   . MET D  1 374 ? -23.29300 19.86600  22.32700  1.000 73.49000  ? 405 MET D C   1 
ATOM   13766 O  O   . MET D  1 374 ? -24.30700 19.65600  21.66000  1.000 78.90000  ? 405 MET D O   1 
ATOM   13767 C  CB  . MET D  1 374 ? -23.83300 20.06300  24.72900  1.000 80.32000  ? 405 MET D CB  1 
ATOM   13768 C  CG  . MET D  1 374 ? -23.52100 20.69500  26.06100  1.000 86.22000  ? 405 MET D CG  1 
ATOM   13769 S  SD  . MET D  1 374 ? -21.80900 20.42500  26.52000  1.000 86.44000  ? 405 MET D SD  1 
ATOM   13770 C  CE  . MET D  1 374 ? -21.98600 20.08700  28.27100  1.000 77.64000  ? 405 MET D CE  1 
ATOM   13771 N  N   . ILE D  1 375 ? -22.13900 19.24500  22.11300  1.000 72.94000  ? 406 ILE D N   1 
ATOM   13772 C  CA  . ILE D  1 375 ? -22.01000 18.08300  21.24500  1.000 67.63000  ? 406 ILE D CA  1 
ATOM   13773 C  C   . ILE D  1 375 ? -21.62700 16.92600  22.15100  1.000 72.01000  ? 406 ILE D C   1 
ATOM   13774 O  O   . ILE D  1 375 ? -20.63800 17.00900  22.88700  1.000 70.41000  ? 406 ILE D O   1 
ATOM   13775 C  CB  . ILE D  1 375 ? -20.96600 18.30400  20.14300  1.000 68.26000  ? 406 ILE D CB  1 
ATOM   13776 C  CG1 . ILE D  1 375 ? -21.48100 19.32000  19.12300  1.000 64.86000  ? 406 ILE D CG1 1 
ATOM   13777 C  CG2 . ILE D  1 375 ? -20.66300 17.00200  19.44300  1.000 67.54000  ? 406 ILE D CG2 1 
ATOM   13778 C  CD1 . ILE D  1 375 ? -20.43400 19.75200  18.13400  1.000 67.39000  ? 406 ILE D CD1 1 
ATOM   13779 N  N   . TYR D  1 376 ? -22.41800 15.86200  22.12200  1.000 73.67000  ? 407 TYR D N   1 
ATOM   13780 C  CA  . TYR D  1 376 ? -22.35700 14.80300  23.11900  1.000 66.51000  ? 407 TYR D CA  1 
ATOM   13781 C  C   . TYR D  1 376 ? -21.78800 13.52000  22.54100  1.000 69.84000  ? 407 TYR D C   1 
ATOM   13782 O  O   . TYR D  1 376 ? -21.60800 13.36000  21.32600  1.000 68.27000  ? 407 TYR D O   1 
ATOM   13783 C  CB  . TYR D  1 376 ? -23.73800 14.50000  23.71600  1.000 72.34000  ? 407 TYR D CB  1 
ATOM   13784 C  CG  . TYR D  1 376 ? -24.29800 15.55700  24.62700  1.000 75.09000  ? 407 TYR D CG  1 
ATOM   13785 C  CD1 . TYR D  1 376 ? -23.66100 15.85600  25.82100  1.000 75.18000  ? 407 TYR D CD1 1 
ATOM   13786 C  CD2 . TYR D  1 376 ? -25.47300 16.23300  24.32100  1.000 77.16000  ? 407 TYR D CD2 1 
ATOM   13787 C  CE1 . TYR D  1 376 ? -24.16000 16.81100  26.68600  1.000 77.72000  ? 407 TYR D CE1 1 
ATOM   13788 C  CE2 . TYR D  1 376 ? -25.98400 17.20200  25.18500  1.000 77.63000  ? 407 TYR D CE2 1 
ATOM   13789 C  CZ  . TYR D  1 376 ? -25.31800 17.48000  26.37000  1.000 81.52000  ? 407 TYR D CZ  1 
ATOM   13790 O  OH  . TYR D  1 376 ? -25.78400 18.42500  27.25900  1.000 84.57000  ? 407 TYR D OH  1 
ATOM   13791 N  N   . SER D  1 377 ? -21.42500 12.64500  23.47400  1.000 70.50000  ? 408 SER D N   1 
ATOM   13792 C  CA  . SER D  1 377 ? -21.21000 11.23100  23.23100  1.000 64.80000  ? 408 SER D CA  1 
ATOM   13793 C  C   . SER D  1 377 ? -21.41800 10.51900  24.55600  1.000 66.87000  ? 408 SER D C   1 
ATOM   13794 O  O   . SER D  1 377 ? -20.98600 11.01900  25.59600  1.000 65.75000  ? 408 SER D O   1 
ATOM   13795 C  CB  . SER D  1 377 ? -19.81600 10.95200  22.67700  1.000 67.94000  ? 408 SER D CB  1 
ATOM   13796 O  OG  . SER D  1 377 ? -19.64200 9.55800   22.52100  1.000 67.07000  ? 408 SER D OG  1 
ATOM   13797 N  N   . LEU D  1 378 ? -22.12100 9.38900   24.53100  1.000 64.24000  ? 409 LEU D N   1 
ATOM   13798 C  CA  . LEU D  1 378 ? -22.23200 8.54400   25.71700  1.000 62.04000  ? 409 LEU D CA  1 
ATOM   13799 C  C   . LEU D  1 378 ? -22.18300 7.09400   25.26700  1.000 62.92000  ? 409 LEU D C   1 
ATOM   13800 O  O   . LEU D  1 378 ? -23.01600 6.67300   24.46400  1.000 66.98000  ? 409 LEU D O   1 
ATOM   13801 C  CB  . LEU D  1 378 ? -23.52200 8.82300   26.50000  1.000 60.54000  ? 409 LEU D CB  1 
ATOM   13802 C  CG  . LEU D  1 378 ? -23.61700 8.11100   27.85500  1.000 64.20000  ? 409 LEU D CG  1 
ATOM   13803 C  CD1 . LEU D  1 378 ? -24.38900 8.96900   28.84900  1.000 67.00000  ? 409 LEU D CD1 1 
ATOM   13804 C  CD2 . LEU D  1 378 ? -24.19800 6.70100   27.79700  1.000 66.19000  ? 409 LEU D CD2 1 
ATOM   13805 N  N   . ARG D  1 379 ? -21.23800 6.32100   25.79000  1.000 60.51000  ? 410 ARG D N   1 
ATOM   13806 C  CA  . ARG D  1 379 ? -21.06100 4.94600   25.35400  1.000 59.37000  ? 410 ARG D CA  1 
ATOM   13807 C  C   . ARG D  1 379 ? -21.25300 3.99200   26.52600  1.000 63.14000  ? 410 ARG D C   1 
ATOM   13808 O  O   . ARG D  1 379 ? -20.59700 4.13500   27.56400  1.000 59.14000  ? 410 ARG D O   1 
ATOM   13809 C  CB  . ARG D  1 379 ? -19.68800 4.76600   24.70900  1.000 61.81000  ? 410 ARG D CB  1 
ATOM   13810 C  CG  . ARG D  1 379 ? -19.46500 3.39900   24.12100  1.000 58.50000  ? 410 ARG D CG  1 
ATOM   13811 C  CD  . ARG D  1 379 ? -18.50300 2.61200   24.95200  1.000 55.96000  ? 410 ARG D CD  1 
ATOM   13812 N  NE  . ARG D  1 379 ? -18.63100 1.18200   24.70700  1.000 58.59000  ? 410 ARG D NE  1 
ATOM   13813 C  CZ  . ARG D  1 379 ? -17.93500 0.51500   23.79500  1.000 59.35000  ? 410 ARG D CZ  1 
ATOM   13814 N  NH1 . ARG D  1 379 ? -17.06000 1.12800   23.00500  1.000 52.03000  ? 410 ARG D NH1 1 
ATOM   13815 N  NH2 . ARG D  1 379 ? -18.10800 -0.80100  23.68300  1.000 52.36000  ? 410 ARG D NH2 1 
ATOM   13816 N  N   . TYR D  1 380 ? -22.14900 3.02300   26.35900  1.000 58.43000  ? 411 TYR D N   1 
ATOM   13817 C  CA  . TYR D  1 380 ? -22.42100 2.06100   27.42000  1.000 61.41000  ? 411 TYR D CA  1 
ATOM   13818 C  C   . TYR D  1 380 ? -21.26900 1.08300   27.57700  1.000 62.53000  ? 411 TYR D C   1 
ATOM   13819 O  O   . TYR D  1 380 ? -20.66300 0.65000   26.59700  1.000 61.68000  ? 411 TYR D O   1 
ATOM   13820 C  CB  . TYR D  1 380 ? -23.71900 1.30800   27.13700  1.000 58.16000  ? 411 TYR D CB  1 
ATOM   13821 C  CG  . TYR D  1 380 ? -24.92700 2.21400   27.10200  1.000 64.42000  ? 411 TYR D CG  1 
ATOM   13822 C  CD1 . TYR D  1 380 ? -25.37500 2.83800   28.25500  1.000 65.53000  ? 411 TYR D CD1 1 
ATOM   13823 C  CD2 . TYR D  1 380 ? -25.60000 2.47300   25.91500  1.000 62.99000  ? 411 TYR D CD2 1 
ATOM   13824 C  CE1 . TYR D  1 380 ? -26.47800 3.68000   28.23300  1.000 69.27000  ? 411 TYR D CE1 1 
ATOM   13825 C  CE2 . TYR D  1 380 ? -26.70700 3.31400   25.88300  1.000 67.40000  ? 411 TYR D CE2 1 
ATOM   13826 C  CZ  . TYR D  1 380 ? -27.14100 3.91300   27.04500  1.000 67.96000  ? 411 TYR D CZ  1 
ATOM   13827 O  OH  . TYR D  1 380 ? -28.23400 4.75100   27.02500  1.000 65.48000  ? 411 TYR D OH  1 
ATOM   13828 N  N   . ARG D  1 381 ? -20.91800 0.79100   28.82100  1.000 62.37000  ? 412 ARG D N   1 
ATOM   13829 C  CA  . ARG D  1 381 ? -19.92500 -0.23200  29.11900  1.000 60.10000  ? 412 ARG D CA  1 
ATOM   13830 C  C   . ARG D  1 381 ? -20.56900 -1.29300  30.01700  1.000 67.28000  ? 412 ARG D C   1 
ATOM   13831 O  O   . ARG D  1 381 ? -21.77600 -1.26400  30.27800  1.000 62.38000  ? 412 ARG D O   1 
ATOM   13832 C  CB  . ARG D  1 381 ? -18.68700 0.39500   29.75400  1.000 58.93000  ? 412 ARG D CB  1 
ATOM   13833 C  CG  . ARG D  1 381 ? -17.90700 1.33700   28.83900  1.000 57.16000  ? 412 ARG D CG  1 
ATOM   13834 C  CD  . ARG D  1 381 ? -16.99500 0.58200   27.88800  1.000 51.09000  ? 412 ARG D CD  1 
ATOM   13835 N  NE  . ARG D  1 381 ? -16.19100 1.49800   27.08700  1.000 55.89000  ? 412 ARG D NE  1 
ATOM   13836 C  CZ  . ARG D  1 381 ? -15.39800 1.12000   26.09300  1.000 56.65000  ? 412 ARG D CZ  1 
ATOM   13837 N  NH1 . ARG D  1 381 ? -15.30500 -0.15100  25.73100  1.000 58.51000  ? 412 ARG D NH1 1 
ATOM   13838 N  NH2 . ARG D  1 381 ? -14.65400 2.03100   25.46800  1.000 47.68000  ? 412 ARG D NH2 1 
ATOM   13839 N  N   . GLU D  1 382 ? -19.75400 -2.23600  30.49600  1.000 62.19000  ? 413 GLU D N   1 
ATOM   13840 C  CA  . GLU D  1 382 ? -20.25100 -3.32000  31.34500  1.000 64.75000  ? 413 GLU D CA  1 
ATOM   13841 C  C   . GLU D  1 382 ? -20.34100 -2.82600  32.78800  1.000 69.06000  ? 413 GLU D C   1 
ATOM   13842 O  O   . GLU D  1 382 ? -19.51900 -3.15100  33.65100  1.000 66.59000  ? 413 GLU D O   1 
ATOM   13843 C  CB  . GLU D  1 382 ? -19.36600 -4.55800  31.23800  1.000 61.72000  ? 413 GLU D CB  1 
ATOM   13844 C  CG  . GLU D  1 382 ? -19.09500 -5.01600  29.83100  1.000 64.06000  ? 413 GLU D CG  1 
ATOM   13845 C  CD  . GLU D  1 382 ? -20.37100 -5.14400  29.02200  1.000 72.79000  ? 413 GLU D CD  1 
ATOM   13846 O  OE1 . GLU D  1 382 ? -21.30400 -5.83800  29.49600  1.000 71.61000  ? 413 GLU D OE1 1 
ATOM   13847 O  OE2 . GLU D  1 382 ? -20.44800 -4.53600  27.93100  1.000 66.47000  ? 413 GLU D OE2 1 
ATOM   13848 N  N   . GLY D  1 383 ? -21.37800 -2.03500  33.05700  1.000 67.88000  ? 414 GLY D N   1 
ATOM   13849 C  CA  . GLY D  1 383 ? -21.66000 -1.58000  34.40400  1.000 68.88000  ? 414 GLY D CA  1 
ATOM   13850 C  C   . GLY D  1 383 ? -21.43500 -0.10900  34.66200  1.000 73.03000  ? 414 GLY D C   1 
ATOM   13851 O  O   . GLY D  1 383 ? -21.62400 0.33200   35.80000  1.000 72.74000  ? 414 GLY D O   1 
ATOM   13852 N  N   . TYR D  1 384 ? -21.02700 0.65900   33.65800  1.000 67.19000  ? 415 TYR D N   1 
ATOM   13853 C  CA  . TYR D  1 384 ? -20.80500 2.09100   33.79900  1.000 63.00000  ? 415 TYR D CA  1 
ATOM   13854 C  C   . TYR D  1 384 ? -20.87700 2.68600   32.40600  1.000 59.68000  ? 415 TYR D C   1 
ATOM   13855 O  O   . TYR D  1 384 ? -20.93100 1.96300   31.41300  1.000 67.37000  ? 415 TYR D O   1 
ATOM   13856 C  CB  . TYR D  1 384 ? -19.45200 2.40400   34.45900  1.000 62.19000  ? 415 TYR D CB  1 
ATOM   13857 C  CG  . TYR D  1 384 ? -18.25900 1.96900   33.62900  1.000 54.35000  ? 415 TYR D CG  1 
ATOM   13858 C  CD1 . TYR D  1 384 ? -17.73900 0.68600   33.74200  1.000 58.60000  ? 415 TYR D CD1 1 
ATOM   13859 C  CD2 . TYR D  1 384 ? -17.67900 2.83300   32.70900  1.000 53.98000  ? 415 TYR D CD2 1 
ATOM   13860 C  CE1 . TYR D  1 384 ? -16.65300 0.28200   32.97200  1.000 60.35000  ? 415 TYR D CE1 1 
ATOM   13861 C  CE2 . TYR D  1 384 ? -16.60300 2.44000   31.93300  1.000 53.66000  ? 415 TYR D CE2 1 
ATOM   13862 C  CZ  . TYR D  1 384 ? -16.09600 1.16700   32.06800  1.000 55.20000  ? 415 TYR D CZ  1 
ATOM   13863 O  OH  . TYR D  1 384 ? -15.03600 0.77800   31.28700  1.000 53.03000  ? 415 TYR D OH  1 
ATOM   13864 N  N   . ASN D  1 385 ? -20.79500 4.00700   32.33200  1.000 59.96000  ? 416 ASN D N   1 
ATOM   13865 C  CA  . ASN D  1 385 ? -20.88400 4.69700   31.05800  1.000 62.30000  ? 416 ASN D CA  1 
ATOM   13866 C  C   . ASN D  1 385 ? -19.66900 5.58500   30.85200  1.000 61.71000  ? 416 ASN D C   1 
ATOM   13867 O  O   . ASN D  1 385 ? -19.22700 6.27100   31.77800  1.000 61.98000  ? 416 ASN D O   1 
ATOM   13868 C  CB  . ASN D  1 385 ? -22.15600 5.54800   30.97700  1.000 66.96000  ? 416 ASN D CB  1 
ATOM   13869 C  CG  . ASN D  1 385 ? -23.40700 4.74100   31.22800  1.000 73.23000  ? 416 ASN D CG  1 
ATOM   13870 O  OD1 . ASN D  1 385 ? -23.57200 3.63800   30.68500  1.000 66.98000  ? 416 ASN D OD1 1 
ATOM   13871 N  ND2 . ASN D  1 385 ? -24.31300 5.29000   32.04100  1.000 70.71000  ? 416 ASN D ND2 1 
ATOM   13872 N  N   . ASP D  1 386 ? -19.14400 5.56800   29.62800  1.000 56.62000  ? 417 ASP D N   1 
ATOM   13873 C  CA  . ASP D  1 386 ? -18.16800 6.55100   29.18100  1.000 59.11000  ? 417 ASP D CA  1 
ATOM   13874 C  C   . ASP D  1 386 ? -18.91900 7.72700   28.59000  1.000 57.59000  ? 417 ASP D C   1 
ATOM   13875 O  O   . ASP D  1 386 ? -19.90700 7.54400   27.87800  1.000 59.08000  ? 417 ASP D O   1 
ATOM   13876 C  CB  . ASP D  1 386 ? -17.21600 5.96800   28.13400  1.000 57.63000  ? 417 ASP D CB  1 
ATOM   13877 C  CG  . ASP D  1 386 ? -16.22900 4.97200   28.72400  1.000 61.17000  ? 417 ASP D CG  1 
ATOM   13878 O  OD1 . ASP D  1 386 ? -15.89900 5.08900   29.93100  1.000 57.57000  ? 417 ASP D OD1 1 
ATOM   13879 O  OD2 . ASP D  1 386 ? -15.78800 4.06500   27.97100  1.000 61.21000  ? 417 ASP D OD2 1 
ATOM   13880 N  N   . VAL D  1 387 ? -18.46900 8.93500   28.90900  1.000 64.68000  ? 418 VAL D N   1 
ATOM   13881 C  CA  . VAL D  1 387 ? -19.17300 10.14600  28.50700  1.000 58.07000  ? 418 VAL D CA  1 
ATOM   13882 C  C   . VAL D  1 387 ? -18.18600 11.13000  27.90800  1.000 60.22000  ? 418 VAL D C   1 
ATOM   13883 O  O   . VAL D  1 387 ? -17.01400 11.18000  28.29400  1.000 61.71000  ? 418 VAL D O   1 
ATOM   13884 C  CB  . VAL D  1 387 ? -19.92800 10.79100  29.69000  1.000 59.45000  ? 418 VAL D CB  1 
ATOM   13885 C  CG1 . VAL D  1 387 ? -20.71000 12.00500  29.23000  1.000 59.33000  ? 418 VAL D CG1 1 
ATOM   13886 C  CG2 . VAL D  1 387 ? -20.85400 9.77500   30.36200  1.000 55.40000  ? 418 VAL D CG2 1 
ATOM   13887 N  N   . GLY D  1 388 ? -18.67200 11.91300  26.95500  1.000 56.56000  ? 419 GLY D N   1 
ATOM   13888 C  CA  . GLY D  1 388 ? -17.94300 13.05500  26.46500  1.000 61.28000  ? 419 GLY D CA  1 
ATOM   13889 C  C   . GLY D  1 388 ? -18.91000 14.15500  26.10000  1.000 67.68000  ? 419 GLY D C   1 
ATOM   13890 O  O   . GLY D  1 388 ? -19.95400 13.88900  25.49300  1.000 69.99000  ? 419 GLY D O   1 
ATOM   13891 N  N   . ALA D  1 389 ? -18.56300 15.39700  26.43600  1.000 69.51000  ? 420 ALA D N   1 
ATOM   13892 C  CA  . ALA D  1 389 ? -19.42100 16.54800  26.17300  1.000 69.36000  ? 420 ALA D CA  1 
ATOM   13893 C  C   . ALA D  1 389 ? -18.54700 17.77600  25.97400  1.000 71.12000  ? 420 ALA D C   1 
ATOM   13894 O  O   . ALA D  1 389 ? -17.71200 18.09700  26.82600  1.000 67.58000  ? 420 ALA D O   1 
ATOM   13895 C  CB  . ALA D  1 389 ? -20.41800 16.78800  27.31400  1.000 58.82000  ? 420 ALA D CB  1 
ATOM   13896 N  N   . ARG D  1 390 ? -18.75300 18.45700  24.85400  1.000 69.42000  ? 421 ARG D N   1 
ATOM   13897 C  CA  . ARG D  1 390 ? -17.97200 19.62100  24.48400  1.000 64.75000  ? 421 ARG D CA  1 
ATOM   13898 C  C   . ARG D  1 390 ? -18.89000 20.82100  24.32000  1.000 71.83000  ? 421 ARG D C   1 
ATOM   13899 O  O   . ARG D  1 390 ? -20.02000 20.69400  23.83700  1.000 73.49000  ? 421 ARG D O   1 
ATOM   13900 C  CB  . ARG D  1 390 ? -17.19800 19.37900  23.19300  1.000 54.93000  ? 421 ARG D CB  1 
ATOM   13901 C  CG  . ARG D  1 390 ? -16.33600 20.53700  22.80400  1.000 59.11000  ? 421 ARG D CG  1 
ATOM   13902 C  CD  . ARG D  1 390 ? -15.74800 20.39800  21.43200  1.000 52.57000  ? 421 ARG D CD  1 
ATOM   13903 N  NE  . ARG D  1 390 ? -15.11300 21.64600  21.02800  1.000 62.48000  ? 421 ARG D NE  1 
ATOM   13904 C  CZ  . ARG D  1 390 ? -14.16900 21.75300  20.10400  1.000 60.54000  ? 421 ARG D CZ  1 
ATOM   13905 N  NH1 . ARG D  1 390 ? -13.70500 20.69200  19.46500  1.000 61.21000  ? 421 ARG D NH1 1 
ATOM   13906 N  NH2 . ARG D  1 390 ? -13.68600 22.95700  19.80600  1.000 58.22000  ? 421 ARG D NH2 1 
ATOM   13907 N  N   . MET D  1 391 ? -18.42800 21.97200  24.79500  1.000 72.09000  ? 422 MET D N   1 
ATOM   13908 C  CA  . MET D  1 391 ? -19.06900 23.25100  24.51700  1.000 72.44000  ? 422 MET D CA  1 
ATOM   13909 C  C   . MET D  1 391 ? -17.94300 24.24100  24.26800  1.000 72.43000  ? 422 MET D C   1 
ATOM   13910 O  O   . MET D  1 391 ? -17.15800 24.51500  25.18400  1.000 73.66000  ? 422 MET D O   1 
ATOM   13911 C  CB  . MET D  1 391 ? -19.95700 23.70000  25.67500  1.000 72.46000  ? 422 MET D CB  1 
ATOM   13912 C  CG  . MET D  1 391 ? -20.83600 24.89500  25.32800  1.000 78.44000  ? 422 MET D CG  1 
ATOM   13913 S  SD  . MET D  1 391 ? -21.87600 25.50900  26.67300  1.000 80.31000  ? 422 MET D SD  1 
ATOM   13914 C  CE  . MET D  1 391 ? -22.06000 24.06800  27.71500  1.000 84.82000  ? 422 MET D CE  1 
ATOM   13915 N  N   . GLY D  1 392 ? -17.84900 24.76600  23.04200  1.000 66.86000  ? 423 GLY D N   1 
ATOM   13916 C  CA  . GLY D  1 392 ? -16.81400 25.73800  22.71500  1.000 61.37000  ? 423 GLY D CA  1 
ATOM   13917 C  C   . GLY D  1 392 ? -15.40400 25.18100  22.73900  1.000 72.81000  ? 423 GLY D C   1 
ATOM   13918 O  O   . GLY D  1 392 ? -15.08200 24.30000  21.93700  1.000 78.02000  ? 423 GLY D O   1 
ATOM   13919 N  N   . ASP D  1 393 ? -14.54100 25.71400  23.61000  1.000 72.68000  ? 424 ASP D N   1 
ATOM   13920 C  CA  . ASP D  1 393 ? -13.17800 25.21600  23.79200  1.000 72.10000  ? 424 ASP D CA  1 
ATOM   13921 C  C   . ASP D  1 393 ? -13.07400 24.18100  24.89400  1.000 67.33000  ? 424 ASP D C   1 
ATOM   13922 O  O   . ASP D  1 393 ? -11.99200 23.64200  25.11600  1.000 70.69000  ? 424 ASP D O   1 
ATOM   13923 C  CB  . ASP D  1 393 ? -12.21800 26.35700  24.14100  1.000 74.64000  ? 424 ASP D CB  1 
ATOM   13924 C  CG  . ASP D  1 393 ? -12.09400 27.38100  23.04300  1.000 73.45000  ? 424 ASP D CG  1 
ATOM   13925 O  OD1 . ASP D  1 393 ? -12.03800 26.98400  21.85900  1.000 70.70000  ? 424 ASP D OD1 1 
ATOM   13926 O  OD2 . ASP D  1 393 ? -12.06600 28.58500  23.37200  1.000 72.13000  ? 424 ASP D OD2 1 
ATOM   13927 N  N   . TRP D  1 394 ? -14.16000 23.88800  25.58500  1.000 70.80000  ? 425 TRP D N   1 
ATOM   13928 C  CA  . TRP D  1 394 ? -14.11400 23.07100  26.78300  1.000 71.91000  ? 425 TRP D CA  1 
ATOM   13929 C  C   . TRP D  1 394 ? -14.78400 21.72700  26.53600  1.000 78.22000  ? 425 TRP D C   1 
ATOM   13930 O  O   . TRP D  1 394 ? -15.86900 21.65800  25.94900  1.000 74.13000  ? 425 TRP D O   1 
ATOM   13931 C  CB  . TRP D  1 394 ? -14.79800 23.78700  27.94600  1.000 77.79000  ? 425 TRP D CB  1 
ATOM   13932 C  CG  . TRP D  1 394 ? -14.11000 25.05900  28.31200  1.000 84.72000  ? 425 TRP D CG  1 
ATOM   13933 C  CD1 . TRP D  1 394 ? -14.41600 26.32200  27.88200  1.000 87.16000  ? 425 TRP D CD1 1 
ATOM   13934 C  CD2 . TRP D  1 394 ? -12.96200 25.18600  29.14400  1.000 78.85000  ? 425 TRP D CD2 1 
ATOM   13935 N  NE1 . TRP D  1 394 ? -13.53800 27.22900  28.42100  1.000 84.82000  ? 425 TRP D NE1 1 
ATOM   13936 C  CE2 . TRP D  1 394 ? -12.63300 26.55300  29.19600  1.000 84.03000  ? 425 TRP D CE2 1 
ATOM   13937 C  CE3 . TRP D  1 394 ? -12.17900 24.27200  29.85600  1.000 81.18000  ? 425 TRP D CE3 1 
ATOM   13938 C  CZ2 . TRP D  1 394 ? -11.55800 27.02800  29.93100  1.000 86.02000  ? 425 TRP D CZ2 1 
ATOM   13939 C  CZ3 . TRP D  1 394 ? -11.11700 24.74300  30.58600  1.000 78.02000  ? 425 TRP D CZ3 1 
ATOM   13940 C  CH2 . TRP D  1 394 ? -10.81600 26.10900  30.62000  1.000 86.62000  ? 425 TRP D CH2 1 
ATOM   13941 N  N   . LYS D  1 395 ? -14.15000 20.66700  27.02500  1.000 74.58000  ? 426 LYS D N   1 
ATOM   13942 C  CA  . LYS D  1 395 ? -14.67900 19.32400  26.89300  1.000 69.53000  ? 426 LYS D CA  1 
ATOM   13943 C  C   . LYS D  1 395 ? -14.54600 18.62300  28.23300  1.000 67.52000  ? 426 LYS D C   1 
ATOM   13944 O  O   . LYS D  1 395 ? -13.52400 18.75200  28.91000  1.000 67.85000  ? 426 LYS D O   1 
ATOM   13945 C  CB  . LYS D  1 395 ? -13.94200 18.57800  25.76400  1.000 71.31000  ? 426 LYS D CB  1 
ATOM   13946 C  CG  . LYS D  1 395 ? -13.42400 17.19600  26.10400  1.000 73.81000  ? 426 LYS D CG  1 
ATOM   13947 C  CD  . LYS D  1 395 ? -14.50000 16.14200  25.95300  1.000 69.17000  ? 426 LYS D CD  1 
ATOM   13948 C  CE  . LYS D  1 395 ? -14.00300 14.95700  25.13100  1.000 61.74000  ? 426 LYS D CE  1 
ATOM   13949 N  NZ  . LYS D  1 395 ? -14.93800 13.83600  25.30900  1.000 61.71000  ? 426 LYS D NZ  1 
ATOM   13950 N  N   . ILE D  1 396 ? -15.59100 17.89900  28.62000  1.000 62.11000  ? 427 ILE D N   1 
ATOM   13951 C  CA  . ILE D  1 396 ? -15.56900 17.04700  29.80300  1.000 69.52000  ? 427 ILE D CA  1 
ATOM   13952 C  C   . ILE D  1 396 ? -15.58100 15.58300  29.38700  1.000 69.62000  ? 427 ILE D C   1 
ATOM   13953 O  O   . ILE D  1 396 ? -16.16000 15.21100  28.36000  1.000 66.03000  ? 427 ILE D O   1 
ATOM   13954 C  CB  . ILE D  1 396 ? -16.74800 17.37300  30.73600  1.000 70.98000  ? 427 ILE D CB  1 
ATOM   13955 C  CG1 . ILE D  1 396 ? -18.05600 17.38500  29.94100  1.000 64.99000  ? 427 ILE D CG1 1 
ATOM   13956 C  CG2 . ILE D  1 396 ? -16.50900 18.69700  31.43000  1.000 75.28000  ? 427 ILE D CG2 1 
ATOM   13957 C  CD1 . ILE D  1 396 ? -19.28100 17.45900  30.79600  1.000 67.62000  ? 427 ILE D CD1 1 
ATOM   13958 N  N   . THR D  1 397 ? -14.94500 14.74500  30.20600  1.000 66.34000  ? 428 THR D N   1 
ATOM   13959 C  CA  . THR D  1 397 ? -14.76500 13.34300  29.86100  1.000 60.31000  ? 428 THR D CA  1 
ATOM   13960 C  C   . THR D  1 397 ? -14.84500 12.49000  31.11600  1.000 61.18000  ? 428 THR D C   1 
ATOM   13961 O  O   . THR D  1 397 ? -14.23000 12.82600  32.13000  1.000 65.80000  ? 428 THR D O   1 
ATOM   13962 C  CB  . THR D  1 397 ? -13.41400 13.13100  29.17500  1.000 58.59000  ? 428 THR D CB  1 
ATOM   13963 O  OG1 . THR D  1 397 ? -13.25400 14.08400  28.11900  1.000 60.58000  ? 428 THR D OG1 1 
ATOM   13964 C  CG2 . THR D  1 397 ? -13.34200 11.74400  28.58800  1.000 57.31000  ? 428 THR D CG2 1 
ATOM   13965 N  N   . ARG D  1 398 ? -15.58500 11.39000  31.05800  1.000 60.90000  ? 429 ARG D N   1 
ATOM   13966 C  CA  . ARG D  1 398 ? -15.43800 10.32900  32.04800  1.000 59.42000  ? 429 ARG D CA  1 
ATOM   13967 C  C   . ARG D  1 398 ? -15.15200 9.03200   31.29600  1.000 59.38000  ? 429 ARG D C   1 
ATOM   13968 O  O   . ARG D  1 398 ? -15.98700 8.56400   30.51600  1.000 56.69000  ? 429 ARG D O   1 
ATOM   13969 C  CB  . ARG D  1 398 ? -16.68300 10.20800  32.94400  1.000 53.82000  ? 429 ARG D CB  1 
ATOM   13970 C  CG  . ARG D  1 398 ? -16.36100 9.54200   34.27200  1.000 61.70000  ? 429 ARG D CG  1 
ATOM   13971 C  CD  . ARG D  1 398 ? -17.52200 9.29100   35.23300  1.000 55.84000  ? 429 ARG D CD  1 
ATOM   13972 N  NE  . ARG D  1 398 ? -17.02900 8.51700   36.37700  1.000 64.78000  ? 429 ARG D NE  1 
ATOM   13973 C  CZ  . ARG D  1 398 ? -17.77200 8.03900   37.37100  1.000 64.36000  ? 429 ARG D CZ  1 
ATOM   13974 N  NH1 . ARG D  1 398 ? -19.07700 8.24600   37.43100  1.000 65.56000  ? 429 ARG D NH1 1 
ATOM   13975 N  NH2 . ARG D  1 398 ? -17.19300 7.31500   38.31900  1.000 62.31000  ? 429 ARG D NH2 1 
ATOM   13976 N  N   . MET D  1 399 ? -13.98700 8.43500   31.55700  1.000 62.15000  ? 430 MET D N   1 
ATOM   13977 C  CA  . MET D  1 399 ? -13.55200 7.20900   30.89600  1.000 57.18000  ? 430 MET D CA  1 
ATOM   13978 C  C   . MET D  1 399 ? -13.26300 6.13700   31.93000  1.000 57.70000  ? 430 MET D C   1 
ATOM   13979 O  O   . MET D  1 399 ? -12.75000 6.42700   33.01300  1.000 60.86000  ? 430 MET D O   1 
ATOM   13980 C  CB  . MET D  1 399 ? -12.29600 7.42900   30.04600  1.000 60.31000  ? 430 MET D CB  1 
ATOM   13981 C  CG  . MET D  1 399 ? -12.57300 7.89600   28.63900  1.000 58.24000  ? 430 MET D CG  1 
ATOM   13982 S  SD  . MET D  1 399 ? -13.51900 6.65600   27.71100  1.000 59.62000  ? 430 MET D SD  1 
ATOM   13983 C  CE  . MET D  1 399 ? -12.25200 5.41200   27.45300  1.000 54.00000  ? 430 MET D CE  1 
ATOM   13984 N  N   . GLY D  1 400 ? -13.65500 4.90600   31.61600  1.000 56.58000  ? 431 GLY D N   1 
ATOM   13985 C  CA  . GLY D  1 400 ? -13.34600 3.78500   32.48600  1.000 52.79000  ? 431 GLY D CA  1 
ATOM   13986 C  C   . GLY D  1 400 ? -13.90400 3.91900   33.87500  1.000 58.95000  ? 431 GLY D C   1 
ATOM   13987 O  O   . GLY D  1 400 ? -13.49200 3.17600   34.77100  1.000 55.18000  ? 431 GLY D O   1 
ATOM   13988 N  N   . ASN D  1 401 ? -14.86400 4.83400   34.06300  1.000 62.41000  ? 432 ASN D N   1 
ATOM   13989 C  CA  . ASN D  1 401 ? -15.47400 5.17600   35.34400  1.000 61.03000  ? 432 ASN D CA  1 
ATOM   13990 C  C   . ASN D  1 401 ? -14.51000 5.85500   36.31300  1.000 64.87000  ? 432 ASN D C   1 
ATOM   13991 O  O   . ASN D  1 401 ? -14.81600 5.98300   37.50300  1.000 63.15000  ? 432 ASN D O   1 
ATOM   13992 C  CB  . ASN D  1 401 ? -16.08900 3.94700   36.01400  1.000 60.82000  ? 432 ASN D CB  1 
ATOM   13993 C  CG  . ASN D  1 401 ? -17.42400 4.24600   36.62800  1.000 60.28000  ? 432 ASN D CG  1 
ATOM   13994 O  OD1 . ASN D  1 401 ? -18.13400 5.14600   36.17400  1.000 57.39000  ? 432 ASN D OD1 1 
ATOM   13995 N  ND2 . ASN D  1 401 ? -17.76000 3.52500   37.69100  1.000 55.35000  ? 432 ASN D ND2 1 
ATOM   13996 N  N   . GLU D  1 402 ? -13.37100 6.33500   35.81800  1.000 65.21000  ? 433 GLU D N   1 
ATOM   13997 C  CA  . GLU D  1 402 ? -12.42900 7.09600   36.60900  1.000 62.67000  ? 433 GLU D CA  1 
ATOM   13998 C  C   . GLU D  1 402 ? -13.02600 8.47200   36.92200  1.000 67.76000  ? 433 GLU D C   1 
ATOM   13999 O  O   . GLU D  1 402 ? -14.09400 8.82600   36.40600  1.000 69.60000  ? 433 GLU D O   1 
ATOM   14000 C  CB  . GLU D  1 402 ? -11.10100 7.18000   35.85200  1.000 57.92000  ? 433 GLU D CB  1 
ATOM   14001 C  CG  . GLU D  1 402 ? -10.25900 5.90100   35.95300  1.000 55.34000  ? 433 GLU D CG  1 
ATOM   14002 C  CD  . GLU D  1 402 ? -9.59900  5.70300   37.32600  1.000 69.72000  ? 433 GLU D CD  1 
ATOM   14003 O  OE1 . GLU D  1 402 ? -8.70700  6.51200   37.66700  1.000 77.48000  ? 433 GLU D OE1 1 
ATOM   14004 O  OE2 . GLU D  1 402 ? -9.97300  4.76700   38.07100  1.000 65.58000  ? 433 GLU D OE2 1 
ATOM   14005 N  N   . PRO D  1 403 ? -12.37100 9.26500   37.78500  1.000 69.48000  ? 434 PRO D N   1 
ATOM   14006 C  CA  . PRO D  1 403 ? -12.85600 10.62800  38.05400  1.000 64.14000  ? 434 PRO D CA  1 
ATOM   14007 C  C   . PRO D  1 403 ? -13.02500 11.46600  36.79300  1.000 65.29000  ? 434 PRO D C   1 
ATOM   14008 O  O   . PRO D  1 403 ? -12.31600 11.29600  35.79600  1.000 59.32000  ? 434 PRO D O   1 
ATOM   14009 C  CB  . PRO D  1 403 ? -11.77900 11.21400  38.97500  1.000 63.48000  ? 434 PRO D CB  1 
ATOM   14010 C  CG  . PRO D  1 403 ? -11.17800 10.02700  39.66100  1.000 66.44000  ? 434 PRO D CG  1 
ATOM   14011 C  CD  . PRO D  1 403 ? -11.34800 8.83700   38.76700  1.000 68.61000  ? 434 PRO D CD  1 
ATOM   14012 N  N   . TRP D  1 404 ? -13.98700 12.38500  36.86300  1.000 60.25000  ? 435 TRP D N   1 
ATOM   14013 C  CA  . TRP D  1 404 ? -14.27700 13.27400  35.74800  1.000 63.83000  ? 435 TRP D CA  1 
ATOM   14014 C  C   . TRP D  1 404 ? -13.08000 14.15000  35.40200  1.000 65.06000  ? 435 TRP D C   1 
ATOM   14015 O  O   . TRP D  1 404 ? -12.34300 14.61500  36.27900  1.000 67.03000  ? 435 TRP D O   1 
ATOM   14016 C  CB  . TRP D  1 404 ? -15.49700 14.14800  36.06700  1.000 64.37000  ? 435 TRP D CB  1 
ATOM   14017 C  CG  . TRP D  1 404 ? -16.80400 13.47100  35.82100  1.000 66.48000  ? 435 TRP D CG  1 
ATOM   14018 C  CD1 . TRP D  1 404 ? -17.54400 12.74200  36.71500  1.000 66.79000  ? 435 TRP D CD1 1 
ATOM   14019 C  CD2 . TRP D  1 404 ? -17.52900 13.45100  34.58900  1.000 66.93000  ? 435 TRP D CD2 1 
ATOM   14020 N  NE1 . TRP D  1 404 ? -18.68000 12.26700  36.11000  1.000 67.69000  ? 435 TRP D NE1 1 
ATOM   14021 C  CE2 . TRP D  1 404 ? -18.69900 12.69000  34.80600  1.000 67.20000  ? 435 TRP D CE2 1 
ATOM   14022 C  CE3 . TRP D  1 404 ? -17.30000 13.99900  33.32100  1.000 63.39000  ? 435 TRP D CE3 1 
ATOM   14023 C  CZ2 . TRP D  1 404 ? -19.64000 12.46900  33.80700  1.000 63.24000  ? 435 TRP D CZ2 1 
ATOM   14024 C  CZ3 . TRP D  1 404 ? -18.23700 13.78200  32.32800  1.000 66.98000  ? 435 TRP D CZ3 1 
ATOM   14025 C  CH2 . TRP D  1 404 ? -19.39300 13.02100  32.57600  1.000 64.11000  ? 435 TRP D CH2 1 
ATOM   14026 N  N   . ARG D  1 405 ? -12.92400 14.40400  34.10900  1.000 65.48000  ? 436 ARG D N   1 
ATOM   14027 C  CA  . ARG D  1 405 ? -11.86300 15.23600  33.56900  1.000 64.72000  ? 436 ARG D CA  1 
ATOM   14028 C  C   . ARG D  1 405 ? -12.47700 16.40200  32.81700  1.000 65.85000  ? 436 ARG D C   1 
ATOM   14029 O  O   . ARG D  1 405 ? -13.54900 16.26600  32.22400  1.000 71.02000  ? 436 ARG D O   1 
ATOM   14030 C  CB  . ARG D  1 405 ? -10.99200 14.43100  32.62600  1.000 62.06000  ? 436 ARG D CB  1 
ATOM   14031 C  CG  . ARG D  1 405 ? -10.55300 13.14800  33.25400  1.000 68.55000  ? 436 ARG D CG  1 
ATOM   14032 C  CD  . ARG D  1 405 ? -9.89900  12.25100  32.24600  1.000 71.76000  ? 436 ARG D CD  1 
ATOM   14033 N  NE  . ARG D  1 405 ? -8.72000  12.88900  31.68000  1.000 62.36000  ? 436 ARG D NE  1 
ATOM   14034 C  CZ  . ARG D  1 405 ? -7.52700  12.84300  32.25100  1.000 64.38000  ? 436 ARG D CZ  1 
ATOM   14035 N  NH1 . ARG D  1 405 ? -7.35800  12.29400  33.44400  1.000 57.91000  ? 436 ARG D NH1 1 
ATOM   14036 N  NH2 . ARG D  1 405 ? -6.48500  13.37400  31.62000  1.000 63.36000  ? 436 ARG D NH2 1 
ATOM   14037 N  N   . LEU D  1 406 ? -11.83100 17.56000  32.89200  1.000 67.44000  ? 437 LEU D N   1 
ATOM   14038 C  CA  . LEU D  1 406 ? -12.20800 18.71900  32.09800  1.000 69.12000  ? 437 LEU D CA  1 
ATOM   14039 C  C   . LEU D  1 406 ? -10.96300 19.19600  31.37300  1.000 65.30000  ? 437 LEU D C   1 
ATOM   14040 O  O   . LEU D  1 406 ? -9.91200  19.37000  31.99500  1.000 66.32000  ? 437 LEU D O   1 
ATOM   14041 C  CB  . LEU D  1 406 ? -12.82100 19.83000  32.96300  1.000 72.04000  ? 437 LEU D CB  1 
ATOM   14042 C  CG  . LEU D  1 406 ? -13.12300 21.15000  32.24600  1.000 73.04000  ? 437 LEU D CG  1 
ATOM   14043 C  CD1 . LEU D  1 406 ? -14.55500 21.56200  32.49200  1.000 73.57000  ? 437 LEU D CD1 1 
ATOM   14044 C  CD2 . LEU D  1 406 ? -12.16900 22.23300  32.71300  1.000 73.74000  ? 437 LEU D CD2 1 
ATOM   14045 N  N   . HIS D  1 407 ? -11.06100 19.35900  30.06500  1.000 59.78000  ? 438 HIS D N   1 
ATOM   14046 C  CA  . HIS D  1 407 ? -9.93300  19.79000  29.26400  1.000 61.17000  ? 438 HIS D CA  1 
ATOM   14047 C  C   . HIS D  1 407 ? -10.33500 21.00400  28.44900  1.000 66.87000  ? 438 HIS D C   1 
ATOM   14048 O  O   . HIS D  1 407 ? -11.50000 21.17000  28.07500  1.000 72.92000  ? 438 HIS D O   1 
ATOM   14049 C  CB  . HIS D  1 407 ? -9.43300  18.67400  28.33300  1.000 64.00000  ? 438 HIS D CB  1 
ATOM   14050 C  CG  . HIS D  1 407 ? -9.05700  17.42200  29.06000  1.000 67.59000  ? 438 HIS D CG  1 
ATOM   14051 N  ND1 . HIS D  1 407 ? -7.87100  17.29000  29.75500  1.000 63.60000  ? 438 HIS D ND1 1 
ATOM   14052 C  CD2 . HIS D  1 407 ? -9.72800  16.25700  29.23800  1.000 67.75000  ? 438 HIS D CD2 1 
ATOM   14053 C  CE1 . HIS D  1 407 ? -7.82400  16.09500  30.32000  1.000 64.62000  ? 438 HIS D CE1 1 
ATOM   14054 N  NE2 . HIS D  1 407 ? -8.93600  15.44700  30.01900  1.000 72.04000  ? 438 HIS D NE2 1 
ATOM   14055 N  N   . ASN D  1 408 ? -9.36200  21.87300  28.22400  1.000 67.43000  ? 439 ASN D N   1 
ATOM   14056 C  CA  . ASN D  1 408 ? -9.44800  22.89400  27.19300  1.000 69.52000  ? 439 ASN D CA  1 
ATOM   14057 C  C   . ASN D  1 408 ? -8.95300  22.22200  25.92600  1.000 70.48000  ? 439 ASN D C   1 
ATOM   14058 O  O   . ASN D  1 408 ? -7.74300  22.11400  25.70100  1.000 68.10000  ? 439 ASN D O   1 
ATOM   14059 C  CB  . ASN D  1 408 ? -8.61500  24.11700  27.55100  1.000 74.40000  ? 439 ASN D CB  1 
ATOM   14060 C  CG  . ASN D  1 408 ? -8.77700  25.23800  26.55100  1.000 73.25000  ? 439 ASN D CG  1 
ATOM   14061 O  OD1 . ASN D  1 408 ? -8.47500  25.07900  25.36400  1.000 71.30000  ? 439 ASN D OD1 1 
ATOM   14062 N  ND2 . ASN D  1 408 ? -9.25200  26.38200  27.02400  1.000 69.65000  ? 439 ASN D ND2 1 
ATOM   14063 N  N   . ILE D  1 409 ? -9.89800  21.72600  25.11800  1.000 68.32000  ? 440 ILE D N   1 
ATOM   14064 C  CA  . ILE D  1 409 ? -9.55600  20.88800  23.97300  1.000 64.28000  ? 440 ILE D CA  1 
ATOM   14065 C  C   . ILE D  1 409 ? -8.84300  21.67500  22.88900  1.000 60.53000  ? 440 ILE D C   1 
ATOM   14066 O  O   . ILE D  1 409 ? -8.13400  21.09200  22.06500  1.000 63.22000  ? 440 ILE D O   1 
ATOM   14067 C  CB  . ILE D  1 409 ? -10.82800 20.19100  23.44100  1.000 70.88000  ? 440 ILE D CB  1 
ATOM   14068 C  CG1 . ILE D  1 409 ? -10.44900 18.97500  22.58400  1.000 70.51000  ? 440 ILE D CG1 1 
ATOM   14069 C  CG2 . ILE D  1 409 ? -11.73000 21.18400  22.69100  1.000 65.78000  ? 440 ILE D CG2 1 
ATOM   14070 C  CD1 . ILE D  1 409 ? -9.71100  17.90000  23.36000  1.000 68.40000  ? 440 ILE D CD1 1 
ATOM   14071 N  N   . THR D  1 410 ? -9.00300  22.99100  22.87300  1.000 62.58000  ? 441 THR D N   1 
ATOM   14072 C  CA  . THR D  1 410 ? -8.27100  23.79300  21.91000  1.000 66.28000  ? 441 THR D CA  1 
ATOM   14073 C  C   . THR D  1 410 ? -6.80700  23.91800  22.32300  1.000 68.38000  ? 441 THR D C   1 
ATOM   14074 O  O   . THR D  1 410 ? -5.92200  24.00200  21.46000  1.000 66.74000  ? 441 THR D O   1 
ATOM   14075 C  CB  . THR D  1 410 ? -8.93400  25.16600  21.76600  1.000 74.12000  ? 441 THR D CB  1 
ATOM   14076 O  OG1 . THR D  1 410 ? -10.31400 25.00100  21.39200  1.000 69.51000  ? 441 THR D OG1 1 
ATOM   14077 C  CG2 . THR D  1 410 ? -8.22800  25.99200  20.68400  1.000 67.77000  ? 441 THR D CG2 1 
ATOM   14078 N  N   . GLN D  1 411 ? -6.54000  23.92900  23.63500  1.000 66.57000  ? 442 GLN D N   1 
ATOM   14079 C  CA  . GLN D  1 411 ? -5.17700  24.01300  24.15900  1.000 75.18000  ? 442 GLN D CA  1 
ATOM   14080 C  C   . GLN D  1 411 ? -4.55400  22.65800  24.44200  1.000 68.09000  ? 442 GLN D C   1 
ATOM   14081 O  O   . GLN D  1 411 ? -3.32700  22.53600  24.44300  1.000 62.63000  ? 442 GLN D O   1 
ATOM   14082 C  CB  . GLN D  1 411 ? -5.15200  24.80300  25.48100  1.000 74.81000  ? 442 GLN D CB  1 
ATOM   14083 C  CG  . GLN D  1 411 ? -5.52500  26.27000  25.38000  1.000 80.55000  ? 442 GLN D CG  1 
ATOM   14084 C  CD  . GLN D  1 411 ? -4.50100  27.06100  24.59900  1.000 85.57000  ? 442 GLN D CD  1 
ATOM   14085 O  OE1 . GLN D  1 411 ? -3.31600  26.71700  24.57500  1.000 90.74000  ? 442 GLN D OE1 1 
ATOM   14086 N  NE2 . GLN D  1 411 ? -4.95700  28.11600  23.93000  1.000 83.31000  ? 442 GLN D NE2 1 
ATOM   14087 N  N   . ASP D  1 412 ? -5.37100  21.64400  24.65900  1.000 71.39000  ? 443 ASP D N   1 
ATOM   14088 C  CA  . ASP D  1 412 ? -4.94200  20.34600  25.14400  1.000 64.83000  ? 443 ASP D CA  1 
ATOM   14089 C  C   . ASP D  1 412 ? -5.70400  19.29100  24.32800  1.000 65.96000  ? 443 ASP D C   1 
ATOM   14090 O  O   . ASP D  1 412 ? -6.58500  18.59000  24.83300  1.000 59.08000  ? 443 ASP D O   1 
ATOM   14091 C  CB  . ASP D  1 412 ? -5.19600  20.25000  26.65100  1.000 60.08000  ? 443 ASP D CB  1 
ATOM   14092 C  CG  . ASP D  1 412 ? -4.93700  18.88800  27.21100  1.000 64.42000  ? 443 ASP D CG  1 
ATOM   14093 O  OD1 . ASP D  1 412 ? -4.15400  18.11400  26.60700  1.000 61.95000  ? 443 ASP D OD1 1 
ATOM   14094 O  OD2 . ASP D  1 412 ? -5.54400  18.59800  28.26800  1.000 67.19000  ? 443 ASP D OD2 1 
ATOM   14095 N  N   . ILE D  1 413 ? -5.37900  19.20900  23.02900  1.000 61.59000  ? 444 ILE D N   1 
ATOM   14096 C  CA  . ILE D  1 413 ? -6.13500  18.34500  22.12900  1.000 61.54000  ? 444 ILE D CA  1 
ATOM   14097 C  C   . ILE D  1 413 ? -6.00400  16.88300  22.54100  1.000 65.42000  ? 444 ILE D C   1 
ATOM   14098 O  O   . ILE D  1 413 ? -6.92000  16.08500  22.31600  1.000 63.44000  ? 444 ILE D O   1 
ATOM   14099 C  CB  . ILE D  1 413 ? -5.68900  18.56900  20.67100  1.000 60.38000  ? 444 ILE D CB  1 
ATOM   14100 C  CG1 . ILE D  1 413 ? -6.67800  17.91200  19.71300  1.000 54.51000  ? 444 ILE D CG1 1 
ATOM   14101 C  CG2 . ILE D  1 413 ? -4.29400  18.02400  20.44300  1.000 59.39000  ? 444 ILE D CG2 1 
ATOM   14102 C  CD1 . ILE D  1 413 ? -6.54900  18.36400  18.28700  1.000 58.21000  ? 444 ILE D CD1 1 
ATOM   14103 N  N   . GLY D  1 414 ? -4.89600  16.51500  23.17500  1.000 59.45000  ? 445 GLY D N   1 
ATOM   14104 C  CA  . GLY D  1 414 ? -4.65300  15.17200  23.65500  1.000 55.74000  ? 445 GLY D CA  1 
ATOM   14105 C  C   . GLY D  1 414 ? -5.24000  14.82100  25.00200  1.000 61.60000  ? 445 GLY D C   1 
ATOM   14106 O  O   . GLY D  1 414 ? -4.98700  13.71600  25.48800  1.000 62.94000  ? 445 GLY D O   1 
ATOM   14107 N  N   . GLU D  1 415 ? -5.99200  15.72400  25.63200  1.000 60.42000  ? 446 GLU D N   1 
ATOM   14108 C  CA  . GLU D  1 415 ? -6.64400  15.46100  26.91700  1.000 62.86000  ? 446 GLU D CA  1 
ATOM   14109 C  C   . GLU D  1 415 ? -5.64100  14.96700  27.96100  1.000 62.62000  ? 446 GLU D C   1 
ATOM   14110 O  O   . GLU D  1 415 ? -5.87600  14.00500  28.69800  1.000 54.70000  ? 446 GLU D O   1 
ATOM   14111 C  CB  . GLU D  1 415 ? -7.82500  14.49400  26.74000  1.000 61.49000  ? 446 GLU D CB  1 
ATOM   14112 C  CG  . GLU D  1 415 ? -8.99900  15.13500  25.94300  1.000 67.09000  ? 446 GLU D CG  1 
ATOM   14113 C  CD  . GLU D  1 415 ? -10.07100 14.13700  25.47300  1.000 71.99000  ? 446 GLU D CD  1 
ATOM   14114 O  OE1 . GLU D  1 415 ? -9.84900  13.48000  24.42000  1.000 69.49000  ? 446 GLU D OE1 1 
ATOM   14115 O  OE2 . GLU D  1 415 ? -11.13200 14.01700  26.14400  1.000 65.50000  ? 446 GLU D OE2 1 
ATOM   14116 N  N   . LYS D  1 416 ? -4.53000  15.68900  28.05700  1.000 64.16000  ? 447 LYS D N   1 
ATOM   14117 C  CA  . LYS D  1 416 ? -3.45500  15.33000  28.97000  1.000 62.42000  ? 447 LYS D CA  1 
ATOM   14118 C  C   . LYS D  1 416 ? -3.57400  16.03600  30.31600  1.000 61.51000  ? 447 LYS D C   1 
ATOM   14119 O  O   . LYS D  1 416 ? -3.20400  15.45100  31.34400  1.000 64.38000  ? 447 LYS D O   1 
ATOM   14120 C  CB  . LYS D  1 416 ? -2.12000  15.66700  28.30300  1.000 61.92000  ? 447 LYS D CB  1 
ATOM   14121 C  CG  . LYS D  1 416 ? -1.82800  14.81600  27.05900  1.000 57.11000  ? 447 LYS D CG  1 
ATOM   14122 C  CD  . LYS D  1 416 ? -0.64100  15.35900  26.26900  1.000 61.21000  ? 447 LYS D CD  1 
ATOM   14123 C  CE  . LYS D  1 416 ? 0.62600   14.55700  26.45800  1.000 64.47000  ? 447 LYS D CE  1 
ATOM   14124 N  NZ  . LYS D  1 416 ? 0.79000   13.53900  25.39800  1.000 69.10000  ? 447 LYS D NZ  1 
ATOM   14125 N  N   . LYS D  1 417 ? -4.15700  17.24500  30.34100  1.000 65.76000  ? 448 LYS D N   1 
ATOM   14126 C  CA  . LYS D  1 417 ? -4.17300  18.13000  31.51300  1.000 60.74000  ? 448 LYS D CA  1 
ATOM   14127 C  C   . LYS D  1 417 ? -5.59500  18.29300  32.05100  1.000 63.22000  ? 448 LYS D C   1 
ATOM   14128 O  O   . LYS D  1 417 ? -6.40400  19.03700  31.48900  1.000 63.91000  ? 448 LYS D O   1 
ATOM   14129 C  CB  . LYS D  1 417 ? -3.57500  19.48400  31.13700  1.000 66.78000  ? 448 LYS D CB  1 
ATOM   14130 C  CG  . LYS D  1 417 ? -3.39100  20.46600  32.29500  1.000 73.66000  ? 448 LYS D CG  1 
ATOM   14131 C  CD  . LYS D  1 417 ? -3.51900  21.92700  31.81100  1.000 79.57000  ? 448 LYS D CD  1 
ATOM   14132 C  CE  . LYS D  1 417 ? -2.30700  22.78400  32.17200  1.000 77.70000  ? 448 LYS D CE  1 
ATOM   14133 N  NZ  . LYS D  1 417 ? -1.15800  22.54900  31.24600  1.000 69.43000  ? 448 LYS D NZ  1 
ATOM   14134 N  N   . ASN D  1 418 ? -5.89900  17.61400  33.15400  1.000 61.51000  ? 449 ASN D N   1 
ATOM   14135 C  CA  . ASN D  1 418 ? -7.21400  17.72000  33.77900  1.000 60.81000  ? 449 ASN D CA  1 
ATOM   14136 C  C   . ASN D  1 418 ? -7.33000  19.03900  34.53400  1.000 68.83000  ? 449 ASN D C   1 
ATOM   14137 O  O   . ASN D  1 418 ? -6.64200  19.24700  35.54100  1.000 69.59000  ? 449 ASN D O   1 
ATOM   14138 C  CB  . ASN D  1 418 ? -7.44600  16.55000  34.73400  1.000 57.95000  ? 449 ASN D CB  1 
ATOM   14139 C  CG  . ASN D  1 418 ? -8.86100  16.50200  35.27400  1.000 64.56000  ? 449 ASN D CG  1 
ATOM   14140 O  OD1 . ASN D  1 418 ? -9.17900  15.71000  36.16300  1.000 65.09000  ? 449 ASN D OD1 1 
ATOM   14141 N  ND2 . ASN D  1 418 ? -9.72100  17.34600  34.73800  1.000 68.74000  ? 449 ASN D ND2 1 
ATOM   14142 N  N   . LEU D  1 419 ? -8.26200  19.88900  34.11000  1.000 69.48000  ? 450 LEU D N   1 
ATOM   14143 C  CA  . LEU D  1 419 ? -8.49700  21.16500  34.76600  1.000 62.69000  ? 450 LEU D CA  1 
ATOM   14144 C  C   . LEU D  1 419 ? -9.70000  21.12100  35.69300  1.000 64.36000  ? 450 LEU D C   1 
ATOM   14145 O  O   . LEU D  1 419 ? -10.17800 22.17000  36.13200  1.000 65.86000  ? 450 LEU D O   1 
ATOM   14146 C  CB  . LEU D  1 419 ? -8.64600  22.27100  33.72600  1.000 60.20000  ? 450 LEU D CB  1 
ATOM   14147 C  CG  . LEU D  1 419 ? -7.37000  22.39600  32.90800  1.000 62.02000  ? 450 LEU D CG  1 
ATOM   14148 C  CD1 . LEU D  1 419 ? -7.51200  23.42500  31.82700  1.000 60.80000  ? 450 LEU D CD1 1 
ATOM   14149 C  CD2 . LEU D  1 419 ? -6.26600  22.79700  33.85600  1.000 64.86000  ? 450 LEU D CD2 1 
ATOM   14150 N  N   . ALA D  1 420 ? -10.18300 19.92300  36.02100  1.000 63.29000  ? 451 ALA D N   1 
ATOM   14151 C  CA  . ALA D  1 420 ? -11.31300 19.81400  36.93400  1.000 71.88000  ? 451 ALA D CA  1 
ATOM   14152 C  C   . ALA D  1 420 ? -11.01300 20.50800  38.25700  1.000 75.55000  ? 451 ALA D C   1 
ATOM   14153 O  O   . ALA D  1 420 ? -11.92100 21.07600  38.87900  1.000 71.32000  ? 451 ALA D O   1 
ATOM   14154 C  CB  . ALA D  1 420 ? -11.67200 18.34600  37.17400  1.000 68.95000  ? 451 ALA D CB  1 
ATOM   14155 N  N   . GLY D  1 421 ? -9.75100  20.46200  38.70500  1.000 75.00000  ? 452 GLY D N   1 
ATOM   14156 C  CA  . GLY D  1 421 ? -9.38900  21.13500  39.94300  1.000 66.47000  ? 452 GLY D CA  1 
ATOM   14157 C  C   . GLY D  1 421 ? -9.34000  22.64600  39.80600  1.000 68.14000  ? 452 GLY D C   1 
ATOM   14158 O  O   . GLY D  1 421 ? -9.77500  23.37100  40.70500  1.000 73.52000  ? 452 GLY D O   1 
ATOM   14159 N  N   . ARG D  1 422 ? -8.85600  23.14200  38.66100  1.000 72.03000  ? 453 ARG D N   1 
ATOM   14160 C  CA  . ARG D  1 422 ? -8.68600  24.58300  38.49400  1.000 70.90000  ? 453 ARG D CA  1 
ATOM   14161 C  C   . ARG D  1 422 ? -10.02300 25.30500  38.32000  1.000 76.38000  ? 453 ARG D C   1 
ATOM   14162 O  O   . ARG D  1 422 ? -10.16600 26.45200  38.75700  1.000 75.26000  ? 453 ARG D O   1 
ATOM   14163 C  CB  . ARG D  1 422 ? -7.77300  24.89000  37.30300  1.000 70.54000  ? 453 ARG D CB  1 
ATOM   14164 C  CG  . ARG D  1 422 ? -7.34000  26.36700  37.26600  1.000 80.71000  ? 453 ARG D CG  1 
ATOM   14165 C  CD  . ARG D  1 422 ? -6.30400  26.71700  36.18500  1.000 87.20000  ? 453 ARG D CD  1 
ATOM   14166 N  NE  . ARG D  1 422 ? -5.11700  25.86400  36.16600  1.000 94.81000  ? 453 ARG D NE  1 
ATOM   14167 C  CZ  . ARG D  1 422 ? -4.25000  25.81500  35.16000  1.000 91.02000  ? 453 ARG D CZ  1 
ATOM   14168 N  NH1 . ARG D  1 422 ? -4.36500  26.61300  34.10800  1.000 93.58000  ? 453 ARG D NH1 1 
ATOM   14169 N  NH2 . ARG D  1 422 ? -3.24600  24.94100  35.20600  1.000 79.13000  ? 453 ARG D NH2 1 
ATOM   14170 N  N   . TYR D  1 423 ? -10.99900 24.69200  37.64300  1.000 78.97000  ? 454 TYR D N   1 
ATOM   14171 C  CA  . TYR D  1 423 ? -12.27600 25.35500  37.36500  1.000 73.07000  ? 454 TYR D CA  1 
ATOM   14172 C  C   . TYR D  1 423 ? -13.46400 24.45200  37.67800  1.000 73.96000  ? 454 TYR D C   1 
ATOM   14173 O  O   . TYR D  1 423 ? -14.22800 24.09800  36.77400  1.000 77.68000  ? 454 TYR D O   1 
ATOM   14174 C  CB  . TYR D  1 423 ? -12.35200 25.79800  35.90400  1.000 75.31000  ? 454 TYR D CB  1 
ATOM   14175 C  CG  . TYR D  1 423 ? -11.14200 26.52400  35.34000  1.000 83.29000  ? 454 TYR D CG  1 
ATOM   14176 C  CD1 . TYR D  1 423 ? -10.68300 27.71600  35.88200  1.000 84.93000  ? 454 TYR D CD1 1 
ATOM   14177 C  CD2 . TYR D  1 423 ? -10.52200 26.05800  34.18600  1.000 85.08000  ? 454 TYR D CD2 1 
ATOM   14178 C  CE1 . TYR D  1 423 ? -9.58900  28.38400  35.32600  1.000 87.48000  ? 454 TYR D CE1 1 
ATOM   14179 C  CE2 . TYR D  1 423 ? -9.44400  26.72000  33.62200  1.000 85.45000  ? 454 TYR D CE2 1 
ATOM   14180 C  CZ  . TYR D  1 423 ? -8.98200  27.88100  34.19200  1.000 89.65000  ? 454 TYR D CZ  1 
ATOM   14181 O  OH  . TYR D  1 423 ? -7.90800  28.52700  33.61800  1.000 92.61000  ? 454 TYR D OH  1 
ATOM   14182 N  N   . PRO D  1 424 ? -13.68300 24.08900  38.94700  1.000 77.01000  ? 455 PRO D N   1 
ATOM   14183 C  CA  . PRO D  1 424 ? -14.77800 23.14100  39.25000  1.000 73.67000  ? 455 PRO D CA  1 
ATOM   14184 C  C   . PRO D  1 424 ? -16.17800 23.67900  38.96100  1.000 80.18000  ? 455 PRO D C   1 
ATOM   14185 O  O   . PRO D  1 424 ? -17.11000 22.87700  38.80200  1.000 75.48000  ? 455 PRO D O   1 
ATOM   14186 C  CB  . PRO D  1 424 ? -14.58700 22.84500  40.74400  1.000 70.15000  ? 455 PRO D CB  1 
ATOM   14187 C  CG  . PRO D  1 424 ? -13.95100 24.07200  41.27300  1.000 77.43000  ? 455 PRO D CG  1 
ATOM   14188 C  CD  . PRO D  1 424 ? -13.00300 24.54000  40.17300  1.000 79.00000  ? 455 PRO D CD  1 
ATOM   14189 N  N   . ASP D  1 425 ? -16.36500 24.99700  38.88600  1.000 81.25000  ? 456 ASP D N   1 
ATOM   14190 C  CA  . ASP D  1 425 ? -17.66900 25.52600  38.49800  1.000 81.27000  ? 456 ASP D CA  1 
ATOM   14191 C  C   . ASP D  1 425 ? -18.01900 25.12800  37.06100  1.000 83.46000  ? 456 ASP D C   1 
ATOM   14192 O  O   . ASP D  1 425 ? -19.14100 24.67800  36.79400  1.000 80.16000  ? 456 ASP D O   1 
ATOM   14193 C  CB  . ASP D  1 425 ? -17.71400 27.04800  38.68100  1.000 83.79000  ? 456 ASP D CB  1 
ATOM   14194 C  CG  . ASP D  1 425 ? -16.48400 27.75300  38.11800  1.000 91.86000  ? 456 ASP D CG  1 
ATOM   14195 O  OD1 . ASP D  1 425 ? -15.33500 27.27500  38.30900  1.000 80.53000  ? 456 ASP D OD1 1 
ATOM   14196 O  OD2 . ASP D  1 425 ? -16.68500 28.79500  37.45600  1.000 98.42000  ? 456 ASP D OD2 1 
ATOM   14197 N  N   . ARG D  1 426 ? -17.07400 25.30000  36.11700  1.000 81.93000  ? 457 ARG D N   1 
ATOM   14198 C  CA  . ARG D  1 426 ? -17.32800 24.90700  34.72800  1.000 80.08000  ? 457 ARG D CA  1 
ATOM   14199 C  C   . ARG D  1 426 ? -17.73000 23.44000  34.66200  1.000 76.66000  ? 457 ARG D C   1 
ATOM   14200 O  O   . ARG D  1 426 ? -18.70900 23.07300  34.00200  1.000 80.75000  ? 457 ARG D O   1 
ATOM   14201 C  CB  . ARG D  1 426 ? -16.07700 25.13200  33.86400  1.000 76.49000  ? 457 ARG D CB  1 
ATOM   14202 C  CG  . ARG D  1 426 ? -16.13000 26.22700  32.78500  1.000 78.24000  ? 457 ARG D CG  1 
ATOM   14203 C  CD  . ARG D  1 426 ? -15.39500 27.48500  33.27900  1.000 91.44000  ? 457 ARG D CD  1 
ATOM   14204 N  NE  . ARG D  1 426 ? -14.46100 28.10200  32.33100  1.000 97.43000  ? 457 ARG D NE  1 
ATOM   14205 C  CZ  . ARG D  1 426 ? -13.52800 28.99400  32.66700  1.000 90.77000  ? 457 ARG D CZ  1 
ATOM   14206 N  NH1 . ARG D  1 426 ? -13.34300 29.36200  33.92500  1.000 84.79000  ? 457 ARG D NH1 1 
ATOM   14207 N  NH2 . ARG D  1 426 ? -12.76200 29.53300  31.71700  1.000 82.64000  ? 457 ARG D NH2 1 
ATOM   14208 N  N   . LEU D  1 427 ? -16.99200 22.59100  35.37600  1.000 76.47000  ? 458 LEU D N   1 
ATOM   14209 C  CA  . LEU D  1 427 ? -17.25900 21.15800  35.38200  1.000 77.99000  ? 458 LEU D CA  1 
ATOM   14210 C  C   . LEU D  1 427 ? -18.67800 20.84200  35.84600  1.000 74.04000  ? 458 LEU D C   1 
ATOM   14211 O  O   . LEU D  1 427 ? -19.41100 20.10800  35.17600  1.000 74.13000  ? 458 LEU D O   1 
ATOM   14212 C  CB  . LEU D  1 427 ? -16.24100 20.45100  36.27600  1.000 67.79000  ? 458 LEU D CB  1 
ATOM   14213 C  CG  . LEU D  1 427 ? -16.57200 18.98500  36.54300  1.000 67.65000  ? 458 LEU D CG  1 
ATOM   14214 C  CD1 . LEU D  1 427 ? -16.40600 18.17700  35.27000  1.000 70.56000  ? 458 LEU D CD1 1 
ATOM   14215 C  CD2 . LEU D  1 427 ? -15.76200 18.41100  37.69100  1.000 69.26000  ? 458 LEU D CD2 1 
ATOM   14216 N  N   . LYS D  1 428 ? -19.08800 21.40000  36.99200  1.000 76.79000  ? 459 LYS D N   1 
ATOM   14217 C  CA  . LYS D  1 428 ? -20.35100 21.00400  37.61000  1.000 73.51000  ? 459 LYS D CA  1 
ATOM   14218 C  C   . LYS D  1 428 ? -21.55600 21.46500  36.79100  1.000 76.87000  ? 459 LYS D C   1 
ATOM   14219 O  O   . LYS D  1 428 ? -22.58800 20.78200  36.76700  1.000 72.69000  ? 459 LYS D O   1 
ATOM   14220 C  CB  . LYS D  1 428 ? -20.43000 21.57700  39.03100  1.000 72.31000  ? 459 LYS D CB  1 
ATOM   14221 C  CG  . LYS D  1 428 ? -19.37800 21.03500  40.00400  1.000 74.36000  ? 459 LYS D CG  1 
ATOM   14222 C  CD  . LYS D  1 428 ? -19.75400 19.70200  40.61400  1.000 80.33000  ? 459 LYS D CD  1 
ATOM   14223 C  CE  . LYS D  1 428 ? -19.20100 19.58100  42.03200  1.000 79.86000  ? 459 LYS D CE  1 
ATOM   14224 N  NZ  . LYS D  1 428 ? -19.90800 18.55200  42.84400  1.000 79.14000  ? 459 LYS D NZ  1 
ATOM   14225 N  N   . GLU D  1 429 ? -21.44800 22.61100  36.11400  1.000 74.29000  ? 460 GLU D N   1 
ATOM   14226 C  CA  . GLU D  1 429 ? -22.51600 23.03900  35.21900  1.000 70.23000  ? 460 GLU D CA  1 
ATOM   14227 C  C   . GLU D  1 429 ? -22.56800 22.16200  33.97500  1.000 77.49000  ? 460 GLU D C   1 
ATOM   14228 O  O   . GLU D  1 429 ? -23.65600 21.80700  33.49800  1.000 75.08000  ? 460 GLU D O   1 
ATOM   14229 C  CB  . GLU D  1 429 ? -22.33300 24.50800  34.83900  1.000 69.40000  ? 460 GLU D CB  1 
ATOM   14230 N  N   . MET D  1 430 ? -21.40000 21.79800  33.43400  1.000 73.67000  ? 461 MET D N   1 
ATOM   14231 C  CA  . MET D  1 430 ? -21.39200 20.91900  32.27200  1.000 73.40000  ? 461 MET D CA  1 
ATOM   14232 C  C   . MET D  1 430 ? -21.89200 19.53100  32.63300  1.000 72.35000  ? 461 MET D C   1 
ATOM   14233 O  O   . MET D  1 430 ? -22.58300 18.89700  31.83200  1.000 69.44000  ? 461 MET D O   1 
ATOM   14234 C  CB  . MET D  1 430 ? -19.99800 20.86400  31.65200  1.000 72.54000  ? 461 MET D CB  1 
ATOM   14235 C  CG  . MET D  1 430 ? -19.60400 22.14100  30.93100  1.000 72.88000  ? 461 MET D CG  1 
ATOM   14236 S  SD  . MET D  1 430 ? -17.95600 22.06100  30.19700  1.000 75.60000  ? 461 MET D SD  1 
ATOM   14237 C  CE  . MET D  1 430 ? -17.95600 23.57700  29.25300  1.000 74.53000  ? 461 MET D CE  1 
ATOM   14238 N  N   . ILE D  1 431 ? -21.60000 19.06200  33.84600  1.000 68.49000  ? 462 ILE D N   1 
ATOM   14239 C  CA  . ILE D  1 431 ? -22.14200 17.77900  34.28700  1.000 73.95000  ? 462 ILE D CA  1 
ATOM   14240 C  C   . ILE D  1 431 ? -23.66400 17.85300  34.39100  1.000 78.77000  ? 462 ILE D C   1 
ATOM   14241 O  O   . ILE D  1 431 ? -24.37400 16.89500  34.05400  1.000 76.59000  ? 462 ILE D O   1 
ATOM   14242 C  CB  . ILE D  1 431 ? -21.51500 17.37700  35.63700  1.000 76.28000  ? 462 ILE D CB  1 
ATOM   14243 C  CG1 . ILE D  1 431 ? -20.03400 17.02200  35.47500  1.000 76.47000  ? 462 ILE D CG1 1 
ATOM   14244 C  CG2 . ILE D  1 431 ? -22.27300 16.19500  36.26700  1.000 74.13000  ? 462 ILE D CG2 1 
ATOM   14245 C  CD1 . ILE D  1 431 ? -19.68500 16.37800  34.15400  1.000 73.23000  ? 462 ILE D CD1 1 
ATOM   14246 N  N   . ALA D  1 432 ? -24.18700 19.00200  34.84700  1.000 78.93000  ? 463 ALA D N   1 
ATOM   14247 C  CA  . ALA D  1 432 ? -25.63400 19.18400  34.98400  1.000 83.60000  ? 463 ALA D CA  1 
ATOM   14248 C  C   . ALA D  1 432 ? -26.34400 19.12300  33.64000  1.000 75.95000  ? 463 ALA D C   1 
ATOM   14249 O  O   . ALA D  1 432 ? -27.34200 18.41300  33.48200  1.000 71.73000  ? 463 ALA D O   1 
ATOM   14250 C  CB  . ALA D  1 432 ? -25.92800 20.52100  35.67000  1.000 76.90000  ? 463 ALA D CB  1 
ATOM   14251 N  N   . LYS D  1 433 ? -25.84800 19.88500  32.67300  1.000 74.43000  ? 464 LYS D N   1 
ATOM   14252 C  CA  . LYS D  1 433 ? -26.44600 19.89900  31.34700  1.000 70.00000  ? 464 LYS D CA  1 
ATOM   14253 C  C   . LYS D  1 433 ? -26.40300 18.52800  30.68600  1.000 76.72000  ? 464 LYS D C   1 
ATOM   14254 O  O   . LYS D  1 433 ? -27.39600 18.08300  30.09800  1.000 78.43000  ? 464 LYS D O   1 
ATOM   14255 C  CB  . LYS D  1 433 ? -25.73900 20.93900  30.48800  1.000 75.01000  ? 464 LYS D CB  1 
ATOM   14256 C  CG  . LYS D  1 433 ? -26.30500 21.04300  29.06700  1.000 87.89000  ? 464 LYS D CG  1 
ATOM   14257 C  CD  . LYS D  1 433 ? -25.94700 22.35900  28.42000  1.000 90.24000  ? 464 LYS D CD  1 
ATOM   14258 C  CE  . LYS D  1 433 ? -26.49100 22.42900  27.01000  1.000 91.92000  ? 464 LYS D CE  1 
ATOM   14259 N  NZ  . LYS D  1 433 ? -27.94300 22.40600  26.81100  1.000 92.94000  ? 464 LYS D NZ  1 
ATOM   14260 N  N   . THR D  1 434 ? -25.26500 17.84200  30.78600  1.000 74.65000  ? 465 THR D N   1 
ATOM   14261 C  CA  . THR D  1 434 ? -25.13500 16.49000  30.25800  1.000 74.84000  ? 465 THR D CA  1 
ATOM   14262 C  C   . THR D  1 434 ? -26.11000 15.54300  30.95000  1.000 76.01000  ? 465 THR D C   1 
ATOM   14263 O  O   . THR D  1 434 ? -26.70100 14.66100  30.31400  1.000 73.39000  ? 465 THR D O   1 
ATOM   14264 C  CB  . THR D  1 434 ? -23.68500 16.02400  30.44900  1.000 75.95000  ? 465 THR D CB  1 
ATOM   14265 O  OG1 . THR D  1 434 ? -22.80600 16.93300  29.77800  1.000 76.52000  ? 465 THR D OG1 1 
ATOM   14266 C  CG2 . THR D  1 434 ? -23.47400 14.61900  29.93400  1.000 73.57000  ? 465 THR D CG2 1 
ATOM   14267 N  N   . GLN D  1 435 ? -26.27900 15.70100  32.26400  1.000 76.75000  ? 466 GLN D N   1 
ATOM   14268 C  CA  . GLN D  1 435 ? -27.26600 14.89400  32.96800  1.000 79.05000  ? 466 GLN D CA  1 
ATOM   14269 C  C   . GLN D  1 435 ? -28.67300 15.20400  32.47600  1.000 81.34000  ? 466 GLN D C   1 
ATOM   14270 O  O   . GLN D  1 435 ? -29.50100 14.29700  32.32500  1.000 79.61000  ? 466 GLN D O   1 
ATOM   14271 C  CB  . GLN D  1 435 ? -27.16300 15.10500  34.47400  1.000 78.85000  ? 466 GLN D CB  1 
ATOM   14272 C  CG  . GLN D  1 435 ? -28.07800 14.16700  35.22800  1.000 74.47000  ? 466 GLN D CG  1 
ATOM   14273 C  CD  . GLN D  1 435 ? -27.72600 14.04800  36.67500  1.000 70.76000  ? 466 GLN D CD  1 
ATOM   14274 O  OE1 . GLN D  1 435 ? -27.99800 13.02700  37.30200  1.000 73.44000  ? 466 GLN D OE1 1 
ATOM   14275 N  NE2 . GLN D  1 435 ? -27.11000 15.08800  37.22500  1.000 75.85000  ? 466 GLN D NE2 1 
ATOM   14276 N  N   . GLU D  1 436 ? -28.97000 16.48500  32.24200  1.000 81.26000  ? 467 GLU D N   1 
ATOM   14277 C  CA  . GLU D  1 436 ? -30.27900 16.83500  31.70300  1.000 84.79000  ? 467 GLU D CA  1 
ATOM   14278 C  C   . GLU D  1 436 ? -30.52100 16.09200  30.39700  1.000 84.33000  ? 467 GLU D C   1 
ATOM   14279 O  O   . GLU D  1 436 ? -31.60400 15.53400  30.17700  1.000 83.07000  ? 467 GLU D O   1 
ATOM   14280 C  CB  . GLU D  1 436 ? -30.37100 18.35200  31.48300  1.000 87.79000  ? 467 GLU D CB  1 
ATOM   14281 C  CG  . GLU D  1 436 ? -31.76300 18.88100  31.11800  1.000 90.62000  ? 467 GLU D CG  1 
ATOM   14282 C  CD  . GLU D  1 436 ? -32.81700 18.54500  32.16500  1.000 95.02000  ? 467 GLU D CD  1 
ATOM   14283 O  OE1 . GLU D  1 436 ? -32.50100 18.61800  33.37300  1.000 93.77000  ? 467 GLU D OE1 1 
ATOM   14284 O  OE2 . GLU D  1 436 ? -33.95700 18.20000  31.78300  1.000 100.64000 ? 467 GLU D OE2 1 
ATOM   14285 N  N   . TRP D  1 437 ? -29.49500 16.03700  29.54500  1.000 77.65000  ? 468 TRP D N   1 
ATOM   14286 C  CA  . TRP D  1 437 ? -29.57600 15.28600  28.29900  1.000 76.49000  ? 468 TRP D CA  1 
ATOM   14287 C  C   . TRP D  1 437 ? -29.93400 13.82700  28.55200  1.000 72.86000  ? 468 TRP D C   1 
ATOM   14288 O  O   . TRP D  1 437 ? -30.81600 13.27800  27.89100  1.000 75.87000  ? 468 TRP D O   1 
ATOM   14289 C  CB  . TRP D  1 437 ? -28.25100 15.41600  27.55000  1.000 81.34000  ? 468 TRP D CB  1 
ATOM   14290 C  CG  . TRP D  1 437 ? -28.12300 14.64000  26.27400  1.000 82.83000  ? 468 TRP D CG  1 
ATOM   14291 C  CD1 . TRP D  1 437 ? -28.86900 14.78700  25.14000  1.000 77.27000  ? 468 TRP D CD1 1 
ATOM   14292 C  CD2 . TRP D  1 437 ? -27.15800 13.61900  25.98900  1.000 81.05000  ? 468 TRP D CD2 1 
ATOM   14293 N  NE1 . TRP D  1 437 ? -28.43400 13.91300  24.17100  1.000 72.12000  ? 468 TRP D NE1 1 
ATOM   14294 C  CE2 . TRP D  1 437 ? -27.38900 13.18100  24.66800  1.000 78.84000  ? 468 TRP D CE2 1 
ATOM   14295 C  CE3 . TRP D  1 437 ? -26.12700 13.02600  26.72700  1.000 74.38000  ? 468 TRP D CE3 1 
ATOM   14296 C  CZ2 . TRP D  1 437 ? -26.62700 12.17700  24.06900  1.000 77.84000  ? 468 TRP D CZ2 1 
ATOM   14297 C  CZ3 . TRP D  1 437 ? -25.37300 12.02800  26.13300  1.000 75.98000  ? 468 TRP D CZ3 1 
ATOM   14298 C  CH2 . TRP D  1 437 ? -25.62800 11.61200  24.81700  1.000 75.91000  ? 468 TRP D CH2 1 
ATOM   14299 N  N   . THR D  1 438 ? -29.31000 13.19400  29.54500  1.000 79.82000  ? 469 THR D N   1 
ATOM   14300 C  CA  . THR D  1 438 ? -29.56900 11.77200  29.75000  1.000 81.60000  ? 469 THR D CA  1 
ATOM   14301 C  C   . THR D  1 438 ? -30.99000 11.47800  30.22500  1.000 82.26000  ? 469 THR D C   1 
ATOM   14302 O  O   . THR D  1 438 ? -31.45700 10.34600  30.05700  1.000 77.88000  ? 469 THR D O   1 
ATOM   14303 C  CB  . THR D  1 438 ? -28.56100 11.17800  30.74700  1.000 77.16000  ? 469 THR D CB  1 
ATOM   14304 O  OG1 . THR D  1 438 ? -28.40100 9.78200   30.48000  1.000 82.57000  ? 469 THR D OG1 1 
ATOM   14305 C  CG2 . THR D  1 438 ? -29.03500 11.32900  32.18600  1.000 78.71000  ? 469 THR D CG2 1 
ATOM   14306 N  N   . LYS D  1 439 ? -31.71500 12.47400  30.74500  1.000 82.81000  ? 470 LYS D N   1 
ATOM   14307 C  CA  . LYS D  1 439 ? -33.07900 12.21600  31.19700  1.000 80.82000  ? 470 LYS D CA  1 
ATOM   14308 C  C   . LYS D  1 439 ? -34.02600 11.89400  30.04700  1.000 81.60000  ? 470 LYS D C   1 
ATOM   14309 O  O   . LYS D  1 439 ? -35.08100 11.30000  30.28800  1.000 83.66000  ? 470 LYS D O   1 
ATOM   14310 C  CB  . LYS D  1 439 ? -33.61100 13.40400  32.00600  1.000 80.07000  ? 470 LYS D CB  1 
ATOM   14311 N  N   . SER D  1 440 ? -33.66400 12.23500  28.80700  1.000 81.14000  ? 471 SER D N   1 
ATOM   14312 C  CA  . SER D  1 440 ? -34.51700 11.97600  27.65000  1.000 77.59000  ? 471 SER D CA  1 
ATOM   14313 C  C   . SER D  1 440 ? -34.24700 10.62700  26.99700  1.000 75.79000  ? 471 SER D C   1 
ATOM   14314 O  O   . SER D  1 440 ? -34.84400 10.32500  25.95900  1.000 72.51000  ? 471 SER D O   1 
ATOM   14315 C  CB  . SER D  1 440 ? -34.36100 13.08800  26.60100  1.000 69.33000  ? 471 SER D CB  1 
ATOM   14316 O  OG  . SER D  1 440 ? -33.09400 13.04200  25.97400  1.000 66.93000  ? 471 SER D OG  1 
ATOM   14317 N  N   . PHE D  1 441 ? -33.36300 9.81200   27.56000  1.000 77.33000  ? 472 PHE D N   1 
ATOM   14318 C  CA  . PHE D  1 441 ? -32.98000 8.59400   26.86700  1.000 76.09000  ? 472 PHE D CA  1 
ATOM   14319 C  C   . PHE D  1 441 ? -34.13300 7.59900   26.85100  1.000 76.84000  ? 472 PHE D C   1 
ATOM   14320 O  O   . PHE D  1 441 ? -35.04200 7.64100   27.68400  1.000 75.49000  ? 472 PHE D O   1 
ATOM   14321 C  CB  . PHE D  1 441 ? -31.74600 7.96600   27.51400  1.000 75.91000  ? 472 PHE D CB  1 
ATOM   14322 C  CG  . PHE D  1 441 ? -30.46900 8.70500   27.21500  1.000 77.71000  ? 472 PHE D CG  1 
ATOM   14323 C  CD1 . PHE D  1 441 ? -30.49100 9.88900   26.48000  1.000 71.20000  ? 472 PHE D CD1 1 
ATOM   14324 C  CD2 . PHE D  1 441 ? -29.25000 8.22000   27.67100  1.000 74.31000  ? 472 PHE D CD2 1 
ATOM   14325 C  CE1 . PHE D  1 441 ? -29.33000 10.57700  26.20000  1.000 73.69000  ? 472 PHE D CE1 1 
ATOM   14326 C  CE2 . PHE D  1 441 ? -28.08100 8.90000   27.39300  1.000 76.27000  ? 472 PHE D CE2 1 
ATOM   14327 C  CZ  . PHE D  1 441 ? -28.12000 10.08500  26.65600  1.000 76.89000  ? 472 PHE D CZ  1 
ATOM   14328 N  N   . VAL D  1 442 ? -34.07900 6.68700   25.88700  1.000 75.82000  ? 473 VAL D N   1 
ATOM   14329 C  CA  . VAL D  1 442 ? -35.03800 5.60000   25.80500  1.000 71.81000  ? 473 VAL D CA  1 
ATOM   14330 C  C   . VAL D  1 442 ? -34.33100 4.30300   26.16900  1.000 69.46000  ? 473 VAL D C   1 
ATOM   14331 O  O   . VAL D  1 442 ? -33.10800 4.24200   26.28600  1.000 73.40000  ? 473 VAL D O   1 
ATOM   14332 C  CB  . VAL D  1 442 ? -35.69300 5.50800   24.41500  1.000 69.28000  ? 473 VAL D CB  1 
ATOM   14333 C  CG1 . VAL D  1 442 ? -36.27700 6.85500   24.02400  1.000 65.06000  ? 473 VAL D CG1 1 
ATOM   14334 C  CG2 . VAL D  1 442 ? -34.69000 5.03200   23.39200  1.000 67.83000  ? 473 VAL D CG2 1 
ATOM   14335 N  N   . LYS D  1 443 ? -35.11700 3.26300   26.36700  1.000 69.60000  ? 474 LYS D N   1 
ATOM   14336 C  CA  . LYS D  1 443 ? -34.52300 1.96300   26.58600  1.000 74.39000  ? 474 LYS D CA  1 
ATOM   14337 C  C   . LYS D  1 443 ? -33.90200 1.47700   25.27800  1.000 73.37000  ? 474 LYS D C   1 
ATOM   14338 O  O   . LYS D  1 443 ? -34.41300 1.78200   24.19200  1.000 72.25000  ? 474 LYS D O   1 
ATOM   14339 C  CB  . LYS D  1 443 ? -35.57500 0.96800   27.09100  1.000 72.42000  ? 474 LYS D CB  1 
ATOM   14340 C  CG  . LYS D  1 443 ? -35.06500 -0.45000  27.32800  1.000 78.03000  ? 474 LYS D CG  1 
ATOM   14341 C  CD  . LYS D  1 443 ? -35.91300 -1.49300  26.60400  1.000 80.29000  ? 474 LYS D CD  1 
ATOM   14342 C  CE  . LYS D  1 443 ? -35.37600 -2.90100  26.84100  1.000 82.93000  ? 474 LYS D CE  1 
ATOM   14343 N  NZ  . LYS D  1 443 ? -33.93100 -3.03200  26.49400  1.000 78.69000  ? 474 LYS D NZ  1 
ATOM   14344 N  N   . PRO D  1 444 ? -32.76900 0.78500   25.33800  1.000 73.73000  ? 475 PRO D N   1 
ATOM   14345 C  CA  . PRO D  1 444 ? -32.24200 0.16200   24.12300  1.000 76.59000  ? 475 PRO D CA  1 
ATOM   14346 C  C   . PRO D  1 444 ? -33.23200 -0.86200  23.59900  1.000 75.87000  ? 475 PRO D C   1 
ATOM   14347 O  O   . PRO D  1 444 ? -33.71900 -1.72100  24.33900  1.000 77.41000  ? 475 PRO D O   1 
ATOM   14348 C  CB  . PRO D  1 444 ? -30.94000 -0.50000  24.59500  1.000 75.64000  ? 475 PRO D CB  1 
ATOM   14349 C  CG  . PRO D  1 444 ? -31.08800 -0.62900  26.08000  1.000 75.85000  ? 475 PRO D CG  1 
ATOM   14350 C  CD  . PRO D  1 444 ? -31.87600 0.58200   26.48700  1.000 74.80000  ? 475 PRO D CD  1 
ATOM   14351 N  N   . LEU D  1 445 ? -33.49000 -0.79900  22.29800  1.000 75.08000  ? 476 LEU D N   1 
ATOM   14352 C  CA  . LEU D  1 445 ? -34.33900 -1.81000  21.69400  1.000 73.04000  ? 476 LEU D CA  1 
ATOM   14353 C  C   . LEU D  1 445 ? -33.65000 -3.16500  21.71900  1.000 72.93000  ? 476 LEU D C   1 
ATOM   14354 O  O   . LEU D  1 445 ? -34.31300 -4.20600  21.79200  1.000 79.21000  ? 476 LEU D O   1 
ATOM   14355 C  CB  . LEU D  1 445 ? -34.66400 -1.39200  20.26800  1.000 69.26000  ? 476 LEU D CB  1 
ATOM   14356 C  CG  . LEU D  1 445 ? -35.40600 -0.06600  20.14100  1.000 70.93000  ? 476 LEU D CG  1 
ATOM   14357 C  CD1 . LEU D  1 445 ? -35.52200 0.30200   18.68000  1.000 67.60000  ? 476 LEU D CD1 1 
ATOM   14358 C  CD2 . LEU D  1 445 ? -36.78700 -0.14600  20.79100  1.000 68.49000  ? 476 LEU D CD2 1 
ATOM   14359 N  N   . TRP D  1 446 ? -32.32400 -3.16700  21.72600  1.000 69.41000  ? 477 TRP D N   1 
ATOM   14360 C  CA  . TRP D  1 446 ? -31.55100 -4.38700  21.86200  1.000 72.35000  ? 477 TRP D CA  1 
ATOM   14361 C  C   . TRP D  1 446 ? -30.20700 -4.02900  22.48300  1.000 69.81000  ? 477 TRP D C   1 
ATOM   14362 O  O   . TRP D  1 446 ? -29.76900 -2.87700  22.44800  1.000 70.08000  ? 477 TRP D O   1 
ATOM   14363 C  CB  . TRP D  1 446 ? -31.37200 -5.07100  20.50000  1.000 67.79000  ? 477 TRP D CB  1 
ATOM   14364 C  CG  . TRP D  1 446 ? -30.66500 -4.19400  19.48800  1.000 65.19000  ? 477 TRP D CG  1 
ATOM   14365 C  CD1 . TRP D  1 446 ? -29.31600 -4.06800  19.31300  1.000 66.25000  ? 477 TRP D CD1 1 
ATOM   14366 C  CD2 . TRP D  1 446 ? -31.27200 -3.31300  18.53200  1.000 68.52000  ? 477 TRP D CD2 1 
ATOM   14367 N  NE1 . TRP D  1 446 ? -29.04800 -3.16900  18.30600  1.000 63.61000  ? 477 TRP D NE1 1 
ATOM   14368 C  CE2 . TRP D  1 446 ? -30.23100 -2.69000  17.81200  1.000 63.01000  ? 477 TRP D CE2 1 
ATOM   14369 C  CE3 . TRP D  1 446 ? -32.59300 -2.99400  18.21300  1.000 68.24000  ? 477 TRP D CE3 1 
ATOM   14370 C  CZ2 . TRP D  1 446 ? -30.47100 -1.77500  16.79100  1.000 59.67000  ? 477 TRP D CZ2 1 
ATOM   14371 C  CZ3 . TRP D  1 446 ? -32.83000 -2.07800  17.20100  1.000 69.84000  ? 477 TRP D CZ3 1 
ATOM   14372 C  CH2 . TRP D  1 446 ? -31.77300 -1.48100  16.50200  1.000 67.49000  ? 477 TRP D CH2 1 
ATOM   14373 N  N   . VAL D  1 447 ? -29.54700 -5.03500  23.03900  1.000 72.06000  ? 478 VAL D N   1 
ATOM   14374 C  CA  . VAL D  1 447 ? -28.20700 -4.85800  23.58000  1.000 69.44000  ? 478 VAL D CA  1 
ATOM   14375 C  C   . VAL D  1 447 ? -27.26800 -5.79700  22.83400  1.000 68.66000  ? 478 VAL D C   1 
ATOM   14376 O  O   . VAL D  1 447 ? -27.66500 -6.42000  21.84400  1.000 75.08000  ? 478 VAL D O   1 
ATOM   14377 C  CB  . VAL D  1 447 ? -28.18300 -5.10100  25.10100  1.000 70.84000  ? 478 VAL D CB  1 
ATOM   14378 C  CG1 . VAL D  1 447 ? -29.09600 -4.10300  25.81500  1.000 67.01000  ? 478 VAL D CG1 1 
ATOM   14379 C  CG2 . VAL D  1 447 ? -28.59900 -6.51600  25.41400  1.000 70.22000  ? 478 VAL D CG2 1 
ATOM   14380 N  N   . TYR D  1 448 ? -26.02400 -5.90800  23.29100  1.000 67.33000  ? 479 TYR D N   1 
ATOM   14381 C  CA  . TYR D  1 448 ? -25.00300 -6.64800  22.56100  1.000 64.74000  ? 479 TYR D CA  1 
ATOM   14382 C  C   . TYR D  1 448 ? -24.57900 -7.94700  23.22600  1.000 70.64000  ? 479 TYR D C   1 
ATOM   14383 O  O   . TYR D  1 448 ? -24.34000 -8.93200  22.52800  1.000 72.16000  ? 479 TYR D O   1 
ATOM   14384 C  CB  . TYR D  1 448 ? -23.76100 -5.77600  22.34600  1.000 64.22000  ? 479 TYR D CB  1 
ATOM   14385 C  CG  . TYR D  1 448 ? -22.76900 -6.38600  21.37900  1.000 63.07000  ? 479 TYR D CG  1 
ATOM   14386 C  CD1 . TYR D  1 448 ? -22.96200 -6.28900  20.01100  1.000 60.30000  ? 479 TYR D CD1 1 
ATOM   14387 C  CD2 . TYR D  1 448 ? -21.65200 -7.06900  21.83300  1.000 66.05000  ? 479 TYR D CD2 1 
ATOM   14388 C  CE1 . TYR D  1 448 ? -22.06300 -6.84500  19.11400  1.000 66.62000  ? 479 TYR D CE1 1 
ATOM   14389 C  CE2 . TYR D  1 448 ? -20.73900 -7.63100  20.94600  1.000 68.47000  ? 479 TYR D CE2 1 
ATOM   14390 C  CZ  . TYR D  1 448 ? -20.95400 -7.51700  19.58400  1.000 72.96000  ? 479 TYR D CZ  1 
ATOM   14391 O  OH  . TYR D  1 448 ? -20.05700 -8.06900  18.69700  1.000 71.94000  ? 479 TYR D OH  1 
ATOM   14392 N  N   . SER D  1 449 ? -24.45500 -8.00200  24.54700  1.000 67.58000  ? 480 SER D N   1 
ATOM   14393 C  CA  . SER D  1 449 ? -23.98700 -9.22600  25.17600  1.000 68.07000  ? 480 SER D CA  1 
ATOM   14394 C  C   . SER D  1 449 ? -24.98400 -9.67900  26.22900  1.000 68.94000  ? 480 SER D C   1 
ATOM   14395 O  O   . SER D  1 449 ? -25.84600 -8.92000  26.67300  1.000 67.60000  ? 480 SER D O   1 
ATOM   14396 C  CB  . SER D  1 449 ? -22.59800 -9.07000  25.82700  1.000 68.75000  ? 480 SER D CB  1 
ATOM   14397 O  OG  . SER D  1 449 ? -22.66400 -8.26300  26.98500  1.000 68.49000  ? 480 SER D OG  1 
ATOM   14398 N  N   . VAL D  1 450 ? -24.85900 -10.95300 26.60100  1.000 67.03000  ? 481 VAL D N   1 
ATOM   14399 C  CA  . VAL D  1 450 ? -25.63400 -11.48500 27.71700  1.000 72.86000  ? 481 VAL D CA  1 
ATOM   14400 C  C   . VAL D  1 450 ? -25.40000 -10.63000 28.95600  1.000 74.11000  ? 481 VAL D C   1 
ATOM   14401 O  O   . VAL D  1 450 ? -26.34400 -10.25200 29.66100  1.000 72.44000  ? 481 VAL D O   1 
ATOM   14402 C  CB  . VAL D  1 450 ? -25.26400 -12.95800 27.96300  1.000 75.83000  ? 481 VAL D CB  1 
ATOM   14403 C  CG1 . VAL D  1 450 ? -25.95500 -13.48200 29.21300  1.000 77.19000  ? 481 VAL D CG1 1 
ATOM   14404 C  CG2 . VAL D  1 450 ? -25.58300 -13.80900 26.73400  1.000 72.41000  ? 481 VAL D CG2 1 
ATOM   14405 N  N   . LYS D  1 451 ? -24.12600 -10.29400 29.21500  1.000 75.50000  ? 482 LYS D N   1 
ATOM   14406 C  CA  . LYS D  1 451 ? -23.76500 -9.38600  30.30200  1.000 69.63000  ? 482 LYS D CA  1 
ATOM   14407 C  C   . LYS D  1 451 ? -24.53500 -8.07300  30.22800  1.000 69.94000  ? 482 LYS D C   1 
ATOM   14408 O  O   . LYS D  1 451 ? -24.97300 -7.54900  31.25600  1.000 72.46000  ? 482 LYS D O   1 
ATOM   14409 C  CB  . LYS D  1 451 ? -22.26100 -9.12100  30.28100  1.000 67.93000  ? 482 LYS D CB  1 
ATOM   14410 N  N   . ASP D  1 452 ? -24.67400 -7.50000  29.02600  1.000 70.84000  ? 483 ASP D N   1 
ATOM   14411 C  CA  . ASP D  1 452 ? -25.49700 -6.30100  28.86500  1.000 68.70000  ? 483 ASP D CA  1 
ATOM   14412 C  C   . ASP D  1 452 ? -26.93900 -6.55400  29.30200  1.000 74.26000  ? 483 ASP D C   1 
ATOM   14413 O  O   . ASP D  1 452 ? -27.55900 -5.71300  29.96700  1.000 75.91000  ? 483 ASP D O   1 
ATOM   14414 C  CB  . ASP D  1 452 ? -25.46100 -5.81000  27.41600  1.000 73.61000  ? 483 ASP D CB  1 
ATOM   14415 C  CG  . ASP D  1 452 ? -24.12100 -5.21200  27.01900  1.000 70.25000  ? 483 ASP D CG  1 
ATOM   14416 O  OD1 . ASP D  1 452 ? -23.32400 -4.84200  27.90700  1.000 64.57000  ? 483 ASP D OD1 1 
ATOM   14417 O  OD2 . ASP D  1 452 ? -23.88300 -5.08600  25.80100  1.000 70.99000  ? 483 ASP D OD2 1 
ATOM   14418 N  N   . LYS D  1 453 ? -27.51200 -7.68500  28.88500  1.000 73.93000  ? 484 LYS D N   1 
ATOM   14419 C  CA  . LYS D  1 453 ? -28.90800 -7.95300  29.21800  1.000 81.16000  ? 484 LYS D CA  1 
ATOM   14420 C  C   . LYS D  1 453 ? -29.09200 -8.11900  30.72300  1.000 78.12000  ? 484 LYS D C   1 
ATOM   14421 O  O   . LYS D  1 453 ? -30.05100 -7.59000  31.29800  1.000 76.40000  ? 484 LYS D O   1 
ATOM   14422 C  CB  . LYS D  1 453 ? -29.41100 -9.18700  28.46400  1.000 77.13000  ? 484 LYS D CB  1 
ATOM   14423 N  N   . GLU D  1 454 ? -28.19500 -8.86400  31.37600  1.000 73.91000  ? 485 GLU D N   1 
ATOM   14424 C  CA  . GLU D  1 454 ? -28.28000 -9.02000  32.82500  1.000 72.83000  ? 485 GLU D CA  1 
ATOM   14425 C  C   . GLU D  1 454 ? -28.18600 -7.66700  33.52300  1.000 77.13000  ? 485 GLU D C   1 
ATOM   14426 O  O   . GLU D  1 454 ? -29.02400 -7.32900  34.36600  1.000 84.00000  ? 485 GLU D O   1 
ATOM   14427 C  CB  . GLU D  1 454 ? -27.16700 -9.95100  33.31700  1.000 73.48000  ? 485 GLU D CB  1 
ATOM   14428 C  CG  . GLU D  1 454 ? -27.07200 -11.30100 32.60300  1.000 74.63000  ? 485 GLU D CG  1 
ATOM   14429 C  CD  . GLU D  1 454 ? -25.93300 -12.18800 33.12400  1.000 82.36000  ? 485 GLU D CD  1 
ATOM   14430 O  OE1 . GLU D  1 454 ? -24.99500 -11.66000 33.75800  1.000 83.67000  ? 485 GLU D OE1 1 
ATOM   14431 O  OE2 . GLU D  1 454 ? -25.95700 -13.41500 32.88100  1.000 81.56000  ? 485 GLU D OE2 1 
ATOM   14432 N  N   . LEU D  1 455 ? -27.19000 -6.85900  33.15300  1.000 73.40000  ? 486 LEU D N   1 
ATOM   14433 C  CA  . LEU D  1 455 ? -26.96800 -5.59600  33.85600  1.000 79.57000  ? 486 LEU D CA  1 
ATOM   14434 C  C   . LEU D  1 455 ? -28.12700 -4.62500  33.65900  1.000 73.33000  ? 486 LEU D C   1 
ATOM   14435 O  O   . LEU D  1 455 ? -28.47500 -3.88300  34.58100  1.000 80.03000  ? 486 LEU D O   1 
ATOM   14436 C  CB  . LEU D  1 455 ? -25.63200 -4.97300  33.42800  1.000 75.72000  ? 486 LEU D CB  1 
ATOM   14437 C  CG  . LEU D  1 455 ? -24.38200 -5.81800  33.74000  1.000 75.71000  ? 486 LEU D CG  1 
ATOM   14438 C  CD1 . LEU D  1 455 ? -23.11200 -5.21900  33.12900  1.000 69.00000  ? 486 LEU D CD1 1 
ATOM   14439 C  CD2 . LEU D  1 455 ? -24.21100 -6.07000  35.24400  1.000 65.76000  ? 486 LEU D CD2 1 
ATOM   14440 N  N   . TRP D  1 456 ? -28.72000 -4.58700  32.46600  1.000 72.98000  ? 487 TRP D N   1 
ATOM   14441 C  CA  . TRP D  1 456 ? -29.87600 -3.71600  32.25300  1.000 76.77000  ? 487 TRP D CA  1 
ATOM   14442 C  C   . TRP D  1 456 ? -31.12300 -4.25700  32.94200  1.000 77.79000  ? 487 TRP D C   1 
ATOM   14443 O  O   . TRP D  1 456 ? -31.97900 -3.47400  33.37400  1.000 73.68000  ? 487 TRP D O   1 
ATOM   14444 C  CB  . TRP D  1 456 ? -30.14800 -3.52200  30.76100  1.000 74.80000  ? 487 TRP D CB  1 
ATOM   14445 C  CG  . TRP D  1 456 ? -29.31600 -2.46000  30.09100  1.000 71.99000  ? 487 TRP D CG  1 
ATOM   14446 C  CD1 . TRP D  1 456 ? -28.06700 -2.60900  29.57500  1.000 66.08000  ? 487 TRP D CD1 1 
ATOM   14447 C  CD2 . TRP D  1 456 ? -29.70600 -1.09900  29.81800  1.000 67.13000  ? 487 TRP D CD2 1 
ATOM   14448 N  NE1 . TRP D  1 456 ? -27.63800 -1.41900  29.02900  1.000 71.09000  ? 487 TRP D NE1 1 
ATOM   14449 C  CE2 . TRP D  1 456 ? -28.62700 -0.47900  29.16200  1.000 67.71000  ? 487 TRP D CE2 1 
ATOM   14450 C  CE3 . TRP D  1 456 ? -30.84800 -0.34400  30.08800  1.000 68.86000  ? 487 TRP D CE3 1 
ATOM   14451 C  CZ2 . TRP D  1 456 ? -28.65800 0.86200   28.76300  1.000 65.35000  ? 487 TRP D CZ2 1 
ATOM   14452 C  CZ3 . TRP D  1 456 ? -30.87700 0.98800   29.69400  1.000 67.34000  ? 487 TRP D CZ3 1 
ATOM   14453 C  CH2 . TRP D  1 456 ? -29.79000 1.57500   29.03700  1.000 66.56000  ? 487 TRP D CH2 1 
ATOM   14454 N  N   . GLU D  1 457 ? -31.24000 -5.58400  33.05900  1.000 77.34000  ? 488 GLU D N   1 
ATOM   14455 C  CA  . GLU D  1 457 ? -32.43600 -6.17800  33.65100  1.000 85.01000  ? 488 GLU D CA  1 
ATOM   14456 C  C   . GLU D  1 457 ? -32.49900 -5.94700  35.15800  1.000 86.28000  ? 488 GLU D C   1 
ATOM   14457 O  O   . GLU D  1 457 ? -33.58500 -5.73500  35.71300  1.000 85.01000  ? 488 GLU D O   1 
ATOM   14458 C  CB  . GLU D  1 457 ? -32.48200 -7.67700  33.33800  1.000 80.14000  ? 488 GLU D CB  1 
ATOM   14459 N  N   . SER D  1 458 ? -31.35200 -6.00100  35.83900  1.000 84.35000  ? 489 SER D N   1 
ATOM   14460 C  CA  . SER D  1 458 ? -31.30600 -5.72900  37.27200  1.000 86.44000  ? 489 SER D CA  1 
ATOM   14461 C  C   . SER D  1 458 ? -31.28400 -4.24200  37.59400  1.000 84.69000  ? 489 SER D C   1 
ATOM   14462 O  O   . SER D  1 458 ? -31.41500 -3.88000  38.76700  1.000 89.23000  ? 489 SER D O   1 
ATOM   14463 C  CB  . SER D  1 458 ? -30.09000 -6.40800  37.90500  1.000 80.79000  ? 489 SER D CB  1 
ATOM   14464 O  OG  . SER D  1 458 ? -28.89900 -5.74700  37.52000  1.000 81.68000  ? 489 SER D OG  1 
ATOM   14465 N  N   . GLY D  1 459 ? -31.10800 -3.37900  36.59300  1.000 83.56000  ? 490 GLY D N   1 
ATOM   14466 C  CA  . GLY D  1 459 ? -30.98500 -1.95300  36.80300  1.000 83.51000  ? 490 GLY D CA  1 
ATOM   14467 C  C   . GLY D  1 459 ? -29.58000 -1.45500  37.08100  1.000 86.85000  ? 490 GLY D C   1 
ATOM   14468 O  O   . GLY D  1 459 ? -29.37200 -0.22900  37.08800  1.000 82.42000  ? 490 GLY D O   1 
ATOM   14469 N  N   . GLN D  1 460 ? -28.60500 -2.36300  37.27800  1.000 82.38000  ? 491 GLN D N   1 
ATOM   14470 C  CA  . GLN D  1 460 ? -27.20900 -1.95500  37.44000  1.000 77.62000  ? 491 GLN D CA  1 
ATOM   14471 C  C   . GLN D  1 460 ? -26.77800 -1.06400  36.28700  1.000 76.87000  ? 491 GLN D C   1 
ATOM   14472 O  O   . GLN D  1 460 ? -25.95100 -0.16500  36.46400  1.000 80.96000  ? 491 GLN D O   1 
ATOM   14473 C  CB  . GLN D  1 460 ? -26.30000 -3.18400  37.54600  1.000 75.11000  ? 491 GLN D CB  1 
ATOM   14474 N  N   . MET D  1 461 ? -27.34100 -1.29200  35.10900  1.000 80.66000  ? 492 MET D N   1 
ATOM   14475 C  CA  . MET D  1 461 ? -27.31200 -0.42000  33.95500  1.000 78.60000  ? 492 MET D CA  1 
ATOM   14476 C  C   . MET D  1 461 ? -28.71300 0.15000   33.73500  1.000 80.21000  ? 492 MET D C   1 
ATOM   14477 O  O   . MET D  1 461 ? -29.71400 -0.53100  33.99300  1.000 81.86000  ? 492 MET D O   1 
ATOM   14478 C  CB  . MET D  1 461 ? -26.86700 -1.17000  32.69300  1.000 72.18000  ? 492 MET D CB  1 
ATOM   14479 C  CG  . MET D  1 461 ? -25.39700 -1.55500  32.67600  1.000 76.35000  ? 492 MET D CG  1 
ATOM   14480 S  SD  . MET D  1 461 ? -24.34200 -0.10100  32.64600  1.000 77.12000  ? 492 MET D SD  1 
ATOM   14481 C  CE  . MET D  1 461 ? -24.40700 0.35900   30.91800  1.000 68.83000  ? 492 MET D CE  1 
ATOM   14482 N  N   . PRO D  1 462 ? -28.82800 1.39000   33.26400  1.000 76.61000  ? 493 PRO D N   1 
ATOM   14483 C  CA  . PRO D  1 462 ? -27.75500 2.30000   32.84400  1.000 77.01000  ? 493 PRO D CA  1 
ATOM   14484 C  C   . PRO D  1 462 ? -27.16000 3.06600   34.02100  1.000 78.24000  ? 493 PRO D C   1 
ATOM   14485 O  O   . PRO D  1 462 ? -26.03100 3.52400   33.91600  1.000 80.78000  ? 493 PRO D O   1 
ATOM   14486 C  CB  . PRO D  1 462 ? -28.47000 3.22900   31.85900  1.000 73.06000  ? 493 PRO D CB  1 
ATOM   14487 C  CG  . PRO D  1 462 ? -29.88500 3.29000   32.37300  1.000 68.97000  ? 493 PRO D CG  1 
ATOM   14488 C  CD  . PRO D  1 462 ? -30.16500 1.96500   33.03500  1.000 68.38000  ? 493 PRO D CD  1 
ATOM   14489 N  N   . ASN D  1 463 ? -27.91000 3.21700   35.11500  1.000 80.49000  ? 494 ASN D N   1 
ATOM   14490 C  CA  . ASN D  1 463 ? -27.48200 3.90500   36.34400  1.000 78.46000  ? 494 ASN D CA  1 
ATOM   14491 C  C   . ASN D  1 463 ? -26.76600 5.22400   36.04200  1.000 71.52000  ? 494 ASN D C   1 
ATOM   14492 O  O   . ASN D  1 463 ? -25.57700 5.40600   36.30700  1.000 73.53000  ? 494 ASN D O   1 
ATOM   14493 C  CB  . ASN D  1 463 ? -26.60700 3.00100   37.21400  1.000 82.56000  ? 494 ASN D CB  1 
ATOM   14494 C  CG  . ASN D  1 463 ? -26.48000 3.51700   38.64400  1.000 77.71000  ? 494 ASN D CG  1 
ATOM   14495 O  OD1 . ASN D  1 463 ? -26.82600 4.66500   38.93700  1.000 74.05000  ? 494 ASN D OD1 1 
ATOM   14496 N  ND2 . ASN D  1 463 ? -25.96800 2.67700   39.53500  1.000 79.27000  ? 494 ASN D ND2 1 
ATOM   14497 N  N   . TYR D  1 464 ? -27.51500 6.13500   35.43000  1.000 72.29000  ? 495 TYR D N   1 
ATOM   14498 C  CA  . TYR D  1 464 ? -26.97500 7.45500   35.13700  1.000 72.84000  ? 495 TYR D CA  1 
ATOM   14499 C  C   . TYR D  1 464 ? -26.61300 8.21900   36.41300  1.000 76.54000  ? 495 TYR D C   1 
ATOM   14500 O  O   . TYR D  1 464 ? -25.63600 8.98000   36.42600  1.000 72.90000  ? 495 TYR D O   1 
ATOM   14501 C  CB  . TYR D  1 464 ? -27.98200 8.22900   34.28600  1.000 70.14000  ? 495 TYR D CB  1 
ATOM   14502 C  CG  . TYR D  1 464 ? -28.33700 7.50800   32.99200  1.000 77.63000  ? 495 TYR D CG  1 
ATOM   14503 C  CD1 . TYR D  1 464 ? -27.36100 7.21800   32.03800  1.000 78.52000  ? 495 TYR D CD1 1 
ATOM   14504 C  CD2 . TYR D  1 464 ? -29.64000 7.10900   32.72500  1.000 78.55000  ? 495 TYR D CD2 1 
ATOM   14505 C  CE1 . TYR D  1 464 ? -27.67600 6.55200   30.85200  1.000 75.35000  ? 495 TYR D CE1 1 
ATOM   14506 C  CE2 . TYR D  1 464 ? -29.96600 6.44700   31.53600  1.000 76.14000  ? 495 TYR D CE2 1 
ATOM   14507 C  CZ  . TYR D  1 464 ? -28.97800 6.17100   30.60900  1.000 77.01000  ? 495 TYR D CZ  1 
ATOM   14508 O  OH  . TYR D  1 464 ? -29.29200 5.51000   29.44200  1.000 76.03000  ? 495 TYR D OH  1 
ATOM   14509 N  N   . GLU D  1 465 ? -27.33900 7.98300   37.51000  1.000 76.94000  ? 496 GLU D N   1 
ATOM   14510 C  CA  . GLU D  1 465 ? -27.09000 8.75500   38.72400  1.000 78.00000  ? 496 GLU D CA  1 
ATOM   14511 C  C   . GLU D  1 465 ? -25.65000 8.58300   39.18100  1.000 79.80000  ? 496 GLU D C   1 
ATOM   14512 O  O   . GLU D  1 465 ? -24.97100 9.56600   39.50400  1.000 79.23000  ? 496 GLU D O   1 
ATOM   14513 C  CB  . GLU D  1 465 ? -28.05800 8.33500   39.83700  1.000 71.27000  ? 496 GLU D CB  1 
ATOM   14514 N  N   . ALA D  1 466 ? -25.15600 7.34400   39.18300  1.000 77.19000  ? 497 ALA D N   1 
ATOM   14515 C  CA  . ALA D  1 466 ? -23.76400 7.11600   39.54100  1.000 75.75000  ? 497 ALA D CA  1 
ATOM   14516 C  C   . ALA D  1 466 ? -22.81700 7.75000   38.53200  1.000 77.07000  ? 497 ALA D C   1 
ATOM   14517 O  O   . ALA D  1 466 ? -21.74700 8.23500   38.91600  1.000 83.35000  ? 497 ALA D O   1 
ATOM   14518 C  CB  . ALA D  1 466 ? -23.49000 5.61900   39.64900  1.000 76.71000  ? 497 ALA D CB  1 
ATOM   14519 N  N   . THR D  1 467 ? -23.20200 7.77000   37.25200  1.000 70.85000  ? 498 THR D N   1 
ATOM   14520 C  CA  . THR D  1 467 ? -22.33900 8.31200   36.20800  1.000 74.50000  ? 498 THR D CA  1 
ATOM   14521 C  C   . THR D  1 467 ? -22.01100 9.77800   36.44100  1.000 72.62000  ? 498 THR D C   1 
ATOM   14522 O  O   . THR D  1 467 ? -20.89300 10.22300  36.15000  1.000 74.08000  ? 498 THR D O   1 
ATOM   14523 C  CB  . THR D  1 467 ? -23.00900 8.13600   34.83400  1.000 72.55000  ? 498 THR D CB  1 
ATOM   14524 O  OG1 . THR D  1 467 ? -23.00600 6.75000   34.46700  1.000 66.52000  ? 498 THR D OG1 1 
ATOM   14525 C  CG2 . THR D  1 467 ? -22.29700 8.95600   33.74400  1.000 64.16000  ? 498 THR D CG2 1 
ATOM   14526 N  N   . PHE D  1 468 ? -22.94700 10.54300  36.98300  1.000 70.33000  ? 499 PHE D N   1 
ATOM   14527 C  CA  . PHE D  1 468 ? -22.73400 11.97400  37.10400  1.000 77.18000  ? 499 PHE D CA  1 
ATOM   14528 C  C   . PHE D  1 468 ? -22.33600 12.40200  38.51000  1.000 73.98000  ? 499 PHE D C   1 
ATOM   14529 O  O   . PHE D  1 468 ? -22.31200 13.60200  38.79600  1.000 71.37000  ? 499 PHE D O   1 
ATOM   14530 C  CB  . PHE D  1 468 ? -23.97200 12.70600  36.61800  1.000 75.41000  ? 499 PHE D CB  1 
ATOM   14531 C  CG  . PHE D  1 468 ? -24.24000 12.48400  35.16500  1.000 78.63000  ? 499 PHE D CG  1 
ATOM   14532 C  CD1 . PHE D  1 468 ? -23.42400 13.06400  34.20800  1.000 76.20000  ? 499 PHE D CD1 1 
ATOM   14533 C  CD2 . PHE D  1 468 ? -25.28300 11.66500  34.75000  1.000 75.42000  ? 499 PHE D CD2 1 
ATOM   14534 C  CE1 . PHE D  1 468 ? -23.65900 12.85700  32.86200  1.000 78.57000  ? 499 PHE D CE1 1 
ATOM   14535 C  CE2 . PHE D  1 468 ? -25.52200 11.45100  33.40400  1.000 75.37000  ? 499 PHE D CE2 1 
ATOM   14536 C  CZ  . PHE D  1 468 ? -24.71000 12.04900  32.45900  1.000 75.48000  ? 499 PHE D CZ  1 
ATOM   14537 N  N   . GLU D  1 469 ? -22.01700 11.44700  39.38200  1.000 73.01000  ? 500 GLU D N   1 
ATOM   14538 C  CA  . GLU D  1 469 ? -21.29600 11.75600  40.60500  1.000 74.77000  ? 500 GLU D CA  1 
ATOM   14539 C  C   . GLU D  1 469 ? -19.97400 12.43400  40.26200  1.000 77.70000  ? 500 GLU D C   1 
ATOM   14540 O  O   . GLU D  1 469 ? -19.36700 12.16500  39.21900  1.000 77.24000  ? 500 GLU D O   1 
ATOM   14541 C  CB  . GLU D  1 469 ? -21.02800 10.47700  41.39700  1.000 73.79000  ? 500 GLU D CB  1 
ATOM   14542 C  CG  . GLU D  1 469 ? -22.25900 9.78700   41.95300  1.000 76.17000  ? 500 GLU D CG  1 
ATOM   14543 C  CD  . GLU D  1 469 ? -21.97500 8.35400   42.39100  1.000 76.79000  ? 500 GLU D CD  1 
ATOM   14544 O  OE1 . GLU D  1 469 ? -20.95100 7.78500   41.95700  1.000 79.04000  ? 500 GLU D OE1 1 
ATOM   14545 O  OE2 . GLU D  1 469 ? -22.76600 7.79800   43.17900  1.000 75.07000  ? 500 GLU D OE2 1 
ATOM   14546 N  N   . VAL D  1 470 ? -19.51900 13.32100  41.15200  1.000 80.84000  ? 501 VAL D N   1 
ATOM   14547 C  CA  . VAL D  1 470 ? -18.26000 14.03800  40.94600  1.000 77.74000  ? 501 VAL D CA  1 
ATOM   14548 C  C   . VAL D  1 470 ? -17.40200 13.99900  42.20500  1.000 79.67000  ? 501 VAL D C   1 
ATOM   14549 O  O   . VAL D  1 470 ? -16.29800 13.44100  42.20200  1.000 80.98000  ? 501 VAL D O   1 
ATOM   14550 C  CB  . VAL D  1 470 ? -18.51200 15.49200  40.50700  1.000 75.51000  ? 501 VAL D CB  1 
ATOM   14551 C  CG1 . VAL D  1 470 ? -17.19100 16.21000  40.29000  1.000 74.37000  ? 501 VAL D CG1 1 
ATOM   14552 C  CG2 . VAL D  1 470 ? -19.34000 15.51900  39.23000  1.000 74.02000  ? 501 VAL D CG2 1 
ATOM   14553 N  N   . ASP D  1 471 ? -17.90800 14.58100  43.29200  1.000 79.37000  ? 502 ASP D N   1 
ATOM   14554 C  CA  . ASP D  1 471 ? -17.08800 14.74600  44.48900  1.000 80.29000  ? 502 ASP D CA  1 
ATOM   14555 C  C   . ASP D  1 471 ? -16.74600 13.39900  45.10100  1.000 78.50000  ? 502 ASP D C   1 
ATOM   14556 O  O   . ASP D  1 471 ? -15.66100 13.22800  45.66800  1.000 80.31000  ? 502 ASP D O   1 
ATOM   14557 C  CB  . ASP D  1 471 ? -17.80000 15.65000  45.49500  1.000 78.49000  ? 502 ASP D CB  1 
ATOM   14558 C  CG  . ASP D  1 471 ? -18.01700 17.06000  44.95500  1.000 83.37000  ? 502 ASP D CG  1 
ATOM   14559 O  OD1 . ASP D  1 471 ? -17.29800 17.47700  44.00800  1.000 79.35000  ? 502 ASP D OD1 1 
ATOM   14560 O  OD2 . ASP D  1 471 ? -18.92900 17.74600  45.46200  1.000 91.21000  ? 502 ASP D OD2 1 
ATOM   14561 N  N   . LYS D  1 472 ? -17.66200 12.43900  45.00400  1.000 77.63000  ? 503 LYS D N   1 
ATOM   14562 C  CA  . LYS D  1 472 ? -17.44300 11.11400  45.56800  1.000 75.41000  ? 503 LYS D CA  1 
ATOM   14563 C  C   . LYS D  1 472 ? -16.23400 10.41900  44.94500  1.000 76.61000  ? 503 LYS D C   1 
ATOM   14564 O  O   . LYS D  1 472 ? -15.67600 9.49700   45.55000  1.000 75.50000  ? 503 LYS D O   1 
ATOM   14565 C  CB  . LYS D  1 472 ? -18.71000 10.28400  45.34300  1.000 80.41000  ? 503 LYS D CB  1 
ATOM   14566 C  CG  . LYS D  1 472 ? -18.77000 8.93300   46.02300  1.000 80.63000  ? 503 LYS D CG  1 
ATOM   14567 C  CD  . LYS D  1 472 ? -19.98600 8.11500   45.54600  1.000 79.75000  ? 503 LYS D CD  1 
ATOM   14568 C  CE  . LYS D  1 472 ? -21.31800 8.65800   46.04300  1.000 71.97000  ? 503 LYS D CE  1 
ATOM   14569 N  NZ  . LYS D  1 472 ? -21.81900 9.79100   45.22400  1.000 79.86000  ? 503 LYS D NZ  1 
ATOM   14570 N  N   . LEU D  1 473 ? -15.80700 10.85900  43.75500  1.000 79.75000  ? 504 LEU D N   1 
ATOM   14571 C  CA  . LEU D  1 473 ? -14.71400 10.20200  43.04700  1.000 76.68000  ? 504 LEU D CA  1 
ATOM   14572 C  C   . LEU D  1 473 ? -13.32600 10.61300  43.52900  1.000 79.67000  ? 504 LEU D C   1 
ATOM   14573 O  O   . LEU D  1 473 ? -12.38400 9.81500   43.43000  1.000 75.60000  ? 504 LEU D O   1 
ATOM   14574 C  CB  . LEU D  1 473 ? -14.82700 10.50200  41.55200  1.000 73.85000  ? 504 LEU D CB  1 
ATOM   14575 C  CG  . LEU D  1 473 ? -16.21300 10.26800  40.95200  1.000 75.72000  ? 504 LEU D CG  1 
ATOM   14576 C  CD1 . LEU D  1 473 ? -16.24100 10.70100  39.48500  1.000 70.91000  ? 504 LEU D CD1 1 
ATOM   14577 C  CD2 . LEU D  1 473 ? -16.66600 8.80700   41.13000  1.000 71.84000  ? 504 LEU D CD2 1 
ATOM   14578 N  N   . VAL D  1 474 ? -13.17600 11.82200  44.06600  1.000 82.74000  ? 505 VAL D N   1 
ATOM   14579 C  CA  . VAL D  1 474 ? -11.85400 12.35300  44.38300  1.000 81.13000  ? 505 VAL D CA  1 
ATOM   14580 C  C   . VAL D  1 474 ? -11.64400 12.62800  45.86700  1.000 72.51000  ? 505 VAL D C   1 
ATOM   14581 O  O   . VAL D  1 474 ? -10.48900 12.69700  46.31400  1.000 72.36000  ? 505 VAL D O   1 
ATOM   14582 C  CB  . VAL D  1 474 ? -11.57300 13.63000  43.56500  1.000 76.73000  ? 505 VAL D CB  1 
ATOM   14583 C  CG1 . VAL D  1 474 ? -11.76800 13.34900  42.07400  1.000 65.31000  ? 505 VAL D CG1 1 
ATOM   14584 C  CG2 . VAL D  1 474 ? -12.48200 14.75400  44.03100  1.000 77.37000  ? 505 VAL D CG2 1 
ATOM   14585 N  N   . ASP D  1 475 ? -12.69100 12.78300  46.65600  1.000 73.89000  ? 506 ASP D N   1 
ATOM   14586 C  CA  . ASP D  1 475 ? -12.51800 13.15900  48.04600  1.000 75.66000  ? 506 ASP D CA  1 
ATOM   14587 C  C   . ASP D  1 475 ? -12.03700 11.97600  48.87200  1.000 78.84000  ? 506 ASP D C   1 
ATOM   14588 O  O   . ASP D  1 475 ? -12.47500 10.83600  48.68400  1.000 77.40000  ? 506 ASP D O   1 
ATOM   14589 C  CB  . ASP D  1 475 ? -13.82000 13.73200  48.60000  1.000 76.29000  ? 506 ASP D CB  1 
ATOM   14590 C  CG  . ASP D  1 475 ? -14.14900 15.08200  47.98900  1.000 80.13000  ? 506 ASP D CG  1 
ATOM   14591 O  OD1 . ASP D  1 475 ? -13.19100 15.76700  47.55800  1.000 81.58000  ? 506 ASP D OD1 1 
ATOM   14592 O  OD2 . ASP D  1 475 ? -15.34600 15.44700  47.91600  1.000 79.17000  ? 506 ASP D OD2 1 
ATOM   14593 N  N   . SER D  1 476 ? -11.13400 12.25300  49.78000  1.000 73.92000  ? 507 SER D N   1 
ATOM   14594 C  CA  . SER D  1 476 ? -10.71000 11.17300  50.64200  1.000 78.42000  ? 507 SER D CA  1 
ATOM   14595 C  C   . SER D  1 476 ? -11.77000 10.92300  51.70900  1.000 79.20000  ? 507 SER D C   1 
ATOM   14596 O  O   . SER D  1 476 ? -12.42000 11.86300  52.17200  1.000 80.23000  ? 507 SER D O   1 
ATOM   14597 C  CB  . SER D  1 476 ? -9.36900  11.50400  51.29700  1.000 74.83000  ? 507 SER D CB  1 
ATOM   14598 O  OG  . SER D  1 476 ? -9.09500  10.61800  52.36700  1.000 78.34000  ? 507 SER D OG  1 
ATOM   14599 N  N   . PRO D  1 477 ? -11.99400 9.66300   52.07900  1.000 79.47000  ? 508 PRO D N   1 
ATOM   14600 C  CA  . PRO D  1 477 ? -12.91900 9.34800   53.17100  1.000 79.58000  ? 508 PRO D CA  1 
ATOM   14601 C  C   . PRO D  1 477 ? -12.34000 9.56700   54.56200  1.000 84.36000  ? 508 PRO D C   1 
ATOM   14602 O  O   . PRO D  1 477 ? -12.92600 9.08100   55.53300  1.000 86.47000  ? 508 PRO D O   1 
ATOM   14603 C  CB  . PRO D  1 477 ? -13.23300 7.86300   52.93800  1.000 78.42000  ? 508 PRO D CB  1 
ATOM   14604 C  CG  . PRO D  1 477 ? -12.07600 7.33100   52.19000  1.000 80.22000  ? 508 PRO D CG  1 
ATOM   14605 C  CD  . PRO D  1 477 ? -11.43300 8.45900   51.44400  1.000 79.22000  ? 508 PRO D CD  1 
ATOM   14606 N  N   . TYR D  1 478 ? -11.18700 10.22700  54.67400  1.000 82.90000  ? 509 TYR D N   1 
ATOM   14607 C  CA  . TYR D  1 478 ? -10.51900 10.42800  55.95500  1.000 82.57000  ? 509 TYR D CA  1 
ATOM   14608 C  C   . TYR D  1 478 ? -10.30900 11.91300  56.25900  1.000 79.47000  ? 509 TYR D C   1 
ATOM   14609 O  O   . TYR D  1 478 ? -10.07900 12.71900  55.35300  1.000 78.86000  ? 509 TYR D O   1 
ATOM   14610 C  CB  . TYR D  1 478 ? -9.17800  9.68800   55.96000  1.000 84.53000  ? 509 TYR D CB  1 
ATOM   14611 C  CG  . TYR D  1 478 ? -9.25400  8.29900   55.36300  1.000 82.91000  ? 509 TYR D CG  1 
ATOM   14612 C  CD1 . TYR D  1 478 ? -9.79200  7.23600   56.08500  1.000 79.41000  ? 509 TYR D CD1 1 
ATOM   14613 C  CD2 . TYR D  1 478 ? -8.82000  8.05700   54.06300  1.000 81.34000  ? 509 TYR D CD2 1 
ATOM   14614 C  CE1 . TYR D  1 478 ? -9.87600  5.96300   55.53400  1.000 82.39000  ? 509 TYR D CE1 1 
ATOM   14615 C  CE2 . TYR D  1 478 ? -8.90100  6.79100   53.50200  1.000 83.13000  ? 509 TYR D CE2 1 
ATOM   14616 C  CZ  . TYR D  1 478 ? -9.43100  5.74900   54.23900  1.000 85.12000  ? 509 TYR D CZ  1 
ATOM   14617 O  OH  . TYR D  1 478 ? -9.51100  4.49000   53.68200  1.000 86.20000  ? 509 TYR D OH  1 
HETATM 14618 BR BR  . BR  E  2 .   ? -23.36400 -31.19600 -44.09800 0.870 44.93000  ? 601 BR  A BR  1 
HETATM 14619 BR BR  . BR  F  2 .   ? -31.75800 -55.07100 -40.18600 0.800 48.19000  ? 602 BR  A BR  1 
HETATM 14620 CL CL  . CL  G  3 .   ? -19.02900 -29.80500 -47.80000 1.000 40.51000  ? 603 CL  A CL  1 
HETATM 14621 CL CL  . CL  H  3 .   ? -9.16100  -41.46800 -17.00200 1.000 39.39000  ? 604 CL  A CL  1 
HETATM 14622 CL CL  . CL  I  3 .   ? -9.08300  -33.49800 -41.94300 1.000 49.44000  ? 605 CL  A CL  1 
HETATM 14623 CL CL  . CL  J  3 .   ? -10.91300 -47.55000 -6.51200  1.000 42.94000  ? 606 CL  A CL  1 
HETATM 14624 CL CL  . CL  K  3 .   ? -8.25200  -68.63800 -7.56700  1.000 50.96000  ? 607 CL  A CL  1 
HETATM 14625 CL CL  . CL  L  3 .   ? -51.83600 -34.82300 -27.77100 1.000 43.60000  ? 608 CL  A CL  1 
HETATM 14626 CL CL  . CL  M  3 .   ? -10.07800 -39.29700 -22.27400 1.000 53.84000  ? 609 CL  A CL  1 
HETATM 14627 CL CL  . CL  N  3 .   ? -22.51000 -65.05900 1.79600   1.000 71.89000  ? 610 CL  A CL  1 
HETATM 14628 CL CL  . CL  O  3 .   ? -9.75000  -61.06200 -34.10000 1.000 77.87000  ? 611 CL  A CL  1 
HETATM 14629 CA CA  . CA  P  4 .   ? -20.88500 -42.61300 -26.25000 1.000 52.08000  ? 612 CA  A CA  1 
HETATM 14630 BR BR  . BR  Q  2 .   ? -0.74900  -51.26300 23.78000  0.790 51.45000  ? 601 BR  B BR  1 
HETATM 14631 BR BR  . BR  R  2 .   ? 20.29800  -49.56600 9.13500   0.880 49.43000  ? 602 BR  B BR  1 
HETATM 14632 BR BR  . BR  S  2 .   ? 13.22600  -21.43000 20.16500  0.820 60.75000  ? 603 BR  B BR  1 
HETATM 14633 BR BR  . BR  T  2 .   ? -10.27400 -49.64500 -1.34100  1.000 96.63000  ? 604 BR  B BR  1 
HETATM 14634 CL CL  . CL  U  3 .   ? 5.02100   -50.55200 -30.20000 1.000 41.71000  ? 605 CL  B CL  1 
HETATM 14635 CL CL  . CL  V  3 .   ? -8.15600  -61.06700 15.43800  1.000 61.22000  ? 606 CL  B CL  1 
HETATM 14636 CL CL  . CL  W  3 .   ? 7.50900   -33.27000 -29.99000 1.000 63.16000  ? 607 CL  B CL  1 
HETATM 14637 CL CL  . CL  X  3 .   ? 10.03100  -63.42600 -6.96700  1.000 84.76000  ? 608 CL  B CL  1 
HETATM 14638 CL CL  . CL  Y  3 .   ? 16.05500  -15.89100 8.32200   1.000 85.87000  ? 609 CL  B CL  1 
HETATM 14639 CA CA  . CA  Z  4 .   ? 0.11800   -45.08000 3.18900   1.000 51.71000  ? 610 CA  B CA  1 
HETATM 14640 BR BR  . BR  AA 2 .   ? 22.49300  -3.79100  -15.11300 0.850 73.36000  ? 601 BR  C BR  1 
HETATM 14641 BR BR  . BR  BA 2 .   ? 26.41400  20.62000  -21.54100 0.830 71.91000  ? 602 BR  C BR  1 
HETATM 14642 CL CL  . CL  CA 3 .   ? 48.44400  -1.79200  -31.81800 1.000 62.68000  ? 603 CL  C CL  1 
HETATM 14643 CL CL  . CL  DA 3 .   ? -7.23700  -16.66200 -42.16500 1.000 70.16000  ? 604 CL  C CL  1 
HETATM 14644 CL CL  . CL  EA 3 .   ? 9.24300   11.98600  -39.93200 1.000 79.45000  ? 605 CL  C CL  1 
HETATM 14645 CL CL  . CL  FA 3 .   ? 13.07600  25.25000  -26.25800 1.000 80.43000  ? 606 CL  C CL  1 
HETATM 14646 CL CL  . CL  GA 3 .   ? 8.54900   5.66500   -36.39700 1.000 83.05000  ? 607 CL  C CL  1 
HETATM 14647 CA CA  . CA  HA 4 .   ? 17.45400  5.65400   -33.88600 1.000 70.60000  ? 608 CA  C CA  1 
HETATM 14648 BR BR  . BR  IA 2 .   ? -21.12200 -11.04800 -4.50400  1.000 72.27000  ? 601 BR  D BR  1 
HETATM 14649 BR BR  . BR  JA 2 .   ? -37.34700 5.60200   6.20100   0.850 70.62000  ? 602 BR  D BR  1 
HETATM 14650 CL CL  . CL  KA 3 .   ? -9.59300  -4.57800  18.95500  1.000 65.33000  ? 603 CL  D CL  1 
HETATM 14651 CL CL  . CL  LA 3 .   ? -20.84100 12.71400  44.54500  1.000 72.75000  ? 604 CL  D CL  1 
HETATM 14652 CL CL  . CL  MA 3 .   ? -14.24300 28.61000  36.07100  1.000 84.06000  ? 605 CL  D CL  1 
HETATM 14653 CL CL  . CL  NA 3 .   ? -5.38200  8.73400   30.35400  1.000 65.11000  ? 606 CL  D CL  1 
HETATM 14654 CL CL  . CL  OA 3 .   ? -18.95000 20.43300  -13.79000 1.000 68.81000  ? 607 CL  D CL  1 
HETATM 14655 CL CL  . CL  PA 3 .   ? -32.83100 -5.26700  27.97400  1.000 85.28000  ? 608 CL  D CL  1 
HETATM 14656 CA CA  . CA  QA 4 .   ? -16.90800 1.99000   11.85700  1.000 67.57000  ? 609 CA  D CA  1 
HETATM 14657 O  O   . HOH RA 5 .   ? -34.24300 -39.27600 -40.74100 1.000 43.01000  ? 701 HOH A O   1 
HETATM 14658 O  O   . HOH RA 5 .   ? -19.06800 -39.74000 -8.23100  1.000 34.61000  ? 702 HOH A O   1 
HETATM 14659 O  O   . HOH RA 5 .   ? -11.48900 -30.81600 -19.41800 1.000 47.52000  ? 703 HOH A O   1 
HETATM 14660 O  O   . HOH RA 5 .   ? -12.61000 -24.21400 -47.70600 1.000 45.51000  ? 704 HOH A O   1 
HETATM 14661 O  O   . HOH RA 5 .   ? -10.85500 -67.94000 -22.89700 1.000 48.65000  ? 705 HOH A O   1 
HETATM 14662 O  O   . HOH RA 5 .   ? -23.92500 -19.09300 -15.25600 1.000 58.35000  ? 706 HOH A O   1 
HETATM 14663 O  O   . HOH RA 5 .   ? -25.39300 -53.86900 -18.50800 1.000 37.48000  ? 707 HOH A O   1 
HETATM 14664 O  O   . HOH RA 5 .   ? -23.87100 -42.60300 -47.94400 1.000 49.00000  ? 708 HOH A O   1 
HETATM 14665 O  O   . HOH RA 5 .   ? -15.30100 -44.71900 -43.14200 1.000 54.81000  ? 709 HOH A O   1 
HETATM 14666 O  O   . HOH RA 5 .   ? -49.08700 -51.27200 -23.53400 1.000 56.70000  ? 710 HOH A O   1 
HETATM 14667 O  O   . HOH RA 5 .   ? -21.58500 -25.79500 -50.46500 1.000 61.47000  ? 711 HOH A O   1 
HETATM 14668 O  O   . HOH RA 5 .   ? -25.26100 -51.56000 -39.28400 1.000 42.39000  ? 712 HOH A O   1 
HETATM 14669 O  O   . HOH RA 5 .   ? -8.00800  -65.85600 -28.34100 1.000 56.51000  ? 713 HOH A O   1 
HETATM 14670 O  O   . HOH RA 5 .   ? -14.93600 -54.00500 -25.35000 1.000 39.23000  ? 714 HOH A O   1 
HETATM 14671 O  O   . HOH RA 5 .   ? -31.39700 -28.06000 -30.71600 1.000 37.83000  ? 715 HOH A O   1 
HETATM 14672 O  O   . HOH RA 5 .   ? -26.73400 -38.12400 -9.54800  1.000 46.00000  ? 716 HOH A O   1 
HETATM 14673 O  O   . HOH RA 5 .   ? -23.91500 -31.68300 -47.18500 1.000 41.67000  ? 717 HOH A O   1 
HETATM 14674 O  O   . HOH RA 5 .   ? -22.12000 -40.53300 -45.78300 1.000 45.88000  ? 718 HOH A O   1 
HETATM 14675 O  O   . HOH RA 5 .   ? -17.34700 -40.52700 -11.61200 1.000 34.67000  ? 719 HOH A O   1 
HETATM 14676 O  O   . HOH RA 5 .   ? -4.75900  -68.74900 -3.46000  1.000 47.23000  ? 720 HOH A O   1 
HETATM 14677 O  O   . HOH RA 5 .   ? -28.37900 -64.13100 -27.35300 1.000 52.69000  ? 721 HOH A O   1 
HETATM 14678 O  O   . HOH RA 5 .   ? -8.17900  -55.79500 -25.95700 1.000 46.68000  ? 722 HOH A O   1 
HETATM 14679 O  O   . HOH RA 5 .   ? -33.31400 -57.55400 -25.90800 1.000 37.33000  ? 723 HOH A O   1 
HETATM 14680 O  O   . HOH RA 5 .   ? -32.74900 -28.51500 -14.96100 1.000 39.02000  ? 724 HOH A O   1 
HETATM 14681 O  O   . HOH RA 5 .   ? -25.20000 -29.60900 -28.66800 1.000 31.90000  ? 725 HOH A O   1 
HETATM 14682 O  O   . HOH RA 5 .   ? -26.46300 -40.57300 -29.59500 1.000 39.41000  ? 726 HOH A O   1 
HETATM 14683 O  O   . HOH RA 5 .   ? -34.41800 -48.32400 -12.59600 1.000 43.40000  ? 727 HOH A O   1 
HETATM 14684 O  O   . HOH RA 5 .   ? -8.39500  -51.57600 -27.26800 1.000 48.48000  ? 728 HOH A O   1 
HETATM 14685 O  O   . HOH RA 5 .   ? -11.94200 -44.83400 -13.43000 1.000 39.38000  ? 729 HOH A O   1 
HETATM 14686 O  O   . HOH RA 5 .   ? -20.13300 -46.40400 -8.59300  1.000 35.75000  ? 730 HOH A O   1 
HETATM 14687 O  O   . HOH RA 5 .   ? -17.96100 -35.08500 -23.64400 1.000 32.87000  ? 731 HOH A O   1 
HETATM 14688 O  O   . HOH RA 5 .   ? -51.79100 -37.17800 -28.54200 1.000 51.89000  ? 732 HOH A O   1 
HETATM 14689 O  O   . HOH RA 5 .   ? -6.39300  -63.15200 -12.81100 1.000 42.47000  ? 733 HOH A O   1 
HETATM 14690 O  O   . HOH RA 5 .   ? -17.29800 -39.72200 -37.91700 1.000 44.70000  ? 734 HOH A O   1 
HETATM 14691 O  O   . HOH RA 5 .   ? -32.20200 -53.35500 -6.01900  1.000 42.09000  ? 735 HOH A O   1 
HETATM 14692 O  O   . HOH RA 5 .   ? -11.60100 -60.38700 -3.97600  1.000 49.16000  ? 736 HOH A O   1 
HETATM 14693 O  O   . HOH RA 5 .   ? -11.60700 -51.19400 -35.05000 1.000 38.14000  ? 737 HOH A O   1 
HETATM 14694 O  O   . HOH RA 5 .   ? -44.86300 -38.42700 -24.92600 1.000 39.08000  ? 738 HOH A O   1 
HETATM 14695 O  O   . HOH RA 5 .   ? -17.36900 -46.10400 -39.37000 1.000 41.05000  ? 739 HOH A O   1 
HETATM 14696 O  O   . HOH RA 5 .   ? -10.57600 -55.96300 -14.33400 1.000 39.55000  ? 740 HOH A O   1 
HETATM 14697 O  O   . HOH RA 5 .   ? -24.87800 -56.19200 -30.00600 1.000 43.06000  ? 741 HOH A O   1 
HETATM 14698 O  O   . HOH RA 5 .   ? -12.16700 -38.49400 -37.68900 1.000 43.83000  ? 742 HOH A O   1 
HETATM 14699 O  O   . HOH RA 5 .   ? -11.60500 -69.45900 -13.35400 1.000 60.75000  ? 743 HOH A O   1 
HETATM 14700 O  O   . HOH RA 5 .   ? -4.04200  -55.37700 -11.08900 1.000 34.94000  ? 744 HOH A O   1 
HETATM 14701 O  O   . HOH RA 5 .   ? -35.69200 -36.61700 -9.63600  1.000 39.87000  ? 745 HOH A O   1 
HETATM 14702 O  O   . HOH RA 5 .   ? -34.03500 -25.71100 -23.16600 1.000 48.58000  ? 746 HOH A O   1 
HETATM 14703 O  O   . HOH RA 5 .   ? -10.73600 -44.33300 -34.04400 1.000 47.12000  ? 747 HOH A O   1 
HETATM 14704 O  O   . HOH RA 5 .   ? -26.00400 -33.31800 -31.32700 1.000 29.60000  ? 748 HOH A O   1 
HETATM 14705 O  O   . HOH RA 5 .   ? -20.22200 -38.30300 -31.22400 1.000 39.16000  ? 749 HOH A O   1 
HETATM 14706 O  O   . HOH RA 5 .   ? -20.50500 -54.90600 -21.79800 1.000 43.39000  ? 750 HOH A O   1 
HETATM 14707 O  O   . HOH RA 5 .   ? -32.32800 -41.52200 -14.58600 1.000 37.49000  ? 751 HOH A O   1 
HETATM 14708 O  O   . HOH RA 5 .   ? -28.85300 -59.19200 -18.71600 1.000 39.33000  ? 752 HOH A O   1 
HETATM 14709 O  O   . HOH RA 5 .   ? -41.06800 -38.88600 -12.35800 1.000 40.38000  ? 753 HOH A O   1 
HETATM 14710 O  O   . HOH RA 5 .   ? -32.86800 -53.01600 -26.90600 1.000 43.12000  ? 754 HOH A O   1 
HETATM 14711 O  O   . HOH RA 5 .   ? -15.89300 -42.77000 -36.74600 1.000 40.55000  ? 755 HOH A O   1 
HETATM 14712 O  O   . HOH RA 5 .   ? -31.51100 -57.99000 -10.56400 1.000 49.81000  ? 756 HOH A O   1 
HETATM 14713 O  O   . HOH RA 5 .   ? -19.03900 -51.77100 -32.03000 1.000 39.62000  ? 757 HOH A O   1 
HETATM 14714 O  O   . HOH RA 5 .   ? -12.28600 -46.36400 -19.08300 1.000 37.83000  ? 758 HOH A O   1 
HETATM 14715 O  O   . HOH RA 5 .   ? -26.63700 -50.38700 -24.68500 1.000 36.90000  ? 759 HOH A O   1 
HETATM 14716 O  O   . HOH RA 5 .   ? 2.20200   -61.93400 0.78500   1.000 55.08000  ? 760 HOH A O   1 
HETATM 14717 O  O   . HOH RA 5 .   ? -18.68200 -37.02900 -21.73600 1.000 36.34000  ? 761 HOH A O   1 
HETATM 14718 O  O   . HOH RA 5 .   ? -38.93500 -58.32300 -39.55200 1.000 37.37000  ? 762 HOH A O   1 
HETATM 14719 O  O   . HOH RA 5 .   ? -26.04600 -44.94000 -33.21900 1.000 41.43000  ? 763 HOH A O   1 
HETATM 14720 O  O   . HOH RA 5 .   ? -34.33000 -51.30200 -44.72500 1.000 49.40000  ? 764 HOH A O   1 
HETATM 14721 O  O   . HOH RA 5 .   ? -29.09800 -19.71500 -16.86700 1.000 63.14000  ? 765 HOH A O   1 
HETATM 14722 O  O   . HOH RA 5 .   ? -28.23400 -22.85000 -34.83700 1.000 47.79000  ? 766 HOH A O   1 
HETATM 14723 O  O   . HOH RA 5 .   ? -42.21900 -58.25600 -27.07200 1.000 60.37000  ? 767 HOH A O   1 
HETATM 14724 O  O   . HOH RA 5 .   ? -35.84200 -43.27600 -6.25200  1.000 46.44000  ? 768 HOH A O   1 
HETATM 14725 O  O   . HOH RA 5 .   ? -10.47200 -61.47100 -5.78600  1.000 42.40000  ? 769 HOH A O   1 
HETATM 14726 O  O   . HOH RA 5 .   ? -21.53700 -44.78500 -1.94300  1.000 50.07000  ? 770 HOH A O   1 
HETATM 14727 O  O   . HOH RA 5 .   ? -19.94000 -46.75200 -39.01200 1.000 44.67000  ? 771 HOH A O   1 
HETATM 14728 O  O   . HOH RA 5 .   ? -24.69700 -46.94600 -49.13000 1.000 55.67000  ? 772 HOH A O   1 
HETATM 14729 O  O   . HOH RA 5 .   ? -9.33000  -51.08200 -15.88800 1.000 36.17000  ? 773 HOH A O   1 
HETATM 14730 O  O   . HOH RA 5 .   ? -11.63400 -54.96000 -8.92100  1.000 41.59000  ? 774 HOH A O   1 
HETATM 14731 O  O   . HOH RA 5 .   ? -30.36200 -44.88700 -13.82600 1.000 36.38000  ? 775 HOH A O   1 
HETATM 14732 O  O   . HOH RA 5 .   ? -16.40300 -42.27700 -29.14300 1.000 49.54000  ? 776 HOH A O   1 
HETATM 14733 O  O   . HOH RA 5 .   ? -12.53700 -33.01600 -34.47800 1.000 50.84000  ? 777 HOH A O   1 
HETATM 14734 O  O   . HOH RA 5 .   ? -16.78700 -60.90900 -28.16700 1.000 53.36000  ? 778 HOH A O   1 
HETATM 14735 O  O   . HOH RA 5 .   ? -20.34800 -58.03300 -40.06600 1.000 52.47000  ? 779 HOH A O   1 
HETATM 14736 O  O   . HOH RA 5 .   ? -8.86000  -51.08400 -23.93500 1.000 46.62000  ? 780 HOH A O   1 
HETATM 14737 O  O   . HOH RA 5 .   ? -30.38600 -49.83000 -5.99600  1.000 42.39000  ? 781 HOH A O   1 
HETATM 14738 O  O   . HOH RA 5 .   ? -10.25700 -46.10500 -16.29600 1.000 50.77000  ? 782 HOH A O   1 
HETATM 14739 O  O   . HOH RA 5 .   ? -30.58100 -63.57900 -33.43900 1.000 57.09000  ? 783 HOH A O   1 
HETATM 14740 O  O   . HOH RA 5 .   ? -23.20300 -47.48300 -44.09100 1.000 40.74000  ? 784 HOH A O   1 
HETATM 14741 O  O   . HOH RA 5 .   ? -14.77300 -39.19300 -24.91800 1.000 41.03000  ? 785 HOH A O   1 
HETATM 14742 O  O   . HOH RA 5 .   ? -19.15600 -35.72700 -31.90600 1.000 39.34000  ? 786 HOH A O   1 
HETATM 14743 O  O   . HOH RA 5 .   ? -35.21900 -55.62600 -11.90700 1.000 47.29000  ? 787 HOH A O   1 
HETATM 14744 O  O   . HOH RA 5 .   ? -37.20800 -25.08100 -26.51000 1.000 46.13000  ? 788 HOH A O   1 
HETATM 14745 O  O   . HOH RA 5 .   ? -15.83200 -56.18300 -32.07000 1.000 44.30000  ? 789 HOH A O   1 
HETATM 14746 O  O   . HOH RA 5 .   ? -12.96200 -45.13500 -30.21300 1.000 53.40000  ? 790 HOH A O   1 
HETATM 14747 O  O   . HOH RA 5 .   ? -6.94200  -34.75000 -41.74700 1.000 52.55000  ? 791 HOH A O   1 
HETATM 14748 O  O   . HOH RA 5 .   ? -15.60200 -41.32600 -32.32500 1.000 42.63000  ? 792 HOH A O   1 
HETATM 14749 O  O   . HOH RA 5 .   ? -31.03400 -31.95100 -46.65600 1.000 57.39000  ? 793 HOH A O   1 
HETATM 14750 O  O   . HOH RA 5 .   ? -17.10800 -27.33600 -36.00300 1.000 37.79000  ? 794 HOH A O   1 
HETATM 14751 O  O   . HOH RA 5 .   ? -17.78100 -38.03400 -12.17800 1.000 42.34000  ? 795 HOH A O   1 
HETATM 14752 O  O   . HOH RA 5 .   ? -17.52800 -23.64000 -28.29300 1.000 43.61000  ? 796 HOH A O   1 
HETATM 14753 O  O   . HOH RA 5 .   ? -17.02700 -36.98400 -25.02300 1.000 36.07000  ? 797 HOH A O   1 
HETATM 14754 O  O   . HOH RA 5 .   ? -12.93100 -27.67200 -31.03300 1.000 37.22000  ? 798 HOH A O   1 
HETATM 14755 O  O   . HOH RA 5 .   ? -10.33600 -54.54000 -5.41800  1.000 46.11000  ? 799 HOH A O   1 
HETATM 14756 O  O   . HOH RA 5 .   ? -41.23800 -43.21400 -46.61200 1.000 36.80000  ? 800 HOH A O   1 
HETATM 14757 O  O   . HOH RA 5 .   ? -28.13400 -48.34000 -6.50500  1.000 42.70000  ? 801 HOH A O   1 
HETATM 14758 O  O   . HOH RA 5 .   ? -21.57900 -38.15200 -46.82100 1.000 52.13000  ? 802 HOH A O   1 
HETATM 14759 O  O   . HOH RA 5 .   ? -22.59500 -42.49800 -15.62000 1.000 37.09000  ? 803 HOH A O   1 
HETATM 14760 O  O   . HOH RA 5 .   ? -14.29600 -41.89500 -9.73200  1.000 37.43000  ? 804 HOH A O   1 
HETATM 14761 O  O   . HOH RA 5 .   ? -42.48000 -58.58100 -30.04600 1.000 58.12000  ? 805 HOH A O   1 
HETATM 14762 O  O   . HOH RA 5 .   ? -17.39600 -43.27200 -5.50300  1.000 34.76000  ? 806 HOH A O   1 
HETATM 14763 O  O   . HOH RA 5 .   ? -29.13900 -16.40500 -23.51300 1.000 61.16000  ? 807 HOH A O   1 
HETATM 14764 O  O   . HOH RA 5 .   ? -18.32000 -30.86300 -44.87000 1.000 36.78000  ? 808 HOH A O   1 
HETATM 14765 O  O   . HOH RA 5 .   ? -16.18200 -44.74600 -27.46100 1.000 41.36000  ? 809 HOH A O   1 
HETATM 14766 O  O   . HOH RA 5 .   ? -17.11000 -54.49000 -51.58400 1.000 48.28000  ? 810 HOH A O   1 
HETATM 14767 O  O   . HOH RA 5 .   ? -22.48800 -22.90200 -38.68900 1.000 22.60000  ? 811 HOH A O   1 
HETATM 14768 O  O   . HOH RA 5 .   ? -11.08500 -38.68500 -34.95800 1.000 57.57000  ? 812 HOH A O   1 
HETATM 14769 O  O   . HOH RA 5 .   ? -18.65000 -49.36200 -33.59900 1.000 37.22000  ? 813 HOH A O   1 
HETATM 14770 O  O   . HOH RA 5 .   ? -12.82300 -50.27100 -28.84900 1.000 39.53000  ? 814 HOH A O   1 
HETATM 14771 O  O   . HOH RA 5 .   ? -33.61200 -51.32000 -6.06100  1.000 54.56000  ? 815 HOH A O   1 
HETATM 14772 O  O   . HOH RA 5 .   ? -33.67200 -59.70100 -6.75100  1.000 60.29000  ? 816 HOH A O   1 
HETATM 14773 O  O   . HOH RA 5 .   ? -30.55100 -29.60500 -44.37400 1.000 52.35000  ? 817 HOH A O   1 
HETATM 14774 O  O   . HOH RA 5 .   ? -12.65900 -19.51300 -19.13300 1.000 55.82000  ? 818 HOH A O   1 
HETATM 14775 O  O   . HOH RA 5 .   ? -24.57500 -41.62200 -17.25300 1.000 35.79000  ? 819 HOH A O   1 
HETATM 14776 O  O   . HOH RA 5 .   ? -46.07600 -33.90800 -19.89000 1.000 52.88000  ? 820 HOH A O   1 
HETATM 14777 O  O   . HOH RA 5 .   ? -18.47100 -17.27300 -11.33500 1.000 64.33000  ? 821 HOH A O   1 
HETATM 14778 O  O   . HOH RA 5 .   ? -3.45400  -54.90200 -4.72100  1.000 58.21000  ? 822 HOH A O   1 
HETATM 14779 O  O   . HOH RA 5 .   ? -26.02200 -45.47600 -1.81100  1.000 43.45000  ? 823 HOH A O   1 
HETATM 14780 O  O   . HOH RA 5 .   ? -12.97500 -57.56400 1.26600   1.000 45.56000  ? 824 HOH A O   1 
HETATM 14781 O  O   . HOH RA 5 .   ? -22.64000 -58.88000 -42.48600 1.000 52.88000  ? 825 HOH A O   1 
HETATM 14782 O  O   . HOH RA 5 .   ? -13.71400 -70.31100 -11.45300 1.000 57.21000  ? 826 HOH A O   1 
HETATM 14783 O  O   . HOH RA 5 .   ? -6.42600  -62.19400 -15.09700 1.000 53.90000  ? 827 HOH A O   1 
HETATM 14784 O  O   . HOH RA 5 .   ? -26.12500 -22.19800 -36.00900 1.000 45.20000  ? 828 HOH A O   1 
HETATM 14785 O  O   . HOH RA 5 .   ? -26.07300 -66.33000 -0.70700  1.000 70.54000  ? 829 HOH A O   1 
HETATM 14786 O  O   . HOH RA 5 .   ? -24.39400 -13.78500 -20.04100 1.000 59.66000  ? 830 HOH A O   1 
HETATM 14787 O  O   . HOH RA 5 .   ? -29.36000 -64.47600 -14.76400 1.000 43.18000  ? 831 HOH A O   1 
HETATM 14788 O  O   . HOH RA 5 .   ? -19.52900 -23.89700 -47.26700 1.000 61.38000  ? 832 HOH A O   1 
HETATM 14789 O  O   . HOH RA 5 .   ? -26.55400 -62.93500 -23.07600 1.000 52.10000  ? 833 HOH A O   1 
HETATM 14790 O  O   . HOH RA 5 .   ? -8.16700  -38.64500 -36.47700 1.000 60.81000  ? 834 HOH A O   1 
HETATM 14791 O  O   . HOH RA 5 .   ? -34.26700 -65.17900 -27.26100 1.000 59.50000  ? 835 HOH A O   1 
HETATM 14792 O  O   . HOH RA 5 .   ? -12.75000 -30.97800 -27.18500 1.000 30.31000  ? 836 HOH A O   1 
HETATM 14793 O  O   . HOH RA 5 .   ? -47.65300 -31.24500 -14.50200 1.000 62.05000  ? 837 HOH A O   1 
HETATM 14794 O  O   . HOH RA 5 .   ? -31.10900 -58.50400 -3.38100  1.000 46.34000  ? 838 HOH A O   1 
HETATM 14795 O  O   . HOH RA 5 .   ? -30.20900 -53.85400 0.70100   1.000 50.25000  ? 839 HOH A O   1 
HETATM 14796 O  O   . HOH RA 5 .   ? -13.04700 -51.54500 1.30900   1.000 40.74000  ? 840 HOH A O   1 
HETATM 14797 O  O   . HOH RA 5 .   ? -25.46600 -18.12600 -30.85700 1.000 43.02000  ? 841 HOH A O   1 
HETATM 14798 O  O   . HOH RA 5 .   ? -41.11500 -29.12400 -40.91800 1.000 57.44000  ? 842 HOH A O   1 
HETATM 14799 O  O   . HOH RA 5 .   ? -13.68100 -41.24800 -25.53500 1.000 50.88000  ? 843 HOH A O   1 
HETATM 14800 O  O   . HOH RA 5 .   ? -51.01800 -49.09300 -26.63100 1.000 42.67000  ? 844 HOH A O   1 
HETATM 14801 O  O   . HOH RA 5 .   ? -30.75400 -44.85900 -6.93900  1.000 53.54000  ? 845 HOH A O   1 
HETATM 14802 O  O   . HOH RA 5 .   ? -13.14300 -46.03600 -23.33200 1.000 47.16000  ? 846 HOH A O   1 
HETATM 14803 O  O   . HOH RA 5 .   ? -34.34900 -57.52000 -5.01000  1.000 63.14000  ? 847 HOH A O   1 
HETATM 14804 O  O   . HOH RA 5 .   ? -19.94200 -42.27600 -46.65100 1.000 63.89000  ? 848 HOH A O   1 
HETATM 14805 O  O   . HOH RA 5 .   ? -23.92300 -31.48000 -10.98800 1.000 53.72000  ? 849 HOH A O   1 
HETATM 14806 O  O   . HOH RA 5 .   ? -40.91900 -26.42100 -19.64000 1.000 58.38000  ? 850 HOH A O   1 
HETATM 14807 O  O   . HOH RA 5 .   ? -18.34400 -30.76600 -12.51300 1.000 49.01000  ? 851 HOH A O   1 
HETATM 14808 O  O   . HOH RA 5 .   ? -11.33300 -50.76800 -41.36200 1.000 46.41000  ? 852 HOH A O   1 
HETATM 14809 O  O   . HOH RA 5 .   ? -46.36900 -31.51600 -20.57300 1.000 52.66000  ? 853 HOH A O   1 
HETATM 14810 O  O   . HOH RA 5 .   ? -18.44900 -42.01400 -43.93300 1.000 57.99000  ? 854 HOH A O   1 
HETATM 14811 O  O   A HOH RA 5 .   ? -22.07900 -26.93500 -9.02700  0.490 42.48000  ? 855 HOH A O   1 
HETATM 14812 O  O   B HOH RA 5 .   ? -23.76900 -25.85300 -8.75900  0.510 43.79000  ? 855 HOH A O   1 
HETATM 14813 O  O   . HOH RA 5 .   ? 2.94900   -60.35200 -30.67900 1.000 58.57000  ? 856 HOH A O   1 
HETATM 14814 O  O   . HOH RA 5 .   ? -35.71300 -29.56100 -43.03800 1.000 47.21000  ? 857 HOH A O   1 
HETATM 14815 O  O   . HOH RA 5 .   ? -20.32700 -58.46800 -49.27200 1.000 62.23000  ? 858 HOH A O   1 
HETATM 14816 O  O   . HOH RA 5 .   ? -8.74300  -54.59000 -46.25900 1.000 64.88000  ? 859 HOH A O   1 
HETATM 14817 O  O   . HOH RA 5 .   ? -22.72500 -19.35200 -32.30600 1.000 44.29000  ? 860 HOH A O   1 
HETATM 14818 O  O   . HOH RA 5 .   ? -26.06700 -56.12400 3.49400   1.000 61.61000  ? 861 HOH A O   1 
HETATM 14819 O  O   . HOH RA 5 .   ? -16.39100 -19.40900 -23.56300 1.000 54.07000  ? 862 HOH A O   1 
HETATM 14820 O  O   . HOH RA 5 .   ? -17.68900 -17.34200 -21.89600 1.000 62.30000  ? 863 HOH A O   1 
HETATM 14821 O  O   . HOH RA 5 .   ? -24.03700 -27.92600 -5.39600  1.000 58.12000  ? 864 HOH A O   1 
HETATM 14822 O  O   . HOH RA 5 .   ? -46.42800 -25.81500 -26.81300 1.000 60.91000  ? 865 HOH A O   1 
HETATM 14823 O  O   . HOH RA 5 .   ? -29.82900 -56.98600 0.91200   1.000 62.25000  ? 866 HOH A O   1 
HETATM 14824 O  O   . HOH RA 5 .   ? -7.16000  -49.07900 -26.76900 1.000 49.68000  ? 867 HOH A O   1 
HETATM 14825 O  O   . HOH RA 5 .   ? -51.96500 -47.97700 -35.56300 1.000 54.57000  ? 868 HOH A O   1 
HETATM 14826 O  O   . HOH RA 5 .   ? -4.55400  -30.57100 -46.78300 1.000 50.25000  ? 869 HOH A O   1 
HETATM 14827 O  O   . HOH RA 5 .   ? -11.37200 -50.85800 -27.03200 1.000 42.45000  ? 870 HOH A O   1 
HETATM 14828 O  O   . HOH RA 5 .   ? -21.28700 -41.88000 -2.95300  1.000 64.28000  ? 871 HOH A O   1 
HETATM 14829 O  O   A HOH RA 5 .   ? -26.51900 -61.28800 3.15300   0.490 42.74000  ? 872 HOH A O   1 
HETATM 14830 O  O   B HOH RA 5 .   ? -25.50600 -61.39300 1.53100   0.510 47.73000  ? 872 HOH A O   1 
HETATM 14831 O  O   . HOH RA 5 .   ? -14.13700 -52.05200 3.21700   1.000 51.17000  ? 873 HOH A O   1 
HETATM 14832 O  O   . HOH RA 5 .   ? -29.48400 -16.44100 -18.62600 1.000 60.76000  ? 874 HOH A O   1 
HETATM 14833 O  O   . HOH RA 5 .   ? -16.12000 -31.63000 -14.94900 1.000 50.08000  ? 875 HOH A O   1 
HETATM 14834 O  O   . HOH RA 5 .   ? -9.57000  -31.64800 -39.51100 1.000 49.14000  ? 876 HOH A O   1 
HETATM 14835 O  O   . HOH RA 5 .   ? -54.42800 -49.13500 -25.51900 1.000 54.58000  ? 877 HOH A O   1 
HETATM 14836 O  O   . HOH RA 5 .   ? -26.16200 -65.47900 -8.27600  1.000 44.43000  ? 878 HOH A O   1 
HETATM 14837 O  O   . HOH RA 5 .   ? -14.34500 -42.66100 -34.44500 1.000 48.57000  ? 879 HOH A O   1 
HETATM 14838 O  O   . HOH RA 5 .   ? -12.31900 -35.69800 -31.29200 1.000 57.53000  ? 880 HOH A O   1 
HETATM 14839 O  O   . HOH RA 5 .   ? -51.15600 -41.70300 -36.48400 1.000 68.96000  ? 881 HOH A O   1 
HETATM 14840 O  O   . HOH RA 5 .   ? -10.35600 -52.07700 -7.74700  1.000 37.77000  ? 882 HOH A O   1 
HETATM 14841 O  O   . HOH RA 5 .   ? -23.70700 -33.43200 -8.39800  1.000 54.56000  ? 883 HOH A O   1 
HETATM 14842 O  O   . HOH RA 5 .   ? -10.25000 -45.98200 -9.26800  1.000 47.33000  ? 884 HOH A O   1 
HETATM 14843 O  O   . HOH RA 5 .   ? -37.81400 -35.14000 -10.78900 1.000 49.10000  ? 885 HOH A O   1 
HETATM 14844 O  O   . HOH RA 5 .   ? -7.88200  -26.74100 -43.97600 1.000 46.16000  ? 886 HOH A O   1 
HETATM 14845 O  O   . HOH RA 5 .   ? -23.90000 -22.51600 -12.17800 1.000 56.71000  ? 887 HOH A O   1 
HETATM 14846 O  O   . HOH RA 5 .   ? -16.77200 -26.54600 -12.84900 1.000 49.54000  ? 888 HOH A O   1 
HETATM 14847 O  O   . HOH RA 5 .   ? -11.74300 -33.26000 -29.08900 1.000 44.63000  ? 889 HOH A O   1 
HETATM 14848 O  O   . HOH RA 5 .   ? -22.18900 -50.67800 2.20600   1.000 46.01000  ? 890 HOH A O   1 
HETATM 14849 O  O   . HOH RA 5 .   ? -36.42200 -26.00800 -35.35300 1.000 60.05000  ? 891 HOH A O   1 
HETATM 14850 O  O   . HOH RA 5 .   ? -34.44400 -23.67700 -16.17600 1.000 50.69000  ? 892 HOH A O   1 
HETATM 14851 O  O   . HOH RA 5 .   ? -28.42500 -40.80400 -7.72300  1.000 46.91000  ? 893 HOH A O   1 
HETATM 14852 O  O   . HOH RA 5 .   ? -11.76200 -36.64300 -12.09500 1.000 58.43000  ? 894 HOH A O   1 
HETATM 14853 O  O   . HOH SA 5 .   ? 14.89000  -17.20600 13.81600  1.000 49.83000  ? 701 HOH B O   1 
HETATM 14854 O  O   . HOH SA 5 .   ? -8.03600  -24.44800 2.81000   1.000 48.71000  ? 702 HOH B O   1 
HETATM 14855 O  O   . HOH SA 5 .   ? 18.29900  -40.77100 -1.81800  1.000 42.22000  ? 703 HOH B O   1 
HETATM 14856 O  O   . HOH SA 5 .   ? 7.40400   -27.48200 -13.78400 1.000 51.53000  ? 704 HOH B O   1 
HETATM 14857 O  O   . HOH SA 5 .   ? 1.35100   -52.87000 25.83400  1.000 50.81000  ? 705 HOH B O   1 
HETATM 14858 O  O   . HOH SA 5 .   ? 2.04500   -57.79700 -9.39000  1.000 45.66000  ? 706 HOH B O   1 
HETATM 14859 O  O   . HOH SA 5 .   ? 8.67100   -42.23200 -0.51700  1.000 34.93000  ? 707 HOH B O   1 
HETATM 14860 O  O   . HOH SA 5 .   ? 14.12000  -39.82500 -9.51500  1.000 35.58000  ? 708 HOH B O   1 
HETATM 14861 O  O   . HOH SA 5 .   ? 6.87400   -54.74600 9.35800   1.000 43.44000  ? 709 HOH B O   1 
HETATM 14862 O  O   . HOH SA 5 .   ? 10.58900  -43.14900 20.24900  1.000 42.03000  ? 710 HOH B O   1 
HETATM 14863 O  O   . HOH SA 5 .   ? -7.07900  -45.99300 -3.34300  1.000 49.43000  ? 711 HOH B O   1 
HETATM 14864 O  O   . HOH SA 5 .   ? 7.06000   -46.36300 -7.55600  1.000 38.93000  ? 712 HOH B O   1 
HETATM 14865 O  O   . HOH SA 5 .   ? 8.31000   -40.33400 -7.17300  1.000 35.46000  ? 713 HOH B O   1 
HETATM 14866 O  O   . HOH SA 5 .   ? 12.10500  -29.66600 -12.37200 1.000 44.67000  ? 714 HOH B O   1 
HETATM 14867 O  O   . HOH SA 5 .   ? 2.66000   -22.13900 -5.90500  1.000 48.73000  ? 715 HOH B O   1 
HETATM 14868 O  O   . HOH SA 5 .   ? -2.15900  -41.98900 14.61100  1.000 39.50000  ? 716 HOH B O   1 
HETATM 14869 O  O   . HOH SA 5 .   ? 20.64400  -29.31500 -6.66700  1.000 56.85000  ? 717 HOH B O   1 
HETATM 14870 O  O   . HOH SA 5 .   ? 3.99600   -27.04900 -8.47100  1.000 44.69000  ? 718 HOH B O   1 
HETATM 14871 O  O   . HOH SA 5 .   ? 1.35700   -17.21500 4.14400   1.000 59.55000  ? 719 HOH B O   1 
HETATM 14872 O  O   . HOH SA 5 .   ? 11.12000  -62.31700 8.37300   1.000 54.37000  ? 720 HOH B O   1 
HETATM 14873 O  O   . HOH SA 5 .   ? 7.11000   -46.55900 8.95100   1.000 40.46000  ? 721 HOH B O   1 
HETATM 14874 O  O   . HOH SA 5 .   ? 13.14500  -36.29600 -22.22100 1.000 55.77000  ? 722 HOH B O   1 
HETATM 14875 O  O   . HOH SA 5 .   ? -1.81300  -47.61200 8.84200   1.000 44.81000  ? 723 HOH B O   1 
HETATM 14876 O  O   . HOH SA 5 .   ? -5.74800  -28.29600 16.12700  1.000 53.15000  ? 724 HOH B O   1 
HETATM 14877 O  O   . HOH SA 5 .   ? -8.43100  -47.54800 -25.07900 1.000 49.07000  ? 725 HOH B O   1 
HETATM 14878 O  O   . HOH SA 5 .   ? 6.34800   -38.50100 -11.82000 1.000 48.18000  ? 726 HOH B O   1 
HETATM 14879 O  O   . HOH SA 5 .   ? 3.04000   -42.66800 8.91200   1.000 37.29000  ? 727 HOH B O   1 
HETATM 14880 O  O   . HOH SA 5 .   ? -6.19900  -47.74900 -28.72600 1.000 44.38000  ? 728 HOH B O   1 
HETATM 14881 O  O   . HOH SA 5 .   ? -7.14300  -25.65800 8.32600   1.000 41.42000  ? 729 HOH B O   1 
HETATM 14882 O  O   . HOH SA 5 .   ? -4.03200  -57.61600 10.60600  1.000 48.61000  ? 730 HOH B O   1 
HETATM 14883 O  O   . HOH SA 5 .   ? -23.20000 -35.16400 13.11400  1.000 58.62000  ? 731 HOH B O   1 
HETATM 14884 O  O   . HOH SA 5 .   ? 24.48400  -42.92200 -4.96000  1.000 52.00000  ? 732 HOH B O   1 
HETATM 14885 O  O   . HOH SA 5 .   ? 4.49900   -21.11000 3.13100   1.000 41.28000  ? 733 HOH B O   1 
HETATM 14886 O  O   . HOH SA 5 .   ? 9.81100   -22.66500 -6.75900  1.000 52.70000  ? 734 HOH B O   1 
HETATM 14887 O  O   . HOH SA 5 .   ? -9.14300  -46.28100 24.83300  1.000 26.23000  ? 735 HOH B O   1 
HETATM 14888 O  O   . HOH SA 5 .   ? 7.48700   -52.80500 1.05700   1.000 42.42000  ? 736 HOH B O   1 
HETATM 14889 O  O   . HOH SA 5 .   ? 1.85800   -53.81500 -6.56300  1.000 39.94000  ? 737 HOH B O   1 
HETATM 14890 O  O   . HOH SA 5 .   ? -4.63600  -47.53000 -7.03800  1.000 38.10000  ? 738 HOH B O   1 
HETATM 14891 O  O   . HOH SA 5 .   ? 2.82400   -31.09600 -3.35800  1.000 33.97000  ? 739 HOH B O   1 
HETATM 14892 O  O   . HOH SA 5 .   ? 4.52200   -36.62900 -11.57700 1.000 42.75000  ? 740 HOH B O   1 
HETATM 14893 O  O   . HOH SA 5 .   ? 13.84300  -48.60200 -1.07800  1.000 42.76000  ? 741 HOH B O   1 
HETATM 14894 O  O   . HOH SA 5 .   ? -15.77300 -28.18700 8.62300   1.000 47.67000  ? 742 HOH B O   1 
HETATM 14895 O  O   . HOH SA 5 .   ? 18.67600  -60.27600 14.91300  1.000 58.89000  ? 743 HOH B O   1 
HETATM 14896 O  O   . HOH SA 5 .   ? -0.21000  -57.46200 -5.74700  1.000 48.72000  ? 744 HOH B O   1 
HETATM 14897 O  O   . HOH SA 5 .   ? 0.29300   -55.03800 4.49100   1.000 46.02000  ? 745 HOH B O   1 
HETATM 14898 O  O   . HOH SA 5 .   ? 11.86600  -32.18200 -13.46000 1.000 42.68000  ? 746 HOH B O   1 
HETATM 14899 O  O   . HOH SA 5 .   ? 0.74100   -55.35900 8.82600   1.000 42.64000  ? 747 HOH B O   1 
HETATM 14900 O  O   . HOH SA 5 .   ? -9.04800  -50.78000 -35.74600 1.000 45.36000  ? 748 HOH B O   1 
HETATM 14901 O  O   . HOH SA 5 .   ? -2.50300  -44.70800 -19.46700 1.000 36.96000  ? 749 HOH B O   1 
HETATM 14902 O  O   . HOH SA 5 .   ? 4.35900   -52.22500 -6.68400  1.000 37.91000  ? 750 HOH B O   1 
HETATM 14903 O  O   . HOH SA 5 .   ? 23.63200  -48.34000 -1.09300  1.000 50.42000  ? 751 HOH B O   1 
HETATM 14904 O  O   . HOH SA 5 .   ? -4.17200  -49.80200 -12.97300 1.000 29.71000  ? 752 HOH B O   1 
HETATM 14905 O  O   . HOH SA 5 .   ? -17.47500 -32.26700 3.55300   1.000 56.66000  ? 753 HOH B O   1 
HETATM 14906 O  O   . HOH SA 5 .   ? -1.79600  -54.87800 -7.82800  1.000 43.00000  ? 754 HOH B O   1 
HETATM 14907 O  O   . HOH SA 5 .   ? 22.86100  -25.33800 10.24300  1.000 46.26000  ? 755 HOH B O   1 
HETATM 14908 O  O   . HOH SA 5 .   ? -6.08100  -39.72200 14.28300  1.000 34.59000  ? 756 HOH B O   1 
HETATM 14909 O  O   . HOH SA 5 .   ? 20.06300  -55.82900 11.92500  1.000 55.43000  ? 757 HOH B O   1 
HETATM 14910 O  O   . HOH SA 5 .   ? -8.83500  -37.89400 -7.08100  1.000 36.24000  ? 758 HOH B O   1 
HETATM 14911 O  O   . HOH SA 5 .   ? -2.12200  -57.60600 4.31600   1.000 44.93000  ? 759 HOH B O   1 
HETATM 14912 O  O   . HOH SA 5 .   ? -0.65100  -49.22200 -17.00200 1.000 40.52000  ? 760 HOH B O   1 
HETATM 14913 O  O   . HOH SA 5 .   ? 10.76200  -21.61400 8.31400   1.000 43.16000  ? 761 HOH B O   1 
HETATM 14914 O  O   . HOH SA 5 .   ? 3.93500   -27.72200 -11.91100 1.000 43.18000  ? 762 HOH B O   1 
HETATM 14915 O  O   . HOH SA 5 .   ? -3.86200  -35.58700 -11.69800 1.000 31.10000  ? 763 HOH B O   1 
HETATM 14916 O  O   . HOH SA 5 .   ? -2.76600  -36.21500 19.04500  1.000 38.10000  ? 764 HOH B O   1 
HETATM 14917 O  O   . HOH SA 5 .   ? -1.17300  -22.48400 0.93800   1.000 48.44000  ? 765 HOH B O   1 
HETATM 14918 O  O   . HOH SA 5 .   ? 4.74200   -56.92500 9.40000   1.000 51.77000  ? 766 HOH B O   1 
HETATM 14919 O  O   . HOH SA 5 .   ? 13.85900  -19.49400 2.53800   1.000 52.03000  ? 767 HOH B O   1 
HETATM 14920 O  O   . HOH SA 5 .   ? 8.95900   -60.58400 -17.91100 1.000 54.18000  ? 768 HOH B O   1 
HETATM 14921 O  O   . HOH SA 5 .   ? 14.98400  -40.13900 1.80200   1.000 39.92000  ? 769 HOH B O   1 
HETATM 14922 O  O   . HOH SA 5 .   ? -0.06100  -54.11800 11.63800  1.000 48.37000  ? 770 HOH B O   1 
HETATM 14923 O  O   . HOH SA 5 .   ? -5.91100  -51.64800 -21.08700 1.000 39.78000  ? 771 HOH B O   1 
HETATM 14924 O  O   . HOH SA 5 .   ? 5.76600   -53.45900 3.44300   1.000 46.96000  ? 772 HOH B O   1 
HETATM 14925 O  O   . HOH SA 5 .   ? 13.41700  -30.68500 -19.99900 1.000 59.63000  ? 773 HOH B O   1 
HETATM 14926 O  O   . HOH SA 5 .   ? -2.59300  -37.27200 -3.55000  1.000 32.02000  ? 774 HOH B O   1 
HETATM 14927 O  O   . HOH SA 5 .   ? 15.99000  -23.24400 18.50700  1.000 55.69000  ? 775 HOH B O   1 
HETATM 14928 O  O   . HOH SA 5 .   ? -13.19300 -61.09700 20.70700  1.000 61.11000  ? 776 HOH B O   1 
HETATM 14929 O  O   . HOH SA 5 .   ? -19.67900 -42.74300 4.51100   1.000 46.97000  ? 777 HOH B O   1 
HETATM 14930 O  O   . HOH SA 5 .   ? 14.84700  -38.86900 -6.94500  1.000 43.74000  ? 778 HOH B O   1 
HETATM 14931 O  O   . HOH SA 5 .   ? 7.56500   -28.73700 -4.76900  1.000 41.22000  ? 779 HOH B O   1 
HETATM 14932 O  O   . HOH SA 5 .   ? -8.36200  -43.34000 4.96300   1.000 39.68000  ? 780 HOH B O   1 
HETATM 14933 O  O   . HOH SA 5 .   ? 13.79000  -52.86700 8.74100   1.000 47.14000  ? 781 HOH B O   1 
HETATM 14934 O  O   . HOH SA 5 .   ? -6.87400  -42.40900 2.61100   1.000 31.38000  ? 782 HOH B O   1 
HETATM 14935 O  O   . HOH SA 5 .   ? 31.00200  -43.95900 -0.30400  1.000 61.80000  ? 783 HOH B O   1 
HETATM 14936 O  O   . HOH SA 5 .   ? -9.97400  -39.43800 -10.37500 1.000 38.32000  ? 784 HOH B O   1 
HETATM 14937 O  O   . HOH SA 5 .   ? 2.13800   -29.06800 -0.16600  1.000 36.76000  ? 785 HOH B O   1 
HETATM 14938 O  O   . HOH SA 5 .   ? 11.04800  -55.92200 13.58300  1.000 46.91000  ? 786 HOH B O   1 
HETATM 14939 O  O   . HOH SA 5 .   ? 6.08300   -48.06300 -30.34800 1.000 45.91000  ? 787 HOH B O   1 
HETATM 14940 O  O   . HOH SA 5 .   ? -2.78800  -35.41300 -28.49500 1.000 46.64000  ? 788 HOH B O   1 
HETATM 14941 O  O   . HOH SA 5 .   ? -14.85200 -42.38300 1.17600   1.000 46.97000  ? 789 HOH B O   1 
HETATM 14942 O  O   . HOH SA 5 .   ? 8.83200   -56.35300 -2.78400  1.000 44.39000  ? 790 HOH B O   1 
HETATM 14943 O  O   . HOH SA 5 .   ? 1.42800   -29.37200 -11.54600 1.000 40.12000  ? 791 HOH B O   1 
HETATM 14944 O  O   . HOH SA 5 .   ? -1.69900  -36.69200 -0.83500  1.000 35.89000  ? 792 HOH B O   1 
HETATM 14945 O  O   . HOH SA 5 .   ? 2.40700   -52.11400 -18.41500 1.000 42.17000  ? 793 HOH B O   1 
HETATM 14946 O  O   . HOH SA 5 .   ? 12.94000  -29.75000 -9.84500  1.000 44.90000  ? 794 HOH B O   1 
HETATM 14947 O  O   . HOH SA 5 .   ? -6.47300  -30.27600 -15.14300 1.000 42.24000  ? 795 HOH B O   1 
HETATM 14948 O  O   . HOH SA 5 .   ? -1.98000  -31.97000 -20.78600 1.000 39.45000  ? 796 HOH B O   1 
HETATM 14949 O  O   A HOH SA 5 .   ? 5.051     -40.897   27.960    0.440 42.11000  ? 797 HOH B O   1 
HETATM 14950 O  O   B HOH SA 5 .   ? 4.920     -39.002   28.794    0.560 29.95000  ? 797 HOH B O   1 
HETATM 14951 O  O   . HOH SA 5 .   ? -9.79700  -34.06900 -8.35700  1.000 38.76000  ? 798 HOH B O   1 
HETATM 14952 O  O   . HOH SA 5 .   ? 22.05400  -25.04200 5.60500   1.000 51.60000  ? 799 HOH B O   1 
HETATM 14953 O  O   . HOH SA 5 .   ? -10.05900 -49.84200 18.15700  1.000 47.87000  ? 800 HOH B O   1 
HETATM 14954 O  O   . HOH SA 5 .   ? -3.96000  -48.06800 10.86600  1.000 35.98000  ? 801 HOH B O   1 
HETATM 14955 O  O   . HOH SA 5 .   ? -8.51100  -43.99500 -10.13500 1.000 39.22000  ? 802 HOH B O   1 
HETATM 14956 O  O   A HOH SA 5 .   ? -14.71900 -45.82300 21.67600  0.470 46.41000  ? 803 HOH B O   1 
HETATM 14957 O  O   B HOH SA 5 .   ? -13.92400 -45.46900 23.49000  0.530 46.22000  ? 803 HOH B O   1 
HETATM 14958 O  O   . HOH SA 5 .   ? 1.52700   -53.41500 -23.60200 1.000 40.53000  ? 804 HOH B O   1 
HETATM 14959 O  O   . HOH SA 5 .   ? -14.01200 -49.77900 12.98100  1.000 43.18000  ? 805 HOH B O   1 
HETATM 14960 O  O   . HOH SA 5 .   ? -7.19500  -47.64600 -9.89300  1.000 43.28000  ? 806 HOH B O   1 
HETATM 14961 O  O   A HOH SA 5 .   ? -19.16000 -36.69300 18.78300  0.530 36.51000  ? 807 HOH B O   1 
HETATM 14962 O  O   B HOH SA 5 .   ? -19.34500 -38.86900 18.24700  0.470 25.98000  ? 807 HOH B O   1 
HETATM 14963 O  O   . HOH SA 5 .   ? 0.67400   -45.40000 -26.50500 1.000 43.03000  ? 808 HOH B O   1 
HETATM 14964 O  O   . HOH SA 5 .   ? -9.89500  -58.95700 15.02800  1.000 50.85000  ? 809 HOH B O   1 
HETATM 14965 O  O   . HOH SA 5 .   ? 1.68400   -54.82800 -2.24700  1.000 38.81000  ? 810 HOH B O   1 
HETATM 14966 O  O   . HOH SA 5 .   ? 2.85100   -56.16500 7.50300   1.000 48.52000  ? 811 HOH B O   1 
HETATM 14967 O  O   . HOH SA 5 .   ? 26.71900  -44.95900 9.20400   1.000 37.54000  ? 812 HOH B O   1 
HETATM 14968 O  O   . HOH SA 5 .   ? -4.91100  -43.39000 -22.47100 1.000 44.01000  ? 813 HOH B O   1 
HETATM 14969 O  O   . HOH SA 5 .   ? -3.74500  -46.43500 -37.60200 1.000 45.19000  ? 814 HOH B O   1 
HETATM 14970 O  O   . HOH SA 5 .   ? 17.14400  -45.02500 -9.70300  1.000 48.40000  ? 815 HOH B O   1 
HETATM 14971 O  O   . HOH SA 5 .   ? -6.39900  -47.96700 2.28600   1.000 50.06000  ? 816 HOH B O   1 
HETATM 14972 O  O   . HOH SA 5 .   ? 13.13000  -29.38900 -16.15300 1.000 47.15000  ? 817 HOH B O   1 
HETATM 14973 O  O   . HOH SA 5 .   ? -1.77800  -52.65100 6.26000   1.000 52.29000  ? 818 HOH B O   1 
HETATM 14974 O  O   . HOH SA 5 .   ? -0.67300  -49.61300 1.11400   1.000 44.38000  ? 819 HOH B O   1 
HETATM 14975 O  O   . HOH SA 5 .   ? -23.29800 -41.19800 6.18700   1.000 56.50000  ? 820 HOH B O   1 
HETATM 14976 O  O   . HOH SA 5 .   ? -8.69800  -41.87300 24.29100  1.000 42.36000  ? 821 HOH B O   1 
HETATM 14977 O  O   . HOH SA 5 .   ? -8.98700  -35.22700 -12.91500 1.000 41.62000  ? 822 HOH B O   1 
HETATM 14978 O  O   . HOH SA 5 .   ? -3.33600  -38.15300 -28.09000 1.000 38.56000  ? 823 HOH B O   1 
HETATM 14979 O  O   . HOH SA 5 .   ? 7.73500   -17.88400 -2.49800  1.000 48.16000  ? 824 HOH B O   1 
HETATM 14980 O  O   . HOH SA 5 .   ? 10.93700  -62.75300 16.84300  1.000 60.54000  ? 825 HOH B O   1 
HETATM 14981 O  O   . HOH SA 5 .   ? 18.44600  -58.57900 5.57900   1.000 56.00000  ? 826 HOH B O   1 
HETATM 14982 O  O   . HOH SA 5 .   ? 11.52800  -57.20300 -19.23100 1.000 44.06000  ? 827 HOH B O   1 
HETATM 14983 O  O   . HOH SA 5 .   ? 23.27300  -34.33700 -3.01200  1.000 49.97000  ? 828 HOH B O   1 
HETATM 14984 O  O   . HOH SA 5 .   ? 17.53800  -42.66400 -17.84000 1.000 53.00000  ? 829 HOH B O   1 
HETATM 14985 O  O   . HOH SA 5 .   ? 25.90300  -30.28200 17.03400  1.000 56.86000  ? 830 HOH B O   1 
HETATM 14986 O  O   . HOH SA 5 .   ? 9.45200   -57.02400 19.59700  1.000 55.69000  ? 831 HOH B O   1 
HETATM 14987 O  O   . HOH SA 5 .   ? -2.89300  -49.83100 -3.60700  1.000 37.37000  ? 832 HOH B O   1 
HETATM 14988 O  O   . HOH SA 5 .   ? 16.90800  -38.23900 -15.50300 1.000 46.64000  ? 833 HOH B O   1 
HETATM 14989 O  O   . HOH SA 5 .   ? -7.71600  -36.17800 -24.46500 1.000 46.23000  ? 834 HOH B O   1 
HETATM 14990 O  O   . HOH SA 5 .   ? -15.67100 -45.64500 14.28300  1.000 60.78000  ? 835 HOH B O   1 
HETATM 14991 O  O   . HOH SA 5 .   ? 5.22000   -60.83200 3.37200   1.000 51.59000  ? 836 HOH B O   1 
HETATM 14992 O  O   . HOH SA 5 .   ? 3.68000   -24.46000 -18.74500 1.000 47.62000  ? 837 HOH B O   1 
HETATM 14993 O  O   . HOH SA 5 .   ? 19.55400  -26.56000 18.54900  1.000 58.74000  ? 838 HOH B O   1 
HETATM 14994 O  O   . HOH SA 5 .   ? -24.30100 -39.96700 9.44100   1.000 61.16000  ? 839 HOH B O   1 
HETATM 14995 O  O   . HOH SA 5 .   ? 3.58800   -57.43900 11.35400  1.000 43.65000  ? 840 HOH B O   1 
HETATM 14996 O  O   . HOH SA 5 .   ? -6.18000  -41.17300 -24.94200 1.000 63.91000  ? 841 HOH B O   1 
HETATM 14997 O  O   . HOH SA 5 .   ? -11.52100 -30.02600 0.58300   1.000 55.15000  ? 842 HOH B O   1 
HETATM 14998 O  O   . HOH SA 5 .   ? 29.34800  -35.06300 12.53000  1.000 53.45000  ? 843 HOH B O   1 
HETATM 14999 O  O   . HOH SA 5 .   ? -12.89300 -48.29200 8.03900   1.000 29.40000  ? 844 HOH B O   1 
HETATM 15000 O  O   . HOH SA 5 .   ? -0.30600  -27.65300 -5.61300  1.000 46.53000  ? 845 HOH B O   1 
HETATM 15001 O  O   . HOH SA 5 .   ? -12.98100 -28.43700 -10.74700 1.000 67.28000  ? 846 HOH B O   1 
HETATM 15002 O  O   . HOH SA 5 .   ? 1.59600   -54.45700 14.32600  1.000 51.40000  ? 847 HOH B O   1 
HETATM 15003 O  O   . HOH SA 5 .   ? -9.93500  -33.59600 -10.97400 1.000 54.32000  ? 848 HOH B O   1 
HETATM 15004 O  O   . HOH SA 5 .   ? 11.02800  -14.45600 6.72500   1.000 48.99000  ? 849 HOH B O   1 
HETATM 15005 O  O   . HOH SA 5 .   ? 9.80700   -28.35800 -19.01300 1.000 40.50000  ? 850 HOH B O   1 
HETATM 15006 O  O   . HOH SA 5 .   ? 16.41300  -22.44200 -11.11900 1.000 50.09000  ? 851 HOH B O   1 
HETATM 15007 O  O   . HOH SA 5 .   ? -24.88500 -34.12600 9.70500   1.000 60.52000  ? 852 HOH B O   1 
HETATM 15008 O  O   . HOH SA 5 .   ? 0.81300   -50.01600 -37.78300 1.000 61.25000  ? 853 HOH B O   1 
HETATM 15009 O  O   . HOH SA 5 .   ? -14.04200 -40.85500 22.61200  1.000 37.47000  ? 854 HOH B O   1 
HETATM 15010 O  O   . HOH SA 5 .   ? -14.24400 -47.03000 17.25300  1.000 50.98000  ? 855 HOH B O   1 
HETATM 15011 O  O   . HOH SA 5 .   ? 29.53500  -38.25200 2.27000   1.000 57.90000  ? 856 HOH B O   1 
HETATM 15012 O  O   A HOH SA 5 .   ? 1.60800   -65.78600 10.09600  0.500 44.13000  ? 857 HOH B O   1 
HETATM 15013 O  O   B HOH SA 5 .   ? 2.85800   -65.12800 11.81300  0.500 40.92000  ? 857 HOH B O   1 
HETATM 15014 O  O   . HOH SA 5 .   ? -14.71100 -31.11500 0.48100   1.000 56.57000  ? 858 HOH B O   1 
HETATM 15015 O  O   A HOH SA 5 .   ? 6.06600   -20.56900 13.01800  0.500 42.18000  ? 859 HOH B O   1 
HETATM 15016 O  O   B HOH SA 5 .   ? 7.70900   -19.47900 12.99700  0.500 41.53000  ? 859 HOH B O   1 
HETATM 15017 O  O   . HOH SA 5 .   ? -3.63700  -63.45400 -16.43400 1.000 58.61000  ? 860 HOH B O   1 
HETATM 15018 O  O   . HOH SA 5 .   ? 2.11000   -60.95300 19.65100  1.000 65.46000  ? 861 HOH B O   1 
HETATM 15019 O  O   . HOH SA 5 .   ? -13.46500 -69.20700 24.36700  1.000 51.95000  ? 862 HOH B O   1 
HETATM 15020 O  O   . HOH SA 5 .   ? 19.28200  -64.29500 9.59500   1.000 60.08000  ? 863 HOH B O   1 
HETATM 15021 O  O   . HOH SA 5 .   ? 18.25700  -67.88000 4.62600   1.000 63.87000  ? 864 HOH B O   1 
HETATM 15022 O  O   . HOH SA 5 .   ? 1.48900   -27.27200 -23.87300 1.000 53.65000  ? 865 HOH B O   1 
HETATM 15023 O  O   . HOH SA 5 .   ? -21.67100 -36.37500 14.81400  1.000 52.12000  ? 866 HOH B O   1 
HETATM 15024 O  O   . HOH SA 5 .   ? -8.90900  -51.93300 8.70000   1.000 45.99000  ? 867 HOH B O   1 
HETATM 15025 O  O   . HOH SA 5 .   ? -3.24900  -34.61400 -32.19900 1.000 53.69000  ? 868 HOH B O   1 
HETATM 15026 O  O   . HOH SA 5 .   ? 0.43100   -55.09000 -4.62500  1.000 36.84000  ? 869 HOH B O   1 
HETATM 15027 O  O   . HOH SA 5 .   ? -5.48400  -44.14500 -19.22900 1.000 40.97000  ? 870 HOH B O   1 
HETATM 15028 O  O   . HOH SA 5 .   ? -23.64100 -28.29200 12.20600  1.000 74.93000  ? 871 HOH B O   1 
HETATM 15029 O  O   . HOH SA 5 .   ? -3.55800  -25.09800 -2.83000  1.000 56.56000  ? 872 HOH B O   1 
HETATM 15030 O  O   . HOH SA 5 .   ? -11.80000 -29.64900 -2.02600  1.000 51.79000  ? 873 HOH B O   1 
HETATM 15031 O  O   . HOH SA 5 .   ? -20.76600 -34.77600 17.12800  1.000 56.41000  ? 874 HOH B O   1 
HETATM 15032 O  O   . HOH SA 5 .   ? -0.62100  -21.25800 3.14300   1.000 53.76000  ? 875 HOH B O   1 
HETATM 15033 O  O   . HOH SA 5 .   ? -1.85300  -54.14000 -2.76400  1.000 56.11000  ? 876 HOH B O   1 
HETATM 15034 O  O   . HOH SA 5 .   ? -9.92600  -42.07400 -11.24600 1.000 37.60000  ? 877 HOH B O   1 
HETATM 15035 O  O   . HOH SA 5 .   ? -1.05000  -54.79500 6.90700   1.000 41.17000  ? 878 HOH B O   1 
HETATM 15036 O  O   . HOH SA 5 .   ? -5.45200  -56.68800 8.04700   1.000 58.79000  ? 879 HOH B O   1 
HETATM 15037 O  O   . HOH SA 5 .   ? -9.67600  -43.11500 -14.60200 1.000 48.96000  ? 880 HOH B O   1 
HETATM 15038 O  O   . HOH SA 5 .   ? -0.03900  -26.04500 -7.28500  1.000 46.23000  ? 881 HOH B O   1 
HETATM 15039 O  O   . HOH SA 5 .   ? -2.82100  -27.80200 -5.60400  1.000 52.36000  ? 882 HOH B O   1 
HETATM 15040 O  O   . HOH SA 5 .   ? -2.97700  -56.56900 25.62400  1.000 37.08000  ? 883 HOH B O   1 
HETATM 15041 O  O   . HOH SA 5 .   ? 16.39900  -19.59900 20.71400  1.000 70.40000  ? 884 HOH B O   1 
HETATM 15042 O  O   . HOH SA 5 .   ? -11.40700 -38.21700 -7.99300  1.000 43.84000  ? 885 HOH B O   1 
HETATM 15043 O  O   . HOH SA 5 .   ? 21.01600  -58.63700 13.24300  1.000 65.49000  ? 886 HOH B O   1 
HETATM 15044 O  O   . HOH SA 5 .   ? -7.36100  -27.12000 -11.50800 1.000 58.83000  ? 887 HOH B O   1 
HETATM 15045 O  O   . HOH TA 5 .   ? 45.04700  1.35300   -40.37000 1.000 67.48000  ? 701 HOH C O   1 
HETATM 15046 O  O   . HOH TA 5 .   ? 2.50500   0.38300   -40.85800 1.000 50.89000  ? 702 HOH C O   1 
HETATM 15047 O  O   . HOH TA 5 .   ? 25.82300  -10.33900 -42.75300 1.000 55.99000  ? 703 HOH C O   1 
HETATM 15048 O  O   . HOH TA 5 .   ? 7.41700   -0.84200  -23.78800 1.000 64.22000  ? 704 HOH C O   1 
HETATM 15049 O  O   . HOH TA 5 .   ? 16.16600  7.66100   -20.77300 1.000 62.46000  ? 705 HOH C O   1 
HETATM 15050 O  O   . HOH TA 5 .   ? 13.847    34.086    -18.926   1.000 73.05000  ? 706 HOH C O   1 
HETATM 15051 O  O   . HOH TA 5 .   ? 37.91900  15.08600  -21.91500 1.000 57.33000  ? 707 HOH C O   1 
HETATM 15052 O  O   . HOH TA 5 .   ? 18.82500  -3.58800  -31.69800 1.000 51.79000  ? 708 HOH C O   1 
HETATM 15053 O  O   . HOH TA 5 .   ? -9.02100  -9.09000  -39.28700 1.000 55.04000  ? 709 HOH C O   1 
HETATM 15054 O  O   . HOH TA 5 .   ? 10.43800  -11.88900 -53.95500 1.000 55.89000  ? 710 HOH C O   1 
HETATM 15055 O  O   . HOH TA 5 .   ? 23.58500  -5.10200  -43.62200 1.000 50.43000  ? 711 HOH C O   1 
HETATM 15056 O  O   . HOH TA 5 .   ? 1.11600   -4.78900  -40.82200 1.000 59.22000  ? 712 HOH C O   1 
HETATM 15057 O  O   . HOH TA 5 .   ? 37.78700  3.55600   -12.94100 1.000 58.97000  ? 713 HOH C O   1 
HETATM 15058 O  O   . HOH TA 5 .   ? 28.90500  25.69100  -29.62200 1.000 47.36000  ? 714 HOH C O   1 
HETATM 15059 O  O   . HOH TA 5 .   ? 21.77000  4.35000   -26.18800 1.000 60.67000  ? 715 HOH C O   1 
HETATM 15060 O  O   . HOH TA 5 .   ? 19.33100  14.11600  -31.31100 1.000 57.60000  ? 716 HOH C O   1 
HETATM 15061 O  O   . HOH TA 5 .   ? 23.17800  -7.53900  -27.87100 1.000 57.47000  ? 717 HOH C O   1 
HETATM 15062 O  O   . HOH TA 5 .   ? 27.34300  -9.48500  -13.70600 1.000 58.69000  ? 718 HOH C O   1 
HETATM 15063 O  O   . HOH TA 5 .   ? 16.59700  11.48200  -37.80500 1.000 58.92000  ? 719 HOH C O   1 
HETATM 15064 O  O   . HOH TA 5 .   ? 17.49800  9.48500   -40.14900 1.000 45.28000  ? 720 HOH C O   1 
HETATM 15065 O  O   . HOH TA 5 .   ? 13.35000  -5.59300  -12.48300 1.000 60.18000  ? 721 HOH C O   1 
HETATM 15066 O  O   . HOH TA 5 .   ? 12.72800  6.70000   -32.87000 1.000 63.44000  ? 722 HOH C O   1 
HETATM 15067 O  O   . HOH TA 5 .   ? 14.94300  -20.73100 -34.67700 1.000 94.81000  ? 723 HOH C O   1 
HETATM 15068 O  O   . HOH TA 5 .   ? 4.554     -1.431    -51.308   1.000 36.56000  ? 724 HOH C O   1 
HETATM 15069 O  O   . HOH TA 5 .   ? 43.22700  -9.38300  -20.36000 1.000 69.54000  ? 725 HOH C O   1 
HETATM 15070 O  O   . HOH TA 5 .   ? 15.63400  18.98100  -38.17200 1.000 46.46000  ? 726 HOH C O   1 
HETATM 15071 O  O   . HOH TA 5 .   ? 18.55800  -8.07600  -55.20900 1.000 63.04000  ? 727 HOH C O   1 
HETATM 15072 O  O   . HOH TA 5 .   ? 15.52900  20.35200  -47.60900 1.000 73.40000  ? 728 HOH C O   1 
HETATM 15073 O  O   . HOH TA 5 .   ? 1.25200   -13.06000 -54.25700 1.000 51.62000  ? 729 HOH C O   1 
HETATM 15074 O  O   . HOH TA 5 .   ? 20.00200  -17.29000 -41.78400 1.000 72.79000  ? 730 HOH C O   1 
HETATM 15075 O  O   . HOH TA 5 .   ? 18.769    -17.551   -53.794   1.000 68.93000  ? 731 HOH C O   1 
HETATM 15076 O  O   . HOH TA 5 .   ? 17.90500  14.55600  -21.83600 1.000 60.56000  ? 732 HOH C O   1 
HETATM 15077 O  O   . HOH TA 5 .   ? 21.16600  -6.71200  -11.90300 1.000 75.13000  ? 733 HOH C O   1 
HETATM 15078 O  O   . HOH TA 5 .   ? 31.88000  23.86700  -32.55900 1.000 57.62000  ? 734 HOH C O   1 
HETATM 15079 O  O   . HOH TA 5 .   ? 0.17000   -0.40200  -20.53000 1.000 62.22000  ? 735 HOH C O   1 
HETATM 15080 O  O   . HOH TA 5 .   ? -8.07500  -5.76900  -37.36900 1.000 65.24000  ? 736 HOH C O   1 
HETATM 15081 O  O   . HOH TA 5 .   ? 1.25300   -23.96800 -55.43400 1.000 63.12000  ? 737 HOH C O   1 
HETATM 15082 O  O   . HOH TA 5 .   ? 45.03200  -13.86800 -38.90100 1.000 70.06000  ? 738 HOH C O   1 
HETATM 15083 O  O   . HOH TA 5 .   ? 23.47300  25.13800  -18.93200 1.000 45.72000  ? 739 HOH C O   1 
HETATM 15084 O  O   . HOH TA 5 .   ? -8.01700  -10.78100 -25.44600 1.000 69.02000  ? 740 HOH C O   1 
HETATM 15085 O  O   . HOH UA 5 .   ? -32.68400 14.63400  24.37900  1.000 65.75000  ? 701 HOH D O   1 
HETATM 15086 O  O   . HOH UA 5 .   ? -32.79200 -0.02000  8.43600   1.000 59.23000  ? 702 HOH D O   1 
HETATM 15087 O  O   . HOH UA 5 .   ? -3.95900  20.95300  22.08400  1.000 62.39000  ? 703 HOH D O   1 
HETATM 15088 O  O   . HOH UA 5 .   ? -4.99800  7.46900   19.92800  1.000 48.79000  ? 704 HOH D O   1 
HETATM 15089 O  O   . HOH UA 5 .   ? -18.13600 31.32600  2.21400   1.000 59.62000  ? 705 HOH D O   1 
HETATM 15090 O  O   . HOH UA 5 .   ? -14.46400 -0.91800  0.79700   1.000 56.78000  ? 706 HOH D O   1 
HETATM 15091 O  O   . HOH UA 5 .   ? -12.27500 9.43600   34.05000  1.000 54.01000  ? 707 HOH D O   1 
HETATM 15092 O  O   . HOH UA 5 .   ? -33.68400 21.01700  -8.66600  1.000 61.58000  ? 708 HOH D O   1 
HETATM 15093 O  O   . HOH UA 5 .   ? -22.78600 9.45100   13.72500  1.000 59.45000  ? 709 HOH D O   1 
HETATM 15094 O  O   . HOH UA 5 .   ? -26.15100 28.35300  13.45800  1.000 74.13000  ? 710 HOH D O   1 
HETATM 15095 O  O   . HOH UA 5 .   ? -9.57400  23.37300  2.60400   1.000 64.10000  ? 711 HOH D O   1 
HETATM 15096 O  O   . HOH UA 5 .   ? -22.90300 8.49700   21.92000  1.000 62.43000  ? 712 HOH D O   1 
HETATM 15097 O  O   . HOH UA 5 .   ? -18.14500 -1.30000  15.46500  1.000 57.56000  ? 713 HOH D O   1 
HETATM 15098 O  O   . HOH UA 5 .   ? -24.05900 -31.71000 2.53700   1.000 57.75000  ? 714 HOH D O   1 
HETATM 15099 O  O   . HOH UA 5 .   ? -13.02200 1.31800   23.20800  1.000 49.50000  ? 715 HOH D O   1 
HETATM 15100 O  O   . HOH UA 5 .   ? -27.09800 22.60000  24.06500  1.000 77.63000  ? 716 HOH D O   1 
HETATM 15101 O  O   . HOH UA 5 .   ? -20.52700 -15.04900 -1.49000  1.000 55.71000  ? 717 HOH D O   1 
HETATM 15102 O  O   . HOH UA 5 .   ? -40.95000 12.09300  4.00800   1.000 50.66000  ? 718 HOH D O   1 
HETATM 15103 O  O   . HOH UA 5 .   ? -39.65900 -1.34000  13.75300  1.000 62.45000  ? 719 HOH D O   1 
HETATM 15104 O  O   . HOH UA 5 .   ? -12.79300 -2.58100  14.62400  1.000 54.30000  ? 720 HOH D O   1 
HETATM 15105 O  O   . HOH UA 5 .   ? -35.07500 5.03000   -10.96300 1.000 57.16000  ? 721 HOH D O   1 
HETATM 15106 O  O   . HOH UA 5 .   ? -21.01300 14.94400  43.40200  1.000 66.25000  ? 722 HOH D O   1 
HETATM 15107 O  O   . HOH UA 5 .   ? -6.19800  -12.68700 -3.89800  1.000 63.14000  ? 723 HOH D O   1 
HETATM 15108 O  O   . HOH UA 5 .   ? -21.87300 -32.10000 4.41200   1.000 51.83000  ? 724 HOH D O   1 
HETATM 15109 O  O   . HOH UA 5 .   ? -7.06800  -8.48900  9.82000   1.000 48.14000  ? 725 HOH D O   1 
HETATM 15110 O  O   . HOH UA 5 .   ? -4.64000  -8.94600  -5.73900  1.000 59.69000  ? 726 HOH D O   1 
HETATM 15111 O  O   . HOH UA 5 .   ? -15.80800 -0.62900  20.47000  1.000 52.42000  ? 727 HOH D O   1 
HETATM 15112 O  O   . HOH UA 5 .   ? -3.90800  15.93200  35.24700  1.000 50.45000  ? 728 HOH D O   1 
HETATM 15113 O  O   . HOH UA 5 .   ? -41.42300 7.15600   2.04500   1.000 74.34000  ? 729 HOH D O   1 
HETATM 15114 O  O   . HOH UA 5 .   ? -15.97700 -17.95100 -7.25700  1.000 66.93000  ? 730 HOH D O   1 
HETATM 15115 O  O   A HOH UA 5 .   ? -9.48000  -23.74800 -5.65100  0.500 44.99000  ? 731 HOH D O   1 
HETATM 15116 O  O   B HOH UA 5 .   ? -7.82800  -24.72400 -6.62200  0.500 39.77000  ? 731 HOH D O   1 
HETATM 15117 O  O   . HOH UA 5 .   ? -18.35500 28.36700  33.70200  1.000 74.69000  ? 732 HOH D O   1 
HETATM 15118 O  O   . HOH UA 5 .   ? -21.94800 -16.97800 -4.01700  1.000 34.89000  ? 733 HOH D O   1 
HETATM 15119 O  O   . HOH UA 5 .   ? -1.54400  2.11300   20.41000  1.000 60.84000  ? 734 HOH D O   1 
HETATM 15120 O  O   . HOH UA 5 .   ? -16.57700 32.06600  41.49700  1.000 71.74000  ? 735 HOH D O   1 
# 
