data_9HH4
# 
_entry.id   9HH4 
# 
_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   9HH4         pdb_00009hh4 10.2210/pdb9hh4/pdb 
WWPDB D_1292143240 ?            ?                   
# 
_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                        9HH4 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-21 
_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 ? 
'Czjzek, M.'      2 ? 
'Michel, G.'      3 ? 
'Ficko-Blean, E.' 4 ? 
# 
_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' 54778.480 4    3.1.6.- ? ? ? 
2 branched    syn 
;3,6-anhydro-alpha-D-galactopyranose-(1-3)-beta-D-galactopyranose-(1-4)-3,6-anhydro-alpha-D-galactopyranose-(1-3)-4-O-sulfo-beta-D-galactopyranose
;
710.611   4    ?       ? ? ? 
3 non-polymer man 'CALCIUM ION' 40.078    4    ?       ? ? ? 
4 non-polymer man 'BROMIDE ION' 79.904    12   ?       ? ? ? 
5 non-polymer syn 'CHLORIDE ION' 35.453    21   ?       ? ? ? 
6 non-polymer syn GLYCEROL 92.094    7    ?       ? ? ? 
7 water       nat water 18.015    1517 ?       ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MGSSHHHHHHGSQETRPNILVVLCDDLGYADVGFNGSTDILTPELDNLAQNGSIFTSAYVAHPF(OSE)GPSRSAILTGR
YPHLTGTAYNLFHNSSEDDKDNMGVPVEETYMSKVLQNAGYYTSAIGKWHLGAAPKFHPNKRGFDDFYGFLGGGHDYFPS
EYQKTYKAQKKAGNPNIRDYVFPMEHNGKPANETEYITDGFSREAIKNIKIAAAKKQPFFIYLAYNAPHVPLQAKAEDVA
KFAHIKDKDRRTYAAMVYAVDRGVGKIVQTLKETKQFDNTLIVFLSDNGGNFNHGANNYPLKGTKGDTWEGGYRVPMFFH
WPKKIKKDQRFDFPVSSLDLYPTFTGLAEAKLPKGKQLDGKNIMDDVLKNTEPYKDEMIYSLRYREGYNDVGARMGDWKI
TRMGNEPWRLHNITQDIGEKKNLAGRYPDRLKEMIAKTQEWTKSFVKPLWVYSVKDKELWESGQMPNYEATFEVDKLVDS
PYHK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHGSQETRPNILVVLCDDLGYADVGFNGSTDILTPELDNLAQNGSIFTSAYVAHPFSGPSRSAILTGRYPHL
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 
3 'CALCIUM ION'  CA  
4 'BROMIDE ION'  BR  
5 'CHLORIDE ION' CL  
6 GLYCEROL       GOL 
7 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  OSE n 
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                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
_pdbx_entity_branch_descriptor.ordinal           1 
_pdbx_entity_branch_descriptor.entity_id         2 
_pdbx_entity_branch_descriptor.descriptor        
'WURCS=2.0/3,4,3/[a2112h-1b_1-5_4*OSO/3=O/3=O][a2112h-1a_1-5_3-6][a2112h-1b_1-5]/1-2-3-2/a3-b1_b4-c1_c3-d1' 
_pdbx_entity_branch_descriptor.type              WURCS 
_pdbx_entity_branch_descriptor.program           PDB2Glycan 
_pdbx_entity_branch_descriptor.program_version   1.1.0 
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 9RN C1 O1 1 G4S O3 HO3 sing ? 
2 2 3 GAL C1 O1 2 9RN O4 HO4 sing ? 
3 2 4 9RN C1 O1 3 GAL O3 HO3 sing ? 
# 
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 
9RN 'D-saccharide, alpha linking' . 3,6-anhydro-alpha-D-galactopyranose ? 'C6 H10 O5'      162.141 
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 
G4S 'D-saccharide, beta linking'  n 4-O-sulfo-beta-D-galactopyranose    
'4-O-sulfo-beta-D-galactose; 4-O-sulfo-D-galactose; 4-O-sulfo-galactose' 'C6 H12 O9 S'    260.219 
GAL 'D-saccharide, beta linking'  . beta-D-galactopyranose              'beta-D-galactose; D-galactose; galactose' 'C6 H12 O6' 
180.156 
GLN 'L-peptide linking'           y GLUTAMINE                           ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID'                     ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'             y GLYCINE                             ? 'C2 H5 N O2'     75.067  
GOL non-polymer                   . GLYCEROL                            'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking'           y HISTIDINE                           ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                   . WATER                               ? 'H2 O'           18.015  
ILE 'L-peptide linking'           y ISOLEUCINE                          ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'           y LEUCINE                             ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'           y LYSINE                              ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'           y METHIONINE                          ? 'C5 H11 N O2 S'  149.211 
OSE 'L-peptide linking'           n O-SULFO-L-SERINE                    ? 'C3 H7 N O6 S'   185.156 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
G4S 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 'DGalp[4S]b'                
G4S 'COMMON NAME'                         GMML     1.0 4-sulfo-b-D-galactopyranose 
G4S 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Galp4SO3                
GAL 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGalpb                      
GAL 'COMMON NAME'                         GMML     1.0 b-D-galactopyranose         
GAL 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Galp                    
GAL 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Gal                         
# 
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  45  GLU GLU 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  OSE 65  96  96  OSE OSE A . n 
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  45  GLU GLU 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  OSE 65  96  96  OSE OSE B . n 
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 479 510 510 HIS HIS 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  OSE 65  96  96  OSE OSE C . n 
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  45  GLU GLU 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  OSE 65  96  96  OSE OSE D . n 
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 479 510 510 HIS HIS D . n 
D 1 480 LYS 480 511 ?   ?   ?   D . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
E 2 G4S 1 I G4S 1 I G4S 1 n 
E 2 9RN 2 I 9RN 2 I 9RN 2 n 
E 2 GAL 3 I GAL 3 I GAL 3 n 
E 2 9RN 4 I 9RN 4 I 9RN 4 n 
F 2 G4S 1 J G4S 1 J G4S 1 n 
F 2 9RN 2 J 9RN 2 J 9RN 2 n 
F 2 GAL 3 J GAL 3 J GAL 3 n 
F 2 9RN 4 J 9RN 4 J 9RN 4 n 
G 2 G4S 1 K G4S 1 K G4S 1 n 
G 2 9RN 2 K 9RN 2 K 9RN 2 n 
G 2 GAL 3 K GAL 3 K GAL 3 n 
G 2 9RN 4 K 9RN 4 K 9RN 4 n 
H 2 G4S 1 L G4S 1 L G4S 1 n 
H 2 9RN 2 L 9RN 2 L 9RN 2 n 
H 2 GAL 3 L GAL 3 L GAL 3 n 
H 2 9RN 4 L 9RN 4 L 9RN 4 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 9RN ? ? 9RN ? ? 'SUBJECT OF INVESTIGATION' ? 
2 G4S ? ? G4S ? ? 'SUBJECT OF INVESTIGATION' ? 
3 GAL ? ? GAL ? ? 'SUBJECT OF INVESTIGATION' ? 
4 OSE ? ? OSE ? ? 'SUBJECT OF INVESTIGATION' ? 
5 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 
I  3 CA  1   601  1    CA  CA  A . 
J  4 BR  1   602  1    BR  BR  A . 
K  4 BR  1   603  3    BR  BR  A . 
L  4 BR  1   604  5    BR  BR  A . 
M  5 CL  1   605  2    CL  CL  A . 
N  5 CL  1   606  5    CL  CL  A . 
O  5 CL  1   607  7    CL  CL  A . 
P  5 CL  1   608  8    CL  CL  A . 
Q  5 CL  1   609  9    CL  CL  A . 
R  5 CL  1   610  11   CL  CL  A . 
S  5 CL  1   611  12   CL  CL  A . 
T  5 CL  1   612  21   CL  CL  A . 
U  6 GOL 1   613  3    GOL GOL A . 
V  6 GOL 1   614  5    GOL GOL A . 
W  6 GOL 1   615  7    GOL GOL A . 
X  3 CA  1   601  2    CA  CA  B . 
Y  4 BR  1   602  2    BR  BR  B . 
Z  4 BR  1   603  4    BR  BR  B . 
AA 4 BR  1   604  6    BR  BR  B . 
BA 5 CL  1   605  1    CL  CL  B . 
CA 5 CL  1   606  13   CL  CL  B . 
DA 5 CL  1   607  14   CL  CL  B . 
EA 5 CL  1   608  22   CL  CL  B . 
FA 6 GOL 1   609  2    GOL GOL B . 
GA 6 GOL 1   610  6    GOL GOL B . 
HA 3 CA  1   601  3    CA  CA  C . 
IA 4 BR  1   602  7    BR  BR  C . 
JA 4 BR  1   603  8    BR  BR  C . 
KA 4 BR  1   604  9    BR  BR  C . 
LA 5 CL  1   605  6    CL  CL  C . 
MA 5 CL  1   606  15   CL  CL  C . 
NA 5 CL  1   607  16   CL  CL  C . 
OA 5 CL  1   608  17   CL  CL  C . 
PA 5 CL  1   609  24   CL  CL  C . 
QA 3 CA  1   601  4    CA  CA  D . 
RA 4 BR  1   602  10   BR  BR  D . 
SA 4 BR  1   603  11   BR  BR  D . 
TA 4 BR  1   604  12   BR  BR  D . 
UA 5 CL  1   605  18   CL  CL  D . 
VA 5 CL  1   606  19   CL  CL  D . 
WA 5 CL  1   607  20   CL  CL  D . 
XA 5 CL  1   608  23   CL  CL  D . 
YA 6 GOL 1   609  1    GOL GOL D . 
ZA 6 GOL 1   610  4    GOL GOL D . 
AB 7 HOH 1   701  776  HOH HOH A . 
AB 7 HOH 2   702  873  HOH HOH A . 
AB 7 HOH 3   703  848  HOH HOH A . 
AB 7 HOH 4   704  1479 HOH HOH A . 
AB 7 HOH 5   705  1545 HOH HOH A . 
AB 7 HOH 6   706  1440 HOH HOH A . 
AB 7 HOH 7   707  1589 HOH HOH A . 
AB 7 HOH 8   708  988  HOH HOH A . 
AB 7 HOH 9   709  1119 HOH HOH A . 
AB 7 HOH 10  710  1181 HOH HOH A . 
AB 7 HOH 11  711  946  HOH HOH A . 
AB 7 HOH 12  712  870  HOH HOH A . 
AB 7 HOH 13  713  1084 HOH HOH A . 
AB 7 HOH 14  714  901  HOH HOH A . 
AB 7 HOH 15  715  1552 HOH HOH A . 
AB 7 HOH 16  716  299  HOH HOH A . 
AB 7 HOH 17  717  1163 HOH HOH A . 
AB 7 HOH 18  718  760  HOH HOH A . 
AB 7 HOH 19  719  866  HOH HOH A . 
AB 7 HOH 20  720  788  HOH HOH A . 
AB 7 HOH 21  721  34   HOH HOH A . 
AB 7 HOH 22  722  112  HOH HOH A . 
AB 7 HOH 23  723  807  HOH HOH A . 
AB 7 HOH 24  724  561  HOH HOH A . 
AB 7 HOH 25  725  408  HOH HOH A . 
AB 7 HOH 26  726  60   HOH HOH A . 
AB 7 HOH 27  727  932  HOH HOH A . 
AB 7 HOH 28  728  1283 HOH HOH A . 
AB 7 HOH 29  729  1491 HOH HOH A . 
AB 7 HOH 30  730  777  HOH HOH A . 
AB 7 HOH 31  731  286  HOH HOH A . 
AB 7 HOH 32  732  1065 HOH HOH A . 
AB 7 HOH 33  733  80   HOH HOH A . 
AB 7 HOH 34  734  531  HOH HOH A . 
AB 7 HOH 35  735  202  HOH HOH A . 
AB 7 HOH 36  736  358  HOH HOH A . 
AB 7 HOH 37  737  1146 HOH HOH A . 
AB 7 HOH 38  738  379  HOH HOH A . 
AB 7 HOH 39  739  783  HOH HOH A . 
AB 7 HOH 40  740  1112 HOH HOH A . 
AB 7 HOH 41  741  764  HOH HOH A . 
AB 7 HOH 42  742  137  HOH HOH A . 
AB 7 HOH 43  743  122  HOH HOH A . 
AB 7 HOH 44  744  636  HOH HOH A . 
AB 7 HOH 45  745  37   HOH HOH A . 
AB 7 HOH 46  746  1557 HOH HOH A . 
AB 7 HOH 47  747  388  HOH HOH A . 
AB 7 HOH 48  748  438  HOH HOH A . 
AB 7 HOH 49  749  646  HOH HOH A . 
AB 7 HOH 50  750  42   HOH HOH A . 
AB 7 HOH 51  751  542  HOH HOH A . 
AB 7 HOH 52  752  1012 HOH HOH A . 
AB 7 HOH 53  753  407  HOH HOH A . 
AB 7 HOH 54  754  790  HOH HOH A . 
AB 7 HOH 55  755  123  HOH HOH A . 
AB 7 HOH 56  756  181  HOH HOH A . 
AB 7 HOH 57  757  816  HOH HOH A . 
AB 7 HOH 58  758  827  HOH HOH A . 
AB 7 HOH 59  759  119  HOH HOH A . 
AB 7 HOH 60  760  479  HOH HOH A . 
AB 7 HOH 61  761  476  HOH HOH A . 
AB 7 HOH 62  762  963  HOH HOH A . 
AB 7 HOH 63  763  949  HOH HOH A . 
AB 7 HOH 64  764  265  HOH HOH A . 
AB 7 HOH 65  765  67   HOH HOH A . 
AB 7 HOH 66  766  445  HOH HOH A . 
AB 7 HOH 67  767  89   HOH HOH A . 
AB 7 HOH 68  768  160  HOH HOH A . 
AB 7 HOH 69  769  778  HOH HOH A . 
AB 7 HOH 70  770  702  HOH HOH A . 
AB 7 HOH 71  771  226  HOH HOH A . 
AB 7 HOH 72  772  837  HOH HOH A . 
AB 7 HOH 73  773  784  HOH HOH A . 
AB 7 HOH 74  774  1573 HOH HOH A . 
AB 7 HOH 75  775  159  HOH HOH A . 
AB 7 HOH 76  776  936  HOH HOH A . 
AB 7 HOH 77  777  532  HOH HOH A . 
AB 7 HOH 78  778  1127 HOH HOH A . 
AB 7 HOH 79  779  762  HOH HOH A . 
AB 7 HOH 80  780  315  HOH HOH A . 
AB 7 HOH 81  781  955  HOH HOH A . 
AB 7 HOH 82  782  251  HOH HOH A . 
AB 7 HOH 83  783  415  HOH HOH A . 
AB 7 HOH 84  784  1063 HOH HOH A . 
AB 7 HOH 85  785  206  HOH HOH A . 
AB 7 HOH 86  786  377  HOH HOH A . 
AB 7 HOH 87  787  923  HOH HOH A . 
AB 7 HOH 88  788  120  HOH HOH A . 
AB 7 HOH 89  789  48   HOH HOH A . 
AB 7 HOH 90  790  260  HOH HOH A . 
AB 7 HOH 91  791  921  HOH HOH A . 
AB 7 HOH 92  792  931  HOH HOH A . 
AB 7 HOH 93  793  818  HOH HOH A . 
AB 7 HOH 94  794  250  HOH HOH A . 
AB 7 HOH 95  795  953  HOH HOH A . 
AB 7 HOH 96  796  766  HOH HOH A . 
AB 7 HOH 97  797  851  HOH HOH A . 
AB 7 HOH 98  798  975  HOH HOH A . 
AB 7 HOH 99  799  1572 HOH HOH A . 
AB 7 HOH 100 800  860  HOH HOH A . 
AB 7 HOH 101 801  1054 HOH HOH A . 
AB 7 HOH 102 802  1214 HOH HOH A . 
AB 7 HOH 103 803  14   HOH HOH A . 
AB 7 HOH 104 804  836  HOH HOH A . 
AB 7 HOH 105 805  1347 HOH HOH A . 
AB 7 HOH 106 806  896  HOH HOH A . 
AB 7 HOH 107 807  83   HOH HOH A . 
AB 7 HOH 108 808  1451 HOH HOH A . 
AB 7 HOH 109 809  266  HOH HOH A . 
AB 7 HOH 110 810  157  HOH HOH A . 
AB 7 HOH 111 811  887  HOH HOH A . 
AB 7 HOH 112 812  191  HOH HOH A . 
AB 7 HOH 113 813  617  HOH HOH A . 
AB 7 HOH 114 814  404  HOH HOH A . 
AB 7 HOH 115 815  391  HOH HOH A . 
AB 7 HOH 116 816  5    HOH HOH A . 
AB 7 HOH 117 817  1116 HOH HOH A . 
AB 7 HOH 118 818  22   HOH HOH A . 
AB 7 HOH 119 819  513  HOH HOH A . 
AB 7 HOH 120 820  814  HOH HOH A . 
AB 7 HOH 121 821  41   HOH HOH A . 
AB 7 HOH 122 822  514  HOH HOH A . 
AB 7 HOH 123 823  252  HOH HOH A . 
AB 7 HOH 124 824  472  HOH HOH A . 
AB 7 HOH 125 825  362  HOH HOH A . 
AB 7 HOH 126 826  1103 HOH HOH A . 
AB 7 HOH 127 827  268  HOH HOH A . 
AB 7 HOH 128 828  1032 HOH HOH A . 
AB 7 HOH 129 829  86   HOH HOH A . 
AB 7 HOH 130 830  895  HOH HOH A . 
AB 7 HOH 131 831  79   HOH HOH A . 
AB 7 HOH 132 832  761  HOH HOH A . 
AB 7 HOH 133 833  915  HOH HOH A . 
AB 7 HOH 134 834  990  HOH HOH A . 
AB 7 HOH 135 835  834  HOH HOH A . 
AB 7 HOH 136 836  305  HOH HOH A . 
AB 7 HOH 137 837  106  HOH HOH A . 
AB 7 HOH 138 838  559  HOH HOH A . 
AB 7 HOH 139 839  422  HOH HOH A . 
AB 7 HOH 140 840  838  HOH HOH A . 
AB 7 HOH 141 841  810  HOH HOH A . 
AB 7 HOH 142 842  555  HOH HOH A . 
AB 7 HOH 143 843  1124 HOH HOH A . 
AB 7 HOH 144 844  470  HOH HOH A . 
AB 7 HOH 145 845  170  HOH HOH A . 
AB 7 HOH 146 846  765  HOH HOH A . 
AB 7 HOH 147 847  875  HOH HOH A . 
AB 7 HOH 148 848  218  HOH HOH A . 
AB 7 HOH 149 849  1134 HOH HOH A . 
AB 7 HOH 150 850  916  HOH HOH A . 
AB 7 HOH 151 851  710  HOH HOH A . 
AB 7 HOH 152 852  1009 HOH HOH A . 
AB 7 HOH 153 853  359  HOH HOH A . 
AB 7 HOH 154 854  427  HOH HOH A . 
AB 7 HOH 155 855  1139 HOH HOH A . 
AB 7 HOH 156 856  464  HOH HOH A . 
AB 7 HOH 157 857  1394 HOH HOH A . 
AB 7 HOH 158 858  69   HOH HOH A . 
AB 7 HOH 159 859  763  HOH HOH A . 
AB 7 HOH 160 860  40   HOH HOH A . 
AB 7 HOH 161 861  868  HOH HOH A . 
AB 7 HOH 162 862  852  HOH HOH A . 
AB 7 HOH 163 863  770  HOH HOH A . 
AB 7 HOH 164 864  152  HOH HOH A . 
AB 7 HOH 165 865  819  HOH HOH A . 
AB 7 HOH 166 866  826  HOH HOH A . 
AB 7 HOH 167 867  966  HOH HOH A . 
AB 7 HOH 168 868  1069 HOH HOH A . 
AB 7 HOH 169 869  222  HOH HOH A . 
AB 7 HOH 170 870  138  HOH HOH A . 
AB 7 HOH 171 871  231  HOH HOH A . 
AB 7 HOH 172 872  323  HOH HOH A . 
AB 7 HOH 173 873  616  HOH HOH A . 
AB 7 HOH 174 874  232  HOH HOH A . 
AB 7 HOH 175 875  1324 HOH HOH A . 
AB 7 HOH 176 876  107  HOH HOH A . 
AB 7 HOH 177 877  43   HOH HOH A . 
AB 7 HOH 178 878  782  HOH HOH A . 
AB 7 HOH 179 879  278  HOH HOH A . 
AB 7 HOH 180 880  767  HOH HOH A . 
AB 7 HOH 181 881  992  HOH HOH A . 
AB 7 HOH 182 882  1105 HOH HOH A . 
AB 7 HOH 183 883  1360 HOH HOH A . 
AB 7 HOH 184 884  861  HOH HOH A . 
AB 7 HOH 185 885  809  HOH HOH A . 
AB 7 HOH 186 886  1072 HOH HOH A . 
AB 7 HOH 187 887  581  HOH HOH A . 
AB 7 HOH 188 888  1392 HOH HOH A . 
AB 7 HOH 189 889  792  HOH HOH A . 
AB 7 HOH 190 890  227  HOH HOH A . 
AB 7 HOH 191 891  772  HOH HOH A . 
AB 7 HOH 192 892  619  HOH HOH A . 
AB 7 HOH 193 893  351  HOH HOH A . 
AB 7 HOH 194 894  892  HOH HOH A . 
AB 7 HOH 195 895  841  HOH HOH A . 
AB 7 HOH 196 896  972  HOH HOH A . 
AB 7 HOH 197 897  1158 HOH HOH A . 
AB 7 HOH 198 898  547  HOH HOH A . 
AB 7 HOH 199 899  1189 HOH HOH A . 
AB 7 HOH 200 900  91   HOH HOH A . 
AB 7 HOH 201 901  840  HOH HOH A . 
AB 7 HOH 202 902  72   HOH HOH A . 
AB 7 HOH 203 903  900  HOH HOH A . 
AB 7 HOH 204 904  905  HOH HOH A . 
AB 7 HOH 205 905  885  HOH HOH A . 
AB 7 HOH 206 906  77   HOH HOH A . 
AB 7 HOH 207 907  214  HOH HOH A . 
AB 7 HOH 208 908  1118 HOH HOH A . 
AB 7 HOH 209 909  598  HOH HOH A . 
AB 7 HOH 210 910  297  HOH HOH A . 
AB 7 HOH 211 911  147  HOH HOH A . 
AB 7 HOH 212 912  983  HOH HOH A . 
AB 7 HOH 213 913  402  HOH HOH A . 
AB 7 HOH 214 914  759  HOH HOH A . 
AB 7 HOH 215 915  697  HOH HOH A . 
AB 7 HOH 216 916  1014 HOH HOH A . 
AB 7 HOH 217 917  420  HOH HOH A . 
AB 7 HOH 218 918  831  HOH HOH A . 
AB 7 HOH 219 919  835  HOH HOH A . 
AB 7 HOH 220 920  1073 HOH HOH A . 
AB 7 HOH 221 921  871  HOH HOH A . 
AB 7 HOH 222 922  894  HOH HOH A . 
AB 7 HOH 223 923  878  HOH HOH A . 
AB 7 HOH 224 924  849  HOH HOH A . 
AB 7 HOH 225 925  919  HOH HOH A . 
AB 7 HOH 226 926  302  HOH HOH A . 
AB 7 HOH 227 927  1358 HOH HOH A . 
AB 7 HOH 228 928  1150 HOH HOH A . 
AB 7 HOH 229 929  363  HOH HOH A . 
AB 7 HOH 230 930  546  HOH HOH A . 
AB 7 HOH 231 931  1166 HOH HOH A . 
AB 7 HOH 232 932  2    HOH HOH A . 
AB 7 HOH 233 933  1020 HOH HOH A . 
AB 7 HOH 234 934  842  HOH HOH A . 
AB 7 HOH 235 935  1102 HOH HOH A . 
AB 7 HOH 236 936  1330 HOH HOH A . 
AB 7 HOH 237 937  1193 HOH HOH A . 
AB 7 HOH 238 938  948  HOH HOH A . 
AB 7 HOH 239 939  785  HOH HOH A . 
AB 7 HOH 240 940  262  HOH HOH A . 
AB 7 HOH 241 941  1582 HOH HOH A . 
AB 7 HOH 242 942  1423 HOH HOH A . 
AB 7 HOH 243 943  881  HOH HOH A . 
AB 7 HOH 244 944  1321 HOH HOH A . 
AB 7 HOH 245 945  276  HOH HOH A . 
AB 7 HOH 246 946  1467 HOH HOH A . 
AB 7 HOH 247 947  21   HOH HOH A . 
AB 7 HOH 248 948  806  HOH HOH A . 
AB 7 HOH 249 949  917  HOH HOH A . 
AB 7 HOH 250 950  943  HOH HOH A . 
AB 7 HOH 251 951  795  HOH HOH A . 
AB 7 HOH 252 952  461  HOH HOH A . 
AB 7 HOH 253 953  1172 HOH HOH A . 
AB 7 HOH 254 954  879  HOH HOH A . 
AB 7 HOH 255 955  228  HOH HOH A . 
AB 7 HOH 256 956  529  HOH HOH A . 
AB 7 HOH 257 957  859  HOH HOH A . 
AB 7 HOH 258 958  771  HOH HOH A . 
AB 7 HOH 259 959  830  HOH HOH A . 
AB 7 HOH 260 960  1157 HOH HOH A . 
AB 7 HOH 261 961  789  HOH HOH A . 
AB 7 HOH 262 962  758  HOH HOH A . 
AB 7 HOH 263 963  1251 HOH HOH A . 
AB 7 HOH 264 964  20   HOH HOH A . 
AB 7 HOH 265 965  503  HOH HOH A . 
AB 7 HOH 266 966  44   HOH HOH A . 
AB 7 HOH 267 967  9    HOH HOH A . 
AB 7 HOH 268 968  188  HOH HOH A . 
AB 7 HOH 269 969  769  HOH HOH A . 
AB 7 HOH 270 970  723  HOH HOH A . 
AB 7 HOH 271 971  1371 HOH HOH A . 
AB 7 HOH 272 972  1306 HOH HOH A . 
AB 7 HOH 273 973  1344 HOH HOH A . 
AB 7 HOH 274 974  1122 HOH HOH A . 
AB 7 HOH 275 975  1010 HOH HOH A . 
AB 7 HOH 276 976  566  HOH HOH A . 
AB 7 HOH 277 977  802  HOH HOH A . 
AB 7 HOH 278 978  956  HOH HOH A . 
AB 7 HOH 279 979  1286 HOH HOH A . 
AB 7 HOH 280 980  1129 HOH HOH A . 
AB 7 HOH 281 981  81   HOH HOH A . 
AB 7 HOH 282 982  1051 HOH HOH A . 
AB 7 HOH 283 983  1388 HOH HOH A . 
AB 7 HOH 284 984  677  HOH HOH A . 
AB 7 HOH 285 985  1039 HOH HOH A . 
AB 7 HOH 286 986  171  HOH HOH A . 
AB 7 HOH 287 987  1369 HOH HOH A . 
AB 7 HOH 288 988  1349 HOH HOH A . 
AB 7 HOH 289 989  1263 HOH HOH A . 
AB 7 HOH 290 990  908  HOH HOH A . 
AB 7 HOH 291 991  1088 HOH HOH A . 
AB 7 HOH 292 992  700  HOH HOH A . 
AB 7 HOH 293 993  1391 HOH HOH A . 
AB 7 HOH 294 994  1174 HOH HOH A . 
AB 7 HOH 295 995  1244 HOH HOH A . 
AB 7 HOH 296 996  348  HOH HOH A . 
AB 7 HOH 297 997  582  HOH HOH A . 
AB 7 HOH 298 998  768  HOH HOH A . 
AB 7 HOH 299 999  1115 HOH HOH A . 
AB 7 HOH 300 1000 1515 HOH HOH A . 
AB 7 HOH 301 1001 844  HOH HOH A . 
AB 7 HOH 302 1002 924  HOH HOH A . 
AB 7 HOH 303 1003 1042 HOH HOH A . 
AB 7 HOH 304 1004 1531 HOH HOH A . 
AB 7 HOH 305 1005 1477 HOH HOH A . 
AB 7 HOH 306 1006 1167 HOH HOH A . 
AB 7 HOH 307 1007 1346 HOH HOH A . 
AB 7 HOH 308 1008 258  HOH HOH A . 
AB 7 HOH 309 1009 1433 HOH HOH A . 
AB 7 HOH 310 1010 1319 HOH HOH A . 
AB 7 HOH 311 1011 1168 HOH HOH A . 
AB 7 HOH 312 1012 750  HOH HOH A . 
AB 7 HOH 313 1013 927  HOH HOH A . 
AB 7 HOH 314 1014 1512 HOH HOH A . 
AB 7 HOH 315 1015 1209 HOH HOH A . 
AB 7 HOH 316 1016 1023 HOH HOH A . 
AB 7 HOH 317 1017 1514 HOH HOH A . 
AB 7 HOH 318 1018 1497 HOH HOH A . 
AB 7 HOH 319 1019 1343 HOH HOH A . 
AB 7 HOH 320 1020 1390 HOH HOH A . 
AB 7 HOH 321 1021 1087 HOH HOH A . 
AB 7 HOH 322 1022 1322 HOH HOH A . 
AB 7 HOH 323 1023 829  HOH HOH A . 
AB 7 HOH 324 1024 1377 HOH HOH A . 
AB 7 HOH 325 1025 1553 HOH HOH A . 
AB 7 HOH 326 1026 1480 HOH HOH A . 
AB 7 HOH 327 1027 1194 HOH HOH A . 
AB 7 HOH 328 1028 1444 HOH HOH A . 
AB 7 HOH 329 1029 938  HOH HOH A . 
AB 7 HOH 330 1030 1220 HOH HOH A . 
AB 7 HOH 331 1031 1292 HOH HOH A . 
AB 7 HOH 332 1032 1473 HOH HOH A . 
AB 7 HOH 333 1033 1389 HOH HOH A . 
AB 7 HOH 334 1034 1320 HOH HOH A . 
AB 7 HOH 335 1035 882  HOH HOH A . 
AB 7 HOH 336 1036 876  HOH HOH A . 
AB 7 HOH 337 1037 958  HOH HOH A . 
AB 7 HOH 338 1038 1442 HOH HOH A . 
AB 7 HOH 339 1039 1453 HOH HOH A . 
AB 7 HOH 340 1040 340  HOH HOH A . 
AB 7 HOH 341 1041 1474 HOH HOH A . 
AB 7 HOH 342 1042 1345 HOH HOH A . 
AB 7 HOH 343 1043 1511 HOH HOH A . 
AB 7 HOH 344 1044 1067 HOH HOH A . 
AB 7 HOH 345 1045 941  HOH HOH A . 
AB 7 HOH 346 1046 1487 HOH HOH A . 
AB 7 HOH 347 1047 486  HOH HOH A . 
AB 7 HOH 348 1048 1400 HOH HOH A . 
AB 7 HOH 349 1049 1380 HOH HOH A . 
AB 7 HOH 350 1050 45   HOH HOH A . 
AB 7 HOH 351 1051 1259 HOH HOH A . 
AB 7 HOH 352 1052 1519 HOH HOH A . 
AB 7 HOH 353 1053 1481 HOH HOH A . 
AB 7 HOH 354 1054 1570 HOH HOH A . 
AB 7 HOH 355 1055 1414 HOH HOH A . 
AB 7 HOH 356 1056 257  HOH HOH A . 
AB 7 HOH 357 1057 1350 HOH HOH A . 
AB 7 HOH 358 1058 1430 HOH HOH A . 
AB 7 HOH 359 1059 1339 HOH HOH A . 
AB 7 HOH 360 1060 1161 HOH HOH A . 
AB 7 HOH 361 1061 950  HOH HOH A . 
AB 7 HOH 362 1062 1494 HOH HOH A . 
AB 7 HOH 363 1063 1510 HOH HOH A . 
AB 7 HOH 364 1064 1227 HOH HOH A . 
AB 7 HOH 365 1065 430  HOH HOH A . 
AB 7 HOH 366 1066 609  HOH HOH A . 
AB 7 HOH 367 1067 742  HOH HOH A . 
AB 7 HOH 368 1068 1478 HOH HOH A . 
AB 7 HOH 369 1069 507  HOH HOH A . 
AB 7 HOH 370 1070 1476 HOH HOH A . 
AB 7 HOH 371 1071 823  HOH HOH A . 
AB 7 HOH 372 1072 1061 HOH HOH A . 
AB 7 HOH 373 1073 1036 HOH HOH A . 
AB 7 HOH 374 1074 1132 HOH HOH A . 
AB 7 HOH 375 1075 1443 HOH HOH A . 
AB 7 HOH 376 1076 1234 HOH HOH A . 
AB 7 HOH 377 1077 740  HOH HOH A . 
AB 7 HOH 378 1078 1059 HOH HOH A . 
AB 7 HOH 379 1079 1109 HOH HOH A . 
AB 7 HOH 380 1080 805  HOH HOH A . 
AB 7 HOH 381 1081 1004 HOH HOH A . 
AB 7 HOH 382 1082 417  HOH HOH A . 
AB 7 HOH 383 1083 1379 HOH HOH A . 
AB 7 HOH 384 1084 504  HOH HOH A . 
AB 7 HOH 385 1085 589  HOH HOH A . 
AB 7 HOH 386 1086 1464 HOH HOH A . 
AB 7 HOH 387 1087 1399 HOH HOH A . 
AB 7 HOH 388 1088 637  HOH HOH A . 
AB 7 HOH 389 1089 685  HOH HOH A . 
AB 7 HOH 390 1090 1513 HOH HOH A . 
AB 7 HOH 391 1091 1273 HOH HOH A . 
AB 7 HOH 392 1092 657  HOH HOH A . 
AB 7 HOH 393 1093 738  HOH HOH A . 
AB 7 HOH 394 1094 1013 HOH HOH A . 
AB 7 HOH 395 1095 982  HOH HOH A . 
AB 7 HOH 396 1096 449  HOH HOH A . 
AB 7 HOH 397 1097 675  HOH HOH A . 
AB 7 HOH 398 1098 737  HOH HOH A . 
AB 7 HOH 399 1099 911  HOH HOH A . 
AB 7 HOH 400 1100 1237 HOH HOH A . 
AB 7 HOH 401 1101 1314 HOH HOH A . 
AB 7 HOH 402 1102 1154 HOH HOH A . 
AB 7 HOH 403 1103 714  HOH HOH A . 
AB 7 HOH 404 1104 347  HOH HOH A . 
AB 7 HOH 405 1105 883  HOH HOH A . 
AB 7 HOH 406 1106 1431 HOH HOH A . 
AB 7 HOH 407 1107 749  HOH HOH A . 
AB 7 HOH 408 1108 954  HOH HOH A . 
AB 7 HOH 409 1109 910  HOH HOH A . 
AB 7 HOH 410 1110 242  HOH HOH A . 
AB 7 HOH 411 1111 1335 HOH HOH A . 
AB 7 HOH 412 1112 721  HOH HOH A . 
AB 7 HOH 413 1113 1332 HOH HOH A . 
AB 7 HOH 414 1114 1452 HOH HOH A . 
AB 7 HOH 415 1115 1024 HOH HOH A . 
AB 7 HOH 416 1116 1475 HOH HOH A . 
AB 7 HOH 417 1117 1471 HOH HOH A . 
AB 7 HOH 418 1118 969  HOH HOH A . 
AB 7 HOH 419 1119 1571 HOH HOH A . 
AB 7 HOH 420 1120 1277 HOH HOH A . 
AB 7 HOH 421 1121 459  HOH HOH A . 
AB 7 HOH 422 1122 1432 HOH HOH A . 
AB 7 HOH 423 1123 474  HOH HOH A . 
AB 7 HOH 424 1124 1294 HOH HOH A . 
AB 7 HOH 425 1125 971  HOH HOH A . 
BB 7 HOH 1   701  1508 HOH HOH B . 
BB 7 HOH 2   702  862  HOH HOH B . 
BB 7 HOH 3   703  1007 HOH HOH B . 
BB 7 HOH 4   704  1549 HOH HOH B . 
BB 7 HOH 5   705  719  HOH HOH B . 
BB 7 HOH 6   706  899  HOH HOH B . 
BB 7 HOH 7   707  1224 HOH HOH B . 
BB 7 HOH 8   708  1298 HOH HOH B . 
BB 7 HOH 9   709  981  HOH HOH B . 
BB 7 HOH 10  710  1198 HOH HOH B . 
BB 7 HOH 11  711  256  HOH HOH B . 
BB 7 HOH 12  712  884  HOH HOH B . 
BB 7 HOH 13  713  629  HOH HOH B . 
BB 7 HOH 14  714  890  HOH HOH B . 
BB 7 HOH 15  715  1447 HOH HOH B . 
BB 7 HOH 16  716  1258 HOH HOH B . 
BB 7 HOH 17  717  364  HOH HOH B . 
BB 7 HOH 18  718  121  HOH HOH B . 
BB 7 HOH 19  719  1091 HOH HOH B . 
BB 7 HOH 20  720  662  HOH HOH B . 
BB 7 HOH 21  721  165  HOH HOH B . 
BB 7 HOH 22  722  448  HOH HOH B . 
BB 7 HOH 23  723  1587 HOH HOH B . 
BB 7 HOH 24  724  979  HOH HOH B . 
BB 7 HOH 25  725  488  HOH HOH B . 
BB 7 HOH 26  726  1492 HOH HOH B . 
BB 7 HOH 27  727  1184 HOH HOH B . 
BB 7 HOH 28  728  1160 HOH HOH B . 
BB 7 HOH 29  729  962  HOH HOH B . 
BB 7 HOH 30  730  118  HOH HOH B . 
BB 7 HOH 31  731  1305 HOH HOH B . 
BB 7 HOH 32  732  63   HOH HOH B . 
BB 7 HOH 33  733  23   HOH HOH B . 
BB 7 HOH 34  734  639  HOH HOH B . 
BB 7 HOH 35  735  794  HOH HOH B . 
BB 7 HOH 36  736  111  HOH HOH B . 
BB 7 HOH 37  737  690  HOH HOH B . 
BB 7 HOH 38  738  177  HOH HOH B . 
BB 7 HOH 39  739  523  HOH HOH B . 
BB 7 HOH 40  740  754  HOH HOH B . 
BB 7 HOH 41  741  678  HOH HOH B . 
BB 7 HOH 42  742  354  HOH HOH B . 
BB 7 HOH 43  743  87   HOH HOH B . 
BB 7 HOH 44  744  117  HOH HOH B . 
BB 7 HOH 45  745  622  HOH HOH B . 
BB 7 HOH 46  746  565  HOH HOH B . 
BB 7 HOH 47  747  487  HOH HOH B . 
BB 7 HOH 48  748  140  HOH HOH B . 
BB 7 HOH 49  749  73   HOH HOH B . 
BB 7 HOH 50  750  167  HOH HOH B . 
BB 7 HOH 51  751  25   HOH HOH B . 
BB 7 HOH 52  752  400  HOH HOH B . 
BB 7 HOH 53  753  241  HOH HOH B . 
BB 7 HOH 54  754  334  HOH HOH B . 
BB 7 HOH 55  755  872  HOH HOH B . 
BB 7 HOH 56  756  1111 HOH HOH B . 
BB 7 HOH 57  757  272  HOH HOH B . 
BB 7 HOH 58  758  432  HOH HOH B . 
BB 7 HOH 59  759  110  HOH HOH B . 
BB 7 HOH 60  760  328  HOH HOH B . 
BB 7 HOH 61  761  357  HOH HOH B . 
BB 7 HOH 62  762  753  HOH HOH B . 
BB 7 HOH 63  763  95   HOH HOH B . 
BB 7 HOH 64  764  310  HOH HOH B . 
BB 7 HOH 65  765  1086 HOH HOH B . 
BB 7 HOH 66  766  93   HOH HOH B . 
BB 7 HOH 67  767  35   HOH HOH B . 
BB 7 HOH 68  768  279  HOH HOH B . 
BB 7 HOH 69  769  84   HOH HOH B . 
BB 7 HOH 70  770  71   HOH HOH B . 
BB 7 HOH 71  771  277  HOH HOH B . 
BB 7 HOH 72  772  563  HOH HOH B . 
BB 7 HOH 73  773  65   HOH HOH B . 
BB 7 HOH 74  774  562  HOH HOH B . 
BB 7 HOH 75  775  803  HOH HOH B . 
BB 7 HOH 76  776  935  HOH HOH B . 
BB 7 HOH 77  777  361  HOH HOH B . 
BB 7 HOH 78  778  425  HOH HOH B . 
BB 7 HOH 79  779  240  HOH HOH B . 
BB 7 HOH 80  780  426  HOH HOH B . 
BB 7 HOH 81  781  239  HOH HOH B . 
BB 7 HOH 82  782  274  HOH HOH B . 
BB 7 HOH 83  783  1048 HOH HOH B . 
BB 7 HOH 84  784  634  HOH HOH B . 
BB 7 HOH 85  785  17   HOH HOH B . 
BB 7 HOH 86  786  178  HOH HOH B . 
BB 7 HOH 87  787  38   HOH HOH B . 
BB 7 HOH 88  788  1008 HOH HOH B . 
BB 7 HOH 89  789  1066 HOH HOH B . 
BB 7 HOH 90  790  306  HOH HOH B . 
BB 7 HOH 91  791  301  HOH HOH B . 
BB 7 HOH 92  792  387  HOH HOH B . 
BB 7 HOH 93  793  554  HOH HOH B . 
BB 7 HOH 94  794  288  HOH HOH B . 
BB 7 HOH 95  795  49   HOH HOH B . 
BB 7 HOH 96  796  134  HOH HOH B . 
BB 7 HOH 97  797  325  HOH HOH B . 
BB 7 HOH 98  798  780  HOH HOH B . 
BB 7 HOH 99  799  141  HOH HOH B . 
BB 7 HOH 100 800  549  HOH HOH B . 
BB 7 HOH 101 801  115  HOH HOH B . 
BB 7 HOH 102 802  1543 HOH HOH B . 
BB 7 HOH 103 803  185  HOH HOH B . 
BB 7 HOH 104 804  298  HOH HOH B . 
BB 7 HOH 105 805  774  HOH HOH B . 
BB 7 HOH 106 806  27   HOH HOH B . 
BB 7 HOH 107 807  1254 HOH HOH B . 
BB 7 HOH 108 808  8    HOH HOH B . 
BB 7 HOH 109 809  798  HOH HOH B . 
BB 7 HOH 110 810  223  HOH HOH B . 
BB 7 HOH 111 811  78   HOH HOH B . 
BB 7 HOH 112 812  212  HOH HOH B . 
BB 7 HOH 113 813  174  HOH HOH B . 
BB 7 HOH 114 814  39   HOH HOH B . 
BB 7 HOH 115 815  441  HOH HOH B . 
BB 7 HOH 116 816  32   HOH HOH B . 
BB 7 HOH 117 817  1081 HOH HOH B . 
BB 7 HOH 118 818  756  HOH HOH B . 
BB 7 HOH 119 819  269  HOH HOH B . 
BB 7 HOH 120 820  811  HOH HOH B . 
BB 7 HOH 121 821  136  HOH HOH B . 
BB 7 HOH 122 822  976  HOH HOH B . 
BB 7 HOH 123 823  651  HOH HOH B . 
BB 7 HOH 124 824  522  HOH HOH B . 
BB 7 HOH 125 825  1125 HOH HOH B . 
BB 7 HOH 126 826  153  HOH HOH B . 
BB 7 HOH 127 827  373  HOH HOH B . 
BB 7 HOH 128 828  16   HOH HOH B . 
BB 7 HOH 129 829  1058 HOH HOH B . 
BB 7 HOH 130 830  1064 HOH HOH B . 
BB 7 HOH 131 831  519  HOH HOH B . 
BB 7 HOH 132 832  1028 HOH HOH B . 
BB 7 HOH 133 833  225  HOH HOH B . 
BB 7 HOH 134 834  1022 HOH HOH B . 
BB 7 HOH 135 835  1247 HOH HOH B . 
BB 7 HOH 136 836  284  HOH HOH B . 
BB 7 HOH 137 837  101  HOH HOH B . 
BB 7 HOH 138 838  36   HOH HOH B . 
BB 7 HOH 139 839  434  HOH HOH B . 
BB 7 HOH 140 840  197  HOH HOH B . 
BB 7 HOH 141 841  28   HOH HOH B . 
BB 7 HOH 142 842  4    HOH HOH B . 
BB 7 HOH 143 843  601  HOH HOH B . 
BB 7 HOH 144 844  61   HOH HOH B . 
BB 7 HOH 145 845  203  HOH HOH B . 
BB 7 HOH 146 846  329  HOH HOH B . 
BB 7 HOH 147 847  454  HOH HOH B . 
BB 7 HOH 148 848  463  HOH HOH B . 
BB 7 HOH 149 849  1221 HOH HOH B . 
BB 7 HOH 150 850  824  HOH HOH B . 
BB 7 HOH 151 851  644  HOH HOH B . 
BB 7 HOH 152 852  458  HOH HOH B . 
BB 7 HOH 153 853  82   HOH HOH B . 
BB 7 HOH 154 854  952  HOH HOH B . 
BB 7 HOH 155 855  1164 HOH HOH B . 
BB 7 HOH 156 856  113  HOH HOH B . 
BB 7 HOH 157 857  1056 HOH HOH B . 
BB 7 HOH 158 858  1190 HOH HOH B . 
BB 7 HOH 159 859  967  HOH HOH B . 
BB 7 HOH 160 860  173  HOH HOH B . 
BB 7 HOH 161 861  502  HOH HOH B . 
BB 7 HOH 162 862  620  HOH HOH B . 
BB 7 HOH 163 863  236  HOH HOH B . 
BB 7 HOH 164 864  922  HOH HOH B . 
BB 7 HOH 165 865  567  HOH HOH B . 
BB 7 HOH 166 866  1359 HOH HOH B . 
BB 7 HOH 167 867  145  HOH HOH B . 
BB 7 HOH 168 868  15   HOH HOH B . 
BB 7 HOH 169 869  124  HOH HOH B . 
BB 7 HOH 170 870  465  HOH HOH B . 
BB 7 HOH 171 871  602  HOH HOH B . 
BB 7 HOH 172 872  215  HOH HOH B . 
BB 7 HOH 173 873  144  HOH HOH B . 
BB 7 HOH 174 874  752  HOH HOH B . 
BB 7 HOH 175 875  196  HOH HOH B . 
BB 7 HOH 176 876  670  HOH HOH B . 
BB 7 HOH 177 877  142  HOH HOH B . 
BB 7 HOH 178 878  116  HOH HOH B . 
BB 7 HOH 179 879  1368 HOH HOH B . 
BB 7 HOH 180 880  169  HOH HOH B . 
BB 7 HOH 181 881  352  HOH HOH B . 
BB 7 HOH 182 882  335  HOH HOH B . 
BB 7 HOH 183 883  1016 HOH HOH B . 
BB 7 HOH 184 884  571  HOH HOH B . 
BB 7 HOH 185 885  755  HOH HOH B . 
BB 7 HOH 186 886  31   HOH HOH B . 
BB 7 HOH 187 887  413  HOH HOH B . 
BB 7 HOH 188 888  210  HOH HOH B . 
BB 7 HOH 189 889  1162 HOH HOH B . 
BB 7 HOH 190 890  349  HOH HOH B . 
BB 7 HOH 191 891  686  HOH HOH B . 
BB 7 HOH 192 892  52   HOH HOH B . 
BB 7 HOH 193 893  88   HOH HOH B . 
BB 7 HOH 194 894  289  HOH HOH B . 
BB 7 HOH 195 895  237  HOH HOH B . 
BB 7 HOH 196 896  1255 HOH HOH B . 
BB 7 HOH 197 897  501  HOH HOH B . 
BB 7 HOH 198 898  1210 HOH HOH B . 
BB 7 HOH 199 899  1248 HOH HOH B . 
BB 7 HOH 200 900  460  HOH HOH B . 
BB 7 HOH 201 901  633  HOH HOH B . 
BB 7 HOH 202 902  1123 HOH HOH B . 
BB 7 HOH 203 903  558  HOH HOH B . 
BB 7 HOH 204 904  1052 HOH HOH B . 
BB 7 HOH 205 905  19   HOH HOH B . 
BB 7 HOH 206 906  1458 HOH HOH B . 
BB 7 HOH 207 907  1241 HOH HOH B . 
BB 7 HOH 208 908  489  HOH HOH B . 
BB 7 HOH 209 909  166  HOH HOH B . 
BB 7 HOH 210 910  50   HOH HOH B . 
BB 7 HOH 211 911  104  HOH HOH B . 
BB 7 HOH 212 912  175  HOH HOH B . 
BB 7 HOH 213 913  473  HOH HOH B . 
BB 7 HOH 214 914  1035 HOH HOH B . 
BB 7 HOH 215 915  858  HOH HOH B . 
BB 7 HOH 216 916  1113 HOH HOH B . 
BB 7 HOH 217 917  33   HOH HOH B . 
BB 7 HOH 218 918  505  HOH HOH B . 
BB 7 HOH 219 919  436  HOH HOH B . 
BB 7 HOH 220 920  360  HOH HOH B . 
BB 7 HOH 221 921  443  HOH HOH B . 
BB 7 HOH 222 922  793  HOH HOH B . 
BB 7 HOH 223 923  974  HOH HOH B . 
BB 7 HOH 224 924  54   HOH HOH B . 
BB 7 HOH 225 925  1437 HOH HOH B . 
BB 7 HOH 226 926  757  HOH HOH B . 
BB 7 HOH 227 927  997  HOH HOH B . 
BB 7 HOH 228 928  162  HOH HOH B . 
BB 7 HOH 229 929  847  HOH HOH B . 
BB 7 HOH 230 930  1353 HOH HOH B . 
BB 7 HOH 231 931  1239 HOH HOH B . 
BB 7 HOH 232 932  353  HOH HOH B . 
BB 7 HOH 233 933  59   HOH HOH B . 
BB 7 HOH 234 934  1232 HOH HOH B . 
BB 7 HOH 235 935  194  HOH HOH B . 
BB 7 HOH 236 936  518  HOH HOH B . 
BB 7 HOH 237 937  317  HOH HOH B . 
BB 7 HOH 238 938  711  HOH HOH B . 
BB 7 HOH 239 939  261  HOH HOH B . 
BB 7 HOH 240 940  1075 HOH HOH B . 
BB 7 HOH 241 941  1152 HOH HOH B . 
BB 7 HOH 242 942  538  HOH HOH B . 
BB 7 HOH 243 943  1383 HOH HOH B . 
BB 7 HOH 244 944  1486 HOH HOH B . 
BB 7 HOH 245 945  386  HOH HOH B . 
BB 7 HOH 246 946  180  HOH HOH B . 
BB 7 HOH 247 947  244  HOH HOH B . 
BB 7 HOH 248 948  370  HOH HOH B . 
BB 7 HOH 249 949  243  HOH HOH B . 
BB 7 HOH 250 950  146  HOH HOH B . 
BB 7 HOH 251 951  150  HOH HOH B . 
BB 7 HOH 252 952  103  HOH HOH B . 
BB 7 HOH 253 953  628  HOH HOH B . 
BB 7 HOH 254 954  556  HOH HOH B . 
BB 7 HOH 255 955  720  HOH HOH B . 
BB 7 HOH 256 956  311  HOH HOH B . 
BB 7 HOH 257 957  914  HOH HOH B . 
BB 7 HOH 258 958  255  HOH HOH B . 
BB 7 HOH 259 959  535  HOH HOH B . 
BB 7 HOH 260 960  235  HOH HOH B . 
BB 7 HOH 261 961  510  HOH HOH B . 
BB 7 HOH 262 962  105  HOH HOH B . 
BB 7 HOH 263 963  446  HOH HOH B . 
BB 7 HOH 264 964  574  HOH HOH B . 
BB 7 HOH 265 965  221  HOH HOH B . 
BB 7 HOH 266 966  394  HOH HOH B . 
BB 7 HOH 267 967  51   HOH HOH B . 
BB 7 HOH 268 968  1424 HOH HOH B . 
BB 7 HOH 269 969  126  HOH HOH B . 
BB 7 HOH 270 970  1418 HOH HOH B . 
BB 7 HOH 271 971  596  HOH HOH B . 
BB 7 HOH 272 972  198  HOH HOH B . 
BB 7 HOH 273 973  1262 HOH HOH B . 
BB 7 HOH 274 974  90   HOH HOH B . 
BB 7 HOH 275 975  70   HOH HOH B . 
BB 7 HOH 276 976  1186 HOH HOH B . 
BB 7 HOH 277 977  151  HOH HOH B . 
BB 7 HOH 278 978  1459 HOH HOH B . 
BB 7 HOH 279 979  654  HOH HOH B . 
BB 7 HOH 280 980  13   HOH HOH B . 
BB 7 HOH 281 981  1131 HOH HOH B . 
BB 7 HOH 282 982  1176 HOH HOH B . 
BB 7 HOH 283 983  495  HOH HOH B . 
BB 7 HOH 284 984  1409 HOH HOH B . 
BB 7 HOH 285 985  1229 HOH HOH B . 
BB 7 HOH 286 986  659  HOH HOH B . 
BB 7 HOH 287 987  135  HOH HOH B . 
BB 7 HOH 288 988  1261 HOH HOH B . 
BB 7 HOH 289 989  925  HOH HOH B . 
BB 7 HOH 290 990  583  HOH HOH B . 
BB 7 HOH 291 991  1043 HOH HOH B . 
BB 7 HOH 292 992  498  HOH HOH B . 
BB 7 HOH 293 993  1204 HOH HOH B . 
BB 7 HOH 294 994  614  HOH HOH B . 
BB 7 HOH 295 995  898  HOH HOH B . 
BB 7 HOH 296 996  47   HOH HOH B . 
BB 7 HOH 297 997  1498 HOH HOH B . 
BB 7 HOH 298 998  30   HOH HOH B . 
BB 7 HOH 299 999  1466 HOH HOH B . 
BB 7 HOH 300 1000 1205 HOH HOH B . 
BB 7 HOH 301 1001 1366 HOH HOH B . 
BB 7 HOH 302 1002 1313 HOH HOH B . 
BB 7 HOH 303 1003 29   HOH HOH B . 
BB 7 HOH 304 1004 1551 HOH HOH B . 
BB 7 HOH 305 1005 1296 HOH HOH B . 
BB 7 HOH 306 1006 934  HOH HOH B . 
BB 7 HOH 307 1007 732  HOH HOH B . 
BB 7 HOH 308 1008 1547 HOH HOH B . 
BB 7 HOH 309 1009 1361 HOH HOH B . 
BB 7 HOH 310 1010 817  HOH HOH B . 
BB 7 HOH 311 1011 745  HOH HOH B . 
BB 7 HOH 312 1012 500  HOH HOH B . 
BB 7 HOH 313 1013 867  HOH HOH B . 
BB 7 HOH 314 1014 1417 HOH HOH B . 
BB 7 HOH 315 1015 1179 HOH HOH B . 
BB 7 HOH 316 1016 1446 HOH HOH B . 
BB 7 HOH 317 1017 996  HOH HOH B . 
BB 7 HOH 318 1018 573  HOH HOH B . 
BB 7 HOH 319 1019 521  HOH HOH B . 
BB 7 HOH 320 1020 1155 HOH HOH B . 
BB 7 HOH 321 1021 731  HOH HOH B . 
BB 7 HOH 322 1022 184  HOH HOH B . 
BB 7 HOH 323 1023 1290 HOH HOH B . 
BB 7 HOH 324 1024 1434 HOH HOH B . 
BB 7 HOH 325 1025 1496 HOH HOH B . 
BB 7 HOH 326 1026 511  HOH HOH B . 
BB 7 HOH 327 1027 1188 HOH HOH B . 
BB 7 HOH 328 1028 987  HOH HOH B . 
BB 7 HOH 329 1029 1370 HOH HOH B . 
BB 7 HOH 330 1030 1070 HOH HOH B . 
BB 7 HOH 331 1031 1169 HOH HOH B . 
BB 7 HOH 332 1032 1416 HOH HOH B . 
BB 7 HOH 333 1033 1386 HOH HOH B . 
BB 7 HOH 334 1034 984  HOH HOH B . 
BB 7 HOH 335 1035 623  HOH HOH B . 
BB 7 HOH 336 1036 1223 HOH HOH B . 
BB 7 HOH 337 1037 1542 HOH HOH B . 
BB 7 HOH 338 1038 1469 HOH HOH B . 
BB 7 HOH 339 1039 1405 HOH HOH B . 
BB 7 HOH 340 1040 1548 HOH HOH B . 
BB 7 HOH 341 1041 475  HOH HOH B . 
BB 7 HOH 342 1042 635  HOH HOH B . 
BB 7 HOH 343 1043 1426 HOH HOH B . 
BB 7 HOH 344 1044 1270 HOH HOH B . 
BB 7 HOH 345 1045 1470 HOH HOH B . 
BB 7 HOH 346 1046 548  HOH HOH B . 
BB 7 HOH 347 1047 1121 HOH HOH B . 
BB 7 HOH 348 1048 1348 HOH HOH B . 
BB 7 HOH 349 1049 733  HOH HOH B . 
BB 7 HOH 350 1050 1427 HOH HOH B . 
BB 7 HOH 351 1051 1185 HOH HOH B . 
BB 7 HOH 352 1052 1097 HOH HOH B . 
BB 7 HOH 353 1053 1106 HOH HOH B . 
BB 7 HOH 354 1054 1165 HOH HOH B . 
BB 7 HOH 355 1055 345  HOH HOH B . 
BB 7 HOH 356 1056 1213 HOH HOH B . 
BB 7 HOH 357 1057 1410 HOH HOH B . 
BB 7 HOH 358 1058 666  HOH HOH B . 
BB 7 HOH 359 1059 224  HOH HOH B . 
BB 7 HOH 360 1060 1249 HOH HOH B . 
BB 7 HOH 361 1061 74   HOH HOH B . 
BB 7 HOH 362 1062 1411 HOH HOH B . 
BB 7 HOH 363 1063 1448 HOH HOH B . 
BB 7 HOH 364 1064 1403 HOH HOH B . 
BB 7 HOH 365 1065 62   HOH HOH B . 
BB 7 HOH 366 1066 1328 HOH HOH B . 
BB 7 HOH 367 1067 412  HOH HOH B . 
BB 7 HOH 368 1068 843  HOH HOH B . 
BB 7 HOH 369 1069 1429 HOH HOH B . 
BB 7 HOH 370 1070 452  HOH HOH B . 
BB 7 HOH 371 1071 1108 HOH HOH B . 
BB 7 HOH 372 1072 1323 HOH HOH B . 
BB 7 HOH 373 1073 1310 HOH HOH B . 
BB 7 HOH 374 1074 411  HOH HOH B . 
BB 7 HOH 375 1075 1308 HOH HOH B . 
BB 7 HOH 376 1076 808  HOH HOH B . 
BB 7 HOH 377 1077 308  HOH HOH B . 
BB 7 HOH 378 1078 904  HOH HOH B . 
BB 7 HOH 379 1079 1550 HOH HOH B . 
BB 7 HOH 380 1080 1457 HOH HOH B . 
BB 7 HOH 381 1081 1293 HOH HOH B . 
BB 7 HOH 382 1082 11   HOH HOH B . 
BB 7 HOH 383 1083 673  HOH HOH B . 
BB 7 HOH 384 1084 800  HOH HOH B . 
BB 7 HOH 385 1085 728  HOH HOH B . 
BB 7 HOH 386 1086 1147 HOH HOH B . 
BB 7 HOH 387 1087 1408 HOH HOH B . 
BB 7 HOH 388 1088 1135 HOH HOH B . 
BB 7 HOH 389 1089 490  HOH HOH B . 
BB 7 HOH 390 1090 493  HOH HOH B . 
BB 7 HOH 391 1091 1191 HOH HOH B . 
BB 7 HOH 392 1092 1594 HOH HOH B . 
BB 7 HOH 393 1093 1502 HOH HOH B . 
BB 7 HOH 394 1094 727  HOH HOH B . 
BB 7 HOH 395 1095 1235 HOH HOH B . 
BB 7 HOH 396 1096 739  HOH HOH B . 
BB 7 HOH 397 1097 1177 HOH HOH B . 
BB 7 HOH 398 1098 383  HOH HOH B . 
BB 7 HOH 399 1099 748  HOH HOH B . 
BB 7 HOH 400 1100 148  HOH HOH B . 
BB 7 HOH 401 1101 1107 HOH HOH B . 
BB 7 HOH 402 1102 428  HOH HOH B . 
BB 7 HOH 403 1103 1218 HOH HOH B . 
BB 7 HOH 404 1104 691  HOH HOH B . 
BB 7 HOH 405 1105 960  HOH HOH B . 
BB 7 HOH 406 1106 557  HOH HOH B . 
BB 7 HOH 407 1107 1544 HOH HOH B . 
BB 7 HOH 408 1108 1021 HOH HOH B . 
BB 7 HOH 409 1109 1555 HOH HOH B . 
BB 7 HOH 410 1110 1089 HOH HOH B . 
BB 7 HOH 411 1111 820  HOH HOH B . 
BB 7 HOH 412 1112 1311 HOH HOH B . 
BB 7 HOH 413 1113 1460 HOH HOH B . 
BB 7 HOH 414 1114 1156 HOH HOH B . 
BB 7 HOH 415 1115 1055 HOH HOH B . 
BB 7 HOH 416 1116 1357 HOH HOH B . 
BB 7 HOH 417 1117 1197 HOH HOH B . 
BB 7 HOH 418 1118 1295 HOH HOH B . 
BB 7 HOH 419 1119 957  HOH HOH B . 
BB 7 HOH 420 1120 1583 HOH HOH B . 
BB 7 HOH 421 1121 1384 HOH HOH B . 
BB 7 HOH 422 1122 478  HOH HOH B . 
BB 7 HOH 423 1123 632  HOH HOH B . 
BB 7 HOH 424 1124 626  HOH HOH B . 
BB 7 HOH 425 1125 1274 HOH HOH B . 
BB 7 HOH 426 1126 751  HOH HOH B . 
BB 7 HOH 427 1127 1101 HOH HOH B . 
BB 7 HOH 428 1128 1145 HOH HOH B . 
BB 7 HOH 429 1129 725  HOH HOH B . 
BB 7 HOH 430 1130 612  HOH HOH B . 
BB 7 HOH 431 1131 517  HOH HOH B . 
BB 7 HOH 432 1132 526  HOH HOH B . 
BB 7 HOH 433 1133 1385 HOH HOH B . 
BB 7 HOH 434 1134 1536 HOH HOH B . 
BB 7 HOH 435 1135 1387 HOH HOH B . 
BB 7 HOH 436 1136 1047 HOH HOH B . 
BB 7 HOH 437 1137 1518 HOH HOH B . 
BB 7 HOH 438 1138 1546 HOH HOH B . 
BB 7 HOH 439 1139 1465 HOH HOH B . 
BB 7 HOH 440 1140 1219 HOH HOH B . 
BB 7 HOH 441 1141 1402 HOH HOH B . 
BB 7 HOH 442 1142 1133 HOH HOH B . 
BB 7 HOH 443 1143 1407 HOH HOH B . 
BB 7 HOH 444 1144 607  HOH HOH B . 
CB 7 HOH 1   701  640  HOH HOH C . 
CB 7 HOH 2   702  1586 HOH HOH C . 
CB 7 HOH 3   703  1053 HOH HOH C . 
CB 7 HOH 4   704  1025 HOH HOH C . 
CB 7 HOH 5   705  799  HOH HOH C . 
CB 7 HOH 6   706  494  HOH HOH C . 
CB 7 HOH 7   707  551  HOH HOH C . 
CB 7 HOH 8   708  1325 HOH HOH C . 
CB 7 HOH 9   709  968  HOH HOH C . 
CB 7 HOH 10  710  775  HOH HOH C . 
CB 7 HOH 11  711  374  HOH HOH C . 
CB 7 HOH 12  712  1159 HOH HOH C . 
CB 7 HOH 13  713  850  HOH HOH C . 
CB 7 HOH 14  714  483  HOH HOH C . 
CB 7 HOH 15  715  1104 HOH HOH C . 
CB 7 HOH 16  716  367  HOH HOH C . 
CB 7 HOH 17  717  897  HOH HOH C . 
CB 7 HOH 18  718  416  HOH HOH C . 
CB 7 HOH 19  719  406  HOH HOH C . 
CB 7 HOH 20  720  346  HOH HOH C . 
CB 7 HOH 21  721  424  HOH HOH C . 
CB 7 HOH 22  722  687  HOH HOH C . 
CB 7 HOH 23  723  980  HOH HOH C . 
CB 7 HOH 24  724  593  HOH HOH C . 
CB 7 HOH 25  725  1376 HOH HOH C . 
CB 7 HOH 26  726  164  HOH HOH C . 
CB 7 HOH 27  727  804  HOH HOH C . 
CB 7 HOH 28  728  270  HOH HOH C . 
CB 7 HOH 29  729  1143 HOH HOH C . 
CB 7 HOH 30  730  1068 HOH HOH C . 
CB 7 HOH 31  731  926  HOH HOH C . 
CB 7 HOH 32  732  207  HOH HOH C . 
CB 7 HOH 33  733  1280 HOH HOH C . 
CB 7 HOH 34  734  99   HOH HOH C . 
CB 7 HOH 35  735  706  HOH HOH C . 
CB 7 HOH 36  736  1246 HOH HOH C . 
CB 7 HOH 37  737  703  HOH HOH C . 
CB 7 HOH 38  738  450  HOH HOH C . 
CB 7 HOH 39  739  293  HOH HOH C . 
CB 7 HOH 40  740  1326 HOH HOH C . 
CB 7 HOH 41  741  254  HOH HOH C . 
CB 7 HOH 42  742  327  HOH HOH C . 
CB 7 HOH 43  743  786  HOH HOH C . 
CB 7 HOH 44  744  100  HOH HOH C . 
CB 7 HOH 45  745  57   HOH HOH C . 
CB 7 HOH 46  746  1300 HOH HOH C . 
CB 7 HOH 47  747  267  HOH HOH C . 
CB 7 HOH 48  748  58   HOH HOH C . 
CB 7 HOH 49  749  1026 HOH HOH C . 
CB 7 HOH 50  750  707  HOH HOH C . 
CB 7 HOH 51  751  382  HOH HOH C . 
CB 7 HOH 52  752  64   HOH HOH C . 
CB 7 HOH 53  753  468  HOH HOH C . 
CB 7 HOH 54  754  553  HOH HOH C . 
CB 7 HOH 55  755  421  HOH HOH C . 
CB 7 HOH 56  756  641  HOH HOH C . 
CB 7 HOH 57  757  575  HOH HOH C . 
CB 7 HOH 58  758  1033 HOH HOH C . 
CB 7 HOH 59  759  332  HOH HOH C . 
CB 7 HOH 60  760  139  HOH HOH C . 
CB 7 HOH 61  761  368  HOH HOH C . 
CB 7 HOH 62  762  1301 HOH HOH C . 
CB 7 HOH 63  763  1340 HOH HOH C . 
CB 7 HOH 64  764  625  HOH HOH C . 
CB 7 HOH 65  765  713  HOH HOH C . 
CB 7 HOH 66  766  253  HOH HOH C . 
CB 7 HOH 67  767  865  HOH HOH C . 
CB 7 HOH 68  768  304  HOH HOH C . 
CB 7 HOH 69  769  536  HOH HOH C . 
CB 7 HOH 70  770  528  HOH HOH C . 
CB 7 HOH 71  771  375  HOH HOH C . 
CB 7 HOH 72  772  524  HOH HOH C . 
CB 7 HOH 73  773  615  HOH HOH C . 
CB 7 HOH 74  774  10   HOH HOH C . 
CB 7 HOH 75  775  986  HOH HOH C . 
CB 7 HOH 76  776  179  HOH HOH C . 
CB 7 HOH 77  777  1079 HOH HOH C . 
CB 7 HOH 78  778  680  HOH HOH C . 
CB 7 HOH 79  779  509  HOH HOH C . 
CB 7 HOH 80  780  395  HOH HOH C . 
CB 7 HOH 81  781  273  HOH HOH C . 
CB 7 HOH 82  782  219  HOH HOH C . 
CB 7 HOH 83  783  213  HOH HOH C . 
CB 7 HOH 84  784  183  HOH HOH C . 
CB 7 HOH 85  785  527  HOH HOH C . 
CB 7 HOH 86  786  655  HOH HOH C . 
CB 7 HOH 87  787  781  HOH HOH C . 
CB 7 HOH 88  788  418  HOH HOH C . 
CB 7 HOH 89  789  1080 HOH HOH C . 
CB 7 HOH 90  790  605  HOH HOH C . 
CB 7 HOH 91  791  939  HOH HOH C . 
CB 7 HOH 92  792  1540 HOH HOH C . 
CB 7 HOH 93  793  656  HOH HOH C . 
CB 7 HOH 94  794  592  HOH HOH C . 
CB 7 HOH 95  795  216  HOH HOH C . 
CB 7 HOH 96  796  1381 HOH HOH C . 
CB 7 HOH 97  797  451  HOH HOH C . 
CB 7 HOH 98  798  229  HOH HOH C . 
CB 7 HOH 99  799  187  HOH HOH C . 
CB 7 HOH 100 800  127  HOH HOH C . 
CB 7 HOH 101 801  773  HOH HOH C . 
CB 7 HOH 102 802  920  HOH HOH C . 
CB 7 HOH 103 803  330  HOH HOH C . 
CB 7 HOH 104 804  1243 HOH HOH C . 
CB 7 HOH 105 805  55   HOH HOH C . 
CB 7 HOH 106 806  863  HOH HOH C . 
CB 7 HOH 107 807  471  HOH HOH C . 
CB 7 HOH 108 808  539  HOH HOH C . 
CB 7 HOH 109 809  456  HOH HOH C . 
CB 7 HOH 110 810  833  HOH HOH C . 
CB 7 HOH 111 811  638  HOH HOH C . 
CB 7 HOH 112 812  671  HOH HOH C . 
CB 7 HOH 113 813  369  HOH HOH C . 
CB 7 HOH 114 814  694  HOH HOH C . 
CB 7 HOH 115 815  991  HOH HOH C . 
CB 7 HOH 116 816  355  HOH HOH C . 
CB 7 HOH 117 817  433  HOH HOH C . 
CB 7 HOH 118 818  66   HOH HOH C . 
CB 7 HOH 119 819  108  HOH HOH C . 
CB 7 HOH 120 820  682  HOH HOH C . 
CB 7 HOH 121 821  440  HOH HOH C . 
CB 7 HOH 122 822  586  HOH HOH C . 
CB 7 HOH 123 823  701  HOH HOH C . 
CB 7 HOH 124 824  576  HOH HOH C . 
CB 7 HOH 125 825  3    HOH HOH C . 
CB 7 HOH 126 826  1196 HOH HOH C . 
CB 7 HOH 127 827  381  HOH HOH C . 
CB 7 HOH 128 828  1578 HOH HOH C . 
CB 7 HOH 129 829  1250 HOH HOH C . 
CB 7 HOH 130 830  928  HOH HOH C . 
CB 7 HOH 131 831  544  HOH HOH C . 
CB 7 HOH 132 832  414  HOH HOH C . 
CB 7 HOH 133 833  1341 HOH HOH C . 
CB 7 HOH 134 834  403  HOH HOH C . 
CB 7 HOH 135 835  249  HOH HOH C . 
CB 7 HOH 136 836  318  HOH HOH C . 
CB 7 HOH 137 837  520  HOH HOH C . 
CB 7 HOH 138 838  109  HOH HOH C . 
CB 7 HOH 139 839  516  HOH HOH C . 
CB 7 HOH 140 840  692  HOH HOH C . 
CB 7 HOH 141 841  569  HOH HOH C . 
CB 7 HOH 142 842  959  HOH HOH C . 
CB 7 HOH 143 843  1100 HOH HOH C . 
CB 7 HOH 144 844  506  HOH HOH C . 
CB 7 HOH 145 845  857  HOH HOH C . 
CB 7 HOH 146 846  645  HOH HOH C . 
CB 7 HOH 147 847  1040 HOH HOH C . 
CB 7 HOH 148 848  998  HOH HOH C . 
CB 7 HOH 149 849  1576 HOH HOH C . 
CB 7 HOH 150 850  455  HOH HOH C . 
CB 7 HOH 151 851  321  HOH HOH C . 
CB 7 HOH 152 852  233  HOH HOH C . 
CB 7 HOH 153 853  912  HOH HOH C . 
CB 7 HOH 154 854  796  HOH HOH C . 
CB 7 HOH 155 855  389  HOH HOH C . 
CB 7 HOH 156 856  211  HOH HOH C . 
CB 7 HOH 157 857  599  HOH HOH C . 
CB 7 HOH 158 858  1098 HOH HOH C . 
CB 7 HOH 159 859  324  HOH HOH C . 
CB 7 HOH 160 860  699  HOH HOH C . 
CB 7 HOH 161 861  125  HOH HOH C . 
CB 7 HOH 162 862  341  HOH HOH C . 
CB 7 HOH 163 863  550  HOH HOH C . 
CB 7 HOH 164 864  1364 HOH HOH C . 
CB 7 HOH 165 865  484  HOH HOH C . 
CB 7 HOH 166 866  496  HOH HOH C . 
CB 7 HOH 167 867  467  HOH HOH C . 
CB 7 HOH 168 868  497  HOH HOH C . 
CB 7 HOH 169 869  163  HOH HOH C . 
CB 7 HOH 170 870  825  HOH HOH C . 
CB 7 HOH 171 871  453  HOH HOH C . 
CB 7 HOH 172 872  787  HOH HOH C . 
CB 7 HOH 173 873  371  HOH HOH C . 
CB 7 HOH 174 874  1312 HOH HOH C . 
CB 7 HOH 175 875  1315 HOH HOH C . 
CB 7 HOH 176 876  1593 HOH HOH C . 
CB 7 HOH 177 877  683  HOH HOH C . 
CB 7 HOH 178 878  307  HOH HOH C . 
CB 7 HOH 179 879  853  HOH HOH C . 
CB 7 HOH 180 880  1398 HOH HOH C . 
CB 7 HOH 181 881  940  HOH HOH C . 
CB 7 HOH 182 882  801  HOH HOH C . 
CB 7 HOH 183 883  385  HOH HOH C . 
CB 7 HOH 184 884  303  HOH HOH C . 
CB 7 HOH 185 885  621  HOH HOH C . 
CB 7 HOH 186 886  246  HOH HOH C . 
CB 7 HOH 187 887  172  HOH HOH C . 
CB 7 HOH 188 888  320  HOH HOH C . 
CB 7 HOH 189 889  376  HOH HOH C . 
CB 7 HOH 190 890  12   HOH HOH C . 
CB 7 HOH 191 891  918  HOH HOH C . 
CB 7 HOH 192 892  336  HOH HOH C . 
CB 7 HOH 193 893  650  HOH HOH C . 
CB 7 HOH 194 894  477  HOH HOH C . 
CB 7 HOH 195 895  133  HOH HOH C . 
CB 7 HOH 196 896  1520 HOH HOH C . 
CB 7 HOH 197 897  674  HOH HOH C . 
CB 7 HOH 198 898  855  HOH HOH C . 
CB 7 HOH 199 899  1562 HOH HOH C . 
CB 7 HOH 200 900  512  HOH HOH C . 
CB 7 HOH 201 901  392  HOH HOH C . 
CB 7 HOH 202 902  292  HOH HOH C . 
CB 7 HOH 203 903  1171 HOH HOH C . 
CB 7 HOH 204 904  1504 HOH HOH C . 
CB 7 HOH 205 905  1001 HOH HOH C . 
CB 7 HOH 206 906  1374 HOH HOH C . 
CB 7 HOH 207 907  688  HOH HOH C . 
CB 7 HOH 208 908  1130 HOH HOH C . 
CB 7 HOH 209 909  1202 HOH HOH C . 
CB 7 HOH 210 910  1269 HOH HOH C . 
CB 7 HOH 211 911  1342 HOH HOH C . 
CB 7 HOH 212 912  568  HOH HOH C . 
CB 7 HOH 213 913  1057 HOH HOH C . 
CB 7 HOH 214 914  1454 HOH HOH C . 
CB 7 HOH 215 915  1303 HOH HOH C . 
CB 7 HOH 216 916  1490 HOH HOH C . 
CB 7 HOH 217 917  845  HOH HOH C . 
CB 7 HOH 218 918  705  HOH HOH C . 
CB 7 HOH 219 919  1017 HOH HOH C . 
CB 7 HOH 220 920  285  HOH HOH C . 
CB 7 HOH 221 921  603  HOH HOH C . 
CB 7 HOH 222 922  663  HOH HOH C . 
CB 7 HOH 223 923  1289 HOH HOH C . 
CB 7 HOH 224 924  1199 HOH HOH C . 
CB 7 HOH 225 925  1148 HOH HOH C . 
CB 7 HOH 226 926  283  HOH HOH C . 
CB 7 HOH 227 927  1483 HOH HOH C . 
CB 7 HOH 228 928  1000 HOH HOH C . 
CB 7 HOH 229 929  889  HOH HOH C . 
CB 7 HOH 230 930  1338 HOH HOH C . 
CB 7 HOH 231 931  356  HOH HOH C . 
CB 7 HOH 232 932  1173 HOH HOH C . 
CB 7 HOH 233 933  1577 HOH HOH C . 
CB 7 HOH 234 934  295  HOH HOH C . 
CB 7 HOH 235 935  1560 HOH HOH C . 
CB 7 HOH 236 936  1363 HOH HOH C . 
CB 7 HOH 237 937  1558 HOH HOH C . 
CB 7 HOH 238 938  399  HOH HOH C . 
CB 7 HOH 239 939  877  HOH HOH C . 
CB 7 HOH 240 940  1142 HOH HOH C . 
CB 7 HOH 241 941  903  HOH HOH C . 
CB 7 HOH 242 942  1272 HOH HOH C . 
CB 7 HOH 243 943  995  HOH HOH C . 
CB 7 HOH 244 944  1138 HOH HOH C . 
CB 7 HOH 245 945  1266 HOH HOH C . 
CB 7 HOH 246 946  1195 HOH HOH C . 
CB 7 HOH 247 947  1485 HOH HOH C . 
CB 7 HOH 248 948  735  HOH HOH C . 
CB 7 HOH 249 949  1499 HOH HOH C . 
CB 7 HOH 250 950  1287 HOH HOH C . 
CB 7 HOH 251 951  624  HOH HOH C . 
CB 7 HOH 252 952  1352 HOH HOH C . 
CB 7 HOH 253 953  1505 HOH HOH C . 
CB 7 HOH 254 954  1503 HOH HOH C . 
CB 7 HOH 255 955  1110 HOH HOH C . 
CB 7 HOH 256 956  746  HOH HOH C . 
CB 7 HOH 257 957  534  HOH HOH C . 
CB 7 HOH 258 958  743  HOH HOH C . 
CB 7 HOH 259 959  1114 HOH HOH C . 
CB 7 HOH 260 960  1500 HOH HOH C . 
CB 7 HOH 261 961  715  HOH HOH C . 
CB 7 HOH 262 962  906  HOH HOH C . 
CB 7 HOH 263 963  1044 HOH HOH C . 
CB 7 HOH 264 964  1579 HOH HOH C . 
CB 7 HOH 265 965  1    HOH HOH C . 
CB 7 HOH 266 966  698  HOH HOH C . 
CB 7 HOH 267 967  1336 HOH HOH C . 
CB 7 HOH 268 968  1242 HOH HOH C . 
CB 7 HOH 269 969  729  HOH HOH C . 
CB 7 HOH 270 970  667  HOH HOH C . 
CB 7 HOH 271 971  1501 HOH HOH C . 
CB 7 HOH 272 972  1365 HOH HOH C . 
CB 7 HOH 273 973  1060 HOH HOH C . 
CB 7 HOH 274 974  994  HOH HOH C . 
CB 7 HOH 275 975  1362 HOH HOH C . 
CB 7 HOH 276 976  1488 HOH HOH C . 
CB 7 HOH 277 977  1591 HOH HOH C . 
CB 7 HOH 278 978  1233 HOH HOH C . 
CB 7 HOH 279 979  1581 HOH HOH C . 
CB 7 HOH 280 980  741  HOH HOH C . 
CB 7 HOH 281 981  734  HOH HOH C . 
CB 7 HOH 282 982  1441 HOH HOH C . 
CB 7 HOH 283 983  676  HOH HOH C . 
CB 7 HOH 284 984  1445 HOH HOH C . 
CB 7 HOH 285 985  821  HOH HOH C . 
CB 7 HOH 286 986  744  HOH HOH C . 
CB 7 HOH 287 987  1252 HOH HOH C . 
CB 7 HOH 288 988  1563 HOH HOH C . 
CB 7 HOH 289 989  716  HOH HOH C . 
CB 7 HOH 290 990  970  HOH HOH C . 
CB 7 HOH 291 991  649  HOH HOH C . 
CB 7 HOH 292 992  1264 HOH HOH C . 
CB 7 HOH 293 993  572  HOH HOH C . 
CB 7 HOH 294 994  1439 HOH HOH C . 
CB 7 HOH 295 995  537  HOH HOH C . 
CB 7 HOH 296 996  1062 HOH HOH C . 
CB 7 HOH 297 997  1461 HOH HOH C . 
CB 7 HOH 298 998  1050 HOH HOH C . 
CB 7 HOH 299 999  1541 HOH HOH C . 
CB 7 HOH 300 1000 595  HOH HOH C . 
CB 7 HOH 301 1001 1027 HOH HOH C . 
CB 7 HOH 302 1002 1327 HOH HOH C . 
CB 7 HOH 303 1003 1178 HOH HOH C . 
CB 7 HOH 304 1004 1090 HOH HOH C . 
CB 7 HOH 305 1005 1225 HOH HOH C . 
CB 7 HOH 306 1006 747  HOH HOH C . 
CB 7 HOH 307 1007 693  HOH HOH C . 
CB 7 HOH 308 1008 1412 HOH HOH C . 
CB 7 HOH 309 1009 1140 HOH HOH C . 
CB 7 HOH 310 1010 1449 HOH HOH C . 
CB 7 HOH 311 1011 1382 HOH HOH C . 
CB 7 HOH 312 1012 1265 HOH HOH C . 
CB 7 HOH 313 1013 1375 HOH HOH C . 
CB 7 HOH 314 1014 1568 HOH HOH C . 
DB 7 HOH 1   701  965  HOH HOH D . 
DB 7 HOH 2   702  1183 HOH HOH D . 
DB 7 HOH 3   703  155  HOH HOH D . 
DB 7 HOH 4   704  610  HOH HOH D . 
DB 7 HOH 5   705  888  HOH HOH D . 
DB 7 HOH 6   706  779  HOH HOH D . 
DB 7 HOH 7   707  1569 HOH HOH D . 
DB 7 HOH 8   708  337  HOH HOH D . 
DB 7 HOH 9   709  1493 HOH HOH D . 
DB 7 HOH 10  710  344  HOH HOH D . 
DB 7 HOH 11  711  384  HOH HOH D . 
DB 7 HOH 12  712  930  HOH HOH D . 
DB 7 HOH 13  713  217  HOH HOH D . 
DB 7 HOH 14  714  545  HOH HOH D . 
DB 7 HOH 15  715  839  HOH HOH D . 
DB 7 HOH 16  716  1094 HOH HOH D . 
DB 7 HOH 17  717  1018 HOH HOH D . 
DB 7 HOH 18  718  1236 HOH HOH D . 
DB 7 HOH 19  719  695  HOH HOH D . 
DB 7 HOH 20  720  652  HOH HOH D . 
DB 7 HOH 21  721  704  HOH HOH D . 
DB 7 HOH 22  722  961  HOH HOH D . 
DB 7 HOH 23  723  401  HOH HOH D . 
DB 7 HOH 24  724  398  HOH HOH D . 
DB 7 HOH 25  725  1304 HOH HOH D . 
DB 7 HOH 26  726  1533 HOH HOH D . 
DB 7 HOH 27  727  815  HOH HOH D . 
DB 7 HOH 28  728  469  HOH HOH D . 
DB 7 HOH 29  729  97   HOH HOH D . 
DB 7 HOH 30  730  275  HOH HOH D . 
DB 7 HOH 31  731  631  HOH HOH D . 
DB 7 HOH 32  732  660  HOH HOH D . 
DB 7 HOH 33  733  132  HOH HOH D . 
DB 7 HOH 34  734  296  HOH HOH D . 
DB 7 HOH 35  735  1096 HOH HOH D . 
DB 7 HOH 36  736  874  HOH HOH D . 
DB 7 HOH 37  737  846  HOH HOH D . 
DB 7 HOH 38  738  314  HOH HOH D . 
DB 7 HOH 39  739  664  HOH HOH D . 
DB 7 HOH 40  740  366  HOH HOH D . 
DB 7 HOH 41  741  1137 HOH HOH D . 
DB 7 HOH 42  742  200  HOH HOH D . 
DB 7 HOH 43  743  611  HOH HOH D . 
DB 7 HOH 44  744  322  HOH HOH D . 
DB 7 HOH 45  745  316  HOH HOH D . 
DB 7 HOH 46  746  435  HOH HOH D . 
DB 7 HOH 47  747  94   HOH HOH D . 
DB 7 HOH 48  748  423  HOH HOH D . 
DB 7 HOH 49  749  131  HOH HOH D . 
DB 7 HOH 50  750  182  HOH HOH D . 
DB 7 HOH 51  751  204  HOH HOH D . 
DB 7 HOH 52  752  76   HOH HOH D . 
DB 7 HOH 53  753  129  HOH HOH D . 
DB 7 HOH 54  754  942  HOH HOH D . 
DB 7 HOH 55  755  1271 HOH HOH D . 
DB 7 HOH 56  756  442  HOH HOH D . 
DB 7 HOH 57  757  248  HOH HOH D . 
DB 7 HOH 58  758  220  HOH HOH D . 
DB 7 HOH 59  759  189  HOH HOH D . 
DB 7 HOH 60  760  466  HOH HOH D . 
DB 7 HOH 61  761  580  HOH HOH D . 
DB 7 HOH 62  762  431  HOH HOH D . 
DB 7 HOH 63  763  186  HOH HOH D . 
DB 7 HOH 64  764  1003 HOH HOH D . 
DB 7 HOH 65  765  533  HOH HOH D . 
DB 7 HOH 66  766  585  HOH HOH D . 
DB 7 HOH 67  767  201  HOH HOH D . 
DB 7 HOH 68  768  280  HOH HOH D . 
DB 7 HOH 69  769  56   HOH HOH D . 
DB 7 HOH 70  770  630  HOH HOH D . 
DB 7 HOH 71  771  24   HOH HOH D . 
DB 7 HOH 72  772  205  HOH HOH D . 
DB 7 HOH 73  773  397  HOH HOH D . 
DB 7 HOH 74  774  1071 HOH HOH D . 
DB 7 HOH 75  775  447  HOH HOH D . 
DB 7 HOH 76  776  350  HOH HOH D . 
DB 7 HOH 77  777  552  HOH HOH D . 
DB 7 HOH 78  778  176  HOH HOH D . 
DB 7 HOH 79  779  75   HOH HOH D . 
DB 7 HOH 80  780  485  HOH HOH D . 
DB 7 HOH 81  781  6    HOH HOH D . 
DB 7 HOH 82  782  1082 HOH HOH D . 
DB 7 HOH 83  783  439  HOH HOH D . 
DB 7 HOH 84  784  68   HOH HOH D . 
DB 7 HOH 85  785  291  HOH HOH D . 
DB 7 HOH 86  786  480  HOH HOH D . 
DB 7 HOH 87  787  143  HOH HOH D . 
DB 7 HOH 88  788  604  HOH HOH D . 
DB 7 HOH 89  789  1267 HOH HOH D . 
DB 7 HOH 90  790  96   HOH HOH D . 
DB 7 HOH 91  791  149  HOH HOH D . 
DB 7 HOH 92  792  1206 HOH HOH D . 
DB 7 HOH 93  793  161  HOH HOH D . 
DB 7 HOH 94  794  709  HOH HOH D . 
DB 7 HOH 95  795  813  HOH HOH D . 
DB 7 HOH 96  796  263  HOH HOH D . 
DB 7 HOH 97  797  326  HOH HOH D . 
DB 7 HOH 98  798  287  HOH HOH D . 
DB 7 HOH 99  799  102  HOH HOH D . 
DB 7 HOH 100 800  128  HOH HOH D . 
DB 7 HOH 101 801  457  HOH HOH D . 
DB 7 HOH 102 802  405  HOH HOH D . 
DB 7 HOH 103 803  540  HOH HOH D . 
DB 7 HOH 104 804  264  HOH HOH D . 
DB 7 HOH 105 805  247  HOH HOH D . 
DB 7 HOH 106 806  26   HOH HOH D . 
DB 7 HOH 107 807  1297 HOH HOH D . 
DB 7 HOH 108 808  85   HOH HOH D . 
DB 7 HOH 109 809  1212 HOH HOH D . 
DB 7 HOH 110 810  933  HOH HOH D . 
DB 7 HOH 111 811  168  HOH HOH D . 
DB 7 HOH 112 812  309  HOH HOH D . 
DB 7 HOH 113 813  429  HOH HOH D . 
DB 7 HOH 114 814  525  HOH HOH D . 
DB 7 HOH 115 815  114  HOH HOH D . 
DB 7 HOH 116 816  378  HOH HOH D . 
DB 7 HOH 117 817  584  HOH HOH D . 
DB 7 HOH 118 818  290  HOH HOH D . 
DB 7 HOH 119 819  1230 HOH HOH D . 
DB 7 HOH 120 820  245  HOH HOH D . 
DB 7 HOH 121 821  588  HOH HOH D . 
DB 7 HOH 122 822  717  HOH HOH D . 
DB 7 HOH 123 823  964  HOH HOH D . 
DB 7 HOH 124 824  372  HOH HOH D . 
DB 7 HOH 125 825  193  HOH HOH D . 
DB 7 HOH 126 826  989  HOH HOH D . 
DB 7 HOH 127 827  606  HOH HOH D . 
DB 7 HOH 128 828  98   HOH HOH D . 
DB 7 HOH 129 829  492  HOH HOH D . 
DB 7 HOH 130 830  594  HOH HOH D . 
DB 7 HOH 131 831  319  HOH HOH D . 
DB 7 HOH 132 832  642  HOH HOH D . 
DB 7 HOH 133 833  491  HOH HOH D . 
DB 7 HOH 134 834  339  HOH HOH D . 
DB 7 HOH 135 835  672  HOH HOH D . 
DB 7 HOH 136 836  1093 HOH HOH D . 
DB 7 HOH 137 837  577  HOH HOH D . 
DB 7 HOH 138 838  294  HOH HOH D . 
DB 7 HOH 139 839  999  HOH HOH D . 
DB 7 HOH 140 840  1085 HOH HOH D . 
DB 7 HOH 141 841  380  HOH HOH D . 
DB 7 HOH 142 842  627  HOH HOH D . 
DB 7 HOH 143 843  482  HOH HOH D . 
DB 7 HOH 144 844  1489 HOH HOH D . 
DB 7 HOH 145 845  1037 HOH HOH D . 
DB 7 HOH 146 846  812  HOH HOH D . 
DB 7 HOH 147 847  1015 HOH HOH D . 
DB 7 HOH 148 848  1077 HOH HOH D . 
DB 7 HOH 149 849  570  HOH HOH D . 
DB 7 HOH 150 850  947  HOH HOH D . 
DB 7 HOH 151 851  156  HOH HOH D . 
DB 7 HOH 152 852  130  HOH HOH D . 
DB 7 HOH 153 853  158  HOH HOH D . 
DB 7 HOH 154 854  53   HOH HOH D . 
DB 7 HOH 155 855  92   HOH HOH D . 
DB 7 HOH 156 856  541  HOH HOH D . 
DB 7 HOH 157 857  343  HOH HOH D . 
DB 7 HOH 158 858  1030 HOH HOH D . 
DB 7 HOH 159 859  195  HOH HOH D . 
DB 7 HOH 160 860  587  HOH HOH D . 
DB 7 HOH 161 861  333  HOH HOH D . 
DB 7 HOH 162 862  410  HOH HOH D . 
DB 7 HOH 163 863  199  HOH HOH D . 
DB 7 HOH 164 864  18   HOH HOH D . 
DB 7 HOH 165 865  259  HOH HOH D . 
DB 7 HOH 166 866  312  HOH HOH D . 
DB 7 HOH 167 867  1307 HOH HOH D . 
DB 7 HOH 168 868  1318 HOH HOH D . 
DB 7 HOH 169 869  342  HOH HOH D . 
DB 7 HOH 170 870  822  HOH HOH D . 
DB 7 HOH 171 871  684  HOH HOH D . 
DB 7 HOH 172 872  1231 HOH HOH D . 
DB 7 HOH 173 873  46   HOH HOH D . 
DB 7 HOH 174 874  1041 HOH HOH D . 
DB 7 HOH 175 875  597  HOH HOH D . 
DB 7 HOH 176 876  154  HOH HOH D . 
DB 7 HOH 177 877  190  HOH HOH D . 
DB 7 HOH 178 878  499  HOH HOH D . 
DB 7 HOH 179 879  669  HOH HOH D . 
DB 7 HOH 180 880  668  HOH HOH D . 
DB 7 HOH 181 881  393  HOH HOH D . 
DB 7 HOH 182 882  1532 HOH HOH D . 
DB 7 HOH 183 883  689  HOH HOH D . 
DB 7 HOH 184 884  481  HOH HOH D . 
DB 7 HOH 185 885  419  HOH HOH D . 
DB 7 HOH 186 886  462  HOH HOH D . 
DB 7 HOH 187 887  1309 HOH HOH D . 
DB 7 HOH 188 888  679  HOH HOH D . 
DB 7 HOH 189 889  658  HOH HOH D . 
DB 7 HOH 190 890  313  HOH HOH D . 
DB 7 HOH 191 891  238  HOH HOH D . 
DB 7 HOH 192 892  192  HOH HOH D . 
DB 7 HOH 193 893  797  HOH HOH D . 
DB 7 HOH 194 894  282  HOH HOH D . 
DB 7 HOH 195 895  665  HOH HOH D . 
DB 7 HOH 196 896  1200 HOH HOH D . 
DB 7 HOH 197 897  590  HOH HOH D . 
DB 7 HOH 198 898  7    HOH HOH D . 
DB 7 HOH 199 899  365  HOH HOH D . 
DB 7 HOH 200 900  1092 HOH HOH D . 
DB 7 HOH 201 901  234  HOH HOH D . 
DB 7 HOH 202 902  902  HOH HOH D . 
DB 7 HOH 203 903  300  HOH HOH D . 
DB 7 HOH 204 904  1126 HOH HOH D . 
DB 7 HOH 205 905  1517 HOH HOH D . 
DB 7 HOH 206 906  618  HOH HOH D . 
DB 7 HOH 207 907  390  HOH HOH D . 
DB 7 HOH 208 908  338  HOH HOH D . 
DB 7 HOH 209 909  891  HOH HOH D . 
DB 7 HOH 210 910  560  HOH HOH D . 
DB 7 HOH 211 911  578  HOH HOH D . 
DB 7 HOH 212 912  1187 HOH HOH D . 
DB 7 HOH 213 913  1078 HOH HOH D . 
DB 7 HOH 214 914  608  HOH HOH D . 
DB 7 HOH 215 915  1535 HOH HOH D . 
DB 7 HOH 216 916  1438 HOH HOH D . 
DB 7 HOH 217 917  653  HOH HOH D . 
DB 7 HOH 218 918  854  HOH HOH D . 
DB 7 HOH 219 919  1045 HOH HOH D . 
DB 7 HOH 220 920  864  HOH HOH D . 
DB 7 HOH 221 921  1278 HOH HOH D . 
DB 7 HOH 222 922  1509 HOH HOH D . 
DB 7 HOH 223 923  613  HOH HOH D . 
DB 7 HOH 224 924  281  HOH HOH D . 
DB 7 HOH 225 925  1151 HOH HOH D . 
DB 7 HOH 226 926  1436 HOH HOH D . 
DB 7 HOH 227 927  937  HOH HOH D . 
DB 7 HOH 228 928  1099 HOH HOH D . 
DB 7 HOH 229 929  1175 HOH HOH D . 
DB 7 HOH 230 930  1011 HOH HOH D . 
DB 7 HOH 231 931  643  HOH HOH D . 
DB 7 HOH 232 932  1211 HOH HOH D . 
DB 7 HOH 233 933  591  HOH HOH D . 
DB 7 HOH 234 934  230  HOH HOH D . 
DB 7 HOH 235 935  696  HOH HOH D . 
DB 7 HOH 236 936  661  HOH HOH D . 
DB 7 HOH 237 937  1567 HOH HOH D . 
DB 7 HOH 238 938  880  HOH HOH D . 
DB 7 HOH 239 939  1222 HOH HOH D . 
DB 7 HOH 240 940  1095 HOH HOH D . 
DB 7 HOH 241 941  791  HOH HOH D . 
DB 7 HOH 242 942  508  HOH HOH D . 
DB 7 HOH 243 943  1034 HOH HOH D . 
DB 7 HOH 244 944  331  HOH HOH D . 
DB 7 HOH 245 945  1215 HOH HOH D . 
DB 7 HOH 246 946  907  HOH HOH D . 
DB 7 HOH 247 947  1588 HOH HOH D . 
DB 7 HOH 248 948  1566 HOH HOH D . 
DB 7 HOH 249 949  1516 HOH HOH D . 
DB 7 HOH 250 950  1031 HOH HOH D . 
DB 7 HOH 251 951  1539 HOH HOH D . 
DB 7 HOH 252 952  1575 HOH HOH D . 
DB 7 HOH 253 953  1425 HOH HOH D . 
DB 7 HOH 254 954  1435 HOH HOH D . 
DB 7 HOH 255 955  1019 HOH HOH D . 
DB 7 HOH 256 956  726  HOH HOH D . 
DB 7 HOH 257 957  1584 HOH HOH D . 
DB 7 HOH 258 958  951  HOH HOH D . 
DB 7 HOH 259 959  1228 HOH HOH D . 
DB 7 HOH 260 960  1257 HOH HOH D . 
DB 7 HOH 261 961  1574 HOH HOH D . 
DB 7 HOH 262 962  1317 HOH HOH D . 
DB 7 HOH 263 963  1526 HOH HOH D . 
DB 7 HOH 264 964  1525 HOH HOH D . 
DB 7 HOH 265 965  1421 HOH HOH D . 
DB 7 HOH 266 966  985  HOH HOH D . 
DB 7 HOH 267 967  1046 HOH HOH D . 
DB 7 HOH 268 968  1201 HOH HOH D . 
DB 7 HOH 269 969  828  HOH HOH D . 
DB 7 HOH 270 970  1534 HOH HOH D . 
DB 7 HOH 271 971  1580 HOH HOH D . 
DB 7 HOH 272 972  1428 HOH HOH D . 
DB 7 HOH 273 973  1226 HOH HOH D . 
DB 7 HOH 274 974  1268 HOH HOH D . 
DB 7 HOH 275 975  1537 HOH HOH D . 
DB 7 HOH 276 976  832  HOH HOH D . 
DB 7 HOH 277 977  945  HOH HOH D . 
DB 7 HOH 278 978  1472 HOH HOH D . 
DB 7 HOH 279 979  1585 HOH HOH D . 
DB 7 HOH 280 980  209  HOH HOH D . 
DB 7 HOH 281 981  1203 HOH HOH D . 
DB 7 HOH 282 982  1468 HOH HOH D . 
DB 7 HOH 283 983  1404 HOH HOH D . 
DB 7 HOH 284 984  1484 HOH HOH D . 
DB 7 HOH 285 985  1275 HOH HOH D . 
DB 7 HOH 286 986  600  HOH HOH D . 
DB 7 HOH 287 987  1521 HOH HOH D . 
DB 7 HOH 288 988  913  HOH HOH D . 
DB 7 HOH 289 989  530  HOH HOH D . 
DB 7 HOH 290 990  1462 HOH HOH D . 
DB 7 HOH 291 991  1522 HOH HOH D . 
DB 7 HOH 292 992  1455 HOH HOH D . 
DB 7 HOH 293 993  681  HOH HOH D . 
DB 7 HOH 294 994  1523 HOH HOH D . 
DB 7 HOH 295 995  1524 HOH HOH D . 
DB 7 HOH 296 996  977  HOH HOH D . 
DB 7 HOH 297 997  730  HOH HOH D . 
DB 7 HOH 298 998  736  HOH HOH D . 
DB 7 HOH 299 999  1592 HOH HOH D . 
DB 7 HOH 300 1000 856  HOH HOH D . 
DB 7 HOH 301 1001 1038 HOH HOH D . 
DB 7 HOH 302 1002 1372 HOH HOH D . 
DB 7 HOH 303 1003 1049 HOH HOH D . 
DB 7 HOH 304 1004 724  HOH HOH D . 
DB 7 HOH 305 1005 543  HOH HOH D . 
DB 7 HOH 306 1006 978  HOH HOH D . 
DB 7 HOH 307 1007 1378 HOH HOH D . 
DB 7 HOH 308 1008 1564 HOH HOH D . 
DB 7 HOH 309 1009 648  HOH HOH D . 
DB 7 HOH 310 1010 1554 HOH HOH D . 
DB 7 HOH 311 1011 869  HOH HOH D . 
DB 7 HOH 312 1012 718  HOH HOH D . 
DB 7 HOH 313 1013 1506 HOH HOH D . 
DB 7 HOH 314 1014 1495 HOH HOH D . 
DB 7 HOH 315 1015 1527 HOH HOH D . 
DB 7 HOH 316 1016 722  HOH HOH D . 
DB 7 HOH 317 1017 993  HOH HOH D . 
DB 7 HOH 318 1018 444  HOH HOH D . 
DB 7 HOH 319 1019 1373 HOH HOH D . 
DB 7 HOH 320 1020 564  HOH HOH D . 
DB 7 HOH 321 1021 579  HOH HOH D . 
DB 7 HOH 322 1022 1507 HOH HOH D . 
DB 7 HOH 323 1023 973  HOH HOH D . 
DB 7 HOH 324 1024 1141 HOH HOH D . 
DB 7 HOH 325 1025 1245 HOH HOH D . 
DB 7 HOH 326 1026 1528 HOH HOH D . 
DB 7 HOH 327 1027 1216 HOH HOH D . 
DB 7 HOH 328 1028 1029 HOH HOH D . 
DB 7 HOH 329 1029 1565 HOH HOH D . 
DB 7 HOH 330 1030 1281 HOH HOH D . 
DB 7 HOH 331 1031 1450 HOH HOH D . 
DB 7 HOH 332 1032 1590 HOH HOH D . 
DB 7 HOH 333 1033 1351 HOH HOH D . 
DB 7 HOH 334 1034 1538 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 353 ? CG  ? A LYS 322 CG  
6   1 Y 1 A LYS 353 ? CD  ? A LYS 322 CD  
7   1 Y 1 A LYS 353 ? CE  ? A LYS 322 CE  
8   1 Y 1 A LYS 353 ? NZ  ? A LYS 322 NZ  
9   1 Y 1 A LYS 378 ? CG  ? A LYS 347 CG  
10  1 Y 1 A LYS 378 ? CD  ? A LYS 347 CD  
11  1 Y 1 A LYS 378 ? CE  ? A LYS 347 CE  
12  1 Y 1 A LYS 378 ? NZ  ? A LYS 347 NZ  
13  1 Y 1 A LYS 381 ? CG  ? A LYS 350 CG  
14  1 Y 1 A LYS 381 ? CD  ? A LYS 350 CD  
15  1 Y 1 A LYS 381 ? CE  ? A LYS 350 CE  
16  1 Y 1 A LYS 381 ? NZ  ? A LYS 350 NZ  
17  1 Y 1 B LYS 127 ? CG  ? B LYS 96  CG  
18  1 Y 1 B LYS 127 ? CD  ? B LYS 96  CD  
19  1 Y 1 B LYS 127 ? CE  ? B LYS 96  CE  
20  1 Y 1 B LYS 127 ? NZ  ? B LYS 96  NZ  
21  1 Y 1 B LYS 273 ? CG  ? B LYS 242 CG  
22  1 Y 1 B LYS 273 ? CD  ? B LYS 242 CD  
23  1 Y 1 B LYS 273 ? CE  ? B LYS 242 CE  
24  1 Y 1 B LYS 273 ? NZ  ? B LYS 242 NZ  
25  1 Y 1 B LYS 353 ? CG  ? B LYS 322 CG  
26  1 Y 1 B LYS 353 ? CD  ? B LYS 322 CD  
27  1 Y 1 B LYS 353 ? CE  ? B LYS 322 CE  
28  1 Y 1 B LYS 353 ? NZ  ? B LYS 322 NZ  
29  1 Y 1 B LYS 378 ? CG  ? B LYS 347 CG  
30  1 Y 1 B LYS 378 ? CD  ? B LYS 347 CD  
31  1 Y 1 B LYS 378 ? CE  ? B LYS 347 CE  
32  1 Y 1 B LYS 378 ? NZ  ? B LYS 347 NZ  
33  1 Y 1 B LYS 381 ? CG  ? B LYS 350 CG  
34  1 Y 1 B LYS 381 ? CD  ? B LYS 350 CD  
35  1 Y 1 B LYS 381 ? CE  ? B LYS 350 CE  
36  1 Y 1 B LYS 381 ? NZ  ? B LYS 350 NZ  
37  1 Y 1 B LYS 474 ? CG  ? B LYS 443 CG  
38  1 Y 1 B LYS 474 ? CD  ? B LYS 443 CD  
39  1 Y 1 B LYS 474 ? CE  ? B LYS 443 CE  
40  1 Y 1 B LYS 474 ? NZ  ? B LYS 443 NZ  
41  1 Y 1 B HIS 510 ? CG  ? B HIS 479 CG  
42  1 Y 1 B HIS 510 ? ND1 ? B HIS 479 ND1 
43  1 Y 1 B HIS 510 ? CD2 ? B HIS 479 CD2 
44  1 Y 1 B HIS 510 ? CE1 ? B HIS 479 CE1 
45  1 Y 1 B HIS 510 ? NE2 ? B HIS 479 NE2 
46  1 Y 1 C LYS 168 ? CG  ? C LYS 137 CG  
47  1 Y 1 C LYS 168 ? CD  ? C LYS 137 CD  
48  1 Y 1 C LYS 168 ? CE  ? C LYS 137 CE  
49  1 Y 1 C LYS 168 ? NZ  ? C LYS 137 NZ  
50  1 Y 1 C LYS 194 ? CG  ? C LYS 163 CG  
51  1 Y 1 C LYS 194 ? CD  ? C LYS 163 CD  
52  1 Y 1 C LYS 194 ? CE  ? C LYS 163 CE  
53  1 Y 1 C LYS 194 ? NZ  ? C LYS 163 NZ  
54  1 Y 1 C LYS 198 ? CG  ? C LYS 167 CG  
55  1 Y 1 C LYS 198 ? CD  ? C LYS 167 CD  
56  1 Y 1 C LYS 198 ? CE  ? C LYS 167 CE  
57  1 Y 1 C LYS 198 ? NZ  ? C LYS 167 NZ  
58  1 Y 1 C LYS 216 ? CG  ? C LYS 185 CG  
59  1 Y 1 C LYS 216 ? CD  ? C LYS 185 CD  
60  1 Y 1 C LYS 216 ? CE  ? C LYS 185 CE  
61  1 Y 1 C LYS 216 ? NZ  ? C LYS 185 NZ  
62  1 Y 1 C LYS 268 ? CG  ? C LYS 237 CG  
63  1 Y 1 C LYS 268 ? CD  ? C LYS 237 CD  
64  1 Y 1 C LYS 268 ? CE  ? C LYS 237 CE  
65  1 Y 1 C LYS 268 ? NZ  ? C LYS 237 NZ  
66  1 Y 1 C LYS 273 ? CG  ? C LYS 242 CG  
67  1 Y 1 C LYS 273 ? CD  ? C LYS 242 CD  
68  1 Y 1 C LYS 273 ? CE  ? C LYS 242 CE  
69  1 Y 1 C LYS 273 ? NZ  ? C LYS 242 NZ  
70  1 Y 1 C LYS 302 ? CG  ? C LYS 271 CG  
71  1 Y 1 C LYS 302 ? CD  ? C LYS 271 CD  
72  1 Y 1 C LYS 302 ? CE  ? C LYS 271 CE  
73  1 Y 1 C LYS 302 ? NZ  ? C LYS 271 NZ  
74  1 Y 1 C LYS 353 ? CG  ? C LYS 322 CG  
75  1 Y 1 C LYS 353 ? CD  ? C LYS 322 CD  
76  1 Y 1 C LYS 353 ? CE  ? C LYS 322 CE  
77  1 Y 1 C LYS 353 ? NZ  ? C LYS 322 NZ  
78  1 Y 1 C LYS 378 ? CG  ? C LYS 347 CG  
79  1 Y 1 C LYS 378 ? CD  ? C LYS 347 CD  
80  1 Y 1 C LYS 378 ? CE  ? C LYS 347 CE  
81  1 Y 1 C LYS 378 ? NZ  ? C LYS 347 NZ  
82  1 Y 1 C LYS 396 ? CG  ? C LYS 365 CG  
83  1 Y 1 C LYS 396 ? CD  ? C LYS 365 CD  
84  1 Y 1 C LYS 396 ? CE  ? C LYS 365 CE  
85  1 Y 1 C LYS 396 ? NZ  ? C LYS 365 NZ  
86  1 Y 1 C LYS 402 ? CG  ? C LYS 371 CG  
87  1 Y 1 C LYS 402 ? CD  ? C LYS 371 CD  
88  1 Y 1 C LYS 402 ? CE  ? C LYS 371 CE  
89  1 Y 1 C LYS 402 ? NZ  ? C LYS 371 NZ  
90  1 Y 1 C GLU 460 ? CG  ? C GLU 429 CG  
91  1 Y 1 C GLU 460 ? CD  ? C GLU 429 CD  
92  1 Y 1 C GLU 460 ? OE1 ? C GLU 429 OE1 
93  1 Y 1 C GLU 460 ? OE2 ? C GLU 429 OE2 
94  1 Y 1 C LYS 474 ? CG  ? C LYS 443 CG  
95  1 Y 1 C LYS 474 ? CD  ? C LYS 443 CD  
96  1 Y 1 C LYS 474 ? CE  ? C LYS 443 CE  
97  1 Y 1 C LYS 474 ? NZ  ? C LYS 443 NZ  
98  1 Y 1 C GLU 496 ? CG  ? C GLU 465 CG  
99  1 Y 1 C GLU 496 ? CD  ? C GLU 465 CD  
100 1 Y 1 C GLU 496 ? OE1 ? C GLU 465 OE1 
101 1 Y 1 C GLU 496 ? OE2 ? C GLU 465 OE2 
102 1 Y 1 D LYS 127 ? CG  ? D LYS 96  CG  
103 1 Y 1 D LYS 127 ? CD  ? D LYS 96  CD  
104 1 Y 1 D LYS 127 ? CE  ? D LYS 96  CE  
105 1 Y 1 D LYS 127 ? NZ  ? D LYS 96  NZ  
106 1 Y 1 D LYS 197 ? CG  ? D LYS 166 CG  
107 1 Y 1 D LYS 197 ? CD  ? D LYS 166 CD  
108 1 Y 1 D LYS 197 ? CE  ? D LYS 166 CE  
109 1 Y 1 D LYS 197 ? NZ  ? D LYS 166 NZ  
110 1 Y 1 D LYS 243 ? CG  ? D LYS 212 CG  
111 1 Y 1 D LYS 243 ? CD  ? D LYS 212 CD  
112 1 Y 1 D LYS 243 ? CE  ? D LYS 212 CE  
113 1 Y 1 D LYS 243 ? NZ  ? D LYS 212 NZ  
114 1 Y 1 D LYS 273 ? CG  ? D LYS 242 CG  
115 1 Y 1 D LYS 273 ? CD  ? D LYS 242 CD  
116 1 Y 1 D LYS 273 ? CE  ? D LYS 242 CE  
117 1 Y 1 D LYS 273 ? NZ  ? D LYS 242 NZ  
118 1 Y 1 D LYS 302 ? CG  ? D LYS 271 CG  
119 1 Y 1 D LYS 302 ? CD  ? D LYS 271 CD  
120 1 Y 1 D LYS 302 ? CE  ? D LYS 271 CE  
121 1 Y 1 D LYS 302 ? NZ  ? D LYS 271 NZ  
122 1 Y 1 D LYS 353 ? CG  ? D LYS 322 CG  
123 1 Y 1 D LYS 353 ? CD  ? D LYS 322 CD  
124 1 Y 1 D LYS 353 ? CE  ? D LYS 322 CE  
125 1 Y 1 D LYS 353 ? NZ  ? D LYS 322 NZ  
126 1 Y 1 D LYS 378 ? CG  ? D LYS 347 CG  
127 1 Y 1 D LYS 378 ? CD  ? D LYS 347 CD  
128 1 Y 1 D LYS 378 ? CE  ? D LYS 347 CE  
129 1 Y 1 D LYS 378 ? NZ  ? D LYS 347 NZ  
130 1 Y 1 D LYS 474 ? CG  ? D LYS 443 CG  
131 1 Y 1 D LYS 474 ? CD  ? D LYS 443 CD  
132 1 Y 1 D LYS 474 ? CE  ? D LYS 443 CE  
133 1 Y 1 D LYS 474 ? NZ  ? D LYS 443 NZ  
134 1 Y 1 D HIS 510 ? CG  ? D HIS 479 CG  
135 1 Y 1 D HIS 510 ? ND1 ? D HIS 479 ND1 
136 1 Y 1 D HIS 510 ? CD2 ? D HIS 479 CD2 
137 1 Y 1 D HIS 510 ? CE1 ? D HIS 479 CE1 
138 1 Y 1 D HIS 510 ? NE2 ? D HIS 479 NE2 
# 
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                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   99.79 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HH4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.230 
_cell.length_a_esd                 ? 
_cell.length_b                     197.600 
_cell.length_b_esd                 ? 
_cell.length_c                     75.020 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9HH4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_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                   9HH4 
_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             2.47 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.29 
_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              ? 
_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, 0.1 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         2023-07-07 
_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                          ? 
_reflns.entry_id                                       9HH4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.92 
_reflns.d_resolution_low                               36.57 
_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                                     159811 
_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                           99.37 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.27 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.92 
_reflns_shell.d_res_low                                     1.99 
_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                             15573 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.694 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_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                               ? 
_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                                 9HH4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.92 
_refine.ls_d_res_low                             36.57 
_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                     159702 
_refine.ls_number_reflns_R_free                  7985 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.39 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1689 
_refine.ls_R_factor_R_free                       0.2074 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1669 
_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       ML 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 22.29 
_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                            0.25 
_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                       1.92 
_refine_hist.d_res_low                        36.57 
_refine_hist.number_atoms_solvent             1517 
_refine_hist.number_atoms_total               16637 
_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        14853 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         267 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  ? 15533 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.010  ? 21085 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.900 ? 5786  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.062  ? 2197  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.014  ? 2728  ? f_plane_restr      ? ? 
# 
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' 1.92 1.95  . . 251 4745 94.00  . . . . 0.3494 . . . . . . . . . . . 0.3688 
'X-RAY DIFFRACTION' 1.95 1.97  . . 266 5045 99.00  . . . . 0.3190 . . . . . . . . . . . 0.3444 
'X-RAY DIFFRACTION' 1.97 1.99  . . 262 4975 99.00  . . . . 0.2956 . . . . . . . . . . . 0.3345 
'X-RAY DIFFRACTION' 1.99 2.02  . . 266 5049 99.00  . . . . 0.2703 . . . . . . . . . . . 0.2930 
'X-RAY DIFFRACTION' 2.02 2.04  . . 265 5037 99.00  . . . . 0.2387 . . . . . . . . . . . 0.2790 
'X-RAY DIFFRACTION' 2.04 2.07  . . 268 5072 99.00  . . . . 0.2257 . . . . . . . . . . . 0.2786 
'X-RAY DIFFRACTION' 2.07 2.10  . . 262 4986 99.00  . . . . 0.2124 . . . . . . . . . . . 0.2592 
'X-RAY DIFFRACTION' 2.10 2.13  . . 266 5088 99.00  . . . . 0.2054 . . . . . . . . . . . 0.2536 
'X-RAY DIFFRACTION' 2.13 2.17  . . 264 5021 99.00  . . . . 0.1963 . . . . . . . . . . . 0.2485 
'X-RAY DIFFRACTION' 2.17 2.20  . . 269 5106 100.00 . . . . 0.1985 . . . . . . . . . . . 0.2520 
'X-RAY DIFFRACTION' 2.20 2.24  . . 266 5048 100.00 . . . . 0.1984 . . . . . . . . . . . 0.2570 
'X-RAY DIFFRACTION' 2.24 2.28  . . 265 5046 100.00 . . . . 0.2010 . . . . . . . . . . . 0.2325 
'X-RAY DIFFRACTION' 2.28 2.32  . . 267 5073 99.00  . . . . 0.1909 . . . . . . . . . . . 0.2307 
'X-RAY DIFFRACTION' 2.32 2.37  . . 265 5025 100.00 . . . . 0.1844 . . . . . . . . . . . 0.2142 
'X-RAY DIFFRACTION' 2.37 2.42  . . 268 5093 100.00 . . . . 0.1783 . . . . . . . . . . . 0.2164 
'X-RAY DIFFRACTION' 2.42 2.48  . . 268 5094 100.00 . . . . 0.1758 . . . . . . . . . . . 0.2387 
'X-RAY DIFFRACTION' 2.48 2.54  . . 264 5025 100.00 . . . . 0.1704 . . . . . . . . . . . 0.2266 
'X-RAY DIFFRACTION' 2.54 2.61  . . 268 5083 100.00 . . . . 0.1679 . . . . . . . . . . . 0.2210 
'X-RAY DIFFRACTION' 2.61 2.69  . . 266 5073 100.00 . . . . 0.1633 . . . . . . . . . . . 0.2175 
'X-RAY DIFFRACTION' 2.69 2.77  . . 268 5103 100.00 . . . . 0.1637 . . . . . . . . . . . 0.2029 
'X-RAY DIFFRACTION' 2.77 2.87  . . 267 5059 100.00 . . . . 0.1587 . . . . . . . . . . . 0.2029 
'X-RAY DIFFRACTION' 2.87 2.99  . . 269 5109 100.00 . . . . 0.1640 . . . . . . . . . . . 0.2136 
'X-RAY DIFFRACTION' 2.99 3.12  . . 268 5094 100.00 . . . . 0.1652 . . . . . . . . . . . 0.2330 
'X-RAY DIFFRACTION' 3.12 3.29  . . 266 5061 100.00 . . . . 0.1556 . . . . . . . . . . . 0.1973 
'X-RAY DIFFRACTION' 3.29 3.49  . . 269 5103 100.00 . . . . 0.1470 . . . . . . . . . . . 0.1967 
'X-RAY DIFFRACTION' 3.49 3.76  . . 268 5100 100.00 . . . . 0.1404 . . . . . . . . . . . 0.1696 
'X-RAY DIFFRACTION' 3.76 4.14  . . 269 5109 100.00 . . . . 0.1367 . . . . . . . . . . . 0.1743 
'X-RAY DIFFRACTION' 4.14 4.74  . . 269 5100 100.00 . . . . 0.1246 . . . . . . . . . . . 0.1664 
'X-RAY DIFFRACTION' 4.74 5.97  . . 268 5110 100.00 . . . . 0.1568 . . . . . . . . . . . 0.1743 
'X-RAY DIFFRACTION' 5.97 36.57 . . 268 5085 98.00  . . . . 0.1724 . . . . . . . . . . . 0.1973 
# 
_struct.entry_id                     9HH4 
_struct.title                        
;Crystal structure of the family S1_19 carrageenan sulfatase ZgCgsA from Zobellia galactanivorans in complex with hybrid b-k-neocarratetraose
;
_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        9HH4 
_struct_keywords.text            'sulfatase, S1_19, carrageenan, covalent intermediate, substrate specificity, complex, 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 2 ? 
H  N N 2 ? 
I  N N 3 ? 
J  N N 4 ? 
K  N N 4 ? 
L  N N 4 ? 
M  N N 5 ? 
N  N N 5 ? 
O  N N 5 ? 
P  N N 5 ? 
Q  N N 5 ? 
R  N N 5 ? 
S  N N 5 ? 
T  N N 5 ? 
U  N N 6 ? 
V  N N 6 ? 
W  N N 6 ? 
X  N N 3 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 4 ? 
BA N N 5 ? 
CA N N 5 ? 
DA N N 5 ? 
EA N N 5 ? 
FA N N 6 ? 
GA N N 6 ? 
HA N N 3 ? 
IA N N 4 ? 
JA N N 4 ? 
KA N N 4 ? 
LA N N 5 ? 
MA N N 5 ? 
NA N N 5 ? 
OA N N 5 ? 
PA N N 5 ? 
QA N N 3 ? 
RA N N 4 ? 
SA N N 4 ? 
TA N N 4 ? 
UA N N 5 ? 
VA N N 5 ? 
WA N N 5 ? 
XA N N 5 ? 
YA N N 6 ? 
ZA N N 6 ? 
AB N N 7 ? 
BB N N 7 ? 
CB N N 7 ? 
DB N N 7 ? 
# 
_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 9HH4 A 13 ? 480 ? G0L000 44 ? 511 ? 44 511 
2 1 9HH4 B 13 ? 480 ? G0L000 44 ? 511 ? 44 511 
3 1 9HH4 C 13 ? 480 ? G0L000 44 ? 511 ? 44 511 
4 1 9HH4 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 9HH4 MET A 1  ? UNP G0L000 ?   ?  'initiating methionine' 32 1  
1 9HH4 GLY A 2  ? UNP G0L000 ?   ?  'expression tag'        33 2  
1 9HH4 SER A 3  ? UNP G0L000 ?   ?  'expression tag'        34 3  
1 9HH4 SER A 4  ? UNP G0L000 ?   ?  'expression tag'        35 4  
1 9HH4 HIS A 5  ? UNP G0L000 ?   ?  'expression tag'        36 5  
1 9HH4 HIS A 6  ? UNP G0L000 ?   ?  'expression tag'        37 6  
1 9HH4 HIS A 7  ? UNP G0L000 ?   ?  'expression tag'        38 7  
1 9HH4 HIS A 8  ? UNP G0L000 ?   ?  'expression tag'        39 8  
1 9HH4 HIS A 9  ? UNP G0L000 ?   ?  'expression tag'        40 9  
1 9HH4 HIS A 10 ? UNP G0L000 ?   ?  'expression tag'        41 10 
1 9HH4 GLY A 11 ? UNP G0L000 ?   ?  'expression tag'        42 11 
1 9HH4 SER A 12 ? UNP G0L000 ?   ?  'expression tag'        43 12 
1 9HH4 OSE A 65 ? UNP G0L000 CYS 96 conflict                96 13 
2 9HH4 MET B 1  ? UNP G0L000 ?   ?  'initiating methionine' 32 14 
2 9HH4 GLY B 2  ? UNP G0L000 ?   ?  'expression tag'        33 15 
2 9HH4 SER B 3  ? UNP G0L000 ?   ?  'expression tag'        34 16 
2 9HH4 SER B 4  ? UNP G0L000 ?   ?  'expression tag'        35 17 
2 9HH4 HIS B 5  ? UNP G0L000 ?   ?  'expression tag'        36 18 
2 9HH4 HIS B 6  ? UNP G0L000 ?   ?  'expression tag'        37 19 
2 9HH4 HIS B 7  ? UNP G0L000 ?   ?  'expression tag'        38 20 
2 9HH4 HIS B 8  ? UNP G0L000 ?   ?  'expression tag'        39 21 
2 9HH4 HIS B 9  ? UNP G0L000 ?   ?  'expression tag'        40 22 
2 9HH4 HIS B 10 ? UNP G0L000 ?   ?  'expression tag'        41 23 
2 9HH4 GLY B 11 ? UNP G0L000 ?   ?  'expression tag'        42 24 
2 9HH4 SER B 12 ? UNP G0L000 ?   ?  'expression tag'        43 25 
2 9HH4 OSE B 65 ? UNP G0L000 CYS 96 conflict                96 26 
3 9HH4 MET C 1  ? UNP G0L000 ?   ?  'initiating methionine' 32 27 
3 9HH4 GLY C 2  ? UNP G0L000 ?   ?  'expression tag'        33 28 
3 9HH4 SER C 3  ? UNP G0L000 ?   ?  'expression tag'        34 29 
3 9HH4 SER C 4  ? UNP G0L000 ?   ?  'expression tag'        35 30 
3 9HH4 HIS C 5  ? UNP G0L000 ?   ?  'expression tag'        36 31 
3 9HH4 HIS C 6  ? UNP G0L000 ?   ?  'expression tag'        37 32 
3 9HH4 HIS C 7  ? UNP G0L000 ?   ?  'expression tag'        38 33 
3 9HH4 HIS C 8  ? UNP G0L000 ?   ?  'expression tag'        39 34 
3 9HH4 HIS C 9  ? UNP G0L000 ?   ?  'expression tag'        40 35 
3 9HH4 HIS C 10 ? UNP G0L000 ?   ?  'expression tag'        41 36 
3 9HH4 GLY C 11 ? UNP G0L000 ?   ?  'expression tag'        42 37 
3 9HH4 SER C 12 ? UNP G0L000 ?   ?  'expression tag'        43 38 
3 9HH4 OSE C 65 ? UNP G0L000 CYS 96 conflict                96 39 
4 9HH4 MET D 1  ? UNP G0L000 ?   ?  'initiating methionine' 32 40 
4 9HH4 GLY D 2  ? UNP G0L000 ?   ?  'expression tag'        33 41 
4 9HH4 SER D 3  ? UNP G0L000 ?   ?  'expression tag'        34 42 
4 9HH4 SER D 4  ? UNP G0L000 ?   ?  'expression tag'        35 43 
4 9HH4 HIS D 5  ? UNP G0L000 ?   ?  'expression tag'        36 44 
4 9HH4 HIS D 6  ? UNP G0L000 ?   ?  'expression tag'        37 45 
4 9HH4 HIS D 7  ? UNP G0L000 ?   ?  'expression tag'        38 46 
4 9HH4 HIS D 8  ? UNP G0L000 ?   ?  'expression tag'        39 47 
4 9HH4 HIS D 9  ? UNP G0L000 ?   ?  'expression tag'        40 48 
4 9HH4 HIS D 10 ? UNP G0L000 ?   ?  'expression tag'        41 49 
4 9HH4 GLY D 11 ? UNP G0L000 ?   ?  'expression tag'        42 50 
4 9HH4 SER D 12 ? UNP G0L000 ?   ?  'expression tag'        43 51 
4 9HH4 OSE D 65 ? UNP G0L000 CYS 96 conflict                96 52 
# 
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 author_defined_assembly   ?    monomeric 1 
2 author_defined_assembly   ?    monomeric 1 
3 author_defined_assembly   ?    monomeric 1 
4 author_defined_assembly   ?    monomeric 1 
5 software_defined_assembly PISA dimeric   2 
6 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 
5 'ABSA (A^2)' 8210  ? 
5 MORE         -112  ? 
5 'SSA (A^2)'  33880 ? 
6 'ABSA (A^2)' 6960  ? 
6 MORE         -82   ? 
6 'SSA (A^2)'  33400 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,AB                                   
2 1 B,F,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,BB                                      
3 1 C,G,HA,IA,JA,KA,LA,MA,NA,OA,PA,CB                                      
4 1 D,H,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA,DB                                   
5 1 A,B,E,F,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,AB,BB 
6 1 D,H,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA,DB                                   
6 2 C,G,HA,IA,JA,KA,LA,MA,NA,OA,PA,CB                                      
# 
_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 on SEC, eluting at the molecular weight 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_554 x,y,z-1 1.0000000000 0.0000000000 0.0000000000 12.7562140341 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 -73.9275280496 
# 
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  ? THR A 81  ? TYR A 108 THR A 112 5 ? 5  
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 ? ALA A 115 ? TYR A 138 ALA A 146 1 ? 9  
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 212 ? TYR A 223 LYS A 243 1 ? 21 
HELX_P HELX_P11 AB2 LYS A 231 ? ALA A 236 ? LYS A 262 ALA A 267 1 ? 6  
HELX_P HELX_P12 AB3 LYS A 237 ? ALA A 239 ? LYS A 268 ALA A 270 5 ? 3  
HELX_P HELX_P13 AB4 ASP A 243 ? THR A 270 ? ASP A 274 THR A 301 1 ? 28 
HELX_P HELX_P14 AB5 TRP A 305 ? TYR A 309 ? TRP A 336 TYR A 340 1 ? 5  
HELX_P HELX_P15 AB6 ASP A 335 ? ALA A 344 ? ASP A 366 ALA A 375 1 ? 10 
HELX_P HELX_P16 AB7 ILE A 359 ? ASN A 366 ? ILE A 390 ASN A 397 1 ? 8  
HELX_P HELX_P17 AB8 TYR A 423 ? SER A 440 ? TYR A 454 SER A 471 1 ? 18 
HELX_P HELX_P18 AB9 SER A 449 ? SER A 458 ? SER A 480 SER A 489 1 ? 10 
HELX_P HELX_P19 AC1 ASN A 463 ? PHE A 468 ? ASN A 494 PHE A 499 1 ? 6  
HELX_P HELX_P20 AC2 VAL A 470 ? ASP A 475 ? VAL A 501 ASP A 506 1 ? 6  
HELX_P HELX_P21 AC3 VAL B 32  ? GLY B 36  ? VAL B 63  GLY B 67  5 ? 5  
HELX_P HELX_P22 AC4 THR B 42  ? ASN B 51  ? THR B 73  ASN B 82  1 ? 10 
HELX_P HELX_P23 AC5 PHE B 64  ? GLY B 75  ? PHE B 95  GLY B 106 1 ? 12 
HELX_P HELX_P24 AC6 TYR B 77  ? GLY B 82  ? TYR B 108 GLY B 113 1 ? 6  
HELX_P HELX_P25 AC7 ASP B 94  ? ASN B 98  ? ASP B 125 ASN B 129 5 ? 5  
HELX_P HELX_P26 AC8 TYR B 107 ? ALA B 115 ? TYR B 138 ALA B 146 1 ? 9  
HELX_P HELX_P27 AC9 ALA B 130 ? ARG B 138 ? ALA B 161 ARG B 169 5 ? 9  
HELX_P HELX_P28 AD1 PHE B 154 ? ALA B 168 ? PHE B 185 ALA B 199 1 ? 15 
HELX_P HELX_P29 AD2 ARG B 174 ? PHE B 178 ? ARG B 205 PHE B 209 5 ? 5  
HELX_P HELX_P30 AD3 TYR B 192 ? LYS B 212 ? TYR B 223 LYS B 243 1 ? 21 
HELX_P HELX_P31 AD4 LYS B 231 ? LYS B 237 ? LYS B 262 LYS B 268 1 ? 7  
HELX_P HELX_P32 AD5 ASP B 243 ? THR B 270 ? ASP B 274 THR B 301 1 ? 28 
HELX_P HELX_P33 AD6 TRP B 305 ? TYR B 309 ? TRP B 336 TYR B 340 1 ? 5  
HELX_P HELX_P34 AD7 ASP B 335 ? ALA B 344 ? ASP B 366 ALA B 375 1 ? 10 
HELX_P HELX_P35 AD8 ILE B 359 ? ASN B 366 ? ILE B 390 ASN B 397 1 ? 8  
HELX_P HELX_P36 AD9 TYR B 423 ? LYS B 439 ? TYR B 454 LYS B 470 1 ? 17 
HELX_P HELX_P37 AE1 SER B 449 ? SER B 458 ? SER B 480 SER B 489 1 ? 10 
HELX_P HELX_P38 AE2 ASN B 463 ? PHE B 468 ? ASN B 494 PHE B 499 1 ? 6  
HELX_P HELX_P39 AE3 VAL B 470 ? ASP B 475 ? VAL B 501 ASP B 506 1 ? 6  
HELX_P HELX_P40 AE4 VAL C 32  ? GLY C 36  ? VAL C 63  GLY C 67  5 ? 5  
HELX_P HELX_P41 AE5 THR C 42  ? ASN C 51  ? THR C 73  ASN C 82  1 ? 10 
HELX_P HELX_P42 AE6 PHE C 64  ? GLY C 75  ? PHE C 95  GLY C 106 1 ? 12 
HELX_P HELX_P43 AE7 TYR C 77  ? GLY C 82  ? TYR C 108 GLY C 113 1 ? 6  
HELX_P HELX_P44 AE8 ASP C 94  ? ASN C 98  ? ASP C 125 ASN C 129 5 ? 5  
HELX_P HELX_P45 AE9 TYR C 107 ? ALA C 115 ? TYR C 138 ALA C 146 1 ? 9  
HELX_P HELX_P46 AF1 ALA C 130 ? ARG C 138 ? ALA C 161 ARG C 169 5 ? 9  
HELX_P HELX_P47 AF2 PHE C 154 ? GLY C 169 ? PHE C 185 GLY C 200 1 ? 16 
HELX_P HELX_P48 AF3 ARG C 174 ? PHE C 178 ? ARG C 205 PHE C 209 5 ? 5  
HELX_P HELX_P49 AF4 TYR C 192 ? LYS C 212 ? TYR C 223 LYS C 243 1 ? 21 
HELX_P HELX_P50 AF5 LYS C 231 ? LYS C 237 ? LYS C 262 LYS C 268 1 ? 7  
HELX_P HELX_P51 AF6 ASP C 243 ? THR C 270 ? ASP C 274 THR C 301 1 ? 28 
HELX_P HELX_P52 AF7 TRP C 305 ? TYR C 309 ? TRP C 336 TYR C 340 1 ? 5  
HELX_P HELX_P53 AF8 ASP C 335 ? ALA C 344 ? ASP C 366 ALA C 375 1 ? 10 
HELX_P HELX_P54 AF9 ILE C 359 ? ASN C 366 ? ILE C 390 ASN C 397 1 ? 8  
HELX_P HELX_P55 AG1 TYR C 423 ? LYS C 439 ? TYR C 454 LYS C 470 1 ? 17 
HELX_P HELX_P56 AG2 SER C 449 ? SER C 458 ? SER C 480 SER C 489 1 ? 10 
HELX_P HELX_P57 AG3 ASN C 463 ? PHE C 468 ? ASN C 494 PHE C 499 1 ? 6  
HELX_P HELX_P58 AG4 VAL C 470 ? ASP C 475 ? VAL C 501 ASP C 506 1 ? 6  
HELX_P HELX_P59 AG5 VAL D 32  ? GLY D 36  ? VAL D 63  GLY D 67  5 ? 5  
HELX_P HELX_P60 AG6 THR D 42  ? ASN D 51  ? THR D 73  ASN D 82  1 ? 10 
HELX_P HELX_P61 AG7 PHE D 64  ? GLY D 75  ? PHE D 95  GLY D 106 1 ? 12 
HELX_P HELX_P62 AG8 TYR D 77  ? GLY D 82  ? TYR D 108 GLY D 113 1 ? 6  
HELX_P HELX_P63 AG9 ASP D 94  ? ASN D 98  ? ASP D 125 ASN D 129 5 ? 5  
HELX_P HELX_P64 AH1 TYR D 107 ? ALA D 115 ? TYR D 138 ALA D 146 1 ? 9  
HELX_P HELX_P65 AH2 ALA D 130 ? ARG D 138 ? ALA D 161 ARG D 169 5 ? 9  
HELX_P HELX_P66 AH3 PHE D 154 ? ALA D 168 ? PHE D 185 ALA D 199 1 ? 15 
HELX_P HELX_P67 AH4 ARG D 174 ? PHE D 178 ? ARG D 205 PHE D 209 5 ? 5  
HELX_P HELX_P68 AH5 TYR D 192 ? LYS D 212 ? TYR D 223 LYS D 243 1 ? 21 
HELX_P HELX_P69 AH6 LYS D 231 ? ALA D 236 ? LYS D 262 ALA D 267 1 ? 6  
HELX_P HELX_P70 AH7 LYS D 237 ? ALA D 239 ? LYS D 268 ALA D 270 5 ? 3  
HELX_P HELX_P71 AH8 ASP D 243 ? THR D 270 ? ASP D 274 THR D 301 1 ? 28 
HELX_P HELX_P72 AH9 TRP D 305 ? TYR D 309 ? TRP D 336 TYR D 340 1 ? 5  
HELX_P HELX_P73 AI1 ASP D 335 ? ALA D 344 ? ASP D 366 ALA D 375 1 ? 10 
HELX_P HELX_P74 AI2 ILE D 359 ? ASN D 366 ? ILE D 390 ASN D 397 1 ? 8  
HELX_P HELX_P75 AI3 TYR D 423 ? LYS D 439 ? TYR D 454 LYS D 470 1 ? 17 
HELX_P HELX_P76 AI4 SER D 449 ? SER D 458 ? SER D 480 SER D 489 1 ? 10 
HELX_P HELX_P77 AI5 ASN D 463 ? PHE D 468 ? ASN D 494 PHE D 499 1 ? 6  
HELX_P HELX_P78 AI6 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  OSE 65 N  ? ? A PHE 95  A OSE 96  1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale2  covale both ? A OSE 65  C   ? ? ? 1_555 A  GLY 66 N  ? ? A OSE 96  A GLY 97  1_555 ? ? ? ? ? ? ? 1.322 ? ? 
covale3  covale both ? B PHE 64  C   ? ? ? 1_555 B  OSE 65 N  ? ? B PHE 95  B OSE 96  1_555 ? ? ? ? ? ? ? 1.342 ? ? 
covale4  covale both ? B OSE 65  C   ? ? ? 1_555 B  GLY 66 N  ? ? B OSE 96  B GLY 97  1_555 ? ? ? ? ? ? ? 1.323 ? ? 
covale5  covale both ? C PHE 64  C   ? ? ? 1_555 C  OSE 65 N  ? ? C PHE 95  C OSE 96  1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale6  covale both ? C OSE 65  C   ? ? ? 1_555 C  GLY 66 N  ? ? C OSE 96  C GLY 97  1_555 ? ? ? ? ? ? ? 1.318 ? ? 
covale7  covale both ? D PHE 64  C   ? ? ? 1_555 D  OSE 65 N  ? ? D PHE 95  D OSE 96  1_555 ? ? ? ? ? ? ? 1.343 ? ? 
covale8  covale both ? D OSE 65  C   ? ? ? 1_555 D  GLY 66 N  ? ? D OSE 96  D GLY 97  1_555 ? ? ? ? ? ? ? 1.342 ? ? 
covale9  covale both ? E G4S .   O3  ? ? ? 1_555 E  9RN .  C1 ? ? I G4S 1   I 9RN 2   1_555 ? ? ? ? ? ? ? 1.389 ? ? 
covale10 covale both ? E 9RN .   O4  ? ? ? 1_555 E  GAL .  C1 ? ? I 9RN 2   I GAL 3   1_555 ? ? ? ? ? ? ? 1.389 ? ? 
covale11 covale both ? E GAL .   O3  ? ? ? 1_555 E  9RN .  C1 ? ? I GAL 3   I 9RN 4   1_555 ? ? ? ? ? ? ? 1.391 ? ? 
covale12 covale both ? F G4S .   O3  ? ? ? 1_555 F  9RN .  C1 ? ? J G4S 1   J 9RN 2   1_555 ? ? ? ? ? ? ? 1.392 ? ? 
covale13 covale both ? F 9RN .   O4  ? ? ? 1_555 F  GAL .  C1 ? ? J 9RN 2   J GAL 3   1_555 ? ? ? ? ? ? ? 1.390 ? ? 
covale14 covale both ? F GAL .   O3  ? ? ? 1_555 F  9RN .  C1 ? ? J GAL 3   J 9RN 4   1_555 ? ? ? ? ? ? ? 1.395 ? ? 
covale15 covale both ? G G4S .   O3  ? ? ? 1_555 G  9RN .  C1 ? ? K G4S 1   K 9RN 2   1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale16 covale both ? G 9RN .   O4  ? ? ? 1_555 G  GAL .  C1 ? ? K 9RN 2   K GAL 3   1_555 ? ? ? ? ? ? ? 1.390 ? ? 
covale17 covale both ? G GAL .   O3  ? ? ? 1_555 G  9RN .  C1 ? ? K GAL 3   K 9RN 4   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale18 covale both ? H G4S .   O3  ? ? ? 1_555 H  9RN .  C1 ? ? L G4S 1   L 9RN 2   1_555 ? ? ? ? ? ? ? 1.399 ? ? 
covale19 covale both ? H 9RN .   O4  ? ? ? 1_555 H  GAL .  C1 ? ? L 9RN 2   L GAL 3   1_555 ? ? ? ? ? ? ? 1.391 ? ? 
covale20 covale both ? H GAL .   O3  ? ? ? 1_555 H  9RN .  C1 ? ? L GAL 3   L 9RN 4   1_555 ? ? ? ? ? ? ? 1.396 ? ? 
metalc1  metalc ?    ? A ASP 25  OD1 ? ? ? 1_555 I  CA  .  CA ? ? A ASP 56  A CA  601 1_555 ? ? ? ? ? ? ? 2.180 ? ? 
metalc2  metalc ?    ? A ASP 26  OD1 ? ? ? 1_555 I  CA  .  CA ? ? A ASP 57  A CA  601 1_555 ? ? ? ? ? ? ? 2.216 ? ? 
metalc3  metalc ?    ? A OSE 65  O3S ? ? ? 1_555 I  CA  .  CA ? ? A OSE 96  A CA  601 1_555 ? ? ? ? ? ? ? 2.416 ? ? 
metalc4  metalc ?    ? A ASP 283 OD1 ? ? ? 1_555 I  CA  .  CA ? ? A ASP 314 A CA  601 1_555 ? ? ? ? ? ? ? 2.566 ? ? 
metalc5  metalc ?    ? A ASP 283 OD2 ? ? ? 1_555 I  CA  .  CA ? ? A ASP 314 A CA  601 1_555 ? ? ? ? ? ? ? 2.384 ? ? 
metalc6  metalc ?    ? A ASN 284 OD1 ? ? ? 1_555 I  CA  .  CA ? ? A ASN 315 A CA  601 1_555 ? ? ? ? ? ? ? 2.508 ? ? 
metalc7  metalc ?    ? B ASP 25  OD1 ? ? ? 1_555 X  CA  .  CA ? ? B ASP 56  B CA  601 1_555 ? ? ? ? ? ? ? 2.153 ? ? 
metalc8  metalc ?    ? B ASP 26  OD1 ? ? ? 1_555 X  CA  .  CA ? ? B ASP 57  B CA  601 1_555 ? ? ? ? ? ? ? 2.183 ? ? 
metalc9  metalc ?    ? B OSE 65  O3S ? ? ? 1_555 X  CA  .  CA ? ? B OSE 96  B CA  601 1_555 ? ? ? ? ? ? ? 2.352 ? ? 
metalc10 metalc ?    ? B ASP 283 OD1 ? ? ? 1_555 X  CA  .  CA ? ? B ASP 314 B CA  601 1_555 ? ? ? ? ? ? ? 2.739 ? ? 
metalc11 metalc ?    ? B ASP 283 OD2 ? ? ? 1_555 X  CA  .  CA ? ? B ASP 314 B CA  601 1_555 ? ? ? ? ? ? ? 2.488 ? ? 
metalc12 metalc ?    ? B ASN 284 OD1 ? ? ? 1_555 X  CA  .  CA ? ? B ASN 315 B CA  601 1_555 ? ? ? ? ? ? ? 2.668 ? ? 
metalc13 metalc ?    ? C ASP 25  OD1 ? ? ? 1_555 HA CA  .  CA ? ? C ASP 56  C CA  601 1_555 ? ? ? ? ? ? ? 2.250 ? ? 
metalc14 metalc ?    ? C ASP 26  OD1 ? ? ? 1_555 HA CA  .  CA ? ? C ASP 57  C CA  601 1_555 ? ? ? ? ? ? ? 2.161 ? ? 
metalc15 metalc ?    ? C OSE 65  O1S ? ? ? 1_555 HA CA  .  CA ? ? C OSE 96  C CA  601 1_555 ? ? ? ? ? ? ? 2.294 ? ? 
metalc16 metalc ?    ? C ASP 283 OD1 ? ? ? 1_555 HA CA  .  CA ? ? C ASP 314 C CA  601 1_555 ? ? ? ? ? ? ? 2.637 ? ? 
metalc17 metalc ?    ? C ASP 283 OD2 ? ? ? 1_555 HA CA  .  CA ? ? C ASP 314 C CA  601 1_555 ? ? ? ? ? ? ? 2.593 ? ? 
metalc18 metalc ?    ? C ASN 284 OD1 ? ? ? 1_555 HA CA  .  CA ? ? C ASN 315 C CA  601 1_555 ? ? ? ? ? ? ? 2.501 ? ? 
metalc19 metalc ?    ? D ASP 25  OD1 ? ? ? 1_555 QA CA  .  CA ? ? D ASP 56  D CA  601 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc20 metalc ?    ? D ASP 26  OD1 ? ? ? 1_555 QA CA  .  CA ? ? D ASP 57  D CA  601 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc21 metalc ?    ? D OSE 65  O1S ? ? ? 1_555 QA CA  .  CA ? ? D OSE 96  D CA  601 1_555 ? ? ? ? ? ? ? 2.503 ? ? 
metalc22 metalc ?    ? D ASP 283 OD1 ? ? ? 1_555 QA CA  .  CA ? ? D ASP 314 D CA  601 1_555 ? ? ? ? ? ? ? 2.390 ? ? 
metalc23 metalc ?    ? D ASP 283 OD2 ? ? ? 1_555 QA CA  .  CA ? ? D ASP 314 D CA  601 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc24 metalc ?    ? D ASN 284 OD1 ? ? ? 1_555 QA CA  .  CA ? ? D ASN 315 D CA  601 1_555 ? ? ? ? ? ? ? 2.678 ? ? 
# 
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 ? I  CA . ? A CA 601 ? 1_555 OD1 ? A ASP 26  ? A ASP 57  ? 1_555 92.6  ? 
2  OD1 ? A ASP 25  ? A ASP 56  ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 O3S ? A OSE 65  ? A OSE 96  ? 1_555 106.4 ? 
3  OD1 ? A ASP 26  ? A ASP 57  ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 O3S ? A OSE 65  ? A OSE 96  ? 1_555 93.3  ? 
4  OD1 ? A ASP 25  ? A ASP 56  ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 OD1 ? A ASP 283 ? A ASP 314 ? 1_555 86.1  ? 
5  OD1 ? A ASP 26  ? A ASP 57  ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 OD1 ? A ASP 283 ? A ASP 314 ? 1_555 110.0 ? 
6  O3S ? A OSE 65  ? A OSE 96  ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 OD1 ? A ASP 283 ? A ASP 314 ? 1_555 153.2 ? 
7  OD1 ? A ASP 25  ? A ASP 56  ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 OD2 ? A ASP 283 ? A ASP 314 ? 1_555 85.0  ? 
8  OD1 ? A ASP 26  ? A ASP 57  ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 OD2 ? A ASP 283 ? A ASP 314 ? 1_555 162.8 ? 
9  O3S ? A OSE 65  ? A OSE 96  ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 OD2 ? A ASP 283 ? A ASP 314 ? 1_555 103.7 ? 
10 OD1 ? A ASP 283 ? A ASP 314 ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 OD2 ? A ASP 283 ? A ASP 314 ? 1_555 52.9  ? 
11 OD1 ? A ASP 25  ? A ASP 56  ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 OD1 ? A ASN 284 ? A ASN 315 ? 1_555 161.7 ? 
12 OD1 ? A ASP 26  ? A ASP 57  ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 OD1 ? A ASN 284 ? A ASN 315 ? 1_555 97.9  ? 
13 O3S ? A OSE 65  ? A OSE 96  ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 OD1 ? A ASN 284 ? A ASN 315 ? 1_555 88.0  ? 
14 OD1 ? A ASP 283 ? A ASP 314 ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 OD1 ? A ASN 284 ? A ASN 315 ? 1_555 76.3  ? 
15 OD2 ? A ASP 283 ? A ASP 314 ? 1_555 CA ? I  CA . ? A CA 601 ? 1_555 OD1 ? A ASN 284 ? A ASN 315 ? 1_555 80.6  ? 
16 OD1 ? B ASP 25  ? B ASP 56  ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD1 ? B ASP 26  ? B ASP 57  ? 1_555 96.0  ? 
17 OD1 ? B ASP 25  ? B ASP 56  ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 O3S ? B OSE 65  ? B OSE 96  ? 1_555 119.3 ? 
18 OD1 ? B ASP 26  ? B ASP 57  ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 O3S ? B OSE 65  ? B OSE 96  ? 1_555 94.9  ? 
19 OD1 ? B ASP 25  ? B ASP 56  ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD1 ? B ASP 283 ? B ASP 314 ? 1_555 85.2  ? 
20 OD1 ? B ASP 26  ? B ASP 57  ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD1 ? B ASP 283 ? B ASP 314 ? 1_555 105.8 ? 
21 O3S ? B OSE 65  ? B OSE 96  ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD1 ? B ASP 283 ? B ASP 314 ? 1_555 146.3 ? 
22 OD1 ? B ASP 25  ? B ASP 56  ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD2 ? B ASP 283 ? B ASP 314 ? 1_555 83.4  ? 
23 OD1 ? B ASP 26  ? B ASP 57  ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD2 ? B ASP 283 ? B ASP 314 ? 1_555 155.4 ? 
24 O3S ? B OSE 65  ? B OSE 96  ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD2 ? B ASP 283 ? B ASP 314 ? 1_555 106.9 ? 
25 OD1 ? B ASP 283 ? B ASP 314 ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD2 ? B ASP 283 ? B ASP 314 ? 1_555 49.6  ? 
26 OD1 ? B ASP 25  ? B ASP 56  ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD1 ? B ASN 284 ? B ASN 315 ? 1_555 156.6 ? 
27 OD1 ? B ASP 26  ? B ASP 57  ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD1 ? B ASN 284 ? B ASN 315 ? 1_555 96.3  ? 
28 O3S ? B OSE 65  ? B OSE 96  ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD1 ? B ASN 284 ? B ASN 315 ? 1_555 79.4  ? 
29 OD1 ? B ASP 283 ? B ASP 314 ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD1 ? B ASN 284 ? B ASN 315 ? 1_555 72.3  ? 
30 OD2 ? B ASP 283 ? B ASP 314 ? 1_555 CA ? X  CA . ? B CA 601 ? 1_555 OD1 ? B ASN 284 ? B ASN 315 ? 1_555 77.2  ? 
31 OD1 ? C ASP 25  ? C ASP 56  ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD1 ? C ASP 26  ? C ASP 57  ? 1_555 97.4  ? 
32 OD1 ? C ASP 25  ? C ASP 56  ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 O1S ? C OSE 65  ? C OSE 96  ? 1_555 115.0 ? 
33 OD1 ? C ASP 26  ? C ASP 57  ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 O1S ? C OSE 65  ? C OSE 96  ? 1_555 95.6  ? 
34 OD1 ? C ASP 25  ? C ASP 56  ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD1 ? C ASP 283 ? C ASP 314 ? 1_555 82.4  ? 
35 OD1 ? C ASP 26  ? C ASP 57  ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD1 ? C ASP 283 ? C ASP 314 ? 1_555 111.7 ? 
36 O1S ? C OSE 65  ? C OSE 96  ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD1 ? C ASP 283 ? C ASP 314 ? 1_555 145.9 ? 
37 OD1 ? C ASP 25  ? C ASP 56  ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD2 ? C ASP 283 ? C ASP 314 ? 1_555 78.4  ? 
38 OD1 ? C ASP 26  ? C ASP 57  ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD2 ? C ASP 283 ? C ASP 314 ? 1_555 161.2 ? 
39 O1S ? C OSE 65  ? C OSE 96  ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD2 ? C ASP 283 ? C ASP 314 ? 1_555 102.8 ? 
40 OD1 ? C ASP 283 ? C ASP 314 ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD2 ? C ASP 283 ? C ASP 314 ? 1_555 49.8  ? 
41 OD1 ? C ASP 25  ? C ASP 56  ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD1 ? C ASN 284 ? C ASN 315 ? 1_555 157.0 ? 
42 OD1 ? C ASP 26  ? C ASP 57  ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD1 ? C ASN 284 ? C ASN 315 ? 1_555 99.7  ? 
43 O1S ? C OSE 65  ? C OSE 96  ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD1 ? C ASN 284 ? C ASN 315 ? 1_555 78.5  ? 
44 OD1 ? C ASP 283 ? C ASP 314 ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD1 ? C ASN 284 ? C ASN 315 ? 1_555 77.0  ? 
45 OD2 ? C ASP 283 ? C ASP 314 ? 1_555 CA ? HA CA . ? C CA 601 ? 1_555 OD1 ? C ASN 284 ? C ASN 315 ? 1_555 80.4  ? 
46 OD1 ? D ASP 25  ? D ASP 56  ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD1 ? D ASP 26  ? D ASP 57  ? 1_555 98.4  ? 
47 OD1 ? D ASP 25  ? D ASP 56  ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 O1S ? D OSE 65  ? D OSE 96  ? 1_555 108.0 ? 
48 OD1 ? D ASP 26  ? D ASP 57  ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 O1S ? D OSE 65  ? D OSE 96  ? 1_555 84.8  ? 
49 OD1 ? D ASP 25  ? D ASP 56  ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD1 ? D ASP 283 ? D ASP 314 ? 1_555 92.1  ? 
50 OD1 ? D ASP 26  ? D ASP 57  ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD1 ? D ASP 283 ? D ASP 314 ? 1_555 114.5 ? 
51 O1S ? D OSE 65  ? D OSE 96  ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD1 ? D ASP 283 ? D ASP 314 ? 1_555 150.2 ? 
52 OD1 ? D ASP 25  ? D ASP 56  ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD2 ? D ASP 283 ? D ASP 314 ? 1_555 85.6  ? 
53 OD1 ? D ASP 26  ? D ASP 57  ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD2 ? D ASP 283 ? D ASP 314 ? 1_555 170.7 ? 
54 O1S ? D OSE 65  ? D OSE 96  ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD2 ? D ASP 283 ? D ASP 314 ? 1_555 101.9 ? 
55 OD1 ? D ASP 283 ? D ASP 314 ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD2 ? D ASP 283 ? D ASP 314 ? 1_555 56.8  ? 
56 OD1 ? D ASP 25  ? D ASP 56  ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD1 ? D ASN 284 ? D ASN 315 ? 1_555 165.1 ? 
57 OD1 ? D ASP 26  ? D ASP 57  ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD1 ? D ASN 284 ? D ASN 315 ? 1_555 95.3  ? 
58 O1S ? D OSE 65  ? D OSE 96  ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD1 ? D ASN 284 ? D ASN 315 ? 1_555 79.0  ? 
59 OD1 ? D ASP 283 ? D ASP 314 ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD1 ? D ASN 284 ? D ASN 315 ? 1_555 76.9  ? 
60 OD2 ? D ASP 283 ? D ASP 314 ? 1_555 CA ? QA CA . ? D CA 601 ? 1_555 OD1 ? D ASN 284 ? D ASN 315 ? 1_555 80.0  ? 
# 
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 OSE A 65 ? . . . . OSE A 96 ? 1_555 . . . . . . . SER 1 OSE Sulfation 'Named protein modification' 
2 OSE B 65 ? . . . . OSE B 96 ? 1_555 . . . . . . . SER 1 OSE Sulfation 'Named protein modification' 
3 OSE C 65 ? . . . . OSE C 96 ? 1_555 . . . . . . . SER 1 OSE Sulfation 'Named protein modification' 
4 OSE D 65 ? . . . . OSE D 96 ? 1_555 . . . . . . . SER 1 OSE Sulfation '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 -2.80 
2  VAL 226 A . ? VAL 257 A PRO 227 A ? PRO 258 A 1 0.77  
3  TYR 295 A . ? TYR 326 A PRO 296 A ? PRO 327 A 1 2.95  
4  MET 461 A . ? MET 492 A PRO 462 A ? PRO 493 A 1 0.96  
5  ALA 223 B . ? ALA 254 B PRO 224 B ? PRO 255 B 1 0.13  
6  VAL 226 B . ? VAL 257 B PRO 227 B ? PRO 258 B 1 1.91  
7  TYR 295 B . ? TYR 326 B PRO 296 B ? PRO 327 B 1 2.96  
8  MET 461 B . ? MET 492 B PRO 462 B ? PRO 493 B 1 0.89  
9  ALA 223 C . ? ALA 254 C PRO 224 C ? PRO 255 C 1 -3.97 
10 VAL 226 C . ? VAL 257 C PRO 227 C ? PRO 258 C 1 3.94  
11 TYR 295 C . ? TYR 326 C PRO 296 C ? PRO 327 C 1 7.17  
12 MET 461 C . ? MET 492 C PRO 462 C ? PRO 493 C 1 1.78  
13 ALA 223 D . ? ALA 254 D PRO 224 D ? PRO 255 D 1 -5.01 
14 VAL 226 D . ? VAL 257 D PRO 227 D ? PRO 258 D 1 4.99  
15 TYR 295 D . ? TYR 326 D PRO 296 D ? PRO 327 D 1 0.99  
16 MET 461 D . ? MET 492 D PRO 462 D ? PRO 493 D 1 10.25 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 3  ? 
AA3 ? 4  ? 
AA4 ? 10 ? 
AA5 ? 3  ? 
AA6 ? 4  ? 
AA7 ? 10 ? 
AA8 ? 10 ? 
AA9 ? 4  ? 
AB1 ? 10 ? 
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  ? 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  ? anti-parallel 
AA8 3 4  ? parallel      
AA8 4 5  ? parallel      
AA8 5 6  ? parallel      
AA8 6 7  ? parallel      
AA8 7 8  ? anti-parallel 
AA8 8 9  ? anti-parallel 
AA8 9 10 ? parallel      
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AB1 1 2  ? anti-parallel 
AB1 2 3  ? anti-parallel 
AB1 3 4  ? parallel      
AB1 4 5  ? parallel      
AB1 5 6  ? parallel      
AB1 6 7  ? parallel      
AB1 7 8  ? anti-parallel 
AB1 8 9  ? anti-parallel 
AB1 9 10 ? 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  MET A 313 ? HIS A 316 ? MET A 344 HIS A 347 
AA1 9  SER A 53  ? PHE A 55  ? SER A 84  PHE A 86  
AA1 10 GLN A 325 ? PHE A 327 ? GLN A 356 PHE A 358 
AA2 1  ARG A 310 ? VAL A 311 ? ARG A 341 VAL A 342 
AA2 2  ALA A 58  ? TYR A 59  ? ALA A 89  TYR A 90  
AA2 3  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  ARG C 310 ? HIS C 316 ? ARG C 341 HIS C 347 
AA7 9  SER C 53  ? TYR C 59  ? SER C 84  TYR C 90  
AA7 10 GLN C 325 ? PHE C 327 ? GLN C 356 PHE C 358 
AA8 1  LYS C 185 ? PRO C 186 ? LYS C 216 PRO C 217 
AA8 2  GLU C 181 ? HIS C 182 ? GLU C 212 HIS C 213 
AA8 3  ASP C 142 ? PHE C 146 ? ASP C 173 PHE C 177 
AA8 4  TYR C 118 ? LYS C 124 ? TYR C 149 LYS C 155 
AA8 5  PHE C 215 ? ALA C 220 ? PHE C 246 ALA C 251 
AA8 6  ASN C 18  ? CYS C 24  ? ASN C 49  CYS C 55  
AA8 7  THR C 276 ? SER C 282 ? THR C 307 SER C 313 
AA8 8  ARG C 310 ? HIS C 316 ? ARG C 341 HIS C 347 
AA8 9  SER C 53  ? TYR C 59  ? SER C 84  TYR C 90  
AA8 10 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  LYS D 185 ? PRO D 186 ? LYS D 216 PRO D 217 
AB1 2  GLU D 181 ? HIS D 182 ? GLU D 212 HIS D 213 
AB1 3  ASP D 142 ? PHE D 146 ? ASP D 173 PHE D 177 
AB1 4  TYR D 118 ? LYS D 124 ? TYR D 149 LYS D 155 
AB1 5  PHE D 215 ? ALA D 220 ? PHE D 246 ALA D 251 
AB1 6  ASN D 18  ? CYS D 24  ? ASN D 49  CYS D 55  
AB1 7  THR D 276 ? SER D 282 ? THR D 307 SER D 313 
AB1 8  MET D 313 ? HIS D 316 ? MET D 344 HIS D 347 
AB1 9  SER D 53  ? PHE D 55  ? SER D 84  PHE D 86  
AB1 10 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 ILE A 122 ? N ILE A 153 O ALA A 220 ? O ALA A 251 
AA1 5 6  O LEU A 219 ? O LEU A 250 N LEU A 23  ? N LEU A 54  
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 VAL A 311 ? O VAL A 342 N ALA A 58  ? N ALA A 89  
AA2 2 3  N TYR A 59  ? N TYR A 90  O VAL A 331 ? O VAL A 362 
AA3 1 2  N SER A 377 ? N SER A 408 O GLY A 388 ? O GLY A 419 
AA3 2 3  N ALA A 389 ? N ALA A 420 O ILE A 396 ? O ILE A 427 
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 LEU B 219 ? O LEU B 250 N VAL B 21  ? N VAL B 52  
AA4 6 7  N VAL B 22  ? N VAL B 53  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 PHE B 315 ? O PHE B 346 N SER B 53  ? N SER B 84  
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 TYR C 144 ? O TYR C 175 N GLY C 123 ? N GLY C 154 
AA7 4 5  N ILE C 122 ? N ILE C 153 O ALA C 220 ? O ALA C 251 
AA7 5 6  O ILE C 217 ? O ILE C 248 N VAL C 21  ? N VAL C 52  
AA7 6 7  N VAL C 22  ? N VAL C 53  O VAL C 279 ? O VAL C 310 
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 LYS C 185 ? O LYS C 216 N HIS C 182 ? N HIS C 213 
AA8 2 3  O GLU C 181 ? O GLU C 212 N GLY C 145 ? N GLY C 176 
AA8 3 4  O TYR C 144 ? O TYR C 175 N GLY C 123 ? N GLY C 154 
AA8 4 5  N ILE C 122 ? N ILE C 153 O ALA C 220 ? O ALA C 251 
AA8 5 6  O ILE C 217 ? O ILE C 248 N VAL C 21  ? N VAL C 52  
AA8 6 7  N VAL C 22  ? N VAL C 53  O VAL C 279 ? O VAL C 310 
AA8 7 8  N ILE C 278 ? N ILE C 309 O HIS C 316 ? O HIS C 347 
AA8 8 9  O MET C 313 ? O MET C 344 N PHE C 55  ? N PHE C 86  
AA8 9 10 N SER C 57  ? N SER C 88  O VAL C 331 ? O VAL C 362 
AA9 1 2  N ARG C 379 ? N ARG C 410 O ASP C 386 ? O ASP C 417 
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 LYS D 185 ? O LYS D 216 N HIS D 182 ? N HIS D 213 
AB1 2 3  O GLU D 181 ? O GLU D 212 N GLY D 145 ? N GLY D 176 
AB1 3 4  O TYR D 144 ? O TYR D 175 N GLY D 123 ? N GLY D 154 
AB1 4 5  N SER D 120 ? N SER D 151 O TYR D 218 ? O TYR D 249 
AB1 5 6  O ILE D 217 ? O ILE D 248 N VAL D 21  ? N VAL D 52  
AB1 6 7  N VAL D 22  ? N VAL D 53  O VAL D 279 ? O VAL D 310 
AB1 7 8  N ILE D 278 ? N ILE D 309 O HIS D 316 ? O HIS D 347 
AB1 8 9  O MET D 313 ? O MET D 344 N PHE D 55  ? N PHE D 86  
AB1 9 10 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 MET D 391 ? N MET D 422 O TRP D 394 ? O TRP D 425 
AB3 3 4  N LYS D 395 ? N LYS D 426 O HIS D 407 ? O HIS D 438 
# 
_pdbx_entry_details.entry_id                   9HH4 
_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 TRP A 156 ? ? -109.63 -75.50  
2  1 ALA A 251 ? ? -105.93 74.15   
3  1 PRO A 255 ? ? -94.31  34.54   
4  1 ASN A 315 ? ? -170.27 -177.94 
5  1 LYS A 332 ? ? -36.48  129.98  
6  1 TRP A 348 ? ? -156.09 84.14   
7  1 VAL A 501 ? ? -130.27 -66.95  
8  1 TRP B 156 ? ? -107.76 -75.52  
9  1 TYR B 223 ? ? -36.88  122.04  
10 1 ALA B 251 ? ? -105.48 78.42   
11 1 PRO B 255 ? ? -99.33  36.79   
12 1 VAL B 257 ? ? -49.85  152.54  
13 1 TRP B 348 ? ? -162.50 87.69   
14 1 LYS B 351 ? ? -131.30 -35.87  
15 1 VAL B 501 ? ? -134.26 -66.85  
16 1 OSE C 96  ? ? -43.20  -71.38  
17 1 TRP C 156 ? ? -110.42 -75.84  
18 1 TYR C 223 ? ? -37.91  119.56  
19 1 ALA C 251 ? ? -110.82 77.57   
20 1 PRO C 255 ? ? -94.36  35.90   
21 1 TRP C 348 ? ? -155.40 87.76   
22 1 LYS C 351 ? ? -130.03 -32.12  
23 1 ASN C 494 ? ? 38.84   62.37   
24 1 VAL C 501 ? ? -131.19 -66.92  
25 1 OSE D 96  ? ? -39.17  -80.75  
26 1 TRP D 156 ? ? -103.73 -82.64  
27 1 TYR D 223 ? ? -38.90  123.05  
28 1 ALA D 251 ? ? -106.06 79.63   
29 1 PRO D 255 ? ? -97.08  39.39   
30 1 TRP D 348 ? ? -159.98 87.49   
31 1 VAL D 501 ? ? -134.20 -68.11  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG B 169 ? ? 0.194 'SIDE CHAIN' 
2 1 ARG C 169 ? ? 0.248 'SIDE CHAIN' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1125 ? 5.89 . 
2 1 O ? B HOH 1144 ? 7.67 . 
3 1 O ? C HOH 1014 ? 6.17 . 
# 
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 HIS 510 ? A HIS 479 
15 1 Y 1 A LYS 511 ? A LYS 480 
16 1 Y 1 B MET 32  ? B MET 1   
17 1 Y 1 B GLY 33  ? B GLY 2   
18 1 Y 1 B SER 34  ? B SER 3   
19 1 Y 1 B SER 35  ? B SER 4   
20 1 Y 1 B HIS 36  ? B HIS 5   
21 1 Y 1 B HIS 37  ? B HIS 6   
22 1 Y 1 B HIS 38  ? B HIS 7   
23 1 Y 1 B HIS 39  ? B HIS 8   
24 1 Y 1 B HIS 40  ? B HIS 9   
25 1 Y 1 B HIS 41  ? B HIS 10  
26 1 Y 1 B GLY 42  ? B GLY 11  
27 1 Y 1 B SER 43  ? B SER 12  
28 1 Y 1 B GLN 44  ? B GLN 13  
29 1 Y 1 B LYS 511 ? B LYS 480 
30 1 Y 1 C MET 32  ? C MET 1   
31 1 Y 1 C GLY 33  ? C GLY 2   
32 1 Y 1 C SER 34  ? C SER 3   
33 1 Y 1 C SER 35  ? C SER 4   
34 1 Y 1 C HIS 36  ? C HIS 5   
35 1 Y 1 C HIS 37  ? C HIS 6   
36 1 Y 1 C HIS 38  ? C HIS 7   
37 1 Y 1 C HIS 39  ? C HIS 8   
38 1 Y 1 C HIS 40  ? C HIS 9   
39 1 Y 1 C HIS 41  ? C HIS 10  
40 1 Y 1 C GLY 42  ? C GLY 11  
41 1 Y 1 C SER 43  ? C SER 12  
42 1 Y 1 C GLN 44  ? C GLN 13  
43 1 Y 1 C GLU 45  ? C GLU 14  
44 1 Y 1 C HIS 510 ? C HIS 479 
45 1 Y 1 C LYS 511 ? C LYS 480 
46 1 Y 1 D MET 32  ? D MET 1   
47 1 Y 1 D GLY 33  ? D GLY 2   
48 1 Y 1 D SER 34  ? D SER 3   
49 1 Y 1 D SER 35  ? D SER 4   
50 1 Y 1 D HIS 36  ? D HIS 5   
51 1 Y 1 D HIS 37  ? D HIS 6   
52 1 Y 1 D HIS 38  ? D HIS 7   
53 1 Y 1 D HIS 39  ? D HIS 8   
54 1 Y 1 D HIS 40  ? D HIS 9   
55 1 Y 1 D HIS 41  ? D HIS 10  
56 1 Y 1 D GLY 42  ? D GLY 11  
57 1 Y 1 D SER 43  ? D SER 12  
58 1 Y 1 D GLN 44  ? D GLN 13  
59 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 
9RN C2   C  N R 1   
9RN C4   C  N S 2   
9RN C5   C  N R 3   
9RN C6   C  N N 4   
9RN O4   O  N N 5   
9RN O5   O  N N 6   
9RN O3   O  N N 7   
9RN C3   C  N S 8   
9RN O2   O  N N 9   
9RN C1   C  N S 10  
9RN O1   O  N N 11  
9RN H2   H  N N 12  
9RN H4   H  N N 13  
9RN H5   H  N N 14  
9RN H61  H  N N 15  
9RN H62  H  N N 16  
9RN HO4  H  N N 17  
9RN H3   H  N N 18  
9RN HO2  H  N N 19  
9RN H1   H  N N 20  
9RN HO1  H  N N 21  
ALA N    N  N N 22  
ALA CA   C  N S 23  
ALA C    C  N N 24  
ALA O    O  N N 25  
ALA CB   C  N N 26  
ALA OXT  O  N N 27  
ALA H    H  N N 28  
ALA H2   H  N N 29  
ALA HA   H  N N 30  
ALA HB1  H  N N 31  
ALA HB2  H  N N 32  
ALA HB3  H  N N 33  
ALA HXT  H  N N 34  
ARG N    N  N N 35  
ARG CA   C  N S 36  
ARG C    C  N N 37  
ARG O    O  N N 38  
ARG CB   C  N N 39  
ARG CG   C  N N 40  
ARG CD   C  N N 41  
ARG NE   N  N N 42  
ARG CZ   C  N N 43  
ARG NH1  N  N N 44  
ARG NH2  N  N N 45  
ARG OXT  O  N N 46  
ARG H    H  N N 47  
ARG H2   H  N N 48  
ARG HA   H  N N 49  
ARG HB2  H  N N 50  
ARG HB3  H  N N 51  
ARG HG2  H  N N 52  
ARG HG3  H  N N 53  
ARG HD2  H  N N 54  
ARG HD3  H  N N 55  
ARG HE   H  N N 56  
ARG HH11 H  N N 57  
ARG HH12 H  N N 58  
ARG HH21 H  N N 59  
ARG HH22 H  N N 60  
ARG HXT  H  N N 61  
ASN N    N  N N 62  
ASN CA   C  N S 63  
ASN C    C  N N 64  
ASN O    O  N N 65  
ASN CB   C  N N 66  
ASN CG   C  N N 67  
ASN OD1  O  N N 68  
ASN ND2  N  N N 69  
ASN OXT  O  N N 70  
ASN H    H  N N 71  
ASN H2   H  N N 72  
ASN HA   H  N N 73  
ASN HB2  H  N N 74  
ASN HB3  H  N N 75  
ASN HD21 H  N N 76  
ASN HD22 H  N N 77  
ASN HXT  H  N N 78  
ASP N    N  N N 79  
ASP CA   C  N S 80  
ASP C    C  N N 81  
ASP O    O  N N 82  
ASP CB   C  N N 83  
ASP CG   C  N N 84  
ASP OD1  O  N N 85  
ASP OD2  O  N N 86  
ASP OXT  O  N N 87  
ASP H    H  N N 88  
ASP H2   H  N N 89  
ASP HA   H  N N 90  
ASP HB2  H  N N 91  
ASP HB3  H  N N 92  
ASP HD2  H  N N 93  
ASP HXT  H  N N 94  
BR  BR   BR N N 95  
CA  CA   CA N N 96  
CL  CL   CL N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
G4S C1   C  N R 112 
G4S C2   C  N R 113 
G4S C3   C  N R 114 
G4S C4   C  N R 115 
G4S C5   C  N R 116 
G4S C6   C  N N 117 
G4S O1   O  N N 118 
G4S O2   O  N N 119 
G4S O3   O  N N 120 
G4S O4   O  N N 121 
G4S O5   O  N N 122 
G4S O6   O  N N 123 
G4S S    S  N N 124 
G4S O7   O  N N 125 
G4S O8   O  N N 126 
G4S O9   O  N N 127 
G4S H1   H  N N 128 
G4S H2   H  N N 129 
G4S H3   H  N N 130 
G4S H4   H  N N 131 
G4S H5   H  N N 132 
G4S H61  H  N N 133 
G4S H62  H  N N 134 
G4S HO1  H  N N 135 
G4S HO2  H  N N 136 
G4S HO3  H  N N 137 
G4S HO6  H  N N 138 
G4S HO4  H  N N 139 
GAL C1   C  N R 140 
GAL C2   C  N R 141 
GAL C3   C  N S 142 
GAL C4   C  N R 143 
GAL C5   C  N R 144 
GAL C6   C  N N 145 
GAL O1   O  N N 146 
GAL O2   O  N N 147 
GAL O3   O  N N 148 
GAL O4   O  N N 149 
GAL O5   O  N N 150 
GAL O6   O  N N 151 
GAL H1   H  N N 152 
GAL H2   H  N N 153 
GAL H3   H  N N 154 
GAL H4   H  N N 155 
GAL H5   H  N N 156 
GAL H61  H  N N 157 
GAL H62  H  N N 158 
GAL HO1  H  N N 159 
GAL HO2  H  N N 160 
GAL HO3  H  N N 161 
GAL HO4  H  N N 162 
GAL HO6  H  N N 163 
GLN N    N  N N 164 
GLN CA   C  N S 165 
GLN C    C  N N 166 
GLN O    O  N N 167 
GLN CB   C  N N 168 
GLN CG   C  N N 169 
GLN CD   C  N N 170 
GLN OE1  O  N N 171 
GLN NE2  N  N N 172 
GLN OXT  O  N N 173 
GLN H    H  N N 174 
GLN H2   H  N N 175 
GLN HA   H  N N 176 
GLN HB2  H  N N 177 
GLN HB3  H  N N 178 
GLN HG2  H  N N 179 
GLN HG3  H  N N 180 
GLN HE21 H  N N 181 
GLN HE22 H  N N 182 
GLN HXT  H  N N 183 
GLU N    N  N N 184 
GLU CA   C  N S 185 
GLU C    C  N N 186 
GLU O    O  N N 187 
GLU CB   C  N N 188 
GLU CG   C  N N 189 
GLU CD   C  N N 190 
GLU OE1  O  N N 191 
GLU OE2  O  N N 192 
GLU OXT  O  N N 193 
GLU H    H  N N 194 
GLU H2   H  N N 195 
GLU HA   H  N N 196 
GLU HB2  H  N N 197 
GLU HB3  H  N N 198 
GLU HG2  H  N N 199 
GLU HG3  H  N N 200 
GLU HE2  H  N N 201 
GLU HXT  H  N N 202 
GLY N    N  N N 203 
GLY CA   C  N N 204 
GLY C    C  N N 205 
GLY O    O  N N 206 
GLY OXT  O  N N 207 
GLY H    H  N N 208 
GLY H2   H  N N 209 
GLY HA2  H  N N 210 
GLY HA3  H  N N 211 
GLY HXT  H  N N 212 
GOL C1   C  N N 213 
GOL O1   O  N N 214 
GOL C2   C  N N 215 
GOL O2   O  N N 216 
GOL C3   C  N N 217 
GOL O3   O  N N 218 
GOL H11  H  N N 219 
GOL H12  H  N N 220 
GOL HO1  H  N N 221 
GOL H2   H  N N 222 
GOL HO2  H  N N 223 
GOL H31  H  N N 224 
GOL H32  H  N N 225 
GOL HO3  H  N N 226 
HIS N    N  N N 227 
HIS CA   C  N S 228 
HIS C    C  N N 229 
HIS O    O  N N 230 
HIS CB   C  N N 231 
HIS CG   C  Y N 232 
HIS ND1  N  Y N 233 
HIS CD2  C  Y N 234 
HIS CE1  C  Y N 235 
HIS NE2  N  Y N 236 
HIS OXT  O  N N 237 
HIS H    H  N N 238 
HIS H2   H  N N 239 
HIS HA   H  N N 240 
HIS HB2  H  N N 241 
HIS HB3  H  N N 242 
HIS HD1  H  N N 243 
HIS HD2  H  N N 244 
HIS HE1  H  N N 245 
HIS HE2  H  N N 246 
HIS HXT  H  N N 247 
HOH O    O  N N 248 
HOH H1   H  N N 249 
HOH H2   H  N N 250 
ILE N    N  N N 251 
ILE CA   C  N S 252 
ILE C    C  N N 253 
ILE O    O  N N 254 
ILE CB   C  N S 255 
ILE CG1  C  N N 256 
ILE CG2  C  N N 257 
ILE CD1  C  N N 258 
ILE OXT  O  N N 259 
ILE H    H  N N 260 
ILE H2   H  N N 261 
ILE HA   H  N N 262 
ILE HB   H  N N 263 
ILE HG12 H  N N 264 
ILE HG13 H  N N 265 
ILE HG21 H  N N 266 
ILE HG22 H  N N 267 
ILE HG23 H  N N 268 
ILE HD11 H  N N 269 
ILE HD12 H  N N 270 
ILE HD13 H  N N 271 
ILE HXT  H  N N 272 
LEU N    N  N N 273 
LEU CA   C  N S 274 
LEU C    C  N N 275 
LEU O    O  N N 276 
LEU CB   C  N N 277 
LEU CG   C  N N 278 
LEU CD1  C  N N 279 
LEU CD2  C  N N 280 
LEU OXT  O  N N 281 
LEU H    H  N N 282 
LEU H2   H  N N 283 
LEU HA   H  N N 284 
LEU HB2  H  N N 285 
LEU HB3  H  N N 286 
LEU HG   H  N N 287 
LEU HD11 H  N N 288 
LEU HD12 H  N N 289 
LEU HD13 H  N N 290 
LEU HD21 H  N N 291 
LEU HD22 H  N N 292 
LEU HD23 H  N N 293 
LEU HXT  H  N N 294 
LYS N    N  N N 295 
LYS CA   C  N S 296 
LYS C    C  N N 297 
LYS O    O  N N 298 
LYS CB   C  N N 299 
LYS CG   C  N N 300 
LYS CD   C  N N 301 
LYS CE   C  N N 302 
LYS NZ   N  N N 303 
LYS OXT  O  N N 304 
LYS H    H  N N 305 
LYS H2   H  N N 306 
LYS HA   H  N N 307 
LYS HB2  H  N N 308 
LYS HB3  H  N N 309 
LYS HG2  H  N N 310 
LYS HG3  H  N N 311 
LYS HD2  H  N N 312 
LYS HD3  H  N N 313 
LYS HE2  H  N N 314 
LYS HE3  H  N N 315 
LYS HZ1  H  N N 316 
LYS HZ2  H  N N 317 
LYS HZ3  H  N N 318 
LYS HXT  H  N N 319 
MET N    N  N N 320 
MET CA   C  N S 321 
MET C    C  N N 322 
MET O    O  N N 323 
MET CB   C  N N 324 
MET CG   C  N N 325 
MET SD   S  N N 326 
MET CE   C  N N 327 
MET OXT  O  N N 328 
MET H    H  N N 329 
MET H2   H  N N 330 
MET HA   H  N N 331 
MET HB2  H  N N 332 
MET HB3  H  N N 333 
MET HG2  H  N N 334 
MET HG3  H  N N 335 
MET HE1  H  N N 336 
MET HE2  H  N N 337 
MET HE3  H  N N 338 
MET HXT  H  N N 339 
OSE N    N  N N 340 
OSE CA   C  N S 341 
OSE CB   C  N N 342 
OSE OG   O  N N 343 
OSE C    C  N N 344 
OSE O    O  N N 345 
OSE S    S  N N 346 
OSE O1S  O  N N 347 
OSE O2S  O  N N 348 
OSE O3S  O  N N 349 
OSE OXT  O  N N 350 
OSE H    H  N N 351 
OSE H2   H  N N 352 
OSE HA   H  N N 353 
OSE HB2  H  N N 354 
OSE HB3  H  N N 355 
OSE H3S  H  N N 356 
OSE HXT  H  N N 357 
PHE N    N  N N 358 
PHE CA   C  N S 359 
PHE C    C  N N 360 
PHE O    O  N N 361 
PHE CB   C  N N 362 
PHE CG   C  Y N 363 
PHE CD1  C  Y N 364 
PHE CD2  C  Y N 365 
PHE CE1  C  Y N 366 
PHE CE2  C  Y N 367 
PHE CZ   C  Y N 368 
PHE OXT  O  N N 369 
PHE H    H  N N 370 
PHE H2   H  N N 371 
PHE HA   H  N N 372 
PHE HB2  H  N N 373 
PHE HB3  H  N N 374 
PHE HD1  H  N N 375 
PHE HD2  H  N N 376 
PHE HE1  H  N N 377 
PHE HE2  H  N N 378 
PHE HZ   H  N N 379 
PHE HXT  H  N N 380 
PRO N    N  N N 381 
PRO CA   C  N S 382 
PRO C    C  N N 383 
PRO O    O  N N 384 
PRO CB   C  N N 385 
PRO CG   C  N N 386 
PRO CD   C  N N 387 
PRO OXT  O  N N 388 
PRO H    H  N N 389 
PRO HA   H  N N 390 
PRO HB2  H  N N 391 
PRO HB3  H  N N 392 
PRO HG2  H  N N 393 
PRO HG3  H  N N 394 
PRO HD2  H  N N 395 
PRO HD3  H  N N 396 
PRO HXT  H  N N 397 
SER N    N  N N 398 
SER CA   C  N S 399 
SER C    C  N N 400 
SER O    O  N N 401 
SER CB   C  N N 402 
SER OG   O  N N 403 
SER OXT  O  N N 404 
SER H    H  N N 405 
SER H2   H  N N 406 
SER HA   H  N N 407 
SER HB2  H  N N 408 
SER HB3  H  N N 409 
SER HG   H  N N 410 
SER HXT  H  N N 411 
THR N    N  N N 412 
THR CA   C  N S 413 
THR C    C  N N 414 
THR O    O  N N 415 
THR CB   C  N R 416 
THR OG1  O  N N 417 
THR CG2  C  N N 418 
THR OXT  O  N N 419 
THR H    H  N N 420 
THR H2   H  N N 421 
THR HA   H  N N 422 
THR HB   H  N N 423 
THR HG1  H  N N 424 
THR HG21 H  N N 425 
THR HG22 H  N N 426 
THR HG23 H  N N 427 
THR HXT  H  N N 428 
TRP N    N  N N 429 
TRP CA   C  N S 430 
TRP C    C  N N 431 
TRP O    O  N N 432 
TRP CB   C  N N 433 
TRP CG   C  Y N 434 
TRP CD1  C  Y N 435 
TRP CD2  C  Y N 436 
TRP NE1  N  Y N 437 
TRP CE2  C  Y N 438 
TRP CE3  C  Y N 439 
TRP CZ2  C  Y N 440 
TRP CZ3  C  Y N 441 
TRP CH2  C  Y N 442 
TRP OXT  O  N N 443 
TRP H    H  N N 444 
TRP H2   H  N N 445 
TRP HA   H  N N 446 
TRP HB2  H  N N 447 
TRP HB3  H  N N 448 
TRP HD1  H  N N 449 
TRP HE1  H  N N 450 
TRP HE3  H  N N 451 
TRP HZ2  H  N N 452 
TRP HZ3  H  N N 453 
TRP HH2  H  N N 454 
TRP HXT  H  N N 455 
TYR N    N  N N 456 
TYR CA   C  N S 457 
TYR C    C  N N 458 
TYR O    O  N N 459 
TYR CB   C  N N 460 
TYR CG   C  Y N 461 
TYR CD1  C  Y N 462 
TYR CD2  C  Y N 463 
TYR CE1  C  Y N 464 
TYR CE2  C  Y N 465 
TYR CZ   C  Y N 466 
TYR OH   O  N N 467 
TYR OXT  O  N N 468 
TYR H    H  N N 469 
TYR H2   H  N N 470 
TYR HA   H  N N 471 
TYR HB2  H  N N 472 
TYR HB3  H  N N 473 
TYR HD1  H  N N 474 
TYR HD2  H  N N 475 
TYR HE1  H  N N 476 
TYR HE2  H  N N 477 
TYR HH   H  N N 478 
TYR HXT  H  N N 479 
VAL N    N  N N 480 
VAL CA   C  N S 481 
VAL C    C  N N 482 
VAL O    O  N N 483 
VAL CB   C  N N 484 
VAL CG1  C  N N 485 
VAL CG2  C  N N 486 
VAL OXT  O  N N 487 
VAL H    H  N N 488 
VAL H2   H  N N 489 
VAL HA   H  N N 490 
VAL HB   H  N N 491 
VAL HG11 H  N N 492 
VAL HG12 H  N N 493 
VAL HG13 H  N N 494 
VAL HG21 H  N N 495 
VAL HG22 H  N N 496 
VAL HG23 H  N N 497 
VAL HXT  H  N N 498 
# 
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 
9RN O4  C4   sing N N 1   
9RN C6  C5   sing N N 2   
9RN C6  O3   sing N N 3   
9RN C5  C4   sing N N 4   
9RN C5  O5   sing N N 5   
9RN C4  C3   sing N N 6   
9RN O3  C3   sing N N 7   
9RN O5  C1   sing N N 8   
9RN C3  C2   sing N N 9   
9RN C1  C2   sing N N 10  
9RN C1  O1   sing N N 11  
9RN C2  O2   sing N N 12  
9RN C2  H2   sing N N 13  
9RN C4  H4   sing N N 14  
9RN C5  H5   sing N N 15  
9RN C6  H61  sing N N 16  
9RN C6  H62  sing N N 17  
9RN O4  HO4  sing N N 18  
9RN C3  H3   sing N N 19  
9RN O2  HO2  sing N N 20  
9RN C1  H1   sing N N 21  
9RN O1  HO1  sing N N 22  
ALA N   CA   sing N N 23  
ALA N   H    sing N N 24  
ALA N   H2   sing N N 25  
ALA CA  C    sing N N 26  
ALA CA  CB   sing N N 27  
ALA CA  HA   sing N N 28  
ALA C   O    doub N N 29  
ALA C   OXT  sing N N 30  
ALA CB  HB1  sing N N 31  
ALA CB  HB2  sing N N 32  
ALA CB  HB3  sing N N 33  
ALA OXT HXT  sing N N 34  
ARG N   CA   sing N N 35  
ARG N   H    sing N N 36  
ARG N   H2   sing N N 37  
ARG CA  C    sing N N 38  
ARG CA  CB   sing N N 39  
ARG CA  HA   sing N N 40  
ARG C   O    doub N N 41  
ARG C   OXT  sing N N 42  
ARG CB  CG   sing N N 43  
ARG CB  HB2  sing N N 44  
ARG CB  HB3  sing N N 45  
ARG CG  CD   sing N N 46  
ARG CG  HG2  sing N N 47  
ARG CG  HG3  sing N N 48  
ARG CD  NE   sing N N 49  
ARG CD  HD2  sing N N 50  
ARG CD  HD3  sing N N 51  
ARG NE  CZ   sing N N 52  
ARG NE  HE   sing N N 53  
ARG CZ  NH1  sing N N 54  
ARG CZ  NH2  doub N N 55  
ARG NH1 HH11 sing N N 56  
ARG NH1 HH12 sing N N 57  
ARG NH2 HH21 sing N N 58  
ARG NH2 HH22 sing N N 59  
ARG OXT HXT  sing N N 60  
ASN N   CA   sing N N 61  
ASN N   H    sing N N 62  
ASN N   H2   sing N N 63  
ASN CA  C    sing N N 64  
ASN CA  CB   sing N N 65  
ASN CA  HA   sing N N 66  
ASN C   O    doub N N 67  
ASN C   OXT  sing N N 68  
ASN CB  CG   sing N N 69  
ASN CB  HB2  sing N N 70  
ASN CB  HB3  sing N N 71  
ASN CG  OD1  doub N N 72  
ASN CG  ND2  sing N N 73  
ASN ND2 HD21 sing N N 74  
ASN ND2 HD22 sing N N 75  
ASN OXT HXT  sing N N 76  
ASP N   CA   sing N N 77  
ASP N   H    sing N N 78  
ASP N   H2   sing N N 79  
ASP CA  C    sing N N 80  
ASP CA  CB   sing N N 81  
ASP CA  HA   sing N N 82  
ASP C   O    doub N N 83  
ASP C   OXT  sing N N 84  
ASP CB  CG   sing N N 85  
ASP CB  HB2  sing N N 86  
ASP CB  HB3  sing N N 87  
ASP CG  OD1  doub N N 88  
ASP CG  OD2  sing N N 89  
ASP OD2 HD2  sing N N 90  
ASP OXT HXT  sing N N 91  
CYS N   CA   sing N N 92  
CYS N   H    sing N N 93  
CYS N   H2   sing N N 94  
CYS CA  C    sing N N 95  
CYS CA  CB   sing N N 96  
CYS CA  HA   sing N N 97  
CYS C   O    doub N N 98  
CYS C   OXT  sing N N 99  
CYS CB  SG   sing N N 100 
CYS CB  HB2  sing N N 101 
CYS CB  HB3  sing N N 102 
CYS SG  HG   sing N N 103 
CYS OXT HXT  sing N N 104 
G4S C1  C2   sing N N 105 
G4S C1  O1   sing N N 106 
G4S C1  O5   sing N N 107 
G4S C1  H1   sing N N 108 
G4S C2  C3   sing N N 109 
G4S C2  O2   sing N N 110 
G4S C2  H2   sing N N 111 
G4S C3  C4   sing N N 112 
G4S C3  O3   sing N N 113 
G4S C3  H3   sing N N 114 
G4S C4  C5   sing N N 115 
G4S C4  O4   sing N N 116 
G4S C4  H4   sing N N 117 
G4S C5  C6   sing N N 118 
G4S C5  O5   sing N N 119 
G4S C5  H5   sing N N 120 
G4S C6  O6   sing N N 121 
G4S C6  H61  sing N N 122 
G4S C6  H62  sing N N 123 
G4S O1  HO1  sing N N 124 
G4S O2  HO2  sing N N 125 
G4S O3  HO3  sing N N 126 
G4S O4  S    sing N N 127 
G4S O6  HO6  sing N N 128 
G4S S   O7   doub N N 129 
G4S S   O8   doub N N 130 
G4S S   O9   sing N N 131 
G4S HO4 O9   sing N N 132 
GAL C1  C2   sing N N 133 
GAL C1  O1   sing N N 134 
GAL C1  O5   sing N N 135 
GAL C1  H1   sing N N 136 
GAL C2  C3   sing N N 137 
GAL C2  O2   sing N N 138 
GAL C2  H2   sing N N 139 
GAL C3  C4   sing N N 140 
GAL C3  O3   sing N N 141 
GAL C3  H3   sing N N 142 
GAL C4  C5   sing N N 143 
GAL C4  O4   sing N N 144 
GAL C4  H4   sing N N 145 
GAL C5  C6   sing N N 146 
GAL C5  O5   sing N N 147 
GAL C5  H5   sing N N 148 
GAL C6  O6   sing N N 149 
GAL C6  H61  sing N N 150 
GAL C6  H62  sing N N 151 
GAL O1  HO1  sing N N 152 
GAL O2  HO2  sing N N 153 
GAL O3  HO3  sing N N 154 
GAL O4  HO4  sing N N 155 
GAL O6  HO6  sing N N 156 
GLN N   CA   sing N N 157 
GLN N   H    sing N N 158 
GLN N   H2   sing N N 159 
GLN CA  C    sing N N 160 
GLN CA  CB   sing N N 161 
GLN CA  HA   sing N N 162 
GLN C   O    doub N N 163 
GLN C   OXT  sing N N 164 
GLN CB  CG   sing N N 165 
GLN CB  HB2  sing N N 166 
GLN CB  HB3  sing N N 167 
GLN CG  CD   sing N N 168 
GLN CG  HG2  sing N N 169 
GLN CG  HG3  sing N N 170 
GLN CD  OE1  doub N N 171 
GLN CD  NE2  sing N N 172 
GLN NE2 HE21 sing N N 173 
GLN NE2 HE22 sing N N 174 
GLN OXT HXT  sing N N 175 
GLU N   CA   sing N N 176 
GLU N   H    sing N N 177 
GLU N   H2   sing N N 178 
GLU CA  C    sing N N 179 
GLU CA  CB   sing N N 180 
GLU CA  HA   sing N N 181 
GLU C   O    doub N N 182 
GLU C   OXT  sing N N 183 
GLU CB  CG   sing N N 184 
GLU CB  HB2  sing N N 185 
GLU CB  HB3  sing N N 186 
GLU CG  CD   sing N N 187 
GLU CG  HG2  sing N N 188 
GLU CG  HG3  sing N N 189 
GLU CD  OE1  doub N N 190 
GLU CD  OE2  sing N N 191 
GLU OE2 HE2  sing N N 192 
GLU OXT HXT  sing N N 193 
GLY N   CA   sing N N 194 
GLY N   H    sing N N 195 
GLY N   H2   sing N N 196 
GLY CA  C    sing N N 197 
GLY CA  HA2  sing N N 198 
GLY CA  HA3  sing N N 199 
GLY C   O    doub N N 200 
GLY C   OXT  sing N N 201 
GLY OXT HXT  sing N N 202 
GOL C1  O1   sing N N 203 
GOL C1  C2   sing N N 204 
GOL C1  H11  sing N N 205 
GOL C1  H12  sing N N 206 
GOL O1  HO1  sing N N 207 
GOL C2  O2   sing N N 208 
GOL C2  C3   sing N N 209 
GOL C2  H2   sing N N 210 
GOL O2  HO2  sing N N 211 
GOL C3  O3   sing N N 212 
GOL C3  H31  sing N N 213 
GOL C3  H32  sing N N 214 
GOL O3  HO3  sing N N 215 
HIS N   CA   sing N N 216 
HIS N   H    sing N N 217 
HIS N   H2   sing N N 218 
HIS CA  C    sing N N 219 
HIS CA  CB   sing N N 220 
HIS CA  HA   sing N N 221 
HIS C   O    doub N N 222 
HIS C   OXT  sing N N 223 
HIS CB  CG   sing N N 224 
HIS CB  HB2  sing N N 225 
HIS CB  HB3  sing N N 226 
HIS CG  ND1  sing Y N 227 
HIS CG  CD2  doub Y N 228 
HIS ND1 CE1  doub Y N 229 
HIS ND1 HD1  sing N N 230 
HIS CD2 NE2  sing Y N 231 
HIS CD2 HD2  sing N N 232 
HIS CE1 NE2  sing Y N 233 
HIS CE1 HE1  sing N N 234 
HIS NE2 HE2  sing N N 235 
HIS OXT HXT  sing N N 236 
HOH O   H1   sing N N 237 
HOH O   H2   sing N N 238 
ILE N   CA   sing N N 239 
ILE N   H    sing N N 240 
ILE N   H2   sing N N 241 
ILE CA  C    sing N N 242 
ILE CA  CB   sing N N 243 
ILE CA  HA   sing N N 244 
ILE C   O    doub N N 245 
ILE C   OXT  sing N N 246 
ILE CB  CG1  sing N N 247 
ILE CB  CG2  sing N N 248 
ILE CB  HB   sing N N 249 
ILE CG1 CD1  sing N N 250 
ILE CG1 HG12 sing N N 251 
ILE CG1 HG13 sing N N 252 
ILE CG2 HG21 sing N N 253 
ILE CG2 HG22 sing N N 254 
ILE CG2 HG23 sing N N 255 
ILE CD1 HD11 sing N N 256 
ILE CD1 HD12 sing N N 257 
ILE CD1 HD13 sing N N 258 
ILE OXT HXT  sing N N 259 
LEU N   CA   sing N N 260 
LEU N   H    sing N N 261 
LEU N   H2   sing N N 262 
LEU CA  C    sing N N 263 
LEU CA  CB   sing N N 264 
LEU CA  HA   sing N N 265 
LEU C   O    doub N N 266 
LEU C   OXT  sing N N 267 
LEU CB  CG   sing N N 268 
LEU CB  HB2  sing N N 269 
LEU CB  HB3  sing N N 270 
LEU CG  CD1  sing N N 271 
LEU CG  CD2  sing N N 272 
LEU CG  HG   sing N N 273 
LEU CD1 HD11 sing N N 274 
LEU CD1 HD12 sing N N 275 
LEU CD1 HD13 sing N N 276 
LEU CD2 HD21 sing N N 277 
LEU CD2 HD22 sing N N 278 
LEU CD2 HD23 sing N N 279 
LEU OXT HXT  sing N N 280 
LYS N   CA   sing N N 281 
LYS N   H    sing N N 282 
LYS N   H2   sing N N 283 
LYS CA  C    sing N N 284 
LYS CA  CB   sing N N 285 
LYS CA  HA   sing N N 286 
LYS C   O    doub N N 287 
LYS C   OXT  sing N N 288 
LYS CB  CG   sing N N 289 
LYS CB  HB2  sing N N 290 
LYS CB  HB3  sing N N 291 
LYS CG  CD   sing N N 292 
LYS CG  HG2  sing N N 293 
LYS CG  HG3  sing N N 294 
LYS CD  CE   sing N N 295 
LYS CD  HD2  sing N N 296 
LYS CD  HD3  sing N N 297 
LYS CE  NZ   sing N N 298 
LYS CE  HE2  sing N N 299 
LYS CE  HE3  sing N N 300 
LYS NZ  HZ1  sing N N 301 
LYS NZ  HZ2  sing N N 302 
LYS NZ  HZ3  sing N N 303 
LYS OXT HXT  sing N N 304 
MET N   CA   sing N N 305 
MET N   H    sing N N 306 
MET N   H2   sing N N 307 
MET CA  C    sing N N 308 
MET CA  CB   sing N N 309 
MET CA  HA   sing N N 310 
MET C   O    doub N N 311 
MET C   OXT  sing N N 312 
MET CB  CG   sing N N 313 
MET CB  HB2  sing N N 314 
MET CB  HB3  sing N N 315 
MET CG  SD   sing N N 316 
MET CG  HG2  sing N N 317 
MET CG  HG3  sing N N 318 
MET SD  CE   sing N N 319 
MET CE  HE1  sing N N 320 
MET CE  HE2  sing N N 321 
MET CE  HE3  sing N N 322 
MET OXT HXT  sing N N 323 
OSE N   CA   sing N N 324 
OSE N   H    sing N N 325 
OSE N   H2   sing N N 326 
OSE CA  CB   sing N N 327 
OSE CA  C    sing N N 328 
OSE CA  HA   sing N N 329 
OSE CB  OG   sing N N 330 
OSE CB  HB2  sing N N 331 
OSE CB  HB3  sing N N 332 
OSE OG  S    sing N N 333 
OSE C   O    doub N N 334 
OSE C   OXT  sing N N 335 
OSE S   O1S  doub N N 336 
OSE S   O2S  doub N N 337 
OSE S   O3S  sing N N 338 
OSE O3S H3S  sing N N 339 
OSE OXT HXT  sing N N 340 
PHE N   CA   sing N N 341 
PHE N   H    sing N N 342 
PHE N   H2   sing N N 343 
PHE CA  C    sing N N 344 
PHE CA  CB   sing N N 345 
PHE CA  HA   sing N N 346 
PHE C   O    doub N N 347 
PHE C   OXT  sing N N 348 
PHE CB  CG   sing N N 349 
PHE CB  HB2  sing N N 350 
PHE CB  HB3  sing N N 351 
PHE CG  CD1  doub Y N 352 
PHE CG  CD2  sing Y N 353 
PHE CD1 CE1  sing Y N 354 
PHE CD1 HD1  sing N N 355 
PHE CD2 CE2  doub Y N 356 
PHE CD2 HD2  sing N N 357 
PHE CE1 CZ   doub Y N 358 
PHE CE1 HE1  sing N N 359 
PHE CE2 CZ   sing Y N 360 
PHE CE2 HE2  sing N N 361 
PHE CZ  HZ   sing N N 362 
PHE OXT HXT  sing N N 363 
PRO N   CA   sing N N 364 
PRO N   CD   sing N N 365 
PRO N   H    sing N N 366 
PRO CA  C    sing N N 367 
PRO CA  CB   sing N N 368 
PRO CA  HA   sing N N 369 
PRO C   O    doub N N 370 
PRO C   OXT  sing N N 371 
PRO CB  CG   sing N N 372 
PRO CB  HB2  sing N N 373 
PRO CB  HB3  sing N N 374 
PRO CG  CD   sing N N 375 
PRO CG  HG2  sing N N 376 
PRO CG  HG3  sing N N 377 
PRO CD  HD2  sing N N 378 
PRO CD  HD3  sing N N 379 
PRO OXT HXT  sing N N 380 
SER N   CA   sing N N 381 
SER N   H    sing N N 382 
SER N   H2   sing N N 383 
SER CA  C    sing N N 384 
SER CA  CB   sing N N 385 
SER CA  HA   sing N N 386 
SER C   O    doub N N 387 
SER C   OXT  sing N N 388 
SER CB  OG   sing N N 389 
SER CB  HB2  sing N N 390 
SER CB  HB3  sing N N 391 
SER OG  HG   sing N N 392 
SER OXT HXT  sing N N 393 
THR N   CA   sing N N 394 
THR N   H    sing N N 395 
THR N   H2   sing N N 396 
THR CA  C    sing N N 397 
THR CA  CB   sing N N 398 
THR CA  HA   sing N N 399 
THR C   O    doub N N 400 
THR C   OXT  sing N N 401 
THR CB  OG1  sing N N 402 
THR CB  CG2  sing N N 403 
THR CB  HB   sing N N 404 
THR OG1 HG1  sing N N 405 
THR CG2 HG21 sing N N 406 
THR CG2 HG22 sing N N 407 
THR CG2 HG23 sing N N 408 
THR OXT HXT  sing N N 409 
TRP N   CA   sing N N 410 
TRP N   H    sing N N 411 
TRP N   H2   sing N N 412 
TRP CA  C    sing N N 413 
TRP CA  CB   sing N N 414 
TRP CA  HA   sing N N 415 
TRP C   O    doub N N 416 
TRP C   OXT  sing N N 417 
TRP CB  CG   sing N N 418 
TRP CB  HB2  sing N N 419 
TRP CB  HB3  sing N N 420 
TRP CG  CD1  doub Y N 421 
TRP CG  CD2  sing Y N 422 
TRP CD1 NE1  sing Y N 423 
TRP CD1 HD1  sing N N 424 
TRP CD2 CE2  doub Y N 425 
TRP CD2 CE3  sing Y N 426 
TRP NE1 CE2  sing Y N 427 
TRP NE1 HE1  sing N N 428 
TRP CE2 CZ2  sing Y N 429 
TRP CE3 CZ3  doub Y N 430 
TRP CE3 HE3  sing N N 431 
TRP CZ2 CH2  doub Y N 432 
TRP CZ2 HZ2  sing N N 433 
TRP CZ3 CH2  sing Y N 434 
TRP CZ3 HZ3  sing N N 435 
TRP CH2 HH2  sing N N 436 
TRP OXT HXT  sing N N 437 
TYR N   CA   sing N N 438 
TYR N   H    sing N N 439 
TYR N   H2   sing N N 440 
TYR CA  C    sing N N 441 
TYR CA  CB   sing N N 442 
TYR CA  HA   sing N N 443 
TYR C   O    doub N N 444 
TYR C   OXT  sing N N 445 
TYR CB  CG   sing N N 446 
TYR CB  HB2  sing N N 447 
TYR CB  HB3  sing N N 448 
TYR CG  CD1  doub Y N 449 
TYR CG  CD2  sing Y N 450 
TYR CD1 CE1  sing Y N 451 
TYR CD1 HD1  sing N N 452 
TYR CD2 CE2  doub Y N 453 
TYR CD2 HD2  sing N N 454 
TYR CE1 CZ   doub Y N 455 
TYR CE1 HE1  sing N N 456 
TYR CE2 CZ   sing Y N 457 
TYR CE2 HE2  sing N N 458 
TYR CZ  OH   sing N N 459 
TYR OH  HH   sing N N 460 
TYR OXT HXT  sing N N 461 
VAL N   CA   sing N N 462 
VAL N   H    sing N N 463 
VAL N   H2   sing N N 464 
VAL CA  C    sing N N 465 
VAL CA  CB   sing N N 466 
VAL CA  HA   sing N N 467 
VAL C   O    doub N N 468 
VAL C   OXT  sing N N 469 
VAL CB  CG1  sing N N 470 
VAL CB  CG2  sing N N 471 
VAL CB  HB   sing N N 472 
VAL CG1 HG11 sing N N 473 
VAL CG1 HG12 sing N N 474 
VAL CG1 HG13 sing N N 475 
VAL CG2 HG21 sing N N 476 
VAL CG2 HG22 sing N N 477 
VAL CG2 HG23 sing N N 478 
VAL OXT HXT  sing N N 479 
# 
_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 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 G4S 1 n 
2 9RN 2 n 
2 GAL 3 n 
2 9RN 4 n 
# 
_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          ? 
# 
_atom_sites.entry_id                    9HH4 
_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]   0.013472 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002325 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005061 
_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]   0.013527 
_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 
BR 
C  
CA 
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . GLU A  1 14  ? 24.152  15.138  18.801  1.00 70.61  ?  45   GLU A N   1 
ATOM   2     C  CA  . GLU A  1 14  ? 25.068  15.164  17.667  1.00 57.96  ?  45   GLU A CA  1 
ATOM   3     C  C   . GLU A  1 14  ? 24.367  15.591  16.385  1.00 62.58  ?  45   GLU A C   1 
ATOM   4     O  O   . GLU A  1 14  ? 23.161  15.874  16.364  1.00 63.48  ?  45   GLU A O   1 
ATOM   5     C  CB  . GLU A  1 14  ? 25.717  13.795  17.462  1.00 64.40  ?  45   GLU A CB  1 
ATOM   6     C  CG  . GLU A  1 14  ? 24.722  12.680  17.146  1.00 60.05  ?  45   GLU A CG  1 
ATOM   7     C  CD  . GLU A  1 14  ? 25.383  11.500  16.461  1.00 55.42  ?  45   GLU A CD  1 
ATOM   8     O  OE1 . GLU A  1 14  ? 25.989  11.717  15.391  1.00 61.04  ?  45   GLU A OE1 1 
ATOM   9     O  OE2 . GLU A  1 14  ? 25.303  10.366  16.986  1.00 52.54  ?  45   GLU A OE2 1 
ATOM   10    N  N   . THR A  1 15  ? 25.127  15.605  15.295  1.00 56.69  ?  46   THR A N   1 
ATOM   11    C  CA  . THR A  1 15  ? 24.628  16.201  14.066  1.00 54.52  ?  46   THR A CA  1 
ATOM   12    C  C   . THR A  1 15  ? 23.655  15.278  13.318  1.00 51.81  ?  46   THR A C   1 
ATOM   13    O  O   . THR A  1 15  ? 22.779  15.769  12.594  1.00 49.00  ?  46   THR A O   1 
ATOM   14    C  CB  . THR A  1 15  ? 25.830  16.610  13.201  1.00 53.02  ?  46   THR A CB  1 
ATOM   15    O  OG1 . THR A  1 15  ? 25.446  17.627  12.269  1.00 63.38  ?  46   THR A OG1 1 
ATOM   16    C  CG2 . THR A  1 15  ? 26.423  15.411  12.459  1.00 57.74  ?  46   THR A CG2 1 
ATOM   17    N  N   . ARG A  1 16  ? 23.759  13.945  13.510  1.00 43.87  ?  47   ARG A N   1 
ATOM   18    C  CA  . ARG A  1 16  ? 23.006  12.990  12.699  1.00 44.69  ?  47   ARG A CA  1 
ATOM   19    C  C   . ARG A  1 16  ? 21.539  12.964  13.127  1.00 37.00  ?  47   ARG A C   1 
ATOM   20    O  O   . ARG A  1 16  ? 21.245  12.934  14.325  1.00 36.68  ?  47   ARG A O   1 
ATOM   21    C  CB  . ARG A  1 16  ? 23.611  11.595  12.830  1.00 40.08  ?  47   ARG A CB  1 
ATOM   22    C  CG  . ARG A  1 16  ? 24.911  11.436  12.049  1.00 41.74  ?  47   ARG A CG  1 
ATOM   23    C  CD  . ARG A  1 16  ? 25.505  10.046  12.194  1.00 41.76  ?  47   ARG A CD  1 
ATOM   24    N  NE  . ARG A  1 16  ? 25.589  9.609   13.584  1.00 38.56  ?  47   ARG A NE  1 
ATOM   25    C  CZ  . ARG A  1 16  ? 25.844  8.364   13.950  1.00 34.82  ?  47   ARG A CZ  1 
ATOM   26    N  NH1 . ARG A  1 16  ? 26.079  7.417   13.060  1.00 32.66  ?  47   ARG A NH1 1 
ATOM   27    N  NH2 . ARG A  1 16  ? 25.852  8.057   15.241  1.00 42.18  ?  47   ARG A NH2 1 
ATOM   28    N  N   . PRO A  1 17  ? 20.606  12.942  12.179  1.00 37.38  ?  48   PRO A N   1 
ATOM   29    C  CA  . PRO A  1 17  ? 19.186  13.034  12.542  1.00 33.60  ?  48   PRO A CA  1 
ATOM   30    C  C   . PRO A  1 17  ? 18.627  11.711  13.044  1.00 30.16  ?  48   PRO A C   1 
ATOM   31    O  O   . PRO A  1 17  ? 19.058  10.629  12.642  1.00 29.83  ?  48   PRO A O   1 
ATOM   32    C  CB  . PRO A  1 17  ? 18.516  13.443  11.222  1.00 30.48  ?  48   PRO A CB  1 
ATOM   33    C  CG  . PRO A  1 17  ? 19.346  12.734  10.170  1.00 35.65  ?  48   PRO A CG  1 
ATOM   34    C  CD  . PRO A  1 17  ? 20.804  12.780  10.730  1.00 31.04  ?  48   PRO A CD  1 
ATOM   35    N  N   . ASN A  1 18  ? 17.642  11.807  13.936  1.00 29.54  ?  49   ASN A N   1 
ATOM   36    C  CA  . ASN A  1 18  ? 16.810  10.641  14.188  1.00 27.70  ?  49   ASN A CA  1 
ATOM   37    C  C   . ASN A  1 18  ? 15.976  10.364  12.933  1.00 26.60  ?  49   ASN A C   1 
ATOM   38    O  O   . ASN A  1 18  ? 15.763  11.252  12.114  1.00 27.52  ?  49   ASN A O   1 
ATOM   39    C  CB  . ASN A  1 18  ? 15.877  10.877  15.367  1.00 24.95  ?  49   ASN A CB  1 
ATOM   40    C  CG  . ASN A  1 18  ? 16.613  11.351  16.619  1.00 32.28  ?  49   ASN A CG  1 
ATOM   41    O  OD1 . ASN A  1 18  ? 17.513  10.672  17.115  1.00 34.72  ?  49   ASN A OD1 1 
ATOM   42    N  ND2 . ASN A  1 18  ? 16.225  12.513  17.134  1.00 29.17  ?  49   ASN A ND2 1 
ATOM   43    N  N   . ILE A  1 19  ? 15.507  9.126   12.795  1.00 26.30  ?  50   ILE A N   1 
ATOM   44    C  CA  . ILE A  1 19  ? 14.679  8.722   11.660  1.00 25.37  ?  50   ILE A CA  1 
ATOM   45    C  C   . ILE A  1 19  ? 13.496  7.911   12.166  1.00 26.77  ?  50   ILE A C   1 
ATOM   46    O  O   . ILE A  1 19  ? 13.672  6.873   12.817  1.00 23.72  ?  50   ILE A O   1 
ATOM   47    C  CB  . ILE A  1 19  ? 15.488  7.909   10.632  1.00 26.83  ?  50   ILE A CB  1 
ATOM   48    C  CG1 . ILE A  1 19  ? 16.679  8.740   10.131  1.00 28.54  ?  50   ILE A CG1 1 
ATOM   49    C  CG2 . ILE A  1 19  ? 14.575  7.477   9.446   1.00 26.30  ?  50   ILE A CG2 1 
ATOM   50    C  CD1 . ILE A  1 19  ? 17.780  7.915   9.469   1.00 32.32  ?  50   ILE A CD1 1 
ATOM   51    N  N   . LEU A  1 20  ? 12.290  8.346   11.797  1.00 29.33  ?  51   LEU A N   1 
ATOM   52    C  CA  . LEU A  1 20  ? 11.053  7.647   12.120  1.00 23.92  ?  51   LEU A CA  1 
ATOM   53    C  C   . LEU A  1 20  ? 10.322  7.382   10.812  1.00 27.81  ?  51   LEU A C   1 
ATOM   54    O  O   . LEU A  1 20  ? 10.002  8.331   10.096  1.00 22.56  ?  51   LEU A O   1 
ATOM   55    C  CB  . LEU A  1 20  ? 10.188  8.502   13.049  1.00 28.65  ?  51   LEU A CB  1 
ATOM   56    C  CG  . LEU A  1 20  ? 8.725   8.043   13.169  1.00 29.61  ?  51   LEU A CG  1 
ATOM   57    C  CD1 . LEU A  1 20  ? 8.678   6.674   13.838  1.00 24.72  ?  51   LEU A CD1 1 
ATOM   58    C  CD2 . LEU A  1 20  ? 7.918   9.068   13.946  1.00 28.63  ?  51   LEU A CD2 1 
ATOM   59    N  N   . VAL A  1 21  ? 10.132  6.103   10.470  1.00 25.20  ?  52   VAL A N   1 
ATOM   60    C  CA  . VAL A  1 21  ? 9.283   5.685   9.360   1.00 25.91  ?  52   VAL A CA  1 
ATOM   61    C  C   . VAL A  1 21  ? 7.923   5.349   9.939   1.00 25.67  ?  52   VAL A C   1 
ATOM   62    O  O   . VAL A  1 21  ? 7.815   4.502   10.831  1.00 27.63  ?  52   VAL A O   1 
ATOM   63    C  CB  . VAL A  1 21  ? 9.851   4.463   8.624   1.00 30.01  ?  52   VAL A CB  1 
ATOM   64    C  CG1 . VAL A  1 21  ? 8.912   4.070   7.424   1.00 22.68  ?  52   VAL A CG1 1 
ATOM   65    C  CG2 . VAL A  1 21  ? 11.290  4.720   8.181   1.00 28.70  ?  52   VAL A CG2 1 
ATOM   66    N  N   . VAL A  1 22  ? 6.879   5.992   9.440   1.00 27.44  ?  53   VAL A N   1 
ATOM   67    C  CA  . VAL A  1 22  ? 5.522   5.644   9.813   1.00 23.07  ?  53   VAL A CA  1 
ATOM   68    C  C   . VAL A  1 22  ? 4.905   5.032   8.570   1.00 25.39  ?  53   VAL A C   1 
ATOM   69    O  O   . VAL A  1 22  ? 4.661   5.735   7.582   1.00 24.90  ?  53   VAL A O   1 
ATOM   70    C  CB  . VAL A  1 22  ? 4.732   6.859   10.305  1.00 25.77  ?  53   VAL A CB  1 
ATOM   71    C  CG1 . VAL A  1 22  ? 3.270   6.450   10.635  1.00 24.54  ?  53   VAL A CG1 1 
ATOM   72    C  CG2 . VAL A  1 22  ? 5.441   7.472   11.484  1.00 24.27  ?  53   VAL A CG2 1 
ATOM   73    N  N   . LEU A  1 23  ? 4.714   3.717   8.597   1.00 24.07  ?  54   LEU A N   1 
ATOM   74    C  CA  . LEU A  1 23  ? 4.310   2.934   7.436   1.00 23.71  ?  54   LEU A CA  1 
ATOM   75    C  C   . LEU A  1 23  ? 2.931   2.346   7.717   1.00 24.30  ?  54   LEU A C   1 
ATOM   76    O  O   . LEU A  1 23  ? 2.781   1.499   8.606   1.00 26.15  ?  54   LEU A O   1 
ATOM   77    C  CB  . LEU A  1 23  ? 5.333   1.831   7.167   1.00 28.34  ?  54   LEU A CB  1 
ATOM   78    C  CG  . LEU A  1 23  ? 5.028   0.859   6.028   1.00 27.41  ?  54   LEU A CG  1 
ATOM   79    C  CD1 . LEU A  1 23  ? 5.174   1.566   4.667   1.00 20.26  ?  54   LEU A CD1 1 
ATOM   80    C  CD2 . LEU A  1 23  ? 5.925   -0.343  6.137   1.00 25.13  ?  54   LEU A CD2 1 
ATOM   81    N  N   . CYS A  1 24  ? 1.927   2.791   6.976   1.00 22.02  ?  55   CYS A N   1 
ATOM   82    C  CA  . CYS A  1 24  ? 0.621   2.167   7.090   1.00 18.83  ?  55   CYS A CA  1 
ATOM   83    C  C   . CYS A  1 24  ? 0.518   1.000   6.114   1.00 25.48  ?  55   CYS A C   1 
ATOM   84    O  O   . CYS A  1 24  ? 1.383   0.788   5.272   1.00 23.77  ?  55   CYS A O   1 
ATOM   85    C  CB  . CYS A  1 24  ? -0.496  3.179   6.814   1.00 23.78  ?  55   CYS A CB  1 
ATOM   86    S  SG  . CYS A  1 24  ? -0.730  4.350   8.171   1.00 30.38  ?  55   CYS A SG  1 
ATOM   87    N  N   . ASP A  1 25  ? -0.592  0.277   6.260   1.00 23.09  ?  56   ASP A N   1 
ATOM   88    C  CA  . ASP A  1 25  ? -0.760  -0.981  5.502   1.00 19.35  ?  56   ASP A CA  1 
ATOM   89    C  C   . ASP A  1 25  ? -2.072  -0.934  4.711   1.00 24.47  ?  56   ASP A C   1 
ATOM   90    O  O   . ASP A  1 25  ? -3.131  -0.918  5.357   1.00 22.58  ?  56   ASP A O   1 
ATOM   91    C  CB  . ASP A  1 25  ? -0.712  -2.129  6.488   1.00 22.63  ?  56   ASP A CB  1 
ATOM   92    C  CG  . ASP A  1 25  ? -0.685  -3.526  5.890   1.00 26.77  ?  56   ASP A CG  1 
ATOM   93    O  OD1 . ASP A  1 25  ? -0.625  -3.632  4.653   1.00 27.66  ?  56   ASP A OD1 1 
ATOM   94    O  OD2 . ASP A  1 25  ? -0.715  -4.492  6.676   1.00 29.69  -1 56   ASP A OD2 1 
ATOM   95    N  N   . ASP A  1 26  ? -1.976  -0.943  3.390   1.00 23.22  ?  57   ASP A N   1 
ATOM   96    C  CA  . ASP A  1 26  ? -3.186  -0.860  2.502   1.00 25.12  ?  57   ASP A CA  1 
ATOM   97    C  C   . ASP A  1 26  ? -3.896  0.501   2.657   1.00 23.70  ?  57   ASP A C   1 
ATOM   98    O  O   . ASP A  1 26  ? -5.120  0.559   2.491   1.00 23.22  ?  57   ASP A O   1 
ATOM   99    C  CB  . ASP A  1 26  ? -4.135  -2.028  2.694   1.00 23.49  ?  57   ASP A CB  1 
ATOM   100   C  CG  . ASP A  1 26  ? -3.584  -3.413  2.386   1.00 25.69  ?  57   ASP A CG  1 
ATOM   101   O  OD1 . ASP A  1 26  ? -2.395  -3.509  2.018   1.00 24.25  ?  57   ASP A OD1 1 
ATOM   102   O  OD2 . ASP A  1 26  ? -4.362  -4.384  2.499   1.00 23.08  -1 57   ASP A OD2 1 
ATOM   103   N  N   . LEU A  1 27  ? -3.146  1.568   2.925   1.00 23.21  ?  58   LEU A N   1 
ATOM   104   C  CA  . LEU A  1 27  ? -3.734  2.900   2.989   1.00 23.22  ?  58   LEU A CA  1 
ATOM   105   C  C   . LEU A  1 27  ? -3.944  3.438   1.569   1.00 24.19  ?  58   LEU A C   1 
ATOM   106   O  O   . LEU A  1 27  ? -3.001  3.500   0.771   1.00 25.23  ?  58   LEU A O   1 
ATOM   107   C  CB  . LEU A  1 27  ? -2.829  3.818   3.816   1.00 23.39  ?  58   LEU A CB  1 
ATOM   108   C  CG  . LEU A  1 27  ? -3.307  5.276   3.833   1.00 25.16  ?  58   LEU A CG  1 
ATOM   109   C  CD1 . LEU A  1 27  ? -4.581  5.428   4.711   1.00 21.24  ?  58   LEU A CD1 1 
ATOM   110   C  CD2 . LEU A  1 27  ? -2.168  6.190   4.325   1.00 24.83  ?  58   LEU A CD2 1 
ATOM   111   N  N   . GLY A  1 28  ? -5.180  3.801   1.238   1.00 19.77  ?  59   GLY A N   1 
ATOM   112   C  CA  . GLY A  1 28  ? -5.481  4.271   -0.097  1.00 22.98  ?  59   GLY A CA  1 
ATOM   113   C  C   . GLY A  1 28  ? -4.954  5.672   -0.370  1.00 24.37  ?  59   GLY A C   1 
ATOM   114   O  O   . GLY A  1 28  ? -4.730  6.489   0.538   1.00 20.33  ?  59   GLY A O   1 
ATOM   115   N  N   . TYR A  1 29  ? -4.834  5.956   -1.670  1.00 21.97  ?  60   TYR A N   1 
ATOM   116   C  CA  . TYR A  1 29  ? -4.168  7.168   -2.138  1.00 22.74  ?  60   TYR A CA  1 
ATOM   117   C  C   . TYR A  1 29  ? -4.896  8.419   -1.683  1.00 24.16  ?  60   TYR A C   1 
ATOM   118   O  O   . TYR A  1 29  ? -4.268  9.426   -1.360  1.00 24.77  ?  60   TYR A O   1 
ATOM   119   C  CB  . TYR A  1 29  ? -4.063  7.167   -3.662  1.00 21.38  ?  60   TYR A CB  1 
ATOM   120   C  CG  . TYR A  1 29  ? -2.920  8.039   -4.191  1.00 23.51  ?  60   TYR A CG  1 
ATOM   121   C  CD1 . TYR A  1 29  ? -1.591  7.773   -3.824  1.00 22.40  ?  60   TYR A CD1 1 
ATOM   122   C  CD2 . TYR A  1 29  ? -3.169  9.116   -5.041  1.00 23.85  ?  60   TYR A CD2 1 
ATOM   123   C  CE1 . TYR A  1 29  ? -0.562  8.549   -4.309  1.00 22.98  ?  60   TYR A CE1 1 
ATOM   124   C  CE2 . TYR A  1 29  ? -2.148  9.888   -5.544  1.00 25.97  ?  60   TYR A CE2 1 
ATOM   125   C  CZ  . TYR A  1 29  ? -0.840  9.609   -5.163  1.00 24.13  ?  60   TYR A CZ  1 
ATOM   126   O  OH  . TYR A  1 29  ? 0.196   10.398  -5.657  1.00 26.79  ?  60   TYR A OH  1 
ATOM   127   N  N   . ALA A  1 30  ? -6.224  8.379   -1.647  1.00 22.04  ?  61   ALA A N   1 
ATOM   128   C  CA  . ALA A  1 30  ? -6.994  9.557   -1.288  1.00 23.66  ?  61   ALA A CA  1 
ATOM   129   C  C   . ALA A  1 30  ? -7.464  9.529   0.150   1.00 24.31  ?  61   ALA A C   1 
ATOM   130   O  O   . ALA A  1 30  ? -8.405  10.249  0.485   1.00 27.70  ?  61   ALA A O   1 
ATOM   131   C  CB  . ALA A  1 30  ? -8.206  9.704   -2.224  1.00 21.93  ?  61   ALA A CB  1 
ATOM   132   N  N   . ASP A  1 31  ? -6.819  8.741   1.017   1.00 23.03  ?  62   ASP A N   1 
ATOM   133   C  CA  . ASP A  1 31  ? -7.352  8.465   2.346   1.00 23.40  ?  62   ASP A CA  1 
ATOM   134   C  C   . ASP A  1 31  ? -6.601  9.193   3.458   1.00 24.00  ?  62   ASP A C   1 
ATOM   135   O  O   . ASP A  1 31  ? -6.773  8.864   4.631   1.00 24.24  ?  62   ASP A O   1 
ATOM   136   C  CB  . ASP A  1 31  ? -7.388  6.952   2.562   1.00 19.33  ?  62   ASP A CB  1 
ATOM   137   C  CG  . ASP A  1 31  ? -8.435  6.286   1.653   1.00 24.37  ?  62   ASP A CG  1 
ATOM   138   O  OD1 . ASP A  1 31  ? -9.333  7.019   1.216   1.00 24.18  ?  62   ASP A OD1 1 
ATOM   139   O  OD2 . ASP A  1 31  ? -8.357  5.081   1.358   1.00 27.66  -1 62   ASP A OD2 1 
ATOM   140   N  N   . VAL A  1 32  ? -5.802  10.208  3.115   1.00 22.67  ?  63   VAL A N   1 
ATOM   141   C  CA  . VAL A  1 32  ? -5.324  11.168  4.099   1.00 23.02  ?  63   VAL A CA  1 
ATOM   142   C  C   . VAL A  1 32  ? -5.612  12.560  3.563   1.00 23.65  ?  63   VAL A C   1 
ATOM   143   O  O   . VAL A  1 32  ? -5.647  12.774  2.347   1.00 26.19  ?  63   VAL A O   1 
ATOM   144   C  CB  . VAL A  1 32  ? -3.814  11.007  4.420   1.00 24.12  ?  63   VAL A CB  1 
ATOM   145   C  CG1 . VAL A  1 32  ? -3.585  9.714   5.172   1.00 24.15  ?  63   VAL A CG1 1 
ATOM   146   C  CG2 . VAL A  1 32  ? -2.999  11.023  3.135   1.00 24.24  ?  63   VAL A CG2 1 
ATOM   147   N  N   . GLY A  1 33  ? -5.801  13.507  4.486   1.00 24.63  ?  64   GLY A N   1 
ATOM   148   C  CA  . GLY A  1 33  ? -6.150  14.865  4.100   1.00 27.22  ?  64   GLY A CA  1 
ATOM   149   C  C   . GLY A  1 33  ? -5.162  15.491  3.131   1.00 27.25  ?  64   GLY A C   1 
ATOM   150   O  O   . GLY A  1 33  ? -5.554  16.041  2.101   1.00 26.58  ?  64   GLY A O   1 
ATOM   151   N  N   . PHE A  1 34  ? -3.866  15.418  3.443   1.00 25.19  ?  65   PHE A N   1 
ATOM   152   C  CA  . PHE A  1 34  ? -2.860  16.078  2.614   1.00 25.49  ?  65   PHE A CA  1 
ATOM   153   C  C   . PHE A  1 34  ? -2.763  15.472  1.221   1.00 28.75  ?  65   PHE A C   1 
ATOM   154   O  O   . PHE A  1 34  ? -2.192  16.104  0.324   1.00 27.71  ?  65   PHE A O   1 
ATOM   155   C  CB  . PHE A  1 34  ? -1.469  16.043  3.288   1.00 23.85  ?  65   PHE A CB  1 
ATOM   156   C  CG  . PHE A  1 34  ? -0.792  14.692  3.273   1.00 24.76  ?  65   PHE A CG  1 
ATOM   157   C  CD1 . PHE A  1 34  ? 0.022   14.299  2.193   1.00 24.09  ?  65   PHE A CD1 1 
ATOM   158   C  CD2 . PHE A  1 34  ? -0.932  13.830  4.351   1.00 23.12  ?  65   PHE A CD2 1 
ATOM   159   C  CE1 . PHE A  1 34  ? 0.640   13.060  2.182   1.00 22.17  ?  65   PHE A CE1 1 
ATOM   160   C  CE2 . PHE A  1 34  ? -0.311  12.585  4.360   1.00 24.71  ?  65   PHE A CE2 1 
ATOM   161   C  CZ  . PHE A  1 34  ? 0.483   12.197  3.284   1.00 23.73  ?  65   PHE A CZ  1 
ATOM   162   N  N   . ASN A  1 35  ? -3.315  14.281  1.004   1.00 25.43  ?  66   ASN A N   1 
ATOM   163   C  CA  . ASN A  1 35  ? -3.298  13.684  -0.324  1.00 25.52  ?  66   ASN A CA  1 
ATOM   164   C  C   . ASN A  1 35  ? -4.672  13.637  -0.972  1.00 27.79  ?  66   ASN A C   1 
ATOM   165   O  O   . ASN A  1 35  ? -4.873  12.863  -1.910  1.00 26.70  ?  66   ASN A O   1 
ATOM   166   C  CB  . ASN A  1 35  ? -2.708  12.274  -0.296  1.00 27.44  ?  66   ASN A CB  1 
ATOM   167   C  CG  . ASN A  1 35  ? -1.818  12.007  -1.497  1.00 29.79  ?  66   ASN A CG  1 
ATOM   168   O  OD1 . ASN A  1 35  ? -0.988  12.840  -1.833  1.00 25.87  ?  66   ASN A OD1 1 
ATOM   169   N  ND2 . ASN A  1 35  ? -2.025  10.879  -2.176  1.00 22.60  ?  66   ASN A ND2 1 
ATOM   170   N  N   . GLY A  1 36  ? -5.622  14.435  -0.495  1.00 29.00  ?  67   GLY A N   1 
ATOM   171   C  CA  . GLY A  1 36  ? -6.881  14.624  -1.194  1.00 27.65  ?  67   GLY A CA  1 
ATOM   172   C  C   . GLY A  1 36  ? -8.124  14.200  -0.430  1.00 32.41  ?  67   GLY A C   1 
ATOM   173   O  O   . GLY A  1 36  ? -9.228  14.393  -0.956  1.00 29.04  ?  67   GLY A O   1 
ATOM   174   N  N   . SER A  1 37  ? -8.038  13.620  0.772   1.00 26.73  ?  68   SER A N   1 
ATOM   175   C  CA  . SER A  1 37  ? -9.249  13.088  1.393   1.00 28.45  ?  68   SER A CA  1 
ATOM   176   C  C   . SER A  1 37  ? -10.210 14.205  1.742   1.00 33.41  ?  68   SER A C   1 
ATOM   177   O  O   . SER A  1 37  ? -9.812  15.215  2.331   1.00 27.72  ?  68   SER A O   1 
ATOM   178   C  CB  . SER A  1 37  ? -8.953  12.304  2.670   1.00 27.12  ?  68   SER A CB  1 
ATOM   179   O  OG  . SER A  1 37  ? -10.147 11.636  3.072   1.00 27.02  ?  68   SER A OG  1 
ATOM   180   N  N   . THR A  1 38  ? -11.484 14.003  1.403   1.00 28.63  ?  69   THR A N   1 
ATOM   181   C  CA  . THR A  1 38  ? -12.534 14.914  1.814   1.00 30.51  ?  69   THR A CA  1 
ATOM   182   C  C   . THR A  1 38  ? -13.386 14.357  2.946   1.00 31.71  ?  69   THR A C   1 
ATOM   183   O  O   . THR A  1 38  ? -14.164 15.107  3.537   1.00 32.53  ?  69   THR A O   1 
ATOM   184   C  CB  . THR A  1 38  ? -13.423 15.263  0.617   1.00 33.13  ?  69   THR A CB  1 
ATOM   185   O  OG1 . THR A  1 38  ? -14.123 14.093  0.197   1.00 35.44  ?  69   THR A OG1 1 
ATOM   186   C  CG2 . THR A  1 38  ? -12.575 15.783  -0.534  1.00 39.23  ?  69   THR A CG2 1 
ATOM   187   N  N   . ASP A  1 39  ? -13.251 13.073  3.285   1.00 26.34  ?  70   ASP A N   1 
ATOM   188   C  CA  . ASP A  1 39  ? -14.031 12.524  4.384   1.00 26.75  ?  70   ASP A CA  1 
ATOM   189   C  C   . ASP A  1 39  ? -13.197 11.962  5.526   1.00 29.42  ?  70   ASP A C   1 
ATOM   190   O  O   . ASP A  1 39  ? -13.692 11.924  6.661   1.00 28.70  ?  70   ASP A O   1 
ATOM   191   C  CB  . ASP A  1 39  ? -15.007 11.441  3.885   1.00 28.54  ?  70   ASP A CB  1 
ATOM   192   C  CG  . ASP A  1 39  ? -14.315 10.276  3.180   1.00 28.71  ?  70   ASP A CG  1 
ATOM   193   O  OD1 . ASP A  1 39  ? -13.168 10.401  2.728   1.00 27.21  ?  70   ASP A OD1 1 
ATOM   194   O  OD2 . ASP A  1 39  ? -14.950 9.214   3.044   1.00 30.11  -1 70   ASP A OD2 1 
ATOM   195   N  N   . ILE A  1 40  ? -11.962 11.562  5.298   1.00 24.39  ?  71   ILE A N   1 
ATOM   196   C  CA  . ILE A  1 40  ? -11.144 11.074  6.405   1.00 24.61  ?  71   ILE A CA  1 
ATOM   197   C  C   . ILE A  1 40  ? -10.359 12.239  6.976   1.00 27.96  ?  71   ILE A C   1 
ATOM   198   O  O   . ILE A  1 40  ? -9.774  13.039  6.235   1.00 29.75  ?  71   ILE A O   1 
ATOM   199   C  CB  . ILE A  1 40  ? -10.234 9.924   5.960   1.00 24.01  ?  71   ILE A CB  1 
ATOM   200   C  CG1 . ILE A  1 40  ? -11.139 8.782   5.460   1.00 24.99  ?  71   ILE A CG1 1 
ATOM   201   C  CG2 . ILE A  1 40  ? -9.298  9.479   7.163   1.00 19.95  ?  71   ILE A CG2 1 
ATOM   202   C  CD1 . ILE A  1 40  ? -10.402 7.612   4.830   1.00 23.91  ?  71   ILE A CD1 1 
ATOM   203   N  N   . LEU A  1 41  ? -10.378 12.366  8.293   1.00 27.98  ?  72   LEU A N   1 
ATOM   204   C  CA  . LEU A  1 41  ? -9.724  13.477  8.968   1.00 26.30  ?  72   LEU A CA  1 
ATOM   205   C  C   . LEU A  1 41  ? -8.377  13.003  9.492   1.00 26.74  ?  72   LEU A C   1 
ATOM   206   O  O   . LEU A  1 41  ? -8.324  12.031  10.248  1.00 23.20  ?  72   LEU A O   1 
ATOM   207   C  CB  . LEU A  1 41  ? -10.588 14.001  10.108  1.00 30.05  ?  72   LEU A CB  1 
ATOM   208   C  CG  . LEU A  1 41  ? -11.981 14.500  9.728   1.00 33.07  ?  72   LEU A CG  1 
ATOM   209   C  CD1 . LEU A  1 41  ? -12.837 14.718  10.970  1.00 30.33  ?  72   LEU A CD1 1 
ATOM   210   C  CD2 . LEU A  1 41  ? -11.836 15.786  8.923   1.00 34.77  ?  72   LEU A CD2 1 
ATOM   211   N  N   . THR A  1 42  ? -7.295  13.657  9.052   1.00 23.40  ?  73   THR A N   1 
ATOM   212   C  CA  . THR A  1 42  ? -5.937  13.344  9.511   1.00 25.45  ?  73   THR A CA  1 
ATOM   213   C  C   . THR A  1 42  ? -5.186  14.637  9.838   1.00 26.12  ?  73   THR A C   1 
ATOM   214   O  O   . THR A  1 42  ? -4.158  14.942  9.235   1.00 27.07  ?  73   THR A O   1 
ATOM   215   C  CB  . THR A  1 42  ? -5.179  12.530  8.459   1.00 30.10  ?  73   THR A CB  1 
ATOM   216   O  OG1 . THR A  1 42  ? -5.090  13.272  7.244   1.00 24.07  ?  73   THR A OG1 1 
ATOM   217   C  CG2 . THR A  1 42  ? -5.868  11.200  8.147   1.00 25.37  ?  73   THR A CG2 1 
ATOM   218   N  N   . PRO A  1 43  ? -5.681  15.426  10.799  1.00 25.00  ?  74   PRO A N   1 
ATOM   219   C  CA  . PRO A  1 43  ? -5.036  16.726  11.078  1.00 27.70  ?  74   PRO A CA  1 
ATOM   220   C  C   . PRO A  1 43  ? -3.568  16.626  11.505  1.00 30.20  ?  74   PRO A C   1 
ATOM   221   O  O   . PRO A  1 43  ? -2.755  17.482  11.122  1.00 25.95  ?  74   PRO A O   1 
ATOM   222   C  CB  . PRO A  1 43  ? -5.910  17.304  12.209  1.00 31.05  ?  74   PRO A CB  1 
ATOM   223   C  CG  . PRO A  1 43  ? -6.511  16.100  12.888  1.00 30.37  ?  74   PRO A CG  1 
ATOM   224   C  CD  . PRO A  1 43  ? -6.777  15.131  11.740  1.00 24.56  ?  74   PRO A CD  1 
ATOM   225   N  N   . GLU A  1 44  ? -3.196  15.608  12.277  1.00 27.58  ?  75   GLU A N   1 
ATOM   226   C  CA  . GLU A  1 44  ? -1.805  15.526  12.727  1.00 28.55  ?  75   GLU A CA  1 
ATOM   227   C  C   . GLU A  1 44  ? -0.874  15.165  11.576  1.00 27.56  ?  75   GLU A C   1 
ATOM   228   O  O   . GLU A  1 44  ? 0.207   15.742  11.440  1.00 27.25  ?  75   GLU A O   1 
ATOM   229   C  CB  . GLU A  1 44  ? -1.657  14.510  13.863  1.00 31.58  ?  75   GLU A CB  1 
ATOM   230   C  CG  . GLU A  1 44  ? -2.467  14.818  15.095  1.00 32.02  ?  75   GLU A CG  1 
ATOM   231   C  CD  . GLU A  1 44  ? -2.002  16.091  15.799  1.00 36.09  ?  75   GLU A CD  1 
ATOM   232   O  OE1 . GLU A  1 44  ? -0.873  16.555  15.542  1.00 38.56  ?  75   GLU A OE1 1 
ATOM   233   O  OE2 . GLU A  1 44  ? -2.769  16.637  16.615  1.00 38.78  -1 75   GLU A OE2 1 
ATOM   234   N  N   . LEU A  1 45  ? -1.279  14.219  10.730  1.00 28.53  ?  76   LEU A N   1 
ATOM   235   C  CA  . LEU A  1 45  ? -0.474  13.909  9.554   1.00 25.10  ?  76   LEU A CA  1 
ATOM   236   C  C   . LEU A  1 45  ? -0.434  15.089  8.595   1.00 27.25  ?  76   LEU A C   1 
ATOM   237   O  O   . LEU A  1 45  ? 0.612   15.381  7.996   1.00 24.76  ?  76   LEU A O   1 
ATOM   238   C  CB  . LEU A  1 45  ? -1.033  12.676  8.844   1.00 24.51  ?  76   LEU A CB  1 
ATOM   239   C  CG  . LEU A  1 45  ? -0.785  11.338  9.526   1.00 26.51  ?  76   LEU A CG  1 
ATOM   240   C  CD1 . LEU A  1 45  ? -1.745  10.310  8.988   1.00 28.04  ?  76   LEU A CD1 1 
ATOM   241   C  CD2 . LEU A  1 45  ? 0.675   10.914  9.301   1.00 27.18  ?  76   LEU A CD2 1 
ATOM   242   N  N   . ASP A  1 46  ? -1.578  15.761  8.417   1.00 26.54  ?  77   ASP A N   1 
ATOM   243   C  CA  . ASP A  1 46  ? -1.633  16.922  7.539   1.00 30.01  ?  77   ASP A CA  1 
ATOM   244   C  C   . ASP A  1 46  ? -0.687  18.020  8.010   1.00 28.71  ?  77   ASP A C   1 
ATOM   245   O  O   . ASP A  1 46  ? -0.038  18.682  7.194   1.00 29.31  ?  77   ASP A O   1 
ATOM   246   C  CB  . ASP A  1 46  ? -3.064  17.461  7.475   1.00 30.65  ?  77   ASP A CB  1 
ATOM   247   C  CG  . ASP A  1 46  ? -4.011  16.562  6.669   1.00 31.48  ?  77   ASP A CG  1 
ATOM   248   O  OD1 . ASP A  1 46  ? -3.599  15.468  6.215   1.00 27.10  ?  77   ASP A OD1 1 
ATOM   249   O  OD2 . ASP A  1 46  ? -5.185  16.957  6.520   1.00 31.99  -1 77   ASP A OD2 1 
ATOM   250   N  N   . ASN A  1 47  ? -0.629  18.257  9.319   1.00 28.46  ?  78   ASN A N   1 
ATOM   251   C  CA  . ASN A  1 47  ? 0.260   19.292  9.844   1.00 31.32  ?  78   ASN A CA  1 
ATOM   252   C  C   . ASN A  1 47  ? 1.714   18.967  9.539   1.00 32.02  ?  78   ASN A C   1 
ATOM   253   O  O   . ASN A  1 47  ? 2.486   19.843  9.119   1.00 27.75  ?  78   ASN A O   1 
ATOM   254   C  CB  . ASN A  1 47  ? 0.041   19.464  11.350  1.00 34.12  ?  78   ASN A CB  1 
ATOM   255   C  CG  . ASN A  1 47  ? 0.859   20.615  11.931  1.00 40.09  ?  78   ASN A CG  1 
ATOM   256   O  OD1 . ASN A  1 47  ? 0.611   21.784  11.633  1.00 45.07  ?  78   ASN A OD1 1 
ATOM   257   N  ND2 . ASN A  1 47  ? 1.859   20.277  12.735  1.00 42.91  ?  78   ASN A ND2 1 
ATOM   258   N  N   . LEU A  1 48  ? 2.106   17.707  9.726   1.00 27.65  ?  79   LEU A N   1 
ATOM   259   C  CA  . LEU A  1 48  ? 3.460   17.310  9.364   1.00 27.06  ?  79   LEU A CA  1 
ATOM   260   C  C   . LEU A  1 48  ? 3.703   17.506  7.870   1.00 28.90  ?  79   LEU A C   1 
ATOM   261   O  O   . LEU A  1 48  ? 4.708   18.112  7.469   1.00 26.71  ?  79   LEU A O   1 
ATOM   262   C  CB  . LEU A  1 48  ? 3.699   15.855  9.774   1.00 26.90  ?  79   LEU A CB  1 
ATOM   263   C  CG  . LEU A  1 48  ? 3.767   15.569  11.270  1.00 29.31  ?  79   LEU A CG  1 
ATOM   264   C  CD1 . LEU A  1 48  ? 4.035   14.087  11.492  1.00 26.37  ?  79   LEU A CD1 1 
ATOM   265   C  CD2 . LEU A  1 48  ? 4.890   16.412  11.914  1.00 30.30  ?  79   LEU A CD2 1 
ATOM   266   N  N   . ALA A  1 49  ? 2.780   17.013  7.023   1.00 28.78  ?  80   ALA A N   1 
ATOM   267   C  CA  . ALA A  1 49  ? 2.965   17.135  5.582   1.00 25.62  ?  80   ALA A CA  1 
ATOM   268   C  C   . ALA A  1 49  ? 3.116   18.596  5.178   1.00 29.56  ?  80   ALA A C   1 
ATOM   269   O  O   . ALA A  1 49  ? 4.018   18.938  4.404   1.00 28.30  ?  80   ALA A O   1 
ATOM   270   C  CB  . ALA A  1 49  ? 1.787   16.489  4.816   1.00 26.84  ?  80   ALA A CB  1 
ATOM   271   N  N   . GLN A  1 50  ? 2.266   19.480  5.731   1.00 29.13  ?  81   GLN A N   1 
ATOM   272   C  CA  . GLN A  1 50  ? 2.329   20.898  5.386   1.00 27.32  ?  81   GLN A CA  1 
ATOM   273   C  C   . GLN A  1 50  ? 3.628   21.539  5.850   1.00 31.41  ?  81   GLN A C   1 
ATOM   274   O  O   . GLN A  1 50  ? 4.074   22.523  5.248   1.00 30.52  ?  81   GLN A O   1 
ATOM   275   C  CB  . GLN A  1 50  ? 1.137   21.656  5.981   1.00 32.08  ?  81   GLN A CB  1 
ATOM   276   C  CG  . GLN A  1 50  ? -0.221  21.162  5.468   1.00 34.31  ?  81   GLN A CG  1 
ATOM   277   C  CD  . GLN A  1 50  ? -1.391  21.644  6.328   1.00 41.49  ?  81   GLN A CD  1 
ATOM   278   O  OE1 . GLN A  1 50  ? -1.201  22.336  7.340   1.00 41.46  ?  81   GLN A OE1 1 
ATOM   279   N  NE2 . GLN A  1 50  ? -2.605  21.259  5.941   1.00 37.22  ?  81   GLN A NE2 1 
ATOM   280   N  N   . ASN A  1 51  ? 4.242   21.014  6.912   1.00 29.03  ?  82   ASN A N   1 
ATOM   281   C  CA  . ASN A  1 51  ? 5.496   21.554  7.421   1.00 30.26  ?  82   ASN A CA  1 
ATOM   282   C  C   . ASN A  1 51  ? 6.707   20.844  6.849   1.00 30.06  ?  82   ASN A C   1 
ATOM   283   O  O   . ASN A  1 51  ? 7.808   20.983  7.386   1.00 31.78  ?  82   ASN A O   1 
ATOM   284   C  CB  . ASN A  1 51  ? 5.509   21.519  8.952   1.00 29.76  ?  82   ASN A CB  1 
ATOM   285   C  CG  . ASN A  1 51  ? 4.640   22.621  9.560   1.00 38.59  ?  82   ASN A CG  1 
ATOM   286   O  OD1 . ASN A  1 51  ? 4.563   23.725  9.026   1.00 44.00  ?  82   ASN A OD1 1 
ATOM   287   N  ND2 . ASN A  1 51  ? 3.984   22.324  10.660  1.00 42.17  ?  82   ASN A ND2 1 
ATOM   288   N  N   . GLY A  1 52  ? 6.529   20.106  5.763   1.00 33.43  ?  83   GLY A N   1 
ATOM   289   C  CA  . GLY A  1 52  ? 7.642   19.494  5.051   1.00 31.59  ?  83   GLY A CA  1 
ATOM   290   C  C   . GLY A  1 52  ? 7.355   19.342  3.583   1.00 28.77  ?  83   GLY A C   1 
ATOM   291   O  O   . GLY A  1 52  ? 6.789   20.240  2.942   1.00 30.71  ?  83   GLY A O   1 
ATOM   292   N  N   . SER A  1 53  ? 7.747   18.203  3.036   1.00 27.04  ?  84   SER A N   1 
ATOM   293   C  CA  . SER A  1 53  ? 7.692   17.967  1.603   1.00 29.60  ?  84   SER A CA  1 
ATOM   294   C  C   . SER A  1 53  ? 6.689   16.864  1.304   1.00 27.91  ?  84   SER A C   1 
ATOM   295   O  O   . SER A  1 53  ? 6.856   15.735  1.777   1.00 27.58  ?  84   SER A O   1 
ATOM   296   C  CB  . SER A  1 53  ? 9.070   17.570  1.077   1.00 27.08  ?  84   SER A CB  1 
ATOM   297   O  OG  . SER A  1 53  ? 8.993   17.295  -0.308  1.00 30.76  ?  84   SER A OG  1 
ATOM   298   N  N   . ILE A  1 54  ? 5.670   17.179  0.496   1.00 24.71  ?  85   ILE A N   1 
ATOM   299   C  CA  . ILE A  1 54  ? 4.706   16.180  0.054   1.00 25.26  ?  85   ILE A CA  1 
ATOM   300   C  C   . ILE A  1 54  ? 5.153   15.626  -1.291  1.00 24.83  ?  85   ILE A C   1 
ATOM   301   O  O   . ILE A  1 54  ? 5.453   16.385  -2.220  1.00 26.12  ?  85   ILE A O   1 
ATOM   302   C  CB  . ILE A  1 54  ? 3.294   16.782  -0.041  1.00 26.03  ?  85   ILE A CB  1 
ATOM   303   C  CG1 . ILE A  1 54  ? 2.744   17.027  1.368   1.00 26.41  ?  85   ILE A CG1 1 
ATOM   304   C  CG2 . ILE A  1 54  ? 2.382   15.842  -0.858  1.00 24.31  ?  85   ILE A CG2 1 
ATOM   305   C  CD1 . ILE A  1 54  ? 1.510   17.944  1.396   1.00 27.15  ?  85   ILE A CD1 1 
ATOM   306   N  N   . PHE A  1 55  ? 5.221   14.303  -1.395  1.00 21.63  ?  86   PHE A N   1 
ATOM   307   C  CA  . PHE A  1 55  ? 5.656   13.636  -2.619  1.00 23.31  ?  86   PHE A CA  1 
ATOM   308   C  C   . PHE A  1 55  ? 4.447   13.212  -3.427  1.00 23.70  ?  86   PHE A C   1 
ATOM   309   O  O   . PHE A  1 55  ? 3.720   12.298  -3.020  1.00 24.83  ?  86   PHE A O   1 
ATOM   310   C  CB  . PHE A  1 55  ? 6.518   12.426  -2.309  1.00 24.31  ?  86   PHE A CB  1 
ATOM   311   C  CG  . PHE A  1 55  ? 7.853   12.786  -1.735  1.00 23.69  ?  86   PHE A CG  1 
ATOM   312   C  CD1 . PHE A  1 55  ? 7.984   13.100  -0.386  1.00 27.06  ?  86   PHE A CD1 1 
ATOM   313   C  CD2 . PHE A  1 55  ? 8.970   12.865  -2.554  1.00 25.94  ?  86   PHE A CD2 1 
ATOM   314   C  CE1 . PHE A  1 55  ? 9.245   13.449  0.158   1.00 25.16  ?  86   PHE A CE1 1 
ATOM   315   C  CE2 . PHE A  1 55  ? 10.239  13.222  -2.017  1.00 30.32  ?  86   PHE A CE2 1 
ATOM   316   C  CZ  . PHE A  1 55  ? 10.362  13.504  -0.672  1.00 28.20  ?  86   PHE A CZ  1 
ATOM   317   N  N   . THR A  1 56  ? 4.261   13.843  -4.591  1.00 24.19  ?  87   THR A N   1 
ATOM   318   C  CA  . THR A  1 56  ? 3.050   13.640  -5.381  1.00 23.10  ?  87   THR A CA  1 
ATOM   319   C  C   . THR A  1 56  ? 3.169   12.482  -6.369  1.00 22.90  ?  87   THR A C   1 
ATOM   320   O  O   . THR A  1 56  ? 2.142   12.060  -6.922  1.00 23.42  ?  87   THR A O   1 
ATOM   321   C  CB  . THR A  1 56  ? 2.651   14.951  -6.095  1.00 28.58  ?  87   THR A CB  1 
ATOM   322   O  OG1 . THR A  1 56  ? 3.669   15.364  -7.007  1.00 26.02  ?  87   THR A OG1 1 
ATOM   323   C  CG2 . THR A  1 56  ? 2.446   16.084  -5.044  1.00 26.94  ?  87   THR A CG2 1 
ATOM   324   N  N   . SER A  1 57  ? 4.383   11.940  -6.574  1.00 23.45  ?  88   SER A N   1 
ATOM   325   C  CA  . SER A  1 57  ? 4.640   10.735  -7.405  1.00 25.28  ?  88   SER A CA  1 
ATOM   326   C  C   . SER A  1 57  ? 5.605   9.793   -6.640  1.00 27.60  ?  88   SER A C   1 
ATOM   327   O  O   . SER A  1 57  ? 6.728   9.498   -7.072  1.00 25.29  ?  88   SER A O   1 
ATOM   328   C  CB  . SER A  1 57  ? 5.215   11.122  -8.782  1.00 24.19  ?  88   SER A CB  1 
ATOM   329   O  OG  . SER A  1 57  ? 4.200   11.582  -9.677  1.00 25.79  ?  88   SER A OG  1 
ATOM   330   N  N   . ALA A  1 58  ? 5.140   9.270   -5.513  1.00 25.84  ?  89   ALA A N   1 
ATOM   331   C  CA  . ALA A  1 58  ? 5.889   8.315   -4.702  1.00 25.18  ?  89   ALA A CA  1 
ATOM   332   C  C   . ALA A  1 58  ? 5.415   6.899   -5.001  1.00 26.27  ?  89   ALA A C   1 
ATOM   333   O  O   . ALA A  1 58  ? 4.206   6.636   -5.026  1.00 26.16  ?  89   ALA A O   1 
ATOM   334   C  CB  . ALA A  1 58  ? 5.713   8.628   -3.214  1.00 26.05  ?  89   ALA A CB  1 
ATOM   335   N  N   . TYR A  1 59  ? 6.358   5.990   -5.220  1.00 25.16  ?  90   TYR A N   1 
ATOM   336   C  CA  . TYR A  1 59  ? 6.044   4.611   -5.573  1.00 22.86  ?  90   TYR A CA  1 
ATOM   337   C  C   . TYR A  1 59  ? 6.682   3.636   -4.591  1.00 27.48  ?  90   TYR A C   1 
ATOM   338   O  O   . TYR A  1 59  ? 7.794   3.868   -4.078  1.00 24.65  ?  90   TYR A O   1 
ATOM   339   C  CB  . TYR A  1 59  ? 6.519   4.288   -6.997  1.00 22.58  ?  90   TYR A CB  1 
ATOM   340   C  CG  . TYR A  1 59  ? 5.838   5.115   -8.041  1.00 21.65  ?  90   TYR A CG  1 
ATOM   341   C  CD1 . TYR A  1 59  ? 4.631   4.698   -8.591  1.00 23.72  ?  90   TYR A CD1 1 
ATOM   342   C  CD2 . TYR A  1 59  ? 6.384   6.326   -8.479  1.00 24.16  ?  90   TYR A CD2 1 
ATOM   343   C  CE1 . TYR A  1 59  ? 3.997   5.426   -9.560  1.00 23.07  ?  90   TYR A CE1 1 
ATOM   344   C  CE2 . TYR A  1 59  ? 5.743   7.073   -9.485  1.00 23.79  ?  90   TYR A CE2 1 
ATOM   345   C  CZ  . TYR A  1 59  ? 4.541   6.618   -9.996  1.00 22.51  ?  90   TYR A CZ  1 
ATOM   346   O  OH  . TYR A  1 59  ? 3.872   7.326   -10.966 1.00 22.76  ?  90   TYR A OH  1 
ATOM   347   N  N   . VAL A  1 60  ? 5.972   2.554   -4.314  1.00 22.71  ?  91   VAL A N   1 
ATOM   348   C  CA  . VAL A  1 60  ? 6.549   1.430   -3.605  1.00 24.12  ?  91   VAL A CA  1 
ATOM   349   C  C   . VAL A  1 60  ? 7.011   0.429   -4.656  1.00 23.62  ?  91   VAL A C   1 
ATOM   350   O  O   . VAL A  1 60  ? 6.568   0.457   -5.795  1.00 22.84  ?  91   VAL A O   1 
ATOM   351   C  CB  . VAL A  1 60  ? 5.558   0.809   -2.591  1.00 22.03  ?  91   VAL A CB  1 
ATOM   352   C  CG1 . VAL A  1 60  ? 5.443   1.747   -1.360  1.00 22.87  ?  91   VAL A CG1 1 
ATOM   353   C  CG2 . VAL A  1 60  ? 4.199   0.532   -3.225  1.00 23.43  ?  91   VAL A CG2 1 
ATOM   354   N  N   . ALA A  1 61  ? 7.952   -0.449  -4.280  1.00 26.40  ?  92   ALA A N   1 
ATOM   355   C  CA  . ALA A  1 61  ? 8.569   -1.381  -5.221  1.00 24.13  ?  92   ALA A CA  1 
ATOM   356   C  C   . ALA A  1 61  ? 7.684   -2.558  -5.609  1.00 25.07  ?  92   ALA A C   1 
ATOM   357   O  O   . ALA A  1 61  ? 8.038   -3.285  -6.543  1.00 27.05  ?  92   ALA A O   1 
ATOM   358   C  CB  . ALA A  1 61  ? 9.880   -1.926  -4.644  1.00 23.83  ?  92   ALA A CB  1 
ATOM   359   N  N   . HIS A  1 62  ? 6.557   -2.778  -4.936  1.00 25.32  ?  93   HIS A N   1 
ATOM   360   C  CA  . HIS A  1 62  ? 5.631   -3.842  -5.325  1.00 25.01  ?  93   HIS A CA  1 
ATOM   361   C  C   . HIS A  1 62  ? 4.222   -3.471  -4.864  1.00 24.83  ?  93   HIS A C   1 
ATOM   362   O  O   . HIS A  1 62  ? 4.073   -2.821  -3.824  1.00 24.44  ?  93   HIS A O   1 
ATOM   363   C  CB  . HIS A  1 62  ? 6.072   -5.173  -4.695  1.00 26.18  ?  93   HIS A CB  1 
ATOM   364   C  CG  . HIS A  1 62  ? 5.559   -6.394  -5.399  1.00 22.10  ?  93   HIS A CG  1 
ATOM   365   N  ND1 . HIS A  1 62  ? 6.025   -6.792  -6.633  1.00 24.74  ?  93   HIS A ND1 1 
ATOM   366   C  CD2 . HIS A  1 62  ? 4.660   -7.330  -5.016  1.00 23.20  ?  93   HIS A CD2 1 
ATOM   367   C  CE1 . HIS A  1 62  ? 5.405   -7.902  -6.999  1.00 24.98  ?  93   HIS A CE1 1 
ATOM   368   N  NE2 . HIS A  1 62  ? 4.572   -8.251  -6.034  1.00 25.35  ?  93   HIS A NE2 1 
ATOM   369   N  N   . PRO A  1 63  ? 3.179   -3.860  -5.599  1.00 26.43  ?  94   PRO A N   1 
ATOM   370   C  CA  . PRO A  1 63  ? 1.814   -3.466  -5.218  1.00 21.45  ?  94   PRO A CA  1 
ATOM   371   C  C   . PRO A  1 63  ? 1.168   -4.305  -4.120  1.00 24.19  ?  94   PRO A C   1 
ATOM   372   O  O   . PRO A  1 63  ? -0.035  -4.158  -3.906  1.00 23.83  ?  94   PRO A O   1 
ATOM   373   C  CB  . PRO A  1 63  ? 1.043   -3.591  -6.539  1.00 23.35  ?  94   PRO A CB  1 
ATOM   374   C  CG  . PRO A  1 63  ? 1.725   -4.704  -7.275  1.00 27.07  ?  94   PRO A CG  1 
ATOM   375   C  CD  . PRO A  1 63  ? 3.219   -4.529  -6.911  1.00 21.53  ?  94   PRO A CD  1 
ATOM   376   N  N   . PHE A  1 64  ? 1.949   -5.110  -3.383  1.00 24.97  ?  95   PHE A N   1 
ATOM   377   C  CA  . PHE A  1 64  ? 1.386   -5.819  -2.186  1.00 24.95  ?  95   PHE A CA  1 
ATOM   378   C  C   . PHE A  1 64  ? 2.453   -5.912  -1.046  1.00 28.39  ?  95   PHE A C   1 
ATOM   379   O  O   . PHE A  1 64  ? 3.643   -5.849  -1.365  1.00 26.29  ?  95   PHE A O   1 
ATOM   380   C  CB  . PHE A  1 64  ? 0.574   -7.088  -2.490  1.00 23.75  ?  95   PHE A CB  1 
ATOM   381   C  CG  . PHE A  1 64  ? 1.239   -8.251  -3.200  1.00 25.83  ?  95   PHE A CG  1 
ATOM   382   C  CD1 . PHE A  1 64  ? 2.045   -9.141  -2.506  1.00 26.31  ?  95   PHE A CD1 1 
ATOM   383   C  CD2 . PHE A  1 64  ? 1.006   -8.482  -4.548  1.00 28.92  ?  95   PHE A CD2 1 
ATOM   384   C  CE1 . PHE A  1 64  ? 2.629   -10.210 -3.156  1.00 27.78  ?  95   PHE A CE1 1 
ATOM   385   C  CE2 . PHE A  1 64  ? 1.590   -9.557  -5.189  1.00 28.41  ?  95   PHE A CE2 1 
ATOM   386   C  CZ  . PHE A  1 64  ? 2.400   -10.415 -4.493  1.00 26.39  ?  95   PHE A CZ  1 
HETATM 387   N  N   . OSE A  1 65  ? 2.022   -6.120  0.204   1.00 30.01  ?  96   OSE A N   1 
HETATM 388   C  CA  . OSE A  1 65  ? 2.886   -6.009  1.419   1.00 30.84  ?  96   OSE A CA  1 
HETATM 389   C  CB  . OSE A  1 65  ? 2.133   -6.501  2.645   1.00 35.69  ?  96   OSE A CB  1 
HETATM 390   O  OG  . OSE A  1 65  ? 1.510   -7.696  2.316   1.00 40.61  ?  96   OSE A OG  1 
HETATM 391   C  C   . OSE A  1 65  ? 4.242   -6.701  1.433   1.00 24.93  ?  96   OSE A C   1 
HETATM 392   O  O   . OSE A  1 65  ? 5.247   -5.995  1.511   1.00 28.43  ?  96   OSE A O   1 
HETATM 393   S  S   . OSE A  1 65  ? -0.026  -7.543  2.201   1.00 40.70  ?  96   OSE A S   1 
HETATM 394   O  O1S . OSE A  1 65  ? -0.406  -8.390  1.103   1.00 38.23  ?  96   OSE A O1S 1 
HETATM 395   O  O2S . OSE A  1 65  ? -0.388  -8.008  3.514   1.00 42.45  ?  96   OSE A O2S 1 
HETATM 396   O  O3S . OSE A  1 65  ? -0.293  -6.145  1.982   1.00 35.84  ?  96   OSE A O3S 1 
ATOM   397   N  N   . GLY A  1 66  ? 4.245   -8.023  1.436   1.00 27.29  ?  97   GLY A N   1 
ATOM   398   C  CA  . GLY A  1 66  ? 5.478   -8.757  1.726   1.00 30.91  ?  97   GLY A CA  1 
ATOM   399   C  C   . GLY A  1 66  ? 6.650   -8.307  0.866   1.00 28.24  ?  97   GLY A C   1 
ATOM   400   O  O   . GLY A  1 66  ? 7.695   -7.901  1.376   1.00 29.61  ?  97   GLY A O   1 
ATOM   401   N  N   . PRO A  1 67  ? 6.473   -8.358  -0.453  1.00 27.56  ?  98   PRO A N   1 
ATOM   402   C  CA  . PRO A  1 67  ? 7.531   -7.853  -1.347  1.00 25.89  ?  98   PRO A CA  1 
ATOM   403   C  C   . PRO A  1 67  ? 7.816   -6.365  -1.185  1.00 29.11  ?  98   PRO A C   1 
ATOM   404   O  O   . PRO A  1 67  ? 8.977   -5.932  -1.300  1.00 27.71  ?  98   PRO A O   1 
ATOM   405   C  CB  . PRO A  1 67  ? 6.970   -8.189  -2.735  1.00 26.64  ?  98   PRO A CB  1 
ATOM   406   C  CG  . PRO A  1 67  ? 6.069   -9.338  -2.493  1.00 28.86  ?  98   PRO A CG  1 
ATOM   407   C  CD  . PRO A  1 67  ? 5.400   -9.023  -1.207  1.00 27.16  ?  98   PRO A CD  1 
ATOM   408   N  N   . SER A  1 68  ? 6.788   -5.557  -0.904  1.00 26.08  ?  99   SER A N   1 
ATOM   409   C  CA  . SER A  1 68  ? 7.032   -4.137  -0.678  1.00 23.72  ?  99   SER A CA  1 
ATOM   410   C  C   . SER A  1 68  ? 7.892   -3.933  0.569   1.00 23.71  ?  99   SER A C   1 
ATOM   411   O  O   . SER A  1 68  ? 8.853   -3.160  0.550   1.00 22.99  ?  99   SER A O   1 
ATOM   412   C  CB  . SER A  1 68  ? 5.702   -3.378  -0.568  1.00 22.68  ?  99   SER A CB  1 
ATOM   413   O  OG  . SER A  1 68  ? 5.926   -2.010  -0.245  1.00 24.27  ?  99   SER A OG  1 
ATOM   414   N  N   . ARG A  1 69  ? 7.583   -4.660  1.633   1.00 24.61  ?  100  ARG A N   1 
ATOM   415   C  CA  . ARG A  1 69  ? 8.320   -4.464  2.910   1.00 24.85  ?  100  ARG A CA  1 
ATOM   416   C  C   . ARG A  1 69  ? 9.758   -4.966  2.702   1.00 26.66  ?  100  ARG A C   1 
ATOM   417   O  O   . ARG A  1 69  ? 10.698  -4.257  3.105   1.00 28.10  ?  100  ARG A O   1 
ATOM   418   C  CB  . ARG A  1 69  ? 7.503   -5.110  4.028   1.00 26.68  ?  100  ARG A CB  1 
ATOM   419   C  CG  . ARG A  1 69  ? 6.265   -4.309  4.396   1.00 25.59  ?  100  ARG A CG  1 
ATOM   420   C  CD  . ARG A  1 69  ? 5.175   -5.161  5.017   1.00 30.34  ?  100  ARG A CD  1 
ATOM   421   N  NE  . ARG A  1 69  ? 3.893   -4.451  5.087   1.00 23.73  ?  100  ARG A NE  1 
ATOM   422   C  CZ  . ARG A  1 69  ? 3.558   -3.574  6.032   1.00 28.34  ?  100  ARG A CZ  1 
ATOM   423   N  NH1 . ARG A  1 69  ? 4.262   -3.490  7.147   1.00 22.69  ?  100  ARG A NH1 1 
ATOM   424   N  NH2 . ARG A  1 69  ? 2.514   -2.787  5.861   1.00 24.38  ?  100  ARG A NH2 1 
ATOM   425   N  N   . SER A  1 70  ? 9.888   -6.150  2.110   1.00 26.44  ?  101  SER A N   1 
ATOM   426   C  CA  . SER A  1 70  ? 11.209  -6.658  1.782   1.00 29.83  ?  101  SER A CA  1 
ATOM   427   C  C   . SER A  1 70  ? 12.031  -5.590  1.072   1.00 30.49  ?  101  SER A C   1 
ATOM   428   O  O   . SER A  1 70  ? 13.188  -5.334  1.419   1.00 28.29  ?  101  SER A O   1 
ATOM   429   C  CB  . SER A  1 70  ? 11.065  -7.900  0.908   1.00 31.79  ?  101  SER A CB  1 
ATOM   430   O  OG  . SER A  1 70  ? 12.285  -8.181  0.241   1.00 39.50  ?  101  SER A OG  1 
ATOM   431   N  N   . ALA A  1 71  ? 11.431  -4.934  0.093   1.00 24.76  ?  102  ALA A N   1 
ATOM   432   C  CA  . ALA A  1 71  ? 12.154  -3.931  -0.675  1.00 23.59  ?  102  ALA A CA  1 
ATOM   433   C  C   . ALA A  1 71  ? 12.526  -2.719  0.165   1.00 26.90  ?  102  ALA A C   1 
ATOM   434   O  O   . ALA A  1 71  ? 13.598  -2.148  -0.036  1.00 29.25  ?  102  ALA A O   1 
ATOM   435   C  CB  . ALA A  1 71  ? 11.326  -3.504  -1.895  1.00 27.35  ?  102  ALA A CB  1 
ATOM   436   N  N   . ILE A  1 72  ? 11.657  -2.286  1.089   1.00 24.72  ?  103  ILE A N   1 
ATOM   437   C  CA  . ILE A  1 72  ? 12.006  -1.144  1.942   1.00 24.55  ?  103  ILE A CA  1 
ATOM   438   C  C   . ILE A  1 72  ? 13.216  -1.476  2.811   1.00 27.04  ?  103  ILE A C   1 
ATOM   439   O  O   . ILE A  1 72  ? 14.143  -0.677  2.938   1.00 29.67  ?  103  ILE A O   1 
ATOM   440   C  CB  . ILE A  1 72  ? 10.818  -0.710  2.826   1.00 25.61  ?  103  ILE A CB  1 
ATOM   441   C  CG1 . ILE A  1 72  ? 9.718   -0.038  1.997   1.00 23.61  ?  103  ILE A CG1 1 
ATOM   442   C  CG2 . ILE A  1 72  ? 11.299  0.254   3.923   1.00 28.53  ?  103  ILE A CG2 1 
ATOM   443   C  CD1 . ILE A  1 72  ? 8.333   -0.084  2.663   1.00 30.43  ?  103  ILE A CD1 1 
ATOM   444   N  N   . LEU A  1 73  ? 13.212  -2.647  3.436   1.00 26.21  ?  104  LEU A N   1 
ATOM   445   C  CA  . LEU A  1 73  ? 14.283  -2.973  4.370   1.00 27.72  ?  104  LEU A CA  1 
ATOM   446   C  C   . LEU A  1 73  ? 15.562  -3.448  3.683   1.00 30.01  ?  104  LEU A C   1 
ATOM   447   O  O   . LEU A  1 73  ? 16.654  -3.163  4.195   1.00 29.38  ?  104  LEU A O   1 
ATOM   448   C  CB  . LEU A  1 73  ? 13.792  -3.996  5.401   1.00 28.48  ?  104  LEU A CB  1 
ATOM   449   C  CG  . LEU A  1 73  ? 13.128  -3.282  6.591   1.00 32.03  ?  104  LEU A CG  1 
ATOM   450   C  CD1 . LEU A  1 73  ? 11.633  -3.173  6.473   1.00 32.51  ?  104  LEU A CD1 1 
ATOM   451   C  CD2 . LEU A  1 73  ? 13.487  -3.905  7.910   1.00 38.21  ?  104  LEU A CD2 1 
ATOM   452   N  N   . THR A  1 74  ? 15.469  -4.155  2.553   1.00 27.24  ?  105  THR A N   1 
ATOM   453   C  CA  . THR A  1 74  ? 16.669  -4.545  1.807   1.00 29.40  ?  105  THR A CA  1 
ATOM   454   C  C   . THR A  1 74  ? 17.164  -3.490  0.828   1.00 30.36  ?  105  THR A C   1 
ATOM   455   O  O   . THR A  1 74  ? 18.333  -3.548  0.418   1.00 28.46  ?  105  THR A O   1 
ATOM   456   C  CB  . THR A  1 74  ? 16.446  -5.835  1.005   1.00 30.86  ?  105  THR A CB  1 
ATOM   457   O  OG1 . THR A  1 74  ? 15.481  -5.609  -0.042  1.00 30.08  ?  105  THR A OG1 1 
ATOM   458   C  CG2 . THR A  1 74  ? 16.011  -7.002  1.899   1.00 30.22  ?  105  THR A CG2 1 
ATOM   459   N  N   . GLY A  1 75  ? 16.315  -2.556  0.403   1.00 30.29  ?  106  GLY A N   1 
ATOM   460   C  CA  . GLY A  1 75  ? 16.727  -1.615  -0.630  1.00 26.19  ?  106  GLY A CA  1 
ATOM   461   C  C   . GLY A  1 75  ? 16.850  -2.187  -2.025  1.00 29.86  ?  106  GLY A C   1 
ATOM   462   O  O   . GLY A  1 75  ? 17.465  -1.545  -2.889  1.00 27.73  ?  106  GLY A O   1 
ATOM   463   N  N   . ARG A  1 76  ? 16.260  -3.365  -2.279  1.00 27.09  ?  107  ARG A N   1 
ATOM   464   C  CA  . ARG A  1 76  ? 16.268  -4.021  -3.580  1.00 27.98  ?  107  ARG A CA  1 
ATOM   465   C  C   . ARG A  1 76  ? 14.852  -4.440  -3.986  1.00 30.47  ?  107  ARG A C   1 
ATOM   466   O  O   . ARG A  1 76  ? 14.024  -4.798  -3.133  1.00 28.83  ?  107  ARG A O   1 
ATOM   467   C  CB  . ARG A  1 76  ? 17.182  -5.256  -3.559  1.00 29.56  ?  107  ARG A CB  1 
ATOM   468   C  CG  . ARG A  1 76  ? 18.636  -4.926  -3.112  1.00 32.90  ?  107  ARG A CG  1 
ATOM   469   C  CD  . ARG A  1 76  ? 19.534  -6.151  -3.189  1.00 35.26  ?  107  ARG A CD  1 
ATOM   470   N  NE  . ARG A  1 76  ? 19.959  -6.380  -4.564  1.00 39.40  ?  107  ARG A NE  1 
ATOM   471   C  CZ  . ARG A  1 76  ? 20.351  -7.552  -5.053  1.00 43.08  ?  107  ARG A CZ  1 
ATOM   472   N  NH1 . ARG A  1 76  ? 20.512  -8.614  -4.273  1.00 41.84  ?  107  ARG A NH1 1 
ATOM   473   N  NH2 . ARG A  1 76  ? 20.602  -7.658  -6.354  1.00 36.99  ?  107  ARG A NH2 1 
ATOM   474   N  N   . TYR A  1 77  ? 14.584  -4.402  -5.292  1.00 28.11  ?  108  TYR A N   1 
ATOM   475   C  CA  . TYR A  1 77  ? 13.342  -4.961  -5.809  1.00 31.72  ?  108  TYR A CA  1 
ATOM   476   C  C   . TYR A  1 77  ? 13.208  -6.408  -5.338  1.00 33.95  ?  108  TYR A C   1 
ATOM   477   O  O   . TYR A  1 77  ? 14.216  -7.127  -5.282  1.00 31.50  ?  108  TYR A O   1 
ATOM   478   C  CB  . TYR A  1 77  ? 13.312  -4.920  -7.346  1.00 30.72  ?  108  TYR A CB  1 
ATOM   479   C  CG  . TYR A  1 77  ? 12.935  -3.579  -7.929  1.00 31.01  ?  108  TYR A CG  1 
ATOM   480   C  CD1 . TYR A  1 77  ? 11.620  -3.102  -7.843  1.00 27.56  ?  108  TYR A CD1 1 
ATOM   481   C  CD2 . TYR A  1 77  ? 13.884  -2.787  -8.574  1.00 28.52  ?  108  TYR A CD2 1 
ATOM   482   C  CE1 . TYR A  1 77  ? 11.267  -1.869  -8.379  1.00 29.13  ?  108  TYR A CE1 1 
ATOM   483   C  CE2 . TYR A  1 77  ? 13.534  -1.552  -9.126  1.00 31.10  ?  108  TYR A CE2 1 
ATOM   484   C  CZ  . TYR A  1 77  ? 12.214  -1.103  -9.021  1.00 31.83  ?  108  TYR A CZ  1 
ATOM   485   O  OH  . TYR A  1 77  ? 11.854  0.130   -9.530  1.00 30.14  ?  108  TYR A OH  1 
ATOM   486   N  N   . PRO A  1 78  ? 11.999  -6.867  -4.985  1.00 29.23  ?  109  PRO A N   1 
ATOM   487   C  CA  . PRO A  1 78  ? 11.846  -8.261  -4.535  1.00 28.73  ?  109  PRO A CA  1 
ATOM   488   C  C   . PRO A  1 78  ? 12.175  -9.280  -5.603  1.00 30.11  ?  109  PRO A C   1 
ATOM   489   O  O   . PRO A  1 78  ? 12.435  -10.442 -5.260  1.00 32.82  ?  109  PRO A O   1 
ATOM   490   C  CB  . PRO A  1 78  ? 10.361  -8.345  -4.144  1.00 26.81  ?  109  PRO A CB  1 
ATOM   491   C  CG  . PRO A  1 78  ? 9.717   -7.345  -5.034  1.00 27.68  ?  109  PRO A CG  1 
ATOM   492   C  CD  . PRO A  1 78  ? 10.692  -6.193  -5.101  1.00 29.08  ?  109  PRO A CD  1 
ATOM   493   N  N   . HIS A  1 79  ? 12.111  -8.900  -6.885  1.00 25.54  ?  110  HIS A N   1 
ATOM   494   C  CA  . HIS A  1 79  ? 12.481  -9.795  -7.979  1.00 29.61  ?  110  HIS A CA  1 
ATOM   495   C  C   . HIS A  1 79  ? 13.963  -10.128 -7.978  1.00 31.71  ?  110  HIS A C   1 
ATOM   496   O  O   . HIS A  1 79  ? 14.363  -11.085 -8.647  1.00 31.07  ?  110  HIS A O   1 
ATOM   497   C  CB  . HIS A  1 79  ? 12.106  -9.168  -9.322  1.00 27.56  ?  110  HIS A CB  1 
ATOM   498   C  CG  . HIS A  1 79  ? 10.797  -8.441  -9.284  1.00 30.04  ?  110  HIS A CG  1 
ATOM   499   N  ND1 . HIS A  1 79  ? 10.637  -7.244  -8.620  1.00 27.85  ?  110  HIS A ND1 1 
ATOM   500   C  CD2 . HIS A  1 79  ? 9.590   -8.744  -9.815  1.00 33.42  ?  110  HIS A CD2 1 
ATOM   501   C  CE1 . HIS A  1 79  ? 9.386   -6.835  -8.750  1.00 29.73  ?  110  HIS A CE1 1 
ATOM   502   N  NE2 . HIS A  1 79  ? 8.730   -7.726  -9.471  1.00 30.44  ?  110  HIS A NE2 1 
ATOM   503   N  N   . LEU A  1 80  ? 14.774  -9.349  -7.260  1.00 31.09  ?  111  LEU A N   1 
ATOM   504   C  CA  . LEU A  1 80  ? 16.206  -9.588  -7.133  1.00 32.94  ?  111  LEU A CA  1 
ATOM   505   C  C   . LEU A  1 80  ? 16.563  -10.360 -5.878  1.00 33.27  ?  111  LEU A C   1 
ATOM   506   O  O   . LEU A  1 80  ? 17.711  -10.787 -5.742  1.00 36.09  ?  111  LEU A O   1 
ATOM   507   C  CB  . LEU A  1 80  ? 16.985  -8.265  -7.149  1.00 32.21  ?  111  LEU A CB  1 
ATOM   508   C  CG  . LEU A  1 80  ? 17.253  -7.596  -8.514  1.00 37.57  ?  111  LEU A CG  1 
ATOM   509   C  CD1 . LEU A  1 80  ? 18.184  -8.471  -9.339  1.00 40.57  ?  111  LEU A CD1 1 
ATOM   510   C  CD2 . LEU A  1 80  ? 15.995  -7.356  -9.317  1.00 34.14  ?  111  LEU A CD2 1 
ATOM   511   N  N   . THR A  1 81  ? 15.615  -10.555 -4.967  1.00 32.53  ?  112  THR A N   1 
ATOM   512   C  CA  . THR A  1 81  ? 15.884  -11.202 -3.694  1.00 35.07  ?  112  THR A CA  1 
ATOM   513   C  C   . THR A  1 81  ? 15.081  -12.470 -3.513  1.00 32.54  ?  112  THR A C   1 
ATOM   514   O  O   . THR A  1 81  ? 15.194  -13.098 -2.463  1.00 32.42  ?  112  THR A O   1 
ATOM   515   C  CB  . THR A  1 81  ? 15.574  -10.262 -2.526  1.00 37.22  ?  112  THR A CB  1 
ATOM   516   O  OG1 . THR A  1 81  ? 14.188  -9.876  -2.596  1.00 34.05  ?  112  THR A OG1 1 
ATOM   517   C  CG2 . THR A  1 81  ? 16.472  -9.032  -2.583  1.00 32.39  ?  112  THR A CG2 1 
ATOM   518   N  N   . GLY A  1 82  ? 14.242  -12.840 -4.484  1.00 33.52  ?  113  GLY A N   1 
ATOM   519   C  CA  . GLY A  1 82  ? 13.438  -14.035 -4.364  1.00 32.35  ?  113  GLY A CA  1 
ATOM   520   C  C   . GLY A  1 82  ? 12.184  -13.873 -3.543  1.00 30.84  ?  113  GLY A C   1 
ATOM   521   O  O   . GLY A  1 82  ? 11.591  -14.882 -3.138  1.00 29.76  ?  113  GLY A O   1 
ATOM   522   N  N   . THR A  1 83  ? 11.758  -12.640 -3.278  1.00 27.71  ?  114  THR A N   1 
ATOM   523   C  CA  . THR A  1 83  ? 10.725  -12.382 -2.285  1.00 27.88  ?  114  THR A CA  1 
ATOM   524   C  C   . THR A  1 83  ? 9.527   -11.643 -2.892  1.00 28.10  ?  114  THR A C   1 
ATOM   525   O  O   . THR A  1 83  ? 8.876   -10.834 -2.224  1.00 28.87  ?  114  THR A O   1 
ATOM   526   C  CB  . THR A  1 83  ? 11.300  -11.594 -1.120  1.00 29.07  ?  114  THR A CB  1 
ATOM   527   O  OG1 . THR A  1 83  ? 11.859  -10.372 -1.615  1.00 29.04  ?  114  THR A OG1 1 
ATOM   528   C  CG2 . THR A  1 83  ? 12.407  -12.428 -0.359  1.00 27.91  ?  114  THR A CG2 1 
ATOM   529   N  N   . ALA A  1 84  ? 9.212   -11.940 -4.146  1.00 26.39  ?  115  ALA A N   1 
ATOM   530   C  CA  . ALA A  1 84  ? 8.138   -11.280 -4.894  1.00 28.71  ?  115  ALA A CA  1 
ATOM   531   C  C   . ALA A  1 84  ? 6.743   -11.868 -4.665  1.00 28.76  ?  115  ALA A C   1 
ATOM   532   O  O   . ALA A  1 84  ? 5.776   -11.357 -5.246  1.00 27.86  ?  115  ALA A O   1 
ATOM   533   C  CB  . ALA A  1 84  ? 8.451   -11.309 -6.397  1.00 30.12  ?  115  ALA A CB  1 
ATOM   534   N  N   . TYR A  1 85  ? 6.606   -12.929 -3.875  1.00 27.20  ?  116  TYR A N   1 
ATOM   535   C  CA  . TYR A  1 85  ? 5.314   -13.419 -3.410  1.00 31.61  ?  116  TYR A CA  1 
ATOM   536   C  C   . TYR A  1 85  ? 5.208   -13.240 -1.897  1.00 28.63  ?  116  TYR A C   1 
ATOM   537   O  O   . TYR A  1 85  ? 6.224   -13.211 -1.183  1.00 29.17  ?  116  TYR A O   1 
ATOM   538   C  CB  . TYR A  1 85  ? 5.111   -14.906 -3.750  1.00 29.62  ?  116  TYR A CB  1 
ATOM   539   C  CG  . TYR A  1 85  ? 4.883   -15.248 -5.218  1.00 31.28  ?  116  TYR A CG  1 
ATOM   540   C  CD1 . TYR A  1 85  ? 3.603   -15.268 -5.758  1.00 28.30  ?  116  TYR A CD1 1 
ATOM   541   C  CD2 . TYR A  1 85  ? 5.943   -15.587 -6.048  1.00 30.69  ?  116  TYR A CD2 1 
ATOM   542   C  CE1 . TYR A  1 85  ? 3.391   -15.599 -7.099  1.00 32.55  ?  116  TYR A CE1 1 
ATOM   543   C  CE2 . TYR A  1 85  ? 5.741   -15.917 -7.378  1.00 30.93  ?  116  TYR A CE2 1 
ATOM   544   C  CZ  . TYR A  1 85  ? 4.463   -15.930 -7.894  1.00 31.74  ?  116  TYR A CZ  1 
ATOM   545   O  OH  . TYR A  1 85  ? 4.261   -16.275 -9.210  1.00 30.69  ?  116  TYR A OH  1 
ATOM   546   N  N   . ASN A  1 86  ? 3.979   -13.145 -1.399  1.00 27.72  ?  117  ASN A N   1 
ATOM   547   C  CA  . ASN A  1 86  ? 3.787   -13.122 0.047   1.00 30.54  ?  117  ASN A CA  1 
ATOM   548   C  C   . ASN A  1 86  ? 4.137   -14.483 0.655   1.00 29.99  ?  117  ASN A C   1 
ATOM   549   O  O   . ASN A  1 86  ? 3.899   -15.538 0.055   1.00 27.63  ?  117  ASN A O   1 
ATOM   550   C  CB  . ASN A  1 86  ? 2.336   -12.794 0.412   1.00 27.32  ?  117  ASN A CB  1 
ATOM   551   C  CG  . ASN A  1 86  ? 2.069   -11.271 0.573   1.00 29.67  ?  117  ASN A CG  1 
ATOM   552   O  OD1 . ASN A  1 86  ? 2.961   -10.437 0.425   1.00 26.92  ?  117  ASN A OD1 1 
ATOM   553   N  ND2 . ASN A  1 86  ? 0.812   -10.926 0.866   1.00 32.55  ?  117  ASN A ND2 1 
ATOM   554   N  N   . LEU A  1 87  ? 4.699   -14.446 1.861   1.00 26.97  ?  118  LEU A N   1 
ATOM   555   C  CA  . LEU A  1 87  ? 4.636   -15.600 2.758   1.00 30.90  ?  118  LEU A CA  1 
ATOM   556   C  C   . LEU A  1 87  ? 3.183   -15.919 3.097   1.00 29.52  ?  118  LEU A C   1 
ATOM   557   O  O   . LEU A  1 87  ? 2.365   -15.011 3.270   1.00 30.63  ?  118  LEU A O   1 
ATOM   558   C  CB  . LEU A  1 87  ? 5.419   -15.292 4.041   1.00 31.81  ?  118  LEU A CB  1 
ATOM   559   C  CG  . LEU A  1 87  ? 6.928   -15.177 3.859   1.00 31.73  ?  118  LEU A CG  1 
ATOM   560   C  CD1 . LEU A  1 87  ? 7.530   -14.573 5.088   1.00 28.65  ?  118  LEU A CD1 1 
ATOM   561   C  CD2 . LEU A  1 87  ? 7.542   -16.560 3.571   1.00 32.70  ?  118  LEU A CD2 1 
ATOM   562   N  N   . PHE A  1 88  ? 2.849   -17.210 3.187   1.00 29.48  ?  119  PHE A N   1 
ATOM   563   C  CA  . PHE A  1 88  ? 1.479   -17.608 3.508   1.00 29.64  ?  119  PHE A CA  1 
ATOM   564   C  C   . PHE A  1 88  ? 1.172   -17.358 4.985   1.00 34.04  ?  119  PHE A C   1 
ATOM   565   O  O   . PHE A  1 88  ? 2.065   -17.149 5.814   1.00 32.16  ?  119  PHE A O   1 
ATOM   566   C  CB  . PHE A  1 88  ? 1.254   -19.086 3.191   1.00 30.02  ?  119  PHE A CB  1 
ATOM   567   C  CG  . PHE A  1 88  ? -0.170  -19.441 2.807   1.00 32.45  ?  119  PHE A CG  1 
ATOM   568   C  CD1 . PHE A  1 88  ? -0.688  -19.085 1.546   1.00 32.43  ?  119  PHE A CD1 1 
ATOM   569   C  CD2 . PHE A  1 88  ? -0.985  -20.160 3.680   1.00 30.93  ?  119  PHE A CD2 1 
ATOM   570   C  CE1 . PHE A  1 88  ? -2.006  -19.436 1.161   1.00 30.89  ?  119  PHE A CE1 1 
ATOM   571   C  CE2 . PHE A  1 88  ? -2.301  -20.510 3.314   1.00 34.21  ?  119  PHE A CE2 1 
ATOM   572   C  CZ  . PHE A  1 88  ? -2.816  -20.146 2.050   1.00 32.50  ?  119  PHE A CZ  1 
ATOM   573   N  N   . HIS A  1 89  ? -0.113  -17.477 5.272   1.00 30.02  ?  120  HIS A N   1 
ATOM   574   C  CA  . HIS A  1 89  ? -0.559  -17.400 6.671   1.00 33.38  ?  120  HIS A CA  1 
ATOM   575   C  C   . HIS A  1 89  ? 0.159   -18.491 7.459   1.00 31.54  ?  120  HIS A C   1 
ATOM   576   O  O   . HIS A  1 89  ? 0.294   -19.608 6.954   1.00 30.67  ?  120  HIS A O   1 
ATOM   577   C  CB  . HIS A  1 89  ? -2.061  -17.679 6.746   1.00 31.03  ?  120  HIS A CB  1 
ATOM   578   C  CG  . HIS A  1 89  ? -2.895  -16.940 5.753   1.00 43.04  ?  120  HIS A CG  1 
ATOM   579   N  ND1 . HIS A  1 89  ? -3.273  -15.626 5.920   1.00 41.54  ?  120  HIS A ND1 1 
ATOM   580   C  CD2 . HIS A  1 89  ? -3.437  -17.331 4.595   1.00 43.25  ?  120  HIS A CD2 1 
ATOM   581   C  CE1 . HIS A  1 89  ? -4.008  -15.247 4.887   1.00 39.82  ?  120  HIS A CE1 1 
ATOM   582   N  NE2 . HIS A  1 89  ? -4.119  -16.267 4.071   1.00 37.42  ?  120  HIS A NE2 1 
ATOM   583   N  N   . ASN A  1 90  ? 0.630   -18.145 8.643   1.00 33.06  ?  121  ASN A N   1 
ATOM   584   C  CA  . ASN A  1 90  ? 1.232   -19.136 9.540   1.00 32.90  ?  121  ASN A CA  1 
ATOM   585   C  C   . ASN A  1 90  ? 2.414   -19.839 8.874   1.00 34.57  ?  121  ASN A C   1 
ATOM   586   O  O   . ASN A  1 90  ? 2.522   -21.066 8.930   1.00 35.18  ?  121  ASN A O   1 
ATOM   587   C  CB  . ASN A  1 90  ? 0.190   -20.182 9.979   1.00 33.05  ?  121  ASN A CB  1 
ATOM   588   C  CG  . ASN A  1 90  ? -0.952  -19.602 10.825  1.00 39.30  ?  121  ASN A CG  1 
ATOM   589   O  OD1 . ASN A  1 90  ? -1.798  -18.849 10.338  1.00 41.81  ?  121  ASN A OD1 1 
ATOM   590   N  ND2 . ASN A  1 90  ? -0.998  -19.993 12.093  1.00 38.87  ?  121  ASN A ND2 1 
ATOM   591   N  N   . SER A  1 91  ? 3.267   -19.073 8.187   1.00 32.84  ?  122  SER A N   1 
ATOM   592   C  CA  . SER A  1 91  ? 4.420   -19.643 7.495   1.00 35.26  ?  122  SER A CA  1 
ATOM   593   C  C   . SER A  1 91  ? 5.389   -20.245 8.511   1.00 35.89  ?  122  SER A C   1 
ATOM   594   O  O   . SER A  1 91  ? 5.349   -19.926 9.704   1.00 36.15  ?  122  SER A O   1 
ATOM   595   C  CB  . SER A  1 91  ? 5.141   -18.590 6.630   1.00 30.26  ?  122  SER A CB  1 
ATOM   596   O  OG  . SER A  1 91  ? 5.594   -17.483 7.408   1.00 30.74  ?  122  SER A OG  1 
ATOM   597   N  N   . SER A  1 92  ? 6.256   -21.138 8.025   1.00 37.63  ?  123  SER A N   1 
ATOM   598   C  CA  . SER A  1 92  ? 7.040   -21.983 8.931   1.00 39.80  ?  123  SER A CA  1 
ATOM   599   C  C   . SER A  1 92  ? 7.915   -21.157 9.852   1.00 35.17  ?  123  SER A C   1 
ATOM   600   O  O   . SER A  1 92  ? 8.595   -20.221 9.421   1.00 34.30  ?  123  SER A O   1 
ATOM   601   C  CB  . SER A  1 92  ? 7.929   -22.957 8.167   1.00 39.28  ?  123  SER A CB  1 
ATOM   602   O  OG  . SER A  1 92  ? 8.778   -23.612 9.093   1.00 43.86  ?  123  SER A OG  1 
ATOM   603   N  N   . GLU A  1 93  ? 7.912   -21.534 11.127  1.00 38.02  ?  124  GLU A N   1 
ATOM   604   C  CA  . GLU A  1 93  ? 8.743   -20.896 12.130  1.00 35.79  ?  124  GLU A CA  1 
ATOM   605   C  C   . GLU A  1 93  ? 10.040  -21.668 12.358  1.00 42.25  ?  124  GLU A C   1 
ATOM   606   O  O   . GLU A  1 93  ? 10.746  -21.405 13.332  1.00 42.00  ?  124  GLU A O   1 
ATOM   607   C  CB  . GLU A  1 93  ? 7.948   -20.745 13.431  1.00 42.71  ?  124  GLU A CB  1 
ATOM   608   C  CG  . GLU A  1 93  ? 6.557   -20.156 13.173  1.00 43.95  ?  124  GLU A CG  1 
ATOM   609   C  CD  . GLU A  1 93  ? 5.733   -19.851 14.430  1.00 56.81  ?  124  GLU A CD  1 
ATOM   610   O  OE1 . GLU A  1 93  ? 5.815   -20.598 15.432  1.00 53.89  ?  124  GLU A OE1 1 
ATOM   611   O  OE2 . GLU A  1 93  ? 4.930   -18.886 14.375  1.00 56.98  -1 124  GLU A OE2 1 
ATOM   612   N  N   . ASP A  1 94  ? 10.364  -22.611 11.476  1.00 44.01  ?  125  ASP A N   1 
ATOM   613   C  CA  . ASP A  1 94  ? 11.582  -23.404 11.567  1.00 41.42  ?  125  ASP A CA  1 
ATOM   614   C  C   . ASP A  1 94  ? 12.635  -22.832 10.636  1.00 41.74  ?  125  ASP A C   1 
ATOM   615   O  O   . ASP A  1 94  ? 12.391  -22.687 9.430   1.00 35.84  ?  125  ASP A O   1 
ATOM   616   C  CB  . ASP A  1 94  ? 11.323  -24.867 11.212  1.00 47.88  ?  125  ASP A CB  1 
ATOM   617   C  CG  . ASP A  1 94  ? 10.388  -25.544 12.187  1.00 52.64  ?  125  ASP A CG  1 
ATOM   618   O  OD1 . ASP A  1 94  ? 10.712  -25.567 13.395  1.00 54.72  ?  125  ASP A OD1 1 
ATOM   619   O  OD2 . ASP A  1 94  ? 9.338   -26.066 11.744  1.00 61.32  -1 125  ASP A OD2 1 
ATOM   620   N  N   . ASP A  1 95  ? 13.808  -22.524 11.199  1.00 37.89  ?  126  ASP A N   1 
ATOM   621   C  CA  . ASP A  1 95  ? 14.898  -21.974 10.403  1.00 41.65  ?  126  ASP A CA  1 
ATOM   622   C  C   . ASP A  1 95  ? 15.177  -22.831 9.179   1.00 41.03  ?  126  ASP A C   1 
ATOM   623   O  O   . ASP A  1 95  ? 15.478  -22.309 8.098   1.00 43.77  ?  126  ASP A O   1 
ATOM   624   C  CB  . ASP A  1 95  ? 16.170  -21.845 11.250  1.00 37.94  ?  126  ASP A CB  1 
ATOM   625   C  CG  . ASP A  1 95  ? 16.172  -20.593 12.116  1.00 46.10  ?  126  ASP A CG  1 
ATOM   626   O  OD1 . ASP A  1 95  ? 15.239  -19.770 11.971  1.00 41.63  ?  126  ASP A OD1 1 
ATOM   627   O  OD2 . ASP A  1 95  ? 17.127  -20.404 12.914  1.00 43.33  -1 126  ASP A OD2 1 
ATOM   628   N  N   . LYS A  1 96  ? 15.052  -24.155 9.324   1.00 40.93  ?  127  LYS A N   1 
ATOM   629   C  CA  . LYS A  1 96  ? 15.391  -25.061 8.235   1.00 40.82  ?  127  LYS A CA  1 
ATOM   630   C  C   . LYS A  1 96  ? 14.522  -24.842 7.001   1.00 41.98  ?  127  LYS A C   1 
ATOM   631   O  O   . LYS A  1 96  ? 14.956  -25.154 5.888   1.00 41.49  ?  127  LYS A O   1 
ATOM   632   C  CB  . LYS A  1 96  ? 15.277  -26.512 8.712   1.00 44.14  ?  127  LYS A CB  1 
ATOM   633   N  N   . ASP A  1 97  ? 13.319  -24.303 7.164   1.00 44.01  ?  128  ASP A N   1 
ATOM   634   C  CA  . ASP A  1 97  ? 12.431  -24.099 6.029   1.00 39.88  ?  128  ASP A CA  1 
ATOM   635   C  C   . ASP A  1 97  ? 12.684  -22.788 5.287   1.00 40.09  ?  128  ASP A C   1 
ATOM   636   O  O   . ASP A  1 97  ? 12.116  -22.595 4.207   1.00 39.66  ?  128  ASP A O   1 
ATOM   637   C  CB  . ASP A  1 97  ? 10.979  -24.174 6.497   1.00 41.55  ?  128  ASP A CB  1 
ATOM   638   C  CG  . ASP A  1 97  ? 10.568  -25.586 6.870   1.00 49.78  ?  128  ASP A CG  1 
ATOM   639   O  OD1 . ASP A  1 97  ? 11.025  -26.543 6.190   1.00 45.70  ?  128  ASP A OD1 1 
ATOM   640   O  OD2 . ASP A  1 97  ? 9.803   -25.740 7.851   1.00 48.55  -1 128  ASP A OD2 1 
ATOM   641   N  N   . ASN A  1 98  ? 13.521  -21.888 5.821   1.00 38.22  ?  129  ASN A N   1 
ATOM   642   C  CA  . ASN A  1 98  ? 13.934  -20.673 5.089   1.00 40.17  ?  129  ASN A CA  1 
ATOM   643   C  C   . ASN A  1 98  ? 12.749  -19.880 4.531   1.00 36.50  ?  129  ASN A C   1 
ATOM   644   O  O   . ASN A  1 98  ? 12.843  -19.260 3.472   1.00 35.87  ?  129  ASN A O   1 
ATOM   645   C  CB  . ASN A  1 98  ? 14.900  -21.013 3.957   1.00 39.08  ?  129  ASN A CB  1 
ATOM   646   C  CG  . ASN A  1 98  ? 16.259  -21.397 4.474   1.00 48.18  ?  129  ASN A CG  1 
ATOM   647   O  OD1 . ASN A  1 98  ? 16.820  -22.428 4.100   1.00 53.03  ?  129  ASN A OD1 1 
ATOM   648   N  ND2 . ASN A  1 98  ? 16.801  -20.562 5.351   1.00 44.67  ?  129  ASN A ND2 1 
ATOM   649   N  N   . MET A  1 99  ? 11.634  -19.874 5.249   1.00 34.17  ?  130  MET A N   1 
ATOM   650   C  CA  . MET A  1 99  ? 10.461  -19.095 4.837   1.00 34.81  ?  130  MET A CA  1 
ATOM   651   C  C   . MET A  1 99  ? 10.642  -17.659 5.328   1.00 30.45  ?  130  MET A C   1 
ATOM   652   O  O   . MET A  1 99  ? 10.053  -17.234 6.326   1.00 30.69  ?  130  MET A O   1 
ATOM   653   C  CB  . MET A  1 99  ? 9.198   -19.724 5.409   1.00 32.13  ?  130  MET A CB  1 
ATOM   654   C  CG  . MET A  1 99  ? 8.481   -20.740 4.535   1.00 40.20  ?  130  MET A CG  1 
ATOM   655   S  SD  . MET A  1 99  ? 8.302   -20.414 2.747   1.00 40.38  ?  130  MET A SD  1 
ATOM   656   C  CE  . MET A  1 99  ? 7.871   -22.058 2.180   1.00 37.83  ?  130  MET A CE  1 
ATOM   657   N  N   . GLY A  1 100 ? 11.499  -16.911 4.635   1.00 29.66  ?  131  GLY A N   1 
ATOM   658   C  CA  . GLY A  1 100 ? 11.785  -15.547 5.046   1.00 28.50  ?  131  GLY A CA  1 
ATOM   659   C  C   . GLY A  1 100 ? 12.797  -14.896 4.127   1.00 30.68  ?  131  GLY A C   1 
ATOM   660   O  O   . GLY A  1 100 ? 13.480  -15.557 3.340   1.00 31.94  ?  131  GLY A O   1 
ATOM   661   N  N   . VAL A  1 101 ? 12.905  -13.577 4.261   1.00 30.10  ?  132  VAL A N   1 
ATOM   662   C  CA  . VAL A  1 101 ? 13.823  -12.814 3.413   1.00 27.10  ?  132  VAL A CA  1 
ATOM   663   C  C   . VAL A  1 101 ? 15.256  -13.267 3.688   1.00 32.71  ?  132  VAL A C   1 
ATOM   664   O  O   . VAL A  1 101 ? 15.657  -13.349 4.860   1.00 31.27  ?  132  VAL A O   1 
ATOM   665   C  CB  . VAL A  1 101 ? 13.665  -11.309 3.675   1.00 31.13  ?  132  VAL A CB  1 
ATOM   666   C  CG1 . VAL A  1 101 ? 14.710  -10.526 2.895   1.00 28.85  ?  132  VAL A CG1 1 
ATOM   667   C  CG2 . VAL A  1 101 ? 12.223  -10.848 3.304   1.00 31.70  ?  132  VAL A CG2 1 
ATOM   668   N  N   . PRO A  1 102 ? 16.071  -13.535 2.671   1.00 33.79  ?  133  PRO A N   1 
ATOM   669   C  CA  . PRO A  1 102 ? 17.400  -14.120 2.909   1.00 32.47  ?  133  PRO A CA  1 
ATOM   670   C  C   . PRO A  1 102 ? 18.228  -13.338 3.916   1.00 33.93  ?  133  PRO A C   1 
ATOM   671   O  O   . PRO A  1 102 ? 18.393  -12.119 3.803   1.00 33.38  ?  133  PRO A O   1 
ATOM   672   C  CB  . PRO A  1 102 ? 18.048  -14.084 1.524   1.00 34.94  ?  133  PRO A CB  1 
ATOM   673   C  CG  . PRO A  1 102 ? 16.871  -14.158 0.559   1.00 38.82  ?  133  PRO A CG  1 
ATOM   674   C  CD  . PRO A  1 102 ? 15.784  -13.358 1.236   1.00 32.96  ?  133  PRO A CD  1 
ATOM   675   N  N   . VAL A  1 103 ? 18.798  -14.062 4.887   1.00 37.60  ?  134  VAL A N   1 
ATOM   676   C  CA  . VAL A  1 103 ? 19.542  -13.402 5.957   1.00 34.62  ?  134  VAL A CA  1 
ATOM   677   C  C   . VAL A  1 103 ? 20.755  -12.645 5.436   1.00 32.93  ?  134  VAL A C   1 
ATOM   678   O  O   . VAL A  1 103 ? 21.201  -11.683 6.075   1.00 37.01  ?  134  VAL A O   1 
ATOM   679   C  CB  . VAL A  1 103 ? 19.935  -14.427 7.027   1.00 37.24  ?  134  VAL A CB  1 
ATOM   680   C  CG1 . VAL A  1 103 ? 18.682  -14.917 7.738   1.00 31.97  ?  134  VAL A CG1 1 
ATOM   681   C  CG2 . VAL A  1 103 ? 20.719  -15.595 6.402   1.00 37.44  ?  134  VAL A CG2 1 
ATOM   682   N  N   . GLU A  1 104 ? 21.276  -13.024 4.268   1.00 35.15  ?  135  GLU A N   1 
ATOM   683   C  CA  . GLU A  1 104 ? 22.444  -12.373 3.669   1.00 36.02  ?  135  GLU A CA  1 
ATOM   684   C  C   . GLU A  1 104 ? 22.149  -10.984 3.110   1.00 42.06  ?  135  GLU A C   1 
ATOM   685   O  O   . GLU A  1 104 ? 23.092  -10.230 2.816   1.00 34.72  ?  135  GLU A O   1 
ATOM   686   C  CB  . GLU A  1 104 ? 22.997  -13.261 2.550   1.00 44.35  ?  135  GLU A CB  1 
ATOM   687   C  CG  . GLU A  1 104 ? 22.857  -14.767 2.852   1.00 49.47  ?  135  GLU A CG  1 
ATOM   688   C  CD  . GLU A  1 104 ? 21.591  -15.383 2.256   1.00 51.10  ?  135  GLU A CD  1 
ATOM   689   O  OE1 . GLU A  1 104 ? 21.289  -15.134 1.058   1.00 62.67  ?  135  GLU A OE1 1 
ATOM   690   O  OE2 . GLU A  1 104 ? 20.873  -16.097 2.997   1.00 56.52  -1 135  GLU A OE2 1 
ATOM   691   N  N   . GLU A  1 105 ? 20.871  -10.644 2.909   1.00 37.68  ?  136  GLU A N   1 
ATOM   692   C  CA  . GLU A  1 105 ? 20.485  -9.337  2.381   1.00 35.96  ?  136  GLU A CA  1 
ATOM   693   C  C   . GLU A  1 105 ? 20.370  -8.381  3.552   1.00 36.76  ?  136  GLU A C   1 
ATOM   694   O  O   . GLU A  1 105 ? 19.310  -8.242  4.158   1.00 38.43  ?  136  GLU A O   1 
ATOM   695   C  CB  . GLU A  1 105 ? 19.163  -9.418  1.626   1.00 38.06  ?  136  GLU A CB  1 
ATOM   696   C  CG  . GLU A  1 105 ? 19.281  -9.649  0.161   1.00 39.23  ?  136  GLU A CG  1 
ATOM   697   C  CD  . GLU A  1 105 ? 20.111  -8.605  -0.565  1.00 38.11  ?  136  GLU A CD  1 
ATOM   698   O  OE1 . GLU A  1 105 ? 20.378  -7.509  -0.034  1.00 41.73  ?  136  GLU A OE1 1 
ATOM   699   O  OE2 . GLU A  1 105 ? 20.506  -8.895  -1.700  1.00 40.17  -1 136  GLU A OE2 1 
ATOM   700   N  N   . THR A  1 106 ? 21.464  -7.688  3.856   1.00 35.76  ?  137  THR A N   1 
ATOM   701   C  CA  . THR A  1 106 ? 21.523  -6.882  5.067   1.00 32.84  ?  137  THR A CA  1 
ATOM   702   C  C   . THR A  1 106 ? 20.512  -5.739  5.061   1.00 33.35  ?  137  THR A C   1 
ATOM   703   O  O   . THR A  1 106 ? 20.515  -4.901  4.149   1.00 32.08  ?  137  THR A O   1 
ATOM   704   C  CB  . THR A  1 106 ? 22.934  -6.336  5.238   1.00 36.20  ?  137  THR A CB  1 
ATOM   705   O  OG1 . THR A  1 106 ? 23.851  -7.434  5.148   1.00 36.89  ?  137  THR A OG1 1 
ATOM   706   C  CG2 . THR A  1 106 ? 23.071  -5.643  6.585   1.00 35.88  ?  137  THR A CG2 1 
ATOM   707   N  N   . TYR A  1 107 ? 19.696  -5.682  6.122   1.00 32.66  ?  138  TYR A N   1 
ATOM   708   C  CA  . TYR A  1 107 ? 18.667  -4.655  6.279   1.00 29.24  ?  138  TYR A CA  1 
ATOM   709   C  C   . TYR A  1 107 ? 19.276  -3.325  6.683   1.00 36.20  ?  138  TYR A C   1 
ATOM   710   O  O   . TYR A  1 107 ? 20.270  -3.254  7.421   1.00 30.07  ?  138  TYR A O   1 
ATOM   711   C  CB  . TYR A  1 107 ? 17.666  -5.051  7.360   1.00 28.03  ?  138  TYR A CB  1 
ATOM   712   C  CG  . TYR A  1 107 ? 16.697  -6.153  6.990   1.00 32.00  ?  138  TYR A CG  1 
ATOM   713   C  CD1 . TYR A  1 107 ? 16.767  -6.803  5.759   1.00 28.52  ?  138  TYR A CD1 1 
ATOM   714   C  CD2 . TYR A  1 107 ? 15.717  -6.554  7.889   1.00 28.57  ?  138  TYR A CD2 1 
ATOM   715   C  CE1 . TYR A  1 107 ? 15.879  -7.822  5.453   1.00 30.84  ?  138  TYR A CE1 1 
ATOM   716   C  CE2 . TYR A  1 107 ? 14.844  -7.551  7.587   1.00 30.66  ?  138  TYR A CE2 1 
ATOM   717   C  CZ  . TYR A  1 107 ? 14.924  -8.188  6.377   1.00 30.53  ?  138  TYR A CZ  1 
ATOM   718   O  OH  . TYR A  1 107 ? 14.013  -9.185  6.107   1.00 27.76  ?  138  TYR A OH  1 
ATOM   719   N  N   . MET A  1 108 ? 18.636  -2.254  6.241   1.00 28.19  ?  139  MET A N   1 
ATOM   720   C  CA  . MET A  1 108 ? 19.082  -0.927  6.649   1.00 31.76  ?  139  MET A CA  1 
ATOM   721   C  C   . MET A  1 108 ? 19.092  -0.744  8.168   1.00 33.64  ?  139  MET A C   1 
ATOM   722   O  O   . MET A  1 108 ? 19.913  0.031   8.687   1.00 32.58  ?  139  MET A O   1 
ATOM   723   C  CB  . MET A  1 108 ? 18.238  0.106   5.912   1.00 32.28  ?  139  MET A CB  1 
ATOM   724   C  CG  . MET A  1 108 ? 16.827  0.311   6.446   1.00 34.18  ?  139  MET A CG  1 
ATOM   725   S  SD  . MET A  1 108 ? 16.158  1.726   5.587   1.00 34.17  ?  139  MET A SD  1 
ATOM   726   C  CE  . MET A  1 108 ? 14.398  1.291   5.469   1.00 34.46  ?  139  MET A CE  1 
ATOM   727   N  N   . SER A  1 109 ? 18.234  -1.467  8.900   1.00 26.63  ?  140  SER A N   1 
ATOM   728   C  CA  . SER A  1 109 ? 18.244  -1.392  10.359  1.00 31.97  ?  140  SER A CA  1 
ATOM   729   C  C   . SER A  1 109 ? 19.592  -1.838  10.933  1.00 31.57  ?  140  SER A C   1 
ATOM   730   O  O   . SER A  1 109 ? 20.170  -1.160  11.786  1.00 31.40  ?  140  SER A O   1 
ATOM   731   C  CB  . SER A  1 109 ? 17.122  -2.255  10.919  1.00 30.29  ?  140  SER A CB  1 
ATOM   732   O  OG  . SER A  1 109 ? 17.004  -3.418  10.117  1.00 31.54  ?  140  SER A OG  1 
ATOM   733   N  N   . LYS A  1 110 ? 20.093  -2.989  10.480  1.00 34.85  ?  141  LYS A N   1 
ATOM   734   C  CA  . LYS A  1 110 ? 21.423  -3.451  10.874  1.00 32.80  ?  141  LYS A CA  1 
ATOM   735   C  C   . LYS A  1 110 ? 22.497  -2.426  10.544  1.00 35.61  ?  141  LYS A C   1 
ATOM   736   O  O   . LYS A  1 110 ? 23.389  -2.157  11.356  1.00 37.99  ?  141  LYS A O   1 
ATOM   737   C  CB  . LYS A  1 110 ? 21.730  -4.781  10.188  1.00 34.59  ?  141  LYS A CB  1 
ATOM   738   C  CG  . LYS A  1 110 ? 22.939  -5.505  10.776  1.00 38.09  ?  141  LYS A CG  1 
ATOM   739   C  CD  . LYS A  1 110 ? 22.961  -6.938  10.316  1.00 45.42  ?  141  LYS A CD  1 
ATOM   740   C  CE  . LYS A  1 110 ? 22.228  -7.829  11.315  1.00 48.86  ?  141  LYS A CE  1 
ATOM   741   N  NZ  . LYS A  1 110 ? 23.082  -8.000  12.533  1.00 52.64  ?  141  LYS A NZ  1 
ATOM   742   N  N   . VAL A  1 111 ? 22.451  -1.859  9.344   1.00 34.47  ?  142  VAL A N   1 
ATOM   743   C  CA  . VAL A  1 111 ? 23.454  -0.863  8.980   1.00 34.24  ?  142  VAL A CA  1 
ATOM   744   C  C   . VAL A  1 111 ? 23.412  0.309   9.951   1.00 36.95  ?  142  VAL A C   1 
ATOM   745   O  O   . VAL A  1 111 ? 24.450  0.782   10.426  1.00 32.00  ?  142  VAL A O   1 
ATOM   746   C  CB  . VAL A  1 111 ? 23.244  -0.411  7.524   1.00 33.10  ?  142  VAL A CB  1 
ATOM   747   C  CG1 . VAL A  1 111 ? 24.285  0.610   7.138   1.00 37.39  ?  142  VAL A CG1 1 
ATOM   748   C  CG2 . VAL A  1 111 ? 23.337  -1.605  6.603   1.00 30.78  ?  142  VAL A CG2 1 
ATOM   749   N  N   . LEU A  1 112 ? 22.210  0.770   10.287  1.00 30.12  ?  143  LEU A N   1 
ATOM   750   C  CA  . LEU A  1 112 ? 22.063  1.905   11.189  1.00 32.35  ?  143  LEU A CA  1 
ATOM   751   C  C   . LEU A  1 112 ? 22.492  1.523   12.599  1.00 33.35  ?  143  LEU A C   1 
ATOM   752   O  O   . LEU A  1 112 ? 23.119  2.317   13.308  1.00 34.56  ?  143  LEU A O   1 
ATOM   753   C  CB  . LEU A  1 112 ? 20.600  2.358   11.174  1.00 28.87  ?  143  LEU A CB  1 
ATOM   754   C  CG  . LEU A  1 112 ? 20.249  3.047   9.837   1.00 30.98  ?  143  LEU A CG  1 
ATOM   755   C  CD1 . LEU A  1 112 ? 18.746  3.288   9.696   1.00 36.73  ?  143  LEU A CD1 1 
ATOM   756   C  CD2 . LEU A  1 112 ? 20.967  4.330   9.681   1.00 34.69  ?  143  LEU A CD2 1 
ATOM   757   N  N   . GLN A  1 113 ? 22.155  0.301   13.011  1.00 32.45  ?  144  GLN A N   1 
ATOM   758   C  CA  . GLN A  1 113 ? 22.534  -0.191  14.323  1.00 35.48  ?  144  GLN A CA  1 
ATOM   759   C  C   . GLN A  1 113 ? 24.049  -0.225  14.478  1.00 39.07  ?  144  GLN A C   1 
ATOM   760   O  O   . GLN A  1 113 ? 24.594  0.182   15.517  1.00 39.02  ?  144  GLN A O   1 
ATOM   761   C  CB  . GLN A  1 113 ? 21.959  -1.585  14.518  1.00 34.86  ?  144  GLN A CB  1 
ATOM   762   C  CG  . GLN A  1 113 ? 22.048  -2.066  15.932  1.00 36.86  ?  144  GLN A CG  1 
ATOM   763   C  CD  . GLN A  1 113 ? 21.628  -3.484  16.023  1.00 36.91  ?  144  GLN A CD  1 
ATOM   764   O  OE1 . GLN A  1 113 ? 22.052  -4.306  15.211  1.00 40.19  ?  144  GLN A OE1 1 
ATOM   765   N  NE2 . GLN A  1 113 ? 20.760  -3.793  16.982  1.00 38.12  ?  144  GLN A NE2 1 
ATOM   766   N  N   . ASN A  1 114 ? 24.746  -0.728  13.455  1.00 37.34  ?  145  ASN A N   1 
ATOM   767   C  CA  . ASN A  1 114 ? 26.206  -0.732  13.476  1.00 38.98  ?  145  ASN A CA  1 
ATOM   768   C  C   . ASN A  1 114 ? 26.805  0.659   13.440  1.00 40.80  ?  145  ASN A C   1 
ATOM   769   O  O   . ASN A  1 114 ? 27.967  0.823   13.828  1.00 44.79  ?  145  ASN A O   1 
ATOM   770   C  CB  . ASN A  1 114 ? 26.740  -1.554  12.316  1.00 40.33  ?  145  ASN A CB  1 
ATOM   771   C  CG  . ASN A  1 114 ? 26.333  -2.987  12.406  1.00 41.15  ?  145  ASN A CG  1 
ATOM   772   O  OD1 . ASN A  1 114 ? 25.995  -3.469  13.491  1.00 46.69  ?  145  ASN A OD1 1 
ATOM   773   N  ND2 . ASN A  1 114 ? 26.365  -3.699  11.272  1.00 47.82  ?  145  ASN A ND2 1 
ATOM   774   N  N   . ALA A  1 115 ? 26.064  1.659   12.982  1.00 35.26  ?  146  ALA A N   1 
ATOM   775   C  CA  . ALA A  1 115 ? 26.550  3.030   12.986  1.00 33.28  ?  146  ALA A CA  1 
ATOM   776   C  C   . ALA A  1 115 ? 26.162  3.779   14.247  1.00 33.41  ?  146  ALA A C   1 
ATOM   777   O  O   . ALA A  1 115 ? 26.315  5.005   14.299  1.00 36.16  ?  146  ALA A O   1 
ATOM   778   C  CB  . ALA A  1 115 ? 26.049  3.787   11.755  1.00 38.85  ?  146  ALA A CB  1 
ATOM   779   N  N   . GLY A  1 116 ? 25.658  3.078   15.255  1.00 37.28  ?  147  GLY A N   1 
ATOM   780   C  CA  . GLY A  1 116 ? 25.405  3.677   16.548  1.00 34.24  ?  147  GLY A CA  1 
ATOM   781   C  C   . GLY A  1 116 ? 23.980  4.111   16.811  1.00 35.01  ?  147  GLY A C   1 
ATOM   782   O  O   . GLY A  1 116 ? 23.736  4.782   17.814  1.00 32.44  ?  147  GLY A O   1 
ATOM   783   N  N   . TYR A  1 117 ? 23.033  3.782   15.938  1.00 33.15  ?  148  TYR A N   1 
ATOM   784   C  CA  . TYR A  1 117 ? 21.658  4.159   16.216  1.00 29.69  ?  148  TYR A CA  1 
ATOM   785   C  C   . TYR A  1 117 ? 21.015  3.176   17.179  1.00 28.30  ?  148  TYR A C   1 
ATOM   786   O  O   . TYR A  1 117 ? 21.289  1.976   17.151  1.00 31.26  ?  148  TYR A O   1 
ATOM   787   C  CB  . TYR A  1 117 ? 20.831  4.205   14.924  1.00 30.27  ?  148  TYR A CB  1 
ATOM   788   C  CG  . TYR A  1 117 ? 20.927  5.506   14.177  1.00 30.93  ?  148  TYR A CG  1 
ATOM   789   C  CD1 . TYR A  1 117 ? 22.145  5.968   13.704  1.00 32.11  ?  148  TYR A CD1 1 
ATOM   790   C  CD2 . TYR A  1 117 ? 19.789  6.253   13.898  1.00 28.08  ?  148  TYR A CD2 1 
ATOM   791   C  CE1 . TYR A  1 117 ? 22.237  7.158   12.993  1.00 31.49  ?  148  TYR A CE1 1 
ATOM   792   C  CE2 . TYR A  1 117 ? 19.865  7.442   13.193  1.00 28.64  ?  148  TYR A CE2 1 
ATOM   793   C  CZ  . TYR A  1 117 ? 21.089  7.891   12.746  1.00 33.37  ?  148  TYR A CZ  1 
ATOM   794   O  OH  . TYR A  1 117 ? 21.154  9.070   12.041  1.00 31.82  ?  148  TYR A OH  1 
ATOM   795   N  N   . TYR A  1 118 ? 20.128  3.700   18.018  1.00 28.26  ?  149  TYR A N   1 
ATOM   796   C  CA  . TYR A  1 118 ? 19.155  2.878   18.731  1.00 30.24  ?  149  TYR A CA  1 
ATOM   797   C  C   . TYR A  1 118 ? 17.993  2.586   17.786  1.00 31.57  ?  149  TYR A C   1 
ATOM   798   O  O   . TYR A  1 118 ? 17.365  3.521   17.280  1.00 28.14  ?  149  TYR A O   1 
ATOM   799   C  CB  . TYR A  1 118 ? 18.646  3.610   19.967  1.00 29.63  ?  149  TYR A CB  1 
ATOM   800   C  CG  . TYR A  1 118 ? 17.475  2.939   20.636  1.00 32.23  ?  149  TYR A CG  1 
ATOM   801   C  CD1 . TYR A  1 118 ? 17.562  1.623   21.055  1.00 37.32  ?  149  TYR A CD1 1 
ATOM   802   C  CD2 . TYR A  1 118 ? 16.277  3.606   20.826  1.00 33.26  ?  149  TYR A CD2 1 
ATOM   803   C  CE1 . TYR A  1 118 ? 16.507  0.994   21.665  1.00 37.99  ?  149  TYR A CE1 1 
ATOM   804   C  CE2 . TYR A  1 118 ? 15.197  2.975   21.421  1.00 35.12  ?  149  TYR A CE2 1 
ATOM   805   C  CZ  . TYR A  1 118 ? 15.321  1.665   21.837  1.00 40.03  ?  149  TYR A CZ  1 
ATOM   806   O  OH  . TYR A  1 118 ? 14.278  1.012   22.457  1.00 36.90  ?  149  TYR A OH  1 
ATOM   807   N  N   . THR A  1 119 ? 17.706  1.308   17.556  1.00 31.61  ?  150  THR A N   1 
ATOM   808   C  CA  . THR A  1 119 ? 16.795  0.876   16.501  1.00 27.67  ?  150  THR A CA  1 
ATOM   809   C  C   . THR A  1 119 ? 15.617  0.112   17.090  1.00 32.03  ?  150  THR A C   1 
ATOM   810   O  O   . THR A  1 119 ? 15.787  -0.731  17.985  1.00 31.99  ?  150  THR A O   1 
ATOM   811   C  CB  . THR A  1 119 ? 17.492  -0.036  15.474  1.00 32.18  ?  150  THR A CB  1 
ATOM   812   O  OG1 . THR A  1 119 ? 17.947  -1.225  16.126  1.00 33.24  ?  150  THR A OG1 1 
ATOM   813   C  CG2 . THR A  1 119 ? 18.664  0.651   14.806  1.00 29.32  ?  150  THR A CG2 1 
ATOM   814   N  N   . SER A  1 120 ? 14.432  0.343   16.517  1.00 25.78  ?  151  SER A N   1 
ATOM   815   C  CA  . SER A  1 120 ? 13.206  -0.211  17.066  1.00 26.08  ?  151  SER A CA  1 
ATOM   816   C  C   . SER A  1 120 ? 12.264  -0.494  15.908  1.00 26.35  ?  151  SER A C   1 
ATOM   817   O  O   . SER A  1 120 ? 12.179  0.312   14.983  1.00 25.87  ?  151  SER A O   1 
ATOM   818   C  CB  . SER A  1 120 ? 12.548  0.771   18.049  1.00 28.37  ?  151  SER A CB  1 
ATOM   819   O  OG  . SER A  1 120 ? 11.161  0.480   18.212  1.00 41.12  ?  151  SER A OG  1 
ATOM   820   N  N   . ALA A  1 121 ? 11.600  -1.651  15.946  1.00 26.05  ?  152  ALA A N   1 
ATOM   821   C  CA  . ALA A  1 121 ? 10.528  -1.975  15.008  1.00 24.63  ?  152  ALA A CA  1 
ATOM   822   C  C   . ALA A  1 121 ? 9.257   -2.238  15.796  1.00 28.85  ?  152  ALA A C   1 
ATOM   823   O  O   . ALA A  1 121 ? 9.290   -2.911  16.828  1.00 28.93  ?  152  ALA A O   1 
ATOM   824   C  CB  . ALA A  1 121 ? 10.864  -3.212  14.162  1.00 25.64  ?  152  ALA A CB  1 
ATOM   825   N  N   . ILE A  1 122 ? 8.124   -1.743  15.290  1.00 26.79  ?  153  ILE A N   1 
ATOM   826   C  CA  . ILE A  1 122 ? 6.864   -1.830  16.012  1.00 23.89  ?  153  ILE A CA  1 
ATOM   827   C  C   . ILE A  1 122 ? 5.801   -2.202  14.993  1.00 25.49  ?  153  ILE A C   1 
ATOM   828   O  O   . ILE A  1 122 ? 5.791   -1.642  13.896  1.00 24.03  ?  153  ILE A O   1 
ATOM   829   C  CB  . ILE A  1 122 ? 6.510   -0.497  16.709  1.00 25.45  ?  153  ILE A CB  1 
ATOM   830   C  CG1 . ILE A  1 122 ? 7.611   -0.095  17.709  1.00 27.57  ?  153  ILE A CG1 1 
ATOM   831   C  CG2 . ILE A  1 122 ? 5.115   -0.580  17.394  1.00 25.59  ?  153  ILE A CG2 1 
ATOM   832   C  CD1 . ILE A  1 122 ? 7.588   1.363   18.120  1.00 27.56  ?  153  ILE A CD1 1 
ATOM   833   N  N   . GLY A  1 123 ? 4.981   -3.189  15.315  1.00 24.54  ?  154  GLY A N   1 
ATOM   834   C  CA  . GLY A  1 123 ? 3.789   -3.483  14.531  1.00 23.33  ?  154  GLY A CA  1 
ATOM   835   C  C   . GLY A  1 123 ? 3.960   -4.724  13.663  1.00 26.88  ?  154  GLY A C   1 
ATOM   836   O  O   . GLY A  1 123 ? 4.363   -5.785  14.148  1.00 28.76  ?  154  GLY A O   1 
ATOM   837   N  N   . LYS A  1 124 ? 3.637   -4.588  12.380  1.00 28.18  ?  155  LYS A N   1 
ATOM   838   C  CA  . LYS A  1 124 ? 3.690   -5.676  11.413  1.00 26.64  ?  155  LYS A CA  1 
ATOM   839   C  C   . LYS A  1 124 ? 5.103   -5.907  10.909  1.00 23.62  ?  155  LYS A C   1 
ATOM   840   O  O   . LYS A  1 124 ? 5.828   -4.954  10.615  1.00 26.66  ?  155  LYS A O   1 
ATOM   841   C  CB  . LYS A  1 124 ? 2.799   -5.346  10.204  1.00 25.60  ?  155  LYS A CB  1 
ATOM   842   C  CG  . LYS A  1 124 ? 2.831   -6.371  9.097   1.00 21.60  ?  155  LYS A CG  1 
ATOM   843   C  CD  . LYS A  1 124 ? 1.625   -6.121  8.131   1.00 23.00  ?  155  LYS A CD  1 
ATOM   844   C  CE  . LYS A  1 124 ? 1.828   -6.753  6.763   1.00 22.95  ?  155  LYS A CE  1 
ATOM   845   N  NZ  . LYS A  1 124 ? 0.467   -6.731  5.989   1.00 20.81  ?  155  LYS A NZ  1 
ATOM   846   N  N   . TRP A  1 125 ? 5.457   -7.185  10.727  1.00 24.55  ?  156  TRP A N   1 
ATOM   847   C  CA  . TRP A  1 125 ? 6.754   -7.588  10.183  1.00 29.36  ?  156  TRP A CA  1 
ATOM   848   C  C   . TRP A  1 125 ? 6.579   -8.162  8.772   1.00 24.68  ?  156  TRP A C   1 
ATOM   849   O  O   . TRP A  1 125 ? 6.833   -7.474  7.773   1.00 24.34  ?  156  TRP A O   1 
ATOM   850   C  CB  . TRP A  1 125 ? 7.407   -8.603  11.135  1.00 28.90  ?  156  TRP A CB  1 
ATOM   851   C  CG  . TRP A  1 125 ? 8.835   -9.027  10.845  1.00 29.94  ?  156  TRP A CG  1 
ATOM   852   C  CD1 . TRP A  1 125 ? 9.279   -10.309 10.620  1.00 29.93  ?  156  TRP A CD1 1 
ATOM   853   C  CD2 . TRP A  1 125 ? 10.004  -8.182  10.771  1.00 27.98  ?  156  TRP A CD2 1 
ATOM   854   N  NE1 . TRP A  1 125 ? 10.646  -10.309 10.422  1.00 27.07  ?  156  TRP A NE1 1 
ATOM   855   C  CE2 . TRP A  1 125 ? 11.112  -9.020  10.505  1.00 27.19  ?  156  TRP A CE2 1 
ATOM   856   C  CE3 . TRP A  1 125 ? 10.218  -6.803  10.898  1.00 26.22  ?  156  TRP A CE3 1 
ATOM   857   C  CZ2 . TRP A  1 125 ? 12.412  -8.522  10.355  1.00 27.12  ?  156  TRP A CZ2 1 
ATOM   858   C  CZ3 . TRP A  1 125 ? 11.505  -6.311  10.770  1.00 29.34  ?  156  TRP A CZ3 1 
ATOM   859   C  CH2 . TRP A  1 125 ? 12.592  -7.174  10.493  1.00 29.80  ?  156  TRP A CH2 1 
ATOM   860   N  N   . HIS A  1 126 ? 6.074   -9.398  8.693   1.00 25.09  ?  157  HIS A N   1 
ATOM   861   C  CA  . HIS A  1 126 ? 5.785   -10.066 7.387   1.00 27.71  ?  157  HIS A CA  1 
ATOM   862   C  C   . HIS A  1 126 ? 7.073   -10.370 6.600   1.00 29.85  ?  157  HIS A C   1 
ATOM   863   O  O   . HIS A  1 126 ? 7.013   -10.480 5.361   1.00 27.61  ?  157  HIS A O   1 
ATOM   864   C  CB  . HIS A  1 126 ? 4.776   -9.263  6.549   1.00 24.78  ?  157  HIS A CB  1 
ATOM   865   C  CG  . HIS A  1 126 ? 3.822   -10.104 5.769   1.00 25.80  ?  157  HIS A CG  1 
ATOM   866   N  ND1 . HIS A  1 126 ? 2.958   -9.609  4.816   1.00 30.66  ?  157  HIS A ND1 1 
ATOM   867   C  CD2 . HIS A  1 126 ? 3.609   -11.423 5.813   1.00 26.90  ?  157  HIS A CD2 1 
ATOM   868   C  CE1 . HIS A  1 126 ? 2.250   -10.611 4.310   1.00 27.02  ?  157  HIS A CE1 1 
ATOM   869   N  NE2 . HIS A  1 126 ? 2.626   -11.721 4.907   1.00 28.80  ?  157  HIS A NE2 1 
ATOM   870   N  N   . LEU A  1 127 ? 8.196   -10.539 7.305   1.00 29.64  ?  158  LEU A N   1 
ATOM   871   C  CA  . LEU A  1 127 ? 9.450   -10.799 6.615   1.00 31.18  ?  158  LEU A CA  1 
ATOM   872   C  C   . LEU A  1 127 ? 10.076  -12.115 7.066   1.00 30.95  ?  158  LEU A C   1 
ATOM   873   O  O   . LEU A  1 127 ? 11.258  -12.338 6.818   1.00 30.11  ?  158  LEU A O   1 
ATOM   874   C  CB  . LEU A  1 127 ? 10.437  -9.648  6.831   1.00 29.09  ?  158  LEU A CB  1 
ATOM   875   C  CG  . LEU A  1 127 ? 9.945   -8.252  6.412   1.00 31.45  ?  158  LEU A CG  1 
ATOM   876   C  CD1 . LEU A  1 127 ? 10.988  -7.180  6.773   1.00 28.44  ?  158  LEU A CD1 1 
ATOM   877   C  CD2 . LEU A  1 127 ? 9.607   -8.182  4.923   1.00 27.31  ?  158  LEU A CD2 1 
ATOM   878   N  N   . GLY A  1 128 ? 9.307   -12.983 7.719   1.00 31.63  ?  159  GLY A N   1 
ATOM   879   C  CA  . GLY A  1 128 ? 9.821   -14.249 8.201   1.00 32.30  ?  159  GLY A CA  1 
ATOM   880   C  C   . GLY A  1 128 ? 9.448   -14.530 9.642   1.00 27.63  ?  159  GLY A C   1 
ATOM   881   O  O   . GLY A  1 128 ? 9.634   -13.681 10.521  1.00 30.96  ?  159  GLY A O   1 
ATOM   882   N  N   . ALA A  1 129 ? 8.913   -15.716 9.906   1.00 27.85  ?  160  ALA A N   1 
ATOM   883   C  CA  . ALA A  1 129 ? 8.423   -16.040 11.236  1.00 32.03  ?  160  ALA A CA  1 
ATOM   884   C  C   . ALA A  1 129 ? 9.349   -16.991 11.982  1.00 38.07  ?  160  ALA A C   1 
ATOM   885   O  O   . ALA A  1 129 ? 8.987   -17.454 13.068  1.00 34.87  ?  160  ALA A O   1 
ATOM   886   C  CB  . ALA A  1 129 ? 7.023   -16.643 11.161  1.00 31.02  ?  160  ALA A CB  1 
ATOM   887   N  N   . ALA A  1 130 ? 10.523  -17.311 11.412  1.00 34.37  ?  161  ALA A N   1 
ATOM   888   C  CA  . ALA A  1 130 ? 11.513  -18.194 12.020  1.00 37.78  ?  161  ALA A CA  1 
ATOM   889   C  C   . ALA A  1 130 ? 12.604  -17.392 12.706  1.00 35.59  ?  161  ALA A C   1 
ATOM   890   O  O   . ALA A  1 130 ? 12.860  -16.235 12.351  1.00 33.32  ?  161  ALA A O   1 
ATOM   891   C  CB  . ALA A  1 130 ? 12.141  -19.118 10.965  1.00 38.30  ?  161  ALA A CB  1 
ATOM   892   N  N   . PRO A  1 131 ? 13.286  -17.989 13.702  1.00 35.69  ?  162  PRO A N   1 
ATOM   893   C  CA  . PRO A  1 131 ? 14.269  -17.220 14.482  1.00 32.95  ?  162  PRO A CA  1 
ATOM   894   C  C   . PRO A  1 131 ? 15.284  -16.462 13.657  1.00 31.45  ?  162  PRO A C   1 
ATOM   895   O  O   . PRO A  1 131 ? 15.556  -15.296 13.968  1.00 31.83  ?  162  PRO A O   1 
ATOM   896   C  CB  . PRO A  1 131 ? 14.927  -18.305 15.351  1.00 36.97  ?  162  PRO A CB  1 
ATOM   897   C  CG  . PRO A  1 131 ? 13.801  -19.243 15.617  1.00 37.67  ?  162  PRO A CG  1 
ATOM   898   C  CD  . PRO A  1 131 ? 13.070  -19.328 14.278  1.00 38.02  ?  162  PRO A CD  1 
ATOM   899   N  N   . LYS A  1 132 ? 15.855  -17.069 12.612  1.00 33.63  ?  163  LYS A N   1 
ATOM   900   C  CA  . LYS A  1 132 ? 16.871  -16.363 11.836  1.00 32.41  ?  163  LYS A CA  1 
ATOM   901   C  C   . LYS A  1 132 ? 16.320  -15.091 11.190  1.00 33.82  ?  163  LYS A C   1 
ATOM   902   O  O   . LYS A  1 132 ? 17.105  -14.203 10.823  1.00 28.65  ?  163  LYS A O   1 
ATOM   903   C  CB  . LYS A  1 132 ? 17.438  -17.275 10.750  1.00 35.55  ?  163  LYS A CB  1 
ATOM   904   C  CG  . LYS A  1 132 ? 16.368  -17.805 9.816   1.00 38.05  ?  163  LYS A CG  1 
ATOM   905   C  CD  . LYS A  1 132 ? 16.820  -18.964 8.934   1.00 39.72  ?  163  LYS A CD  1 
ATOM   906   C  CE  . LYS A  1 132 ? 18.069  -18.629 8.171   1.00 39.18  ?  163  LYS A CE  1 
ATOM   907   N  NZ  . LYS A  1 132 ? 18.502  -19.789 7.332   1.00 42.77  ?  163  LYS A NZ  1 
ATOM   908   N  N   . PHE A  1 133 ? 14.991  -14.984 11.054  1.00 31.18  ?  164  PHE A N   1 
ATOM   909   C  CA  . PHE A  1 133 ? 14.336  -13.877 10.362  1.00 34.19  ?  164  PHE A CA  1 
ATOM   910   C  C   . PHE A  1 133 ? 13.795  -12.830 11.309  1.00 36.50  ?  164  PHE A C   1 
ATOM   911   O  O   . PHE A  1 133 ? 13.233  -11.833 10.845  1.00 31.29  ?  164  PHE A O   1 
ATOM   912   C  CB  . PHE A  1 133 ? 13.177  -14.391 9.511   1.00 26.47  ?  164  PHE A CB  1 
ATOM   913   C  CG  . PHE A  1 133 ? 13.588  -15.394 8.483   1.00 29.19  ?  164  PHE A CG  1 
ATOM   914   C  CD1 . PHE A  1 133 ? 14.505  -15.067 7.508   1.00 28.94  ?  164  PHE A CD1 1 
ATOM   915   C  CD2 . PHE A  1 133 ? 13.068  -16.675 8.501   1.00 31.85  ?  164  PHE A CD2 1 
ATOM   916   C  CE1 . PHE A  1 133 ? 14.895  -15.984 6.578   1.00 29.32  ?  164  PHE A CE1 1 
ATOM   917   C  CE2 . PHE A  1 133 ? 13.470  -17.605 7.558   1.00 33.34  ?  164  PHE A CE2 1 
ATOM   918   C  CZ  . PHE A  1 133 ? 14.379  -17.252 6.603   1.00 27.84  ?  164  PHE A CZ  1 
ATOM   919   N  N   . HIS A  1 134 ? 13.955  -13.045 12.616  1.00 32.40  ?  165  HIS A N   1 
ATOM   920   C  CA  . HIS A  1 134 ? 13.335  -12.208 13.627  1.00 32.03  ?  165  HIS A CA  1 
ATOM   921   C  C   . HIS A  1 134 ? 13.935  -10.801 13.610  1.00 32.42  ?  165  HIS A C   1 
ATOM   922   O  O   . HIS A  1 134 ? 15.143  -10.639 13.381  1.00 34.50  ?  165  HIS A O   1 
ATOM   923   C  CB  . HIS A  1 134 ? 13.519  -12.861 15.005  1.00 32.22  ?  165  HIS A CB  1 
ATOM   924   C  CG  . HIS A  1 134 ? 12.734  -12.215 16.096  1.00 28.36  ?  165  HIS A CG  1 
ATOM   925   N  ND1 . HIS A  1 134 ? 13.093  -11.010 16.660  1.00 28.26  ?  165  HIS A ND1 1 
ATOM   926   C  CD2 . HIS A  1 134 ? 11.597  -12.602 16.721  1.00 29.25  ?  165  HIS A CD2 1 
ATOM   927   C  CE1 . HIS A  1 134 ? 12.206  -10.675 17.581  1.00 29.13  ?  165  HIS A CE1 1 
ATOM   928   N  NE2 . HIS A  1 134 ? 11.286  -11.624 17.635  1.00 34.75  ?  165  HIS A NE2 1 
ATOM   929   N  N   . PRO A  1 135 ? 13.122  -9.764  13.851  1.00 28.47  ?  166  PRO A N   1 
ATOM   930   C  CA  . PRO A  1 135 ? 13.672  -8.401  13.919  1.00 28.10  ?  166  PRO A CA  1 
ATOM   931   C  C   . PRO A  1 135 ? 14.928  -8.275  14.783  1.00 30.73  ?  166  PRO A C   1 
ATOM   932   O  O   . PRO A  1 135 ? 15.879  -7.592  14.384  1.00 31.53  ?  166  PRO A O   1 
ATOM   933   C  CB  . PRO A  1 135 ? 12.501  -7.612  14.506  1.00 29.11  ?  166  PRO A CB  1 
ATOM   934   C  CG  . PRO A  1 135 ? 11.282  -8.290  13.886  1.00 30.88  ?  166  PRO A CG  1 
ATOM   935   C  CD  . PRO A  1 135 ? 11.648  -9.771  13.966  1.00 31.04  ?  166  PRO A CD  1 
ATOM   936   N  N   . ASN A  1 136 ? 14.963  -8.926  15.949  1.00 30.75  ?  167  ASN A N   1 
ATOM   937   C  CA  . ASN A  1 136 ? 16.139  -8.809  16.833  1.00 32.39  ?  167  ASN A CA  1 
ATOM   938   C  C   . ASN A  1 136 ? 17.409  -9.355  16.185  1.00 33.81  ?  167  ASN A C   1 
ATOM   939   O  O   . ASN A  1 136 ? 18.517  -8.970  16.590  1.00 37.29  ?  167  ASN A O   1 
ATOM   940   C  CB  . ASN A  1 136 ? 15.910  -9.544  18.160  1.00 28.70  ?  167  ASN A CB  1 
ATOM   941   C  CG  . ASN A  1 136 ? 14.881  -8.869  19.064  1.00 31.02  ?  167  ASN A CG  1 
ATOM   942   O  OD1 . ASN A  1 136 ? 14.082  -9.550  19.708  1.00 33.53  ?  167  ASN A OD1 1 
ATOM   943   N  ND2 . ASN A  1 136 ? 14.899  -7.539  19.126  1.00 33.27  ?  167  ASN A ND2 1 
ATOM   944   N  N   . LYS A  1 137 ? 17.278  -10.258 15.208  1.00 34.50  ?  168  LYS A N   1 
ATOM   945   C  CA  . LYS A  1 137 ? 18.411  -10.754 14.436  1.00 36.54  ?  168  LYS A CA  1 
ATOM   946   C  C   . LYS A  1 137 ? 18.709  -9.912  13.214  1.00 35.72  ?  168  LYS A C   1 
ATOM   947   O  O   . LYS A  1 137 ? 19.747  -10.122 12.580  1.00 33.47  ?  168  LYS A O   1 
ATOM   948   C  CB  . LYS A  1 137 ? 18.180  -12.194 13.973  1.00 34.93  ?  168  LYS A CB  1 
ATOM   949   C  CG  . LYS A  1 137 ? 17.967  -13.173 15.094  1.00 40.19  ?  168  LYS A CG  1 
ATOM   950   C  CD  . LYS A  1 137 ? 19.230  -13.388 15.915  1.00 38.59  ?  168  LYS A CD  1 
ATOM   951   C  CE  . LYS A  1 137 ? 19.263  -14.810 16.495  1.00 49.20  ?  168  LYS A CE  1 
ATOM   952   N  NZ  . LYS A  1 137 ? 20.657  -15.343 16.691  1.00 54.90  ?  168  LYS A NZ  1 
ATOM   953   N  N   . ARG A  1 138 ? 17.821  -8.981  12.861  1.00 38.63  ?  169  ARG A N   1 
ATOM   954   C  CA  . ARG A  1 138 ? 17.915  -8.231  11.617  1.00 33.43  ?  169  ARG A CA  1 
ATOM   955   C  C   . ARG A  1 138 ? 18.129  -6.753  11.905  1.00 37.85  ?  169  ARG A C   1 
ATOM   956   O  O   . ARG A  1 138 ? 17.636  -5.898  11.167  1.00 35.06  ?  169  ARG A O   1 
ATOM   957   C  CB  . ARG A  1 138 ? 16.663  -8.395  10.751  1.00 32.67  ?  169  ARG A CB  1 
ATOM   958   C  CG  . ARG A  1 138 ? 16.049  -9.793  10.559  1.00 33.89  ?  169  ARG A CG  1 
ATOM   959   C  CD  . ARG A  1 138 ? 16.770  -10.744 9.628   1.00 37.01  ?  169  ARG A CD  1 
ATOM   960   N  NE  . ARG A  1 138 ? 17.341  -10.114 8.449   1.00 34.94  ?  169  ARG A NE  1 
ATOM   961   C  CZ  . ARG A  1 138 ? 17.257  -10.584 7.210   1.00 34.90  ?  169  ARG A CZ  1 
ATOM   962   N  NH1 . ARG A  1 138 ? 16.395  -11.538 6.887   1.00 32.44  ?  169  ARG A NH1 1 
ATOM   963   N  NH2 . ARG A  1 138 ? 18.063  -10.086 6.271   1.00 32.86  ?  169  ARG A NH2 1 
ATOM   964   N  N   . GLY A  1 139 ? 18.808  -6.432  13.005  1.00 34.13  ?  170  GLY A N   1 
ATOM   965   C  CA  . GLY A  1 139 ? 19.220  -5.072  13.271  1.00 33.80  ?  170  GLY A CA  1 
ATOM   966   C  C   . GLY A  1 139 ? 18.363  -4.266  14.229  1.00 30.00  ?  170  GLY A C   1 
ATOM   967   O  O   . GLY A  1 139 ? 18.654  -3.080  14.425  1.00 32.60  ?  170  GLY A O   1 
ATOM   968   N  N   . PHE A  1 140 ? 17.321  -4.841  14.830  1.00 33.62  ?  171  PHE A N   1 
ATOM   969   C  CA  . PHE A  1 140 ? 16.444  -4.069  15.713  1.00 31.71  ?  171  PHE A CA  1 
ATOM   970   C  C   . PHE A  1 140 ? 16.759  -4.388  17.175  1.00 31.56  ?  171  PHE A C   1 
ATOM   971   O  O   . PHE A  1 140 ? 16.619  -5.536  17.604  1.00 28.93  ?  171  PHE A O   1 
ATOM   972   C  CB  . PHE A  1 140 ? 14.965  -4.321  15.390  1.00 28.72  ?  171  PHE A CB  1 
ATOM   973   C  CG  . PHE A  1 140 ? 14.539  -3.694  14.086  1.00 25.79  ?  171  PHE A CG  1 
ATOM   974   C  CD1 . PHE A  1 140 ? 14.343  -2.323  13.995  1.00 26.18  ?  171  PHE A CD1 1 
ATOM   975   C  CD2 . PHE A  1 140 ? 14.388  -4.469  12.940  1.00 28.08  ?  171  PHE A CD2 1 
ATOM   976   C  CE1 . PHE A  1 140 ? 13.979  -1.722  12.774  1.00 27.89  ?  171  PHE A CE1 1 
ATOM   977   C  CE2 . PHE A  1 140 ? 14.031  -3.888  11.727  1.00 24.83  ?  171  PHE A CE2 1 
ATOM   978   C  CZ  . PHE A  1 140 ? 13.807  -2.512  11.650  1.00 28.09  ?  171  PHE A CZ  1 
ATOM   979   N  N   . ASP A  1 141 ? 17.204  -3.370  17.931  1.00 32.32  ?  172  ASP A N   1 
ATOM   980   C  CA  . ASP A  1 141 ? 17.414  -3.563  19.367  1.00 31.54  ?  172  ASP A CA  1 
ATOM   981   C  C   . ASP A  1 141 ? 16.129  -3.989  20.042  1.00 38.02  ?  172  ASP A C   1 
ATOM   982   O  O   . ASP A  1 141 ? 16.148  -4.829  20.944  1.00 33.58  ?  172  ASP A O   1 
ATOM   983   C  CB  . ASP A  1 141 ? 17.930  -2.289  20.043  1.00 34.53  ?  172  ASP A CB  1 
ATOM   984   C  CG  . ASP A  1 141 ? 19.274  -1.858  19.533  1.00 32.62  ?  172  ASP A CG  1 
ATOM   985   O  OD1 . ASP A  1 141 ? 20.135  -2.740  19.382  1.00 35.67  ?  172  ASP A OD1 1 
ATOM   986   O  OD2 . ASP A  1 141 ? 19.488  -0.638  19.323  1.00 32.94  -1 172  ASP A OD2 1 
ATOM   987   N  N   . ASP A  1 142 ? 14.990  -3.435  19.597  1.00 29.29  ?  173  ASP A N   1 
ATOM   988   C  CA  . ASP A  1 142 ? 13.707  -3.694  20.211  1.00 30.14  ?  173  ASP A CA  1 
ATOM   989   C  C   . ASP A  1 142 ? 12.692  -4.026  19.131  1.00 30.35  ?  173  ASP A C   1 
ATOM   990   O  O   . ASP A  1 142 ? 12.746  -3.466  18.037  1.00 25.70  ?  173  ASP A O   1 
ATOM   991   C  CB  . ASP A  1 142 ? 13.219  -2.480  21.026  1.00 31.84  ?  173  ASP A CB  1 
ATOM   992   C  CG  . ASP A  1 142 ? 12.030  -2.825  21.898  1.00 41.42  ?  173  ASP A CG  1 
ATOM   993   O  OD1 . ASP A  1 142 ? 10.887  -2.731  21.395  1.00 42.68  -1 173  ASP A OD1 1 
ATOM   994   O  OD2 . ASP A  1 142 ? 12.231  -3.244  23.063  1.00 42.84  ?  173  ASP A OD2 1 
ATOM   995   N  N   . PHE A  1 143 ? 11.805  -4.968  19.441  1.00 29.93  ?  174  PHE A N   1 
ATOM   996   C  CA  . PHE A  1 143 ? 10.678  -5.322  18.588  1.00 29.80  ?  174  PHE A CA  1 
ATOM   997   C  C   . PHE A  1 143 ? 9.452   -5.522  19.453  1.00 31.12  ?  174  PHE A C   1 
ATOM   998   O  O   . PHE A  1 143 ? 9.509   -6.223  20.464  1.00 30.95  ?  174  PHE A O   1 
ATOM   999   C  CB  . PHE A  1 143 ? 10.926  -6.603  17.796  1.00 29.61  ?  174  PHE A CB  1 
ATOM   1000  C  CG  . PHE A  1 143 ? 9.724   -7.079  17.013  1.00 32.18  ?  174  PHE A CG  1 
ATOM   1001  C  CD1 . PHE A  1 143 ? 9.131   -6.254  16.050  1.00 28.41  ?  174  PHE A CD1 1 
ATOM   1002  C  CD2 . PHE A  1 143 ? 9.191   -8.344  17.231  1.00 30.23  ?  174  PHE A CD2 1 
ATOM   1003  C  CE1 . PHE A  1 143 ? 8.025   -6.691  15.314  1.00 28.26  ?  174  PHE A CE1 1 
ATOM   1004  C  CE2 . PHE A  1 143 ? 8.085   -8.788  16.495  1.00 30.17  ?  174  PHE A CE2 1 
ATOM   1005  C  CZ  . PHE A  1 143 ? 7.508   -7.962  15.542  1.00 27.66  ?  174  PHE A CZ  1 
ATOM   1006  N  N   . TYR A  1 144 ? 8.336   -4.946  19.011  1.00 31.70  ?  175  TYR A N   1 
ATOM   1007  C  CA  . TYR A  1 144 ? 7.046   -5.091  19.668  1.00 27.62  ?  175  TYR A CA  1 
ATOM   1008  C  C   . TYR A  1 144 ? 6.021   -5.189  18.549  1.00 27.41  ?  175  TYR A C   1 
ATOM   1009  O  O   . TYR A  1 144 ? 5.838   -4.218  17.815  1.00 26.74  ?  175  TYR A O   1 
ATOM   1010  C  CB  . TYR A  1 144 ? 6.742   -3.896  20.585  1.00 25.75  ?  175  TYR A CB  1 
ATOM   1011  C  CG  . TYR A  1 144 ? 5.444   -4.066  21.344  1.00 31.80  ?  175  TYR A CG  1 
ATOM   1012  C  CD1 . TYR A  1 144 ? 4.205   -3.845  20.719  1.00 30.68  ?  175  TYR A CD1 1 
ATOM   1013  C  CD2 . TYR A  1 144 ? 5.448   -4.458  22.679  1.00 33.11  ?  175  TYR A CD2 1 
ATOM   1014  C  CE1 . TYR A  1 144 ? 3.023   -4.013  21.413  1.00 32.00  ?  175  TYR A CE1 1 
ATOM   1015  C  CE2 . TYR A  1 144 ? 4.268   -4.617  23.389  1.00 30.66  ?  175  TYR A CE2 1 
ATOM   1016  C  CZ  . TYR A  1 144 ? 3.058   -4.394  22.758  1.00 32.36  ?  175  TYR A CZ  1 
ATOM   1017  O  OH  . TYR A  1 144 ? 1.892   -4.567  23.468  1.00 31.60  ?  175  TYR A OH  1 
ATOM   1018  N  N   . GLY A  1 145 ? 5.377   -6.341  18.409  1.00 25.67  ?  176  GLY A N   1 
ATOM   1019  C  CA  . GLY A  1 145 ? 4.407   -6.514  17.335  1.00 27.23  ?  176  GLY A CA  1 
ATOM   1020  C  C   . GLY A  1 145 ? 4.168   -7.969  17.008  1.00 28.48  ?  176  GLY A C   1 
ATOM   1021  O  O   . GLY A  1 145 ? 4.152   -8.808  17.908  1.00 29.57  ?  176  GLY A O   1 
ATOM   1022  N  N   . PHE A  1 146 ? 3.947   -8.273  15.730  1.00 29.91  ?  177  PHE A N   1 
ATOM   1023  C  CA  . PHE A  1 146 ? 3.649   -9.621  15.281  1.00 27.83  ?  177  PHE A CA  1 
ATOM   1024  C  C   . PHE A  1 146 ? 4.443   -9.903  14.020  1.00 26.87  ?  177  PHE A C   1 
ATOM   1025  O  O   . PHE A  1 146 ? 4.809   -8.993  13.272  1.00 26.32  ?  177  PHE A O   1 
ATOM   1026  C  CB  . PHE A  1 146 ? 2.147   -9.830  15.026  1.00 30.13  ?  177  PHE A CB  1 
ATOM   1027  C  CG  . PHE A  1 146 ? 1.540   -8.830  14.061  1.00 30.26  ?  177  PHE A CG  1 
ATOM   1028  C  CD1 . PHE A  1 146 ? 1.030   -7.624  14.525  1.00 26.16  ?  177  PHE A CD1 1 
ATOM   1029  C  CD2 . PHE A  1 146 ? 1.463   -9.109  12.703  1.00 27.36  ?  177  PHE A CD2 1 
ATOM   1030  C  CE1 . PHE A  1 146 ? 0.475   -6.702  13.661  1.00 28.17  ?  177  PHE A CE1 1 
ATOM   1031  C  CE2 . PHE A  1 146 ? 0.884   -8.193  11.829  1.00 24.38  ?  177  PHE A CE2 1 
ATOM   1032  C  CZ  . PHE A  1 146 ? 0.394   -6.991  12.310  1.00 25.87  ?  177  PHE A CZ  1 
ATOM   1033  N  N   . LEU A  1 147 ? 4.721   -11.171 13.800  1.00 25.54  ?  178  LEU A N   1 
ATOM   1034  C  CA  . LEU A  1 147 ? 5.667   -11.555 12.767  1.00 30.45  ?  178  LEU A CA  1 
ATOM   1035  C  C   . LEU A  1 147 ? 5.025   -11.756 11.399  1.00 29.99  ?  178  LEU A C   1 
ATOM   1036  O  O   . LEU A  1 147 ? 5.729   -11.666 10.382  1.00 28.60  ?  178  LEU A O   1 
ATOM   1037  C  CB  . LEU A  1 147 ? 6.396   -12.841 13.193  1.00 29.09  ?  178  LEU A CB  1 
ATOM   1038  C  CG  . LEU A  1 147 ? 7.332   -12.707 14.395  1.00 31.52  ?  178  LEU A CG  1 
ATOM   1039  C  CD1 . LEU A  1 147 ? 7.756   -14.083 14.905  1.00 30.31  ?  178  LEU A CD1 1 
ATOM   1040  C  CD2 . LEU A  1 147 ? 8.538   -11.890 13.998  1.00 33.51  ?  178  LEU A CD2 1 
ATOM   1041  N  N   . GLY A  1 148 ? 3.729   -12.020 11.339  1.00 26.90  ?  179  GLY A N   1 
ATOM   1042  C  CA  . GLY A  1 148 ? 3.067   -12.342 10.088  1.00 26.70  ?  179  GLY A CA  1 
ATOM   1043  C  C   . GLY A  1 148 ? 2.428   -11.140 9.416   1.00 26.19  ?  179  GLY A C   1 
ATOM   1044  O  O   . GLY A  1 148 ? 2.850   -9.990  9.604   1.00 25.93  ?  179  GLY A O   1 
ATOM   1045  N  N   . GLY A  1 149 ? 1.380   -11.415 8.631   1.00 30.94  ?  180  GLY A N   1 
ATOM   1046  C  CA  . GLY A  1 149 ? 0.804   -10.461 7.696   1.00 29.98  ?  180  GLY A CA  1 
ATOM   1047  C  C   . GLY A  1 149 ? -0.349  -9.619  8.201   1.00 31.12  ?  180  GLY A C   1 
ATOM   1048  O  O   . GLY A  1 149 ? -0.753  -8.667  7.523   1.00 27.73  ?  180  GLY A O   1 
ATOM   1049  N  N   . GLY A  1 150 ? -0.897  -9.929  9.368   1.00 30.13  ?  181  GLY A N   1 
ATOM   1050  C  CA  . GLY A  1 150 ? -1.945  -9.092  9.918   1.00 31.37  ?  181  GLY A CA  1 
ATOM   1051  C  C   . GLY A  1 150 ? -2.301  -9.540  11.318  1.00 31.04  ?  181  GLY A C   1 
ATOM   1052  O  O   . GLY A  1 150 ? -1.750  -10.512 11.845  1.00 28.39  ?  181  GLY A O   1 
ATOM   1053  N  N   . HIS A  1 151 ? -3.237  -8.810  11.920  1.00 28.48  ?  182  HIS A N   1 
ATOM   1054  C  CA  . HIS A  1 151 ? -3.653  -9.117  13.275  1.00 27.38  ?  182  HIS A CA  1 
ATOM   1055  C  C   . HIS A  1 151 ? -5.007  -8.486  13.568  1.00 28.38  ?  182  HIS A C   1 
ATOM   1056  O  O   . HIS A  1 151 ? -5.307  -7.367  13.126  1.00 25.22  ?  182  HIS A O   1 
ATOM   1057  C  CB  . HIS A  1 151 ? -2.605  -8.641  14.309  1.00 26.56  ?  182  HIS A CB  1 
ATOM   1058  C  CG  . HIS A  1 151 ? -2.597  -9.464  15.558  1.00 28.35  ?  182  HIS A CG  1 
ATOM   1059  N  ND1 . HIS A  1 151 ? -3.531  -9.298  16.560  1.00 28.42  ?  182  HIS A ND1 1 
ATOM   1060  C  CD2 . HIS A  1 151 ? -1.800  -10.488 15.948  1.00 29.66  ?  182  HIS A CD2 1 
ATOM   1061  C  CE1 . HIS A  1 151 ? -3.312  -10.190 17.513  1.00 29.68  ?  182  HIS A CE1 1 
ATOM   1062  N  NE2 . HIS A  1 151 ? -2.271  -10.925 17.163  1.00 30.32  ?  182  HIS A NE2 1 
ATOM   1063  N  N   . ASP A  1 152 ? -5.820  -9.221  14.313  1.00 28.64  ?  183  ASP A N   1 
ATOM   1064  C  CA  . ASP A  1 152 ? -7.025  -8.652  14.898  1.00 26.79  ?  183  ASP A CA  1 
ATOM   1065  C  C   . ASP A  1 152 ? -6.672  -7.529  15.868  1.00 28.77  ?  183  ASP A C   1 
ATOM   1066  O  O   . ASP A  1 152 ? -5.627  -7.547  16.525  1.00 25.40  ?  183  ASP A O   1 
ATOM   1067  C  CB  . ASP A  1 152 ? -7.824  -9.753  15.589  1.00 27.38  ?  183  ASP A CB  1 
ATOM   1068  C  CG  . ASP A  1 152 ? -8.589  -10.611 14.576  1.00 38.21  ?  183  ASP A CG  1 
ATOM   1069  O  OD1 . ASP A  1 152 ? -8.091  -10.725 13.444  1.00 32.43  ?  183  ASP A OD1 1 
ATOM   1070  O  OD2 . ASP A  1 152 ? -9.679  -11.142 14.884  1.00 41.22  -1 183  ASP A OD2 1 
ATOM   1071  N  N   . TYR A  1 153 ? -7.574  -6.556  15.985  1.00 24.38  ?  184  TYR A N   1 
ATOM   1072  C  CA  . TYR A  1 153 ? -7.215  -5.299  16.624  1.00 26.90  ?  184  TYR A CA  1 
ATOM   1073  C  C   . TYR A  1 153 ? -7.549  -5.216  18.118  1.00 29.95  ?  184  TYR A C   1 
ATOM   1074  O  O   . TYR A  1 153 ? -6.974  -4.361  18.801  1.00 25.84  ?  184  TYR A O   1 
ATOM   1075  C  CB  . TYR A  1 153 ? -7.904  -4.136  15.888  1.00 25.62  ?  184  TYR A CB  1 
ATOM   1076  C  CG  . TYR A  1 153 ? -7.301  -3.813  14.534  1.00 24.90  ?  184  TYR A CG  1 
ATOM   1077  C  CD1 . TYR A  1 153 ? -7.685  -4.513  13.386  1.00 25.50  ?  184  TYR A CD1 1 
ATOM   1078  C  CD2 . TYR A  1 153 ? -6.367  -2.798  14.400  1.00 27.09  ?  184  TYR A CD2 1 
ATOM   1079  C  CE1 . TYR A  1 153 ? -7.139  -4.207  12.135  1.00 21.68  ?  184  TYR A CE1 1 
ATOM   1080  C  CE2 . TYR A  1 153 ? -5.811  -2.492  13.178  1.00 24.87  ?  184  TYR A CE2 1 
ATOM   1081  C  CZ  . TYR A  1 153 ? -6.192  -3.188  12.051  1.00 24.11  ?  184  TYR A CZ  1 
ATOM   1082  O  OH  . TYR A  1 153 ? -5.624  -2.853  10.847  1.00 24.63  ?  184  TYR A OH  1 
ATOM   1083  N  N   . PHE A  1 154 ? -8.476  -6.036  18.649  1.00 26.55  ?  185  PHE A N   1 
ATOM   1084  C  CA  . PHE A  1 154 ? -8.887  -5.867  20.048  1.00 27.67  ?  185  PHE A CA  1 
ATOM   1085  C  C   . PHE A  1 154 ? -8.391  -7.019  20.917  1.00 27.97  ?  185  PHE A C   1 
ATOM   1086  O  O   . PHE A  1 154 ? -8.881  -8.149  20.779  1.00 29.20  ?  185  PHE A O   1 
ATOM   1087  C  CB  . PHE A  1 154 ? -10.408 -5.731  20.160  1.00 28.99  ?  185  PHE A CB  1 
ATOM   1088  C  CG  . PHE A  1 154 ? -10.918 -4.393  19.733  1.00 28.31  ?  185  PHE A CG  1 
ATOM   1089  C  CD1 . PHE A  1 154 ? -10.854 -3.313  20.587  1.00 28.77  ?  185  PHE A CD1 1 
ATOM   1090  C  CD2 . PHE A  1 154 ? -11.450 -4.213  18.458  1.00 33.11  ?  185  PHE A CD2 1 
ATOM   1091  C  CE1 . PHE A  1 154 ? -11.314 -2.066  20.191  1.00 31.22  ?  185  PHE A CE1 1 
ATOM   1092  C  CE2 . PHE A  1 154 ? -11.923 -2.978  18.052  1.00 30.83  ?  185  PHE A CE2 1 
ATOM   1093  C  CZ  . PHE A  1 154 ? -11.859 -1.899  18.916  1.00 30.07  ?  185  PHE A CZ  1 
ATOM   1094  N  N   . PRO A  1 155 ? -7.404  -6.783  21.794  1.00 29.16  ?  186  PRO A N   1 
ATOM   1095  C  CA  . PRO A  1 155 ? -6.896  -7.857  22.677  1.00 32.71  ?  186  PRO A CA  1 
ATOM   1096  C  C   . PRO A  1 155 ? -7.976  -8.609  23.449  1.00 31.40  ?  186  PRO A C   1 
ATOM   1097  O  O   . PRO A  1 155 ? -7.950  -9.846  23.489  1.00 31.47  ?  186  PRO A O   1 
ATOM   1098  C  CB  . PRO A  1 155 ? -5.942  -7.105  23.629  1.00 31.73  ?  186  PRO A CB  1 
ATOM   1099  C  CG  . PRO A  1 155 ? -5.529  -5.888  22.908  1.00 30.95  ?  186  PRO A CG  1 
ATOM   1100  C  CD  . PRO A  1 155 ? -6.732  -5.494  22.014  1.00 27.18  ?  186  PRO A CD  1 
ATOM   1101  N  N   . SER A  1 156 ? -8.932  -7.899  24.049  1.00 31.16  ?  187  SER A N   1 
ATOM   1102  C  CA  . SER A  1 156 ? -10.020 -8.576  24.735  1.00 34.88  ?  187  SER A CA  1 
ATOM   1103  C  C   . SER A  1 156 ? -10.716 -9.577  23.823  1.00 39.24  ?  187  SER A C   1 
ATOM   1104  O  O   . SER A  1 156 ? -11.155 -10.631 24.291  1.00 39.24  ?  187  SER A O   1 
ATOM   1105  C  CB  . SER A  1 156 ? -11.028 -7.557  25.266  1.00 35.52  ?  187  SER A CB  1 
ATOM   1106  O  OG  . SER A  1 156 ? -11.509 -6.754  24.192  1.00 37.71  ?  187  SER A OG  1 
ATOM   1107  N  N   . GLU A  1 157 ? -10.797 -9.292  22.514  1.00 35.95  ?  188  GLU A N   1 
ATOM   1108  C  CA  . GLU A  1 157 ? -11.450 -10.232 21.607  1.00 33.14  ?  188  GLU A CA  1 
ATOM   1109  C  C   . GLU A  1 157 ? -10.500 -11.338 21.158  1.00 34.44  ?  188  GLU A C   1 
ATOM   1110  O  O   . GLU A  1 157 ? -10.863 -12.517 21.187  1.00 32.13  ?  188  GLU A O   1 
ATOM   1111  C  CB  . GLU A  1 157 ? -12.014 -9.497  20.383  1.00 34.76  ?  188  GLU A CB  1 
ATOM   1112  C  CG  . GLU A  1 157 ? -13.015 -8.417  20.736  1.00 32.84  ?  188  GLU A CG  1 
ATOM   1113  C  CD  . GLU A  1 157 ? -13.602 -7.717  19.508  1.00 47.19  ?  188  GLU A CD  1 
ATOM   1114  O  OE1 . GLU A  1 157 ? -12.909 -7.624  18.463  1.00 46.06  ?  188  GLU A OE1 1 
ATOM   1115  O  OE2 . GLU A  1 157 ? -14.777 -7.284  19.579  1.00 53.86  -1 188  GLU A OE2 1 
ATOM   1116  N  N   . TYR A  1 158 ? -9.280  -10.992 20.722  1.00 28.85  ?  189  TYR A N   1 
ATOM   1117  C  CA  . TYR A  1 158 ? -8.460  -12.043 20.121  1.00 34.68  ?  189  TYR A CA  1 
ATOM   1118  C  C   . TYR A  1 158 ? -7.806  -12.936 21.172  1.00 34.97  ?  189  TYR A C   1 
ATOM   1119  O  O   . TYR A  1 158 ? -7.534  -14.111 20.888  1.00 31.89  ?  189  TYR A O   1 
ATOM   1120  C  CB  . TYR A  1 158 ? -7.409  -11.464 19.142  1.00 29.75  ?  189  TYR A CB  1 
ATOM   1121  C  CG  . TYR A  1 158 ? -6.242  -10.623 19.678  1.00 29.87  ?  189  TYR A CG  1 
ATOM   1122  C  CD1 . TYR A  1 158 ? -5.219  -11.193 20.429  1.00 33.17  ?  189  TYR A CD1 1 
ATOM   1123  C  CD2 . TYR A  1 158 ? -6.132  -9.266  19.352  1.00 27.49  ?  189  TYR A CD2 1 
ATOM   1124  C  CE1 . TYR A  1 158 ? -4.142  -10.429 20.894  1.00 31.32  ?  189  TYR A CE1 1 
ATOM   1125  C  CE2 . TYR A  1 158 ? -5.056  -8.491  19.801  1.00 26.50  ?  189  TYR A CE2 1 
ATOM   1126  C  CZ  . TYR A  1 158 ? -4.068  -9.080  20.574  1.00 33.65  ?  189  TYR A CZ  1 
ATOM   1127  O  OH  . TYR A  1 158 ? -3.001  -8.330  21.035  1.00 31.48  ?  189  TYR A OH  1 
ATOM   1128  N  N   . GLN A  1 159 ? -7.543  -12.411 22.374  1.00 33.23  ?  190  GLN A N   1 
ATOM   1129  C  CA  . GLN A  1 159 ? -7.013  -13.268 23.433  1.00 34.40  ?  190  GLN A CA  1 
ATOM   1130  C  C   . GLN A  1 159 ? -8.051  -14.285 23.894  1.00 34.85  ?  190  GLN A C   1 
ATOM   1131  O  O   . GLN A  1 159 ? -7.709  -15.438 24.181  1.00 37.62  ?  190  GLN A O   1 
ATOM   1132  C  CB  . GLN A  1 159 ? -6.516  -12.417 24.596  1.00 34.58  ?  190  GLN A CB  1 
ATOM   1133  C  CG  . GLN A  1 159 ? -5.209  -11.708 24.285  1.00 38.48  ?  190  GLN A CG  1 
ATOM   1134  C  CD  . GLN A  1 159 ? -4.920  -10.559 25.245  1.00 41.04  ?  190  GLN A CD  1 
ATOM   1135  O  OE1 . GLN A  1 159 ? -5.749  -10.223 26.089  1.00 42.83  ?  190  GLN A OE1 1 
ATOM   1136  N  NE2 . GLN A  1 159 ? -3.745  -9.947  25.112  1.00 37.70  ?  190  GLN A NE2 1 
ATOM   1137  N  N   . LYS A  1 160 ? -9.325  -13.888 23.952  1.00 32.36  ?  191  LYS A N   1 
ATOM   1138  C  CA  . LYS A  1 160 ? -10.392 -14.851 24.224  1.00 39.74  ?  191  LYS A CA  1 
ATOM   1139  C  C   . LYS A  1 160 ? -10.444 -15.931 23.161  1.00 39.97  ?  191  LYS A C   1 
ATOM   1140  O  O   . LYS A  1 160 ? -10.515 -17.123 23.476  1.00 37.67  ?  191  LYS A O   1 
ATOM   1141  C  CB  . LYS A  1 160 ? -11.749 -14.160 24.299  1.00 40.28  ?  191  LYS A CB  1 
ATOM   1142  C  CG  . LYS A  1 160 ? -11.971 -13.262 25.490  1.00 47.27  ?  191  LYS A CG  1 
ATOM   1143  C  CD  . LYS A  1 160 ? -13.457 -13.272 25.872  1.00 55.19  ?  191  LYS A CD  1 
ATOM   1144  C  CE  . LYS A  1 160 ? -14.341 -13.704 24.695  1.00 58.27  ?  191  LYS A CE  1 
ATOM   1145  N  NZ  . LYS A  1 160 ? -15.796 -13.391 24.898  1.00 67.76  ?  191  LYS A NZ  1 
ATOM   1146  N  N   . THR A  1 161 ? -10.462 -15.521 21.887  1.00 37.15  ?  192  THR A N   1 
ATOM   1147  C  CA  . THR A  1 161 ? -10.499 -16.480 20.793  1.00 35.04  ?  192  THR A CA  1 
ATOM   1148  C  C   . THR A  1 161 ? -9.296  -17.407 20.824  1.00 33.86  ?  192  THR A C   1 
ATOM   1149  O  O   . THR A  1 161 ? -9.434  -18.614 20.602  1.00 36.69  ?  192  THR A O   1 
ATOM   1150  C  CB  . THR A  1 161 ? -10.575 -15.744 19.454  1.00 37.56  ?  192  THR A CB  1 
ATOM   1151  O  OG1 . THR A  1 161 ? -11.804 -15.000 19.403  1.00 35.53  ?  192  THR A OG1 1 
ATOM   1152  C  CG2 . THR A  1 161 ? -10.529 -16.741 18.298  1.00 34.74  ?  192  THR A CG2 1 
ATOM   1153  N  N   . TYR A  1 162 ? -8.106  -16.867 21.095  1.00 33.34  ?  193  TYR A N   1 
ATOM   1154  C  CA  . TYR A  1 162 ? -6.907  -17.704 21.133  1.00 37.43  ?  193  TYR A CA  1 
ATOM   1155  C  C   . TYR A  1 162 ? -7.020  -18.770 22.215  1.00 40.81  ?  193  TYR A C   1 
ATOM   1156  O  O   . TYR A  1 162 ? -6.746  -19.951 21.969  1.00 41.40  ?  193  TYR A O   1 
ATOM   1157  C  CB  . TYR A  1 162 ? -5.654  -16.851 21.367  1.00 32.71  ?  193  TYR A CB  1 
ATOM   1158  C  CG  . TYR A  1 162 ? -4.356  -17.650 21.421  1.00 38.86  ?  193  TYR A CG  1 
ATOM   1159  C  CD1 . TYR A  1 162 ? -3.827  -18.227 20.273  1.00 36.44  ?  193  TYR A CD1 1 
ATOM   1160  C  CD2 . TYR A  1 162 ? -3.654  -17.817 22.621  1.00 40.19  ?  193  TYR A CD2 1 
ATOM   1161  C  CE1 . TYR A  1 162 ? -2.634  -18.950 20.305  1.00 39.11  ?  193  TYR A CE1 1 
ATOM   1162  C  CE2 . TYR A  1 162 ? -2.464  -18.551 22.664  1.00 37.16  ?  193  TYR A CE2 1 
ATOM   1163  C  CZ  . TYR A  1 162 ? -1.959  -19.110 21.503  1.00 43.52  ?  193  TYR A CZ  1 
ATOM   1164  O  OH  . TYR A  1 162 ? -0.778  -19.832 21.516  1.00 44.45  ?  193  TYR A OH  1 
ATOM   1165  N  N   . LYS A  1 163 ? -7.417  -18.366 23.426  1.00 38.87  ?  194  LYS A N   1 
ATOM   1166  C  CA  . LYS A  1 163 ? -7.543  -19.329 24.518  1.00 41.92  ?  194  LYS A CA  1 
ATOM   1167  C  C   . LYS A  1 163 ? -8.634  -20.346 24.208  1.00 39.15  ?  194  LYS A C   1 
ATOM   1168  O  O   . LYS A  1 163 ? -8.447  -21.553 24.403  1.00 42.09  ?  194  LYS A O   1 
ATOM   1169  C  CB  . LYS A  1 163 ? -7.829  -18.598 25.839  1.00 39.82  ?  194  LYS A CB  1 
ATOM   1170  C  CG  . LYS A  1 163 ? -6.633  -17.804 26.376  1.00 43.79  ?  194  LYS A CG  1 
ATOM   1171  C  CD  . LYS A  1 163 ? -6.885  -17.125 27.751  1.00 51.93  ?  194  LYS A CD  1 
ATOM   1172  C  CE  . LYS A  1 163 ? -7.851  -15.938 27.679  1.00 52.07  ?  194  LYS A CE  1 
ATOM   1173  N  NZ  . LYS A  1 163 ? -7.271  -14.693 28.282  1.00 60.04  ?  194  LYS A NZ  1 
ATOM   1174  N  N   . ALA A  1 164 ? -9.767  -19.874 23.679  1.00 39.40  ?  195  ALA A N   1 
ATOM   1175  C  CA  . ALA A  1 164 ? -10.876 -20.766 23.351  1.00 37.71  ?  195  ALA A CA  1 
ATOM   1176  C  C   . ALA A  1 164 ? -10.478 -21.798 22.299  1.00 39.38  ?  195  ALA A C   1 
ATOM   1177  O  O   . ALA A  1 164 ? -10.906 -22.955 22.362  1.00 38.19  ?  195  ALA A O   1 
ATOM   1178  C  CB  . ALA A  1 164 ? -12.076 -19.948 22.878  1.00 37.67  ?  195  ALA A CB  1 
ATOM   1179  N  N   . GLN A  1 165 ? -9.658  -21.405 21.329  1.00 35.53  ?  196  GLN A N   1 
ATOM   1180  C  CA  . GLN A  1 165 ? -9.251  -22.338 20.286  1.00 39.41  ?  196  GLN A CA  1 
ATOM   1181  C  C   . GLN A  1 165 ? -8.176  -23.300 20.779  1.00 39.85  ?  196  GLN A C   1 
ATOM   1182  O  O   . GLN A  1 165 ? -8.115  -24.448 20.318  1.00 39.97  ?  196  GLN A O   1 
ATOM   1183  C  CB  . GLN A  1 165 ? -8.756  -21.569 19.059  1.00 35.95  ?  196  GLN A CB  1 
ATOM   1184  C  CG  . GLN A  1 165 ? -9.863  -20.854 18.316  1.00 32.78  ?  196  GLN A CG  1 
ATOM   1185  C  CD  . GLN A  1 165 ? -10.974 -21.800 17.915  1.00 38.77  ?  196  GLN A CD  1 
ATOM   1186  O  OE1 . GLN A  1 165 ? -10.748 -22.753 17.161  1.00 35.69  ?  196  GLN A OE1 1 
ATOM   1187  N  NE2 . GLN A  1 165 ? -12.181 -21.552 18.422  1.00 38.36  ?  196  GLN A NE2 1 
ATOM   1188  N  N   . LYS A  1 166 ? -7.311  -22.848 21.683  1.00 37.41  ?  197  LYS A N   1 
ATOM   1189  C  CA  . LYS A  1 166 ? -6.393  -23.770 22.344  1.00 43.82  ?  197  LYS A CA  1 
ATOM   1190  C  C   . LYS A  1 166 ? -7.161  -24.811 23.154  1.00 43.48  ?  197  LYS A C   1 
ATOM   1191  O  O   . LYS A  1 166 ? -6.867  -26.009 23.068  1.00 43.75  ?  197  LYS A O   1 
ATOM   1192  C  CB  . LYS A  1 166 ? -5.416  -23.004 23.237  1.00 41.93  ?  197  LYS A CB  1 
ATOM   1193  C  CG  . LYS A  1 166 ? -4.223  -22.413 22.481  1.00 45.36  ?  197  LYS A CG  1 
ATOM   1194  C  CD  . LYS A  1 166 ? -2.947  -22.446 23.318  1.00 45.59  ?  197  LYS A CD  1 
ATOM   1195  C  CE  . LYS A  1 166 ? -2.039  -23.611 22.921  1.00 57.72  ?  197  LYS A CE  1 
ATOM   1196  N  NZ  . LYS A  1 166 ? -1.613  -23.593 21.482  1.00 50.78  ?  197  LYS A NZ  1 
ATOM   1197  N  N   . LYS A  1 167 ? -8.176  -24.374 23.913  1.00 40.22  ?  198  LYS A N   1 
ATOM   1198  C  CA  . LYS A  1 167 ? -8.980  -25.311 24.697  1.00 44.95  ?  198  LYS A CA  1 
ATOM   1199  C  C   . LYS A  1 167 ? -9.717  -26.307 23.811  1.00 45.56  ?  198  LYS A C   1 
ATOM   1200  O  O   . LYS A  1 167 ? -9.847  -27.484 24.165  1.00 46.83  ?  198  LYS A O   1 
ATOM   1201  C  CB  . LYS A  1 167 ? -9.970  -24.553 25.575  1.00 47.51  ?  198  LYS A CB  1 
ATOM   1202  C  CG  . LYS A  1 167 ? -10.668 -25.445 26.585  1.00 50.68  ?  198  LYS A CG  1 
ATOM   1203  C  CD  . LYS A  1 167 ? -11.383 -24.624 27.629  1.00 51.06  ?  198  LYS A CD  1 
ATOM   1204  C  CE  . LYS A  1 167 ? -12.863 -24.536 27.311  1.00 59.74  ?  198  LYS A CE  1 
ATOM   1205  N  NZ  . LYS A  1 167 ? -13.668 -25.264 28.327  1.00 60.88  ?  198  LYS A NZ  1 
ATOM   1206  N  N   . ALA A  1 168 ? -10.211 -25.862 22.656  1.00 42.58  ?  199  ALA A N   1 
ATOM   1207  C  CA  . ALA A  1 168 ? -10.861 -26.785 21.737  1.00 43.60  ?  199  ALA A CA  1 
ATOM   1208  C  C   . ALA A  1 168 ? -9.874  -27.695 21.013  1.00 41.91  ?  199  ALA A C   1 
ATOM   1209  O  O   . ALA A  1 168 ? -10.308 -28.541 20.224  1.00 43.44  ?  199  ALA A O   1 
ATOM   1210  C  CB  . ALA A  1 168 ? -11.696 -26.005 20.711  1.00 40.33  ?  199  ALA A CB  1 
ATOM   1211  N  N   . GLY A  1 169 ? -8.572  -27.544 21.246  1.00 44.96  ?  200  GLY A N   1 
ATOM   1212  C  CA  . GLY A  1 169 ? -7.588  -28.352 20.546  1.00 44.84  ?  200  GLY A CA  1 
ATOM   1213  C  C   . GLY A  1 169 ? -7.383  -28.006 19.084  1.00 46.97  ?  200  GLY A C   1 
ATOM   1214  O  O   . GLY A  1 169 ? -7.051  -28.894 18.284  1.00 43.31  ?  200  GLY A O   1 
ATOM   1215  N  N   . ASN A  1 170 ? -7.578  -26.741 18.709  1.00 44.21  ?  201  ASN A N   1 
ATOM   1216  C  CA  . ASN A  1 170 ? -7.315  -26.295 17.338  1.00 41.98  ?  201  ASN A CA  1 
ATOM   1217  C  C   . ASN A  1 170 ? -5.845  -26.519 17.003  1.00 41.25  ?  201  ASN A C   1 
ATOM   1218  O  O   . ASN A  1 170 ? -4.970  -25.939 17.664  1.00 41.43  ?  201  ASN A O   1 
ATOM   1219  C  CB  . ASN A  1 170 ? -7.665  -24.812 17.176  1.00 40.19  ?  201  ASN A CB  1 
ATOM   1220  C  CG  . ASN A  1 170 ? -7.730  -24.364 15.712  1.00 43.45  ?  201  ASN A CG  1 
ATOM   1221  O  OD1 . ASN A  1 170 ? -6.969  -24.839 14.849  1.00 44.12  ?  201  ASN A OD1 1 
ATOM   1222  N  ND2 . ASN A  1 170 ? -8.634  -23.426 15.435  1.00 40.58  ?  201  ASN A ND2 1 
ATOM   1223  N  N   . PRO A  1 171 ? -5.525  -27.349 16.010  1.00 41.87  ?  202  PRO A N   1 
ATOM   1224  C  CA  . PRO A  1 171 ? -4.117  -27.565 15.658  1.00 41.53  ?  202  PRO A CA  1 
ATOM   1225  C  C   . PRO A  1 171 ? -3.555  -26.510 14.715  1.00 45.31  ?  202  PRO A C   1 
ATOM   1226  O  O   . PRO A  1 171 ? -2.334  -26.480 14.513  1.00 43.61  ?  202  PRO A O   1 
ATOM   1227  C  CB  . PRO A  1 171 ? -4.147  -28.942 14.988  1.00 42.06  ?  202  PRO A CB  1 
ATOM   1228  C  CG  . PRO A  1 171 ? -5.493  -28.977 14.327  1.00 42.71  ?  202  PRO A CG  1 
ATOM   1229  C  CD  . PRO A  1 171 ? -6.437  -28.178 15.198  1.00 40.67  ?  202  PRO A CD  1 
ATOM   1230  N  N   . ASN A  1 172 ? -4.400  -25.645 14.143  1.00 45.24  ?  203  ASN A N   1 
ATOM   1231  C  CA  . ASN A  1 172 ? -3.986  -24.651 13.147  1.00 44.12  ?  203  ASN A CA  1 
ATOM   1232  C  C   . ASN A  1 172 ? -4.614  -23.292 13.465  1.00 38.26  ?  203  ASN A C   1 
ATOM   1233  O  O   . ASN A  1 172 ? -5.382  -22.737 12.681  1.00 38.03  ?  203  ASN A O   1 
ATOM   1234  C  CB  . ASN A  1 172 ? -4.372  -25.099 11.745  1.00 41.84  ?  203  ASN A CB  1 
ATOM   1235  C  CG  . ASN A  1 172 ? -3.498  -26.228 11.236  1.00 51.48  ?  203  ASN A CG  1 
ATOM   1236  O  OD1 . ASN A  1 172 ? -2.284  -26.070 11.083  1.00 54.11  ?  203  ASN A OD1 1 
ATOM   1237  N  ND2 . ASN A  1 172 ? -4.110  -27.380 10.975  1.00 53.39  ?  203  ASN A ND2 1 
ATOM   1238  N  N   . ILE A  1 173 ? -4.286  -22.752 14.639  1.00 41.09  ?  204  ILE A N   1 
ATOM   1239  C  CA  . ILE A  1 173 ? -4.811  -21.447 15.035  1.00 41.26  ?  204  ILE A CA  1 
ATOM   1240  C  C   . ILE A  1 173 ? -4.261  -20.368 14.104  1.00 37.12  ?  204  ILE A C   1 
ATOM   1241  O  O   . ILE A  1 173 ? -3.055  -20.328 13.819  1.00 32.53  ?  204  ILE A O   1 
ATOM   1242  C  CB  . ILE A  1 173 ? -4.460  -21.160 16.500  1.00 37.12  ?  204  ILE A CB  1 
ATOM   1243  C  CG1 . ILE A  1 173 ? -4.888  -22.344 17.375  1.00 42.83  ?  204  ILE A CG1 1 
ATOM   1244  C  CG2 . ILE A  1 173 ? -5.131  -19.881 16.974  1.00 32.56  ?  204  ILE A CG2 1 
ATOM   1245  C  CD1 . ILE A  1 173 ? -4.996  -22.000 18.849  1.00 38.74  ?  204  ILE A CD1 1 
ATOM   1246  N  N   . ARG A  1 174 ? -5.142  -19.489 13.631  1.00 33.35  ?  205  ARG A N   1 
ATOM   1247  C  CA  A ARG A  1 174 ? -4.719  -18.439 12.716  0.54 34.87  ?  205  ARG A CA  1 
ATOM   1248  C  CA  B ARG A  1 174 ? -4.728  -18.428 12.720  0.46 34.88  ?  205  ARG A CA  1 
ATOM   1249  C  C   . ARG A  1 174 ? -3.819  -17.443 13.431  1.00 31.38  ?  205  ARG A C   1 
ATOM   1250  O  O   . ARG A  1 174 ? -4.090  -17.030 14.560  1.00 33.83  ?  205  ARG A O   1 
ATOM   1251  C  CB  A ARG A  1 174 ? -5.943  -17.740 12.103  0.54 36.89  ?  205  ARG A CB  1 
ATOM   1252  C  CB  B ARG A  1 174 ? -5.944  -17.684 12.166  0.46 36.88  ?  205  ARG A CB  1 
ATOM   1253  C  CG  A ARG A  1 174 ? -6.902  -17.059 13.092  0.54 37.52  ?  205  ARG A CG  1 
ATOM   1254  C  CG  B ARG A  1 174 ? -6.830  -18.504 11.262  0.46 37.08  ?  205  ARG A CG  1 
ATOM   1255  C  CD  A ARG A  1 174 ? -8.193  -16.621 12.364  0.54 42.22  ?  205  ARG A CD  1 
ATOM   1256  C  CD  B ARG A  1 174 ? -7.896  -17.630 10.609  0.46 43.37  ?  205  ARG A CD  1 
ATOM   1257  N  NE  A ARG A  1 174 ? -9.018  -15.654 13.087  0.54 38.73  ?  205  ARG A NE  1 
ATOM   1258  N  NE  B ARG A  1 174 ? -8.473  -16.658 11.532  0.46 42.87  ?  205  ARG A NE  1 
ATOM   1259  C  CZ  A ARG A  1 174 ? -9.887  -15.962 14.043  0.54 40.75  ?  205  ARG A CZ  1 
ATOM   1260  C  CZ  B ARG A  1 174 ? -8.504  -15.346 11.340  0.46 41.79  ?  205  ARG A CZ  1 
ATOM   1261  N  NH1 A ARG A  1 174 ? -10.039 -17.208 14.467  0.54 34.27  ?  205  ARG A NH1 1 
ATOM   1262  N  NH1 B ARG A  1 174 ? -8.032  -14.793 10.233  0.46 43.51  ?  205  ARG A NH1 1 
ATOM   1263  N  NH2 A ARG A  1 174 ? -10.621 -14.992 14.590  0.54 38.62  ?  205  ARG A NH2 1 
ATOM   1264  N  NH2 B ARG A  1 174 ? -9.028  -14.568 12.282  0.46 40.77  ?  205  ARG A NH2 1 
ATOM   1265  N  N   . ASP A  1 175 ? -2.732  -17.054 12.761  1.00 33.80  ?  206  ASP A N   1 
ATOM   1266  C  CA  . ASP A  1 175 ? -1.789  -16.149 13.408  1.00 33.39  ?  206  ASP A CA  1 
ATOM   1267  C  C   . ASP A  1 175 ? -2.412  -14.783 13.692  1.00 30.08  ?  206  ASP A C   1 
ATOM   1268  O  O   . ASP A  1 175 ? -1.891  -14.036 14.534  1.00 29.57  ?  206  ASP A O   1 
ATOM   1269  C  CB  . ASP A  1 175 ? -0.482  -16.004 12.588  1.00 31.88  ?  206  ASP A CB  1 
ATOM   1270  C  CG  . ASP A  1 175 ? -0.702  -15.713 11.099  1.00 33.09  ?  206  ASP A CG  1 
ATOM   1271  O  OD1 . ASP A  1 175 ? -1.814  -15.310 10.699  1.00 32.48  ?  206  ASP A OD1 1 
ATOM   1272  O  OD2 . ASP A  1 175 ? 0.271   -15.869 10.306  1.00 29.50  -1 206  ASP A OD2 1 
ATOM   1273  N  N   . TYR A  1 176 ? -3.545  -14.464 13.060  1.00 29.70  ?  207  TYR A N   1 
ATOM   1274  C  CA  . TYR A  1 176 ? -4.217  -13.202 13.346  1.00 31.22  ?  207  TYR A CA  1 
ATOM   1275  C  C   . TYR A  1 176 ? -4.681  -13.091 14.798  1.00 30.07  ?  207  TYR A C   1 
ATOM   1276  O  O   . TYR A  1 176 ? -4.924  -11.976 15.274  1.00 30.79  ?  207  TYR A O   1 
ATOM   1277  C  CB  . TYR A  1 176 ? -5.402  -13.036 12.407  1.00 33.77  ?  207  TYR A CB  1 
ATOM   1278  C  CG  . TYR A  1 176 ? -5.085  -12.276 11.136  1.00 31.57  ?  207  TYR A CG  1 
ATOM   1279  C  CD1 . TYR A  1 176 ? -4.131  -12.749 10.240  1.00 31.91  ?  207  TYR A CD1 1 
ATOM   1280  C  CD2 . TYR A  1 176 ? -5.787  -11.118 10.802  1.00 29.85  ?  207  TYR A CD2 1 
ATOM   1281  C  CE1 . TYR A  1 176 ? -3.855  -12.068 9.048   1.00 30.77  ?  207  TYR A CE1 1 
ATOM   1282  C  CE2 . TYR A  1 176 ? -5.528  -10.431 9.611   1.00 31.23  ?  207  TYR A CE2 1 
ATOM   1283  C  CZ  . TYR A  1 176 ? -4.570  -10.912 8.742   1.00 34.26  ?  207  TYR A CZ  1 
ATOM   1284  O  OH  . TYR A  1 176 ? -4.321  -10.229 7.581   1.00 29.28  ?  207  TYR A OH  1 
ATOM   1285  N  N   . VAL A  1 177 ? -4.811  -14.204 15.524  1.00 28.75  ?  208  VAL A N   1 
ATOM   1286  C  CA  . VAL A  1 177 ? -5.225  -14.124 16.918  1.00 30.02  ?  208  VAL A CA  1 
ATOM   1287  C  C   . VAL A  1 177 ? -4.104  -14.538 17.876  1.00 31.77  ?  208  VAL A C   1 
ATOM   1288  O  O   . VAL A  1 177 ? -4.330  -14.597 19.093  1.00 28.36  ?  208  VAL A O   1 
ATOM   1289  C  CB  . VAL A  1 177 ? -6.525  -14.925 17.174  1.00 34.37  ?  208  VAL A CB  1 
ATOM   1290  C  CG1 . VAL A  1 177 ? -7.686  -14.372 16.315  1.00 33.65  ?  208  VAL A CG1 1 
ATOM   1291  C  CG2 . VAL A  1 177 ? -6.357  -16.423 16.879  1.00 36.32  ?  208  VAL A CG2 1 
ATOM   1292  N  N   . PHE A  1 178 ? -2.889  -14.785 17.364  1.00 30.32  ?  209  PHE A N   1 
ATOM   1293  C  CA  . PHE A  1 178 ? -1.748  -15.126 18.218  1.00 30.46  ?  209  PHE A CA  1 
ATOM   1294  C  C   . PHE A  1 178 ? -1.443  -13.991 19.192  1.00 33.65  ?  209  PHE A C   1 
ATOM   1295  O  O   . PHE A  1 178 ? -1.525  -12.814 18.829  1.00 34.93  ?  209  PHE A O   1 
ATOM   1296  C  CB  . PHE A  1 178 ? -0.465  -15.345 17.408  1.00 33.22  ?  209  PHE A CB  1 
ATOM   1297  C  CG  . PHE A  1 178 ? -0.360  -16.655 16.693  1.00 32.42  ?  209  PHE A CG  1 
ATOM   1298  C  CD1 . PHE A  1 178 ? -1.360  -17.618 16.757  1.00 32.82  ?  209  PHE A CD1 1 
ATOM   1299  C  CD2 . PHE A  1 178 ? 0.772   -16.908 15.906  1.00 36.91  ?  209  PHE A CD2 1 
ATOM   1300  C  CE1 . PHE A  1 178 ? -1.218  -18.822 16.058  1.00 32.94  ?  209  PHE A CE1 1 
ATOM   1301  C  CE2 . PHE A  1 178 ? 0.914   -18.102 15.202  1.00 35.08  ?  209  PHE A CE2 1 
ATOM   1302  C  CZ  . PHE A  1 178 ? -0.082  -19.063 15.283  1.00 32.41  ?  209  PHE A CZ  1 
ATOM   1303  N  N   . PRO A  1 179 ? -0.979  -14.310 20.400  1.00 36.48  ?  210  PRO A N   1 
ATOM   1304  C  CA  . PRO A  1 179 ? -0.440  -13.258 21.274  1.00 30.93  ?  210  PRO A CA  1 
ATOM   1305  C  C   . PRO A  1 179 ? 0.679   -12.511 20.568  1.00 26.95  ?  210  PRO A C   1 
ATOM   1306  O  O   . PRO A  1 179 ? 1.480   -13.103 19.847  1.00 33.54  ?  210  PRO A O   1 
ATOM   1307  C  CB  . PRO A  1 179 ? 0.086   -14.039 22.495  1.00 33.97  ?  210  PRO A CB  1 
ATOM   1308  C  CG  . PRO A  1 179 ? -0.747  -15.297 22.505  1.00 42.27  ?  210  PRO A CG  1 
ATOM   1309  C  CD  . PRO A  1 179 ? -0.955  -15.638 21.042  1.00 34.81  ?  210  PRO A CD  1 
ATOM   1310  N  N   . MET A  1 180 ? 0.723   -11.191 20.757  1.00 28.58  ?  211  MET A N   1 
ATOM   1311  C  CA  . MET A  1 180 ? 1.848   -10.474 20.191  1.00 28.96  ?  211  MET A CA  1 
ATOM   1312  C  C   . MET A  1 180 ? 3.049   -10.603 21.124  1.00 34.20  ?  211  MET A C   1 
ATOM   1313  O  O   . MET A  1 180 ? 2.945   -11.131 22.228  1.00 30.80  ?  211  MET A O   1 
ATOM   1314  C  CB  . MET A  1 180 ? 1.515   -9.006  19.918  1.00 27.97  ?  211  MET A CB  1 
ATOM   1315  C  CG  . MET A  1 180 ? 0.333   -8.796  18.921  1.00 27.03  ?  211  MET A CG  1 
ATOM   1316  S  SD  . MET A  1 180 ? 0.181   -7.045  18.458  1.00 29.67  ?  211  MET A SD  1 
ATOM   1317  C  CE  . MET A  1 180 ? -0.182  -6.205  19.991  1.00 28.46  ?  211  MET A CE  1 
ATOM   1318  N  N   . GLU A  1 181 ? 4.192   -10.108 20.676  1.00 29.03  ?  212  GLU A N   1 
ATOM   1319  C  CA  . GLU A  1 181 ? 5.433   -10.330 21.404  1.00 32.19  ?  212  GLU A CA  1 
ATOM   1320  C  C   . GLU A  1 181 ? 6.203   -9.039  21.595  1.00 34.81  ?  212  GLU A C   1 
ATOM   1321  O  O   . GLU A  1 181 ? 6.030   -8.052  20.869  1.00 27.71  ?  212  GLU A O   1 
ATOM   1322  C  CB  . GLU A  1 181 ? 6.335   -11.346 20.688  1.00 35.84  ?  212  GLU A CB  1 
ATOM   1323  C  CG  . GLU A  1 181 ? 6.892   -10.831 19.359  1.00 32.11  ?  212  GLU A CG  1 
ATOM   1324  C  CD  . GLU A  1 181 ? 8.094   -11.615 18.903  1.00 34.05  ?  212  GLU A CD  1 
ATOM   1325  O  OE1 . GLU A  1 181 ? 7.915   -12.638 18.206  1.00 35.13  ?  212  GLU A OE1 1 
ATOM   1326  O  OE2 . GLU A  1 181 ? 9.217   -11.215 19.272  1.00 36.60  -1 212  GLU A OE2 1 
ATOM   1327  N  N   . HIS A  1 182 ? 7.091   -9.073  22.588  1.00 30.30  ?  213  HIS A N   1 
ATOM   1328  C  CA  . HIS A  1 182 ? 8.014   -7.986  22.847  1.00 32.29  ?  213  HIS A CA  1 
ATOM   1329  C  C   . HIS A  1 182 ? 9.378   -8.629  23.044  1.00 36.01  ?  213  HIS A C   1 
ATOM   1330  O  O   . HIS A  1 182 ? 9.579   -9.349  24.024  1.00 34.33  ?  213  HIS A O   1 
ATOM   1331  C  CB  . HIS A  1 182 ? 7.593   -7.186  24.069  1.00 32.70  ?  213  HIS A CB  1 
ATOM   1332  C  CG  . HIS A  1 182 ? 8.542   -6.085  24.411  1.00 37.91  ?  213  HIS A CG  1 
ATOM   1333  N  ND1 . HIS A  1 182 ? 8.708   -5.619  25.698  1.00 43.43  ?  213  HIS A ND1 1 
ATOM   1334  C  CD2 . HIS A  1 182 ? 9.370   -5.348  23.634  1.00 35.90  ?  213  HIS A CD2 1 
ATOM   1335  C  CE1 . HIS A  1 182 ? 9.603   -4.647  25.699  1.00 43.04  ?  213  HIS A CE1 1 
ATOM   1336  N  NE2 . HIS A  1 182 ? 10.016  -4.459  24.459  1.00 40.41  ?  213  HIS A NE2 1 
ATOM   1337  N  N   . ASN A  1 183 ? 10.284  -8.413  22.093  1.00 33.27  ?  214  ASN A N   1 
ATOM   1338  C  CA  . ASN A  1 183 ? 11.599  -9.066  22.057  1.00 38.24  ?  214  ASN A CA  1 
ATOM   1339  C  C   . ASN A  1 183 ? 11.498  -10.549 22.404  1.00 41.87  ?  214  ASN A C   1 
ATOM   1340  O  O   . ASN A  1 183 ? 12.290  -11.097 23.169  1.00 33.19  ?  214  ASN A O   1 
ATOM   1341  C  CB  . ASN A  1 183 ? 12.589  -8.367  22.977  1.00 35.34  ?  214  ASN A CB  1 
ATOM   1342  C  CG  . ASN A  1 183 ? 12.825  -6.939  22.576  1.00 38.25  ?  214  ASN A CG  1 
ATOM   1343  O  OD1 . ASN A  1 183 ? 12.862  -6.613  21.383  1.00 34.54  ?  214  ASN A OD1 1 
ATOM   1344  N  ND2 . ASN A  1 183 ? 12.985  -6.070  23.562  1.00 40.57  ?  214  ASN A ND2 1 
ATOM   1345  N  N   . GLY A  1 184 ? 10.502  -11.208 21.827  1.00 33.62  ?  215  GLY A N   1 
ATOM   1346  C  CA  . GLY A  1 184 ? 10.369  -12.639 21.977  1.00 32.93  ?  215  GLY A CA  1 
ATOM   1347  C  C   . GLY A  1 184 ? 9.572   -13.094 23.173  1.00 35.89  ?  215  GLY A C   1 
ATOM   1348  O  O   . GLY A  1 184 ? 9.307   -14.295 23.287  1.00 39.55  ?  215  GLY A O   1 
ATOM   1349  N  N   . LYS A  1 185 ? 9.166   -12.172 24.070  1.00 35.82  ?  216  LYS A N   1 
ATOM   1350  C  CA  . LYS A  1 185 ? 8.311   -12.481 25.207  1.00 36.01  ?  216  LYS A CA  1 
ATOM   1351  C  C   . LYS A  1 185 ? 6.882   -12.060 24.911  1.00 38.10  ?  216  LYS A C   1 
ATOM   1352  O  O   . LYS A  1 185 ? 6.644   -11.226 24.036  1.00 36.19  ?  216  LYS A O   1 
ATOM   1353  C  CB  . LYS A  1 185 ? 8.811   -11.761 26.468  1.00 39.88  ?  216  LYS A CB  1 
ATOM   1354  C  CG  . LYS A  1 185 ? 10.293  -12.018 26.792  1.00 49.49  ?  216  LYS A CG  1 
ATOM   1355  C  CD  . LYS A  1 185 ? 10.747  -11.324 28.086  1.00 51.64  ?  216  LYS A CD  1 
ATOM   1356  C  CE  . LYS A  1 185 ? 11.805  -12.152 28.840  1.00 63.52  ?  216  LYS A CE  1 
ATOM   1357  N  NZ  . LYS A  1 185 ? 12.420  -11.417 30.012  1.00 62.01  ?  216  LYS A NZ  1 
ATOM   1358  N  N   . PRO A  1 186 ? 5.903   -12.613 25.625  1.00 41.27  ?  217  PRO A N   1 
ATOM   1359  C  CA  . PRO A  1 186 ? 4.517   -12.195 25.420  1.00 40.34  ?  217  PRO A CA  1 
ATOM   1360  C  C   . PRO A  1 186 ? 4.336   -10.706 25.670  1.00 43.65  ?  217  PRO A C   1 
ATOM   1361  O  O   . PRO A  1 186 ? 4.922   -10.132 26.590  1.00 36.94  ?  217  PRO A O   1 
ATOM   1362  C  CB  . PRO A  1 186 ? 3.741   -13.047 26.433  1.00 38.58  ?  217  PRO A CB  1 
ATOM   1363  C  CG  . PRO A  1 186 ? 4.771   -13.486 27.416  1.00 45.61  ?  217  PRO A CG  1 
ATOM   1364  C  CD  . PRO A  1 186 ? 5.973   -13.737 26.578  1.00 47.44  ?  217  PRO A CD  1 
ATOM   1365  N  N   . ALA A  1 187 ? 3.516   -10.079 24.814  1.00 36.07  ?  218  ALA A N   1 
ATOM   1366  C  CA  . ALA A  1 187 ? 3.293   -8.639  24.875  1.00 33.92  ?  218  ALA A CA  1 
ATOM   1367  C  C   . ALA A  1 187 ? 2.262   -8.263  25.929  1.00 33.94  ?  218  ALA A C   1 
ATOM   1368  O  O   . ALA A  1 187 ? 2.346   -7.170  26.503  1.00 35.88  ?  218  ALA A O   1 
ATOM   1369  C  CB  . ALA A  1 187 ? 2.838   -8.113  23.506  1.00 30.41  ?  218  ALA A CB  1 
ATOM   1370  N  N   . ASN A  1 188 ? 1.296   -9.143  26.195  1.00 35.15  ?  219  ASN A N   1 
ATOM   1371  C  CA  . ASN A  1 188 ? 0.158   -8.841  27.077  1.00 35.24  ?  219  ASN A CA  1 
ATOM   1372  C  C   . ASN A  1 188 ? -0.422  -7.459  26.771  1.00 38.41  ?  219  ASN A C   1 
ATOM   1373  O  O   . ASN A  1 188 ? -0.627  -6.622  27.654  1.00 32.83  ?  219  ASN A O   1 
ATOM   1374  C  CB  . ASN A  1 188 ? 0.552   -8.961  28.555  1.00 41.05  ?  219  ASN A CB  1 
ATOM   1375  C  CG  . ASN A  1 188 ? 1.261   -10.268 28.863  1.00 38.20  ?  219  ASN A CG  1 
ATOM   1376  O  OD1 . ASN A  1 188 ? 0.691   -11.355 28.691  1.00 38.91  ?  219  ASN A OD1 1 
ATOM   1377  N  ND2 . ASN A  1 188 ? 2.509   -10.172 29.320  1.00 38.88  ?  219  ASN A ND2 1 
ATOM   1378  N  N   . GLU A  1 189 ? -0.689  -7.227  25.484  1.00 36.46  ?  220  GLU A N   1 
ATOM   1379  C  CA  . GLU A  1 189 ? -1.311  -5.978  25.060  1.00 30.74  ?  220  GLU A CA  1 
ATOM   1380  C  C   . GLU A  1 189 ? -2.672  -5.832  25.725  1.00 28.49  ?  220  GLU A C   1 
ATOM   1381  O  O   . GLU A  1 189 ? -3.425  -6.795  25.844  1.00 33.24  ?  220  GLU A O   1 
ATOM   1382  C  CB  . GLU A  1 189 ? -1.465  -5.959  23.531  1.00 31.05  ?  220  GLU A CB  1 
ATOM   1383  C  CG  . GLU A  1 189 ? -2.147  -4.701  22.980  1.00 27.97  ?  220  GLU A CG  1 
ATOM   1384  C  CD  . GLU A  1 189 ? -1.356  -3.443  23.310  1.00 30.91  ?  220  GLU A CD  1 
ATOM   1385  O  OE1 . GLU A  1 189 ? -0.250  -3.282  22.756  1.00 33.38  ?  220  GLU A OE1 1 
ATOM   1386  O  OE2 . GLU A  1 189 ? -1.814  -2.635  24.149  1.00 32.14  -1 220  GLU A OE2 1 
ATOM   1387  N  N   . THR A  1 190 ? -2.992  -4.622  26.161  1.00 27.18  ?  221  THR A N   1 
ATOM   1388  C  CA  . THR A  1 190 ? -4.317  -4.342  26.692  1.00 35.21  ?  221  THR A CA  1 
ATOM   1389  C  C   . THR A  1 190 ? -5.104  -3.318  25.892  1.00 33.72  ?  221  THR A C   1 
ATOM   1390  O  O   . THR A  1 190 ? -6.277  -3.092  26.218  1.00 30.20  ?  221  THR A O   1 
ATOM   1391  C  CB  . THR A  1 190 ? -4.234  -3.823  28.130  1.00 35.83  ?  221  THR A CB  1 
ATOM   1392  O  OG1 . THR A  1 190 ? -3.399  -2.666  28.140  1.00 36.87  ?  221  THR A OG1 1 
ATOM   1393  C  CG2 . THR A  1 190 ? -3.659  -4.885  29.069  1.00 35.79  ?  221  THR A CG2 1 
ATOM   1394  N  N   . GLU A  1 191 ? -4.507  -2.673  24.890  1.00 29.83  ?  222  GLU A N   1 
ATOM   1395  C  CA  . GLU A  1 191 ? -5.184  -1.617  24.143  1.00 30.96  ?  222  GLU A CA  1 
ATOM   1396  C  C   . GLU A  1 191 ? -5.492  -2.063  22.716  1.00 26.33  ?  222  GLU A C   1 
ATOM   1397  O  O   . GLU A  1 191 ? -4.852  -2.967  22.163  1.00 26.84  ?  222  GLU A O   1 
ATOM   1398  C  CB  . GLU A  1 191 ? -4.321  -0.344  24.115  1.00 31.74  ?  222  GLU A CB  1 
ATOM   1399  C  CG  . GLU A  1 191 ? -4.069  0.266   25.479  1.00 32.71  ?  222  GLU A CG  1 
ATOM   1400  C  CD  . GLU A  1 191 ? -3.443  1.640   25.389  1.00 40.08  ?  222  GLU A CD  1 
ATOM   1401  O  OE1 . GLU A  1 191 ? -4.101  2.569   24.874  1.00 35.67  ?  222  GLU A OE1 1 
ATOM   1402  O  OE2 . GLU A  1 191 ? -2.278  1.785   25.823  1.00 36.70  -1 222  GLU A OE2 1 
ATOM   1403  N  N   . TYR A  1 192 ? -6.476  -1.410  22.108  1.00 31.02  ?  223  TYR A N   1 
ATOM   1404  C  CA  . TYR A  1 192 ? -6.627  -1.462  20.653  1.00 27.07  ?  223  TYR A CA  1 
ATOM   1405  C  C   . TYR A  1 192 ? -5.250  -1.301  20.024  1.00 24.49  ?  223  TYR A C   1 
ATOM   1406  O  O   . TYR A  1 192 ? -4.497  -0.399  20.403  1.00 26.14  ?  223  TYR A O   1 
ATOM   1407  C  CB  . TYR A  1 192 ? -7.560  -0.332  20.217  1.00 30.48  ?  223  TYR A CB  1 
ATOM   1408  C  CG  . TYR A  1 192 ? -7.825  -0.172  18.738  1.00 30.97  ?  223  TYR A CG  1 
ATOM   1409  C  CD1 . TYR A  1 192 ? -8.690  -1.035  18.066  1.00 30.01  ?  223  TYR A CD1 1 
ATOM   1410  C  CD2 . TYR A  1 192 ? -7.291  0.904   18.032  1.00 29.51  ?  223  TYR A CD2 1 
ATOM   1411  C  CE1 . TYR A  1 192 ? -8.980  -0.860  16.714  1.00 26.01  ?  223  TYR A CE1 1 
ATOM   1412  C  CE2 . TYR A  1 192 ? -7.578  1.084   16.673  1.00 25.11  ?  223  TYR A CE2 1 
ATOM   1413  C  CZ  . TYR A  1 192 ? -8.413  0.200   16.020  1.00 28.05  ?  223  TYR A CZ  1 
ATOM   1414  O  OH  . TYR A  1 192 ? -8.685  0.402   14.674  1.00 27.05  ?  223  TYR A OH  1 
ATOM   1415  N  N   . ILE A  1 193 ? -4.870  -2.224  19.131  1.00 24.04  ?  224  ILE A N   1 
ATOM   1416  C  CA  . ILE A  1 193 ? -3.419  -2.392  18.944  1.00 24.53  ?  224  ILE A CA  1 
ATOM   1417  C  C   . ILE A  1 193 ? -2.788  -1.196  18.251  1.00 27.91  ?  224  ILE A C   1 
ATOM   1418  O  O   . ILE A  1 193 ? -1.603  -0.934  18.453  1.00 25.58  ?  224  ILE A O   1 
ATOM   1419  C  CB  . ILE A  1 193 ? -3.052  -3.694  18.208  1.00 26.47  ?  224  ILE A CB  1 
ATOM   1420  C  CG1 . ILE A  1 193 ? -3.566  -3.686  16.757  1.00 27.32  ?  224  ILE A CG1 1 
ATOM   1421  C  CG2 . ILE A  1 193 ? -3.558  -4.918  19.005  1.00 27.35  ?  224  ILE A CG2 1 
ATOM   1422  C  CD1 . ILE A  1 193 ? -3.094  -4.929  15.932  1.00 25.70  ?  224  ILE A CD1 1 
ATOM   1423  N  N   . THR A  1 194 ? -3.551  -0.438  17.471  1.00 26.06  ?  225  THR A N   1 
ATOM   1424  C  CA  . THR A  1 194 ? -3.021  0.817   16.942  1.00 25.75  ?  225  THR A CA  1 
ATOM   1425  C  C   . THR A  1 194 ? -2.567  1.723   18.075  1.00 25.43  ?  225  THR A C   1 
ATOM   1426  O  O   . THR A  1 194 ? -1.478  2.307   18.021  1.00 26.92  ?  225  THR A O   1 
ATOM   1427  C  CB  . THR A  1 194 ? -4.092  1.512   16.086  1.00 24.48  ?  225  THR A CB  1 
ATOM   1428  O  OG1 . THR A  1 194 ? -4.463  0.645   15.012  1.00 23.17  ?  225  THR A OG1 1 
ATOM   1429  C  CG2 . THR A  1 194 ? -3.571  2.846   15.540  1.00 24.05  ?  225  THR A CG2 1 
ATOM   1430  N  N   . ASP A  1 195 ? -3.391  1.839   19.123  1.00 26.67  ?  226  ASP A N   1 
ATOM   1431  C  CA  . ASP A  1 195 ? -3.028  2.655   20.278  1.00 26.75  ?  226  ASP A CA  1 
ATOM   1432  C  C   . ASP A  1 195 ? -1.831  2.058   21.006  1.00 29.10  ?  226  ASP A C   1 
ATOM   1433  O  O   . ASP A  1 195 ? -0.990  2.791   21.541  1.00 29.67  ?  226  ASP A O   1 
ATOM   1434  C  CB  . ASP A  1 195 ? -4.210  2.784   21.257  1.00 29.55  ?  226  ASP A CB  1 
ATOM   1435  C  CG  . ASP A  1 195 ? -5.384  3.589   20.698  1.00 29.81  ?  226  ASP A CG  1 
ATOM   1436  O  OD1 . ASP A  1 195 ? -5.200  4.434   19.801  1.00 29.68  ?  226  ASP A OD1 1 
ATOM   1437  O  OD2 . ASP A  1 195 ? -6.514  3.401   21.194  1.00 31.49  -1 226  ASP A OD2 1 
ATOM   1438  N  N   . GLY A  1 196 ? -1.750  0.726   21.054  1.00 27.92  ?  227  GLY A N   1 
ATOM   1439  C  CA  . GLY A  1 196 ? -0.585  0.092   21.641  1.00 28.01  ?  227  GLY A CA  1 
ATOM   1440  C  C   . GLY A  1 196 ? 0.685   0.371   20.867  1.00 27.52  ?  227  GLY A C   1 
ATOM   1441  O  O   . GLY A  1 196 ? 1.733   0.648   21.462  1.00 26.83  ?  227  GLY A O   1 
ATOM   1442  N  N   . PHE A  1 197 ? 0.625   0.274   19.528  1.00 25.79  ?  228  PHE A N   1 
ATOM   1443  C  CA  . PHE A  1 197 ? 1.812   0.581   18.728  1.00 25.06  ?  228  PHE A CA  1 
ATOM   1444  C  C   . PHE A  1 197 ? 2.224   2.041   18.896  1.00 26.33  ?  228  PHE A C   1 
ATOM   1445  O  O   . PHE A  1 197 ? 3.418   2.343   19.035  1.00 29.62  ?  228  PHE A O   1 
ATOM   1446  C  CB  . PHE A  1 197 ? 1.564   0.233   17.252  1.00 26.79  ?  228  PHE A CB  1 
ATOM   1447  C  CG  . PHE A  1 197 ? 1.256   -1.219  17.021  1.00 27.86  ?  228  PHE A CG  1 
ATOM   1448  C  CD1 . PHE A  1 197 ? 1.827   -2.201  17.830  1.00 27.00  ?  228  PHE A CD1 1 
ATOM   1449  C  CD2 . PHE A  1 197 ? 0.370   -1.606  16.013  1.00 26.50  ?  228  PHE A CD2 1 
ATOM   1450  C  CE1 . PHE A  1 197 ? 1.536   -3.539  17.639  1.00 29.46  ?  228  PHE A CE1 1 
ATOM   1451  C  CE2 . PHE A  1 197 ? 0.080   -2.939  15.802  1.00 27.62  ?  228  PHE A CE2 1 
ATOM   1452  C  CZ  . PHE A  1 197 ? 0.662   -3.920  16.608  1.00 24.09  ?  228  PHE A CZ  1 
ATOM   1453  N  N   . SER A  1 198 ? 1.252   2.957   18.960  1.00 23.14  ?  229  SER A N   1 
ATOM   1454  C  CA  . SER A  1 198 ? 1.589   4.348   19.254  1.00 24.45  ?  229  SER A CA  1 
ATOM   1455  C  C   . SER A  1 198 ? 2.255   4.479   20.627  1.00 27.34  ?  229  SER A C   1 
ATOM   1456  O  O   . SER A  1 198 ? 3.224   5.225   20.780  1.00 26.07  ?  229  SER A O   1 
ATOM   1457  C  CB  . SER A  1 198 ? 0.341   5.226   19.173  1.00 25.52  ?  229  SER A CB  1 
ATOM   1458  O  OG  . SER A  1 198 ? -0.362  5.017   17.945  1.00 26.38  ?  229  SER A OG  1 
ATOM   1459  N  N   . ARG A  1 199 ? 1.766   3.737   21.628  1.00 29.62  ?  230  ARG A N   1 
ATOM   1460  C  CA  . ARG A  1 199 ? 2.360   3.787   22.968  1.00 30.79  ?  230  ARG A CA  1 
ATOM   1461  C  C   . ARG A  1 199 ? 3.816   3.336   22.950  1.00 30.24  ?  230  ARG A C   1 
ATOM   1462  O  O   . ARG A  1 199 ? 4.687   3.982   23.544  1.00 32.55  ?  230  ARG A O   1 
ATOM   1463  C  CB  . ARG A  1 199 ? 1.549   2.915   23.933  1.00 30.91  ?  230  ARG A CB  1 
ATOM   1464  C  CG  . ARG A  1 199 ? 2.102   2.833   25.365  1.00 34.52  ?  230  ARG A CG  1 
ATOM   1465  C  CD  . ARG A  1 199 ? 1.519   1.623   26.113  1.00 32.05  ?  230  ARG A CD  1 
ATOM   1466  N  NE  . ARG A  1 199 ? 1.894   0.362   25.484  1.00 30.88  ?  230  ARG A NE  1 
ATOM   1467  C  CZ  . ARG A  1 199 ? 1.033   -0.544  25.040  1.00 31.43  ?  230  ARG A CZ  1 
ATOM   1468  N  NH1 . ARG A  1 199 ? -0.274  -0.354  25.121  1.00 31.20  ?  230  ARG A NH1 1 
ATOM   1469  N  NH2 . ARG A  1 199 ? 1.495   -1.664  24.483  1.00 29.20  ?  230  ARG A NH2 1 
ATOM   1470  N  N   . GLU A  1 200 ? 4.097   2.224   22.275  1.00 28.42  ?  231  GLU A N   1 
ATOM   1471  C  CA  . GLU A  1 200 ? 5.459   1.703   22.204  1.00 30.88  ?  231  GLU A CA  1 
ATOM   1472  C  C   . GLU A  1 200 ? 6.391   2.629   21.431  1.00 32.06  ?  231  GLU A C   1 
ATOM   1473  O  O   . GLU A  1 200 ? 7.600   2.691   21.728  1.00 28.45  ?  231  GLU A O   1 
ATOM   1474  C  CB  . GLU A  1 200 ? 5.431   0.312   21.568  1.00 29.63  ?  231  GLU A CB  1 
ATOM   1475  C  CG  . GLU A  1 200 ? 4.674   -0.742  22.411  1.00 29.85  ?  231  GLU A CG  1 
ATOM   1476  C  CD  . GLU A  1 200 ? 5.198   -0.864  23.837  1.00 31.68  ?  231  GLU A CD  1 
ATOM   1477  O  OE1 . GLU A  1 200 ? 6.415   -0.971  24.017  1.00 31.37  ?  231  GLU A OE1 1 
ATOM   1478  O  OE2 . GLU A  1 200 ? 4.394   -0.863  24.780  1.00 34.06  -1 231  GLU A OE2 1 
ATOM   1479  N  N   . ALA A  1 201 ? 5.869   3.337   20.427  1.00 26.96  ?  232  ALA A N   1 
ATOM   1480  C  CA  . ALA A  1 201 ? 6.690   4.314   19.718  1.00 24.95  ?  232  ALA A CA  1 
ATOM   1481  C  C   . ALA A  1 201 ? 7.115   5.434   20.653  1.00 30.73  ?  232  ALA A C   1 
ATOM   1482  O  O   . ALA A  1 201 ? 8.304   5.785   20.729  1.00 30.44  ?  232  ALA A O   1 
ATOM   1483  C  CB  . ALA A  1 201 ? 5.924   4.867   18.503  1.00 28.76  ?  232  ALA A CB  1 
ATOM   1484  N  N   . ILE A  1 202 ? 6.149   5.994   21.384  1.00 28.08  ?  233  ILE A N   1 
ATOM   1485  C  CA  . ILE A  1 202 ? 6.428   7.014   22.396  1.00 26.30  ?  233  ILE A CA  1 
ATOM   1486  C  C   . ILE A  1 202 ? 7.486   6.526   23.388  1.00 33.37  ?  233  ILE A C   1 
ATOM   1487  O  O   . ILE A  1 202 ? 8.433   7.250   23.715  1.00 28.81  ?  233  ILE A O   1 
ATOM   1488  C  CB  . ILE A  1 202 ? 5.123   7.408   23.110  1.00 29.91  ?  233  ILE A CB  1 
ATOM   1489  C  CG1 . ILE A  1 202 ? 4.188   8.143   22.117  1.00 32.24  ?  233  ILE A CG1 1 
ATOM   1490  C  CG2 . ILE A  1 202 ? 5.385   8.199   24.406  1.00 35.22  ?  233  ILE A CG2 1 
ATOM   1491  C  CD1 . ILE A  1 202 ? 2.765   8.186   22.541  1.00 28.58  ?  233  ILE A CD1 1 
ATOM   1492  N  N   . LYS A  1 203 ? 7.339   5.294   23.879  1.00 30.86  ?  234  LYS A N   1 
ATOM   1493  C  CA  . LYS A  1 203 ? 8.280   4.771   24.866  1.00 32.01  ?  234  LYS A CA  1 
ATOM   1494  C  C   . LYS A  1 203 ? 9.681   4.664   24.271  1.00 35.50  ?  234  LYS A C   1 
ATOM   1495  O  O   . LYS A  1 203 ? 10.661  5.132   24.862  1.00 30.94  ?  234  LYS A O   1 
ATOM   1496  C  CB  . LYS A  1 203 ? 7.780   3.417   25.374  1.00 34.66  ?  234  LYS A CB  1 
ATOM   1497  C  CG  . LYS A  1 203 ? 8.739   2.675   26.290  1.00 35.37  ?  234  LYS A CG  1 
ATOM   1498  C  CD  . LYS A  1 203 ? 8.351   1.202   26.403  1.00 35.47  ?  234  LYS A CD  1 
ATOM   1499  C  CE  . LYS A  1 203 ? 8.645   0.629   27.787  1.00 43.14  ?  234  LYS A CE  1 
ATOM   1500  N  NZ  . LYS A  1 203 ? 8.895   -0.863  27.747  1.00 44.13  ?  234  LYS A NZ  1 
ATOM   1501  N  N   . ASN A  1 204 ? 9.793   4.083   23.081  1.00 30.37  ?  235  ASN A N   1 
ATOM   1502  C  CA  . ASN A  1 204 ? 11.095  4.014   22.424  1.00 33.71  ?  235  ASN A CA  1 
ATOM   1503  C  C   . ASN A  1 204 ? 11.686  5.390   22.135  1.00 33.37  ?  235  ASN A C   1 
ATOM   1504  O  O   . ASN A  1 204 ? 12.904  5.583   22.288  1.00 33.48  ?  235  ASN A O   1 
ATOM   1505  C  CB  . ASN A  1 204 ? 10.994  3.118   21.190  1.00 29.99  ?  235  ASN A CB  1 
ATOM   1506  C  CG  . ASN A  1 204 ? 10.822  1.662   21.592  1.00 34.58  ?  235  ASN A CG  1 
ATOM   1507  O  OD1 . ASN A  1 204 ? 9.729   1.169   21.787  1.00 40.66  ?  235  ASN A OD1 1 
ATOM   1508  N  ND2 . ASN A  1 204 ? 11.950  0.975   21.766  1.00 39.12  ?  235  ASN A ND2 1 
ATOM   1509  N  N   . ILE A  1 205 ? 10.861  6.376   21.763  1.00 29.17  ?  236  ILE A N   1 
ATOM   1510  C  CA  . ILE A  1 205 ? 11.388  7.740   21.660  1.00 32.30  ?  236  ILE A CA  1 
ATOM   1511  C  C   . ILE A  1 205 ? 11.960  8.200   23.005  1.00 35.57  ?  236  ILE A C   1 
ATOM   1512  O  O   . ILE A  1 205 ? 13.021  8.837   23.060  1.00 29.79  ?  236  ILE A O   1 
ATOM   1513  C  CB  . ILE A  1 205 ? 10.304  8.707   21.145  1.00 29.89  ?  236  ILE A CB  1 
ATOM   1514  C  CG1 . ILE A  1 205 ? 9.972   8.428   19.682  1.00 31.18  ?  236  ILE A CG1 1 
ATOM   1515  C  CG2 . ILE A  1 205 ? 10.750  10.161  21.269  1.00 28.80  ?  236  ILE A CG2 1 
ATOM   1516  C  CD1 . ILE A  1 205 ? 8.676   9.083   19.259  1.00 25.37  ?  236  ILE A CD1 1 
ATOM   1517  N  N   . LYS A  1 206 ? 11.275  7.883   24.114  1.00 34.04  ?  237  LYS A N   1 
ATOM   1518  C  CA  . LYS A  1 206 ? 11.774  8.335   25.414  1.00 33.62  ?  237  LYS A CA  1 
ATOM   1519  C  C   . LYS A  1 206 ? 13.028  7.577   25.819  1.00 34.99  ?  237  LYS A C   1 
ATOM   1520  O  O   . LYS A  1 206 ? 13.926  8.155   26.443  1.00 37.44  ?  237  LYS A O   1 
ATOM   1521  C  CB  . LYS A  1 206 ? 10.708  8.201   26.501  1.00 36.34  ?  237  LYS A CB  1 
ATOM   1522  C  CG  . LYS A  1 206 ? 9.549   9.183   26.353  1.00 37.20  ?  237  LYS A CG  1 
ATOM   1523  C  CD  . LYS A  1 206 ? 8.371   8.730   27.144  1.00 36.38  ?  237  LYS A CD  1 
ATOM   1524  C  CE  . LYS A  1 206 ? 7.496   9.913   27.536  1.00 45.39  ?  237  LYS A CE  1 
ATOM   1525  N  NZ  . LYS A  1 206 ? 6.139   9.466   27.993  1.00 45.15  ?  237  LYS A NZ  1 
ATOM   1526  N  N   . ILE A  1 207 ? 13.113  6.289   25.472  1.00 31.94  ?  238  ILE A N   1 
ATOM   1527  C  CA  . ILE A  1 207 ? 14.333  5.533   25.743  1.00 36.44  ?  238  ILE A CA  1 
ATOM   1528  C  C   . ILE A  1 207 ? 15.513  6.149   24.996  1.00 34.47  ?  238  ILE A C   1 
ATOM   1529  O  O   . ILE A  1 207 ? 16.590  6.375   25.566  1.00 32.23  ?  238  ILE A O   1 
ATOM   1530  C  CB  . ILE A  1 207 ? 14.134  4.048   25.383  1.00 36.83  ?  238  ILE A CB  1 
ATOM   1531  C  CG1 . ILE A  1 207 ? 13.145  3.375   26.353  1.00 32.49  ?  238  ILE A CG1 1 
ATOM   1532  C  CG2 . ILE A  1 207 ? 15.484  3.324   25.349  1.00 30.26  ?  238  ILE A CG2 1 
ATOM   1533  C  CD1 . ILE A  1 207 ? 12.661  1.977   25.897  1.00 28.39  ?  238  ILE A CD1 1 
ATOM   1534  N  N   . ALA A  1 208 ? 15.325  6.452   23.710  1.00 33.62  ?  239  ALA A N   1 
ATOM   1535  C  CA  . ALA A  1 208 ? 16.400  7.061   22.925  1.00 29.85  ?  239  ALA A CA  1 
ATOM   1536  C  C   . ALA A  1 208 ? 16.826  8.396   23.517  1.00 31.14  ?  239  ALA A C   1 
ATOM   1537  O  O   . ALA A  1 208 ? 18.024  8.701   23.588  1.00 31.68  ?  239  ALA A O   1 
ATOM   1538  C  CB  . ALA A  1 208 ? 15.960  7.251   21.473  1.00 34.63  ?  239  ALA A CB  1 
ATOM   1539  N  N   . ALA A  1 209 ? 15.861  9.201   23.956  1.00 30.34  ?  240  ALA A N   1 
ATOM   1540  C  CA  . ALA A  1 209 ? 16.192  10.447  24.643  1.00 35.40  ?  240  ALA A CA  1 
ATOM   1541  C  C   . ALA A  1 209 ? 17.034  10.183  25.889  1.00 36.25  ?  240  ALA A C   1 
ATOM   1542  O  O   . ALA A  1 209 ? 18.023  10.886  26.139  1.00 32.62  ?  240  ALA A O   1 
ATOM   1543  C  CB  . ALA A  1 209 ? 14.911  11.204  25.011  1.00 30.06  ?  240  ALA A CB  1 
ATOM   1544  N  N   . ALA A  1 210 ? 16.662  9.166   26.677  1.00 30.74  ?  241  ALA A N   1 
ATOM   1545  C  CA  . ALA A  1 210 ? 17.405  8.874   27.903  1.00 36.36  ?  241  ALA A CA  1 
ATOM   1546  C  C   . ALA A  1 210 ? 18.807  8.372   27.598  1.00 34.70  ?  241  ALA A C   1 
ATOM   1547  O  O   . ALA A  1 210 ? 19.757  8.670   28.342  1.00 36.30  ?  241  ALA A O   1 
ATOM   1548  C  CB  . ALA A  1 210 ? 16.645  7.851   28.757  1.00 32.10  ?  241  ALA A CB  1 
ATOM   1549  N  N   . LYS A  1 211 ? 18.959  7.581   26.535  1.00 34.38  ?  242  LYS A N   1 
ATOM   1550  C  CA  . LYS A  1 211 ? 20.275  7.093   26.146  1.00 32.13  ?  242  LYS A CA  1 
ATOM   1551  C  C   . LYS A  1 211 ? 21.114  8.152   25.456  1.00 36.16  ?  242  LYS A C   1 
ATOM   1552  O  O   . LYS A  1 211 ? 22.325  7.947   25.304  1.00 37.28  ?  242  LYS A O   1 
ATOM   1553  C  CB  . LYS A  1 211 ? 20.169  5.877   25.214  1.00 34.22  ?  242  LYS A CB  1 
ATOM   1554  C  CG  . LYS A  1 211 ? 19.444  4.657   25.781  1.00 32.21  ?  242  LYS A CG  1 
ATOM   1555  C  CD  . LYS A  1 211 ? 19.353  3.512   24.762  1.00 33.58  ?  242  LYS A CD  1 
ATOM   1556  C  CE  . LYS A  1 211 ? 20.416  2.428   25.053  1.00 41.00  ?  242  LYS A CE  1 
ATOM   1557  N  NZ  . LYS A  1 211 ? 21.025  1.771   23.842  1.00 41.19  ?  242  LYS A NZ  1 
ATOM   1558  N  N   . LYS A  1 212 ? 20.513  9.262   25.022  1.00 35.05  ?  243  LYS A N   1 
ATOM   1559  C  CA  . LYS A  1 212 ? 21.256  10.318  24.335  1.00 38.78  ?  243  LYS A CA  1 
ATOM   1560  C  C   . LYS A  1 212 ? 21.867  9.776   23.043  1.00 41.30  ?  243  LYS A C   1 
ATOM   1561  O  O   . LYS A  1 212 ? 23.026  10.035  22.717  1.00 35.09  ?  243  LYS A O   1 
ATOM   1562  C  CB  . LYS A  1 212 ? 22.332  10.902  25.262  1.00 41.04  ?  243  LYS A CB  1 
ATOM   1563  C  CG  . LYS A  1 212 ? 21.816  11.896  26.306  1.00 43.52  ?  243  LYS A CG  1 
ATOM   1564  C  CD  . LYS A  1 212 ? 23.015  12.440  27.129  1.00 55.38  ?  243  LYS A CD  1 
ATOM   1565  C  CE  . LYS A  1 212 ? 22.589  13.249  28.355  1.00 55.22  ?  243  LYS A CE  1 
ATOM   1566  N  NZ  . LYS A  1 212 ? 22.605  14.713  28.067  1.00 59.88  ?  243  LYS A NZ  1 
ATOM   1567  N  N   . GLN A  1 213 ? 21.069  9.010   22.302  1.00 35.40  ?  244  GLN A N   1 
ATOM   1568  C  CA  . GLN A  1 213 ? 21.485  8.256   21.137  1.00 35.15  ?  244  GLN A CA  1 
ATOM   1569  C  C   . GLN A  1 213 ? 20.507  8.509   19.998  1.00 33.70  ?  244  GLN A C   1 
ATOM   1570  O  O   . GLN A  1 213 ? 19.300  8.622   20.235  1.00 34.24  ?  244  GLN A O   1 
ATOM   1571  C  CB  . GLN A  1 213 ? 21.529  6.765   21.490  1.00 35.93  ?  244  GLN A CB  1 
ATOM   1572  C  CG  . GLN A  1 213 ? 21.958  5.856   20.407  1.00 35.21  ?  244  GLN A CG  1 
ATOM   1573  C  CD  . GLN A  1 213 ? 22.052  4.431   20.885  1.00 36.74  ?  244  GLN A CD  1 
ATOM   1574  O  OE1 . GLN A  1 213 ? 21.555  4.095   21.960  1.00 40.20  ?  244  GLN A OE1 1 
ATOM   1575  N  NE2 . GLN A  1 213 ? 22.644  3.565   20.066  1.00 35.92  ?  244  GLN A NE2 1 
ATOM   1576  N  N   . PRO A  1 214 ? 20.991  8.671   18.772  1.00 37.06  ?  245  PRO A N   1 
ATOM   1577  C  CA  . PRO A  1 214 ? 20.063  8.802   17.640  1.00 33.49  ?  245  PRO A CA  1 
ATOM   1578  C  C   . PRO A  1 214 ? 19.222  7.545   17.529  1.00 32.84  ?  245  PRO A C   1 
ATOM   1579  O  O   . PRO A  1 214 ? 19.675  6.447   17.858  1.00 30.72  ?  245  PRO A O   1 
ATOM   1580  C  CB  . PRO A  1 214 ? 20.983  8.960   16.421  1.00 36.91  ?  245  PRO A CB  1 
ATOM   1581  C  CG  . PRO A  1 214 ? 22.388  9.027   16.948  1.00 39.96  ?  245  PRO A CG  1 
ATOM   1582  C  CD  . PRO A  1 214 ? 22.371  9.047   18.432  1.00 39.77  ?  245  PRO A CD  1 
ATOM   1583  N  N   . PHE A  1 215 ? 17.982  7.702   17.051  1.00 30.46  ?  246  PHE A N   1 
ATOM   1584  C  CA  . PHE A  1 215 ? 17.104  6.551   16.936  1.00 31.70  ?  246  PHE A CA  1 
ATOM   1585  C  C   . PHE A  1 215 ? 16.698  6.332   15.484  1.00 29.46  ?  246  PHE A C   1 
ATOM   1586  O  O   . PHE A  1 215 ? 16.751  7.247   14.656  1.00 28.27  ?  246  PHE A O   1 
ATOM   1587  C  CB  . PHE A  1 215 ? 15.848  6.664   17.851  1.00 33.36  ?  246  PHE A CB  1 
ATOM   1588  C  CG  . PHE A  1 215 ? 14.833  7.724   17.430  1.00 30.60  ?  246  PHE A CG  1 
ATOM   1589  C  CD1 . PHE A  1 215 ? 13.996  7.538   16.328  1.00 30.98  ?  246  PHE A CD1 1 
ATOM   1590  C  CD2 . PHE A  1 215 ? 14.672  8.872   18.193  1.00 35.44  ?  246  PHE A CD2 1 
ATOM   1591  C  CE1 . PHE A  1 215 ? 13.071  8.502   15.977  1.00 29.91  ?  246  PHE A CE1 1 
ATOM   1592  C  CE2 . PHE A  1 215 ? 13.738  9.842   17.851  1.00 32.10  ?  246  PHE A CE2 1 
ATOM   1593  C  CZ  . PHE A  1 215 ? 12.930  9.655   16.757  1.00 25.70  ?  246  PHE A CZ  1 
ATOM   1594  N  N   . PHE A  1 216 ? 16.381  5.076   15.181  1.00 30.12  ?  247  PHE A N   1 
ATOM   1595  C  CA  . PHE A  1 216 ? 15.672  4.687   13.971  1.00 27.36  ?  247  PHE A CA  1 
ATOM   1596  C  C   . PHE A  1 216 ? 14.504  3.828   14.416  1.00 29.94  ?  247  PHE A C   1 
ATOM   1597  O  O   . PHE A  1 216 ? 14.703  2.772   15.027  1.00 28.40  ?  247  PHE A O   1 
ATOM   1598  C  CB  . PHE A  1 216 ? 16.579  3.929   13.002  1.00 26.98  ?  247  PHE A CB  1 
ATOM   1599  C  CG  . PHE A  1 216 ? 15.850  3.300   11.851  1.00 28.00  ?  247  PHE A CG  1 
ATOM   1600  C  CD1 . PHE A  1 216 ? 15.384  4.067   10.804  1.00 30.73  ?  247  PHE A CD1 1 
ATOM   1601  C  CD2 . PHE A  1 216 ? 15.628  1.931   11.825  1.00 31.60  ?  247  PHE A CD2 1 
ATOM   1602  C  CE1 . PHE A  1 216 ? 14.706  3.484   9.746   1.00 30.43  ?  247  PHE A CE1 1 
ATOM   1603  C  CE2 . PHE A  1 216 ? 14.960  1.341   10.769  1.00 30.78  ?  247  PHE A CE2 1 
ATOM   1604  C  CZ  . PHE A  1 216 ? 14.497  2.114   9.734   1.00 29.45  ?  247  PHE A CZ  1 
ATOM   1605  N  N   . ILE A  1 217 ? 13.288  4.281   14.139  1.00 26.62  ?  248  ILE A N   1 
ATOM   1606  C  CA  . ILE A  1 217 ? 12.096  3.560   14.560  1.00 25.60  ?  248  ILE A CA  1 
ATOM   1607  C  C   . ILE A  1 217 ? 11.311  3.205   13.308  1.00 25.41  ?  248  ILE A C   1 
ATOM   1608  O  O   . ILE A  1 217 ? 10.997  4.088   12.506  1.00 26.49  ?  248  ILE A O   1 
ATOM   1609  C  CB  . ILE A  1 217 ? 11.241  4.384   15.532  1.00 26.61  ?  248  ILE A CB  1 
ATOM   1610  C  CG1 . ILE A  1 217 ? 11.953  4.506   16.886  1.00 30.99  ?  248  ILE A CG1 1 
ATOM   1611  C  CG2 . ILE A  1 217 ? 9.883   3.721   15.702  1.00 27.33  ?  248  ILE A CG2 1 
ATOM   1612  C  CD1 . ILE A  1 217 ? 11.360  5.575   17.827  1.00 26.78  ?  248  ILE A CD1 1 
ATOM   1613  N  N   . TYR A  1 218 ? 11.044  1.922   13.120  1.00 23.92  ?  249  TYR A N   1 
ATOM   1614  C  CA  . TYR A  1 218 ? 10.241  1.425   12.008  1.00 28.42  ?  249  TYR A CA  1 
ATOM   1615  C  C   . TYR A  1 218 ? 8.867   1.096   12.578  1.00 24.18  ?  249  TYR A C   1 
ATOM   1616  O  O   . TYR A  1 218 ? 8.667   0.033   13.169  1.00 25.59  ?  249  TYR A O   1 
ATOM   1617  C  CB  . TYR A  1 218 ? 10.930  0.224   11.375  1.00 25.48  ?  249  TYR A CB  1 
ATOM   1618  C  CG  . TYR A  1 218 ? 10.201  -0.499  10.258  1.00 28.16  ?  249  TYR A CG  1 
ATOM   1619  C  CD1 . TYR A  1 218 ? 10.191  -0.001  8.963   1.00 28.44  ?  249  TYR A CD1 1 
ATOM   1620  C  CD2 . TYR A  1 218 ? 9.613   -1.733  10.484  1.00 30.86  ?  249  TYR A CD2 1 
ATOM   1621  C  CE1 . TYR A  1 218 ? 9.576   -0.687  7.928   1.00 27.82  ?  249  TYR A CE1 1 
ATOM   1622  C  CE2 . TYR A  1 218 ? 8.994   -2.437  9.452   1.00 23.94  ?  249  TYR A CE2 1 
ATOM   1623  C  CZ  . TYR A  1 218 ? 8.991   -1.911  8.180   1.00 25.71  ?  249  TYR A CZ  1 
ATOM   1624  O  OH  . TYR A  1 218 ? 8.380   -2.610  7.159   1.00 27.41  ?  249  TYR A OH  1 
ATOM   1625  N  N   . LEU A  1 219 ? 7.936   2.043   12.447  1.00 27.27  ?  250  LEU A N   1 
ATOM   1626  C  CA  . LEU A  1 219 ? 6.590   1.935   13.026  1.00 25.67  ?  250  LEU A CA  1 
ATOM   1627  C  C   . LEU A  1 219 ? 5.620   1.480   11.926  1.00 25.27  ?  250  LEU A C   1 
ATOM   1628  O  O   . LEU A  1 219 ? 5.165   2.288   11.107  1.00 24.36  ?  250  LEU A O   1 
ATOM   1629  C  CB  . LEU A  1 219 ? 6.191   3.274   13.657  1.00 24.71  ?  250  LEU A CB  1 
ATOM   1630  C  CG  . LEU A  1 219 ? 4.743   3.489   14.122  1.00 26.44  ?  250  LEU A CG  1 
ATOM   1631  C  CD1 . LEU A  1 219 ? 4.264   2.385   15.059  1.00 22.83  ?  250  LEU A CD1 1 
ATOM   1632  C  CD2 . LEU A  1 219 ? 4.549   4.861   14.745  1.00 23.52  ?  250  LEU A CD2 1 
ATOM   1633  N  N   . ALA A  1 220 ? 5.313   0.182   11.925  1.00 26.49  ?  251  ALA A N   1 
ATOM   1634  C  CA  . ALA A  1 220 ? 4.545   -0.485  10.879  1.00 27.26  ?  251  ALA A CA  1 
ATOM   1635  C  C   . ALA A  1 220 ? 3.135   -0.789  11.381  1.00 24.90  ?  251  ALA A C   1 
ATOM   1636  O  O   . ALA A  1 220 ? 2.787   -1.928  11.704  1.00 22.40  ?  251  ALA A O   1 
ATOM   1637  C  CB  . ALA A  1 220 ? 5.273   -1.785  10.426  1.00 26.32  ?  251  ALA A CB  1 
ATOM   1638  N  N   . TYR A  1 221 ? 2.321   0.249   11.470  1.00 23.74  ?  252  TYR A N   1 
ATOM   1639  C  CA  . TYR A  1 221 ? 0.912   0.030   11.778  1.00 24.85  ?  252  TYR A CA  1 
ATOM   1640  C  C   . TYR A  1 221 ? 0.322   -0.999  10.827  1.00 23.22  ?  252  TYR A C   1 
ATOM   1641  O  O   . TYR A  1 221 ? 0.584   -0.970  9.620   1.00 25.03  ?  252  TYR A O   1 
ATOM   1642  C  CB  . TYR A  1 221 ? 0.129   1.332   11.643  1.00 24.46  ?  252  TYR A CB  1 
ATOM   1643  C  CG  . TYR A  1 221 ? 0.406   2.373   12.705  1.00 23.27  ?  252  TYR A CG  1 
ATOM   1644  C  CD1 . TYR A  1 221 ? -0.064  2.211   14.005  1.00 21.81  ?  252  TYR A CD1 1 
ATOM   1645  C  CD2 . TYR A  1 221 ? 1.075   3.541   12.384  1.00 24.49  ?  252  TYR A CD2 1 
ATOM   1646  C  CE1 . TYR A  1 221 ? 0.144   3.185   14.963  1.00 24.92  ?  252  TYR A CE1 1 
ATOM   1647  C  CE2 . TYR A  1 221 ? 1.304   4.511   13.322  1.00 25.34  ?  252  TYR A CE2 1 
ATOM   1648  C  CZ  . TYR A  1 221 ? 0.827   4.333   14.624  1.00 27.76  ?  252  TYR A CZ  1 
ATOM   1649  O  OH  . TYR A  1 221 ? 1.051   5.312   15.571  1.00 28.44  ?  252  TYR A OH  1 
ATOM   1650  N  N   . ASN A  1 222 ? -0.498  -1.914  11.361  1.00 23.68  ?  253  ASN A N   1 
ATOM   1651  C  CA  . ASN A  1 222 ? -1.271  -2.724  10.421  1.00 22.41  ?  253  ASN A CA  1 
ATOM   1652  C  C   . ASN A  1 222 ? -2.509  -1.983  9.907   1.00 23.63  ?  253  ASN A C   1 
ATOM   1653  O  O   . ASN A  1 222 ? -3.024  -2.341  8.854   1.00 22.05  ?  253  ASN A O   1 
ATOM   1654  C  CB  . ASN A  1 222 ? -1.648  -4.089  11.029  1.00 23.79  ?  253  ASN A CB  1 
ATOM   1655  C  CG  . ASN A  1 222 ? -2.523  -4.000  12.291  1.00 23.35  ?  253  ASN A CG  1 
ATOM   1656  O  OD1 . ASN A  1 222 ? -2.283  -3.201  13.203  1.00 23.72  ?  253  ASN A OD1 1 
ATOM   1657  N  ND2 . ASN A  1 222 ? -3.523  -4.867  12.354  1.00 25.10  ?  253  ASN A ND2 1 
ATOM   1658  N  N   . ALA A  1 223 ? -2.953  -0.920  10.572  1.00 23.03  ?  254  ALA A N   1 
ATOM   1659  C  CA  . ALA A  1 223 ? -4.073  -0.137  10.047  1.00 23.26  ?  254  ALA A CA  1 
ATOM   1660  C  C   . ALA A  1 223 ? -3.696  0.527   8.714   1.00 22.30  ?  254  ALA A C   1 
ATOM   1661  O  O   . ALA A  1 223 ? -2.543  0.910   8.514   1.00 20.25  ?  254  ALA A O   1 
ATOM   1662  C  CB  . ALA A  1 223 ? -4.464  0.936   11.061  1.00 24.61  ?  254  ALA A CB  1 
ATOM   1663  N  N   . PRO A  1 224 ? -4.663  0.685   7.768   1.00 21.23  ?  255  PRO A N   1 
ATOM   1664  C  CA  . PRO A  1 224 ? -6.070  0.251   7.802   1.00 19.56  ?  255  PRO A CA  1 
ATOM   1665  C  C   . PRO A  1 224 ? -6.329  -1.122  7.143   1.00 21.55  ?  255  PRO A C   1 
ATOM   1666  O  O   . PRO A  1 224 ? -7.370  -1.304  6.485   1.00 21.73  ?  255  PRO A O   1 
ATOM   1667  C  CB  . PRO A  1 224 ? -6.772  1.393   7.047   1.00 22.45  ?  255  PRO A CB  1 
ATOM   1668  C  CG  . PRO A  1 224 ? -5.775  1.747   5.936   1.00 20.37  ?  255  PRO A CG  1 
ATOM   1669  C  CD  . PRO A  1 224 ? -4.395  1.577   6.610   1.00 21.84  ?  255  PRO A CD  1 
ATOM   1670  N  N   . HIS A  1 225 ? -5.387  -2.062  7.246   1.00 21.05  ?  256  HIS A N   1 
ATOM   1671  C  CA  . HIS A  1 225 ? -5.550  -3.410  6.696   1.00 23.80  ?  256  HIS A CA  1 
ATOM   1672  C  C   . HIS A  1 225 ? -6.660  -4.142  7.449   1.00 23.43  ?  256  HIS A C   1 
ATOM   1673  O  O   . HIS A  1 225 ? -6.871  -3.916  8.652   1.00 23.14  ?  256  HIS A O   1 
ATOM   1674  C  CB  . HIS A  1 225 ? -4.207  -4.168  6.813   1.00 25.93  ?  256  HIS A CB  1 
ATOM   1675  C  CG  . HIS A  1 225 ? -4.147  -5.504  6.118   1.00 25.61  ?  256  HIS A CG  1 
ATOM   1676  N  ND1 . HIS A  1 225 ? -4.906  -6.593  6.499   1.00 24.45  ?  256  HIS A ND1 1 
ATOM   1677  C  CD2 . HIS A  1 225 ? -3.353  -5.939  5.105   1.00 24.46  ?  256  HIS A CD2 1 
ATOM   1678  C  CE1 . HIS A  1 225 ? -4.592  -7.634  5.741   1.00 25.80  ?  256  HIS A CE1 1 
ATOM   1679  N  NE2 . HIS A  1 225 ? -3.644  -7.264  4.895   1.00 25.17  ?  256  HIS A NE2 1 
ATOM   1680  N  N   . VAL A  1 226 ? -7.390  -4.989  6.720   1.00 22.44  ?  257  VAL A N   1 
ATOM   1681  C  CA  . VAL A  1 226 ? -8.456  -5.824  7.267   1.00 23.63  ?  257  VAL A CA  1 
ATOM   1682  C  C   . VAL A  1 226 ? -7.884  -6.632  8.427   1.00 25.83  ?  257  VAL A C   1 
ATOM   1683  O  O   . VAL A  1 226 ? -6.678  -6.893  8.454   1.00 24.49  ?  257  VAL A O   1 
ATOM   1684  C  CB  . VAL A  1 226 ? -9.066  -6.766  6.208   1.00 25.57  ?  257  VAL A CB  1 
ATOM   1685  C  CG1 . VAL A  1 226 ? -10.014 -5.997  5.216   1.00 24.13  ?  257  VAL A CG1 1 
ATOM   1686  C  CG2 . VAL A  1 226 ? -8.000  -7.594  5.484   1.00 25.97  ?  257  VAL A CG2 1 
ATOM   1687  N  N   . PRO A  1 227 ? -8.702  -7.073  9.381   1.00 27.36  ?  258  PRO A N   1 
ATOM   1688  C  CA  . PRO A  1 227 ? -10.157 -6.887  9.459   1.00 25.59  ?  258  PRO A CA  1 
ATOM   1689  C  C   . PRO A  1 227 ? -10.473 -5.460  9.857   1.00 23.20  ?  258  PRO A C   1 
ATOM   1690  O  O   . PRO A  1 227 ? -9.753  -4.852  10.649  1.00 22.79  ?  258  PRO A O   1 
ATOM   1691  C  CB  . PRO A  1 227 ? -10.592 -7.922  10.517  1.00 25.35  ?  258  PRO A CB  1 
ATOM   1692  C  CG  . PRO A  1 227 ? -9.389  -8.019  11.433  1.00 25.23  ?  258  PRO A CG  1 
ATOM   1693  C  CD  . PRO A  1 227 ? -8.177  -7.847  10.528  1.00 23.58  ?  258  PRO A CD  1 
ATOM   1694  N  N   . LEU A  1 228 ? -11.540 -4.894  9.300   1.00 22.70  ?  259  LEU A N   1 
ATOM   1695  C  CA  . LEU A  1 228 ? -11.942 -3.533  9.636   1.00 25.81  ?  259  LEU A CA  1 
ATOM   1696  C  C   . LEU A  1 228 ? -12.562 -3.557  11.025  1.00 28.11  ?  259  LEU A C   1 
ATOM   1697  O  O   . LEU A  1 228 ? -13.715 -3.964  11.201  1.00 26.11  ?  259  LEU A O   1 
ATOM   1698  C  CB  . LEU A  1 228 ? -12.922 -2.962  8.611   1.00 23.74  ?  259  LEU A CB  1 
ATOM   1699  C  CG  . LEU A  1 228 ? -12.462 -3.010  7.147   1.00 21.05  ?  259  LEU A CG  1 
ATOM   1700  C  CD1 . LEU A  1 228 ? -13.520 -2.424  6.192   1.00 28.21  ?  259  LEU A CD1 1 
ATOM   1701  C  CD2 . LEU A  1 228 ? -11.094 -2.353  6.956   1.00 20.28  ?  259  LEU A CD2 1 
ATOM   1702  N  N   . GLN A  1 229 ? -11.792 -3.102  12.007  1.00 23.94  ?  260  GLN A N   1 
ATOM   1703  C  CA  . GLN A  1 229 ? -12.199 -3.076  13.403  1.00 27.92  ?  260  GLN A CA  1 
ATOM   1704  C  C   . GLN A  1 229 ? -11.735 -1.752  13.971  1.00 27.78  ?  260  GLN A C   1 
ATOM   1705  O  O   . GLN A  1 229 ? -10.576 -1.374  13.790  1.00 26.12  ?  260  GLN A O   1 
ATOM   1706  C  CB  . GLN A  1 229 ? -11.602 -4.261  14.181  1.00 24.44  ?  260  GLN A CB  1 
ATOM   1707  C  CG  . GLN A  1 229 ? -11.966 -5.619  13.555  1.00 24.89  ?  260  GLN A CG  1 
ATOM   1708  C  CD  . GLN A  1 229 ? -11.297 -6.814  14.241  1.00 26.67  ?  260  GLN A CD  1 
ATOM   1709  O  OE1 . GLN A  1 229 ? -10.318 -6.668  14.981  1.00 27.18  ?  260  GLN A OE1 1 
ATOM   1710  N  NE2 . GLN A  1 229 ? -11.816 -8.000  13.980  1.00 26.85  ?  260  GLN A NE2 1 
ATOM   1711  N  N   . ALA A  1 230 ? -12.635 -1.036  14.634  1.00 25.07  ?  261  ALA A N   1 
ATOM   1712  C  CA  . ALA A  1 230 ? -12.335 0.330   15.047  1.00 26.16  ?  261  ALA A CA  1 
ATOM   1713  C  C   . ALA A  1 230 ? -12.953 0.599   16.410  1.00 27.70  ?  261  ALA A C   1 
ATOM   1714  O  O   . ALA A  1 230 ? -13.961 -0.013  16.776  1.00 26.60  ?  261  ALA A O   1 
ATOM   1715  C  CB  . ALA A  1 230 ? -12.884 1.357   14.024  1.00 24.68  ?  261  ALA A CB  1 
ATOM   1716  N  N   . LYS A  1 231 ? -12.369 1.555   17.134  1.00 25.75  ?  262  LYS A N   1 
ATOM   1717  C  CA  . LYS A  1 231 ? -12.908 1.959   18.424  1.00 26.73  ?  262  LYS A CA  1 
ATOM   1718  C  C   . LYS A  1 231 ? -14.162 2.803   18.255  1.00 28.82  ?  262  LYS A C   1 
ATOM   1719  O  O   . LYS A  1 231 ? -14.284 3.602   17.323  1.00 26.53  ?  262  LYS A O   1 
ATOM   1720  C  CB  . LYS A  1 231 ? -11.875 2.749   19.218  1.00 24.14  ?  262  LYS A CB  1 
ATOM   1721  C  CG  . LYS A  1 231 ? -10.620 1.950   19.544  1.00 27.21  ?  262  LYS A CG  1 
ATOM   1722  C  CD  . LYS A  1 231 ? -9.533  2.836   20.145  1.00 33.13  ?  262  LYS A CD  1 
ATOM   1723  C  CE  . LYS A  1 231 ? -10.049 3.650   21.320  1.00 33.01  ?  262  LYS A CE  1 
ATOM   1724  N  NZ  . LYS A  1 231 ? -9.001  4.593   21.836  1.00 26.83  ?  262  LYS A NZ  1 
ATOM   1725  N  N   . ALA A  1 232 ? -15.095 2.644   19.202  1.00 25.61  ?  263  ALA A N   1 
ATOM   1726  C  CA  . ALA A  1 232 ? -16.350 3.385   19.110  1.00 29.17  ?  263  ALA A CA  1 
ATOM   1727  C  C   . ALA A  1 232 ? -16.097 4.889   19.112  1.00 30.37  ?  263  ALA A C   1 
ATOM   1728  O  O   . ALA A  1 232 ? -16.787 5.639   18.416  1.00 27.47  ?  263  ALA A O   1 
ATOM   1729  C  CB  . ALA A  1 232 ? -17.287 2.982   20.256  1.00 28.23  ?  263  ALA A CB  1 
ATOM   1730  N  N   . GLU A  1 233 ? -15.091 5.345   19.871  1.00 26.91  ?  264  GLU A N   1 
ATOM   1731  C  CA  . GLU A  1 233 ? -14.805 6.775   19.941  1.00 29.86  ?  264  GLU A CA  1 
ATOM   1732  C  C   . GLU A  1 233 ? -14.274 7.304   18.618  1.00 30.07  ?  264  GLU A C   1 
ATOM   1733  O  O   . GLU A  1 233 ? -14.501 8.480   18.288  1.00 30.05  ?  264  GLU A O   1 
ATOM   1734  C  CB  . GLU A  1 233 ? -13.792 7.080   21.062  1.00 31.28  ?  264  GLU A CB  1 
ATOM   1735  C  CG  . GLU A  1 233 ? -14.226 6.588   22.447  1.00 35.09  ?  264  GLU A CG  1 
ATOM   1736  C  CD  . GLU A  1 233 ? -13.616 5.241   22.819  1.00 37.77  ?  264  GLU A CD  1 
ATOM   1737  O  OE1 . GLU A  1 233 ? -13.685 4.281   22.011  1.00 31.11  ?  264  GLU A OE1 1 
ATOM   1738  O  OE2 . GLU A  1 233 ? -13.100 5.130   23.943  1.00 40.95  -1 264  GLU A OE2 1 
ATOM   1739  N  N   . ASP A  1 234 ? -13.544 6.473   17.863  1.00 26.39  ?  265  ASP A N   1 
ATOM   1740  C  CA  . ASP A  1 234 ? -13.094 6.916   16.546  1.00 28.38  ?  265  ASP A CA  1 
ATOM   1741  C  C   . ASP A  1 234 ? -14.239 6.841   15.529  1.00 28.27  ?  265  ASP A C   1 
ATOM   1742  O  O   . ASP A  1 234 ? -14.378 7.726   14.680  1.00 25.64  ?  265  ASP A O   1 
ATOM   1743  C  CB  . ASP A  1 234 ? -11.889 6.079   16.088  1.00 26.67  ?  265  ASP A CB  1 
ATOM   1744  C  CG  . ASP A  1 234 ? -10.649 6.284   16.981  1.00 28.11  ?  265  ASP A CG  1 
ATOM   1745  O  OD1 . ASP A  1 234 ? -10.439 7.420   17.475  1.00 28.58  ?  265  ASP A OD1 1 
ATOM   1746  O  OD2 . ASP A  1 234 ? -9.891  5.311   17.194  1.00 25.89  -1 265  ASP A OD2 1 
ATOM   1747  N  N   . VAL A  1 235 ? -15.063 5.794   15.612  1.00 24.74  ?  266  VAL A N   1 
ATOM   1748  C  CA  . VAL A  1 235 ? -16.226 5.673   14.737  1.00 25.82  ?  266  VAL A CA  1 
ATOM   1749  C  C   . VAL A  1 235 ? -17.134 6.892   14.862  1.00 27.84  ?  266  VAL A C   1 
ATOM   1750  O  O   . VAL A  1 235 ? -17.681 7.380   13.867  1.00 28.94  ?  266  VAL A O   1 
ATOM   1751  C  CB  . VAL A  1 235 ? -16.974 4.359   15.026  1.00 25.78  ?  266  VAL A CB  1 
ATOM   1752  C  CG1 . VAL A  1 235 ? -18.309 4.301   14.236  1.00 27.56  ?  266  VAL A CG1 1 
ATOM   1753  C  CG2 . VAL A  1 235 ? -16.097 3.173   14.634  1.00 28.26  ?  266  VAL A CG2 1 
ATOM   1754  N  N   . ALA A  1 236 ? -17.312 7.407   16.078  1.00 29.13  ?  267  ALA A N   1 
ATOM   1755  C  CA  . ALA A  1 236 ? -18.232 8.529   16.266  1.00 31.00  ?  267  ALA A CA  1 
ATOM   1756  C  C   . ALA A  1 236 ? -17.781 9.782   15.517  1.00 28.83  ?  267  ALA A C   1 
ATOM   1757  O  O   . ALA A  1 236 ? -18.614 10.628  15.168  1.00 28.69  ?  267  ALA A O   1 
ATOM   1758  C  CB  . ALA A  1 236 ? -18.398 8.831   17.760  1.00 29.01  ?  267  ALA A CB  1 
ATOM   1759  N  N   . LYS A  1 237 ? -16.479 9.917   15.261  1.00 28.32  ?  268  LYS A N   1 
ATOM   1760  C  CA  . LYS A  1 237 ? -15.954 11.003  14.441  1.00 28.23  ?  268  LYS A CA  1 
ATOM   1761  C  C   . LYS A  1 237 ? -16.521 10.961  13.030  1.00 29.20  ?  268  LYS A C   1 
ATOM   1762  O  O   . LYS A  1 237 ? -16.508 11.980  12.330  1.00 29.74  ?  268  LYS A O   1 
ATOM   1763  C  CB  . LYS A  1 237 ? -14.435 10.883  14.338  1.00 30.56  ?  268  LYS A CB  1 
ATOM   1764  C  CG  . LYS A  1 237 ? -13.553 11.349  15.513  1.00 39.86  ?  268  LYS A CG  1 
ATOM   1765  C  CD  . LYS A  1 237 ? -13.440 12.859  15.667  1.00 50.01  ?  268  LYS A CD  1 
ATOM   1766  C  CE  . LYS A  1 237 ? -13.122 13.231  17.127  1.00 55.95  ?  268  LYS A CE  1 
ATOM   1767  N  NZ  . LYS A  1 237 ? -13.727 14.531  17.550  1.00 61.60  ?  268  LYS A NZ  1 
ATOM   1768  N  N   . PHE A  1 238 ? -16.998 9.797   12.592  1.00 24.44  ?  269  PHE A N   1 
ATOM   1769  C  CA  . PHE A  1 238 ? -17.460 9.586   11.226  1.00 27.61  ?  269  PHE A CA  1 
ATOM   1770  C  C   . PHE A  1 238 ? -18.850 8.968   11.205  1.00 28.27  ?  269  PHE A C   1 
ATOM   1771  O  O   . PHE A  1 238 ? -19.196 8.256   10.269  1.00 27.78  ?  269  PHE A O   1 
ATOM   1772  C  CB  . PHE A  1 238 ? -16.447 8.730   10.461  1.00 24.12  ?  269  PHE A CB  1 
ATOM   1773  C  CG  . PHE A  1 238 ? -15.043 9.284   10.535  1.00 24.97  ?  269  PHE A CG  1 
ATOM   1774  C  CD1 . PHE A  1 238 ? -14.665 10.318  9.689   1.00 28.28  ?  269  PHE A CD1 1 
ATOM   1775  C  CD2 . PHE A  1 238 ? -14.136 8.826   11.480  1.00 23.04  ?  269  PHE A CD2 1 
ATOM   1776  C  CE1 . PHE A  1 238 ? -13.390 10.879  9.756   1.00 25.82  ?  269  PHE A CE1 1 
ATOM   1777  C  CE2 . PHE A  1 238 ? -12.857 9.372   11.567  1.00 25.02  ?  269  PHE A CE2 1 
ATOM   1778  C  CZ  . PHE A  1 238 ? -12.470 10.399  10.695  1.00 25.56  ?  269  PHE A CZ  1 
ATOM   1779  N  N   . ALA A  1 239 ? -19.675 9.261   12.219  1.00 26.67  ?  270  ALA A N   1 
ATOM   1780  C  CA  . ALA A  1 239 ? -20.886 8.469   12.434  1.00 30.14  ?  270  ALA A CA  1 
ATOM   1781  C  C   . ALA A  1 239 ? -21.878 8.631   11.289  1.00 29.78  ?  270  ALA A C   1 
ATOM   1782  O  O   . ALA A  1 239 ? -22.686 7.727   11.034  1.00 32.37  ?  270  ALA A O   1 
ATOM   1783  C  CB  . ALA A  1 239 ? -21.539 8.853   13.761  1.00 27.00  ?  270  ALA A CB  1 
ATOM   1784  N  N   . HIS A  1 240 ? -21.820 9.761   10.581  1.00 26.22  ?  271  HIS A N   1 
ATOM   1785  C  CA  . HIS A  1 240 ? -22.749 10.032  9.494   1.00 29.73  ?  271  HIS A CA  1 
ATOM   1786  C  C   . HIS A  1 240 ? -22.410 9.276   8.203   1.00 31.55  ?  271  HIS A C   1 
ATOM   1787  O  O   . HIS A  1 240 ? -23.263 9.182   7.316   1.00 29.88  ?  271  HIS A O   1 
ATOM   1788  C  CB  . HIS A  1 240 ? -22.775 11.535  9.231   1.00 33.12  ?  271  HIS A CB  1 
ATOM   1789  C  CG  . HIS A  1 240 ? -21.494 12.050  8.670   1.00 33.93  ?  271  HIS A CG  1 
ATOM   1790  N  ND1 . HIS A  1 240 ? -20.441 12.438  9.468   1.00 35.24  ?  271  HIS A ND1 1 
ATOM   1791  C  CD2 . HIS A  1 240 ? -21.080 12.212  7.393   1.00 36.11  ?  271  HIS A CD2 1 
ATOM   1792  C  CE1 . HIS A  1 240 ? -19.438 12.834  8.706   1.00 36.59  ?  271  HIS A CE1 1 
ATOM   1793  N  NE2 . HIS A  1 240 ? -19.799 12.704  7.443   1.00 31.70  ?  271  HIS A NE2 1 
ATOM   1794  N  N   . ILE A  1 241 ? -21.212 8.709   8.086   1.00 27.50  ?  272  ILE A N   1 
ATOM   1795  C  CA  . ILE A  1 241 ? -20.839 7.998   6.868   1.00 26.65  ?  272  ILE A CA  1 
ATOM   1796  C  C   . ILE A  1 241 ? -21.659 6.716   6.791   1.00 28.73  ?  272  ILE A C   1 
ATOM   1797  O  O   . ILE A  1 241 ? -21.535 5.826   7.643   1.00 29.21  ?  272  ILE A O   1 
ATOM   1798  C  CB  . ILE A  1 241 ? -19.323 7.724   6.841   1.00 29.07  ?  272  ILE A CB  1 
ATOM   1799  C  CG1 . ILE A  1 241 ? -18.552 9.030   6.613   1.00 28.66  ?  272  ILE A CG1 1 
ATOM   1800  C  CG2 . ILE A  1 241 ? -18.957 6.730   5.732   1.00 29.31  ?  272  ILE A CG2 1 
ATOM   1801  C  CD1 . ILE A  1 241 ? -17.009 8.838   6.567   1.00 32.77  ?  272  ILE A CD1 1 
ATOM   1802  N  N   . LYS A  1 242 ? -22.520 6.623   5.768   1.00 29.69  ?  273  LYS A N   1 
ATOM   1803  C  CA  . LYS A  1 242 ? -23.497 5.539   5.704   1.00 32.42  ?  273  LYS A CA  1 
ATOM   1804  C  C   . LYS A  1 242 ? -22.865 4.204   5.342   1.00 32.11  ?  273  LYS A C   1 
ATOM   1805  O  O   . LYS A  1 242 ? -23.346 3.155   5.788   1.00 31.76  ?  273  LYS A O   1 
ATOM   1806  C  CB  . LYS A  1 242 ? -24.606 5.879   4.690   1.00 37.02  ?  273  LYS A CB  1 
ATOM   1807  C  CG  . LYS A  1 242 ? -25.476 7.053   5.117   1.00 45.03  ?  273  LYS A CG  1 
ATOM   1808  C  CD  . LYS A  1 242 ? -26.595 7.351   4.110   1.00 46.71  ?  273  LYS A CD  1 
ATOM   1809  C  CE  . LYS A  1 242 ? -27.284 8.677   4.469   1.00 54.19  ?  273  LYS A CE  1 
ATOM   1810  N  NZ  . LYS A  1 242 ? -26.506 9.875   3.973   1.00 49.96  ?  273  LYS A NZ  1 
ATOM   1811  N  N   . ASP A  1 243 ? -21.821 4.200   4.519   1.00 30.24  ?  274  ASP A N   1 
ATOM   1812  C  CA  . ASP A  1 243 ? -21.192 2.929   4.187   1.00 31.59  ?  274  ASP A CA  1 
ATOM   1813  C  C   . ASP A  1 243 ? -20.378 2.450   5.384   1.00 28.56  ?  274  ASP A C   1 
ATOM   1814  O  O   . ASP A  1 243 ? -19.425 3.114   5.794   1.00 25.19  ?  274  ASP A O   1 
ATOM   1815  C  CB  . ASP A  1 243 ? -20.311 3.042   2.946   1.00 30.27  ?  274  ASP A CB  1 
ATOM   1816  C  CG  . ASP A  1 243 ? -19.719 1.688   2.551   1.00 36.50  ?  274  ASP A CG  1 
ATOM   1817  O  OD1 . ASP A  1 243 ? -20.450 0.875   1.957   1.00 42.53  ?  274  ASP A OD1 1 
ATOM   1818  O  OD2 . ASP A  1 243 ? -18.550 1.400   2.882   1.00 32.91  -1 274  ASP A OD2 1 
ATOM   1819  N  N   . LYS A  1 244 ? -20.750 1.287   5.926   1.00 27.66  ?  275  LYS A N   1 
ATOM   1820  C  CA  . LYS A  1 244 ? -20.154 0.814   7.166   1.00 26.65  ?  275  LYS A CA  1 
ATOM   1821  C  C   . LYS A  1 244 ? -18.666 0.544   7.007   1.00 27.23  ?  275  LYS A C   1 
ATOM   1822  O  O   . LYS A  1 244 ? -17.886 0.788   7.931   1.00 25.44  ?  275  LYS A O   1 
ATOM   1823  C  CB  . LYS A  1 244 ? -20.870 -0.447  7.650   1.00 31.68  ?  275  LYS A CB  1 
ATOM   1824  C  CG  . LYS A  1 244 ? -20.578 -0.765  9.120   1.00 42.75  ?  275  LYS A CG  1 
ATOM   1825  C  CD  . LYS A  1 244 ? -21.239 -2.052  9.577   1.00 45.85  ?  275  LYS A CD  1 
ATOM   1826  C  CE  . LYS A  1 244 ? -20.207 -3.077  10.025  1.00 51.08  ?  275  LYS A CE  1 
ATOM   1827  N  NZ  . LYS A  1 244 ? -20.845 -4.281  10.635  1.00 61.28  ?  275  LYS A NZ  1 
ATOM   1828  N  N   . ASP A  1 245 ? -18.260 -0.007  5.861   1.00 30.89  ?  276  ASP A N   1 
ATOM   1829  C  CA  . ASP A  1 245 ? -16.839 -0.222  5.613   1.00 28.99  ?  276  ASP A CA  1 
ATOM   1830  C  C   . ASP A  1 245 ? -16.090 1.098   5.571   1.00 25.93  ?  276  ASP A C   1 
ATOM   1831  O  O   . ASP A  1 245 ? -15.050 1.254   6.221   1.00 22.00  ?  276  ASP A O   1 
ATOM   1832  C  CB  . ASP A  1 245 ? -16.637 -0.985  4.307   1.00 30.03  ?  276  ASP A CB  1 
ATOM   1833  C  CG  . ASP A  1 245 ? -16.814 -2.478  4.473   1.00 36.31  ?  276  ASP A CG  1 
ATOM   1834  O  OD1 . ASP A  1 245 ? -17.239 -2.918  5.562   1.00 38.34  -1 276  ASP A OD1 1 
ATOM   1835  O  OD2 . ASP A  1 245 ? -16.524 -3.205  3.506   1.00 44.06  ?  276  ASP A OD2 1 
ATOM   1836  N  N   . ARG A  1 246 ? -16.581 2.055   4.786   1.00 23.20  ?  277  ARG A N   1 
ATOM   1837  C  CA  . ARG A  1 246 ? -15.904 3.343   4.732   1.00 25.37  ?  277  ARG A CA  1 
ATOM   1838  C  C   . ARG A  1 246 ? -15.853 3.979   6.116   1.00 22.56  ?  277  ARG A C   1 
ATOM   1839  O  O   . ARG A  1 246 ? -14.844 4.579   6.496   1.00 23.40  ?  277  ARG A O   1 
ATOM   1840  C  CB  . ARG A  1 246 ? -16.596 4.282   3.739   1.00 23.14  ?  277  ARG A CB  1 
ATOM   1841  C  CG  . ARG A  1 246 ? -15.854 5.620   3.561   1.00 28.34  ?  277  ARG A CG  1 
ATOM   1842  C  CD  . ARG A  1 246 ? -14.453 5.411   2.978   1.00 22.89  ?  277  ARG A CD  1 
ATOM   1843  N  NE  . ARG A  1 246 ? -13.785 6.677   2.666   1.00 25.79  ?  277  ARG A NE  1 
ATOM   1844  C  CZ  . ARG A  1 246 ? -12.567 6.770   2.150   1.00 25.25  ?  277  ARG A CZ  1 
ATOM   1845  N  NH1 . ARG A  1 246 ? -11.855 5.687   1.862   1.00 21.22  ?  277  ARG A NH1 1 
ATOM   1846  N  NH2 . ARG A  1 246 ? -12.062 7.976   1.885   1.00 23.76  ?  277  ARG A NH2 1 
ATOM   1847  N  N   . ARG A  1 247 ? -16.924 3.836   6.899   1.00 21.44  ?  278  ARG A N   1 
ATOM   1848  C  CA  . ARG A  1 247 ? -16.953 4.474   8.212   1.00 23.73  ?  278  ARG A CA  1 
ATOM   1849  C  C   . ARG A  1 247 ? -15.916 3.854   9.142   1.00 24.95  ?  278  ARG A C   1 
ATOM   1850  O  O   . ARG A  1 247 ? -15.198 4.567   9.856   1.00 21.64  ?  278  ARG A O   1 
ATOM   1851  C  CB  . ARG A  1 247 ? -18.356 4.368   8.814   1.00 24.39  ?  278  ARG A CB  1 
ATOM   1852  C  CG  . ARG A  1 247 ? -18.481 5.032   10.195  1.00 24.39  ?  278  ARG A CG  1 
ATOM   1853  C  CD  . ARG A  1 247 ? -19.933 5.027   10.637  1.00 32.37  ?  278  ARG A CD  1 
ATOM   1854  N  NE  . ARG A  1 247 ? -20.357 3.663   10.899  1.00 31.40  ?  278  ARG A NE  1 
ATOM   1855  C  CZ  . ARG A  1 247 ? -21.359 3.038   10.299  1.00 34.57  ?  278  ARG A CZ  1 
ATOM   1856  N  NH1 . ARG A  1 247 ? -22.084 3.625   9.355   1.00 36.43  ?  278  ARG A NH1 1 
ATOM   1857  N  NH2 . ARG A  1 247 ? -21.641 1.790   10.656  1.00 37.39  ?  278  ARG A NH2 1 
ATOM   1858  N  N   . THR A  1 248 ? -15.799 2.526   9.114   1.00 22.70  ?  279  THR A N   1 
ATOM   1859  C  CA  . THR A  1 248 ? -14.857 1.848   10.000  1.00 24.34  ?  279  THR A CA  1 
ATOM   1860  C  C   . THR A  1 248 ? -13.415 2.128   9.586   1.00 23.46  ?  279  THR A C   1 
ATOM   1861  O  O   . THR A  1 248 ? -12.544 2.348   10.436  1.00 22.83  ?  279  THR A O   1 
ATOM   1862  C  CB  . THR A  1 248 ? -15.156 0.347   9.970   1.00 26.59  ?  279  THR A CB  1 
ATOM   1863  O  OG1 . THR A  1 248 ? -16.547 0.154   10.235  1.00 25.74  ?  279  THR A OG1 1 
ATOM   1864  C  CG2 . THR A  1 248 ? -14.357 -0.407  11.022  1.00 24.80  ?  279  THR A CG2 1 
ATOM   1865  N  N   . TYR A  1 249 ? -13.154 2.105   8.277   1.00 23.89  ?  280  TYR A N   1 
ATOM   1866  C  CA  . TYR A  1 249 ? -11.822 2.375   7.732   1.00 25.29  ?  280  TYR A CA  1 
ATOM   1867  C  C   . TYR A  1 249 ? -11.338 3.773   8.093   1.00 24.15  ?  280  TYR A C   1 
ATOM   1868  O  O   . TYR A  1 249 ? -10.174 3.961   8.500   1.00 25.30  ?  280  TYR A O   1 
ATOM   1869  C  CB  . TYR A  1 249 ? -11.903 2.183   6.213   1.00 21.56  ?  280  TYR A CB  1 
ATOM   1870  C  CG  . TYR A  1 249 ? -10.682 2.517   5.400   1.00 21.81  ?  280  TYR A CG  1 
ATOM   1871  C  CD1 . TYR A  1 249 ? -10.398 3.837   5.040   1.00 21.06  ?  280  TYR A CD1 1 
ATOM   1872  C  CD2 . TYR A  1 249 ? -9.860  1.502   4.916   1.00 23.76  ?  280  TYR A CD2 1 
ATOM   1873  C  CE1 . TYR A  1 249 ? -9.298  4.140   4.288   1.00 20.07  ?  280  TYR A CE1 1 
ATOM   1874  C  CE2 . TYR A  1 249 ? -8.752  1.784   4.138   1.00 22.19  ?  280  TYR A CE2 1 
ATOM   1875  C  CZ  . TYR A  1 249 ? -8.482  3.100   3.823   1.00 19.63  ?  280  TYR A CZ  1 
ATOM   1876  O  OH  . TYR A  1 249 ? -7.403  3.396   3.040   1.00 23.02  ?  280  TYR A OH  1 
ATOM   1877  N  N   . ALA A  1 250 ? -12.218 4.767   7.956   1.00 24.78  ?  281  ALA A N   1 
ATOM   1878  C  CA  . ALA A  1 250 ? -11.866 6.143   8.322   1.00 24.43  ?  281  ALA A CA  1 
ATOM   1879  C  C   . ALA A  1 250 ? -11.478 6.234   9.782   1.00 23.91  ?  281  ALA A C   1 
ATOM   1880  O  O   . ALA A  1 250 ? -10.485 6.885   10.137  1.00 22.39  ?  281  ALA A O   1 
ATOM   1881  C  CB  . ALA A  1 250 ? -13.047 7.077   8.049   1.00 23.25  ?  281  ALA A CB  1 
ATOM   1882  N  N   . ALA A  1 251 ? -12.258 5.576   10.646  1.00 24.57  ?  282  ALA A N   1 
ATOM   1883  C  CA  . ALA A  1 251 ? -11.933 5.541   12.060  1.00 23.02  ?  282  ALA A CA  1 
ATOM   1884  C  C   . ALA A  1 251 ? -10.611 4.837   12.291  1.00 21.58  ?  282  ALA A C   1 
ATOM   1885  O  O   . ALA A  1 251 ? -9.882  5.208   13.214  1.00 23.39  ?  282  ALA A O   1 
ATOM   1886  C  CB  . ALA A  1 251 ? -13.048 4.855   12.859  1.00 21.86  ?  282  ALA A CB  1 
ATOM   1887  N  N   . MET A  1 252 ? -10.270 3.859   11.467  1.00 22.78  ?  283  MET A N   1 
ATOM   1888  C  CA  . MET A  1 252 ? -8.995  3.145   11.701  1.00 20.74  ?  283  MET A CA  1 
ATOM   1889  C  C   . MET A  1 252 ? -7.836  4.100   11.361  1.00 23.92  ?  283  MET A C   1 
ATOM   1890  O  O   . MET A  1 252 ? -6.859  4.148   12.124  1.00 23.31  ?  283  MET A O   1 
ATOM   1891  C  CB  . MET A  1 252 ? -8.920  1.880   10.858  1.00 23.43  ?  283  MET A CB  1 
ATOM   1892  C  CG  . MET A  1 252 ? -9.801  0.772   11.386  1.00 23.79  ?  283  MET A CG  1 
ATOM   1893  S  SD  . MET A  1 252 ? -10.070 -0.522  10.161  1.00 24.93  ?  283  MET A SD  1 
ATOM   1894  C  CE  . MET A  1 252 ? -8.500  -1.378  10.324  1.00 26.06  ?  283  MET A CE  1 
ATOM   1895  N  N   . VAL A  1 253 ? -7.989  4.850   10.270  1.00 21.90  ?  284  VAL A N   1 
ATOM   1896  C  CA  . VAL A  1 253 ? -6.953  5.791   9.852   1.00 22.23  ?  284  VAL A CA  1 
ATOM   1897  C  C   . VAL A  1 253 ? -6.853  6.915   10.857  1.00 24.53  ?  284  VAL A C   1 
ATOM   1898  O  O   . VAL A  1 253 ? -5.759  7.359   11.217  1.00 23.20  ?  284  VAL A O   1 
ATOM   1899  C  CB  . VAL A  1 253 ? -7.268  6.337   8.444   1.00 24.53  ?  284  VAL A CB  1 
ATOM   1900  C  CG1 . VAL A  1 253 ? -6.292  7.460   8.060   1.00 21.84  ?  284  VAL A CG1 1 
ATOM   1901  C  CG2 . VAL A  1 253 ? -7.283  5.200   7.383   1.00 23.57  ?  284  VAL A CG2 1 
ATOM   1902  N  N   . TYR A  1 254 ? -8.004  7.393   11.329  1.00 22.19  ?  285  TYR A N   1 
ATOM   1903  C  CA  . TYR A  1 254 ? -8.013  8.405   12.373  1.00 23.82  ?  285  TYR A CA  1 
ATOM   1904  C  C   . TYR A  1 254 ? -7.216  7.966   13.604  1.00 25.36  ?  285  TYR A C   1 
ATOM   1905  O  O   . TYR A  1 254 ? -6.517  8.780   14.219  1.00 25.74  ?  285  TYR A O   1 
ATOM   1906  C  CB  . TYR A  1 254 ? -9.457  8.722   12.766  1.00 23.73  ?  285  TYR A CB  1 
ATOM   1907  C  CG  . TYR A  1 254 ? -9.555  9.850   13.753  1.00 28.09  ?  285  TYR A CG  1 
ATOM   1908  C  CD1 . TYR A  1 254 ? -9.288  11.161  13.364  1.00 27.28  ?  285  TYR A CD1 1 
ATOM   1909  C  CD2 . TYR A  1 254 ? -9.878  9.606   15.083  1.00 30.84  ?  285  TYR A CD2 1 
ATOM   1910  C  CE1 . TYR A  1 254 ? -9.365  12.207  14.270  1.00 33.70  ?  285  TYR A CE1 1 
ATOM   1911  C  CE2 . TYR A  1 254 ? -9.939  10.646  16.005  1.00 32.55  ?  285  TYR A CE2 1 
ATOM   1912  C  CZ  . TYR A  1 254 ? -9.688  11.937  15.589  1.00 35.89  ?  285  TYR A CZ  1 
ATOM   1913  O  OH  . TYR A  1 254 ? -9.770  12.969  16.485  1.00 40.25  ?  285  TYR A OH  1 
ATOM   1914  N  N   . ALA A  1 255 ? -7.309  6.689   13.983  1.00 25.47  ?  286  ALA A N   1 
ATOM   1915  C  CA  . ALA A  1 255 ? -6.550  6.232   15.155  1.00 25.58  ?  286  ALA A CA  1 
ATOM   1916  C  C   . ALA A  1 255 ? -5.051  6.354   14.927  1.00 28.21  ?  286  ALA A C   1 
ATOM   1917  O  O   . ALA A  1 255 ? -4.289  6.666   15.865  1.00 25.14  ?  286  ALA A O   1 
ATOM   1918  C  CB  . ALA A  1 255 ? -6.911  4.789   15.498  1.00 24.16  ?  286  ALA A CB  1 
ATOM   1919  N  N   . VAL A  1 256 ? -4.594  6.077   13.703  1.00 24.77  ?  287  VAL A N   1 
ATOM   1920  C  CA  . VAL A  1 256 ? -3.186  6.317   13.396  1.00 26.40  ?  287  VAL A CA  1 
ATOM   1921  C  C   . VAL A  1 256 ? -2.871  7.791   13.570  1.00 27.05  ?  287  VAL A C   1 
ATOM   1922  O  O   . VAL A  1 256 ? -1.882  8.168   14.224  1.00 26.28  ?  287  VAL A O   1 
ATOM   1923  C  CB  . VAL A  1 256 ? -2.846  5.849   11.973  1.00 28.38  ?  287  VAL A CB  1 
ATOM   1924  C  CG1 . VAL A  1 256 ? -1.410  6.257   11.608  1.00 24.89  ?  287  VAL A CG1 1 
ATOM   1925  C  CG2 . VAL A  1 256 ? -3.055  4.352   11.858  1.00 23.10  ?  287  VAL A CG2 1 
ATOM   1926  N  N   . ASP A  1 257 ? -3.721  8.650   12.999  1.00 22.99  ?  288  ASP A N   1 
ATOM   1927  C  CA  . ASP A  1 257 ? -3.494  10.085  13.116  1.00 26.10  ?  288  ASP A CA  1 
ATOM   1928  C  C   . ASP A  1 257 ? -3.413  10.521  14.578  1.00 26.26  ?  288  ASP A C   1 
ATOM   1929  O  O   . ASP A  1 257 ? -2.572  11.351  14.934  1.00 26.84  ?  288  ASP A O   1 
ATOM   1930  C  CB  . ASP A  1 257 ? -4.585  10.863  12.391  1.00 22.51  ?  288  ASP A CB  1 
ATOM   1931  C  CG  . ASP A  1 257 ? -4.203  12.300  12.214  1.00 26.82  ?  288  ASP A CG  1 
ATOM   1932  O  OD1 . ASP A  1 257 ? -3.374  12.567  11.320  1.00 27.44  ?  288  ASP A OD1 1 
ATOM   1933  O  OD2 . ASP A  1 257 ? -4.680  13.165  12.983  1.00 27.76  -1 288  ASP A OD2 1 
ATOM   1934  N  N   . ARG A  1 258 ? -4.271  9.964   15.444  1.00 26.75  ?  289  ARG A N   1 
ATOM   1935  C  CA  . ARG A  1 258 ? -4.161  10.260  16.877  1.00 27.27  ?  289  ARG A CA  1 
ATOM   1936  C  C   . ARG A  1 258 ? -2.789  9.883   17.408  1.00 25.48  ?  289  ARG A C   1 
ATOM   1937  O  O   . ARG A  1 258 ? -2.163  10.642  18.167  1.00 26.84  ?  289  ARG A O   1 
ATOM   1938  C  CB  . ARG A  1 258 ? -5.230  9.505   17.666  1.00 27.85  ?  289  ARG A CB  1 
ATOM   1939  C  CG  . ARG A  1 258 ? -6.641  10.068  17.550  1.00 27.77  ?  289  ARG A CG  1 
ATOM   1940  C  CD  . ARG A  1 258 ? -7.529  9.494   18.638  1.00 30.48  ?  289  ARG A CD  1 
ATOM   1941  N  NE  . ARG A  1 258 ? -7.819  8.074   18.446  1.00 25.18  ?  289  ARG A NE  1 
ATOM   1942  C  CZ  . ARG A  1 258 ? -7.212  7.070   19.067  1.00 30.04  ?  289  ARG A CZ  1 
ATOM   1943  N  NH1 . ARG A  1 258 ? -6.208  7.272   19.927  1.00 26.36  ?  289  ARG A NH1 1 
ATOM   1944  N  NH2 . ARG A  1 258 ? -7.607  5.830   18.812  1.00 27.28  ?  289  ARG A NH2 1 
ATOM   1945  N  N   . GLY A  1 259 ? -2.318  8.692   17.046  1.00 26.41  ?  290  GLY A N   1 
ATOM   1946  C  CA  . GLY A  1 259 ? -1.033  8.240   17.547  1.00 25.92  ?  290  GLY A CA  1 
ATOM   1947  C  C   . GLY A  1 259 ? 0.111   9.101   17.057  1.00 27.67  ?  290  GLY A C   1 
ATOM   1948  O  O   . GLY A  1 259 ? 1.081   9.339   17.785  1.00 27.00  ?  290  GLY A O   1 
ATOM   1949  N  N   . VAL A  1 260 ? 0.026   9.570   15.818  1.00 25.89  ?  291  VAL A N   1 
ATOM   1950  C  CA  . VAL A  1 260 ? 1.074   10.435  15.282  1.00 27.11  ?  291  VAL A CA  1 
ATOM   1951  C  C   . VAL A  1 260 ? 1.106   11.746  16.052  1.00 24.26  ?  291  VAL A C   1 
ATOM   1952  O  O   . VAL A  1 260 ? 2.179   12.268  16.383  1.00 30.54  ?  291  VAL A O   1 
ATOM   1953  C  CB  . VAL A  1 260 ? 0.856   10.636  13.762  1.00 30.06  ?  291  VAL A CB  1 
ATOM   1954  C  CG1 . VAL A  1 260 ? 1.683   11.831  13.182  1.00 22.99  ?  291  VAL A CG1 1 
ATOM   1955  C  CG2 . VAL A  1 260 ? 1.168   9.342   13.015  1.00 26.48  ?  291  VAL A CG2 1 
ATOM   1956  N  N   . GLY A  1 261 ? -0.066  12.256  16.420  1.00 28.55  ?  292  GLY A N   1 
ATOM   1957  C  CA  . GLY A  1 261 ? -0.113  13.487  17.197  1.00 27.50  ?  292  GLY A CA  1 
ATOM   1958  C  C   . GLY A  1 261 ? 0.560   13.346  18.546  1.00 29.64  ?  292  GLY A C   1 
ATOM   1959  O  O   . GLY A  1 261 ? 1.285   14.241  18.981  1.00 30.86  ?  292  GLY A O   1 
ATOM   1960  N  N   . LYS A  1 262 ? 0.374   12.199  19.199  1.00 26.47  ?  293  LYS A N   1 
ATOM   1961  C  CA  . LYS A  1 262 ? 1.009   11.981  20.495  1.00 31.26  ?  293  LYS A CA  1 
ATOM   1962  C  C   . LYS A  1 262 ? 2.503   11.760  20.325  1.00 31.65  ?  293  LYS A C   1 
ATOM   1963  O  O   . LYS A  1 262 ? 3.311   12.218  21.149  1.00 31.25  ?  293  LYS A O   1 
ATOM   1964  C  CB  . LYS A  1 262 ? 0.348   10.785  21.185  1.00 30.89  ?  293  LYS A CB  1 
ATOM   1965  C  CG  . LYS A  1 262 ? -1.085  11.099  21.692  1.00 35.49  ?  293  LYS A CG  1 
ATOM   1966  C  CD  . LYS A  1 262 ? -1.603  10.062  22.700  1.00 41.82  ?  293  LYS A CD  1 
ATOM   1967  C  CE  . LYS A  1 262 ? -0.511  9.597   23.675  1.00 49.94  ?  293  LYS A CE  1 
ATOM   1968  N  NZ  . LYS A  1 262 ? -1.045  8.671   24.741  1.00 49.31  ?  293  LYS A NZ  1 
ATOM   1969  N  N   . ILE A  1 263 ? 2.888   11.037  19.273  1.00 26.75  ?  294  ILE A N   1 
ATOM   1970  C  CA  . ILE A  1 263 ? 4.302   10.850  18.975  1.00 28.37  ?  294  ILE A CA  1 
ATOM   1971  C  C   . ILE A  1 263 ? 4.982   12.193  18.759  1.00 31.09  ?  294  ILE A C   1 
ATOM   1972  O  O   . ILE A  1 263 ? 6.076   12.463  19.298  1.00 27.92  ?  294  ILE A O   1 
ATOM   1973  C  CB  . ILE A  1 263 ? 4.458   9.926   17.758  1.00 24.73  ?  294  ILE A CB  1 
ATOM   1974  C  CG1 . ILE A  1 263 ? 4.223   8.478   18.179  1.00 28.23  ?  294  ILE A CG1 1 
ATOM   1975  C  CG2 . ILE A  1 263 ? 5.836   10.094  17.096  1.00 24.03  ?  294  ILE A CG2 1 
ATOM   1976  C  CD1 . ILE A  1 263 ? 3.722   7.576   17.053  1.00 26.36  ?  294  ILE A CD1 1 
ATOM   1977  N  N   . VAL A  1 264 ? 4.334   13.064  17.994  1.00 25.93  ?  295  VAL A N   1 
ATOM   1978  C  CA  . VAL A  1 264 ? 4.868   14.397  17.734  1.00 28.99  ?  295  VAL A CA  1 
ATOM   1979  C  C   . VAL A  1 264 ? 5.026   15.179  19.031  1.00 32.21  ?  295  VAL A C   1 
ATOM   1980  O  O   . VAL A  1 264 ? 6.035   15.870  19.233  1.00 32.13  ?  295  VAL A O   1 
ATOM   1981  C  CB  . VAL A  1 264 ? 3.969   15.153  16.735  1.00 33.01  ?  295  VAL A CB  1 
ATOM   1982  C  CG1 . VAL A  1 264 ? 4.273   16.652  16.786  1.00 30.85  ?  295  VAL A CG1 1 
ATOM   1983  C  CG2 . VAL A  1 264 ? 4.141   14.595  15.315  1.00 26.25  ?  295  VAL A CG2 1 
ATOM   1984  N  N   . GLN A  1 265 ? 4.044   15.106  19.935  1.00 32.83  ?  296  GLN A N   1 
ATOM   1985  C  CA  . GLN A  1 265 ? 4.237   15.865  21.170  1.00 33.10  ?  296  GLN A CA  1 
ATOM   1986  C  C   . GLN A  1 265 ? 5.394   15.285  21.969  1.00 33.03  ?  296  GLN A C   1 
ATOM   1987  O  O   . GLN A  1 265 ? 6.151   16.029  22.600  1.00 31.13  ?  296  GLN A O   1 
ATOM   1988  C  CB  . GLN A  1 265 ? 2.986   15.889  22.043  1.00 35.28  ?  296  GLN A CB  1 
ATOM   1989  C  CG  . GLN A  1 265 ? 1.973   17.032  21.699  1.00 50.75  ?  296  GLN A CG  1 
ATOM   1990  C  CD  . GLN A  1 265 ? 2.595   18.371  21.252  1.00 45.22  ?  296  GLN A CD  1 
ATOM   1991  O  OE1 . GLN A  1 265 ? 3.081   19.164  22.059  1.00 40.33  ?  296  GLN A OE1 1 
ATOM   1992  N  NE2 . GLN A  1 265 ? 2.478   18.656  19.945  1.00 46.59  ?  296  GLN A NE2 1 
ATOM   1993  N  N   . THR A  1 266 ? 5.560   13.959  21.937  1.00 32.55  ?  297  THR A N   1 
ATOM   1994  C  CA  . THR A  1 266 ? 6.687   13.338  22.631  1.00 30.39  ?  297  THR A CA  1 
ATOM   1995  C  C   . THR A  1 266 ? 8.017   13.805  22.054  1.00 32.05  ?  297  THR A C   1 
ATOM   1996  O  O   . THR A  1 266 ? 8.965   14.088  22.798  1.00 33.71  ?  297  THR A O   1 
ATOM   1997  C  CB  . THR A  1 266 ? 6.582   11.815  22.548  1.00 29.31  ?  297  THR A CB  1 
ATOM   1998  O  OG1 . THR A  1 266 ? 5.376   11.394  23.190  1.00 28.91  ?  297  THR A OG1 1 
ATOM   1999  C  CG2 . THR A  1 266 ? 7.775   11.152  23.277  1.00 33.37  ?  297  THR A CG2 1 
ATOM   2000  N  N   . LEU A  1 267 ? 8.109   13.889  20.729  1.00 29.28  ?  298  LEU A N   1 
ATOM   2001  C  CA  . LEU A  1 267 ? 9.339   14.347  20.092  1.00 30.12  ?  298  LEU A CA  1 
ATOM   2002  C  C   . LEU A  1 267 ? 9.674   15.782  20.488  1.00 31.95  ?  298  LEU A C   1 
ATOM   2003  O  O   . LEU A  1 267 ? 10.854  16.134  20.622  1.00 30.71  ?  298  LEU A O   1 
ATOM   2004  C  CB  . LEU A  1 267 ? 9.210   14.235  18.576  1.00 29.33  ?  298  LEU A CB  1 
ATOM   2005  C  CG  . LEU A  1 267 ? 9.322   12.825  17.968  1.00 31.99  ?  298  LEU A CG  1 
ATOM   2006  C  CD1 . LEU A  1 267 ? 8.953   12.853  16.470  1.00 33.42  ?  298  LEU A CD1 1 
ATOM   2007  C  CD2 . LEU A  1 267 ? 10.725  12.218  18.186  1.00 29.55  ?  298  LEU A CD2 1 
ATOM   2008  N  N   . LYS A  1 268 ? 8.650   16.629  20.646  1.00 32.08  ?  299  LYS A N   1 
ATOM   2009  C  CA  . LYS A  1 268 ? 8.871   18.004  21.085  1.00 33.19  ?  299  LYS A CA  1 
ATOM   2010  C  C   . LYS A  1 268 ? 9.291   18.059  22.551  1.00 34.77  ?  299  LYS A C   1 
ATOM   2011  O  O   . LYS A  1 268 ? 10.185  18.830  22.913  1.00 34.16  ?  299  LYS A O   1 
ATOM   2012  C  CB  . LYS A  1 268 ? 7.608   18.845  20.861  1.00 32.07  ?  299  LYS A CB  1 
ATOM   2013  C  CG  . LYS A  1 268 ? 7.281   19.017  19.383  1.00 36.87  ?  299  LYS A CG  1 
ATOM   2014  C  CD  . LYS A  1 268 ? 5.925   19.636  19.174  1.00 36.77  ?  299  LYS A CD  1 
ATOM   2015  C  CE  . LYS A  1 268 ? 5.683   19.952  17.695  1.00 41.70  ?  299  LYS A CE  1 
ATOM   2016  N  NZ  . LYS A  1 268 ? 5.161   21.342  17.527  1.00 48.96  ?  299  LYS A NZ  1 
ATOM   2017  N  N   . GLU A  1 269 ? 8.647   17.254  23.409  1.00 34.09  ?  300  GLU A N   1 
ATOM   2018  C  CA  . GLU A  1 269 ? 8.958   17.267  24.836  1.00 33.91  ?  300  GLU A CA  1 
ATOM   2019  C  C   . GLU A  1 269 ? 10.376  16.798  25.118  1.00 34.29  ?  300  GLU A C   1 
ATOM   2020  O  O   . GLU A  1 269 ? 11.007  17.277  26.067  1.00 31.42  ?  300  GLU A O   1 
ATOM   2021  C  CB  . GLU A  1 269 ? 7.960   16.399  25.594  1.00 33.29  ?  300  GLU A CB  1 
ATOM   2022  C  CG  . GLU A  1 269 ? 6.638   17.121  25.829  1.00 39.63  ?  300  GLU A CG  1 
ATOM   2023  C  CD  . GLU A  1 269 ? 5.499   16.177  26.141  1.00 41.18  ?  300  GLU A CD  1 
ATOM   2024  O  OE1 . GLU A  1 269 ? 5.768   14.993  26.454  1.00 42.07  ?  300  GLU A OE1 1 
ATOM   2025  O  OE2 . GLU A  1 269 ? 4.334   16.632  26.093  1.00 47.13  -1 300  GLU A OE2 1 
ATOM   2026  N  N   . THR A  1 270 ? 10.884  15.864  24.321  1.00 33.05  ?  301  THR A N   1 
ATOM   2027  C  CA  . THR A  1 270 ? 12.249  15.357  24.441  1.00 32.41  ?  301  THR A CA  1 
ATOM   2028  C  C   . THR A  1 270 ? 13.247  16.148  23.602  1.00 34.04  ?  301  THR A C   1 
ATOM   2029  O  O   . THR A  1 270 ? 14.436  15.806  23.588  1.00 37.21  ?  301  THR A O   1 
ATOM   2030  C  CB  . THR A  1 270 ? 12.301  13.877  24.037  1.00 34.20  ?  301  THR A CB  1 
ATOM   2031  O  OG1 . THR A  1 270 ? 11.912  13.738  22.667  1.00 33.79  ?  301  THR A OG1 1 
ATOM   2032  C  CG2 . THR A  1 270 ? 11.361  13.029  24.906  1.00 34.69  ?  301  THR A CG2 1 
ATOM   2033  N  N   . LYS A  1 271 ? 12.800  17.200  22.922  1.00 33.46  ?  302  LYS A N   1 
ATOM   2034  C  CA  . LYS A  1 271 ? 13.657  18.047  22.091  1.00 34.72  ?  302  LYS A CA  1 
ATOM   2035  C  C   . LYS A  1 271 ? 14.317  17.265  20.966  1.00 33.24  ?  302  LYS A C   1 
ATOM   2036  O  O   . LYS A  1 271 ? 15.432  17.584  20.544  1.00 37.57  ?  302  LYS A O   1 
ATOM   2037  C  CB  . LYS A  1 271 ? 14.718  18.771  22.931  1.00 37.55  ?  302  LYS A CB  1 
ATOM   2038  C  CG  . LYS A  1 271 ? 14.131  19.553  24.096  1.00 39.34  ?  302  LYS A CG  1 
ATOM   2039  C  CD  . LYS A  1 271 ? 13.867  20.989  23.668  1.00 46.83  ?  302  LYS A CD  1 
ATOM   2040  C  CE  . LYS A  1 271 ? 12.538  21.508  24.192  1.00 52.87  ?  302  LYS A CE  1 
ATOM   2041  N  NZ  . LYS A  1 271 ? 12.011  22.591  23.315  1.00 51.83  ?  302  LYS A NZ  1 
ATOM   2042  N  N   . GLN A  1 272 ? 13.642  16.245  20.447  1.00 29.79  ?  303  GLN A N   1 
ATOM   2043  C  CA  . GLN A  1 272 ? 14.139  15.544  19.275  1.00 30.87  ?  303  GLN A CA  1 
ATOM   2044  C  C   . GLN A  1 272 ? 13.391  15.889  17.986  1.00 33.34  ?  303  GLN A C   1 
ATOM   2045  O  O   . GLN A  1 272 ? 13.788  15.416  16.923  1.00 35.86  ?  303  GLN A O   1 
ATOM   2046  C  CB  . GLN A  1 272 ? 14.130  14.032  19.515  1.00 30.92  ?  303  GLN A CB  1 
ATOM   2047  C  CG  . GLN A  1 272 ? 14.822  13.586  20.816  1.00 33.89  ?  303  GLN A CG  1 
ATOM   2048  C  CD  . GLN A  1 272 ? 14.480  12.159  21.193  1.00 38.18  ?  303  GLN A CD  1 
ATOM   2049  O  OE1 . GLN A  1 272 ? 13.399  11.890  21.721  1.00 44.19  ?  303  GLN A OE1 1 
ATOM   2050  N  NE2 . GLN A  1 272 ? 15.395  11.229  20.923  1.00 35.73  ?  303  GLN A NE2 1 
ATOM   2051  N  N   . PHE A  1 273 ? 12.387  16.767  18.048  1.00 32.49  ?  304  PHE A N   1 
ATOM   2052  C  CA  . PHE A  1 273 ? 11.497  17.025  16.917  1.00 31.69  ?  304  PHE A CA  1 
ATOM   2053  C  C   . PHE A  1 273 ? 12.232  17.710  15.767  1.00 37.57  ?  304  PHE A C   1 
ATOM   2054  O  O   . PHE A  1 273 ? 12.082  17.329  14.592  1.00 32.30  ?  304  PHE A O   1 
ATOM   2055  C  CB  . PHE A  1 273 ? 10.331  17.890  17.402  1.00 33.96  ?  304  PHE A CB  1 
ATOM   2056  C  CG  . PHE A  1 273 ? 9.253   18.142  16.365  1.00 33.32  ?  304  PHE A CG  1 
ATOM   2057  C  CD1 . PHE A  1 273 ? 8.480   17.106  15.874  1.00 33.51  ?  304  PHE A CD1 1 
ATOM   2058  C  CD2 . PHE A  1 273 ? 9.017   19.427  15.892  1.00 35.45  ?  304  PHE A CD2 1 
ATOM   2059  C  CE1 . PHE A  1 273 ? 7.470   17.353  14.917  1.00 32.01  ?  304  PHE A CE1 1 
ATOM   2060  C  CE2 . PHE A  1 273 ? 8.012   19.679  14.942  1.00 37.78  ?  304  PHE A CE2 1 
ATOM   2061  C  CZ  . PHE A  1 273 ? 7.244   18.646  14.470  1.00 33.12  ?  304  PHE A CZ  1 
ATOM   2062  N  N   . ASP A  1 274 ? 13.017  18.743  16.084  1.00 33.08  ?  305  ASP A N   1 
ATOM   2063  C  CA  . ASP A  1 274 ? 13.623  19.549  15.033  1.00 32.74  ?  305  ASP A CA  1 
ATOM   2064  C  C   . ASP A  1 274 ? 14.588  18.728  14.187  1.00 34.05  ?  305  ASP A C   1 
ATOM   2065  O  O   . ASP A  1 274 ? 14.686  18.935  12.972  1.00 32.22  ?  305  ASP A O   1 
ATOM   2066  C  CB  . ASP A  1 274 ? 14.331  20.761  15.639  1.00 39.32  ?  305  ASP A CB  1 
ATOM   2067  C  CG  . ASP A  1 274 ? 14.982  21.642  14.579  1.00 45.32  ?  305  ASP A CG  1 
ATOM   2068  O  OD1 . ASP A  1 274 ? 14.258  22.488  14.004  1.00 46.32  -1 305  ASP A OD1 1 
ATOM   2069  O  OD2 . ASP A  1 274 ? 16.208  21.521  14.337  1.00 47.83  ?  305  ASP A OD2 1 
ATOM   2070  N  N   . ASN A  1 275 ? 15.313  17.796  14.805  1.00 35.07  ?  306  ASN A N   1 
ATOM   2071  C  CA  . ASN A  1 275 ? 16.330  17.015  14.106  1.00 33.91  ?  306  ASN A CA  1 
ATOM   2072  C  C   . ASN A  1 275 ? 15.917  15.555  13.946  1.00 31.38  ?  306  ASN A C   1 
ATOM   2073  O  O   . ASN A  1 275 ? 16.752  14.650  14.013  1.00 28.67  ?  306  ASN A O   1 
ATOM   2074  C  CB  . ASN A  1 275 ? 17.691  17.107  14.801  1.00 33.55  ?  306  ASN A CB  1 
ATOM   2075  C  CG  . ASN A  1 275 ? 18.831  16.701  13.872  1.00 35.59  ?  306  ASN A CG  1 
ATOM   2076  O  OD1 . ASN A  1 275 ? 18.723  16.868  12.663  1.00 34.20  ?  306  ASN A OD1 1 
ATOM   2077  N  ND2 . ASN A  1 275 ? 19.897  16.126  14.425  1.00 37.47  ?  306  ASN A ND2 1 
ATOM   2078  N  N   . THR A  1 276 ? 14.623  15.318  13.708  1.00 33.12  ?  307  THR A N   1 
ATOM   2079  C  CA  . THR A  1 276 ? 14.107  14.005  13.350  1.00 29.89  ?  307  THR A CA  1 
ATOM   2080  C  C   . THR A  1 276 ? 13.507  14.078  11.944  1.00 28.67  ?  307  THR A C   1 
ATOM   2081  O  O   . THR A  1 276 ? 12.664  14.942  11.661  1.00 28.79  ?  307  THR A O   1 
ATOM   2082  C  CB  . THR A  1 276 ? 13.041  13.513  14.338  1.00 32.69  ?  307  THR A CB  1 
ATOM   2083  O  OG1 . THR A  1 276 ? 13.620  13.291  15.638  1.00 33.69  ?  307  THR A OG1 1 
ATOM   2084  C  CG2 . THR A  1 276 ? 12.435  12.190  13.826  1.00 28.16  ?  307  THR A CG2 1 
ATOM   2085  N  N   . LEU A  1 277 ? 13.974  13.200  11.058  1.00 29.82  ?  308  LEU A N   1 
ATOM   2086  C  CA  . LEU A  1 277 ? 13.330  13.015  9.766   1.00 28.97  ?  308  LEU A CA  1 
ATOM   2087  C  C   . LEU A  1 277 ? 12.176  12.025  9.924   1.00 27.71  ?  308  LEU A C   1 
ATOM   2088  O  O   . LEU A  1 277 ? 12.399  10.842  10.207  1.00 24.57  ?  308  LEU A O   1 
ATOM   2089  C  CB  . LEU A  1 277 ? 14.333  12.512  8.726   1.00 27.45  ?  308  LEU A CB  1 
ATOM   2090  C  CG  . LEU A  1 277 ? 13.675  12.014  7.411   1.00 31.39  ?  308  LEU A CG  1 
ATOM   2091  C  CD1 . LEU A  1 277 ? 12.994  13.145  6.678   1.00 24.57  ?  308  LEU A CD1 1 
ATOM   2092  C  CD2 . LEU A  1 277 ? 14.706  11.363  6.517   1.00 32.70  ?  308  LEU A CD2 1 
ATOM   2093  N  N   . ILE A  1 278 ? 10.948  12.496  9.713   1.00 27.99  ?  309  ILE A N   1 
ATOM   2094  C  CA  . ILE A  1 278 ? 9.778   11.634  9.735   1.00 28.23  ?  309  ILE A CA  1 
ATOM   2095  C  C   . ILE A  1 278 ? 9.384   11.350  8.288   1.00 26.19  ?  309  ILE A C   1 
ATOM   2096  O  O   . ILE A  1 278 ? 9.174   12.283  7.506   1.00 25.38  ?  309  ILE A O   1 
ATOM   2097  C  CB  . ILE A  1 278 ? 8.617   12.281  10.511  1.00 26.36  ?  309  ILE A CB  1 
ATOM   2098  C  CG1 . ILE A  1 278 ? 9.010   12.501  11.975  1.00 26.71  ?  309  ILE A CG1 1 
ATOM   2099  C  CG2 . ILE A  1 278 ? 7.367   11.421  10.387  1.00 24.84  ?  309  ILE A CG2 1 
ATOM   2100  C  CD1 . ILE A  1 278 ? 8.041   13.406  12.777  1.00 28.72  ?  309  ILE A CD1 1 
ATOM   2101  N  N   . VAL A  1 279 ? 9.359   10.073  7.914   1.00 24.11  ?  310  VAL A N   1 
ATOM   2102  C  CA  . VAL A  1 279 ? 8.895   9.632   6.599   1.00 23.16  ?  310  VAL A CA  1 
ATOM   2103  C  C   . VAL A  1 279 ? 7.591   8.865   6.810   1.00 21.52  ?  310  VAL A C   1 
ATOM   2104  O  O   . VAL A  1 279 ? 7.565   7.868   7.540   1.00 25.61  ?  310  VAL A O   1 
ATOM   2105  C  CB  . VAL A  1 279 ? 9.951   8.762   5.894   1.00 28.77  ?  310  VAL A CB  1 
ATOM   2106  C  CG1 . VAL A  1 279 ? 9.441   8.274   4.555   1.00 25.74  ?  310  VAL A CG1 1 
ATOM   2107  C  CG2 . VAL A  1 279 ? 11.280  9.552   5.701   1.00 26.92  ?  310  VAL A CG2 1 
ATOM   2108  N  N   . PHE A  1 280 ? 6.511   9.312   6.173   1.00 25.25  ?  311  PHE A N   1 
ATOM   2109  C  CA  . PHE A  1 280 ? 5.220   8.636   6.276   1.00 25.57  ?  311  PHE A CA  1 
ATOM   2110  C  C   . PHE A  1 280 ? 4.851   8.105   4.899   1.00 22.44  ?  311  PHE A C   1 
ATOM   2111  O  O   . PHE A  1 280 ? 4.974   8.836   3.917   1.00 23.49  ?  311  PHE A O   1 
ATOM   2112  C  CB  . PHE A  1 280 ? 4.132   9.595   6.792   1.00 25.85  ?  311  PHE A CB  1 
ATOM   2113  C  CG  . PHE A  1 280 ? 2.716   9.066   6.624   1.00 22.48  ?  311  PHE A CG  1 
ATOM   2114  C  CD1 . PHE A  1 280 ? 2.181   8.174   7.556   1.00 23.01  ?  311  PHE A CD1 1 
ATOM   2115  C  CD2 . PHE A  1 280 ? 1.935   9.437   5.540   1.00 23.67  ?  311  PHE A CD2 1 
ATOM   2116  C  CE1 . PHE A  1 280 ? 0.879   7.654   7.408   1.00 26.53  ?  311  PHE A CE1 1 
ATOM   2117  C  CE2 . PHE A  1 280 ? 0.631   8.928   5.378   1.00 23.65  ?  311  PHE A CE2 1 
ATOM   2118  C  CZ  . PHE A  1 280 ? 0.112   8.033   6.319   1.00 23.97  ?  311  PHE A CZ  1 
ATOM   2119  N  N   . LEU A  1 281 ? 4.427   6.838   4.821   1.00 20.55  ?  312  LEU A N   1 
ATOM   2120  C  CA  . LEU A  1 281 ? 3.944   6.278   3.559   1.00 24.53  ?  312  LEU A CA  1 
ATOM   2121  C  C   . LEU A  1 281 ? 3.084   5.037   3.820   1.00 22.69  ?  312  LEU A C   1 
ATOM   2122  O  O   . LEU A  1 281 ? 2.935   4.576   4.953   1.00 24.09  ?  312  LEU A O   1 
ATOM   2123  C  CB  . LEU A  1 281 ? 5.118   5.975   2.610   1.00 22.65  ?  312  LEU A CB  1 
ATOM   2124  C  CG  . LEU A  1 281 ? 6.008   4.759   2.899   1.00 22.53  ?  312  LEU A CG  1 
ATOM   2125  C  CD1 . LEU A  1 281 ? 6.794   4.372   1.600   1.00 21.63  ?  312  LEU A CD1 1 
ATOM   2126  C  CD2 . LEU A  1 281 ? 6.960   4.976   4.106   1.00 25.04  ?  312  LEU A CD2 1 
ATOM   2127  N  N   . SER A  1 282 ? 2.460   4.544   2.748   1.00 22.81  ?  313  SER A N   1 
ATOM   2128  C  CA  . SER A  1 282 ? 1.746   3.282   2.735   1.00 22.13  ?  313  SER A CA  1 
ATOM   2129  C  C   . SER A  1 282 ? 2.612   2.219   2.087   1.00 22.06  ?  313  SER A C   1 
ATOM   2130  O  O   . SER A  1 282 ? 3.442   2.523   1.228   1.00 23.35  ?  313  SER A O   1 
ATOM   2131  C  CB  . SER A  1 282 ? 0.446   3.389   1.935   1.00 22.36  ?  313  SER A CB  1 
ATOM   2132  O  OG  . SER A  1 282 ? -0.205  2.134   1.987   1.00 22.18  ?  313  SER A OG  1 
ATOM   2133  N  N   . ASP A  1 283 ? 2.455   0.967   2.517   1.00 21.69  ?  314  ASP A N   1 
ATOM   2134  C  CA  . ASP A  1 283 ? 3.235   -0.143  1.892   1.00 24.43  ?  314  ASP A CA  1 
ATOM   2135  C  C   . ASP A  1 283 ? 2.710   -0.464  0.485   1.00 22.67  ?  314  ASP A C   1 
ATOM   2136  O  O   . ASP A  1 283 ? 3.463   -1.065  -0.298  1.00 21.27  ?  314  ASP A O   1 
ATOM   2137  C  CB  . ASP A  1 283 ? 3.275   -1.395  2.745   1.00 25.68  ?  314  ASP A CB  1 
ATOM   2138  C  CG  . ASP A  1 283 ? 1.964   -2.152  2.859   1.00 27.44  ?  314  ASP A CG  1 
ATOM   2139  O  OD1 . ASP A  1 283 ? 0.904   -1.507  2.723   1.00 27.23  ?  314  ASP A OD1 1 
ATOM   2140  O  OD2 . ASP A  1 283 ? 2.024   -3.377  3.087   1.00 25.60  -1 314  ASP A OD2 1 
ATOM   2141  N  N   . ASN A  1 284 ? 1.475   -0.081  0.196   1.00 23.88  ?  315  ASN A N   1 
ATOM   2142  C  CA  . ASN A  1 284 ? 0.960   -0.298  -1.178  1.00 22.62  ?  315  ASN A CA  1 
ATOM   2143  C  C   . ASN A  1 284 ? -0.378  0.433   -1.343  1.00 21.70  ?  315  ASN A C   1 
ATOM   2144  O  O   . ASN A  1 284 ? -0.844  1.099   -0.403  1.00 20.53  ?  315  ASN A O   1 
ATOM   2145  C  CB  . ASN A  1 284 ? 0.875   -1.785  -1.545  1.00 21.08  ?  315  ASN A CB  1 
ATOM   2146  C  CG  . ASN A  1 284 ? 0.098   -2.584  -0.524  1.00 27.23  ?  315  ASN A CG  1 
ATOM   2147  O  OD1 . ASN A  1 284 ? 0.683   -3.380  0.220   1.00 26.58  ?  315  ASN A OD1 1 
ATOM   2148  N  ND2 . ASN A  1 284 ? -1.212  -2.395  -0.471  1.00 22.95  ?  315  ASN A ND2 1 
ATOM   2149  N  N   . GLY A  1 285 ? -0.982  0.293   -2.516  1.00 22.32  ?  316  GLY A N   1 
ATOM   2150  C  CA  . GLY A  1 285 ? -2.241  0.971   -2.774  1.00 22.92  ?  316  GLY A CA  1 
ATOM   2151  C  C   . GLY A  1 285 ? -3.370  0.448   -1.910  1.00 24.93  ?  316  GLY A C   1 
ATOM   2152  O  O   . GLY A  1 285 ? -3.291  -0.629  -1.305  1.00 23.00  ?  316  GLY A O   1 
ATOM   2153  N  N   . GLY A  1 286 ? -4.447  1.237   -1.849  1.00 21.97  ?  317  GLY A N   1 
ATOM   2154  C  CA  . GLY A  1 286 ? -5.590  0.832   -1.058  1.00 22.77  ?  317  GLY A CA  1 
ATOM   2155  C  C   . GLY A  1 286 ? -6.341  -0.292  -1.741  1.00 23.73  ?  317  GLY A C   1 
ATOM   2156  O  O   . GLY A  1 286 ? -6.351  -0.401  -2.961  1.00 21.51  ?  317  GLY A O   1 
ATOM   2157  N  N   . ASN A  1 287 ? -6.946  -1.164  -0.938  1.00 23.53  ?  318  ASN A N   1 
ATOM   2158  C  CA  . ASN A  1 287 ? -7.809  -2.219  -1.459  1.00 20.78  ?  318  ASN A CA  1 
ATOM   2159  C  C   . ASN A  1 287 ? -9.233  -1.669  -1.503  1.00 22.69  ?  318  ASN A C   1 
ATOM   2160  O  O   . ASN A  1 287 ? -9.884  -1.547  -0.456  1.00 21.89  ?  318  ASN A O   1 
ATOM   2161  C  CB  . ASN A  1 287 ? -7.729  -3.479  -0.592  1.00 22.24  ?  318  ASN A CB  1 
ATOM   2162  C  CG  . ASN A  1 287 ? -8.546  -4.635  -1.152  1.00 25.75  ?  318  ASN A CG  1 
ATOM   2163  O  OD1 . ASN A  1 287 ? -9.520  -4.426  -1.876  1.00 24.44  ?  318  ASN A OD1 1 
ATOM   2164  N  ND2 . ASN A  1 287 ? -8.146  -5.865  -0.822  1.00 24.29  ?  318  ASN A ND2 1 
ATOM   2165  N  N   . PHE A  1 288 ? -9.732  -1.354  -2.706  1.00 22.93  ?  319  PHE A N   1 
ATOM   2166  C  CA  . PHE A  1 288 ? -11.026 -0.679  -2.742  1.00 20.88  ?  319  PHE A CA  1 
ATOM   2167  C  C   . PHE A  1 288 ? -12.193 -1.624  -2.472  1.00 25.37  ?  319  PHE A C   1 
ATOM   2168  O  O   . PHE A  1 288 ? -13.353 -1.191  -2.502  1.00 25.64  ?  319  PHE A O   1 
ATOM   2169  C  CB  . PHE A  1 288 ? -11.221 0.151   -4.052  1.00 24.92  ?  319  PHE A CB  1 
ATOM   2170  C  CG  . PHE A  1 288 ? -11.131 -0.609  -5.388  1.00 21.66  ?  319  PHE A CG  1 
ATOM   2171  C  CD1 . PHE A  1 288 ? -11.355 -1.975  -5.506  1.00 20.81  ?  319  PHE A CD1 1 
ATOM   2172  C  CD2 . PHE A  1 288 ? -10.842 0.121   -6.553  1.00 24.50  ?  319  PHE A CD2 1 
ATOM   2173  C  CE1 . PHE A  1 288 ? -11.306 -2.611  -6.768  1.00 23.30  ?  319  PHE A CE1 1 
ATOM   2174  C  CE2 . PHE A  1 288 ? -10.763 -0.491  -7.820  1.00 24.45  ?  319  PHE A CE2 1 
ATOM   2175  C  CZ  . PHE A  1 288 ? -10.998 -1.862  -7.935  1.00 24.01  ?  319  PHE A CZ  1 
ATOM   2176  N  N   . ASN A  1 289 ? -11.921 -2.886  -2.163  1.00 21.55  ?  320  ASN A N   1 
ATOM   2177  C  CA  . ASN A  1 289 ? -12.985 -3.766  -1.694  1.00 25.10  ?  320  ASN A CA  1 
ATOM   2178  C  C   . ASN A  1 289 ? -13.249 -3.641  -0.202  1.00 27.42  ?  320  ASN A C   1 
ATOM   2179  O  O   . ASN A  1 289 ? -14.298 -4.102  0.261   1.00 26.01  ?  320  ASN A O   1 
ATOM   2180  C  CB  . ASN A  1 289 ? -12.644 -5.223  -2.007  1.00 26.08  ?  320  ASN A CB  1 
ATOM   2181  C  CG  . ASN A  1 289 ? -12.649 -5.507  -3.489  1.00 30.29  ?  320  ASN A CG  1 
ATOM   2182  O  OD1 . ASN A  1 289 ? -13.535 -5.043  -4.224  1.00 25.85  ?  320  ASN A OD1 1 
ATOM   2183  N  ND2 . ASN A  1 289 ? -11.664 -6.277  -3.944  1.00 30.99  ?  320  ASN A ND2 1 
ATOM   2184  N  N   . HIS A  1 290 ? -12.339 -3.021  0.553   1.00 24.86  ?  321  HIS A N   1 
ATOM   2185  C  CA  . HIS A  1 290 ? -12.379 -3.001  2.009   1.00 24.96  ?  321  HIS A CA  1 
ATOM   2186  C  C   . HIS A  1 290 ? -12.128 -1.586  2.531   1.00 26.57  ?  321  HIS A C   1 
ATOM   2187  O  O   . HIS A  1 290 ? -11.285 -1.337  3.396   1.00 22.95  ?  321  HIS A O   1 
ATOM   2188  C  CB  . HIS A  1 290 ? -11.370 -4.013  2.562   1.00 27.16  ?  321  HIS A CB  1 
ATOM   2189  C  CG  . HIS A  1 290 ? -11.661 -5.421  2.136   1.00 27.35  ?  321  HIS A CG  1 
ATOM   2190  N  ND1 . HIS A  1 290 ? -12.731 -6.135  2.632   1.00 34.18  ?  321  HIS A ND1 1 
ATOM   2191  C  CD2 . HIS A  1 290 ? -11.037 -6.242  1.255   1.00 28.56  ?  321  HIS A CD2 1 
ATOM   2192  C  CE1 . HIS A  1 290 ? -12.760 -7.332  2.067   1.00 36.51  ?  321  HIS A CE1 1 
ATOM   2193  N  NE2 . HIS A  1 290 ? -11.746 -7.421  1.224   1.00 32.51  ?  321  HIS A NE2 1 
ATOM   2194  N  N   . GLY A  1 291 ? -12.855 -0.629  1.976   1.00 24.03  ?  322  GLY A N   1 
ATOM   2195  C  CA  . GLY A  1 291 ? -12.924 0.698   2.539   1.00 25.09  ?  322  GLY A CA  1 
ATOM   2196  C  C   . GLY A  1 291 ? -12.013 1.725   1.904   1.00 21.81  ?  322  GLY A C   1 
ATOM   2197  O  O   . GLY A  1 291 ? -12.198 2.913   2.165   1.00 22.01  ?  322  GLY A O   1 
ATOM   2198  N  N   . ALA A  1 292 ? -11.045 1.321   1.079   1.00 21.38  ?  323  ALA A N   1 
ATOM   2199  C  CA  . ALA A  1 292 ? -10.045 2.286   0.632   1.00 21.47  ?  323  ALA A CA  1 
ATOM   2200  C  C   . ALA A  1 292 ? -10.516 3.022   -0.631  1.00 23.56  ?  323  ALA A C   1 
ATOM   2201  O  O   . ALA A  1 292 ? -11.411 2.574   -1.355  1.00 22.79  ?  323  ALA A O   1 
ATOM   2202  C  CB  . ALA A  1 292 ? -8.690  1.594   0.388   1.00 21.85  ?  323  ALA A CB  1 
ATOM   2203  N  N   . ASN A  1 293 ? -9.916  4.187   -0.869  1.00 23.93  ?  324  ASN A N   1 
ATOM   2204  C  CA  . ASN A  1 293 ? -10.205 5.000   -2.046  1.00 21.14  ?  324  ASN A CA  1 
ATOM   2205  C  C   . ASN A  1 293 ? -8.875  5.497   -2.608  1.00 22.23  ?  324  ASN A C   1 
ATOM   2206  O  O   . ASN A  1 293 ? -8.147  6.202   -1.914  1.00 18.97  ?  324  ASN A O   1 
ATOM   2207  C  CB  . ASN A  1 293 ? -11.124 6.178   -1.682  1.00 24.94  ?  324  ASN A CB  1 
ATOM   2208  C  CG  . ASN A  1 293 ? -11.678 6.914   -2.905  1.00 28.01  ?  324  ASN A CG  1 
ATOM   2209  O  OD1 . ASN A  1 293 ? -10.983 7.137   -3.886  1.00 23.93  ?  324  ASN A OD1 1 
ATOM   2210  N  ND2 . ASN A  1 293 ? -12.932 7.318   -2.822  1.00 33.31  ?  324  ASN A ND2 1 
ATOM   2211  N  N   . ASN A  1 294 ? -8.572  5.165   -3.868  1.00 21.82  ?  325  ASN A N   1 
ATOM   2212  C  CA  . ASN A  1 294 ? -7.313  5.553   -4.509  1.00 21.69  ?  325  ASN A CA  1 
ATOM   2213  C  C   . ASN A  1 294 ? -7.442  6.731   -5.483  1.00 22.32  ?  325  ASN A C   1 
ATOM   2214  O  O   . ASN A  1 294 ? -6.539  6.923   -6.300  1.00 21.55  ?  325  ASN A O   1 
ATOM   2215  C  CB  . ASN A  1 294 ? -6.712  4.352   -5.246  1.00 21.47  ?  325  ASN A CB  1 
ATOM   2216  C  CG  . ASN A  1 294 ? -6.388  3.204   -4.303  1.00 21.48  ?  325  ASN A CG  1 
ATOM   2217  O  OD1 . ASN A  1 294 ? -5.886  3.437   -3.223  1.00 20.17  ?  325  ASN A OD1 1 
ATOM   2218  N  ND2 . ASN A  1 294 ? -6.688  1.975   -4.704  1.00 20.70  ?  325  ASN A ND2 1 
ATOM   2219  N  N   . TYR A  1 295 ? -8.549  7.488   -5.442  1.00 25.26  ?  326  TYR A N   1 
ATOM   2220  C  CA  . TYR A  1 295 ? -8.756  8.615   -6.355  1.00 20.66  ?  326  TYR A CA  1 
ATOM   2221  C  C   . TYR A  1 295 ? -7.530  9.531   -6.365  1.00 24.04  ?  326  TYR A C   1 
ATOM   2222  O  O   . TYR A  1 295 ? -7.002  9.854   -5.297  1.00 25.09  ?  326  TYR A O   1 
ATOM   2223  C  CB  . TYR A  1 295 ? -9.971  9.431   -5.918  1.00 25.34  ?  326  TYR A CB  1 
ATOM   2224  C  CG  . TYR A  1 295 ? -10.302 10.561  -6.870  1.00 29.82  ?  326  TYR A CG  1 
ATOM   2225  C  CD1 . TYR A  1 295 ? -11.067 10.330  -8.004  1.00 27.73  ?  326  TYR A CD1 1 
ATOM   2226  C  CD2 . TYR A  1 295 ? -9.808  11.848  -6.657  1.00 33.03  ?  326  TYR A CD2 1 
ATOM   2227  C  CE1 . TYR A  1 295 ? -11.373 11.368  -8.904  1.00 32.93  ?  326  TYR A CE1 1 
ATOM   2228  C  CE2 . TYR A  1 295 ? -10.121 12.885  -7.543  1.00 34.64  ?  326  TYR A CE2 1 
ATOM   2229  C  CZ  . TYR A  1 295 ? -10.891 12.631  -8.654  1.00 32.32  ?  326  TYR A CZ  1 
ATOM   2230  O  OH  . TYR A  1 295 ? -11.170 13.654  -9.515  1.00 39.95  ?  326  TYR A OH  1 
ATOM   2231  N  N   . PRO A  1 296 ? -7.099  10.039  -7.531  1.00 25.11  ?  327  PRO A N   1 
ATOM   2232  C  CA  . PRO A  1 296 ? -7.682  9.894   -8.879  1.00 24.83  ?  327  PRO A CA  1 
ATOM   2233  C  C   . PRO A  1 296 ? -7.069  8.724   -9.660  1.00 24.31  ?  327  PRO A C   1 
ATOM   2234  O  O   . PRO A  1 296 ? -7.215  8.634   -10.878 1.00 23.03  ?  327  PRO A O   1 
ATOM   2235  C  CB  . PRO A  1 296 ? -7.331  11.243  -9.523  1.00 24.77  ?  327  PRO A CB  1 
ATOM   2236  C  CG  . PRO A  1 296 ? -5.917  11.519  -8.954  1.00 26.86  ?  327  PRO A CG  1 
ATOM   2237  C  CD  . PRO A  1 296 ? -5.923  10.938  -7.553  1.00 21.55  ?  327  PRO A CD  1 
ATOM   2238  N  N   . LEU A  1 297 ? -6.359  7.821   -8.985  1.00 22.07  ?  328  LEU A N   1 
ATOM   2239  C  CA  . LEU A  1 297 ? -5.703  6.701   -9.653  1.00 22.07  ?  328  LEU A CA  1 
ATOM   2240  C  C   . LEU A  1 297 ? -6.686  5.594   -10.019 1.00 23.76  ?  328  LEU A C   1 
ATOM   2241  O  O   . LEU A  1 297 ? -7.683  5.356   -9.327  1.00 23.61  ?  328  LEU A O   1 
ATOM   2242  C  CB  . LEU A  1 297 ? -4.617  6.089   -8.765  1.00 20.80  ?  328  LEU A CB  1 
ATOM   2243  C  CG  . LEU A  1 297 ? -3.737  7.118   -8.066  1.00 19.36  ?  328  LEU A CG  1 
ATOM   2244  C  CD1 . LEU A  1 297 ? -2.670  6.432   -7.201  1.00 19.74  ?  328  LEU A CD1 1 
ATOM   2245  C  CD2 . LEU A  1 297 ? -3.133  8.014   -9.146  1.00 20.25  ?  328  LEU A CD2 1 
ATOM   2246  N  N   . LYS A  1 298 ? -6.339  4.867   -11.077 1.00 21.51  ?  329  LYS A N   1 
ATOM   2247  C  CA  . LYS A  1 298 ? -7.055  3.666   -11.457 1.00 22.92  ?  329  LYS A CA  1 
ATOM   2248  C  C   . LYS A  1 298 ? -6.581  2.469   -10.642 1.00 24.92  ?  329  LYS A C   1 
ATOM   2249  O  O   . LYS A  1 298 ? -5.381  2.309   -10.362 1.00 21.80  ?  329  LYS A O   1 
ATOM   2250  C  CB  . LYS A  1 298 ? -6.867  3.390   -12.958 1.00 24.91  ?  329  LYS A CB  1 
ATOM   2251  C  CG  . LYS A  1 298 ? -7.539  2.085   -13.455 1.00 24.73  ?  329  LYS A CG  1 
ATOM   2252  C  CD  . LYS A  1 298 ? -7.312  1.840   -14.960 1.00 24.61  ?  329  LYS A CD  1 
ATOM   2253  C  CE  . LYS A  1 298 ? -8.134  2.808   -15.817 1.00 27.86  ?  329  LYS A CE  1 
ATOM   2254  N  NZ  . LYS A  1 298 ? -7.918  2.598   -17.277 1.00 26.31  ?  329  LYS A NZ  1 
ATOM   2255  N  N   . GLY A  1 299 ? -7.523  1.622   -10.258 1.00 21.90  ?  330  GLY A N   1 
ATOM   2256  C  CA  . GLY A  1 299 ? -7.140  0.309   -9.771  1.00 24.99  ?  330  GLY A CA  1 
ATOM   2257  C  C   . GLY A  1 299 ? -7.017  0.227   -8.260  1.00 24.65  ?  330  GLY A C   1 
ATOM   2258  O  O   . GLY A  1 299 ? -7.397  1.139   -7.513  1.00 20.28  ?  330  GLY A O   1 
ATOM   2259  N  N   . THR A  1 300 ? -6.467  -0.906  -7.812  1.00 22.77  ?  331  THR A N   1 
ATOM   2260  C  CA  . THR A  1 300 ? -6.548  -1.312  -6.416  1.00 21.50  ?  331  THR A CA  1 
ATOM   2261  C  C   . THR A  1 300 ? -5.252  -2.034  -6.032  1.00 22.99  ?  331  THR A C   1 
ATOM   2262  O  O   . THR A  1 300 ? -4.449  -2.396  -6.886  1.00 21.63  ?  331  THR A O   1 
ATOM   2263  C  CB  . THR A  1 300 ? -7.773  -2.207  -6.230  1.00 25.40  ?  331  THR A CB  1 
ATOM   2264  O  OG1 . THR A  1 300 ? -7.964  -2.524  -4.850  1.00 22.01  ?  331  THR A OG1 1 
ATOM   2265  C  CG2 . THR A  1 300 ? -7.599  -3.500  -7.056  1.00 19.35  ?  331  THR A CG2 1 
ATOM   2266  N  N   . LYS A  1 301 ? -5.048  -2.226  -4.726  1.00 21.94  ?  332  LYS A N   1 
ATOM   2267  C  CA  . LYS A  1 301 ? -3.959  -3.060  -4.200  1.00 23.70  ?  332  LYS A CA  1 
ATOM   2268  C  C   . LYS A  1 301 ? -3.699  -4.281  -5.076  1.00 22.04  ?  332  LYS A C   1 
ATOM   2269  O  O   . LYS A  1 301 ? -4.630  -5.002  -5.436  1.00 21.72  ?  332  LYS A O   1 
ATOM   2270  C  CB  . LYS A  1 301 ? -4.309  -3.515  -2.770  1.00 20.58  ?  332  LYS A CB  1 
ATOM   2271  C  CG  . LYS A  1 301 ? -3.340  -4.553  -2.149  1.00 21.95  ?  332  LYS A CG  1 
ATOM   2272  C  CD  . LYS A  1 301 ? -3.952  -5.118  -0.874  1.00 22.33  ?  332  LYS A CD  1 
ATOM   2273  C  CE  . LYS A  1 301 ? -3.035  -6.097  -0.158  1.00 23.80  ?  332  LYS A CE  1 
ATOM   2274  N  NZ  . LYS A  1 301 ? -3.756  -6.588  1.062   1.00 26.10  ?  332  LYS A NZ  1 
ATOM   2275  N  N   . GLY A  1 302 ? -2.424  -4.497  -5.434  1.00 23.17  ?  333  GLY A N   1 
ATOM   2276  C  CA  . GLY A  1 302 ? -2.022  -5.610  -6.282  1.00 25.28  ?  333  GLY A CA  1 
ATOM   2277  C  C   . GLY A  1 302 ? -1.881  -5.301  -7.771  1.00 24.51  ?  333  GLY A C   1 
ATOM   2278  O  O   . GLY A  1 302 ? -1.250  -6.094  -8.499  1.00 24.09  ?  333  GLY A O   1 
ATOM   2279  N  N   . ASP A  1 303 ? -2.463  -4.197  -8.255  1.00 22.05  ?  334  ASP A N   1 
ATOM   2280  C  CA  . ASP A  1 303 ? -2.419  -3.863  -9.674  1.00 24.36  ?  334  ASP A CA  1 
ATOM   2281  C  C   . ASP A  1 303 ? -1.108  -3.144  -10.016 1.00 23.15  ?  334  ASP A C   1 
ATOM   2282  O  O   . ASP A  1 303 ? -0.453  -2.563  -9.151  1.00 22.28  ?  334  ASP A O   1 
ATOM   2283  C  CB  . ASP A  1 303 ? -3.585  -2.949  -10.077 1.00 22.81  ?  334  ASP A CB  1 
ATOM   2284  C  CG  . ASP A  1 303 ? -4.986  -3.619  -9.980  1.00 26.13  ?  334  ASP A CG  1 
ATOM   2285  O  OD1 . ASP A  1 303 ? -5.132  -4.874  -9.976  1.00 22.84  ?  334  ASP A OD1 1 
ATOM   2286  O  OD2 . ASP A  1 303 ? -5.973  -2.839  -9.947  1.00 23.64  -1 334  ASP A OD2 1 
ATOM   2287  N  N   . THR A  1 304 ? -0.759  -3.146  -11.311 1.00 23.34  ?  335  THR A N   1 
ATOM   2288  C  CA  . THR A  1 304 ? 0.305   -2.272  -11.814 1.00 25.69  ?  335  THR A CA  1 
ATOM   2289  C  C   . THR A  1 304 ? -0.249  -1.024  -12.497 1.00 24.05  ?  335  THR A C   1 
ATOM   2290  O  O   . THR A  1 304 ? 0.520   -0.259  -13.105 1.00 22.89  ?  335  THR A O   1 
ATOM   2291  C  CB  . THR A  1 304 ? 1.230   -3.026  -12.767 1.00 24.37  ?  335  THR A CB  1 
ATOM   2292  O  OG1 . THR A  1 304 ? 0.463   -3.547  -13.868 1.00 22.09  ?  335  THR A OG1 1 
ATOM   2293  C  CG2 . THR A  1 304 ? 1.920   -4.166  -12.027 1.00 22.83  ?  335  THR A CG2 1 
ATOM   2294  N  N   . TRP A  1 305 ? -1.565  -0.816  -12.434 1.00 22.63  ?  336  TRP A N   1 
ATOM   2295  C  CA  . TRP A  1 305 ? -2.103  0.538   -12.507 1.00 23.48  ?  336  TRP A CA  1 
ATOM   2296  C  C   . TRP A  1 305 ? -1.480  1.349   -11.378 1.00 21.57  ?  336  TRP A C   1 
ATOM   2297  O  O   . TRP A  1 305 ? -1.060  0.794   -10.368 1.00 23.90  ?  336  TRP A O   1 
ATOM   2298  C  CB  . TRP A  1 305 ? -3.635  0.540   -12.342 1.00 22.23  ?  336  TRP A CB  1 
ATOM   2299  C  CG  . TRP A  1 305 ? -4.449  -0.241  -13.347 1.00 24.50  ?  336  TRP A CG  1 
ATOM   2300  C  CD1 . TRP A  1 305 ? -5.275  -1.287  -13.065 1.00 25.75  ?  336  TRP A CD1 1 
ATOM   2301  C  CD2 . TRP A  1 305 ? -4.541  -0.034  -14.768 1.00 23.28  ?  336  TRP A CD2 1 
ATOM   2302  N  NE1 . TRP A  1 305 ? -5.844  -1.764  -14.205 1.00 23.80  ?  336  TRP A NE1 1 
ATOM   2303  C  CE2 . TRP A  1 305 ? -5.426  -1.011  -15.269 1.00 24.49  ?  336  TRP A CE2 1 
ATOM   2304  C  CE3 . TRP A  1 305 ? -3.950  0.868   -15.666 1.00 25.13  ?  336  TRP A CE3 1 
ATOM   2305  C  CZ2 . TRP A  1 305 ? -5.761  -1.108  -16.627 1.00 26.01  ?  336  TRP A CZ2 1 
ATOM   2306  C  CZ3 . TRP A  1 305 ? -4.294  0.781   -17.030 1.00 26.42  ?  336  TRP A CZ3 1 
ATOM   2307  C  CH2 . TRP A  1 305 ? -5.185  -0.206  -17.492 1.00 27.68  ?  336  TRP A CH2 1 
ATOM   2308  N  N   . GLU A  1 306 ? -1.435  2.682   -11.535 1.00 20.93  ?  337  GLU A N   1 
ATOM   2309  C  CA  . GLU A  1 306 ? -0.898  3.529   -10.462 1.00 22.42  ?  337  GLU A CA  1 
ATOM   2310  C  C   . GLU A  1 306 ? -1.535  3.215   -9.115  1.00 25.05  ?  337  GLU A C   1 
ATOM   2311  O  O   . GLU A  1 306 ? -0.880  3.338   -8.071  1.00 20.10  ?  337  GLU A O   1 
ATOM   2312  C  CB  . GLU A  1 306 ? -1.114  5.016   -10.756 1.00 22.84  ?  337  GLU A CB  1 
ATOM   2313  C  CG  . GLU A  1 306 ? -0.458  5.537   -12.045 1.00 25.28  ?  337  GLU A CG  1 
ATOM   2314  C  CD  . GLU A  1 306 ? 1.026   5.650   -11.901 1.00 23.55  ?  337  GLU A CD  1 
ATOM   2315  O  OE1 . GLU A  1 306 ? 1.691   4.608   -12.114 1.00 24.86  ?  337  GLU A OE1 1 
ATOM   2316  O  OE2 . GLU A  1 306 ? 1.534   6.760   -11.548 1.00 26.28  -1 337  GLU A OE2 1 
ATOM   2317  N  N   . GLY A  1 307 ? -2.820  2.834   -9.117  1.00 22.13  ?  338  GLY A N   1 
ATOM   2318  C  CA  . GLY A  1 307 ? -3.508  2.579   -7.865  1.00 21.55  ?  338  GLY A CA  1 
ATOM   2319  C  C   . GLY A  1 307 ? -2.894  1.479   -7.015  1.00 24.31  ?  338  GLY A C   1 
ATOM   2320  O  O   . GLY A  1 307 ? -3.074  1.467   -5.801  1.00 22.97  ?  338  GLY A O   1 
ATOM   2321  N  N   . GLY A  1 308 ? -2.190  0.526   -7.629  1.00 21.36  ?  339  GLY A N   1 
ATOM   2322  C  CA  . GLY A  1 308 ? -1.618  -0.557  -6.838  1.00 20.81  ?  339  GLY A CA  1 
ATOM   2323  C  C   . GLY A  1 308 ? -0.334  -0.196  -6.106  1.00 21.47  ?  339  GLY A C   1 
ATOM   2324  O  O   . GLY A  1 308 ? -0.049  -0.763  -5.041  1.00 22.01  ?  339  GLY A O   1 
ATOM   2325  N  N   . TYR A  1 309 ? 0.444   0.766   -6.621  1.00 22.04  ?  340  TYR A N   1 
ATOM   2326  C  CA  . TYR A  1 309 ? 1.754   0.987   -5.996  1.00 20.14  ?  340  TYR A CA  1 
ATOM   2327  C  C   . TYR A  1 309 ? 2.216   2.437   -5.921  1.00 20.08  ?  340  TYR A C   1 
ATOM   2328  O  O   . TYR A  1 309 ? 3.356   2.689   -5.496  1.00 25.59  ?  340  TYR A O   1 
ATOM   2329  C  CB  . TYR A  1 309 ? 2.804   0.104   -6.709  1.00 23.56  ?  340  TYR A CB  1 
ATOM   2330  C  CG  . TYR A  1 309 ? 3.117   0.408   -8.154  1.00 24.63  ?  340  TYR A CG  1 
ATOM   2331  C  CD1 . TYR A  1 309 ? 2.243   0.044   -9.178  1.00 25.28  ?  340  TYR A CD1 1 
ATOM   2332  C  CD2 . TYR A  1 309 ? 4.332   0.994   -8.504  1.00 26.16  ?  340  TYR A CD2 1 
ATOM   2333  C  CE1 . TYR A  1 309 ? 2.551   0.304   -10.496 1.00 28.38  ?  340  TYR A CE1 1 
ATOM   2334  C  CE2 . TYR A  1 309 ? 4.638   1.265   -9.813  1.00 25.20  ?  340  TYR A CE2 1 
ATOM   2335  C  CZ  . TYR A  1 309 ? 3.750   0.908   -10.803 1.00 26.75  ?  340  TYR A CZ  1 
ATOM   2336  O  OH  . TYR A  1 309 ? 4.052   1.159   -12.093 1.00 24.42  ?  340  TYR A OH  1 
ATOM   2337  N  N   . ARG A  1 310 ? 1.384   3.401   -6.283  1.00 21.80  ?  341  ARG A N   1 
ATOM   2338  C  CA  . ARG A  1 310 ? 1.660   4.814   -6.051  1.00 22.22  ?  341  ARG A CA  1 
ATOM   2339  C  C   . ARG A  1 310 ? 0.960   5.214   -4.753  1.00 21.73  ?  341  ARG A C   1 
ATOM   2340  O  O   . ARG A  1 310 ? -0.229  4.926   -4.584  1.00 21.03  ?  341  ARG A O   1 
ATOM   2341  C  CB  . ARG A  1 310 ? 1.184   5.645   -7.249  1.00 20.96  ?  341  ARG A CB  1 
ATOM   2342  C  CG  . ARG A  1 310 ? 1.481   7.152   -7.178  1.00 25.45  ?  341  ARG A CG  1 
ATOM   2343  C  CD  . ARG A  1 310 ? 1.063   7.834   -8.481  1.00 23.72  ?  341  ARG A CD  1 
ATOM   2344  N  NE  . ARG A  1 310 ? 1.200   9.290   -8.476  1.00 25.11  ?  341  ARG A NE  1 
ATOM   2345  C  CZ  . ARG A  1 310 ? 1.139   10.064  -9.560  1.00 26.81  ?  341  ARG A CZ  1 
ATOM   2346  N  NH1 . ARG A  1 310 ? 1.111   9.554   -10.788 1.00 24.44  ?  341  ARG A NH1 1 
ATOM   2347  N  NH2 . ARG A  1 310 ? 1.100   11.381  -9.411  1.00 23.64  ?  341  ARG A NH2 1 
ATOM   2348  N  N   . VAL A  1 311 ? 1.711   5.786   -3.806  1.00 23.07  ?  342  VAL A N   1 
ATOM   2349  C  CA  . VAL A  1 311 ? 1.247   5.871   -2.417  1.00 25.22  ?  342  VAL A CA  1 
ATOM   2350  C  C   . VAL A  1 311 ? 1.444   7.287   -1.891  1.00 24.82  ?  342  VAL A C   1 
ATOM   2351  O  O   . VAL A  1 311 ? 2.249   8.059   -2.433  1.00 25.55  ?  342  VAL A O   1 
ATOM   2352  C  CB  . VAL A  1 311 ? 1.975   4.851   -1.513  1.00 23.06  ?  342  VAL A CB  1 
ATOM   2353  C  CG1 . VAL A  1 311 ? 1.699   3.431   -2.032  1.00 20.16  ?  342  VAL A CG1 1 
ATOM   2354  C  CG2 . VAL A  1 311 ? 3.514   5.156   -1.480  1.00 22.43  ?  342  VAL A CG2 1 
ATOM   2355  N  N   . PRO A  1 312 ? 0.709   7.677   -0.841  1.00 24.99  ?  343  PRO A N   1 
ATOM   2356  C  CA  . PRO A  1 312 ? 0.993   8.973   -0.225  1.00 24.48  ?  343  PRO A CA  1 
ATOM   2357  C  C   . PRO A  1 312 ? 2.339   8.899   0.477   1.00 24.82  ?  343  PRO A C   1 
ATOM   2358  O  O   . PRO A  1 312 ? 2.731   7.840   0.968   1.00 22.56  ?  343  PRO A O   1 
ATOM   2359  C  CB  . PRO A  1 312 ? -0.156  9.161   0.780   1.00 23.17  ?  343  PRO A CB  1 
ATOM   2360  C  CG  . PRO A  1 312 ? -1.212  8.116   0.379   1.00 25.15  ?  343  PRO A CG  1 
ATOM   2361  C  CD  . PRO A  1 312 ? -0.379  6.975   -0.128  1.00 23.71  ?  343  PRO A CD  1 
ATOM   2362  N  N   . MET A  1 313 ? 3.066   10.019  0.468   1.00 21.71  ?  344  MET A N   1 
ATOM   2363  C  CA  . MET A  1 313 ? 4.349   10.132  1.184   1.00 22.13  ?  344  MET A CA  1 
ATOM   2364  C  C   . MET A  1 313 ? 4.687   11.572  1.522   1.00 23.82  ?  344  MET A C   1 
ATOM   2365  O  O   . MET A  1 313 ? 4.589   12.456  0.667   1.00 23.58  ?  344  MET A O   1 
ATOM   2366  C  CB  . MET A  1 313 ? 5.535   9.573   0.388   1.00 23.00  ?  344  MET A CB  1 
ATOM   2367  C  CG  . MET A  1 313 ? 6.803   9.332   1.296   1.00 22.38  ?  344  MET A CG  1 
ATOM   2368  S  SD  . MET A  1 313 ? 8.055   8.245   0.617   1.00 29.69  ?  344  MET A SD  1 
ATOM   2369  C  CE  . MET A  1 313 ? 8.722   9.211   -0.723  1.00 25.94  ?  344  MET A CE  1 
ATOM   2370  N  N   . PHE A  1 314 ? 5.198   11.789  2.734   1.00 23.68  ?  345  PHE A N   1 
ATOM   2371  C  CA  . PHE A  1 314 ? 5.847   13.049  3.022   1.00 25.25  ?  345  PHE A CA  1 
ATOM   2372  C  C   . PHE A  1 314 ? 7.161   12.769  3.756   1.00 25.21  ?  345  PHE A C   1 
ATOM   2373  O  O   . PHE A  1 314 ? 7.371   11.679  4.300   1.00 23.14  ?  345  PHE A O   1 
ATOM   2374  C  CB  . PHE A  1 314 ? 4.901   14.022  3.787   1.00 22.04  ?  345  PHE A CB  1 
ATOM   2375  C  CG  . PHE A  1 314 ? 4.526   13.596  5.196   1.00 26.41  ?  345  PHE A CG  1 
ATOM   2376  C  CD1 . PHE A  1 314 ? 5.469   13.599  6.233   1.00 26.05  ?  345  PHE A CD1 1 
ATOM   2377  C  CD2 . PHE A  1 314 ? 3.214   13.256  5.500   1.00 24.31  ?  345  PHE A CD2 1 
ATOM   2378  C  CE1 . PHE A  1 314 ? 5.107   13.227  7.539   1.00 24.76  ?  345  PHE A CE1 1 
ATOM   2379  C  CE2 . PHE A  1 314 ? 2.846   12.876  6.792   1.00 21.77  ?  345  PHE A CE2 1 
ATOM   2380  C  CZ  . PHE A  1 314 ? 3.798   12.890  7.820   1.00 24.99  ?  345  PHE A CZ  1 
ATOM   2381  N  N   . PHE A  1 315 ? 8.080   13.730  3.649   1.00 24.21  ?  346  PHE A N   1 
ATOM   2382  C  CA  . PHE A  1 315 ? 9.264   13.845  4.503   1.00 24.36  ?  346  PHE A CA  1 
ATOM   2383  C  C   . PHE A  1 315 ? 9.070   15.065  5.395   1.00 26.32  ?  346  PHE A C   1 
ATOM   2384  O  O   . PHE A  1 315 ? 8.739   16.139  4.886   1.00 29.26  ?  346  PHE A O   1 
ATOM   2385  C  CB  . PHE A  1 315 ? 10.552  14.081  3.687   1.00 26.03  ?  346  PHE A CB  1 
ATOM   2386  C  CG  . PHE A  1 315 ? 11.146  12.851  3.019   1.00 29.54  ?  346  PHE A CG  1 
ATOM   2387  C  CD1 . PHE A  1 315 ? 10.427  11.682  2.863   1.00 27.25  ?  346  PHE A CD1 1 
ATOM   2388  C  CD2 . PHE A  1 315 ? 12.444  12.911  2.499   1.00 25.84  ?  346  PHE A CD2 1 
ATOM   2389  C  CE1 . PHE A  1 315 ? 10.981  10.582  2.205   1.00 29.67  ?  346  PHE A CE1 1 
ATOM   2390  C  CE2 . PHE A  1 315 ? 13.011  11.817  1.848   1.00 29.37  ?  346  PHE A CE2 1 
ATOM   2391  C  CZ  . PHE A  1 315 ? 12.292  10.652  1.705   1.00 30.51  ?  346  PHE A CZ  1 
ATOM   2392  N  N   . HIS A  1 316 ? 9.315   14.929  6.704   1.00 25.49  ?  347  HIS A N   1 
ATOM   2393  C  CA  . HIS A  1 316 ? 9.229   16.056  7.639   1.00 24.94  ?  347  HIS A CA  1 
ATOM   2394  C  C   . HIS A  1 316 ? 10.495  16.086  8.502   1.00 29.22  ?  347  HIS A C   1 
ATOM   2395  O  O   . HIS A  1 316 ? 10.772  15.128  9.232   1.00 27.82  ?  347  HIS A O   1 
ATOM   2396  C  CB  . HIS A  1 316 ? 7.980   15.953  8.524   1.00 26.01  ?  347  HIS A CB  1 
ATOM   2397  C  CG  . HIS A  1 316 ? 7.881   17.029  9.565   1.00 27.90  ?  347  HIS A CG  1 
ATOM   2398  N  ND1 . HIS A  1 316 ? 8.523   16.953  10.786  1.00 30.83  ?  347  HIS A ND1 1 
ATOM   2399  C  CD2 . HIS A  1 316 ? 7.235   18.221  9.556   1.00 31.37  ?  347  HIS A CD2 1 
ATOM   2400  C  CE1 . HIS A  1 316 ? 8.257   18.039  11.489  1.00 27.37  ?  347  HIS A CE1 1 
ATOM   2401  N  NE2 . HIS A  1 316 ? 7.478   18.825  10.767  1.00 29.86  ?  347  HIS A NE2 1 
ATOM   2402  N  N   . TRP A  1 317 ? 11.264  17.192  8.411   1.00 29.70  ?  348  TRP A N   1 
ATOM   2403  C  CA  . TRP A  1 317 ? 12.582  17.342  9.041   1.00 30.17  ?  348  TRP A CA  1 
ATOM   2404  C  C   . TRP A  1 317 ? 12.866  18.827  9.235   1.00 29.43  ?  348  TRP A C   1 
ATOM   2405  O  O   . TRP A  1 317 ? 13.449  19.463  8.342   1.00 27.78  ?  348  TRP A O   1 
ATOM   2406  C  CB  . TRP A  1 317 ? 13.667  16.717  8.174   1.00 28.40  ?  348  TRP A CB  1 
ATOM   2407  C  CG  . TRP A  1 317 ? 15.018  16.660  8.834   1.00 30.42  ?  348  TRP A CG  1 
ATOM   2408  C  CD1 . TRP A  1 317 ? 15.300  16.873  10.151  1.00 32.69  ?  348  TRP A CD1 1 
ATOM   2409  C  CD2 . TRP A  1 317 ? 16.257  16.341  8.201   1.00 33.69  ?  348  TRP A CD2 1 
ATOM   2410  N  NE1 . TRP A  1 317 ? 16.655  16.706  10.380  1.00 34.06  ?  348  TRP A NE1 1 
ATOM   2411  C  CE2 . TRP A  1 317 ? 17.261  16.389  9.190   1.00 33.34  ?  348  TRP A CE2 1 
ATOM   2412  C  CE3 . TRP A  1 317 ? 16.620  16.033  6.886   1.00 33.83  ?  348  TRP A CE3 1 
ATOM   2413  C  CZ2 . TRP A  1 317 ? 18.604  16.131  8.903   1.00 34.32  ?  348  TRP A CZ2 1 
ATOM   2414  C  CZ3 . TRP A  1 317 ? 17.961  15.763  6.609   1.00 37.46  ?  348  TRP A CZ3 1 
ATOM   2415  C  CH2 . TRP A  1 317 ? 18.932  15.814  7.614   1.00 32.83  ?  348  TRP A CH2 1 
ATOM   2416  N  N   . PRO A  1 318 ? 12.381  19.432  10.319  1.00 28.62  ?  349  PRO A N   1 
ATOM   2417  C  CA  . PRO A  1 318 ? 12.380  20.906  10.390  1.00 33.61  ?  349  PRO A CA  1 
ATOM   2418  C  C   . PRO A  1 318 ? 13.750  21.538  10.181  1.00 33.47  ?  349  PRO A C   1 
ATOM   2419  O  O   . PRO A  1 318 ? 13.840  22.632  9.611   1.00 33.59  ?  349  PRO A O   1 
ATOM   2420  C  CB  . PRO A  1 318 ? 11.817  21.178  11.790  1.00 34.59  ?  349  PRO A CB  1 
ATOM   2421  C  CG  . PRO A  1 318 ? 10.926  19.980  12.051  1.00 32.17  ?  349  PRO A CG  1 
ATOM   2422  C  CD  . PRO A  1 318 ? 11.697  18.822  11.472  1.00 30.11  ?  349  PRO A CD  1 
ATOM   2423  N  N   . LYS A  1 319 ? 14.820  20.851  10.582  1.00 35.73  ?  350  LYS A N   1 
ATOM   2424  C  CA  . LYS A  1 319 ? 16.175  21.387  10.451  1.00 38.20  ?  350  LYS A CA  1 
ATOM   2425  C  C   . LYS A  1 319 ? 16.552  21.677  9.006   1.00 42.73  ?  350  LYS A C   1 
ATOM   2426  O  O   . LYS A  1 319 ? 17.315  22.618  8.742   1.00 36.53  ?  350  LYS A O   1 
ATOM   2427  C  CB  . LYS A  1 319 ? 17.175  20.399  11.043  1.00 34.38  ?  350  LYS A CB  1 
ATOM   2428  C  CG  . LYS A  1 319 ? 18.622  20.860  11.006  1.00 48.55  ?  350  LYS A CG  1 
ATOM   2429  C  CD  . LYS A  1 319 ? 19.542  19.665  10.741  1.00 45.57  ?  350  LYS A CD  1 
ATOM   2430  C  CE  . LYS A  1 319 ? 20.449  19.410  11.909  1.00 50.30  ?  350  LYS A CE  1 
ATOM   2431  N  NZ  . LYS A  1 319 ? 21.260  20.621  12.217  1.00 54.73  ?  350  LYS A NZ  1 
ATOM   2432  N  N   . LYS A  1 320 ? 16.054  20.878  8.064   1.00 31.78  ?  351  LYS A N   1 
ATOM   2433  C  CA  . LYS A  1 320 ? 16.556  20.947  6.699   1.00 31.92  ?  351  LYS A CA  1 
ATOM   2434  C  C   . LYS A  1 320 ? 15.461  21.149  5.658   1.00 33.69  ?  351  LYS A C   1 
ATOM   2435  O  O   . LYS A  1 320 ? 15.641  21.933  4.728   1.00 30.62  ?  351  LYS A O   1 
ATOM   2436  C  CB  . LYS A  1 320 ? 17.354  19.667  6.405   1.00 33.66  ?  351  LYS A CB  1 
ATOM   2437  C  CG  . LYS A  1 320 ? 18.633  19.536  7.244   1.00 34.39  ?  351  LYS A CG  1 
ATOM   2438  C  CD  . LYS A  1 320 ? 19.841  20.163  6.555   1.00 45.33  ?  351  LYS A CD  1 
ATOM   2439  C  CE  . LYS A  1 320 ? 21.096  19.302  6.719   1.00 55.62  ?  351  LYS A CE  1 
ATOM   2440  N  NZ  . LYS A  1 320 ? 22.041  19.358  5.546   1.00 65.41  ?  351  LYS A NZ  1 
ATOM   2441  N  N   . ILE A  1 321 ? 14.319  20.497  5.804   1.00 32.84  ?  352  ILE A N   1 
ATOM   2442  C  CA  . ILE A  1 321 ? 13.298  20.512  4.760   1.00 27.33  ?  352  ILE A CA  1 
ATOM   2443  C  C   . ILE A  1 321 ? 12.358  21.683  4.985   1.00 29.51  ?  352  ILE A C   1 
ATOM   2444  O  O   . ILE A  1 321 ? 11.787  21.834  6.074   1.00 32.96  ?  352  ILE A O   1 
ATOM   2445  C  CB  . ILE A  1 321 ? 12.537  19.177  4.723   1.00 28.50  ?  352  ILE A CB  1 
ATOM   2446  C  CG1 . ILE A  1 321 ? 13.544  18.048  4.428   1.00 30.84  ?  352  ILE A CG1 1 
ATOM   2447  C  CG2 . ILE A  1 321 ? 11.421  19.245  3.686   1.00 28.13  ?  352  ILE A CG2 1 
ATOM   2448  C  CD1 . ILE A  1 321 ? 12.990  16.608  4.363   1.00 25.68  ?  352  ILE A CD1 1 
ATOM   2449  N  N   . LYS A  1 322 ? 12.202  22.522  3.959   1.00 32.94  ?  353  LYS A N   1 
ATOM   2450  C  CA  . LYS A  1 322 ? 11.349  23.696  4.059   1.00 32.36  ?  353  LYS A CA  1 
ATOM   2451  C  C   . LYS A  1 322 ? 9.889   23.286  4.200   1.00 36.63  ?  353  LYS A C   1 
ATOM   2452  O  O   . LYS A  1 322 ? 9.496   22.170  3.857   1.00 35.19  ?  353  LYS A O   1 
ATOM   2453  C  CB  . LYS A  1 322 ? 11.495  24.589  2.821   1.00 36.94  ?  353  LYS A CB  1 
ATOM   2454  N  N   . LYS A  1 323 ? 9.079   24.225  4.685   1.00 35.30  ?  354  LYS A N   1 
ATOM   2455  C  CA  . LYS A  1 323 ? 7.642   24.034  4.805   1.00 39.84  ?  354  LYS A CA  1 
ATOM   2456  C  C   . LYS A  1 323 ? 6.959   24.211  3.448   1.00 38.24  ?  354  LYS A C   1 
ATOM   2457  O  O   . LYS A  1 323 ? 7.510   24.818  2.527   1.00 34.40  ?  354  LYS A O   1 
ATOM   2458  C  CB  . LYS A  1 323 ? 7.066   25.028  5.811   1.00 38.47  ?  354  LYS A CB  1 
ATOM   2459  C  CG  . LYS A  1 323 ? 7.639   24.859  7.224   1.00 41.49  ?  354  LYS A CG  1 
ATOM   2460  C  CD  . LYS A  1 323 ? 7.389   26.106  8.069   1.00 45.20  ?  354  LYS A CD  1 
ATOM   2461  C  CE  . LYS A  1 323 ? 7.915   25.950  9.483   1.00 45.39  ?  354  LYS A CE  1 
ATOM   2462  N  NZ  . LYS A  1 323 ? 6.821   26.144  10.472  1.00 50.09  ?  354  LYS A NZ  1 
ATOM   2463  N  N   . ASP A  1 324 ? 5.738   23.672  3.342   1.00 34.76  ?  355  ASP A N   1 
ATOM   2464  C  CA  . ASP A  1 324 ? 4.870   23.829  2.166   1.00 34.05  ?  355  ASP A CA  1 
ATOM   2465  C  C   . ASP A  1 324 ? 5.529   23.378  0.868   1.00 36.14  ?  355  ASP A C   1 
ATOM   2466  O  O   . ASP A  1 324 ? 5.201   23.880  -0.205  1.00 35.19  ?  355  ASP A O   1 
ATOM   2467  C  CB  . ASP A  1 324 ? 4.374   25.270  1.990   1.00 42.00  ?  355  ASP A CB  1 
ATOM   2468  C  CG  . ASP A  1 324 ? 3.929   25.905  3.287   1.00 47.79  ?  355  ASP A CG  1 
ATOM   2469  O  OD1 . ASP A  1 324 ? 3.016   25.348  3.939   1.00 47.34  ?  355  ASP A OD1 1 
ATOM   2470  O  OD2 . ASP A  1 324 ? 4.495   26.960  3.661   1.00 53.21  -1 355  ASP A OD2 1 
ATOM   2471  N  N   . GLN A  1 325 ? 6.432   22.420  0.920   1.00 32.22  ?  356  GLN A N   1 
ATOM   2472  C  CA  . GLN A  1 325 ? 7.049   21.941  -0.301  1.00 28.93  ?  356  GLN A CA  1 
ATOM   2473  C  C   . GLN A  1 325 ? 6.201   20.834  -0.919  1.00 35.62  ?  356  GLN A C   1 
ATOM   2474  O  O   . GLN A  1 325 ? 5.629   19.999  -0.208  1.00 31.90  ?  356  GLN A O   1 
ATOM   2475  C  CB  . GLN A  1 325 ? 8.460   21.433  -0.009  1.00 32.61  ?  356  GLN A CB  1 
ATOM   2476  C  CG  . GLN A  1 325 ? 8.946   20.359  -0.955  1.00 34.75  ?  356  GLN A CG  1 
ATOM   2477  C  CD  . GLN A  1 325 ? 10.445  20.181  -0.902  1.00 38.46  ?  356  GLN A CD  1 
ATOM   2478  O  OE1 . GLN A  1 325 ? 11.041  19.554  -1.784  1.00 46.66  ?  356  GLN A OE1 1 
ATOM   2479  N  NE2 . GLN A  1 325 ? 11.065  20.687  0.169   1.00 37.51  ?  356  GLN A NE2 1 
ATOM   2480  N  N   . ARG A  1 326 ? 6.091   20.854  -2.249  1.00 30.55  ?  357  ARG A N   1 
ATOM   2481  C  CA  . ARG A  1 326 ? 5.572   19.722  -3.005  1.00 26.73  ?  357  ARG A CA  1 
ATOM   2482  C  C   . ARG A  1 326 ? 6.679   19.249  -3.936  1.00 31.82  ?  357  ARG A C   1 
ATOM   2483  O  O   . ARG A  1 326 ? 7.218   20.039  -4.720  1.00 30.03  ?  357  ARG A O   1 
ATOM   2484  C  CB  . ARG A  1 326 ? 4.314   20.111  -3.783  1.00 28.88  ?  357  ARG A CB  1 
ATOM   2485  C  CG  . ARG A  1 326 ? 3.270   20.799  -2.912  1.00 30.06  ?  357  ARG A CG  1 
ATOM   2486  C  CD  . ARG A  1 326 ? 1.968   21.111  -3.675  1.00 28.91  ?  357  ARG A CD  1 
ATOM   2487  N  NE  . ARG A  1 326 ? 1.281   19.912  -4.142  1.00 37.03  ?  357  ARG A NE  1 
ATOM   2488  C  CZ  . ARG A  1 326 ? 0.428   19.209  -3.408  1.00 35.96  ?  357  ARG A CZ  1 
ATOM   2489  N  NH1 . ARG A  1 326 ? 0.210   19.499  -2.137  1.00 35.32  ?  357  ARG A NH1 1 
ATOM   2490  N  NH2 . ARG A  1 326 ? -0.232  18.201  -3.969  1.00 36.23  ?  357  ARG A NH2 1 
ATOM   2491  N  N   . PHE A  1 327 ? 7.046   17.983  -3.824  1.00 27.04  ?  358  PHE A N   1 
ATOM   2492  C  CA  . PHE A  1 327 ? 8.072   17.382  -4.666  1.00 27.36  ?  358  PHE A CA  1 
ATOM   2493  C  C   . PHE A  1 327 ? 7.361   16.526  -5.714  1.00 30.93  ?  358  PHE A C   1 
ATOM   2494  O  O   . PHE A  1 327 ? 6.825   15.460  -5.388  1.00 28.06  ?  358  PHE A O   1 
ATOM   2495  C  CB  . PHE A  1 327 ? 9.030   16.546  -3.819  1.00 28.63  ?  358  PHE A CB  1 
ATOM   2496  C  CG  . PHE A  1 327 ? 10.264  16.128  -4.541  1.00 30.58  ?  358  PHE A CG  1 
ATOM   2497  C  CD1 . PHE A  1 327 ? 11.378  16.961  -4.584  1.00 29.39  ?  358  PHE A CD1 1 
ATOM   2498  C  CD2 . PHE A  1 327 ? 10.313  14.911  -5.199  1.00 28.60  ?  358  PHE A CD2 1 
ATOM   2499  C  CE1 . PHE A  1 327 ? 12.513  16.571  -5.265  1.00 32.38  ?  358  PHE A CE1 1 
ATOM   2500  C  CE2 . PHE A  1 327 ? 11.460  14.507  -5.879  1.00 29.39  ?  358  PHE A CE2 1 
ATOM   2501  C  CZ  . PHE A  1 327 ? 12.559  15.338  -5.915  1.00 31.84  ?  358  PHE A CZ  1 
ATOM   2502  N  N   . ASP A  1 328 ? 7.396   16.967  -6.979  1.00 24.97  ?  359  ASP A N   1 
ATOM   2503  C  CA  . ASP A  1 328 ? 6.593   16.358  -8.028  1.00 30.98  ?  359  ASP A CA  1 
ATOM   2504  C  C   . ASP A  1 328 ? 7.363   15.364  -8.887  1.00 29.33  ?  359  ASP A C   1 
ATOM   2505  O  O   . ASP A  1 328 ? 6.744   14.698  -9.723  1.00 28.42  ?  359  ASP A O   1 
ATOM   2506  C  CB  . ASP A  1 328 ? 5.964   17.443  -8.931  1.00 30.41  ?  359  ASP A CB  1 
ATOM   2507  C  CG  . ASP A  1 328 ? 4.953   18.331  -8.181  1.00 34.98  ?  359  ASP A CG  1 
ATOM   2508  O  OD1 . ASP A  1 328 ? 4.258   17.847  -7.267  1.00 31.55  ?  359  ASP A OD1 1 
ATOM   2509  O  OD2 . ASP A  1 328 ? 4.834   19.528  -8.511  1.00 36.44  -1 359  ASP A OD2 1 
ATOM   2510  N  N   . PHE A  1 329 ? 8.705   15.240  -8.712  1.00 25.20  ?  360  PHE A N   1 
ATOM   2511  C  CA  . PHE A  1 329 ? 9.413   14.237  -9.490  1.00 25.57  ?  360  PHE A CA  1 
ATOM   2512  C  C   . PHE A  1 329 ? 9.229   12.851  -8.869  1.00 26.49  ?  360  PHE A C   1 
ATOM   2513  O  O   . PHE A  1 329 ? 9.167   12.714  -7.648  1.00 26.96  ?  360  PHE A O   1 
ATOM   2514  C  CB  . PHE A  1 329 ? 10.916  14.561  -9.567  1.00 29.09  ?  360  PHE A CB  1 
ATOM   2515  C  CG  . PHE A  1 329 ? 11.223  15.898  -10.216 1.00 28.92  ?  360  PHE A CG  1 
ATOM   2516  C  CD1 . PHE A  1 329 ? 10.890  16.134  -11.552 1.00 32.31  ?  360  PHE A CD1 1 
ATOM   2517  C  CD2 . PHE A  1 329 ? 11.853  16.917  -9.493  1.00 31.08  ?  360  PHE A CD2 1 
ATOM   2518  C  CE1 . PHE A  1 329 ? 11.164  17.364  -12.154 1.00 31.18  ?  360  PHE A CE1 1 
ATOM   2519  C  CE2 . PHE A  1 329 ? 12.132  18.154  -10.096 1.00 33.43  ?  360  PHE A CE2 1 
ATOM   2520  C  CZ  . PHE A  1 329 ? 11.781  18.369  -11.426 1.00 34.67  ?  360  PHE A CZ  1 
ATOM   2521  N  N   . PRO A  1 330 ? 9.223   11.800  -9.681  1.00 27.83  ?  361  PRO A N   1 
ATOM   2522  C  CA  . PRO A  1 330 ? 8.996   10.460  -9.132  1.00 28.81  ?  361  PRO A CA  1 
ATOM   2523  C  C   . PRO A  1 330 ? 10.149  9.951   -8.269  1.00 32.25  ?  361  PRO A C   1 
ATOM   2524  O  O   . PRO A  1 330 ? 11.332  10.204  -8.536  1.00 29.79  ?  361  PRO A O   1 
ATOM   2525  C  CB  . PRO A  1 330 ? 8.796   9.597   -10.379 1.00 26.74  ?  361  PRO A CB  1 
ATOM   2526  C  CG  . PRO A  1 330 ? 9.256   10.429  -11.510 1.00 29.69  ?  361  PRO A CG  1 
ATOM   2527  C  CD  . PRO A  1 330 ? 9.043   11.826  -11.141 1.00 24.03  ?  361  PRO A CD  1 
ATOM   2528  N  N   . VAL A  1 331 ? 9.773   9.234   -7.202  1.00 26.71  ?  362  VAL A N   1 
ATOM   2529  C  CA  . VAL A  1 331 ? 10.693  8.639   -6.239  1.00 26.94  ?  362  VAL A CA  1 
ATOM   2530  C  C   . VAL A  1 331 ? 10.171  7.253   -5.890  1.00 26.17  ?  362  VAL A C   1 
ATOM   2531  O  O   . VAL A  1 331 ? 9.030   6.893   -6.205  1.00 26.62  ?  362  VAL A O   1 
ATOM   2532  C  CB  . VAL A  1 331 ? 10.851  9.491   -4.954  1.00 28.11  ?  362  VAL A CB  1 
ATOM   2533  C  CG1 . VAL A  1 331 ? 11.362  10.897  -5.300  1.00 24.69  ?  362  VAL A CG1 1 
ATOM   2534  C  CG2 . VAL A  1 331 ? 9.504   9.566   -4.200  1.00 24.97  ?  362  VAL A CG2 1 
ATOM   2535  N  N   . SER A  1 332 ? 11.026  6.473   -5.238  1.00 24.34  ?  363  SER A N   1 
ATOM   2536  C  CA  . SER A  1 332 ? 10.751  5.088   -4.897  1.00 24.24  ?  363  SER A CA  1 
ATOM   2537  C  C   . SER A  1 332 ? 10.979  4.868   -3.414  1.00 28.75  ?  363  SER A C   1 
ATOM   2538  O  O   . SER A  1 332 ? 11.853  5.491   -2.803  1.00 27.23  ?  363  SER A O   1 
ATOM   2539  C  CB  . SER A  1 332 ? 11.648  4.121   -5.693  1.00 28.36  ?  363  SER A CB  1 
ATOM   2540  O  OG  . SER A  1 332 ? 11.495  2.786   -5.217  1.00 28.93  ?  363  SER A OG  1 
ATOM   2541  N  N   . SER A  1 333 ? 10.192  3.959   -2.831  1.00 26.57  ?  364  SER A N   1 
ATOM   2542  C  CA  . SER A  1 333 ? 10.504  3.501   -1.484  1.00 27.60  ?  364  SER A CA  1 
ATOM   2543  C  C   . SER A  1 333 ? 11.889  2.851   -1.416  1.00 28.14  ?  364  SER A C   1 
ATOM   2544  O  O   . SER A  1 333 ? 12.458  2.738   -0.322  1.00 25.84  ?  364  SER A O   1 
ATOM   2545  C  CB  . SER A  1 333 ? 9.432   2.529   -0.997  1.00 24.31  ?  364  SER A CB  1 
ATOM   2546  O  OG  . SER A  1 333 ? 9.462   1.331   -1.745  1.00 24.96  ?  364  SER A OG  1 
ATOM   2547  N  N   . LEU A  1 334 ? 12.443  2.434   -2.559  1.00 28.39  ?  365  LEU A N   1 
ATOM   2548  C  CA  . LEU A  1 334 ? 13.834  1.973   -2.599  1.00 26.68  ?  365  LEU A CA  1 
ATOM   2549  C  C   . LEU A  1 334 ? 14.814  3.068   -2.223  1.00 28.57  ?  365  LEU A C   1 
ATOM   2550  O  O   . LEU A  1 334 ? 15.951  2.760   -1.854  1.00 29.01  ?  365  LEU A O   1 
ATOM   2551  C  CB  . LEU A  1 334 ? 14.161  1.426   -3.997  1.00 27.47  ?  365  LEU A CB  1 
ATOM   2552  C  CG  . LEU A  1 334 ? 13.361  0.160   -4.295  1.00 30.13  ?  365  LEU A CG  1 
ATOM   2553  C  CD1 . LEU A  1 334 ? 13.362  -0.212  -5.794  1.00 26.27  ?  365  LEU A CD1 1 
ATOM   2554  C  CD2 . LEU A  1 334 ? 13.879  -0.976  -3.454  1.00 25.13  ?  365  LEU A CD2 1 
ATOM   2555  N  N   . ASP A  1 335 ? 14.406  4.340   -2.285  1.00 28.78  ?  366  ASP A N   1 
ATOM   2556  C  CA  . ASP A  1 335 ? 15.335  5.409   -1.936  1.00 29.51  ?  366  ASP A CA  1 
ATOM   2557  C  C   . ASP A  1 335 ? 15.566  5.523   -0.434  1.00 31.99  ?  366  ASP A C   1 
ATOM   2558  O  O   . ASP A  1 335 ? 16.559  6.131   -0.026  1.00 30.03  ?  366  ASP A O   1 
ATOM   2559  C  CB  . ASP A  1 335 ? 14.839  6.747   -2.497  1.00 25.17  ?  366  ASP A CB  1 
ATOM   2560  C  CG  . ASP A  1 335 ? 14.593  6.693   -4.001  1.00 30.45  ?  366  ASP A CG  1 
ATOM   2561  O  OD1 . ASP A  1 335 ? 15.249  5.888   -4.708  1.00 30.70  ?  366  ASP A OD1 1 
ATOM   2562  O  OD2 . ASP A  1 335 ? 13.751  7.477   -4.491  1.00 31.60  -1 366  ASP A OD2 1 
ATOM   2563  N  N   . LEU A  1 336 ? 14.685  4.952   0.403   1.00 30.55  ?  367  LEU A N   1 
ATOM   2564  C  CA  . LEU A  1 336 ? 14.830  5.117   1.849   1.00 29.59  ?  367  LEU A CA  1 
ATOM   2565  C  C   . LEU A  1 336 ? 16.142  4.526   2.362   1.00 30.78  ?  367  LEU A C   1 
ATOM   2566  O  O   . LEU A  1 336 ? 16.829  5.154   3.171   1.00 28.06  ?  367  LEU A O   1 
ATOM   2567  C  CB  . LEU A  1 336 ? 13.646  4.479   2.572   1.00 29.78  ?  367  LEU A CB  1 
ATOM   2568  C  CG  . LEU A  1 336 ? 12.295  5.088   2.188   1.00 26.39  ?  367  LEU A CG  1 
ATOM   2569  C  CD1 . LEU A  1 336 ? 11.206  4.549   3.113   1.00 28.20  ?  367  LEU A CD1 1 
ATOM   2570  C  CD2 . LEU A  1 336 ? 12.317  6.618   2.175   1.00 26.26  ?  367  LEU A CD2 1 
ATOM   2571  N  N   . TYR A  1 337 ? 16.509  3.326   1.901   1.00 28.57  ?  368  TYR A N   1 
ATOM   2572  C  CA  . TYR A  1 337 ? 17.767  2.717   2.338   1.00 28.63  ?  368  TYR A CA  1 
ATOM   2573  C  C   . TYR A  1 337 ? 18.971  3.618   2.067   1.00 31.12  ?  368  TYR A C   1 
ATOM   2574  O  O   . TYR A  1 337 ? 19.612  4.070   3.035   1.00 32.61  ?  368  TYR A O   1 
ATOM   2575  C  CB  . TYR A  1 337 ? 17.884  1.326   1.701   1.00 29.75  ?  368  TYR A CB  1 
ATOM   2576  C  CG  . TYR A  1 337 ? 18.887  0.348   2.304   1.00 30.61  ?  368  TYR A CG  1 
ATOM   2577  C  CD1 . TYR A  1 337 ? 20.230  0.690   2.493   1.00 34.54  ?  368  TYR A CD1 1 
ATOM   2578  C  CD2 . TYR A  1 337 ? 18.493  -0.947  2.632   1.00 29.02  ?  368  TYR A CD2 1 
ATOM   2579  C  CE1 . TYR A  1 337 ? 21.130  -0.230  3.022   1.00 31.93  ?  368  TYR A CE1 1 
ATOM   2580  C  CE2 . TYR A  1 337 ? 19.383  -1.867  3.150   1.00 30.10  ?  368  TYR A CE2 1 
ATOM   2581  C  CZ  . TYR A  1 337 ? 20.690  -1.502  3.344   1.00 32.60  ?  368  TYR A CZ  1 
ATOM   2582  O  OH  . TYR A  1 337 ? 21.546  -2.437  3.855   1.00 29.21  ?  368  TYR A OH  1 
ATOM   2583  N  N   . PRO A  1 338 ? 19.333  3.941   0.821   1.00 32.49  ?  369  PRO A N   1 
ATOM   2584  C  CA  . PRO A  1 338 ? 20.534  4.785   0.639   1.00 32.88  ?  369  PRO A CA  1 
ATOM   2585  C  C   . PRO A  1 338 ? 20.384  6.162   1.247   1.00 34.66  ?  369  PRO A C   1 
ATOM   2586  O  O   . PRO A  1 338 ? 21.374  6.736   1.711   1.00 32.40  ?  369  PRO A O   1 
ATOM   2587  C  CB  . PRO A  1 338 ? 20.689  4.881   -0.886  1.00 30.33  ?  369  PRO A CB  1 
ATOM   2588  C  CG  . PRO A  1 338 ? 19.294  4.524   -1.427  1.00 31.31  ?  369  PRO A CG  1 
ATOM   2589  C  CD  . PRO A  1 338 ? 18.748  3.531   -0.472  1.00 31.31  ?  369  PRO A CD  1 
ATOM   2590  N  N   . THR A  1 339 ? 19.177  6.727   1.252   1.00 30.31  ?  370  THR A N   1 
ATOM   2591  C  CA  . THR A  1 339 ? 19.007  8.041   1.861   1.00 28.87  ?  370  THR A CA  1 
ATOM   2592  C  C   . THR A  1 339 ? 19.277  7.994   3.363   1.00 29.36  ?  370  THR A C   1 
ATOM   2593  O  O   . THR A  1 339 ? 19.990  8.853   3.901   1.00 31.56  ?  370  THR A O   1 
ATOM   2594  C  CB  . THR A  1 339 ? 17.601  8.568   1.596   1.00 29.63  ?  370  THR A CB  1 
ATOM   2595  O  OG1 . THR A  1 339 ? 17.326  8.497   0.192   1.00 29.38  ?  370  THR A OG1 1 
ATOM   2596  C  CG2 . THR A  1 339 ? 17.495  10.001  2.067   1.00 32.57  ?  370  THR A CG2 1 
ATOM   2597  N  N   . PHE A  1 340 ? 18.715  6.994   4.061   1.00 26.91  ?  371  PHE A N   1 
ATOM   2598  C  CA  . PHE A  1 340 ? 18.877  6.924   5.508   1.00 28.14  ?  371  PHE A CA  1 
ATOM   2599  C  C   . PHE A  1 340 ? 20.327  6.619   5.880   1.00 30.13  ?  371  PHE A C   1 
ATOM   2600  O  O   . PHE A  1 340 ? 20.880  7.221   6.809   1.00 33.62  ?  371  PHE A O   1 
ATOM   2601  C  CB  . PHE A  1 340 ? 17.957  5.861   6.116   1.00 29.02  ?  371  PHE A CB  1 
ATOM   2602  C  CG  . PHE A  1 340 ? 16.468  6.181   6.014   1.00 30.42  ?  371  PHE A CG  1 
ATOM   2603  C  CD1 . PHE A  1 340 ? 16.026  7.439   5.636   1.00 31.56  ?  371  PHE A CD1 1 
ATOM   2604  C  CD2 . PHE A  1 340 ? 15.532  5.215   6.338   1.00 29.95  ?  371  PHE A CD2 1 
ATOM   2605  C  CE1 . PHE A  1 340 ? 14.656  7.725   5.566   1.00 34.61  ?  371  PHE A CE1 1 
ATOM   2606  C  CE2 . PHE A  1 340 ? 14.164  5.484   6.278   1.00 26.94  ?  371  PHE A CE2 1 
ATOM   2607  C  CZ  . PHE A  1 340 ? 13.732  6.740   5.896   1.00 27.45  ?  371  PHE A CZ  1 
ATOM   2608  N  N   . THR A  1 341 ? 20.954  5.665   5.186   1.00 30.30  ?  372  THR A N   1 
ATOM   2609  C  CA  . THR A  1 341 ? 22.330  5.323   5.554   1.00 35.48  ?  372  THR A CA  1 
ATOM   2610  C  C   . THR A  1 341 ? 23.266  6.480   5.231   1.00 35.91  ?  372  THR A C   1 
ATOM   2611  O  O   . THR A  1 341 ? 24.260  6.692   5.935   1.00 35.74  ?  372  THR A O   1 
ATOM   2612  C  CB  . THR A  1 341 ? 22.783  4.030   4.855   1.00 33.60  ?  372  THR A CB  1 
ATOM   2613  O  OG1 . THR A  1 341 ? 22.655  4.173   3.444   1.00 35.99  ?  372  THR A OG1 1 
ATOM   2614  C  CG2 . THR A  1 341 ? 21.962  2.811   5.300   1.00 32.70  ?  372  THR A CG2 1 
ATOM   2615  N  N   . GLY A  1 342 ? 22.948  7.251   4.191   1.00 35.07  ?  373  GLY A N   1 
ATOM   2616  C  CA  . GLY A  1 342 ? 23.690  8.472   3.934   1.00 34.54  ?  373  GLY A CA  1 
ATOM   2617  C  C   . GLY A  1 342 ? 23.542  9.485   5.053   1.00 40.89  ?  373  GLY A C   1 
ATOM   2618  O  O   . GLY A  1 342 ? 24.523  10.084  5.504   1.00 37.27  ?  373  GLY A O   1 
ATOM   2619  N  N   . LEU A  1 343 ? 22.310  9.689   5.527   1.00 34.72  ?  374  LEU A N   1 
ATOM   2620  C  CA  . LEU A  1 343 ? 22.098  10.647  6.611   1.00 35.99  ?  374  LEU A CA  1 
ATOM   2621  C  C   . LEU A  1 343 ? 22.807  10.197  7.882   1.00 38.84  ?  374  LEU A C   1 
ATOM   2622  O  O   . LEU A  1 343 ? 23.263  11.026  8.685   1.00 37.75  ?  374  LEU A O   1 
ATOM   2623  C  CB  . LEU A  1 343 ? 20.599  10.815  6.879   1.00 33.54  ?  374  LEU A CB  1 
ATOM   2624  C  CG  . LEU A  1 343 ? 19.773  11.548  5.815   1.00 39.55  ?  374  LEU A CG  1 
ATOM   2625  C  CD1 . LEU A  1 343 ? 18.318  11.641  6.267   1.00 34.98  ?  374  LEU A CD1 1 
ATOM   2626  C  CD2 . LEU A  1 343 ? 20.317  12.935  5.505   1.00 35.13  ?  374  LEU A CD2 1 
ATOM   2627  N  N   . ALA A  1 344 ? 22.901  8.893   8.076   1.00 35.49  ?  375  ALA A N   1 
ATOM   2628  C  CA  . ALA A  1 344 ? 23.521  8.316   9.244   1.00 35.14  ?  375  ALA A CA  1 
ATOM   2629  C  C   . ALA A  1 344 ? 25.032  8.248   9.124   1.00 40.04  ?  375  ALA A C   1 
ATOM   2630  O  O   . ALA A  1 344 ? 25.681  7.752   10.051  1.00 39.38  ?  375  ALA A O   1 
ATOM   2631  C  CB  . ALA A  1 344 ? 22.974  6.921   9.467   1.00 33.10  ?  375  ALA A CB  1 
ATOM   2632  N  N   . GLU A  1 345 ? 25.576  8.713   7.997   1.00 34.37  ?  376  GLU A N   1 
ATOM   2633  C  CA  . GLU A  1 345 ? 26.987  8.591   7.669   1.00 44.44  ?  376  GLU A CA  1 
ATOM   2634  C  C   . GLU A  1 345 ? 27.459  7.162   7.887   1.00 42.59  ?  376  GLU A C   1 
ATOM   2635  O  O   . GLU A  1 345 ? 28.567  6.919   8.357   1.00 43.57  ?  376  GLU A O   1 
ATOM   2636  C  CB  . GLU A  1 345 ? 27.816  9.587   8.481   1.00 44.99  ?  376  GLU A CB  1 
ATOM   2637  C  CG  . GLU A  1 345 ? 27.226  10.981  8.451   1.00 42.59  ?  376  GLU A CG  1 
ATOM   2638  C  CD  . GLU A  1 345 ? 27.958  11.944  9.365   1.00 52.32  ?  376  GLU A CD  1 
ATOM   2639  O  OE1 . GLU A  1 345 ? 28.715  11.480  10.246  1.00 57.87  ?  376  GLU A OE1 1 
ATOM   2640  O  OE2 . GLU A  1 345 ? 27.752  13.165  9.221   1.00 56.53  -1 376  GLU A OE2 1 
ATOM   2641  N  N   . ALA A  1 346 ? 26.588  6.210   7.564   1.00 37.39  ?  377  ALA A N   1 
ATOM   2642  C  CA  . ALA A  1 346 ? 26.839  4.799   7.808   1.00 39.17  ?  377  ALA A CA  1 
ATOM   2643  C  C   . ALA A  1 346 ? 27.501  4.169   6.596   1.00 44.32  ?  377  ALA A C   1 
ATOM   2644  O  O   . ALA A  1 346 ? 27.270  4.581   5.458   1.00 51.20  ?  377  ALA A O   1 
ATOM   2645  C  CB  . ALA A  1 346 ? 25.543  4.061   8.140   1.00 40.67  ?  377  ALA A CB  1 
ATOM   2646  N  N   . LYS A  1 347 ? 28.355  3.178   6.855   1.00 45.07  ?  378  LYS A N   1 
ATOM   2647  C  CA  . LYS A  1 347 ? 29.080  2.479   5.807   1.00 43.71  ?  378  LYS A CA  1 
ATOM   2648  C  C   . LYS A  1 347 ? 28.297  1.253   5.363   1.00 36.55  ?  378  LYS A C   1 
ATOM   2649  O  O   . LYS A  1 347 ? 27.854  0.459   6.196   1.00 42.06  ?  378  LYS A O   1 
ATOM   2650  C  CB  . LYS A  1 347 ? 30.470  2.058   6.298   1.00 48.11  ?  378  LYS A CB  1 
ATOM   2651  N  N   . LEU A  1 348 ? 28.166  1.078   4.051   1.00 43.57  ?  379  LEU A N   1 
ATOM   2652  C  CA  . LEU A  1 348 ? 27.431  -0.087  3.582   1.00 45.60  ?  379  LEU A CA  1 
ATOM   2653  C  C   . LEU A  1 348 ? 28.301  -1.337  3.683   1.00 46.61  ?  379  LEU A C   1 
ATOM   2654  O  O   . LEU A  1 348 ? 29.510  -1.264  3.447   1.00 46.46  ?  379  LEU A O   1 
ATOM   2655  C  CB  . LEU A  1 348 ? 26.986  0.110   2.136   1.00 45.84  ?  379  LEU A CB  1 
ATOM   2656  C  CG  . LEU A  1 348 ? 25.985  1.237   1.923   1.00 44.37  ?  379  LEU A CG  1 
ATOM   2657  C  CD1 . LEU A  1 348 ? 25.461  1.226   0.489   1.00 44.46  ?  379  LEU A CD1 1 
ATOM   2658  C  CD2 . LEU A  1 348 ? 24.854  1.113   2.938   1.00 45.03  ?  379  LEU A CD2 1 
ATOM   2659  N  N   . PRO A  1 349 ? 27.714  -2.489  4.013   1.00 39.66  ?  380  PRO A N   1 
ATOM   2660  C  CA  . PRO A  1 349 ? 28.487  -3.731  4.013   1.00 42.15  ?  380  PRO A CA  1 
ATOM   2661  C  C   . PRO A  1 349 ? 29.079  -3.969  2.640   1.00 46.30  ?  380  PRO A C   1 
ATOM   2662  O  O   . PRO A  1 349 ? 28.516  -3.565  1.622   1.00 45.13  ?  380  PRO A O   1 
ATOM   2663  C  CB  . PRO A  1 349 ? 27.445  -4.803  4.362   1.00 47.45  ?  380  PRO A CB  1 
ATOM   2664  C  CG  . PRO A  1 349 ? 26.298  -4.046  4.957   1.00 40.71  ?  380  PRO A CG  1 
ATOM   2665  C  CD  . PRO A  1 349 ? 26.280  -2.755  4.200   1.00 45.00  ?  380  PRO A CD  1 
ATOM   2666  N  N   . LYS A  1 350 ? 30.237  -4.621  2.612   1.00 48.73  ?  381  LYS A N   1 
ATOM   2667  C  CA  . LYS A  1 350 ? 30.887  -4.862  1.335   1.00 42.36  ?  381  LYS A CA  1 
ATOM   2668  C  C   . LYS A  1 350 ? 30.020  -5.776  0.486   1.00 41.33  ?  381  LYS A C   1 
ATOM   2669  O  O   . LYS A  1 350 ? 29.468  -6.768  0.975   1.00 40.44  ?  381  LYS A O   1 
ATOM   2670  C  CB  . LYS A  1 350 ? 32.278  -5.473  1.532   1.00 45.58  ?  381  LYS A CB  1 
ATOM   2671  N  N   . GLY A  1 351 ? 29.891  -5.428  -0.795  1.00 41.39  ?  382  GLY A N   1 
ATOM   2672  C  CA  . GLY A  1 351 ? 29.063  -6.185  -1.709  1.00 43.16  ?  382  GLY A CA  1 
ATOM   2673  C  C   . GLY A  1 351 ? 27.582  -5.870  -1.662  1.00 41.63  ?  382  GLY A C   1 
ATOM   2674  O  O   . GLY A  1 351 ? 26.813  -6.478  -2.417  1.00 37.40  ?  382  GLY A O   1 
ATOM   2675  N  N   . LYS A  1 352 ? 27.148  -4.939  -0.821  1.00 38.33  ?  383  LYS A N   1 
ATOM   2676  C  CA  . LYS A  1 352 ? 25.717  -4.654  -0.740  1.00 40.56  ?  383  LYS A CA  1 
ATOM   2677  C  C   . LYS A  1 352 ? 25.228  -3.978  -2.019  1.00 39.82  ?  383  LYS A C   1 
ATOM   2678  O  O   . LYS A  1 352 ? 25.815  -2.994  -2.484  1.00 39.59  ?  383  LYS A O   1 
ATOM   2679  C  CB  . LYS A  1 352 ? 25.411  -3.780  0.480   1.00 42.66  ?  383  LYS A CB  1 
ATOM   2680  C  CG  . LYS A  1 352 ? 23.934  -3.351  0.600   1.00 36.40  ?  383  LYS A CG  1 
ATOM   2681  C  CD  . LYS A  1 352 ? 23.015  -4.517  0.909   1.00 35.68  ?  383  LYS A CD  1 
ATOM   2682  C  CE  . LYS A  1 352 ? 21.544  -4.110  0.655   1.00 35.03  ?  383  LYS A CE  1 
ATOM   2683  N  NZ  . LYS A  1 352 ? 20.612  -5.094  1.235   1.00 33.79  ?  383  LYS A NZ  1 
ATOM   2684  N  N   . GLN A  1 353 ? 24.135  -4.502  -2.576  1.00 35.95  ?  384  GLN A N   1 
ATOM   2685  C  CA  . GLN A  1 353 ? 23.501  -3.967  -3.777  1.00 41.84  ?  384  GLN A CA  1 
ATOM   2686  C  C   . GLN A  1 353 ? 22.222  -3.220  -3.409  1.00 38.22  ?  384  GLN A C   1 
ATOM   2687  O  O   . GLN A  1 353 ? 21.476  -3.662  -2.534  1.00 33.11  ?  384  GLN A O   1 
ATOM   2688  C  CB  . GLN A  1 353 ? 23.187  -5.105  -4.749  1.00 35.91  ?  384  GLN A CB  1 
ATOM   2689  C  CG  . GLN A  1 353 ? 24.442  -5.916  -5.111  1.00 44.91  ?  384  GLN A CG  1 
ATOM   2690  C  CD  . GLN A  1 353 ? 24.817  -5.744  -6.557  1.00 53.26  ?  384  GLN A CD  1 
ATOM   2691  O  OE1 . GLN A  1 353 ? 25.305  -4.688  -6.960  1.00 56.15  ?  384  GLN A OE1 1 
ATOM   2692  N  NE2 . GLN A  1 353 ? 24.598  -6.790  -7.356  1.00 59.96  ?  384  GLN A NE2 1 
ATOM   2693  N  N   . LEU A  1 354 ? 21.985  -2.081  -4.074  1.00 38.44  ?  385  LEU A N   1 
ATOM   2694  C  CA  . LEU A  1 354 ? 20.855  -1.199  -3.793  1.00 37.02  ?  385  LEU A CA  1 
ATOM   2695  C  C   . LEU A  1 354 ? 20.228  -0.739  -5.104  1.00 38.08  ?  385  LEU A C   1 
ATOM   2696  O  O   . LEU A  1 354 ? 20.940  -0.380  -6.049  1.00 33.48  ?  385  LEU A O   1 
ATOM   2697  C  CB  . LEU A  1 354 ? 21.296  0.038   -2.987  1.00 32.86  ?  385  LEU A CB  1 
ATOM   2698  C  CG  . LEU A  1 354 ? 21.751  -0.142  -1.535  1.00 35.87  ?  385  LEU A CG  1 
ATOM   2699  C  CD1 . LEU A  1 354 ? 22.121  1.205   -0.946  1.00 32.61  ?  385  LEU A CD1 1 
ATOM   2700  C  CD2 . LEU A  1 354 ? 20.669  -0.833  -0.683  1.00 31.88  ?  385  LEU A CD2 1 
ATOM   2701  N  N   . ASP A  1 355 ? 18.891  -0.709  -5.156  1.00 35.31  ?  386  ASP A N   1 
ATOM   2702  C  CA  . ASP A  1 355 ? 18.216  -0.313  -6.384  1.00 28.93  ?  386  ASP A CA  1 
ATOM   2703  C  C   . ASP A  1 355 ? 17.747  1.139   -6.368  1.00 34.76  ?  386  ASP A C   1 
ATOM   2704  O  O   . ASP A  1 355 ? 17.373  1.668   -7.423  1.00 35.02  ?  386  ASP A O   1 
ATOM   2705  C  CB  . ASP A  1 355 ? 17.040  -1.273  -6.665  1.00 30.01  ?  386  ASP A CB  1 
ATOM   2706  C  CG  . ASP A  1 355 ? 17.517  -2.640  -7.178  1.00 35.42  ?  386  ASP A CG  1 
ATOM   2707  O  OD1 . ASP A  1 355 ? 18.405  -2.639  -8.044  1.00 42.29  ?  386  ASP A OD1 1 
ATOM   2708  O  OD2 . ASP A  1 355 ? 17.042  -3.716  -6.726  1.00 33.87  -1 386  ASP A OD2 1 
ATOM   2709  N  N   . GLY A  1 356 ? 17.803  1.814   -5.222  1.00 32.34  ?  387  GLY A N   1 
ATOM   2710  C  CA  . GLY A  1 356 ? 17.385  3.193   -5.121  1.00 30.25  ?  387  GLY A CA  1 
ATOM   2711  C  C   . GLY A  1 356 ? 18.549  4.164   -5.043  1.00 35.66  ?  387  GLY A C   1 
ATOM   2712  O  O   . GLY A  1 356 ? 19.722  3.816   -5.212  1.00 31.06  ?  387  GLY A O   1 
ATOM   2713  N  N   . LYS A  1 357 ? 18.204  5.415   -4.778  1.00 36.04  ?  388  LYS A N   1 
ATOM   2714  C  CA  . LYS A  1 357 ? 19.169  6.494   -4.730  1.00 36.23  ?  388  LYS A CA  1 
ATOM   2715  C  C   . LYS A  1 357 ? 19.003  7.275   -3.442  1.00 35.23  ?  388  LYS A C   1 
ATOM   2716  O  O   . LYS A  1 357 ? 17.923  7.305   -2.841  1.00 29.33  ?  388  LYS A O   1 
ATOM   2717  C  CB  . LYS A  1 357 ? 19.022  7.477   -5.900  1.00 36.84  ?  388  LYS A CB  1 
ATOM   2718  C  CG  . LYS A  1 357 ? 18.402  6.938   -7.139  1.00 36.36  ?  388  LYS A CG  1 
ATOM   2719  C  CD  . LYS A  1 357 ? 18.355  8.026   -8.194  1.00 39.15  ?  388  LYS A CD  1 
ATOM   2720  C  CE  . LYS A  1 357 ? 18.277  7.414   -9.584  1.00 40.94  ?  388  LYS A CE  1 
ATOM   2721  N  NZ  . LYS A  1 357 ? 19.600  6.867   -10.014 1.00 48.11  ?  388  LYS A NZ  1 
ATOM   2722  N  N   . ASN A  1 358 ? 20.092  7.912   -3.037  1.00 28.18  ?  389  ASN A N   1 
ATOM   2723  C  CA  . ASN A  1 358 ? 20.077  8.865   -1.937  1.00 31.24  ?  389  ASN A CA  1 
ATOM   2724  C  C   . ASN A  1 358 ? 19.525  10.168  -2.493  1.00 31.96  ?  389  ASN A C   1 
ATOM   2725  O  O   . ASN A  1 358 ? 20.225  10.903  -3.191  1.00 36.79  ?  389  ASN A O   1 
ATOM   2726  C  CB  . ASN A  1 358 ? 21.491  9.036   -1.380  1.00 29.69  ?  389  ASN A CB  1 
ATOM   2727  C  CG  . ASN A  1 358 ? 21.578  10.076  -0.292  1.00 34.69  ?  389  ASN A CG  1 
ATOM   2728  O  OD1 . ASN A  1 358 ? 20.647  10.842  -0.052  1.00 34.39  ?  389  ASN A OD1 1 
ATOM   2729  N  ND2 . ASN A  1 358 ? 22.743  10.144  0.351   1.00 37.47  ?  389  ASN A ND2 1 
ATOM   2730  N  N   . ILE A  1 359 ? 18.271  10.482  -2.171  1.00 31.00  ?  390  ILE A N   1 
ATOM   2731  C  CA  . ILE A  1 359 ? 17.559  11.563  -2.826  1.00 28.94  ?  390  ILE A CA  1 
ATOM   2732  C  C   . ILE A  1 359 ? 17.506  12.833  -1.985  1.00 28.75  ?  390  ILE A C   1 
ATOM   2733  O  O   . ILE A  1 359 ? 16.852  13.797  -2.387  1.00 29.91  ?  390  ILE A O   1 
ATOM   2734  C  CB  . ILE A  1 359 ? 16.125  11.129  -3.226  1.00 31.06  ?  390  ILE A CB  1 
ATOM   2735  C  CG1 . ILE A  1 359 ? 15.288  10.771  -1.970  1.00 26.99  ?  390  ILE A CG1 1 
ATOM   2736  C  CG2 . ILE A  1 359 ? 16.193  9.977   -4.231  1.00 26.18  ?  390  ILE A CG2 1 
ATOM   2737  C  CD1 . ILE A  1 359 ? 13.717  10.679  -2.249  1.00 26.47  ?  390  ILE A CD1 1 
ATOM   2738  N  N   . MET A  1 360 ? 18.192  12.883  -0.841  1.00 34.53  ?  391  MET A N   1 
ATOM   2739  C  CA  . MET A  1 360 ? 17.909  14.009  0.036   1.00 32.09  ?  391  MET A CA  1 
ATOM   2740  C  C   . MET A  1 360 ? 18.415  15.316  -0.571  1.00 32.33  ?  391  MET A C   1 
ATOM   2741  O  O   . MET A  1 360 ? 17.747  16.354  -0.462  1.00 32.73  ?  391  MET A O   1 
ATOM   2742  C  CB  . MET A  1 360 ? 18.473  13.760  1.439   1.00 34.37  ?  391  MET A CB  1 
ATOM   2743  C  CG  . MET A  1 360 ? 18.277  14.935  2.391   1.00 36.56  ?  391  MET A CG  1 
ATOM   2744  S  SD  . MET A  1 360 ? 16.504  15.218  2.745   1.00 36.23  ?  391  MET A SD  1 
ATOM   2745  C  CE  . MET A  1 360 ? 16.117  13.760  3.703   1.00 30.44  ?  391  MET A CE  1 
ATOM   2746  N  N   . ASP A  1 361 ? 19.567  15.291  -1.255  1.00 35.24  ?  392  ASP A N   1 
ATOM   2747  C  CA  . ASP A  1 361 ? 20.005  16.509  -1.933  1.00 31.43  ?  392  ASP A CA  1 
ATOM   2748  C  C   . ASP A  1 361 ? 19.010  16.932  -3.009  1.00 35.18  ?  392  ASP A C   1 
ATOM   2749  O  O   . ASP A  1 361 ? 18.758  18.131  -3.198  1.00 36.82  ?  392  ASP A O   1 
ATOM   2750  C  CB  . ASP A  1 361 ? 21.390  16.326  -2.545  1.00 40.46  ?  392  ASP A CB  1 
ATOM   2751  C  CG  . ASP A  1 361 ? 21.924  17.616  -3.142  1.00 48.48  ?  392  ASP A CG  1 
ATOM   2752  O  OD1 . ASP A  1 361 ? 22.134  18.578  -2.363  1.00 52.34  -1 392  ASP A OD1 1 
ATOM   2753  O  OD2 . ASP A  1 361 ? 22.105  17.680  -4.383  1.00 50.29  ?  392  ASP A OD2 1 
ATOM   2754  N  N   . ASP A  1 362 ? 18.431  15.965  -3.730  1.00 30.40  ?  393  ASP A N   1 
ATOM   2755  C  CA  . ASP A  1 362 ? 17.421  16.313  -4.734  1.00 31.77  ?  393  ASP A CA  1 
ATOM   2756  C  C   . ASP A  1 362 ? 16.193  16.955  -4.103  1.00 32.66  ?  393  ASP A C   1 
ATOM   2757  O  O   . ASP A  1 362 ? 15.614  17.898  -4.663  1.00 32.10  ?  393  ASP A O   1 
ATOM   2758  C  CB  . ASP A  1 362 ? 17.006  15.077  -5.516  1.00 33.98  ?  393  ASP A CB  1 
ATOM   2759  C  CG  . ASP A  1 362 ? 18.079  14.612  -6.464  1.00 35.12  ?  393  ASP A CG  1 
ATOM   2760  O  OD1 . ASP A  1 362 ? 18.319  15.318  -7.467  1.00 36.70  ?  393  ASP A OD1 1 
ATOM   2761  O  OD2 . ASP A  1 362 ? 18.664  13.542  -6.209  1.00 37.69  -1 393  ASP A OD2 1 
ATOM   2762  N  N   . VAL A  1 363 ? 15.760  16.448  -2.946  1.00 32.87  ?  394  VAL A N   1 
ATOM   2763  C  CA  . VAL A  1 363 ? 14.596  17.038  -2.292  1.00 29.43  ?  394  VAL A CA  1 
ATOM   2764  C  C   . VAL A  1 363 ? 14.911  18.457  -1.832  1.00 33.14  ?  394  VAL A C   1 
ATOM   2765  O  O   . VAL A  1 363 ? 14.089  19.363  -1.971  1.00 32.23  ?  394  VAL A O   1 
ATOM   2766  C  CB  . VAL A  1 363 ? 14.141  16.148  -1.120  1.00 31.76  ?  394  VAL A CB  1 
ATOM   2767  C  CG1 . VAL A  1 363 ? 13.035  16.821  -0.344  1.00 34.29  ?  394  VAL A CG1 1 
ATOM   2768  C  CG2 . VAL A  1 363 ? 13.710  14.754  -1.614  1.00 26.53  ?  394  VAL A CG2 1 
ATOM   2769  N  N   . LEU A  1 364 ? 16.123  18.683  -1.315  1.00 31.36  ?  395  LEU A N   1 
ATOM   2770  C  CA  . LEU A  1 364 ? 16.469  20.002  -0.797  1.00 33.44  ?  395  LEU A CA  1 
ATOM   2771  C  C   . LEU A  1 364 ? 16.614  21.015  -1.919  1.00 37.04  ?  395  LEU A C   1 
ATOM   2772  O  O   . LEU A  1 364 ? 16.277  22.191  -1.739  1.00 39.13  ?  395  LEU A O   1 
ATOM   2773  C  CB  . LEU A  1 364 ? 17.769  19.923  0.015   1.00 33.68  ?  395  LEU A CB  1 
ATOM   2774  C  CG  . LEU A  1 364 ? 17.678  19.090  1.284   1.00 32.29  ?  395  LEU A CG  1 
ATOM   2775  C  CD1 . LEU A  1 364 ? 18.976  19.127  2.130   1.00 34.11  ?  395  LEU A CD1 1 
ATOM   2776  C  CD2 . LEU A  1 364 ? 16.483  19.544  2.114   1.00 34.27  ?  395  LEU A CD2 1 
ATOM   2777  N  N   . LYS A  1 365 ? 17.072  20.576  -3.088  1.00 32.04  ?  396  LYS A N   1 
ATOM   2778  C  CA  . LYS A  1 365 ? 17.264  21.469  -4.221  1.00 34.57  ?  396  LYS A CA  1 
ATOM   2779  C  C   . LYS A  1 365 ? 16.175  21.362  -5.275  1.00 37.35  ?  396  LYS A C   1 
ATOM   2780  O  O   . LYS A  1 365 ? 16.264  22.050  -6.293  1.00 36.81  ?  396  LYS A O   1 
ATOM   2781  C  CB  . LYS A  1 365 ? 18.627  21.212  -4.850  1.00 36.01  ?  396  LYS A CB  1 
ATOM   2782  C  CG  . LYS A  1 365 ? 19.731  21.235  -3.784  1.00 39.33  ?  396  LYS A CG  1 
ATOM   2783  C  CD  . LYS A  1 365 ? 20.973  21.989  -4.251  1.00 47.60  ?  396  LYS A CD  1 
ATOM   2784  C  CE  . LYS A  1 365 ? 22.078  21.977  -3.176  1.00 48.64  ?  396  LYS A CE  1 
ATOM   2785  N  NZ  . LYS A  1 365 ? 23.044  20.837  -3.350  1.00 54.97  ?  396  LYS A NZ  1 
ATOM   2786  N  N   . ASN A  1 366 ? 15.143  20.549  -5.045  1.00 33.39  ?  397  ASN A N   1 
ATOM   2787  C  CA  . ASN A  1 366 ? 14.070  20.338  -6.025  1.00 31.47  ?  397  ASN A CA  1 
ATOM   2788  C  C   . ASN A  1 366 ? 14.630  19.975  -7.397  1.00 34.35  ?  397  ASN A C   1 
ATOM   2789  O  O   . ASN A  1 366 ? 14.312  20.595  -8.412  1.00 34.41  ?  397  ASN A O   1 
ATOM   2790  C  CB  . ASN A  1 366 ? 13.153  21.549  -6.122  1.00 33.52  ?  397  ASN A CB  1 
ATOM   2791  C  CG  . ASN A  1 366 ? 11.892  21.243  -6.912  1.00 38.84  ?  397  ASN A CG  1 
ATOM   2792  O  OD1 . ASN A  1 366 ? 11.290  20.180  -6.752  1.00 36.82  ?  397  ASN A OD1 1 
ATOM   2793  N  ND2 . ASN A  1 366 ? 11.511  22.151  -7.797  1.00 37.06  ?  397  ASN A ND2 1 
ATOM   2794  N  N   . THR A  1 367 ? 15.484  18.957  -7.422  1.00 36.97  ?  398  THR A N   1 
ATOM   2795  C  CA  . THR A  1 367 ? 15.985  18.397  -8.666  1.00 34.61  ?  398  THR A CA  1 
ATOM   2796  C  C   . THR A  1 367 ? 15.473  16.966  -8.804  1.00 37.02  ?  398  THR A C   1 
ATOM   2797  O  O   . THR A  1 367 ? 14.968  16.377  -7.842  1.00 33.13  ?  398  THR A O   1 
ATOM   2798  C  CB  . THR A  1 367 ? 17.523  18.452  -8.735  1.00 36.18  ?  398  THR A CB  1 
ATOM   2799  O  OG1 . THR A  1 367 ? 18.100  17.819  -7.585  1.00 36.60  ?  398  THR A OG1 1 
ATOM   2800  C  CG2 . THR A  1 367 ? 17.997  19.901  -8.793  1.00 37.89  ?  398  THR A CG2 1 
ATOM   2801  N  N   . GLU A  1 368 ? 15.620  16.410  -10.026 1.00 33.64  ?  399  GLU A N   1 
ATOM   2802  C  CA  . GLU A  1 368 ? 14.945  15.201  -10.493 1.00 33.98  ?  399  GLU A CA  1 
ATOM   2803  C  C   . GLU A  1 368 ? 15.838  13.980  -10.324 1.00 33.91  ?  399  GLU A C   1 
ATOM   2804  O  O   . GLU A  1 368 ? 16.725  13.754  -11.155 1.00 36.69  ?  399  GLU A O   1 
ATOM   2805  C  CB  . GLU A  1 368 ? 14.549  15.365  -11.960 1.00 34.66  ?  399  GLU A CB  1 
ATOM   2806  C  CG  . GLU A  1 368 ? 13.707  14.226  -12.545 1.00 32.76  ?  399  GLU A CG  1 
ATOM   2807  C  CD  . GLU A  1 368 ? 13.291  14.507  -13.976 1.00 38.87  ?  399  GLU A CD  1 
ATOM   2808  O  OE1 . GLU A  1 368 ? 13.663  15.588  -14.492 1.00 37.61  ?  399  GLU A OE1 1 
ATOM   2809  O  OE2 . GLU A  1 368 ? 12.597  13.650  -14.587 1.00 37.67  -1 399  GLU A OE2 1 
ATOM   2810  N  N   . PRO A  1 369 ? 15.635  13.143  -9.304  1.00 35.13  ?  400  PRO A N   1 
ATOM   2811  C  CA  . PRO A  1 369 ? 16.593  12.046  -9.075  1.00 32.90  ?  400  PRO A CA  1 
ATOM   2812  C  C   . PRO A  1 369 ? 16.551  10.965  -10.140 1.00 34.87  ?  400  PRO A C   1 
ATOM   2813  O  O   . PRO A  1 369 ? 17.584  10.350  -10.429 1.00 36.77  ?  400  PRO A O   1 
ATOM   2814  C  CB  . PRO A  1 369 ? 16.184  11.498  -7.699  1.00 35.69  ?  400  PRO A CB  1 
ATOM   2815  C  CG  . PRO A  1 369 ? 14.757  11.933  -7.507  1.00 25.81  ?  400  PRO A CG  1 
ATOM   2816  C  CD  . PRO A  1 369 ? 14.662  13.268  -8.204  1.00 30.58  ?  400  PRO A CD  1 
ATOM   2817  N  N   . TYR A  1 370 ? 15.398  10.704  -10.741 1.00 30.36  ?  401  TYR A N   1 
ATOM   2818  C  CA  . TYR A  1 370 ? 15.278  9.613   -11.695 1.00 34.88  ?  401  TYR A CA  1 
ATOM   2819  C  C   . TYR A  1 370 ? 15.257  10.098  -13.140 1.00 36.46  ?  401  TYR A C   1 
ATOM   2820  O  O   . TYR A  1 370 ? 14.689  9.421   -14.006 1.00 33.79  ?  401  TYR A O   1 
ATOM   2821  C  CB  . TYR A  1 370 ? 14.034  8.781   -11.378 1.00 33.70  ?  401  TYR A CB  1 
ATOM   2822  C  CG  . TYR A  1 370 ? 14.305  7.821   -10.244 1.00 28.37  ?  401  TYR A CG  1 
ATOM   2823  C  CD1 . TYR A  1 370 ? 14.175  8.220   -8.915  1.00 25.79  ?  401  TYR A CD1 1 
ATOM   2824  C  CD2 . TYR A  1 370 ? 14.714  6.523   -10.507 1.00 32.17  ?  401  TYR A CD2 1 
ATOM   2825  C  CE1 . TYR A  1 370 ? 14.444  7.336   -7.876  1.00 26.68  ?  401  TYR A CE1 1 
ATOM   2826  C  CE2 . TYR A  1 370 ? 14.984  5.641   -9.484  1.00 32.32  ?  401  TYR A CE2 1 
ATOM   2827  C  CZ  . TYR A  1 370 ? 14.848  6.051   -8.171  1.00 29.69  ?  401  TYR A CZ  1 
ATOM   2828  O  OH  . TYR A  1 370 ? 15.134  5.152   -7.170  1.00 31.98  ?  401  TYR A OH  1 
ATOM   2829  N  N   . LYS A  1 371 ? 15.874  11.252  -13.418 1.00 35.66  ?  402  LYS A N   1 
ATOM   2830  C  CA  . LYS A  1 371 ? 15.828  11.814  -14.764 1.00 35.27  ?  402  LYS A CA  1 
ATOM   2831  C  C   . LYS A  1 371 ? 16.360  10.806  -15.773 1.00 33.72  ?  402  LYS A C   1 
ATOM   2832  O  O   . LYS A  1 371 ? 17.430  10.229  -15.585 1.00 40.78  ?  402  LYS A O   1 
ATOM   2833  C  CB  . LYS A  1 371 ? 16.620  13.114  -14.835 1.00 38.64  ?  402  LYS A CB  1 
ATOM   2834  C  CG  . LYS A  1 371 ? 16.422  13.875  -16.155 1.00 44.80  ?  402  LYS A CG  1 
ATOM   2835  C  CD  . LYS A  1 371 ? 17.339  15.089  -16.200 1.00 47.40  ?  402  LYS A CD  1 
ATOM   2836  C  CE  . LYS A  1 371 ? 17.105  15.928  -17.440 1.00 53.52  ?  402  LYS A CE  1 
ATOM   2837  N  NZ  . LYS A  1 371 ? 18.171  16.962  -17.562 1.00 59.35  ?  402  LYS A NZ  1 
ATOM   2838  N  N   . ASP A  1 372 ? 15.561  10.534  -16.804 1.00 36.80  ?  403  ASP A N   1 
ATOM   2839  C  CA  . ASP A  1 372 ? 15.866  9.520   -17.811 1.00 41.17  ?  403  ASP A CA  1 
ATOM   2840  C  C   . ASP A  1 372 ? 16.089  8.136   -17.222 1.00 39.49  ?  403  ASP A C   1 
ATOM   2841  O  O   . ASP A  1 372 ? 16.770  7.315   -17.845 1.00 39.59  ?  403  ASP A O   1 
ATOM   2842  C  CB  . ASP A  1 372 ? 17.093  9.914   -18.645 1.00 46.47  ?  403  ASP A CB  1 
ATOM   2843  C  CG  . ASP A  1 372 ? 16.937  11.259  -19.285 1.00 45.16  ?  403  ASP A CG  1 
ATOM   2844  O  OD1 . ASP A  1 372 ? 15.902  11.478  -19.948 1.00 48.59  ?  403  ASP A OD1 1 
ATOM   2845  O  OD2 . ASP A  1 372 ? 17.827  12.107  -19.095 1.00 54.15  -1 403  ASP A OD2 1 
ATOM   2846  N  N   . GLU A  1 373 ? 15.560  7.846   -16.029 1.00 35.66  ?  404  GLU A N   1 
ATOM   2847  C  CA  . GLU A  1 373 ? 15.632  6.498   -15.482 1.00 36.45  ?  404  GLU A CA  1 
ATOM   2848  C  C   . GLU A  1 373 ? 14.244  5.995   -15.080 1.00 34.44  ?  404  GLU A C   1 
ATOM   2849  O  O   . GLU A  1 373 ? 13.304  6.775   -14.905 1.00 36.53  ?  404  GLU A O   1 
ATOM   2850  C  CB  . GLU A  1 373 ? 16.572  6.425   -14.280 1.00 35.92  ?  404  GLU A CB  1 
ATOM   2851  C  CG  . GLU A  1 373 ? 17.991  6.879   -14.574 1.00 37.47  ?  404  GLU A CG  1 
ATOM   2852  C  CD  . GLU A  1 373 ? 18.893  6.703   -13.366 1.00 44.70  ?  404  GLU A CD  1 
ATOM   2853  O  OE1 . GLU A  1 373 ? 18.841  5.623   -12.726 1.00 48.04  ?  404  GLU A OE1 1 
ATOM   2854  O  OE2 . GLU A  1 373 ? 19.624  7.655   -13.030 1.00 52.27  -1 404  GLU A OE2 1 
ATOM   2855  N  N   . MET A  1 374 ? 14.199  4.691   -14.874 1.00 31.98  ?  405  MET A N   1 
ATOM   2856  C  CA  . MET A  1 374 ? 12.894  4.041   -14.686 1.00 36.12  ?  405  MET A CA  1 
ATOM   2857  C  C   . MET A  1 374 ? 12.557  3.610   -13.270 1.00 33.17  ?  405  MET A C   1 
ATOM   2858  O  O   . MET A  1 374 ? 13.468  3.264   -12.510 1.00 31.46  ?  405  MET A O   1 
ATOM   2859  C  CB  . MET A  1 374 ? 12.909  2.715   -15.451 1.00 32.16  ?  405  MET A CB  1 
ATOM   2860  C  CG  . MET A  1 374 ? 12.872  2.841   -16.949 1.00 36.02  ?  405  MET A CG  1 
ATOM   2861  S  SD  . MET A  1 374 ? 11.194  3.108   -17.547 1.00 37.02  ?  405  MET A SD  1 
ATOM   2862  C  CE  . MET A  1 374 ? 11.133  1.878   -18.854 1.00 34.82  ?  405  MET A CE  1 
ATOM   2863  N  N   . ILE A  1 375 ? 11.289  3.724   -12.930 1.00 31.90  ?  406  ILE A N   1 
ATOM   2864  C  CA  . ILE A  1 375 ? 10.741  3.113   -11.729 1.00 28.31  ?  406  ILE A CA  1 
ATOM   2865  C  C   . ILE A  1 375 ? 9.743   2.061   -12.188 1.00 29.93  ?  406  ILE A C   1 
ATOM   2866  O  O   . ILE A  1 375 ? 8.904   2.331   -13.054 1.00 30.26  ?  406  ILE A O   1 
ATOM   2867  C  CB  . ILE A  1 375 ? 10.096  4.159   -10.803 1.00 30.49  ?  406  ILE A CB  1 
ATOM   2868  C  CG1 . ILE A  1 375 ? 11.183  5.089   -10.245 1.00 28.78  ?  406  ILE A CG1 1 
ATOM   2869  C  CG2 . ILE A  1 375 ? 9.341   3.496   -9.663  1.00 28.49  ?  406  ILE A CG2 1 
ATOM   2870  C  CD1 . ILE A  1 375 ? 10.618  6.195   -9.393  1.00 28.91  ?  406  ILE A CD1 1 
ATOM   2871  N  N   . TYR A  1 376 ? 9.853   0.861   -11.635 1.00 30.30  ?  407  TYR A N   1 
ATOM   2872  C  CA  . TYR A  1 376 ? 9.246   -0.334  -12.202 1.00 29.08  ?  407  TYR A CA  1 
ATOM   2873  C  C   . TYR A  1 376 ? 8.298   -0.991  -11.221 1.00 32.40  ?  407  TYR A C   1 
ATOM   2874  O  O   . TYR A  1 376 ? 8.480   -0.895  -10.000 1.00 28.99  ?  407  TYR A O   1 
ATOM   2875  C  CB  . TYR A  1 376 ? 10.278  -1.403  -12.524 1.00 31.18  ?  407  TYR A CB  1 
ATOM   2876  C  CG  . TYR A  1 376 ? 11.289  -1.101  -13.575 1.00 31.63  ?  407  TYR A CG  1 
ATOM   2877  C  CD1 . TYR A  1 376 ? 10.910  -1.004  -14.900 1.00 32.29  ?  407  TYR A CD1 1 
ATOM   2878  C  CD2 . TYR A  1 376 ? 12.646  -0.985  -13.253 1.00 37.13  ?  407  TYR A CD2 1 
ATOM   2879  C  CE1 . TYR A  1 376 ? 11.826  -0.772  -15.885 1.00 33.72  ?  407  TYR A CE1 1 
ATOM   2880  C  CE2 . TYR A  1 376 ? 13.585  -0.747  -14.246 1.00 38.93  ?  407  TYR A CE2 1 
ATOM   2881  C  CZ  . TYR A  1 376 ? 13.157  -0.653  -15.561 1.00 37.10  ?  407  TYR A CZ  1 
ATOM   2882  O  OH  . TYR A  1 376 ? 14.037  -0.413  -16.578 1.00 41.18  ?  407  TYR A OH  1 
ATOM   2883  N  N   . SER A  1 377 ? 7.320   -1.715  -11.778 1.00 28.34  ?  408  SER A N   1 
ATOM   2884  C  CA  . SER A  1 377 ? 6.675   -2.784  -11.040 1.00 25.95  ?  408  SER A CA  1 
ATOM   2885  C  C   . SER A  1 377 ? 6.400   -3.957  -11.968 1.00 26.10  ?  408  SER A C   1 
ATOM   2886  O  O   . SER A  1 377 ? 6.027   -3.781  -13.142 1.00 25.61  ?  408  SER A O   1 
ATOM   2887  C  CB  . SER A  1 377 ? 5.376   -2.300  -10.375 1.00 25.97  ?  408  SER A CB  1 
ATOM   2888  O  OG  . SER A  1 377 ? 4.758   -3.377  -9.681  1.00 26.59  ?  408  SER A OG  1 
ATOM   2889  N  N   . LEU A  1 378 ? 6.573   -5.160  -11.438 1.00 25.61  ?  409  LEU A N   1 
ATOM   2890  C  CA  . LEU A  1 378 ? 6.106   -6.350  -12.136 1.00 28.33  ?  409  LEU A CA  1 
ATOM   2891  C  C   . LEU A  1 378 ? 5.467   -7.259  -11.102 1.00 27.30  ?  409  LEU A C   1 
ATOM   2892  O  O   . LEU A  1 378 ? 6.090   -7.571  -10.089 1.00 27.24  ?  409  LEU A O   1 
ATOM   2893  C  CB  . LEU A  1 378 ? 7.254   -7.089  -12.852 1.00 29.46  ?  409  LEU A CB  1 
ATOM   2894  C  CG  . LEU A  1 378 ? 6.827   -8.284  -13.709 1.00 25.80  ?  409  LEU A CG  1 
ATOM   2895  C  CD1 . LEU A  1 378 ? 7.765   -8.463  -14.897 1.00 30.20  ?  409  LEU A CD1 1 
ATOM   2896  C  CD2 . LEU A  1 378 ? 6.764   -9.558  -12.877 1.00 28.20  ?  409  LEU A CD2 1 
ATOM   2897  N  N   . ARG A  1 379 ? 4.247   -7.702  -11.363 1.00 25.68  ?  410  ARG A N   1 
ATOM   2898  C  CA  . ARG A  1 379 ? 3.502   -8.481  -10.386 1.00 26.66  ?  410  ARG A CA  1 
ATOM   2899  C  C   . ARG A  1 379 ? 3.069   -9.784  -11.033 1.00 26.57  ?  410  ARG A C   1 
ATOM   2900  O  O   . ARG A  1 379 ? 2.409   -9.761  -12.077 1.00 28.56  ?  410  ARG A O   1 
ATOM   2901  C  CB  . ARG A  1 379 ? 2.290   -7.693  -9.872  1.00 25.35  ?  410  ARG A CB  1 
ATOM   2902  C  CG  . ARG A  1 379 ? 1.436   -8.436  -8.835  1.00 26.40  ?  410  ARG A CG  1 
ATOM   2903  C  CD  . ARG A  1 379 ? 0.216   -9.014  -9.498  1.00 25.40  ?  410  ARG A CD  1 
ATOM   2904  N  NE  . ARG A  1 379 ? -0.353  -10.129 -8.754  1.00 24.94  ?  410  ARG A NE  1 
ATOM   2905  C  CZ  . ARG A  1 379 ? -1.110  -9.971  -7.680  1.00 26.65  ?  410  ARG A CZ  1 
ATOM   2906  N  NH1 . ARG A  1 379 ? -1.401  -8.765  -7.220  1.00 22.42  ?  410  ARG A NH1 1 
ATOM   2907  N  NH2 . ARG A  1 379 ? -1.558  -11.046 -7.035  1.00 25.68  ?  410  ARG A NH2 1 
ATOM   2908  N  N   . TYR A  1 380 ? 3.415   -10.915 -10.405 1.00 25.78  ?  411  TYR A N   1 
ATOM   2909  C  CA  . TYR A  1 380 ? 3.091   -12.218 -10.984 1.00 27.70  ?  411  TYR A CA  1 
ATOM   2910  C  C   . TYR A  1 380 ? 1.609   -12.555 -10.833 1.00 26.88  ?  411  TYR A C   1 
ATOM   2911  O  O   . TYR A  1 380 ? 1.045   -12.454 -9.740  1.00 26.38  ?  411  TYR A O   1 
ATOM   2912  C  CB  . TYR A  1 380 ? 3.928   -13.313 -10.334 1.00 26.90  ?  411  TYR A CB  1 
ATOM   2913  C  CG  . TYR A  1 380 ? 5.413   -13.115 -10.514 1.00 26.09  ?  411  TYR A CG  1 
ATOM   2914  C  CD1 . TYR A  1 380 ? 6.006   -13.244 -11.762 1.00 28.18  ?  411  TYR A CD1 1 
ATOM   2915  C  CD2 . TYR A  1 380 ? 6.224   -12.793 -9.430  1.00 30.75  ?  411  TYR A CD2 1 
ATOM   2916  C  CE1 . TYR A  1 380 ? 7.396   -13.055 -11.938 1.00 29.67  ?  411  TYR A CE1 1 
ATOM   2917  C  CE2 . TYR A  1 380 ? 7.611   -12.609 -9.591  1.00 30.53  ?  411  TYR A CE2 1 
ATOM   2918  C  CZ  . TYR A  1 380 ? 8.182   -12.736 -10.844 1.00 31.87  ?  411  TYR A CZ  1 
ATOM   2919  O  OH  . TYR A  1 380 ? 9.554   -12.542 -10.976 1.00 34.23  ?  411  TYR A OH  1 
ATOM   2920  N  N   . ARG A  1 381 ? 0.989   -12.985 -11.931 1.00 28.51  ?  412  ARG A N   1 
ATOM   2921  C  CA  . ARG A  1 381 ? -0.398  -13.440 -11.935 1.00 25.97  ?  412  ARG A CA  1 
ATOM   2922  C  C   . ARG A  1 381 ? -0.420  -14.935 -12.221 1.00 26.70  ?  412  ARG A C   1 
ATOM   2923  O  O   . ARG A  1 381 ? 0.635   -15.586 -12.248 1.00 27.12  ?  412  ARG A O   1 
ATOM   2924  C  CB  . ARG A  1 381 ? -1.222  -12.623 -12.940 1.00 26.73  ?  412  ARG A CB  1 
ATOM   2925  C  CG  . ARG A  1 381 ? -1.337  -11.149 -12.525 1.00 28.32  ?  412  ARG A CG  1 
ATOM   2926  C  CD  . ARG A  1 381 ? -2.471  -10.976 -11.507 1.00 26.04  ?  412  ARG A CD  1 
ATOM   2927  N  NE  . ARG A  1 381 ? -2.664  -9.576  -11.162 1.00 26.46  ?  412  ARG A NE  1 
ATOM   2928  C  CZ  . ARG A  1 381 ? -3.445  -9.145  -10.183 1.00 28.48  ?  412  ARG A CZ  1 
ATOM   2929  N  NH1 . ARG A  1 381 ? -4.112  -9.985  -9.411  1.00 27.73  ?  412  ARG A NH1 1 
ATOM   2930  N  NH2 . ARG A  1 381 ? -3.560  -7.841  -9.977  1.00 23.63  ?  412  ARG A NH2 1 
ATOM   2931  N  N   . GLU A  1 382 ? -1.623  -15.487 -12.409 1.00 26.95  ?  413  GLU A N   1 
ATOM   2932  C  CA  . GLU A  1 382 ? -1.782  -16.924 -12.640 1.00 31.36  ?  413  GLU A CA  1 
ATOM   2933  C  C   . GLU A  1 382 ? -1.634  -17.202 -14.135 1.00 31.58  ?  413  GLU A C   1 
ATOM   2934  O  O   . GLU A  1 382 ? -2.602  -17.400 -14.869 1.00 30.89  ?  413  GLU A O   1 
ATOM   2935  C  CB  . GLU A  1 382 ? -3.119  -17.421 -12.107 1.00 28.72  ?  413  GLU A CB  1 
ATOM   2936  C  CG  . GLU A  1 382 ? -3.355  -17.208 -10.608 1.00 30.76  ?  413  GLU A CG  1 
ATOM   2937  C  CD  . GLU A  1 382 ? -2.093  -17.398 -9.771  1.00 34.05  ?  413  GLU A CD  1 
ATOM   2938  O  OE1 . GLU A  1 382 ? -1.575  -18.533 -9.762  1.00 32.14  ?  413  GLU A OE1 1 
ATOM   2939  O  OE2 . GLU A  1 382 ? -1.674  -16.428 -9.078  1.00 33.97  -1 413  GLU A OE2 1 
ATOM   2940  N  N   . GLY A  1 383 ? -0.383  -17.174 -14.598 1.00 32.17  ?  414  GLY A N   1 
ATOM   2941  C  CA  . GLY A  1 383 ? -0.063  -17.509 -15.972 1.00 29.66  ?  414  GLY A CA  1 
ATOM   2942  C  C   . GLY A  1 383 ? 0.471   -16.368 -16.810 1.00 33.90  ?  414  GLY A C   1 
ATOM   2943  O  O   . GLY A  1 383 ? 0.726   -16.569 -18.003 1.00 34.52  ?  414  GLY A O   1 
ATOM   2944  N  N   . TYR A  1 384 ? 0.607   -15.174 -16.248 1.00 27.43  ?  415  TYR A N   1 
ATOM   2945  C  CA  . TYR A  1 384 ? 1.052   -13.996 -16.990 1.00 26.55  ?  415  TYR A CA  1 
ATOM   2946  C  C   . TYR A  1 384 ? 1.512   -12.991 -15.943 1.00 24.34  ?  415  TYR A C   1 
ATOM   2947  O  O   . TYR A  1 384 ? 1.409   -13.241 -14.738 1.00 28.00  ?  415  TYR A O   1 
ATOM   2948  C  CB  . TYR A  1 384 ? -0.065  -13.430 -17.895 1.00 28.00  ?  415  TYR A CB  1 
ATOM   2949  C  CG  . TYR A  1 384 ? -1.214  -12.832 -17.100 1.00 26.71  ?  415  TYR A CG  1 
ATOM   2950  C  CD1 . TYR A  1 384 ? -2.254  -13.642 -16.632 1.00 26.09  ?  415  TYR A CD1 1 
ATOM   2951  C  CD2 . TYR A  1 384 ? -1.255  -11.462 -16.801 1.00 25.06  ?  415  TYR A CD2 1 
ATOM   2952  C  CE1 . TYR A  1 384 ? -3.304  -13.114 -15.880 1.00 25.17  ?  415  TYR A CE1 1 
ATOM   2953  C  CE2 . TYR A  1 384 ? -2.317  -10.916 -16.044 1.00 24.34  ?  415  TYR A CE2 1 
ATOM   2954  C  CZ  . TYR A  1 384 ? -3.326  -11.753 -15.584 1.00 25.66  ?  415  TYR A CZ  1 
ATOM   2955  O  OH  . TYR A  1 384 ? -4.359  -11.254 -14.815 1.00 24.35  ?  415  TYR A OH  1 
ATOM   2956  N  N   . ASN A  1 385 ? 2.032   -11.859 -16.406 1.00 28.16  ?  416  ASN A N   1 
ATOM   2957  C  CA  . ASN A  1 385 ? 2.576   -10.817 -15.549 1.00 26.34  ?  416  ASN A CA  1 
ATOM   2958  C  C   . ASN A  1 385 ? 1.877   -9.492  -15.812 1.00 23.90  ?  416  ASN A C   1 
ATOM   2959  O  O   . ASN A  1 385 ? 1.713   -9.098  -16.970 1.00 26.25  ?  416  ASN A O   1 
ATOM   2960  C  CB  . ASN A  1 385 ? 4.085   -10.648 -15.786 1.00 26.70  ?  416  ASN A CB  1 
ATOM   2961  C  CG  . ASN A  1 385 ? 4.854   -11.937 -15.556 1.00 31.20  ?  416  ASN A CG  1 
ATOM   2962  O  OD1 . ASN A  1 385 ? 4.681   -12.598 -14.520 1.00 29.97  ?  416  ASN A OD1 1 
ATOM   2963  N  ND2 . ASN A  1 385 ? 5.682   -12.322 -16.531 1.00 26.59  ?  416  ASN A ND2 1 
ATOM   2964  N  N   . ASP A  1 386 ? 1.482   -8.804  -14.731 1.00 25.22  ?  417  ASP A N   1 
ATOM   2965  C  CA  . ASP A  1 386 ? 1.167   -7.379  -14.795 1.00 26.58  ?  417  ASP A CA  1 
ATOM   2966  C  C   . ASP A  1 386 ? 2.463   -6.583  -14.663 1.00 25.81  ?  417  ASP A C   1 
ATOM   2967  O  O   . ASP A  1 386 ? 3.338   -6.949  -13.878 1.00 26.37  ?  417  ASP A O   1 
ATOM   2968  C  CB  . ASP A  1 386 ? 0.196   -6.974  -13.668 1.00 23.07  ?  417  ASP A CB  1 
ATOM   2969  C  CG  . ASP A  1 386 ? -1.196  -7.599  -13.820 1.00 28.60  ?  417  ASP A CG  1 
ATOM   2970  O  OD1 . ASP A  1 386 ? -1.563  -7.868  -14.970 1.00 25.17  ?  417  ASP A OD1 1 
ATOM   2971  O  OD2 . ASP A  1 386 ? -1.910  -7.813  -12.792 1.00 27.81  -1 417  ASP A OD2 1 
ATOM   2972  N  N   . VAL A  1 387 ? 2.571   -5.473  -15.403 1.00 27.61  ?  418  VAL A N   1 
ATOM   2973  C  CA  . VAL A  1 387 ? 3.795   -4.669  -15.453 1.00 26.43  ?  418  VAL A CA  1 
ATOM   2974  C  C   . VAL A  1 387 ? 3.436   -3.185  -15.414 1.00 25.95  ?  418  VAL A C   1 
ATOM   2975  O  O   . VAL A  1 387 ? 2.434   -2.764  -16.008 1.00 25.78  ?  418  VAL A O   1 
ATOM   2976  C  CB  . VAL A  1 387 ? 4.598   -4.957  -16.752 1.00 28.99  ?  418  VAL A CB  1 
ATOM   2977  C  CG1 . VAL A  1 387 ? 5.872   -4.142  -16.797 1.00 28.61  ?  418  VAL A CG1 1 
ATOM   2978  C  CG2 . VAL A  1 387 ? 4.900   -6.450  -16.914 1.00 23.10  ?  418  VAL A CG2 1 
ATOM   2979  N  N   . GLY A  1 388 ? 4.265   -2.390  -14.753 1.00 23.57  ?  419  GLY A N   1 
ATOM   2980  C  CA  . GLY A  1 388 ? 4.257   -0.944  -14.940 1.00 26.00  ?  419  GLY A CA  1 
ATOM   2981  C  C   . GLY A  1 388 ? 5.677   -0.404  -14.975 1.00 26.25  ?  419  GLY A C   1 
ATOM   2982  O  O   . GLY A  1 388 ? 6.565   -0.921  -14.306 1.00 27.34  ?  419  GLY A O   1 
ATOM   2983  N  N   . ALA A  1 389 ? 5.892   0.650   -15.763 1.00 25.45  ?  420  ALA A N   1 
ATOM   2984  C  CA  . ALA A  1 389 ? 7.226   1.243   -15.842 1.00 30.56  ?  420  ALA A CA  1 
ATOM   2985  C  C   . ALA A  1 389 ? 7.091   2.714   -16.191 1.00 31.78  ?  420  ALA A C   1 
ATOM   2986  O  O   . ALA A  1 389 ? 6.403   3.058   -17.159 1.00 28.85  ?  420  ALA A O   1 
ATOM   2987  C  CB  . ALA A  1 389 ? 8.091   0.527   -16.896 1.00 28.21  ?  420  ALA A CB  1 
ATOM   2988  N  N   . ARG A  1 390 ? 7.754   3.570   -15.424 1.00 25.78  ?  421  ARG A N   1 
ATOM   2989  C  CA  . ARG A  1 390 ? 7.643   5.012   -15.594 1.00 27.66  ?  421  ARG A CA  1 
ATOM   2990  C  C   . ARG A  1 390 ? 9.015   5.660   -15.781 1.00 30.27  ?  421  ARG A C   1 
ATOM   2991  O  O   . ARG A  1 390 ? 9.946   5.359   -15.041 1.00 27.29  ?  421  ARG A O   1 
ATOM   2992  C  CB  . ARG A  1 390 ? 6.971   5.650   -14.372 1.00 24.40  ?  421  ARG A CB  1 
ATOM   2993  C  CG  . ARG A  1 390 ? 6.733   7.130   -14.567 1.00 26.95  ?  421  ARG A CG  1 
ATOM   2994  C  CD  . ARG A  1 390 ? 6.116   7.812   -13.356 1.00 24.72  ?  421  ARG A CD  1 
ATOM   2995  N  NE  . ARG A  1 390 ? 6.212   9.248   -13.569 1.00 24.41  ?  421  ARG A NE  1 
ATOM   2996  C  CZ  . ARG A  1 390 ? 5.577   10.179  -12.874 1.00 25.85  ?  421  ARG A CZ  1 
ATOM   2997  N  NH1 . ARG A  1 390 ? 4.725   9.863   -11.899 1.00 24.13  ?  421  ARG A NH1 1 
ATOM   2998  N  NH2 . ARG A  1 390 ? 5.802   11.464  -13.165 1.00 27.02  ?  421  ARG A NH2 1 
ATOM   2999  N  N   . MET A  1 391 ? 9.105   6.588   -16.738 1.00 32.36  ?  422  MET A N   1 
ATOM   3000  C  CA  . MET A  1 391 ? 10.248  7.489   -16.939 1.00 31.65  ?  422  MET A CA  1 
ATOM   3001  C  C   . MET A  1 391 ? 9.721   8.889   -17.165 1.00 29.72  ?  422  MET A C   1 
ATOM   3002  O  O   . MET A  1 391 ? 9.028   9.128   -18.163 1.00 33.36  ?  422  MET A O   1 
ATOM   3003  C  CB  . MET A  1 391 ? 11.093  7.127   -18.168 1.00 33.82  ?  422  MET A CB  1 
ATOM   3004  C  CG  . MET A  1 391 ? 12.558  7.543   -18.079 1.00 36.28  ?  422  MET A CG  1 
ATOM   3005  S  SD  . MET A  1 391 ? 13.532  6.999   -19.506 1.00 43.09  ?  422  MET A SD  1 
ATOM   3006  C  CE  . MET A  1 391 ? 13.931  5.331   -19.031 1.00 38.89  ?  422  MET A CE  1 
ATOM   3007  N  N   . GLY A  1 392 ? 10.087  9.820   -16.296 1.00 28.47  ?  423  GLY A N   1 
ATOM   3008  C  CA  . GLY A  1 392 ? 9.640   11.188  -16.519 1.00 31.40  ?  423  GLY A CA  1 
ATOM   3009  C  C   . GLY A  1 392 ? 8.117   11.229  -16.526 1.00 29.82  ?  423  GLY A C   1 
ATOM   3010  O  O   . GLY A  1 392 ? 7.466   10.681  -15.627 1.00 30.02  ?  423  GLY A O   1 
ATOM   3011  N  N   . ASP A  1 393 ? 7.536   11.883  -17.540 1.00 28.48  ?  424  ASP A N   1 
ATOM   3012  C  CA  . ASP A  1 393 ? 6.079   11.991  -17.667 1.00 29.64  ?  424  ASP A CA  1 
ATOM   3013  C  C   . ASP A  1 393 ? 5.393   10.787  -18.293 1.00 28.97  ?  424  ASP A C   1 
ATOM   3014  O  O   . ASP A  1 393 ? 4.162   10.839  -18.470 1.00 28.53  ?  424  ASP A O   1 
ATOM   3015  C  CB  . ASP A  1 393 ? 5.681   13.218  -18.488 1.00 30.48  ?  424  ASP A CB  1 
ATOM   3016  C  CG  . ASP A  1 393 ? 6.086   14.516  -17.846 1.00 35.34  ?  424  ASP A CG  1 
ATOM   3017  O  OD1 . ASP A  1 393 ? 6.015   14.609  -16.606 1.00 37.12  ?  424  ASP A OD1 1 
ATOM   3018  O  OD2 . ASP A  1 393 ? 6.427   15.459  -18.578 1.00 38.10  -1 424  ASP A OD2 1 
ATOM   3019  N  N   . TRP A  1 394 ? 6.113   9.720   -18.637 1.00 26.05  ?  425  TRP A N   1 
ATOM   3020  C  CA  . TRP A  1 394 ? 5.552   8.661   -19.468 1.00 28.06  ?  425  TRP A CA  1 
ATOM   3021  C  C   . TRP A  1 394 ? 5.531   7.357   -18.697 1.00 28.25  ?  425  TRP A C   1 
ATOM   3022  O  O   . TRP A  1 394 ? 6.441   7.076   -17.927 1.00 24.96  ?  425  TRP A O   1 
ATOM   3023  C  CB  . TRP A  1 394 ? 6.360   8.491   -20.763 1.00 28.68  ?  425  TRP A CB  1 
ATOM   3024  C  CG  . TRP A  1 394 ? 6.176   9.668   -21.647 1.00 27.97  ?  425  TRP A CG  1 
ATOM   3025  C  CD1 . TRP A  1 394 ? 6.960   10.776  -21.696 1.00 30.32  ?  425  TRP A CD1 1 
ATOM   3026  C  CD2 . TRP A  1 394 ? 5.112   9.882   -22.580 1.00 31.03  ?  425  TRP A CD2 1 
ATOM   3027  N  NE1 . TRP A  1 394 ? 6.464   11.662  -22.609 1.00 32.96  ?  425  TRP A NE1 1 
ATOM   3028  C  CE2 . TRP A  1 394 ? 5.326   11.141  -23.169 1.00 30.82  ?  425  TRP A CE2 1 
ATOM   3029  C  CE3 . TRP A  1 394 ? 3.988   9.134   -22.964 1.00 28.09  ?  425  TRP A CE3 1 
ATOM   3030  C  CZ2 . TRP A  1 394 ? 4.477   11.667  -24.141 1.00 31.89  ?  425  TRP A CZ2 1 
ATOM   3031  C  CZ3 . TRP A  1 394 ? 3.148   9.647   -23.943 1.00 29.29  ?  425  TRP A CZ3 1 
ATOM   3032  C  CH2 . TRP A  1 394 ? 3.388   10.909  -24.510 1.00 31.75  ?  425  TRP A CH2 1 
ATOM   3033  N  N   . LYS A  1 395 ? 4.484   6.563   -18.890 1.00 27.70  ?  426  LYS A N   1 
ATOM   3034  C  CA  . LYS A  1 395 ? 4.412   5.272   -18.220 1.00 27.77  ?  426  LYS A CA  1 
ATOM   3035  C  C   . LYS A  1 395 ? 3.894   4.222   -19.180 1.00 27.81  ?  426  LYS A C   1 
ATOM   3036  O  O   . LYS A  1 395 ? 2.971   4.493   -19.945 1.00 28.09  ?  426  LYS A O   1 
ATOM   3037  C  CB  . LYS A  1 395 ? 3.479   5.309   -17.010 1.00 28.22  ?  426  LYS A CB  1 
ATOM   3038  C  CG  . LYS A  1 395 ? 3.506   4.016   -16.188 1.00 30.28  ?  426  LYS A CG  1 
ATOM   3039  C  CD  . LYS A  1 395 ? 2.177   3.769   -15.520 1.00 28.27  ?  426  LYS A CD  1 
ATOM   3040  C  CE  . LYS A  1 395 ? 2.198   2.427   -14.747 1.00 26.16  ?  426  LYS A CE  1 
ATOM   3041  N  NZ  . LYS A  1 395 ? 0.945   2.359   -13.916 1.00 24.63  ?  426  LYS A NZ  1 
ATOM   3042  N  N   . ILE A  1 396 ? 4.428   3.009   -19.096 1.00 28.37  ?  427  ILE A N   1 
ATOM   3043  C  CA  . ILE A  1 396 ? 3.837   1.870   -19.792 1.00 26.70  ?  427  ILE A CA  1 
ATOM   3044  C  C   . ILE A  1 396 ? 3.217   0.931   -18.768 1.00 27.84  ?  427  ILE A C   1 
ATOM   3045  O  O   . ILE A  1 396 ? 3.729   0.773   -17.650 1.00 27.77  ?  427  ILE A O   1 
ATOM   3046  C  CB  . ILE A  1 396 ? 4.847   1.136   -20.689 1.00 29.21  ?  427  ILE A CB  1 
ATOM   3047  C  CG1 . ILE A  1 396 ? 6.039   0.624   -19.872 1.00 26.71  ?  427  ILE A CG1 1 
ATOM   3048  C  CG2 . ILE A  1 396 ? 5.306   2.084   -21.814 1.00 28.27  ?  427  ILE A CG2 1 
ATOM   3049  C  CD1 . ILE A  1 396 ? 6.861   -0.428  -20.622 1.00 33.29  ?  427  ILE A CD1 1 
ATOM   3050  N  N   . THR A  1 397 ? 2.102   0.329   -19.154 1.00 25.18  ?  428  THR A N   1 
ATOM   3051  C  CA  . THR A  1 397 ? 1.299   -0.521  -18.286 1.00 27.64  ?  428  THR A CA  1 
ATOM   3052  C  C   . THR A  1 397 ? 0.823   -1.722  -19.075 1.00 23.63  ?  428  THR A C   1 
ATOM   3053  O  O   . THR A  1 397 ? 0.339   -1.571  -20.192 1.00 25.48  ?  428  THR A O   1 
ATOM   3054  C  CB  . THR A  1 397 ? 0.065   0.225   -17.738 1.00 25.63  ?  428  THR A CB  1 
ATOM   3055  O  OG1 . THR A  1 397 ? 0.466   1.509   -17.247 1.00 24.61  ?  428  THR A OG1 1 
ATOM   3056  C  CG2 . THR A  1 397 ? -0.590  -0.587  -16.592 1.00 25.34  ?  428  THR A CG2 1 
ATOM   3057  N  N   . ARG A  1 398 ? 0.928   -2.907  -18.487 1.00 28.56  ?  429  ARG A N   1 
ATOM   3058  C  CA  . ARG A  1 398 ? 0.212   -4.065  -18.995 1.00 25.79  ?  429  ARG A CA  1 
ATOM   3059  C  C   . ARG A  1 398 ? -0.558  -4.676  -17.828 1.00 24.41  ?  429  ARG A C   1 
ATOM   3060  O  O   . ARG A  1 398 ? 0.044   -5.024  -16.811 1.00 23.99  ?  429  ARG A O   1 
ATOM   3061  C  CB  . ARG A  1 398 ? 1.169   -5.093  -19.626 1.00 25.74  ?  429  ARG A CB  1 
ATOM   3062  C  CG  . ARG A  1 398 ? 0.389   -6.231  -20.284 1.00 28.89  ?  429  ARG A CG  1 
ATOM   3063  C  CD  . ARG A  1 398 ? 1.212   -7.042  -21.267 1.00 27.65  ?  429  ARG A CD  1 
ATOM   3064  N  NE  . ARG A  1 398 ? 0.342   -7.886  -22.089 1.00 29.42  ?  429  ARG A NE  1 
ATOM   3065  C  CZ  . ARG A  1 398 ? 0.750   -9.002  -22.680 1.00 30.90  ?  429  ARG A CZ  1 
ATOM   3066  N  NH1 . ARG A  1 398 ? 2.020   -9.393  -22.621 1.00 28.63  ?  429  ARG A NH1 1 
ATOM   3067  N  NH2 . ARG A  1 398 ? -0.125  -9.736  -23.354 1.00 24.92  ?  429  ARG A NH2 1 
ATOM   3068  N  N   . MET A  1 399 ? -1.889  -4.765  -17.963 1.00 23.64  ?  430  MET A N   1 
ATOM   3069  C  CA  . MET A  1 399 ? -2.773  -5.315  -16.942 1.00 28.51  ?  430  MET A CA  1 
ATOM   3070  C  C   . MET A  1 399 ? -3.650  -6.405  -17.542 1.00 25.50  ?  430  MET A C   1 
ATOM   3071  O  O   . MET A  1 399 ? -4.166  -6.248  -18.648 1.00 25.28  ?  430  MET A O   1 
ATOM   3072  C  CB  . MET A  1 399 ? -3.681  -4.208  -16.317 1.00 23.93  ?  430  MET A CB  1 
ATOM   3073  C  CG  . MET A  1 399 ? -2.993  -3.471  -15.141 1.00 25.36  ?  430  MET A CG  1 
ATOM   3074  S  SD  . MET A  1 399 ? -2.619  -4.586  -13.747 1.00 25.20  ?  430  MET A SD  1 
ATOM   3075  C  CE  . MET A  1 399 ? -4.267  -5.119  -13.273 1.00 22.92  ?  430  MET A CE  1 
ATOM   3076  N  N   . GLY A  1 400 ? -3.819  -7.508  -16.815 1.00 26.57  ?  431  GLY A N   1 
ATOM   3077  C  CA  . GLY A  1 400 ? -4.655  -8.600  -17.295 1.00 20.03  ?  431  GLY A CA  1 
ATOM   3078  C  C   . GLY A  1 400 ? -4.191  -9.281  -18.576 1.00 25.11  ?  431  GLY A C   1 
ATOM   3079  O  O   . GLY A  1 400 ? -4.999  -9.959  -19.238 1.00 26.30  ?  431  GLY A O   1 
ATOM   3080  N  N   . ASN A  1 401 ? -2.924  -9.107  -18.955 1.00 25.30  ?  432  ASN A N   1 
ATOM   3081  C  CA  . ASN A  1 401 ? -2.351  -9.606  -20.212 1.00 28.79  ?  432  ASN A CA  1 
ATOM   3082  C  C   . ASN A  1 401 ? -2.998  -8.971  -21.449 1.00 29.72  ?  432  ASN A C   1 
ATOM   3083  O  O   . ASN A  1 401 ? -2.873  -9.497  -22.565 1.00 26.30  ?  432  ASN A O   1 
ATOM   3084  C  CB  . ASN A  1 401 ? -2.414  -11.142 -20.305 1.00 23.24  ?  432  ASN A CB  1 
ATOM   3085  C  CG  . ASN A  1 401 ? -1.089  -11.737 -20.789 1.00 24.98  ?  432  ASN A CG  1 
ATOM   3086  O  OD1 . ASN A  1 401 ? -0.035  -11.187 -20.497 1.00 26.65  ?  432  ASN A OD1 1 
ATOM   3087  N  ND2 . ASN A  1 401 ? -1.141  -12.852 -21.505 1.00 27.11  ?  432  ASN A ND2 1 
ATOM   3088  N  N   . GLU A  1 402 ? -3.648  -7.819  -21.274 1.00 23.42  ?  433  GLU A N   1 
ATOM   3089  C  CA  . GLU A  1 402 ? -4.203  -7.058  -22.382 1.00 25.43  ?  433  GLU A CA  1 
ATOM   3090  C  C   . GLU A  1 402 ? -3.088  -6.406  -23.196 1.00 25.12  ?  433  GLU A C   1 
ATOM   3091  O  O   . GLU A  1 402 ? -1.923  -6.457  -22.811 1.00 25.83  ?  433  GLU A O   1 
ATOM   3092  C  CB  . GLU A  1 402 ? -5.170  -6.010  -21.833 1.00 24.61  ?  433  GLU A CB  1 
ATOM   3093  C  CG  . GLU A  1 402 ? -6.472  -6.660  -21.393 1.00 24.35  ?  433  GLU A CG  1 
ATOM   3094  C  CD  . GLU A  1 402 ? -7.262  -7.124  -22.586 1.00 27.29  ?  433  GLU A CD  1 
ATOM   3095  O  OE1 . GLU A  1 402 ? -7.682  -6.251  -23.355 1.00 27.38  ?  433  GLU A OE1 1 
ATOM   3096  O  OE2 . GLU A  1 402 ? -7.452  -8.346  -22.767 1.00 29.18  -1 433  GLU A OE2 1 
ATOM   3097  N  N   . PRO A  1 403 ? -3.419  -5.789  -24.333 1.00 25.69  ?  434  PRO A N   1 
ATOM   3098  C  CA  . PRO A  1 403 ? -2.401  -5.039  -25.089 1.00 27.31  ?  434  PRO A CA  1 
ATOM   3099  C  C   . PRO A  1 403 ? -1.739  -3.960  -24.246 1.00 29.89  ?  434  PRO A C   1 
ATOM   3100  O  O   . PRO A  1 403 ? -2.359  -3.378  -23.349 1.00 27.06  ?  434  PRO A O   1 
ATOM   3101  C  CB  . PRO A  1 403 ? -3.207  -4.423  -26.242 1.00 26.46  ?  434  PRO A CB  1 
ATOM   3102  C  CG  . PRO A  1 403 ? -4.289  -5.440  -26.474 1.00 24.98  ?  434  PRO A CG  1 
ATOM   3103  C  CD  . PRO A  1 403 ? -4.678  -5.908  -25.112 1.00 25.38  ?  434  PRO A CD  1 
ATOM   3104  N  N   . TRP A  1 404 ? -0.461  -3.699  -24.558 1.00 27.51  ?  435  TRP A N   1 
ATOM   3105  C  CA  . TRP A  1 404 ? 0.326   -2.690  -23.860 1.00 26.80  ?  435  TRP A CA  1 
ATOM   3106  C  C   . TRP A  1 404 ? -0.311  -1.310  -23.972 1.00 27.37  ?  435  TRP A C   1 
ATOM   3107  O  O   . TRP A  1 404 ? -0.955  -0.964  -24.973 1.00 30.03  ?  435  TRP A O   1 
ATOM   3108  C  CB  . TRP A  1 404 ? 1.753   -2.637  -24.419 1.00 27.42  ?  435  TRP A CB  1 
ATOM   3109  C  CG  . TRP A  1 404 ? 2.606   -3.681  -23.817 1.00 27.47  ?  435  TRP A CG  1 
ATOM   3110  C  CD1 . TRP A  1 404 ? 2.855   -4.927  -24.321 1.00 26.47  ?  435  TRP A CD1 1 
ATOM   3111  C  CD2 . TRP A  1 404 ? 3.302   -3.602  -22.568 1.00 31.55  ?  435  TRP A CD2 1 
ATOM   3112  N  NE1 . TRP A  1 404 ? 3.681   -5.623  -23.470 1.00 26.50  ?  435  TRP A NE1 1 
ATOM   3113  C  CE2 . TRP A  1 404 ? 3.979   -4.828  -22.392 1.00 28.14  ?  435  TRP A CE2 1 
ATOM   3114  C  CE3 . TRP A  1 404 ? 3.428   -2.609  -21.583 1.00 27.06  ?  435  TRP A CE3 1 
ATOM   3115  C  CZ2 . TRP A  1 404 ? 4.752   -5.096  -21.263 1.00 29.83  ?  435  TRP A CZ2 1 
ATOM   3116  C  CZ3 . TRP A  1 404 ? 4.214   -2.870  -20.476 1.00 28.90  ?  435  TRP A CZ3 1 
ATOM   3117  C  CH2 . TRP A  1 404 ? 4.869   -4.102  -20.328 1.00 27.54  ?  435  TRP A CH2 1 
ATOM   3118  N  N   . ARG A  1 405 ? -0.150  -0.529  -22.908 1.00 27.77  ?  436  ARG A N   1 
ATOM   3119  C  CA  . ARG A  1 405 ? -0.628  0.843   -22.871 1.00 27.80  ?  436  ARG A CA  1 
ATOM   3120  C  C   . ARG A  1 405 ? 0.539   1.781   -22.641 1.00 24.93  ?  436  ARG A C   1 
ATOM   3121  O  O   . ARG A  1 405 ? 1.485   1.460   -21.911 1.00 28.74  ?  436  ARG A O   1 
ATOM   3122  C  CB  . ARG A  1 405 ? -1.695  1.034   -21.773 1.00 28.81  ?  436  ARG A CB  1 
ATOM   3123  C  CG  . ARG A  1 405 ? -2.818  0.018   -21.871 1.00 26.72  ?  436  ARG A CG  1 
ATOM   3124  C  CD  . ARG A  1 405 ? -3.737  0.049   -20.648 1.00 30.42  ?  436  ARG A CD  1 
ATOM   3125  N  NE  . ARG A  1 405 ? -4.475  1.301   -20.545 1.00 25.74  ?  436  ARG A NE  1 
ATOM   3126  C  CZ  . ARG A  1 405 ? -5.648  1.491   -21.129 1.00 29.35  ?  436  ARG A CZ  1 
ATOM   3127  N  NH1 . ARG A  1 405 ? -6.148  0.591   -21.954 1.00 29.48  ?  436  ARG A NH1 1 
ATOM   3128  N  NH2 . ARG A  1 405 ? -6.316  2.620   -20.902 1.00 22.50  ?  436  ARG A NH2 1 
ATOM   3129  N  N   . LEU A  1 406 ? 0.465   2.943   -23.267 1.00 26.80  ?  437  LEU A N   1 
ATOM   3130  C  CA  . LEU A  1 406 ? 1.413   4.021   -23.048 1.00 28.06  ?  437  LEU A CA  1 
ATOM   3131  C  C   . LEU A  1 406 ? 0.601   5.217   -22.590 1.00 26.78  ?  437  LEU A C   1 
ATOM   3132  O  O   . LEU A  1 406 ? -0.366  5.592   -23.258 1.00 25.66  ?  437  LEU A O   1 
ATOM   3133  C  CB  . LEU A  1 406 ? 2.202   4.352   -24.337 1.00 28.32  ?  437  LEU A CB  1 
ATOM   3134  C  CG  . LEU A  1 406 ? 3.081   5.618   -24.252 1.00 27.42  ?  437  LEU A CG  1 
ATOM   3135  C  CD1 . LEU A  1 406 ? 4.307   5.329   -23.383 1.00 31.42  ?  437  LEU A CD1 1 
ATOM   3136  C  CD2 . LEU A  1 406 ? 3.518   6.116   -25.636 1.00 29.80  ?  437  LEU A CD2 1 
ATOM   3137  N  N   . HIS A  1 407 ? 0.973   5.806   -21.454 1.00 25.66  ?  438  HIS A N   1 
ATOM   3138  C  CA  . HIS A  1 407 ? 0.239   6.952   -20.942 1.00 23.56  ?  438  HIS A CA  1 
ATOM   3139  C  C   . HIS A  1 407 ? 1.190   8.098   -20.678 1.00 26.61  ?  438  HIS A C   1 
ATOM   3140  O  O   . HIS A  1 407 ? 2.302   7.882   -20.195 1.00 29.83  ?  438  HIS A O   1 
ATOM   3141  C  CB  . HIS A  1 407 ? -0.517  6.594   -19.645 1.00 23.28  ?  438  HIS A CB  1 
ATOM   3142  C  CG  . HIS A  1 407 ? -1.574  5.553   -19.847 1.00 26.34  ?  438  HIS A CG  1 
ATOM   3143  N  ND1 . HIS A  1 407 ? -2.721  5.795   -20.570 1.00 26.76  ?  438  HIS A ND1 1 
ATOM   3144  C  CD2 . HIS A  1 407 ? -1.644  4.262   -19.447 1.00 23.19  ?  438  HIS A CD2 1 
ATOM   3145  C  CE1 . HIS A  1 407 ? -3.464  4.701   -20.591 1.00 23.86  ?  438  HIS A CE1 1 
ATOM   3146  N  NE2 . HIS A  1 407 ? -2.828  3.757   -19.916 1.00 22.23  ?  438  HIS A NE2 1 
ATOM   3147  N  N   . ASN A  1 408 ? 0.740   9.315   -20.962 1.00 26.94  ?  439  ASN A N   1 
ATOM   3148  C  CA  . ASN A  1 408 ? 1.362   10.488  -20.349 1.00 29.71  ?  439  ASN A CA  1 
ATOM   3149  C  C   . ASN A  1 408 ? 0.774   10.606  -18.948 1.00 29.11  ?  439  ASN A C   1 
ATOM   3150  O  O   . ASN A  1 408 ? -0.323  11.141  -18.767 1.00 27.42  ?  439  ASN A O   1 
ATOM   3151  C  CB  . ASN A  1 408 ? 1.119   11.750  -21.175 1.00 28.53  ?  439  ASN A CB  1 
ATOM   3152  C  CG  . ASN A  1 408 ? 1.851   12.957  -20.605 1.00 31.80  ?  439  ASN A CG  1 
ATOM   3153  O  OD1 . ASN A  1 408 ? 1.798   13.224  -19.409 1.00 26.96  ?  439  ASN A OD1 1 
ATOM   3154  N  ND2 . ASN A  1 408 ? 2.558   13.678  -21.461 1.00 32.44  ?  439  ASN A ND2 1 
ATOM   3155  N  N   . ILE A  1 409 ? 1.498   10.088  -17.949 1.00 25.33  ?  440  ILE A N   1 
ATOM   3156  C  CA  . ILE A  1 409 ? 0.927   9.955   -16.608 1.00 23.07  ?  440  ILE A CA  1 
ATOM   3157  C  C   . ILE A  1 409 ? 0.782   11.308  -15.938 1.00 26.84  ?  440  ILE A C   1 
ATOM   3158  O  O   . ILE A  1 409 ? -0.051  11.470  -15.039 1.00 29.04  ?  440  ILE A O   1 
ATOM   3159  C  CB  . ILE A  1 409 ? 1.773   8.967   -15.786 1.00 27.61  ?  440  ILE A CB  1 
ATOM   3160  C  CG1 . ILE A  1 409 ? 0.951   8.364   -14.633 1.00 28.86  ?  440  ILE A CG1 1 
ATOM   3161  C  CG2 . ILE A  1 409 ? 3.057   9.653   -15.282 1.00 24.14  ?  440  ILE A CG2 1 
ATOM   3162  C  CD1 . ILE A  1 409 ? -0.213  7.498   -15.114 1.00 24.69  ?  440  ILE A CD1 1 
ATOM   3163  N  N   . THR A  1 410 ? 1.528   12.315  -16.401 1.00 26.32  ?  441  THR A N   1 
ATOM   3164  C  CA  . THR A  1 410 ? 1.320   13.668  -15.902 1.00 26.47  ?  441  THR A CA  1 
ATOM   3165  C  C   . THR A  1 410 ? 0.011   14.253  -16.408 1.00 27.69  ?  441  THR A C   1 
ATOM   3166  O  O   . THR A  1 410 ? -0.729  14.881  -15.643 1.00 29.42  ?  441  THR A O   1 
ATOM   3167  C  CB  . THR A  1 410 ? 2.497   14.543  -16.309 1.00 28.24  ?  441  THR A CB  1 
ATOM   3168  O  OG1 . THR A  1 410 ? 3.666   14.000  -15.697 1.00 26.99  ?  441  THR A OG1 1 
ATOM   3169  C  CG2 . THR A  1 410 ? 2.278   15.963  -15.830 1.00 33.60  ?  441  THR A CG2 1 
ATOM   3170  N  N   . GLN A  1 411 ? -0.289  14.072  -17.703 1.00 30.18  ?  442  GLN A N   1 
ATOM   3171  C  CA  . GLN A  1 411 ? -1.535  14.569  -18.281 1.00 32.21  ?  442  GLN A CA  1 
ATOM   3172  C  C   . GLN A  1 411 ? -2.726  13.659  -18.033 1.00 29.03  ?  442  GLN A C   1 
ATOM   3173  O  O   . GLN A  1 411 ? -3.866  14.130  -18.120 1.00 27.95  ?  442  GLN A O   1 
ATOM   3174  C  CB  . GLN A  1 411 ? -1.392  14.748  -19.798 1.00 33.08  ?  442  GLN A CB  1 
ATOM   3175  C  CG  . GLN A  1 411 ? -0.518  15.925  -20.202 1.00 39.67  ?  442  GLN A CG  1 
ATOM   3176  C  CD  . GLN A  1 411 ? -1.181  17.249  -19.875 1.00 51.43  ?  442  GLN A CD  1 
ATOM   3177  O  OE1 . GLN A  1 411 ? -0.918  17.840  -18.826 1.00 58.13  ?  442  GLN A OE1 1 
ATOM   3178  N  NE2 . GLN A  1 411 ? -2.063  17.715  -20.765 1.00 60.83  ?  442  GLN A NE2 1 
ATOM   3179  N  N   . ASP A  1 412 ? -2.490  12.365  -17.798 1.00 27.85  ?  443  ASP A N   1 
ATOM   3180  C  CA  . ASP A  1 412 ? -3.535  11.334  -17.777 1.00 29.88  ?  443  ASP A CA  1 
ATOM   3181  C  C   . ASP A  1 412 ? -3.288  10.426  -16.563 1.00 25.35  ?  443  ASP A C   1 
ATOM   3182  O  O   . ASP A  1 412 ? -2.965  9.243   -16.675 1.00 22.39  ?  443  ASP A O   1 
ATOM   3183  C  CB  . ASP A  1 412 ? -3.520  10.609  -19.124 1.00 29.60  ?  443  ASP A CB  1 
ATOM   3184  C  CG  . ASP A  1 412 ? -4.496  9.430   -19.221 1.00 28.22  ?  443  ASP A CG  1 
ATOM   3185  O  OD1 . ASP A  1 412 ? -5.545  9.414   -18.549 1.00 27.53  ?  443  ASP A OD1 1 
ATOM   3186  O  OD2 . ASP A  1 412 ? -4.196  8.501   -20.015 1.00 25.49  -1 443  ASP A OD2 1 
ATOM   3187  N  N   . ILE A  1 413 ? -3.418  11.012  -15.364 1.00 25.70  ?  444  ILE A N   1 
ATOM   3188  C  CA  . ILE A  1 413 ? -3.036  10.306  -14.130 1.00 25.52  ?  444  ILE A CA  1 
ATOM   3189  C  C   . ILE A  1 413 ? -3.902  9.062   -13.962 1.00 26.52  ?  444  ILE A C   1 
ATOM   3190  O  O   . ILE A  1 413 ? -3.465  8.058   -13.381 1.00 24.97  ?  444  ILE A O   1 
ATOM   3191  C  CB  . ILE A  1 413 ? -3.123  11.253  -12.898 1.00 21.76  ?  444  ILE A CB  1 
ATOM   3192  C  CG1 . ILE A  1 413 ? -2.407  10.656  -11.681 1.00 27.32  ?  444  ILE A CG1 1 
ATOM   3193  C  CG2 . ILE A  1 413 ? -4.595  11.621  -12.542 1.00 23.62  ?  444  ILE A CG2 1 
ATOM   3194  C  CD1 . ILE A  1 413 ? -2.260  11.641  -10.500 1.00 26.49  ?  444  ILE A CD1 1 
ATOM   3195  N  N   . GLY A  1 414 ? -5.121  9.087   -14.515 1.00 23.92  ?  445  GLY A N   1 
ATOM   3196  C  CA  . GLY A  1 414 ? -6.042  7.969   -14.413 1.00 25.83  ?  445  GLY A CA  1 
ATOM   3197  C  C   . GLY A  1 414 ? -5.823  6.855   -15.408 1.00 25.44  ?  445  GLY A C   1 
ATOM   3198  O  O   . GLY A  1 414 ? -6.607  5.896   -15.428 1.00 22.57  ?  445  GLY A O   1 
ATOM   3199  N  N   . GLU A  1 415 ? -4.798  6.975   -16.260 1.00 22.49  ?  446  GLU A N   1 
ATOM   3200  C  CA  . GLU A  1 415 ? -4.454  5.947   -17.255 1.00 22.57  ?  446  GLU A CA  1 
ATOM   3201  C  C   . GLU A  1 415 ? -5.664  5.579   -18.126 1.00 19.13  ?  446  GLU A C   1 
ATOM   3202  O  O   . GLU A  1 415 ? -5.944  4.415   -18.406 1.00 19.91  ?  446  GLU A O   1 
ATOM   3203  C  CB  . GLU A  1 415 ? -3.857  4.716   -16.575 1.00 24.59  ?  446  GLU A CB  1 
ATOM   3204  C  CG  . GLU A  1 415 ? -2.477  4.983   -15.926 1.00 23.43  ?  446  GLU A CG  1 
ATOM   3205  C  CD  . GLU A  1 415 ? -1.997  3.844   -15.010 1.00 29.74  ?  446  GLU A CD  1 
ATOM   3206  O  OE1 . GLU A  1 415 ? -2.566  3.713   -13.897 1.00 25.64  ?  446  GLU A OE1 1 
ATOM   3207  O  OE2 . GLU A  1 415 ? -1.056  3.097   -15.394 1.00 27.40  -1 446  GLU A OE2 1 
ATOM   3208  N  N   . LYS A  1 416 ? -6.349  6.594   -18.598 1.00 18.76  ?  447  LYS A N   1 
ATOM   3209  C  CA  . LYS A  1 416 ? -7.533  6.380   -19.434 1.00 21.83  ?  447  LYS A CA  1 
ATOM   3210  C  C   . LYS A  1 416 ? -7.260  6.409   -20.936 1.00 23.01  ?  447  LYS A C   1 
ATOM   3211  O  O   . LYS A  1 416 ? -8.046  5.827   -21.691 1.00 25.52  ?  447  LYS A O   1 
ATOM   3212  C  CB  . LYS A  1 416 ? -8.598  7.432   -19.118 1.00 23.75  ?  447  LYS A CB  1 
ATOM   3213  C  CG  . LYS A  1 416 ? -9.065  7.415   -17.702 1.00 25.06  ?  447  LYS A CG  1 
ATOM   3214  C  CD  . LYS A  1 416 ? -9.971  8.602   -17.441 1.00 26.56  ?  447  LYS A CD  1 
ATOM   3215  C  CE  . LYS A  1 416 ? -10.799 8.387   -16.183 1.00 32.65  ?  447  LYS A CE  1 
ATOM   3216  N  NZ  . LYS A  1 416 ? -11.588 9.602   -15.834 1.00 41.51  ?  447  LYS A NZ  1 
ATOM   3217  N  N   . LYS A  1 417 ? -6.188  7.073   -21.392 1.00 22.01  ?  448  LYS A N   1 
ATOM   3218  C  CA  . LYS A  1 417 ? -6.000  7.374   -22.816 1.00 25.89  ?  448  LYS A CA  1 
ATOM   3219  C  C   . LYS A  1 417 ? -4.771  6.633   -23.322 1.00 27.80  ?  448  LYS A C   1 
ATOM   3220  O  O   . LYS A  1 417 ? -3.645  7.092   -23.117 1.00 24.79  ?  448  LYS A O   1 
ATOM   3221  C  CB  . LYS A  1 417 ? -5.854  8.876   -23.054 1.00 26.63  ?  448  LYS A CB  1 
ATOM   3222  C  CG  . LYS A  1 417 ? -6.967  9.714   -22.461 1.00 29.15  ?  448  LYS A CG  1 
ATOM   3223  C  CD  . LYS A  1 417 ? -8.341  9.253   -22.999 1.00 32.05  ?  448  LYS A CD  1 
ATOM   3224  C  CE  . LYS A  1 417 ? -9.452  9.714   -22.081 1.00 32.25  ?  448  LYS A CE  1 
ATOM   3225  N  NZ  . LYS A  1 417 ? -10.744 9.633   -22.749 1.00 38.94  ?  448  LYS A NZ  1 
ATOM   3226  N  N   . ASN A  1 418 ? -4.973  5.504   -23.992 1.00 23.79  ?  449  ASN A N   1 
ATOM   3227  C  CA  . ASN A  1 418 ? -3.833  4.694   -24.408 1.00 28.64  ?  449  ASN A CA  1 
ATOM   3228  C  C   . ASN A  1 418 ? -3.188  5.356   -25.622 1.00 29.93  ?  449  ASN A C   1 
ATOM   3229  O  O   . ASN A  1 418 ? -3.843  5.533   -26.656 1.00 25.82  ?  449  ASN A O   1 
ATOM   3230  C  CB  . ASN A  1 418 ? -4.273  3.271   -24.734 1.00 29.79  ?  449  ASN A CB  1 
ATOM   3231  C  CG  . ASN A  1 418 ? -3.098  2.369   -25.072 1.00 30.44  ?  449  ASN A CG  1 
ATOM   3232  O  OD1 . ASN A  1 418 ? -1.955  2.809   -25.061 1.00 29.15  ?  449  ASN A OD1 1 
ATOM   3233  N  ND2 . ASN A  1 418 ? -3.379  1.125   -25.412 1.00 27.79  ?  449  ASN A ND2 1 
ATOM   3234  N  N   . LEU A  1 419 ? -1.923  5.748   -25.494 1.00 27.40  ?  450  LEU A N   1 
ATOM   3235  C  CA  . LEU A  1 419 ? -1.224  6.438   -26.569 1.00 29.05  ?  450  LEU A CA  1 
ATOM   3236  C  C   . LEU A  1 419 ? -0.255  5.525   -27.313 1.00 31.50  ?  450  LEU A C   1 
ATOM   3237  O  O   . LEU A  1 419 ? 0.572   6.013   -28.093 1.00 34.99  ?  450  LEU A O   1 
ATOM   3238  C  CB  . LEU A  1 419 ? -0.485  7.658   -26.022 1.00 29.55  ?  450  LEU A CB  1 
ATOM   3239  C  CG  . LEU A  1 419 ? -1.340  8.762   -25.395 1.00 29.41  ?  450  LEU A CG  1 
ATOM   3240  C  CD1 . LEU A  1 419 ? -0.487  9.925   -24.900 1.00 30.97  ?  450  LEU A CD1 1 
ATOM   3241  C  CD2 . LEU A  1 419 ? -2.438  9.232   -26.360 1.00 35.50  ?  450  LEU A CD2 1 
ATOM   3242  N  N   . ALA A  1 420 ? -0.359  4.212   -27.108 1.00 29.87  ?  451  ALA A N   1 
ATOM   3243  C  CA  . ALA A  1 420 ? 0.560   3.268   -27.733 1.00 31.19  ?  451  ALA A CA  1 
ATOM   3244  C  C   . ALA A  1 420 ? 0.533   3.354   -29.257 1.00 36.25  ?  451  ALA A C   1 
ATOM   3245  O  O   . ALA A  1 420 ? 1.553   3.113   -29.909 1.00 35.60  ?  451  ALA A O   1 
ATOM   3246  C  CB  . ALA A  1 420 ? 0.218   1.847   -27.286 1.00 28.22  ?  451  ALA A CB  1 
ATOM   3247  N  N   . GLY A  1 421 ? -0.612  3.681   -29.845 1.00 36.98  ?  452  GLY A N   1 
ATOM   3248  C  CA  . GLY A  1 421 ? -0.695  3.765   -31.291 1.00 34.48  ?  452  GLY A CA  1 
ATOM   3249  C  C   . GLY A  1 421 ? -0.093  5.045   -31.831 1.00 36.36  ?  452  GLY A C   1 
ATOM   3250  O  O   . GLY A  1 421 ? 0.467   5.069   -32.928 1.00 43.24  ?  452  GLY A O   1 
ATOM   3251  N  N   . ARG A  1 422 ? -0.206  6.122   -31.064 1.00 33.56  ?  453  ARG A N   1 
ATOM   3252  C  CA  . ARG A  1 422 ? 0.328   7.402   -31.508 1.00 37.70  ?  453  ARG A CA  1 
ATOM   3253  C  C   . ARG A  1 422 ? 1.848   7.444   -31.422 1.00 38.79  ?  453  ARG A C   1 
ATOM   3254  O  O   . ARG A  1 422 ? 2.499   8.047   -32.281 1.00 37.52  ?  453  ARG A O   1 
ATOM   3255  C  CB  . ARG A  1 422 ? -0.299  8.547   -30.702 1.00 37.27  ?  453  ARG A CB  1 
ATOM   3256  C  CG  . ARG A  1 422 ? -0.174  9.906   -31.387 1.00 45.61  ?  453  ARG A CG  1 
ATOM   3257  C  CD  . ARG A  1 422 ? -1.154  10.952  -30.872 1.00 54.61  ?  453  ARG A CD  1 
ATOM   3258  N  NE  . ARG A  1 422 ? -2.439  10.373  -30.499 1.00 61.88  ?  453  ARG A NE  1 
ATOM   3259  C  CZ  . ARG A  1 422 ? -3.324  10.953  -29.700 1.00 62.40  ?  453  ARG A CZ  1 
ATOM   3260  N  NH1 . ARG A  1 422 ? -3.064  12.106  -29.100 1.00 60.88  ?  453  ARG A NH1 1 
ATOM   3261  N  NH2 . ARG A  1 422 ? -4.498  10.358  -29.494 1.00 62.89  ?  453  ARG A NH2 1 
ATOM   3262  N  N   . TYR A  1 423 ? 2.433   6.820   -30.408 1.00 33.89  ?  454  TYR A N   1 
ATOM   3263  C  CA  . TYR A  1 423 ? 3.868   6.941   -30.130 1.00 34.24  ?  454  TYR A CA  1 
ATOM   3264  C  C   . TYR A  1 423 ? 4.506   5.572   -29.969 1.00 35.40  ?  454  TYR A C   1 
ATOM   3265  O  O   . TYR A  1 423 ? 5.047   5.245   -28.904 1.00 37.58  ?  454  TYR A O   1 
ATOM   3266  C  CB  . TYR A  1 423 ? 4.090   7.777   -28.879 1.00 32.67  ?  454  TYR A CB  1 
ATOM   3267  C  CG  . TYR A  1 423 ? 3.463   9.142   -28.941 1.00 40.20  ?  454  TYR A CG  1 
ATOM   3268  C  CD1 . TYR A  1 423 ? 3.810   10.038  -29.945 1.00 44.89  ?  454  TYR A CD1 1 
ATOM   3269  C  CD2 . TYR A  1 423 ? 2.518   9.541   -28.001 1.00 37.81  ?  454  TYR A CD2 1 
ATOM   3270  C  CE1 . TYR A  1 423 ? 3.249   11.300  -29.999 1.00 41.55  ?  454  TYR A CE1 1 
ATOM   3271  C  CE2 . TYR A  1 423 ? 1.954   10.798  -28.042 1.00 37.62  ?  454  TYR A CE2 1 
ATOM   3272  C  CZ  . TYR A  1 423 ? 2.320   11.675  -29.049 1.00 47.53  ?  454  TYR A CZ  1 
ATOM   3273  O  OH  . TYR A  1 423 ? 1.761   12.934  -29.117 1.00 49.28  ?  454  TYR A OH  1 
ATOM   3274  N  N   . PRO A  1 424 ? 4.470   4.741   -31.018 1.00 35.67  ?  455  PRO A N   1 
ATOM   3275  C  CA  . PRO A  1 424 ? 4.952   3.359   -30.867 1.00 35.34  ?  455  PRO A CA  1 
ATOM   3276  C  C   . PRO A  1 424 ? 6.440   3.262   -30.589 1.00 36.29  ?  455  PRO A C   1 
ATOM   3277  O  O   . PRO A  1 424 ? 6.872   2.291   -29.958 1.00 34.84  ?  455  PRO A O   1 
ATOM   3278  C  CB  . PRO A  1 424 ? 4.589   2.710   -32.214 1.00 38.30  ?  455  PRO A CB  1 
ATOM   3279  C  CG  . PRO A  1 424 ? 4.530   3.847   -33.176 1.00 42.15  ?  455  PRO A CG  1 
ATOM   3280  C  CD  . PRO A  1 424 ? 3.970   5.002   -32.383 1.00 39.86  ?  455  PRO A CD  1 
ATOM   3281  N  N   . ASP A  1 425 ? 7.245   4.214   -31.060 1.00 34.53  ?  456  ASP A N   1 
ATOM   3282  C  CA  . ASP A  1 425 ? 8.675   4.160   -30.756 1.00 39.08  ?  456  ASP A CA  1 
ATOM   3283  C  C   . ASP A  1 425 ? 8.927   4.333   -29.268 1.00 35.78  ?  456  ASP A C   1 
ATOM   3284  O  O   . ASP A  1 425 ? 9.765   3.631   -28.681 1.00 34.13  ?  456  ASP A O   1 
ATOM   3285  C  CB  . ASP A  1 425 ? 9.430   5.237   -31.530 1.00 39.37  ?  456  ASP A CB  1 
ATOM   3286  C  CG  . ASP A  1 425 ? 9.493   4.951   -33.020 1.00 49.05  ?  456  ASP A CG  1 
ATOM   3287  O  OD1 . ASP A  1 425 ? 9.024   3.876   -33.456 1.00 49.16  ?  456  ASP A OD1 1 
ATOM   3288  O  OD2 . ASP A  1 425 ? 9.995   5.825   -33.755 1.00 58.36  -1 456  ASP A OD2 1 
ATOM   3289  N  N   . ARG A  1 426 ? 8.252   5.300   -28.648 1.00 38.10  ?  457  ARG A N   1 
ATOM   3290  C  CA  . ARG A  1 426 ? 8.426   5.474   -27.212 1.00 33.71  ?  457  ARG A CA  1 
ATOM   3291  C  C   . ARG A  1 426 ? 7.974   4.237   -26.458 1.00 32.57  ?  457  ARG A C   1 
ATOM   3292  O  O   . ARG A  1 426 ? 8.629   3.810   -25.495 1.00 31.79  ?  457  ARG A O   1 
ATOM   3293  C  CB  . ARG A  1 426 ? 7.669   6.698   -26.706 1.00 35.74  ?  457  ARG A CB  1 
ATOM   3294  C  CG  . ARG A  1 426 ? 7.884   6.866   -25.196 1.00 36.22  ?  457  ARG A CG  1 
ATOM   3295  C  CD  . ARG A  1 426 ? 7.305   8.137   -24.630 1.00 36.09  ?  457  ARG A CD  1 
ATOM   3296  N  NE  . ARG A  1 426 ? 7.721   9.318   -25.372 1.00 38.28  ?  457  ARG A NE  1 
ATOM   3297  C  CZ  . ARG A  1 426 ? 8.688   10.134  -24.984 1.00 40.55  ?  457  ARG A CZ  1 
ATOM   3298  N  NH1 . ARG A  1 426 ? 9.465   9.844   -23.946 1.00 37.41  ?  457  ARG A NH1 1 
ATOM   3299  N  NH2 . ARG A  1 426 ? 8.889   11.263  -25.658 1.00 40.05  ?  457  ARG A NH2 1 
ATOM   3300  N  N   . LEU A  1 427 ? 6.857   3.642   -26.885 1.00 33.30  ?  458  LEU A N   1 
ATOM   3301  C  CA  . LEU A  1 427 ? 6.398   2.408   -26.260 1.00 35.40  ?  458  LEU A CA  1 
ATOM   3302  C  C   . LEU A  1 427 ? 7.486   1.346   -26.333 1.00 35.90  ?  458  LEU A C   1 
ATOM   3303  O  O   . LEU A  1 427 ? 7.923   0.806   -25.306 1.00 33.86  ?  458  LEU A O   1 
ATOM   3304  C  CB  . LEU A  1 427 ? 5.111   1.913   -26.928 1.00 26.86  ?  458  LEU A CB  1 
ATOM   3305  C  CG  . LEU A  1 427 ? 4.720   0.489   -26.507 1.00 31.87  ?  458  LEU A CG  1 
ATOM   3306  C  CD1 . LEU A  1 427 ? 4.320   0.457   -25.033 1.00 36.95  ?  458  LEU A CD1 1 
ATOM   3307  C  CD2 . LEU A  1 427 ? 3.591   -0.061  -27.361 1.00 38.32  ?  458  LEU A CD2 1 
ATOM   3308  N  N   . LYS A  1 428 ? 7.961   1.064   -27.549 1.00 34.87  ?  459  LYS A N   1 
ATOM   3309  C  CA  . LYS A  1 428 ? 8.943   -0.001  -27.733 1.00 38.84  ?  459  LYS A CA  1 
ATOM   3310  C  C   . LYS A  1 428 ? 10.237  0.304   -26.990 1.00 31.17  ?  459  LYS A C   1 
ATOM   3311  O  O   . LYS A  1 428 ? 10.850  -0.596  -26.408 1.00 37.53  ?  459  LYS A O   1 
ATOM   3312  C  CB  . LYS A  1 428 ? 9.207   -0.205  -29.220 1.00 37.84  ?  459  LYS A CB  1 
ATOM   3313  C  CG  . LYS A  1 428 ? 7.966   -0.595  -30.006 1.00 41.72  ?  459  LYS A CG  1 
ATOM   3314  C  CD  . LYS A  1 428 ? 7.811   -2.090  -30.144 1.00 45.97  ?  459  LYS A CD  1 
ATOM   3315  C  CE  . LYS A  1 428 ? 6.594   -2.410  -31.014 1.00 46.21  ?  459  LYS A CE  1 
ATOM   3316  N  NZ  . LYS A  1 428 ? 6.867   -2.488  -32.477 1.00 45.29  ?  459  LYS A NZ  1 
ATOM   3317  N  N   . GLU A  1 429 ? 10.667  1.567   -27.004 1.00 33.16  ?  460  GLU A N   1 
ATOM   3318  C  CA  . GLU A  1 429 ? 11.819  1.979   -26.209 1.00 34.43  ?  460  GLU A CA  1 
ATOM   3319  C  C   . GLU A  1 429 ? 11.648  1.574   -24.750 1.00 37.85  ?  460  GLU A C   1 
ATOM   3320  O  O   . GLU A  1 429 ? 12.548  0.980   -24.136 1.00 32.85  ?  460  GLU A O   1 
ATOM   3321  C  CB  . GLU A  1 429 ? 11.985  3.494   -26.271 1.00 39.78  ?  460  GLU A CB  1 
ATOM   3322  C  CG  . GLU A  1 429 ? 12.976  4.047   -27.255 1.00 44.63  ?  460  GLU A CG  1 
ATOM   3323  C  CD  . GLU A  1 429 ? 12.613  5.476   -27.649 1.00 53.55  ?  460  GLU A CD  1 
ATOM   3324  O  OE1 . GLU A  1 429 ? 12.041  6.204   -26.788 1.00 52.89  ?  460  GLU A OE1 1 
ATOM   3325  O  OE2 . GLU A  1 429 ? 12.873  5.869   -28.813 1.00 59.82  -1 460  GLU A OE2 1 
ATOM   3326  N  N   . MET A  1 430 ? 10.506  1.936   -24.153 1.00 32.58  ?  461  MET A N   1 
ATOM   3327  C  CA  . MET A  1 430 ? 10.340  1.638   -22.735 1.00 31.26  ?  461  MET A CA  1 
ATOM   3328  C  C   . MET A  1 430 ? 10.158  0.155   -22.474 1.00 32.88  ?  461  MET A C   1 
ATOM   3329  O  O   . MET A  1 430 ? 10.649  -0.343  -21.453 1.00 32.09  ?  461  MET A O   1 
ATOM   3330  C  CB  . MET A  1 430 ? 9.221   2.459   -22.105 1.00 28.12  ?  461  MET A CB  1 
ATOM   3331  C  CG  . MET A  1 430 ? 9.444   3.951   -22.212 1.00 33.94  ?  461  MET A CG  1 
ATOM   3332  S  SD  . MET A  1 430 ? 7.998   4.925   -21.732 1.00 31.74  ?  461  MET A SD  1 
ATOM   3333  C  CE  . MET A  1 430 ? 8.096   4.779   -19.962 1.00 24.70  ?  461  MET A CE  1 
ATOM   3334  N  N   . ILE A  1 431 ? 9.516   -0.567  -23.392 1.00 32.31  ?  462  ILE A N   1 
ATOM   3335  C  CA  . ILE A  1 431 ? 9.465   -2.027  -23.304 1.00 31.76  ?  462  ILE A CA  1 
ATOM   3336  C  C   . ILE A  1 431 ? 10.870  -2.616  -23.224 1.00 36.22  ?  462  ILE A C   1 
ATOM   3337  O  O   . ILE A  1 431 ? 11.158  -3.450  -22.359 1.00 31.86  ?  462  ILE A O   1 
ATOM   3338  C  CB  . ILE A  1 431 ? 8.705   -2.612  -24.505 1.00 34.85  ?  462  ILE A CB  1 
ATOM   3339  C  CG1 . ILE A  1 431 ? 7.283   -2.065  -24.573 1.00 39.84  ?  462  ILE A CG1 1 
ATOM   3340  C  CG2 . ILE A  1 431 ? 8.785   -4.150  -24.498 1.00 37.89  ?  462  ILE A CG2 1 
ATOM   3341  C  CD1 . ILE A  1 431 ? 6.305   -2.864  -23.811 1.00 42.30  ?  462  ILE A CD1 1 
ATOM   3342  N  N   . ALA A  1 432 ? 11.759  -2.201  -24.141 1.00 35.20  ?  463  ALA A N   1 
ATOM   3343  C  CA  . ALA A  1 432 ? 13.091  -2.809  -24.222 1.00 34.90  ?  463  ALA A CA  1 
ATOM   3344  C  C   . ALA A  1 432 ? 13.865  -2.637  -22.921 1.00 31.03  ?  463  ALA A C   1 
ATOM   3345  O  O   . ALA A  1 432 ? 14.522  -3.570  -22.451 1.00 35.23  ?  463  ALA A O   1 
ATOM   3346  C  CB  . ALA A  1 432 ? 13.871  -2.206  -25.392 1.00 30.42  ?  463  ALA A CB  1 
ATOM   3347  N  N   . LYS A  1 433 ? 13.805  -1.443  -22.332 1.00 32.02  ?  464  LYS A N   1 
ATOM   3348  C  CA  . LYS A  1 433 ? 14.475  -1.203  -21.066 1.00 33.16  ?  464  LYS A CA  1 
ATOM   3349  C  C   . LYS A  1 433 ? 13.877  -2.066  -19.965 1.00 35.48  ?  464  LYS A C   1 
ATOM   3350  O  O   . LYS A  1 433 ? 14.599  -2.607  -19.124 1.00 27.49  ?  464  LYS A O   1 
ATOM   3351  C  CB  . LYS A  1 433 ? 14.375  0.287   -20.721 1.00 38.55  ?  464  LYS A CB  1 
ATOM   3352  C  CG  . LYS A  1 433 ? 15.292  1.164   -21.564 1.00 45.83  ?  464  LYS A CG  1 
ATOM   3353  C  CD  . LYS A  1 433 ? 15.064  2.644   -21.327 1.00 54.97  ?  464  LYS A CD  1 
ATOM   3354  C  CE  . LYS A  1 433 ? 16.229  3.474   -21.868 1.00 59.45  ?  464  LYS A CE  1 
ATOM   3355  N  NZ  . LYS A  1 433 ? 15.944  4.945   -21.810 1.00 59.82  ?  464  LYS A NZ  1 
ATOM   3356  N  N   . THR A  1 434 ? 12.547  -2.210  -19.955 1.00 29.04  ?  465  THR A N   1 
ATOM   3357  C  CA  . THR A  1 434 ? 11.910  -3.011  -18.917 1.00 29.22  ?  465  THR A CA  1 
ATOM   3358  C  C   . THR A  1 434 ? 12.216  -4.490  -19.092 1.00 28.86  ?  465  THR A C   1 
ATOM   3359  O  O   . THR A  1 434 ? 12.444  -5.200  -18.110 1.00 28.18  ?  465  THR A O   1 
ATOM   3360  C  CB  . THR A  1 434 ? 10.391  -2.784  -18.923 1.00 30.62  ?  465  THR A CB  1 
ATOM   3361  O  OG1 . THR A  1 434 ? 10.133  -1.380  -18.836 1.00 28.77  ?  465  THR A OG1 1 
ATOM   3362  C  CG2 . THR A  1 434 ? 9.789   -3.444  -17.690 1.00 28.07  ?  465  THR A CG2 1 
ATOM   3363  N  N   . GLN A  1 435 ? 12.199  -4.988  -20.329 1.00 29.38  ?  466  GLN A N   1 
ATOM   3364  C  CA  . GLN A  1 435 ? 12.581  -6.381  -20.534 1.00 32.74  ?  466  GLN A CA  1 
ATOM   3365  C  C   . GLN A  1 435 ? 14.031  -6.630  -20.098 1.00 29.67  ?  466  GLN A C   1 
ATOM   3366  O  O   . GLN A  1 435 ? 14.353  -7.697  -19.561 1.00 29.95  ?  466  GLN A O   1 
ATOM   3367  C  CB  . GLN A  1 435 ? 12.405  -6.768  -21.991 1.00 32.16  ?  466  GLN A CB  1 
ATOM   3368  C  CG  . GLN A  1 435 ? 12.839  -8.189  -22.261 1.00 33.67  ?  466  GLN A CG  1 
ATOM   3369  C  CD  . GLN A  1 435 ? 12.296  -8.687  -23.559 1.00 37.74  ?  466  GLN A CD  1 
ATOM   3370  O  OE1 . GLN A  1 435 ? 12.011  -7.894  -24.438 1.00 38.57  ?  466  GLN A OE1 1 
ATOM   3371  N  NE2 . GLN A  1 435 ? 12.148  -10.004 -23.693 1.00 39.88  ?  466  GLN A NE2 1 
ATOM   3372  N  N   . GLU A  1 436 ? 14.914  -5.657  -20.309 1.00 32.09  ?  467  GLU A N   1 
ATOM   3373  C  CA  . GLU A  1 436 ? 16.303  -5.872  -19.905 1.00 34.89  ?  467  GLU A CA  1 
ATOM   3374  C  C   . GLU A  1 436 ? 16.389  -5.984  -18.388 1.00 36.45  ?  467  GLU A C   1 
ATOM   3375  O  O   . GLU A  1 436 ? 17.064  -6.870  -17.856 1.00 34.93  ?  467  GLU A O   1 
ATOM   3376  C  CB  . GLU A  1 436 ? 17.176  -4.735  -20.436 1.00 35.01  ?  467  GLU A CB  1 
ATOM   3377  C  CG  . GLU A  1 436 ? 18.679  -4.772  -20.087 1.00 40.40  ?  467  GLU A CG  1 
ATOM   3378  C  CD  . GLU A  1 436 ? 19.377  -6.022  -20.657 1.00 45.09  ?  467  GLU A CD  1 
ATOM   3379  O  OE1 . GLU A  1 436 ? 19.032  -6.424  -21.803 1.00 44.39  ?  467  GLU A OE1 1 
ATOM   3380  O  OE2 . GLU A  1 436 ? 20.191  -6.652  -19.941 1.00 48.32  -1 467  GLU A OE2 1 
ATOM   3381  N  N   . TRP A  1 437 ? 15.648  -5.129  -17.680 1.00 33.79  ?  468  TRP A N   1 
ATOM   3382  C  CA  . TRP A  1 437 ? 15.535  -5.224  -16.230 1.00 35.26  ?  468  TRP A CA  1 
ATOM   3383  C  C   . TRP A  1 437 ? 15.204  -6.643  -15.781 1.00 32.17  ?  468  TRP A C   1 
ATOM   3384  O  O   . TRP A  1 437 ? 15.840  -7.173  -14.864 1.00 32.01  ?  468  TRP A O   1 
ATOM   3385  C  CB  . TRP A  1 437 ? 14.474  -4.226  -15.741 1.00 32.96  ?  468  TRP A CB  1 
ATOM   3386  C  CG  . TRP A  1 437 ? 14.155  -4.269  -14.259 1.00 35.84  ?  468  TRP A CG  1 
ATOM   3387  C  CD1 . TRP A  1 437 ? 15.026  -4.102  -13.221 1.00 32.52  ?  468  TRP A CD1 1 
ATOM   3388  C  CD2 . TRP A  1 437 ? 12.854  -4.445  -13.671 1.00 30.85  ?  468  TRP A CD2 1 
ATOM   3389  N  NE1 . TRP A  1 437 ? 14.353  -4.186  -12.018 1.00 35.31  ?  468  TRP A NE1 1 
ATOM   3390  C  CE2 . TRP A  1 437 ? 13.017  -4.387  -12.269 1.00 32.85  ?  468  TRP A CE2 1 
ATOM   3391  C  CE3 . TRP A  1 437 ? 11.566  -4.640  -14.200 1.00 33.38  ?  468  TRP A CE3 1 
ATOM   3392  C  CZ2 . TRP A  1 437 ? 11.939  -4.535  -11.375 1.00 31.68  ?  468  TRP A CZ2 1 
ATOM   3393  C  CZ3 . TRP A  1 437 ? 10.492  -4.797  -13.313 1.00 32.24  ?  468  TRP A CZ3 1 
ATOM   3394  C  CH2 . TRP A  1 437 ? 10.684  -4.740  -11.919 1.00 31.20  ?  468  TRP A CH2 1 
ATOM   3395  N  N   . THR A  1 438 ? 14.233  -7.291  -16.433 1.00 31.01  ?  469  THR A N   1 
ATOM   3396  C  CA  . THR A  1 438 ? 13.812  -8.615  -15.967 1.00 30.42  ?  469  THR A CA  1 
ATOM   3397  C  C   . THR A  1 438 ? 14.870  -9.683  -16.197 1.00 33.76  ?  469  THR A C   1 
ATOM   3398  O  O   . THR A  1 438 ? 14.769  -10.768 -15.616 1.00 33.26  ?  469  THR A O   1 
ATOM   3399  C  CB  . THR A  1 438 ? 12.502  -9.068  -16.635 1.00 33.92  ?  469  THR A CB  1 
ATOM   3400  O  OG1 . THR A  1 438 ? 12.755  -9.492  -17.983 1.00 34.66  ?  469  THR A OG1 1 
ATOM   3401  C  CG2 . THR A  1 438 ? 11.434  -7.940  -16.615 1.00 29.93  ?  469  THR A CG2 1 
ATOM   3402  N  N   . LYS A  1 439 ? 15.886  -9.403  -17.010 1.00 35.77  ?  470  LYS A N   1 
ATOM   3403  C  CA  . LYS A  1 439 ? 16.929  -10.393 -17.220 1.00 34.33  ?  470  LYS A CA  1 
ATOM   3404  C  C   . LYS A  1 439 ? 17.815  -10.559 -15.983 1.00 33.98  ?  470  LYS A C   1 
ATOM   3405  O  O   . LYS A  1 439 ? 18.467  -11.599 -15.836 1.00 35.13  ?  470  LYS A O   1 
ATOM   3406  C  CB  . LYS A  1 439 ? 17.749  -10.016 -18.461 1.00 33.84  ?  470  LYS A CB  1 
ATOM   3407  C  CG  . LYS A  1 439 ? 16.929  -10.014 -19.758 1.00 35.40  ?  470  LYS A CG  1 
ATOM   3408  C  CD  . LYS A  1 439 ? 17.411  -11.104 -20.692 1.00 39.37  ?  470  LYS A CD  1 
ATOM   3409  C  CE  . LYS A  1 439 ? 16.872  -10.951 -22.127 1.00 51.91  ?  470  LYS A CE  1 
ATOM   3410  N  NZ  . LYS A  1 439 ? 16.957  -9.563  -22.664 1.00 48.07  ?  470  LYS A NZ  1 
ATOM   3411  N  N   . SER A  1 440 ? 17.816  -9.584  -15.072 1.00 33.91  ?  471  SER A N   1 
ATOM   3412  C  CA  . SER A  1 440 ? 18.552  -9.706  -13.819 1.00 30.80  ?  471  SER A CA  1 
ATOM   3413  C  C   . SER A  1 440 ? 17.783  -10.451 -12.734 1.00 36.58  ?  471  SER A C   1 
ATOM   3414  O  O   . SER A  1 440 ? 18.355  -10.698 -11.668 1.00 34.23  ?  471  SER A O   1 
ATOM   3415  C  CB  . SER A  1 440 ? 18.949  -8.321  -13.287 1.00 37.56  ?  471  SER A CB  1 
ATOM   3416  O  OG  . SER A  1 440 ? 17.809  -7.521  -12.966 1.00 40.14  ?  471  SER A OG  1 
ATOM   3417  N  N   . PHE A  1 441 ? 16.520  -10.824 -12.964 1.00 30.61  ?  472  PHE A N   1 
ATOM   3418  C  CA  . PHE A  1 441 ? 15.703  -11.368 -11.887 1.00 33.52  ?  472  PHE A CA  1 
ATOM   3419  C  C   . PHE A  1 441 ? 16.229  -12.722 -11.421 1.00 37.45  ?  472  PHE A C   1 
ATOM   3420  O  O   . PHE A  1 441 ? 16.962  -13.408 -12.133 1.00 39.37  ?  472  PHE A O   1 
ATOM   3421  C  CB  . PHE A  1 441 ? 14.245  -11.532 -12.331 1.00 30.21  ?  472  PHE A CB  1 
ATOM   3422  C  CG  . PHE A  1 441 ? 13.512  -10.229 -12.516 1.00 30.98  ?  472  PHE A CG  1 
ATOM   3423  C  CD1 . PHE A  1 441 ? 14.173  -9.018  -12.375 1.00 32.04  ?  472  PHE A CD1 1 
ATOM   3424  C  CD2 . PHE A  1 441 ? 12.147  -10.221 -12.816 1.00 33.83  ?  472  PHE A CD2 1 
ATOM   3425  C  CE1 . PHE A  1 441 ? 13.507  -7.819  -12.537 1.00 32.23  ?  472  PHE A CE1 1 
ATOM   3426  C  CE2 . PHE A  1 441 ? 11.468  -9.031  -12.974 1.00 29.32  ?  472  PHE A CE2 1 
ATOM   3427  C  CZ  . PHE A  1 441 ? 12.144  -7.821  -12.826 1.00 32.33  ?  472  PHE A CZ  1 
ATOM   3428  N  N   . VAL A  1 442 ? 15.822  -13.110 -10.213 1.00 33.00  ?  473  VAL A N   1 
ATOM   3429  C  CA  . VAL A  1 442 ? 16.057  -14.452 -9.694  1.00 35.67  ?  473  VAL A CA  1 
ATOM   3430  C  C   . VAL A  1 442 ? 14.737  -15.218 -9.659  1.00 41.98  ?  473  VAL A C   1 
ATOM   3431  O  O   . VAL A  1 442 ? 13.658  -14.671 -9.921  1.00 36.66  ?  473  VAL A O   1 
ATOM   3432  C  CB  . VAL A  1 442 ? 16.724  -14.430 -8.298  1.00 37.01  ?  473  VAL A CB  1 
ATOM   3433  C  CG1 . VAL A  1 442 ? 18.062  -13.728 -8.363  1.00 38.37  ?  473  VAL A CG1 1 
ATOM   3434  C  CG2 . VAL A  1 442 ? 15.808  -13.750 -7.273  1.00 31.42  ?  473  VAL A CG2 1 
ATOM   3435  N  N   . LYS A  1 443 ? 14.832  -16.522 -9.367  1.00 37.03  ?  474  LYS A N   1 
ATOM   3436  C  CA  . LYS A  1 443 ? 13.575  -17.222 -9.169  1.00 38.42  ?  474  LYS A CA  1 
ATOM   3437  C  C   . LYS A  1 443 ? 13.031  -16.953 -7.770  1.00 35.36  ?  474  LYS A C   1 
ATOM   3438  O  O   . LYS A  1 443 ? 13.794  -16.685 -6.849  1.00 36.84  ?  474  LYS A O   1 
ATOM   3439  C  CB  . LYS A  1 443 ? 13.724  -18.732 -9.373  1.00 42.88  ?  474  LYS A CB  1 
ATOM   3440  C  CG  . LYS A  1 443 ? 13.916  -19.156 -10.832 1.00 49.62  ?  474  LYS A CG  1 
ATOM   3441  C  CD  . LYS A  1 443 ? 13.225  -20.499 -11.092 1.00 58.67  ?  474  LYS A CD  1 
ATOM   3442  C  CE  . LYS A  1 443 ? 13.734  -21.201 -12.341 1.00 58.81  ?  474  LYS A CE  1 
ATOM   3443  N  NZ  . LYS A  1 443 ? 14.025  -22.645 -12.079 1.00 62.12  ?  474  LYS A NZ  1 
ATOM   3444  N  N   . PRO A  1 444 ? 11.709  -17.004 -7.597  1.00 38.33  ?  475  PRO A N   1 
ATOM   3445  C  CA  . PRO A  1 444 ? 11.137  -16.849 -6.258  1.00 32.37  ?  475  PRO A CA  1 
ATOM   3446  C  C   . PRO A  1 444 ? 11.581  -17.982 -5.354  1.00 36.17  ?  475  PRO A C   1 
ATOM   3447  O  O   . PRO A  1 444 ? 11.638  -19.138 -5.772  1.00 34.07  ?  475  PRO A O   1 
ATOM   3448  C  CB  . PRO A  1 444 ? 9.623   -16.904 -6.506  1.00 36.54  ?  475  PRO A CB  1 
ATOM   3449  C  CG  . PRO A  1 444 ? 9.467   -16.537 -7.972  1.00 37.83  ?  475  PRO A CG  1 
ATOM   3450  C  CD  . PRO A  1 444 ? 10.664  -17.177 -8.620  1.00 36.71  ?  475  PRO A CD  1 
ATOM   3451  N  N   . LEU A  1 445 ? 11.887  -17.636 -4.099  1.00 33.55  ?  476  LEU A N   1 
ATOM   3452  C  CA  . LEU A  1 445 ? 12.203  -18.653 -3.096  1.00 34.18  ?  476  LEU A CA  1 
ATOM   3453  C  C   . LEU A  1 445 ? 10.962  -19.420 -2.668  1.00 37.55  ?  476  LEU A C   1 
ATOM   3454  O  O   . LEU A  1 445 ? 11.057  -20.582 -2.261  1.00 36.54  ?  476  LEU A O   1 
ATOM   3455  C  CB  . LEU A  1 445 ? 12.856  -18.001 -1.883  1.00 32.21  ?  476  LEU A CB  1 
ATOM   3456  C  CG  . LEU A  1 445 ? 14.154  -17.267 -2.193  1.00 37.12  ?  476  LEU A CG  1 
ATOM   3457  C  CD1 . LEU A  1 445 ? 14.558  -16.454 -0.989  1.00 35.78  ?  476  LEU A CD1 1 
ATOM   3458  C  CD2 . LEU A  1 445 ? 15.221  -18.279 -2.562  1.00 40.15  ?  476  LEU A CD2 1 
ATOM   3459  N  N   . TRP A  1 446 ? 9.796   -18.777 -2.726  1.00 33.05  ?  477  TRP A N   1 
ATOM   3460  C  CA  . TRP A  1 446 ? 8.523   -19.434 -2.509  1.00 30.87  ?  477  TRP A CA  1 
ATOM   3461  C  C   . TRP A  1 446 ? 7.518   -18.749 -3.421  1.00 32.20  ?  477  TRP A C   1 
ATOM   3462  O  O   . TRP A  1 446 ? 7.714   -17.601 -3.833  1.00 33.05  ?  477  TRP A O   1 
ATOM   3463  C  CB  . TRP A  1 446 ? 8.069   -19.351 -1.046  1.00 30.90  ?  477  TRP A CB  1 
ATOM   3464  C  CG  . TRP A  1 446 ? 8.009   -17.926 -0.554  1.00 32.31  ?  477  TRP A CG  1 
ATOM   3465  C  CD1 . TRP A  1 446 ? 6.995   -17.033 -0.746  1.00 32.03  ?  477  TRP A CD1 1 
ATOM   3466  C  CD2 . TRP A  1 446 ? 9.030   -17.226 0.166   1.00 34.40  ?  477  TRP A CD2 1 
ATOM   3467  N  NE1 . TRP A  1 446 ? 7.312   -15.826 -0.170  1.00 32.13  ?  477  TRP A NE1 1 
ATOM   3468  C  CE2 . TRP A  1 446 ? 8.560   -15.916 0.389   1.00 35.06  ?  477  TRP A CE2 1 
ATOM   3469  C  CE3 . TRP A  1 446 ? 10.292  -17.583 0.651   1.00 34.52  ?  477  TRP A CE3 1 
ATOM   3470  C  CZ2 . TRP A  1 446 ? 9.309   -14.959 1.067   1.00 32.71  ?  477  TRP A CZ2 1 
ATOM   3471  C  CZ3 . TRP A  1 446 ? 11.035  -16.635 1.322   1.00 32.88  ?  477  TRP A CZ3 1 
ATOM   3472  C  CH2 . TRP A  1 446 ? 10.540  -15.336 1.534   1.00 35.99  ?  477  TRP A CH2 1 
ATOM   3473  N  N   . VAL A  1 447 ? 6.447   -19.469 -3.735  1.00 26.07  ?  478  VAL A N   1 
ATOM   3474  C  CA  . VAL A  1 447 ? 5.304   -18.892 -4.447  1.00 27.92  ?  478  VAL A CA  1 
ATOM   3475  C  C   . VAL A  1 447 ? 4.136   -18.903 -3.473  1.00 30.77  ?  478  VAL A C   1 
ATOM   3476  O  O   . VAL A  1 447 ? 4.323   -19.231 -2.298  1.00 31.63  ?  478  VAL A O   1 
ATOM   3477  C  CB  . VAL A  1 447 ? 4.994   -19.661 -5.746  1.00 29.14  ?  478  VAL A CB  1 
ATOM   3478  C  CG1 . VAL A  1 447 ? 6.192   -19.588 -6.701  1.00 34.63  ?  478  VAL A CG1 1 
ATOM   3479  C  CG2 . VAL A  1 447 ? 4.600   -21.111 -5.472  1.00 31.08  ?  478  VAL A CG2 1 
ATOM   3480  N  N   . TYR A  1 448 ? 2.928   -18.547 -3.924  1.00 27.95  ?  479  TYR A N   1 
ATOM   3481  C  CA  . TYR A  1 448 ? 1.818   -18.404 -2.991  1.00 25.90  ?  479  TYR A CA  1 
ATOM   3482  C  C   . TYR A  1 448 ? 0.807   -19.534 -3.070  1.00 32.05  ?  479  TYR A C   1 
ATOM   3483  O  O   . TYR A  1 448 ? 0.346   -20.026 -2.036  1.00 31.66  ?  479  TYR A O   1 
ATOM   3484  C  CB  . TYR A  1 448 ? 1.095   -17.062 -3.218  1.00 28.77  ?  479  TYR A CB  1 
ATOM   3485  C  CG  . TYR A  1 448 ? 0.180   -16.676 -2.078  1.00 31.07  ?  479  TYR A CG  1 
ATOM   3486  C  CD1 . TYR A  1 448 ? 0.698   -16.164 -0.894  1.00 27.33  ?  479  TYR A CD1 1 
ATOM   3487  C  CD2 . TYR A  1 448 ? -1.201  -16.832 -2.176  1.00 29.39  ?  479  TYR A CD2 1 
ATOM   3488  C  CE1 . TYR A  1 448 ? -0.133  -15.802 0.160   1.00 29.40  ?  479  TYR A CE1 1 
ATOM   3489  C  CE2 . TYR A  1 448 ? -2.044  -16.477 -1.115  1.00 30.62  ?  479  TYR A CE2 1 
ATOM   3490  C  CZ  . TYR A  1 448 ? -1.499  -15.963 0.043   1.00 33.43  ?  479  TYR A CZ  1 
ATOM   3491  O  OH  . TYR A  1 448 ? -2.309  -15.606 1.103   1.00 31.93  ?  479  TYR A OH  1 
ATOM   3492  N  N   . SER A  1 449 ? 0.401   -19.934 -4.269  1.00 31.52  ?  480  SER A N   1 
ATOM   3493  C  CA  . SER A  1 449 ? -0.603  -20.972 -4.410  1.00 29.99  ?  480  SER A CA  1 
ATOM   3494  C  C   . SER A  1 449 ? -0.004  -22.188 -5.104  1.00 29.50  ?  480  SER A C   1 
ATOM   3495  O  O   . SER A  1 449 ? 1.077   -22.127 -5.690  1.00 32.62  ?  480  SER A O   1 
ATOM   3496  C  CB  . SER A  1 449 ? -1.816  -20.476 -5.209  1.00 31.75  ?  480  SER A CB  1 
ATOM   3497  O  OG  . SER A  1 449 ? -1.428  -20.258 -6.551  1.00 31.05  ?  480  SER A OG  1 
ATOM   3498  N  N   . VAL A  1 450 ? -0.723  -23.302 -5.004  1.00 31.40  ?  481  VAL A N   1 
ATOM   3499  C  CA  . VAL A  1 450 ? -0.323  -24.519 -5.697  1.00 29.80  ?  481  VAL A CA  1 
ATOM   3500  C  C   . VAL A  1 450 ? -0.325  -24.275 -7.200  1.00 35.08  ?  481  VAL A C   1 
ATOM   3501  O  O   . VAL A  1 450 ? 0.586   -24.707 -7.918  1.00 32.10  ?  481  VAL A O   1 
ATOM   3502  C  CB  . VAL A  1 450 ? -1.263  -25.671 -5.286  1.00 36.68  ?  481  VAL A CB  1 
ATOM   3503  C  CG1 . VAL A  1 450 ? -1.104  -26.879 -6.197  1.00 37.12  ?  481  VAL A CG1 1 
ATOM   3504  C  CG2 . VAL A  1 450 ? -1.036  -26.037 -3.826  1.00 33.52  ?  481  VAL A CG2 1 
ATOM   3505  N  N   . LYS A  1 451 ? -1.338  -23.549 -7.695  1.00 32.09  ?  482  LYS A N   1 
ATOM   3506  C  CA  . LYS A  1 451 ? -1.343  -23.124 -9.091  1.00 33.29  ?  482  LYS A CA  1 
ATOM   3507  C  C   . LYS A  1 451 ? -0.021  -22.445 -9.453  1.00 34.19  ?  482  LYS A C   1 
ATOM   3508  O  O   . LYS A  1 451 ? 0.603   -22.779 -10.471 1.00 34.24  ?  482  LYS A O   1 
ATOM   3509  C  CB  . LYS A  1 451 ? -2.542  -22.192 -9.348  1.00 33.21  ?  482  LYS A CB  1 
ATOM   3510  C  CG  . LYS A  1 451 ? -2.689  -21.737 -10.772 1.00 34.78  ?  482  LYS A CG  1 
ATOM   3511  C  CD  . LYS A  1 451 ? -3.130  -22.890 -11.686 1.00 35.03  ?  482  LYS A CD  1 
ATOM   3512  C  CE  . LYS A  1 451 ? -3.158  -22.449 -13.133 1.00 37.02  ?  482  LYS A CE  1 
ATOM   3513  N  NZ  . LYS A  1 451 ? -3.782  -23.478 -14.015 1.00 39.07  ?  482  LYS A NZ  1 
ATOM   3514  N  N   . ASP A  1 452 ? 0.434   -21.501 -8.616  1.00 32.78  ?  483  ASP A N   1 
ATOM   3515  C  CA  . ASP A  1 452 ? 1.739   -20.869 -8.845  1.00 34.82  ?  483  ASP A CA  1 
ATOM   3516  C  C   . ASP A  1 452 ? 2.836   -21.912 -9.040  1.00 33.66  ?  483  ASP A C   1 
ATOM   3517  O  O   . ASP A  1 452 ? 3.631   -21.837 -9.986  1.00 35.18  ?  483  ASP A O   1 
ATOM   3518  C  CB  . ASP A  1 452 ? 2.125   -19.970 -7.673  1.00 32.19  ?  483  ASP A CB  1 
ATOM   3519  C  CG  . ASP A  1 452 ? 1.310   -18.690 -7.591  1.00 29.94  ?  483  ASP A CG  1 
ATOM   3520  O  OD1 . ASP A  1 452 ? 0.771   -18.210 -8.605  1.00 33.15  ?  483  ASP A OD1 1 
ATOM   3521  O  OD2 . ASP A  1 452 ? 1.230   -18.160 -6.478  1.00 30.85  -1 483  ASP A OD2 1 
ATOM   3522  N  N   . LYS A  1 453 ? 2.908   -22.877 -8.125  1.00 35.63  ?  484  LYS A N   1 
ATOM   3523  C  CA  . LYS A  1 453 ? 3.990   -23.851 -8.176  1.00 35.97  ?  484  LYS A CA  1 
ATOM   3524  C  C   . LYS A  1 453 ? 3.912   -24.685 -9.449  1.00 35.48  ?  484  LYS A C   1 
ATOM   3525  O  O   . LYS A  1 453 ? 4.932   -24.912 -10.102 1.00 37.20  ?  484  LYS A O   1 
ATOM   3526  C  CB  . LYS A  1 453 ? 3.958   -24.723 -6.919  1.00 36.51  ?  484  LYS A CB  1 
ATOM   3527  C  CG  . LYS A  1 453 ? 4.999   -25.854 -6.889  1.00 40.30  ?  484  LYS A CG  1 
ATOM   3528  C  CD  . LYS A  1 453 ? 4.350   -27.189 -6.544  1.00 47.31  ?  484  LYS A CD  1 
ATOM   3529  C  CE  . LYS A  1 453 ? 3.700   -27.863 -7.756  1.00 50.75  ?  484  LYS A CE  1 
ATOM   3530  N  NZ  . LYS A  1 453 ? 3.220   -29.248 -7.429  1.00 59.03  ?  484  LYS A NZ  1 
ATOM   3531  N  N   . GLU A  1 454 ? 2.703   -25.081 -9.864  1.00 36.08  ?  485  GLU A N   1 
ATOM   3532  C  CA  . GLU A  1 454 ? 2.563   -25.823 -11.119 1.00 35.48  ?  485  GLU A CA  1 
ATOM   3533  C  C   . GLU A  1 454 ? 3.059   -25.006 -12.306 1.00 38.81  ?  485  GLU A C   1 
ATOM   3534  O  O   . GLU A  1 454 ? 3.800   -25.515 -13.155 1.00 44.51  ?  485  GLU A O   1 
ATOM   3535  C  CB  . GLU A  1 454 ? 1.111   -26.250 -11.334 1.00 36.60  ?  485  GLU A CB  1 
ATOM   3536  C  CG  . GLU A  1 454 ? 0.591   -27.196 -10.279 1.00 36.79  ?  485  GLU A CG  1 
ATOM   3537  C  CD  . GLU A  1 454 ? -0.844  -27.614 -10.519 1.00 39.38  ?  485  GLU A CD  1 
ATOM   3538  O  OE1 . GLU A  1 454 ? -1.488  -27.081 -11.450 1.00 40.74  ?  485  GLU A OE1 1 
ATOM   3539  O  OE2 . GLU A  1 454 ? -1.340  -28.475 -9.766  1.00 46.56  -1 485  GLU A OE2 1 
ATOM   3540  N  N   . LEU A  1 455 ? 2.676   -23.728 -12.378 1.00 32.85  ?  486  LEU A N   1 
ATOM   3541  C  CA  . LEU A  1 455 ? 3.058   -22.920 -13.531 1.00 31.60  ?  486  LEU A CA  1 
ATOM   3542  C  C   . LEU A  1 455 ? 4.566   -22.708 -13.594 1.00 35.51  ?  486  LEU A C   1 
ATOM   3543  O  O   . LEU A  1 455 ? 5.167   -22.809 -14.672 1.00 37.24  ?  486  LEU A O   1 
ATOM   3544  C  CB  . LEU A  1 455 ? 2.331   -21.578 -13.497 1.00 36.89  ?  486  LEU A CB  1 
ATOM   3545  C  CG  . LEU A  1 455 ? 0.807   -21.615 -13.681 1.00 36.01  ?  486  LEU A CG  1 
ATOM   3546  C  CD1 . LEU A  1 455 ? 0.189   -20.229 -13.418 1.00 39.40  ?  486  LEU A CD1 1 
ATOM   3547  C  CD2 . LEU A  1 455 ? 0.420   -22.137 -15.058 1.00 37.55  ?  486  LEU A CD2 1 
ATOM   3548  N  N   . TRP A  1 456 ? 5.196   -22.395 -12.459 1.00 35.04  ?  487  TRP A N   1 
ATOM   3549  C  CA  . TRP A  1 456 ? 6.640   -22.179 -12.459 1.00 34.95  ?  487  TRP A CA  1 
ATOM   3550  C  C   . TRP A  1 456 ? 7.386   -23.473 -12.768 1.00 36.76  ?  487  TRP A C   1 
ATOM   3551  O  O   . TRP A  1 456 ? 8.396   -23.458 -13.481 1.00 39.08  ?  487  TRP A O   1 
ATOM   3552  C  CB  . TRP A  1 456 ? 7.082   -21.612 -11.113 1.00 32.00  ?  487  TRP A CB  1 
ATOM   3553  C  CG  . TRP A  1 456 ? 6.838   -20.130 -10.972 1.00 34.87  ?  487  TRP A CG  1 
ATOM   3554  C  CD1 . TRP A  1 456 ? 5.686   -19.520 -10.559 1.00 33.23  ?  487  TRP A CD1 1 
ATOM   3555  C  CD2 . TRP A  1 456 ? 7.779   -19.079 -11.219 1.00 34.23  ?  487  TRP A CD2 1 
ATOM   3556  N  NE1 . TRP A  1 456 ? 5.847   -18.153 -10.554 1.00 32.24  ?  487  TRP A NE1 1 
ATOM   3557  C  CE2 . TRP A  1 456 ? 7.125   -17.858 -10.946 1.00 31.10  ?  487  TRP A CE2 1 
ATOM   3558  C  CE3 . TRP A  1 456 ? 9.109   -19.053 -11.654 1.00 31.03  ?  487  TRP A CE3 1 
ATOM   3559  C  CZ2 . TRP A  1 456 ? 7.756   -16.628 -11.091 1.00 31.20  ?  487  TRP A CZ2 1 
ATOM   3560  C  CZ3 . TRP A  1 456 ? 9.739   -17.832 -11.799 1.00 31.74  ?  487  TRP A CZ3 1 
ATOM   3561  C  CH2 . TRP A  1 456 ? 9.065   -16.634 -11.516 1.00 35.61  ?  487  TRP A CH2 1 
ATOM   3562  N  N   . GLU A  1 457 ? 6.902   -24.595 -12.238 1.00 33.12  ?  488  GLU A N   1 
ATOM   3563  C  CA  . GLU A  1 457 ? 7.583   -25.872 -12.427 1.00 42.91  ?  488  GLU A CA  1 
ATOM   3564  C  C   . GLU A  1 457 ? 7.537   -26.327 -13.878 1.00 42.82  ?  488  GLU A C   1 
ATOM   3565  O  O   . GLU A  1 457 ? 8.462   -27.002 -14.344 1.00 40.99  ?  488  GLU A O   1 
ATOM   3566  C  CB  . GLU A  1 457 ? 6.950   -26.926 -11.513 1.00 39.27  ?  488  GLU A CB  1 
ATOM   3567  C  CG  . GLU A  1 457 ? 7.326   -26.738 -10.051 1.00 44.71  ?  488  GLU A CG  1 
ATOM   3568  C  CD  . GLU A  1 457 ? 7.120   -27.978 -9.203  1.00 53.88  ?  488  GLU A CD  1 
ATOM   3569  O  OE1 . GLU A  1 457 ? 6.143   -28.728 -9.467  1.00 58.78  ?  488  GLU A OE1 1 
ATOM   3570  O  OE2 . GLU A  1 457 ? 7.923   -28.188 -8.263  1.00 54.90  -1 488  GLU A OE2 1 
ATOM   3571  N  N   . SER A  1 458 ? 6.477   -25.974 -14.603 1.00 40.42  ?  489  SER A N   1 
ATOM   3572  C  CA  . SER A  1 458 ? 6.330   -26.354 -15.994 1.00 37.35  ?  489  SER A CA  1 
ATOM   3573  C  C   . SER A  1 458 ? 6.889   -25.320 -16.956 1.00 41.39  ?  489  SER A C   1 
ATOM   3574  O  O   . SER A  1 458 ? 6.811   -25.528 -18.170 1.00 44.35  ?  489  SER A O   1 
ATOM   3575  C  CB  . SER A  1 458 ? 4.849   -26.601 -16.322 1.00 41.49  ?  489  SER A CB  1 
ATOM   3576  O  OG  . SER A  1 458 ? 4.125   -25.381 -16.329 1.00 42.57  ?  489  SER A OG  1 
ATOM   3577  N  N   . GLY A  1 459 ? 7.414   -24.201 -16.460 1.00 35.64  ?  490  GLY A N   1 
ATOM   3578  C  CA  . GLY A  1 459 ? 7.893   -23.141 -17.330 1.00 41.17  ?  490  GLY A CA  1 
ATOM   3579  C  C   . GLY A  1 459 ? 6.828   -22.233 -17.934 1.00 37.34  ?  490  GLY A C   1 
ATOM   3580  O  O   . GLY A  1 459 ? 7.176   -21.326 -18.705 1.00 40.72  ?  490  GLY A O   1 
ATOM   3581  N  N   . GLN A  1 460 ? 5.552   -22.430 -17.606 1.00 38.02  ?  491  GLN A N   1 
ATOM   3582  C  CA  . GLN A  1 460 ? 4.519   -21.492 -18.045 1.00 36.91  ?  491  GLN A CA  1 
ATOM   3583  C  C   . GLN A  1 460 ? 4.728   -20.095 -17.448 1.00 39.59  ?  491  GLN A C   1 
ATOM   3584  O  O   . GLN A  1 460 ? 4.502   -19.085 -18.122 1.00 36.85  ?  491  GLN A O   1 
ATOM   3585  C  CB  . GLN A  1 460 ? 3.146   -22.056 -17.694 1.00 42.35  ?  491  GLN A CB  1 
ATOM   3586  C  CG  . GLN A  1 460 ? 2.827   -23.321 -18.479 1.00 48.60  ?  491  GLN A CG  1 
ATOM   3587  C  CD  . GLN A  1 460 ? 1.545   -24.009 -18.049 1.00 50.78  ?  491  GLN A CD  1 
ATOM   3588  O  OE1 . GLN A  1 460 ? 0.448   -23.606 -18.441 1.00 57.50  ?  491  GLN A OE1 1 
ATOM   3589  N  NE2 . GLN A  1 460 ? 1.682   -25.089 -17.267 1.00 45.86  ?  491  GLN A NE2 1 
ATOM   3590  N  N   . MET A  1 461 ? 5.280   -20.089 -16.244 1.00 34.04  ?  492  MET A N   1 
ATOM   3591  C  CA  . MET A  1 461 ? 5.673   -18.820 -15.591 1.00 36.42  ?  492  MET A CA  1 
ATOM   3592  C  C   . MET A  1 461 ? 7.194   -18.943 -15.479 1.00 37.51  ?  492  MET A C   1 
ATOM   3593  O  O   . MET A  1 461 ? 7.665   -20.097 -15.343 1.00 36.66  ?  492  MET A O   1 
ATOM   3594  C  CB  . MET A  1 461 ? 5.033   -18.657 -14.204 1.00 33.60  ?  492  MET A CB  1 
ATOM   3595  C  CG  . MET A  1 461 ? 3.548   -18.415 -14.221 1.00 35.49  ?  492  MET A CG  1 
ATOM   3596  S  SD  . MET A  1 461 ? 3.124   -16.789 -14.868 1.00 32.75  ?  492  MET A SD  1 
ATOM   3597  C  CE  . MET A  1 461 ? 3.850   -15.734 -13.610 1.00 29.58  ?  492  MET A CE  1 
ATOM   3598  N  N   . PRO A  1 462 ? 7.966   -17.843 -15.521 1.00 37.48  ?  493  PRO A N   1 
ATOM   3599  C  CA  . PRO A  1 462 ? 7.441   -16.460 -15.653 1.00 33.90  ?  493  PRO A CA  1 
ATOM   3600  C  C   . PRO A  1 462 ? 7.181   -15.968 -17.071 1.00 34.69  ?  493  PRO A C   1 
ATOM   3601  O  O   . PRO A  1 462 ? 6.468   -14.982 -17.252 1.00 32.40  ?  493  PRO A O   1 
ATOM   3602  C  CB  . PRO A  1 462 ? 8.546   -15.628 -15.004 1.00 33.21  ?  493  PRO A CB  1 
ATOM   3603  C  CG  . PRO A  1 462 ? 9.809   -16.394 -15.333 1.00 33.10  ?  493  PRO A CG  1 
ATOM   3604  C  CD  . PRO A  1 462 ? 9.426   -17.856 -15.311 1.00 33.44  ?  493  PRO A CD  1 
ATOM   3605  N  N   . ASN A  1 463 ? 7.769   -16.616 -18.075 1.00 35.88  ?  494  ASN A N   1 
ATOM   3606  C  CA  . ASN A  1 463 ? 7.636   -16.263 -19.488 1.00 34.18  ?  494  ASN A CA  1 
ATOM   3607  C  C   . ASN A  1 463 ? 7.667   -14.748 -19.726 1.00 35.67  ?  494  ASN A C   1 
ATOM   3608  O  O   . ASN A  1 463 ? 6.736   -14.148 -20.282 1.00 30.53  ?  494  ASN A O   1 
ATOM   3609  C  CB  . ASN A  1 463 ? 6.370   -16.878 -20.088 1.00 36.09  ?  494  ASN A CB  1 
ATOM   3610  C  CG  . ASN A  1 463 ? 6.451   -16.982 -21.600 1.00 37.76  ?  494  ASN A CG  1 
ATOM   3611  O  OD1 . ASN A  1 463 ? 7.354   -16.410 -22.211 1.00 39.35  ?  494  ASN A OD1 1 
ATOM   3612  N  ND2 . ASN A  1 463 ? 5.516   -17.697 -22.209 1.00 36.29  ?  494  ASN A ND2 1 
ATOM   3613  N  N   . TYR A  1 464 ? 8.783   -14.136 -19.319 1.00 29.91  ?  495  TYR A N   1 
ATOM   3614  C  CA  . TYR A  1 464 ? 8.979   -12.713 -19.577 1.00 32.00  ?  495  TYR A CA  1 
ATOM   3615  C  C   . TYR A  1 464 ? 8.948   -12.417 -21.066 1.00 33.13  ?  495  TYR A C   1 
ATOM   3616  O  O   . TYR A  1 464 ? 8.534   -11.326 -21.471 1.00 34.61  ?  495  TYR A O   1 
ATOM   3617  C  CB  . TYR A  1 464 ? 10.305  -12.217 -18.956 1.00 29.83  ?  495  TYR A CB  1 
ATOM   3618  C  CG  . TYR A  1 464 ? 10.407  -12.470 -17.463 1.00 35.33  ?  495  TYR A CG  1 
ATOM   3619  C  CD1 . TYR A  1 464 ? 9.514   -11.852 -16.570 1.00 30.60  ?  495  TYR A CD1 1 
ATOM   3620  C  CD2 . TYR A  1 464 ? 11.399  -13.314 -16.932 1.00 32.33  ?  495  TYR A CD2 1 
ATOM   3621  C  CE1 . TYR A  1 464 ? 9.592   -12.069 -15.188 1.00 30.71  ?  495  TYR A CE1 1 
ATOM   3622  C  CE2 . TYR A  1 464 ? 11.485  -13.537 -15.553 1.00 35.47  ?  495  TYR A CE2 1 
ATOM   3623  C  CZ  . TYR A  1 464 ? 10.572  -12.917 -14.689 1.00 34.94  ?  495  TYR A CZ  1 
ATOM   3624  O  OH  . TYR A  1 464 ? 10.652  -13.141 -13.336 1.00 32.86  ?  495  TYR A OH  1 
ATOM   3625  N  N   . GLU A  1 465 ? 9.370   -13.370 -21.902 1.00 34.78  ?  496  GLU A N   1 
ATOM   3626  C  CA  . GLU A  1 465 ? 9.354   -13.138 -23.344 1.00 34.22  ?  496  GLU A CA  1 
ATOM   3627  C  C   . GLU A  1 465 ? 7.935   -12.808 -23.820 1.00 32.88  ?  496  GLU A C   1 
ATOM   3628  O  O   . GLU A  1 465 ? 7.714   -11.820 -24.530 1.00 31.80  ?  496  GLU A O   1 
ATOM   3629  C  CB  . GLU A  1 465 ? 9.900   -14.367 -24.091 1.00 40.49  ?  496  GLU A CB  1 
ATOM   3630  C  CG  . GLU A  1 465 ? 11.407  -14.657 -23.877 1.00 46.88  ?  496  GLU A CG  1 
ATOM   3631  C  CD  . GLU A  1 465 ? 11.767  -15.037 -22.428 1.00 49.85  ?  496  GLU A CD  1 
ATOM   3632  O  OE1 . GLU A  1 465 ? 10.940  -15.714 -21.744 1.00 48.00  ?  496  GLU A OE1 1 
ATOM   3633  O  OE2 . GLU A  1 465 ? 12.862  -14.628 -21.959 1.00 51.35  -1 496  GLU A OE2 1 
ATOM   3634  N  N   . ALA A  1 466 ? 6.960   -13.623 -23.419 1.00 28.98  ?  497  ALA A N   1 
ATOM   3635  C  CA  . ALA A  1 466 ? 5.562   -13.370 -23.772 1.00 33.71  ?  497  ALA A CA  1 
ATOM   3636  C  C   . ALA A  1 466 ? 5.041   -12.066 -23.160 1.00 31.52  ?  497  ALA A C   1 
ATOM   3637  O  O   . ALA A  1 466 ? 4.239   -11.358 -23.778 1.00 31.10  ?  497  ALA A O   1 
ATOM   3638  C  CB  . ALA A  1 466 ? 4.710   -14.556 -23.331 1.00 33.94  ?  497  ALA A CB  1 
ATOM   3639  N  N   . THR A  1 467 ? 5.478   -11.731 -21.948 1.00 28.92  ?  498  THR A N   1 
ATOM   3640  C  CA  . THR A  1 467 ? 5.082   -10.460 -21.346 1.00 29.77  ?  498  THR A CA  1 
ATOM   3641  C  C   . THR A  1 467 ? 5.426   -9.272  -22.247 1.00 33.87  ?  498  THR A C   1 
ATOM   3642  O  O   . THR A  1 467 ? 4.662   -8.302  -22.321 1.00 30.72  ?  498  THR A O   1 
ATOM   3643  C  CB  . THR A  1 467 ? 5.751   -10.314 -19.969 1.00 30.23  ?  498  THR A CB  1 
ATOM   3644  O  OG1 . THR A  1 467 ? 5.215   -11.305 -19.091 1.00 29.23  ?  498  THR A OG1 1 
ATOM   3645  C  CG2 . THR A  1 467 ? 5.516   -8.932  -19.359 1.00 27.64  ?  498  THR A CG2 1 
ATOM   3646  N  N   . PHE A  1 468 ? 6.564   -9.321  -22.952 1.00 32.06  ?  499  PHE A N   1 
ATOM   3647  C  CA  . PHE A  1 468 ? 6.998   -8.140  -23.690 1.00 30.95  ?  499  PHE A CA  1 
ATOM   3648  C  C   . PHE A  1 468 ? 6.692   -8.208  -25.183 1.00 31.39  ?  499  PHE A C   1 
ATOM   3649  O  O   . PHE A  1 468 ? 7.198   -7.375  -25.945 1.00 32.56  ?  499  PHE A O   1 
ATOM   3650  C  CB  . PHE A  1 468 ? 8.477   -7.870  -23.417 1.00 31.63  ?  499  PHE A CB  1 
ATOM   3651  C  CG  . PHE A  1 468 ? 8.741   -7.539  -21.973 1.00 31.88  ?  499  PHE A CG  1 
ATOM   3652  C  CD1 . PHE A  1 468 ? 8.288   -6.346  -21.434 1.00 27.73  ?  499  PHE A CD1 1 
ATOM   3653  C  CD2 . PHE A  1 468 ? 9.394   -8.436  -21.149 1.00 34.18  ?  499  PHE A CD2 1 
ATOM   3654  C  CE1 . PHE A  1 468 ? 8.498   -6.042  -20.093 1.00 30.65  ?  499  PHE A CE1 1 
ATOM   3655  C  CE2 . PHE A  1 468 ? 9.621   -8.138  -19.807 1.00 32.59  ?  499  PHE A CE2 1 
ATOM   3656  C  CZ  . PHE A  1 468 ? 9.173   -6.933  -19.281 1.00 33.95  ?  499  PHE A CZ  1 
ATOM   3657  N  N   . GLU A  1 469 ? 5.827   -9.136  -25.604 1.00 30.08  ?  500  GLU A N   1 
ATOM   3658  C  CA  . GLU A  1 469 ? 5.216   -9.053  -26.929 1.00 33.75  ?  500  GLU A CA  1 
ATOM   3659  C  C   . GLU A  1 469 ? 4.413   -7.763  -27.047 1.00 38.44  ?  500  GLU A C   1 
ATOM   3660  O  O   . GLU A  1 469 ? 3.837   -7.279  -26.064 1.00 37.13  ?  500  GLU A O   1 
ATOM   3661  C  CB  . GLU A  1 469 ? 4.293   -10.256 -27.177 1.00 29.09  ?  500  GLU A CB  1 
ATOM   3662  C  CG  . GLU A  1 469 ? 5.030   -11.599 -27.286 1.00 32.88  ?  500  GLU A CG  1 
ATOM   3663  C  CD  . GLU A  1 469 ? 4.129   -12.811 -27.143 1.00 37.12  ?  500  GLU A CD  1 
ATOM   3664  O  OE1 . GLU A  1 469 ? 3.007   -12.697 -26.578 1.00 36.60  ?  500  GLU A OE1 1 
ATOM   3665  O  OE2 . GLU A  1 469 ? 4.552   -13.904 -27.582 1.00 34.21  -1 500  GLU A OE2 1 
ATOM   3666  N  N   . VAL A  1 470 ? 4.366   -7.202  -28.265 1.00 32.06  ?  501  VAL A N   1 
ATOM   3667  C  CA  . VAL A  1 470 ? 3.634   -5.959  -28.496 1.00 33.73  ?  501  VAL A CA  1 
ATOM   3668  C  C   . VAL A  1 470 ? 2.691   -6.057  -29.699 1.00 34.60  ?  501  VAL A C   1 
ATOM   3669  O  O   . VAL A  1 470 ? 1.461   -6.019  -29.538 1.00 33.63  ?  501  VAL A O   1 
ATOM   3670  C  CB  . VAL A  1 470 ? 4.594   -4.762  -28.664 1.00 30.50  ?  501  VAL A CB  1 
ATOM   3671  C  CG1 . VAL A  1 470 ? 3.797   -3.488  -28.971 1.00 34.37  ?  501  VAL A CG1 1 
ATOM   3672  C  CG2 . VAL A  1 470 ? 5.452   -4.568  -27.424 1.00 33.98  ?  501  VAL A CG2 1 
ATOM   3673  N  N   . ASP A  1 471 ? 3.247   -6.187  -30.916 1.00 32.47  ?  502  ASP A N   1 
ATOM   3674  C  CA  . ASP A  1 471 ? 2.419   -6.047  -32.122 1.00 36.41  ?  502  ASP A CA  1 
ATOM   3675  C  C   . ASP A  1 471 ? 1.381   -7.162  -32.262 1.00 30.81  ?  502  ASP A C   1 
ATOM   3676  O  O   . ASP A  1 471 ? 0.258   -6.914  -32.731 1.00 32.68  ?  502  ASP A O   1 
ATOM   3677  C  CB  . ASP A  1 471 ? 3.300   -5.989  -33.378 1.00 37.98  ?  502  ASP A CB  1 
ATOM   3678  C  CG  . ASP A  1 471 ? 4.252   -4.807  -33.366 1.00 46.28  ?  502  ASP A CG  1 
ATOM   3679  O  OD1 . ASP A  1 471 ? 4.001   -3.834  -32.624 1.00 47.13  ?  502  ASP A OD1 1 
ATOM   3680  O  OD2 . ASP A  1 471 ? 5.256   -4.846  -34.103 1.00 51.55  -1 502  ASP A OD2 1 
ATOM   3681  N  N   . LYS A  1 472 ? 1.723   -8.399  -31.890 1.00 32.27  ?  503  LYS A N   1 
ATOM   3682  C  CA  . LYS A  1 472 ? 0.760   -9.485  -32.070 1.00 32.56  ?  503  LYS A CA  1 
ATOM   3683  C  C   . LYS A  1 472 ? -0.458  -9.332  -31.164 1.00 32.23  ?  503  LYS A C   1 
ATOM   3684  O  O   . LYS A  1 472 ? -1.497  -9.962  -31.422 1.00 32.22  ?  503  LYS A O   1 
ATOM   3685  C  CB  . LYS A  1 472 ? 1.418   -10.845 -31.824 1.00 31.81  ?  503  LYS A CB  1 
ATOM   3686  C  CG  . LYS A  1 472 ? 1.791   -11.093 -30.355 1.00 32.94  ?  503  LYS A CG  1 
ATOM   3687  C  CD  . LYS A  1 472 ? 2.266   -12.528 -30.135 1.00 38.17  ?  503  LYS A CD  1 
ATOM   3688  C  CE  . LYS A  1 472 ? 3.464   -12.866 -31.016 1.00 37.04  ?  503  LYS A CE  1 
ATOM   3689  N  NZ  . LYS A  1 472 ? 4.119   -14.089 -30.484 1.00 35.46  ?  503  LYS A NZ  1 
ATOM   3690  N  N   . LEU A  1 473 ? -0.358  -8.511  -30.112 1.00 31.70  ?  504  LEU A N   1 
ATOM   3691  C  CA  . LEU A  1 473 ? -1.514  -8.247  -29.261 1.00 29.43  ?  504  LEU A CA  1 
ATOM   3692  C  C   . LEU A  1 473 ? -2.536  -7.338  -29.935 1.00 29.57  ?  504  LEU A C   1 
ATOM   3693  O  O   . LEU A  1 473 ? -3.712  -7.356  -29.537 1.00 29.00  ?  504  LEU A O   1 
ATOM   3694  C  CB  . LEU A  1 473 ? -1.059  -7.622  -27.934 1.00 28.09  ?  504  LEU A CB  1 
ATOM   3695  C  CG  . LEU A  1 473 ? 0.035   -8.394  -27.159 1.00 27.75  ?  504  LEU A CG  1 
ATOM   3696  C  CD1 . LEU A  1 473 ? 0.418   -7.681  -25.862 1.00 30.48  ?  504  LEU A CD1 1 
ATOM   3697  C  CD2 . LEU A  1 473 ? -0.340  -9.847  -26.879 1.00 26.56  ?  504  LEU A CD2 1 
ATOM   3698  N  N   . VAL A  1 474 ? -2.124  -6.536  -30.924 1.00 27.48  ?  505  VAL A N   1 
ATOM   3699  C  CA  . VAL A  1 474 ? -3.022  -5.579  -31.561 1.00 30.67  ?  505  VAL A CA  1 
ATOM   3700  C  C   . VAL A  1 474 ? -3.270  -5.863  -33.043 1.00 32.17  ?  505  VAL A C   1 
ATOM   3701  O  O   . VAL A  1 474 ? -4.266  -5.359  -33.591 1.00 31.58  ?  505  VAL A O   1 
ATOM   3702  C  CB  . VAL A  1 474 ? -2.509  -4.132  -31.389 1.00 33.91  ?  505  VAL A CB  1 
ATOM   3703  C  CG1 . VAL A  1 474 ? -2.468  -3.730  -29.900 1.00 33.02  ?  505  VAL A CG1 1 
ATOM   3704  C  CG2 . VAL A  1 474 ? -1.129  -3.976  -32.030 1.00 35.82  ?  505  VAL A CG2 1 
ATOM   3705  N  N   . ASP A  1 475 ? -2.404  -6.610  -33.729 1.00 34.71  ?  506  ASP A N   1 
ATOM   3706  C  CA  . ASP A  1 475 ? -2.584  -6.868  -35.154 1.00 34.02  ?  506  ASP A CA  1 
ATOM   3707  C  C   . ASP A  1 475 ? -3.732  -7.830  -35.377 1.00 29.65  ?  506  ASP A C   1 
ATOM   3708  O  O   . ASP A  1 475 ? -3.923  -8.776  -34.612 1.00 35.22  ?  506  ASP A O   1 
ATOM   3709  C  CB  . ASP A  1 475 ? -1.317  -7.468  -35.761 1.00 29.49  ?  506  ASP A CB  1 
ATOM   3710  C  CG  . ASP A  1 475 ? -0.157  -6.487  -35.806 1.00 40.15  ?  506  ASP A CG  1 
ATOM   3711  O  OD1 . ASP A  1 475 ? -0.376  -5.252  -35.797 1.00 38.31  ?  506  ASP A OD1 1 
ATOM   3712  O  OD2 . ASP A  1 475 ? 0.993   -6.965  -35.839 1.00 37.45  -1 506  ASP A OD2 1 
ATOM   3713  N  N   . SER A  1 476 ? -4.490  -7.596  -36.443 1.00 32.26  ?  507  SER A N   1 
ATOM   3714  C  CA  . SER A  1 476 ? -5.479  -8.583  -36.828 1.00 32.07  ?  507  SER A CA  1 
ATOM   3715  C  C   . SER A  1 476 ? -4.816  -9.657  -37.686 1.00 36.79  ?  507  SER A C   1 
ATOM   3716  O  O   . SER A  1 476 ? -4.013  -9.334  -38.561 1.00 33.69  ?  507  SER A O   1 
ATOM   3717  C  CB  . SER A  1 476 ? -6.605  -7.939  -37.622 1.00 32.01  ?  507  SER A CB  1 
ATOM   3718  O  OG  . SER A  1 476 ? -7.281  -8.922  -38.397 1.00 29.67  ?  507  SER A OG  1 
ATOM   3719  N  N   . PRO A  1 477 ? -5.139  -10.934 -37.470 1.00 31.45  ?  508  PRO A N   1 
ATOM   3720  C  CA  . PRO A  1 477 ? -4.621  -11.987 -38.358 1.00 34.93  ?  508  PRO A CA  1 
ATOM   3721  C  C   . PRO A  1 477 ? -5.254  -12.003 -39.759 1.00 40.98  ?  508  PRO A C   1 
ATOM   3722  O  O   . PRO A  1 477 ? -4.886  -12.855 -40.576 1.00 37.98  ?  508  PRO A O   1 
ATOM   3723  C  CB  . PRO A  1 477 ? -4.956  -13.273 -37.592 1.00 34.10  ?  508  PRO A CB  1 
ATOM   3724  C  CG  . PRO A  1 477 ? -6.144  -12.917 -36.762 1.00 35.60  ?  508  PRO A CG  1 
ATOM   3725  C  CD  . PRO A  1 477 ? -5.957  -11.472 -36.371 1.00 33.02  ?  508  PRO A CD  1 
ATOM   3726  N  N   . TYR A  1 478 ? -6.177  -11.100 -40.078 1.00 36.73  ?  509  TYR A N   1 
ATOM   3727  C  CA  . TYR A  1 478 ? -6.883  -11.131 -41.367 1.00 39.74  ?  509  TYR A CA  1 
ATOM   3728  C  C   . TYR A  1 478 ? -6.530  -9.974  -42.316 1.00 41.83  ?  509  TYR A C   1 
ATOM   3729  O  O   . TYR A  1 478 ? -5.766  -9.070  -41.958 1.00 46.32  ?  509  TYR A O   1 
ATOM   3730  C  CB  . TYR A  1 478 ? -8.382  -11.142 -41.113 1.00 36.06  ?  509  TYR A CB  1 
ATOM   3731  C  CG  . TYR A  1 478 ? -8.771  -12.159 -40.062 1.00 35.00  ?  509  TYR A CG  1 
ATOM   3732  C  CD1 . TYR A  1 478 ? -8.607  -13.516 -40.303 1.00 30.74  ?  509  TYR A CD1 1 
ATOM   3733  C  CD2 . TYR A  1 478 ? -9.263  -11.761 -38.820 1.00 34.13  ?  509  TYR A CD2 1 
ATOM   3734  C  CE1 . TYR A  1 478 ? -8.943  -14.455 -39.364 1.00 37.63  ?  509  TYR A CE1 1 
ATOM   3735  C  CE2 . TYR A  1 478 ? -9.603  -12.704 -37.856 1.00 32.43  ?  509  TYR A CE2 1 
ATOM   3736  C  CZ  . TYR A  1 478 ? -9.432  -14.050 -38.130 1.00 33.90  ?  509  TYR A CZ  1 
ATOM   3737  O  OH  . TYR A  1 478 ? -9.742  -15.008 -37.187 1.00 36.05  ?  509  TYR A OH  1 
ATOM   3738  N  N   . GLU B  1 14  ? -56.309 -6.671  -36.229 1.00 54.89  ?  45   GLU B N   1 
ATOM   3739  C  CA  . GLU B  1 14  ? -54.895 -6.600  -35.840 1.00 58.46  ?  45   GLU B CA  1 
ATOM   3740  C  C   . GLU B  1 14  ? -54.667 -5.892  -34.500 1.00 55.14  ?  45   GLU B C   1 
ATOM   3741  O  O   . GLU B  1 14  ? -54.915 -4.694  -34.369 1.00 56.62  ?  45   GLU B O   1 
ATOM   3742  C  CB  . GLU B  1 14  ? -54.073 -5.903  -36.935 1.00 56.81  ?  45   GLU B CB  1 
ATOM   3743  C  CG  . GLU B  1 14  ? -52.575 -5.789  -36.613 1.00 55.12  ?  45   GLU B CG  1 
ATOM   3744  C  CD  . GLU B  1 14  ? -51.893 -7.139  -36.525 1.00 47.04  ?  45   GLU B CD  1 
ATOM   3745  O  OE1 . GLU B  1 14  ? -51.935 -7.742  -35.438 1.00 49.22  ?  45   GLU B OE1 1 
ATOM   3746  O  OE2 . GLU B  1 14  ? -51.319 -7.601  -37.532 1.00 46.47  ?  45   GLU B OE2 1 
ATOM   3747  N  N   . THR B  1 15  ? -54.178 -6.643  -33.509 1.00 49.54  ?  46   THR B N   1 
ATOM   3748  C  CA  . THR B  1 15  ? -53.909 -6.102  -32.186 1.00 48.16  ?  46   THR B CA  1 
ATOM   3749  C  C   . THR B  1 15  ? -52.495 -6.408  -31.692 1.00 45.32  ?  46   THR B C   1 
ATOM   3750  O  O   . THR B  1 15  ? -52.161 -6.045  -30.558 1.00 41.29  ?  46   THR B O   1 
ATOM   3751  C  CB  . THR B  1 15  ? -54.917 -6.651  -31.162 1.00 50.58  ?  46   THR B CB  1 
ATOM   3752  O  OG1 . THR B  1 15  ? -54.707 -8.062  -31.000 1.00 54.00  ?  46   THR B OG1 1 
ATOM   3753  C  CG2 . THR B  1 15  ? -56.350 -6.411  -31.631 1.00 51.51  ?  46   THR B CG2 1 
ATOM   3754  N  N   . ARG B  1 16  ? -51.672 -7.083  -32.488 1.00 44.12  ?  47   ARG B N   1 
ATOM   3755  C  CA  . ARG B  1 16  ? -50.295 -7.333  -32.084 1.00 37.10  ?  47   ARG B CA  1 
ATOM   3756  C  C   . ARG B  1 16  ? -49.557 -6.004  -31.934 1.00 37.71  ?  47   ARG B C   1 
ATOM   3757  O  O   . ARG B  1 16  ? -49.796 -5.073  -32.708 1.00 37.44  ?  47   ARG B O   1 
ATOM   3758  C  CB  . ARG B  1 16  ? -49.613 -8.229  -33.112 1.00 36.65  ?  47   ARG B CB  1 
ATOM   3759  C  CG  . ARG B  1 16  ? -49.953 -9.697  -32.940 1.00 38.05  ?  47   ARG B CG  1 
ATOM   3760  C  CD  . ARG B  1 16  ? -49.627 -10.491 -34.180 1.00 40.32  ?  47   ARG B CD  1 
ATOM   3761  N  NE  . ARG B  1 16  ? -49.710 -9.705  -35.411 1.00 36.52  ?  47   ARG B NE  1 
ATOM   3762  C  CZ  . ARG B  1 16  ? -49.113 -10.044 -36.546 1.00 36.87  ?  47   ARG B CZ  1 
ATOM   3763  N  NH1 . ARG B  1 16  ? -48.290 -11.079 -36.610 1.00 33.54  ?  47   ARG B NH1 1 
ATOM   3764  N  NH2 . ARG B  1 16  ? -49.356 -9.337  -37.652 1.00 41.12  ?  47   ARG B NH2 1 
ATOM   3765  N  N   . PRO B  1 17  ? -48.673 -5.867  -30.949 1.00 35.90  ?  48   PRO B N   1 
ATOM   3766  C  CA  . PRO B  1 17  ? -48.072 -4.556  -30.700 1.00 33.77  ?  48   PRO B CA  1 
ATOM   3767  C  C   . PRO B  1 17  ? -46.920 -4.249  -31.642 1.00 31.37  ?  48   PRO B C   1 
ATOM   3768  O  O   . PRO B  1 17  ? -46.267 -5.140  -32.195 1.00 29.83  ?  48   PRO B O   1 
ATOM   3769  C  CB  . PRO B  1 17  ? -47.582 -4.660  -29.249 1.00 31.15  ?  48   PRO B CB  1 
ATOM   3770  C  CG  . PRO B  1 17  ? -47.261 -6.116  -29.067 1.00 35.91  ?  48   PRO B CG  1 
ATOM   3771  C  CD  . PRO B  1 17  ? -48.317 -6.851  -29.914 1.00 35.78  ?  48   PRO B CD  1 
ATOM   3772  N  N   . ASN B  1 18  ? -46.701 -2.950  -31.833 1.00 29.60  ?  49   ASN B N   1 
ATOM   3773  C  CA  . ASN B  1 18  ? -45.445 -2.471  -32.372 1.00 31.72  ?  49   ASN B CA  1 
ATOM   3774  C  C   . ASN B  1 18  ? -44.336 -2.730  -31.349 1.00 27.53  ?  49   ASN B C   1 
ATOM   3775  O  O   . ASN B  1 18  ? -44.580 -2.843  -30.145 1.00 30.77  ?  49   ASN B O   1 
ATOM   3776  C  CB  . ASN B  1 18  ? -45.519 -0.975  -32.688 1.00 27.69  ?  49   ASN B CB  1 
ATOM   3777  C  CG  . ASN B  1 18  ? -46.727 -0.612  -33.547 1.00 33.24  ?  49   ASN B CG  1 
ATOM   3778  O  OD1 . ASN B  1 18  ? -46.909 -1.139  -34.645 1.00 32.99  ?  49   ASN B OD1 1 
ATOM   3779  N  ND2 . ASN B  1 18  ? -47.524 0.331   -33.065 1.00 30.53  ?  49   ASN B ND2 1 
ATOM   3780  N  N   . ILE B  1 19  ? -43.106 -2.832  -31.846 1.00 28.17  ?  50   ILE B N   1 
ATOM   3781  C  CA  . ILE B  1 19  ? -41.944 -3.066  -31.002 1.00 26.24  ?  50   ILE B CA  1 
ATOM   3782  C  C   . ILE B  1 19  ? -40.834 -2.124  -31.444 1.00 27.74  ?  50   ILE B C   1 
ATOM   3783  O  O   . ILE B  1 19  ? -40.425 -2.143  -32.610 1.00 26.01  ?  50   ILE B O   1 
ATOM   3784  C  CB  . ILE B  1 19  ? -41.471 -4.529  -31.077 1.00 27.24  ?  50   ILE B CB  1 
ATOM   3785  C  CG1 . ILE B  1 19  ? -42.567 -5.484  -30.590 1.00 30.30  ?  50   ILE B CG1 1 
ATOM   3786  C  CG2 . ILE B  1 19  ? -40.163 -4.722  -30.266 1.00 26.60  ?  50   ILE B CG2 1 
ATOM   3787  C  CD1 . ILE B  1 19  ? -42.239 -6.982  -30.834 1.00 31.85  ?  50   ILE B CD1 1 
ATOM   3788  N  N   . LEU B  1 20  ? -40.311 -1.346  -30.494 1.00 29.96  ?  51   LEU B N   1 
ATOM   3789  C  CA  . LEU B  1 20  ? -39.199 -0.429  -30.715 1.00 26.06  ?  51   LEU B CA  1 
ATOM   3790  C  C   . LEU B  1 20  ? -38.105 -0.792  -29.718 1.00 23.94  ?  51   LEU B C   1 
ATOM   3791  O  O   . LEU B  1 20  ? -38.317 -0.682  -28.511 1.00 22.79  ?  51   LEU B O   1 
ATOM   3792  C  CB  . LEU B  1 20  ? -39.651 1.014   -30.525 1.00 24.96  ?  51   LEU B CB  1 
ATOM   3793  C  CG  . LEU B  1 20  ? -38.534 2.044   -30.488 1.00 28.48  ?  51   LEU B CG  1 
ATOM   3794  C  CD1 . LEU B  1 20  ? -37.757 2.028   -31.802 1.00 27.63  ?  51   LEU B CD1 1 
ATOM   3795  C  CD2 . LEU B  1 20  ? -39.070 3.427   -30.152 1.00 26.36  ?  51   LEU B CD2 1 
ATOM   3796  N  N   . VAL B  1 21  ? -36.970 -1.272  -30.219 1.00 22.46  ?  52   VAL B N   1 
ATOM   3797  C  CA  . VAL B  1 21  ? -35.779 -1.485  -29.401 1.00 24.60  ?  52   VAL B CA  1 
ATOM   3798  C  C   . VAL B  1 21  ? -34.921 -0.243  -29.555 1.00 26.01  ?  52   VAL B C   1 
ATOM   3799  O  O   . VAL B  1 21  ? -34.509 0.093   -30.674 1.00 25.79  ?  52   VAL B O   1 
ATOM   3800  C  CB  . VAL B  1 21  ? -34.998 -2.731  -29.845 1.00 24.05  ?  52   VAL B CB  1 
ATOM   3801  C  CG1 . VAL B  1 21  ? -33.678 -2.846  -29.047 1.00 25.97  ?  52   VAL B CG1 1 
ATOM   3802  C  CG2 . VAL B  1 21  ? -35.832 -3.968  -29.685 1.00 24.97  ?  52   VAL B CG2 1 
ATOM   3803  N  N   . VAL B  1 22  ? -34.677 0.459   -28.453 1.00 26.71  ?  53   VAL B N   1 
ATOM   3804  C  CA  . VAL B  1 22  ? -33.706 1.544   -28.440 1.00 24.72  ?  53   VAL B CA  1 
ATOM   3805  C  C   . VAL B  1 22  ? -32.467 1.002   -27.752 1.00 26.56  ?  53   VAL B C   1 
ATOM   3806  O  O   . VAL B  1 22  ? -32.483 0.736   -26.548 1.00 25.72  ?  53   VAL B O   1 
ATOM   3807  C  CB  . VAL B  1 22  ? -34.242 2.798   -27.742 1.00 23.79  ?  53   VAL B CB  1 
ATOM   3808  C  CG1 . VAL B  1 22  ? -33.193 3.892   -27.785 1.00 23.46  ?  53   VAL B CG1 1 
ATOM   3809  C  CG2 . VAL B  1 22  ? -35.590 3.260   -28.418 1.00 25.30  ?  53   VAL B CG2 1 
ATOM   3810  N  N   . LEU B  1 23  ? -31.407 0.780   -28.518 1.00 26.65  ?  54   LEU B N   1 
ATOM   3811  C  CA  . LEU B  1 23  ? -30.197 0.163   -27.993 1.00 23.54  ?  54   LEU B CA  1 
ATOM   3812  C  C   . LEU B  1 23  ? -29.085 1.196   -28.032 1.00 23.66  ?  54   LEU B C   1 
ATOM   3813  O  O   . LEU B  1 23  ? -28.720 1.665   -29.113 1.00 24.62  ?  54   LEU B O   1 
ATOM   3814  C  CB  . LEU B  1 23  ? -29.816 -1.069  -28.822 1.00 25.41  ?  54   LEU B CB  1 
ATOM   3815  C  CG  . LEU B  1 23  ? -28.522 -1.791  -28.461 1.00 27.17  ?  54   LEU B CG  1 
ATOM   3816  C  CD1 . LEU B  1 23  ? -28.734 -2.499  -27.115 1.00 19.06  ?  54   LEU B CD1 1 
ATOM   3817  C  CD2 . LEU B  1 23  ? -28.177 -2.807  -29.564 1.00 23.79  ?  54   LEU B CD2 1 
ATOM   3818  N  N   . CYS B  1 24  ? -28.546 1.553   -26.866 1.00 24.02  ?  55   CYS B N   1 
ATOM   3819  C  CA  . CYS B  1 24  ? -27.397 2.434   -26.867 1.00 25.09  ?  55   CYS B CA  1 
ATOM   3820  C  C   . CYS B  1 24  ? -26.133 1.593   -26.884 1.00 24.47  ?  55   CYS B C   1 
ATOM   3821  O  O   . CYS B  1 24  ? -26.171 0.380   -26.695 1.00 22.96  ?  55   CYS B O   1 
ATOM   3822  C  CB  . CYS B  1 24  ? -27.400 3.384   -25.659 1.00 26.66  ?  55   CYS B CB  1 
ATOM   3823  S  SG  . CYS B  1 24  ? -28.563 4.749   -25.905 1.00 28.26  ?  55   CYS B SG  1 
ATOM   3824  N  N   . ASP B  1 25  ? -25.024 2.292   -27.164 1.00 24.95  ?  56   ASP B N   1 
ATOM   3825  C  CA  . ASP B  1 25  ? -23.709 1.620   -27.310 1.00 24.61  ?  56   ASP B CA  1 
ATOM   3826  C  C   . ASP B  1 25  ? -22.752 2.091   -26.212 1.00 22.68  ?  56   ASP B C   1 
ATOM   3827  O  O   . ASP B  1 25  ? -22.358 3.282   -26.226 1.00 25.61  ?  56   ASP B O   1 
ATOM   3828  C  CB  . ASP B  1 25  ? -23.138 1.901   -28.688 1.00 24.57  ?  56   ASP B CB  1 
ATOM   3829  C  CG  . ASP B  1 25  ? -21.920 1.095   -29.109 1.00 27.62  ?  56   ASP B CG  1 
ATOM   3830  O  OD1 . ASP B  1 25  ? -21.451 0.264   -28.308 1.00 26.72  ?  56   ASP B OD1 1 
ATOM   3831  O  OD2 . ASP B  1 25  ? -21.457 1.315   -30.245 1.00 25.37  -1 56   ASP B OD2 1 
ATOM   3832  N  N   . ASP B  1 26  ? -22.336 1.177   -25.330 1.00 21.49  ?  57   ASP B N   1 
ATOM   3833  C  CA  . ASP B  1 26  ? -21.382 1.521   -24.227 1.00 24.11  ?  57   ASP B CA  1 
ATOM   3834  C  C   . ASP B  1 26  ? -22.015 2.537   -23.262 1.00 22.45  ?  57   ASP B C   1 
ATOM   3835  O  O   . ASP B  1 26  ? -21.295 3.382   -22.725 1.00 21.49  ?  57   ASP B O   1 
ATOM   3836  C  CB  . ASP B  1 26  ? -20.041 2.025   -24.735 1.00 22.38  ?  57   ASP B CB  1 
ATOM   3837  C  CG  . ASP B  1 26  ? -19.202 1.038   -25.537 1.00 26.52  ?  57   ASP B CG  1 
ATOM   3838  O  OD1 . ASP B  1 26  ? -19.629 -0.125  -25.679 1.00 22.68  ?  57   ASP B OD1 1 
ATOM   3839  O  OD2 . ASP B  1 26  ? -18.111 1.440   -25.997 1.00 25.95  -1 57   ASP B OD2 1 
ATOM   3840  N  N   . LEU B  1 27  ? -23.334 2.473   -23.079 1.00 20.09  ?  58   LEU B N   1 
ATOM   3841  C  CA  . LEU B  1 27  ? -23.958 3.321   -22.063 1.00 22.33  ?  58   LEU B CA  1 
ATOM   3842  C  C   . LEU B  1 27  ? -23.709 2.767   -20.660 1.00 23.24  ?  58   LEU B C   1 
ATOM   3843  O  O   . LEU B  1 27  ? -24.022 1.602   -20.374 1.00 22.70  ?  58   LEU B O   1 
ATOM   3844  C  CB  . LEU B  1 27  ? -25.463 3.433   -22.323 1.00 20.60  ?  58   LEU B CB  1 
ATOM   3845  C  CG  . LEU B  1 27  ? -26.269 4.217   -21.271 1.00 20.56  ?  58   LEU B CG  1 
ATOM   3846  C  CD1 . LEU B  1 27  ? -25.968 5.743   -21.349 1.00 21.26  ?  58   LEU B CD1 1 
ATOM   3847  C  CD2 . LEU B  1 27  ? -27.770 3.946   -21.461 1.00 25.98  ?  58   LEU B CD2 1 
ATOM   3848  N  N   . GLY B  1 28  ? -23.157 3.621   -19.778 1.00 20.60  ?  59   GLY B N   1 
ATOM   3849  C  CA  . GLY B  1 28  ? -22.823 3.206   -18.429 1.00 23.74  ?  59   GLY B CA  1 
ATOM   3850  C  C   . GLY B  1 28  ? -24.041 3.025   -17.537 1.00 21.71  ?  59   GLY B C   1 
ATOM   3851  O  O   . GLY B  1 28  ? -25.117 3.568   -17.782 1.00 22.57  ?  59   GLY B O   1 
ATOM   3852  N  N   . TYR B  1 29  ? -23.855 2.222   -16.479 1.00 23.88  ?  60   TYR B N   1 
ATOM   3853  C  CA  . TYR B  1 29  ? -24.983 1.801   -15.641 1.00 24.21  ?  60   TYR B CA  1 
ATOM   3854  C  C   . TYR B  1 29  ? -25.632 2.987   -14.934 1.00 26.72  ?  60   TYR B C   1 
ATOM   3855  O  O   . TYR B  1 29  ? -26.851 3.020   -14.757 1.00 25.29  ?  60   TYR B O   1 
ATOM   3856  C  CB  . TYR B  1 29  ? -24.516 0.784   -14.595 1.00 18.41  ?  60   TYR B CB  1 
ATOM   3857  C  CG  . TYR B  1 29  ? -25.603 -0.133  -14.070 1.00 24.15  ?  60   TYR B CG  1 
ATOM   3858  C  CD1 . TYR B  1 29  ? -26.335 -0.959  -14.939 1.00 22.44  ?  60   TYR B CD1 1 
ATOM   3859  C  CD2 . TYR B  1 29  ? -25.941 -0.143  -12.712 1.00 24.40  ?  60   TYR B CD2 1 
ATOM   3860  C  CE1 . TYR B  1 29  ? -27.336 -1.803  -14.447 1.00 24.23  ?  60   TYR B CE1 1 
ATOM   3861  C  CE2 . TYR B  1 29  ? -26.934 -0.989  -12.209 1.00 22.29  ?  60   TYR B CE2 1 
ATOM   3862  C  CZ  . TYR B  1 29  ? -27.632 -1.808  -13.079 1.00 26.41  ?  60   TYR B CZ  1 
ATOM   3863  O  OH  . TYR B  1 29  ? -28.631 -2.645  -12.598 1.00 26.15  ?  60   TYR B OH  1 
ATOM   3864  N  N   . ALA B  1 30  ? -24.827 3.951   -14.494 1.00 22.23  ?  61   ALA B N   1 
ATOM   3865  C  CA  . ALA B  1 30  ? -25.310 5.102   -13.743 1.00 24.39  ?  61   ALA B CA  1 
ATOM   3866  C  C   . ALA B  1 30  ? -25.506 6.328   -14.625 1.00 25.79  ?  61   ALA B C   1 
ATOM   3867  O  O   . ALA B  1 30  ? -25.422 7.457   -14.139 1.00 28.07  ?  61   ALA B O   1 
ATOM   3868  C  CB  . ALA B  1 30  ? -24.335 5.416   -12.597 1.00 23.22  ?  61   ALA B CB  1 
ATOM   3869  N  N   . ASP B  1 31  ? -25.739 6.140   -15.923 1.00 22.62  ?  62   ASP B N   1 
ATOM   3870  C  CA  . ASP B  1 31  ? -25.677 7.242   -16.876 1.00 22.86  ?  62   ASP B CA  1 
ATOM   3871  C  C   . ASP B  1 31  ? -27.025 7.599   -17.491 1.00 24.65  ?  62   ASP B C   1 
ATOM   3872  O  O   . ASP B  1 31  ? -27.065 8.359   -18.464 1.00 23.43  ?  62   ASP B O   1 
ATOM   3873  C  CB  . ASP B  1 31  ? -24.635 6.925   -17.958 1.00 19.05  ?  62   ASP B CB  1 
ATOM   3874  C  CG  . ASP B  1 31  ? -23.232 6.933   -17.379 1.00 25.61  ?  62   ASP B CG  1 
ATOM   3875  O  OD1 . ASP B  1 31  ? -23.101 7.542   -16.304 1.00 24.44  ?  62   ASP B OD1 1 
ATOM   3876  O  OD2 . ASP B  1 31  ? -22.288 6.348   -17.960 1.00 26.65  -1 62   ASP B OD2 1 
ATOM   3877  N  N   . VAL B  1 32  ? -28.125 7.100   -16.925 1.00 23.38  ?  63   VAL B N   1 
ATOM   3878  C  CA  . VAL B  1 32  ? -29.461 7.596   -17.217 1.00 24.33  ?  63   VAL B CA  1 
ATOM   3879  C  C   . VAL B  1 32  ? -30.150 7.886   -15.885 1.00 26.86  ?  63   VAL B C   1 
ATOM   3880  O  O   . VAL B  1 32  ? -29.860 7.254   -14.864 1.00 27.50  ?  63   VAL B O   1 
ATOM   3881  C  CB  . VAL B  1 32  ? -30.289 6.597   -18.070 1.00 23.22  ?  63   VAL B CB  1 
ATOM   3882  C  CG1 . VAL B  1 32  ? -29.712 6.473   -19.455 1.00 26.58  ?  63   VAL B CG1 1 
ATOM   3883  C  CG2 . VAL B  1 32  ? -30.339 5.215   -17.408 1.00 24.84  ?  63   VAL B CG2 1 
ATOM   3884  N  N   . GLY B  1 33  ? -31.067 8.853   -15.895 1.00 29.15  ?  64   GLY B N   1 
ATOM   3885  C  CA  . GLY B  1 33  ? -31.671 9.286   -14.639 1.00 30.35  ?  64   GLY B CA  1 
ATOM   3886  C  C   . GLY B  1 33  ? -32.380 8.159   -13.910 1.00 29.87  ?  64   GLY B C   1 
ATOM   3887  O  O   . GLY B  1 33  ? -32.199 7.976   -12.703 1.00 32.04  ?  64   GLY B O   1 
ATOM   3888  N  N   . PHE B  1 34  ? -33.152 7.352   -14.641 1.00 28.44  ?  65   PHE B N   1 
ATOM   3889  C  CA  . PHE B  1 34  ? -33.948 6.315   -13.988 1.00 27.38  ?  65   PHE B CA  1 
ATOM   3890  C  C   . PHE B  1 34  ? -33.083 5.219   -13.370 1.00 31.10  ?  65   PHE B C   1 
ATOM   3891  O  O   . PHE B  1 34  ? -33.573 4.455   -12.530 1.00 27.33  ?  65   PHE B O   1 
ATOM   3892  C  CB  . PHE B  1 34  ? -34.968 5.727   -14.986 1.00 27.79  ?  65   PHE B CB  1 
ATOM   3893  C  CG  . PHE B  1 34  ? -34.364 4.824   -16.054 1.00 24.80  ?  65   PHE B CG  1 
ATOM   3894  C  CD1 . PHE B  1 34  ? -34.116 3.473   -15.797 1.00 21.25  ?  65   PHE B CD1 1 
ATOM   3895  C  CD2 . PHE B  1 34  ? -34.072 5.327   -17.314 1.00 26.67  ?  65   PHE B CD2 1 
ATOM   3896  C  CE1 . PHE B  1 34  ? -33.579 2.643   -16.777 1.00 22.72  ?  65   PHE B CE1 1 
ATOM   3897  C  CE2 . PHE B  1 34  ? -33.517 4.503   -18.316 1.00 26.09  ?  65   PHE B CE2 1 
ATOM   3898  C  CZ  . PHE B  1 34  ? -33.261 3.166   -18.040 1.00 22.01  ?  65   PHE B CZ  1 
ATOM   3899  N  N   . ASN B  1 35  ? -31.811 5.114   -13.760 1.00 26.78  ?  66   ASN B N   1 
ATOM   3900  C  CA  . ASN B  1 35  ? -30.949 4.092   -13.190 1.00 27.21  ?  66   ASN B CA  1 
ATOM   3901  C  C   . ASN B  1 35  ? -29.890 4.694   -12.279 1.00 29.52  ?  66   ASN B C   1 
ATOM   3902  O  O   . ASN B  1 35  ? -28.889 4.037   -11.983 1.00 30.73  ?  66   ASN B O   1 
ATOM   3903  C  CB  . ASN B  1 35  ? -30.296 3.243   -14.286 1.00 24.42  ?  66   ASN B CB  1 
ATOM   3904  C  CG  . ASN B  1 35  ? -30.184 1.794   -13.891 1.00 28.41  ?  66   ASN B CG  1 
ATOM   3905  O  OD1 . ASN B  1 35  ? -31.152 1.214   -13.385 1.00 30.09  ?  66   ASN B OD1 1 
ATOM   3906  N  ND2 . ASN B  1 35  ? -29.002 1.193   -14.092 1.00 27.45  ?  66   ASN B ND2 1 
ATOM   3907  N  N   . GLY B  1 36  ? -30.086 5.933   -11.838 1.00 27.51  ?  67   GLY B N   1 
ATOM   3908  C  CA  . GLY B  1 36  ? -29.282 6.503   -10.772 1.00 30.38  ?  67   GLY B CA  1 
ATOM   3909  C  C   . GLY B  1 36  ? -28.418 7.686   -11.146 1.00 27.04  ?  67   GLY B C   1 
ATOM   3910  O  O   . GLY B  1 36  ? -27.684 8.174   -10.280 1.00 32.52  ?  67   GLY B O   1 
ATOM   3911  N  N   . SER B  1 37  ? -28.433 8.193   -12.370 1.00 30.05  ?  68   SER B N   1 
ATOM   3912  C  CA  . SER B  1 37  ? -27.534 9.290   -12.703 1.00 28.61  ?  68   SER B CA  1 
ATOM   3913  C  C   . SER B  1 37  ? -27.908 10.536  -11.920 1.00 33.11  ?  68   SER B C   1 
ATOM   3914  O  O   . SER B  1 37  ? -29.075 10.904  -11.851 1.00 27.50  ?  68   SER B O   1 
ATOM   3915  C  CB  . SER B  1 37  ? -27.561 9.607   -14.203 1.00 27.79  ?  68   SER B CB  1 
ATOM   3916  O  OG  . SER B  1 37  ? -26.505 10.518  -14.509 1.00 29.68  ?  68   SER B OG  1 
ATOM   3917  N  N   . THR B  1 38  ? -26.909 11.186  -11.329 1.00 33.19  ?  69   THR B N   1 
ATOM   3918  C  CA  . THR B  1 38  ? -27.150 12.476  -10.709 1.00 36.97  ?  69   THR B CA  1 
ATOM   3919  C  C   . THR B  1 38  ? -26.722 13.646  -11.588 1.00 36.13  ?  69   THR B C   1 
ATOM   3920  O  O   . THR B  1 38  ? -27.173 14.768  -11.353 1.00 37.74  ?  69   THR B O   1 
ATOM   3921  C  CB  . THR B  1 38  ? -26.448 12.541  -9.343  1.00 39.32  ?  69   THR B CB  1 
ATOM   3922  O  OG1 . THR B  1 38  ? -25.027 12.457  -9.522  1.00 39.87  ?  69   THR B OG1 1 
ATOM   3923  C  CG2 . THR B  1 38  ? -26.901 11.361  -8.469  1.00 37.92  ?  69   THR B CG2 1 
ATOM   3924  N  N   . ASP B  1 39  ? -25.902 13.422  -12.614 1.00 31.71  ?  70   ASP B N   1 
ATOM   3925  C  CA  . ASP B  1 39  ? -25.443 14.539  -13.435 1.00 27.23  ?  70   ASP B CA  1 
ATOM   3926  C  C   . ASP B  1 39  ? -25.933 14.491  -14.871 1.00 32.12  ?  70   ASP B C   1 
ATOM   3927  O  O   . ASP B  1 39  ? -26.076 15.545  -15.491 1.00 32.91  ?  70   ASP B O   1 
ATOM   3928  C  CB  . ASP B  1 39  ? -23.904 14.642  -13.423 1.00 31.09  ?  70   ASP B CB  1 
ATOM   3929  C  CG  . ASP B  1 39  ? -23.206 13.320  -13.755 1.00 34.15  ?  70   ASP B CG  1 
ATOM   3930  O  OD1 . ASP B  1 39  ? -23.866 12.260  -13.757 1.00 32.34  ?  70   ASP B OD1 1 
ATOM   3931  O  OD2 . ASP B  1 39  ? -21.980 13.340  -14.005 1.00 34.61  -1 70   ASP B OD2 1 
ATOM   3932  N  N   . ILE B  1 40  ? -26.239 13.321  -15.408 1.00 30.43  ?  71   ILE B N   1 
ATOM   3933  C  CA  . ILE B  1 40  ? -26.730 13.237  -16.772 1.00 27.01  ?  71   ILE B CA  1 
ATOM   3934  C  C   . ILE B  1 40  ? -28.252 13.315  -16.755 1.00 30.38  ?  71   ILE B C   1 
ATOM   3935  O  O   . ILE B  1 40  ? -28.913 12.532  -16.072 1.00 29.92  ?  71   ILE B O   1 
ATOM   3936  C  CB  . ILE B  1 40  ? -26.247 11.949  -17.453 1.00 27.86  ?  71   ILE B CB  1 
ATOM   3937  C  CG1 . ILE B  1 40  ? -24.712 11.881  -17.450 1.00 24.36  ?  71   ILE B CG1 1 
ATOM   3938  C  CG2 . ILE B  1 40  ? -26.746 11.919  -18.887 1.00 22.41  ?  71   ILE B CG2 1 
ATOM   3939  C  CD1 . ILE B  1 40  ? -24.196 10.653  -18.208 1.00 22.54  ?  71   ILE B CD1 1 
ATOM   3940  N  N   . LEU B  1 41  ? -28.805 14.235  -17.533 1.00 30.29  ?  72   LEU B N   1 
ATOM   3941  C  CA  . LEU B  1 41  ? -30.241 14.490  -17.568 1.00 29.76  ?  72   LEU B CA  1 
ATOM   3942  C  C   . LEU B  1 41  ? -30.876 13.714  -18.722 1.00 27.60  ?  72   LEU B C   1 
ATOM   3943  O  O   . LEU B  1 41  ? -30.492 13.897  -19.882 1.00 27.62  ?  72   LEU B O   1 
ATOM   3944  C  CB  . LEU B  1 41  ? -30.495 15.990  -17.718 1.00 29.61  ?  72   LEU B CB  1 
ATOM   3945  C  CG  . LEU B  1 41  ? -29.971 16.867  -16.577 1.00 40.12  ?  72   LEU B CG  1 
ATOM   3946  C  CD1 . LEU B  1 41  ? -30.148 18.353  -16.896 1.00 44.35  ?  72   LEU B CD1 1 
ATOM   3947  C  CD2 . LEU B  1 41  ? -30.677 16.510  -15.271 1.00 39.39  ?  72   LEU B CD2 1 
ATOM   3948  N  N   . THR B  1 42  ? -31.812 12.821  -18.401 1.00 23.82  ?  73   THR B N   1 
ATOM   3949  C  CA  . THR B  1 42  ? -32.521 12.025  -19.403 1.00 25.36  ?  73   THR B CA  1 
ATOM   3950  C  C   . THR B  1 42  ? -34.021 12.061  -19.111 1.00 26.24  ?  73   THR B C   1 
ATOM   3951  O  O   . THR B  1 42  ? -34.647 11.024  -18.881 1.00 28.27  ?  73   THR B O   1 
ATOM   3952  C  CB  . THR B  1 42  ? -32.000 10.586  -19.431 1.00 25.12  ?  73   THR B CB  1 
ATOM   3953  O  OG1 . THR B  1 42  ? -32.187 9.983   -18.147 1.00 26.38  ?  73   THR B OG1 1 
ATOM   3954  C  CG2 . THR B  1 42  ? -30.460 10.561  -19.744 1.00 24.36  ?  73   THR B CG2 1 
ATOM   3955  N  N   . PRO B  1 43  ? -34.638 13.245  -19.170 1.00 27.67  ?  74   PRO B N   1 
ATOM   3956  C  CA  . PRO B  1 43  ? -36.059 13.352  -18.784 1.00 29.00  ?  74   PRO B CA  1 
ATOM   3957  C  C   . PRO B  1 43  ? -37.025 12.522  -19.632 1.00 29.14  ?  74   PRO B C   1 
ATOM   3958  O  O   . PRO B  1 43  ? -38.020 12.010  -19.098 1.00 27.49  ?  74   PRO B O   1 
ATOM   3959  C  CB  . PRO B  1 43  ? -36.330 14.856  -18.935 1.00 31.37  ?  74   PRO B CB  1 
ATOM   3960  C  CG  . PRO B  1 43  ? -35.366 15.294  -19.987 1.00 29.78  ?  74   PRO B CG  1 
ATOM   3961  C  CD  . PRO B  1 43  ? -34.112 14.541  -19.632 1.00 27.44  ?  74   PRO B CD  1 
ATOM   3962  N  N   . GLU B  1 44  ? -36.776 12.376  -20.935 1.00 27.23  ?  75   GLU B N   1 
ATOM   3963  C  CA  . GLU B  1 44  ? -37.727 11.647  -21.779 1.00 27.23  ?  75   GLU B CA  1 
ATOM   3964  C  C   . GLU B  1 44  ? -37.635 10.150  -21.525 1.00 29.46  ?  75   GLU B C   1 
ATOM   3965  O  O   . GLU B  1 44  ? -38.656 9.460   -21.456 1.00 27.66  ?  75   GLU B O   1 
ATOM   3966  C  CB  . GLU B  1 44  ? -37.478 11.948  -23.263 1.00 27.42  ?  75   GLU B CB  1 
ATOM   3967  C  CG  . GLU B  1 44  ? -37.604 13.422  -23.648 1.00 25.78  ?  75   GLU B CG  1 
ATOM   3968  C  CD  . GLU B  1 44  ? -39.050 13.915  -23.645 1.00 30.44  ?  75   GLU B CD  1 
ATOM   3969  O  OE1 . GLU B  1 44  ? -39.987 13.091  -23.593 1.00 31.56  ?  75   GLU B OE1 1 
ATOM   3970  O  OE2 . GLU B  1 44  ? -39.238 15.140  -23.717 1.00 36.17  -1 75   GLU B OE2 1 
ATOM   3971  N  N   . LEU B  1 45  ? -36.410 9.631   -21.381 1.00 27.21  ?  76   LEU B N   1 
ATOM   3972  C  CA  . LEU B  1 45  ? -36.224 8.240   -20.992 1.00 27.40  ?  76   LEU B CA  1 
ATOM   3973  C  C   . LEU B  1 45  ? -36.758 7.990   -19.591 1.00 28.14  ?  76   LEU B C   1 
ATOM   3974  O  O   . LEU B  1 45  ? -37.404 6.961   -19.344 1.00 29.65  ?  76   LEU B O   1 
ATOM   3975  C  CB  . LEU B  1 45  ? -34.733 7.870   -21.058 1.00 27.04  ?  76   LEU B CB  1 
ATOM   3976  C  CG  . LEU B  1 45  ? -34.131 7.740   -22.465 1.00 29.98  ?  76   LEU B CG  1 
ATOM   3977  C  CD1 . LEU B  1 45  ? -32.588 7.854   -22.392 1.00 28.84  ?  76   LEU B CD1 1 
ATOM   3978  C  CD2 . LEU B  1 45  ? -34.580 6.468   -23.202 1.00 25.89  ?  76   LEU B CD2 1 
ATOM   3979  N  N   . ASP B  1 46  ? -36.453 8.893   -18.644 1.00 25.48  ?  77   ASP B N   1 
ATOM   3980  C  CA  . ASP B  1 46  ? -36.998 8.757   -17.297 1.00 25.70  ?  77   ASP B CA  1 
ATOM   3981  C  C   . ASP B  1 46  ? -38.518 8.682   -17.343 1.00 30.77  ?  77   ASP B C   1 
ATOM   3982  O  O   . ASP B  1 46  ? -39.119 7.854   -16.659 1.00 30.00  ?  77   ASP B O   1 
ATOM   3983  C  CB  . ASP B  1 46  ? -36.565 9.929   -16.425 1.00 27.58  ?  77   ASP B CB  1 
ATOM   3984  C  CG  . ASP B  1 46  ? -35.058 9.923   -16.165 1.00 30.65  ?  77   ASP B CG  1 
ATOM   3985  O  OD1 . ASP B  1 46  ? -34.393 8.973   -16.641 1.00 27.94  ?  77   ASP B OD1 1 
ATOM   3986  O  OD2 . ASP B  1 46  ? -34.556 10.845  -15.494 1.00 31.82  -1 77   ASP B OD2 1 
ATOM   3987  N  N   . ASN B  1 47  ? -39.145 9.507   -18.189 1.00 26.76  ?  78   ASN B N   1 
ATOM   3988  C  CA  . ASN B  1 47  ? -40.608 9.535   -18.284 1.00 28.67  ?  78   ASN B CA  1 
ATOM   3989  C  C   . ASN B  1 47  ? -41.153 8.183   -18.727 1.00 31.03  ?  78   ASN B C   1 
ATOM   3990  O  O   . ASN B  1 47  ? -42.113 7.659   -18.148 1.00 30.43  ?  78   ASN B O   1 
ATOM   3991  C  CB  . ASN B  1 47  ? -41.040 10.637  -19.257 1.00 30.84  ?  78   ASN B CB  1 
ATOM   3992  C  CG  . ASN B  1 47  ? -42.561 10.717  -19.431 1.00 38.55  ?  78   ASN B CG  1 
ATOM   3993  O  OD1 . ASN B  1 47  ? -43.290 10.906  -18.459 1.00 44.41  ?  78   ASN B OD1 1 
ATOM   3994  N  ND2 . ASN B  1 47  ? -43.034 10.593  -20.667 1.00 44.21  ?  78   ASN B ND2 1 
ATOM   3995  N  N   . LEU B  1 48  ? -40.552 7.601   -19.759 1.00 26.43  ?  79   LEU B N   1 
ATOM   3996  C  CA  . LEU B  1 48  ? -40.954 6.268   -20.189 1.00 25.94  ?  79   LEU B CA  1 
ATOM   3997  C  C   . LEU B  1 48  ? -40.691 5.234   -19.102 1.00 27.80  ?  79   LEU B C   1 
ATOM   3998  O  O   . LEU B  1 48  ? -41.534 4.369   -18.839 1.00 29.36  ?  79   LEU B O   1 
ATOM   3999  C  CB  . LEU B  1 48  ? -40.198 5.891   -21.466 1.00 26.32  ?  79   LEU B CB  1 
ATOM   4000  C  CG  . LEU B  1 48  ? -40.565 6.612   -22.756 1.00 29.01  ?  79   LEU B CG  1 
ATOM   4001  C  CD1 . LEU B  1 48  ? -39.634 6.127   -23.879 1.00 24.40  ?  79   LEU B CD1 1 
ATOM   4002  C  CD2 . LEU B  1 48  ? -42.061 6.325   -23.094 1.00 26.61  ?  79   LEU B CD2 1 
ATOM   4003  N  N   . ALA B  1 49  ? -39.512 5.286   -18.472 1.00 26.08  ?  80   ALA B N   1 
ATOM   4004  C  CA  . ALA B  1 49  ? -39.195 4.291   -17.460 1.00 25.07  ?  80   ALA B CA  1 
ATOM   4005  C  C   . ALA B  1 49  ? -40.220 4.308   -16.333 1.00 27.85  ?  80   ALA B C   1 
ATOM   4006  O  O   . ALA B  1 49  ? -40.676 3.257   -15.881 1.00 25.54  ?  80   ALA B O   1 
ATOM   4007  C  CB  . ALA B  1 49  ? -37.785 4.529   -16.897 1.00 25.96  ?  80   ALA B CB  1 
ATOM   4008  N  N   . GLN B  1 50  ? -40.571 5.492   -15.833 1.00 28.87  ?  81   GLN B N   1 
ATOM   4009  C  CA  . GLN B  1 50  ? -41.461 5.471   -14.689 1.00 33.86  ?  81   GLN B CA  1 
ATOM   4010  C  C   . GLN B  1 50  ? -42.892 5.152   -15.089 1.00 32.76  ?  81   GLN B C   1 
ATOM   4011  O  O   . GLN B  1 50  ? -43.703 4.834   -14.216 1.00 33.69  ?  81   GLN B O   1 
ATOM   4012  C  CB  . GLN B  1 50  ? -41.384 6.785   -13.905 1.00 38.52  ?  81   GLN B CB  1 
ATOM   4013  C  CG  . GLN B  1 50  ? -41.091 7.999   -14.694 1.00 43.11  ?  81   GLN B CG  1 
ATOM   4014  C  CD  . GLN B  1 50  ? -40.685 9.198   -13.839 1.00 46.07  ?  81   GLN B CD  1 
ATOM   4015  O  OE1 . GLN B  1 50  ? -39.519 9.337   -13.447 1.00 47.64  ?  81   GLN B OE1 1 
ATOM   4016  N  NE2 . GLN B  1 50  ? -41.643 10.073  -13.558 1.00 49.30  ?  81   GLN B NE2 1 
ATOM   4017  N  N   . ASN B  1 51  ? -43.205 5.190   -16.382 1.00 30.79  ?  82   ASN B N   1 
ATOM   4018  C  CA  . ASN B  1 51  ? -44.510 4.774   -16.872 1.00 31.08  ?  82   ASN B CA  1 
ATOM   4019  C  C   . ASN B  1 51  ? -44.493 3.344   -17.398 1.00 31.89  ?  82   ASN B C   1 
ATOM   4020  O  O   . ASN B  1 51  ? -45.458 2.918   -18.033 1.00 31.28  ?  82   ASN B O   1 
ATOM   4021  C  CB  . ASN B  1 51  ? -45.014 5.741   -17.948 1.00 32.28  ?  82   ASN B CB  1 
ATOM   4022  C  CG  . ASN B  1 51  ? -45.467 7.068   -17.359 1.00 40.73  ?  82   ASN B CG  1 
ATOM   4023  O  OD1 . ASN B  1 51  ? -46.297 7.105   -16.448 1.00 43.99  ?  82   ASN B OD1 1 
ATOM   4024  N  ND2 . ASN B  1 51  ? -44.922 8.162   -17.873 1.00 44.47  ?  82   ASN B ND2 1 
ATOM   4025  N  N   . GLY B  1 52  ? -43.428 2.586   -17.119 1.00 29.64  ?  83   GLY B N   1 
ATOM   4026  C  CA  . GLY B  1 52  ? -43.395 1.163   -17.420 1.00 28.72  ?  83   GLY B CA  1 
ATOM   4027  C  C   . GLY B  1 52  ? -42.657 0.396   -16.341 1.00 31.41  ?  83   GLY B C   1 
ATOM   4028  O  O   . GLY B  1 52  ? -42.786 0.711   -15.157 1.00 31.80  ?  83   GLY B O   1 
ATOM   4029  N  N   . SER B  1 53  ? -41.858 -0.593  -16.736 1.00 30.09  ?  84   SER B N   1 
ATOM   4030  C  CA  . SER B  1 53  ? -41.134 -1.460  -15.815 1.00 27.89  ?  84   SER B CA  1 
ATOM   4031  C  C   . SER B  1 53  ? -39.631 -1.233  -15.954 1.00 27.19  ?  84   SER B C   1 
ATOM   4032  O  O   . SER B  1 53  ? -39.084 -1.396  -17.046 1.00 30.29  ?  84   SER B O   1 
ATOM   4033  C  CB  . SER B  1 53  ? -41.464 -2.922  -16.099 1.00 31.80  ?  84   SER B CB  1 
ATOM   4034  O  OG  . SER B  1 53  ? -40.843 -3.767  -15.156 1.00 31.68  ?  84   SER B OG  1 
ATOM   4035  N  N   . ILE B  1 54  ? -38.972 -0.885  -14.846 1.00 25.64  ?  85   ILE B N   1 
ATOM   4036  C  CA  . ILE B  1 54  ? -37.516 -0.745  -14.780 1.00 25.05  ?  85   ILE B CA  1 
ATOM   4037  C  C   . ILE B  1 54  ? -36.911 -2.072  -14.340 1.00 27.40  ?  85   ILE B C   1 
ATOM   4038  O  O   . ILE B  1 54  ? -37.279 -2.613  -13.290 1.00 31.16  ?  85   ILE B O   1 
ATOM   4039  C  CB  . ILE B  1 54  ? -37.123 0.382   -13.802 1.00 25.23  ?  85   ILE B CB  1 
ATOM   4040  C  CG1 . ILE B  1 54  ? -37.483 1.752   -14.382 1.00 28.97  ?  85   ILE B CG1 1 
ATOM   4041  C  CG2 . ILE B  1 54  ? -35.622 0.297   -13.448 1.00 25.40  ?  85   ILE B CG2 1 
ATOM   4042  C  CD1 . ILE B  1 54  ? -37.279 2.902   -13.408 1.00 25.64  ?  85   ILE B CD1 1 
ATOM   4043  N  N   . PHE B  1 55  ? -35.963 -2.598  -15.117 1.00 24.87  ?  86   PHE B N   1 
ATOM   4044  C  CA  . PHE B  1 55  ? -35.323 -3.870  -14.791 1.00 22.35  ?  86   PHE B CA  1 
ATOM   4045  C  C   . PHE B  1 55  ? -34.034 -3.594  -14.024 1.00 27.15  ?  86   PHE B C   1 
ATOM   4046  O  O   . PHE B  1 55  ? -33.069 -3.040  -14.581 1.00 24.17  ?  86   PHE B O   1 
ATOM   4047  C  CB  . PHE B  1 55  ? -35.059 -4.697  -16.046 1.00 21.37  ?  86   PHE B CB  1 
ATOM   4048  C  CG  . PHE B  1 55  ? -36.321 -5.225  -16.685 1.00 25.31  ?  86   PHE B CG  1 
ATOM   4049  C  CD1 . PHE B  1 55  ? -37.161 -4.365  -17.364 1.00 26.95  ?  86   PHE B CD1 1 
ATOM   4050  C  CD2 . PHE B  1 55  ? -36.680 -6.565  -16.575 1.00 24.99  ?  86   PHE B CD2 1 
ATOM   4051  C  CE1 . PHE B  1 55  ? -38.345 -4.826  -17.950 1.00 26.21  ?  86   PHE B CE1 1 
ATOM   4052  C  CE2 . PHE B  1 55  ? -37.850 -7.029  -17.148 1.00 31.16  ?  86   PHE B CE2 1 
ATOM   4053  C  CZ  . PHE B  1 55  ? -38.687 -6.155  -17.838 1.00 31.26  ?  86   PHE B CZ  1 
ATOM   4054  N  N   . THR B  1 56  ? -34.012 -3.999  -12.757 1.00 23.74  ?  87   THR B N   1 
ATOM   4055  C  CA  . THR B  1 56  ? -32.868 -3.679  -11.902 1.00 25.27  ?  87   THR B CA  1 
ATOM   4056  C  C   . THR B  1 56  ? -31.766 -4.731  -11.947 1.00 26.14  ?  87   THR B C   1 
ATOM   4057  O  O   . THR B  1 56  ? -30.672 -4.481  -11.413 1.00 25.86  ?  87   THR B O   1 
ATOM   4058  C  CB  . THR B  1 56  ? -33.309 -3.454  -10.442 1.00 28.21  ?  87   THR B CB  1 
ATOM   4059  O  OG1 . THR B  1 56  ? -33.820 -4.676  -9.875  1.00 24.53  ?  87   THR B OG1 1 
ATOM   4060  C  CG2 . THR B  1 56  ? -34.381 -2.325  -10.369 1.00 29.23  ?  87   THR B CG2 1 
ATOM   4061  N  N   . SER B  1 57  ? -32.005 -5.883  -12.577 1.00 26.91  ?  88   SER B N   1 
ATOM   4062  C  CA  . SER B  1 57  ? -30.967 -6.886  -12.820 1.00 26.94  ?  88   SER B CA  1 
ATOM   4063  C  C   . SER B  1 57  ? -31.047 -7.380  -14.275 1.00 26.62  ?  88   SER B C   1 
ATOM   4064  O  O   . SER B  1 57  ? -31.288 -8.560  -14.545 1.00 24.69  ?  88   SER B O   1 
ATOM   4065  C  CB  . SER B  1 57  ? -31.086 -8.070  -11.852 1.00 27.76  ?  88   SER B CB  1 
ATOM   4066  O  OG  . SER B  1 57  ? -30.468 -7.820  -10.590 1.00 27.49  ?  88   SER B OG  1 
ATOM   4067  N  N   . ALA B  1 58  ? -30.788 -6.480  -15.229 1.00 24.62  ?  89   ALA B N   1 
ATOM   4068  C  CA  . ALA B  1 58  ? -30.825 -6.831  -16.645 1.00 25.45  ?  89   ALA B CA  1 
ATOM   4069  C  C   . ALA B  1 58  ? -29.405 -7.066  -17.153 1.00 26.77  ?  89   ALA B C   1 
ATOM   4070  O  O   . ALA B  1 58  ? -28.512 -6.254  -16.893 1.00 25.13  ?  89   ALA B O   1 
ATOM   4071  C  CB  . ALA B  1 58  ? -31.512 -5.737  -17.471 1.00 23.17  ?  89   ALA B CB  1 
ATOM   4072  N  N   . TYR B  1 59  ? -29.211 -8.160  -17.907 1.00 25.27  ?  90   TYR B N   1 
ATOM   4073  C  CA  . TYR B  1 59  ? -27.903 -8.590  -18.384 1.00 25.93  ?  90   TYR B CA  1 
ATOM   4074  C  C   . TYR B  1 59  ? -27.902 -8.758  -19.898 1.00 26.49  ?  90   TYR B C   1 
ATOM   4075  O  O   . TYR B  1 59  ? -28.870 -9.258  -20.473 1.00 24.92  ?  90   TYR B O   1 
ATOM   4076  C  CB  . TYR B  1 59  ? -27.493 -9.919  -17.736 1.00 21.60  ?  90   TYR B CB  1 
ATOM   4077  C  CG  . TYR B  1 59  ? -27.308 -9.826  -16.257 1.00 26.84  ?  90   TYR B CG  1 
ATOM   4078  C  CD1 . TYR B  1 59  ? -26.105 -9.365  -15.714 1.00 23.51  ?  90   TYR B CD1 1 
ATOM   4079  C  CD2 . TYR B  1 59  ? -28.335 -10.178 -15.389 1.00 23.46  ?  90   TYR B CD2 1 
ATOM   4080  C  CE1 . TYR B  1 59  ? -25.931 -9.287  -14.344 1.00 26.53  ?  90   TYR B CE1 1 
ATOM   4081  C  CE2 . TYR B  1 59  ? -28.187 -10.084 -14.039 1.00 25.62  ?  90   TYR B CE2 1 
ATOM   4082  C  CZ  . TYR B  1 59  ? -26.976 -9.649  -13.506 1.00 24.62  ?  90   TYR B CZ  1 
ATOM   4083  O  OH  . TYR B  1 59  ? -26.828 -9.557  -12.146 1.00 27.53  ?  90   TYR B OH  1 
ATOM   4084  N  N   . VAL B  1 60  ? -26.803 -8.351  -20.542 1.00 25.85  ?  91   VAL B N   1 
ATOM   4085  C  CA  . VAL B  1 60  ? -26.535 -8.736  -21.922 1.00 25.56  ?  91   VAL B CA  1 
ATOM   4086  C  C   . VAL B  1 60  ? -25.675 -9.995  -21.900 1.00 23.96  ?  91   VAL B C   1 
ATOM   4087  O  O   . VAL B  1 60  ? -25.067 -10.343 -20.888 1.00 23.39  ?  91   VAL B O   1 
ATOM   4088  C  CB  . VAL B  1 60  ? -25.867 -7.596  -22.731 1.00 20.73  ?  91   VAL B CB  1 
ATOM   4089  C  CG1 . VAL B  1 60  ? -26.887 -6.458  -22.970 1.00 20.26  ?  91   VAL B CG1 1 
ATOM   4090  C  CG2 . VAL B  1 60  ? -24.675 -7.025  -21.990 1.00 22.60  ?  91   VAL B CG2 1 
ATOM   4091  N  N   . ALA B  1 61  ? -25.648 -10.705 -23.032 1.00 23.53  ?  92   ALA B N   1 
ATOM   4092  C  CA  . ALA B  1 61  ? -25.026 -12.020 -23.120 1.00 26.57  ?  92   ALA B CA  1 
ATOM   4093  C  C   . ALA B  1 61  ? -23.511 -11.975 -23.291 1.00 26.01  ?  92   ALA B C   1 
ATOM   4094  O  O   . ALA B  1 61  ? -22.879 -13.040 -23.310 1.00 27.72  ?  92   ALA B O   1 
ATOM   4095  C  CB  . ALA B  1 61  ? -25.655 -12.798 -24.286 1.00 28.24  ?  92   ALA B CB  1 
ATOM   4096  N  N   . HIS B  1 62  ? -22.915 -10.792 -23.448 1.00 24.46  ?  93   HIS B N   1 
ATOM   4097  C  CA  . HIS B  1 62  ? -21.461 -10.656 -23.538 1.00 22.93  ?  93   HIS B CA  1 
ATOM   4098  C  C   . HIS B  1 62  ? -21.107 -9.227  -23.144 1.00 22.84  ?  93   HIS B C   1 
ATOM   4099  O  O   . HIS B  1 62  ? -21.882 -8.315  -23.418 1.00 24.25  ?  93   HIS B O   1 
ATOM   4100  C  CB  . HIS B  1 62  ? -20.956 -10.966 -24.960 1.00 22.56  ?  93   HIS B CB  1 
ATOM   4101  C  CG  . HIS B  1 62  ? -19.508 -11.354 -25.037 1.00 25.21  ?  93   HIS B CG  1 
ATOM   4102  N  ND1 . HIS B  1 62  ? -19.058 -12.611 -24.698 1.00 27.12  ?  93   HIS B ND1 1 
ATOM   4103  C  CD2 . HIS B  1 62  ? -18.417 -10.671 -25.465 1.00 21.08  ?  93   HIS B CD2 1 
ATOM   4104  C  CE1 . HIS B  1 62  ? -17.747 -12.676 -24.876 1.00 27.92  ?  93   HIS B CE1 1 
ATOM   4105  N  NE2 . HIS B  1 62  ? -17.336 -11.513 -25.350 1.00 24.80  ?  93   HIS B NE2 1 
ATOM   4106  N  N   . PRO B  1 63  ? -19.950 -8.995  -22.497 1.00 24.39  ?  94   PRO B N   1 
ATOM   4107  C  CA  . PRO B  1 63  ? -19.642 -7.627  -22.048 1.00 23.25  ?  94   PRO B CA  1 
ATOM   4108  C  C   . PRO B  1 63  ? -19.067 -6.702  -23.117 1.00 25.52  ?  94   PRO B C   1 
ATOM   4109  O  O   . PRO B  1 63  ? -18.523 -5.655  -22.753 1.00 24.29  ?  94   PRO B O   1 
ATOM   4110  C  CB  . PRO B  1 63  ? -18.638 -7.852  -20.917 1.00 23.37  ?  94   PRO B CB  1 
ATOM   4111  C  CG  . PRO B  1 63  ? -17.904 -9.131  -21.338 1.00 25.46  ?  94   PRO B CG  1 
ATOM   4112  C  CD  . PRO B  1 63  ? -18.997 -9.983  -21.980 1.00 23.21  ?  94   PRO B CD  1 
ATOM   4113  N  N   . PHE B  1 64  ? -19.207 -7.052  -24.407 1.00 24.60  ?  95   PHE B N   1 
ATOM   4114  C  CA  . PHE B  1 64  ? -18.789 -6.112  -25.498 1.00 24.84  ?  95   PHE B CA  1 
ATOM   4115  C  C   . PHE B  1 64  ? -19.737 -6.214  -26.724 1.00 29.14  ?  95   PHE B C   1 
ATOM   4116  O  O   . PHE B  1 64  ? -20.376 -7.257  -26.862 1.00 28.35  ?  95   PHE B O   1 
ATOM   4117  C  CB  . PHE B  1 64  ? -17.288 -6.086  -25.812 1.00 23.56  ?  95   PHE B CB  1 
ATOM   4118  C  CG  . PHE B  1 64  ? -16.558 -7.343  -26.247 1.00 28.19  ?  95   PHE B CG  1 
ATOM   4119  C  CD1 . PHE B  1 64  ? -16.555 -7.737  -27.576 1.00 25.13  ?  95   PHE B CD1 1 
ATOM   4120  C  CD2 . PHE B  1 64  ? -15.812 -8.077  -25.336 1.00 24.71  ?  95   PHE B CD2 1 
ATOM   4121  C  CE1 . PHE B  1 64  ? -15.863 -8.864  -27.972 1.00 24.18  ?  95   PHE B CE1 1 
ATOM   4122  C  CE2 . PHE B  1 64  ? -15.121 -9.203  -25.742 1.00 25.44  ?  95   PHE B CE2 1 
ATOM   4123  C  CZ  . PHE B  1 64  ? -15.151 -9.594  -27.056 1.00 27.64  ?  95   PHE B CZ  1 
HETATM 4124  N  N   . OSE B  1 65  ? -19.745 -5.202  -27.606 1.00 31.18  ?  96   OSE B N   1 
HETATM 4125  C  CA  . OSE B  1 65  ? -20.748 -5.056  -28.707 1.00 33.10  ?  96   OSE B CA  1 
HETATM 4126  C  CB  . OSE B  1 65  ? -20.361 -3.877  -29.580 1.00 36.66  ?  96   OSE B CB  1 
HETATM 4127  O  OG  . OSE B  1 65  ? -19.003 -3.975  -29.795 1.00 39.45  ?  96   OSE B OG  1 
HETATM 4128  C  C   . OSE B  1 65  ? -21.023 -6.239  -29.635 1.00 27.84  ?  96   OSE B C   1 
HETATM 4129  O  O   . OSE B  1 65  ? -22.166 -6.701  -29.651 1.00 28.07  ?  96   OSE B O   1 
HETATM 4130  S  S   . OSE B  1 65  ? -18.197 -2.893  -29.046 1.00 38.42  ?  96   OSE B S   1 
HETATM 4131  O  O1S . OSE B  1 65  ? -16.906 -3.510  -28.894 1.00 40.35  ?  96   OSE B O1S 1 
HETATM 4132  O  O2S . OSE B  1 65  ? -18.303 -1.849  -30.036 1.00 44.83  ?  96   OSE B O2S 1 
HETATM 4133  O  O3S . OSE B  1 65  ? -18.853 -2.585  -27.806 1.00 38.59  ?  96   OSE B O3S 1 
ATOM   4134  N  N   . GLY B  1 66  ? -20.043 -6.659  -30.419 1.00 31.53  ?  97   GLY B N   1 
ATOM   4135  C  CA  . GLY B  1 66  ? -20.282 -7.614  -31.502 1.00 28.93  ?  97   GLY B CA  1 
ATOM   4136  C  C   . GLY B  1 66  ? -21.001 -8.864  -31.029 1.00 28.78  ?  97   GLY B C   1 
ATOM   4137  O  O   . GLY B  1 66  ? -22.077 -9.200  -31.538 1.00 26.74  ?  97   GLY B O   1 
ATOM   4138  N  N   . PRO B  1 67  ? -20.403 -9.551  -30.052 1.00 27.76  ?  98   PRO B N   1 
ATOM   4139  C  CA  . PRO B  1 67  ? -21.059 -10.740 -29.485 1.00 24.09  ?  98   PRO B CA  1 
ATOM   4140  C  C   . PRO B  1 67  ? -22.383 -10.429 -28.806 1.00 24.80  ?  98   PRO B C   1 
ATOM   4141  O  O   . PRO B  1 67  ? -23.299 -11.259 -28.841 1.00 26.99  ?  98   PRO B O   1 
ATOM   4142  C  CB  . PRO B  1 67  ? -20.012 -11.268 -28.488 1.00 22.70  ?  98   PRO B CB  1 
ATOM   4143  C  CG  . PRO B  1 67  ? -18.686 -10.772 -29.061 1.00 28.04  ?  98   PRO B CG  1 
ATOM   4144  C  CD  . PRO B  1 67  ? -19.004 -9.414  -29.612 1.00 27.48  ?  98   PRO B CD  1 
ATOM   4145  N  N   . SER B  1 68  ? -22.504 -9.265  -28.157 1.00 26.63  ?  99   SER B N   1 
ATOM   4146  C  CA  . SER B  1 68  ? -23.772 -8.896  -27.535 1.00 26.16  ?  99   SER B CA  1 
ATOM   4147  C  C   . SER B  1 68  ? -24.849 -8.700  -28.589 1.00 24.72  ?  99   SER B C   1 
ATOM   4148  O  O   . SER B  1 68  ? -25.975 -9.195  -28.446 1.00 25.05  ?  99   SER B O   1 
ATOM   4149  C  CB  . SER B  1 68  ? -23.595 -7.627  -26.697 1.00 24.37  ?  99   SER B CB  1 
ATOM   4150  O  OG  . SER B  1 68  ? -24.829 -7.177  -26.174 1.00 23.93  ?  99   SER B OG  1 
ATOM   4151  N  N   . ARG B  1 69  ? -24.532 -7.943  -29.634 1.00 26.58  ?  100  ARG B N   1 
ATOM   4152  C  CA  . ARG B  1 69  ? -25.523 -7.680  -30.713 1.00 23.61  ?  100  ARG B CA  1 
ATOM   4153  C  C   . ARG B  1 69  ? -25.865 -9.013  -31.405 1.00 25.65  ?  100  ARG B C   1 
ATOM   4154  O  O   . ARG B  1 69  ? -27.056 -9.257  -31.653 1.00 28.55  ?  100  ARG B O   1 
ATOM   4155  C  CB  . ARG B  1 69  ? -24.954 -6.602  -31.630 1.00 25.86  ?  100  ARG B CB  1 
ATOM   4156  C  CG  . ARG B  1 69  ? -25.061 -5.192  -31.072 1.00 25.99  ?  100  ARG B CG  1 
ATOM   4157  C  CD  . ARG B  1 69  ? -23.938 -4.291  -31.544 1.00 23.65  ?  100  ARG B CD  1 
ATOM   4158  N  NE  . ARG B  1 69  ? -23.750 -3.117  -30.683 1.00 24.44  ?  100  ARG B NE  1 
ATOM   4159  C  CZ  . ARG B  1 69  ? -24.502 -2.023  -30.711 1.00 25.96  ?  100  ARG B CZ  1 
ATOM   4160  N  NH1 . ARG B  1 69  ? -25.423 -1.865  -31.648 1.00 22.23  ?  100  ARG B NH1 1 
ATOM   4161  N  NH2 . ARG B  1 69  ? -24.316 -1.077  -29.809 1.00 21.37  ?  100  ARG B NH2 1 
ATOM   4162  N  N   . SER B  1 70  ? -24.855 -9.827  -31.695 1.00 24.39  ?  101  SER B N   1 
ATOM   4163  C  CA  . SER B  1 70  ? -25.104 -11.156 -32.260 1.00 26.95  ?  101  SER B CA  1 
ATOM   4164  C  C   . SER B  1 70  ? -26.136 -11.916 -31.432 1.00 26.66  ?  101  SER B C   1 
ATOM   4165  O  O   . SER B  1 70  ? -27.095 -12.493 -31.971 1.00 30.18  ?  101  SER B O   1 
ATOM   4166  C  CB  . SER B  1 70  ? -23.781 -11.932 -32.326 1.00 29.08  ?  101  SER B CB  1 
ATOM   4167  O  OG  . SER B  1 70  ? -23.984 -13.292 -32.655 1.00 35.34  ?  101  SER B OG  1 
ATOM   4168  N  N   . ALA B  1 71  ? -25.965 -11.896 -30.109 1.00 26.67  ?  102  ALA B N   1 
ATOM   4169  C  CA  . ALA B  1 71  ? -26.871 -12.596 -29.202 1.00 28.34  ?  102  ALA B CA  1 
ATOM   4170  C  C   . ALA B  1 71  ? -28.269 -12.007 -29.242 1.00 27.79  ?  102  ALA B C   1 
ATOM   4171  O  O   . ALA B  1 71  ? -29.259 -12.738 -29.149 1.00 30.45  ?  102  ALA B O   1 
ATOM   4172  C  CB  . ALA B  1 71  ? -26.339 -12.535 -27.771 1.00 24.91  ?  102  ALA B CB  1 
ATOM   4173  N  N   . ILE B  1 72  ? -28.371 -10.681 -29.326 1.00 27.29  ?  103  ILE B N   1 
ATOM   4174  C  CA  . ILE B  1 72  ? -29.688 -10.045 -29.348 1.00 24.12  ?  103  ILE B CA  1 
ATOM   4175  C  C   . ILE B  1 72  ? -30.476 -10.501 -30.570 1.00 31.41  ?  103  ILE B C   1 
ATOM   4176  O  O   . ILE B  1 72  ? -31.648 -10.885 -30.473 1.00 29.17  ?  103  ILE B O   1 
ATOM   4177  C  CB  . ILE B  1 72  ? -29.537 -8.510  -29.306 1.00 24.76  ?  103  ILE B CB  1 
ATOM   4178  C  CG1 . ILE B  1 72  ? -29.125 -8.052  -27.894 1.00 26.81  ?  103  ILE B CG1 1 
ATOM   4179  C  CG2 . ILE B  1 72  ? -30.847 -7.825  -29.728 1.00 26.04  ?  103  ILE B CG2 1 
ATOM   4180  C  CD1 . ILE B  1 72  ? -28.916 -6.523  -27.808 1.00 24.16  ?  103  ILE B CD1 1 
ATOM   4181  N  N   . LEU B  1 73  ? -29.852 -10.478 -31.744 1.00 28.49  ?  104  LEU B N   1 
ATOM   4182  C  CA  A LEU B  1 73  ? -30.635 -10.768 -32.943 0.70 28.51  ?  104  LEU B CA  1 
ATOM   4183  C  CA  B LEU B  1 73  ? -30.627 -10.771 -32.945 0.30 28.52  ?  104  LEU B CA  1 
ATOM   4184  C  C   . LEU B  1 73  ? -30.800 -12.268 -33.176 1.00 30.51  ?  104  LEU B C   1 
ATOM   4185  O  O   . LEU B  1 73  ? -31.862 -12.698 -33.636 1.00 31.91  ?  104  LEU B O   1 
ATOM   4186  C  CB  A LEU B  1 73  ? -30.007 -10.076 -34.155 0.70 28.15  ?  104  LEU B CB  1 
ATOM   4187  C  CB  B LEU B  1 73  ? -29.985 -10.089 -34.151 0.30 28.23  ?  104  LEU B CB  1 
ATOM   4188  C  CG  A LEU B  1 73  ? -30.407 -8.590  -34.241 0.70 30.08  ?  104  LEU B CG  1 
ATOM   4189  C  CG  B LEU B  1 73  ? -30.356 -8.602  -34.135 0.30 29.97  ?  104  LEU B CG  1 
ATOM   4190  C  CD1 A LEU B  1 73  ? -29.645 -7.834  -35.309 0.70 26.21  ?  104  LEU B CD1 1 
ATOM   4191  C  CD1 B LEU B  1 73  ? -29.154 -7.727  -33.854 0.30 28.08  ?  104  LEU B CD1 1 
ATOM   4192  C  CD2 A LEU B  1 73  ? -31.921 -8.439  -34.485 0.70 29.87  ?  104  LEU B CD2 1 
ATOM   4193  C  CD2 B LEU B  1 73  ? -31.048 -8.188  -35.431 0.30 28.65  ?  104  LEU B CD2 1 
ATOM   4194  N  N   . THR B  1 74  ? -29.797 -13.085 -32.841 1.00 28.13  ?  105  THR B N   1 
ATOM   4195  C  CA  . THR B  1 74  ? -29.944 -14.539 -32.966 1.00 28.19  ?  105  THR B CA  1 
ATOM   4196  C  C   . THR B  1 74  ? -30.647 -15.190 -31.774 1.00 31.65  ?  105  THR B C   1 
ATOM   4197  O  O   . THR B  1 74  ? -31.136 -16.321 -31.894 1.00 28.53  ?  105  THR B O   1 
ATOM   4198  C  CB  . THR B  1 74  ? -28.587 -15.212 -33.136 1.00 30.77  ?  105  THR B CB  1 
ATOM   4199  O  OG1 . THR B  1 74  ? -27.836 -15.144 -31.909 1.00 30.50  ?  105  THR B OG1 1 
ATOM   4200  C  CG2 . THR B  1 74  ? -27.805 -14.574 -34.287 1.00 30.47  ?  105  THR B CG2 1 
ATOM   4201  N  N   . GLY B  1 75  ? -30.694 -14.526 -30.620 1.00 29.79  ?  106  GLY B N   1 
ATOM   4202  C  CA  . GLY B  1 75  ? -31.243 -15.174 -29.447 1.00 29.38  ?  106  GLY B CA  1 
ATOM   4203  C  C   . GLY B  1 75  ? -30.412 -16.293 -28.865 1.00 27.95  ?  106  GLY B C   1 
ATOM   4204  O  O   . GLY B  1 75  ? -30.917 -17.056 -28.037 1.00 28.58  ?  106  GLY B O   1 
ATOM   4205  N  N   . ARG B  1 76  ? -29.135 -16.400 -29.232 1.00 29.23  ?  107  ARG B N   1 
ATOM   4206  C  CA  . ARG B  1 76  ? -28.256 -17.398 -28.638 1.00 28.91  ?  107  ARG B CA  1 
ATOM   4207  C  C   . ARG B  1 76  ? -26.981 -16.743 -28.125 1.00 27.96  ?  107  ARG B C   1 
ATOM   4208  O  O   . ARG B  1 76  ? -26.523 -15.731 -28.667 1.00 29.86  ?  107  ARG B O   1 
ATOM   4209  C  CB  . ARG B  1 76  ? -27.892 -18.501 -29.640 1.00 29.37  ?  107  ARG B CB  1 
ATOM   4210  C  CG  . ARG B  1 76  ? -29.120 -19.143 -30.309 1.00 34.16  ?  107  ARG B CG  1 
ATOM   4211  C  CD  . ARG B  1 76  ? -28.695 -20.238 -31.264 1.00 32.64  ?  107  ARG B CD  1 
ATOM   4212  N  NE  . ARG B  1 76  ? -28.223 -21.419 -30.549 1.00 41.11  ?  107  ARG B NE  1 
ATOM   4213  C  CZ  . ARG B  1 76  ? -27.549 -22.412 -31.115 1.00 39.17  ?  107  ARG B CZ  1 
ATOM   4214  N  NH1 . ARG B  1 76  ? -27.204 -22.376 -32.395 1.00 37.98  ?  107  ARG B NH1 1 
ATOM   4215  N  NH2 . ARG B  1 76  ? -27.213 -23.466 -30.380 1.00 42.33  ?  107  ARG B NH2 1 
ATOM   4216  N  N   . TYR B  1 77  ? -26.406 -17.342 -27.084 1.00 28.79  ?  108  TYR B N   1 
ATOM   4217  C  CA  . TYR B  1 77  ? -25.082 -16.928 -26.622 1.00 25.51  ?  108  TYR B CA  1 
ATOM   4218  C  C   . TYR B  1 77  ? -24.084 -16.972 -27.780 1.00 31.29  ?  108  TYR B C   1 
ATOM   4219  O  O   . TYR B  1 77  ? -24.151 -17.878 -28.629 1.00 29.44  ?  108  TYR B O   1 
ATOM   4220  C  CB  . TYR B  1 77  ? -24.591 -17.845 -25.494 1.00 28.83  ?  108  TYR B CB  1 
ATOM   4221  C  CG  . TYR B  1 77  ? -25.134 -17.522 -24.130 1.00 29.87  ?  108  TYR B CG  1 
ATOM   4222  C  CD1 . TYR B  1 77  ? -24.686 -16.407 -23.416 1.00 26.66  ?  108  TYR B CD1 1 
ATOM   4223  C  CD2 . TYR B  1 77  ? -26.113 -18.326 -23.546 1.00 30.02  ?  108  TYR B CD2 1 
ATOM   4224  C  CE1 . TYR B  1 77  ? -25.201 -16.111 -22.129 1.00 30.28  ?  108  TYR B CE1 1 
ATOM   4225  C  CE2 . TYR B  1 77  ? -26.625 -18.032 -22.268 1.00 29.87  ?  108  TYR B CE2 1 
ATOM   4226  C  CZ  . TYR B  1 77  ? -26.161 -16.922 -21.573 1.00 26.75  ?  108  TYR B CZ  1 
ATOM   4227  O  OH  . TYR B  1 77  ? -26.685 -16.618 -20.328 1.00 27.62  ?  108  TYR B OH  1 
ATOM   4228  N  N   . PRO B  1 78  ? -23.141 -16.026 -27.849 1.00 30.59  ?  109  PRO B N   1 
ATOM   4229  C  CA  . PRO B  1 78  ? -22.222 -15.999 -28.992 1.00 28.48  ?  109  PRO B CA  1 
ATOM   4230  C  C   . PRO B  1 78  ? -21.249 -17.158 -29.001 1.00 30.94  ?  109  PRO B C   1 
ATOM   4231  O  O   . PRO B  1 78  ? -20.628 -17.412 -30.038 1.00 31.72  ?  109  PRO B O   1 
ATOM   4232  C  CB  . PRO B  1 78  ? -21.484 -14.664 -28.821 1.00 30.27  ?  109  PRO B CB  1 
ATOM   4233  C  CG  . PRO B  1 78  ? -21.538 -14.402 -27.353 1.00 28.08  ?  109  PRO B CG  1 
ATOM   4234  C  CD  . PRO B  1 78  ? -22.921 -14.886 -26.936 1.00 27.02  ?  109  PRO B CD  1 
ATOM   4235  N  N   . HIS B  1 79  ? -21.069 -17.831 -27.865 1.00 30.52  ?  110  HIS B N   1 
ATOM   4236  C  CA  . HIS B  1 79  ? -20.215 -19.007 -27.771 1.00 32.74  ?  110  HIS B CA  1 
ATOM   4237  C  C   . HIS B  1 79  ? -20.824 -20.210 -28.478 1.00 32.87  ?  110  HIS B C   1 
ATOM   4238  O  O   . HIS B  1 79  ? -20.123 -21.206 -28.695 1.00 29.85  ?  110  HIS B O   1 
ATOM   4239  C  CB  . HIS B  1 79  ? -19.971 -19.345 -26.303 1.00 29.00  ?  110  HIS B CB  1 
ATOM   4240  C  CG  . HIS B  1 79  ? -19.831 -18.137 -25.421 1.00 30.32  ?  110  HIS B CG  1 
ATOM   4241  N  ND1 . HIS B  1 79  ? -20.898 -17.336 -25.079 1.00 27.40  ?  110  HIS B ND1 1 
ATOM   4242  C  CD2 . HIS B  1 79  ? -18.746 -17.590 -24.824 1.00 27.79  ?  110  HIS B CD2 1 
ATOM   4243  C  CE1 . HIS B  1 79  ? -20.482 -16.348 -24.306 1.00 29.02  ?  110  HIS B CE1 1 
ATOM   4244  N  NE2 . HIS B  1 79  ? -19.179 -16.484 -24.129 1.00 28.96  ?  110  HIS B NE2 1 
ATOM   4245  N  N   . LEU B  1 80  ? -22.113 -20.141 -28.812 1.00 33.92  ?  111  LEU B N   1 
ATOM   4246  C  CA  . LEU B  1 80  ? -22.830 -21.206 -29.510 1.00 34.28  ?  111  LEU B CA  1 
ATOM   4247  C  C   . LEU B  1 80  ? -22.961 -20.943 -31.001 1.00 39.04  ?  111  LEU B C   1 
ATOM   4248  O  O   . LEU B  1 80  ? -23.249 -21.877 -31.760 1.00 36.31  ?  111  LEU B O   1 
ATOM   4249  C  CB  . LEU B  1 80  ? -24.241 -21.376 -28.923 1.00 35.74  ?  111  LEU B CB  1 
ATOM   4250  C  CG  . LEU B  1 80  ? -24.436 -22.323 -27.736 1.00 39.19  ?  111  LEU B CG  1 
ATOM   4251  C  CD1 . LEU B  1 80  ? -23.979 -23.720 -28.089 1.00 36.20  ?  111  LEU B CD1 1 
ATOM   4252  C  CD2 . LEU B  1 80  ? -23.632 -21.802 -26.544 1.00 38.97  ?  111  LEU B CD2 1 
ATOM   4253  N  N   . THR B  1 81  ? -22.756 -19.700 -31.429 1.00 36.20  ?  112  THR B N   1 
ATOM   4254  C  CA  . THR B  1 81  ? -22.852 -19.322 -32.830 1.00 36.36  ?  112  THR B CA  1 
ATOM   4255  C  C   . THR B  1 81  ? -21.493 -19.019 -33.445 1.00 35.66  ?  112  THR B C   1 
ATOM   4256  O  O   . THR B  1 81  ? -21.422 -18.740 -34.648 1.00 36.86  ?  112  THR B O   1 
ATOM   4257  C  CB  . THR B  1 81  ? -23.776 -18.108 -32.979 1.00 37.81  ?  112  THR B CB  1 
ATOM   4258  O  OG1 . THR B  1 81  ? -23.316 -17.045 -32.130 1.00 33.34  ?  112  THR B OG1 1 
ATOM   4259  C  CG2 . THR B  1 81  ? -25.224 -18.474 -32.602 1.00 35.18  ?  112  THR B CG2 1 
ATOM   4260  N  N   . GLY B  1 82  ? -20.420 -19.045 -32.651 1.00 35.43  ?  113  GLY B N   1 
ATOM   4261  C  CA  . GLY B  1 82  ? -19.085 -18.775 -33.149 1.00 31.03  ?  113  GLY B CA  1 
ATOM   4262  C  C   . GLY B  1 82  ? -18.703 -17.315 -33.220 1.00 29.32  ?  113  GLY B C   1 
ATOM   4263  O  O   . GLY B  1 82  ? -17.715 -16.982 -33.885 1.00 28.55  ?  113  GLY B O   1 
ATOM   4264  N  N   . THR B  1 83  ? -19.426 -16.432 -32.524 1.00 29.88  ?  114  THR B N   1 
ATOM   4265  C  CA  . THR B  1 83  ? -19.309 -14.989 -32.715 1.00 25.69  ?  114  THR B CA  1 
ATOM   4266  C  C   . THR B  1 83  ? -18.921 -14.267 -31.427 1.00 29.22  ?  114  THR B C   1 
ATOM   4267  O  O   . THR B  1 83  ? -19.359 -13.143 -31.169 1.00 26.62  ?  114  THR B O   1 
ATOM   4268  C  CB  . THR B  1 83  ? -20.612 -14.425 -33.277 1.00 28.21  ?  114  THR B CB  1 
ATOM   4269  O  OG1 . THR B  1 83  ? -21.683 -14.744 -32.391 1.00 28.24  ?  114  THR B OG1 1 
ATOM   4270  C  CG2 . THR B  1 83  ? -20.916 -15.050 -34.629 1.00 26.52  ?  114  THR B CG2 1 
ATOM   4271  N  N   . ALA B  1 84  ? -18.074 -14.894 -30.613 1.00 28.94  ?  115  ALA B N   1 
ATOM   4272  C  CA  . ALA B  1 84  ? -17.671 -14.320 -29.330 1.00 28.43  ?  115  ALA B CA  1 
ATOM   4273  C  C   . ALA B  1 84  ? -16.520 -13.319 -29.426 1.00 27.15  ?  115  ALA B C   1 
ATOM   4274  O  O   . ALA B  1 84  ? -16.128 -12.764 -28.395 1.00 26.86  ?  115  ALA B O   1 
ATOM   4275  C  CB  . ALA B  1 84  ? -17.296 -15.430 -28.348 1.00 29.05  ?  115  ALA B CB  1 
ATOM   4276  N  N   . TYR B  1 85  ? -15.972 -13.066 -30.606 1.00 26.19  ?  116  TYR B N   1 
ATOM   4277  C  CA  . TYR B  1 85  ? -15.007 -11.994 -30.799 1.00 26.77  ?  116  TYR B CA  1 
ATOM   4278  C  C   . TYR B  1 85  ? -15.612 -10.914 -31.691 1.00 27.27  ?  116  TYR B C   1 
ATOM   4279  O  O   . TYR B  1 85  ? -16.491 -11.196 -32.514 1.00 29.01  ?  116  TYR B O   1 
ATOM   4280  C  CB  . TYR B  1 85  ? -13.712 -12.526 -31.431 1.00 25.03  ?  116  TYR B CB  1 
ATOM   4281  C  CG  . TYR B  1 85  ? -12.831 -13.348 -30.495 1.00 29.69  ?  116  TYR B CG  1 
ATOM   4282  C  CD1 . TYR B  1 85  ? -13.008 -14.723 -30.361 1.00 29.39  ?  116  TYR B CD1 1 
ATOM   4283  C  CD2 . TYR B  1 85  ? -11.824 -12.743 -29.733 1.00 28.92  ?  116  TYR B CD2 1 
ATOM   4284  C  CE1 . TYR B  1 85  ? -12.199 -15.472 -29.508 1.00 31.16  ?  116  TYR B CE1 1 
ATOM   4285  C  CE2 . TYR B  1 85  ? -11.001 -13.497 -28.890 1.00 27.60  ?  116  TYR B CE2 1 
ATOM   4286  C  CZ  . TYR B  1 85  ? -11.196 -14.861 -28.791 1.00 29.29  ?  116  TYR B CZ  1 
ATOM   4287  O  OH  . TYR B  1 85  ? -10.392 -15.617 -27.949 1.00 28.87  ?  116  TYR B OH  1 
ATOM   4288  N  N   . ASN B  1 86  ? -15.157 -9.667  -31.520 1.00 27.14  ?  117  ASN B N   1 
ATOM   4289  C  CA  . ASN B  1 86  ? -15.531 -8.618  -32.469 1.00 24.51  ?  117  ASN B CA  1 
ATOM   4290  C  C   . ASN B  1 86  ? -14.949 -8.914  -33.849 1.00 28.20  ?  117  ASN B C   1 
ATOM   4291  O  O   . ASN B  1 86  ? -13.837 -9.428  -33.982 1.00 30.29  ?  117  ASN B O   1 
ATOM   4292  C  CB  . ASN B  1 86  ? -15.003 -7.247  -32.043 1.00 26.04  ?  117  ASN B CB  1 
ATOM   4293  C  CG  . ASN B  1 86  ? -15.953 -6.498  -31.113 1.00 28.05  ?  117  ASN B CG  1 
ATOM   4294  O  OD1 . ASN B  1 86  ? -17.022 -6.999  -30.750 1.00 28.23  ?  117  ASN B OD1 1 
ATOM   4295  N  ND2 . ASN B  1 86  ? -15.546 -5.287  -30.706 1.00 26.70  ?  117  ASN B ND2 1 
ATOM   4296  N  N   . LEU B  1 87  ? -15.701 -8.554  -34.886 1.00 27.32  ?  118  LEU B N   1 
ATOM   4297  C  CA  . LEU B  1 87  ? -15.080 -8.346  -36.184 1.00 27.56  ?  118  LEU B CA  1 
ATOM   4298  C  C   . LEU B  1 87  ? -14.108 -7.182  -36.102 1.00 28.60  ?  118  LEU B C   1 
ATOM   4299  O  O   . LEU B  1 87  ? -14.351 -6.192  -35.403 1.00 27.37  ?  118  LEU B O   1 
ATOM   4300  C  CB  . LEU B  1 87  ? -16.147 -8.061  -37.254 1.00 26.06  ?  118  LEU B CB  1 
ATOM   4301  C  CG  . LEU B  1 87  ? -17.125 -9.188  -37.548 1.00 27.41  ?  118  LEU B CG  1 
ATOM   4302  C  CD1 . LEU B  1 87  ? -18.281 -8.631  -38.366 1.00 28.51  ?  118  LEU B CD1 1 
ATOM   4303  C  CD2 . LEU B  1 87  ? -16.406 -10.309 -38.327 1.00 29.45  ?  118  LEU B CD2 1 
ATOM   4304  N  N   . PHE B  1 88  ? -13.006 -7.284  -36.839 1.00 30.78  ?  119  PHE B N   1 
ATOM   4305  C  CA  . PHE B  1 88  ? -12.007 -6.229  -36.808 1.00 27.22  ?  119  PHE B CA  1 
ATOM   4306  C  C   . PHE B  1 88  ? -12.494 -5.011  -37.592 1.00 30.11  ?  119  PHE B C   1 
ATOM   4307  O  O   . PHE B  1 88  ? -13.432 -5.099  -38.387 1.00 30.19  ?  119  PHE B O   1 
ATOM   4308  C  CB  . PHE B  1 88  ? -10.683 -6.731  -37.395 1.00 27.93  ?  119  PHE B CB  1 
ATOM   4309  C  CG  . PHE B  1 88  ? -9.489  -6.007  -36.870 1.00 31.65  ?  119  PHE B CG  1 
ATOM   4310  C  CD1 . PHE B  1 88  ? -9.004  -6.286  -35.608 1.00 27.38  ?  119  PHE B CD1 1 
ATOM   4311  C  CD2 . PHE B  1 88  ? -8.862  -5.040  -37.634 1.00 34.77  ?  119  PHE B CD2 1 
ATOM   4312  C  CE1 . PHE B  1 88  ? -7.900  -5.621  -35.114 1.00 32.68  ?  119  PHE B CE1 1 
ATOM   4313  C  CE2 . PHE B  1 88  ? -7.754  -4.369  -37.154 1.00 34.73  ?  119  PHE B CE2 1 
ATOM   4314  C  CZ  . PHE B  1 88  ? -7.281  -4.650  -35.885 1.00 32.84  ?  119  PHE B CZ  1 
ATOM   4315  N  N   . HIS B  1 89  ? -11.842 -3.867  -37.356 1.00 28.51  ?  120  HIS B N   1 
ATOM   4316  C  CA  . HIS B  1 89  ? -12.063 -2.681  -38.180 1.00 33.27  ?  120  HIS B CA  1 
ATOM   4317  C  C   . HIS B  1 89  ? -11.990 -3.041  -39.662 1.00 33.53  ?  120  HIS B C   1 
ATOM   4318  O  O   . HIS B  1 89  ? -11.131 -3.822  -40.078 1.00 29.95  ?  120  HIS B O   1 
ATOM   4319  C  CB  . HIS B  1 89  ? -11.029 -1.586  -37.869 1.00 33.30  ?  120  HIS B CB  1 
ATOM   4320  C  CG  . HIS B  1 89  ? -10.714 -1.423  -36.407 1.00 41.88  ?  120  HIS B CG  1 
ATOM   4321  N  ND1 . HIS B  1 89  ? -11.610 -0.873  -35.508 1.00 41.12  ?  120  HIS B ND1 1 
ATOM   4322  C  CD2 . HIS B  1 89  ? -9.600  -1.721  -35.692 1.00 42.24  ?  120  HIS B CD2 1 
ATOM   4323  C  CE1 . HIS B  1 89  ? -11.066 -0.852  -34.303 1.00 40.56  ?  120  HIS B CE1 1 
ATOM   4324  N  NE2 . HIS B  1 89  ? -9.844  -1.352  -34.389 1.00 43.44  ?  120  HIS B NE2 1 
ATOM   4325  N  N   . ASN B  1 90  ? -12.913 -2.486  -40.456 1.00 31.15  ?  121  ASN B N   1 
ATOM   4326  C  CA  . ASN B  1 90  ? -12.878 -2.652  -41.925 1.00 33.26  ?  121  ASN B CA  1 
ATOM   4327  C  C   . ASN B  1 90  ? -12.850 -4.129  -42.329 1.00 32.39  ?  121  ASN B C   1 
ATOM   4328  O  O   . ASN B  1 90  ? -12.084 -4.539  -43.201 1.00 30.89  ?  121  ASN B O   1 
ATOM   4329  C  CB  . ASN B  1 90  ? -11.665 -1.926  -42.536 1.00 34.73  ?  121  ASN B CB  1 
ATOM   4330  C  CG  . ASN B  1 90  ? -11.755 -0.405  -42.441 1.00 35.61  ?  121  ASN B CG  1 
ATOM   4331  O  OD1 . ASN B  1 90  ? -11.900 0.163   -41.361 1.00 33.68  ?  121  ASN B OD1 1 
ATOM   4332  N  ND2 . ASN B  1 90  ? -11.645 0.262   -43.590 1.00 37.50  ?  121  ASN B ND2 1 
ATOM   4333  N  N   . SER B  1 91  ? -13.647 -4.948  -41.655 1.00 30.95  ?  122  SER B N   1 
ATOM   4334  C  CA  . SER B  1 91  ? -13.640 -6.374  -41.934 1.00 30.05  ?  122  SER B CA  1 
ATOM   4335  C  C   . SER B  1 91  ? -14.166 -6.657  -43.348 1.00 32.47  ?  122  SER B C   1 
ATOM   4336  O  O   . SER B  1 91  ? -14.867 -5.847  -43.958 1.00 31.15  ?  122  SER B O   1 
ATOM   4337  C  CB  . SER B  1 91  ? -14.483 -7.125  -40.899 1.00 27.95  ?  122  SER B CB  1 
ATOM   4338  O  OG  . SER B  1 91  ? -15.842 -6.691  -40.970 1.00 30.18  ?  122  SER B OG  1 
ATOM   4339  N  N   . SER B  1 92  ? -13.850 -7.852  -43.842 1.00 32.69  ?  123  SER B N   1 
ATOM   4340  C  CA  . SER B  1 92  ? -13.976 -8.142  -45.262 1.00 30.04  ?  123  SER B CA  1 
ATOM   4341  C  C   . SER B  1 92  ? -15.410 -8.014  -45.740 1.00 33.58  ?  123  SER B C   1 
ATOM   4342  O  O   . SER B  1 92  ? -16.335 -8.561  -45.128 1.00 32.66  ?  123  SER B O   1 
ATOM   4343  C  CB  . SER B  1 92  ? -13.481 -9.547  -45.552 1.00 35.95  ?  123  SER B CB  1 
ATOM   4344  O  OG  . SER B  1 92  ? -13.854 -9.899  -46.863 1.00 37.14  ?  123  SER B OG  1 
ATOM   4345  N  N   . GLU B  1 93  ? -15.588 -7.307  -46.857 1.00 33.23  ?  124  GLU B N   1 
ATOM   4346  C  CA  . GLU B  1 93  ? -16.890 -7.147  -47.486 1.00 34.93  ?  124  GLU B CA  1 
ATOM   4347  C  C   . GLU B  1 93  ? -17.148 -8.185  -48.587 1.00 38.77  ?  124  GLU B C   1 
ATOM   4348  O  O   . GLU B  1 93  ? -18.085 -8.022  -49.375 1.00 36.68  ?  124  GLU B O   1 
ATOM   4349  C  CB  . GLU B  1 93  ? -17.019 -5.714  -48.021 1.00 38.48  ?  124  GLU B CB  1 
ATOM   4350  C  CG  . GLU B  1 93  ? -16.707 -4.676  -46.923 1.00 38.29  ?  124  GLU B CG  1 
ATOM   4351  C  CD  . GLU B  1 93  ? -16.630 -3.217  -47.391 1.00 48.77  ?  124  GLU B CD  1 
ATOM   4352  O  OE1 . GLU B  1 93  ? -16.680 -2.942  -48.608 1.00 45.50  ?  124  GLU B OE1 1 
ATOM   4353  O  OE2 . GLU B  1 93  ? -16.456 -2.331  -46.506 1.00 49.51  -1 124  GLU B OE2 1 
ATOM   4354  N  N   . ASP B  1 94  ? -16.365 -9.262  -48.636 1.00 42.96  ?  125  ASP B N   1 
ATOM   4355  C  CA  . ASP B  1 94  ? -16.576 -10.350 -49.592 1.00 40.12  ?  125  ASP B CA  1 
ATOM   4356  C  C   . ASP B  1 94  ? -17.282 -11.512 -48.913 1.00 37.12  ?  125  ASP B C   1 
ATOM   4357  O  O   . ASP B  1 94  ? -16.809 -12.007 -47.890 1.00 38.93  ?  125  ASP B O   1 
ATOM   4358  C  CB  . ASP B  1 94  ? -15.249 -10.852 -50.172 1.00 46.00  ?  125  ASP B CB  1 
ATOM   4359  C  CG  . ASP B  1 94  ? -14.604 -9.874  -51.133 1.00 60.90  ?  125  ASP B CG  1 
ATOM   4360  O  OD1 . ASP B  1 94  ? -15.327 -9.057  -51.756 1.00 64.84  -1 125  ASP B OD1 1 
ATOM   4361  O  OD2 . ASP B  1 94  ? -13.361 -9.918  -51.264 1.00 64.73  ?  125  ASP B OD2 1 
ATOM   4362  N  N   . ASP B  1 95  ? -18.390 -11.969 -49.501 1.00 39.54  ?  126  ASP B N   1 
ATOM   4363  C  CA  . ASP B  1 95  ? -19.101 -13.125 -48.956 1.00 36.08  ?  126  ASP B CA  1 
ATOM   4364  C  C   . ASP B  1 95  ? -18.200 -14.329 -48.780 1.00 40.75  ?  126  ASP B C   1 
ATOM   4365  O  O   . ASP B  1 95  ? -18.482 -15.194 -47.945 1.00 44.20  ?  126  ASP B O   1 
ATOM   4366  C  CB  . ASP B  1 95  ? -20.256 -13.538 -49.869 1.00 39.89  ?  126  ASP B CB  1 
ATOM   4367  C  CG  . ASP B  1 95  ? -21.404 -12.575 -49.824 1.00 44.41  ?  126  ASP B CG  1 
ATOM   4368  O  OD1 . ASP B  1 95  ? -21.355 -11.665 -48.976 1.00 41.57  ?  126  ASP B OD1 1 
ATOM   4369  O  OD2 . ASP B  1 95  ? -22.365 -12.741 -50.614 1.00 45.44  -1 126  ASP B OD2 1 
ATOM   4370  N  N   . LYS B  1 96  ? -17.155 -14.441 -49.602 1.00 40.88  ?  127  LYS B N   1 
ATOM   4371  C  CA  . LYS B  1 96  ? -16.311 -15.629 -49.553 1.00 45.28  ?  127  LYS B CA  1 
ATOM   4372  C  C   . LYS B  1 96  ? -15.603 -15.740 -48.213 1.00 43.18  ?  127  LYS B C   1 
ATOM   4373  O  O   . LYS B  1 96  ? -15.301 -16.849 -47.759 1.00 44.02  ?  127  LYS B O   1 
ATOM   4374  C  CB  . LYS B  1 96  ? -15.303 -15.602 -50.707 1.00 38.22  ?  127  LYS B CB  1 
ATOM   4375  N  N   . ASP B  1 97  ? -15.372 -14.612 -47.545 1.00 43.35  ?  128  ASP B N   1 
ATOM   4376  C  CA  . ASP B  1 97  ? -14.588 -14.604 -46.317 1.00 39.01  ?  128  ASP B CA  1 
ATOM   4377  C  C   . ASP B  1 97  ? -15.416 -14.903 -45.072 1.00 38.04  ?  128  ASP B C   1 
ATOM   4378  O  O   . ASP B  1 97  ? -14.834 -15.141 -44.008 1.00 38.90  ?  128  ASP B O   1 
ATOM   4379  C  CB  . ASP B  1 97  ? -13.876 -13.257 -46.179 1.00 38.46  ?  128  ASP B CB  1 
ATOM   4380  C  CG  . ASP B  1 97  ? -12.787 -13.072 -47.226 1.00 44.19  ?  128  ASP B CG  1 
ATOM   4381  O  OD1 . ASP B  1 97  ? -12.118 -14.071 -47.562 1.00 45.44  ?  128  ASP B OD1 1 
ATOM   4382  O  OD2 . ASP B  1 97  ? -12.607 -11.938 -47.727 1.00 46.69  -1 128  ASP B OD2 1 
ATOM   4383  N  N   . ASN B  1 98  ? -16.750 -14.908 -45.174 1.00 35.81  ?  129  ASN B N   1 
ATOM   4384  C  CA  . ASN B  1 98  ? -17.617 -15.354 -44.077 1.00 36.97  ?  129  ASN B CA  1 
ATOM   4385  C  C   . ASN B  1 98  ? -17.388 -14.556 -42.794 1.00 34.86  ?  129  ASN B C   1 
ATOM   4386  O  O   . ASN B  1 98  ? -17.435 -15.090 -41.683 1.00 37.02  ?  129  ASN B O   1 
ATOM   4387  C  CB  . ASN B  1 98  ? -17.435 -16.849 -43.821 1.00 37.11  ?  129  ASN B CB  1 
ATOM   4388  C  CG  . ASN B  1 98  ? -18.211 -17.685 -44.804 1.00 47.94  ?  129  ASN B CG  1 
ATOM   4389  O  OD1 . ASN B  1 98  ? -19.058 -17.166 -45.529 1.00 47.99  ?  129  ASN B OD1 1 
ATOM   4390  N  ND2 . ASN B  1 98  ? -17.924 -18.983 -44.848 1.00 57.83  ?  129  ASN B ND2 1 
ATOM   4391  N  N   . MET B  1 99  ? -17.136 -13.265 -42.944 1.00 32.39  ?  130  MET B N   1 
ATOM   4392  C  CA  . MET B  1 99  ? -16.799 -12.429 -41.803 1.00 30.81  ?  130  MET B CA  1 
ATOM   4393  C  C   . MET B  1 99  ? -18.104 -11.758 -41.351 1.00 30.22  ?  130  MET B C   1 
ATOM   4394  O  O   . MET B  1 99  ? -18.369 -10.577 -41.612 1.00 29.99  ?  130  MET B O   1 
ATOM   4395  C  CB  . MET B  1 99  ? -15.742 -11.412 -42.215 1.00 33.45  ?  130  MET B CB  1 
ATOM   4396  C  CG  . MET B  1 99  ? -14.268 -11.728 -41.862 1.00 37.83  ?  130  MET B CG  1 
ATOM   4397  S  SD  . MET B  1 99  ? -13.768 -12.405 -40.259 1.00 40.39  ?  130  MET B SD  1 
ATOM   4398  C  CE  . MET B  1 99  ? -12.293 -13.325 -40.714 1.00 35.80  ?  130  MET B CE  1 
ATOM   4399  N  N   . GLY B  1 100 ? -18.967 -12.565 -40.738 1.00 24.73  ?  131  GLY B N   1 
ATOM   4400  C  CA  . GLY B  1 100 ? -20.261 -12.089 -40.256 1.00 28.67  ?  131  GLY B CA  1 
ATOM   4401  C  C   . GLY B  1 100 ? -20.985 -13.213 -39.541 1.00 28.18  ?  131  GLY B C   1 
ATOM   4402  O  O   . GLY B  1 100 ? -20.534 -14.362 -39.528 1.00 31.06  ?  131  GLY B O   1 
ATOM   4403  N  N   . VAL B  1 101 ? -22.110 -12.865 -38.928 1.00 32.22  ?  132  VAL B N   1 
ATOM   4404  C  CA  . VAL B  1 101 ? -22.853 -13.852 -38.120 1.00 31.02  ?  132  VAL B CA  1 
ATOM   4405  C  C   . VAL B  1 101 ? -23.442 -14.907 -39.055 1.00 34.47  ?  132  VAL B C   1 
ATOM   4406  O  O   . VAL B  1 101 ? -24.015 -14.543 -40.089 1.00 29.87  ?  132  VAL B O   1 
ATOM   4407  C  CB  . VAL B  1 101 ? -23.957 -13.161 -37.306 1.00 29.34  ?  132  VAL B CB  1 
ATOM   4408  C  CG1 . VAL B  1 101 ? -24.786 -14.174 -36.542 1.00 28.92  ?  132  VAL B CG1 1 
ATOM   4409  C  CG2 . VAL B  1 101 ? -23.368 -12.107 -36.334 1.00 31.56  ?  132  VAL B CG2 1 
ATOM   4410  N  N   . PRO B  1 102 ? -23.311 -16.201 -38.759 1.00 34.25  ?  133  PRO B N   1 
ATOM   4411  C  CA  . PRO B  1 102 ? -23.766 -17.242 -39.699 1.00 32.31  ?  133  PRO B CA  1 
ATOM   4412  C  C   . PRO B  1 102 ? -25.160 -16.992 -40.253 1.00 33.06  ?  133  PRO B C   1 
ATOM   4413  O  O   . PRO B  1 102 ? -26.119 -16.802 -39.507 1.00 31.19  ?  133  PRO B O   1 
ATOM   4414  C  CB  . PRO B  1 102 ? -23.734 -18.510 -38.843 1.00 35.44  ?  133  PRO B CB  1 
ATOM   4415  C  CG  . PRO B  1 102 ? -22.564 -18.288 -37.959 1.00 34.49  ?  133  PRO B CG  1 
ATOM   4416  C  CD  . PRO B  1 102 ? -22.617 -16.794 -37.605 1.00 35.71  ?  133  PRO B CD  1 
ATOM   4417  N  N   . VAL B  1 103 ? -25.264 -17.007 -41.583 1.00 36.79  ?  134  VAL B N   1 
ATOM   4418  C  CA  . VAL B  1 103 ? -26.537 -16.732 -42.253 1.00 36.79  ?  134  VAL B CA  1 
ATOM   4419  C  C   . VAL B  1 103 ? -27.620 -17.708 -41.834 1.00 35.46  ?  134  VAL B C   1 
ATOM   4420  O  O   . VAL B  1 103 ? -28.809 -17.368 -41.865 1.00 36.53  ?  134  VAL B O   1 
ATOM   4421  C  CB  . VAL B  1 103 ? -26.356 -16.752 -43.778 1.00 35.50  ?  134  VAL B CB  1 
ATOM   4422  C  CG1 . VAL B  1 103 ? -25.476 -15.597 -44.220 1.00 32.65  ?  134  VAL B CG1 1 
ATOM   4423  C  CG2 . VAL B  1 103 ? -25.790 -18.106 -44.217 1.00 32.81  ?  134  VAL B CG2 1 
ATOM   4424  N  N   . GLU B  1 104 ? -27.246 -18.921 -41.432 1.00 34.75  ?  135  GLU B N   1 
ATOM   4425  C  CA  . GLU B  1 104 ? -28.239 -19.932 -41.077 1.00 39.43  ?  135  GLU B CA  1 
ATOM   4426  C  C   . GLU B  1 104 ? -28.872 -19.695 -39.716 1.00 38.28  ?  135  GLU B C   1 
ATOM   4427  O  O   . GLU B  1 104 ? -29.842 -20.374 -39.380 1.00 36.21  ?  135  GLU B O   1 
ATOM   4428  C  CB  . GLU B  1 104 ? -27.615 -21.336 -41.095 1.00 42.21  ?  135  GLU B CB  1 
ATOM   4429  C  CG  . GLU B  1 104 ? -26.586 -21.545 -42.208 1.00 47.23  ?  135  GLU B CG  1 
ATOM   4430  C  CD  . GLU B  1 104 ? -25.231 -20.952 -41.833 1.00 46.08  ?  135  GLU B CD  1 
ATOM   4431  O  OE1 . GLU B  1 104 ? -25.008 -20.745 -40.628 1.00 51.59  ?  135  GLU B OE1 1 
ATOM   4432  O  OE2 . GLU B  1 104 ? -24.405 -20.665 -42.726 1.00 57.80  -1 135  GLU B OE2 1 
ATOM   4433  N  N   . GLU B  1 105 ? -28.344 -18.765 -38.917 1.00 39.64  ?  136  GLU B N   1 
ATOM   4434  C  CA  . GLU B  1 105 ? -28.901 -18.456 -37.600 1.00 35.41  ?  136  GLU B CA  1 
ATOM   4435  C  C   . GLU B  1 105 ? -29.920 -17.335 -37.755 1.00 35.85  ?  136  GLU B C   1 
ATOM   4436  O  O   . GLU B  1 105 ? -29.588 -16.152 -37.676 1.00 35.62  ?  136  GLU B O   1 
ATOM   4437  C  CB  . GLU B  1 105 ? -27.784 -18.078 -36.633 1.00 34.97  ?  136  GLU B CB  1 
ATOM   4438  C  CG  . GLU B  1 105 ? -28.192 -18.142 -35.181 1.00 37.02  ?  136  GLU B CG  1 
ATOM   4439  C  CD  . GLU B  1 105 ? -28.522 -19.543 -34.749 1.00 35.35  ?  136  GLU B CD  1 
ATOM   4440  O  OE1 . GLU B  1 105 ? -27.621 -20.390 -34.772 1.00 36.63  ?  136  GLU B OE1 1 
ATOM   4441  O  OE2 . GLU B  1 105 ? -29.688 -19.800 -34.400 1.00 41.63  -1 136  GLU B OE2 1 
ATOM   4442  N  N   . THR B  1 106 ? -31.183 -17.708 -37.962 1.00 32.83  ?  137  THR B N   1 
ATOM   4443  C  CA  . THR B  1 106 ? -32.206 -16.731 -38.315 1.00 30.08  ?  137  THR B CA  1 
ATOM   4444  C  C   . THR B  1 106 ? -32.435 -15.699 -37.206 1.00 32.52  ?  137  THR B C   1 
ATOM   4445  O  O   . THR B  1 106 ? -32.708 -16.057 -36.054 1.00 33.13  ?  137  THR B O   1 
ATOM   4446  C  CB  . THR B  1 106 ? -33.514 -17.456 -38.638 1.00 36.85  ?  137  THR B CB  1 
ATOM   4447  O  OG1 . THR B  1 106 ? -33.232 -18.555 -39.512 1.00 39.10  ?  137  THR B OG1 1 
ATOM   4448  C  CG2 . THR B  1 106 ? -34.519 -16.509 -39.301 1.00 32.49  ?  137  THR B CG2 1 
ATOM   4449  N  N   . TYR B  1 107 ? -32.333 -14.415 -37.573 1.00 32.02  ?  138  TYR B N   1 
ATOM   4450  C  CA  . TYR B  1 107 ? -32.564 -13.291 -36.658 1.00 31.78  ?  138  TYR B CA  1 
ATOM   4451  C  C   . TYR B  1 107 ? -34.051 -13.109 -36.358 1.00 38.40  ?  138  TYR B C   1 
ATOM   4452  O  O   . TYR B  1 107 ? -34.909 -13.451 -37.185 1.00 33.66  ?  138  TYR B O   1 
ATOM   4453  C  CB  . TYR B  1 107 ? -32.060 -11.977 -37.269 1.00 28.05  ?  138  TYR B CB  1 
ATOM   4454  C  CG  . TYR B  1 107 ? -30.574 -11.807 -37.427 1.00 28.77  ?  138  TYR B CG  1 
ATOM   4455  C  CD1 . TYR B  1 107 ? -29.688 -12.797 -37.052 1.00 29.32  ?  138  TYR B CD1 1 
ATOM   4456  C  CD2 . TYR B  1 107 ? -30.062 -10.626 -37.959 1.00 26.40  ?  138  TYR B CD2 1 
ATOM   4457  C  CE1 . TYR B  1 107 ? -28.299 -12.610 -37.188 1.00 30.74  ?  138  TYR B CE1 1 
ATOM   4458  C  CE2 . TYR B  1 107 ? -28.698 -10.437 -38.108 1.00 29.70  ?  138  TYR B CE2 1 
ATOM   4459  C  CZ  . TYR B  1 107 ? -27.830 -11.424 -37.728 1.00 29.44  ?  138  TYR B CZ  1 
ATOM   4460  O  OH  . TYR B  1 107 ? -26.503 -11.209 -37.905 1.00 28.62  ?  138  TYR B OH  1 
ATOM   4461  N  N   . MET B  1 108 ? -34.360 -12.512 -35.206 1.00 33.75  ?  139  MET B N   1 
ATOM   4462  C  CA  . MET B  1 108 ? -35.785 -12.235 -34.890 1.00 32.62  ?  139  MET B CA  1 
ATOM   4463  C  C   . MET B  1 108 ? -36.371 -11.333 -35.987 1.00 32.94  ?  139  MET B C   1 
ATOM   4464  O  O   . MET B  1 108 ? -37.576 -11.474 -36.277 1.00 32.34  ?  139  MET B O   1 
ATOM   4465  C  CB  . MET B  1 108 ? -35.943 -11.556 -33.524 1.00 34.65  ?  139  MET B CB  1 
ATOM   4466  C  CG  . MET B  1 108 ? -34.742 -10.743 -33.086 1.00 30.03  ?  139  MET B CG  1 
ATOM   4467  S  SD  . MET B  1 108 ? -34.890 -10.216 -31.367 1.00 36.17  ?  139  MET B SD  1 
ATOM   4468  C  CE  . MET B  1 108 ? -34.371 -8.499  -31.475 1.00 30.49  ?  139  MET B CE  1 
ATOM   4469  N  N   . SER B  1 109 ? -35.553 -10.460 -36.585 1.00 28.34  ?  140  SER B N   1 
ATOM   4470  C  CA  . SER B  1 109 ? -36.093 -9.528  -37.568 1.00 32.98  ?  140  SER B CA  1 
ATOM   4471  C  C   . SER B  1 109 ? -36.781 -10.284 -38.706 1.00 33.14  ?  140  SER B C   1 
ATOM   4472  O  O   . SER B  1 109 ? -37.917 -9.972  -39.072 1.00 32.33  ?  140  SER B O   1 
ATOM   4473  C  CB  . SER B  1 109 ? -34.982 -8.628  -38.112 1.00 30.36  ?  140  SER B CB  1 
ATOM   4474  O  OG  . SER B  1 109 ? -33.821 -9.381  -38.410 1.00 30.87  ?  140  SER B OG  1 
ATOM   4475  N  N   . LYS B  1 110 ? -36.114 -11.304 -39.257 1.00 34.38  ?  141  LYS B N   1 
ATOM   4476  C  CA  . LYS B  1 110 ? -36.734 -12.093 -40.322 1.00 35.05  ?  141  LYS B CA  1 
ATOM   4477  C  C   . LYS B  1 110 ? -37.981 -12.825 -39.836 1.00 33.90  ?  141  LYS B C   1 
ATOM   4478  O  O   . LYS B  1 110 ? -38.972 -12.933 -40.573 1.00 36.26  ?  141  LYS B O   1 
ATOM   4479  C  CB  . LYS B  1 110 ? -35.738 -13.098 -40.907 1.00 35.46  ?  141  LYS B CB  1 
ATOM   4480  C  CG  . LYS B  1 110 ? -36.129 -13.530 -42.336 1.00 39.57  ?  141  LYS B CG  1 
ATOM   4481  C  CD  . LYS B  1 110 ? -35.092 -14.440 -42.945 1.00 42.92  ?  141  LYS B CD  1 
ATOM   4482  C  CE  . LYS B  1 110 ? -33.974 -13.658 -43.626 1.00 41.85  ?  141  LYS B CE  1 
ATOM   4483  N  NZ  . LYS B  1 110 ? -32.853 -14.554 -44.062 1.00 42.92  ?  141  LYS B NZ  1 
ATOM   4484  N  N   . VAL B  1 111 ? -37.947 -13.349 -38.606 1.00 33.88  ?  142  VAL B N   1 
ATOM   4485  C  CA  . VAL B  1 111 ? -39.122 -14.019 -38.058 1.00 33.23  ?  142  VAL B CA  1 
ATOM   4486  C  C   . VAL B  1 111 ? -40.296 -13.051 -37.959 1.00 38.05  ?  142  VAL B C   1 
ATOM   4487  O  O   . VAL B  1 111 ? -41.430 -13.397 -38.320 1.00 38.13  ?  142  VAL B O   1 
ATOM   4488  C  CB  . VAL B  1 111 ? -38.801 -14.672 -36.701 1.00 34.66  ?  142  VAL B CB  1 
ATOM   4489  C  CG1 . VAL B  1 111 ? -40.025 -15.369 -36.154 1.00 34.51  ?  142  VAL B CG1 1 
ATOM   4490  C  CG2 . VAL B  1 111 ? -37.668 -15.688 -36.846 1.00 35.08  ?  142  VAL B CG2 1 
ATOM   4491  N  N   . LEU B  1 112 ? -40.055 -11.814 -37.501 1.00 32.16  ?  143  LEU B N   1 
ATOM   4492  C  CA  . LEU B  1 112 ? -41.170 -10.864 -37.422 1.00 31.54  ?  143  LEU B CA  1 
ATOM   4493  C  C   . LEU B  1 112 ? -41.605 -10.394 -38.803 1.00 34.31  ?  143  LEU B C   1 
ATOM   4494  O  O   . LEU B  1 112 ? -42.809 -10.246 -39.059 1.00 33.90  ?  143  LEU B O   1 
ATOM   4495  C  CB  . LEU B  1 112 ? -40.810 -9.659  -36.554 1.00 28.91  ?  143  LEU B CB  1 
ATOM   4496  C  CG  . LEU B  1 112 ? -40.276 -10.033 -35.175 1.00 37.97  ?  143  LEU B CG  1 
ATOM   4497  C  CD1 . LEU B  1 112 ? -39.578 -8.840  -34.522 1.00 35.96  ?  143  LEU B CD1 1 
ATOM   4498  C  CD2 . LEU B  1 112 ? -41.446 -10.483 -34.349 1.00 33.29  ?  143  LEU B CD2 1 
ATOM   4499  N  N   . GLN B  1 113 ? -40.638 -10.121 -39.690 1.00 34.59  ?  144  GLN B N   1 
ATOM   4500  C  CA  . GLN B  1 113 ? -40.945 -9.809  -41.083 1.00 34.20  ?  144  GLN B CA  1 
ATOM   4501  C  C   . GLN B  1 113 ? -41.883 -10.850 -41.674 1.00 37.15  ?  144  GLN B C   1 
ATOM   4502  O  O   . GLN B  1 113 ? -42.896 -10.520 -42.296 1.00 37.53  ?  144  GLN B O   1 
ATOM   4503  C  CB  . GLN B  1 113 ? -39.653 -9.765  -41.903 1.00 32.14  ?  144  GLN B CB  1 
ATOM   4504  C  CG  . GLN B  1 113 ? -39.736 -8.937  -43.180 1.00 37.00  ?  144  GLN B CG  1 
ATOM   4505  C  CD  . GLN B  1 113 ? -38.506 -9.108  -44.048 1.00 37.10  ?  144  GLN B CD  1 
ATOM   4506  O  OE1 . GLN B  1 113 ? -37.914 -10.186 -44.105 1.00 41.26  ?  144  GLN B OE1 1 
ATOM   4507  N  NE2 . GLN B  1 113 ? -38.102 -8.037  -44.713 1.00 36.55  ?  144  GLN B NE2 1 
ATOM   4508  N  N   . ASN B  1 114 ? -41.534 -12.121 -41.482 1.00 36.03  ?  145  ASN B N   1 
ATOM   4509  C  CA  . ASN B  1 114 ? -42.269 -13.248 -42.023 1.00 39.73  ?  145  ASN B CA  1 
ATOM   4510  C  C   . ASN B  1 114 ? -43.674 -13.312 -41.443 1.00 43.21  ?  145  ASN B C   1 
ATOM   4511  O  O   . ASN B  1 114 ? -44.585 -13.861 -42.077 1.00 40.82  ?  145  ASN B O   1 
ATOM   4512  C  CB  . ASN B  1 114 ? -41.474 -14.508 -41.688 1.00 38.47  ?  145  ASN B CB  1 
ATOM   4513  C  CG  . ASN B  1 114 ? -40.555 -14.937 -42.810 1.00 46.10  ?  145  ASN B CG  1 
ATOM   4514  O  OD1 . ASN B  1 114 ? -39.930 -16.005 -42.750 1.00 53.50  ?  145  ASN B OD1 1 
ATOM   4515  N  ND2 . ASN B  1 114 ? -40.415 -14.072 -43.821 1.00 45.16  ?  145  ASN B ND2 1 
ATOM   4516  N  N   . ALA B  1 115 ? -43.870 -12.741 -40.257 1.00 39.32  ?  146  ALA B N   1 
ATOM   4517  C  CA  . ALA B  1 115 ? -45.156 -12.697 -39.578 1.00 36.59  ?  146  ALA B CA  1 
ATOM   4518  C  C   . ALA B  1 115 ? -45.942 -11.418 -39.864 1.00 39.60  ?  146  ALA B C   1 
ATOM   4519  O  O   . ALA B  1 115 ? -46.964 -11.169 -39.216 1.00 39.57  ?  146  ALA B O   1 
ATOM   4520  C  CB  . ALA B  1 115 ? -44.950 -12.861 -38.072 1.00 37.42  ?  146  ALA B CB  1 
ATOM   4521  N  N   . GLY B  1 116 ? -45.494 -10.601 -40.809 1.00 37.32  ?  147  GLY B N   1 
ATOM   4522  C  CA  . GLY B  1 116 ? -46.260 -9.443  -41.204 1.00 38.34  ?  147  GLY B CA  1 
ATOM   4523  C  C   . GLY B  1 116 ? -45.805 -8.120  -40.637 1.00 38.16  ?  147  GLY B C   1 
ATOM   4524  O  O   . GLY B  1 116 ? -46.491 -7.115  -40.848 1.00 33.99  ?  147  GLY B O   1 
ATOM   4525  N  N   . TYR B  1 117 ? -44.674 -8.074  -39.924 1.00 35.68  ?  148  TYR B N   1 
ATOM   4526  C  CA  . TYR B  1 117 ? -44.192 -6.799  -39.420 1.00 34.16  ?  148  TYR B CA  1 
ATOM   4527  C  C   . TYR B  1 117 ? -43.441 -6.057  -40.518 1.00 29.69  ?  148  TYR B C   1 
ATOM   4528  O  O   . TYR B  1 117 ? -42.774 -6.668  -41.357 1.00 30.47  ?  148  TYR B O   1 
ATOM   4529  C  CB  . TYR B  1 117 ? -43.287 -7.007  -38.196 1.00 31.78  ?  148  TYR B CB  1 
ATOM   4530  C  CG  . TYR B  1 117 ? -44.061 -7.114  -36.893 1.00 31.02  ?  148  TYR B CG  1 
ATOM   4531  C  CD1 . TYR B  1 117 ? -44.958 -8.146  -36.688 1.00 32.16  ?  148  TYR B CD1 1 
ATOM   4532  C  CD2 . TYR B  1 117 ? -43.874 -6.198  -35.860 1.00 29.67  ?  148  TYR B CD2 1 
ATOM   4533  C  CE1 . TYR B  1 117 ? -45.675 -8.260  -35.497 1.00 34.38  ?  148  TYR B CE1 1 
ATOM   4534  C  CE2 . TYR B  1 117 ? -44.569 -6.309  -34.658 1.00 30.63  ?  148  TYR B CE2 1 
ATOM   4535  C  CZ  . TYR B  1 117 ? -45.472 -7.338  -34.483 1.00 33.19  ?  148  TYR B CZ  1 
ATOM   4536  O  OH  . TYR B  1 117 ? -46.179 -7.441  -33.297 1.00 30.18  ?  148  TYR B OH  1 
ATOM   4537  N  N   . TYR B  1 118 ? -43.583 -4.736  -40.522 1.00 30.24  ?  149  TYR B N   1 
ATOM   4538  C  CA  . TYR B  1 118 ? -42.654 -3.857  -41.222 1.00 30.44  ?  149  TYR B CA  1 
ATOM   4539  C  C   . TYR B  1 118 ? -41.398 -3.684  -40.364 1.00 27.30  ?  149  TYR B C   1 
ATOM   4540  O  O   . TYR B  1 118 ? -41.483 -3.225  -39.221 1.00 29.43  ?  149  TYR B O   1 
ATOM   4541  C  CB  . TYR B  1 118 ? -43.314 -2.507  -41.471 1.00 30.79  ?  149  TYR B CB  1 
ATOM   4542  C  CG  . TYR B  1 118 ? -42.369 -1.451  -41.983 1.00 30.91  ?  149  TYR B CG  1 
ATOM   4543  C  CD1 . TYR B  1 118 ? -41.698 -1.620  -43.179 1.00 37.81  ?  149  TYR B CD1 1 
ATOM   4544  C  CD2 . TYR B  1 118 ? -42.139 -0.290  -41.262 1.00 32.83  ?  149  TYR B CD2 1 
ATOM   4545  C  CE1 . TYR B  1 118 ? -40.832 -0.653  -43.654 1.00 37.22  ?  149  TYR B CE1 1 
ATOM   4546  C  CE2 . TYR B  1 118 ? -41.258 0.688   -41.730 1.00 31.71  ?  149  TYR B CE2 1 
ATOM   4547  C  CZ  . TYR B  1 118 ? -40.609 0.492   -42.918 1.00 34.26  ?  149  TYR B CZ  1 
ATOM   4548  O  OH  . TYR B  1 118 ? -39.760 1.457   -43.412 1.00 34.73  ?  149  TYR B OH  1 
ATOM   4549  N  N   . THR B  1 119 ? -40.238 -4.036  -40.906 1.00 32.67  ?  150  THR B N   1 
ATOM   4550  C  CA  . THR B  1 119 ? -39.017 -4.111  -40.107 1.00 28.48  ?  150  THR B CA  1 
ATOM   4551  C  C   . THR B  1 119 ? -38.012 -3.058  -40.549 1.00 31.75  ?  150  THR B C   1 
ATOM   4552  O  O   . THR B  1 119 ? -37.857 -2.783  -41.744 1.00 30.98  ?  150  THR B O   1 
ATOM   4553  C  CB  . THR B  1 119 ? -38.400 -5.500  -40.197 1.00 31.31  ?  150  THR B CB  1 
ATOM   4554  O  OG1 . THR B  1 119 ? -38.304 -5.888  -41.573 1.00 32.57  ?  150  THR B OG1 1 
ATOM   4555  C  CG2 . THR B  1 119 ? -39.223 -6.520  -39.403 1.00 30.52  ?  150  THR B CG2 1 
ATOM   4556  N  N   . SER B  1 120 ? -37.303 -2.487  -39.578 1.00 30.19  ?  151  SER B N   1 
ATOM   4557  C  CA  . SER B  1 120 ? -36.436 -1.359  -39.861 1.00 25.31  ?  151  SER B CA  1 
ATOM   4558  C  C   . SER B  1 120 ? -35.273 -1.384  -38.873 1.00 26.50  ?  151  SER B C   1 
ATOM   4559  O  O   . SER B  1 120 ? -35.489 -1.531  -37.666 1.00 29.65  ?  151  SER B O   1 
ATOM   4560  C  CB  . SER B  1 120 ? -37.215 -0.045  -39.752 1.00 29.32  ?  151  SER B CB  1 
ATOM   4561  O  OG  . SER B  1 120 ? -36.348 1.032   -39.410 1.00 36.41  ?  151  SER B OG  1 
ATOM   4562  N  N   . ALA B  1 121 ? -34.054 -1.290  -39.400 1.00 25.92  ?  152  ALA B N   1 
ATOM   4563  C  CA  . ALA B  1 121 ? -32.829 -1.184  -38.615 1.00 24.55  ?  152  ALA B CA  1 
ATOM   4564  C  C   . ALA B  1 121 ? -32.195 0.173   -38.886 1.00 27.22  ?  152  ALA B C   1 
ATOM   4565  O  O   . ALA B  1 121 ? -32.231 0.668   -40.021 1.00 30.46  ?  152  ALA B O   1 
ATOM   4566  C  CB  . ALA B  1 121 ? -31.863 -2.313  -38.980 1.00 25.42  ?  152  ALA B CB  1 
ATOM   4567  N  N   . ILE B  1 122 ? -31.654 0.795   -37.835 1.00 27.05  ?  153  ILE B N   1 
ATOM   4568  C  CA  . ILE B  1 122 ? -31.137 2.159   -37.886 1.00 22.69  ?  153  ILE B CA  1 
ATOM   4569  C  C   . ILE B  1 122 ? -29.876 2.223   -37.033 1.00 25.71  ?  153  ILE B C   1 
ATOM   4570  O  O   . ILE B  1 122 ? -29.870 1.740   -35.899 1.00 24.47  ?  153  ILE B O   1 
ATOM   4571  C  CB  . ILE B  1 122 ? -32.165 3.187   -37.362 1.00 21.83  ?  153  ILE B CB  1 
ATOM   4572  C  CG1 . ILE B  1 122 ? -33.470 3.122   -38.168 1.00 25.02  ?  153  ILE B CG1 1 
ATOM   4573  C  CG2 . ILE B  1 122 ? -31.608 4.613   -37.408 1.00 21.34  ?  153  ILE B CG2 1 
ATOM   4574  C  CD1 . ILE B  1 122 ? -34.565 3.909   -37.522 1.00 25.10  ?  153  ILE B CD1 1 
ATOM   4575  N  N   . GLY B  1 123 ? -28.828 2.854   -37.559 1.00 26.87  ?  154  GLY B N   1 
ATOM   4576  C  CA  . GLY B  1 123 ? -27.610 3.092   -36.780 1.00 20.56  ?  154  GLY B CA  1 
ATOM   4577  C  C   . GLY B  1 123 ? -26.571 2.015   -37.014 1.00 26.21  ?  154  GLY B C   1 
ATOM   4578  O  O   . GLY B  1 123 ? -26.266 1.675   -38.162 1.00 25.88  ?  154  GLY B O   1 
ATOM   4579  N  N   . LYS B  1 124 ? -26.037 1.474   -35.912 1.00 24.49  ?  155  LYS B N   1 
ATOM   4580  C  CA  . LYS B  1 124 ? -24.919 0.547   -35.910 1.00 22.20  ?  155  LYS B CA  1 
ATOM   4581  C  C   . LYS B  1 124 ? -25.354 -0.890  -36.185 1.00 26.70  ?  155  LYS B C   1 
ATOM   4582  O  O   . LYS B  1 124 ? -26.370 -1.372  -35.662 1.00 26.32  ?  155  LYS B O   1 
ATOM   4583  C  CB  . LYS B  1 124 ? -24.203 0.610   -34.539 1.00 23.29  ?  155  LYS B CB  1 
ATOM   4584  C  CG  . LYS B  1 124 ? -23.151 -0.462  -34.284 1.00 25.24  ?  155  LYS B CG  1 
ATOM   4585  C  CD  . LYS B  1 124 ? -22.342 -0.118  -33.011 1.00 22.64  ?  155  LYS B CD  1 
ATOM   4586  C  CE  . LYS B  1 124 ? -21.530 -1.293  -32.551 1.00 26.72  ?  155  LYS B CE  1 
ATOM   4587  N  NZ  . LYS B  1 124 ? -20.386 -0.861  -31.659 1.00 27.46  ?  155  LYS B NZ  1 
ATOM   4588  N  N   . TRP B  1 125 ? -24.538 -1.594  -36.969 1.00 23.92  ?  156  TRP B N   1 
ATOM   4589  C  CA  . TRP B  1 125 ? -24.802 -2.999  -37.274 1.00 26.57  ?  156  TRP B CA  1 
ATOM   4590  C  C   . TRP B  1 125 ? -23.825 -3.925  -36.552 1.00 24.30  ?  156  TRP B C   1 
ATOM   4591  O  O   . TRP B  1 125 ? -24.166 -4.543  -35.530 1.00 27.06  ?  156  TRP B O   1 
ATOM   4592  C  CB  . TRP B  1 125 ? -24.722 -3.210  -38.793 1.00 24.47  ?  156  TRP B CB  1 
ATOM   4593  C  CG  . TRP B  1 125 ? -25.206 -4.549  -39.324 1.00 24.88  ?  156  TRP B CG  1 
ATOM   4594  C  CD1 . TRP B  1 125 ? -24.511 -5.409  -40.141 1.00 25.72  ?  156  TRP B CD1 1 
ATOM   4595  C  CD2 . TRP B  1 125 ? -26.498 -5.154  -39.117 1.00 24.98  ?  156  TRP B CD2 1 
ATOM   4596  N  NE1 . TRP B  1 125 ? -25.282 -6.513  -40.425 1.00 24.59  ?  156  TRP B NE1 1 
ATOM   4597  C  CE2 . TRP B  1 125 ? -26.504 -6.381  -39.817 1.00 27.36  ?  156  TRP B CE2 1 
ATOM   4598  C  CE3 . TRP B  1 125 ? -27.644 -4.781  -38.403 1.00 24.81  ?  156  TRP B CE3 1 
ATOM   4599  C  CZ2 . TRP B  1 125 ? -27.622 -7.234  -39.839 1.00 25.68  ?  156  TRP B CZ2 1 
ATOM   4600  C  CZ3 . TRP B  1 125 ? -28.746 -5.633  -38.419 1.00 27.34  ?  156  TRP B CZ3 1 
ATOM   4601  C  CH2 . TRP B  1 125 ? -28.726 -6.845  -39.137 1.00 26.36  ?  156  TRP B CH2 1 
ATOM   4602  N  N   . HIS B  1 126 ? -22.588 -3.981  -37.059 1.00 26.72  ?  157  HIS B N   1 
ATOM   4603  C  CA  . HIS B  1 126 ? -21.489 -4.764  -36.414 1.00 25.59  ?  157  HIS B CA  1 
ATOM   4604  C  C   . HIS B  1 126 ? -21.720 -6.291  -36.491 1.00 29.55  ?  157  HIS B C   1 
ATOM   4605  O  O   . HIS B  1 126 ? -21.161 -7.014  -35.639 1.00 27.73  ?  157  HIS B O   1 
ATOM   4606  C  CB  . HIS B  1 126 ? -21.240 -4.260  -34.986 1.00 28.41  ?  157  HIS B CB  1 
ATOM   4607  C  CG  . HIS B  1 126 ? -19.808 -4.233  -34.577 1.00 25.48  ?  157  HIS B CG  1 
ATOM   4608  N  ND1 . HIS B  1 126 ? -19.405 -3.951  -33.289 1.00 28.83  ?  157  HIS B ND1 1 
ATOM   4609  C  CD2 . HIS B  1 126 ? -18.693 -4.469  -35.276 1.00 25.38  ?  157  HIS B CD2 1 
ATOM   4610  C  CE1 . HIS B  1 126 ? -18.083 -4.010  -33.229 1.00 30.73  ?  157  HIS B CE1 1 
ATOM   4611  N  NE2 . HIS B  1 126 ? -17.630 -4.321  -34.424 1.00 27.46  ?  157  HIS B NE2 1 
ATOM   4612  N  N   . LEU B  1 127 ? -22.491 -6.763  -37.481 1.00 28.83  ?  158  LEU B N   1 
ATOM   4613  C  CA  . LEU B  1 127 ? -22.757 -8.194  -37.601 1.00 28.81  ?  158  LEU B CA  1 
ATOM   4614  C  C   . LEU B  1 127 ? -22.355 -8.737  -38.969 1.00 28.18  ?  158  LEU B C   1 
ATOM   4615  O  O   . LEU B  1 127 ? -22.798 -9.825  -39.351 1.00 27.59  ?  158  LEU B O   1 
ATOM   4616  C  CB  . LEU B  1 127 ? -24.238 -8.499  -37.335 1.00 27.51  ?  158  LEU B CB  1 
ATOM   4617  C  CG  . LEU B  1 127 ? -24.789 -7.860  -36.054 1.00 26.71  ?  158  LEU B CG  1 
ATOM   4618  C  CD1 . LEU B  1 127 ? -26.307 -7.887  -36.087 1.00 27.20  ?  158  LEU B CD1 1 
ATOM   4619  C  CD2 . LEU B  1 127 ? -24.249 -8.569  -34.823 1.00 26.19  ?  158  LEU B CD2 1 
ATOM   4620  N  N   . GLY B  1 128 ? -21.507 -8.018  -39.701 1.00 29.93  ?  159  GLY B N   1 
ATOM   4621  C  CA  . GLY B  1 128 ? -21.047 -8.482  -41.003 1.00 30.67  ?  159  GLY B CA  1 
ATOM   4622  C  C   . GLY B  1 128 ? -21.172 -7.388  -42.038 1.00 27.14  ?  159  GLY B C   1 
ATOM   4623  O  O   . GLY B  1 128 ? -22.236 -6.773  -42.174 1.00 28.50  ?  159  GLY B O   1 
ATOM   4624  N  N   . ALA B  1 129 ? -20.084 -7.089  -42.738 1.00 27.09  ?  160  ALA B N   1 
ATOM   4625  C  CA  . ALA B  1 129 ? -20.117 -6.053  -43.760 1.00 30.85  ?  160  ALA B CA  1 
ATOM   4626  C  C   . ALA B  1 129 ? -20.148 -6.604  -45.189 1.00 32.13  ?  160  ALA B C   1 
ATOM   4627  O  O   . ALA B  1 129 ? -20.116 -5.815  -46.132 1.00 34.11  ?  160  ALA B O   1 
ATOM   4628  C  CB  . ALA B  1 129 ? -18.926 -5.111  -43.599 1.00 33.36  ?  160  ALA B CB  1 
ATOM   4629  N  N   . ALA B  1 130 ? -20.210 -7.932  -45.375 1.00 32.09  ?  161  ALA B N   1 
ATOM   4630  C  CA  . ALA B  1 130 ? -20.345 -8.521  -46.705 1.00 35.53  ?  161  ALA B CA  1 
ATOM   4631  C  C   . ALA B  1 130 ? -21.818 -8.632  -47.076 1.00 32.32  ?  161  ALA B C   1 
ATOM   4632  O  O   . ALA B  1 130 ? -22.691 -8.614  -46.194 1.00 32.04  ?  161  ALA B O   1 
ATOM   4633  C  CB  . ALA B  1 130 ? -19.681 -9.901  -46.749 1.00 34.04  ?  161  ALA B CB  1 
ATOM   4634  N  N   . PRO B  1 131 ? -22.138 -8.730  -48.382 1.00 37.14  ?  162  PRO B N   1 
ATOM   4635  C  CA  . PRO B  1 131 ? -23.554 -8.679  -48.793 1.00 34.91  ?  162  PRO B CA  1 
ATOM   4636  C  C   . PRO B  1 131 ? -24.464 -9.684  -48.106 1.00 33.31  ?  162  PRO B C   1 
ATOM   4637  O  O   . PRO B  1 131 ? -25.586 -9.325  -47.744 1.00 33.61  ?  162  PRO B O   1 
ATOM   4638  C  CB  . PRO B  1 131 ? -23.476 -8.931  -50.312 1.00 39.84  ?  162  PRO B CB  1 
ATOM   4639  C  CG  . PRO B  1 131 ? -22.159 -8.322  -50.694 1.00 39.95  ?  162  PRO B CG  1 
ATOM   4640  C  CD  . PRO B  1 131 ? -21.235 -8.694  -49.552 1.00 36.63  ?  162  PRO B CD  1 
ATOM   4641  N  N   . LYS B  1 132 ? -24.032 -10.935 -47.928 1.00 34.42  ?  163  LYS B N   1 
ATOM   4642  C  CA  . LYS B  1 132 ? -24.915 -11.927 -47.322 1.00 32.76  ?  163  LYS B CA  1 
ATOM   4643  C  C   . LYS B  1 132 ? -25.277 -11.572 -45.878 1.00 33.42  ?  163  LYS B C   1 
ATOM   4644  O  O   . LYS B  1 132 ? -26.256 -12.113 -45.345 1.00 27.74  ?  163  LYS B O   1 
ATOM   4645  C  CB  . LYS B  1 132 ? -24.249 -13.309 -47.362 1.00 34.69  ?  163  LYS B CB  1 
ATOM   4646  C  CG  . LYS B  1 132 ? -22.927 -13.334 -46.611 1.00 36.12  ?  163  LYS B CG  1 
ATOM   4647  C  CD  . LYS B  1 132 ? -22.054 -14.542 -46.977 1.00 42.22  ?  163  LYS B CD  1 
ATOM   4648  C  CE  . LYS B  1 132 ? -22.715 -15.865 -46.651 1.00 41.25  ?  163  LYS B CE  1 
ATOM   4649  N  NZ  . LYS B  1 132 ? -21.718 -16.980 -46.807 1.00 51.13  ?  163  LYS B NZ  1 
ATOM   4650  N  N   . PHE B  1 133 ? -24.497 -10.693 -45.233 1.00 31.27  ?  164  PHE B N   1 
ATOM   4651  C  CA  . PHE B  1 133 ? -24.709 -10.293 -43.844 1.00 34.11  ?  164  PHE B CA  1 
ATOM   4652  C  C   . PHE B  1 133 ? -25.504 -8.999  -43.718 1.00 32.85  ?  164  PHE B C   1 
ATOM   4653  O  O   . PHE B  1 133 ? -25.724 -8.512  -42.598 1.00 29.91  ?  164  PHE B O   1 
ATOM   4654  C  CB  . PHE B  1 133 ? -23.344 -10.146 -43.147 1.00 28.61  ?  164  PHE B CB  1 
ATOM   4655  C  CG  . PHE B  1 133 ? -22.507 -11.396 -43.208 1.00 27.38  ?  164  PHE B CG  1 
ATOM   4656  C  CD1 . PHE B  1 133 ? -22.980 -12.582 -42.663 1.00 27.83  ?  164  PHE B CD1 1 
ATOM   4657  C  CD2 . PHE B  1 133 ? -21.260 -11.391 -43.815 1.00 31.23  ?  164  PHE B CD2 1 
ATOM   4658  C  CE1 . PHE B  1 133 ? -22.220 -13.743 -42.713 1.00 30.87  ?  164  PHE B CE1 1 
ATOM   4659  C  CE2 . PHE B  1 133 ? -20.479 -12.558 -43.864 1.00 28.81  ?  164  PHE B CE2 1 
ATOM   4660  C  CZ  . PHE B  1 133 ? -20.971 -13.737 -43.313 1.00 29.86  ?  164  PHE B CZ  1 
ATOM   4661  N  N   . HIS B  1 134 ? -25.966 -8.447  -44.837 1.00 32.96  ?  165  HIS B N   1 
ATOM   4662  C  CA  . HIS B  1 134 ? -26.572 -7.129  -44.825 1.00 28.78  ?  165  HIS B CA  1 
ATOM   4663  C  C   . HIS B  1 134 ? -27.944 -7.163  -44.147 1.00 31.10  ?  165  HIS B C   1 
ATOM   4664  O  O   . HIS B  1 134 ? -28.691 -8.143  -44.273 1.00 33.95  ?  165  HIS B O   1 
ATOM   4665  C  CB  . HIS B  1 134 ? -26.715 -6.607  -46.254 1.00 31.12  ?  165  HIS B CB  1 
ATOM   4666  C  CG  . HIS B  1 134 ? -27.044 -5.152  -46.335 1.00 27.23  ?  165  HIS B CG  1 
ATOM   4667  N  ND1 . HIS B  1 134 ? -28.330 -4.672  -46.197 1.00 27.97  ?  165  HIS B ND1 1 
ATOM   4668  C  CD2 . HIS B  1 134 ? -26.256 -4.069  -46.536 1.00 25.56  ?  165  HIS B CD2 1 
ATOM   4669  C  CE1 . HIS B  1 134 ? -28.318 -3.355  -46.311 1.00 28.72  ?  165  HIS B CE1 1 
ATOM   4670  N  NE2 . HIS B  1 134 ? -27.072 -2.966  -46.517 1.00 30.38  ?  165  HIS B NE2 1 
ATOM   4671  N  N   . PRO B  1 135 ? -28.299 -6.092  -43.425 1.00 26.48  ?  166  PRO B N   1 
ATOM   4672  C  CA  . PRO B  1 135 ? -29.645 -6.006  -42.835 1.00 28.17  ?  166  PRO B CA  1 
ATOM   4673  C  C   . PRO B  1 135 ? -30.779 -6.366  -43.785 1.00 28.21  ?  166  PRO B C   1 
ATOM   4674  O  O   . PRO B  1 135 ? -31.705 -7.070  -43.373 1.00 28.74  ?  166  PRO B O   1 
ATOM   4675  C  CB  . PRO B  1 135 ? -29.724 -4.538  -42.405 1.00 25.32  ?  166  PRO B CB  1 
ATOM   4676  C  CG  . PRO B  1 135 ? -28.310 -4.207  -42.014 1.00 29.66  ?  166  PRO B CG  1 
ATOM   4677  C  CD  . PRO B  1 135 ? -27.461 -4.937  -43.060 1.00 28.84  ?  166  PRO B CD  1 
ATOM   4678  N  N   . ASN B  1 136 ? -30.736 -5.903  -45.041 1.00 32.48  ?  167  ASN B N   1 
ATOM   4679  C  CA  . ASN B  1 136 ? -31.833 -6.171  -45.979 1.00 33.60  ?  167  ASN B CA  1 
ATOM   4680  C  C   . ASN B  1 136 ? -31.965 -7.650  -46.305 1.00 36.51  ?  167  ASN B C   1 
ATOM   4681  O  O   . ASN B  1 136 ? -33.050 -8.091  -46.711 1.00 37.44  ?  167  ASN B O   1 
ATOM   4682  C  CB  . ASN B  1 136 ? -31.633 -5.383  -47.273 1.00 31.28  ?  167  ASN B CB  1 
ATOM   4683  C  CG  . ASN B  1 136 ? -31.871 -3.900  -47.095 1.00 33.43  ?  167  ASN B CG  1 
ATOM   4684  O  OD1 . ASN B  1 136 ? -31.158 -3.084  -47.672 1.00 32.95  ?  167  ASN B OD1 1 
ATOM   4685  N  ND2 . ASN B  1 136 ? -32.879 -3.540  -46.294 1.00 32.91  ?  167  ASN B ND2 1 
ATOM   4686  N  N   . LYS B  1 137 ? -30.893 -8.421  -46.128 1.00 31.96  ?  168  LYS B N   1 
ATOM   4687  C  CA  . LYS B  1 137 ? -30.932 -9.866  -46.287 1.00 35.12  ?  168  LYS B CA  1 
ATOM   4688  C  C   . LYS B  1 137 ? -31.200 -10.599 -44.980 1.00 37.51  ?  168  LYS B C   1 
ATOM   4689  O  O   . LYS B  1 137 ? -31.430 -11.812 -45.006 1.00 38.79  ?  168  LYS B O   1 
ATOM   4690  C  CB  . LYS B  1 137 ? -29.610 -10.363 -46.879 1.00 34.32  ?  168  LYS B CB  1 
ATOM   4691  C  CG  . LYS B  1 137 ? -29.273 -9.730  -48.209 1.00 41.52  ?  168  LYS B CG  1 
ATOM   4692  C  CD  . LYS B  1 137 ? -29.215 -10.770 -49.318 1.00 46.09  ?  168  LYS B CD  1 
ATOM   4693  C  CE  . LYS B  1 137 ? -29.035 -10.131 -50.700 1.00 49.96  ?  168  LYS B CE  1 
ATOM   4694  N  NZ  . LYS B  1 137 ? -30.287 -9.524  -51.258 1.00 58.22  ?  168  LYS B NZ  1 
ATOM   4695  N  N   . ARG B  1 138 ? -31.182 -9.869  -43.859 1.00 34.91  ?  169  ARG B N   1 
ATOM   4696  C  CA  . ARG B  1 138 ? -31.354 -10.514 -42.529 1.00 33.52  ?  169  ARG B CA  1 
ATOM   4697  C  C   . ARG B  1 138 ? -32.750 -10.214 -41.958 1.00 34.03  ?  169  ARG B C   1 
ATOM   4698  O  O   . ARG B  1 138 ? -32.919 -10.351 -40.726 1.00 30.56  ?  169  ARG B O   1 
ATOM   4699  C  CB  . ARG B  1 138 ? -30.266 -10.025 -41.566 1.00 34.98  ?  169  ARG B CB  1 
ATOM   4700  C  CG  . ARG B  1 138 ? -28.847 -10.456 -41.912 1.00 36.53  ?  169  ARG B CG  1 
ATOM   4701  C  CD  . ARG B  1 138 ? -28.719 -11.959 -42.114 1.00 40.85  ?  169  ARG B CD  1 
ATOM   4702  N  NE  . ARG B  1 138 ? -28.701 -12.702 -40.849 1.00 37.93  ?  169  ARG B NE  1 
ATOM   4703  C  CZ  . ARG B  1 138 ? -27.786 -13.603 -40.510 1.00 30.94  ?  169  ARG B CZ  1 
ATOM   4704  N  NH1 . ARG B  1 138 ? -26.508 -13.372 -40.751 1.00 35.00  ?  169  ARG B NH1 1 
ATOM   4705  N  NH2 . ARG B  1 138 ? -28.154 -14.728 -39.922 1.00 31.32  ?  169  ARG B NH2 1 
ATOM   4706  N  N   . GLY B  1 139 ? -33.710 -9.830  -42.806 1.00 33.80  ?  170  GLY B N   1 
ATOM   4707  C  CA  . GLY B  1 139 ? -35.052 -9.581  -42.329 1.00 28.40  ?  170  GLY B CA  1 
ATOM   4708  C  C   . GLY B  1 139 ? -35.443 -8.138  -42.094 1.00 31.78  ?  170  GLY B C   1 
ATOM   4709  O  O   . GLY B  1 139 ? -36.500 -7.902  -41.505 1.00 33.08  ?  170  GLY B O   1 
ATOM   4710  N  N   . PHE B  1 140 ? -34.655 -7.157  -42.543 1.00 30.68  ?  171  PHE B N   1 
ATOM   4711  C  CA  . PHE B  1 140 ? -35.039 -5.754  -42.387 1.00 31.67  ?  171  PHE B CA  1 
ATOM   4712  C  C   . PHE B  1 140 ? -35.536 -5.171  -43.716 1.00 33.68  ?  171  PHE B C   1 
ATOM   4713  O  O   . PHE B  1 140 ? -34.807 -5.180  -44.713 1.00 33.38  ?  171  PHE B O   1 
ATOM   4714  C  CB  . PHE B  1 140 ? -33.869 -4.946  -41.827 1.00 29.58  ?  171  PHE B CB  1 
ATOM   4715  C  CG  . PHE B  1 140 ? -33.628 -5.199  -40.349 1.00 28.72  ?  171  PHE B CG  1 
ATOM   4716  C  CD1 . PHE B  1 140 ? -34.493 -4.685  -39.393 1.00 29.34  ?  171  PHE B CD1 1 
ATOM   4717  C  CD2 . PHE B  1 140 ? -32.572 -5.987  -39.936 1.00 29.80  ?  171  PHE B CD2 1 
ATOM   4718  C  CE1 . PHE B  1 140 ? -34.295 -4.923  -38.037 1.00 28.66  ?  171  PHE B CE1 1 
ATOM   4719  C  CE2 . PHE B  1 140 ? -32.353 -6.232  -38.580 1.00 26.27  ?  171  PHE B CE2 1 
ATOM   4720  C  CZ  . PHE B  1 140 ? -33.224 -5.689  -37.628 1.00 28.81  ?  171  PHE B CZ  1 
ATOM   4721  N  N   . ASP B  1 141 ? -36.772 -4.656  -43.723 1.00 33.68  ?  172  ASP B N   1 
ATOM   4722  C  CA  . ASP B  1 141 ? -37.286 -3.967  -44.911 1.00 33.64  ?  172  ASP B CA  1 
ATOM   4723  C  C   . ASP B  1 141 ? -36.467 -2.729  -45.241 1.00 36.28  ?  172  ASP B C   1 
ATOM   4724  O  O   . ASP B  1 141 ? -36.143 -2.488  -46.414 1.00 31.07  ?  172  ASP B O   1 
ATOM   4725  C  CB  . ASP B  1 141 ? -38.754 -3.593  -44.717 1.00 32.25  ?  172  ASP B CB  1 
ATOM   4726  C  CG  . ASP B  1 141 ? -39.655 -4.814  -44.613 1.00 32.78  ?  172  ASP B CG  1 
ATOM   4727  O  OD1 . ASP B  1 141 ? -39.485 -5.746  -45.427 1.00 37.28  ?  172  ASP B OD1 1 
ATOM   4728  O  OD2 . ASP B  1 141 ? -40.524 -4.849  -43.721 1.00 30.60  -1 172  ASP B OD2 1 
ATOM   4729  N  N   . ASP B  1 142 ? -36.115 -1.940  -44.215 1.00 28.95  ?  173  ASP B N   1 
ATOM   4730  C  CA  . ASP B  1 142 ? -35.328 -0.719  -44.337 1.00 29.65  ?  173  ASP B CA  1 
ATOM   4731  C  C   . ASP B  1 142 ? -34.092 -0.812  -43.443 1.00 31.03  ?  173  ASP B C   1 
ATOM   4732  O  O   . ASP B  1 142 ? -34.163 -1.339  -42.325 1.00 30.25  ?  173  ASP B O   1 
ATOM   4733  C  CB  . ASP B  1 142 ? -36.180 0.524   -43.954 1.00 27.33  ?  173  ASP B CB  1 
ATOM   4734  C  CG  . ASP B  1 142 ? -35.592 1.855   -44.483 1.00 40.01  ?  173  ASP B CG  1 
ATOM   4735  O  OD1 . ASP B  1 142 ? -34.607 2.380   -43.894 1.00 40.87  -1 173  ASP B OD1 1 
ATOM   4736  O  OD2 . ASP B  1 142 ? -36.102 2.385   -45.504 1.00 42.73  ?  173  ASP B OD2 1 
ATOM   4737  N  N   . PHE B  1 143 ? -32.963 -0.305  -43.942 1.00 31.04  ?  174  PHE B N   1 
ATOM   4738  C  CA  . PHE B  1 143 ? -31.758 -0.106  -43.141 1.00 26.24  ?  174  PHE B CA  1 
ATOM   4739  C  C   . PHE B  1 143 ? -31.222 1.286   -43.423 1.00 29.29  ?  174  PHE B C   1 
ATOM   4740  O  O   . PHE B  1 143 ? -31.030 1.657   -44.586 1.00 28.72  ?  174  PHE B O   1 
ATOM   4741  C  CB  . PHE B  1 143 ? -30.677 -1.130  -43.452 1.00 30.74  ?  174  PHE B CB  1 
ATOM   4742  C  CG  . PHE B  1 143 ? -29.381 -0.868  -42.718 1.00 27.05  ?  174  PHE B CG  1 
ATOM   4743  C  CD1 . PHE B  1 143 ? -29.361 -0.825  -41.332 1.00 25.56  ?  174  PHE B CD1 1 
ATOM   4744  C  CD2 . PHE B  1 143 ? -28.203 -0.634  -43.414 1.00 28.00  ?  174  PHE B CD2 1 
ATOM   4745  C  CE1 . PHE B  1 143 ? -28.178 -0.582  -40.658 1.00 28.52  ?  174  PHE B CE1 1 
ATOM   4746  C  CE2 . PHE B  1 143 ? -27.021 -0.386  -42.736 1.00 30.66  ?  174  PHE B CE2 1 
ATOM   4747  C  CZ  . PHE B  1 143 ? -27.013 -0.362  -41.369 1.00 23.59  ?  174  PHE B CZ  1 
ATOM   4748  N  N   . TYR B  1 144 ? -30.986 2.059   -42.368 1.00 27.69  ?  175  TYR B N   1 
ATOM   4749  C  CA  . TYR B  1 144 ? -30.293 3.341   -42.471 1.00 27.80  ?  175  TYR B CA  1 
ATOM   4750  C  C   . TYR B  1 144 ? -29.174 3.343   -41.427 1.00 26.81  ?  175  TYR B C   1 
ATOM   4751  O  O   . TYR B  1 144 ? -29.453 3.384   -40.228 1.00 26.62  ?  175  TYR B O   1 
ATOM   4752  C  CB  . TYR B  1 144 ? -31.257 4.512   -42.251 1.00 25.57  ?  175  TYR B CB  1 
ATOM   4753  C  CG  . TYR B  1 144 ? -30.633 5.868   -42.484 1.00 30.34  ?  175  TYR B CG  1 
ATOM   4754  C  CD1 . TYR B  1 144 ? -29.882 6.483   -41.492 1.00 31.36  ?  175  TYR B CD1 1 
ATOM   4755  C  CD2 . TYR B  1 144 ? -30.766 6.518   -43.704 1.00 32.19  ?  175  TYR B CD2 1 
ATOM   4756  C  CE1 . TYR B  1 144 ? -29.289 7.704   -41.697 1.00 29.81  ?  175  TYR B CE1 1 
ATOM   4757  C  CE2 . TYR B  1 144 ? -30.169 7.747   -43.919 1.00 29.31  ?  175  TYR B CE2 1 
ATOM   4758  C  CZ  . TYR B  1 144 ? -29.430 8.331   -42.914 1.00 29.81  ?  175  TYR B CZ  1 
ATOM   4759  O  OH  . TYR B  1 144 ? -28.813 9.554   -43.101 1.00 31.25  ?  175  TYR B OH  1 
ATOM   4760  N  N   . GLY B  1 145 ? -27.916 3.319   -41.870 1.00 25.05  ?  176  GLY B N   1 
ATOM   4761  C  CA  . GLY B  1 145 ? -26.821 3.389   -40.907 1.00 25.68  ?  176  GLY B CA  1 
ATOM   4762  C  C   . GLY B  1 145 ? -25.473 2.976   -41.466 1.00 26.82  ?  176  GLY B C   1 
ATOM   4763  O  O   . GLY B  1 145 ? -25.166 3.242   -42.633 1.00 28.70  ?  176  GLY B O   1 
ATOM   4764  N  N   . PHE B  1 146 ? -24.655 2.334   -40.634 1.00 28.53  ?  177  PHE B N   1 
ATOM   4765  C  CA  . PHE B  1 146 ? -23.322 1.896   -41.016 1.00 23.61  ?  177  PHE B CA  1 
ATOM   4766  C  C   . PHE B  1 146 ? -23.149 0.454   -40.577 1.00 25.14  ?  177  PHE B C   1 
ATOM   4767  O  O   . PHE B  1 146 ? -23.757 0.010   -39.599 1.00 25.27  ?  177  PHE B O   1 
ATOM   4768  C  CB  . PHE B  1 146 ? -22.235 2.790   -40.404 1.00 26.86  ?  177  PHE B CB  1 
ATOM   4769  C  CG  . PHE B  1 146 ? -22.297 2.889   -38.899 1.00 29.77  ?  177  PHE B CG  1 
ATOM   4770  C  CD1 . PHE B  1 146 ? -23.069 3.877   -38.281 1.00 26.85  ?  177  PHE B CD1 1 
ATOM   4771  C  CD2 . PHE B  1 146 ? -21.572 2.005   -38.104 1.00 24.28  ?  177  PHE B CD2 1 
ATOM   4772  C  CE1 . PHE B  1 146 ? -23.111 3.987   -36.892 1.00 26.71  ?  177  PHE B CE1 1 
ATOM   4773  C  CE2 . PHE B  1 146 ? -21.608 2.098   -36.722 1.00 25.03  ?  177  PHE B CE2 1 
ATOM   4774  C  CZ  . PHE B  1 146 ? -22.367 3.103   -36.106 1.00 21.76  ?  177  PHE B CZ  1 
ATOM   4775  N  N   . LEU B  1 147 ? -22.310 -0.277  -41.301 1.00 26.18  ?  178  LEU B N   1 
ATOM   4776  C  CA  . LEU B  1 147 ? -22.245 -1.725  -41.135 1.00 26.07  ?  178  LEU B CA  1 
ATOM   4777  C  C   . LEU B  1 147 ? -21.263 -2.168  -40.066 1.00 25.57  ?  178  LEU B C   1 
ATOM   4778  O  O   . LEU B  1 147 ? -21.413 -3.278  -39.538 1.00 26.53  ?  178  LEU B O   1 
ATOM   4779  C  CB  . LEU B  1 147 ? -21.862 -2.398  -42.469 1.00 28.74  ?  178  LEU B CB  1 
ATOM   4780  C  CG  . LEU B  1 147 ? -22.874 -2.272  -43.615 1.00 29.23  ?  178  LEU B CG  1 
ATOM   4781  C  CD1 . LEU B  1 147 ? -22.294 -2.870  -44.899 1.00 28.57  ?  178  LEU B CD1 1 
ATOM   4782  C  CD2 . LEU B  1 147 ? -24.147 -2.989  -43.250 1.00 26.19  ?  178  LEU B CD2 1 
ATOM   4783  N  N   . GLY B  1 148 ? -20.272 -1.346  -39.746 1.00 26.16  ?  179  GLY B N   1 
ATOM   4784  C  CA  . GLY B  1 148 ? -19.222 -1.718  -38.819 1.00 27.71  ?  179  GLY B CA  1 
ATOM   4785  C  C   . GLY B  1 148 ? -19.518 -1.336  -37.382 1.00 25.36  ?  179  GLY B C   1 
ATOM   4786  O  O   . GLY B  1 148 ? -20.674 -1.219  -36.959 1.00 26.26  ?  179  GLY B O   1 
ATOM   4787  N  N   . GLY B  1 149 ? -18.438 -1.166  -36.610 1.00 24.15  ?  180  GLY B N   1 
ATOM   4788  C  CA  . GLY B  1 149 ? -18.535 -1.026  -35.170 1.00 23.92  ?  180  GLY B CA  1 
ATOM   4789  C  C   . GLY B  1 149 ? -18.605 0.384   -34.607 1.00 28.60  ?  180  GLY B C   1 
ATOM   4790  O  O   . GLY B  1 149 ? -18.805 0.528   -33.393 1.00 27.55  ?  180  GLY B O   1 
ATOM   4791  N  N   . GLY B  1 150 ? -18.458 1.421   -35.430 1.00 23.30  ?  181  GLY B N   1 
ATOM   4792  C  CA  . GLY B  1 150 ? -18.514 2.790   -34.929 1.00 23.71  ?  181  GLY B CA  1 
ATOM   4793  C  C   . GLY B  1 150 ? -18.559 3.788   -36.068 1.00 27.40  ?  181  GLY B C   1 
ATOM   4794  O  O   . GLY B  1 150 ? -18.415 3.431   -37.242 1.00 23.94  ?  181  GLY B O   1 
ATOM   4795  N  N   . HIS B  1 151 ? -18.778 5.058   -35.713 1.00 24.36  ?  182  HIS B N   1 
ATOM   4796  C  CA  . HIS B  1 151 ? -18.806 6.107   -36.725 1.00 22.47  ?  182  HIS B CA  1 
ATOM   4797  C  C   . HIS B  1 151 ? -18.556 7.479   -36.107 1.00 26.76  ?  182  HIS B C   1 
ATOM   4798  O  O   . HIS B  1 151 ? -19.044 7.770   -35.014 1.00 25.05  ?  182  HIS B O   1 
ATOM   4799  C  CB  . HIS B  1 151 ? -20.142 6.129   -37.491 1.00 24.55  ?  182  HIS B CB  1 
ATOM   4800  C  CG  . HIS B  1 151 ? -19.982 6.603   -38.903 1.00 26.71  ?  182  HIS B CG  1 
ATOM   4801  N  ND1 . HIS B  1 151 ? -19.859 7.941   -39.224 1.00 26.10  ?  182  HIS B ND1 1 
ATOM   4802  C  CD2 . HIS B  1 151 ? -19.817 5.919   -40.060 1.00 25.43  ?  182  HIS B CD2 1 
ATOM   4803  C  CE1 . HIS B  1 151 ? -19.680 8.061   -40.529 1.00 28.63  ?  182  HIS B CE1 1 
ATOM   4804  N  NE2 . HIS B  1 151 ? -19.642 6.848   -41.057 1.00 27.82  ?  182  HIS B NE2 1 
ATOM   4805  N  N   . ASP B  1 152 ? -17.815 8.334   -36.815 1.00 27.31  ?  183  ASP B N   1 
ATOM   4806  C  CA  . ASP B  1 152 ? -17.742 9.732   -36.387 1.00 26.26  ?  183  ASP B CA  1 
ATOM   4807  C  C   . ASP B  1 152 ? -19.118 10.382  -36.509 1.00 26.68  ?  183  ASP B C   1 
ATOM   4808  O  O   . ASP B  1 152 ? -19.937 10.003  -37.357 1.00 24.00  ?  183  ASP B O   1 
ATOM   4809  C  CB  . ASP B  1 152 ? -16.711 10.500  -37.210 1.00 25.20  ?  183  ASP B CB  1 
ATOM   4810  C  CG  . ASP B  1 152 ? -15.253 10.118  -36.838 1.00 31.54  ?  183  ASP B CG  1 
ATOM   4811  O  OD1 . ASP B  1 152 ? -15.030 9.095   -36.151 1.00 27.05  ?  183  ASP B OD1 1 
ATOM   4812  O  OD2 . ASP B  1 152 ? -14.334 10.842  -37.249 1.00 35.40  -1 183  ASP B OD2 1 
ATOM   4813  N  N   . TYR B  1 153 ? -19.362 11.403  -35.680 1.00 25.71  ?  184  TYR B N   1 
ATOM   4814  C  CA  . TYR B  1 153 ? -20.728 11.876  -35.488 1.00 27.74  ?  184  TYR B CA  1 
ATOM   4815  C  C   . TYR B  1 153 ? -21.133 13.058  -36.369 1.00 29.28  ?  184  TYR B C   1 
ATOM   4816  O  O   . TYR B  1 153 ? -22.339 13.268  -36.554 1.00 26.97  ?  184  TYR B O   1 
ATOM   4817  C  CB  . TYR B  1 153 ? -20.951 12.273  -34.021 1.00 25.21  ?  184  TYR B CB  1 
ATOM   4818  C  CG  . TYR B  1 153 ? -21.057 11.104  -33.069 1.00 23.05  ?  184  TYR B CG  1 
ATOM   4819  C  CD1 . TYR B  1 153 ? -19.910 10.497  -32.562 1.00 25.49  ?  184  TYR B CD1 1 
ATOM   4820  C  CD2 . TYR B  1 153 ? -22.296 10.612  -32.673 1.00 26.19  ?  184  TYR B CD2 1 
ATOM   4821  C  CE1 . TYR B  1 153 ? -20.002 9.432   -31.695 1.00 24.80  ?  184  TYR B CE1 1 
ATOM   4822  C  CE2 . TYR B  1 153 ? -22.404 9.548   -31.812 1.00 22.73  ?  184  TYR B CE2 1 
ATOM   4823  C  CZ  . TYR B  1 153 ? -21.255 8.959   -31.319 1.00 23.86  ?  184  TYR B CZ  1 
ATOM   4824  O  OH  . TYR B  1 153 ? -21.341 7.888   -30.447 1.00 24.64  ?  184  TYR B OH  1 
ATOM   4825  N  N   . PHE B  1 154 ? -20.186 13.863  -36.883 1.00 27.23  ?  185  PHE B N   1 
ATOM   4826  C  CA  . PHE B  1 154 ? -20.563 15.067  -37.636 1.00 28.83  ?  185  PHE B CA  1 
ATOM   4827  C  C   . PHE B  1 154 ? -20.339 14.892  -39.140 1.00 28.61  ?  185  PHE B C   1 
ATOM   4828  O  O   . PHE B  1 154 ? -19.179 14.880  -39.593 1.00 26.72  ?  185  PHE B O   1 
ATOM   4829  C  CB  . PHE B  1 154 ? -19.789 16.287  -37.129 1.00 28.88  ?  185  PHE B CB  1 
ATOM   4830  C  CG  . PHE B  1 154 ? -20.330 16.862  -35.827 1.00 32.22  ?  185  PHE B CG  1 
ATOM   4831  C  CD1 . PHE B  1 154 ? -21.437 17.713  -35.828 1.00 32.56  ?  185  PHE B CD1 1 
ATOM   4832  C  CD2 . PHE B  1 154 ? -19.725 16.548  -34.609 1.00 29.51  ?  185  PHE B CD2 1 
ATOM   4833  C  CE1 . PHE B  1 154 ? -21.936 18.254  -34.629 1.00 33.64  ?  185  PHE B CE1 1 
ATOM   4834  C  CE2 . PHE B  1 154 ? -20.206 17.085  -33.400 1.00 29.75  ?  185  PHE B CE2 1 
ATOM   4835  C  CZ  . PHE B  1 154 ? -21.320 17.931  -33.413 1.00 30.19  ?  185  PHE B CZ  1 
ATOM   4836  N  N   . PRO B  1 155 ? -21.394 14.804  -39.961 1.00 28.28  ?  186  PRO B N   1 
ATOM   4837  C  CA  . PRO B  1 155 ? -21.173 14.612  -41.408 1.00 28.04  ?  186  PRO B CA  1 
ATOM   4838  C  C   . PRO B  1 155 ? -20.344 15.712  -42.054 1.00 31.26  ?  186  PRO B C   1 
ATOM   4839  O  O   . PRO B  1 155 ? -19.560 15.416  -42.959 1.00 29.49  ?  186  PRO B O   1 
ATOM   4840  C  CB  . PRO B  1 155 ? -22.602 14.534  -41.985 1.00 29.72  ?  186  PRO B CB  1 
ATOM   4841  C  CG  . PRO B  1 155 ? -23.510 15.087  -40.916 1.00 31.27  ?  186  PRO B CG  1 
ATOM   4842  C  CD  . PRO B  1 155 ? -22.826 14.773  -39.606 1.00 25.54  ?  186  PRO B CD  1 
ATOM   4843  N  N   . SER B  1 156 ? -20.431 16.961  -41.588 1.00 29.85  ?  187  SER B N   1 
ATOM   4844  C  CA  . SER B  1 156 ? -19.576 17.991  -42.167 1.00 30.53  ?  187  SER B CA  1 
ATOM   4845  C  C   . SER B  1 156 ? -18.109 17.708  -41.920 1.00 38.16  ?  187  SER B C   1 
ATOM   4846  O  O   . SER B  1 156 ? -17.259 18.193  -42.678 1.00 33.53  ?  187  SER B O   1 
ATOM   4847  C  CB  . SER B  1 156 ? -19.928 19.374  -41.610 1.00 36.39  ?  187  SER B CB  1 
ATOM   4848  O  OG  . SER B  1 156 ? -19.679 19.462  -40.220 1.00 34.99  ?  187  SER B OG  1 
ATOM   4849  N  N   . GLU B  1 157 ? -17.793 16.928  -40.885 1.00 31.99  ?  188  GLU B N   1 
ATOM   4850  C  CA  . GLU B  1 157 ? -16.405 16.590  -40.651 1.00 30.16  ?  188  GLU B CA  1 
ATOM   4851  C  C   . GLU B  1 157 ? -16.018 15.302  -41.366 1.00 30.52  ?  188  GLU B C   1 
ATOM   4852  O  O   . GLU B  1 157 ? -15.026 15.273  -42.102 1.00 32.45  ?  188  GLU B O   1 
ATOM   4853  C  CB  . GLU B  1 157 ? -16.119 16.439  -39.153 1.00 32.26  ?  188  GLU B CB  1 
ATOM   4854  C  CG  . GLU B  1 157 ? -16.094 17.768  -38.435 1.00 32.15  ?  188  GLU B CG  1 
ATOM   4855  C  CD  . GLU B  1 157 ? -16.122 17.636  -36.927 1.00 40.65  ?  188  GLU B CD  1 
ATOM   4856  O  OE1 . GLU B  1 157 ? -16.344 16.526  -36.395 1.00 41.97  ?  188  GLU B OE1 1 
ATOM   4857  O  OE2 . GLU B  1 157 ? -15.966 18.685  -36.265 1.00 52.03  -1 188  GLU B OE2 1 
ATOM   4858  N  N   . TYR B  1 158 ? -16.773 14.223  -41.164 1.00 26.76  ?  189  TYR B N   1 
ATOM   4859  C  CA  . TYR B  1 158 ? -16.312 12.945  -41.709 1.00 29.84  ?  189  TYR B CA  1 
ATOM   4860  C  C   . TYR B  1 158 ? -16.453 12.860  -43.232 1.00 29.35  ?  189  TYR B C   1 
ATOM   4861  O  O   . TYR B  1 158 ? -15.654 12.166  -43.873 1.00 28.65  ?  189  TYR B O   1 
ATOM   4862  C  CB  . TYR B  1 158 ? -17.005 11.767  -41.006 1.00 26.52  ?  189  TYR B CB  1 
ATOM   4863  C  CG  . TYR B  1 158 ? -18.493 11.512  -41.251 1.00 27.06  ?  189  TYR B CG  1 
ATOM   4864  C  CD1 . TYR B  1 158 ? -18.958 11.056  -42.473 1.00 27.71  ?  189  TYR B CD1 1 
ATOM   4865  C  CD2 . TYR B  1 158 ? -19.415 11.658  -40.217 1.00 28.90  ?  189  TYR B CD2 1 
ATOM   4866  C  CE1 . TYR B  1 158 ? -20.318 10.797  -42.695 1.00 26.45  ?  189  TYR B CE1 1 
ATOM   4867  C  CE2 . TYR B  1 158 ? -20.781 11.391  -40.416 1.00 26.71  ?  189  TYR B CE2 1 
ATOM   4868  C  CZ  . TYR B  1 158 ? -21.218 10.963  -41.662 1.00 30.11  ?  189  TYR B CZ  1 
ATOM   4869  O  OH  . TYR B  1 158 ? -22.554 10.693  -41.878 1.00 27.74  ?  189  TYR B OH  1 
ATOM   4870  N  N   . GLN B  1 159 ? -17.450 13.528  -43.828 1.00 28.70  ?  190  GLN B N   1 
ATOM   4871  C  CA  . GLN B  1 159 ? -17.570 13.501  -45.285 1.00 28.77  ?  190  GLN B CA  1 
ATOM   4872  C  C   . GLN B  1 159 ? -16.427 14.261  -45.930 1.00 31.21  ?  190  GLN B C   1 
ATOM   4873  O  O   . GLN B  1 159 ? -15.912 13.843  -46.969 1.00 30.37  ?  190  GLN B O   1 
ATOM   4874  C  CB  . GLN B  1 159 ? -18.914 14.089  -45.734 1.00 29.97  ?  190  GLN B CB  1 
ATOM   4875  C  CG  . GLN B  1 159 ? -20.103 13.191  -45.470 1.00 29.82  ?  190  GLN B CG  1 
ATOM   4876  C  CD  . GLN B  1 159 ? -21.418 13.937  -45.533 1.00 33.23  ?  190  GLN B CD  1 
ATOM   4877  O  OE1 . GLN B  1 159 ? -21.440 15.156  -45.714 1.00 33.74  ?  190  GLN B OE1 1 
ATOM   4878  N  NE2 . GLN B  1 159 ? -22.519 13.220  -45.346 1.00 27.70  ?  190  GLN B NE2 1 
ATOM   4879  N  N   . LYS B  1 160 ? -16.025 15.386  -45.325 1.00 30.15  ?  191  LYS B N   1 
ATOM   4880  C  CA  . LYS B  1 160 ? -14.824 16.109  -45.750 1.00 32.66  ?  191  LYS B CA  1 
ATOM   4881  C  C   . LYS B  1 160 ? -13.584 15.224  -45.697 1.00 36.56  ?  191  LYS B C   1 
ATOM   4882  O  O   . LYS B  1 160 ? -12.787 15.191  -46.641 1.00 31.85  ?  191  LYS B O   1 
ATOM   4883  C  CB  . LYS B  1 160 ? -14.622 17.346  -44.869 1.00 38.88  ?  191  LYS B CB  1 
ATOM   4884  C  CG  . LYS B  1 160 ? -13.420 18.239  -45.254 1.00 41.70  ?  191  LYS B CG  1 
ATOM   4885  C  CD  . LYS B  1 160 ? -13.393 19.509  -44.400 1.00 45.52  ?  191  LYS B CD  1 
ATOM   4886  C  CE  . LYS B  1 160 ? -12.224 20.439  -44.766 1.00 54.06  ?  191  LYS B CE  1 
ATOM   4887  N  NZ  . LYS B  1 160 ? -12.406 21.151  -46.073 1.00 52.43  ?  191  LYS B NZ  1 
ATOM   4888  N  N   . THR B  1 161 ? -13.382 14.525  -44.581 1.00 28.76  ?  192  THR B N   1 
ATOM   4889  C  CA  . THR B  1 161 ? -12.217 13.664  -44.472 1.00 33.45  ?  192  THR B CA  1 
ATOM   4890  C  C   . THR B  1 161 ? -12.256 12.547  -45.503 1.00 29.76  ?  192  THR B C   1 
ATOM   4891  O  O   . THR B  1 161 ? -11.264 12.298  -46.201 1.00 31.71  ?  192  THR B O   1 
ATOM   4892  C  CB  . THR B  1 161 ? -12.121 13.107  -43.052 1.00 33.46  ?  192  THR B CB  1 
ATOM   4893  O  OG1 . THR B  1 161 ? -11.907 14.204  -42.151 1.00 32.26  ?  192  THR B OG1 1 
ATOM   4894  C  CG2 . THR B  1 161 ? -10.969 12.116  -42.949 1.00 30.76  ?  192  THR B CG2 1 
ATOM   4895  N  N   . TYR B  1 162 ? -13.391 11.857  -45.608 1.00 29.16  ?  193  TYR B N   1 
ATOM   4896  C  CA  . TYR B  1 162 ? -13.509 10.766  -46.563 1.00 30.11  ?  193  TYR B CA  1 
ATOM   4897  C  C   . TYR B  1 162 ? -13.174 11.236  -47.975 1.00 33.83  ?  193  TYR B C   1 
ATOM   4898  O  O   . TYR B  1 162 ? -12.358 10.611  -48.664 1.00 29.57  ?  193  TYR B O   1 
ATOM   4899  C  CB  . TYR B  1 162 ? -14.920 10.173  -46.524 1.00 27.63  ?  193  TYR B CB  1 
ATOM   4900  C  CG  . TYR B  1 162 ? -15.113 9.026   -47.478 1.00 30.35  ?  193  TYR B CG  1 
ATOM   4901  C  CD1 . TYR B  1 162 ? -14.639 7.764   -47.179 1.00 30.01  ?  193  TYR B CD1 1 
ATOM   4902  C  CD2 . TYR B  1 162 ? -15.750 9.215   -48.707 1.00 33.13  ?  193  TYR B CD2 1 
ATOM   4903  C  CE1 . TYR B  1 162 ? -14.809 6.708   -48.056 1.00 32.17  ?  193  TYR B CE1 1 
ATOM   4904  C  CE2 . TYR B  1 162 ? -15.911 8.173   -49.592 1.00 33.46  ?  193  TYR B CE2 1 
ATOM   4905  C  CZ  . TYR B  1 162 ? -15.444 6.922   -49.265 1.00 34.16  ?  193  TYR B CZ  1 
ATOM   4906  O  OH  . TYR B  1 162 ? -15.615 5.875   -50.138 1.00 30.87  ?  193  TYR B OH  1 
ATOM   4907  N  N   . LYS B  1 163 ? -13.804 12.337  -48.423 1.00 33.46  ?  194  LYS B N   1 
ATOM   4908  C  CA  . LYS B  1 163 ? -13.591 12.812  -49.788 1.00 33.64  ?  194  LYS B CA  1 
ATOM   4909  C  C   . LYS B  1 163 ? -12.126 13.132  -50.049 1.00 34.91  ?  194  LYS B C   1 
ATOM   4910  O  O   . LYS B  1 163 ? -11.594 12.773  -51.104 1.00 35.30  ?  194  LYS B O   1 
ATOM   4911  C  CB  . LYS B  1 163 ? -14.465 14.032  -50.086 1.00 33.02  ?  194  LYS B CB  1 
ATOM   4912  C  CG  . LYS B  1 163 ? -15.947 13.696  -50.324 1.00 37.20  ?  194  LYS B CG  1 
ATOM   4913  C  CD  . LYS B  1 163 ? -16.807 14.945  -50.490 1.00 47.33  ?  194  LYS B CD  1 
ATOM   4914  C  CE  . LYS B  1 163 ? -18.227 14.763  -49.936 1.00 51.19  ?  194  LYS B CE  1 
ATOM   4915  N  NZ  . LYS B  1 163 ? -18.739 16.007  -49.275 1.00 56.23  ?  194  LYS B NZ  1 
ATOM   4916  N  N   . ALA B  1 164 ? -11.461 13.803  -49.103 1.00 32.91  ?  195  ALA B N   1 
ATOM   4917  C  CA  . ALA B  1 164 ? -10.055 14.146  -49.293 1.00 33.83  ?  195  ALA B CA  1 
ATOM   4918  C  C   . ALA B  1 164 ? -9.186  12.900  -49.321 1.00 35.46  ?  195  ALA B C   1 
ATOM   4919  O  O   . ALA B  1 164 ? -8.215  12.825  -50.083 1.00 34.24  ?  195  ALA B O   1 
ATOM   4920  C  CB  . ALA B  1 164 ? -9.583  15.089  -48.190 1.00 33.27  ?  195  ALA B CB  1 
ATOM   4921  N  N   . GLN B  1 165 ? -9.494  11.925  -48.469 1.00 33.42  ?  196  GLN B N   1 
ATOM   4922  C  CA  . GLN B  1 165 ? -8.692  10.709  -48.432 1.00 32.47  ?  196  GLN B CA  1 
ATOM   4923  C  C   . GLN B  1 165 ? -8.928  9.861   -49.672 1.00 31.44  ?  196  GLN B C   1 
ATOM   4924  O  O   . GLN B  1 165 ? -7.995  9.234   -50.180 1.00 30.58  ?  196  GLN B O   1 
ATOM   4925  C  CB  . GLN B  1 165 ? -9.008  9.929   -47.155 1.00 30.01  ?  196  GLN B CB  1 
ATOM   4926  C  CG  . GLN B  1 165 ? -8.305  10.524  -45.952 1.00 33.45  ?  196  GLN B CG  1 
ATOM   4927  C  CD  . GLN B  1 165 ? -8.619  9.795   -44.661 1.00 44.74  ?  196  GLN B CD  1 
ATOM   4928  O  OE1 . GLN B  1 165 ? -9.107  8.670   -44.687 1.00 44.54  ?  196  GLN B OE1 1 
ATOM   4929  N  NE2 . GLN B  1 165 ? -8.211  10.378  -43.524 1.00 44.74  ?  196  GLN B NE2 1 
ATOM   4930  N  N   . LYS B  1 166 ? -10.167 9.838   -50.173 1.00 29.62  ?  197  LYS B N   1 
ATOM   4931  C  CA  . LYS B  1 166 ? -10.461 9.095   -51.391 1.00 34.43  ?  197  LYS B CA  1 
ATOM   4932  C  C   . LYS B  1 166 ? -9.781  9.758   -52.588 1.00 33.19  ?  197  LYS B C   1 
ATOM   4933  O  O   . LYS B  1 166 ? -9.230  9.078   -53.458 1.00 32.22  ?  197  LYS B O   1 
ATOM   4934  C  CB  . LYS B  1 166 ? -11.973 9.050   -51.613 1.00 31.99  ?  197  LYS B CB  1 
ATOM   4935  C  CG  . LYS B  1 166 ? -12.504 7.890   -52.441 1.00 44.02  ?  197  LYS B CG  1 
ATOM   4936  C  CD  . LYS B  1 166 ? -12.389 6.580   -51.639 1.00 46.67  ?  197  LYS B CD  1 
ATOM   4937  C  CE  . LYS B  1 166 ? -12.454 5.315   -52.515 1.00 56.64  ?  197  LYS B CE  1 
ATOM   4938  N  NZ  . LYS B  1 166 ? -11.126 4.581   -52.512 1.00 60.84  ?  197  LYS B NZ  1 
ATOM   4939  N  N   . LYS B  1 167 ? -9.807  11.096  -52.634 1.00 35.92  ?  198  LYS B N   1 
ATOM   4940  C  CA  . LYS B  1 167 ? -9.095  11.854  -53.665 1.00 35.78  ?  198  LYS B CA  1 
ATOM   4941  C  C   . LYS B  1 167 ? -7.598  11.581  -53.625 1.00 34.54  ?  198  LYS B C   1 
ATOM   4942  O  O   . LYS B  1 167 ? -6.936  11.520  -54.670 1.00 35.40  ?  198  LYS B O   1 
ATOM   4943  C  CB  . LYS B  1 167 ? -9.365  13.348  -53.479 1.00 37.52  ?  198  LYS B CB  1 
ATOM   4944  C  CG  . LYS B  1 167 ? -8.879  14.259  -54.602 1.00 41.28  ?  198  LYS B CG  1 
ATOM   4945  C  CD  . LYS B  1 167 ? -9.493  15.657  -54.444 1.00 49.57  ?  198  LYS B CD  1 
ATOM   4946  C  CE  . LYS B  1 167 ? -8.612  16.749  -55.054 1.00 59.06  ?  198  LYS B CE  1 
ATOM   4947  N  NZ  . LYS B  1 167 ? -8.112  17.727  -54.018 1.00 56.18  ?  198  LYS B NZ  1 
ATOM   4948  N  N   . ALA B  1 168 ? -7.047  11.397  -52.437 1.00 34.26  ?  199  ALA B N   1 
ATOM   4949  C  CA  . ALA B  1 168 ? -5.622  11.152  -52.327 1.00 33.68  ?  199  ALA B CA  1 
ATOM   4950  C  C   . ALA B  1 168 ? -5.266  9.688   -52.527 1.00 32.91  ?  199  ALA B C   1 
ATOM   4951  O  O   . ALA B  1 168 ? -4.091  9.341   -52.441 1.00 31.51  ?  199  ALA B O   1 
ATOM   4952  C  CB  . ALA B  1 168 ? -5.116  11.635  -50.969 1.00 36.44  ?  199  ALA B CB  1 
ATOM   4953  N  N   . GLY B  1 169 ? -6.240  8.833   -52.805 1.00 31.72  ?  200  GLY B N   1 
ATOM   4954  C  CA  . GLY B  1 169 ? -5.973  7.420   -52.992 1.00 30.40  ?  200  GLY B CA  1 
ATOM   4955  C  C   . GLY B  1 169 ? -5.512  6.695   -51.744 1.00 34.14  ?  200  GLY B C   1 
ATOM   4956  O  O   . GLY B  1 169 ? -4.747  5.733   -51.849 1.00 31.59  ?  200  GLY B O   1 
ATOM   4957  N  N   . ASN B  1 170 ? -5.967  7.121   -50.567 1.00 33.89  ?  201  ASN B N   1 
ATOM   4958  C  CA  . ASN B  1 170 ? -5.598  6.476   -49.302 1.00 30.54  ?  201  ASN B CA  1 
ATOM   4959  C  C   . ASN B  1 170 ? -6.134  5.054   -49.323 1.00 28.96  ?  201  ASN B C   1 
ATOM   4960  O  O   . ASN B  1 170 ? -7.343  4.857   -49.516 1.00 31.54  ?  201  ASN B O   1 
ATOM   4961  C  CB  . ASN B  1 170 ? -6.171  7.281   -48.128 1.00 30.87  ?  201  ASN B CB  1 
ATOM   4962  C  CG  . ASN B  1 170 ? -5.722  6.778   -46.743 1.00 37.41  ?  201  ASN B CG  1 
ATOM   4963  O  OD1 . ASN B  1 170 ? -5.498  5.578   -46.509 1.00 34.33  ?  201  ASN B OD1 1 
ATOM   4964  N  ND2 . ASN B  1 170 ? -5.583  7.724   -45.820 1.00 33.73  ?  201  ASN B ND2 1 
ATOM   4965  N  N   . PRO B  1 171 ? -5.278  4.037   -49.217 1.00 33.27  ?  202  PRO B N   1 
ATOM   4966  C  CA  . PRO B  1 171 ? -5.782  2.667   -49.241 1.00 36.39  ?  202  PRO B CA  1 
ATOM   4967  C  C   . PRO B  1 171 ? -6.239  2.177   -47.879 1.00 38.64  ?  202  PRO B C   1 
ATOM   4968  O  O   . PRO B  1 171 ? -6.812  1.080   -47.806 1.00 40.99  ?  202  PRO B O   1 
ATOM   4969  C  CB  . PRO B  1 171 ? -4.576  1.870   -49.755 1.00 36.11  ?  202  PRO B CB  1 
ATOM   4970  C  CG  . PRO B  1 171 ? -3.423  2.599   -49.239 1.00 35.14  ?  202  PRO B CG  1 
ATOM   4971  C  CD  . PRO B  1 171 ? -3.808  4.074   -49.229 1.00 38.39  ?  202  PRO B CD  1 
ATOM   4972  N  N   . ASN B  1 172 ? -6.025  2.952   -46.813 1.00 34.30  ?  203  ASN B N   1 
ATOM   4973  C  CA  . ASN B  1 172 ? -6.439  2.523   -45.476 1.00 39.42  ?  203  ASN B CA  1 
ATOM   4974  C  C   . ASN B  1 172 ? -7.393  3.517   -44.825 1.00 33.79  ?  203  ASN B C   1 
ATOM   4975  O  O   . ASN B  1 172 ? -7.144  3.982   -43.710 1.00 35.96  ?  203  ASN B O   1 
ATOM   4976  C  CB  . ASN B  1 172 ? -5.230  2.326   -44.548 1.00 38.35  ?  203  ASN B CB  1 
ATOM   4977  C  CG  . ASN B  1 172 ? -4.061  1.622   -45.232 1.00 46.81  ?  203  ASN B CG  1 
ATOM   4978  O  OD1 . ASN B  1 172 ? -4.211  0.503   -45.749 1.00 48.21  ?  203  ASN B OD1 1 
ATOM   4979  N  ND2 . ASN B  1 172 ? -2.881  2.258   -45.201 1.00 42.32  ?  203  ASN B ND2 1 
ATOM   4980  N  N   . ILE B  1 173 ? -8.476  3.865   -45.511 1.00 33.33  ?  204  ILE B N   1 
ATOM   4981  C  CA  . ILE B  1 173 ? -9.450  4.777   -44.933 1.00 33.01  ?  204  ILE B CA  1 
ATOM   4982  C  C   . ILE B  1 173 ? -10.234 4.064   -43.837 1.00 32.06  ?  204  ILE B C   1 
ATOM   4983  O  O   . ILE B  1 173 ? -10.748 2.952   -44.038 1.00 29.08  ?  204  ILE B O   1 
ATOM   4984  C  CB  . ILE B  1 173 ? -10.383 5.314   -46.025 1.00 31.43  ?  204  ILE B CB  1 
ATOM   4985  C  CG1 . ILE B  1 173 ? -9.555  6.115   -47.058 1.00 31.19  ?  204  ILE B CG1 1 
ATOM   4986  C  CG2 . ILE B  1 173 ? -11.482 6.136   -45.375 1.00 25.66  ?  204  ILE B CG2 1 
ATOM   4987  C  CD1 . ILE B  1 173 ? -10.367 6.633   -48.306 1.00 28.01  ?  204  ILE B CD1 1 
ATOM   4988  N  N   . ARG B  1 174 ? -10.349 4.714   -42.680 1.00 29.93  ?  205  ARG B N   1 
ATOM   4989  C  CA  . ARG B  1 174 ? -11.042 4.114   -41.544 1.00 31.72  ?  205  ARG B CA  1 
ATOM   4990  C  C   . ARG B  1 174 ? -12.540 4.048   -41.807 1.00 28.91  ?  205  ARG B C   1 
ATOM   4991  O  O   . ARG B  1 174 ? -13.140 5.008   -42.297 1.00 29.25  ?  205  ARG B O   1 
ATOM   4992  C  CB  . ARG B  1 174 ? -10.793 4.935   -40.296 1.00 30.41  ?  205  ARG B CB  1 
ATOM   4993  C  CG  . ARG B  1 174 ? -9.347  5.012   -39.903 1.00 40.47  ?  205  ARG B CG  1 
ATOM   4994  C  CD  . ARG B  1 174 ? -9.237  6.069   -38.836 1.00 50.27  ?  205  ARG B CD  1 
ATOM   4995  N  NE  . ARG B  1 174 ? -10.134 5.754   -37.731 1.00 52.83  ?  205  ARG B NE  1 
ATOM   4996  C  CZ  . ARG B  1 174 ? -10.874 6.645   -37.090 1.00 49.30  ?  205  ARG B CZ  1 
ATOM   4997  N  NH1 . ARG B  1 174 ? -10.929 7.908   -37.490 1.00 44.60  ?  205  ARG B NH1 1 
ATOM   4998  N  NH2 . ARG B  1 174 ? -11.600 6.250   -36.044 1.00 47.42  ?  205  ARG B NH2 1 
ATOM   4999  N  N   . ASP B  1 175 ? -13.160 2.927   -41.438 1.00 25.64  ?  206  ASP B N   1 
ATOM   5000  C  CA  . ASP B  1 175 ? -14.583 2.844   -41.739 1.00 29.26  ?  206  ASP B CA  1 
ATOM   5001  C  C   . ASP B  1 175 ? -15.403 3.831   -40.915 1.00 27.52  ?  206  ASP B C   1 
ATOM   5002  O  O   . ASP B  1 175 ? -16.547 4.106   -41.283 1.00 31.11  ?  206  ASP B O   1 
ATOM   5003  C  CB  . ASP B  1 175 ? -15.088 1.396   -41.588 1.00 30.09  ?  206  ASP B CB  1 
ATOM   5004  C  CG  . ASP B  1 175 ? -14.839 0.777   -40.214 1.00 33.14  ?  206  ASP B CG  1 
ATOM   5005  O  OD1 . ASP B  1 175 ? -14.402 1.456   -39.251 1.00 30.04  ?  206  ASP B OD1 1 
ATOM   5006  O  OD2 . ASP B  1 175 ? -15.083 -0.454  -40.112 1.00 32.40  -1 206  ASP B OD2 1 
ATOM   5007  N  N   . TYR B  1 176 ? -14.820 4.426   -39.864 1.00 25.12  ?  207  TYR B N   1 
ATOM   5008  C  CA  . TYR B  1 176 ? -15.528 5.436   -39.080 1.00 25.70  ?  207  TYR B CA  1 
ATOM   5009  C  C   . TYR B  1 176 ? -15.873 6.682   -39.891 1.00 27.75  ?  207  TYR B C   1 
ATOM   5010  O  O   . TYR B  1 176 ? -16.651 7.516   -39.417 1.00 28.12  ?  207  TYR B O   1 
ATOM   5011  C  CB  . TYR B  1 176 ? -14.684 5.850   -37.871 1.00 26.79  ?  207  TYR B CB  1 
ATOM   5012  C  CG  . TYR B  1 176 ? -14.905 5.014   -36.625 1.00 30.55  ?  207  TYR B CG  1 
ATOM   5013  C  CD1 . TYR B  1 176 ? -14.778 3.619   -36.650 1.00 28.87  ?  207  TYR B CD1 1 
ATOM   5014  C  CD2 . TYR B  1 176 ? -15.249 5.627   -35.414 1.00 29.44  ?  207  TYR B CD2 1 
ATOM   5015  C  CE1 . TYR B  1 176 ? -15.000 2.857   -35.498 1.00 28.86  ?  207  TYR B CE1 1 
ATOM   5016  C  CE2 . TYR B  1 176 ? -15.493 4.872   -34.257 1.00 29.34  ?  207  TYR B CE2 1 
ATOM   5017  C  CZ  . TYR B  1 176 ? -15.355 3.503   -34.300 1.00 28.49  ?  207  TYR B CZ  1 
ATOM   5018  O  OH  . TYR B  1 176 ? -15.575 2.781   -33.147 1.00 27.14  ?  207  TYR B OH  1 
ATOM   5019  N  N   . VAL B  1 177 ? -15.256 6.884   -41.057 1.00 24.18  ?  208  VAL B N   1 
ATOM   5020  C  CA  . VAL B  1 177 ? -15.589 8.029   -41.897 1.00 28.26  ?  208  VAL B CA  1 
ATOM   5021  C  C   . VAL B  1 177 ? -16.270 7.624   -43.208 1.00 26.99  ?  208  VAL B C   1 
ATOM   5022  O  O   . VAL B  1 177 ? -16.561 8.505   -44.040 1.00 28.24  ?  208  VAL B O   1 
ATOM   5023  C  CB  . VAL B  1 177 ? -14.351 8.912   -42.165 1.00 26.07  ?  208  VAL B CB  1 
ATOM   5024  C  CG1 . VAL B  1 177 ? -13.738 9.408   -40.834 1.00 30.39  ?  208  VAL B CG1 1 
ATOM   5025  C  CG2 . VAL B  1 177 ? -13.284 8.165   -42.973 1.00 26.16  ?  208  VAL B CG2 1 
ATOM   5026  N  N   . PHE B  1 178 ? -16.543 6.332   -43.422 1.00 27.16  ?  209  PHE B N   1 
ATOM   5027  C  CA  . PHE B  1 178 ? -17.232 5.918   -44.651 1.00 29.43  ?  209  PHE B CA  1 
ATOM   5028  C  C   . PHE B  1 178 ? -18.599 6.580   -44.730 1.00 30.49  ?  209  PHE B C   1 
ATOM   5029  O  O   . PHE B  1 178 ? -19.262 6.747   -43.701 1.00 27.49  ?  209  PHE B O   1 
ATOM   5030  C  CB  . PHE B  1 178 ? -17.476 4.413   -44.707 1.00 29.82  ?  209  PHE B CB  1 
ATOM   5031  C  CG  . PHE B  1 178 ? -16.258 3.602   -44.972 1.00 30.81  ?  209  PHE B CG  1 
ATOM   5032  C  CD1 . PHE B  1 178 ? -15.043 4.208   -45.234 1.00 29.58  ?  209  PHE B CD1 1 
ATOM   5033  C  CD2 . PHE B  1 178 ? -16.337 2.216   -44.962 1.00 33.96  ?  209  PHE B CD2 1 
ATOM   5034  C  CE1 . PHE B  1 178 ? -13.911 3.442   -45.495 1.00 30.17  ?  209  PHE B CE1 1 
ATOM   5035  C  CE2 . PHE B  1 178 ? -15.218 1.434   -45.219 1.00 33.38  ?  209  PHE B CE2 1 
ATOM   5036  C  CZ  . PHE B  1 178 ? -14.001 2.049   -45.478 1.00 34.02  ?  209  PHE B CZ  1 
ATOM   5037  N  N   . PRO B  1 179 ? -19.060 6.925   -45.938 1.00 26.97  ?  210  PRO B N   1 
ATOM   5038  C  CA  . PRO B  1 179 ? -20.461 7.330   -46.106 1.00 30.70  ?  210  PRO B CA  1 
ATOM   5039  C  C   . PRO B  1 179 ? -21.396 6.325   -45.457 1.00 26.42  ?  210  PRO B C   1 
ATOM   5040  O  O   . PRO B  1 179 ? -21.194 5.117   -45.517 1.00 27.81  ?  210  PRO B O   1 
ATOM   5041  C  CB  . PRO B  1 179 ? -20.646 7.368   -47.633 1.00 31.75  ?  210  PRO B CB  1 
ATOM   5042  C  CG  . PRO B  1 179 ? -19.265 7.620   -48.150 1.00 33.52  ?  210  PRO B CG  1 
ATOM   5043  C  CD  . PRO B  1 179 ? -18.354 6.846   -47.225 1.00 29.92  ?  210  PRO B CD  1 
ATOM   5044  N  N   . MET B  1 180 ? -22.437 6.842   -44.847 1.00 28.00  ?  211  MET B N   1 
ATOM   5045  C  CA  . MET B  1 180 ? -23.456 6.033   -44.229 1.00 29.46  ?  211  MET B CA  1 
ATOM   5046  C  C   . MET B  1 180 ? -24.364 5.563   -45.385 1.00 31.84  ?  211  MET B C   1 
ATOM   5047  O  O   . MET B  1 180 ? -24.293 6.102   -46.495 1.00 31.88  ?  211  MET B O   1 
ATOM   5048  C  CB  . MET B  1 180 ? -24.129 6.952   -43.220 1.00 32.45  ?  211  MET B CB  1 
ATOM   5049  C  CG  . MET B  1 180 ? -23.446 6.931   -41.802 1.00 28.77  ?  211  MET B CG  1 
ATOM   5050  S  SD  . MET B  1 180 ? -24.462 7.004   -40.371 1.00 27.18  ?  211  MET B SD  1 
ATOM   5051  C  CE  . MET B  1 180 ? -25.237 8.566   -40.697 1.00 30.96  ?  211  MET B CE  1 
ATOM   5052  N  N   . GLU B  1 181 ? -25.199 4.547   -45.175 1.00 26.48  ?  212  GLU B N   1 
ATOM   5053  C  CA  . GLU B  1 181 ? -26.000 4.049   -46.290 1.00 31.33  ?  212  GLU B CA  1 
ATOM   5054  C  C   . GLU B  1 181 ? -27.471 3.978   -45.932 1.00 31.51  ?  212  GLU B C   1 
ATOM   5055  O  O   . GLU B  1 181 ? -27.856 3.888   -44.762 1.00 30.99  ?  212  GLU B O   1 
ATOM   5056  C  CB  . GLU B  1 181 ? -25.540 2.666   -46.759 1.00 31.78  ?  212  GLU B CB  1 
ATOM   5057  C  CG  . GLU B  1 181 ? -25.792 1.591   -45.733 1.00 30.78  ?  212  GLU B CG  1 
ATOM   5058  C  CD  . GLU B  1 181 ? -25.765 0.210   -46.327 1.00 32.51  ?  212  GLU B CD  1 
ATOM   5059  O  OE1 . GLU B  1 181 ? -26.828 -0.230  -46.815 1.00 32.16  ?  212  GLU B OE1 1 
ATOM   5060  O  OE2 . GLU B  1 181 ? -24.678 -0.426  -46.304 1.00 30.05  -1 212  GLU B OE2 1 
ATOM   5061  N  N   . HIS B  1 182 ? -28.296 4.013   -46.983 1.00 32.50  ?  213  HIS B N   1 
ATOM   5062  C  CA  . HIS B  1 182 ? -29.738 3.795   -46.896 1.00 30.98  ?  213  HIS B CA  1 
ATOM   5063  C  C   . HIS B  1 182 ? -30.088 2.695   -47.888 1.00 33.89  ?  213  HIS B C   1 
ATOM   5064  O  O   . HIS B  1 182 ? -30.110 2.938   -49.095 1.00 32.03  ?  213  HIS B O   1 
ATOM   5065  C  CB  . HIS B  1 182 ? -30.532 5.049   -47.216 1.00 33.18  ?  213  HIS B CB  1 
ATOM   5066  C  CG  . HIS B  1 182 ? -31.999 4.880   -47.009 1.00 34.65  ?  213  HIS B CG  1 
ATOM   5067  N  ND1 . HIS B  1 182 ? -32.935 5.729   -47.561 1.00 39.49  ?  213  HIS B ND1 1 
ATOM   5068  C  CD2 . HIS B  1 182 ? -32.695 3.966   -46.293 1.00 34.90  ?  213  HIS B CD2 1 
ATOM   5069  C  CE1 . HIS B  1 182 ? -34.146 5.339   -47.200 1.00 40.15  ?  213  HIS B CE1 1 
ATOM   5070  N  NE2 . HIS B  1 182 ? -34.029 4.267   -46.439 1.00 39.82  ?  213  HIS B NE2 1 
ATOM   5071  N  N   . ASN B  1 183 ? -30.346 1.495   -47.384 1.00 33.25  ?  214  ASN B N   1 
ATOM   5072  C  CA  . ASN B  1 183 ? -30.714 0.358   -48.217 1.00 39.07  ?  214  ASN B CA  1 
ATOM   5073  C  C   . ASN B  1 183 ? -29.707 0.173   -49.352 1.00 40.82  ?  214  ASN B C   1 
ATOM   5074  O  O   . ASN B  1 183 ? -30.072 0.002   -50.516 1.00 39.90  ?  214  ASN B O   1 
ATOM   5075  C  CB  . ASN B  1 183 ? -32.125 0.544   -48.767 1.00 34.60  ?  214  ASN B CB  1 
ATOM   5076  C  CG  . ASN B  1 183 ? -33.190 0.336   -47.710 1.00 36.46  ?  214  ASN B CG  1 
ATOM   5077  O  OD1 . ASN B  1 183 ? -32.953 -0.304  -46.675 1.00 38.34  ?  214  ASN B OD1 1 
ATOM   5078  N  ND2 . ASN B  1 183 ? -34.345 0.960   -47.916 1.00 38.75  ?  214  ASN B ND2 1 
ATOM   5079  N  N   . GLY B  1 184 ? -28.417 0.250   -49.011 1.00 36.07  ?  215  GLY B N   1 
ATOM   5080  C  CA  . GLY B  1 184 ? -27.363 0.071   -49.990 1.00 36.82  ?  215  GLY B CA  1 
ATOM   5081  C  C   . GLY B  1 184 ? -26.985 1.307   -50.780 1.00 40.52  ?  215  GLY B C   1 
ATOM   5082  O  O   . GLY B  1 184 ? -25.995 1.266   -51.525 1.00 41.12  ?  215  GLY B O   1 
ATOM   5083  N  N   . LYS B  1 185 ? -27.704 2.409   -50.624 1.00 34.23  ?  216  LYS B N   1 
ATOM   5084  C  CA  . LYS B  1 185 ? -27.439 3.653   -51.330 1.00 37.16  ?  216  LYS B CA  1 
ATOM   5085  C  C   . LYS B  1 185 ? -26.812 4.680   -50.390 1.00 38.61  ?  216  LYS B C   1 
ATOM   5086  O  O   . LYS B  1 185 ? -26.945 4.573   -49.168 1.00 37.23  ?  216  LYS B O   1 
ATOM   5087  C  CB  . LYS B  1 185 ? -28.748 4.219   -51.898 1.00 40.06  ?  216  LYS B CB  1 
ATOM   5088  C  CG  . LYS B  1 185 ? -29.487 3.292   -52.829 1.00 42.55  ?  216  LYS B CG  1 
ATOM   5089  C  CD  . LYS B  1 185 ? -30.021 4.057   -54.020 1.00 55.14  ?  216  LYS B CD  1 
ATOM   5090  C  CE  . LYS B  1 185 ? -31.541 4.228   -53.916 1.00 56.92  ?  216  LYS B CE  1 
ATOM   5091  N  NZ  . LYS B  1 185 ? -32.120 5.128   -54.987 1.00 65.22  ?  216  LYS B NZ  1 
ATOM   5092  N  N   . PRO B  1 186 ? -26.113 5.682   -50.925 1.00 38.62  ?  217  PRO B N   1 
ATOM   5093  C  CA  . PRO B  1 186 ? -25.577 6.759   -50.079 1.00 36.05  ?  217  PRO B CA  1 
ATOM   5094  C  C   . PRO B  1 186 ? -26.655 7.420   -49.230 1.00 38.43  ?  217  PRO B C   1 
ATOM   5095  O  O   . PRO B  1 186 ? -27.728 7.782   -49.725 1.00 33.54  ?  217  PRO B O   1 
ATOM   5096  C  CB  . PRO B  1 186 ? -24.992 7.736   -51.103 1.00 37.42  ?  217  PRO B CB  1 
ATOM   5097  C  CG  . PRO B  1 186 ? -24.547 6.829   -52.220 1.00 36.03  ?  217  PRO B CG  1 
ATOM   5098  C  CD  . PRO B  1 186 ? -25.653 5.814   -52.323 1.00 40.43  ?  217  PRO B CD  1 
ATOM   5099  N  N   . ALA B  1 187 ? -26.355 7.582   -47.935 1.00 33.42  ?  218  ALA B N   1 
ATOM   5100  C  CA  . ALA B  1 187 ? -27.319 8.188   -47.015 1.00 31.48  ?  218  ALA B CA  1 
ATOM   5101  C  C   . ALA B  1 187 ? -27.402 9.694   -47.202 1.00 32.52  ?  218  ALA B C   1 
ATOM   5102  O  O   . ALA B  1 187 ? -28.467 10.284  -46.976 1.00 36.40  ?  218  ALA B O   1 
ATOM   5103  C  CB  . ALA B  1 187 ? -26.944 7.876   -45.551 1.00 29.93  ?  218  ALA B CB  1 
ATOM   5104  N  N   . ASN B  1 188 ? -26.298 10.328  -47.600 1.00 30.89  ?  219  ASN B N   1 
ATOM   5105  C  CA  . ASN B  1 188 ? -26.204 11.792  -47.691 1.00 29.85  ?  219  ASN B CA  1 
ATOM   5106  C  C   . ASN B  1 188 ? -26.673 12.465  -46.400 1.00 34.61  ?  219  ASN B C   1 
ATOM   5107  O  O   . ASN B  1 188 ? -27.516 13.370  -46.397 1.00 28.69  ?  219  ASN B O   1 
ATOM   5108  C  CB  . ASN B  1 188 ? -26.961 12.306  -48.917 1.00 33.12  ?  219  ASN B CB  1 
ATOM   5109  C  CG  . ASN B  1 188 ? -26.458 11.661  -50.202 1.00 39.03  ?  219  ASN B CG  1 
ATOM   5110  O  OD1 . ASN B  1 188 ? -25.260 11.710  -50.503 1.00 38.88  ?  219  ASN B OD1 1 
ATOM   5111  N  ND2 . ASN B  1 188 ? -27.357 11.026  -50.941 1.00 40.89  ?  219  ASN B ND2 1 
ATOM   5112  N  N   . GLU B  1 189 ? -26.097 12.016  -45.279 1.00 29.99  ?  220  GLU B N   1 
ATOM   5113  C  CA  . GLU B  1 189 ? -26.555 12.500  -43.990 1.00 27.56  ?  220  GLU B CA  1 
ATOM   5114  C  C   . GLU B  1 189 ? -26.134 13.945  -43.836 1.00 29.37  ?  220  GLU B C   1 
ATOM   5115  O  O   . GLU B  1 189 ? -25.029 14.322  -44.221 1.00 29.39  ?  220  GLU B O   1 
ATOM   5116  C  CB  . GLU B  1 189 ? -25.980 11.649  -42.855 1.00 29.15  ?  220  GLU B CB  1 
ATOM   5117  C  CG  . GLU B  1 189 ? -26.339 12.171  -41.458 1.00 25.69  ?  220  GLU B CG  1 
ATOM   5118  C  CD  . GLU B  1 189 ? -27.830 12.264  -41.261 1.00 31.87  ?  220  GLU B CD  1 
ATOM   5119  O  OE1 . GLU B  1 189 ? -28.481 11.201  -41.215 1.00 31.17  ?  220  GLU B OE1 1 
ATOM   5120  O  OE2 . GLU B  1 189 ? -28.357 13.392  -41.173 1.00 33.63  -1 220  GLU B OE2 1 
ATOM   5121  N  N   . THR B  1 190 ? -27.017 14.761  -43.278 1.00 31.47  ?  221  THR B N   1 
ATOM   5122  C  CA  . THR B  1 190 ? -26.715 16.170  -43.073 1.00 31.72  ?  221  THR B CA  1 
ATOM   5123  C  C   . THR B  1 190 ? -26.668 16.572  -41.606 1.00 29.94  ?  221  THR B C   1 
ATOM   5124  O  O   . THR B  1 190 ? -26.210 17.682  -41.301 1.00 33.10  ?  221  THR B O   1 
ATOM   5125  C  CB  . THR B  1 190 ? -27.757 17.048  -43.797 1.00 32.50  ?  221  THR B CB  1 
ATOM   5126  O  OG1 . THR B  1 190 ? -29.053 16.820  -43.230 1.00 33.81  ?  221  THR B OG1 1 
ATOM   5127  C  CG2 . THR B  1 190 ? -27.837 16.665  -45.275 1.00 33.61  ?  221  THR B CG2 1 
ATOM   5128  N  N   . GLU B  1 191 ? -27.111 15.711  -40.692 1.00 26.38  ?  222  GLU B N   1 
ATOM   5129  C  CA  . GLU B  1 191 ? -27.227 16.053  -39.283 1.00 31.63  ?  222  GLU B CA  1 
ATOM   5130  C  C   . GLU B  1 191 ? -26.226 15.259  -38.454 1.00 28.86  ?  222  GLU B C   1 
ATOM   5131  O  O   . GLU B  1 191 ? -25.789 14.173  -38.861 1.00 27.43  ?  222  GLU B O   1 
ATOM   5132  C  CB  . GLU B  1 191 ? -28.646 15.772  -38.777 1.00 29.47  ?  222  GLU B CB  1 
ATOM   5133  C  CG  . GLU B  1 191 ? -29.741 16.528  -39.531 1.00 31.64  ?  222  GLU B CG  1 
ATOM   5134  C  CD  . GLU B  1 191 ? -31.079 16.386  -38.847 1.00 37.13  ?  222  GLU B CD  1 
ATOM   5135  O  OE1 . GLU B  1 191 ? -31.189 16.816  -37.683 1.00 38.68  ?  222  GLU B OE1 1 
ATOM   5136  O  OE2 . GLU B  1 191 ? -32.019 15.846  -39.471 1.00 36.37  -1 222  GLU B OE2 1 
ATOM   5137  N  N   . TYR B  1 192 ? -25.843 15.827  -37.304 1.00 27.95  ?  223  TYR B N   1 
ATOM   5138  C  CA  . TYR B  1 192 ? -25.254 15.048  -36.213 1.00 23.85  ?  223  TYR B CA  1 
ATOM   5139  C  C   . TYR B  1 192 ? -25.953 13.698  -36.162 1.00 25.40  ?  223  TYR B C   1 
ATOM   5140  O  O   . TYR B  1 192 ? -27.186 13.640  -36.078 1.00 25.42  ?  223  TYR B O   1 
ATOM   5141  C  CB  . TYR B  1 192 ? -25.449 15.791  -34.881 1.00 26.58  ?  223  TYR B CB  1 
ATOM   5142  C  CG  . TYR B  1 192 ? -24.862 15.138  -33.613 1.00 26.92  ?  223  TYR B CG  1 
ATOM   5143  C  CD1 . TYR B  1 192 ? -23.493 15.043  -33.422 1.00 27.18  ?  223  TYR B CD1 1 
ATOM   5144  C  CD2 . TYR B  1 192 ? -25.705 14.680  -32.582 1.00 26.93  ?  223  TYR B CD2 1 
ATOM   5145  C  CE1 . TYR B  1 192 ? -22.962 14.497  -32.247 1.00 24.93  ?  223  TYR B CE1 1 
ATOM   5146  C  CE2 . TYR B  1 192 ? -25.187 14.128  -31.408 1.00 25.77  ?  223  TYR B CE2 1 
ATOM   5147  C  CZ  . TYR B  1 192 ? -23.828 14.037  -31.252 1.00 25.93  ?  223  TYR B CZ  1 
ATOM   5148  O  OH  . TYR B  1 192 ? -23.335 13.493  -30.098 1.00 29.81  ?  223  TYR B OH  1 
ATOM   5149  N  N   . ILE B  1 193 ? -25.188 12.607  -36.292 1.00 25.86  ?  224  ILE B N   1 
ATOM   5150  C  CA  . ILE B  1 193 ? -25.844 11.372  -36.716 1.00 25.42  ?  224  ILE B CA  1 
ATOM   5151  C  C   . ILE B  1 193 ? -26.790 10.834  -35.657 1.00 26.00  ?  224  ILE B C   1 
ATOM   5152  O  O   . ILE B  1 193 ? -27.736 10.121  -36.002 1.00 26.70  ?  224  ILE B O   1 
ATOM   5153  C  CB  . ILE B  1 193 ? -24.850 10.282  -37.148 1.00 26.30  ?  224  ILE B CB  1 
ATOM   5154  C  CG1 . ILE B  1 193 ? -24.050 9.727   -35.941 1.00 26.08  ?  224  ILE B CG1 1 
ATOM   5155  C  CG2 . ILE B  1 193 ? -23.967 10.801  -38.315 1.00 25.26  ?  224  ILE B CG2 1 
ATOM   5156  C  CD1 . ILE B  1 193 ? -23.117 8.584   -36.300 1.00 21.24  ?  224  ILE B CD1 1 
ATOM   5157  N  N   . THR B  1 194 ? -26.624 11.203  -34.387 1.00 25.70  ?  225  THR B N   1 
ATOM   5158  C  CA  . THR B  1 194 ? -27.661 10.832  -33.419 1.00 25.86  ?  225  THR B CA  1 
ATOM   5159  C  C   . THR B  1 194 ? -29.004 11.463  -33.797 1.00 24.82  ?  225  THR B C   1 
ATOM   5160  O  O   . THR B  1 194 ? -30.041 10.788  -33.788 1.00 22.80  ?  225  THR B O   1 
ATOM   5161  C  CB  . THR B  1 194 ? -27.240 11.230  -32.004 1.00 22.57  ?  225  THR B CB  1 
ATOM   5162  O  OG1 . THR B  1 194 ? -26.072 10.477  -31.658 1.00 26.76  ?  225  THR B OG1 1 
ATOM   5163  C  CG2 . THR B  1 194 ? -28.358 10.892  -30.976 1.00 21.89  ?  225  THR B CG2 1 
ATOM   5164  N  N   . ASP B  1 195 ? -28.996 12.751  -34.172 1.00 27.11  ?  226  ASP B N   1 
ATOM   5165  C  CA  . ASP B  1 195 ? -30.222 13.387  -34.659 1.00 23.73  ?  226  ASP B CA  1 
ATOM   5166  C  C   . ASP B  1 195 ? -30.715 12.739  -35.950 1.00 29.18  ?  226  ASP B C   1 
ATOM   5167  O  O   . ASP B  1 195 ? -31.927 12.636  -36.174 1.00 28.80  ?  226  ASP B O   1 
ATOM   5168  C  CB  . ASP B  1 195 ? -30.008 14.887  -34.892 1.00 28.91  ?  226  ASP B CB  1 
ATOM   5169  C  CG  . ASP B  1 195 ? -29.708 15.647  -33.623 1.00 29.16  ?  226  ASP B CG  1 
ATOM   5170  O  OD1 . ASP B  1 195 ? -29.980 15.125  -32.520 1.00 30.86  ?  226  ASP B OD1 1 
ATOM   5171  O  OD2 . ASP B  1 195 ? -29.255 16.807  -33.735 1.00 32.12  -1 226  ASP B OD2 1 
ATOM   5172  N  N   . GLY B  1 196 ? -29.801 12.342  -36.839 1.00 27.89  ?  227  GLY B N   1 
ATOM   5173  C  CA  . GLY B  1 196 ? -30.235 11.692  -38.065 1.00 24.93  ?  227  GLY B CA  1 
ATOM   5174  C  C   . GLY B  1 196 ? -30.928 10.359  -37.815 1.00 26.47  ?  227  GLY B C   1 
ATOM   5175  O  O   . GLY B  1 196 ? -31.937 10.038  -38.456 1.00 25.08  ?  227  GLY B O   1 
ATOM   5176  N  N   . PHE B  1 197 ? -30.390 9.558   -36.888 1.00 25.36  ?  228  PHE B N   1 
ATOM   5177  C  CA  . PHE B  1 197 ? -31.005 8.270   -36.557 1.00 21.92  ?  228  PHE B CA  1 
ATOM   5178  C  C   . PHE B  1 197 ? -32.385 8.456   -35.930 1.00 26.41  ?  228  PHE B C   1 
ATOM   5179  O  O   . PHE B  1 197 ? -33.308 7.661   -36.180 1.00 27.06  ?  228  PHE B O   1 
ATOM   5180  C  CB  . PHE B  1 197 ? -30.082 7.480   -35.614 1.00 21.25  ?  228  PHE B CB  1 
ATOM   5181  C  CG  . PHE B  1 197 ? -28.731 7.130   -36.219 1.00 25.86  ?  228  PHE B CG  1 
ATOM   5182  C  CD1 . PHE B  1 197 ? -28.609 6.880   -37.588 1.00 24.29  ?  228  PHE B CD1 1 
ATOM   5183  C  CD2 . PHE B  1 197 ? -27.586 7.027   -35.405 1.00 25.23  ?  228  PHE B CD2 1 
ATOM   5184  C  CE1 . PHE B  1 197 ? -27.360 6.546   -38.141 1.00 25.78  ?  228  PHE B CE1 1 
ATOM   5185  C  CE2 . PHE B  1 197 ? -26.342 6.695   -35.944 1.00 24.98  ?  228  PHE B CE2 1 
ATOM   5186  C  CZ  . PHE B  1 197 ? -26.224 6.465   -37.330 1.00 23.68  ?  228  PHE B CZ  1 
ATOM   5187  N  N   . SER B  1 198 ? -32.549 9.491   -35.100 1.00 24.62  ?  229  SER B N   1 
ATOM   5188  C  CA  . SER B  1 198 ? -33.872 9.787   -34.547 1.00 27.21  ?  229  SER B CA  1 
ATOM   5189  C  C   . SER B  1 198 ? -34.830 10.215  -35.649 1.00 28.28  ?  229  SER B C   1 
ATOM   5190  O  O   . SER B  1 198 ? -35.998 9.801   -35.663 1.00 26.02  ?  229  SER B O   1 
ATOM   5191  C  CB  . SER B  1 198 ? -33.781 10.878  -33.470 1.00 24.22  ?  229  SER B CB  1 
ATOM   5192  O  OG  . SER B  1 198 ? -32.784 10.578  -32.476 1.00 24.54  ?  229  SER B OG  1 
ATOM   5193  N  N   . ARG B  1 199 ? -34.358 11.051  -36.580 1.00 29.21  ?  230  ARG B N   1 
ATOM   5194  C  CA  . ARG B  1 199 ? -35.205 11.454  -37.704 1.00 27.73  ?  230  ARG B CA  1 
ATOM   5195  C  C   . ARG B  1 199 ? -35.667 10.240  -38.505 1.00 30.35  ?  230  ARG B C   1 
ATOM   5196  O  O   . ARG B  1 199 ? -36.847 10.142  -38.897 1.00 29.26  ?  230  ARG B O   1 
ATOM   5197  C  CB  . ARG B  1 199 ? -34.437 12.434  -38.595 1.00 27.07  ?  230  ARG B CB  1 
ATOM   5198  C  CG  . ARG B  1 199 ? -35.145 12.838  -39.904 1.00 33.34  ?  230  ARG B CG  1 
ATOM   5199  C  CD  . ARG B  1 199 ? -34.131 13.469  -40.873 1.00 30.09  ?  230  ARG B CD  1 
ATOM   5200  N  NE  . ARG B  1 199 ? -33.290 12.436  -41.469 1.00 29.57  ?  230  ARG B NE  1 
ATOM   5201  C  CZ  . ARG B  1 199 ? -31.963 12.417  -41.411 1.00 28.65  ?  230  ARG B CZ  1 
ATOM   5202  N  NH1 . ARG B  1 199 ? -31.270 13.429  -40.888 1.00 31.22  ?  230  ARG B NH1 1 
ATOM   5203  N  NH2 . ARG B  1 199 ? -31.312 11.351  -41.874 1.00 29.66  ?  230  ARG B NH2 1 
ATOM   5204  N  N   . GLU B  1 200 ? -34.749 9.300   -38.755 1.00 26.53  ?  231  GLU B N   1 
ATOM   5205  C  CA  . GLU B  1 200 ? -35.097 8.105   -39.514 1.00 29.34  ?  231  GLU B CA  1 
ATOM   5206  C  C   . GLU B  1 200 ? -36.077 7.224   -38.747 1.00 32.58  ?  231  GLU B C   1 
ATOM   5207  O  O   . GLU B  1 200 ? -36.959 6.596   -39.350 1.00 30.70  ?  231  GLU B O   1 
ATOM   5208  C  CB  . GLU B  1 200 ? -33.834 7.327   -39.893 1.00 27.74  ?  231  GLU B CB  1 
ATOM   5209  C  CG  . GLU B  1 200 ? -32.964 8.049   -40.944 1.00 29.63  ?  231  GLU B CG  1 
ATOM   5210  C  CD  . GLU B  1 200 ? -33.743 8.457   -42.187 1.00 31.25  ?  231  GLU B CD  1 
ATOM   5211  O  OE1 . GLU B  1 200 ? -34.383 7.585   -42.785 1.00 29.97  ?  231  GLU B OE1 1 
ATOM   5212  O  OE2 . GLU B  1 200 ? -33.700 9.645   -42.567 1.00 34.42  -1 231  GLU B OE2 1 
ATOM   5213  N  N   . ALA B  1 201 ? -35.946 7.158   -37.423 1.00 26.34  ?  232  ALA B N   1 
ATOM   5214  C  CA  . ALA B  1 201 ? -36.907 6.389   -36.631 1.00 27.08  ?  232  ALA B CA  1 
ATOM   5215  C  C   . ALA B  1 201 ? -38.298 6.967   -36.785 1.00 29.63  ?  232  ALA B C   1 
ATOM   5216  O  O   . ALA B  1 201 ? -39.276 6.242   -37.008 1.00 26.80  ?  232  ALA B O   1 
ATOM   5217  C  CB  . ALA B  1 201 ? -36.497 6.376   -35.152 1.00 24.54  ?  232  ALA B CB  1 
ATOM   5218  N  N   . ILE B  1 202 ? -38.394 8.289   -36.686 1.00 32.19  ?  233  ILE B N   1 
ATOM   5219  C  CA  . ILE B  1 202 ? -39.672 8.958   -36.848 1.00 28.37  ?  233  ILE B CA  1 
ATOM   5220  C  C   . ILE B  1 202 ? -40.237 8.691   -38.238 1.00 30.19  ?  233  ILE B C   1 
ATOM   5221  O  O   . ILE B  1 202 ? -41.448 8.484   -38.401 1.00 31.29  ?  233  ILE B O   1 
ATOM   5222  C  CB  . ILE B  1 202 ? -39.494 10.463  -36.583 1.00 30.67  ?  233  ILE B CB  1 
ATOM   5223  C  CG1 . ILE B  1 202 ? -39.104 10.707  -35.108 1.00 28.17  ?  233  ILE B CG1 1 
ATOM   5224  C  CG2 . ILE B  1 202 ? -40.719 11.244  -37.069 1.00 31.75  ?  233  ILE B CG2 1 
ATOM   5225  C  CD1 . ILE B  1 202 ? -38.474 12.041  -34.887 1.00 27.13  ?  233  ILE B CD1 1 
ATOM   5226  N  N   . LYS B  1 203 ? -39.373 8.711   -39.260 1.00 30.34  ?  234  LYS B N   1 
ATOM   5227  C  CA  . LYS B  1 203 ? -39.815 8.452   -40.628 1.00 30.72  ?  234  LYS B CA  1 
ATOM   5228  C  C   . LYS B  1 203 ? -40.408 7.056   -40.747 1.00 35.76  ?  234  LYS B C   1 
ATOM   5229  O  O   . LYS B  1 203 ? -41.496 6.871   -41.317 1.00 32.11  ?  234  LYS B O   1 
ATOM   5230  C  CB  . LYS B  1 203 ? -38.649 8.637   -41.605 1.00 29.13  ?  234  LYS B CB  1 
ATOM   5231  C  CG  . LYS B  1 203 ? -39.040 8.507   -43.113 1.00 35.49  ?  234  LYS B CG  1 
ATOM   5232  C  CD  . LYS B  1 203 ? -37.793 8.349   -44.014 1.00 32.60  ?  234  LYS B CD  1 
ATOM   5233  C  CE  . LYS B  1 203 ? -37.942 8.994   -45.395 1.00 44.32  ?  234  LYS B CE  1 
ATOM   5234  N  NZ  . LYS B  1 203 ? -37.045 8.372   -46.441 1.00 39.53  ?  234  LYS B NZ  1 
ATOM   5235  N  N   . ASN B  1 204 ? -39.720 6.061   -40.187 1.00 29.77  ?  235  ASN B N   1 
ATOM   5236  C  CA  . ASN B  1 204 ? -40.188 4.683   -40.304 1.00 30.11  ?  235  ASN B CA  1 
ATOM   5237  C  C   . ASN B  1 204 ? -41.448 4.415   -39.488 1.00 32.98  ?  235  ASN B C   1 
ATOM   5238  O  O   . ASN B  1 204 ? -42.303 3.630   -39.927 1.00 31.72  ?  235  ASN B O   1 
ATOM   5239  C  CB  . ASN B  1 204 ? -39.066 3.720   -39.924 1.00 30.55  ?  235  ASN B CB  1 
ATOM   5240  C  CG  . ASN B  1 204 ? -38.049 3.568   -41.036 1.00 34.69  ?  235  ASN B CG  1 
ATOM   5241  O  OD1 . ASN B  1 204 ? -38.180 2.697   -41.892 1.00 39.29  ?  235  ASN B OD1 1 
ATOM   5242  N  ND2 . ASN B  1 204 ? -37.070 4.438   -41.065 1.00 37.85  ?  235  ASN B ND2 1 
ATOM   5243  N  N   . ILE B  1 205 ? -41.602 5.062   -38.326 1.00 30.99  ?  236  ILE B N   1 
ATOM   5244  C  CA  . ILE B  1 205 ? -42.865 4.976   -37.591 1.00 30.56  ?  236  ILE B CA  1 
ATOM   5245  C  C   . ILE B  1 205 ? -44.018 5.464   -38.462 1.00 31.11  ?  236  ILE B C   1 
ATOM   5246  O  O   . ILE B  1 205 ? -45.080 4.843   -38.515 1.00 30.27  ?  236  ILE B O   1 
ATOM   5247  C  CB  . ILE B  1 205 ? -42.765 5.780   -36.279 1.00 29.02  ?  236  ILE B CB  1 
ATOM   5248  C  CG1 . ILE B  1 205 ? -41.876 5.042   -35.269 1.00 29.03  ?  236  ILE B CG1 1 
ATOM   5249  C  CG2 . ILE B  1 205 ? -44.119 5.991   -35.672 1.00 28.53  ?  236  ILE B CG2 1 
ATOM   5250  C  CD1 . ILE B  1 205 ? -41.349 5.985   -34.196 1.00 26.59  ?  236  ILE B CD1 1 
ATOM   5251  N  N   . LYS B  1 206 ? -43.808 6.571   -39.180 1.00 30.89  ?  237  LYS B N   1 
ATOM   5252  C  CA  . LYS B  1 206 ? -44.856 7.116   -40.037 1.00 31.37  ?  237  LYS B CA  1 
ATOM   5253  C  C   . LYS B  1 206 ? -45.117 6.222   -41.244 1.00 31.03  ?  237  LYS B C   1 
ATOM   5254  O  O   . LYS B  1 206 ? -46.271 6.054   -41.664 1.00 34.10  ?  237  LYS B O   1 
ATOM   5255  C  CB  . LYS B  1 206 ? -44.480 8.541   -40.452 1.00 28.17  ?  237  LYS B CB  1 
ATOM   5256  C  CG  . LYS B  1 206 ? -44.362 9.415   -39.235 1.00 37.28  ?  237  LYS B CG  1 
ATOM   5257  C  CD  . LYS B  1 206 ? -44.793 10.808  -39.504 1.00 40.73  ?  237  LYS B CD  1 
ATOM   5258  C  CE  . LYS B  1 206 ? -43.656 11.700  -39.801 1.00 41.76  ?  237  LYS B CE  1 
ATOM   5259  N  NZ  . LYS B  1 206 ? -43.782 12.834  -38.853 1.00 44.10  ?  237  LYS B NZ  1 
ATOM   5260  N  N   . ILE B  1 207 ? -44.071 5.614   -41.795 1.00 32.50  ?  238  ILE B N   1 
ATOM   5261  C  CA  . ILE B  1 207 ? -44.256 4.650   -42.875 1.00 34.38  ?  238  ILE B CA  1 
ATOM   5262  C  C   . ILE B  1 207 ? -45.131 3.496   -42.410 1.00 34.97  ?  238  ILE B C   1 
ATOM   5263  O  O   . ILE B  1 207 ? -46.067 3.075   -43.108 1.00 38.03  ?  238  ILE B O   1 
ATOM   5264  C  CB  . ILE B  1 207 ? -42.887 4.169   -43.392 1.00 30.68  ?  238  ILE B CB  1 
ATOM   5265  C  CG1 . ILE B  1 207 ? -42.101 5.369   -43.939 1.00 32.46  ?  238  ILE B CG1 1 
ATOM   5266  C  CG2 . ILE B  1 207 ? -43.053 3.058   -44.459 1.00 33.11  ?  238  ILE B CG2 1 
ATOM   5267  C  CD1 . ILE B  1 207 ? -40.779 5.004   -44.641 1.00 36.82  ?  238  ILE B CD1 1 
ATOM   5268  N  N   . ALA B  1 208 ? -44.847 2.970   -41.222 1.00 30.07  ?  239  ALA B N   1 
ATOM   5269  C  CA  . ALA B  1 208 ? -45.648 1.869   -40.693 1.00 31.98  ?  239  ALA B CA  1 
ATOM   5270  C  C   . ALA B  1 208 ? -47.087 2.295   -40.470 1.00 30.78  ?  239  ALA B C   1 
ATOM   5271  O  O   . ALA B  1 208 ? -48.014 1.506   -40.691 1.00 30.85  ?  239  ALA B O   1 
ATOM   5272  C  CB  . ALA B  1 208 ? -45.051 1.354   -39.382 1.00 31.57  ?  239  ALA B CB  1 
ATOM   5273  N  N   . ALA B  1 209 ? -47.296 3.525   -39.991 1.00 28.76  ?  240  ALA B N   1 
ATOM   5274  C  CA  . ALA B  1 209 ? -48.666 3.992   -39.802 1.00 34.70  ?  240  ALA B CA  1 
ATOM   5275  C  C   . ALA B  1 209 ? -49.386 4.102   -41.136 1.00 35.51  ?  240  ALA B C   1 
ATOM   5276  O  O   . ALA B  1 209 ? -50.555 3.711   -41.245 1.00 34.40  ?  240  ALA B O   1 
ATOM   5277  C  CB  . ALA B  1 209 ? -48.695 5.338   -39.074 1.00 30.53  ?  240  ALA B CB  1 
ATOM   5278  N  N   . ALA B  1 210 ? -48.706 4.634   -42.162 1.00 32.82  ?  241  ALA B N   1 
ATOM   5279  C  CA  . ALA B  1 210 ? -49.329 4.747   -43.486 1.00 40.00  ?  241  ALA B CA  1 
ATOM   5280  C  C   . ALA B  1 210 ? -49.641 3.373   -44.073 1.00 35.71  ?  241  ALA B C   1 
ATOM   5281  O  O   . ALA B  1 210 ? -50.666 3.187   -44.747 1.00 36.20  ?  241  ALA B O   1 
ATOM   5282  C  CB  . ALA B  1 210 ? -48.421 5.537   -44.433 1.00 35.20  ?  241  ALA B CB  1 
ATOM   5283  N  N   . LYS B  1 211 ? -48.757 2.399   -43.833 1.00 34.50  ?  242  LYS B N   1 
ATOM   5284  C  CA  . LYS B  1 211 ? -48.934 1.027   -44.290 1.00 35.83  ?  242  LYS B CA  1 
ATOM   5285  C  C   . LYS B  1 211 ? -49.982 0.277   -43.483 1.00 35.49  ?  242  LYS B C   1 
ATOM   5286  O  O   . LYS B  1 211 ? -50.428 -0.789  -43.924 1.00 37.20  ?  242  LYS B O   1 
ATOM   5287  C  CB  . LYS B  1 211 ? -47.604 0.273   -44.196 1.00 38.34  ?  242  LYS B CB  1 
ATOM   5288  C  CG  . LYS B  1 211 ? -46.650 0.469   -45.364 1.00 38.46  ?  242  LYS B CG  1 
ATOM   5289  C  CD  . LYS B  1 211 ? -45.365 -0.372  -45.171 1.00 42.00  ?  242  LYS B CD  1 
ATOM   5290  C  CE  . LYS B  1 211 ? -45.105 -1.303  -46.387 1.00 50.57  ?  242  LYS B CE  1 
ATOM   5291  N  NZ  . LYS B  1 211 ? -44.729 -2.712  -45.982 1.00 51.07  ?  242  LYS B NZ  1 
ATOM   5292  N  N   . LYS B  1 212 ? -50.381 0.815   -42.327 1.00 34.45  ?  243  LYS B N   1 
ATOM   5293  C  CA  . LYS B  1 212 ? -51.280 0.151   -41.378 1.00 35.68  ?  243  LYS B CA  1 
ATOM   5294  C  C   . LYS B  1 212 ? -50.745 -1.231  -41.028 1.00 39.70  ?  243  LYS B C   1 
ATOM   5295  O  O   . LYS B  1 212 ? -51.453 -2.235  -41.058 1.00 35.40  ?  243  LYS B O   1 
ATOM   5296  C  CB  . LYS B  1 212 ? -52.714 0.083   -41.922 1.00 39.94  ?  243  LYS B CB  1 
ATOM   5297  C  CG  . LYS B  1 212 ? -53.356 1.457   -42.076 1.00 39.46  ?  243  LYS B CG  1 
ATOM   5298  C  CD  . LYS B  1 212 ? -54.518 1.445   -43.088 1.00 51.71  ?  243  LYS B CD  1 
ATOM   5299  C  CE  . LYS B  1 212 ? -55.453 2.639   -42.902 1.00 55.75  ?  243  LYS B CE  1 
ATOM   5300  N  NZ  . LYS B  1 212 ? -55.253 3.691   -43.943 1.00 55.37  ?  243  LYS B NZ  1 
ATOM   5301  N  N   . GLN B  1 213 ? -49.458 -1.272  -40.685 1.00 33.91  ?  244  GLN B N   1 
ATOM   5302  C  CA  . GLN B  1 213 ? -48.791 -2.526  -40.426 1.00 34.35  ?  244  GLN B CA  1 
ATOM   5303  C  C   . GLN B  1 213 ? -48.056 -2.415  -39.092 1.00 35.44  ?  244  GLN B C   1 
ATOM   5304  O  O   . GLN B  1 213 ? -47.592 -1.321  -38.733 1.00 31.42  ?  244  GLN B O   1 
ATOM   5305  C  CB  . GLN B  1 213 ? -47.857 -2.813  -41.615 1.00 35.04  ?  244  GLN B CB  1 
ATOM   5306  C  CG  . GLN B  1 213 ? -47.166 -4.144  -41.647 1.00 41.05  ?  244  GLN B CG  1 
ATOM   5307  C  CD  . GLN B  1 213 ? -46.414 -4.371  -42.957 1.00 40.04  ?  244  GLN B CD  1 
ATOM   5308  O  OE1 . GLN B  1 213 ? -46.295 -3.475  -43.788 1.00 36.97  ?  244  GLN B OE1 1 
ATOM   5309  N  NE2 . GLN B  1 213 ? -45.871 -5.568  -43.122 1.00 44.51  ?  244  GLN B NE2 1 
ATOM   5310  N  N   . PRO B  1 214 ? -48.017 -3.478  -38.284 1.00 36.74  ?  245  PRO B N   1 
ATOM   5311  C  CA  . PRO B  1 214 ? -47.186 -3.429  -37.069 1.00 32.92  ?  245  PRO B CA  1 
ATOM   5312  C  C   . PRO B  1 214 ? -45.723 -3.291  -37.438 1.00 33.15  ?  245  PRO B C   1 
ATOM   5313  O  O   . PRO B  1 214 ? -45.270 -3.823  -38.454 1.00 31.99  ?  245  PRO B O   1 
ATOM   5314  C  CB  . PRO B  1 214 ? -47.463 -4.774  -36.375 1.00 35.77  ?  245  PRO B CB  1 
ATOM   5315  C  CG  . PRO B  1 214 ? -47.997 -5.660  -37.449 1.00 43.83  ?  245  PRO B CG  1 
ATOM   5316  C  CD  . PRO B  1 214 ? -48.775 -4.738  -38.376 1.00 36.62  ?  245  PRO B CD  1 
ATOM   5317  N  N   . PHE B  1 215 ? -44.970 -2.580  -36.589 1.00 28.48  ?  246  PHE B N   1 
ATOM   5318  C  CA  . PHE B  1 215 ? -43.573 -2.314  -36.889 1.00 31.51  ?  246  PHE B CA  1 
ATOM   5319  C  C   . PHE B  1 215 ? -42.654 -2.952  -35.855 1.00 25.31  ?  246  PHE B C   1 
ATOM   5320  O  O   . PHE B  1 215 ? -43.026 -3.170  -34.704 1.00 28.36  ?  246  PHE B O   1 
ATOM   5321  C  CB  . PHE B  1 215 ? -43.276 -0.784  -37.035 1.00 29.80  ?  246  PHE B CB  1 
ATOM   5322  C  CG  . PHE B  1 215 ? -43.308 0.018   -35.739 1.00 30.66  ?  246  PHE B CG  1 
ATOM   5323  C  CD1 . PHE B  1 215 ? -42.323 -0.135  -34.756 1.00 28.61  ?  246  PHE B CD1 1 
ATOM   5324  C  CD2 . PHE B  1 215 ? -44.274 0.990   -35.555 1.00 30.11  ?  246  PHE B CD2 1 
ATOM   5325  C  CE1 . PHE B  1 215 ? -42.364 0.619   -33.597 1.00 26.53  ?  246  PHE B CE1 1 
ATOM   5326  C  CE2 . PHE B  1 215 ? -44.311 1.761   -34.398 1.00 28.41  ?  246  PHE B CE2 1 
ATOM   5327  C  CZ  . PHE B  1 215 ? -43.343 1.578   -33.422 1.00 32.42  ?  246  PHE B CZ  1 
ATOM   5328  N  N   . PHE B  1 216 ? -41.466 -3.300  -36.325 1.00 29.20  ?  247  PHE B N   1 
ATOM   5329  C  CA  . PHE B  1 216 ? -40.322 -3.642  -35.494 1.00 27.91  ?  247  PHE B CA  1 
ATOM   5330  C  C   . PHE B  1 216 ? -39.190 -2.729  -35.933 1.00 29.53  ?  247  PHE B C   1 
ATOM   5331  O  O   . PHE B  1 216 ? -38.703 -2.848  -37.063 1.00 29.25  ?  247  PHE B O   1 
ATOM   5332  C  CB  . PHE B  1 216 ? -39.933 -5.111  -35.655 1.00 25.81  ?  247  PHE B CB  1 
ATOM   5333  C  CG  . PHE B  1 216 ? -38.622 -5.461  -35.003 1.00 29.45  ?  247  PHE B CG  1 
ATOM   5334  C  CD1 . PHE B  1 216 ? -38.500 -5.472  -33.611 1.00 28.33  ?  247  PHE B CD1 1 
ATOM   5335  C  CD2 . PHE B  1 216 ? -37.512 -5.761  -35.777 1.00 26.17  ?  247  PHE B CD2 1 
ATOM   5336  C  CE1 . PHE B  1 216 ? -37.272 -5.789  -32.995 1.00 27.23  ?  247  PHE B CE1 1 
ATOM   5337  C  CE2 . PHE B  1 216 ? -36.285 -6.076  -35.177 1.00 28.07  ?  247  PHE B CE2 1 
ATOM   5338  C  CZ  . PHE B  1 216 ? -36.173 -6.085  -33.784 1.00 25.81  ?  247  PHE B CZ  1 
ATOM   5339  N  N   . ILE B  1 217 ? -38.765 -1.824  -35.052 1.00 27.51  ?  248  ILE B N   1 
ATOM   5340  C  CA  . ILE B  1 217 ? -37.653 -0.917  -35.332 1.00 25.56  ?  248  ILE B CA  1 
ATOM   5341  C  C   . ILE B  1 217 ? -36.528 -1.230  -34.359 1.00 26.00  ?  248  ILE B C   1 
ATOM   5342  O  O   . ILE B  1 217 ? -36.734 -1.238  -33.140 1.00 25.88  ?  248  ILE B O   1 
ATOM   5343  C  CB  . ILE B  1 217 ? -38.083 0.551   -35.216 1.00 26.62  ?  248  ILE B CB  1 
ATOM   5344  C  CG1 . ILE B  1 217 ? -39.160 0.850   -36.242 1.00 27.62  ?  248  ILE B CG1 1 
ATOM   5345  C  CG2 . ILE B  1 217 ? -36.892 1.491   -35.393 1.00 24.19  ?  248  ILE B CG2 1 
ATOM   5346  C  CD1 . ILE B  1 217 ? -39.804 2.205   -36.011 1.00 30.54  ?  248  ILE B CD1 1 
ATOM   5347  N  N   . TYR B  1 218 ? -35.357 -1.507  -34.899 1.00 28.67  ?  249  TYR B N   1 
ATOM   5348  C  CA  . TYR B  1 218 ? -34.159 -1.815  -34.136 1.00 26.17  ?  249  TYR B CA  1 
ATOM   5349  C  C   . TYR B  1 218 ? -33.296 -0.556  -34.273 1.00 24.67  ?  249  TYR B C   1 
ATOM   5350  O  O   . TYR B  1 218 ? -32.603 -0.369  -35.273 1.00 23.52  ?  249  TYR B O   1 
ATOM   5351  C  CB  . TYR B  1 218 ? -33.513 -3.106  -34.690 1.00 24.91  ?  249  TYR B CB  1 
ATOM   5352  C  CG  . TYR B  1 218 ? -32.131 -3.488  -34.133 1.00 26.43  ?  249  TYR B CG  1 
ATOM   5353  C  CD1 . TYR B  1 218 ? -32.000 -4.126  -32.888 1.00 27.27  ?  249  TYR B CD1 1 
ATOM   5354  C  CD2 . TYR B  1 218 ? -30.983 -3.271  -34.872 1.00 26.43  ?  249  TYR B CD2 1 
ATOM   5355  C  CE1 . TYR B  1 218 ? -30.720 -4.511  -32.385 1.00 25.47  ?  249  TYR B CE1 1 
ATOM   5356  C  CE2 . TYR B  1 218 ? -29.711 -3.629  -34.377 1.00 24.60  ?  249  TYR B CE2 1 
ATOM   5357  C  CZ  . TYR B  1 218 ? -29.595 -4.242  -33.146 1.00 26.56  ?  249  TYR B CZ  1 
ATOM   5358  O  OH  . TYR B  1 218 ? -28.342 -4.605  -32.705 1.00 26.99  ?  249  TYR B OH  1 
ATOM   5359  N  N   . LEU B  1 219 ? -33.405 0.337   -33.282 1.00 23.76  ?  250  LEU B N   1 
ATOM   5360  C  CA  . LEU B  1 219 ? -32.797 1.668   -33.305 1.00 23.68  ?  250  LEU B CA  1 
ATOM   5361  C  C   . LEU B  1 219 ? -31.503 1.596   -32.495 1.00 24.43  ?  250  LEU B C   1 
ATOM   5362  O  O   . LEU B  1 219 ? -31.521 1.694   -31.264 1.00 25.37  ?  250  LEU B O   1 
ATOM   5363  C  CB  . LEU B  1 219 ? -33.766 2.697   -32.729 1.00 22.48  ?  250  LEU B CB  1 
ATOM   5364  C  CG  . LEU B  1 219 ? -33.256 4.127   -32.501 1.00 23.52  ?  250  LEU B CG  1 
ATOM   5365  C  CD1 . LEU B  1 219 ? -32.519 4.712   -33.713 1.00 19.98  ?  250  LEU B CD1 1 
ATOM   5366  C  CD2 . LEU B  1 219 ? -34.411 5.033   -32.058 1.00 24.17  ?  250  LEU B CD2 1 
ATOM   5367  N  N   . ALA B  1 220 ? -30.388 1.398   -33.192 1.00 24.42  ?  251  ALA B N   1 
ATOM   5368  C  CA  . ALA B  1 220 ? -29.091 1.092   -32.595 1.00 22.12  ?  251  ALA B CA  1 
ATOM   5369  C  C   . ALA B  1 220 ? -28.202 2.330   -32.668 1.00 25.07  ?  251  ALA B C   1 
ATOM   5370  O  O   . ALA B  1 220 ? -27.315 2.444   -33.516 1.00 23.00  ?  251  ALA B O   1 
ATOM   5371  C  CB  . ALA B  1 220 ? -28.459 -0.114  -33.317 1.00 23.17  ?  251  ALA B CB  1 
ATOM   5372  N  N   . TYR B  1 221 ? -28.442 3.269   -31.757 1.00 21.52  ?  252  TYR B N   1 
ATOM   5373  C  CA  . TYR B  1 221 ? -27.571 4.430   -31.669 1.00 22.78  ?  252  TYR B CA  1 
ATOM   5374  C  C   . TYR B  1 221 ? -26.126 4.018   -31.407 1.00 24.46  ?  252  TYR B C   1 
ATOM   5375  O  O   . TYR B  1 221 ? -25.854 3.138   -30.584 1.00 26.15  ?  252  TYR B O   1 
ATOM   5376  C  CB  . TYR B  1 221 ? -28.009 5.343   -30.535 1.00 23.87  ?  252  TYR B CB  1 
ATOM   5377  C  CG  . TYR B  1 221 ? -29.322 6.067   -30.745 1.00 26.30  ?  252  TYR B CG  1 
ATOM   5378  C  CD1 . TYR B  1 221 ? -29.397 7.185   -31.560 1.00 23.89  ?  252  TYR B CD1 1 
ATOM   5379  C  CD2 . TYR B  1 221 ? -30.459 5.686   -30.033 1.00 22.72  ?  252  TYR B CD2 1 
ATOM   5380  C  CE1 . TYR B  1 221 ? -30.586 7.889   -31.701 1.00 23.05  ?  252  TYR B CE1 1 
ATOM   5381  C  CE2 . TYR B  1 221 ? -31.655 6.381   -30.164 1.00 26.58  ?  252  TYR B CE2 1 
ATOM   5382  C  CZ  . TYR B  1 221 ? -31.718 7.475   -31.004 1.00 25.16  ?  252  TYR B CZ  1 
ATOM   5383  O  OH  . TYR B  1 221 ? -32.918 8.163   -31.130 1.00 25.58  ?  252  TYR B OH  1 
ATOM   5384  N  N   . ASN B  1 222 ? -25.184 4.696   -32.059 1.00 22.70  ?  253  ASN B N   1 
ATOM   5385  C  CA  . ASN B  1 222 ? -23.811 4.481   -31.597 1.00 23.13  ?  253  ASN B CA  1 
ATOM   5386  C  C   . ASN B  1 222 ? -23.466 5.292   -30.349 1.00 21.97  ?  253  ASN B C   1 
ATOM   5387  O  O   . ASN B  1 222 ? -22.481 4.960   -29.679 1.00 23.75  ?  253  ASN B O   1 
ATOM   5388  C  CB  . ASN B  1 222 ? -22.777 4.750   -32.731 1.00 20.39  ?  253  ASN B CB  1 
ATOM   5389  C  CG  . ASN B  1 222 ? -22.778 6.199   -33.237 1.00 25.25  ?  253  ASN B CG  1 
ATOM   5390  O  OD1 . ASN B  1 222 ? -23.825 6.788   -33.477 1.00 25.65  ?  253  ASN B OD1 1 
ATOM   5391  N  ND2 . ASN B  1 222 ? -21.591 6.751   -33.458 1.00 25.15  ?  253  ASN B ND2 1 
ATOM   5392  N  N   . ALA B  1 223 ? -24.265 6.288   -29.977 1.00 24.29  ?  254  ALA B N   1 
ATOM   5393  C  CA  . ALA B  1 223 ? -24.000 7.028   -28.745 1.00 25.91  ?  254  ALA B CA  1 
ATOM   5394  C  C   . ALA B  1 223 ? -24.240 6.135   -27.523 1.00 23.47  ?  254  ALA B C   1 
ATOM   5395  O  O   . ALA B  1 223 ? -25.168 5.324   -27.509 1.00 26.70  ?  254  ALA B O   1 
ATOM   5396  C  CB  . ALA B  1 223 ? -24.898 8.266   -28.651 1.00 22.85  ?  254  ALA B CB  1 
ATOM   5397  N  N   . PRO B  1 224 ? -23.458 6.302   -26.473 1.00 21.13  ?  255  PRO B N   1 
ATOM   5398  C  CA  . PRO B  1 224 ? -22.357 7.269   -26.330 1.00 21.05  ?  255  PRO B CA  1 
ATOM   5399  C  C   . PRO B  1 224 ? -20.970 6.665   -26.571 1.00 20.18  ?  255  PRO B C   1 
ATOM   5400  O  O   . PRO B  1 224 ? -19.989 7.014   -25.877 1.00 21.28  ?  255  PRO B O   1 
ATOM   5401  C  CB  . PRO B  1 224 ? -22.543 7.740   -24.882 1.00 22.92  ?  255  PRO B CB  1 
ATOM   5402  C  CG  . PRO B  1 224 ? -22.900 6.433   -24.153 1.00 22.57  ?  255  PRO B CG  1 
ATOM   5403  C  CD  . PRO B  1 224 ? -23.808 5.682   -25.177 1.00 20.85  ?  255  PRO B CD  1 
ATOM   5404  N  N   . HIS B  1 225 ? -20.850 5.735   -27.522 1.00 22.12  ?  256  HIS B N   1 
ATOM   5405  C  CA  . HIS B  1 225 ? -19.560 5.135   -27.865 1.00 23.60  ?  256  HIS B CA  1 
ATOM   5406  C  C   . HIS B  1 225 ? -18.621 6.175   -28.492 1.00 22.61  ?  256  HIS B C   1 
ATOM   5407  O  O   . HIS B  1 225 ? -19.059 7.069   -29.221 1.00 23.71  ?  256  HIS B O   1 
ATOM   5408  C  CB  . HIS B  1 225 ? -19.829 3.967   -28.817 1.00 23.42  ?  256  HIS B CB  1 
ATOM   5409  C  CG  . HIS B  1 225 ? -18.642 3.141   -29.208 1.00 24.32  ?  256  HIS B CG  1 
ATOM   5410  N  ND1 . HIS B  1 225 ? -17.582 3.638   -29.934 1.00 25.38  ?  256  HIS B ND1 1 
ATOM   5411  C  CD2 . HIS B  1 225 ? -18.416 1.810   -29.076 1.00 24.78  ?  256  HIS B CD2 1 
ATOM   5412  C  CE1 . HIS B  1 225 ? -16.743 2.654   -30.206 1.00 27.02  ?  256  HIS B CE1 1 
ATOM   5413  N  NE2 . HIS B  1 225 ? -17.224 1.536   -29.691 1.00 26.62  ?  256  HIS B NE2 1 
ATOM   5414  N  N   . VAL B  1 226 ? -17.327 6.067   -28.185 1.00 22.03  ?  257  VAL B N   1 
ATOM   5415  C  CA  . VAL B  1 226 ? -16.290 6.921   -28.775 1.00 22.45  ?  257  VAL B CA  1 
ATOM   5416  C  C   . VAL B  1 226 ? -16.419 6.953   -30.298 1.00 26.04  ?  257  VAL B C   1 
ATOM   5417  O  O   . VAL B  1 226 ? -16.913 5.986   -30.891 1.00 22.50  ?  257  VAL B O   1 
ATOM   5418  C  CB  . VAL B  1 226 ? -14.889 6.450   -28.364 1.00 25.71  ?  257  VAL B CB  1 
ATOM   5419  C  CG1 . VAL B  1 226 ? -14.659 6.760   -26.891 1.00 27.61  ?  257  VAL B CG1 1 
ATOM   5420  C  CG2 . VAL B  1 226 ? -14.682 4.943   -28.667 1.00 24.96  ?  257  VAL B CG2 1 
ATOM   5421  N  N   . PRO B  1 227 ? -15.983 8.037   -30.966 1.00 26.25  ?  258  PRO B N   1 
ATOM   5422  C  CA  . PRO B  1 227 ? -15.336 9.225   -30.372 1.00 29.08  ?  258  PRO B CA  1 
ATOM   5423  C  C   . PRO B  1 227 ? -16.329 10.112  -29.615 1.00 25.93  ?  258  PRO B C   1 
ATOM   5424  O  O   . PRO B  1 227 ? -17.487 10.229  -29.994 1.00 25.11  ?  258  PRO B O   1 
ATOM   5425  C  CB  . PRO B  1 227 ? -14.742 9.944   -31.597 1.00 28.26  ?  258  PRO B CB  1 
ATOM   5426  C  CG  . PRO B  1 227 ? -15.732 9.607   -32.718 1.00 27.58  ?  258  PRO B CG  1 
ATOM   5427  C  CD  . PRO B  1 227 ? -16.177 8.182   -32.425 1.00 28.81  ?  258  PRO B CD  1 
ATOM   5428  N  N   . LEU B  1 228 ? -15.882 10.744  -28.532 1.00 25.13  ?  259  LEU B N   1 
ATOM   5429  C  CA  . LEU B  1 228 ? -16.705 11.667  -27.752 1.00 21.68  ?  259  LEU B CA  1 
ATOM   5430  C  C   . LEU B  1 228 ? -16.856 12.952  -28.548 1.00 28.17  ?  259  LEU B C   1 
ATOM   5431  O  O   . LEU B  1 228 ? -15.947 13.782  -28.604 1.00 24.35  ?  259  LEU B O   1 
ATOM   5432  C  CB  . LEU B  1 228 ? -16.070 11.927  -26.393 1.00 26.15  ?  259  LEU B CB  1 
ATOM   5433  C  CG  . LEU B  1 228 ? -15.894 10.660  -25.550 1.00 29.65  ?  259  LEU B CG  1 
ATOM   5434  C  CD1 . LEU B  1 228 ? -15.350 11.011  -24.163 1.00 27.98  ?  259  LEU B CD1 1 
ATOM   5435  C  CD2 . LEU B  1 228 ? -17.188 9.837   -25.485 1.00 27.11  ?  259  LEU B CD2 1 
ATOM   5436  N  N   . GLN B  1 229 ? -18.012 13.108  -29.179 1.00 24.14  ?  260  GLN B N   1 
ATOM   5437  C  CA  . GLN B  1 229 ? -18.295 14.219  -30.083 1.00 28.98  ?  260  GLN B CA  1 
ATOM   5438  C  C   . GLN B  1 229 ? -19.738 14.624  -29.837 1.00 27.16  ?  260  GLN B C   1 
ATOM   5439  O  O   . GLN B  1 229 ? -20.629 13.776  -29.915 1.00 28.95  ?  260  GLN B O   1 
ATOM   5440  C  CB  . GLN B  1 229 ? -18.080 13.827  -31.555 1.00 23.31  ?  260  GLN B CB  1 
ATOM   5441  C  CG  . GLN B  1 229 ? -16.641 13.345  -31.856 1.00 28.73  ?  260  GLN B CG  1 
ATOM   5442  C  CD  . GLN B  1 229 ? -16.382 12.966  -33.318 1.00 32.45  ?  260  GLN B CD  1 
ATOM   5443  O  OE1 . GLN B  1 229 ? -17.305 12.735  -34.099 1.00 28.80  ?  260  GLN B OE1 1 
ATOM   5444  N  NE2 . GLN B  1 229 ? -15.099 12.881  -33.679 1.00 26.64  ?  260  GLN B NE2 1 
ATOM   5445  N  N   . ALA B  1 230 ? -19.976 15.900  -29.518 1.00 27.84  ?  261  ALA B N   1 
ATOM   5446  C  CA  . ALA B  1 230 ? -21.328 16.329  -29.181 1.00 31.08  ?  261  ALA B CA  1 
ATOM   5447  C  C   . ALA B  1 230 ? -21.608 17.714  -29.743 1.00 29.56  ?  261  ALA B C   1 
ATOM   5448  O  O   . ALA B  1 230 ? -20.699 18.494  -30.022 1.00 28.69  ?  261  ALA B O   1 
ATOM   5449  C  CB  . ALA B  1 230 ? -21.567 16.349  -27.663 1.00 26.55  ?  261  ALA B CB  1 
ATOM   5450  N  N   . LYS B  1 231 ? -22.894 18.014  -29.870 1.00 27.70  ?  262  LYS B N   1 
ATOM   5451  C  CA  . LYS B  1 231 ? -23.348 19.314  -30.349 1.00 30.43  ?  262  LYS B CA  1 
ATOM   5452  C  C   . LYS B  1 231 ? -23.147 20.388  -29.282 1.00 31.94  ?  262  LYS B C   1 
ATOM   5453  O  O   . LYS B  1 231 ? -23.301 20.142  -28.082 1.00 30.34  ?  262  LYS B O   1 
ATOM   5454  C  CB  . LYS B  1 231 ? -24.830 19.241  -30.730 1.00 31.15  ?  262  LYS B CB  1 
ATOM   5455  C  CG  . LYS B  1 231 ? -25.120 18.316  -31.912 1.00 29.99  ?  262  LYS B CG  1 
ATOM   5456  C  CD  . LYS B  1 231 ? -26.615 18.121  -32.152 1.00 32.36  ?  262  LYS B CD  1 
ATOM   5457  C  CE  . LYS B  1 231 ? -27.314 19.400  -32.550 1.00 35.26  ?  262  LYS B CE  1 
ATOM   5458  N  NZ  . LYS B  1 231 ? -28.783 19.214  -32.479 1.00 30.02  ?  262  LYS B NZ  1 
ATOM   5459  N  N   . ALA B  1 232 ? -22.812 21.599  -29.732 1.00 32.04  ?  263  ALA B N   1 
ATOM   5460  C  CA  . ALA B  1 232 ? -22.573 22.691  -28.790 1.00 31.48  ?  263  ALA B CA  1 
ATOM   5461  C  C   . ALA B  1 232 ? -23.805 22.979  -27.939 1.00 31.37  ?  263  ALA B C   1 
ATOM   5462  O  O   . ALA B  1 232 ? -23.688 23.242  -26.740 1.00 33.60  ?  263  ALA B O   1 
ATOM   5463  C  CB  . ALA B  1 232 ? -22.135 23.952  -29.540 1.00 36.27  ?  263  ALA B CB  1 
ATOM   5464  N  N   . GLU B  1 233 ? -24.992 22.934  -28.538 1.00 30.21  ?  264  GLU B N   1 
ATOM   5465  C  CA  . GLU B  1 233 ? -26.220 23.188  -27.792 1.00 33.76  ?  264  GLU B CA  1 
ATOM   5466  C  C   . GLU B  1 233 ? -26.440 22.158  -26.696 1.00 36.44  ?  264  GLU B C   1 
ATOM   5467  O  O   . GLU B  1 233 ? -26.979 22.489  -25.632 1.00 36.63  ?  264  GLU B O   1 
ATOM   5468  C  CB  . GLU B  1 233 ? -27.403 23.187  -28.754 1.00 37.37  ?  264  GLU B CB  1 
ATOM   5469  C  CG  . GLU B  1 233 ? -27.141 24.071  -29.950 1.00 48.99  ?  264  GLU B CG  1 
ATOM   5470  C  CD  . GLU B  1 233 ? -26.785 23.274  -31.215 1.00 51.87  ?  264  GLU B CD  1 
ATOM   5471  O  OE1 . GLU B  1 233 ? -25.583 22.876  -31.376 1.00 37.52  ?  264  GLU B OE1 1 
ATOM   5472  O  OE2 . GLU B  1 233 ? -27.726 23.037  -32.027 1.00 51.87  -1 264  GLU B OE2 1 
ATOM   5473  N  N   . ASP B  1 234 ? -26.036 20.908  -26.935 1.00 30.71  ?  265  ASP B N   1 
ATOM   5474  C  CA  . ASP B  1 234 ? -26.188 19.879  -25.916 1.00 27.84  ?  265  ASP B CA  1 
ATOM   5475  C  C   . ASP B  1 234 ? -25.134 20.034  -24.823 1.00 31.12  ?  265  ASP B C   1 
ATOM   5476  O  O   . ASP B  1 234 ? -25.435 19.882  -23.630 1.00 32.31  ?  265  ASP B O   1 
ATOM   5477  C  CB  . ASP B  1 234 ? -26.114 18.500  -26.577 1.00 28.28  ?  265  ASP B CB  1 
ATOM   5478  C  CG  . ASP B  1 234 ? -27.317 18.217  -27.491 1.00 34.10  ?  265  ASP B CG  1 
ATOM   5479  O  OD1 . ASP B  1 234 ? -28.396 18.790  -27.259 1.00 31.67  ?  265  ASP B OD1 1 
ATOM   5480  O  OD2 . ASP B  1 234 ? -27.188 17.436  -28.454 1.00 31.61  -1 265  ASP B OD2 1 
ATOM   5481  N  N   . VAL B  1 235 ? -23.891 20.345  -25.207 1.00 31.01  ?  266  VAL B N   1 
ATOM   5482  C  CA  . VAL B  1 235 ? -22.829 20.565  -24.223 1.00 31.74  ?  266  VAL B CA  1 
ATOM   5483  C  C   . VAL B  1 235 ? -23.190 21.718  -23.292 1.00 35.34  ?  266  VAL B C   1 
ATOM   5484  O  O   . VAL B  1 235 ? -22.822 21.711  -22.105 1.00 33.59  ?  266  VAL B O   1 
ATOM   5485  C  CB  . VAL B  1 235 ? -21.475 20.803  -24.940 1.00 30.45  ?  266  VAL B CB  1 
ATOM   5486  C  CG1 . VAL B  1 235 ? -20.395 21.274  -23.966 1.00 30.19  ?  266  VAL B CG1 1 
ATOM   5487  C  CG2 . VAL B  1 235 ? -21.007 19.533  -25.642 1.00 28.51  ?  266  VAL B CG2 1 
ATOM   5488  N  N   . ALA B  1 236 ? -23.935 22.706  -23.796 1.00 33.42  ?  267  ALA B N   1 
ATOM   5489  C  CA  . ALA B  1 236 ? -24.291 23.859  -22.978 1.00 37.73  ?  267  ALA B CA  1 
ATOM   5490  C  C   . ALA B  1 236 ? -25.144 23.470  -21.782 1.00 37.54  ?  267  ALA B C   1 
ATOM   5491  O  O   . ALA B  1 236 ? -25.040 24.104  -20.731 1.00 36.23  ?  267  ALA B O   1 
ATOM   5492  C  CB  . ALA B  1 236 ? -25.029 24.902  -23.814 1.00 37.40  ?  267  ALA B CB  1 
ATOM   5493  N  N   . LYS B  1 237 ? -26.001 22.450  -21.924 1.00 36.69  ?  268  LYS B N   1 
ATOM   5494  C  CA  . LYS B  1 237 ? -26.816 21.983  -20.803 1.00 36.01  ?  268  LYS B CA  1 
ATOM   5495  C  C   . LYS B  1 237 ? -26.003 21.313  -19.704 1.00 38.03  ?  268  LYS B C   1 
ATOM   5496  O  O   . LYS B  1 237 ? -26.548 21.036  -18.632 1.00 36.66  ?  268  LYS B O   1 
ATOM   5497  C  CB  . LYS B  1 237 ? -27.890 20.992  -21.268 1.00 41.70  ?  268  LYS B CB  1 
ATOM   5498  C  CG  . LYS B  1 237 ? -28.469 21.253  -22.651 1.00 43.44  ?  268  LYS B CG  1 
ATOM   5499  C  CD  . LYS B  1 237 ? -29.229 22.559  -22.734 1.00 47.48  ?  268  LYS B CD  1 
ATOM   5500  C  CE  . LYS B  1 237 ? -30.538 22.373  -23.503 1.00 49.75  ?  268  LYS B CE  1 
ATOM   5501  N  NZ  . LYS B  1 237 ? -31.673 22.049  -22.577 1.00 51.70  ?  268  LYS B NZ  1 
ATOM   5502  N  N   . PHE B  1 238 ? -24.732 21.018  -19.943 1.00 34.82  ?  269  PHE B N   1 
ATOM   5503  C  CA  . PHE B  1 238 ? -23.927 20.309  -18.959 1.00 35.24  ?  269  PHE B CA  1 
ATOM   5504  C  C   . PHE B  1 238 ? -22.690 21.106  -18.595 1.00 36.47  ?  269  PHE B C   1 
ATOM   5505  O  O   . PHE B  1 238 ? -21.724 20.556  -18.060 1.00 34.61  ?  269  PHE B O   1 
ATOM   5506  C  CB  . PHE B  1 238 ? -23.587 18.909  -19.480 1.00 29.29  ?  269  PHE B CB  1 
ATOM   5507  C  CG  . PHE B  1 238 ? -24.810 18.068  -19.688 1.00 27.62  ?  269  PHE B CG  1 
ATOM   5508  C  CD1 . PHE B  1 238 ? -25.407 17.430  -18.611 1.00 30.74  ?  269  PHE B CD1 1 
ATOM   5509  C  CD2 . PHE B  1 238 ? -25.413 17.997  -20.936 1.00 29.14  ?  269  PHE B CD2 1 
ATOM   5510  C  CE1 . PHE B  1 238 ? -26.580 16.693  -18.782 1.00 32.03  ?  269  PHE B CE1 1 
ATOM   5511  C  CE2 . PHE B  1 238 ? -26.575 17.268  -21.129 1.00 29.91  ?  269  PHE B CE2 1 
ATOM   5512  C  CZ  . PHE B  1 238 ? -27.166 16.609  -20.039 1.00 32.14  ?  269  PHE B CZ  1 
ATOM   5513  N  N   . ALA B  1 239 ? -22.729 22.411  -18.851 1.00 41.90  ?  270  ALA B N   1 
ATOM   5514  C  CA  . ALA B  1 239 ? -21.574 23.251  -18.604 1.00 49.59  ?  270  ALA B CA  1 
ATOM   5515  C  C   . ALA B  1 239 ? -21.160 23.239  -17.142 1.00 44.64  ?  270  ALA B C   1 
ATOM   5516  O  O   . ALA B  1 239 ? -20.030 23.633  -16.840 1.00 53.26  ?  270  ALA B O   1 
ATOM   5517  C  CB  . ALA B  1 239 ? -21.857 24.675  -19.090 1.00 51.02  ?  270  ALA B CB  1 
ATOM   5518  N  N   . HIS B  1 240 ? -22.016 22.760  -16.232 1.00 45.37  ?  271  HIS B N   1 
ATOM   5519  C  CA  . HIS B  1 240 ? -21.554 22.595  -14.862 1.00 43.16  ?  271  HIS B CA  1 
ATOM   5520  C  C   . HIS B  1 240 ? -20.495 21.498  -14.767 1.00 48.85  ?  271  HIS B C   1 
ATOM   5521  O  O   . HIS B  1 240 ? -19.499 21.665  -14.053 1.00 45.11  ?  271  HIS B O   1 
ATOM   5522  C  CB  . HIS B  1 240 ? -22.705 22.282  -13.895 1.00 46.52  ?  271  HIS B CB  1 
ATOM   5523  C  CG  . HIS B  1 240 ? -23.677 21.247  -14.368 1.00 42.90  ?  271  HIS B CG  1 
ATOM   5524  N  ND1 . HIS B  1 240 ? -24.500 21.422  -15.462 1.00 47.19  ?  271  HIS B ND1 1 
ATOM   5525  C  CD2 . HIS B  1 240 ? -24.003 20.039  -13.843 1.00 39.78  ?  271  HIS B CD2 1 
ATOM   5526  C  CE1 . HIS B  1 240 ? -25.266 20.353  -15.608 1.00 38.96  ?  271  HIS B CE1 1 
ATOM   5527  N  NE2 . HIS B  1 240 ? -24.978 19.496  -14.644 1.00 42.69  ?  271  HIS B NE2 1 
ATOM   5528  N  N   . ILE B  1 241 ? -20.710 20.363  -15.450 1.00 44.74  ?  272  ILE B N   1 
ATOM   5529  C  CA  . ILE B  1 241 ? -19.786 19.226  -15.391 1.00 39.26  ?  272  ILE B CA  1 
ATOM   5530  C  C   . ILE B  1 241 ? -18.395 19.683  -15.799 1.00 38.61  ?  272  ILE B C   1 
ATOM   5531  O  O   . ILE B  1 241 ? -18.168 20.082  -16.946 1.00 39.13  ?  272  ILE B O   1 
ATOM   5532  C  CB  . ILE B  1 241 ? -20.287 18.072  -16.276 1.00 35.86  ?  272  ILE B CB  1 
ATOM   5533  C  CG1 . ILE B  1 241 ? -21.752 17.763  -15.978 1.00 33.44  ?  272  ILE B CG1 1 
ATOM   5534  C  CG2 . ILE B  1 241 ? -19.433 16.819  -16.089 1.00 32.65  ?  272  ILE B CG2 1 
ATOM   5535  C  CD1 . ILE B  1 241 ? -22.204 16.402  -16.498 1.00 32.52  ?  272  ILE B CD1 1 
ATOM   5536  N  N   . LYS B  1 242 ? -17.448 19.603  -14.858 1.00 36.96  ?  273  LYS B N   1 
ATOM   5537  C  CA  . LYS B  1 242 ? -16.122 20.167  -15.065 1.00 39.68  ?  273  LYS B CA  1 
ATOM   5538  C  C   . LYS B  1 242 ? -15.248 19.277  -15.940 1.00 38.52  ?  273  LYS B C   1 
ATOM   5539  O  O   . LYS B  1 242 ? -14.471 19.783  -16.756 1.00 41.11  ?  273  LYS B O   1 
ATOM   5540  C  CB  . LYS B  1 242 ? -15.445 20.408  -13.709 1.00 39.05  ?  273  LYS B CB  1 
ATOM   5541  N  N   . ASP B  1 243 ? -15.330 17.961  -15.762 1.00 36.27  ?  274  ASP B N   1 
ATOM   5542  C  CA  . ASP B  1 243 ? -14.507 17.041  -16.542 1.00 33.72  ?  274  ASP B CA  1 
ATOM   5543  C  C   . ASP B  1 243 ? -14.968 17.041  -17.994 1.00 34.23  ?  274  ASP B C   1 
ATOM   5544  O  O   . ASP B  1 243 ? -16.139 16.760  -18.271 1.00 30.74  ?  274  ASP B O   1 
ATOM   5545  C  CB  . ASP B  1 243 ? -14.594 15.633  -15.964 1.00 31.92  ?  274  ASP B CB  1 
ATOM   5546  C  CG  . ASP B  1 243 ? -13.764 14.631  -16.750 1.00 37.24  ?  274  ASP B CG  1 
ATOM   5547  O  OD1 . ASP B  1 243 ? -12.516 14.618  -16.598 1.00 35.96  ?  274  ASP B OD1 1 
ATOM   5548  O  OD2 . ASP B  1 243 ? -14.338 13.867  -17.545 1.00 33.70  -1 274  ASP B OD2 1 
ATOM   5549  N  N   . LYS B  1 244 ? -14.041 17.319  -18.920 1.00 30.81  ?  275  LYS B N   1 
ATOM   5550  C  CA  . LYS B  1 244 ? -14.393 17.470  -20.330 1.00 32.55  ?  275  LYS B CA  1 
ATOM   5551  C  C   . LYS B  1 244 ? -14.998 16.199  -20.921 1.00 31.50  ?  275  LYS B C   1 
ATOM   5552  O  O   . LYS B  1 244 ? -15.997 16.257  -21.656 1.00 31.86  ?  275  LYS B O   1 
ATOM   5553  C  CB  . LYS B  1 244 ? -13.161 17.891  -21.129 1.00 35.62  ?  275  LYS B CB  1 
ATOM   5554  C  CG  . LYS B  1 244 ? -13.471 18.289  -22.578 1.00 41.17  ?  275  LYS B CG  1 
ATOM   5555  C  CD  . LYS B  1 244 ? -12.532 17.613  -23.584 1.00 45.48  ?  275  LYS B CD  1 
ATOM   5556  C  CE  . LYS B  1 244 ? -12.925 16.165  -23.967 1.00 48.58  ?  275  LYS B CE  1 
ATOM   5557  N  NZ  . LYS B  1 244 ? -14.331 15.880  -24.473 1.00 37.19  ?  275  LYS B NZ  1 
ATOM   5558  N  N   . ASP B  1 245 ? -14.384 15.047  -20.662 1.00 29.41  ?  276  ASP B N   1 
ATOM   5559  C  CA  . ASP B  1 245 ? -14.934 13.806  -21.204 1.00 30.89  ?  276  ASP B CA  1 
ATOM   5560  C  C   . ASP B  1 245 ? -16.327 13.534  -20.656 1.00 28.87  ?  276  ASP B C   1 
ATOM   5561  O  O   . ASP B  1 245 ? -17.245 13.203  -21.408 1.00 24.66  ?  276  ASP B O   1 
ATOM   5562  C  CB  . ASP B  1 245 ? -14.017 12.633  -20.900 1.00 31.01  ?  276  ASP B CB  1 
ATOM   5563  C  CG  . ASP B  1 245 ? -12.849 12.562  -21.848 1.00 38.07  ?  276  ASP B CG  1 
ATOM   5564  O  OD1 . ASP B  1 245 ? -12.670 13.503  -22.653 1.00 30.91  ?  276  ASP B OD1 1 
ATOM   5565  O  OD2 . ASP B  1 245 ? -12.123 11.560  -21.783 1.00 44.72  -1 276  ASP B OD2 1 
ATOM   5566  N  N   . ARG B  1 246 ? -16.503 13.667  -19.343 1.00 28.44  ?  277  ARG B N   1 
ATOM   5567  C  CA  . ARG B  1 246 ? -17.828 13.447  -18.761 1.00 28.03  ?  277  ARG B CA  1 
ATOM   5568  C  C   . ARG B  1 246 ? -18.850 14.421  -19.340 1.00 27.18  ?  277  ARG B C   1 
ATOM   5569  O  O   . ARG B  1 246 ? -19.977 14.032  -19.666 1.00 24.33  ?  277  ARG B O   1 
ATOM   5570  C  CB  . ARG B  1 246 ? -17.735 13.557  -17.228 1.00 27.79  ?  277  ARG B CB  1 
ATOM   5571  C  CG  . ARG B  1 246 ? -19.046 13.307  -16.457 1.00 31.97  ?  277  ARG B CG  1 
ATOM   5572  C  CD  . ARG B  1 246 ? -19.613 11.918  -16.731 1.00 30.59  ?  277  ARG B CD  1 
ATOM   5573  N  NE  . ARG B  1 246 ? -20.704 11.556  -15.833 1.00 28.81  ?  277  ARG B NE  1 
ATOM   5574  C  CZ  . ARG B  1 246 ? -21.303 10.371  -15.844 1.00 29.61  ?  277  ARG B CZ  1 
ATOM   5575  N  NH1 . ARG B  1 246 ? -20.872 9.387   -16.625 1.00 22.23  ?  277  ARG B NH1 1 
ATOM   5576  N  NH2 . ARG B  1 246 ? -22.369 10.172  -15.066 1.00 27.10  ?  277  ARG B NH2 1 
ATOM   5577  N  N   . ARG B  1 247 ? -18.462 15.687  -19.518 1.00 28.32  ?  278  ARG B N   1 
ATOM   5578  C  CA  . ARG B  1 247 ? -19.397 16.671  -20.064 1.00 26.89  ?  278  ARG B CA  1 
ATOM   5579  C  C   . ARG B  1 247 ? -19.804 16.350  -21.507 1.00 26.65  ?  278  ARG B C   1 
ATOM   5580  O  O   . ARG B  1 247 ? -20.985 16.468  -21.864 1.00 23.71  ?  278  ARG B O   1 
ATOM   5581  C  CB  . ARG B  1 247 ? -18.781 18.067  -19.970 1.00 28.83  ?  278  ARG B CB  1 
ATOM   5582  C  CG  . ARG B  1 247 ? -19.694 19.152  -20.499 1.00 29.30  ?  278  ARG B CG  1 
ATOM   5583  C  CD  . ARG B  1 247 ? -19.080 20.525  -20.300 1.00 36.79  ?  278  ARG B CD  1 
ATOM   5584  N  NE  . ARG B  1 247 ? -17.816 20.690  -21.012 1.00 38.51  ?  278  ARG B NE  1 
ATOM   5585  C  CZ  . ARG B  1 247 ? -16.643 20.874  -20.415 1.00 42.08  ?  278  ARG B CZ  1 
ATOM   5586  N  NH1 . ARG B  1 247 ? -16.529 20.880  -19.095 1.00 43.09  ?  278  ARG B NH1 1 
ATOM   5587  N  NH2 . ARG B  1 247 ? -15.554 21.043  -21.160 1.00 42.09  ?  278  ARG B NH2 1 
ATOM   5588  N  N   . THR B  1 248 ? -18.842 15.960  -22.351 1.00 24.30  ?  279  THR B N   1 
ATOM   5589  C  CA  . THR B  1 248 ? -19.147 15.606  -23.734 1.00 26.91  ?  279  THR B CA  1 
ATOM   5590  C  C   . THR B  1 248 ? -20.003 14.348  -23.785 1.00 24.95  ?  279  THR B C   1 
ATOM   5591  O  O   . THR B  1 248 ? -21.016 14.298  -24.490 1.00 24.06  ?  279  THR B O   1 
ATOM   5592  C  CB  . THR B  1 248 ? -17.843 15.401  -24.516 1.00 29.52  ?  279  THR B CB  1 
ATOM   5593  O  OG1 . THR B  1 248 ? -16.991 16.526  -24.307 1.00 29.44  ?  279  THR B OG1 1 
ATOM   5594  C  CG2 . THR B  1 248 ? -18.114 15.236  -26.005 1.00 26.61  ?  279  THR B CG2 1 
ATOM   5595  N  N   . TYR B  1 249 ? -19.622 13.333  -23.002 1.00 25.74  ?  280  TYR B N   1 
ATOM   5596  C  CA  . TYR B  1 249 ? -20.404 12.099  -22.924 1.00 24.05  ?  280  TYR B CA  1 
ATOM   5597  C  C   . TYR B  1 249 ? -21.831 12.386  -22.471 1.00 23.55  ?  280  TYR B C   1 
ATOM   5598  O  O   . TYR B  1 249 ? -22.798 11.887  -23.062 1.00 23.12  ?  280  TYR B O   1 
ATOM   5599  C  CB  . TYR B  1 249 ? -19.691 11.142  -21.957 1.00 22.82  ?  280  TYR B CB  1 
ATOM   5600  C  CG  . TYR B  1 249 ? -20.392 9.838   -21.610 1.00 23.70  ?  280  TYR B CG  1 
ATOM   5601  C  CD1 . TYR B  1 249 ? -21.364 9.786   -20.627 1.00 19.63  ?  280  TYR B CD1 1 
ATOM   5602  C  CD2 . TYR B  1 249 ? -20.016 8.642   -22.233 1.00 23.01  ?  280  TYR B CD2 1 
ATOM   5603  C  CE1 . TYR B  1 249 ? -21.976 8.582   -20.283 1.00 22.93  ?  280  TYR B CE1 1 
ATOM   5604  C  CE2 . TYR B  1 249 ? -20.601 7.419   -21.884 1.00 20.93  ?  280  TYR B CE2 1 
ATOM   5605  C  CZ  . TYR B  1 249 ? -21.589 7.403   -20.922 1.00 22.39  ?  280  TYR B CZ  1 
ATOM   5606  O  OH  . TYR B  1 249 ? -22.164 6.209   -20.565 1.00 23.16  ?  280  TYR B OH  1 
ATOM   5607  N  N   . ALA B  1 250 ? -21.991 13.184  -21.406 1.00 24.40  ?  281  ALA B N   1 
ATOM   5608  C  CA  . ALA B  1 250 ? -23.341 13.565  -20.980 1.00 24.40  ?  281  ALA B CA  1 
ATOM   5609  C  C   . ALA B  1 250 ? -24.127 14.163  -22.132 1.00 22.73  ?  281  ALA B C   1 
ATOM   5610  O  O   . ALA B  1 250 ? -25.310 13.848  -22.331 1.00 23.49  ?  281  ALA B O   1 
ATOM   5611  C  CB  . ALA B  1 250 ? -23.280 14.567  -19.817 1.00 22.79  ?  281  ALA B CB  1 
ATOM   5612  N  N   . ALA B  1 251 ? -23.488 15.049  -22.901 1.00 24.53  ?  282  ALA B N   1 
ATOM   5613  C  CA  . ALA B  1 251 ? -24.182 15.690  -24.013 1.00 25.71  ?  282  ALA B CA  1 
ATOM   5614  C  C   . ALA B  1 251 ? -24.585 14.678  -25.069 1.00 24.66  ?  282  ALA B C   1 
ATOM   5615  O  O   . ALA B  1 251 ? -25.665 14.802  -25.673 1.00 24.87  ?  282  ALA B O   1 
ATOM   5616  C  CB  . ALA B  1 251 ? -23.309 16.803  -24.618 1.00 22.66  ?  282  ALA B CB  1 
ATOM   5617  N  N   . MET B  1 252 ? -23.754 13.652  -25.296 1.00 22.94  ?  283  MET B N   1 
ATOM   5618  C  CA  . MET B  1 252 ? -24.145 12.635  -26.271 1.00 23.66  ?  283  MET B CA  1 
ATOM   5619  C  C   . MET B  1 252 ? -25.327 11.802  -25.812 1.00 26.26  ?  283  MET B C   1 
ATOM   5620  O  O   . MET B  1 252 ? -26.196 11.453  -26.632 1.00 23.43  ?  283  MET B O   1 
ATOM   5621  C  CB  . MET B  1 252 ? -22.996 11.690  -26.671 1.00 23.19  ?  283  MET B CB  1 
ATOM   5622  C  CG  . MET B  1 252 ? -21.750 12.290  -27.279 1.00 24.98  ?  283  MET B CG  1 
ATOM   5623  S  SD  . MET B  1 252 ? -20.244 11.406  -26.911 1.00 25.43  ?  283  MET B SD  1 
ATOM   5624  C  CE  . MET B  1 252 ? -20.332 10.231  -28.229 1.00 23.18  ?  283  MET B CE  1 
ATOM   5625  N  N   . VAL B  1 253 ? -25.367 11.452  -24.521 1.00 23.99  ?  284  VAL B N   1 
ATOM   5626  C  CA  . VAL B  1 253 ? -26.541 10.758  -23.990 1.00 24.16  ?  284  VAL B CA  1 
ATOM   5627  C  C   . VAL B  1 253 ? -27.768 11.651  -24.096 1.00 24.11  ?  284  VAL B C   1 
ATOM   5628  O  O   . VAL B  1 253 ? -28.844 11.207  -24.513 1.00 26.25  ?  284  VAL B O   1 
ATOM   5629  C  CB  . VAL B  1 253 ? -26.284 10.303  -22.537 1.00 22.30  ?  284  VAL B CB  1 
ATOM   5630  C  CG1 . VAL B  1 253 ? -27.554 9.672   -21.928 1.00 23.93  ?  284  VAL B CG1 1 
ATOM   5631  C  CG2 . VAL B  1 253 ? -25.147 9.292   -22.489 1.00 21.66  ?  284  VAL B CG2 1 
ATOM   5632  N  N   . TYR B  1 254 ? -27.620 12.933  -23.758 1.00 26.20  ?  285  TYR B N   1 
ATOM   5633  C  CA  . TYR B  1 254 ? -28.750 13.865  -23.843 1.00 25.46  ?  285  TYR B CA  1 
ATOM   5634  C  C   . TYR B  1 254 ? -29.335 13.933  -25.252 1.00 25.81  ?  285  TYR B C   1 
ATOM   5635  O  O   . TYR B  1 254 ? -30.558 14.050  -25.418 1.00 26.52  ?  285  TYR B O   1 
ATOM   5636  C  CB  . TYR B  1 254 ? -28.320 15.259  -23.374 1.00 24.40  ?  285  TYR B CB  1 
ATOM   5637  C  CG  . TYR B  1 254 ? -29.479 16.256  -23.329 1.00 25.63  ?  285  TYR B CG  1 
ATOM   5638  C  CD1 . TYR B  1 254 ? -30.453 16.179  -22.345 1.00 27.97  ?  285  TYR B CD1 1 
ATOM   5639  C  CD2 . TYR B  1 254 ? -29.597 17.252  -24.292 1.00 27.98  ?  285  TYR B CD2 1 
ATOM   5640  C  CE1 . TYR B  1 254 ? -31.497 17.089  -22.300 1.00 32.51  ?  285  TYR B CE1 1 
ATOM   5641  C  CE2 . TYR B  1 254 ? -30.635 18.156  -24.266 1.00 31.77  ?  285  TYR B CE2 1 
ATOM   5642  C  CZ  . TYR B  1 254 ? -31.586 18.063  -23.277 1.00 36.49  ?  285  TYR B CZ  1 
ATOM   5643  O  OH  . TYR B  1 254 ? -32.611 18.971  -23.247 1.00 40.27  ?  285  TYR B OH  1 
ATOM   5644  N  N   . ALA B  1 255 ? -28.489 13.854  -26.291 1.00 27.65  ?  286  ALA B N   1 
ATOM   5645  C  CA  . ALA B  1 255 ? -29.008 13.885  -27.660 1.00 27.56  ?  286  ALA B CA  1 
ATOM   5646  C  C   . ALA B  1 255 ? -29.880 12.672  -27.955 1.00 25.49  ?  286  ALA B C   1 
ATOM   5647  O  O   . ALA B  1 255 ? -30.893 12.788  -28.660 1.00 25.04  ?  286  ALA B O   1 
ATOM   5648  C  CB  . ALA B  1 255 ? -27.870 13.960  -28.681 1.00 26.24  ?  286  ALA B CB  1 
ATOM   5649  N  N   . VAL B  1 256 ? -29.479 11.492  -27.469 1.00 24.72  ?  287  VAL B N   1 
ATOM   5650  C  CA  . VAL B  1 256 ? -30.358 10.326  -27.547 1.00 25.16  ?  287  VAL B CA  1 
ATOM   5651  C  C   . VAL B  1 256 ? -31.677 10.615  -26.837 1.00 28.12  ?  287  VAL B C   1 
ATOM   5652  O  O   . VAL B  1 256 ? -32.754 10.366  -27.384 1.00 25.16  ?  287  VAL B O   1 
ATOM   5653  C  CB  . VAL B  1 256 ? -29.665 9.081   -26.965 1.00 25.97  ?  287  VAL B CB  1 
ATOM   5654  C  CG1 . VAL B  1 256 ? -30.655 7.931   -26.785 1.00 20.11  ?  287  VAL B CG1 1 
ATOM   5655  C  CG2 . VAL B  1 256 ? -28.477 8.646   -27.862 1.00 22.68  ?  287  VAL B CG2 1 
ATOM   5656  N  N   . ASP B  1 257 ? -31.616 11.158  -25.611 1.00 25.86  ?  288  ASP B N   1 
ATOM   5657  C  CA  . ASP B  1 257 ? -32.861 11.499  -24.911 1.00 28.57  ?  288  ASP B CA  1 
ATOM   5658  C  C   . ASP B  1 257 ? -33.752 12.433  -25.734 1.00 28.33  ?  288  ASP B C   1 
ATOM   5659  O  O   . ASP B  1 257 ? -34.974 12.237  -25.807 1.00 25.78  ?  288  ASP B O   1 
ATOM   5660  C  CB  . ASP B  1 257 ? -32.558 12.128  -23.552 1.00 26.91  ?  288  ASP B CB  1 
ATOM   5661  C  CG  . ASP B  1 257 ? -33.758 12.082  -22.620 1.00 27.40  ?  288  ASP B CG  1 
ATOM   5662  O  OD1 . ASP B  1 257 ? -34.106 10.976  -22.134 1.00 26.11  ?  288  ASP B OD1 1 
ATOM   5663  O  OD2 . ASP B  1 257 ? -34.362 13.156  -22.394 1.00 29.45  -1 288  ASP B OD2 1 
ATOM   5664  N  N   . ARG B  1 258 ? -33.174 13.469  -26.348 1.00 29.32  ?  289  ARG B N   1 
ATOM   5665  C  CA  . ARG B  1 258 ? -33.997 14.361  -27.166 1.00 28.03  ?  289  ARG B CA  1 
ATOM   5666  C  C   . ARG B  1 258 ? -34.697 13.593  -28.278 1.00 32.88  ?  289  ARG B C   1 
ATOM   5667  O  O   . ARG B  1 258 ? -35.882 13.842  -28.584 1.00 26.63  ?  289  ARG B O   1 
ATOM   5668  C  CB  . ARG B  1 258 ? -33.139 15.464  -27.788 1.00 31.29  ?  289  ARG B CB  1 
ATOM   5669  C  CG  . ARG B  1 258 ? -32.605 16.543  -26.850 1.00 34.67  ?  289  ARG B CG  1 
ATOM   5670  C  CD  . ARG B  1 258 ? -32.020 17.717  -27.675 1.00 36.75  ?  289  ARG B CD  1 
ATOM   5671  N  NE  . ARG B  1 258 ? -30.748 17.371  -28.314 1.00 30.17  ?  289  ARG B NE  1 
ATOM   5672  C  CZ  . ARG B  1 258 ? -30.619 16.976  -29.578 1.00 33.92  ?  289  ARG B CZ  1 
ATOM   5673  N  NH1 . ARG B  1 258 ? -31.673 16.845  -30.379 1.00 31.09  ?  289  ARG B NH1 1 
ATOM   5674  N  NH2 . ARG B  1 258 ? -29.406 16.710  -30.055 1.00 25.55  ?  289  ARG B NH2 1 
ATOM   5675  N  N   . GLY B  1 259 ? -33.963 12.683  -28.928 1.00 25.63  ?  290  GLY B N   1 
ATOM   5676  C  CA  . GLY B  1 259 ? -34.547 11.937  -30.031 1.00 26.11  ?  290  GLY B CA  1 
ATOM   5677  C  C   . GLY B  1 259 ? -35.655 11.024  -29.563 1.00 29.56  ?  290  GLY B C   1 
ATOM   5678  O  O   . GLY B  1 259 ? -36.664 10.845  -30.260 1.00 27.46  ?  290  GLY B O   1 
ATOM   5679  N  N   . VAL B  1 260 ? -35.492 10.441  -28.375 1.00 27.75  ?  291  VAL B N   1 
ATOM   5680  C  CA  . VAL B  1 260 ? -36.549 9.606   -27.809 1.00 29.54  ?  291  VAL B CA  1 
ATOM   5681  C  C   . VAL B  1 260 ? -37.810 10.433  -27.557 1.00 29.22  ?  291  VAL B C   1 
ATOM   5682  O  O   . VAL B  1 260 ? -38.932 9.979   -27.823 1.00 29.59  ?  291  VAL B O   1 
ATOM   5683  C  CB  . VAL B  1 260 ? -36.034 8.912   -26.534 1.00 29.05  ?  291  VAL B CB  1 
ATOM   5684  C  CG1 . VAL B  1 260 ? -37.171 8.210   -25.794 1.00 27.30  ?  291  VAL B CG1 1 
ATOM   5685  C  CG2 . VAL B  1 260 ? -34.930 7.906   -26.919 1.00 26.27  ?  291  VAL B CG2 1 
ATOM   5686  N  N   . GLY B  1 261 ? -37.643 11.667  -27.078 1.00 29.43  ?  292  GLY B N   1 
ATOM   5687  C  CA  . GLY B  1 261 ? -38.787 12.553  -26.930 1.00 29.54  ?  292  GLY B CA  1 
ATOM   5688  C  C   . GLY B  1 261 ? -39.518 12.786  -28.238 1.00 31.92  ?  292  GLY B C   1 
ATOM   5689  O  O   . GLY B  1 261 ? -40.754 12.798  -28.276 1.00 31.51  ?  292  GLY B O   1 
ATOM   5690  N  N   . LYS B  1 262 ? -38.772 12.989  -29.332 1.00 30.54  ?  293  LYS B N   1 
ATOM   5691  C  CA  . LYS B  1 262 ? -39.425 13.219  -30.627 1.00 30.51  ?  293  LYS B CA  1 
ATOM   5692  C  C   . LYS B  1 262 ? -40.108 11.952  -31.130 1.00 32.36  ?  293  LYS B C   1 
ATOM   5693  O  O   . LYS B  1 262 ? -41.182 12.009  -31.747 1.00 32.57  ?  293  LYS B O   1 
ATOM   5694  C  CB  . LYS B  1 262 ? -38.404 13.709  -31.659 1.00 31.19  ?  293  LYS B CB  1 
ATOM   5695  C  CG  . LYS B  1 262 ? -37.909 15.132  -31.450 1.00 35.38  ?  293  LYS B CG  1 
ATOM   5696  C  CD  . LYS B  1 262 ? -39.072 16.120  -31.449 1.00 39.88  ?  293  LYS B CD  1 
ATOM   5697  C  CE  . LYS B  1 262 ? -38.676 17.472  -30.848 1.00 54.72  ?  293  LYS B CE  1 
ATOM   5698  N  NZ  . LYS B  1 262 ? -39.440 17.819  -29.599 1.00 57.92  ?  293  LYS B NZ  1 
ATOM   5699  N  N   . ILE B  1 263 ? -39.483 10.801  -30.902 1.00 26.34  ?  294  ILE B N   1 
ATOM   5700  C  CA  . ILE B  1 263 ? -40.088 9.528   -31.270 1.00 30.35  ?  294  ILE B CA  1 
ATOM   5701  C  C   . ILE B  1 263 ? -41.387 9.331   -30.505 1.00 29.34  ?  294  ILE B C   1 
ATOM   5702  O  O   . ILE B  1 263 ? -42.422 8.970   -31.079 1.00 29.69  ?  294  ILE B O   1 
ATOM   5703  C  CB  . ILE B  1 263 ? -39.091 8.379   -31.020 1.00 27.15  ?  294  ILE B CB  1 
ATOM   5704  C  CG1 . ILE B  1 263 ? -37.989 8.399   -32.076 1.00 27.71  ?  294  ILE B CG1 1 
ATOM   5705  C  CG2 . ILE B  1 263 ? -39.788 7.027   -30.970 1.00 24.01  ?  294  ILE B CG2 1 
ATOM   5706  C  CD1 . ILE B  1 263 ? -36.702 7.717   -31.628 1.00 26.02  ?  294  ILE B CD1 1 
ATOM   5707  N  N   . VAL B  1 264 ? -41.360 9.593   -29.200 1.00 30.48  ?  295  VAL B N   1 
ATOM   5708  C  CA  . VAL B  1 264 ? -42.560 9.426   -28.384 1.00 31.54  ?  295  VAL B CA  1 
ATOM   5709  C  C   . VAL B  1 264 ? -43.686 10.328  -28.893 1.00 35.71  ?  295  VAL B C   1 
ATOM   5710  O  O   . VAL B  1 264 ? -44.850 9.914   -28.987 1.00 33.58  ?  295  VAL B O   1 
ATOM   5711  C  CB  . VAL B  1 264 ? -42.227 9.704   -26.907 1.00 33.07  ?  295  VAL B CB  1 
ATOM   5712  C  CG1 . VAL B  1 264 ? -43.513 9.929   -26.098 1.00 30.46  ?  295  VAL B CG1 1 
ATOM   5713  C  CG2 . VAL B  1 264 ? -41.386 8.565   -26.317 1.00 31.88  ?  295  VAL B CG2 1 
ATOM   5714  N  N   . GLN B  1 265 ? -43.364 11.569  -29.247 1.00 34.63  ?  296  GLN B N   1 
ATOM   5715  C  CA  . GLN B  1 265 ? -44.428 12.466  -29.688 1.00 32.82  ?  296  GLN B CA  1 
ATOM   5716  C  C   . GLN B  1 265 ? -45.009 11.996  -31.024 1.00 36.56  ?  296  GLN B C   1 
ATOM   5717  O  O   . GLN B  1 265 ? -46.230 12.034  -31.236 1.00 34.76  ?  296  GLN B O   1 
ATOM   5718  C  CB  . GLN B  1 265 ? -43.879 13.897  -29.734 1.00 38.02  ?  296  GLN B CB  1 
ATOM   5719  C  CG  . GLN B  1 265 ? -44.661 14.923  -30.548 1.00 43.30  ?  296  GLN B CG  1 
ATOM   5720  C  CD  . GLN B  1 265 ? -43.823 16.168  -30.880 1.00 58.72  ?  296  GLN B CD  1 
ATOM   5721  O  OE1 . GLN B  1 265 ? -44.061 16.845  -31.887 1.00 61.25  ?  296  GLN B OE1 1 
ATOM   5722  N  NE2 . GLN B  1 265 ? -42.835 16.472  -30.024 1.00 54.58  ?  296  GLN B NE2 1 
ATOM   5723  N  N   . THR B  1 266 ? -44.153 11.503  -31.918 1.00 32.39  ?  297  THR B N   1 
ATOM   5724  C  CA  . THR B  1 266 ? -44.628 10.895  -33.153 1.00 31.42  ?  297  THR B CA  1 
ATOM   5725  C  C   . THR B  1 266 ? -45.556 9.722   -32.869 1.00 35.74  ?  297  THR B C   1 
ATOM   5726  O  O   . THR B  1 266 ? -46.614 9.582   -33.510 1.00 34.85  ?  297  THR B O   1 
ATOM   5727  C  CB  . THR B  1 266 ? -43.432 10.450  -33.993 1.00 30.45  ?  297  THR B CB  1 
ATOM   5728  O  OG1 . THR B  1 266 ? -42.621 11.592  -34.282 1.00 31.97  ?  297  THR B OG1 1 
ATOM   5729  C  CG2 . THR B  1 266 ? -43.884 9.830   -35.307 1.00 32.32  ?  297  THR B CG2 1 
ATOM   5730  N  N   . LEU B  1 267 ? -45.183 8.864   -31.917 1.00 30.58  ?  298  LEU B N   1 
ATOM   5731  C  CA  . LEU B  1 267 ? -46.024 7.708   -31.604 1.00 34.60  ?  298  LEU B CA  1 
ATOM   5732  C  C   . LEU B  1 267 ? -47.390 8.140   -31.099 1.00 33.04  ?  298  LEU B C   1 
ATOM   5733  O  O   . LEU B  1 267 ? -48.399 7.469   -31.367 1.00 35.83  ?  298  LEU B O   1 
ATOM   5734  C  CB  . LEU B  1 267 ? -45.337 6.809   -30.568 1.00 29.79  ?  298  LEU B CB  1 
ATOM   5735  C  CG  . LEU B  1 267 ? -44.129 6.022   -31.090 1.00 33.33  ?  298  LEU B CG  1 
ATOM   5736  C  CD1 . LEU B  1 267 ? -43.387 5.333   -29.934 1.00 32.39  ?  298  LEU B CD1 1 
ATOM   5737  C  CD2 . LEU B  1 267 ? -44.548 5.011   -32.168 1.00 30.06  ?  298  LEU B CD2 1 
ATOM   5738  N  N   . LYS B  1 268 ? -47.450 9.251   -30.367 1.00 30.94  ?  299  LYS B N   1 
ATOM   5739  C  CA  . LYS B  1 268 ? -48.746 9.718   -29.888 1.00 35.57  ?  299  LYS B CA  1 
ATOM   5740  C  C   . LYS B  1 268 ? -49.555 10.325  -31.024 1.00 35.58  ?  299  LYS B C   1 
ATOM   5741  O  O   . LYS B  1 268 ? -50.767 10.090  -31.123 1.00 40.69  ?  299  LYS B O   1 
ATOM   5742  C  CB  . LYS B  1 268 ? -48.562 10.725  -28.755 1.00 34.42  ?  299  LYS B CB  1 
ATOM   5743  C  CG  . LYS B  1 268 ? -47.983 10.128  -27.470 1.00 35.12  ?  299  LYS B CG  1 
ATOM   5744  C  CD  . LYS B  1 268 ? -47.622 11.215  -26.465 1.00 33.16  ?  299  LYS B CD  1 
ATOM   5745  C  CE  . LYS B  1 268 ? -47.133 10.618  -25.169 1.00 40.19  ?  299  LYS B CE  1 
ATOM   5746  N  NZ  . LYS B  1 268 ? -46.764 11.678  -24.191 1.00 42.71  ?  299  LYS B NZ  1 
ATOM   5747  N  N   . GLU B  1 269 ? -48.901 11.094  -31.900 1.00 38.44  ?  300  GLU B N   1 
ATOM   5748  C  CA  . GLU B  1 269 ? -49.595 11.696  -33.041 1.00 36.76  ?  300  GLU B CA  1 
ATOM   5749  C  C   . GLU B  1 269 ? -50.147 10.645  -33.996 1.00 41.11  ?  300  GLU B C   1 
ATOM   5750  O  O   . GLU B  1 269 ? -51.236 10.821  -34.559 1.00 40.09  ?  300  GLU B O   1 
ATOM   5751  C  CB  . GLU B  1 269 ? -48.654 12.627  -33.797 1.00 37.12  ?  300  GLU B CB  1 
ATOM   5752  C  CG  . GLU B  1 269 ? -48.189 13.832  -33.008 1.00 39.34  ?  300  GLU B CG  1 
ATOM   5753  C  CD  . GLU B  1 269 ? -47.183 14.650  -33.773 1.00 42.52  ?  300  GLU B CD  1 
ATOM   5754  O  OE1 . GLU B  1 269 ? -46.817 14.234  -34.900 1.00 47.23  ?  300  GLU B OE1 1 
ATOM   5755  O  OE2 . GLU B  1 269 ? -46.789 15.721  -33.267 1.00 44.95  -1 300  GLU B OE2 1 
ATOM   5756  N  N   . THR B  1 270 ? -49.395 9.572   -34.242 1.00 35.52  ?  301  THR B N   1 
ATOM   5757  C  CA  . THR B  1 270 ? -49.905 8.530   -35.123 1.00 38.93  ?  301  THR B CA  1 
ATOM   5758  C  C   . THR B  1 270 ? -50.804 7.536   -34.409 1.00 39.66  ?  301  THR B C   1 
ATOM   5759  O  O   . THR B  1 270 ? -51.234 6.565   -35.041 1.00 38.78  ?  301  THR B O   1 
ATOM   5760  C  CB  . THR B  1 270 ? -48.769 7.756   -35.779 1.00 36.85  ?  301  THR B CB  1 
ATOM   5761  O  OG1 . THR B  1 270 ? -48.034 7.058   -34.762 1.00 39.54  ?  301  THR B OG1 1 
ATOM   5762  C  CG2 . THR B  1 270 ? -47.861 8.694   -36.555 1.00 35.37  ?  301  THR B CG2 1 
ATOM   5763  N  N   . LYS B  1 271 ? -51.060 7.727   -33.114 1.00 34.96  ?  302  LYS B N   1 
ATOM   5764  C  CA  . LYS B  1 271 ? -51.910 6.846   -32.319 1.00 39.31  ?  302  LYS B CA  1 
ATOM   5765  C  C   . LYS B  1 271 ? -51.329 5.436   -32.185 1.00 41.14  ?  302  LYS B C   1 
ATOM   5766  O  O   . LYS B  1 271 ? -52.066 4.472   -31.950 1.00 36.10  ?  302  LYS B O   1 
ATOM   5767  C  CB  . LYS B  1 271 ? -53.331 6.803   -32.917 1.00 43.81  ?  302  LYS B CB  1 
ATOM   5768  C  CG  . LYS B  1 271 ? -54.228 7.959   -32.449 1.00 45.86  ?  302  LYS B CG  1 
ATOM   5769  C  CD  . LYS B  1 271 ? -54.967 8.575   -33.653 1.00 52.27  ?  302  LYS B CD  1 
ATOM   5770  C  CE  . LYS B  1 271 ? -55.507 9.984   -33.383 1.00 54.82  ?  302  LYS B CE  1 
ATOM   5771  N  NZ  . LYS B  1 271 ? -56.958 9.989   -33.004 1.00 59.16  ?  302  LYS B NZ  1 
ATOM   5772  N  N   . GLN B  1 272 ? -50.012 5.286   -32.320 1.00 39.12  ?  303  GLN B N   1 
ATOM   5773  C  CA  . GLN B  1 272 ? -49.346 4.002   -32.120 1.00 38.46  ?  303  GLN B CA  1 
ATOM   5774  C  C   . GLN B  1 272 ? -48.757 3.843   -30.715 1.00 35.29  ?  303  GLN B C   1 
ATOM   5775  O  O   . GLN B  1 272 ? -48.269 2.762   -30.389 1.00 38.06  ?  303  GLN B O   1 
ATOM   5776  C  CB  . GLN B  1 272 ? -48.230 3.811   -33.169 1.00 39.19  ?  303  GLN B CB  1 
ATOM   5777  C  CG  . GLN B  1 272 ? -48.684 3.392   -34.588 1.00 40.86  ?  303  GLN B CG  1 
ATOM   5778  C  CD  . GLN B  1 272 ? -47.630 3.711   -35.676 1.00 40.18  ?  303  GLN B CD  1 
ATOM   5779  O  OE1 . GLN B  1 272 ? -47.246 2.847   -36.483 1.00 36.48  ?  303  GLN B OE1 1 
ATOM   5780  N  NE2 . GLN B  1 272 ? -47.178 4.958   -35.705 1.00 40.24  ?  303  GLN B NE2 1 
ATOM   5781  N  N   . PHE B  1 273 ? -48.833 4.872   -29.869 1.00 32.50  ?  304  PHE B N   1 
ATOM   5782  C  CA  . PHE B  1 273 ? -48.109 4.889   -28.590 1.00 35.41  ?  304  PHE B CA  1 
ATOM   5783  C  C   . PHE B  1 273 ? -48.600 3.810   -27.622 1.00 36.40  ?  304  PHE B C   1 
ATOM   5784  O  O   . PHE B  1 273 ? -47.793 3.123   -26.982 1.00 30.73  ?  304  PHE B O   1 
ATOM   5785  C  CB  . PHE B  1 273 ? -48.259 6.273   -27.960 1.00 32.99  ?  304  PHE B CB  1 
ATOM   5786  C  CG  . PHE B  1 273 ? -47.448 6.492   -26.712 1.00 38.59  ?  304  PHE B CG  1 
ATOM   5787  C  CD1 . PHE B  1 273 ? -46.059 6.471   -26.740 1.00 36.01  ?  304  PHE B CD1 1 
ATOM   5788  C  CD2 . PHE B  1 273 ? -48.081 6.751   -25.510 1.00 39.91  ?  304  PHE B CD2 1 
ATOM   5789  C  CE1 . PHE B  1 273 ? -45.328 6.695   -25.590 1.00 39.08  ?  304  PHE B CE1 1 
ATOM   5790  C  CE2 . PHE B  1 273 ? -47.344 6.976   -24.354 1.00 40.76  ?  304  PHE B CE2 1 
ATOM   5791  C  CZ  . PHE B  1 273 ? -45.975 6.950   -24.398 1.00 37.16  ?  304  PHE B CZ  1 
ATOM   5792  N  N   . ASP B  1 274 ? -49.923 3.653   -27.492 1.00 33.12  ?  305  ASP B N   1 
ATOM   5793  C  CA  . ASP B  1 274 ? -50.477 2.823   -26.427 1.00 34.10  ?  305  ASP B CA  1 
ATOM   5794  C  C   . ASP B  1 274 ? -50.185 1.346   -26.642 1.00 29.03  ?  305  ASP B C   1 
ATOM   5795  O  O   . ASP B  1 274 ? -50.040 0.599   -25.673 1.00 32.62  ?  305  ASP B O   1 
ATOM   5796  C  CB  . ASP B  1 274 ? -51.992 3.058   -26.322 1.00 36.85  ?  305  ASP B CB  1 
ATOM   5797  C  CG  . ASP B  1 274 ? -52.500 2.915   -24.905 1.00 50.25  ?  305  ASP B CG  1 
ATOM   5798  O  OD1 . ASP B  1 274 ? -52.388 3.897   -24.128 1.00 55.50  -1 305  ASP B OD1 1 
ATOM   5799  O  OD2 . ASP B  1 274 ? -53.022 1.826   -24.576 1.00 50.03  ?  305  ASP B OD2 1 
ATOM   5800  N  N   . ASN B  1 275 ? -50.105 0.907   -27.888 1.00 28.24  ?  306  ASN B N   1 
ATOM   5801  C  CA  . ASN B  1 275 ? -49.830 -0.484  -28.238 1.00 29.89  ?  306  ASN B CA  1 
ATOM   5802  C  C   . ASN B  1 275 ? -48.467 -0.628  -28.926 1.00 31.83  ?  306  ASN B C   1 
ATOM   5803  O  O   . ASN B  1 275 ? -48.285 -1.419  -29.863 1.00 30.47  ?  306  ASN B O   1 
ATOM   5804  C  CB  . ASN B  1 275 ? -50.943 -1.046  -29.124 1.00 35.11  ?  306  ASN B CB  1 
ATOM   5805  C  CG  . ASN B  1 275 ? -50.937 -2.550  -29.152 1.00 35.41  ?  306  ASN B CG  1 
ATOM   5806  O  OD1 . ASN B  1 275 ? -50.506 -3.181  -28.196 1.00 34.72  ?  306  ASN B OD1 1 
ATOM   5807  N  ND2 . ASN B  1 275 ? -51.387 -3.136  -30.254 1.00 37.95  ?  306  ASN B ND2 1 
ATOM   5808  N  N   . THR B  1 276 ? -47.490 0.145   -28.462 1.00 31.64  ?  307  THR B N   1 
ATOM   5809  C  CA  . THR B  1 276 ? -46.093 -0.065  -28.815 1.00 29.76  ?  307  THR B CA  1 
ATOM   5810  C  C   . THR B  1 276 ? -45.363 -0.484  -27.550 1.00 28.20  ?  307  THR B C   1 
ATOM   5811  O  O   . THR B  1 276 ? -45.522 0.153   -26.504 1.00 27.89  ?  307  THR B O   1 
ATOM   5812  C  CB  . THR B  1 276 ? -45.469 1.207   -29.399 1.00 30.86  ?  307  THR B CB  1 
ATOM   5813  O  OG1 . THR B  1 276 ? -46.089 1.508   -30.656 1.00 32.31  ?  307  THR B OG1 1 
ATOM   5814  C  CG2 . THR B  1 276 ? -43.961 1.023   -29.639 1.00 26.98  ?  307  THR B CG2 1 
ATOM   5815  N  N   . LEU B  1 277 ? -44.620 -1.582  -27.630 1.00 29.41  ?  308  LEU B N   1 
ATOM   5816  C  CA  . LEU B  1 277 ? -43.708 -1.972  -26.561 1.00 27.98  ?  308  LEU B CA  1 
ATOM   5817  C  C   . LEU B  1 277 ? -42.355 -1.346  -26.871 1.00 30.00  ?  308  LEU B C   1 
ATOM   5818  O  O   . LEU B  1 277 ? -41.758 -1.639  -27.916 1.00 28.80  ?  308  LEU B O   1 
ATOM   5819  C  CB  . LEU B  1 277 ? -43.571 -3.493  -26.454 1.00 27.36  ?  308  LEU B CB  1 
ATOM   5820  C  CG  . LEU B  1 277 ? -42.296 -3.935  -25.680 1.00 28.39  ?  308  LEU B CG  1 
ATOM   5821  C  CD1 . LEU B  1 277 ? -42.404 -3.571  -24.212 1.00 26.53  ?  308  LEU B CD1 1 
ATOM   5822  C  CD2 . LEU B  1 277 ? -42.059 -5.420  -25.858 1.00 29.94  ?  308  LEU B CD2 1 
ATOM   5823  N  N   . ILE B  1 278 ? -41.888 -0.470  -25.989 1.00 30.23  ?  309  ILE B N   1 
ATOM   5824  C  CA  . ILE B  1 278 ? -40.583 0.156   -26.132 1.00 29.31  ?  309  ILE B CA  1 
ATOM   5825  C  C   . ILE B  1 278 ? -39.639 -0.522  -25.148 1.00 25.35  ?  309  ILE B C   1 
ATOM   5826  O  O   . ILE B  1 278 ? -39.965 -0.657  -23.960 1.00 26.47  ?  309  ILE B O   1 
ATOM   5827  C  CB  . ILE B  1 278 ? -40.647 1.671   -25.886 1.00 26.99  ?  309  ILE B CB  1 
ATOM   5828  C  CG1 . ILE B  1 278 ? -41.567 2.341   -26.898 1.00 26.69  ?  309  ILE B CG1 1 
ATOM   5829  C  CG2 . ILE B  1 278 ? -39.228 2.295   -26.003 1.00 24.85  ?  309  ILE B CG2 1 
ATOM   5830  C  CD1 . ILE B  1 278 ? -41.724 3.816   -26.689 1.00 26.72  ?  309  ILE B CD1 1 
ATOM   5831  N  N   . VAL B  1 279 ? -38.508 -1.007  -25.657 1.00 24.55  ?  310  VAL B N   1 
ATOM   5832  C  CA  . VAL B  1 279 ? -37.470 -1.640  -24.846 1.00 25.16  ?  310  VAL B CA  1 
ATOM   5833  C  C   . VAL B  1 279 ? -36.221 -0.810  -25.036 1.00 25.85  ?  310  VAL B C   1 
ATOM   5834  O  O   . VAL B  1 279 ? -35.767 -0.625  -26.173 1.00 26.57  ?  310  VAL B O   1 
ATOM   5835  C  CB  . VAL B  1 279 ? -37.205 -3.101  -25.246 1.00 27.17  ?  310  VAL B CB  1 
ATOM   5836  C  CG1 . VAL B  1 279 ? -36.104 -3.689  -24.352 1.00 22.51  ?  310  VAL B CG1 1 
ATOM   5837  C  CG2 . VAL B  1 279 ? -38.494 -3.941  -25.150 1.00 25.72  ?  310  VAL B CG2 1 
ATOM   5838  N  N   . PHE B  1 280 ? -35.681 -0.300  -23.937 1.00 26.49  ?  311  PHE B N   1 
ATOM   5839  C  CA  . PHE B  1 280 ? -34.479 0.519   -23.968 1.00 23.72  ?  311  PHE B CA  1 
ATOM   5840  C  C   . PHE B  1 280 ? -33.401 -0.225  -23.193 1.00 24.86  ?  311  PHE B C   1 
ATOM   5841  O  O   . PHE B  1 280 ? -33.671 -0.720  -22.095 1.00 22.11  ?  311  PHE B O   1 
ATOM   5842  C  CB  . PHE B  1 280 ? -34.757 1.902   -23.351 1.00 23.89  ?  311  PHE B CB  1 
ATOM   5843  C  CG  . PHE B  1 280 ? -33.511 2.724   -23.142 1.00 26.35  ?  311  PHE B CG  1 
ATOM   5844  C  CD1 . PHE B  1 280 ? -32.960 3.458   -24.202 1.00 23.33  ?  311  PHE B CD1 1 
ATOM   5845  C  CD2 . PHE B  1 280 ? -32.886 2.744   -21.897 1.00 24.76  ?  311  PHE B CD2 1 
ATOM   5846  C  CE1 . PHE B  1 280 ? -31.790 4.199   -24.007 1.00 28.31  ?  311  PHE B CE1 1 
ATOM   5847  C  CE2 . PHE B  1 280 ? -31.687 3.471   -21.679 1.00 27.08  ?  311  PHE B CE2 1 
ATOM   5848  C  CZ  . PHE B  1 280 ? -31.147 4.206   -22.723 1.00 23.28  ?  311  PHE B CZ  1 
ATOM   5849  N  N   . LEU B  1 281 ? -32.192 -0.323  -23.760 1.00 23.46  ?  312  LEU B N   1 
ATOM   5850  C  CA  . LEU B  1 281 ? -31.082 -0.916  -23.017 1.00 22.80  ?  312  LEU B CA  1 
ATOM   5851  C  C   . LEU B  1 281 ? -29.763 -0.497  -23.661 1.00 24.45  ?  312  LEU B C   1 
ATOM   5852  O  O   . LEU B  1 281 ? -29.736 0.206   -24.679 1.00 25.55  ?  312  LEU B O   1 
ATOM   5853  C  CB  . LEU B  1 281 ? -31.230 -2.439  -22.955 1.00 20.69  ?  312  LEU B CB  1 
ATOM   5854  C  CG  . LEU B  1 281 ? -30.950 -3.226  -24.247 1.00 21.96  ?  312  LEU B CG  1 
ATOM   5855  C  CD1 . LEU B  1 281 ? -30.732 -4.681  -23.883 1.00 26.79  ?  312  LEU B CD1 1 
ATOM   5856  C  CD2 . LEU B  1 281 ? -32.032 -3.078  -25.353 1.00 24.86  ?  312  LEU B CD2 1 
ATOM   5857  N  N   . SER B  1 282 ? -28.662 -0.933  -23.045 1.00 23.35  ?  313  SER B N   1 
ATOM   5858  C  CA  . SER B  1 282 ? -27.321 -0.752  -23.570 1.00 21.35  ?  313  SER B CA  1 
ATOM   5859  C  C   . SER B  1 282 ? -26.822 -2.105  -24.057 1.00 21.74  ?  313  SER B C   1 
ATOM   5860  O  O   . SER B  1 282 ? -27.254 -3.145  -23.554 1.00 22.73  ?  313  SER B O   1 
ATOM   5861  C  CB  . SER B  1 282 ? -26.372 -0.206  -22.489 1.00 23.17  ?  313  SER B CB  1 
ATOM   5862  O  OG  . SER B  1 282 ? -25.124 0.095   -23.074 1.00 24.14  ?  313  SER B OG  1 
ATOM   5863  N  N   . ASP B  1 283 ? -25.928 -2.080  -25.047 1.00 23.17  ?  314  ASP B N   1 
ATOM   5864  C  CA  . ASP B  1 283 ? -25.369 -3.352  -25.579 1.00 21.35  ?  314  ASP B CA  1 
ATOM   5865  C  C   . ASP B  1 283 ? -24.380 -3.968  -24.572 1.00 23.98  ?  314  ASP B C   1 
ATOM   5866  O  O   . ASP B  1 283 ? -24.157 -5.181  -24.645 1.00 24.50  ?  314  ASP B O   1 
ATOM   5867  C  CB  . ASP B  1 283 ? -24.757 -3.167  -26.956 1.00 25.19  ?  314  ASP B CB  1 
ATOM   5868  C  CG  . ASP B  1 283 ? -23.494 -2.331  -27.030 1.00 27.92  ?  314  ASP B CG  1 
ATOM   5869  O  OD1 . ASP B  1 283 ? -23.299 -1.480  -26.143 1.00 26.12  ?  314  ASP B OD1 1 
ATOM   5870  O  OD2 . ASP B  1 283 ? -22.736 -2.536  -27.996 1.00 28.16  -1 314  ASP B OD2 1 
ATOM   5871  N  N   . ASN B  1 284 ? -23.799 -3.149  -23.681 1.00 21.95  ?  315  ASN B N   1 
ATOM   5872  C  CA  . ASN B  1 284 ? -22.823 -3.648  -22.670 1.00 20.58  ?  315  ASN B CA  1 
ATOM   5873  C  C   . ASN B  1 284 ? -22.526 -2.523  -21.673 1.00 23.85  ?  315  ASN B C   1 
ATOM   5874  O  O   . ASN B  1 284 ? -23.043 -1.401  -21.868 1.00 23.41  ?  315  ASN B O   1 
ATOM   5875  C  CB  . ASN B  1 284 ? -21.555 -4.192  -23.319 1.00 21.62  ?  315  ASN B CB  1 
ATOM   5876  C  CG  . ASN B  1 284 ? -20.967 -3.222  -24.323 1.00 24.99  ?  315  ASN B CG  1 
ATOM   5877  O  OD1 . ASN B  1 284 ? -20.918 -3.512  -25.523 1.00 27.72  ?  315  ASN B OD1 1 
ATOM   5878  N  ND2 . ASN B  1 284 ? -20.517 -2.066  -23.862 1.00 23.90  ?  315  ASN B ND2 1 
ATOM   5879  N  N   . GLY B  1 285 ? -21.673 -2.787  -20.684 1.00 21.95  ?  316  GLY B N   1 
ATOM   5880  C  CA  . GLY B  1 285 ? -21.425 -1.793  -19.664 1.00 22.60  ?  316  GLY B CA  1 
ATOM   5881  C  C   . GLY B  1 285 ? -20.645 -0.618  -20.215 1.00 22.26  ?  316  GLY B C   1 
ATOM   5882  O  O   . GLY B  1 285 ? -20.077 -0.683  -21.307 1.00 21.64  ?  316  GLY B O   1 
ATOM   5883  N  N   . GLY B  1 286 ? -20.635 0.477   -19.450 1.00 18.76  ?  317  GLY B N   1 
ATOM   5884  C  CA  . GLY B  1 286 ? -19.889 1.648   -19.856 1.00 17.27  ?  317  GLY B CA  1 
ATOM   5885  C  C   . GLY B  1 286 ? -18.385 1.409   -19.810 1.00 19.14  ?  317  GLY B C   1 
ATOM   5886  O  O   . GLY B  1 286 ? -17.886 0.613   -19.030 1.00 22.45  ?  317  GLY B O   1 
ATOM   5887  N  N   . ASN B  1 287 ? -17.648 2.127   -20.658 1.00 20.03  ?  318  ASN B N   1 
ATOM   5888  C  CA  . ASN B  1 287 ? -16.185 2.142   -20.601 1.00 22.17  ?  318  ASN B CA  1 
ATOM   5889  C  C   . ASN B  1 287 ? -15.779 3.313   -19.718 1.00 21.72  ?  318  ASN B C   1 
ATOM   5890  O  O   . ASN B  1 287 ? -15.843 4.463   -20.156 1.00 21.67  ?  318  ASN B O   1 
ATOM   5891  C  CB  . ASN B  1 287 ? -15.590 2.302   -22.002 1.00 21.92  ?  318  ASN B CB  1 
ATOM   5892  C  CG  . ASN B  1 287 ? -14.082 2.177   -22.022 1.00 25.44  ?  318  ASN B CG  1 
ATOM   5893  O  OD1 . ASN B  1 287 ? -13.412 2.470   -21.028 1.00 25.76  ?  318  ASN B OD1 1 
ATOM   5894  N  ND2 . ASN B  1 287 ? -13.537 1.721   -23.152 1.00 25.37  ?  318  ASN B ND2 1 
ATOM   5895  N  N   . PHE B  1 288 ? -15.302 3.033   -18.505 1.00 21.59  ?  319  PHE B N   1 
ATOM   5896  C  CA  . PHE B  1 288 ? -15.045 4.169   -17.631 1.00 23.44  ?  319  PHE B CA  1 
ATOM   5897  C  C   . PHE B  1 288 ? -13.759 4.910   -17.988 1.00 24.57  ?  319  PHE B C   1 
ATOM   5898  O  O   . PHE B  1 288 ? -13.417 5.884   -17.319 1.00 26.74  ?  319  PHE B O   1 
ATOM   5899  C  CB  . PHE B  1 288 ? -15.102 3.747   -16.150 1.00 22.35  ?  319  PHE B CB  1 
ATOM   5900  C  CG  . PHE B  1 288 ? -14.162 2.628   -15.726 1.00 24.70  ?  319  PHE B CG  1 
ATOM   5901  C  CD1 . PHE B  1 288 ? -12.951 2.371   -16.373 1.00 22.24  ?  319  PHE B CD1 1 
ATOM   5902  C  CD2 . PHE B  1 288 ? -14.503 1.853   -14.606 1.00 24.49  ?  319  PHE B CD2 1 
ATOM   5903  C  CE1 . PHE B  1 288 ? -12.081 1.337   -15.906 1.00 23.69  ?  319  PHE B CE1 1 
ATOM   5904  C  CE2 . PHE B  1 288 ? -13.646 0.816   -14.130 1.00 26.32  ?  319  PHE B CE2 1 
ATOM   5905  C  CZ  . PHE B  1 288 ? -12.438 0.559   -14.787 1.00 23.46  ?  319  PHE B CZ  1 
ATOM   5906  N  N   . ASN B  1 289 ? -13.070 4.509   -19.052 1.00 23.59  ?  320  ASN B N   1 
ATOM   5907  C  CA  . ASN B  1 289 ? -12.009 5.331   -19.616 1.00 22.96  ?  320  ASN B CA  1 
ATOM   5908  C  C   . ASN B  1 289 ? -12.509 6.463   -20.496 1.00 24.85  ?  320  ASN B C   1 
ATOM   5909  O  O   . ASN B  1 289 ? -11.747 7.395   -20.767 1.00 24.91  ?  320  ASN B O   1 
ATOM   5910  C  CB  . ASN B  1 289 ? -11.057 4.461   -20.428 1.00 25.51  ?  320  ASN B CB  1 
ATOM   5911  C  CG  . ASN B  1 289 ? -10.294 3.506   -19.550 1.00 28.42  ?  320  ASN B CG  1 
ATOM   5912  O  OD1 . ASN B  1 289 ? -9.889  3.872   -18.448 1.00 28.19  ?  320  ASN B OD1 1 
ATOM   5913  N  ND2 . ASN B  1 289 ? -10.138 2.275   -19.998 1.00 31.50  ?  320  ASN B ND2 1 
ATOM   5914  N  N   . HIS B  1 290 ? -13.753 6.407   -20.968 1.00 25.91  ?  321  HIS B N   1 
ATOM   5915  C  CA  . HIS B  1 290 ? -14.256 7.382   -21.939 1.00 23.55  ?  321  HIS B CA  1 
ATOM   5916  C  C   . HIS B  1 290 ? -15.603 7.942   -21.497 1.00 26.07  ?  321  HIS B C   1 
ATOM   5917  O  O   . HIS B  1 290 ? -16.578 7.947   -22.249 1.00 27.42  ?  321  HIS B O   1 
ATOM   5918  C  CB  . HIS B  1 290 ? -14.335 6.733   -23.311 1.00 25.43  ?  321  HIS B CB  1 
ATOM   5919  C  CG  . HIS B  1 290 ? -13.013 6.232   -23.798 1.00 28.35  ?  321  HIS B CG  1 
ATOM   5920  N  ND1 . HIS B  1 290 ? -11.982 7.082   -24.137 1.00 28.56  ?  321  HIS B ND1 1 
ATOM   5921  C  CD2 . HIS B  1 290 ? -12.534 4.977   -23.949 1.00 29.15  ?  321  HIS B CD2 1 
ATOM   5922  C  CE1 . HIS B  1 290 ? -10.935 6.369   -24.512 1.00 33.08  ?  321  HIS B CE1 1 
ATOM   5923  N  NE2 . HIS B  1 290 ? -11.240 5.089   -24.402 1.00 31.16  ?  321  HIS B NE2 1 
ATOM   5924  N  N   . GLY B  1 291 ? -15.665 8.411   -20.254 1.00 21.99  ?  322  GLY B N   1 
ATOM   5925  C  CA  . GLY B  1 291 ? -16.757 9.228   -19.782 1.00 24.86  ?  322  GLY B CA  1 
ATOM   5926  C  C   . GLY B  1 291 ? -17.854 8.495   -19.034 1.00 22.27  ?  322  GLY B C   1 
ATOM   5927  O  O   . GLY B  1 291 ? -18.648 9.154   -18.357 1.00 25.53  ?  322  GLY B O   1 
ATOM   5928  N  N   . ALA B  1 292 ? -17.896 7.165   -19.092 1.00 22.58  ?  323  ALA B N   1 
ATOM   5929  C  CA  . ALA B  1 292 ? -19.009 6.422   -18.505 1.00 25.62  ?  323  ALA B CA  1 
ATOM   5930  C  C   . ALA B  1 292 ? -18.827 6.178   -17.003 1.00 25.98  ?  323  ALA B C   1 
ATOM   5931  O  O   . ALA B  1 292 ? -17.716 6.194   -16.459 1.00 22.70  ?  323  ALA B O   1 
ATOM   5932  C  CB  . ALA B  1 292 ? -19.200 5.086   -19.231 1.00 22.93  ?  323  ALA B CB  1 
ATOM   5933  N  N   . ASN B  1 293 ? -19.955 5.908   -16.339 1.00 25.75  ?  324  ASN B N   1 
ATOM   5934  C  CA  . ASN B  1 293 ? -19.996 5.627   -14.908 1.00 25.96  ?  324  ASN B CA  1 
ATOM   5935  C  C   . ASN B  1 293 ? -20.927 4.435   -14.668 1.00 23.28  ?  324  ASN B C   1 
ATOM   5936  O  O   . ASN B  1 293 ? -22.111 4.501   -14.988 1.00 22.94  ?  324  ASN B O   1 
ATOM   5937  C  CB  . ASN B  1 293 ? -20.467 6.875   -14.131 1.00 27.28  ?  324  ASN B CB  1 
ATOM   5938  C  CG  . ASN B  1 293 ? -20.234 6.766   -12.600 1.00 31.53  ?  324  ASN B CG  1 
ATOM   5939  O  OD1 . ASN B  1 293 ? -20.340 5.690   -12.017 1.00 27.85  ?  324  ASN B OD1 1 
ATOM   5940  N  ND2 . ASN B  1 293 ? -19.912 7.892   -11.962 1.00 32.91  ?  324  ASN B ND2 1 
ATOM   5941  N  N   . ASN B  1 294 ? -20.408 3.351   -14.091 1.00 22.86  ?  325  ASN B N   1 
ATOM   5942  C  CA  . ASN B  1 294 ? -21.204 2.148   -13.848 1.00 23.55  ?  325  ASN B CA  1 
ATOM   5943  C  C   . ASN B  1 294 ? -21.607 1.979   -12.379 1.00 23.69  ?  325  ASN B C   1 
ATOM   5944  O  O   . ASN B  1 294 ? -22.006 0.875   -11.982 1.00 23.28  ?  325  ASN B O   1 
ATOM   5945  C  CB  . ASN B  1 294 ? -20.465 0.887   -14.333 1.00 20.74  ?  325  ASN B CB  1 
ATOM   5946  C  CG  . ASN B  1 294 ? -20.173 0.902   -15.851 1.00 22.57  ?  325  ASN B CG  1 
ATOM   5947  O  OD1 . ASN B  1 294 ? -21.037 1.259   -16.664 1.00 21.95  ?  325  ASN B OD1 1 
ATOM   5948  N  ND2 . ASN B  1 294 ? -18.935 0.517   -16.232 1.00 20.35  ?  325  ASN B ND2 1 
ATOM   5949  N  N   . TYR B  1 295 ? -21.560 3.050   -11.582 1.00 21.99  ?  326  TYR B N   1 
ATOM   5950  C  CA  . TYR B  1 295 ? -21.909 2.947   -10.169 1.00 26.88  ?  326  TYR B CA  1 
ATOM   5951  C  C   . TYR B  1 295 ? -23.290 2.302   -10.016 1.00 23.43  ?  326  TYR B C   1 
ATOM   5952  O  O   . TYR B  1 295 ? -24.206 2.627   -10.779 1.00 24.09  ?  326  TYR B O   1 
ATOM   5953  C  CB  . TYR B  1 295 ? -21.897 4.339   -9.529  1.00 28.52  ?  326  TYR B CB  1 
ATOM   5954  C  CG  . TYR B  1 295 ? -22.173 4.334   -8.042  1.00 28.28  ?  326  TYR B CG  1 
ATOM   5955  C  CD1 . TYR B  1 295 ? -21.142 4.156   -7.124  1.00 33.76  ?  326  TYR B CD1 1 
ATOM   5956  C  CD2 . TYR B  1 295 ? -23.469 4.470   -7.558  1.00 30.92  ?  326  TYR B CD2 1 
ATOM   5957  C  CE1 . TYR B  1 295 ? -21.391 4.137   -5.763  1.00 31.37  ?  326  TYR B CE1 1 
ATOM   5958  C  CE2 . TYR B  1 295 ? -23.723 4.450   -6.200  1.00 34.21  ?  326  TYR B CE2 1 
ATOM   5959  C  CZ  . TYR B  1 295 ? -22.683 4.290   -5.318  1.00 35.86  ?  326  TYR B CZ  1 
ATOM   5960  O  OH  . TYR B  1 295 ? -22.949 4.265   -3.981  1.00 46.49  ?  326  TYR B OH  1 
ATOM   5961  N  N   . PRO B  1 296 ? -23.490 1.392   -9.038  1.00 24.52  ?  327  PRO B N   1 
ATOM   5962  C  CA  . PRO B  1 296 ? -22.548 0.928   -7.989  1.00 24.94  ?  327  PRO B CA  1 
ATOM   5963  C  C   . PRO B  1 296 ? -21.821 -0.354  -8.356  1.00 22.87  ?  327  PRO B C   1 
ATOM   5964  O  O   . PRO B  1 296 ? -21.323 -1.060  -7.476  1.00 23.33  ?  327  PRO B O   1 
ATOM   5965  C  CB  . PRO B  1 296 ? -23.474 0.666   -6.791  1.00 23.58  ?  327  PRO B CB  1 
ATOM   5966  C  CG  . PRO B  1 296 ? -24.734 0.109   -7.474  1.00 24.31  ?  327  PRO B CG  1 
ATOM   5967  C  CD  . PRO B  1 296 ? -24.849 0.868   -8.809  1.00 22.92  ?  327  PRO B CD  1 
ATOM   5968  N  N   . LEU B  1 297 ? -21.780 -0.686  -9.636  1.00 21.93  ?  328  LEU B N   1 
ATOM   5969  C  CA  . LEU B  1 297 ? -21.170 -1.922  -10.080 1.00 20.71  ?  328  LEU B CA  1 
ATOM   5970  C  C   . LEU B  1 297 ? -19.656 -1.777  -10.182 1.00 24.09  ?  328  LEU B C   1 
ATOM   5971  O  O   . LEU B  1 297 ? -19.131 -0.695  -10.485 1.00 23.74  ?  328  LEU B O   1 
ATOM   5972  C  CB  . LEU B  1 297 ? -21.719 -2.325  -11.445 1.00 21.59  ?  328  LEU B CB  1 
ATOM   5973  C  CG  . LEU B  1 297 ? -23.229 -2.255  -11.621 1.00 22.49  ?  328  LEU B CG  1 
ATOM   5974  C  CD1 . LEU B  1 297 ? -23.573 -2.695  -13.036 1.00 21.11  ?  328  LEU B CD1 1 
ATOM   5975  C  CD2 . LEU B  1 297 ? -23.937 -3.172  -10.579 1.00 20.54  ?  328  LEU B CD2 1 
ATOM   5976  N  N   . LYS B  1 298 ? -18.960 -2.896  -9.958  1.00 22.64  ?  329  LYS B N   1 
ATOM   5977  C  CA  . LYS B  1 298 ? -17.508 -2.975  -10.170 1.00 22.53  ?  329  LYS B CA  1 
ATOM   5978  C  C   . LYS B  1 298 ? -17.214 -3.155  -11.658 1.00 23.32  ?  329  LYS B C   1 
ATOM   5979  O  O   . LYS B  1 298 ? -17.955 -3.836  -12.375 1.00 24.48  ?  329  LYS B O   1 
ATOM   5980  C  CB  . LYS B  1 298 ? -16.923 -4.159  -9.393  1.00 21.93  ?  329  LYS B CB  1 
ATOM   5981  C  CG  . LYS B  1 298 ? -15.417 -4.374  -9.639  1.00 26.82  ?  329  LYS B CG  1 
ATOM   5982  C  CD  . LYS B  1 298 ? -14.852 -5.501  -8.757  1.00 28.68  ?  329  LYS B CD  1 
ATOM   5983  C  CE  . LYS B  1 298 ? -14.691 -5.078  -7.309  1.00 28.29  ?  329  LYS B CE  1 
ATOM   5984  N  NZ  . LYS B  1 298 ? -14.015 -6.173  -6.525  1.00 26.16  ?  329  LYS B NZ  1 
ATOM   5985  N  N   . GLY B  1 299 ? -16.174 -2.505  -12.139 1.00 22.35  ?  330  GLY B N   1 
ATOM   5986  C  CA  . GLY B  1 299 ? -15.630 -2.851  -13.440 1.00 23.27  ?  330  GLY B CA  1 
ATOM   5987  C  C   . GLY B  1 299 ? -16.156 -2.001  -14.588 1.00 23.52  ?  330  GLY B C   1 
ATOM   5988  O  O   . GLY B  1 299 ? -16.839 -0.990  -14.418 1.00 21.70  ?  330  GLY B O   1 
ATOM   5989  N  N   . THR B  1 300 ? -15.800 -2.436  -15.787 1.00 24.41  ?  331  THR B N   1 
ATOM   5990  C  CA  . THR B  1 300 ? -15.905 -1.636  -17.000 1.00 22.81  ?  331  THR B CA  1 
ATOM   5991  C  C   . THR B  1 300 ? -16.271 -2.560  -18.165 1.00 23.07  ?  331  THR B C   1 
ATOM   5992  O  O   . THR B  1 300 ? -16.245 -3.786  -18.041 1.00 21.87  ?  331  THR B O   1 
ATOM   5993  C  CB  . THR B  1 300 ? -14.582 -0.873  -17.240 1.00 23.63  ?  331  THR B CB  1 
ATOM   5994  O  OG1 . THR B  1 300 ? -14.721 0.071   -18.321 1.00 20.84  ?  331  THR B OG1 1 
ATOM   5995  C  CG2 . THR B  1 300 ? -13.425 -1.852  -17.541 1.00 23.42  ?  331  THR B CG2 1 
ATOM   5996  N  N   . LYS B  1 301 ? -16.613 -1.931  -19.291 1.00 23.62  ?  332  LYS B N   1 
ATOM   5997  C  CA  . LYS B  1 301 ? -16.905 -2.657  -20.548 1.00 22.96  ?  332  LYS B CA  1 
ATOM   5998  C  C   . LYS B  1 301 ? -15.881 -3.768  -20.744 1.00 23.32  ?  332  LYS B C   1 
ATOM   5999  O  O   . LYS B  1 301 ? -14.667 -3.521  -20.553 1.00 21.17  ?  332  LYS B O   1 
ATOM   6000  C  CB  . LYS B  1 301 ? -16.789 -1.740  -21.770 1.00 23.02  ?  332  LYS B CB  1 
ATOM   6001  C  CG  . LYS B  1 301 ? -16.873 -2.332  -23.164 1.00 21.29  ?  332  LYS B CG  1 
ATOM   6002  C  CD  . LYS B  1 301 ? -16.663 -1.258  -24.225 1.00 27.98  ?  332  LYS B CD  1 
ATOM   6003  C  CE  . LYS B  1 301 ? -16.673 -1.766  -25.628 1.00 22.86  ?  332  LYS B CE  1 
ATOM   6004  N  NZ  . LYS B  1 301 ? -16.374 -0.727  -26.616 1.00 23.88  ?  332  LYS B NZ  1 
ATOM   6005  N  N   . GLY B  1 302 ? -16.362 -4.924  -21.136 1.00 23.60  ?  333  GLY B N   1 
ATOM   6006  C  CA  . GLY B  1 302 ? -15.509 -6.071  -21.369 1.00 22.90  ?  333  GLY B CA  1 
ATOM   6007  C  C   . GLY B  1 302 ? -15.247 -6.962  -20.161 1.00 25.27  ?  333  GLY B C   1 
ATOM   6008  O  O   . GLY B  1 302 ? -14.791 -8.097  -20.352 1.00 22.42  ?  333  GLY B O   1 
ATOM   6009  N  N   . ASP B  1 303 ? -15.529 -6.500  -18.927 1.00 21.35  ?  334  ASP B N   1 
ATOM   6010  C  CA  . ASP B  1 303 ? -15.326 -7.324  -17.740 1.00 20.77  ?  334  ASP B CA  1 
ATOM   6011  C  C   . ASP B  1 303 ? -16.465 -8.323  -17.545 1.00 20.78  ?  334  ASP B C   1 
ATOM   6012  O  O   . ASP B  1 303 ? -17.567 -8.142  -18.056 1.00 22.59  ?  334  ASP B O   1 
ATOM   6013  C  CB  . ASP B  1 303 ? -15.239 -6.476  -16.462 1.00 24.34  ?  334  ASP B CB  1 
ATOM   6014  C  CG  . ASP B  1 303 ? -14.001 -5.574  -16.412 1.00 27.42  ?  334  ASP B CG  1 
ATOM   6015  O  OD1 . ASP B  1 303 ? -13.041 -5.794  -17.189 1.00 22.42  ?  334  ASP B OD1 1 
ATOM   6016  O  OD2 . ASP B  1 303 ? -14.007 -4.661  -15.549 1.00 24.66  -1 334  ASP B OD2 1 
ATOM   6017  N  N   . THR B  1 304 ? -16.207 -9.360  -16.743 1.00 22.42  ?  335  THR B N   1 
ATOM   6018  C  CA  . THR B  1 304 ? -17.288 -10.195 -16.215 1.00 20.57  ?  335  THR B CA  1 
ATOM   6019  C  C   . THR B  1 304 ? -17.651 -9.843  -14.772 1.00 22.56  ?  335  THR B C   1 
ATOM   6020  O  O   . THR B  1 304 ? -18.504 -10.519 -14.166 1.00 23.17  ?  335  THR B O   1 
ATOM   6021  C  CB  . THR B  1 304 ? -16.965 -11.694 -16.305 1.00 21.64  ?  335  THR B CB  1 
ATOM   6022  O  OG1 . THR B  1 304 ? -15.755 -11.966 -15.589 1.00 24.97  ?  335  THR B OG1 1 
ATOM   6023  C  CG2 . THR B  1 304 ? -16.815 -12.117 -17.742 1.00 20.22  ?  335  THR B CG2 1 
ATOM   6024  N  N   . TRP B  1 305 ? -17.054 -8.792  -14.220 1.00 22.90  ?  336  TRP B N   1 
ATOM   6025  C  CA  . TRP B  1 305 ? -17.725 -8.078  -13.146 1.00 22.91  ?  336  TRP B CA  1 
ATOM   6026  C  C   . TRP B  1 305 ? -19.074 -7.594  -13.666 1.00 22.15  ?  336  TRP B C   1 
ATOM   6027  O  O   . TRP B  1 305 ? -19.269 -7.471  -14.875 1.00 23.27  ?  336  TRP B O   1 
ATOM   6028  C  CB  . TRP B  1 305 ? -16.917 -6.871  -12.696 1.00 22.62  ?  336  TRP B CB  1 
ATOM   6029  C  CG  . TRP B  1 305 ? -15.505 -7.131  -12.190 1.00 24.20  ?  336  TRP B CG  1 
ATOM   6030  C  CD1 . TRP B  1 305 ? -14.340 -6.628  -12.718 1.00 22.79  ?  336  TRP B CD1 1 
ATOM   6031  C  CD2 . TRP B  1 305 ? -15.126 -7.887  -11.027 1.00 23.67  ?  336  TRP B CD2 1 
ATOM   6032  N  NE1 . TRP B  1 305 ? -13.266 -7.049  -11.972 1.00 23.74  ?  336  TRP B NE1 1 
ATOM   6033  C  CE2 . TRP B  1 305 ? -13.714 -7.818  -10.925 1.00 23.09  ?  336  TRP B CE2 1 
ATOM   6034  C  CE3 . TRP B  1 305 ? -15.842 -8.616  -10.067 1.00 23.81  ?  336  TRP B CE3 1 
ATOM   6035  C  CZ2 . TRP B  1 305 ? -12.991 -8.446  -9.889  1.00 27.86  ?  336  TRP B CZ2 1 
ATOM   6036  C  CZ3 . TRP B  1 305 ? -15.125 -9.241  -9.026  1.00 22.17  ?  336  TRP B CZ3 1 
ATOM   6037  C  CH2 . TRP B  1 305 ? -13.708 -9.158  -8.958  1.00 28.63  ?  336  TRP B CH2 1 
ATOM   6038  N  N   . GLU B  1 306 ? -20.000 -7.294  -12.738 1.00 21.41  ?  337  GLU B N   1 
ATOM   6039  C  CA  . GLU B  1 306 ? -21.341 -6.802  -13.118 1.00 23.49  ?  337  GLU B CA  1 
ATOM   6040  C  C   . GLU B  1 306 ? -21.230 -5.620  -14.076 1.00 21.64  ?  337  GLU B C   1 
ATOM   6041  O  O   . GLU B  1 306 ? -22.029 -5.471  -15.012 1.00 21.44  ?  337  GLU B O   1 
ATOM   6042  C  CB  . GLU B  1 306 ? -22.099 -6.365  -11.849 1.00 24.15  ?  337  GLU B CB  1 
ATOM   6043  C  CG  . GLU B  1 306 ? -22.546 -7.503  -10.895 1.00 23.96  ?  337  GLU B CG  1 
ATOM   6044  C  CD  . GLU B  1 306 ? -23.516 -8.494  -11.490 1.00 24.61  ?  337  GLU B CD  1 
ATOM   6045  O  OE1 . GLU B  1 306 ? -24.749 -8.232  -11.451 1.00 26.53  ?  337  GLU B OE1 1 
ATOM   6046  O  OE2 . GLU B  1 306 ? -23.046 -9.468  -12.107 1.00 27.18  -1 337  GLU B OE2 1 
ATOM   6047  N  N   . GLY B  1 307 ? -20.231 -4.761  -13.860 1.00 24.63  ?  338  GLY B N   1 
ATOM   6048  C  CA  . GLY B  1 307 ? -20.163 -3.548  -14.659 1.00 25.12  ?  338  GLY B CA  1 
ATOM   6049  C  C   . GLY B  1 307 ? -19.955 -3.791  -16.145 1.00 26.35  ?  338  GLY B C   1 
ATOM   6050  O  O   . GLY B  1 307 ? -20.173 -2.880  -16.946 1.00 21.89  ?  338  GLY B O   1 
ATOM   6051  N  N   . GLY B  1 308 ? -19.505 -4.991  -16.526 1.00 24.96  ?  339  GLY B N   1 
ATOM   6052  C  CA  . GLY B  1 308 ? -19.303 -5.281  -17.933 1.00 21.83  ?  339  GLY B CA  1 
ATOM   6053  C  C   . GLY B  1 308 ? -20.568 -5.612  -18.690 1.00 22.60  ?  339  GLY B C   1 
ATOM   6054  O  O   . GLY B  1 308 ? -20.660 -5.333  -19.894 1.00 24.23  ?  339  GLY B O   1 
ATOM   6055  N  N   . TYR B  1 309 ? -21.560 -6.209  -18.027 1.00 22.62  ?  340  TYR B N   1 
ATOM   6056  C  CA  . TYR B  1 309 ? -22.698 -6.721  -18.791 1.00 24.19  ?  340  TYR B CA  1 
ATOM   6057  C  C   . TYR B  1 309 ? -24.050 -6.600  -18.100 1.00 23.20  ?  340  TYR B C   1 
ATOM   6058  O  O   . TYR B  1 309 ? -25.052 -7.092  -18.641 1.00 23.22  ?  340  TYR B O   1 
ATOM   6059  C  CB  . TYR B  1 309 ? -22.466 -8.184  -19.218 1.00 22.83  ?  340  TYR B CB  1 
ATOM   6060  C  CG  . TYR B  1 309 ? -22.330 -9.229  -18.116 1.00 24.10  ?  340  TYR B CG  1 
ATOM   6061  C  CD1 . TYR B  1 309 ? -21.186 -9.290  -17.326 1.00 21.72  ?  340  TYR B CD1 1 
ATOM   6062  C  CD2 . TYR B  1 309 ? -23.317 -10.198 -17.919 1.00 22.19  ?  340  TYR B CD2 1 
ATOM   6063  C  CE1 . TYR B  1 309 ? -21.039 -10.258 -16.340 1.00 24.26  ?  340  TYR B CE1 1 
ATOM   6064  C  CE2 . TYR B  1 309 ? -23.182 -11.175 -16.937 1.00 22.93  ?  340  TYR B CE2 1 
ATOM   6065  C  CZ  . TYR B  1 309 ? -22.028 -11.195 -16.153 1.00 26.44  ?  340  TYR B CZ  1 
ATOM   6066  O  OH  . TYR B  1 309 ? -21.867 -12.159 -15.192 1.00 26.08  ?  340  TYR B OH  1 
ATOM   6067  N  N   . ARG B  1 310 ? -24.123 -5.947  -16.958 1.00 25.32  ?  341  ARG B N   1 
ATOM   6068  C  CA  . ARG B  1 310 ? -25.391 -5.560  -16.368 1.00 23.05  ?  341  ARG B CA  1 
ATOM   6069  C  C   . ARG B  1 310 ? -25.679 -4.136  -16.813 1.00 25.19  ?  341  ARG B C   1 
ATOM   6070  O  O   . ARG B  1 310 ? -24.821 -3.257  -16.653 1.00 25.88  ?  341  ARG B O   1 
ATOM   6071  C  CB  . ARG B  1 310 ? -25.310 -5.673  -14.848 1.00 23.71  ?  341  ARG B CB  1 
ATOM   6072  C  CG  . ARG B  1 310 ? -26.615 -5.493  -14.085 1.00 24.17  ?  341  ARG B CG  1 
ATOM   6073  C  CD  . ARG B  1 310 ? -26.352 -5.772  -12.601 1.00 24.51  ?  341  ARG B CD  1 
ATOM   6074  N  NE  . ARG B  1 310 ? -27.471 -5.403  -11.733 1.00 27.34  ?  341  ARG B NE  1 
ATOM   6075  C  CZ  . ARG B  1 310 ? -27.640 -5.850  -10.491 1.00 28.07  ?  341  ARG B CZ  1 
ATOM   6076  N  NH1 . ARG B  1 310 ? -26.820 -6.742  -9.955  1.00 22.69  ?  341  ARG B NH1 1 
ATOM   6077  N  NH2 . ARG B  1 310 ? -28.653 -5.379  -9.765  1.00 25.80  ?  341  ARG B NH2 1 
ATOM   6078  N  N   . VAL B  1 311 ? -26.858 -3.922  -17.403 1.00 18.94  ?  342  VAL B N   1 
ATOM   6079  C  CA  . VAL B  1 311 ? -27.145 -2.709  -18.173 1.00 21.39  ?  342  VAL B CA  1 
ATOM   6080  C  C   . VAL B  1 311 ? -28.484 -2.137  -17.720 1.00 20.83  ?  342  VAL B C   1 
ATOM   6081  O  O   . VAL B  1 311 ? -29.336 -2.858  -17.175 1.00 24.29  ?  342  VAL B O   1 
ATOM   6082  C  CB  . VAL B  1 311 ? -27.166 -2.999  -19.697 1.00 24.95  ?  342  VAL B CB  1 
ATOM   6083  C  CG1 . VAL B  1 311 ? -25.792 -3.576  -20.186 1.00 20.30  ?  342  VAL B CG1 1 
ATOM   6084  C  CG2 . VAL B  1 311 ? -28.306 -3.943  -20.047 1.00 25.35  ?  342  VAL B CG2 1 
ATOM   6085  N  N   . PRO B  1 312 ? -28.715 -0.844  -17.922 1.00 20.53  ?  343  PRO B N   1 
ATOM   6086  C  CA  . PRO B  1 312 ? -30.059 -0.323  -17.660 1.00 25.30  ?  343  PRO B CA  1 
ATOM   6087  C  C   . PRO B  1 312 ? -30.995 -0.880  -18.718 1.00 22.58  ?  343  PRO B C   1 
ATOM   6088  O  O   . PRO B  1 312 ? -30.570 -1.218  -19.825 1.00 23.13  ?  343  PRO B O   1 
ATOM   6089  C  CB  . PRO B  1 312 ? -29.903 1.201   -17.754 1.00 28.11  ?  343  PRO B CB  1 
ATOM   6090  C  CG  . PRO B  1 312 ? -28.524 1.445   -18.339 1.00 24.31  ?  343  PRO B CG  1 
ATOM   6091  C  CD  . PRO B  1 312 ? -27.727 0.211   -18.218 1.00 28.47  ?  343  PRO B CD  1 
ATOM   6092  N  N   . MET B  1 313 ? -32.250 -1.096  -18.325 1.00 20.76  ?  344  MET B N   1 
ATOM   6093  C  CA  . MET B  1 313 ? -33.287 -1.599  -19.230 1.00 20.80  ?  344  MET B CA  1 
ATOM   6094  C  C   . MET B  1 313 ? -34.635 -1.158  -18.685 1.00 22.97  ?  344  MET B C   1 
ATOM   6095  O  O   . MET B  1 313 ? -34.866 -1.261  -17.474 1.00 24.61  ?  344  MET B O   1 
ATOM   6096  C  CB  . MET B  1 313 ? -33.353 -3.125  -19.269 1.00 22.88  ?  344  MET B CB  1 
ATOM   6097  C  CG  . MET B  1 313 ? -34.448 -3.727  -20.201 1.00 26.24  ?  344  MET B CG  1 
ATOM   6098  S  SD  . MET B  1 313 ? -33.932 -5.128  -21.197 1.00 29.92  ?  344  MET B SD  1 
ATOM   6099  C  CE  . MET B  1 313 ? -34.408 -6.323  -19.926 1.00 25.10  ?  344  MET B CE  1 
ATOM   6100  N  N   . PHE B  1 314 ? -35.556 -0.776  -19.577 1.00 25.97  ?  345  PHE B N   1 
ATOM   6101  C  CA  . PHE B  1 314 ? -36.958 -0.674  -19.195 1.00 26.37  ?  345  PHE B CA  1 
ATOM   6102  C  C   . PHE B  1 314 ? -37.808 -1.228  -20.331 1.00 24.88  ?  345  PHE B C   1 
ATOM   6103  O  O   . PHE B  1 314 ? -37.373 -1.267  -21.483 1.00 24.45  ?  345  PHE B O   1 
ATOM   6104  C  CB  . PHE B  1 314 ? -37.393 0.773   -18.818 1.00 22.02  ?  345  PHE B CB  1 
ATOM   6105  C  CG  . PHE B  1 314 ? -37.403 1.775   -19.976 1.00 24.68  ?  345  PHE B CG  1 
ATOM   6106  C  CD1 . PHE B  1 314 ? -38.373 1.726   -20.981 1.00 25.60  ?  345  PHE B CD1 1 
ATOM   6107  C  CD2 . PHE B  1 314 ? -36.488 2.815   -20.000 1.00 26.32  ?  345  PHE B CD2 1 
ATOM   6108  C  CE1 . PHE B  1 314 ? -38.390 2.644   -22.015 1.00 24.98  ?  345  PHE B CE1 1 
ATOM   6109  C  CE2 . PHE B  1 314 ? -36.492 3.762   -21.023 1.00 22.93  ?  345  PHE B CE2 1 
ATOM   6110  C  CZ  . PHE B  1 314 ? -37.463 3.681   -22.032 1.00 25.17  ?  345  PHE B CZ  1 
ATOM   6111  N  N   . PHE B  1 315 ? -38.988 -1.723  -19.964 1.00 26.27  ?  346  PHE B N   1 
ATOM   6112  C  CA  . PHE B  1 315 ? -40.085 -2.034  -20.877 1.00 23.60  ?  346  PHE B CA  1 
ATOM   6113  C  C   . PHE B  1 315 ? -41.188 -0.998  -20.679 1.00 28.59  ?  346  PHE B C   1 
ATOM   6114  O  O   . PHE B  1 315 ? -41.604 -0.764  -19.542 1.00 26.46  ?  346  PHE B O   1 
ATOM   6115  C  CB  . PHE B  1 315 ? -40.689 -3.408  -20.570 1.00 26.63  ?  346  PHE B CB  1 
ATOM   6116  C  CG  . PHE B  1 315 ? -39.907 -4.581  -21.076 1.00 27.01  ?  346  PHE B CG  1 
ATOM   6117  C  CD1 . PHE B  1 315 ? -38.576 -4.469  -21.438 1.00 26.85  ?  346  PHE B CD1 1 
ATOM   6118  C  CD2 . PHE B  1 315 ? -40.516 -5.831  -21.132 1.00 26.40  ?  346  PHE B CD2 1 
ATOM   6119  C  CE1 . PHE B  1 315 ? -37.871 -5.568  -21.890 1.00 29.71  ?  346  PHE B CE1 1 
ATOM   6120  C  CE2 . PHE B  1 315 ? -39.824 -6.940  -21.582 1.00 33.98  ?  346  PHE B CE2 1 
ATOM   6121  C  CZ  . PHE B  1 315 ? -38.491 -6.821  -21.958 1.00 32.53  ?  346  PHE B CZ  1 
ATOM   6122  N  N   . HIS B  1 316 ? -41.704 -0.423  -21.775 1.00 27.58  ?  347  HIS B N   1 
ATOM   6123  C  CA  . HIS B  1 316 ? -42.788 0.555   -21.701 1.00 30.40  ?  347  HIS B CA  1 
ATOM   6124  C  C   . HIS B  1 316 ? -43.862 0.172   -22.721 1.00 28.59  ?  347  HIS B C   1 
ATOM   6125  O  O   . HIS B  1 316 ? -43.579 0.069   -23.919 1.00 29.90  ?  347  HIS B O   1 
ATOM   6126  C  CB  . HIS B  1 316 ? -42.265 1.976   -21.957 1.00 25.18  ?  347  HIS B CB  1 
ATOM   6127  C  CG  . HIS B  1 316 ? -43.341 3.022   -22.012 1.00 32.44  ?  347  HIS B CG  1 
ATOM   6128  N  ND1 . HIS B  1 316 ? -44.089 3.273   -23.150 1.00 31.14  ?  347  HIS B ND1 1 
ATOM   6129  C  CD2 . HIS B  1 316 ? -43.797 3.876   -21.065 1.00 30.00  ?  347  HIS B CD2 1 
ATOM   6130  C  CE1 . HIS B  1 316 ? -44.950 4.246   -22.899 1.00 30.73  ?  347  HIS B CE1 1 
ATOM   6131  N  NE2 . HIS B  1 316 ? -44.797 4.628   -21.641 1.00 28.85  ?  347  HIS B NE2 1 
ATOM   6132  N  N   . TRP B  1 317 ? -45.087 -0.039  -22.252 1.00 30.32  ?  348  TRP B N   1 
ATOM   6133  C  CA  . TRP B  1 317 ? -46.167 -0.545  -23.102 1.00 27.54  ?  348  TRP B CA  1 
ATOM   6134  C  C   . TRP B  1 317 ? -47.486 -0.260  -22.404 1.00 31.06  ?  348  TRP B C   1 
ATOM   6135  O  O   . TRP B  1 317 ? -47.955 -1.095  -21.619 1.00 28.75  ?  348  TRP B O   1 
ATOM   6136  C  CB  . TRP B  1 317 ? -45.997 -2.042  -23.347 1.00 28.31  ?  348  TRP B CB  1 
ATOM   6137  C  CG  . TRP B  1 317 ? -46.999 -2.678  -24.286 1.00 31.33  ?  348  TRP B CG  1 
ATOM   6138  C  CD1 . TRP B  1 317 ? -47.821 -2.050  -25.196 1.00 30.10  ?  348  TRP B CD1 1 
ATOM   6139  C  CD2 . TRP B  1 317 ? -47.264 -4.077  -24.408 1.00 28.68  ?  348  TRP B CD2 1 
ATOM   6140  N  NE1 . TRP B  1 317 ? -48.566 -2.990  -25.874 1.00 33.27  ?  348  TRP B NE1 1 
ATOM   6141  C  CE2 . TRP B  1 317 ? -48.257 -4.236  -25.392 1.00 30.47  ?  348  TRP B CE2 1 
ATOM   6142  C  CE3 . TRP B  1 317 ? -46.778 -5.216  -23.750 1.00 33.15  ?  348  TRP B CE3 1 
ATOM   6143  C  CZ2 . TRP B  1 317 ? -48.750 -5.486  -25.753 1.00 33.09  ?  348  TRP B CZ2 1 
ATOM   6144  C  CZ3 . TRP B  1 317 ? -47.269 -6.460  -24.113 1.00 35.62  ?  348  TRP B CZ3 1 
ATOM   6145  C  CH2 . TRP B  1 317 ? -48.240 -6.584  -25.104 1.00 34.84  ?  348  TRP B CH2 1 
ATOM   6146  N  N   . PRO B  1 318 ? -48.067 0.926   -22.626 1.00 29.44  ?  349  PRO B N   1 
ATOM   6147  C  CA  . PRO B  1 318 ? -49.189 1.382   -21.799 1.00 37.69  ?  349  PRO B CA  1 
ATOM   6148  C  C   . PRO B  1 318 ? -50.351 0.425   -21.747 1.00 33.29  ?  349  PRO B C   1 
ATOM   6149  O  O   . PRO B  1 318 ? -50.978 0.323   -20.697 1.00 35.66  ?  349  PRO B O   1 
ATOM   6150  C  CB  . PRO B  1 318 ? -49.578 2.710   -22.459 1.00 36.95  ?  349  PRO B CB  1 
ATOM   6151  C  CG  . PRO B  1 318 ? -48.244 3.229   -22.963 1.00 33.76  ?  349  PRO B CG  1 
ATOM   6152  C  CD  . PRO B  1 318 ? -47.566 1.998   -23.507 1.00 31.62  ?  349  PRO B CD  1 
ATOM   6153  N  N   . LYS B  1 319 ? -50.628 -0.304  -22.831 1.00 35.98  ?  350  LYS B N   1 
ATOM   6154  C  CA  . LYS B  1 319 ? -51.803 -1.173  -22.879 1.00 39.03  ?  350  LYS B CA  1 
ATOM   6155  C  C   . LYS B  1 319 ? -51.749 -2.239  -21.785 1.00 44.29  ?  350  LYS B C   1 
ATOM   6156  O  O   . LYS B  1 319 ? -52.786 -2.600  -21.211 1.00 38.41  ?  350  LYS B O   1 
ATOM   6157  C  CB  . LYS B  1 319 ? -51.902 -1.804  -24.272 1.00 33.60  ?  350  LYS B CB  1 
ATOM   6158  C  CG  . LYS B  1 319 ? -53.286 -2.379  -24.662 1.00 44.52  ?  350  LYS B CG  1 
ATOM   6159  C  CD  . LYS B  1 319 ? -53.175 -3.810  -25.200 1.00 47.61  ?  350  LYS B CD  1 
ATOM   6160  C  CE  . LYS B  1 319 ? -52.994 -3.869  -26.723 1.00 47.75  ?  350  LYS B CE  1 
ATOM   6161  N  NZ  . LYS B  1 319 ? -52.419 -5.187  -27.225 1.00 46.12  ?  350  LYS B NZ  1 
ATOM   6162  N  N   . LYS B  1 320 ? -50.540 -2.682  -21.411 1.00 35.89  ?  351  LYS B N   1 
ATOM   6163  C  CA  . LYS B  1 320 ? -50.422 -3.889  -20.609 1.00 31.08  ?  351  LYS B CA  1 
ATOM   6164  C  C   . LYS B  1 320 ? -49.518 -3.728  -19.399 1.00 35.08  ?  351  LYS B C   1 
ATOM   6165  O  O   . LYS B  1 320 ? -49.792 -4.324  -18.355 1.00 36.20  ?  351  LYS B O   1 
ATOM   6166  C  CB  . LYS B  1 320 ? -49.904 -5.037  -21.514 1.00 36.71  ?  351  LYS B CB  1 
ATOM   6167  C  CG  . LYS B  1 320 ? -50.941 -5.544  -22.532 1.00 45.23  ?  351  LYS B CG  1 
ATOM   6168  C  CD  . LYS B  1 320 ? -51.545 -6.900  -22.172 1.00 43.61  ?  351  LYS B CD  1 
ATOM   6169  C  CE  . LYS B  1 320 ? -52.183 -7.560  -23.391 1.00 50.73  ?  351  LYS B CE  1 
ATOM   6170  N  NZ  . LYS B  1 320 ? -51.481 -8.805  -23.852 1.00 58.43  ?  351  LYS B NZ  1 
ATOM   6171  N  N   . ILE B  1 321 ? -48.438 -2.956  -19.506 1.00 34.13  ?  352  ILE B N   1 
ATOM   6172  C  CA  . ILE B  1 321 ? -47.466 -2.848  -18.420 1.00 32.18  ?  352  ILE B CA  1 
ATOM   6173  C  C   . ILE B  1 321 ? -47.834 -1.656  -17.552 1.00 29.00  ?  352  ILE B C   1 
ATOM   6174  O  O   . ILE B  1 321 ? -47.936 -0.525  -18.043 1.00 29.59  ?  352  ILE B O   1 
ATOM   6175  C  CB  . ILE B  1 321 ? -46.031 -2.712  -18.952 1.00 30.77  ?  352  ILE B CB  1 
ATOM   6176  C  CG1 . ILE B  1 321 ? -45.641 -3.979  -19.724 1.00 32.25  ?  352  ILE B CG1 1 
ATOM   6177  C  CG2 . ILE B  1 321 ? -45.063 -2.420  -17.750 1.00 32.84  ?  352  ILE B CG2 1 
ATOM   6178  C  CD1 . ILE B  1 321 ? -44.259 -3.920  -20.438 1.00 32.39  ?  352  ILE B CD1 1 
ATOM   6179  N  N   . LYS B  1 322 ? -48.013 -1.911  -16.261 1.00 30.41  ?  353  LYS B N   1 
ATOM   6180  C  CA  . LYS B  1 322 ? -48.389 -0.864  -15.318 1.00 39.71  ?  353  LYS B CA  1 
ATOM   6181  C  C   . LYS B  1 322 ? -47.244 0.123   -15.102 1.00 37.39  ?  353  LYS B C   1 
ATOM   6182  O  O   . LYS B  1 322 ? -46.065 -0.202  -15.281 1.00 33.50  ?  353  LYS B O   1 
ATOM   6183  C  CB  . LYS B  1 322 ? -48.785 -1.473  -13.969 1.00 38.39  ?  353  LYS B CB  1 
ATOM   6184  N  N   . LYS B  1 323 ? -47.612 1.338   -14.682 1.00 33.05  ?  354  LYS B N   1 
ATOM   6185  C  CA  . LYS B  1 323 ? -46.640 2.379   -14.378 1.00 37.29  ?  354  LYS B CA  1 
ATOM   6186  C  C   . LYS B  1 323 ? -45.902 2.075   -13.080 1.00 35.44  ?  354  LYS B C   1 
ATOM   6187  O  O   . LYS B  1 323 ? -46.396 1.358   -12.209 1.00 32.43  ?  354  LYS B O   1 
ATOM   6188  C  CB  . LYS B  1 323 ? -47.315 3.743   -14.235 1.00 38.19  ?  354  LYS B CB  1 
ATOM   6189  C  CG  . LYS B  1 323 ? -48.189 4.154   -15.395 1.00 41.45  ?  354  LYS B CG  1 
ATOM   6190  C  CD  . LYS B  1 323 ? -49.172 5.237   -14.962 1.00 42.89  ?  354  LYS B CD  1 
ATOM   6191  C  CE  . LYS B  1 323 ? -49.347 6.265   -16.050 1.00 50.44  ?  354  LYS B CE  1 
ATOM   6192  N  NZ  . LYS B  1 323 ? -49.753 5.601   -17.315 1.00 45.97  ?  354  LYS B NZ  1 
ATOM   6193  N  N   . ASP B  1 324 ? -44.707 2.659   -12.956 1.00 34.09  ?  355  ASP B N   1 
ATOM   6194  C  CA  . ASP B  1 324 ? -43.932 2.674   -11.707 1.00 35.04  ?  355  ASP B CA  1 
ATOM   6195  C  C   . ASP B  1 324 ? -43.556 1.277   -11.224 1.00 33.75  ?  355  ASP B C   1 
ATOM   6196  O  O   . ASP B  1 324 ? -43.422 1.034   -10.019 1.00 38.01  ?  355  ASP B O   1 
ATOM   6197  C  CB  . ASP B  1 324 ? -44.667 3.426   -10.594 1.00 43.81  ?  355  ASP B CB  1 
ATOM   6198  C  CG  . ASP B  1 324 ? -44.984 4.863   -10.970 1.00 47.47  ?  355  ASP B CG  1 
ATOM   6199  O  OD1 . ASP B  1 324 ? -44.041 5.678   -11.138 1.00 55.50  -1 355  ASP B OD1 1 
ATOM   6200  O  OD2 . ASP B  1 324 ? -46.189 5.175   -11.099 1.00 55.44  ?  355  ASP B OD2 1 
ATOM   6201  N  N   . GLN B  1 325 ? -43.365 0.353   -12.147 1.00 34.02  ?  356  GLN B N   1 
ATOM   6202  C  CA  . GLN B  1 325 ? -42.975 -0.997  -11.795 1.00 32.77  ?  356  GLN B CA  1 
ATOM   6203  C  C   . GLN B  1 325 ? -41.456 -1.090  -11.782 1.00 35.91  ?  356  GLN B C   1 
ATOM   6204  O  O   . GLN B  1 325 ? -40.779 -0.440  -12.587 1.00 29.66  ?  356  GLN B O   1 
ATOM   6205  C  CB  . GLN B  1 325 ? -43.558 -2.000  -12.792 1.00 35.34  ?  356  GLN B CB  1 
ATOM   6206  C  CG  . GLN B  1 325 ? -42.760 -3.298  -12.884 1.00 39.55  ?  356  GLN B CG  1 
ATOM   6207  C  CD  . GLN B  1 325 ? -43.483 -4.402  -13.643 1.00 41.65  ?  356  GLN B CD  1 
ATOM   6208  O  OE1 . GLN B  1 325 ? -43.068 -5.572  -13.622 1.00 37.68  ?  356  GLN B OE1 1 
ATOM   6209  N  NE2 . GLN B  1 325 ? -44.582 -4.035  -14.318 1.00 44.46  ?  356  GLN B NE2 1 
ATOM   6210  N  N   . ARG B  1 326 ? -40.938 -1.855  -10.823 1.00 29.08  ?  357  ARG B N   1 
ATOM   6211  C  CA  . ARG B  1 326 ? -39.540 -2.248  -10.745 1.00 32.84  ?  357  ARG B CA  1 
ATOM   6212  C  C   . ARG B  1 326 ? -39.496 -3.767  -10.767 1.00 31.12  ?  357  ARG B C   1 
ATOM   6213  O  O   . ARG B  1 326 ? -40.054 -4.419  -9.879  1.00 34.88  ?  357  ARG B O   1 
ATOM   6214  C  CB  . ARG B  1 326 ? -38.901 -1.694  -9.469  1.00 29.34  ?  357  ARG B CB  1 
ATOM   6215  C  CG  . ARG B  1 326 ? -38.924 -0.178  -9.429  1.00 30.65  ?  357  ARG B CG  1 
ATOM   6216  C  CD  . ARG B  1 326 ? -38.233 0.372   -8.212  1.00 30.32  ?  357  ARG B CD  1 
ATOM   6217  N  NE  . ARG B  1 326 ? -36.780 0.290   -8.335  1.00 38.80  ?  357  ARG B NE  1 
ATOM   6218  C  CZ  . ARG B  1 326 ? -36.027 1.196   -8.948  1.00 41.02  ?  357  ARG B CZ  1 
ATOM   6219  N  NH1 . ARG B  1 326 ? -36.560 2.250   -9.548  1.00 39.95  ?  357  ARG B NH1 1 
ATOM   6220  N  NH2 . ARG B  1 326 ? -34.707 1.034   -8.973  1.00 40.11  ?  357  ARG B NH2 1 
ATOM   6221  N  N   . PHE B  1 327 ? -38.874 -4.331  -11.788 1.00 28.67  ?  358  PHE B N   1 
ATOM   6222  C  CA  . PHE B  1 327 ? -38.739 -5.781  -11.908 1.00 30.06  ?  358  PHE B CA  1 
ATOM   6223  C  C   . PHE B  1 327 ? -37.325 -6.149  -11.461 1.00 30.00  ?  358  PHE B C   1 
ATOM   6224  O  O   . PHE B  1 327 ? -36.354 -5.799  -12.133 1.00 28.41  ?  358  PHE B O   1 
ATOM   6225  C  CB  . PHE B  1 327 ? -39.010 -6.239  -13.336 1.00 27.71  ?  358  PHE B CB  1 
ATOM   6226  C  CG  . PHE B  1 327 ? -39.135 -7.729  -13.484 1.00 31.89  ?  358  PHE B CG  1 
ATOM   6227  C  CD1 . PHE B  1 327 ? -40.370 -8.371  -13.279 1.00 30.40  ?  358  PHE B CD1 1 
ATOM   6228  C  CD2 . PHE B  1 327 ? -38.032 -8.494  -13.855 1.00 28.06  ?  358  PHE B CD2 1 
ATOM   6229  C  CE1 . PHE B  1 327 ? -40.477 -9.757  -13.411 1.00 31.94  ?  358  PHE B CE1 1 
ATOM   6230  C  CE2 . PHE B  1 327 ? -38.124 -9.878  -13.979 1.00 30.17  ?  358  PHE B CE2 1 
ATOM   6231  C  CZ  . PHE B  1 327 ? -39.362 -10.513 -13.763 1.00 30.67  ?  358  PHE B CZ  1 
ATOM   6232  N  N   . ASP B  1 328 ? -37.222 -6.872  -10.340 1.00 23.82  ?  359  ASP B N   1 
ATOM   6233  C  CA  . ASP B  1 328 ? -35.955 -7.131  -9.663  1.00 28.73  ?  359  ASP B CA  1 
ATOM   6234  C  C   . ASP B  1 328 ? -35.401 -8.520  -9.931  1.00 28.06  ?  359  ASP B C   1 
ATOM   6235  O  O   . ASP B  1 328 ? -34.310 -8.833  -9.458  1.00 31.54  ?  359  ASP B O   1 
ATOM   6236  C  CB  . ASP B  1 328 ? -36.116 -6.967  -8.150  1.00 29.78  ?  359  ASP B CB  1 
ATOM   6237  C  CG  . ASP B  1 328 ? -36.405 -5.534  -7.727  1.00 34.66  ?  359  ASP B CG  1 
ATOM   6238  O  OD1 . ASP B  1 328 ? -36.035 -4.584  -8.440  1.00 31.13  ?  359  ASP B OD1 1 
ATOM   6239  O  OD2 . ASP B  1 328 ? -36.974 -5.353  -6.630  1.00 40.01  -1 359  ASP B OD2 1 
ATOM   6240  N  N   . PHE B  1 329 ? -36.131 -9.361  -10.622 1.00 29.89  ?  360  PHE B N   1 
ATOM   6241  C  CA  . PHE B  1 329 ? -35.574 -10.665 -10.930 1.00 28.29  ?  360  PHE B CA  1 
ATOM   6242  C  C   . PHE B  1 329 ? -34.637 -10.551 -12.128 1.00 28.36  ?  360  PHE B C   1 
ATOM   6243  O  O   . PHE B  1 329 ? -34.905 -9.778  -13.055 1.00 28.07  ?  360  PHE B O   1 
ATOM   6244  C  CB  . PHE B  1 329 ? -36.699 -11.652 -11.237 1.00 28.91  ?  360  PHE B CB  1 
ATOM   6245  C  CG  . PHE B  1 329 ? -37.575 -11.935 -10.050 1.00 32.08  ?  360  PHE B CG  1 
ATOM   6246  C  CD1 . PHE B  1 329 ? -37.033 -12.454 -8.881  1.00 33.21  ?  360  PHE B CD1 1 
ATOM   6247  C  CD2 . PHE B  1 329 ? -38.932 -11.682 -10.097 1.00 33.73  ?  360  PHE B CD2 1 
ATOM   6248  C  CE1 . PHE B  1 329 ? -37.833 -12.715 -7.767  1.00 38.55  ?  360  PHE B CE1 1 
ATOM   6249  C  CE2 . PHE B  1 329 ? -39.745 -11.956 -8.997  1.00 33.52  ?  360  PHE B CE2 1 
ATOM   6250  C  CZ  . PHE B  1 329 ? -39.201 -12.469 -7.837  1.00 35.24  ?  360  PHE B CZ  1 
ATOM   6251  N  N   . PRO B  1 330 ? -33.543 -11.299 -12.143 1.00 29.86  ?  361  PRO B N   1 
ATOM   6252  C  CA  . PRO B  1 330 ? -32.603 -11.177 -13.259 1.00 33.52  ?  361  PRO B CA  1 
ATOM   6253  C  C   . PRO B  1 330 ? -33.217 -11.641 -14.584 1.00 33.87  ?  361  PRO B C   1 
ATOM   6254  O  O   . PRO B  1 330 ? -33.974 -12.619 -14.643 1.00 29.63  ?  361  PRO B O   1 
ATOM   6255  C  CB  . PRO B  1 330 ? -31.420 -12.052 -12.816 1.00 29.39  ?  361  PRO B CB  1 
ATOM   6256  C  CG  . PRO B  1 330 ? -31.976 -12.995 -11.832 1.00 33.60  ?  361  PRO B CG  1 
ATOM   6257  C  CD  . PRO B  1 330 ? -33.062 -12.233 -11.111 1.00 30.36  ?  361  PRO B CD  1 
ATOM   6258  N  N   . VAL B  1 331 ? -32.912 -10.897 -15.655 1.00 28.70  ?  362  VAL B N   1 
ATOM   6259  C  CA  . VAL B  1 331 ? -33.342 -11.222 -17.014 1.00 28.78  ?  362  VAL B CA  1 
ATOM   6260  C  C   . VAL B  1 331 ? -32.158 -11.036 -17.954 1.00 28.20  ?  362  VAL B C   1 
ATOM   6261  O  O   . VAL B  1 331 ? -31.134 -10.464 -17.589 1.00 25.22  ?  362  VAL B O   1 
ATOM   6262  C  CB  . VAL B  1 331 ? -34.514 -10.348 -17.497 1.00 28.49  ?  362  VAL B CB  1 
ATOM   6263  C  CG1 . VAL B  1 331 ? -35.722 -10.546 -16.623 1.00 22.17  ?  362  VAL B CG1 1 
ATOM   6264  C  CG2 . VAL B  1 331 ? -34.082 -8.872  -17.505 1.00 27.53  ?  362  VAL B CG2 1 
ATOM   6265  N  N   . SER B  1 332 ? -32.327 -11.495 -19.190 1.00 26.78  ?  363  SER B N   1 
ATOM   6266  C  CA  . SER B  1 332 ? -31.266 -11.479 -20.190 1.00 26.17  ?  363  SER B CA  1 
ATOM   6267  C  C   . SER B  1 332 ? -31.756 -10.850 -21.486 1.00 30.14  ?  363  SER B C   1 
ATOM   6268  O  O   . SER B  1 332 ? -32.933 -10.965 -21.840 1.00 26.56  ?  363  SER B O   1 
ATOM   6269  C  CB  . SER B  1 332 ? -30.755 -12.895 -20.499 1.00 31.41  ?  363  SER B CB  1 
ATOM   6270  O  OG  . SER B  1 332 ? -29.946 -12.892 -21.672 1.00 27.05  ?  363  SER B OG  1 
ATOM   6271  N  N   . SER B  1 333 ? -30.825 -10.212 -22.215 1.00 27.03  ?  364  SER B N   1 
ATOM   6272  C  CA  . SER B  1 333 ? -31.160 -9.713  -23.543 1.00 27.77  ?  364  SER B CA  1 
ATOM   6273  C  C   . SER B  1 333 ? -31.500 -10.858 -24.481 1.00 25.61  ?  364  SER B C   1 
ATOM   6274  O  O   . SER B  1 333 ? -32.159 -10.634 -25.493 1.00 26.31  ?  364  SER B O   1 
ATOM   6275  C  CB  . SER B  1 333 ? -30.001 -8.904  -24.140 1.00 26.48  ?  364  SER B CB  1 
ATOM   6276  O  OG  . SER B  1 333 ? -28.812 -9.702  -24.229 1.00 23.76  ?  364  SER B OG  1 
ATOM   6277  N  N   . LEU B  1 334 ? -31.081 -12.082 -24.139 1.00 25.16  ?  365  LEU B N   1 
ATOM   6278  C  CA  . LEU B  1 334 ? -31.520 -13.276 -24.854 1.00 28.18  ?  365  LEU B CA  1 
ATOM   6279  C  C   . LEU B  1 334 ? -33.030 -13.453 -24.798 1.00 28.00  ?  365  LEU B C   1 
ATOM   6280  O  O   . LEU B  1 334 ? -33.603 -14.131 -25.665 1.00 29.95  ?  365  LEU B O   1 
ATOM   6281  C  CB  . LEU B  1 334 ? -30.819 -14.504 -24.268 1.00 26.71  ?  365  LEU B CB  1 
ATOM   6282  C  CG  . LEU B  1 334 ? -29.302 -14.487 -24.517 1.00 28.49  ?  365  LEU B CG  1 
ATOM   6283  C  CD1 . LEU B  1 334 ? -28.602 -15.509 -23.652 1.00 26.44  ?  365  LEU B CD1 1 
ATOM   6284  C  CD2 . LEU B  1 334 ? -29.026 -14.737 -26.019 1.00 24.03  ?  365  LEU B CD2 1 
ATOM   6285  N  N   . ASP B  1 335 ? -33.688 -12.844 -23.813 1.00 28.35  ?  366  ASP B N   1 
ATOM   6286  C  CA  . ASP B  1 335 ? -35.138 -12.963 -23.709 1.00 27.87  ?  366  ASP B CA  1 
ATOM   6287  C  C   . ASP B  1 335 ? -35.868 -12.167 -24.768 1.00 30.93  ?  366  ASP B C   1 
ATOM   6288  O  O   . ASP B  1 335 ? -37.056 -12.427 -25.001 1.00 29.93  ?  366  ASP B O   1 
ATOM   6289  C  CB  . ASP B  1 335 ? -35.613 -12.500 -22.332 1.00 28.46  ?  366  ASP B CB  1 
ATOM   6290  C  CG  . ASP B  1 335 ? -34.982 -13.286 -21.211 1.00 28.35  ?  366  ASP B CG  1 
ATOM   6291  O  OD1 . ASP B  1 335 ? -34.567 -14.443 -21.434 1.00 30.83  ?  366  ASP B OD1 1 
ATOM   6292  O  OD2 . ASP B  1 335 ? -34.888 -12.744 -20.096 1.00 27.56  -1 366  ASP B OD2 1 
ATOM   6293  N  N   . LEU B  1 336 ? -35.222 -11.181 -25.400 1.00 26.01  ?  367  LEU B N   1 
ATOM   6294  C  CA  . LEU B  1 336 ? -35.977 -10.348 -26.342 1.00 28.62  ?  367  LEU B CA  1 
ATOM   6295  C  C   . LEU B  1 336 ? -36.503 -11.170 -27.519 1.00 27.03  ?  367  LEU B C   1 
ATOM   6296  O  O   . LEU B  1 336 ? -37.656 -11.005 -27.931 1.00 30.14  ?  367  LEU B O   1 
ATOM   6297  C  CB  . LEU B  1 336 ? -35.116 -9.182  -26.834 1.00 27.15  ?  367  LEU B CB  1 
ATOM   6298  C  CG  . LEU B  1 336 ? -34.674 -8.234  -25.703 1.00 29.63  ?  367  LEU B CG  1 
ATOM   6299  C  CD1 . LEU B  1 336 ? -33.844 -7.064  -26.236 1.00 28.97  ?  367  LEU B CD1 1 
ATOM   6300  C  CD2 . LEU B  1 336 ? -35.884 -7.715  -24.918 1.00 29.73  ?  367  LEU B CD2 1 
ATOM   6301  N  N   . TYR B  1 337 ? -35.680 -12.068 -28.064 1.00 29.18  ?  368  TYR B N   1 
ATOM   6302  C  CA  . TYR B  1 337 ? -36.100 -12.860 -29.223 1.00 32.55  ?  368  TYR B CA  1 
ATOM   6303  C  C   . TYR B  1 337 ? -37.373 -13.661 -28.953 1.00 30.42  ?  368  TYR B C   1 
ATOM   6304  O  O   . TYR B  1 337 ? -38.376 -13.444 -29.655 1.00 29.22  ?  368  TYR B O   1 
ATOM   6305  C  CB  . TYR B  1 337 ? -34.911 -13.720 -29.677 1.00 31.13  ?  368  TYR B CB  1 
ATOM   6306  C  CG  . TYR B  1 337 ? -34.998 -14.387 -31.047 1.00 33.19  ?  368  TYR B CG  1 
ATOM   6307  C  CD1 . TYR B  1 337 ? -36.125 -15.114 -31.444 1.00 32.48  ?  368  TYR B CD1 1 
ATOM   6308  C  CD2 . TYR B  1 337 ? -33.936 -14.304 -31.933 1.00 30.09  ?  368  TYR B CD2 1 
ATOM   6309  C  CE1 . TYR B  1 337 ? -36.175 -15.738 -32.688 1.00 28.67  ?  368  TYR B CE1 1 
ATOM   6310  C  CE2 . TYR B  1 337 ? -33.977 -14.921 -33.162 1.00 32.38  ?  368  TYR B CE2 1 
ATOM   6311  C  CZ  . TYR B  1 337 ? -35.110 -15.627 -33.538 1.00 35.37  ?  368  TYR B CZ  1 
ATOM   6312  O  OH  . TYR B  1 337 ? -35.132 -16.230 -34.760 1.00 32.18  ?  368  TYR B OH  1 
ATOM   6313  N  N   . PRO B  1 338 ? -37.424 -14.571 -27.970 1.00 31.03  ?  369  PRO B N   1 
ATOM   6314  C  CA  . PRO B  1 338 ? -38.690 -15.289 -27.737 1.00 31.88  ?  369  PRO B CA  1 
ATOM   6315  C  C   . PRO B  1 338 ? -39.791 -14.402 -27.189 1.00 32.65  ?  369  PRO B C   1 
ATOM   6316  O  O   . PRO B  1 338 ? -40.970 -14.702 -27.403 1.00 30.59  ?  369  PRO B O   1 
ATOM   6317  C  CB  . PRO B  1 338 ? -38.309 -16.383 -26.726 1.00 32.54  ?  369  PRO B CB  1 
ATOM   6318  C  CG  . PRO B  1 338 ? -37.104 -15.821 -26.019 1.00 29.11  ?  369  PRO B CG  1 
ATOM   6319  C  CD  . PRO B  1 338 ? -36.354 -15.067 -27.088 1.00 28.68  ?  369  PRO B CD  1 
ATOM   6320  N  N   . THR B  1 339 ? -39.467 -13.323 -26.475 1.00 32.50  ?  370  THR B N   1 
ATOM   6321  C  CA  . THR B  1 339 ? -40.541 -12.442 -26.020 1.00 30.43  ?  370  THR B CA  1 
ATOM   6322  C  C   . THR B  1 339 ? -41.193 -11.753 -27.203 1.00 31.72  ?  370  THR B C   1 
ATOM   6323  O  O   . THR B  1 339 ? -42.423 -11.766 -27.341 1.00 32.84  ?  370  THR B O   1 
ATOM   6324  C  CB  . THR B  1 339 ? -40.017 -11.423 -25.002 1.00 28.34  ?  370  THR B CB  1 
ATOM   6325  O  OG1 . THR B  1 339 ? -39.579 -12.123 -23.828 1.00 29.10  ?  370  THR B OG1 1 
ATOM   6326  C  CG2 . THR B  1 339 ? -41.114 -10.453 -24.578 1.00 29.75  ?  370  THR B CG2 1 
ATOM   6327  N  N   . PHE B  1 340 ? -40.380 -11.173 -28.094 1.00 31.58  ?  371  PHE B N   1 
ATOM   6328  C  CA  . PHE B  1 340 ? -40.931 -10.461 -29.247 1.00 32.31  ?  371  PHE B CA  1 
ATOM   6329  C  C   . PHE B  1 340 ? -41.715 -11.397 -30.171 1.00 31.90  ?  371  PHE B C   1 
ATOM   6330  O  O   . PHE B  1 340 ? -42.827 -11.068 -30.596 1.00 32.31  ?  371  PHE B O   1 
ATOM   6331  C  CB  . PHE B  1 340 ? -39.803 -9.761  -30.004 1.00 33.62  ?  371  PHE B CB  1 
ATOM   6332  C  CG  . PHE B  1 340 ? -39.177 -8.621  -29.246 1.00 28.81  ?  371  PHE B CG  1 
ATOM   6333  C  CD1 . PHE B  1 340 ? -39.764 -8.135  -28.080 1.00 28.88  ?  371  PHE B CD1 1 
ATOM   6334  C  CD2 . PHE B  1 340 ? -38.015 -8.023  -29.712 1.00 34.37  ?  371  PHE B CD2 1 
ATOM   6335  C  CE1 . PHE B  1 340 ? -39.189 -7.080  -27.378 1.00 31.71  ?  371  PHE B CE1 1 
ATOM   6336  C  CE2 . PHE B  1 340 ? -37.437 -6.955  -29.017 1.00 28.60  ?  371  PHE B CE2 1 
ATOM   6337  C  CZ  . PHE B  1 340 ? -38.026 -6.488  -27.851 1.00 27.25  ?  371  PHE B CZ  1 
ATOM   6338  N  N   . THR B  1 341 ? -41.154 -12.568 -30.498 1.00 31.12  ?  372  THR B N   1 
ATOM   6339  C  CA  . THR B  1 341 ? -41.845 -13.477 -31.409 1.00 36.87  ?  372  THR B CA  1 
ATOM   6340  C  C   . THR B  1 341 ? -43.115 -14.014 -30.772 1.00 39.58  ?  372  THR B C   1 
ATOM   6341  O  O   . THR B  1 341 ? -44.109 -14.261 -31.472 1.00 37.65  ?  372  THR B O   1 
ATOM   6342  C  CB  . THR B  1 341 ? -40.942 -14.644 -31.832 1.00 35.21  ?  372  THR B CB  1 
ATOM   6343  O  OG1 . THR B  1 341 ? -40.513 -15.360 -30.675 1.00 35.25  ?  372  THR B OG1 1 
ATOM   6344  C  CG2 . THR B  1 341 ? -39.738 -14.165 -32.592 1.00 34.30  ?  372  THR B CG2 1 
ATOM   6345  N  N   . GLY B  1 342 ? -43.103 -14.186 -29.449 1.00 33.38  ?  373  GLY B N   1 
ATOM   6346  C  CA  . GLY B  1 342 ? -44.340 -14.456 -28.741 1.00 36.37  ?  373  GLY B CA  1 
ATOM   6347  C  C   . GLY B  1 342 ? -45.391 -13.389 -28.986 1.00 39.25  ?  373  GLY B C   1 
ATOM   6348  O  O   . GLY B  1 342 ? -46.533 -13.697 -29.325 1.00 39.18  ?  373  GLY B O   1 
ATOM   6349  N  N   . LEU B  1 343 ? -45.024 -12.115 -28.801 1.00 37.66  ?  374  LEU B N   1 
ATOM   6350  C  CA  . LEU B  1 343 ? -46.009 -11.052 -28.976 1.00 37.74  ?  374  LEU B CA  1 
ATOM   6351  C  C   . LEU B  1 343 ? -46.467 -10.927 -30.418 1.00 37.47  ?  374  LEU B C   1 
ATOM   6352  O  O   . LEU B  1 343 ? -47.603 -10.496 -30.671 1.00 37.12  ?  374  LEU B O   1 
ATOM   6353  C  CB  . LEU B  1 343 ? -45.467 -9.701  -28.505 1.00 37.59  ?  374  LEU B CB  1 
ATOM   6354  C  CG  . LEU B  1 343 ? -44.921 -9.542  -27.099 1.00 39.71  ?  374  LEU B CG  1 
ATOM   6355  C  CD1 . LEU B  1 343 ? -44.193 -8.206  -26.999 1.00 39.76  ?  374  LEU B CD1 1 
ATOM   6356  C  CD2 . LEU B  1 343 ? -46.073 -9.605  -26.109 1.00 39.18  ?  374  LEU B CD2 1 
ATOM   6357  N  N   . ALA B  1 344 ? -45.601 -11.270 -31.367 1.00 32.02  ?  375  ALA B N   1 
ATOM   6358  C  CA  . ALA B  1 344 ? -45.940 -11.252 -32.779 1.00 40.02  ?  375  ALA B CA  1 
ATOM   6359  C  C   . ALA B  1 344 ? -46.719 -12.479 -33.207 1.00 39.51  ?  375  ALA B C   1 
ATOM   6360  O  O   . ALA B  1 344 ? -47.125 -12.554 -34.370 1.00 34.65  ?  375  ALA B O   1 
ATOM   6361  C  CB  . ALA B  1 344 ? -44.678 -11.165 -33.628 1.00 33.85  ?  375  ALA B CB  1 
ATOM   6362  N  N   . GLU B  1 345 ? -46.886 -13.454 -32.316 1.00 36.18  ?  376  GLU B N   1 
ATOM   6363  C  CA  . GLU B  1 345 ? -47.630 -14.652 -32.640 1.00 41.43  ?  376  GLU B CA  1 
ATOM   6364  C  C   . GLU B  1 345 ? -46.974 -15.342 -33.832 1.00 42.29  ?  376  GLU B C   1 
ATOM   6365  O  O   . GLU B  1 345 ? -47.637 -15.844 -34.735 1.00 44.47  ?  376  GLU B O   1 
ATOM   6366  C  CB  . GLU B  1 345 ? -49.086 -14.278 -32.917 1.00 41.26  ?  376  GLU B CB  1 
ATOM   6367  C  CG  . GLU B  1 345 ? -49.920 -14.196 -31.644 1.00 42.85  ?  376  GLU B CG  1 
ATOM   6368  C  CD  . GLU B  1 345 ? -51.312 -13.638 -31.902 1.00 50.90  ?  376  GLU B CD  1 
ATOM   6369  O  OE1 . GLU B  1 345 ? -52.017 -14.183 -32.780 1.00 57.28  ?  376  GLU B OE1 1 
ATOM   6370  O  OE2 . GLU B  1 345 ? -51.690 -12.636 -31.250 1.00 53.73  -1 376  GLU B OE2 1 
ATOM   6371  N  N   . ALA B  1 346 ? -45.646 -15.319 -33.856 1.00 40.29  ?  377  ALA B N   1 
ATOM   6372  C  CA  . ALA B  1 346 ? -44.875 -15.700 -35.030 1.00 38.92  ?  377  ALA B CA  1 
ATOM   6373  C  C   . ALA B  1 346 ? -44.280 -17.083 -34.834 1.00 45.83  ?  377  ALA B C   1 
ATOM   6374  O  O   . ALA B  1 346 ? -43.627 -17.344 -33.820 1.00 51.81  ?  377  ALA B O   1 
ATOM   6375  C  CB  . ALA B  1 346 ? -43.765 -14.683 -35.295 1.00 42.20  ?  377  ALA B CB  1 
ATOM   6376  N  N   . LYS B  1 347 ? -44.497 -17.960 -35.805 1.00 48.24  ?  378  LYS B N   1 
ATOM   6377  C  CA  . LYS B  1 347 ? -43.941 -19.303 -35.726 1.00 49.51  ?  378  LYS B CA  1 
ATOM   6378  C  C   . LYS B  1 347 ? -42.427 -19.252 -35.860 1.00 49.03  ?  378  LYS B C   1 
ATOM   6379  O  O   . LYS B  1 347 ? -41.882 -18.471 -36.643 1.00 52.04  ?  378  LYS B O   1 
ATOM   6380  C  CB  . LYS B  1 347 ? -44.533 -20.192 -36.822 1.00 44.88  ?  378  LYS B CB  1 
ATOM   6381  N  N   . LEU B  1 348 ? -41.771 -20.082 -35.132 1.00 48.85  ?  379  LEU B N   1 
ATOM   6382  C  CA  . LEU B  1 348 ? -40.320 -20.134 -35.186 1.00 49.34  ?  379  LEU B CA  1 
ATOM   6383  C  C   . LEU B  1 348 ? -39.849 -21.043 -36.320 1.00 47.26  ?  379  LEU B C   1 
ATOM   6384  O  O   . LEU B  1 348 ? -40.482 -22.059 -36.612 1.00 46.81  ?  379  LEU B O   1 
ATOM   6385  C  CB  . LEU B  1 348 ? -39.766 -20.650 -33.865 1.00 47.20  ?  379  LEU B CB  1 
ATOM   6386  C  CG  . LEU B  1 348 ? -39.678 -19.637 -32.722 1.00 50.68  ?  379  LEU B CG  1 
ATOM   6387  C  CD1 . LEU B  1 348 ? -38.843 -20.213 -31.599 1.00 46.58  ?  379  LEU B CD1 1 
ATOM   6388  C  CD2 . LEU B  1 348 ? -39.095 -18.309 -33.220 1.00 46.46  ?  379  LEU B CD2 1 
ATOM   6389  N  N   . PRO B  1 349 ? -38.732 -20.719 -36.967 1.00 48.45  ?  380  PRO B N   1 
ATOM   6390  C  CA  . PRO B  1 349 ? -38.212 -21.602 -38.023 1.00 47.23  ?  380  PRO B CA  1 
ATOM   6391  C  C   . PRO B  1 349 ? -37.838 -22.965 -37.457 1.00 47.27  ?  380  PRO B C   1 
ATOM   6392  O  O   . PRO B  1 349 ? -37.312 -23.062 -36.346 1.00 40.26  ?  380  PRO B O   1 
ATOM   6393  C  CB  . PRO B  1 349 ? -36.970 -20.856 -38.529 1.00 49.14  ?  380  PRO B CB  1 
ATOM   6394  C  CG  . PRO B  1 349 ? -37.179 -19.417 -38.098 1.00 45.06  ?  380  PRO B CG  1 
ATOM   6395  C  CD  . PRO B  1 349 ? -37.890 -19.524 -36.774 1.00 46.26  ?  380  PRO B CD  1 
ATOM   6396  N  N   . LYS B  1 350 ? -38.100 -24.025 -38.234 1.00 45.10  ?  381  LYS B N   1 
ATOM   6397  C  CA  . LYS B  1 350 ? -37.783 -25.376 -37.770 1.00 44.18  ?  381  LYS B CA  1 
ATOM   6398  C  C   . LYS B  1 350 ? -36.312 -25.482 -37.386 1.00 40.95  ?  381  LYS B C   1 
ATOM   6399  O  O   . LYS B  1 350 ? -35.429 -25.013 -38.109 1.00 41.73  ?  381  LYS B O   1 
ATOM   6400  C  CB  . LYS B  1 350 ? -38.111 -26.415 -38.846 1.00 45.29  ?  381  LYS B CB  1 
ATOM   6401  N  N   . GLY B  1 351 ? -36.052 -26.098 -36.236 1.00 41.72  ?  382  GLY B N   1 
ATOM   6402  C  CA  . GLY B  1 351 ? -34.693 -26.285 -35.770 1.00 42.75  ?  382  GLY B CA  1 
ATOM   6403  C  C   . GLY B  1 351 ? -34.100 -25.114 -35.015 1.00 44.26  ?  382  GLY B C   1 
ATOM   6404  O  O   . GLY B  1 351 ? -33.046 -25.283 -34.373 1.00 46.72  ?  382  GLY B O   1 
ATOM   6405  N  N   . LYS B  1 352 ? -34.734 -23.942 -35.062 1.00 41.06  ?  383  LYS B N   1 
ATOM   6406  C  CA  . LYS B  1 352 ? -34.217 -22.758 -34.372 1.00 41.94  ?  383  LYS B CA  1 
ATOM   6407  C  C   . LYS B  1 352 ? -34.084 -23.004 -32.873 1.00 42.02  ?  383  LYS B C   1 
ATOM   6408  O  O   . LYS B  1 352 ? -35.050 -23.405 -32.213 1.00 37.81  ?  383  LYS B O   1 
ATOM   6409  C  CB  . LYS B  1 352 ? -35.146 -21.568 -34.626 1.00 42.71  ?  383  LYS B CB  1 
ATOM   6410  C  CG  . LYS B  1 352 ? -34.768 -20.289 -33.884 1.00 38.74  ?  383  LYS B CG  1 
ATOM   6411  C  CD  . LYS B  1 352 ? -33.501 -19.688 -34.457 1.00 39.00  ?  383  LYS B CD  1 
ATOM   6412  C  CE  . LYS B  1 352 ? -32.787 -18.832 -33.416 1.00 39.29  ?  383  LYS B CE  1 
ATOM   6413  N  NZ  . LYS B  1 352 ? -31.725 -18.025 -34.052 1.00 33.32  ?  383  LYS B NZ  1 
ATOM   6414  N  N   . GLN B  1 353 ? -32.881 -22.745 -32.338 1.00 41.17  ?  384  GLN B N   1 
ATOM   6415  C  CA  . GLN B  1 353 ? -32.571 -22.874 -30.917 1.00 40.18  ?  384  GLN B CA  1 
ATOM   6416  C  C   . GLN B  1 353 ? -32.427 -21.498 -30.273 1.00 37.14  ?  384  GLN B C   1 
ATOM   6417  O  O   . GLN B  1 353 ? -31.821 -20.594 -30.857 1.00 33.80  ?  384  GLN B O   1 
ATOM   6418  C  CB  . GLN B  1 353 ? -31.274 -23.645 -30.707 1.00 38.67  ?  384  GLN B CB  1 
ATOM   6419  C  CG  . GLN B  1 353 ? -31.247 -25.002 -31.372 1.00 44.36  ?  384  GLN B CG  1 
ATOM   6420  C  CD  . GLN B  1 353 ? -30.929 -26.091 -30.395 1.00 53.62  ?  384  GLN B CD  1 
ATOM   6421  O  OE1 . GLN B  1 353 ? -31.740 -26.419 -29.525 1.00 58.54  ?  384  GLN B OE1 1 
ATOM   6422  N  NE2 . GLN B  1 353 ? -29.729 -26.654 -30.512 1.00 58.66  ?  384  GLN B NE2 1 
ATOM   6423  N  N   . LEU B  1 354 ? -32.968 -21.353 -29.064 1.00 34.27  ?  385  LEU B N   1 
ATOM   6424  C  CA  . LEU B  1 354 ? -33.020 -20.078 -28.350 1.00 36.07  ?  385  LEU B CA  1 
ATOM   6425  C  C   . LEU B  1 354 ? -32.527 -20.295 -26.930 1.00 39.30  ?  385  LEU B C   1 
ATOM   6426  O  O   . LEU B  1 354 ? -32.950 -21.248 -26.270 1.00 41.91  ?  385  LEU B O   1 
ATOM   6427  C  CB  . LEU B  1 354 ? -34.445 -19.519 -28.327 1.00 38.33  ?  385  LEU B CB  1 
ATOM   6428  C  CG  . LEU B  1 354 ? -35.039 -18.995 -29.635 1.00 34.45  ?  385  LEU B CG  1 
ATOM   6429  C  CD1 . LEU B  1 354 ? -36.455 -18.508 -29.407 1.00 33.50  ?  385  LEU B CD1 1 
ATOM   6430  C  CD2 . LEU B  1 354 ? -34.182 -17.853 -30.174 1.00 34.15  ?  385  LEU B CD2 1 
ATOM   6431  N  N   . ASP B  1 355 ? -31.635 -19.419 -26.457 1.00 37.57  ?  386  ASP B N   1 
ATOM   6432  C  CA  . ASP B  1 355 ? -31.107 -19.539 -25.107 1.00 32.36  ?  386  ASP B CA  1 
ATOM   6433  C  C   . ASP B  1 355 ? -31.896 -18.737 -24.078 1.00 35.51  ?  386  ASP B C   1 
ATOM   6434  O  O   . ASP B  1 355 ? -31.696 -18.937 -22.872 1.00 40.78  ?  386  ASP B O   1 
ATOM   6435  C  CB  . ASP B  1 355 ? -29.621 -19.120 -25.071 1.00 34.54  ?  386  ASP B CB  1 
ATOM   6436  C  CG  . ASP B  1 355 ? -28.706 -20.162 -25.693 1.00 40.87  ?  386  ASP B CG  1 
ATOM   6437  O  OD1 . ASP B  1 355 ? -28.945 -21.366 -25.460 1.00 45.48  ?  386  ASP B OD1 1 
ATOM   6438  O  OD2 . ASP B  1 355 ? -27.771 -19.793 -26.440 1.00 35.91  -1 386  ASP B OD2 1 
ATOM   6439  N  N   . GLY B  1 356 ? -32.782 -17.840 -24.507 1.00 32.64  ?  387  GLY B N   1 
ATOM   6440  C  CA  . GLY B  1 356 ? -33.555 -17.021 -23.599 1.00 30.08  ?  387  GLY B CA  1 
ATOM   6441  C  C   . GLY B  1 356 ? -34.981 -17.522 -23.404 1.00 35.35  ?  387  GLY B C   1 
ATOM   6442  O  O   . GLY B  1 356 ? -35.347 -18.643 -23.769 1.00 31.58  ?  387  GLY B O   1 
ATOM   6443  N  N   . LYS B  1 357 ? -35.796 -16.664 -22.792 1.00 34.16  ?  388  LYS B N   1 
ATOM   6444  C  CA  . LYS B  1 357 ? -37.147 -17.019 -22.385 1.00 34.55  ?  388  LYS B CA  1 
ATOM   6445  C  C   . LYS B  1 357 ? -38.120 -15.929 -22.789 1.00 32.24  ?  388  LYS B C   1 
ATOM   6446  O  O   . LYS B  1 357 ? -37.797 -14.742 -22.758 1.00 30.29  ?  388  LYS B O   1 
ATOM   6447  C  CB  . LYS B  1 357 ? -37.268 -17.208 -20.867 1.00 31.53  ?  388  LYS B CB  1 
ATOM   6448  C  CG  . LYS B  1 357 ? -36.315 -18.218 -20.279 1.00 36.78  ?  388  LYS B CG  1 
ATOM   6449  C  CD  . LYS B  1 357 ? -36.597 -18.422 -18.799 1.00 39.97  ?  388  LYS B CD  1 
ATOM   6450  C  CE  . LYS B  1 357 ? -35.670 -19.454 -18.221 1.00 39.65  ?  388  LYS B CE  1 
ATOM   6451  N  NZ  . LYS B  1 357 ? -35.948 -20.798 -18.799 1.00 45.29  ?  388  LYS B NZ  1 
ATOM   6452  N  N   . ASN B  1 358 ? -39.326 -16.340 -23.151 1.00 33.20  ?  389  ASN B N   1 
ATOM   6453  C  CA  . ASN B  1 358 ? -40.422 -15.393 -23.294 1.00 31.42  ?  389  ASN B CA  1 
ATOM   6454  C  C   . ASN B  1 358 ? -40.855 -14.947 -21.892 1.00 34.73  ?  389  ASN B C   1 
ATOM   6455  O  O   . ASN B  1 358 ? -41.462 -15.731 -21.153 1.00 32.21  ?  389  ASN B O   1 
ATOM   6456  C  CB  . ASN B  1 358 ? -41.552 -16.074 -24.072 1.00 32.95  ?  389  ASN B CB  1 
ATOM   6457  C  CG  . ASN B  1 358 ? -42.772 -15.209 -24.228 1.00 37.48  ?  389  ASN B CG  1 
ATOM   6458  O  OD1 . ASN B  1 358 ? -42.887 -14.150 -23.605 1.00 34.93  ?  389  ASN B OD1 1 
ATOM   6459  N  ND2 . ASN B  1 358 ? -43.730 -15.678 -25.055 1.00 35.86  ?  389  ASN B ND2 1 
ATOM   6460  N  N   . ILE B  1 359 ? -40.552 -13.698 -21.507 1.00 30.58  ?  390  ILE B N   1 
ATOM   6461  C  CA  . ILE B  1 359 ? -40.715 -13.258 -20.120 1.00 30.19  ?  390  ILE B CA  1 
ATOM   6462  C  C   . ILE B  1 359 ? -41.879 -12.305 -19.910 1.00 32.15  ?  390  ILE B C   1 
ATOM   6463  O  O   . ILE B  1 359 ? -42.046 -11.816 -18.787 1.00 33.39  ?  390  ILE B O   1 
ATOM   6464  C  CB  . ILE B  1 359 ? -39.415 -12.627 -19.567 1.00 29.32  ?  390  ILE B CB  1 
ATOM   6465  C  CG1 . ILE B  1 359 ? -39.096 -11.310 -20.299 1.00 28.50  ?  390  ILE B CG1 1 
ATOM   6466  C  CG2 . ILE B  1 359 ? -38.283 -13.636 -19.620 1.00 29.11  ?  390  ILE B CG2 1 
ATOM   6467  C  CD1 . ILE B  1 359 ? -38.043 -10.378 -19.581 1.00 30.45  ?  390  ILE B CD1 1 
ATOM   6468  N  N   . MET B  1 360 ? -42.709 -12.034 -20.923 1.00 31.24  ?  391  MET B N   1 
ATOM   6469  C  CA  . MET B  1 360 ? -43.744 -11.015 -20.732 1.00 34.29  ?  391  MET B CA  1 
ATOM   6470  C  C   . MET B  1 360 ? -44.690 -11.391 -19.600 1.00 34.38  ?  391  MET B C   1 
ATOM   6471  O  O   . MET B  1 360 ? -45.030 -10.552 -18.750 1.00 32.05  ?  391  MET B O   1 
ATOM   6472  C  CB  . MET B  1 360 ? -44.515 -10.801 -22.033 1.00 31.58  ?  391  MET B CB  1 
ATOM   6473  C  CG  . MET B  1 360 ? -45.324 -9.489  -22.149 1.00 33.79  ?  391  MET B CG  1 
ATOM   6474  S  SD  . MET B  1 360 ? -44.565 -8.006  -21.430 1.00 36.11  ?  391  MET B SD  1 
ATOM   6475  C  CE  . MET B  1 360 ? -44.209 -7.091  -22.917 1.00 35.57  ?  391  MET B CE  1 
ATOM   6476  N  N   . ASP B  1 361 ? -45.079 -12.659 -19.545 1.00 35.25  ?  392  ASP B N   1 
ATOM   6477  C  CA  . ASP B  1 361 ? -45.977 -13.127 -18.461 1.00 39.08  ?  392  ASP B CA  1 
ATOM   6478  C  C   . ASP B  1 361 ? -45.329 -12.851 -17.102 1.00 39.02  ?  392  ASP B C   1 
ATOM   6479  O  O   . ASP B  1 361 ? -46.004 -12.292 -16.229 1.00 36.34  ?  392  ASP B O   1 
ATOM   6480  C  CB  . ASP B  1 361 ? -46.324 -14.595 -18.593 1.00 41.34  ?  392  ASP B CB  1 
ATOM   6481  C  CG  . ASP B  1 361 ? -47.672 -14.981 -18.012 1.00 56.60  ?  392  ASP B CG  1 
ATOM   6482  O  OD1 . ASP B  1 361 ? -48.615 -14.181 -18.160 1.00 58.43  -1 392  ASP B OD1 1 
ATOM   6483  O  OD2 . ASP B  1 361 ? -47.761 -16.071 -17.415 1.00 63.18  ?  392  ASP B OD2 1 
ATOM   6484  N  N   . ASP B  1 362 ? -44.064 -13.232 -16.954 1.00 34.27  ?  393  ASP B N   1 
ATOM   6485  C  CA  . ASP B  1 362 ? -43.419 -12.974 -15.673 1.00 36.36  ?  393  ASP B CA  1 
ATOM   6486  C  C   . ASP B  1 362 ? -43.396 -11.489 -15.371 1.00 34.40  ?  393  ASP B C   1 
ATOM   6487  O  O   . ASP B  1 362 ? -43.599 -11.079 -14.227 1.00 35.48  ?  393  ASP B O   1 
ATOM   6488  C  CB  . ASP B  1 362 ? -42.007 -13.531 -15.680 1.00 34.50  ?  393  ASP B CB  1 
ATOM   6489  C  CG  . ASP B  1 362 ? -41.989 -15.035 -15.742 1.00 40.69  ?  393  ASP B CG  1 
ATOM   6490  O  OD1 . ASP B  1 362 ? -42.251 -15.676 -14.698 1.00 38.52  ?  393  ASP B OD1 1 
ATOM   6491  O  OD2 . ASP B  1 362 ? -41.705 -15.566 -16.838 1.00 40.11  -1 393  ASP B OD2 1 
ATOM   6492  N  N   . VAL B  1 363 ? -43.148 -10.666 -16.391 1.00 31.97  ?  394  VAL B N   1 
ATOM   6493  C  CA  . VAL B  1 363 ? -43.131 -9.226  -16.177 1.00 31.35  ?  394  VAL B CA  1 
ATOM   6494  C  C   . VAL B  1 363 ? -44.493 -8.760  -15.678 1.00 33.51  ?  394  VAL B C   1 
ATOM   6495  O  O   . VAL B  1 363 ? -44.597 -7.999  -14.710 1.00 35.21  ?  394  VAL B O   1 
ATOM   6496  C  CB  . VAL B  1 363 ? -42.709 -8.509  -17.475 1.00 31.08  ?  394  VAL B CB  1 
ATOM   6497  C  CG1 . VAL B  1 363 ? -42.966 -7.024  -17.374 1.00 30.23  ?  394  VAL B CG1 1 
ATOM   6498  C  CG2 . VAL B  1 363 ? -41.218 -8.780  -17.759 1.00 35.08  ?  394  VAL B CG2 1 
ATOM   6499  N  N   . LEU B  1 364 ? -45.563 -9.227  -16.316 1.00 33.19  ?  395  LEU B N   1 
ATOM   6500  C  CA  . LEU B  1 364 ? -46.922 -8.727  -15.978 1.00 34.03  ?  395  LEU B CA  1 
ATOM   6501  C  C   . LEU B  1 364 ? -47.376 -9.260  -14.617 1.00 34.82  ?  395  LEU B C   1 
ATOM   6502  O  O   . LEU B  1 364 ? -48.175 -8.599  -13.964 1.00 37.91  ?  395  LEU B O   1 
ATOM   6503  C  CB  . LEU B  1 364 ? -47.872 -9.143  -17.095 1.00 35.16  ?  395  LEU B CB  1 
ATOM   6504  C  CG  . LEU B  1 364 ? -47.674 -8.434  -18.435 1.00 38.95  ?  395  LEU B CG  1 
ATOM   6505  C  CD1 . LEU B  1 364 ? -48.688 -8.917  -19.451 1.00 35.46  ?  395  LEU B CD1 1 
ATOM   6506  C  CD2 . LEU B  1 364 ? -47.780 -6.938  -18.236 1.00 34.96  ?  395  LEU B CD2 1 
ATOM   6507  N  N   . LYS B  1 365 ? -46.882 -10.427 -14.238 1.00 31.90  ?  396  LYS B N   1 
ATOM   6508  C  CA  . LYS B  1 365 ? -47.316 -11.030 -12.953 1.00 36.23  ?  396  LYS B CA  1 
ATOM   6509  C  C   . LYS B  1 365 ? -46.238 -10.882 -11.860 1.00 40.31  ?  396  LYS B C   1 
ATOM   6510  O  O   . LYS B  1 365 ? -46.507 -11.310 -10.733 1.00 40.14  ?  396  LYS B O   1 
ATOM   6511  C  CB  . LYS B  1 365 ? -47.675 -12.492 -13.241 1.00 41.40  ?  396  LYS B CB  1 
ATOM   6512  C  CG  . LYS B  1 365 ? -48.833 -12.703 -14.195 1.00 43.15  ?  396  LYS B CG  1 
ATOM   6513  C  CD  . LYS B  1 365 ? -49.104 -14.180 -14.440 1.00 50.56  ?  396  LYS B CD  1 
ATOM   6514  C  CE  . LYS B  1 365 ? -50.411 -14.404 -15.126 1.00 53.72  ?  396  LYS B CE  1 
ATOM   6515  N  NZ  . LYS B  1 365 ? -50.448 -13.754 -16.437 1.00 59.58  ?  396  LYS B NZ  1 
ATOM   6516  N  N   . ASN B  1 366 ? -45.067 -10.328 -12.193 1.00 39.23  ?  397  ASN B N   1 
ATOM   6517  C  CA  . ASN B  1 366 ? -43.968 -10.177 -11.228 1.00 34.62  ?  397  ASN B CA  1 
ATOM   6518  C  C   . ASN B  1 366 ? -43.496 -11.528 -10.686 1.00 31.23  ?  397  ASN B C   1 
ATOM   6519  O  O   . ASN B  1 366 ? -43.353 -11.725 -9.480  1.00 34.95  ?  397  ASN B O   1 
ATOM   6520  C  CB  . ASN B  1 366 ? -44.343 -9.239  -10.077 1.00 37.68  ?  397  ASN B CB  1 
ATOM   6521  C  CG  . ASN B  1 366 ? -43.113 -8.763  -9.303  1.00 41.58  ?  397  ASN B CG  1 
ATOM   6522  O  OD1 . ASN B  1 366 ? -42.062 -8.528  -9.898  1.00 35.73  ?  397  ASN B OD1 1 
ATOM   6523  N  ND2 . ASN B  1 366 ? -43.230 -8.644  -7.980  1.00 43.16  ?  397  ASN B ND2 1 
ATOM   6524  N  N   . THR B  1 367 ? -43.250 -12.468 -11.589 1.00 33.65  ?  398  THR B N   1 
ATOM   6525  C  CA  . THR B  1 367 ? -42.708 -13.756 -11.199 1.00 34.87  ?  398  THR B CA  1 
ATOM   6526  C  C   . THR B  1 367 ? -41.310 -13.907 -11.785 1.00 37.42  ?  398  THR B C   1 
ATOM   6527  O  O   . THR B  1 367 ? -40.892 -13.153 -12.667 1.00 33.68  ?  398  THR B O   1 
ATOM   6528  C  CB  . THR B  1 367 ? -43.617 -14.920 -11.632 1.00 37.12  ?  398  THR B CB  1 
ATOM   6529  O  OG1 . THR B  1 367 ? -43.868 -14.847 -13.035 1.00 36.98  ?  398  THR B OG1 1 
ATOM   6530  C  CG2 . THR B  1 367 ? -44.949 -14.860 -10.874 1.00 36.12  ?  398  THR B CG2 1 
ATOM   6531  N  N   . GLU B  1 368 ? -40.597 -14.915 -11.291 1.00 37.90  ?  399  GLU B N   1 
ATOM   6532  C  CA  . GLU B  1 368 ? -39.160 -15.023 -11.470 1.00 35.74  ?  399  GLU B CA  1 
ATOM   6533  C  C   . GLU B  1 368 ? -38.832 -15.946 -12.644 1.00 35.80  ?  399  GLU B C   1 
ATOM   6534  O  O   . GLU B  1 368 ? -38.882 -17.172 -12.495 1.00 34.90  ?  399  GLU B O   1 
ATOM   6535  C  CB  . GLU B  1 368 ? -38.527 -15.535 -10.173 1.00 34.16  ?  399  GLU B CB  1 
ATOM   6536  C  CG  . GLU B  1 368 ? -37.028 -15.746 -10.240 1.00 36.18  ?  399  GLU B CG  1 
ATOM   6537  C  CD  . GLU B  1 368 ? -36.472 -16.325 -8.954  1.00 40.03  ?  399  GLU B CD  1 
ATOM   6538  O  OE1 . GLU B  1 368 ? -37.274 -16.678 -8.054  1.00 39.55  ?  399  GLU B OE1 1 
ATOM   6539  O  OE2 . GLU B  1 368 ? -35.233 -16.424 -8.851  1.00 36.39  -1 399  GLU B OE2 1 
ATOM   6540  N  N   . PRO B  1 369 ? -38.470 -15.417 -13.820 1.00 31.85  ?  400  PRO B N   1 
ATOM   6541  C  CA  . PRO B  1 369 ? -38.292 -16.298 -14.986 1.00 33.81  ?  400  PRO B CA  1 
ATOM   6542  C  C   . PRO B  1 369 ? -37.078 -17.208 -14.904 1.00 35.79  ?  400  PRO B C   1 
ATOM   6543  O  O   . PRO B  1 369 ? -37.093 -18.292 -15.498 1.00 36.54  ?  400  PRO B O   1 
ATOM   6544  C  CB  . PRO B  1 369 ? -38.189 -15.310 -16.154 1.00 34.34  ?  400  PRO B CB  1 
ATOM   6545  C  CG  . PRO B  1 369 ? -37.663 -14.067 -15.528 1.00 33.93  ?  400  PRO B CG  1 
ATOM   6546  C  CD  . PRO B  1 369 ? -38.315 -13.997 -14.171 1.00 32.87  ?  400  PRO B CD  1 
ATOM   6547  N  N   . TYR B  1 370 ? -36.018 -16.821 -14.201 1.00 31.24  ?  401  TYR B N   1 
ATOM   6548  C  CA  . TYR B  1 370 ? -34.807 -17.623 -14.175 1.00 33.72  ?  401  TYR B CA  1 
ATOM   6549  C  C   . TYR B  1 370 ? -34.634 -18.326 -12.826 1.00 37.52  ?  401  TYR B C   1 
ATOM   6550  O  O   . TYR B  1 370 ? -33.509 -18.604 -12.393 1.00 33.88  ?  401  TYR B O   1 
ATOM   6551  C  CB  . TYR B  1 370 ? -33.595 -16.756 -14.533 1.00 32.17  ?  401  TYR B CB  1 
ATOM   6552  C  CG  . TYR B  1 370 ? -33.455 -16.556 -16.035 1.00 32.12  ?  401  TYR B CG  1 
ATOM   6553  C  CD1 . TYR B  1 370 ? -34.111 -15.510 -16.679 1.00 28.71  ?  401  TYR B CD1 1 
ATOM   6554  C  CD2 . TYR B  1 370 ? -32.692 -17.432 -16.813 1.00 33.38  ?  401  TYR B CD2 1 
ATOM   6555  C  CE1 . TYR B  1 370 ? -34.001 -15.321 -18.060 1.00 29.41  ?  401  TYR B CE1 1 
ATOM   6556  C  CE2 . TYR B  1 370 ? -32.578 -17.262 -18.194 1.00 32.26  ?  401  TYR B CE2 1 
ATOM   6557  C  CZ  . TYR B  1 370 ? -33.240 -16.200 -18.817 1.00 31.09  ?  401  TYR B CZ  1 
ATOM   6558  O  OH  . TYR B  1 370 ? -33.129 -16.012 -20.187 1.00 30.11  ?  401  TYR B OH  1 
ATOM   6559  N  N   . LYS B  1 371 ? -35.752 -18.630 -12.158 1.00 35.64  ?  402  LYS B N   1 
ATOM   6560  C  CA  . LYS B  1 371 ? -35.688 -19.293 -10.862 1.00 38.28  ?  402  LYS B CA  1 
ATOM   6561  C  C   . LYS B  1 371 ? -34.928 -20.602 -10.998 1.00 35.25  ?  402  LYS B C   1 
ATOM   6562  O  O   . LYS B  1 371 ? -35.212 -21.406 -11.888 1.00 33.73  ?  402  LYS B O   1 
ATOM   6563  C  CB  . LYS B  1 371 ? -37.094 -19.536 -10.316 1.00 39.69  ?  402  LYS B CB  1 
ATOM   6564  C  CG  . LYS B  1 371 ? -37.131 -20.059 -8.869  1.00 41.25  ?  402  LYS B CG  1 
ATOM   6565  C  CD  . LYS B  1 371 ? -38.561 -20.420 -8.460  1.00 48.82  ?  402  LYS B CD  1 
ATOM   6566  C  CE  . LYS B  1 371 ? -38.893 -19.974 -7.031  1.00 50.40  ?  402  LYS B CE  1 
ATOM   6567  N  NZ  . LYS B  1 371 ? -37.711 -20.065 -6.109  1.00 53.92  ?  402  LYS B NZ  1 
ATOM   6568  N  N   . ASP B  1 372 ? -33.895 -20.762 -10.172 1.00 35.80  ?  403  ASP B N   1 
ATOM   6569  C  CA  . ASP B  1 372 ? -33.008 -21.927 -10.188 1.00 37.81  ?  403  ASP B CA  1 
ATOM   6570  C  C   . ASP B  1 372 ? -32.354 -22.158 -11.547 1.00 37.50  ?  403  ASP B C   1 
ATOM   6571  O  O   . ASP B  1 372 ? -31.934 -23.280 -11.857 1.00 37.01  ?  403  ASP B O   1 
ATOM   6572  C  CB  . ASP B  1 372 ? -33.747 -23.194 -9.727  1.00 44.32  ?  403  ASP B CB  1 
ATOM   6573  C  CG  . ASP B  1 372 ? -34.328 -23.042 -8.324  1.00 42.12  ?  403  ASP B CG  1 
ATOM   6574  O  OD1 . ASP B  1 372 ? -33.670 -22.408 -7.473  1.00 48.51  ?  403  ASP B OD1 1 
ATOM   6575  O  OD2 . ASP B  1 372 ? -35.440 -23.538 -8.076  1.00 51.96  -1 403  ASP B OD2 1 
ATOM   6576  N  N   . GLU B  1 373 ? -32.226 -21.113 -12.358 1.00 31.87  ?  404  GLU B N   1 
ATOM   6577  C  CA  . GLU B  1 373 ? -31.513 -21.211 -13.620 1.00 34.35  ?  404  GLU B CA  1 
ATOM   6578  C  C   . GLU B  1 373 ? -30.479 -20.098 -13.710 1.00 35.83  ?  404  GLU B C   1 
ATOM   6579  O  O   . GLU B  1 373 ? -30.558 -19.089 -13.006 1.00 32.23  ?  404  GLU B O   1 
ATOM   6580  C  CB  . GLU B  1 373 ? -32.477 -21.137 -14.796 1.00 36.24  ?  404  GLU B CB  1 
ATOM   6581  C  CG  . GLU B  1 373 ? -33.420 -22.327 -14.797 1.00 37.84  ?  404  GLU B CG  1 
ATOM   6582  C  CD  . GLU B  1 373 ? -34.311 -22.353 -15.992 1.00 44.43  ?  404  GLU B CD  1 
ATOM   6583  O  OE1 . GLU B  1 373 ? -33.776 -22.304 -17.119 1.00 47.68  ?  404  GLU B OE1 1 
ATOM   6584  O  OE2 . GLU B  1 373 ? -35.546 -22.422 -15.802 1.00 48.43  -1 404  GLU B OE2 1 
ATOM   6585  N  N   . MET B  1 374 ? -29.523 -20.293 -14.612 1.00 33.95  ?  405  MET B N   1 
ATOM   6586  C  CA  . MET B  1 374 ? -28.310 -19.499 -14.665 1.00 34.26  ?  405  MET B CA  1 
ATOM   6587  C  C   . MET B  1 374 ? -28.402 -18.455 -15.778 1.00 34.25  ?  405  MET B C   1 
ATOM   6588  O  O   . MET B  1 374 ? -28.984 -18.700 -16.840 1.00 33.50  ?  405  MET B O   1 
ATOM   6589  C  CB  . MET B  1 374 ? -27.102 -20.403 -14.916 1.00 36.88  ?  405  MET B CB  1 
ATOM   6590  C  CG  . MET B  1 374 ? -26.671 -21.192 -13.723 1.00 35.04  ?  405  MET B CG  1 
ATOM   6591  S  SD  . MET B  1 374 ? -25.684 -20.186 -12.633 1.00 37.64  ?  405  MET B SD  1 
ATOM   6592  C  CE  . MET B  1 374 ? -24.571 -21.422 -11.976 1.00 42.03  ?  405  MET B CE  1 
ATOM   6593  N  N   . ILE B  1 375 ? -27.834 -17.285 -15.513 1.00 32.63  ?  406  ILE B N   1 
ATOM   6594  C  CA  . ILE B  1 375 ? -27.468 -16.312 -16.531 1.00 30.07  ?  406  ILE B CA  1 
ATOM   6595  C  C   . ILE B  1 375 ? -25.952 -16.170 -16.458 1.00 29.11  ?  406  ILE B C   1 
ATOM   6596  O  O   . ILE B  1 375 ? -25.404 -16.025 -15.359 1.00 30.88  ?  406  ILE B O   1 
ATOM   6597  C  CB  . ILE B  1 375 ? -28.175 -14.968 -16.291 1.00 31.16  ?  406  ILE B CB  1 
ATOM   6598  C  CG1 . ILE B  1 375 ? -29.651 -15.084 -16.668 1.00 31.84  ?  406  ILE B CG1 1 
ATOM   6599  C  CG2 . ILE B  1 375 ? -27.489 -13.839 -17.061 1.00 27.16  ?  406  ILE B CG2 1 
ATOM   6600  C  CD1 . ILE B  1 375 ? -30.510 -13.957 -16.085 1.00 30.50  ?  406  ILE B CD1 1 
ATOM   6601  N  N   . TYR B  1 376 ? -25.292 -16.199 -17.626 1.00 25.75  ?  407  TYR B N   1 
ATOM   6602  C  CA  . TYR B  1 376 ? -23.863 -16.449 -17.775 1.00 30.63  ?  407  TYR B CA  1 
ATOM   6603  C  C   . TYR B  1 376 ? -23.150 -15.343 -18.550 1.00 30.22  ?  407  TYR B C   1 
ATOM   6604  O  O   . TYR B  1 376 ? -23.731 -14.668 -19.400 1.00 28.39  ?  407  TYR B O   1 
ATOM   6605  C  CB  . TYR B  1 376 ? -23.598 -17.723 -18.567 1.00 31.55  ?  407  TYR B CB  1 
ATOM   6606  C  CG  . TYR B  1 376 ? -24.023 -19.037 -17.991 1.00 32.00  ?  407  TYR B CG  1 
ATOM   6607  C  CD1 . TYR B  1 376 ? -23.406 -19.542 -16.861 1.00 33.40  ?  407  TYR B CD1 1 
ATOM   6608  C  CD2 . TYR B  1 376 ? -24.992 -19.821 -18.638 1.00 36.31  ?  407  TYR B CD2 1 
ATOM   6609  C  CE1 . TYR B  1 376 ? -23.751 -20.771 -16.352 1.00 39.63  ?  407  TYR B CE1 1 
ATOM   6610  C  CE2 . TYR B  1 376 ? -25.360 -21.063 -18.130 1.00 35.80  ?  407  TYR B CE2 1 
ATOM   6611  C  CZ  . TYR B  1 376 ? -24.735 -21.530 -16.991 1.00 38.76  ?  407  TYR B CZ  1 
ATOM   6612  O  OH  . TYR B  1 376 ? -25.071 -22.758 -16.460 1.00 42.17  ?  407  TYR B OH  1 
ATOM   6613  N  N   . SER B  1 377 ? -21.846 -15.231 -18.318 1.00 28.92  ?  408  SER B N   1 
ATOM   6614  C  CA  . SER B  1 377 ? -20.975 -14.570 -19.285 1.00 25.70  ?  408  SER B CA  1 
ATOM   6615  C  C   . SER B  1 377 ? -19.615 -15.248 -19.290 1.00 25.68  ?  408  SER B C   1 
ATOM   6616  O  O   . SER B  1 377 ? -19.093 -15.604 -18.235 1.00 27.43  ?  408  SER B O   1 
ATOM   6617  C  CB  . SER B  1 377 ? -20.770 -13.080 -18.977 1.00 25.75  ?  408  SER B CB  1 
ATOM   6618  O  OG  . SER B  1 377 ? -19.810 -12.556 -19.894 1.00 26.42  ?  408  SER B OG  1 
ATOM   6619  N  N   . LEU B  1 378 ? -19.030 -15.405 -20.470 1.00 29.10  ?  409  LEU B N   1 
ATOM   6620  C  CA  . LEU B  1 378 ? -17.651 -15.877 -20.563 1.00 30.03  ?  409  LEU B CA  1 
ATOM   6621  C  C   . LEU B  1 378 ? -16.954 -15.040 -21.619 1.00 26.14  ?  409  LEU B C   1 
ATOM   6622  O  O   . LEU B  1 378 ? -17.416 -14.968 -22.763 1.00 23.44  ?  409  LEU B O   1 
ATOM   6623  C  CB  . LEU B  1 378 ? -17.571 -17.370 -20.919 1.00 28.42  ?  409  LEU B CB  1 
ATOM   6624  C  CG  . LEU B  1 378 ? -16.146 -17.928 -20.834 1.00 25.15  ?  409  LEU B CG  1 
ATOM   6625  C  CD1 . LEU B  1 378 ? -16.159 -19.352 -20.312 1.00 30.51  ?  409  LEU B CD1 1 
ATOM   6626  C  CD2 . LEU B  1 378 ? -15.414 -17.827 -22.196 1.00 26.93  ?  409  LEU B CD2 1 
ATOM   6627  N  N   . ARG B  1 379 ? -15.843 -14.422 -21.252 1.00 25.22  ?  410  ARG B N   1 
ATOM   6628  C  CA  . ARG B  1 379 ? -15.143 -13.514 -22.155 1.00 23.53  ?  410  ARG B CA  1 
ATOM   6629  C  C   . ARG B  1 379 ? -13.703 -13.999 -22.294 1.00 26.38  ?  410  ARG B C   1 
ATOM   6630  O  O   . ARG B  1 379 ? -12.997 -14.156 -21.294 1.00 23.79  ?  410  ARG B O   1 
ATOM   6631  C  CB  . ARG B  1 379 ? -15.218 -12.073 -21.626 1.00 24.89  ?  410  ARG B CB  1 
ATOM   6632  C  CG  . ARG B  1 379 ? -14.467 -11.048 -22.462 1.00 23.49  ?  410  ARG B CG  1 
ATOM   6633  C  CD  . ARG B  1 379 ? -13.096 -10.736 -21.885 1.00 22.40  ?  410  ARG B CD  1 
ATOM   6634  N  NE  . ARG B  1 379 ? -12.247 -10.125 -22.905 1.00 24.47  ?  410  ARG B NE  1 
ATOM   6635  C  CZ  . ARG B  1 379 ? -12.300 -8.851  -23.277 1.00 26.66  ?  410  ARG B CZ  1 
ATOM   6636  N  NH1 . ARG B  1 379 ? -13.131 -7.982  -22.697 1.00 24.21  ?  410  ARG B NH1 1 
ATOM   6637  N  NH2 . ARG B  1 379 ? -11.492 -8.427  -24.244 1.00 24.36  ?  410  ARG B NH2 1 
ATOM   6638  N  N   . TYR B  1 380 ? -13.280 -14.242 -23.529 1.00 27.80  ?  411  TYR B N   1 
ATOM   6639  C  CA  . TYR B  1 380 ? -11.938 -14.724 -23.796 1.00 25.82  ?  411  TYR B CA  1 
ATOM   6640  C  C   . TYR B  1 380 ? -10.926 -13.614 -23.580 1.00 26.28  ?  411  TYR B C   1 
ATOM   6641  O  O   . TYR B  1 380 ? -11.126 -12.486 -24.038 1.00 26.71  ?  411  TYR B O   1 
ATOM   6642  C  CB  . TYR B  1 380 ? -11.836 -15.249 -25.237 1.00 25.43  ?  411  TYR B CB  1 
ATOM   6643  C  CG  . TYR B  1 380 ? -12.778 -16.389 -25.524 1.00 27.18  ?  411  TYR B CG  1 
ATOM   6644  C  CD1 . TYR B  1 380 ? -12.643 -17.611 -24.872 1.00 32.65  ?  411  TYR B CD1 1 
ATOM   6645  C  CD2 . TYR B  1 380 ? -13.799 -16.251 -26.445 1.00 29.19  ?  411  TYR B CD2 1 
ATOM   6646  C  CE1 . TYR B  1 380 ? -13.518 -18.661 -25.122 1.00 28.72  ?  411  TYR B CE1 1 
ATOM   6647  C  CE2 . TYR B  1 380 ? -14.674 -17.294 -26.700 1.00 37.21  ?  411  TYR B CE2 1 
ATOM   6648  C  CZ  . TYR B  1 380 ? -14.529 -18.492 -26.026 1.00 32.39  ?  411  TYR B CZ  1 
ATOM   6649  O  OH  . TYR B  1 380 ? -15.400 -19.528 -26.292 1.00 34.19  ?  411  TYR B OH  1 
ATOM   6650  N  N   . ARG B  1 381 ? -9.832  -13.945 -22.903 1.00 26.61  ?  412  ARG B N   1 
ATOM   6651  C  CA  . ARG B  1 381 ? -8.689  -13.062 -22.701 1.00 25.60  ?  412  ARG B CA  1 
ATOM   6652  C  C   . ARG B  1 381 ? -7.459  -13.669 -23.376 1.00 25.87  ?  412  ARG B C   1 
ATOM   6653  O  O   . ARG B  1 381 ? -7.526  -14.714 -24.030 1.00 28.14  ?  412  ARG B O   1 
ATOM   6654  C  CB  . ARG B  1 381 ? -8.447  -12.827 -21.203 1.00 25.67  ?  412  ARG B CB  1 
ATOM   6655  C  CG  . ARG B  1 381 ? -9.579  -12.070 -20.483 1.00 24.41  ?  412  ARG B CG  1 
ATOM   6656  C  CD  . ARG B  1 381 ? -9.544  -10.566 -20.802 1.00 24.78  ?  412  ARG B CD  1 
ATOM   6657  N  NE  . ARG B  1 381 ? -10.581 -9.818  -20.089 1.00 21.91  ?  412  ARG B NE  1 
ATOM   6658  C  CZ  . ARG B  1 381 ? -10.773 -8.516  -20.225 1.00 25.47  ?  412  ARG B CZ  1 
ATOM   6659  N  NH1 . ARG B  1 381 ? -10.020 -7.790  -21.042 1.00 25.19  ?  412  ARG B NH1 1 
ATOM   6660  N  NH2 . ARG B  1 381 ? -11.737 -7.926  -19.520 1.00 26.43  ?  412  ARG B NH2 1 
ATOM   6661  N  N   . GLU B  1 382 ? -6.315  -13.021 -23.208 1.00 27.43  ?  413  GLU B N   1 
ATOM   6662  C  CA  . GLU B  1 382 ? -5.086  -13.493 -23.843 1.00 28.30  ?  413  GLU B CA  1 
ATOM   6663  C  C   . GLU B  1 382 ? -4.489  -14.625 -23.009 1.00 29.18  ?  413  GLU B C   1 
ATOM   6664  O  O   . GLU B  1 382 ? -3.522  -14.458 -22.263 1.00 29.26  ?  413  GLU B O   1 
ATOM   6665  C  CB  . GLU B  1 382 ? -4.103  -12.346 -24.021 1.00 28.52  ?  413  GLU B CB  1 
ATOM   6666  C  CG  . GLU B  1 382 ? -4.638  -11.180 -24.864 1.00 31.08  ?  413  GLU B CG  1 
ATOM   6667  C  CD  . GLU B  1 382 ? -5.595  -11.633 -25.953 1.00 37.40  ?  413  GLU B CD  1 
ATOM   6668  O  OE1 . GLU B  1 382 ? -5.109  -12.338 -26.866 1.00 32.87  ?  413  GLU B OE1 1 
ATOM   6669  O  OE2 . GLU B  1 382 ? -6.801  -11.257 -25.940 1.00 35.75  -1 413  GLU B OE2 1 
ATOM   6670  N  N   . GLY B  1 383 ? -5.083  -15.807 -23.140 1.00 29.11  ?  414  GLY B N   1 
ATOM   6671  C  CA  . GLY B  1 383 ? -4.554  -16.988 -22.486 1.00 29.11  ?  414  GLY B CA  1 
ATOM   6672  C  C   . GLY B  1 383 ? -5.334  -17.476 -21.295 1.00 31.32  ?  414  GLY B C   1 
ATOM   6673  O  O   . GLY B  1 383 ? -4.883  -18.422 -20.645 1.00 27.58  ?  414  GLY B O   1 
ATOM   6674  N  N   . TYR B  1 384 ? -6.492  -16.881 -20.988 1.00 29.90  ?  415  TYR B N   1 
ATOM   6675  C  CA  . TYR B  1 384 ? -7.364  -17.341 -19.908 1.00 26.47  ?  415  TYR B CA  1 
ATOM   6676  C  C   . TYR B  1 384 ? -8.761  -16.810 -20.208 1.00 25.37  ?  415  TYR B C   1 
ATOM   6677  O  O   . TYR B  1 384 ? -8.982  -16.131 -21.213 1.00 26.88  ?  415  TYR B O   1 
ATOM   6678  C  CB  . TYR B  1 384 ? -6.856  -16.901 -18.516 1.00 30.10  ?  415  TYR B CB  1 
ATOM   6679  C  CG  . TYR B  1 384 ? -6.896  -15.397 -18.310 1.00 29.01  ?  415  TYR B CG  1 
ATOM   6680  C  CD1 . TYR B  1 384 ? -5.818  -14.597 -18.696 1.00 28.11  ?  415  TYR B CD1 1 
ATOM   6681  C  CD2 . TYR B  1 384 ? -8.031  -14.774 -17.756 1.00 27.99  ?  415  TYR B CD2 1 
ATOM   6682  C  CE1 . TYR B  1 384 ? -5.849  -13.216 -18.546 1.00 26.93  ?  415  TYR B CE1 1 
ATOM   6683  C  CE2 . TYR B  1 384 ? -8.073  -13.382 -17.589 1.00 27.22  ?  415  TYR B CE2 1 
ATOM   6684  C  CZ  . TYR B  1 384 ? -6.982  -12.616 -17.994 1.00 27.51  ?  415  TYR B CZ  1 
ATOM   6685  O  OH  . TYR B  1 384 ? -7.011  -11.248 -17.868 1.00 25.74  ?  415  TYR B OH  1 
ATOM   6686  N  N   . ASN B  1 385 ? -9.710  -17.127 -19.338 1.00 27.36  ?  416  ASN B N   1 
ATOM   6687  C  CA  . ASN B  1 385 ? -11.090 -16.707 -19.526 1.00 27.30  ?  416  ASN B CA  1 
ATOM   6688  C  C   . ASN B  1 385 ? -11.622 -15.988 -18.296 1.00 26.68  ?  416  ASN B C   1 
ATOM   6689  O  O   . ASN B  1 385 ? -11.433 -16.457 -17.172 1.00 25.50  ?  416  ASN B O   1 
ATOM   6690  C  CB  . ASN B  1 385 ? -12.002 -17.891 -19.813 1.00 26.20  ?  416  ASN B CB  1 
ATOM   6691  C  CG  . ASN B  1 385 ? -11.591 -18.637 -21.049 1.00 34.71  ?  416  ASN B CG  1 
ATOM   6692  O  OD1 . ASN B  1 385 ? -11.342 -18.024 -22.096 1.00 31.61  ?  416  ASN B OD1 1 
ATOM   6693  N  ND2 . ASN B  1 385 ? -11.455 -19.960 -20.929 1.00 29.71  ?  416  ASN B ND2 1 
ATOM   6694  N  N   . ASP B  1 386 ? -12.315 -14.866 -18.524 1.00 28.32  ?  417  ASP B N   1 
ATOM   6695  C  CA  . ASP B  1 386 ? -13.083 -14.210 -17.477 1.00 26.37  ?  417  ASP B CA  1 
ATOM   6696  C  C   . ASP B  1 386 ? -14.470 -14.830 -17.486 1.00 27.32  ?  417  ASP B C   1 
ATOM   6697  O  O   . ASP B  1 386 ? -15.017 -15.117 -18.560 1.00 28.10  ?  417  ASP B O   1 
ATOM   6698  C  CB  . ASP B  1 386 ? -13.166 -12.690 -17.690 1.00 24.06  ?  417  ASP B CB  1 
ATOM   6699  C  CG  . ASP B  1 386 ? -11.843 -11.965 -17.426 1.00 26.34  ?  417  ASP B CG  1 
ATOM   6700  O  OD1 . ASP B  1 386 ? -10.991 -12.482 -16.669 1.00 25.54  ?  417  ASP B OD1 1 
ATOM   6701  O  OD2 . ASP B  1 386 ? -11.657 -10.851 -17.982 1.00 26.93  -1 417  ASP B OD2 1 
ATOM   6702  N  N   . VAL B  1 387 ? -15.039 -15.055 -16.297 1.00 24.51  ?  418  VAL B N   1 
ATOM   6703  C  CA  . VAL B  1 387 ? -16.330 -15.742 -16.194 1.00 24.56  ?  418  VAL B CA  1 
ATOM   6704  C  C   . VAL B  1 387 ? -17.237 -15.016 -15.207 1.00 25.35  ?  418  VAL B C   1 
ATOM   6705  O  O   . VAL B  1 387 ? -16.775 -14.421 -14.230 1.00 24.53  ?  418  VAL B O   1 
ATOM   6706  C  CB  . VAL B  1 387 ? -16.147 -17.218 -15.758 1.00 26.30  ?  418  VAL B CB  1 
ATOM   6707  C  CG1 . VAL B  1 387 ? -17.475 -17.977 -15.780 1.00 27.60  ?  418  VAL B CG1 1 
ATOM   6708  C  CG2 . VAL B  1 387 ? -15.114 -17.942 -16.667 1.00 26.99  ?  418  VAL B CG2 1 
ATOM   6709  N  N   . GLY B  1 388 ? -18.538 -15.047 -15.471 1.00 25.18  ?  419  GLY B N   1 
ATOM   6710  C  CA  . GLY B  1 388 ? -19.518 -14.692 -14.457 1.00 27.94  ?  419  GLY B CA  1 
ATOM   6711  C  C   . GLY B  1 388 ? -20.753 -15.558 -14.604 1.00 28.68  ?  419  GLY B C   1 
ATOM   6712  O  O   . GLY B  1 388 ? -21.124 -15.947 -15.707 1.00 27.89  ?  419  GLY B O   1 
ATOM   6713  N  N   . ALA B  1 389 ? -21.383 -15.884 -13.475 1.00 28.80  ?  420  ALA B N   1 
ATOM   6714  C  CA  . ALA B  1 389 ? -22.584 -16.714 -13.546 1.00 30.75  ?  420  ALA B CA  1 
ATOM   6715  C  C   . ALA B  1 389 ? -23.482 -16.421 -12.358 1.00 29.91  ?  420  ALA B C   1 
ATOM   6716  O  O   . ALA B  1 389 ? -23.036 -16.479 -11.212 1.00 27.50  ?  420  ALA B O   1 
ATOM   6717  C  CB  . ALA B  1 389 ? -22.236 -18.214 -13.599 1.00 27.42  ?  420  ALA B CB  1 
ATOM   6718  N  N   . ARG B  1 390 ? -24.751 -16.130 -12.622 1.00 26.27  ?  421  ARG B N   1 
ATOM   6719  C  CA  . ARG B  1 390 ? -25.677 -15.770 -11.565 1.00 27.61  ?  421  ARG B CA  1 
ATOM   6720  C  C   . ARG B  1 390 ? -26.864 -16.724 -11.495 1.00 32.54  ?  421  ARG B C   1 
ATOM   6721  O  O   . ARG B  1 390 ? -27.502 -17.021 -12.515 1.00 32.68  ?  421  ARG B O   1 
ATOM   6722  C  CB  . ARG B  1 390 ? -26.187 -14.351 -11.746 1.00 25.59  ?  421  ARG B CB  1 
ATOM   6723  C  CG  . ARG B  1 390 ? -27.070 -13.916 -10.576 1.00 28.27  ?  421  ARG B CG  1 
ATOM   6724  C  CD  . ARG B  1 390 ? -27.746 -12.567 -10.824 1.00 30.88  ?  421  ARG B CD  1 
ATOM   6725  N  NE  . ARG B  1 390 ? -28.739 -12.279 -9.798  1.00 26.96  ?  421  ARG B NE  1 
ATOM   6726  C  CZ  . ARG B  1 390 ? -29.239 -11.079 -9.547  1.00 28.96  ?  421  ARG B CZ  1 
ATOM   6727  N  NH1 . ARG B  1 390 ? -28.799 -10.006 -10.185 1.00 23.69  ?  421  ARG B NH1 1 
ATOM   6728  N  NH2 . ARG B  1 390 ? -30.216 -10.955 -8.640  1.00 26.24  ?  421  ARG B NH2 1 
ATOM   6729  N  N   . MET B  1 391 ? -27.196 -17.146 -10.280 1.00 31.27  ?  422  MET B N   1 
ATOM   6730  C  CA  . MET B  1 391 ? -28.442 -17.848 -10.015 1.00 31.89  ?  422  MET B CA  1 
ATOM   6731  C  C   . MET B  1 391 ? -29.077 -17.247 -8.771  1.00 29.93  ?  422  MET B C   1 
ATOM   6732  O  O   . MET B  1 391 ? -28.486 -17.293 -7.683  1.00 34.05  ?  422  MET B O   1 
ATOM   6733  C  CB  . MET B  1 391 ? -28.212 -19.348 -9.841  1.00 28.70  ?  422  MET B CB  1 
ATOM   6734  C  CG  . MET B  1 391 ? -29.517 -20.126 -9.727  1.00 31.08  ?  422  MET B CG  1 
ATOM   6735  S  SD  . MET B  1 391 ? -29.266 -21.891 -9.552  1.00 42.23  ?  422  MET B SD  1 
ATOM   6736  C  CE  . MET B  1 391 ? -28.890 -22.350 -11.241 1.00 39.47  ?  422  MET B CE  1 
ATOM   6737  N  N   . GLY B  1 392 ? -30.273 -16.686 -8.931  1.00 29.04  ?  423  GLY B N   1 
ATOM   6738  C  CA  . GLY B  1 392 ? -30.951 -16.071 -7.806  1.00 29.59  ?  423  GLY B CA  1 
ATOM   6739  C  C   . GLY B  1 392 ? -30.080 -14.978 -7.223  1.00 31.52  ?  423  GLY B C   1 
ATOM   6740  O  O   . GLY B  1 392 ? -29.585 -14.098 -7.943  1.00 33.10  ?  423  GLY B O   1 
ATOM   6741  N  N   . ASP B  1 393 ? -29.872 -15.033 -5.911  1.00 29.26  ?  424  ASP B N   1 
ATOM   6742  C  CA  . ASP B  1 393 ? -29.120 -14.006 -5.198  1.00 29.56  ?  424  ASP B CA  1 
ATOM   6743  C  C   . ASP B  1 393 ? -27.610 -14.164 -5.302  1.00 28.72  ?  424  ASP B C   1 
ATOM   6744  O  O   . ASP B  1 393 ? -26.885 -13.339 -4.730  1.00 27.78  ?  424  ASP B O   1 
ATOM   6745  C  CB  . ASP B  1 393 ? -29.492 -13.996 -3.712  1.00 29.29  ?  424  ASP B CB  1 
ATOM   6746  C  CG  . ASP B  1 393 ? -30.919 -13.507 -3.463  1.00 35.44  ?  424  ASP B CG  1 
ATOM   6747  O  OD1 . ASP B  1 393 ? -31.356 -12.575 -4.155  1.00 36.09  ?  424  ASP B OD1 1 
ATOM   6748  O  OD2 . ASP B  1 393 ? -31.592 -14.033 -2.555  1.00 37.98  -1 424  ASP B OD2 1 
ATOM   6749  N  N   . TRP B  1 394 ? -27.115 -15.199 -5.976  1.00 26.68  ?  425  TRP B N   1 
ATOM   6750  C  CA  . TRP B  1 394 ? -25.707 -15.570 -5.913  1.00 29.27  ?  425  TRP B CA  1 
ATOM   6751  C  C   . TRP B  1 394 ? -25.044 -15.452 -7.274  1.00 27.90  ?  425  TRP B C   1 
ATOM   6752  O  O   . TRP B  1 394 ? -25.627 -15.818 -8.293  1.00 27.21  ?  425  TRP B O   1 
ATOM   6753  C  CB  . TRP B  1 394 ? -25.550 -17.002 -5.397  1.00 32.25  ?  425  TRP B CB  1 
ATOM   6754  C  CG  . TRP B  1 394 ? -26.040 -17.126 -4.010  1.00 31.87  ?  425  TRP B CG  1 
ATOM   6755  C  CD1 . TRP B  1 394 ? -27.292 -17.511 -3.614  1.00 30.73  ?  425  TRP B CD1 1 
ATOM   6756  C  CD2 . TRP B  1 394 ? -25.306 -16.837 -2.814  1.00 31.19  ?  425  TRP B CD2 1 
ATOM   6757  N  NE1 . TRP B  1 394 ? -27.372 -17.482 -2.240  1.00 30.97  ?  425  TRP B NE1 1 
ATOM   6758  C  CE2 . TRP B  1 394 ? -26.174 -17.068 -1.727  1.00 32.44  ?  425  TRP B CE2 1 
ATOM   6759  C  CE3 . TRP B  1 394 ? -23.999 -16.410 -2.557  1.00 28.71  ?  425  TRP B CE3 1 
ATOM   6760  C  CZ2 . TRP B  1 394 ? -25.778 -16.881 -0.406  1.00 33.47  ?  425  TRP B CZ2 1 
ATOM   6761  C  CZ3 . TRP B  1 394 ? -23.604 -16.232 -1.252  1.00 33.22  ?  425  TRP B CZ3 1 
ATOM   6762  C  CH2 . TRP B  1 394 ? -24.497 -16.466 -0.187  1.00 34.43  ?  425  TRP B CH2 1 
ATOM   6763  N  N   . LYS B  1 395 ? -23.793 -15.004 -7.283  1.00 29.27  ?  426  LYS B N   1 
ATOM   6764  C  CA  . LYS B  1 395 ? -23.018 -14.938 -8.508  1.00 27.14  ?  426  LYS B CA  1 
ATOM   6765  C  C   . LYS B  1 395 ? -21.622 -15.483 -8.270  1.00 27.48  ?  426  LYS B C   1 
ATOM   6766  O  O   . LYS B  1 395 ? -21.032 -15.220 -7.224  1.00 27.50  ?  426  LYS B O   1 
ATOM   6767  C  CB  . LYS B  1 395 ? -22.926 -13.498 -9.007  1.00 31.35  ?  426  LYS B CB  1 
ATOM   6768  C  CG  . LYS B  1 395 ? -22.230 -13.394 -10.347 1.00 31.31  ?  426  LYS B CG  1 
ATOM   6769  C  CD  . LYS B  1 395 ? -21.725 -12.007 -10.612 1.00 28.97  ?  426  LYS B CD  1 
ATOM   6770  C  CE  . LYS B  1 395 ? -20.904 -11.996 -11.917 1.00 25.50  ?  426  LYS B CE  1 
ATOM   6771  N  NZ  . LYS B  1 395 ? -20.494 -10.587 -12.229 1.00 28.84  ?  426  LYS B NZ  1 
ATOM   6772  N  N   . ILE B  1 396 ? -21.070 -16.219 -9.237  1.00 26.86  ?  427  ILE B N   1 
ATOM   6773  C  CA  . ILE B  1 396 ? -19.645 -16.559 -9.197  1.00 29.26  ?  427  ILE B CA  1 
ATOM   6774  C  C   . ILE B  1 396 ? -18.920 -15.721 -10.245 1.00 27.12  ?  427  ILE B C   1 
ATOM   6775  O  O   . ILE B  1 396 ? -19.465 -15.440 -11.312 1.00 25.06  ?  427  ILE B O   1 
ATOM   6776  C  CB  . ILE B  1 396 ? -19.381 -18.068 -9.392  1.00 28.85  ?  427  ILE B CB  1 
ATOM   6777  C  CG1 . ILE B  1 396 ? -20.138 -18.631 -10.602 1.00 30.89  ?  427  ILE B CG1 1 
ATOM   6778  C  CG2 . ILE B  1 396 ? -19.802 -18.827 -8.131  1.00 31.33  ?  427  ILE B CG2 1 
ATOM   6779  C  CD1 . ILE B  1 396 ? -19.531 -19.976 -11.122 1.00 30.64  ?  427  ILE B CD1 1 
ATOM   6780  N  N   . THR B  1 397 ? -17.698 -15.297 -9.926  1.00 29.24  ?  428  THR B N   1 
ATOM   6781  C  CA  . THR B  1 397 ? -16.939 -14.452 -10.833 1.00 23.90  ?  428  THR B CA  1 
ATOM   6782  C  C   . THR B  1 397 ? -15.513 -14.950 -10.853 1.00 25.74  ?  428  THR B C   1 
ATOM   6783  O  O   . THR B  1 397 ? -14.946 -15.267 -9.801  1.00 28.75  ?  428  THR B O   1 
ATOM   6784  C  CB  . THR B  1 397 ? -16.990 -12.966 -10.413 1.00 24.83  ?  428  THR B CB  1 
ATOM   6785  O  OG1 . THR B  1 397 ? -18.334 -12.581 -10.095 1.00 27.54  ?  428  THR B OG1 1 
ATOM   6786  C  CG2 . THR B  1 397 ? -16.438 -12.035 -11.524 1.00 24.41  ?  428  THR B CG2 1 
ATOM   6787  N  N   . ARG B  1 398 ? -14.930 -15.018 -12.046 1.00 27.22  ?  429  ARG B N   1 
ATOM   6788  C  CA  . ARG B  1 398 ? -13.479 -15.118 -12.144 1.00 23.07  ?  429  ARG B CA  1 
ATOM   6789  C  C   . ARG B  1 398 ? -12.985 -14.031 -13.096 1.00 24.90  ?  429  ARG B C   1 
ATOM   6790  O  O   . ARG B  1 398 ? -13.485 -13.903 -14.220 1.00 26.38  ?  429  ARG B O   1 
ATOM   6791  C  CB  . ARG B  1 398 ? -13.034 -16.510 -12.601 1.00 26.85  ?  429  ARG B CB  1 
ATOM   6792  C  CG  . ARG B  1 398 ? -11.506 -16.674 -12.549 1.00 27.97  ?  429  ARG B CG  1 
ATOM   6793  C  CD  . ARG B  1 398 ? -11.036 -18.109 -12.725 1.00 26.37  ?  429  ARG B CD  1 
ATOM   6794  N  NE  . ARG B  1 398 ? -9.611  -18.234 -12.405 1.00 27.99  ?  429  ARG B NE  1 
ATOM   6795  C  CZ  . ARG B  1 398 ? -8.860  -19.272 -12.761 1.00 32.44  ?  429  ARG B CZ  1 
ATOM   6796  N  NH1 . ARG B  1 398 ? -9.374  -20.304 -13.408 1.00 28.54  ?  429  ARG B NH1 1 
ATOM   6797  N  NH2 . ARG B  1 398 ? -7.570  -19.290 -12.428 1.00 29.15  ?  429  ARG B NH2 1 
ATOM   6798  N  N   . MET B  1 399 ? -12.048 -13.225 -12.620 1.00 24.75  ?  430  MET B N   1 
ATOM   6799  C  CA  . MET B  1 399 ? -11.521 -12.061 -13.319 1.00 23.67  ?  430  MET B CA  1 
ATOM   6800  C  C   . MET B  1 399 ? -9.997  -12.083 -13.229 1.00 28.50  ?  430  MET B C   1 
ATOM   6801  O  O   . MET B  1 399 ? -9.447  -12.417 -12.179 1.00 27.35  ?  430  MET B O   1 
ATOM   6802  C  CB  . MET B  1 399 ? -12.112 -10.800 -12.660 1.00 27.38  ?  430  MET B CB  1 
ATOM   6803  C  CG  . MET B  1 399 ? -13.230 -10.005 -13.408 1.00 29.89  ?  430  MET B CG  1 
ATOM   6804  S  SD  . MET B  1 399 ? -13.273 -9.982  -15.198 1.00 23.29  ?  430  MET B SD  1 
ATOM   6805  C  CE  . MET B  1 399 ? -12.138 -8.574  -15.361 1.00 26.00  ?  430  MET B CE  1 
ATOM   6806  N  N   . GLY B  1 400 ? -9.315  -11.790 -14.345 1.00 25.68  ?  431  GLY B N   1 
ATOM   6807  C  CA  . GLY B  1 400 ? -7.864  -11.735 -14.375 1.00 24.62  ?  431  GLY B CA  1 
ATOM   6808  C  C   . GLY B  1 400 ? -7.169  -13.047 -14.071 1.00 29.33  ?  431  GLY B C   1 
ATOM   6809  O  O   . GLY B  1 400 ? -5.959  -13.045 -13.777 1.00 27.43  ?  431  GLY B O   1 
ATOM   6810  N  N   . ASN B  1 401 ? -7.910  -14.165 -14.132 1.00 26.11  ?  432  ASN B N   1 
ATOM   6811  C  CA  . ASN B  1 401 ? -7.467  -15.515 -13.778 1.00 29.67  ?  432  ASN B CA  1 
ATOM   6812  C  C   . ASN B  1 401 ? -7.150  -15.670 -12.284 1.00 29.47  ?  432  ASN B C   1 
ATOM   6813  O  O   . ASN B  1 401 ? -6.497  -16.635 -11.886 1.00 26.31  ?  432  ASN B O   1 
ATOM   6814  C  CB  . ASN B  1 401 ? -6.260  -15.965 -14.623 1.00 27.95  ?  432  ASN B CB  1 
ATOM   6815  C  CG  . ASN B  1 401 ? -6.419  -17.388 -15.122 1.00 31.26  ?  432  ASN B CG  1 
ATOM   6816  O  OD1 . ASN B  1 401 ? -7.548  -17.830 -15.367 1.00 30.24  ?  432  ASN B OD1 1 
ATOM   6817  N  ND2 . ASN B  1 401 ? -5.309  -18.112 -15.271 1.00 27.91  ?  432  ASN B ND2 1 
ATOM   6818  N  N   . GLU B  1 402 ? -7.645  -14.756 -11.444 1.00 24.60  ?  433  GLU B N   1 
ATOM   6819  C  CA  . GLU B  1 402 ? -7.512  -14.816 -10.004 1.00 27.25  ?  433  GLU B CA  1 
ATOM   6820  C  C   . GLU B  1 402 ? -8.344  -15.967 -9.420  1.00 24.32  ?  433  GLU B C   1 
ATOM   6821  O  O   . GLU B  1 402 ? -9.114  -16.612 -10.138 1.00 31.73  ?  433  GLU B O   1 
ATOM   6822  C  CB  . GLU B  1 402 ? -7.942  -13.466 -9.411  1.00 26.51  ?  433  GLU B CB  1 
ATOM   6823  C  CG  . GLU B  1 402 ? -6.908  -12.378 -9.632  1.00 29.32  ?  433  GLU B CG  1 
ATOM   6824  C  CD  . GLU B  1 402 ? -5.651  -12.640 -8.808  1.00 29.77  ?  433  GLU B CD  1 
ATOM   6825  O  OE1 . GLU B  1 402 ? -5.755  -12.634 -7.560  1.00 28.66  ?  433  GLU B OE1 1 
ATOM   6826  O  OE2 . GLU B  1 402 ? -4.571  -12.853 -9.411  1.00 30.35  -1 433  GLU B OE2 1 
ATOM   6827  N  N   . PRO B  1 403 ? -8.233  -16.226 -8.108  1.00 27.16  ?  434  PRO B N   1 
ATOM   6828  C  CA  . PRO B  1 403 ? -9.123  -17.213 -7.476  1.00 24.56  ?  434  PRO B CA  1 
ATOM   6829  C  C   . PRO B  1 403 ? -10.601 -16.869 -7.650  1.00 31.41  ?  434  PRO B C   1 
ATOM   6830  O  O   . PRO B  1 403 ? -11.002 -15.699 -7.723  1.00 23.56  ?  434  PRO B O   1 
ATOM   6831  C  CB  . PRO B  1 403 ? -8.704  -17.168 -6.001  1.00 29.51  ?  434  PRO B CB  1 
ATOM   6832  C  CG  . PRO B  1 403 ? -7.229  -16.844 -6.057  1.00 31.24  ?  434  PRO B CG  1 
ATOM   6833  C  CD  . PRO B  1 403 ? -7.134  -15.823 -7.195  1.00 25.00  ?  434  PRO B CD  1 
ATOM   6834  N  N   . TRP B  1 404 ? -11.420 -17.917 -7.695  1.00 25.13  ?  435  TRP B N   1 
ATOM   6835  C  CA  . TRP B  1 404 ? -12.849 -17.746 -7.892  1.00 27.41  ?  435  TRP B CA  1 
ATOM   6836  C  C   . TRP B  1 404 ? -13.496 -16.960 -6.758  1.00 28.15  ?  435  TRP B C   1 
ATOM   6837  O  O   . TRP B  1 404 ? -13.106 -17.044 -5.594  1.00 31.00  ?  435  TRP B O   1 
ATOM   6838  C  CB  . TRP B  1 404 ? -13.535 -19.110 -8.012  1.00 28.86  ?  435  TRP B CB  1 
ATOM   6839  C  CG  . TRP B  1 404 ? -13.482 -19.675 -9.392  1.00 28.32  ?  435  TRP B CG  1 
ATOM   6840  C  CD1 . TRP B  1 404 ? -12.566 -20.562 -9.884  1.00 29.82  ?  435  TRP B CD1 1 
ATOM   6841  C  CD2 . TRP B  1 404 ? -14.392 -19.400 -10.458 1.00 31.96  ?  435  TRP B CD2 1 
ATOM   6842  N  NE1 . TRP B  1 404 ? -12.855 -20.859 -11.197 1.00 29.26  ?  435  TRP B NE1 1 
ATOM   6843  C  CE2 . TRP B  1 404 ? -13.967 -20.157 -11.578 1.00 29.57  ?  435  TRP B CE2 1 
ATOM   6844  C  CE3 . TRP B  1 404 ? -15.524 -18.590 -10.578 1.00 29.70  ?  435  TRP B CE3 1 
ATOM   6845  C  CZ2 . TRP B  1 404 ? -14.636 -20.128 -12.802 1.00 26.37  ?  435  TRP B CZ2 1 
ATOM   6846  C  CZ3 . TRP B  1 404 ? -16.200 -18.560 -11.812 1.00 28.85  ?  435  TRP B CZ3 1 
ATOM   6847  C  CH2 . TRP B  1 404 ? -15.750 -19.332 -12.896 1.00 29.49  ?  435  TRP B CH2 1 
ATOM   6848  N  N   . ARG B  1 405 ? -14.543 -16.232 -7.105  1.00 27.19  ?  436  ARG B N   1 
ATOM   6849  C  CA  . ARG B  1 405 ? -15.290 -15.448 -6.148  1.00 27.76  ?  436  ARG B CA  1 
ATOM   6850  C  C   . ARG B  1 405 ? -16.725 -15.937 -6.134  1.00 27.71  ?  436  ARG B C   1 
ATOM   6851  O  O   . ARG B  1 405 ? -17.270 -16.372 -7.155  1.00 31.58  ?  436  ARG B O   1 
ATOM   6852  C  CB  . ARG B  1 405 ? -15.209 -13.948 -6.473  1.00 27.93  ?  436  ARG B CB  1 
ATOM   6853  C  CG  . ARG B  1 405 ? -13.738 -13.462 -6.502  1.00 24.64  ?  436  ARG B CG  1 
ATOM   6854  C  CD  . ARG B  1 405 ? -13.631 -12.038 -7.000  1.00 30.34  ?  436  ARG B CD  1 
ATOM   6855  N  NE  . ARG B  1 405 ? -14.170 -11.056 -6.060  1.00 24.96  ?  436  ARG B NE  1 
ATOM   6856  C  CZ  . ARG B  1 405 ? -13.472 -10.516 -5.080  1.00 29.29  ?  436  ARG B CZ  1 
ATOM   6857  N  NH1 . ARG B  1 405 ? -12.229 -10.902 -4.827  1.00 26.54  ?  436  ARG B NH1 1 
ATOM   6858  N  NH2 . ARG B  1 405 ? -14.032 -9.569  -4.335  1.00 26.02  ?  436  ARG B NH2 1 
ATOM   6859  N  N   . LEU B  1 406 ? -17.308 -15.875 -4.948  1.00 26.26  ?  437  LEU B N   1 
ATOM   6860  C  CA  . LEU B  1 406 ? -18.717 -16.125 -4.713  1.00 29.15  ?  437  LEU B CA  1 
ATOM   6861  C  C   . LEU B  1 406 ? -19.274 -14.900 -4.001  1.00 26.70  ?  437  LEU B C   1 
ATOM   6862  O  O   . LEU B  1 406 ? -18.763 -14.506 -2.942  1.00 26.48  ?  437  LEU B O   1 
ATOM   6863  C  CB  . LEU B  1 406 ? -18.929 -17.386 -3.866  1.00 29.91  ?  437  LEU B CB  1 
ATOM   6864  C  CG  . LEU B  1 406 ? -20.402 -17.620 -3.481  1.00 29.18  ?  437  LEU B CG  1 
ATOM   6865  C  CD1 . LEU B  1 406 ? -21.271 -18.001 -4.722  1.00 25.58  ?  437  LEU B CD1 1 
ATOM   6866  C  CD2 . LEU B  1 406 ? -20.544 -18.669 -2.338  1.00 31.67  ?  437  LEU B CD2 1 
ATOM   6867  N  N   . HIS B  1 407 ? -20.306 -14.299 -4.587  1.00 27.19  ?  438  HIS B N   1 
ATOM   6868  C  CA  . HIS B  1 407 ? -20.906 -13.094 -4.043  1.00 28.10  ?  438  HIS B CA  1 
ATOM   6869  C  C   . HIS B  1 407 ? -22.391 -13.306 -3.850  1.00 26.21  ?  438  HIS B C   1 
ATOM   6870  O  O   . HIS B  1 407 ? -23.047 -13.940 -4.678  1.00 26.87  ?  438  HIS B O   1 
ATOM   6871  C  CB  . HIS B  1 407 ? -20.656 -11.886 -4.968  1.00 25.74  ?  438  HIS B CB  1 
ATOM   6872  C  CG  . HIS B  1 407 ? -19.222 -11.495 -5.018  1.00 25.20  ?  438  HIS B CG  1 
ATOM   6873  N  ND1 . HIS B  1 407 ? -18.574 -10.969 -3.924  1.00 24.33  ?  438  HIS B ND1 1 
ATOM   6874  C  CD2 . HIS B  1 407 ? -18.288 -11.615 -5.991  1.00 26.49  ?  438  HIS B CD2 1 
ATOM   6875  C  CE1 . HIS B  1 407 ? -17.300 -10.772 -4.223  1.00 27.07  ?  438  HIS B CE1 1 
ATOM   6876  N  NE2 . HIS B  1 407 ? -17.100 -11.148 -5.471  1.00 23.69  ?  438  HIS B NE2 1 
ATOM   6877  N  N   . ASN B  1 408 ? -22.911 -12.804 -2.737  1.00 30.22  ?  439  ASN B N   1 
ATOM   6878  C  CA  . ASN B  1 408 ? -24.345 -12.556 -2.660  1.00 29.77  ?  439  ASN B CA  1 
ATOM   6879  C  C   . ASN B  1 408 ? -24.551 -11.222 -3.348  1.00 29.28  ?  439  ASN B C   1 
ATOM   6880  O  O   . ASN B  1 408 ? -24.336 -10.167 -2.744  1.00 30.52  ?  439  ASN B O   1 
ATOM   6881  C  CB  . ASN B  1 408 ? -24.855 -12.524 -1.222  1.00 27.63  ?  439  ASN B CB  1 
ATOM   6882  C  CG  . ASN B  1 408 ? -26.366 -12.447 -1.174  1.00 33.98  ?  439  ASN B CG  1 
ATOM   6883  O  OD1 . ASN B  1 408 ? -26.955 -11.599 -1.842  1.00 29.15  ?  439  ASN B OD1 1 
ATOM   6884  N  ND2 . ASN B  1 408 ? -27.006 -13.343 -0.423  1.00 33.35  ?  439  ASN B ND2 1 
ATOM   6885  N  N   . ILE B  1 409 ? -24.946 -11.271 -4.622  1.00 29.54  ?  440  ILE B N   1 
ATOM   6886  C  CA  . ILE B  1 409 ? -24.980 -10.070 -5.445  1.00 26.23  ?  440  ILE B CA  1 
ATOM   6887  C  C   . ILE B  1 409 ? -26.130 -9.168  -5.024  1.00 26.88  ?  440  ILE B C   1 
ATOM   6888  O  O   . ILE B  1 409 ? -26.124 -7.973  -5.314  1.00 28.84  ?  440  ILE B O   1 
ATOM   6889  C  CB  . ILE B  1 409 ? -25.070 -10.452 -6.934  1.00 27.75  ?  440  ILE B CB  1 
ATOM   6890  C  CG1 . ILE B  1 409 ? -24.514 -9.338  -7.848  1.00 23.69  ?  440  ILE B CG1 1 
ATOM   6891  C  CG2 . ILE B  1 409 ? -26.517 -10.853 -7.328  1.00 24.86  ?  440  ILE B CG2 1 
ATOM   6892  C  CD1 . ILE B  1 409 ? -23.034 -9.094  -7.676  1.00 26.32  ?  440  ILE B CD1 1 
ATOM   6893  N  N   . THR B  1 410 ? -27.124 -9.715  -4.336  1.00 23.11  ?  441  THR B N   1 
ATOM   6894  C  CA  . THR B  1 410 ? -28.185 -8.874  -3.802  1.00 29.35  ?  441  THR B CA  1 
ATOM   6895  C  C   . THR B  1 410 ? -27.696 -8.046  -2.624  1.00 27.74  ?  441  THR B C   1 
ATOM   6896  O  O   . THR B  1 410 ? -28.041 -6.865  -2.501  1.00 28.81  ?  441  THR B O   1 
ATOM   6897  C  CB  . THR B  1 410 ? -29.367 -9.757  -3.416  1.00 29.84  ?  441  THR B CB  1 
ATOM   6898  O  OG1 . THR B  1 410 ? -29.792 -10.467 -4.585  1.00 29.81  ?  441  THR B OG1 1 
ATOM   6899  C  CG2 . THR B  1 410 ? -30.507 -8.926  -2.864  1.00 28.61  ?  441  THR B CG2 1 
ATOM   6900  N  N   A GLN B  1 411 ? -26.902 -8.650  -1.733  0.50 30.22  ?  442  GLN B N   1 
ATOM   6901  N  N   B GLN B  1 411 ? -26.879 -8.635  -1.758  0.50 30.21  ?  442  GLN B N   1 
ATOM   6902  C  CA  A GLN B  1 411 ? -26.341 -7.938  -0.589  0.50 30.87  ?  442  GLN B CA  1 
ATOM   6903  C  CA  B GLN B  1 411 ? -26.351 -7.934  -0.599  0.50 30.86  ?  442  GLN B CA  1 
ATOM   6904  C  C   A GLN B  1 411 ? -25.076 -7.158  -0.937  0.50 32.27  ?  442  GLN B C   1 
ATOM   6905  C  C   B GLN B  1 411 ? -25.021 -7.240  -0.876  0.50 32.27  ?  442  GLN B C   1 
ATOM   6906  O  O   A GLN B  1 411 ? -24.756 -6.178  -0.255  0.50 29.80  ?  442  GLN B O   1 
ATOM   6907  O  O   B GLN B  1 411 ? -24.602 -6.391  -0.083  0.50 29.93  ?  442  GLN B O   1 
ATOM   6908  C  CB  A GLN B  1 411 ? -26.019 -8.922  0.549   0.50 33.40  ?  442  GLN B CB  1 
ATOM   6909  C  CB  B GLN B  1 411 ? -26.189 -8.919  0.566   0.50 33.49  ?  442  GLN B CB  1 
ATOM   6910  C  CG  A GLN B  1 411 ? -27.242 -9.534  1.230   0.50 36.53  ?  442  GLN B CG  1 
ATOM   6911  C  CG  B GLN B  1 411 ? -27.522 -9.459  1.081   0.50 36.28  ?  442  GLN B CG  1 
ATOM   6912  C  CD  A GLN B  1 411 ? -26.912 -10.746 2.091   0.50 36.61  ?  442  GLN B CD  1 
ATOM   6913  C  CD  B GLN B  1 411 ? -28.386 -8.374  1.683   0.50 34.98  ?  442  GLN B CD  1 
ATOM   6914  O  OE1 A GLN B  1 411 ? -25.745 -11.055 2.344   0.50 40.58  ?  442  GLN B OE1 1 
ATOM   6915  O  OE1 B GLN B  1 411 ? -27.969 -7.682  2.607   0.50 38.81  ?  442  GLN B OE1 1 
ATOM   6916  N  NE2 A GLN B  1 411 ? -27.951 -11.448 2.537   0.50 38.50  ?  442  GLN B NE2 1 
ATOM   6917  N  NE2 B GLN B  1 411 ? -29.598 -8.218  1.159   0.50 39.51  ?  442  GLN B NE2 1 
ATOM   6918  N  N   . ASP B  1 412 ? -24.358 -7.563  -1.985  1.00 26.95  ?  443  ASP B N   1 
ATOM   6919  C  CA  . ASP B  1 412 ? -23.005 -7.088  -2.247  1.00 32.37  ?  443  ASP B CA  1 
ATOM   6920  C  C   . ASP B  1 412 ? -22.913 -6.828  -3.754  1.00 27.02  ?  443  ASP B C   1 
ATOM   6921  O  O   . ASP B  1 412 ? -22.213 -7.492  -4.500  1.00 27.08  ?  443  ASP B O   1 
ATOM   6922  C  CB  . ASP B  1 412 ? -21.985 -8.114  -1.722  1.00 26.06  ?  443  ASP B CB  1 
ATOM   6923  C  CG  . ASP B  1 412 ? -20.551 -7.821  -2.119  1.00 28.37  ?  443  ASP B CG  1 
ATOM   6924  O  OD1 . ASP B  1 412 ? -20.168 -6.641  -2.254  1.00 27.63  ?  443  ASP B OD1 1 
ATOM   6925  O  OD2 . ASP B  1 412 ? -19.789 -8.806  -2.279  1.00 27.98  -1 443  ASP B OD2 1 
ATOM   6926  N  N   . ILE B  1 413 ? -23.673 -5.836  -4.228  1.00 25.86  ?  444  ILE B N   1 
ATOM   6927  C  CA  . ILE B  1 413 ? -23.773 -5.597  -5.666  1.00 24.75  ?  444  ILE B CA  1 
ATOM   6928  C  C   . ILE B  1 413 ? -22.436 -5.175  -6.275  1.00 24.29  ?  444  ILE B C   1 
ATOM   6929  O  O   . ILE B  1 413 ? -22.212 -5.377  -7.473  1.00 24.75  ?  444  ILE B O   1 
ATOM   6930  C  CB  . ILE B  1 413 ? -24.857 -4.545  -5.952  1.00 27.63  ?  444  ILE B CB  1 
ATOM   6931  C  CG1 . ILE B  1 413 ? -25.209 -4.536  -7.447  1.00 24.17  ?  444  ILE B CG1 1 
ATOM   6932  C  CG2 . ILE B  1 413 ? -24.406 -3.149  -5.444  1.00 27.49  ?  444  ILE B CG2 1 
ATOM   6933  C  CD1 . ILE B  1 413 ? -26.405 -3.612  -7.762  1.00 28.06  ?  444  ILE B CD1 1 
ATOM   6934  N  N   . GLY B  1 414 ? -21.537 -4.613  -5.474  1.00 24.60  ?  445  GLY B N   1 
ATOM   6935  C  CA  . GLY B  1 414 ? -20.211 -4.213  -5.899  1.00 23.12  ?  445  GLY B CA  1 
ATOM   6936  C  C   . GLY B  1 414 ? -19.185 -5.320  -5.943  1.00 25.33  ?  445  GLY B C   1 
ATOM   6937  O  O   . GLY B  1 414 ? -18.032 -5.050  -6.279  1.00 24.16  ?  445  GLY B O   1 
ATOM   6938  N  N   . GLU B  1 415 ? -19.558 -6.553  -5.578  1.00 24.59  ?  446  GLU B N   1 
ATOM   6939  C  CA  . GLU B  1 415 ? -18.659 -7.705  -5.622  1.00 23.81  ?  446  GLU B CA  1 
ATOM   6940  C  C   . GLU B  1 415 ? -17.389 -7.473  -4.792  1.00 25.63  ?  446  GLU B C   1 
ATOM   6941  O  O   . GLU B  1 415 ? -16.271 -7.763  -5.226  1.00 22.20  ?  446  GLU B O   1 
ATOM   6942  C  CB  . GLU B  1 415 ? -18.319 -8.084  -7.071  1.00 24.11  ?  446  GLU B CB  1 
ATOM   6943  C  CG  . GLU B  1 415 ? -19.549 -8.634  -7.839  1.00 25.08  ?  446  GLU B CG  1 
ATOM   6944  C  CD  . GLU B  1 415 ? -19.298 -8.744  -9.331  1.00 24.48  ?  446  GLU B CD  1 
ATOM   6945  O  OE1 . GLU B  1 415 ? -19.261 -7.681  -9.974  1.00 24.12  ?  446  GLU B OE1 1 
ATOM   6946  O  OE2 . GLU B  1 415 ? -19.141 -9.875  -9.852  1.00 25.08  -1 446  GLU B OE2 1 
ATOM   6947  N  N   . LYS B  1 416 ? -17.575 -6.989  -3.566  1.00 22.86  ?  447  LYS B N   1 
ATOM   6948  C  CA  . LYS B  1 416 ? -16.449 -6.661  -2.683  1.00 24.75  ?  447  LYS B CA  1 
ATOM   6949  C  C   . LYS B  1 416 ? -16.091 -7.759  -1.695  1.00 25.33  ?  447  LYS B C   1 
ATOM   6950  O  O   . LYS B  1 416 ? -14.926 -7.832  -1.268  1.00 28.14  ?  447  LYS B O   1 
ATOM   6951  C  CB  . LYS B  1 416 ? -16.757 -5.386  -1.894  1.00 27.87  ?  447  LYS B CB  1 
ATOM   6952  C  CG  . LYS B  1 416 ? -16.990 -4.189  -2.778  1.00 25.55  ?  447  LYS B CG  1 
ATOM   6953  C  CD  . LYS B  1 416 ? -17.312 -2.968  -1.944  1.00 33.50  ?  447  LYS B CD  1 
ATOM   6954  C  CE  . LYS B  1 416 ? -16.983 -1.702  -2.715  1.00 38.26  ?  447  LYS B CE  1 
ATOM   6955  N  NZ  . LYS B  1 416 ? -17.314 -0.472  -1.957  1.00 45.59  ?  447  LYS B NZ  1 
ATOM   6956  N  N   . LYS B  1 417 ? -17.050 -8.606  -1.307  1.00 25.55  ?  448  LYS B N   1 
ATOM   6957  C  CA  . LYS B  1 417 ? -16.873 -9.586  -0.226  1.00 28.16  ?  448  LYS B CA  1 
ATOM   6958  C  C   . LYS B  1 417 ? -16.911 -11.001 -0.788  1.00 28.82  ?  448  LYS B C   1 
ATOM   6959  O  O   . LYS B  1 417 ? -17.988 -11.532 -1.065  1.00 28.39  ?  448  LYS B O   1 
ATOM   6960  C  CB  . LYS B  1 417 ? -17.961 -9.421  0.821   1.00 29.24  ?  448  LYS B CB  1 
ATOM   6961  C  CG  . LYS B  1 417 ? -18.158 -7.991  1.265   1.00 30.91  ?  448  LYS B CG  1 
ATOM   6962  C  CD  . LYS B  1 417 ? -16.872 -7.445  1.873   1.00 32.55  ?  448  LYS B CD  1 
ATOM   6963  C  CE  . LYS B  1 417 ? -16.936 -5.917  1.994   1.00 31.76  ?  448  LYS B CE  1 
ATOM   6964  N  NZ  . LYS B  1 417 ? -15.711 -5.439  2.695   1.00 39.26  ?  448  LYS B NZ  1 
ATOM   6965  N  N   . ASN B  1 418 ? -15.748 -11.624 -0.933  1.00 23.80  ?  449  ASN B N   1 
ATOM   6966  C  CA  . ASN B  1 418 ? -15.698 -12.967 -1.500  1.00 26.94  ?  449  ASN B CA  1 
ATOM   6967  C  C   . ASN B  1 418 ? -16.111 -13.992 -0.437  1.00 27.75  ?  449  ASN B C   1 
ATOM   6968  O  O   . ASN B  1 418 ? -15.454 -14.113 0.603   1.00 29.55  ?  449  ASN B O   1 
ATOM   6969  C  CB  . ASN B  1 418 ? -14.298 -13.263 -2.031  1.00 26.95  ?  449  ASN B CB  1 
ATOM   6970  C  CG  . ASN B  1 418 ? -14.225 -14.594 -2.747  1.00 27.09  ?  449  ASN B CG  1 
ATOM   6971  O  OD1 . ASN B  1 418 ? -15.232 -15.290 -2.876  1.00 29.13  ?  449  ASN B OD1 1 
ATOM   6972  N  ND2 . ASN B  1 418 ? -13.044 -14.941 -3.240  1.00 32.16  ?  449  ASN B ND2 1 
ATOM   6973  N  N   . LEU B  1 419 ? -17.181 -14.733 -0.703  1.00 30.56  ?  450  LEU B N   1 
ATOM   6974  C  CA  . LEU B  1 419 ? -17.713 -15.732 0.226   1.00 31.16  ?  450  LEU B CA  1 
ATOM   6975  C  C   . LEU B  1 419 ? -17.335 -17.155 -0.164  1.00 33.53  ?  450  LEU B C   1 
ATOM   6976  O  O   . LEU B  1 419 ? -17.904 -18.110 0.384   1.00 33.10  ?  450  LEU B O   1 
ATOM   6977  C  CB  . LEU B  1 419 ? -19.237 -15.620 0.312   1.00 31.35  ?  450  LEU B CB  1 
ATOM   6978  C  CG  . LEU B  1 419 ? -19.725 -14.244 0.778   1.00 29.92  ?  450  LEU B CG  1 
ATOM   6979  C  CD1 . LEU B  1 419 ? -21.241 -14.195 0.774   1.00 30.90  ?  450  LEU B CD1 1 
ATOM   6980  C  CD2 . LEU B  1 419 ? -19.162 -13.922 2.150   1.00 34.36  ?  450  LEU B CD2 1 
ATOM   6981  N  N   . ALA B  1 420 ? -16.395 -17.312 -1.101  1.00 30.25  ?  451  ALA B N   1 
ATOM   6982  C  CA  . ALA B  1 420 ? -16.024 -18.638 -1.580  1.00 32.31  ?  451  ALA B CA  1 
ATOM   6983  C  C   . ALA B  1 420 ? -15.548 -19.529 -0.441  1.00 37.08  ?  451  ALA B C   1 
ATOM   6984  O  O   . ALA B  1 420 ? -15.863 -20.728 -0.405  1.00 37.00  ?  451  ALA B O   1 
ATOM   6985  C  CB  . ALA B  1 420 ? -14.947 -18.518 -2.660  1.00 31.35  ?  451  ALA B CB  1 
ATOM   6986  N  N   . GLY B  1 421 ? -14.788 -18.959 0.500   1.00 39.61  ?  452  GLY B N   1 
ATOM   6987  C  CA  . GLY B  1 421 ? -14.334 -19.728 1.646   1.00 42.12  ?  452  GLY B CA  1 
ATOM   6988  C  C   . GLY B  1 421 ? -15.458 -20.135 2.576   1.00 43.46  ?  452  GLY B C   1 
ATOM   6989  O  O   . GLY B  1 421 ? -15.387 -21.193 3.212   1.00 45.80  ?  452  GLY B O   1 
ATOM   6990  N  N   . ARG B  1 422 ? -16.508 -19.315 2.664   1.00 38.73  ?  453  ARG B N   1 
ATOM   6991  C  CA  . ARG B  1 422 ? -17.585 -19.557 3.613   1.00 39.93  ?  453  ARG B CA  1 
ATOM   6992  C  C   . ARG B  1 422 ? -18.575 -20.591 3.097   1.00 44.11  ?  453  ARG B C   1 
ATOM   6993  O  O   . ARG B  1 422 ? -19.146 -21.347 3.890   1.00 42.71  ?  453  ARG B O   1 
ATOM   6994  C  CB  . ARG B  1 422 ? -18.329 -18.252 3.915   1.00 45.27  ?  453  ARG B CB  1 
ATOM   6995  C  CG  . ARG B  1 422 ? -19.269 -18.303 5.116   1.00 47.11  ?  453  ARG B CG  1 
ATOM   6996  C  CD  . ARG B  1 422 ? -19.262 -16.954 5.833   1.00 50.98  ?  453  ARG B CD  1 
ATOM   6997  N  NE  . ARG B  1 422 ? -17.894 -16.460 5.935   1.00 64.54  ?  453  ARG B NE  1 
ATOM   6998  C  CZ  . ARG B  1 422 ? -17.531 -15.192 5.783   1.00 64.22  ?  453  ARG B CZ  1 
ATOM   6999  N  NH1 . ARG B  1 422 ? -18.420 -14.211 5.784   1.00 65.72  ?  453  ARG B NH1 1 
ATOM   7000  N  NH2 . ARG B  1 422 ? -16.242 -14.900 5.622   1.00 63.95  ?  453  ARG B NH2 1 
ATOM   7001  N  N   . TYR B  1 423 ? -18.817 -20.626 1.785   1.00 46.32  ?  454  TYR B N   1 
ATOM   7002  C  CA  . TYR B  1 423 ? -19.800 -21.525 1.178   1.00 38.24  ?  454  TYR B CA  1 
ATOM   7003  C  C   . TYR B  1 423 ? -19.167 -22.259 -0.001  1.00 38.64  ?  454  TYR B C   1 
ATOM   7004  O  O   . TYR B  1 423 ? -19.544 -22.050 -1.163  1.00 34.88  ?  454  TYR B O   1 
ATOM   7005  C  CB  . TYR B  1 423 ? -21.043 -20.744 0.755   1.00 42.24  ?  454  TYR B CB  1 
ATOM   7006  C  CG  . TYR B  1 423 ? -21.601 -19.879 1.869   1.00 44.05  ?  454  TYR B CG  1 
ATOM   7007  C  CD1 . TYR B  1 423 ? -21.974 -20.443 3.084   1.00 44.95  ?  454  TYR B CD1 1 
ATOM   7008  C  CD2 . TYR B  1 423 ? -21.745 -18.509 1.714   1.00 38.66  ?  454  TYR B CD2 1 
ATOM   7009  C  CE1 . TYR B  1 423 ? -22.482 -19.669 4.108   1.00 47.90  ?  454  TYR B CE1 1 
ATOM   7010  C  CE2 . TYR B  1 423 ? -22.258 -17.720 2.734   1.00 43.23  ?  454  TYR B CE2 1 
ATOM   7011  C  CZ  . TYR B  1 423 ? -22.617 -18.306 3.935   1.00 52.49  ?  454  TYR B CZ  1 
ATOM   7012  O  OH  . TYR B  1 423 ? -23.112 -17.539 4.967   1.00 47.59  ?  454  TYR B OH  1 
ATOM   7013  N  N   . PRO B  1 424 ? -18.196 -23.134 0.265   1.00 39.40  ?  455  PRO B N   1 
ATOM   7014  C  CA  . PRO B  1 424 ? -17.540 -23.833 -0.849  1.00 42.01  ?  455  PRO B CA  1 
ATOM   7015  C  C   . PRO B  1 424 ? -18.493 -24.722 -1.622  1.00 41.08  ?  455  PRO B C   1 
ATOM   7016  O  O   . PRO B  1 424 ? -18.321 -24.873 -2.833  1.00 39.05  ?  455  PRO B O   1 
ATOM   7017  C  CB  . PRO B  1 424 ? -16.435 -24.645 -0.154  1.00 42.63  ?  455  PRO B CB  1 
ATOM   7018  C  CG  . PRO B  1 424 ? -16.901 -24.777 1.249   1.00 42.77  ?  455  PRO B CG  1 
ATOM   7019  C  CD  . PRO B  1 424 ? -17.578 -23.483 1.557   1.00 41.99  ?  455  PRO B CD  1 
ATOM   7020  N  N   . ASP B  1 425 ? -19.510 -25.292 -0.965  1.00 37.55  ?  456  ASP B N   1 
ATOM   7021  C  CA  . ASP B  1 425 ? -20.455 -26.147 -1.677  1.00 40.96  ?  456  ASP B CA  1 
ATOM   7022  C  C   . ASP B  1 425 ? -21.238 -25.366 -2.724  1.00 39.12  ?  456  ASP B C   1 
ATOM   7023  O  O   . ASP B  1 425 ? -21.454 -25.857 -3.840  1.00 43.67  ?  456  ASP B O   1 
ATOM   7024  C  CB  . ASP B  1 425 ? -21.425 -26.802 -0.700  1.00 40.74  ?  456  ASP B CB  1 
ATOM   7025  C  CG  . ASP B  1 425 ? -20.771 -27.858 0.150   1.00 47.20  ?  456  ASP B CG  1 
ATOM   7026  O  OD1 . ASP B  1 425 ? -19.602 -28.220 -0.129  1.00 51.61  ?  456  ASP B OD1 1 
ATOM   7027  O  OD2 . ASP B  1 425 ? -21.438 -28.326 1.100   1.00 44.72  -1 456  ASP B OD2 1 
ATOM   7028  N  N   . ARG B  1 426 ? -21.720 -24.171 -2.375  1.00 41.39  ?  457  ARG B N   1 
ATOM   7029  C  CA  . ARG B  1 426 ? -22.447 -23.386 -3.370  1.00 39.40  ?  457  ARG B CA  1 
ATOM   7030  C  C   . ARG B  1 426 ? -21.546 -23.021 -4.543  1.00 39.18  ?  457  ARG B C   1 
ATOM   7031  O  O   . ARG B  1 426 ? -21.963 -23.100 -5.706  1.00 35.13  ?  457  ARG B O   1 
ATOM   7032  C  CB  . ARG B  1 426 ? -23.033 -22.120 -2.747  1.00 39.63  ?  457  ARG B CB  1 
ATOM   7033  C  CG  . ARG B  1 426 ? -24.031 -21.417 -3.685  1.00 38.76  ?  457  ARG B CG  1 
ATOM   7034  C  CD  . ARG B  1 426 ? -24.693 -20.251 -3.006  1.00 40.02  ?  457  ARG B CD  1 
ATOM   7035  N  NE  . ARG B  1 426 ? -25.603 -20.670 -1.951  1.00 42.04  ?  457  ARG B NE  1 
ATOM   7036  C  CZ  . ARG B  1 426 ? -26.869 -21.017 -2.138  1.00 43.85  ?  457  ARG B CZ  1 
ATOM   7037  N  NH1 . ARG B  1 426 ? -27.425 -21.000 -3.341  1.00 38.11  ?  457  ARG B NH1 1 
ATOM   7038  N  NH2 . ARG B  1 426 ? -27.599 -21.395 -1.088  1.00 44.99  ?  457  ARG B NH2 1 
ATOM   7039  N  N   . LEU B  1 427 ? -20.311 -22.603 -4.250  1.00 34.39  ?  458  LEU B N   1 
ATOM   7040  C  CA  . LEU B  1 427 ? -19.358 -22.237 -5.293  1.00 35.20  ?  458  LEU B CA  1 
ATOM   7041  C  C   . LEU B  1 427 ? -19.143 -23.388 -6.268  1.00 37.91  ?  458  LEU B C   1 
ATOM   7042  O  O   . LEU B  1 427 ? -19.305 -23.229 -7.487  1.00 33.96  ?  458  LEU B O   1 
ATOM   7043  C  CB  . LEU B  1 427 ? -18.032 -21.816 -4.648  1.00 34.54  ?  458  LEU B CB  1 
ATOM   7044  C  CG  . LEU B  1 427 ? -16.838 -21.675 -5.603  1.00 36.71  ?  458  LEU B CG  1 
ATOM   7045  C  CD1 . LEU B  1 427 ? -17.016 -20.449 -6.464  1.00 34.89  ?  458  LEU B CD1 1 
ATOM   7046  C  CD2 . LEU B  1 427 ? -15.521 -21.588 -4.842  1.00 37.52  ?  458  LEU B CD2 1 
ATOM   7047  N  N   . LYS B  1 428 ? -18.822 -24.573 -5.737  1.00 35.98  ?  459  LYS B N   1 
ATOM   7048  C  CA  . LYS B  1 428 ? -18.585 -25.742 -6.581  1.00 39.76  ?  459  LYS B CA  1 
ATOM   7049  C  C   . LYS B  1 428 ? -19.825 -26.148 -7.365  1.00 35.56  ?  459  LYS B C   1 
ATOM   7050  O  O   . LYS B  1 428 ? -19.710 -26.608 -8.506  1.00 39.95  ?  459  LYS B O   1 
ATOM   7051  C  CB  . LYS B  1 428 ? -18.086 -26.909 -5.733  1.00 38.04  ?  459  LYS B CB  1 
ATOM   7052  C  CG  . LYS B  1 428 ? -16.924 -26.539 -4.847  1.00 45.29  ?  459  LYS B CG  1 
ATOM   7053  C  CD  . LYS B  1 428 ? -15.703 -27.391 -5.116  1.00 48.86  ?  459  LYS B CD  1 
ATOM   7054  C  CE  . LYS B  1 428 ? -14.571 -26.997 -4.181  1.00 46.84  ?  459  LYS B CE  1 
ATOM   7055  N  NZ  . LYS B  1 428 ? -13.420 -27.913 -4.291  1.00 53.20  ?  459  LYS B NZ  1 
ATOM   7056  N  N   . GLU B  1 429 ? -21.013 -26.009 -6.767  1.00 34.59  ?  460  GLU B N   1 
ATOM   7057  C  CA  . GLU B  1 429 ? -22.261 -26.269 -7.491  1.00 40.85  ?  460  GLU B CA  1 
ATOM   7058  C  C   . GLU B  1 429 ? -22.395 -25.346 -8.699  1.00 40.74  ?  460  GLU B C   1 
ATOM   7059  O  O   . GLU B  1 429 ? -22.747 -25.782 -9.808  1.00 35.18  ?  460  GLU B O   1 
ATOM   7060  C  CB  . GLU B  1 429 ? -23.451 -26.061 -6.554  1.00 41.52  ?  460  GLU B CB  1 
ATOM   7061  C  CG  . GLU B  1 429 ? -23.991 -27.291 -5.848  1.00 50.92  ?  460  GLU B CG  1 
ATOM   7062  C  CD  . GLU B  1 429 ? -24.821 -26.921 -4.613  1.00 56.46  ?  460  GLU B CD  1 
ATOM   7063  O  OE1 . GLU B  1 429 ? -25.516 -25.874 -4.626  1.00 52.89  ?  460  GLU B OE1 1 
ATOM   7064  O  OE2 . GLU B  1 429 ? -24.756 -27.670 -3.614  1.00 64.13  -1 460  GLU B OE2 1 
ATOM   7065  N  N   . MET B  1 430 ? -22.168 -24.046 -8.487  1.00 35.13  ?  461  MET B N   1 
ATOM   7066  C  CA  . MET B  1 430 ? -22.300 -23.098 -9.592  1.00 37.75  ?  461  MET B CA  1 
ATOM   7067  C  C   . MET B  1 430 ? -21.207 -23.323 -10.619 1.00 31.78  ?  461  MET B C   1 
ATOM   7068  O  O   . MET B  1 430 ? -21.455 -23.234 -11.825 1.00 37.11  ?  461  MET B O   1 
ATOM   7069  C  CB  . MET B  1 430 ? -22.275 -21.669 -9.047  1.00 34.65  ?  461  MET B CB  1 
ATOM   7070  C  CG  . MET B  1 430 ? -23.278 -21.486 -7.934  1.00 35.89  ?  461  MET B CG  1 
ATOM   7071  S  SD  . MET B  1 430 ? -23.754 -19.810 -7.487  1.00 35.60  ?  461  MET B SD  1 
ATOM   7072  C  CE  . MET B  1 430 ? -23.929 -19.000 -9.066  1.00 31.37  ?  461  MET B CE  1 
ATOM   7073  N  N   . ILE B  1 431 ? -20.001 -23.650 -10.149 1.00 36.18  ?  462  ILE B N   1 
ATOM   7074  C  CA  . ILE B  1 431 ? -18.884 -23.948 -11.042 1.00 39.25  ?  462  ILE B CA  1 
ATOM   7075  C  C   . ILE B  1 431 ? -19.233 -25.117 -11.956 1.00 39.95  ?  462  ILE B C   1 
ATOM   7076  O  O   . ILE B  1 431 ? -19.068 -25.039 -13.178 1.00 38.89  ?  462  ILE B O   1 
ATOM   7077  C  CB  . ILE B  1 431 ? -17.610 -24.235 -10.221 1.00 39.91  ?  462  ILE B CB  1 
ATOM   7078  C  CG1 . ILE B  1 431 ? -17.075 -22.945 -9.602  1.00 39.38  ?  462  ILE B CG1 1 
ATOM   7079  C  CG2 . ILE B  1 431 ? -16.536 -24.942 -11.065 1.00 36.99  ?  462  ILE B CG2 1 
ATOM   7080  C  CD1 . ILE B  1 431 ? -16.226 -22.183 -10.529 1.00 38.48  ?  462  ILE B CD1 1 
ATOM   7081  N  N   . ALA B  1 432 ? -19.718 -26.217 -11.371 1.00 38.96  ?  463  ALA B N   1 
ATOM   7082  C  CA  . ALA B  1 432 ? -20.091 -27.392 -12.157 1.00 40.37  ?  463  ALA B CA  1 
ATOM   7083  C  C   . ALA B  1 432 ? -21.136 -27.051 -13.206 1.00 34.63  ?  463  ALA B C   1 
ATOM   7084  O  O   . ALA B  1 432 ? -21.031 -27.469 -14.367 1.00 35.59  ?  463  ALA B O   1 
ATOM   7085  C  CB  . ALA B  1 432 ? -20.618 -28.493 -11.236 1.00 43.45  ?  463  ALA B CB  1 
ATOM   7086  N  N   . LYS B  1 433 ? -22.162 -26.301 -12.812 1.00 36.85  ?  464  LYS B N   1 
ATOM   7087  C  CA  . LYS B  1 433 ? -23.185 -25.900 -13.769 1.00 36.43  ?  464  LYS B CA  1 
ATOM   7088  C  C   . LYS B  1 433 ? -22.583 -25.066 -14.898 1.00 37.43  ?  464  LYS B C   1 
ATOM   7089  O  O   . LYS B  1 433 ? -22.871 -25.292 -16.079 1.00 37.74  ?  464  LYS B O   1 
ATOM   7090  C  CB  . LYS B  1 433 ? -24.292 -25.140 -13.043 1.00 39.07  ?  464  LYS B CB  1 
ATOM   7091  C  CG  . LYS B  1 433 ? -25.691 -25.610 -13.381 1.00 44.10  ?  464  LYS B CG  1 
ATOM   7092  C  CD  . LYS B  1 433 ? -26.695 -25.162 -12.334 1.00 49.79  ?  464  LYS B CD  1 
ATOM   7093  C  CE  . LYS B  1 433 ? -27.594 -26.321 -11.892 1.00 61.23  ?  464  LYS B CE  1 
ATOM   7094  N  NZ  . LYS B  1 433 ? -28.323 -26.034 -10.616 1.00 64.07  ?  464  LYS B NZ  1 
ATOM   7095  N  N   . THR B  1 434 ? -21.720 -24.110 -14.554 1.00 37.35  ?  465  THR B N   1 
ATOM   7096  C  CA  . THR B  1 434 ? -21.125 -23.261 -15.580 1.00 36.68  ?  465  THR B CA  1 
ATOM   7097  C  C   . THR B  1 434 ? -20.208 -24.064 -16.488 1.00 34.80  ?  465  THR B C   1 
ATOM   7098  O  O   . THR B  1 434 ? -20.217 -23.869 -17.708 1.00 33.90  ?  465  THR B O   1 
ATOM   7099  C  CB  . THR B  1 434 ? -20.370 -22.097 -14.929 1.00 34.86  ?  465  THR B CB  1 
ATOM   7100  O  OG1 . THR B  1 434 ? -21.251 -21.423 -14.024 1.00 31.18  ?  465  THR B OG1 1 
ATOM   7101  C  CG2 . THR B  1 434 ? -19.863 -21.096 -15.996 1.00 32.18  ?  465  THR B CG2 1 
ATOM   7102  N  N   . GLN B  1 435 ? -19.407 -24.970 -15.915 1.00 36.44  ?  466  GLN B N   1 
ATOM   7103  C  CA  . GLN B  1 435 ? -18.529 -25.799 -16.740 1.00 35.11  ?  466  GLN B CA  1 
ATOM   7104  C  C   . GLN B  1 435 ? -19.333 -26.621 -17.740 1.00 37.55  ?  466  GLN B C   1 
ATOM   7105  O  O   . GLN B  1 435 ? -18.921 -26.795 -18.893 1.00 36.15  ?  466  GLN B O   1 
ATOM   7106  C  CB  . GLN B  1 435 ? -17.699 -26.723 -15.857 1.00 37.29  ?  466  GLN B CB  1 
ATOM   7107  C  CG  . GLN B  1 435 ? -16.720 -27.571 -16.634 1.00 36.49  ?  466  GLN B CG  1 
ATOM   7108  C  CD  . GLN B  1 435 ? -15.623 -28.121 -15.752 1.00 40.37  ?  466  GLN B CD  1 
ATOM   7109  O  OE1 . GLN B  1 435 ? -15.858 -28.466 -14.595 1.00 45.12  ?  466  GLN B OE1 1 
ATOM   7110  N  NE2 . GLN B  1 435 ? -14.418 -28.214 -16.296 1.00 43.43  ?  466  GLN B NE2 1 
ATOM   7111  N  N   . GLU B  1 436 ? -20.478 -27.141 -17.300 1.00 36.76  ?  467  GLU B N   1 
ATOM   7112  C  CA  . GLU B  1 436 ? -21.334 -27.931 -18.175 1.00 41.09  ?  467  GLU B CA  1 
ATOM   7113  C  C   . GLU B  1 436 ? -21.847 -27.095 -19.346 1.00 41.42  ?  467  GLU B C   1 
ATOM   7114  O  O   . GLU B  1 436 ? -21.932 -27.580 -20.482 1.00 40.72  ?  467  GLU B O   1 
ATOM   7115  C  CB  . GLU B  1 436 ? -22.481 -28.512 -17.347 1.00 40.37  ?  467  GLU B CB  1 
ATOM   7116  C  CG  . GLU B  1 436 ? -23.269 -29.610 -18.056 1.00 50.66  ?  467  GLU B CG  1 
ATOM   7117  C  CD  . GLU B  1 436 ? -22.404 -30.813 -18.396 1.00 59.07  ?  467  GLU B CD  1 
ATOM   7118  O  OE1 . GLU B  1 436 ? -21.482 -31.144 -17.604 1.00 57.70  ?  467  GLU B OE1 1 
ATOM   7119  O  OE2 . GLU B  1 436 ? -22.627 -31.406 -19.476 1.00 62.72  -1 467  GLU B OE2 1 
ATOM   7120  N  N   . TRP B  1 437 ? -22.183 -25.831 -19.090 1.00 35.57  ?  468  TRP B N   1 
ATOM   7121  C  CA  . TRP B  1 437 ? -22.565 -24.928 -20.168 1.00 36.44  ?  468  TRP B CA  1 
ATOM   7122  C  C   . TRP B  1 437 ? -21.466 -24.867 -21.230 1.00 34.97  ?  468  TRP B C   1 
ATOM   7123  O  O   . TRP B  1 437 ? -21.729 -25.051 -22.426 1.00 33.73  ?  468  TRP B O   1 
ATOM   7124  C  CB  . TRP B  1 437 ? -22.889 -23.547 -19.569 1.00 34.67  ?  468  TRP B CB  1 
ATOM   7125  C  CG  . TRP B  1 437 ? -23.106 -22.390 -20.535 1.00 35.83  ?  468  TRP B CG  1 
ATOM   7126  C  CD1 . TRP B  1 437 ? -24.034 -22.312 -21.541 1.00 35.75  ?  468  TRP B CD1 1 
ATOM   7127  C  CD2 . TRP B  1 437 ? -22.404 -21.132 -20.542 1.00 30.99  ?  468  TRP B CD2 1 
ATOM   7128  N  NE1 . TRP B  1 437 ? -23.942 -21.095 -22.180 1.00 33.66  ?  468  TRP B NE1 1 
ATOM   7129  C  CE2 . TRP B  1 437 ? -22.950 -20.353 -21.582 1.00 34.62  ?  468  TRP B CE2 1 
ATOM   7130  C  CE3 . TRP B  1 437 ? -21.370 -20.594 -19.765 1.00 33.08  ?  468  TRP B CE3 1 
ATOM   7131  C  CZ2 . TRP B  1 437 ? -22.481 -19.068 -21.879 1.00 32.99  ?  468  TRP B CZ2 1 
ATOM   7132  C  CZ3 . TRP B  1 437 ? -20.907 -19.321 -20.062 1.00 29.07  ?  468  TRP B CZ3 1 
ATOM   7133  C  CH2 . TRP B  1 437 ? -21.467 -18.572 -21.102 1.00 30.22  ?  468  TRP B CH2 1 
ATOM   7134  N  N   . THR B  1 438 ? -20.213 -24.709 -20.802 1.00 32.90  ?  469  THR B N   1 
ATOM   7135  C  CA  . THR B  1 438 ? -19.114 -24.577 -21.751 1.00 35.34  ?  469  THR B CA  1 
ATOM   7136  C  C   . THR B  1 438 ? -18.916 -25.824 -22.609 1.00 35.30  ?  469  THR B C   1 
ATOM   7137  O  O   . THR B  1 438 ? -18.259 -25.743 -23.651 1.00 34.82  ?  469  THR B O   1 
ATOM   7138  C  CB  . THR B  1 438 ? -17.823 -24.240 -21.009 1.00 34.66  ?  469  THR B CB  1 
ATOM   7139  O  OG1 . THR B  1 438 ? -17.407 -25.361 -20.210 1.00 36.95  ?  469  THR B OG1 1 
ATOM   7140  C  CG2 . THR B  1 438 ? -18.036 -23.010 -20.111 1.00 32.62  ?  469  THR B CG2 1 
ATOM   7141  N  N   . LYS B  1 439 ? -19.452 -26.972 -22.192 1.00 36.95  ?  470  LYS B N   1 
ATOM   7142  C  CA  . LYS B  1 439 ? -19.304 -28.195 -22.978 1.00 41.73  ?  470  LYS B CA  1 
ATOM   7143  C  C   . LYS B  1 439 ? -20.016 -28.090 -24.324 1.00 41.83  ?  470  LYS B C   1 
ATOM   7144  O  O   . LYS B  1 439 ? -19.641 -28.794 -25.269 1.00 43.49  ?  470  LYS B O   1 
ATOM   7145  C  CB  . LYS B  1 439 ? -19.860 -29.394 -22.193 1.00 44.19  ?  470  LYS B CB  1 
ATOM   7146  C  CG  . LYS B  1 439 ? -18.957 -30.049 -21.086 1.00 46.47  ?  470  LYS B CG  1 
ATOM   7147  C  CD  . LYS B  1 439 ? -17.434 -29.849 -21.163 1.00 48.95  ?  470  LYS B CD  1 
ATOM   7148  C  CE  . LYS B  1 439 ? -16.767 -30.341 -22.472 1.00 55.99  ?  470  LYS B CE  1 
ATOM   7149  N  NZ  . LYS B  1 439 ? -15.307 -30.669 -22.312 1.00 58.26  ?  470  LYS B NZ  1 
ATOM   7150  N  N   . SER B  1 440 ? -21.031 -27.227 -24.435 1.00 36.63  ?  471  SER B N   1 
ATOM   7151  C  CA  . SER B  1 440 ? -21.782 -27.060 -25.672 1.00 36.83  ?  471  SER B CA  1 
ATOM   7152  C  C   . SER B  1 440 ? -21.168 -26.037 -26.619 1.00 39.47  ?  471  SER B C   1 
ATOM   7153  O  O   . SER B  1 440 ? -21.700 -25.843 -27.718 1.00 33.19  ?  471  SER B O   1 
ATOM   7154  C  CB  . SER B  1 440 ? -23.234 -26.671 -25.362 1.00 38.08  ?  471  SER B CB  1 
ATOM   7155  O  OG  . SER B  1 440 ? -23.302 -25.422 -24.686 1.00 39.59  ?  471  SER B OG  1 
ATOM   7156  N  N   . PHE B  1 441 ? -20.051 -25.411 -26.252 1.00 30.20  ?  472  PHE B N   1 
ATOM   7157  C  CA  . PHE B  1 441 ? -19.525 -24.311 -27.052 1.00 32.55  ?  472  PHE B CA  1 
ATOM   7158  C  C   . PHE B  1 441 ? -18.961 -24.805 -28.384 1.00 38.46  ?  472  PHE B C   1 
ATOM   7159  O  O   . PHE B  1 441 ? -18.498 -25.943 -28.509 1.00 42.51  ?  472  PHE B O   1 
ATOM   7160  C  CB  . PHE B  1 441 ? -18.428 -23.568 -26.287 1.00 33.44  ?  472  PHE B CB  1 
ATOM   7161  C  CG  . PHE B  1 441 ? -18.946 -22.693 -25.167 1.00 34.93  ?  472  PHE B CG  1 
ATOM   7162  C  CD1 . PHE B  1 441 ? -20.307 -22.654 -24.858 1.00 33.16  ?  472  PHE B CD1 1 
ATOM   7163  C  CD2 . PHE B  1 441 ? -18.075 -21.911 -24.433 1.00 32.77  ?  472  PHE B CD2 1 
ATOM   7164  C  CE1 . PHE B  1 441 ? -20.772 -21.857 -23.836 1.00 33.34  ?  472  PHE B CE1 1 
ATOM   7165  C  CE2 . PHE B  1 441 ? -18.538 -21.114 -23.409 1.00 33.27  ?  472  PHE B CE2 1 
ATOM   7166  C  CZ  . PHE B  1 441 ? -19.886 -21.086 -23.110 1.00 32.33  ?  472  PHE B CZ  1 
ATOM   7167  N  N   . VAL B  1 442 ? -18.986 -23.922 -29.382 1.00 35.22  ?  473  VAL B N   1 
ATOM   7168  C  CA  . VAL B  1 442 ? -18.335 -24.171 -30.662 1.00 34.56  ?  473  VAL B CA  1 
ATOM   7169  C  C   . VAL B  1 442 ? -17.023 -23.404 -30.690 1.00 38.43  ?  473  VAL B C   1 
ATOM   7170  O  O   . VAL B  1 442 ? -16.698 -22.660 -29.755 1.00 38.41  ?  473  VAL B O   1 
ATOM   7171  C  CB  . VAL B  1 442 ? -19.234 -23.777 -31.850 1.00 41.20  ?  473  VAL B CB  1 
ATOM   7172  C  CG1 . VAL B  1 442 ? -20.537 -24.567 -31.826 1.00 37.20  ?  473  VAL B CG1 1 
ATOM   7173  C  CG2 . VAL B  1 442 ? -19.516 -22.267 -31.851 1.00 33.41  ?  473  VAL B CG2 1 
ATOM   7174  N  N   . LYS B  1 443 ? -16.253 -23.592 -31.744 1.00 38.31  ?  474  LYS B N   1 
ATOM   7175  C  CA  . LYS B  1 443 ? -15.054 -22.790 -31.916 1.00 42.61  ?  474  LYS B CA  1 
ATOM   7176  C  C   . LYS B  1 443 ? -15.422 -21.424 -32.495 1.00 35.73  ?  474  LYS B C   1 
ATOM   7177  O  O   . LYS B  1 443 ? -16.402 -21.302 -33.234 1.00 35.38  ?  474  LYS B O   1 
ATOM   7178  C  CB  . LYS B  1 443 ? -14.065 -23.493 -32.837 1.00 41.56  ?  474  LYS B CB  1 
ATOM   7179  N  N   . PRO B  1 444 ? -14.681 -20.377 -32.135 1.00 35.98  ?  475  PRO B N   1 
ATOM   7180  C  CA  . PRO B  1 444 ? -14.919 -19.065 -32.742 1.00 33.29  ?  475  PRO B CA  1 
ATOM   7181  C  C   . PRO B  1 444 ? -14.708 -19.157 -34.241 1.00 36.65  ?  475  PRO B C   1 
ATOM   7182  O  O   . PRO B  1 444 ? -13.763 -19.801 -34.705 1.00 33.98  ?  475  PRO B O   1 
ATOM   7183  C  CB  . PRO B  1 444 ? -13.838 -18.184 -32.102 1.00 34.66  ?  475  PRO B CB  1 
ATOM   7184  C  CG  . PRO B  1 444 ? -13.525 -18.877 -30.808 1.00 34.82  ?  475  PRO B CG  1 
ATOM   7185  C  CD  . PRO B  1 444 ? -13.552 -20.329 -31.193 1.00 29.85  ?  475  PRO B CD  1 
ATOM   7186  N  N   . LEU B  1 445 ? -15.576 -18.479 -35.003 1.00 34.08  ?  476  LEU B N   1 
ATOM   7187  C  CA  . LEU B  1 445 ? -15.373 -18.409 -36.446 1.00 33.73  ?  476  LEU B CA  1 
ATOM   7188  C  C   . LEU B  1 445 ? -14.220 -17.488 -36.811 1.00 39.16  ?  476  LEU B C   1 
ATOM   7189  O  O   . LEU B  1 445 ? -13.652 -17.603 -37.903 1.00 37.45  ?  476  LEU B O   1 
ATOM   7190  C  CB  . LEU B  1 445 ? -16.643 -17.928 -37.139 1.00 33.50  ?  476  LEU B CB  1 
ATOM   7191  C  CG  . LEU B  1 445 ? -17.834 -18.855 -36.986 1.00 34.20  ?  476  LEU B CG  1 
ATOM   7192  C  CD1 . LEU B  1 445 ? -19.104 -18.078 -37.223 1.00 38.45  ?  476  LEU B CD1 1 
ATOM   7193  C  CD2 . LEU B  1 445 ? -17.728 -20.002 -37.992 1.00 40.49  ?  476  LEU B CD2 1 
ATOM   7194  N  N   . TRP B  1 446 ? -13.919 -16.523 -35.949 1.00 31.07  ?  477  TRP B N   1 
ATOM   7195  C  CA  . TRP B  1 446 ? -12.784 -15.631 -36.115 1.00 31.86  ?  477  TRP B CA  1 
ATOM   7196  C  C   . TRP B  1 446 ? -12.334 -15.243 -34.716 1.00 30.59  ?  477  TRP B C   1 
ATOM   7197  O  O   . TRP B  1 446 ? -13.098 -15.357 -33.753 1.00 29.72  ?  477  TRP B O   1 
ATOM   7198  C  CB  . TRP B  1 446 ? -13.131 -14.387 -36.953 1.00 30.73  ?  477  TRP B CB  1 
ATOM   7199  C  CG  . TRP B  1 446 ? -14.297 -13.607 -36.364 1.00 32.88  ?  477  TRP B CG  1 
ATOM   7200  C  CD1 . TRP B  1 446 ? -14.254 -12.726 -35.306 1.00 28.27  ?  477  TRP B CD1 1 
ATOM   7201  C  CD2 . TRP B  1 446 ? -15.672 -13.680 -36.765 1.00 29.86  ?  477  TRP B CD2 1 
ATOM   7202  N  NE1 . TRP B  1 446 ? -15.517 -12.238 -35.048 1.00 28.61  ?  477  TRP B NE1 1 
ATOM   7203  C  CE2 . TRP B  1 446 ? -16.402 -12.806 -35.926 1.00 30.29  ?  477  TRP B CE2 1 
ATOM   7204  C  CE3 . TRP B  1 446 ? -16.354 -14.383 -37.761 1.00 29.38  ?  477  TRP B CE3 1 
ATOM   7205  C  CZ2 . TRP B  1 446 ? -17.784 -12.628 -36.046 1.00 30.61  ?  477  TRP B CZ2 1 
ATOM   7206  C  CZ3 . TRP B  1 446 ? -17.725 -14.209 -37.879 1.00 30.43  ?  477  TRP B CZ3 1 
ATOM   7207  C  CH2 . TRP B  1 446 ? -18.426 -13.338 -37.027 1.00 30.08  ?  477  TRP B CH2 1 
ATOM   7208  N  N   . VAL B  1 447 ? -11.081 -14.808 -34.599 1.00 29.72  ?  478  VAL B N   1 
ATOM   7209  C  CA  . VAL B  1 447 ? -10.623 -14.274 -33.320 1.00 29.61  ?  478  VAL B CA  1 
ATOM   7210  C  C   . VAL B  1 447 ? -10.285 -12.815 -33.579 1.00 30.39  ?  478  VAL B C   1 
ATOM   7211  O  O   . VAL B  1 447 ? -10.528 -12.318 -34.683 1.00 31.66  ?  478  VAL B O   1 
ATOM   7212  C  CB  . VAL B  1 447 ? -9.432  -15.071 -32.760 1.00 30.37  ?  478  VAL B CB  1 
ATOM   7213  C  CG1 . VAL B  1 447 ? -9.899  -16.460 -32.343 1.00 30.94  ?  478  VAL B CG1 1 
ATOM   7214  C  CG2 . VAL B  1 447 ? -8.290  -15.119 -33.781 1.00 29.47  ?  478  VAL B CG2 1 
ATOM   7215  N  N   . TYR B  1 448 ? -9.723  -12.112 -32.594 1.00 28.66  ?  479  TYR B N   1 
ATOM   7216  C  CA  . TYR B  1 448 ? -9.481  -10.680 -32.775 1.00 27.38  ?  479  TYR B CA  1 
ATOM   7217  C  C   . TYR B  1 448 ? -8.028  -10.330 -33.105 1.00 30.80  ?  479  TYR B C   1 
ATOM   7218  O  O   . TYR B  1 448 ? -7.791  -9.529  -34.013 1.00 31.87  ?  479  TYR B O   1 
ATOM   7219  C  CB  . TYR B  1 448 ? -9.935  -9.897  -31.535 1.00 27.70  ?  479  TYR B CB  1 
ATOM   7220  C  CG  . TYR B  1 448 ? -10.096 -8.413  -31.807 1.00 28.20  ?  479  TYR B CG  1 
ATOM   7221  C  CD1 . TYR B  1 448 ? -11.201 -7.931  -32.512 1.00 28.20  ?  479  TYR B CD1 1 
ATOM   7222  C  CD2 . TYR B  1 448 ? -9.133  -7.496  -31.377 1.00 29.13  ?  479  TYR B CD2 1 
ATOM   7223  C  CE1 . TYR B  1 448 ? -11.348 -6.569  -32.771 1.00 29.69  ?  479  TYR B CE1 1 
ATOM   7224  C  CE2 . TYR B  1 448 ? -9.264  -6.137  -31.623 1.00 27.08  ?  479  TYR B CE2 1 
ATOM   7225  C  CZ  . TYR B  1 448 ? -10.379 -5.682  -32.332 1.00 30.84  ?  479  TYR B CZ  1 
ATOM   7226  O  OH  . TYR B  1 448 ? -10.540 -4.338  -32.587 1.00 29.94  ?  479  TYR B OH  1 
ATOM   7227  N  N   . SER B  1 449 ? -7.045  -10.869 -32.377 1.00 30.07  ?  480  SER B N   1 
ATOM   7228  C  CA  . SER B  1 449 ? -5.642  -10.530 -32.593 1.00 30.76  ?  480  SER B CA  1 
ATOM   7229  C  C   . SER B  1 449 ? -4.849  -11.741 -33.077 1.00 33.58  ?  480  SER B C   1 
ATOM   7230  O  O   . SER B  1 449 ? -5.287  -12.895 -32.992 1.00 29.52  ?  480  SER B O   1 
ATOM   7231  C  CB  . SER B  1 449 ? -4.974  -10.004 -31.308 1.00 25.97  ?  480  SER B CB  1 
ATOM   7232  O  OG  . SER B  1 449 ? -5.092  -11.012 -30.314 1.00 28.92  ?  480  SER B OG  1 
ATOM   7233  N  N   . VAL B  1 450 ? -3.647  -11.447 -33.568 1.00 32.93  ?  481  VAL B N   1 
ATOM   7234  C  CA  . VAL B  1 450 ? -2.711  -12.502 -33.949 1.00 31.53  ?  481  VAL B CA  1 
ATOM   7235  C  C   . VAL B  1 450 ? -2.357  -13.352 -32.739 1.00 33.22  ?  481  VAL B C   1 
ATOM   7236  O  O   . VAL B  1 450 ? -2.271  -14.584 -32.831 1.00 30.50  ?  481  VAL B O   1 
ATOM   7237  C  CB  . VAL B  1 450 ? -1.461  -11.881 -34.599 1.00 33.54  ?  481  VAL B CB  1 
ATOM   7238  C  CG1 . VAL B  1 450 ? -0.314  -12.906 -34.662 1.00 38.17  ?  481  VAL B CG1 1 
ATOM   7239  C  CG2 . VAL B  1 450 ? -1.809  -11.334 -35.981 1.00 33.98  ?  481  VAL B CG2 1 
ATOM   7240  N  N   . LYS B  1 451 ? -2.176  -12.709 -31.573 1.00 30.90  ?  482  LYS B N   1 
ATOM   7241  C  CA  . LYS B  1 451 ? -1.975  -13.460 -30.335 1.00 30.84  ?  482  LYS B CA  1 
ATOM   7242  C  C   . LYS B  1 451 ? -3.111  -14.451 -30.102 1.00 27.42  ?  482  LYS B C   1 
ATOM   7243  O  O   . LYS B  1 451 ? -2.870  -15.606 -29.742 1.00 28.74  ?  482  LYS B O   1 
ATOM   7244  C  CB  . LYS B  1 451 ? -1.839  -12.497 -29.147 1.00 28.84  ?  482  LYS B CB  1 
ATOM   7245  C  CG  . LYS B  1 451 ? -1.663  -13.198 -27.802 1.00 34.82  ?  482  LYS B CG  1 
ATOM   7246  C  CD  . LYS B  1 451 ? -0.252  -13.808 -27.705 1.00 31.14  ?  482  LYS B CD  1 
ATOM   7247  C  CE  . LYS B  1 451 ? 0.056   -14.358 -26.316 1.00 34.75  ?  482  LYS B CE  1 
ATOM   7248  N  NZ  . LYS B  1 451 ? 1.529   -14.655 -26.219 1.00 34.42  ?  482  LYS B NZ  1 
ATOM   7249  N  N   . ASP B  1 452 ? -4.365  -14.016 -30.296 1.00 29.92  ?  483  ASP B N   1 
ATOM   7250  C  CA  . ASP B  1 452 ? -5.499  -14.942 -30.183 1.00 28.09  ?  483  ASP B CA  1 
ATOM   7251  C  C   . ASP B  1 452 ? -5.295  -16.171 -31.073 1.00 34.98  ?  483  ASP B C   1 
ATOM   7252  O  O   . ASP B  1 452 ? -5.439  -17.317 -30.623 1.00 32.83  ?  483  ASP B O   1 
ATOM   7253  C  CB  . ASP B  1 452 ? -6.826  -14.279 -30.598 1.00 28.64  ?  483  ASP B CB  1 
ATOM   7254  C  CG  . ASP B  1 452 ? -7.341  -13.205 -29.616 1.00 30.30  ?  483  ASP B CG  1 
ATOM   7255  O  OD1 . ASP B  1 452 ? -6.977  -13.210 -28.433 1.00 29.45  ?  483  ASP B OD1 1 
ATOM   7256  O  OD2 . ASP B  1 452 ? -8.155  -12.373 -30.066 1.00 31.60  -1 483  ASP B OD2 1 
ATOM   7257  N  N   . LYS B  1 453 ? -5.019  -15.942 -32.363 1.00 32.49  ?  484  LYS B N   1 
ATOM   7258  C  CA  . LYS B  1 453 ? -4.858  -17.054 -33.300 1.00 33.84  ?  484  LYS B CA  1 
ATOM   7259  C  C   . LYS B  1 453 ? -3.813  -18.052 -32.806 1.00 33.24  ?  484  LYS B C   1 
ATOM   7260  O  O   . LYS B  1 453 ? -4.045  -19.266 -32.805 1.00 35.26  ?  484  LYS B O   1 
ATOM   7261  C  CB  . LYS B  1 453 ? -4.476  -16.527 -34.679 1.00 35.38  ?  484  LYS B CB  1 
ATOM   7262  C  CG  . LYS B  1 453 ? -4.706  -17.563 -35.799 1.00 45.19  ?  484  LYS B CG  1 
ATOM   7263  C  CD  . LYS B  1 453 ? -3.802  -17.302 -37.005 1.00 45.97  ?  484  LYS B CD  1 
ATOM   7264  C  CE  . LYS B  1 453 ? -4.196  -18.186 -38.201 1.00 51.19  ?  484  LYS B CE  1 
ATOM   7265  N  NZ  . LYS B  1 453 ? -5.587  -17.926 -38.704 1.00 54.60  ?  484  LYS B NZ  1 
ATOM   7266  N  N   . GLU B  1 454 ? -2.663  -17.554 -32.359 1.00 33.28  ?  485  GLU B N   1 
ATOM   7267  C  CA  . GLU B  1 454 ? -1.614  -18.463 -31.901 1.00 36.65  ?  485  GLU B CA  1 
ATOM   7268  C  C   . GLU B  1 454 ? -2.093  -19.282 -30.714 1.00 36.76  ?  485  GLU B C   1 
ATOM   7269  O  O   . GLU B  1 454 ? -1.878  -20.500 -30.658 1.00 38.89  ?  485  GLU B O   1 
ATOM   7270  C  CB  . GLU B  1 454 ? -0.354  -17.681 -31.532 1.00 35.42  ?  485  GLU B CB  1 
ATOM   7271  C  CG  . GLU B  1 454 ? 0.149   -16.726 -32.620 1.00 36.84  ?  485  GLU B CG  1 
ATOM   7272  C  CD  . GLU B  1 454 ? 1.462   -16.063 -32.242 1.00 40.73  ?  485  GLU B CD  1 
ATOM   7273  O  OE1 . GLU B  1 454 ? 1.827   -16.101 -31.042 1.00 44.97  ?  485  GLU B OE1 1 
ATOM   7274  O  OE2 . GLU B  1 454 ? 2.125   -15.483 -33.131 1.00 42.19  -1 485  GLU B OE2 1 
ATOM   7275  N  N   . LEU B  1 455 ? -2.778  -18.628 -29.771 1.00 31.49  ?  486  LEU B N   1 
ATOM   7276  C  CA  . LEU B  1 455 ? -3.250  -19.306 -28.567 1.00 32.99  ?  486  LEU B CA  1 
ATOM   7277  C  C   . LEU B  1 455 ? -4.266  -20.397 -28.888 1.00 34.81  ?  486  LEU B C   1 
ATOM   7278  O  O   . LEU B  1 455 ? -4.213  -21.494 -28.320 1.00 36.22  ?  486  LEU B O   1 
ATOM   7279  C  CB  . LEU B  1 455 ? -3.862  -18.281 -27.615 1.00 30.94  ?  486  LEU B CB  1 
ATOM   7280  C  CG  . LEU B  1 455 ? -2.895  -17.328 -26.907 1.00 37.33  ?  486  LEU B CG  1 
ATOM   7281  C  CD1 . LEU B  1 455 ? -3.678  -16.235 -26.187 1.00 33.53  ?  486  LEU B CD1 1 
ATOM   7282  C  CD2 . LEU B  1 455 ? -1.962  -18.061 -25.939 1.00 36.50  ?  486  LEU B CD2 1 
ATOM   7283  N  N   . TRP B  1 456 ? -5.229  -20.100 -29.760 1.00 31.97  ?  487  TRP B N   1 
ATOM   7284  C  CA  . TRP B  1 456 ? -6.209  -21.112 -30.151 1.00 33.47  ?  487  TRP B CA  1 
ATOM   7285  C  C   . TRP B  1 456 ? -5.566  -22.230 -30.970 1.00 37.41  ?  487  TRP B C   1 
ATOM   7286  O  O   . TRP B  1 456 ? -5.929  -23.402 -30.818 1.00 35.16  ?  487  TRP B O   1 
ATOM   7287  C  CB  . TRP B  1 456 ? -7.347  -20.470 -30.951 1.00 33.11  ?  487  TRP B CB  1 
ATOM   7288  C  CG  . TRP B  1 456 ? -8.340  -19.765 -30.083 1.00 34.43  ?  487  TRP B CG  1 
ATOM   7289  C  CD1 . TRP B  1 456 ? -8.263  -18.481 -29.643 1.00 34.05  ?  487  TRP B CD1 1 
ATOM   7290  C  CD2 . TRP B  1 456 ? -9.552  -20.305 -29.542 1.00 31.79  ?  487  TRP B CD2 1 
ATOM   7291  N  NE1 . TRP B  1 456 ? -9.351  -18.185 -28.863 1.00 29.29  ?  487  TRP B NE1 1 
ATOM   7292  C  CE2 . TRP B  1 456 ? -10.159 -19.288 -28.788 1.00 31.65  ?  487  TRP B CE2 1 
ATOM   7293  C  CE3 . TRP B  1 456 ? -10.185 -21.545 -29.629 1.00 37.55  ?  487  TRP B CE3 1 
ATOM   7294  C  CZ2 . TRP B  1 456 ? -11.369 -19.474 -28.122 1.00 34.04  ?  487  TRP B CZ2 1 
ATOM   7295  C  CZ3 . TRP B  1 456 ? -11.387 -21.726 -28.972 1.00 33.12  ?  487  TRP B CZ3 1 
ATOM   7296  C  CH2 . TRP B  1 456 ? -11.965 -20.698 -28.228 1.00 34.26  ?  487  TRP B CH2 1 
ATOM   7297  N  N   . GLU B  1 457 ? -4.620  -21.887 -31.847 1.00 38.24  ?  488  GLU B N   1 
ATOM   7298  C  CA  . GLU B  1 457 ? -3.992  -22.906 -32.681 1.00 37.72  ?  488  GLU B CA  1 
ATOM   7299  C  C   . GLU B  1 457 ? -3.098  -23.825 -31.870 1.00 44.00  ?  488  GLU B C   1 
ATOM   7300  O  O   . GLU B  1 457 ? -3.040  -25.024 -32.158 1.00 44.25  ?  488  GLU B O   1 
ATOM   7301  C  CB  . GLU B  1 457 ? -3.208  -22.252 -33.811 1.00 36.39  ?  488  GLU B CB  1 
ATOM   7302  C  CG  . GLU B  1 457 ? -4.115  -21.897 -34.973 1.00 42.94  ?  488  GLU B CG  1 
ATOM   7303  C  CD  . GLU B  1 457 ? -3.421  -21.119 -36.079 1.00 48.05  ?  488  GLU B CD  1 
ATOM   7304  O  OE1 . GLU B  1 457 ? -2.238  -20.738 -35.911 1.00 50.33  ?  488  GLU B OE1 1 
ATOM   7305  O  OE2 . GLU B  1 457 ? -4.084  -20.864 -37.108 1.00 52.67  -1 488  GLU B OE2 1 
ATOM   7306  N  N   . SER B  1 458 ? -2.425  -23.294 -30.839 1.00 40.39  ?  489  SER B N   1 
ATOM   7307  C  CA  . SER B  1 458 ? -1.620  -24.104 -29.931 1.00 40.23  ?  489  SER B CA  1 
ATOM   7308  C  C   . SER B  1 458 ? -2.442  -24.857 -28.895 1.00 42.62  ?  489  SER B C   1 
ATOM   7309  O  O   . SER B  1 458 ? -1.869  -25.657 -28.146 1.00 44.39  ?  489  SER B O   1 
ATOM   7310  C  CB  . SER B  1 458 ? -0.609  -23.229 -29.193 1.00 40.29  ?  489  SER B CB  1 
ATOM   7311  O  OG  . SER B  1 458 ? -1.266  -22.462 -28.192 1.00 40.36  ?  489  SER B OG  1 
ATOM   7312  N  N   . GLY B  1 459 ? -3.754  -24.622 -28.820 1.00 40.79  ?  490  GLY B N   1 
ATOM   7313  C  CA  . GLY B  1 459 ? -4.559  -25.210 -27.769 1.00 40.49  ?  490  GLY B CA  1 
ATOM   7314  C  C   . GLY B  1 459 ? -4.379  -24.589 -26.400 1.00 36.35  ?  490  GLY B C   1 
ATOM   7315  O  O   . GLY B  1 459 ? -4.974  -25.081 -25.435 1.00 36.60  ?  490  GLY B O   1 
ATOM   7316  N  N   . GLN B  1 460 ? -3.560  -23.540 -26.285 1.00 39.49  ?  491  GLN B N   1 
ATOM   7317  C  CA  . GLN B  1 460 ? -3.492  -22.752 -25.058 1.00 36.37  ?  491  GLN B CA  1 
ATOM   7318  C  C   . GLN B  1 460 ? -4.832  -22.088 -24.747 1.00 36.85  ?  491  GLN B C   1 
ATOM   7319  O  O   . GLN B  1 460 ? -5.174  -21.900 -23.578 1.00 33.51  ?  491  GLN B O   1 
ATOM   7320  C  CB  . GLN B  1 460 ? -2.390  -21.705 -25.192 1.00 39.77  ?  491  GLN B CB  1 
ATOM   7321  C  CG  . GLN B  1 460 ? -1.000  -22.254 -25.005 1.00 45.60  ?  491  GLN B CG  1 
ATOM   7322  C  CD  . GLN B  1 460 ? 0.074   -21.280 -25.459 1.00 53.05  ?  491  GLN B CD  1 
ATOM   7323  O  OE1 . GLN B  1 460 ? 0.329   -21.144 -26.665 1.00 51.94  ?  491  GLN B OE1 1 
ATOM   7324  N  NE2 . GLN B  1 460 ? 0.716   -20.606 -24.503 1.00 50.96  ?  491  GLN B NE2 1 
ATOM   7325  N  N   . MET B  1 461 ? -5.598  -21.715 -25.770 1.00 35.73  ?  492  MET B N   1 
ATOM   7326  C  CA  . MET B  1 461 ? -7.008  -21.444 -25.573 1.00 34.83  ?  492  MET B CA  1 
ATOM   7327  C  C   . MET B  1 461 ? -7.842  -22.530 -26.242 1.00 33.59  ?  492  MET B C   1 
ATOM   7328  O  O   . MET B  1 461 ? -7.384  -23.179 -27.184 1.00 35.84  ?  492  MET B O   1 
ATOM   7329  C  CB  . MET B  1 461 ? -7.418  -20.065 -26.112 1.00 32.69  ?  492  MET B CB  1 
ATOM   7330  C  CG  . MET B  1 461 ? -6.643  -18.913 -25.489 1.00 34.53  ?  492  MET B CG  1 
ATOM   7331  S  SD  . MET B  1 461 ? -7.494  -18.459 -23.946 1.00 35.45  ?  492  MET B SD  1 
ATOM   7332  C  CE  . MET B  1 461 ? -8.910  -17.501 -24.514 1.00 28.99  ?  492  MET B CE  1 
ATOM   7333  N  N   . PRO B  1 462 ? -9.072  -22.769 -25.772 1.00 34.63  ?  493  PRO B N   1 
ATOM   7334  C  CA  . PRO B  1 462 ? -9.756  -22.084 -24.665 1.00 35.34  ?  493  PRO B CA  1 
ATOM   7335  C  C   . PRO B  1 462 ? -9.397  -22.600 -23.273 1.00 39.31  ?  493  PRO B C   1 
ATOM   7336  O  O   . PRO B  1 462 ? -9.572  -21.847 -22.317 1.00 35.82  ?  493  PRO B O   1 
ATOM   7337  C  CB  . PRO B  1 462 ? -11.237 -22.320 -24.985 1.00 33.36  ?  493  PRO B CB  1 
ATOM   7338  C  CG  . PRO B  1 462 ? -11.256 -23.653 -25.697 1.00 35.89  ?  493  PRO B CG  1 
ATOM   7339  C  CD  . PRO B  1 462 ? -9.950  -23.753 -26.445 1.00 35.93  ?  493  PRO B CD  1 
ATOM   7340  N  N   . ASN B  1 463 ? -8.908  -23.833 -23.132 1.00 36.03  ?  494  ASN B N   1 
ATOM   7341  C  CA  . ASN B  1 463 ? -8.607  -24.468 -21.840 1.00 36.24  ?  494  ASN B CA  1 
ATOM   7342  C  C   . ASN B  1 463 ? -9.680  -24.164 -20.792 1.00 36.55  ?  494  ASN B C   1 
ATOM   7343  O  O   . ASN B  1 463 ? -9.414  -23.593 -19.733 1.00 34.83  ?  494  ASN B O   1 
ATOM   7344  C  CB  . ASN B  1 463 ? -7.213  -24.072 -21.324 1.00 33.41  ?  494  ASN B CB  1 
ATOM   7345  C  CG  . ASN B  1 463 ? -6.673  -25.048 -20.279 1.00 33.71  ?  494  ASN B CG  1 
ATOM   7346  O  OD1 . ASN B  1 463 ? -7.400  -25.885 -19.739 1.00 38.02  ?  494  ASN B OD1 1 
ATOM   7347  N  ND2 . ASN B  1 463 ? -5.401  -24.912 -19.961 1.00 36.67  ?  494  ASN B ND2 1 
ATOM   7348  N  N   . TYR B  1 464 ? -10.917 -24.568 -21.105 1.00 36.46  ?  495  TYR B N   1 
ATOM   7349  C  CA  . TYR B  1 464 ? -11.990 -24.437 -20.119 1.00 36.94  ?  495  TYR B CA  1 
ATOM   7350  C  C   . TYR B  1 464 ? -11.680 -25.223 -18.856 1.00 36.43  ?  495  TYR B C   1 
ATOM   7351  O  O   . TYR B  1 464 ? -12.129 -24.848 -17.764 1.00 37.65  ?  495  TYR B O   1 
ATOM   7352  C  CB  . TYR B  1 464 ? -13.331 -24.894 -20.701 1.00 32.66  ?  495  TYR B CB  1 
ATOM   7353  C  CG  . TYR B  1 464 ? -13.753 -24.122 -21.934 1.00 36.52  ?  495  TYR B CG  1 
ATOM   7354  C  CD1 . TYR B  1 464 ? -13.933 -22.737 -21.892 1.00 34.44  ?  495  TYR B CD1 1 
ATOM   7355  C  CD2 . TYR B  1 464 ? -13.956 -24.774 -23.148 1.00 35.97  ?  495  TYR B CD2 1 
ATOM   7356  C  CE1 . TYR B  1 464 ? -14.318 -22.026 -23.031 1.00 34.23  ?  495  TYR B CE1 1 
ATOM   7357  C  CE2 . TYR B  1 464 ? -14.334 -24.070 -24.296 1.00 32.88  ?  495  TYR B CE2 1 
ATOM   7358  C  CZ  . TYR B  1 464 ? -14.511 -22.703 -24.229 1.00 33.20  ?  495  TYR B CZ  1 
ATOM   7359  O  OH  . TYR B  1 464 ? -14.874 -22.025 -25.373 1.00 36.11  ?  495  TYR B OH  1 
ATOM   7360  N  N   . GLU B  1 465 ? -10.922 -26.312 -18.975 1.00 34.26  ?  496  GLU B N   1 
ATOM   7361  C  CA  . GLU B  1 465 ? -10.587 -27.103 -17.798 1.00 36.84  ?  496  GLU B CA  1 
ATOM   7362  C  C   . GLU B  1 465 ? -9.813  -26.261 -16.787 1.00 36.99  ?  496  GLU B C   1 
ATOM   7363  O  O   . GLU B  1 465 ? -10.104 -26.289 -15.586 1.00 34.05  ?  496  GLU B O   1 
ATOM   7364  C  CB  . GLU B  1 465 ? -9.786  -28.358 -18.184 1.00 35.28  ?  496  GLU B CB  1 
ATOM   7365  C  CG  . GLU B  1 465 ? -10.272 -29.196 -19.407 1.00 47.69  ?  496  GLU B CG  1 
ATOM   7366  C  CD  . GLU B  1 465 ? -10.344 -28.436 -20.747 1.00 48.09  ?  496  GLU B CD  1 
ATOM   7367  O  OE1 . GLU B  1 465 ? -9.289  -28.001 -21.265 1.00 51.36  ?  496  GLU B OE1 1 
ATOM   7368  O  OE2 . GLU B  1 465 ? -11.461 -28.284 -21.294 1.00 56.82  -1 496  GLU B OE2 1 
ATOM   7369  N  N   . ALA B  1 466 ? -8.819  -25.498 -17.255 1.00 32.07  ?  497  ALA B N   1 
ATOM   7370  C  CA  . ALA B  1 466 ? -8.077  -24.652 -16.320 1.00 36.41  ?  497  ALA B CA  1 
ATOM   7371  C  C   . ALA B  1 466 ? -8.973  -23.563 -15.742 1.00 33.75  ?  497  ALA B C   1 
ATOM   7372  O  O   . ALA B  1 466 ? -8.799  -23.154 -14.588 1.00 33.28  ?  497  ALA B O   1 
ATOM   7373  C  CB  . ALA B  1 466 ? -6.861  -24.027 -17.008 1.00 31.63  ?  497  ALA B CB  1 
ATOM   7374  N  N   . THR B  1 467 ? -9.959  -23.125 -16.518 1.00 31.63  ?  498  THR B N   1 
ATOM   7375  C  CA  . THR B  1 467 ? -10.830 -22.043 -16.085 1.00 32.58  ?  498  THR B CA  1 
ATOM   7376  C  C   . THR B  1 467 ? -11.621 -22.432 -14.847 1.00 32.86  ?  498  THR B C   1 
ATOM   7377  O  O   . THR B  1 467 ? -11.826 -21.610 -13.949 1.00 32.11  ?  498  THR B O   1 
ATOM   7378  C  CB  . THR B  1 467 ? -11.751 -21.649 -17.247 1.00 31.26  ?  498  THR B CB  1 
ATOM   7379  O  OG1 . THR B  1 467 ? -10.955 -21.008 -18.244 1.00 33.80  ?  498  THR B OG1 1 
ATOM   7380  C  CG2 . THR B  1 467 ? -12.855 -20.701 -16.804 1.00 28.81  ?  498  THR B CG2 1 
ATOM   7381  N  N   . PHE B  1 468 ? -12.029 -23.693 -14.751 1.00 28.82  ?  499  PHE B N   1 
ATOM   7382  C  CA  . PHE B  1 468 ? -12.850 -24.135 -13.636 1.00 33.90  ?  499  PHE B CA  1 
ATOM   7383  C  C   . PHE B  1 468 ? -12.050 -24.877 -12.566 1.00 34.18  ?  499  PHE B C   1 
ATOM   7384  O  O   . PHE B  1 468 ? -12.641 -25.594 -11.752 1.00 31.93  ?  499  PHE B O   1 
ATOM   7385  C  CB  . PHE B  1 468 ? -14.012 -24.975 -14.166 1.00 34.54  ?  499  PHE B CB  1 
ATOM   7386  C  CG  . PHE B  1 468 ? -14.901 -24.207 -15.090 1.00 33.19  ?  499  PHE B CG  1 
ATOM   7387  C  CD1 . PHE B  1 468 ? -15.719 -23.197 -14.598 1.00 34.14  ?  499  PHE B CD1 1 
ATOM   7388  C  CD2 . PHE B  1 468 ? -14.874 -24.441 -16.457 1.00 33.29  ?  499  PHE B CD2 1 
ATOM   7389  C  CE1 . PHE B  1 468 ? -16.532 -22.445 -15.470 1.00 32.02  ?  499  PHE B CE1 1 
ATOM   7390  C  CE2 . PHE B  1 468 ? -15.678 -23.715 -17.319 1.00 34.38  ?  499  PHE B CE2 1 
ATOM   7391  C  CZ  . PHE B  1 468 ? -16.510 -22.709 -16.816 1.00 34.78  ?  499  PHE B CZ  1 
ATOM   7392  N  N   . GLU B  1 469 ? -10.722 -24.725 -12.566 1.00 34.94  ?  500  GLU B N   1 
ATOM   7393  C  CA  . GLU B  1 469 ? -9.917  -25.066 -11.396 1.00 30.02  ?  500  GLU B CA  1 
ATOM   7394  C  C   . GLU B  1 469 ? -10.342 -24.191 -10.224 1.00 35.18  ?  500  GLU B C   1 
ATOM   7395  O  O   . GLU B  1 469 ? -10.777 -23.048 -10.402 1.00 35.53  ?  500  GLU B O   1 
ATOM   7396  C  CB  . GLU B  1 469 ? -8.434  -24.875 -11.703 1.00 31.15  ?  500  GLU B CB  1 
ATOM   7397  C  CG  . GLU B  1 469 ? -7.863  -25.934 -12.646 1.00 29.54  ?  500  GLU B CG  1 
ATOM   7398  C  CD  . GLU B  1 469 ? -6.474  -25.596 -13.180 1.00 37.86  ?  500  GLU B CD  1 
ATOM   7399  O  OE1 . GLU B  1 469 ? -6.075  -24.411 -13.146 1.00 36.46  ?  500  GLU B OE1 1 
ATOM   7400  O  OE2 . GLU B  1 469 ? -5.777  -26.522 -13.659 1.00 39.23  -1 500  GLU B OE2 1 
ATOM   7401  N  N   . VAL B  1 470 ? -10.271 -24.747 -9.018  1.00 28.52  ?  501  VAL B N   1 
ATOM   7402  C  CA  . VAL B  1 470 ? -10.726 -24.010 -7.846  1.00 32.10  ?  501  VAL B CA  1 
ATOM   7403  C  C   . VAL B  1 470 ? -9.713  -24.128 -6.716  1.00 34.79  ?  501  VAL B C   1 
ATOM   7404  O  O   . VAL B  1 470 ? -9.084  -23.128 -6.344  1.00 33.14  ?  501  VAL B O   1 
ATOM   7405  C  CB  . VAL B  1 470 ? -12.117 -24.473 -7.374  1.00 31.62  ?  501  VAL B CB  1 
ATOM   7406  C  CG1 . VAL B  1 470 ? -12.515 -23.718 -6.104  1.00 38.12  ?  501  VAL B CG1 1 
ATOM   7407  C  CG2 . VAL B  1 470 ? -13.165 -24.221 -8.459  1.00 35.18  ?  501  VAL B CG2 1 
ATOM   7408  N  N   . ASP B  1 471 ? -9.545  -25.341 -6.168  1.00 34.99  ?  502  ASP B N   1 
ATOM   7409  C  CA  . ASP B  1 471 ? -8.772  -25.504 -4.931  1.00 34.65  ?  502  ASP B CA  1 
ATOM   7410  C  C   . ASP B  1 471 ? -7.317  -25.085 -5.105  1.00 36.36  ?  502  ASP B C   1 
ATOM   7411  O  O   . ASP B  1 471 ? -6.731  -24.466 -4.212  1.00 38.05  ?  502  ASP B O   1 
ATOM   7412  C  CB  . ASP B  1 471 ? -8.840  -26.954 -4.441  1.00 37.00  ?  502  ASP B CB  1 
ATOM   7413  C  CG  . ASP B  1 471 ? -10.233 -27.361 -3.997  1.00 44.70  ?  502  ASP B CG  1 
ATOM   7414  O  OD1 . ASP B  1 471 ? -11.070 -26.473 -3.716  1.00 48.21  ?  502  ASP B OD1 1 
ATOM   7415  O  OD2 . ASP B  1 471 ? -10.498 -28.579 -3.927  1.00 51.26  -1 502  ASP B OD2 1 
ATOM   7416  N  N   . LYS B  1 472 ? -6.706  -25.434 -6.236  1.00 32.54  ?  503  LYS B N   1 
ATOM   7417  C  CA  . LYS B  1 472 ? -5.293  -25.131 -6.416  1.00 36.12  ?  503  LYS B CA  1 
ATOM   7418  C  C   . LYS B  1 472 ? -5.029  -23.635 -6.493  1.00 34.61  ?  503  LYS B C   1 
ATOM   7419  O  O   . LYS B  1 472 ? -3.879  -23.215 -6.320  1.00 34.28  ?  503  LYS B O   1 
ATOM   7420  C  CB  . LYS B  1 472 ? -4.756  -25.829 -7.664  1.00 33.51  ?  503  LYS B CB  1 
ATOM   7421  C  CG  . LYS B  1 472 ? -5.258  -25.237 -8.960  1.00 31.70  ?  503  LYS B CG  1 
ATOM   7422  C  CD  . LYS B  1 472 ? -4.627  -25.883 -10.209 1.00 34.48  ?  503  LYS B CD  1 
ATOM   7423  C  CE  . LYS B  1 472 ? -4.988  -27.365 -10.335 1.00 38.44  ?  503  LYS B CE  1 
ATOM   7424  N  NZ  . LYS B  1 472 ? -4.423  -27.944 -11.596 1.00 40.35  ?  503  LYS B NZ  1 
ATOM   7425  N  N   . LEU B  1 473 ? -6.070  -22.820 -6.713  1.00 33.82  ?  504  LEU B N   1 
ATOM   7426  C  CA  . LEU B  1 473 ? -5.887  -21.374 -6.779  1.00 33.16  ?  504  LEU B CA  1 
ATOM   7427  C  C   . LEU B  1 473 ? -5.717  -20.751 -5.404  1.00 31.98  ?  504  LEU B C   1 
ATOM   7428  O  O   . LEU B  1 473 ? -5.120  -19.674 -5.298  1.00 32.82  ?  504  LEU B O   1 
ATOM   7429  C  CB  . LEU B  1 473 ? -7.074  -20.722 -7.506  1.00 28.37  ?  504  LEU B CB  1 
ATOM   7430  C  CG  . LEU B  1 473 ? -7.370  -21.278 -8.896  1.00 32.52  ?  504  LEU B CG  1 
ATOM   7431  C  CD1 . LEU B  1 473 ? -8.612  -20.633 -9.515  1.00 27.52  ?  504  LEU B CD1 1 
ATOM   7432  C  CD2 . LEU B  1 473 ? -6.143  -21.085 -9.795  1.00 33.90  ?  504  LEU B CD2 1 
ATOM   7433  N  N   . VAL B  1 474 ? -6.211  -21.407 -4.353  1.00 29.00  ?  505  VAL B N   1 
ATOM   7434  C  CA  . VAL B  1 474 ? -6.140  -20.864 -3.004  1.00 32.53  ?  505  VAL B CA  1 
ATOM   7435  C  C   . VAL B  1 474 ? -5.261  -21.684 -2.051  1.00 33.86  ?  505  VAL B C   1 
ATOM   7436  O  O   . VAL B  1 474 ? -4.781  -21.125 -1.057  1.00 28.13  ?  505  VAL B O   1 
ATOM   7437  C  CB  . VAL B  1 474 ? -7.551  -20.687 -2.413  1.00 35.74  ?  505  VAL B CB  1 
ATOM   7438  C  CG1 . VAL B  1 474 ? -8.368  -19.764 -3.306  1.00 31.65  ?  505  VAL B CG1 1 
ATOM   7439  C  CG2 . VAL B  1 474 ? -8.234  -22.033 -2.266  1.00 33.47  ?  505  VAL B CG2 1 
ATOM   7440  N  N   . ASP B  1 475 ? -5.030  -22.970 -2.315  1.00 34.64  ?  506  ASP B N   1 
ATOM   7441  C  CA  . ASP B  1 475 ? -4.257  -23.794 -1.387  1.00 36.20  ?  506  ASP B CA  1 
ATOM   7442  C  C   . ASP B  1 475 ? -2.786  -23.424 -1.467  1.00 34.08  ?  506  ASP B C   1 
ATOM   7443  O  O   . ASP B  1 475 ? -2.269  -23.121 -2.547  1.00 36.53  ?  506  ASP B O   1 
ATOM   7444  C  CB  . ASP B  1 475 ? -4.412  -25.283 -1.706  1.00 34.00  ?  506  ASP B CB  1 
ATOM   7445  C  CG  . ASP B  1 475 ? -5.811  -25.804 -1.445  1.00 34.14  ?  506  ASP B CG  1 
ATOM   7446  O  OD1 . ASP B  1 475 ? -6.538  -25.241 -0.608  1.00 36.70  ?  506  ASP B OD1 1 
ATOM   7447  O  OD2 . ASP B  1 475 ? -6.182  -26.805 -2.085  1.00 43.68  -1 506  ASP B OD2 1 
ATOM   7448  N  N   . SER B  1 476 ? -2.107  -23.452 -0.308  1.00 33.21  ?  507  SER B N   1 
ATOM   7449  C  CA  . SER B  1 476 ? -0.681  -23.192 -0.265  1.00 33.60  ?  507  SER B CA  1 
ATOM   7450  C  C   . SER B  1 476 ? 0.084   -24.478 -0.587  1.00 38.70  ?  507  SER B C   1 
ATOM   7451  O  O   . SER B  1 476 ? -0.355  -25.567 -0.207  1.00 33.40  ?  507  SER B O   1 
ATOM   7452  C  CB  . SER B  1 476 ? -0.282  -22.672 1.114   1.00 38.28  ?  507  SER B CB  1 
ATOM   7453  O  OG  . SER B  1 476 ? 1.117   -22.742 1.325   1.00 31.17  ?  507  SER B OG  1 
ATOM   7454  N  N   . PRO B  1 477 ? 1.218   -24.387 -1.297  1.00 32.70  ?  508  PRO B N   1 
ATOM   7455  C  CA  . PRO B  1 477 ? 2.017   -25.593 -1.558  1.00 38.18  ?  508  PRO B CA  1 
ATOM   7456  C  C   . PRO B  1 477 ? 2.706   -26.128 -0.316  1.00 39.70  ?  508  PRO B C   1 
ATOM   7457  O  O   . PRO B  1 477 ? 3.186   -27.264 -0.342  1.00 40.77  ?  508  PRO B O   1 
ATOM   7458  C  CB  . PRO B  1 477 ? 3.056   -25.113 -2.581  1.00 37.93  ?  508  PRO B CB  1 
ATOM   7459  C  CG  . PRO B  1 477 ? 2.581   -23.774 -3.043  1.00 36.71  ?  508  PRO B CG  1 
ATOM   7460  C  CD  . PRO B  1 477 ? 1.837   -23.199 -1.900  1.00 32.99  ?  508  PRO B CD  1 
ATOM   7461  N  N   . TYR B  1 478 ? 2.751   -25.354 0.766   1.00 37.53  ?  509  TYR B N   1 
ATOM   7462  C  CA  . TYR B  1 478 ? 3.576   -25.651 1.928   1.00 40.88  ?  509  TYR B CA  1 
ATOM   7463  C  C   . TYR B  1 478 ? 2.788   -26.115 3.146   1.00 39.84  ?  509  TYR B C   1 
ATOM   7464  O  O   . TYR B  1 478 ? 3.398   -26.381 4.183   1.00 50.15  ?  509  TYR B O   1 
ATOM   7465  C  CB  . TYR B  1 478 ? 4.425   -24.418 2.262   1.00 35.03  ?  509  TYR B CB  1 
ATOM   7466  C  CG  . TYR B  1 478 ? 5.036   -23.802 1.017   1.00 39.23  ?  509  TYR B CG  1 
ATOM   7467  C  CD1 . TYR B  1 478 ? 6.024   -24.475 0.311   1.00 36.56  ?  509  TYR B CD1 1 
ATOM   7468  C  CD2 . TYR B  1 478 ? 4.581   -22.592 0.504   1.00 34.65  ?  509  TYR B CD2 1 
ATOM   7469  C  CE1 . TYR B  1 478 ? 6.586   -23.948 -0.831  1.00 37.06  ?  509  TYR B CE1 1 
ATOM   7470  C  CE2 . TYR B  1 478 ? 5.137   -22.057 -0.644  1.00 35.15  ?  509  TYR B CE2 1 
ATOM   7471  C  CZ  . TYR B  1 478 ? 6.141   -22.743 -1.310  1.00 37.25  ?  509  TYR B CZ  1 
ATOM   7472  O  OH  . TYR B  1 478 ? 6.717   -22.226 -2.458  1.00 33.97  ?  509  TYR B OH  1 
ATOM   7473  N  N   . HIS B  1 479 ? 1.466   -26.237 3.048   1.00 42.02  ?  510  HIS B N   1 
ATOM   7474  C  CA  . HIS B  1 479 ? 0.661   -26.926 4.071   1.00 53.94  ?  510  HIS B CA  1 
ATOM   7475  C  C   . HIS B  1 479 ? 1.216   -28.322 4.396   1.00 58.70  ?  510  HIS B C   1 
ATOM   7476  O  O   . HIS B  1 479 ? 1.549   -28.631 5.550   1.00 65.21  ?  510  HIS B O   1 
ATOM   7477  C  CB  . HIS B  1 479 ? -0.799  -27.056 3.615   1.00 50.64  ?  510  HIS B CB  1 
ATOM   7478  N  N   . THR C  1 15  ? -31.832 66.175  -8.735  1.00 63.02  ?  46   THR C N   1 
ATOM   7479  C  CA  . THR C  1 15  ? -31.648 64.726  -8.707  1.00 64.19  ?  46   THR C CA  1 
ATOM   7480  C  C   . THR C  1 15  ? -31.046 64.240  -7.392  1.00 57.85  ?  46   THR C C   1 
ATOM   7481  O  O   . THR C  1 15  ? -29.908 64.574  -7.035  1.00 59.17  ?  46   THR C O   1 
ATOM   7482  C  CB  . THR C  1 15  ? -30.759 64.236  -9.877  1.00 65.71  ?  46   THR C CB  1 
ATOM   7483  O  OG1 . THR C  1 15  ? -31.485 64.345  -11.106 1.00 67.77  ?  46   THR C OG1 1 
ATOM   7484  C  CG2 . THR C  1 15  ? -30.324 62.789  -9.669  1.00 61.47  ?  46   THR C CG2 1 
ATOM   7485  N  N   . ARG C  1 16  ? -31.843 63.459  -6.675  1.00 56.06  ?  47   ARG C N   1 
ATOM   7486  C  CA  . ARG C  1 16  ? -31.363 62.811  -5.467  1.00 48.36  ?  47   ARG C CA  1 
ATOM   7487  C  C   . ARG C  1 16  ? -30.122 61.981  -5.783  1.00 41.45  ?  47   ARG C C   1 
ATOM   7488  O  O   . ARG C  1 16  ? -30.029 61.376  -6.857  1.00 45.38  ?  47   ARG C O   1 
ATOM   7489  C  CB  . ARG C  1 16  ? -32.459 61.930  -4.873  1.00 47.61  ?  47   ARG C CB  1 
ATOM   7490  C  CG  . ARG C  1 16  ? -33.659 62.708  -4.385  1.00 46.79  ?  47   ARG C CG  1 
ATOM   7491  C  CD  . ARG C  1 16  ? -34.816 61.770  -4.099  1.00 48.91  ?  47   ARG C CD  1 
ATOM   7492  N  NE  . ARG C  1 16  ? -35.191 60.995  -5.277  1.00 46.20  ?  47   ARG C NE  1 
ATOM   7493  C  CZ  . ARG C  1 16  ? -36.054 59.989  -5.261  1.00 44.89  ?  47   ARG C CZ  1 
ATOM   7494  N  NH1 . ARG C  1 16  ? -36.680 59.631  -4.149  1.00 43.48  ?  47   ARG C NH1 1 
ATOM   7495  N  NH2 . ARG C  1 16  ? -36.289 59.319  -6.386  1.00 47.99  ?  47   ARG C NH2 1 
ATOM   7496  N  N   . PRO C  1 17  ? -29.151 61.936  -4.882  1.00 44.82  ?  48   PRO C N   1 
ATOM   7497  C  CA  . PRO C  1 17  ? -27.901 61.238  -5.175  1.00 41.83  ?  48   PRO C CA  1 
ATOM   7498  C  C   . PRO C  1 17  ? -28.029 59.735  -4.990  1.00 34.27  ?  48   PRO C C   1 
ATOM   7499  O  O   . PRO C  1 17  ? -28.840 59.241  -4.205  1.00 38.63  ?  48   PRO C O   1 
ATOM   7500  C  CB  . PRO C  1 17  ? -26.934 61.838  -4.148  1.00 41.51  ?  48   PRO C CB  1 
ATOM   7501  C  CG  . PRO C  1 17  ? -27.824 62.066  -2.952  1.00 39.59  ?  48   PRO C CG  1 
ATOM   7502  C  CD  . PRO C  1 17  ? -29.178 62.471  -3.512  1.00 41.09  ?  48   PRO C CD  1 
ATOM   7503  N  N   . ASN C  1 18  ? -27.219 59.006  -5.743  1.00 37.57  ?  49   ASN C N   1 
ATOM   7504  C  CA  . ASN C  1 18  ? -26.992 57.604  -5.435  1.00 37.73  ?  49   ASN C CA  1 
ATOM   7505  C  C   . ASN C  1 18  ? -26.264 57.483  -4.102  1.00 41.03  ?  49   ASN C C   1 
ATOM   7506  O  O   . ASN C  1 18  ? -25.554 58.400  -3.677  1.00 41.25  ?  49   ASN C O   1 
ATOM   7507  C  CB  . ASN C  1 18  ? -26.158 56.947  -6.524  1.00 39.20  ?  49   ASN C CB  1 
ATOM   7508  C  CG  . ASN C  1 18  ? -26.697 57.215  -7.906  1.00 46.31  ?  49   ASN C CG  1 
ATOM   7509  O  OD1 . ASN C  1 18  ? -27.888 57.026  -8.165  1.00 41.54  ?  49   ASN C OD1 1 
ATOM   7510  N  ND2 . ASN C  1 18  ? -25.820 57.639  -8.810  1.00 43.14  ?  49   ASN C ND2 1 
ATOM   7511  N  N   . ILE C  1 19  ? -26.441 56.339  -3.442  1.00 35.48  ?  50   ILE C N   1 
ATOM   7512  C  CA  . ILE C  1 19  ? -25.830 56.087  -2.143  1.00 32.46  ?  50   ILE C CA  1 
ATOM   7513  C  C   . ILE C  1 19  ? -25.163 54.728  -2.201  1.00 40.16  ?  50   ILE C C   1 
ATOM   7514  O  O   . ILE C  1 19  ? -25.824 53.723  -2.483  1.00 35.10  ?  50   ILE C O   1 
ATOM   7515  C  CB  . ILE C  1 19  ? -26.846 56.127  -0.995  1.00 36.98  ?  50   ILE C CB  1 
ATOM   7516  C  CG1 . ILE C  1 19  ? -27.426 57.529  -0.857  1.00 35.91  ?  50   ILE C CG1 1 
ATOM   7517  C  CG2 . ILE C  1 19  ? -26.158 55.693  0.321   1.00 33.86  ?  50   ILE C CG2 1 
ATOM   7518  C  CD1 . ILE C  1 19  ? -28.743 57.561  -0.149  1.00 41.21  ?  50   ILE C CD1 1 
ATOM   7519  N  N   . LEU C  1 20  ? -23.859 54.692  -1.937  1.00 34.03  ?  51   LEU C N   1 
ATOM   7520  C  CA  . LEU C  1 20  ? -23.095 53.454  -1.939  1.00 35.80  ?  51   LEU C CA  1 
ATOM   7521  C  C   . LEU C  1 20  ? -22.418 53.329  -0.589  1.00 37.04  ?  51   LEU C C   1 
ATOM   7522  O  O   . LEU C  1 20  ? -21.595 54.181  -0.236  1.00 37.19  ?  51   LEU C O   1 
ATOM   7523  C  CB  . LEU C  1 20  ? -22.057 53.444  -3.062  1.00 31.47  ?  51   LEU C CB  1 
ATOM   7524  C  CG  . LEU C  1 20  ? -20.994 52.354  -2.907  1.00 37.13  ?  51   LEU C CG  1 
ATOM   7525  C  CD1 . LEU C  1 20  ? -21.622 50.949  -2.987  1.00 33.92  ?  51   LEU C CD1 1 
ATOM   7526  C  CD2 . LEU C  1 20  ? -19.884 52.516  -3.930  1.00 32.30  ?  51   LEU C CD2 1 
ATOM   7527  N  N   . VAL C  1 21  ? -22.798 52.300  0.174   1.00 32.23  ?  52   VAL C N   1 
ATOM   7528  C  CA  . VAL C  1 21  ? -22.193 51.986  1.462   1.00 34.28  ?  52   VAL C CA  1 
ATOM   7529  C  C   . VAL C  1 21  ? -21.165 50.900  1.223   1.00 35.61  ?  52   VAL C C   1 
ATOM   7530  O  O   . VAL C  1 21  ? -21.494 49.825  0.708   1.00 31.33  ?  52   VAL C O   1 
ATOM   7531  C  CB  . VAL C  1 21  ? -23.241 51.527  2.489   1.00 33.67  ?  52   VAL C CB  1 
ATOM   7532  C  CG1 . VAL C  1 21  ? -22.559 51.123  3.799   1.00 32.05  ?  52   VAL C CG1 1 
ATOM   7533  C  CG2 . VAL C  1 21  ? -24.278 52.604  2.712   1.00 36.65  ?  52   VAL C CG2 1 
ATOM   7534  N  N   . VAL C  1 22  ? -19.910 51.180  1.554   1.00 34.09  ?  53   VAL C N   1 
ATOM   7535  C  CA  . VAL C  1 22  ? -18.873 50.163  1.519   1.00 34.04  ?  53   VAL C CA  1 
ATOM   7536  C  C   . VAL C  1 22  ? -18.541 49.872  2.964   1.00 35.60  ?  53   VAL C C   1 
ATOM   7537  O  O   . VAL C  1 22  ? -18.014 50.741  3.668   1.00 33.70  ?  53   VAL C O   1 
ATOM   7538  C  CB  . VAL C  1 22  ? -17.635 50.605  0.732   1.00 32.67  ?  53   VAL C CB  1 
ATOM   7539  C  CG1 . VAL C  1 22  ? -16.665 49.475  0.680   1.00 32.37  ?  53   VAL C CG1 1 
ATOM   7540  C  CG2 . VAL C  1 22  ? -18.027 50.986  -0.689  1.00 33.98  ?  53   VAL C CG2 1 
ATOM   7541  N  N   . LEU C  1 23  ? -18.903 48.673  3.416   1.00 32.09  ?  54   LEU C N   1 
ATOM   7542  C  CA  . LEU C  1 23  ? -18.773 48.260  4.806   1.00 33.03  ?  54   LEU C CA  1 
ATOM   7543  C  C   . LEU C  1 23  ? -17.840 47.061  4.846   1.00 34.50  ?  54   LEU C C   1 
ATOM   7544  O  O   . LEU C  1 23  ? -18.159 46.005  4.289   1.00 31.59  ?  54   LEU C O   1 
ATOM   7545  C  CB  . LEU C  1 23  ? -20.134 47.918  5.399   1.00 30.38  ?  54   LEU C CB  1 
ATOM   7546  C  CG  . LEU C  1 23  ? -20.149 47.436  6.854   1.00 31.30  ?  54   LEU C CG  1 
ATOM   7547  C  CD1 . LEU C  1 23  ? -19.892 48.584  7.787   1.00 27.66  ?  54   LEU C CD1 1 
ATOM   7548  C  CD2 . LEU C  1 23  ? -21.481 46.768  7.191   1.00 31.09  ?  54   LEU C CD2 1 
ATOM   7549  N  N   . CYS C  1 24  ? -16.673 47.240  5.459   1.00 31.85  ?  55   CYS C N   1 
ATOM   7550  C  CA  . CYS C  1 24  ? -15.767 46.138  5.717   1.00 28.20  ?  55   CYS C CA  1 
ATOM   7551  C  C   . CYS C  1 24  ? -16.093 45.485  7.062   1.00 28.49  ?  55   CYS C C   1 
ATOM   7552  O  O   . CYS C  1 24  ? -16.831 46.019  7.892   1.00 31.48  ?  55   CYS C O   1 
ATOM   7553  C  CB  . CYS C  1 24  ? -14.312 46.626  5.698   1.00 36.12  ?  55   CYS C CB  1 
ATOM   7554  S  SG  . CYS C  1 24  ? -13.696 47.021  4.052   1.00 36.89  ?  55   CYS C SG  1 
ATOM   7555  N  N   . ASP C  1 25  ? -15.525 44.293  7.216   1.00 27.71  ?  56   ASP C N   1 
ATOM   7556  C  CA  . ASP C  1 25  ? -15.847 43.481  8.408   1.00 29.92  ?  56   ASP C CA  1 
ATOM   7557  C  C   . ASP C  1 25  ? -14.578 43.305  9.248   1.00 25.39  ?  56   ASP C C   1 
ATOM   7558  O  O   . ASP C  1 25  ? -13.644 42.665  8.745   1.00 29.70  ?  56   ASP C O   1 
ATOM   7559  C  CB  . ASP C  1 25  ? -16.458 42.171  7.961   1.00 28.26  ?  56   ASP C CB  1 
ATOM   7560  C  CG  . ASP C  1 25  ? -17.085 41.329  9.061   1.00 32.85  ?  56   ASP C CG  1 
ATOM   7561  O  OD1 . ASP C  1 25  ? -17.156 41.823  10.206  1.00 29.45  ?  56   ASP C OD1 1 
ATOM   7562  O  OD2 . ASP C  1 25  ? -17.504 40.198  8.754   1.00 31.61  -1 56   ASP C OD2 1 
ATOM   7563  N  N   . ASP C  1 26  ? -14.572 43.850  10.466  1.00 27.64  ?  57   ASP C N   1 
ATOM   7564  C  CA  . ASP C  1 26  ? -13.386 43.759  11.386  1.00 26.93  ?  57   ASP C CA  1 
ATOM   7565  C  C   . ASP C  1 26  ? -12.147 44.481  10.821  1.00 29.52  ?  57   ASP C C   1 
ATOM   7566  O  O   . ASP C  1 26  ? -11.028 43.992  11.026  1.00 32.12  ?  57   ASP C O   1 
ATOM   7567  C  CB  . ASP C  1 26  ? -13.017 42.339  11.781  1.00 29.03  ?  57   ASP C CB  1 
ATOM   7568  C  CG  . ASP C  1 26  ? -14.077 41.549  12.536  1.00 33.19  ?  57   ASP C CG  1 
ATOM   7569  O  OD1 . ASP C  1 26  ? -15.144 42.123  12.824  1.00 30.87  ?  57   ASP C OD1 1 
ATOM   7570  O  OD2 . ASP C  1 26  ? -13.815 40.366  12.837  1.00 31.00  -1 57   ASP C OD2 1 
ATOM   7571  N  N   . LEU C  1 27  ? -12.337 45.619  10.161  1.00 31.63  ?  58   LEU C N   1 
ATOM   7572  C  CA  . LEU C  1 27  ? -11.211 46.411  9.682   1.00 31.52  ?  58   LEU C CA  1 
ATOM   7573  C  C   . LEU C  1 27  ? -10.647 47.247  10.823  1.00 32.62  ?  58   LEU C C   1 
ATOM   7574  O  O   . LEU C  1 27  ? -11.383 48.016  11.454  1.00 31.68  ?  58   LEU C O   1 
ATOM   7575  C  CB  . LEU C  1 27  ? -11.668 47.314  8.539   1.00 32.87  ?  58   LEU C CB  1 
ATOM   7576  C  CG  . LEU C  1 27  ? -10.628 48.279  7.965   1.00 33.27  ?  58   LEU C CG  1 
ATOM   7577  C  CD1 . LEU C  1 27  ? -9.507  47.533  7.252   1.00 30.77  ?  58   LEU C CD1 1 
ATOM   7578  C  CD2 . LEU C  1 27  ? -11.321 49.284  7.031   1.00 32.46  ?  58   LEU C CD2 1 
ATOM   7579  N  N   . GLY C  1 28  ? -9.335  47.108  11.080  1.00 28.29  ?  59   GLY C N   1 
ATOM   7580  C  CA  . GLY C  1 28  ? -8.710  47.821  12.182  1.00 31.46  ?  59   GLY C CA  1 
ATOM   7581  C  C   . GLY C  1 28  ? -8.518  49.308  11.921  1.00 34.94  ?  59   GLY C C   1 
ATOM   7582  O  O   . GLY C  1 28  ? -8.427  49.769  10.784  1.00 34.66  ?  59   GLY C O   1 
ATOM   7583  N  N   . TYR C  1 29  ? -8.430  50.076  13.015  1.00 31.06  ?  60   TYR C N   1 
ATOM   7584  C  CA  . TYR C  1 29  ? -8.451  51.536  12.901  1.00 34.90  ?  60   TYR C CA  1 
ATOM   7585  C  C   . TYR C  1 29  ? -7.308  52.050  12.043  1.00 36.96  ?  60   TYR C C   1 
ATOM   7586  O  O   . TYR C  1 29  ? -7.474  53.002  11.273  1.00 35.89  ?  60   TYR C O   1 
ATOM   7587  C  CB  . TYR C  1 29  ? -8.388  52.173  14.285  1.00 30.75  ?  60   TYR C CB  1 
ATOM   7588  C  CG  . TYR C  1 29  ? -8.978  53.564  14.347  1.00 32.83  ?  60   TYR C CG  1 
ATOM   7589  C  CD1 . TYR C  1 29  ? -10.294 53.785  13.983  1.00 32.15  ?  60   TYR C CD1 1 
ATOM   7590  C  CD2 . TYR C  1 29  ? -8.227  54.652  14.810  1.00 35.16  ?  60   TYR C CD2 1 
ATOM   7591  C  CE1 . TYR C  1 29  ? -10.862 55.045  14.050  1.00 31.25  ?  60   TYR C CE1 1 
ATOM   7592  C  CE2 . TYR C  1 29  ? -8.790  55.935  14.890  1.00 34.21  ?  60   TYR C CE2 1 
ATOM   7593  C  CZ  . TYR C  1 29  ? -10.115 56.117  14.489  1.00 34.05  ?  60   TYR C CZ  1 
ATOM   7594  O  OH  . TYR C  1 29  ? -10.706 57.356  14.571  1.00 30.72  ?  60   TYR C OH  1 
ATOM   7595  N  N   . ALA C  1 30  ? -6.144  51.422  12.148  1.00 35.27  ?  61   ALA C N   1 
ATOM   7596  C  CA  . ALA C  1 30  ? -4.942  51.885  11.471  1.00 38.50  ?  61   ALA C CA  1 
ATOM   7597  C  C   . ALA C  1 30  ? -4.627  51.065  10.230  1.00 37.46  ?  61   ALA C C   1 
ATOM   7598  O  O   . ALA C  1 30  ? -3.466  50.961  9.845   1.00 38.93  ?  61   ALA C O   1 
ATOM   7599  C  CB  . ALA C  1 30  ? -3.756  51.860  12.449  1.00 35.45  ?  61   ALA C CB  1 
ATOM   7600  N  N   . ASP C  1 31  ? -5.633  50.463  9.595   1.00 34.90  ?  62   ASP C N   1 
ATOM   7601  C  CA  . ASP C  1 31  ? -5.402  49.524  8.500   1.00 36.21  ?  62   ASP C CA  1 
ATOM   7602  C  C   . ASP C  1 31  ? -5.846  50.038  7.137   1.00 36.76  ?  62   ASP C C   1 
ATOM   7603  O  O   . ASP C  1 31  ? -5.901  49.257  6.178   1.00 34.13  ?  62   ASP C O   1 
ATOM   7604  C  CB  . ASP C  1 31  ? -6.053  48.169  8.835   1.00 34.46  ?  62   ASP C CB  1 
ATOM   7605  C  CG  . ASP C  1 31  ? -5.432  47.521  10.091  1.00 36.01  ?  62   ASP C CG  1 
ATOM   7606  O  OD1 . ASP C  1 31  ? -4.288  47.888  10.450  1.00 34.43  -1 62   ASP C OD1 1 
ATOM   7607  O  OD2 . ASP C  1 31  ? -5.990  46.528  10.610  1.00 34.10  ?  62   ASP C OD2 1 
ATOM   7608  N  N   . VAL C  1 32  ? -6.115  51.329  7.008   1.00 36.08  ?  63   VAL C N   1 
ATOM   7609  C  CA  . VAL C  1 32  ? -6.173  51.952  5.694   1.00 36.68  ?  63   VAL C CA  1 
ATOM   7610  C  C   . VAL C  1 32  ? -5.257  53.167  5.705   1.00 36.78  ?  63   VAL C C   1 
ATOM   7611  O  O   . VAL C  1 32  ? -5.033  53.786  6.752   1.00 38.56  ?  63   VAL C O   1 
ATOM   7612  C  CB  . VAL C  1 32  ? -7.611  52.343  5.294   1.00 33.26  ?  63   VAL C CB  1 
ATOM   7613  C  CG1 . VAL C  1 32  ? -8.411  51.090  5.011   1.00 35.66  ?  63   VAL C CG1 1 
ATOM   7614  C  CG2 . VAL C  1 32  ? -8.271  53.167  6.389   1.00 36.96  ?  63   VAL C CG2 1 
ATOM   7615  N  N   . GLY C  1 33  ? -4.708  53.486  4.529   1.00 35.86  ?  64   GLY C N   1 
ATOM   7616  C  CA  . GLY C  1 33  ? -3.765  54.592  4.432   1.00 38.95  ?  64   GLY C CA  1 
ATOM   7617  C  C   . GLY C  1 33  ? -4.310  55.879  5.012   1.00 39.58  ?  64   GLY C C   1 
ATOM   7618  O  O   . GLY C  1 33  ? -3.655  56.538  5.823   1.00 38.87  ?  64   GLY C O   1 
ATOM   7619  N  N   . PHE C  1 34  ? -5.543  56.236  4.643   1.00 35.37  ?  65   PHE C N   1 
ATOM   7620  C  CA  . PHE C  1 34  ? -6.069  57.534  5.047   1.00 37.17  ?  65   PHE C CA  1 
ATOM   7621  C  C   . PHE C  1 34  ? -6.311  57.620  6.546   1.00 39.87  ?  65   PHE C C   1 
ATOM   7622  O  O   . PHE C  1 34  ? -6.500  58.722  7.070   1.00 35.41  ?  65   PHE C O   1 
ATOM   7623  C  CB  . PHE C  1 34  ? -7.363  57.872  4.271   1.00 40.86  ?  65   PHE C CB  1 
ATOM   7624  C  CG  . PHE C  1 34  ? -8.582  57.070  4.688   1.00 36.72  ?  65   PHE C CG  1 
ATOM   7625  C  CD1 . PHE C  1 34  ? -9.412  57.507  5.708   1.00 36.61  ?  65   PHE C CD1 1 
ATOM   7626  C  CD2 . PHE C  1 34  ? -8.921  55.909  4.016   1.00 38.11  ?  65   PHE C CD2 1 
ATOM   7627  C  CE1 . PHE C  1 34  ? -10.531 56.770  6.082   1.00 34.22  ?  65   PHE C CE1 1 
ATOM   7628  C  CE2 . PHE C  1 34  ? -10.054 55.170  4.374   1.00 33.80  ?  65   PHE C CE2 1 
ATOM   7629  C  CZ  . PHE C  1 34  ? -10.849 55.597  5.400   1.00 31.94  ?  65   PHE C CZ  1 
ATOM   7630  N  N   . ASN C  1 35  ? -6.314  56.492  7.250   1.00 36.49  ?  66   ASN C N   1 
ATOM   7631  C  CA  . ASN C  1 35  ? -6.509  56.526  8.684   1.00 38.31  ?  66   ASN C CA  1 
ATOM   7632  C  C   . ASN C  1 35  ? -5.237  56.186  9.446   1.00 40.62  ?  66   ASN C C   1 
ATOM   7633  O  O   . ASN C  1 35  ? -5.305  55.894  10.642  1.00 40.88  ?  66   ASN C O   1 
ATOM   7634  C  CB  . ASN C  1 35  ? -7.652  55.600  9.093   1.00 31.76  ?  66   ASN C CB  1 
ATOM   7635  C  CG  . ASN C  1 35  ? -8.465  56.181  10.221  1.00 32.79  ?  66   ASN C CG  1 
ATOM   7636  O  OD1 . ASN C  1 35  ? -8.839  57.347  10.177  1.00 33.01  ?  66   ASN C OD1 1 
ATOM   7637  N  ND2 . ASN C  1 35  ? -8.698  55.385  11.271  1.00 35.48  ?  66   ASN C ND2 1 
ATOM   7638  N  N   . GLY C  1 36  ? -4.087  56.212  8.779   1.00 37.64  ?  67   GLY C N   1 
ATOM   7639  C  CA  . GLY C  1 36  ? -2.806  56.094  9.436   1.00 40.70  ?  67   GLY C CA  1 
ATOM   7640  C  C   . GLY C  1 36  ? -1.981  54.891  9.044   1.00 42.96  ?  67   GLY C C   1 
ATOM   7641  O  O   . GLY C  1 36  ? -0.893  54.724  9.602   1.00 40.66  ?  67   GLY C O   1 
ATOM   7642  N  N   . SER C  1 37  ? -2.388  54.019  8.127   1.00 42.59  ?  68   SER C N   1 
ATOM   7643  C  CA  . SER C  1 37  ? -1.576  52.830  7.893   1.00 41.04  ?  68   SER C CA  1 
ATOM   7644  C  C   . SER C  1 37  ? -0.263  53.186  7.210   1.00 46.53  ?  68   SER C C   1 
ATOM   7645  O  O   . SER C  1 37  ? -0.227  53.973  6.263   1.00 47.11  ?  68   SER C O   1 
ATOM   7646  C  CB  . SER C  1 37  ? -2.310  51.801  7.050   1.00 36.11  ?  68   SER C CB  1 
ATOM   7647  O  OG  . SER C  1 37  ? -1.587  50.583  7.032   1.00 35.21  ?  68   SER C OG  1 
ATOM   7648  N  N   . THR C  1 38  ? 0.821   52.576  7.688   1.00 39.69  ?  69   THR C N   1 
ATOM   7649  C  CA  . THR C  1 38  ? 2.114   52.720  7.052   1.00 44.65  ?  69   THR C CA  1 
ATOM   7650  C  C   . THR C  1 38  ? 2.573   51.448  6.371   1.00 45.11  ?  69   THR C C   1 
ATOM   7651  O  O   . THR C  1 38  ? 3.611   51.472  5.709   1.00 48.31  ?  69   THR C O   1 
ATOM   7652  C  CB  . THR C  1 38  ? 3.181   53.151  8.075   1.00 44.60  ?  69   THR C CB  1 
ATOM   7653  O  OG1 . THR C  1 38  ? 3.264   52.175  9.123   1.00 46.49  ?  69   THR C OG1 1 
ATOM   7654  C  CG2 . THR C  1 38  ? 2.824   54.507  8.681   1.00 42.58  ?  69   THR C CG2 1 
ATOM   7655  N  N   . ASP C  1 39  ? 1.850   50.334  6.524   1.00 41.03  ?  70   ASP C N   1 
ATOM   7656  C  CA  . ASP C  1 39  ? 2.205   49.118  5.802   1.00 37.87  ?  70   ASP C CA  1 
ATOM   7657  C  C   . ASP C  1 39  ? 1.126   48.599  4.857   1.00 39.08  ?  70   ASP C C   1 
ATOM   7658  O  O   . ASP C  1 39  ? 1.457   47.898  3.898   1.00 38.63  ?  70   ASP C O   1 
ATOM   7659  C  CB  . ASP C  1 39  ? 2.580   47.987  6.768   1.00 37.80  ?  70   ASP C CB  1 
ATOM   7660  C  CG  . ASP C  1 39  ? 1.526   47.738  7.857   1.00 41.27  ?  70   ASP C CG  1 
ATOM   7661  O  OD1 . ASP C  1 39  ? 0.598   48.550  8.057   1.00 40.24  ?  70   ASP C OD1 1 
ATOM   7662  O  OD2 . ASP C  1 39  ? 1.665   46.703  8.547   1.00 42.77  -1 70   ASP C OD2 1 
ATOM   7663  N  N   . ILE C  1 40  ? -0.140  48.891  5.099   1.00 39.80  ?  71   ILE C N   1 
ATOM   7664  C  CA  . ILE C  1 40  ? -1.207  48.406  4.224   1.00 37.52  ?  71   ILE C CA  1 
ATOM   7665  C  C   . ILE C  1 40  ? -1.498  49.490  3.196   1.00 37.25  ?  71   ILE C C   1 
ATOM   7666  O  O   . ILE C  1 40  ? -1.753  50.644  3.556   1.00 42.74  ?  71   ILE C O   1 
ATOM   7667  C  CB  . ILE C  1 40  ? -2.464  48.040  5.033   1.00 34.89  ?  71   ILE C CB  1 
ATOM   7668  C  CG1 . ILE C  1 40  ? -2.120  46.975  6.091   1.00 35.16  ?  71   ILE C CG1 1 
ATOM   7669  C  CG2 . ILE C  1 40  ? -3.580  47.542  4.085   1.00 36.27  ?  71   ILE C CG2 1 
ATOM   7670  C  CD1 . ILE C  1 40  ? -3.332  46.297  6.760   1.00 35.19  ?  71   ILE C CD1 1 
ATOM   7671  N  N   . LEU C  1 41  ? -1.432  49.130  1.916   1.00 37.99  ?  72   LEU C N   1 
ATOM   7672  C  CA  . LEU C  1 41  ? -1.609  50.076  0.816   1.00 41.38  ?  72   LEU C CA  1 
ATOM   7673  C  C   . LEU C  1 41  ? -3.049  50.040  0.316   1.00 38.71  ?  72   LEU C C   1 
ATOM   7674  O  O   . LEU C  1 41  ? -3.518  48.995  -0.131  1.00 39.18  ?  72   LEU C O   1 
ATOM   7675  C  CB  . LEU C  1 41  ? -0.648  49.740  -0.323  1.00 40.55  ?  72   LEU C CB  1 
ATOM   7676  C  CG  . LEU C  1 41  ? 0.798   49.730  0.169   1.00 45.57  ?  72   LEU C CG  1 
ATOM   7677  C  CD1 . LEU C  1 41  ? 1.740   49.350  -0.948  1.00 47.49  ?  72   LEU C CD1 1 
ATOM   7678  C  CD2 . LEU C  1 41  ? 1.111   51.128  0.683   1.00 41.25  ?  72   LEU C CD2 1 
ATOM   7679  N  N   . THR C  1 42  ? -3.748  51.175  0.401   1.00 35.16  ?  73   THR C N   1 
ATOM   7680  C  CA  . THR C  1 42  ? -5.122  51.294  -0.090  1.00 38.50  ?  73   THR C CA  1 
ATOM   7681  C  C   . THR C  1 42  ? -5.267  52.566  -0.926  1.00 37.90  ?  73   THR C C   1 
ATOM   7682  O  O   . THR C  1 42  ? -5.976  53.507  -0.549  1.00 36.23  ?  73   THR C O   1 
ATOM   7683  C  CB  . THR C  1 42  ? -6.100  51.287  1.080   1.00 36.25  ?  73   THR C CB  1 
ATOM   7684  O  OG1 . THR C  1 42  ? -5.765  52.351  1.970   1.00 38.12  ?  73   THR C OG1 1 
ATOM   7685  C  CG2 . THR C  1 42  ? -6.010  49.965  1.837   1.00 37.02  ?  73   THR C CG2 1 
ATOM   7686  N  N   . PRO C  1 43  ? -4.586  52.630  -2.070  1.00 35.68  ?  74   PRO C N   1 
ATOM   7687  C  CA  . PRO C  1 43  ? -4.576  53.888  -2.834  1.00 39.22  ?  74   PRO C CA  1 
ATOM   7688  C  C   . PRO C  1 43  ? -5.952  54.345  -3.305  1.00 42.43  ?  74   PRO C C   1 
ATOM   7689  O  O   . PRO C  1 43  ? -6.229  55.557  -3.297  1.00 38.03  ?  74   PRO C O   1 
ATOM   7690  C  CB  . PRO C  1 43  ? -3.641  53.566  -4.010  1.00 36.63  ?  74   PRO C CB  1 
ATOM   7691  C  CG  . PRO C  1 43  ? -3.587  52.084  -4.082  1.00 37.86  ?  74   PRO C CG  1 
ATOM   7692  C  CD  . PRO C  1 43  ? -3.726  51.607  -2.682  1.00 37.45  ?  74   PRO C CD  1 
ATOM   7693  N  N   . GLU C  1 44  ? -6.841  53.422  -3.695  1.00 40.35  ?  75   GLU C N   1 
ATOM   7694  C  CA  . GLU C  1 44  ? -8.142  53.855  -4.201  1.00 37.20  ?  75   GLU C CA  1 
ATOM   7695  C  C   . GLU C  1 44  ? -8.998  54.429  -3.077  1.00 43.04  ?  75   GLU C C   1 
ATOM   7696  O  O   . GLU C  1 44  ? -9.621  55.494  -3.227  1.00 38.63  ?  75   GLU C O   1 
ATOM   7697  C  CB  . GLU C  1 44  ? -8.853  52.692  -4.899  1.00 43.22  ?  75   GLU C CB  1 
ATOM   7698  C  CG  . GLU C  1 44  ? -8.032  52.006  -5.998  1.00 35.27  ?  75   GLU C CG  1 
ATOM   7699  C  CD  . GLU C  1 44  ? -7.947  52.844  -7.270  1.00 43.04  ?  75   GLU C CD  1 
ATOM   7700  O  OE1 . GLU C  1 44  ? -8.668  53.870  -7.365  1.00 45.80  ?  75   GLU C OE1 1 
ATOM   7701  O  OE2 . GLU C  1 44  ? -7.165  52.475  -8.177  1.00 45.12  -1 75   GLU C OE2 1 
ATOM   7702  N  N   . LEU C  1 45  ? -9.037  53.734  -1.934  1.00 37.80  ?  76   LEU C N   1 
ATOM   7703  C  CA  . LEU C  1 45  ? -9.777  54.250  -0.793  1.00 36.79  ?  76   LEU C CA  1 
ATOM   7704  C  C   . LEU C  1 45  ? -9.192  55.577  -0.339  1.00 37.35  ?  76   LEU C C   1 
ATOM   7705  O  O   . LEU C  1 45  ? -9.929  56.508  0.005   1.00 38.35  ?  76   LEU C O   1 
ATOM   7706  C  CB  . LEU C  1 45  ? -9.757  53.223  0.345   1.00 38.45  ?  76   LEU C CB  1 
ATOM   7707  C  CG  . LEU C  1 45  ? -10.629 51.984  0.091   1.00 37.04  ?  76   LEU C CG  1 
ATOM   7708  C  CD1 . LEU C  1 45  ? -10.316 50.883  1.092   1.00 36.91  ?  76   LEU C CD1 1 
ATOM   7709  C  CD2 . LEU C  1 45  ? -12.106 52.357  0.117   1.00 33.95  ?  76   LEU C CD2 1 
ATOM   7710  N  N   . ASP C  1 46  ? -7.858  55.683  -0.336  1.00 40.32  ?  77   ASP C N   1 
ATOM   7711  C  CA  . ASP C  1 46  ? -7.236  56.935  0.075   1.00 43.03  ?  77   ASP C CA  1 
ATOM   7712  C  C   . ASP C  1 46  ? -7.603  58.060  -0.882  1.00 38.72  ?  77   ASP C C   1 
ATOM   7713  O  O   . ASP C  1 46  ? -7.938  59.170  -0.449  1.00 42.65  ?  77   ASP C O   1 
ATOM   7714  C  CB  . ASP C  1 46  ? -5.717  56.791  0.158   1.00 40.63  ?  77   ASP C CB  1 
ATOM   7715  C  CG  . ASP C  1 46  ? -5.274  55.883  1.300   1.00 45.79  ?  77   ASP C CG  1 
ATOM   7716  O  OD1 . ASP C  1 46  ? -6.050  55.713  2.280   1.00 41.40  -1 77   ASP C OD1 1 
ATOM   7717  O  OD2 . ASP C  1 46  ? -4.098  55.440  1.260   1.00 41.35  ?  77   ASP C OD2 1 
ATOM   7718  N  N   . ASN C  1 47  ? -7.571  57.790  -2.189  1.00 36.86  ?  78   ASN C N   1 
ATOM   7719  C  CA  . ASN C  1 47  ? -7.961  58.837  -3.131  1.00 45.38  ?  78   ASN C CA  1 
ATOM   7720  C  C   . ASN C  1 47  ? -9.383  59.325  -2.874  1.00 44.58  ?  78   ASN C C   1 
ATOM   7721  O  O   . ASN C  1 47  ? -9.647  60.537  -2.903  1.00 41.63  ?  78   ASN C O   1 
ATOM   7722  C  CB  . ASN C  1 47  ? -7.814  58.357  -4.568  1.00 47.35  ?  78   ASN C CB  1 
ATOM   7723  C  CG  . ASN C  1 47  ? -7.700  59.510  -5.538  1.00 52.55  ?  78   ASN C CG  1 
ATOM   7724  O  OD1 . ASN C  1 47  ? -8.689  59.912  -6.152  1.00 54.52  ?  78   ASN C OD1 1 
ATOM   7725  N  ND2 . ASN C  1 47  ? -6.499  60.069  -5.660  1.00 55.73  ?  78   ASN C ND2 1 
ATOM   7726  N  N   . LEU C  1 48  ? -10.317 58.409  -2.596  1.00 39.18  ?  79   LEU C N   1 
ATOM   7727  C  CA  . LEU C  1 48  ? -11.679 58.855  -2.327  1.00 39.20  ?  79   LEU C CA  1 
ATOM   7728  C  C   . LEU C  1 48  ? -11.730 59.696  -1.065  1.00 36.68  ?  79   LEU C C   1 
ATOM   7729  O  O   . LEU C  1 48  ? -12.332 60.777  -1.048  1.00 37.34  ?  79   LEU C O   1 
ATOM   7730  C  CB  . LEU C  1 48  ? -12.628 57.656  -2.214  1.00 42.67  ?  79   LEU C CB  1 
ATOM   7731  C  CG  . LEU C  1 48  ? -12.846 56.826  -3.475  1.00 41.56  ?  79   LEU C CG  1 
ATOM   7732  C  CD1 . LEU C  1 48  ? -13.810 55.687  -3.191  1.00 38.14  ?  79   LEU C CD1 1 
ATOM   7733  C  CD2 . LEU C  1 48  ? -13.366 57.713  -4.602  1.00 43.24  ?  79   LEU C CD2 1 
ATOM   7734  N  N   . ALA C  1 49  ? -11.078 59.216  0.006   1.00 37.18  ?  80   ALA C N   1 
ATOM   7735  C  CA  . ALA C  1 49  ? -11.090 59.926  1.280   1.00 38.39  ?  80   ALA C CA  1 
ATOM   7736  C  C   . ALA C  1 49  ? -10.480 61.315  1.150   1.00 37.38  ?  80   ALA C C   1 
ATOM   7737  O  O   . ALA C  1 49  ? -11.016 62.292  1.694   1.00 33.86  ?  80   ALA C O   1 
ATOM   7738  C  CB  . ALA C  1 49  ? -10.335 59.110  2.335   1.00 38.75  ?  80   ALA C CB  1 
ATOM   7739  N  N   . GLN C  1 50  ? -9.339  61.410  0.455   1.00 38.65  ?  81   GLN C N   1 
ATOM   7740  C  CA  . GLN C  1 50  ? -8.698  62.696  0.199   1.00 44.01  ?  81   GLN C CA  1 
ATOM   7741  C  C   . GLN C  1 50  ? -9.649  63.676  -0.474  1.00 45.70  ?  81   GLN C C   1 
ATOM   7742  O  O   . GLN C  1 50  ? -9.550  64.887  -0.244  1.00 41.05  ?  81   GLN C O   1 
ATOM   7743  C  CB  . GLN C  1 50  ? -7.466  62.499  -0.688  1.00 45.47  ?  81   GLN C CB  1 
ATOM   7744  C  CG  . GLN C  1 50  ? -6.186  62.162  0.066   1.00 47.08  ?  81   GLN C CG  1 
ATOM   7745  C  CD  . GLN C  1 50  ? -5.199  61.364  -0.780  1.00 49.83  ?  81   GLN C CD  1 
ATOM   7746  O  OE1 . GLN C  1 50  ? -5.289  61.338  -2.014  1.00 54.93  ?  81   GLN C OE1 1 
ATOM   7747  N  NE2 . GLN C  1 50  ? -4.266  60.683  -0.115  1.00 52.27  ?  81   GLN C NE2 1 
ATOM   7748  N  N   . ASN C  1 51  ? -10.578 63.179  -1.299  1.00 42.56  ?  82   ASN C N   1 
ATOM   7749  C  CA  . ASN C  1 51  ? -11.486 64.038  -2.047  1.00 44.40  ?  82   ASN C CA  1 
ATOM   7750  C  C   . ASN C  1 51  ? -12.831 64.180  -1.375  1.00 45.28  ?  82   ASN C C   1 
ATOM   7751  O  O   . ASN C  1 51  ? -13.783 64.654  -2.001  1.00 44.68  ?  82   ASN C O   1 
ATOM   7752  C  CB  . ASN C  1 51  ? -11.662 63.517  -3.471  1.00 41.43  ?  82   ASN C CB  1 
ATOM   7753  C  CG  . ASN C  1 51  ? -10.405 63.674  -4.285  1.00 48.28  ?  82   ASN C CG  1 
ATOM   7754  O  OD1 . ASN C  1 51  ? -9.929  64.794  -4.497  1.00 51.74  ?  82   ASN C OD1 1 
ATOM   7755  N  ND2 . ASN C  1 51  ? -9.843  62.557  -4.735  1.00 51.14  ?  82   ASN C ND2 1 
ATOM   7756  N  N   . GLY C  1 52  ? -12.930 63.776  -0.118  1.00 42.15  ?  83   GLY C N   1 
ATOM   7757  C  CA  . GLY C  1 52  ? -14.134 63.986  0.637   1.00 40.19  ?  83   GLY C CA  1 
ATOM   7758  C  C   . GLY C  1 52  ? -13.825 64.335  2.070   1.00 44.51  ?  83   GLY C C   1 
ATOM   7759  O  O   . GLY C  1 52  ? -12.864 65.054  2.358   1.00 44.23  ?  83   GLY C O   1 
ATOM   7760  N  N   . SER C  1 53  ? -14.635 63.819  2.980   1.00 40.28  ?  84   SER C N   1 
ATOM   7761  C  CA  . SER C  1 53  ? -14.548 64.151  4.389   1.00 43.35  ?  84   SER C CA  1 
ATOM   7762  C  C   . SER C  1 53  ? -14.140 62.899  5.166   1.00 44.09  ?  84   SER C C   1 
ATOM   7763  O  O   . SER C  1 53  ? -14.865 61.898  5.159   1.00 38.68  ?  84   SER C O   1 
ATOM   7764  C  CB  . SER C  1 53  ? -15.890 64.702  4.869   1.00 37.72  ?  84   SER C CB  1 
ATOM   7765  O  OG  . SER C  1 53  ? -15.902 64.876  6.267   1.00 48.22  ?  84   SER C OG  1 
ATOM   7766  N  N   . ILE C  1 54  ? -12.969 62.943  5.807   1.00 41.64  ?  85   ILE C N   1 
ATOM   7767  C  CA  . ILE C  1 54  ? -12.547 61.867  6.698   1.00 36.06  ?  85   ILE C CA  1 
ATOM   7768  C  C   . ILE C  1 54  ? -13.140 62.136  8.074   1.00 39.15  ?  85   ILE C C   1 
ATOM   7769  O  O   . ILE C  1 54  ? -13.064 63.259  8.579   1.00 42.21  ?  85   ILE C O   1 
ATOM   7770  C  CB  . ILE C  1 54  ? -11.011 61.780  6.744   1.00 39.75  ?  85   ILE C CB  1 
ATOM   7771  C  CG1 . ILE C  1 54  ? -10.455 61.357  5.383   1.00 38.93  ?  85   ILE C CG1 1 
ATOM   7772  C  CG2 . ILE C  1 54  ? -10.528 60.812  7.832   1.00 32.06  ?  85   ILE C CG2 1 
ATOM   7773  C  CD1 . ILE C  1 54  ? -8.950  61.396  5.316   1.00 35.04  ?  85   ILE C CD1 1 
ATOM   7774  N  N   . PHE C  1 55  ? -13.764 61.119  8.679   1.00 34.37  ?  86   PHE C N   1 
ATOM   7775  C  CA  . PHE C  1 55  ? -14.346 61.247  10.016  1.00 34.36  ?  86   PHE C CA  1 
ATOM   7776  C  C   . PHE C  1 55  ? -13.362 60.668  11.032  1.00 38.01  ?  86   PHE C C   1 
ATOM   7777  O  O   . PHE C  1 55  ? -13.063 59.466  11.009  1.00 34.85  ?  86   PHE C O   1 
ATOM   7778  C  CB  . PHE C  1 55  ? -15.709 60.562  10.097  1.00 37.10  ?  86   PHE C CB  1 
ATOM   7779  C  CG  . PHE C  1 55  ? -16.794 61.315  9.379   1.00 36.06  ?  86   PHE C CG  1 
ATOM   7780  C  CD1 . PHE C  1 55  ? -16.830 61.333  8.002   1.00 34.50  ?  86   PHE C CD1 1 
ATOM   7781  C  CD2 . PHE C  1 55  ? -17.743 62.043  10.085  1.00 36.54  ?  86   PHE C CD2 1 
ATOM   7782  C  CE1 . PHE C  1 55  ? -17.807 62.046  7.323   1.00 37.72  ?  86   PHE C CE1 1 
ATOM   7783  C  CE2 . PHE C  1 55  ? -18.729 62.756  9.415   1.00 40.92  ?  86   PHE C CE2 1 
ATOM   7784  C  CZ  . PHE C  1 55  ? -18.756 62.753  8.026   1.00 34.93  ?  86   PHE C CZ  1 
ATOM   7785  N  N   . THR C  1 56  ? -12.822 61.535  11.896  1.00 35.21  ?  87   THR C N   1 
ATOM   7786  C  CA  . THR C  1 56  ? -11.764 61.125  12.808  1.00 35.50  ?  87   THR C CA  1 
ATOM   7787  C  C   . THR C  1 56  ? -12.300 60.614  14.140  1.00 34.53  ?  87   THR C C   1 
ATOM   7788  O  O   . THR C  1 56  ? -11.529 60.011  14.898  1.00 33.12  ?  87   THR C O   1 
ATOM   7789  C  CB  . THR C  1 56  ? -10.766 62.283  13.051  1.00 38.52  ?  87   THR C CB  1 
ATOM   7790  O  OG1 . THR C  1 56  ? -11.423 63.383  13.706  1.00 36.77  ?  87   THR C OG1 1 
ATOM   7791  C  CG2 . THR C  1 56  ? -10.129 62.755  11.737  1.00 38.25  ?  87   THR C CG2 1 
ATOM   7792  N  N   . SER C  1 57  ? -13.591 60.830  14.426  1.00 32.30  ?  88   SER C N   1 
ATOM   7793  C  CA  . SER C  1 57  ? -14.285 60.290  15.606  1.00 34.98  ?  88   SER C CA  1 
ATOM   7794  C  C   . SER C  1 57  ? -15.628 59.650  15.185  1.00 37.83  ?  88   SER C C   1 
ATOM   7795  O  O   . SER C  1 57  ? -16.711 60.067  15.606  1.00 37.05  ?  88   SER C O   1 
ATOM   7796  C  CB  . SER C  1 57  ? -14.509 61.387  16.652  1.00 36.61  ?  88   SER C CB  1 
ATOM   7797  O  OG  . SER C  1 57  ? -13.332 61.604  17.440  1.00 39.15  ?  88   SER C OG  1 
ATOM   7798  N  N   . ALA C  1 58  ? -15.546 58.598  14.366  1.00 32.68  ?  89   ALA C N   1 
ATOM   7799  C  CA  . ALA C  1 58  ? -16.712 57.846  13.904  1.00 35.57  ?  89   ALA C CA  1 
ATOM   7800  C  C   . ALA C  1 58  ? -16.919 56.603  14.765  1.00 36.73  ?  89   ALA C C   1 
ATOM   7801  O  O   . ALA C  1 58  ? -15.970 55.857  15.031  1.00 36.86  ?  89   ALA C O   1 
ATOM   7802  C  CB  . ALA C  1 58  ? -16.552 57.442  12.438  1.00 32.45  ?  89   ALA C CB  1 
ATOM   7803  N  N   . TYR C  1 59  ? -18.155 56.372  15.181  1.00 34.00  ?  90   TYR C N   1 
ATOM   7804  C  CA  . TYR C  1 59  ? -18.481 55.271  16.075  1.00 34.36  ?  90   TYR C CA  1 
ATOM   7805  C  C   . TYR C  1 59  ? -19.593 54.418  15.478  1.00 34.77  ?  90   TYR C C   1 
ATOM   7806  O  O   . TYR C  1 59  ? -20.556 54.951  14.923  1.00 32.12  ?  90   TYR C O   1 
ATOM   7807  C  CB  . TYR C  1 59  ? -18.934 55.786  17.441  1.00 33.18  ?  90   TYR C CB  1 
ATOM   7808  C  CG  . TYR C  1 59  ? -17.843 56.518  18.206  1.00 35.48  ?  90   TYR C CG  1 
ATOM   7809  C  CD1 . TYR C  1 59  ? -16.903 55.812  18.960  1.00 33.74  ?  90   TYR C CD1 1 
ATOM   7810  C  CD2 . TYR C  1 59  ? -17.764 57.905  18.182  1.00 34.55  ?  90   TYR C CD2 1 
ATOM   7811  C  CE1 . TYR C  1 59  ? -15.918 56.480  19.686  1.00 34.76  ?  90   TYR C CE1 1 
ATOM   7812  C  CE2 . TYR C  1 59  ? -16.772 58.583  18.886  1.00 35.89  ?  90   TYR C CE2 1 
ATOM   7813  C  CZ  . TYR C  1 59  ? -15.856 57.864  19.639  1.00 36.88  ?  90   TYR C CZ  1 
ATOM   7814  O  OH  . TYR C  1 59  ? -14.871 58.522  20.344  1.00 33.96  ?  90   TYR C OH  1 
ATOM   7815  N  N   . VAL C  1 60  ? -19.457 53.098  15.611  1.00 35.10  ?  91   VAL C N   1 
ATOM   7816  C  CA  . VAL C  1 60  ? -20.549 52.173  15.348  1.00 31.63  ?  91   VAL C CA  1 
ATOM   7817  C  C   . VAL C  1 60  ? -21.281 51.937  16.660  1.00 32.38  ?  91   VAL C C   1 
ATOM   7818  O  O   . VAL C  1 60  ? -20.764 52.229  17.735  1.00 31.20  ?  91   VAL C O   1 
ATOM   7819  C  CB  . VAL C  1 60  ? -20.050 50.857  14.718  1.00 31.22  ?  91   VAL C CB  1 
ATOM   7820  C  CG1 . VAL C  1 60  ? -19.498 51.127  13.328  1.00 29.86  ?  91   VAL C CG1 1 
ATOM   7821  C  CG2 . VAL C  1 60  ? -18.991 50.191  15.601  1.00 32.43  ?  91   VAL C CG2 1 
ATOM   7822  N  N   . ALA C  1 61  ? -22.528 51.437  16.575  1.00 28.00  ?  92   ALA C N   1 
ATOM   7823  C  CA  . ALA C  1 61  ? -23.381 51.334  17.755  1.00 27.29  ?  92   ALA C CA  1 
ATOM   7824  C  C   . ALA C  1 61  ? -23.041 50.152  18.656  1.00 30.53  ?  92   ALA C C   1 
ATOM   7825  O  O   . ALA C  1 61  ? -23.573 50.071  19.766  1.00 32.57  ?  92   ALA C O   1 
ATOM   7826  C  CB  . ALA C  1 61  ? -24.862 51.239  17.340  1.00 31.76  ?  92   ALA C CB  1 
ATOM   7827  N  N   . HIS C  1 62  ? -22.194 49.223  18.220  1.00 29.61  ?  93   HIS C N   1 
ATOM   7828  C  CA  . HIS C  1 62  ? -21.851 48.085  19.062  1.00 31.35  ?  93   HIS C CA  1 
ATOM   7829  C  C   . HIS C  1 62  ? -20.503 47.567  18.601  1.00 31.23  ?  93   HIS C C   1 
ATOM   7830  O  O   . HIS C  1 62  ? -20.195 47.650  17.409  1.00 28.61  ?  93   HIS C O   1 
ATOM   7831  C  CB  . HIS C  1 62  ? -22.922 46.979  18.966  1.00 27.63  ?  93   HIS C CB  1 
ATOM   7832  C  CG  . HIS C  1 62  ? -22.877 45.974  20.080  1.00 26.88  ?  93   HIS C CG  1 
ATOM   7833  N  ND1 . HIS C  1 62  ? -23.471 46.191  21.306  1.00 25.76  ?  93   HIS C ND1 1 
ATOM   7834  C  CD2 . HIS C  1 62  ? -22.345 44.724  20.137  1.00 26.30  ?  93   HIS C CD2 1 
ATOM   7835  C  CE1 . HIS C  1 62  ? -23.289 45.130  22.079  1.00 29.31  ?  93   HIS C CE1 1 
ATOM   7836  N  NE2 . HIS C  1 62  ? -22.613 44.224  21.393  1.00 26.43  ?  93   HIS C NE2 1 
ATOM   7837  N  N   . PRO C  1 63  ? -19.666 47.055  19.505  1.00 30.00  ?  94   PRO C N   1 
ATOM   7838  C  CA  . PRO C  1 63  ? -18.308 46.653  19.109  1.00 26.42  ?  94   PRO C CA  1 
ATOM   7839  C  C   . PRO C  1 63  ? -18.197 45.286  18.447  1.00 29.72  ?  94   PRO C C   1 
ATOM   7840  O  O   . PRO C  1 63  ? -17.077 44.790  18.298  1.00 28.66  ?  94   PRO C O   1 
ATOM   7841  C  CB  . PRO C  1 63  ? -17.531 46.696  20.444  1.00 30.49  ?  94   PRO C CB  1 
ATOM   7842  C  CG  . PRO C  1 63  ? -18.556 46.401  21.488  1.00 27.52  ?  94   PRO C CG  1 
ATOM   7843  C  CD  . PRO C  1 63  ? -19.845 47.078  20.969  1.00 28.37  ?  94   PRO C CD  1 
ATOM   7844  N  N   . PHE C  1 64  ? -19.288 44.646  18.008  1.00 28.68  ?  95   PHE C N   1 
ATOM   7845  C  CA  . PHE C  1 64  ? -19.131 43.516  17.081  1.00 28.37  ?  95   PHE C CA  1 
ATOM   7846  C  C   . PHE C  1 64  ? -20.360 43.414  16.133  1.00 31.10  ?  95   PHE C C   1 
ATOM   7847  O  O   . PHE C  1 64  ? -21.310 44.168  16.296  1.00 29.59  ?  95   PHE C O   1 
ATOM   7848  C  CB  . PHE C  1 64  ? -18.821 42.192  17.840  1.00 25.77  ?  95   PHE C CB  1 
ATOM   7849  C  CG  . PHE C  1 64  ? -19.847 41.796  18.864  1.00 28.88  ?  95   PHE C CG  1 
ATOM   7850  C  CD1 . PHE C  1 64  ? -21.055 41.195  18.454  1.00 29.09  ?  95   PHE C CD1 1 
ATOM   7851  C  CD2 . PHE C  1 64  ? -19.600 41.966  20.225  1.00 28.46  ?  95   PHE C CD2 1 
ATOM   7852  C  CE1 . PHE C  1 64  ? -22.003 40.811  19.385  1.00 27.27  ?  95   PHE C CE1 1 
ATOM   7853  C  CE2 . PHE C  1 64  ? -20.533 41.581  21.167  1.00 32.36  ?  95   PHE C CE2 1 
ATOM   7854  C  CZ  . PHE C  1 64  ? -21.769 40.993  20.730  1.00 27.05  ?  95   PHE C CZ  1 
HETATM 7855  N  N   . OSE C  1 65  ? -20.148 42.646  15.058  1.00 33.34  ?  96   OSE C N   1 
HETATM 7856  C  CA  . OSE C  1 65  ? -21.007 42.646  13.849  1.00 38.69  ?  96   OSE C CA  1 
HETATM 7857  C  CB  . OSE C  1 65  ? -20.652 41.474  12.986  1.00 41.85  ?  96   OSE C CB  1 
HETATM 7858  O  OG  . OSE C  1 65  ? -20.425 40.376  13.800  1.00 46.17  ?  96   OSE C OG  1 
HETATM 7859  C  C   . OSE C  1 65  ? -22.515 42.664  13.980  1.00 32.28  ?  96   OSE C C   1 
HETATM 7860  O  O   . OSE C  1 65  ? -23.101 43.672  13.598  1.00 32.33  ?  96   OSE C O   1 
HETATM 7861  S  S   . OSE C  1 65  ? -18.933 39.984  13.898  1.00 43.29  ?  96   OSE C S   1 
HETATM 7862  O  O1S . OSE C  1 65  ? -18.134 41.176  13.854  1.00 45.08  ?  96   OSE C O1S 1 
HETATM 7863  O  O2S . OSE C  1 65  ? -18.873 39.291  15.158  1.00 46.51  ?  96   OSE C O2S 1 
HETATM 7864  O  O3S . OSE C  1 65  ? -18.817 39.163  12.716  1.00 46.74  ?  96   OSE C O3S 1 
ATOM   7865  N  N   . GLY C  1 66  ? -23.081 41.556  14.415  1.00 32.83  ?  97   GLY C N   1 
ATOM   7866  C  CA  . GLY C  1 66  ? -24.521 41.365  14.332  1.00 35.34  ?  97   GLY C CA  1 
ATOM   7867  C  C   . GLY C  1 66  ? -25.279 42.586  14.818  1.00 33.24  ?  97   GLY C C   1 
ATOM   7868  O  O   . GLY C  1 66  ? -26.061 43.198  14.054  1.00 33.29  ?  97   GLY C O   1 
ATOM   7869  N  N   . PRO C  1 67  ? -25.033 42.954  16.078  1.00 34.00  ?  98   PRO C N   1 
ATOM   7870  C  CA  . PRO C  1 67  ? -25.711 44.130  16.641  1.00 30.55  ?  98   PRO C CA  1 
ATOM   7871  C  C   . PRO C  1 67  ? -25.302 45.421  15.966  1.00 33.22  ?  98   PRO C C   1 
ATOM   7872  O  O   . PRO C  1 67  ? -26.125 46.342  15.860  1.00 33.45  ?  98   PRO C O   1 
ATOM   7873  C  CB  . PRO C  1 67  ? -25.283 44.111  18.111  1.00 30.91  ?  98   PRO C CB  1 
ATOM   7874  C  CG  . PRO C  1 67  ? -24.869 42.705  18.377  1.00 32.74  ?  98   PRO C CG  1 
ATOM   7875  C  CD  . PRO C  1 67  ? -24.259 42.224  17.099  1.00 33.41  ?  98   PRO C CD  1 
ATOM   7876  N  N   . SER C  1 68  ? -24.051 45.520  15.507  1.00 32.00  ?  99   SER C N   1 
ATOM   7877  C  CA  . SER C  1 68  ? -23.634 46.698  14.749  1.00 32.50  ?  99   SER C CA  1 
ATOM   7878  C  C   . SER C  1 68  ? -24.418 46.814  13.444  1.00 30.90  ?  99   SER C C   1 
ATOM   7879  O  O   . SER C  1 68  ? -24.951 47.880  13.112  1.00 27.73  ?  99   SER C O   1 
ATOM   7880  C  CB  . SER C  1 68  ? -22.131 46.633  14.464  1.00 30.05  ?  99   SER C CB  1 
ATOM   7881  O  OG  . SER C  1 68  ? -21.734 47.712  13.639  1.00 28.01  ?  99   SER C OG  1 
ATOM   7882  N  N   . ARG C  1 69  ? -24.479 45.720  12.678  1.00 31.12  ?  100  ARG C N   1 
ATOM   7883  C  CA  . ARG C  1 69  ? -25.157 45.752  11.389  1.00 29.55  ?  100  ARG C CA  1 
ATOM   7884  C  C   . ARG C  1 69  ? -26.647 45.976  11.565  1.00 30.49  ?  100  ARG C C   1 
ATOM   7885  O  O   . ARG C  1 69  ? -27.274 46.656  10.744  1.00 33.49  ?  100  ARG C O   1 
ATOM   7886  C  CB  . ARG C  1 69  ? -24.884 44.450  10.633  1.00 30.90  ?  100  ARG C CB  1 
ATOM   7887  C  CG  . ARG C  1 69  ? -23.434 44.362  10.127  1.00 33.29  ?  100  ARG C CG  1 
ATOM   7888  C  CD  . ARG C  1 69  ? -22.914 42.935  9.967   1.00 30.64  ?  100  ARG C CD  1 
ATOM   7889  N  NE  . ARG C  1 69  ? -21.474 42.954  9.713   1.00 31.82  ?  100  ARG C NE  1 
ATOM   7890  C  CZ  . ARG C  1 69  ? -20.940 43.192  8.522   1.00 31.09  ?  100  ARG C CZ  1 
ATOM   7891  N  NH1 . ARG C  1 69  ? -21.695 43.317  7.440   1.00 28.07  ?  100  ARG C NH1 1 
ATOM   7892  N  NH2 . ARG C  1 69  ? -19.618 43.332  8.417   1.00 31.78  ?  100  ARG C NH2 1 
ATOM   7893  N  N   . SER C  1 70  ? -27.223 45.385  12.619  1.00 31.38  ?  101  SER C N   1 
ATOM   7894  C  CA  . SER C  1 70  ? -28.608 45.634  13.011  1.00 32.40  ?  101  SER C CA  1 
ATOM   7895  C  C   . SER C  1 70  ? -28.856 47.121  13.228  1.00 35.93  ?  101  SER C C   1 
ATOM   7896  O  O   . SER C  1 70  ? -29.851 47.679  12.749  1.00 36.06  ?  101  SER C O   1 
ATOM   7897  C  CB  . SER C  1 70  ? -28.917 44.842  14.291  1.00 33.85  ?  101  SER C CB  1 
ATOM   7898  O  OG  . SER C  1 70  ? -30.123 45.265  14.913  1.00 43.15  ?  101  SER C OG  1 
ATOM   7899  N  N   . ALA C  1 71  ? -27.962 47.779  13.973  1.00 33.07  ?  102  ALA C N   1 
ATOM   7900  C  CA  . ALA C  1 71  ? -28.119 49.206  14.223  1.00 28.90  ?  102  ALA C CA  1 
ATOM   7901  C  C   . ALA C  1 71  ? -28.008 50.020  12.934  1.00 28.40  ?  102  ALA C C   1 
ATOM   7902  O  O   . ALA C  1 71  ? -28.694 51.035  12.776  1.00 33.21  ?  102  ALA C O   1 
ATOM   7903  C  CB  . ALA C  1 71  ? -27.085 49.667  15.259  1.00 28.15  ?  102  ALA C CB  1 
ATOM   7904  N  N   . ILE C  1 72  ? -27.158 49.598  11.999  1.00 25.40  ?  103  ILE C N   1 
ATOM   7905  C  CA  . ILE C  1 72  ? -26.996 50.367  10.763  1.00 28.83  ?  103  ILE C CA  1 
ATOM   7906  C  C   . ILE C  1 72  ? -28.280 50.343  9.953   1.00 37.93  ?  103  ILE C C   1 
ATOM   7907  O  O   . ILE C  1 72  ? -28.705 51.366  9.392   1.00 33.93  ?  103  ILE C O   1 
ATOM   7908  C  CB  . ILE C  1 72  ? -25.828 49.827  9.921   1.00 29.63  ?  103  ILE C CB  1 
ATOM   7909  C  CG1 . ILE C  1 72  ? -24.488 50.125  10.595  1.00 28.37  ?  103  ILE C CG1 1 
ATOM   7910  C  CG2 . ILE C  1 72  ? -25.887 50.401  8.501   1.00 33.48  ?  103  ILE C CG2 1 
ATOM   7911  C  CD1 . ILE C  1 72  ? -23.332 49.283  10.049  1.00 33.42  ?  103  ILE C CD1 1 
ATOM   7912  N  N   . LEU C  1 73  ? -28.913 49.176  9.865   1.00 32.15  ?  104  LEU C N   1 
ATOM   7913  C  CA  . LEU C  1 73  ? -30.053 49.078  8.977   1.00 32.09  ?  104  LEU C CA  1 
ATOM   7914  C  C   . LEU C  1 73  ? -31.357 49.468  9.654   1.00 32.12  ?  104  LEU C C   1 
ATOM   7915  O  O   . LEU C  1 73  ? -32.248 49.981  8.974   1.00 33.77  ?  104  LEU C O   1 
ATOM   7916  C  CB  . LEU C  1 73  ? -30.125 47.672  8.396   1.00 34.41  ?  104  LEU C CB  1 
ATOM   7917  C  CG  . LEU C  1 73  ? -29.193 47.572  7.187   1.00 40.05  ?  104  LEU C CG  1 
ATOM   7918  C  CD1 . LEU C  1 73  ? -29.010 46.140  6.742   1.00 42.62  ?  104  LEU C CD1 1 
ATOM   7919  C  CD2 . LEU C  1 73  ? -29.700 48.430  6.041   1.00 34.89  ?  104  LEU C CD2 1 
ATOM   7920  N  N   . THR C  1 74  ? -31.485 49.268  10.971  1.00 32.11  ?  105  THR C N   1 
ATOM   7921  C  CA  . THR C  1 74  ? -32.666 49.731  11.698  1.00 34.85  ?  105  THR C CA  1 
ATOM   7922  C  C   . THR C  1 74  ? -32.565 51.181  12.153  1.00 39.33  ?  105  THR C C   1 
ATOM   7923  O  O   . THR C  1 74  ? -33.599 51.818  12.386  1.00 35.81  ?  105  THR C O   1 
ATOM   7924  C  CB  . THR C  1 74  ? -32.928 48.891  12.955  1.00 34.97  ?  105  THR C CB  1 
ATOM   7925  O  OG1 . THR C  1 74  ? -31.828 49.031  13.871  1.00 36.72  ?  105  THR C OG1 1 
ATOM   7926  C  CG2 . THR C  1 74  ? -33.149 47.425  12.611  1.00 33.03  ?  105  THR C CG2 1 
ATOM   7927  N  N   . GLY C  1 75  ? -31.355 51.704  12.331  1.00 33.17  ?  106  GLY C N   1 
ATOM   7928  C  CA  . GLY C  1 75  ? -31.208 53.031  12.891  1.00 33.51  ?  106  GLY C CA  1 
ATOM   7929  C  C   . GLY C  1 75  ? -31.432 53.122  14.381  1.00 36.12  ?  106  GLY C C   1 
ATOM   7930  O  O   . GLY C  1 75  ? -31.628 54.229  14.892  1.00 38.06  ?  106  GLY C O   1 
ATOM   7931  N  N   . ARG C  1 76  ? -31.405 51.992  15.106  1.00 32.92  ?  107  ARG C N   1 
ATOM   7932  C  CA  . ARG C  1 76  ? -31.585 51.984  16.551  1.00 37.86  ?  107  ARG C CA  1 
ATOM   7933  C  C   . ARG C  1 76  ? -30.499 51.158  17.233  1.00 37.74  ?  107  ARG C C   1 
ATOM   7934  O  O   . ARG C  1 76  ? -29.976 50.191  16.665  1.00 36.22  ?  107  ARG C O   1 
ATOM   7935  C  CB  . ARG C  1 76  ? -32.955 51.434  16.920  1.00 37.51  ?  107  ARG C CB  1 
ATOM   7936  C  CG  . ARG C  1 76  ? -34.093 52.172  16.196  1.00 37.38  ?  107  ARG C CG  1 
ATOM   7937  C  CD  . ARG C  1 76  ? -35.433 51.674  16.634  1.00 41.37  ?  107  ARG C CD  1 
ATOM   7938  N  NE  . ARG C  1 76  ? -35.748 52.074  18.001  1.00 45.89  ?  107  ARG C NE  1 
ATOM   7939  C  CZ  . ARG C  1 76  ? -36.746 51.565  18.711  1.00 46.80  ?  107  ARG C CZ  1 
ATOM   7940  N  NH1 . ARG C  1 76  ? -37.519 50.603  18.226  1.00 47.02  ?  107  ARG C NH1 1 
ATOM   7941  N  NH2 . ARG C  1 76  ? -36.983 52.038  19.931  1.00 39.34  ?  107  ARG C NH2 1 
ATOM   7942  N  N   . TYR C  1 77  ? -30.164 51.560  18.453  1.00 36.08  ?  108  TYR C N   1 
ATOM   7943  C  CA  . TYR C  1 77  ? -29.270 50.772  19.288  1.00 36.70  ?  108  TYR C CA  1 
ATOM   7944  C  C   . TYR C  1 77  ? -29.800 49.344  19.402  1.00 37.38  ?  108  TYR C C   1 
ATOM   7945  O  O   . TYR C  1 77  ? -31.017 49.142  19.561  1.00 34.59  ?  108  TYR C O   1 
ATOM   7946  C  CB  . TYR C  1 77  ? -29.136 51.395  20.684  1.00 34.42  ?  108  TYR C CB  1 
ATOM   7947  C  CG  . TYR C  1 77  ? -28.116 52.526  20.751  1.00 37.77  ?  108  TYR C CG  1 
ATOM   7948  C  CD1 . TYR C  1 77  ? -26.748 52.265  20.729  1.00 37.94  ?  108  TYR C CD1 1 
ATOM   7949  C  CD2 . TYR C  1 77  ? -28.525 53.856  20.820  1.00 36.33  ?  108  TYR C CD2 1 
ATOM   7950  C  CE1 . TYR C  1 77  ? -25.808 53.306  20.779  1.00 32.07  ?  108  TYR C CE1 1 
ATOM   7951  C  CE2 . TYR C  1 77  ? -27.593 54.899  20.881  1.00 37.92  ?  108  TYR C CE2 1 
ATOM   7952  C  CZ  . TYR C  1 77  ? -26.242 54.617  20.852  1.00 37.95  ?  108  TYR C CZ  1 
ATOM   7953  O  OH  . TYR C  1 77  ? -25.338 55.658  20.886  1.00 34.86  ?  108  TYR C OH  1 
ATOM   7954  N  N   . PRO C  1 78  ? -28.930 48.336  19.312  1.00 34.57  ?  109  PRO C N   1 
ATOM   7955  C  CA  . PRO C  1 78  ? -29.403 46.945  19.397  1.00 34.46  ?  109  PRO C CA  1 
ATOM   7956  C  C   . PRO C  1 78  ? -30.054 46.626  20.723  1.00 34.39  ?  109  PRO C C   1 
ATOM   7957  O  O   . PRO C  1 78  ? -30.868 45.694  20.784  1.00 33.40  ?  109  PRO C O   1 
ATOM   7958  C  CB  . PRO C  1 78  ? -28.122 46.124  19.189  1.00 29.49  ?  109  PRO C CB  1 
ATOM   7959  C  CG  . PRO C  1 78  ? -27.016 47.067  19.614  1.00 35.06  ?  109  PRO C CG  1 
ATOM   7960  C  CD  . PRO C  1 78  ? -27.469 48.419  19.126  1.00 32.43  ?  109  PRO C CD  1 
ATOM   7961  N  N   . HIS C  1 79  ? -29.723 47.379  21.781  1.00 31.88  ?  110  HIS C N   1 
ATOM   7962  C  CA  . HIS C  1 79  ? -30.354 47.233  23.087  1.00 32.83  ?  110  HIS C CA  1 
ATOM   7963  C  C   . HIS C  1 79  ? -31.825 47.625  23.055  1.00 36.39  ?  110  HIS C C   1 
ATOM   7964  O  O   . HIS C  1 79  ? -32.568 47.281  23.980  1.00 36.98  ?  110  HIS C O   1 
ATOM   7965  C  CB  . HIS C  1 79  ? -29.614 48.090  24.119  1.00 37.11  ?  110  HIS C CB  1 
ATOM   7966  C  CG  . HIS C  1 79  ? -28.126 48.124  23.917  1.00 32.71  ?  110  HIS C CG  1 
ATOM   7967  N  ND1 . HIS C  1 79  ? -27.527 48.790  22.865  1.00 32.32  ?  110  HIS C ND1 1 
ATOM   7968  C  CD2 . HIS C  1 79  ? -27.120 47.577  24.636  1.00 33.19  ?  110  HIS C CD2 1 
ATOM   7969  C  CE1 . HIS C  1 79  ? -26.217 48.645  22.944  1.00 30.56  ?  110  HIS C CE1 1 
ATOM   7970  N  NE2 . HIS C  1 79  ? -25.945 47.908  24.006  1.00 33.67  ?  110  HIS C NE2 1 
ATOM   7971  N  N   . LEU C  1 80  ? -32.248 48.334  22.011  1.00 35.83  ?  111  LEU C N   1 
ATOM   7972  C  CA  . LEU C  1 80  ? -33.638 48.737  21.840  1.00 37.43  ?  111  LEU C CA  1 
ATOM   7973  C  C   . LEU C  1 80  ? -34.420 47.801  20.928  1.00 41.44  ?  111  LEU C C   1 
ATOM   7974  O  O   . LEU C  1 80  ? -35.654 47.809  20.977  1.00 37.28  ?  111  LEU C O   1 
ATOM   7975  C  CB  . LEU C  1 80  ? -33.713 50.163  21.274  1.00 39.72  ?  111  LEU C CB  1 
ATOM   7976  C  CG  . LEU C  1 80  ? -33.594 51.319  22.286  1.00 43.18  ?  111  LEU C CG  1 
ATOM   7977  C  CD1 . LEU C  1 80  ? -34.682 51.227  23.326  1.00 43.71  ?  111  LEU C CD1 1 
ATOM   7978  C  CD2 . LEU C  1 80  ? -32.218 51.330  22.978  1.00 40.91  ?  111  LEU C CD2 1 
ATOM   7979  N  N   . THR C  1 81  ? -33.741 47.000  20.102  1.00 34.74  ?  112  THR C N   1 
ATOM   7980  C  CA  . THR C  1 81  ? -34.403 46.096  19.173  1.00 36.62  ?  112  THR C CA  1 
ATOM   7981  C  C   . THR C  1 81  ? -34.290 44.641  19.595  1.00 35.46  ?  112  THR C C   1 
ATOM   7982  O  O   . THR C  1 81  ? -34.865 43.774  18.939  1.00 35.09  ?  112  THR C O   1 
ATOM   7983  C  CB  . THR C  1 81  ? -33.835 46.293  17.757  1.00 36.92  ?  112  THR C CB  1 
ATOM   7984  O  OG1 . THR C  1 81  ? -32.417 46.020  17.763  1.00 37.30  ?  112  THR C OG1 1 
ATOM   7985  C  CG2 . THR C  1 81  ? -34.047 47.733  17.307  1.00 36.08  ?  112  THR C CG2 1 
ATOM   7986  N  N   . GLY C  1 82  ? -33.580 44.352  20.681  1.00 34.04  ?  113  GLY C N   1 
ATOM   7987  C  CA  . GLY C  1 82  ? -33.403 42.994  21.155  1.00 37.40  ?  113  GLY C CA  1 
ATOM   7988  C  C   . GLY C  1 82  ? -32.291 42.213  20.486  1.00 34.61  ?  113  GLY C C   1 
ATOM   7989  O  O   . GLY C  1 82  ? -32.244 40.987  20.645  1.00 32.26  ?  113  GLY C O   1 
ATOM   7990  N  N   . THR C  1 83  ? -31.390 42.881  19.756  1.00 30.06  ?  114  THR C N   1 
ATOM   7991  C  CA  . THR C  1 83  ? -30.413 42.234  18.894  1.00 29.97  ?  114  THR C CA  1 
ATOM   7992  C  C   . THR C  1 83  ? -28.969 42.565  19.303  1.00 31.58  ?  114  THR C C   1 
ATOM   7993  O  O   . THR C  1 83  ? -28.107 42.781  18.445  1.00 32.24  ?  114  THR C O   1 
ATOM   7994  C  CB  . THR C  1 83  ? -30.635 42.645  17.447  1.00 34.48  ?  114  THR C CB  1 
ATOM   7995  O  OG1 . THR C  1 83  ? -30.521 44.067  17.358  1.00 32.82  ?  114  THR C OG1 1 
ATOM   7996  C  CG2 . THR C  1 83  ? -32.059 42.221  16.953  1.00 33.21  ?  114  THR C CG2 1 
ATOM   7997  N  N   . ALA C  1 84  ? -28.686 42.598  20.600  1.00 29.93  ?  115  ALA C N   1 
ATOM   7998  C  CA  . ALA C  1 84  ? -27.356 42.955  21.106  1.00 28.76  ?  115  ALA C CA  1 
ATOM   7999  C  C   . ALA C  1 84  ? -26.419 41.757  21.260  1.00 33.71  ?  115  ALA C C   1 
ATOM   8000  O  O   . ALA C  1 84  ? -25.282 41.925  21.736  1.00 29.82  ?  115  ALA C O   1 
ATOM   8001  C  CB  . ALA C  1 84  ? -27.488 43.689  22.444  1.00 30.91  ?  115  ALA C CB  1 
ATOM   8002  N  N   . TYR C  1 85  ? -26.863 40.557  20.888  1.00 30.20  ?  116  TYR C N   1 
ATOM   8003  C  CA  . TYR C  1 85  ? -26.000 39.395  20.771  1.00 30.16  ?  116  TYR C CA  1 
ATOM   8004  C  C   . TYR C  1 85  ? -25.955 38.953  19.314  1.00 33.44  ?  116  TYR C C   1 
ATOM   8005  O  O   . TYR C  1 85  ? -26.886 39.222  18.535  1.00 31.77  ?  116  TYR C O   1 
ATOM   8006  C  CB  . TYR C  1 85  ? -26.495 38.228  21.653  1.00 29.12  ?  116  TYR C CB  1 
ATOM   8007  C  CG  . TYR C  1 85  ? -26.291 38.383  23.149  1.00 32.09  ?  116  TYR C CG  1 
ATOM   8008  C  CD1 . TYR C  1 85  ? -25.099 37.985  23.759  1.00 30.54  ?  116  TYR C CD1 1 
ATOM   8009  C  CD2 . TYR C  1 85  ? -27.292 38.910  23.966  1.00 31.57  ?  116  TYR C CD2 1 
ATOM   8010  C  CE1 . TYR C  1 85  ? -24.906 38.112  25.139  1.00 34.33  ?  116  TYR C CE1 1 
ATOM   8011  C  CE2 . TYR C  1 85  ? -27.102 39.038  25.366  1.00 32.88  ?  116  TYR C CE2 1 
ATOM   8012  C  CZ  . TYR C  1 85  ? -25.916 38.630  25.935  1.00 31.90  ?  116  TYR C CZ  1 
ATOM   8013  O  OH  . TYR C  1 85  ? -25.711 38.748  27.303  1.00 29.75  ?  116  TYR C OH  1 
ATOM   8014  N  N   . ASN C  1 86  ? -24.865 38.277  18.941  1.00 29.09  ?  117  ASN C N   1 
ATOM   8015  C  CA  . ASN C  1 86  ? -24.790 37.653  17.624  1.00 30.74  ?  117  ASN C CA  1 
ATOM   8016  C  C   . ASN C  1 86  ? -25.770 36.481  17.529  1.00 31.42  ?  117  ASN C C   1 
ATOM   8017  O  O   . ASN C  1 86  ? -26.024 35.772  18.512  1.00 30.39  ?  117  ASN C O   1 
ATOM   8018  C  CB  . ASN C  1 86  ? -23.380 37.127  17.344  1.00 30.80  ?  117  ASN C CB  1 
ATOM   8019  C  CG  . ASN C  1 86  ? -22.493 38.145  16.629  1.00 34.37  ?  117  ASN C CG  1 
ATOM   8020  O  OD1 . ASN C  1 86  ? -22.879 39.294  16.431  1.00 29.56  ?  117  ASN C OD1 1 
ATOM   8021  N  ND2 . ASN C  1 86  ? -21.285 37.720  16.257  1.00 34.85  ?  117  ASN C ND2 1 
ATOM   8022  N  N   . LEU C  1 87  ? -26.330 36.284  16.335  1.00 31.83  ?  118  LEU C N   1 
ATOM   8023  C  CA  . LEU C  1 87  ? -26.879 34.977  15.989  1.00 30.08  ?  118  LEU C CA  1 
ATOM   8024  C  C   . LEU C  1 87  ? -25.746 33.955  15.943  1.00 33.96  ?  118  LEU C C   1 
ATOM   8025  O  O   . LEU C  1 87  ? -24.635 34.274  15.515  1.00 29.48  ?  118  LEU C O   1 
ATOM   8026  C  CB  . LEU C  1 87  ? -27.569 35.036  14.635  1.00 28.18  ?  118  LEU C CB  1 
ATOM   8027  C  CG  . LEU C  1 87  ? -28.777 35.942  14.526  1.00 30.44  ?  118  LEU C CG  1 
ATOM   8028  C  CD1 . LEU C  1 87  ? -29.146 36.141  13.046  1.00 29.86  ?  118  LEU C CD1 1 
ATOM   8029  C  CD2 . LEU C  1 87  ? -29.922 35.308  15.317  1.00 32.84  ?  118  LEU C CD2 1 
ATOM   8030  N  N   . PHE C  1 88  ? -26.017 32.727  16.390  1.00 30.64  ?  119  PHE C N   1 
ATOM   8031  C  CA  . PHE C  1 88  ? -24.988 31.692  16.380  1.00 32.53  ?  119  PHE C CA  1 
ATOM   8032  C  C   . PHE C  1 88  ? -24.714 31.206  14.949  1.00 32.61  ?  119  PHE C C   1 
ATOM   8033  O  O   . PHE C  1 88  ? -25.459 31.488  14.017  1.00 32.82  ?  119  PHE C O   1 
ATOM   8034  C  CB  . PHE C  1 88  ? -25.398 30.522  17.277  1.00 31.12  ?  119  PHE C CB  1 
ATOM   8035  C  CG  . PHE C  1 88  ? -24.239 29.743  17.837  1.00 34.89  ?  119  PHE C CG  1 
ATOM   8036  C  CD1 . PHE C  1 88  ? -23.427 30.296  18.825  1.00 36.50  ?  119  PHE C CD1 1 
ATOM   8037  C  CD2 . PHE C  1 88  ? -23.967 28.445  17.394  1.00 32.45  ?  119  PHE C CD2 1 
ATOM   8038  C  CE1 . PHE C  1 88  ? -22.356 29.580  19.348  1.00 31.07  ?  119  PHE C CE1 1 
ATOM   8039  C  CE2 . PHE C  1 88  ? -22.909 27.722  17.920  1.00 37.67  ?  119  PHE C CE2 1 
ATOM   8040  C  CZ  . PHE C  1 88  ? -22.092 28.289  18.896  1.00 34.17  ?  119  PHE C CZ  1 
ATOM   8041  N  N   . HIS C  1 89  ? -23.606 30.476  14.777  1.00 31.62  ?  120  HIS C N   1 
ATOM   8042  C  CA  . HIS C  1 89  ? -23.340 29.820  13.503  1.00 33.58  ?  120  HIS C CA  1 
ATOM   8043  C  C   . HIS C  1 89  ? -24.529 28.938  13.126  1.00 34.43  ?  120  HIS C C   1 
ATOM   8044  O  O   . HIS C  1 89  ? -25.097 28.252  13.982  1.00 32.76  ?  120  HIS C O   1 
ATOM   8045  C  CB  . HIS C  1 89  ? -22.083 28.945  13.594  1.00 37.63  ?  120  HIS C CB  1 
ATOM   8046  C  CG  . HIS C  1 89  ? -20.943 29.568  14.351  1.00 36.49  ?  120  HIS C CG  1 
ATOM   8047  N  ND1 . HIS C  1 89  ? -20.315 30.727  13.943  1.00 44.17  ?  120  HIS C ND1 1 
ATOM   8048  C  CD2 . HIS C  1 89  ? -20.323 29.191  15.497  1.00 43.46  ?  120  HIS C CD2 1 
ATOM   8049  C  CE1 . HIS C  1 89  ? -19.343 31.027  14.792  1.00 38.79  ?  120  HIS C CE1 1 
ATOM   8050  N  NE2 . HIS C  1 89  ? -19.332 30.114  15.748  1.00 41.84  ?  120  HIS C NE2 1 
ATOM   8051  N  N   . ASN C  1 90  ? -24.886 28.936  11.840  1.00 32.21  ?  121  ASN C N   1 
ATOM   8052  C  CA  . ASN C  1 90  ? -25.979 28.090  11.335  1.00 36.77  ?  121  ASN C CA  1 
ATOM   8053  C  C   . ASN C  1 90  ? -27.281 28.308  12.112  1.00 36.05  ?  121  ASN C C   1 
ATOM   8054  O  O   . ASN C  1 90  ? -27.984 27.349  12.451  1.00 34.80  ?  121  ASN C O   1 
ATOM   8055  C  CB  . ASN C  1 90  ? -25.606 26.597  11.381  1.00 36.38  ?  121  ASN C CB  1 
ATOM   8056  C  CG  . ASN C  1 90  ? -24.413 26.239  10.497  1.00 41.45  ?  121  ASN C CG  1 
ATOM   8057  O  OD1 . ASN C  1 90  ? -23.285 26.688  10.728  1.00 37.57  ?  121  ASN C OD1 1 
ATOM   8058  N  ND2 . ASN C  1 90  ? -24.655 25.399  9.498   1.00 41.43  ?  121  ASN C ND2 1 
ATOM   8059  N  N   . SER C  1 91  ? -27.617 29.572  12.395  1.00 32.97  ?  122  SER C N   1 
ATOM   8060  C  CA  . SER C  1 91  ? -28.856 29.874  13.112  1.00 32.41  ?  122  SER C CA  1 
ATOM   8061  C  C   . SER C  1 91  ? -30.082 29.453  12.296  1.00 34.42  ?  122  SER C C   1 
ATOM   8062  O  O   . SER C  1 91  ? -30.025 29.290  11.073  1.00 34.69  ?  122  SER C O   1 
ATOM   8063  C  CB  . SER C  1 91  ? -28.947 31.367  13.445  1.00 28.91  ?  122  SER C CB  1 
ATOM   8064  O  OG  . SER C  1 91  ? -28.967 32.161  12.266  1.00 29.95  ?  122  SER C OG  1 
ATOM   8065  N  N   . SER C  1 92  ? -31.214 29.313  12.993  1.00 35.82  ?  123  SER C N   1 
ATOM   8066  C  CA  . SER C  1 92  ? -32.369 28.636  12.411  1.00 39.50  ?  123  SER C CA  1 
ATOM   8067  C  C   . SER C  1 92  ? -32.864 29.348  11.162  1.00 38.23  ?  123  SER C C   1 
ATOM   8068  O  O   . SER C  1 92  ? -33.104 30.560  11.161  1.00 35.55  ?  123  SER C O   1 
ATOM   8069  C  CB  . SER C  1 92  ? -33.515 28.523  13.414  1.00 38.30  ?  123  SER C CB  1 
ATOM   8070  O  OG  . SER C  1 92  ? -34.684 28.070  12.737  1.00 41.99  ?  123  SER C OG  1 
ATOM   8071  N  N   . GLU C  1 93  ? -33.027 28.576  10.098  1.00 37.65  ?  124  GLU C N   1 
ATOM   8072  C  CA  . GLU C  1 93  ? -33.603 29.055  8.860   1.00 37.69  ?  124  GLU C CA  1 
ATOM   8073  C  C   . GLU C  1 93  ? -35.116 28.914  8.830   1.00 38.01  ?  124  GLU C C   1 
ATOM   8074  O  O   . GLU C  1 93  ? -35.710 29.108  7.771   1.00 37.33  ?  124  GLU C O   1 
ATOM   8075  C  CB  . GLU C  1 93  ? -32.961 28.317  7.682   1.00 39.06  ?  124  GLU C CB  1 
ATOM   8076  C  CG  . GLU C  1 93  ? -31.437 28.416  7.746   1.00 43.13  ?  124  GLU C CG  1 
ATOM   8077  C  CD  . GLU C  1 93  ? -30.718 27.558  6.725   1.00 47.45  ?  124  GLU C CD  1 
ATOM   8078  O  OE1 . GLU C  1 93  ? -31.383 26.803  5.997   1.00 50.78  ?  124  GLU C OE1 1 
ATOM   8079  O  OE2 . GLU C  1 93  ? -29.471 27.638  6.670   1.00 54.26  -1 124  GLU C OE2 1 
ATOM   8080  N  N   . ASP C  1 94  ? -35.757 28.619  9.960   1.00 41.75  ?  125  ASP C N   1 
ATOM   8081  C  CA  . ASP C  1 94  ? -37.204 28.428  9.993   1.00 42.84  ?  125  ASP C CA  1 
ATOM   8082  C  C   . ASP C  1 94  ? -37.831 29.688  10.587  1.00 42.04  ?  125  ASP C C   1 
ATOM   8083  O  O   . ASP C  1 94  ? -37.417 30.147  11.659  1.00 39.04  ?  125  ASP C O   1 
ATOM   8084  C  CB  . ASP C  1 94  ? -37.585 27.219  10.855  1.00 43.16  ?  125  ASP C CB  1 
ATOM   8085  C  CG  . ASP C  1 94  ? -39.108 26.957  10.887  1.00 57.17  ?  125  ASP C CG  1 
ATOM   8086  O  OD1 . ASP C  1 94  ? -39.936 27.899  10.843  1.00 53.75  ?  125  ASP C OD1 1 
ATOM   8087  O  OD2 . ASP C  1 94  ? -39.484 25.774  11.050  1.00 63.14  -1 125  ASP C OD2 1 
ATOM   8088  N  N   . ASP C  1 95  ? -38.851 30.223  9.914   1.00 36.90  ?  126  ASP C N   1 
ATOM   8089  C  CA  . ASP C  1 95  ? -39.482 31.469  10.357  1.00 39.92  ?  126  ASP C CA  1 
ATOM   8090  C  C   . ASP C  1 95  ? -40.041 31.391  11.776  1.00 42.37  ?  126  ASP C C   1 
ATOM   8091  O  O   . ASP C  1 95  ? -40.069 32.406  12.485  1.00 42.93  ?  126  ASP C O   1 
ATOM   8092  C  CB  . ASP C  1 95  ? -40.601 31.860  9.387   1.00 44.01  ?  126  ASP C CB  1 
ATOM   8093  C  CG  . ASP C  1 95  ? -40.097 32.658  8.202   1.00 41.47  ?  126  ASP C CG  1 
ATOM   8094  O  OD1 . ASP C  1 95  ? -38.895 32.970  8.169   1.00 38.24  ?  126  ASP C OD1 1 
ATOM   8095  O  OD2 . ASP C  1 95  ? -40.907 32.975  7.302   1.00 45.40  -1 126  ASP C OD2 1 
ATOM   8096  N  N   . LYS C  1 96  ? -40.498 30.214  12.219  1.00 43.72  ?  127  LYS C N   1 
ATOM   8097  C  CA  . LYS C  1 96  ? -41.100 30.126  13.551  1.00 45.34  ?  127  LYS C CA  1 
ATOM   8098  C  C   . LYS C  1 96  ? -40.093 30.378  14.669  1.00 41.22  ?  127  LYS C C   1 
ATOM   8099  O  O   . LYS C  1 96  ? -40.497 30.650  15.803  1.00 42.23  ?  127  LYS C O   1 
ATOM   8100  C  CB  . LYS C  1 96  ? -41.740 28.748  13.781  1.00 48.26  ?  127  LYS C CB  1 
ATOM   8101  C  CG  . LYS C  1 96  ? -40.773 27.596  13.549  1.00 51.33  ?  127  LYS C CG  1 
ATOM   8102  C  CD  . LYS C  1 96  ? -41.236 26.236  14.062  1.00 59.55  ?  127  LYS C CD  1 
ATOM   8103  C  CE  . LYS C  1 96  ? -40.030 25.360  14.414  1.00 54.31  ?  127  LYS C CE  1 
ATOM   8104  N  NZ  . LYS C  1 96  ? -39.787 25.280  15.882  1.00 59.45  ?  127  LYS C NZ  1 
ATOM   8105  N  N   . ASP C  1 97  ? -38.797 30.281  14.396  1.00 43.35  ?  128  ASP C N   1 
ATOM   8106  C  CA  . ASP C  1 97  ? -37.827 30.437  15.473  1.00 39.01  ?  128  ASP C CA  1 
ATOM   8107  C  C   . ASP C  1 97  ? -37.388 31.887  15.673  1.00 36.92  ?  128  ASP C C   1 
ATOM   8108  O  O   . ASP C  1 97  ? -36.645 32.164  16.624  1.00 39.70  ?  128  ASP C O   1 
ATOM   8109  C  CB  . ASP C  1 97  ? -36.613 29.540  15.209  1.00 37.79  ?  128  ASP C CB  1 
ATOM   8110  C  CG  . ASP C  1 97  ? -36.937 28.051  15.357  1.00 45.53  ?  128  ASP C CG  1 
ATOM   8111  O  OD1 . ASP C  1 97  ? -37.602 27.663  16.344  1.00 46.49  ?  128  ASP C OD1 1 
ATOM   8112  O  OD2 . ASP C  1 97  ? -36.498 27.258  14.494  1.00 44.52  -1 128  ASP C OD2 1 
ATOM   8113  N  N   . ASN C  1 98  ? -37.817 32.802  14.799  1.00 34.04  ?  129  ASN C N   1 
ATOM   8114  C  CA  . ASN C  1 98  ? -37.556 34.243  14.925  1.00 37.76  ?  129  ASN C CA  1 
ATOM   8115  C  C   . ASN C  1 98  ? -36.098 34.558  15.266  1.00 32.16  ?  129  ASN C C   1 
ATOM   8116  O  O   . ASN C  1 98  ? -35.799 35.444  16.063  1.00 39.72  ?  129  ASN C O   1 
ATOM   8117  C  CB  . ASN C  1 98  ? -38.490 34.876  15.951  1.00 38.22  ?  129  ASN C CB  1 
ATOM   8118  C  CG  . ASN C  1 98  ? -39.904 34.907  15.467  1.00 43.18  ?  129  ASN C CG  1 
ATOM   8119  O  OD1 . ASN C  1 98  ? -40.161 35.285  14.323  1.00 47.05  ?  129  ASN C OD1 1 
ATOM   8120  N  ND2 . ASN C  1 98  ? -40.834 34.483  16.312  1.00 44.85  ?  129  ASN C ND2 1 
ATOM   8121  N  N   . MET C  1 99  ? -35.180 33.840  14.640  1.00 31.27  ?  130  MET C N   1 
ATOM   8122  C  CA  . MET C  1 99  ? -33.744 34.092  14.815  1.00 30.54  ?  130  MET C CA  1 
ATOM   8123  C  C   . MET C  1 99  ? -33.318 35.133  13.787  1.00 30.46  ?  130  MET C C   1 
ATOM   8124  O  O   . MET C  1 99  ? -32.686 34.833  12.772  1.00 31.84  ?  130  MET C O   1 
ATOM   8125  C  CB  . MET C  1 99  ? -32.979 32.785  14.677  1.00 32.94  ?  130  MET C CB  1 
ATOM   8126  C  CG  . MET C  1 99  ? -32.798 31.963  15.953  1.00 35.26  ?  130  MET C CG  1 
ATOM   8127  S  SD  . MET C  1 99  ? -32.187 32.800  17.459  1.00 39.77  ?  130  MET C SD  1 
ATOM   8128  C  CE  . MET C  1 99  ? -32.366 31.455  18.644  1.00 32.78  ?  130  MET C CE  1 
ATOM   8129  N  N   . GLY C  1 100 ? -33.682 36.382  14.057  1.00 29.72  ?  131  GLY C N   1 
ATOM   8130  C  CA  . GLY C  1 100 ? -33.408 37.459  13.118  1.00 28.51  ?  131  GLY C CA  1 
ATOM   8131  C  C   . GLY C  1 100 ? -33.923 38.768  13.676  1.00 30.04  ?  131  GLY C C   1 
ATOM   8132  O  O   . GLY C  1 100 ? -34.687 38.798  14.646  1.00 33.83  ?  131  GLY C O   1 
ATOM   8133  N  N   . VAL C  1 101 ? -33.478 39.858  13.055  1.00 29.58  ?  132  VAL C N   1 
ATOM   8134  C  CA  . VAL C  1 101 ? -33.898 41.179  13.530  1.00 26.12  ?  132  VAL C CA  1 
ATOM   8135  C  C   . VAL C  1 101 ? -35.401 41.319  13.338  1.00 33.85  ?  132  VAL C C   1 
ATOM   8136  O  O   . VAL C  1 101 ? -35.898 41.022  12.238  1.00 31.62  ?  132  VAL C O   1 
ATOM   8137  C  CB  . VAL C  1 101 ? -33.156 42.286  12.775  1.00 32.80  ?  132  VAL C CB  1 
ATOM   8138  C  CG1 . VAL C  1 101 ? -33.590 43.633  13.296  1.00 32.72  ?  132  VAL C CG1 1 
ATOM   8139  C  CG2 . VAL C  1 101 ? -31.627 42.133  12.966  1.00 34.87  ?  132  VAL C CG2 1 
ATOM   8140  N  N   . PRO C  1 102 ? -36.161 41.784  14.362  1.00 34.66  ?  133  PRO C N   1 
ATOM   8141  C  CA  . PRO C  1 102 ? -37.621 41.927  14.224  1.00 38.11  ?  133  PRO C CA  1 
ATOM   8142  C  C   . PRO C  1 102 ? -38.078 42.488  12.885  1.00 33.06  ?  133  PRO C C   1 
ATOM   8143  O  O   . PRO C  1 102 ? -37.619 43.549  12.459  1.00 33.30  ?  133  PRO C O   1 
ATOM   8144  C  CB  . PRO C  1 102 ? -37.987 42.883  15.369  1.00 38.02  ?  133  PRO C CB  1 
ATOM   8145  C  CG  . PRO C  1 102 ? -36.954 42.633  16.408  1.00 36.48  ?  133  PRO C CG  1 
ATOM   8146  C  CD  . PRO C  1 102 ? -35.673 42.316  15.648  1.00 35.19  ?  133  PRO C CD  1 
ATOM   8147  N  N   . VAL C  1 103 ? -39.010 41.794  12.219  1.00 37.43  ?  134  VAL C N   1 
ATOM   8148  C  CA  . VAL C  1 103 ? -39.465 42.245  10.906  1.00 34.67  ?  134  VAL C CA  1 
ATOM   8149  C  C   . VAL C  1 103 ? -40.167 43.591  10.976  1.00 37.71  ?  134  VAL C C   1 
ATOM   8150  O  O   . VAL C  1 103 ? -40.292 44.278  9.955   1.00 40.21  ?  134  VAL C O   1 
ATOM   8151  C  CB  . VAL C  1 103 ? -40.399 41.199  10.252  1.00 43.48  ?  134  VAL C CB  1 
ATOM   8152  C  CG1 . VAL C  1 103 ? -39.583 39.976  9.791   1.00 38.88  ?  134  VAL C CG1 1 
ATOM   8153  C  CG2 . VAL C  1 103 ? -41.529 40.819  11.206  1.00 39.25  ?  134  VAL C CG2 1 
ATOM   8154  N  N   . GLU C  1 104 ? -40.644 43.985  12.151  1.00 35.01  ?  135  GLU C N   1 
ATOM   8155  C  CA  . GLU C  1 104 ? -41.365 45.245  12.261  1.00 40.43  ?  135  GLU C CA  1 
ATOM   8156  C  C   . GLU C  1 104 ? -40.456 46.466  12.397  1.00 41.88  ?  135  GLU C C   1 
ATOM   8157  O  O   . GLU C  1 104 ? -40.948 47.591  12.266  1.00 40.47  ?  135  GLU C O   1 
ATOM   8158  C  CB  . GLU C  1 104 ? -42.330 45.156  13.437  1.00 42.14  ?  135  GLU C CB  1 
ATOM   8159  C  CG  . GLU C  1 104 ? -41.656 45.210  14.770  1.00 50.78  ?  135  GLU C CG  1 
ATOM   8160  C  CD  . GLU C  1 104 ? -41.693 43.859  15.471  1.00 55.41  ?  135  GLU C CD  1 
ATOM   8161  O  OE1 . GLU C  1 104 ? -41.951 42.847  14.773  1.00 54.42  ?  135  GLU C OE1 1 
ATOM   8162  O  OE2 . GLU C  1 104 ? -41.409 43.808  16.695  1.00 59.58  -1 135  GLU C OE2 1 
ATOM   8163  N  N   . GLU C  1 105 ? -39.157 46.288  12.656  1.00 38.05  ?  136  GLU C N   1 
ATOM   8164  C  CA  . GLU C  1 105 ? -38.203 47.399  12.606  1.00 36.10  ?  136  GLU C CA  1 
ATOM   8165  C  C   . GLU C  1 105 ? -37.830 47.636  11.154  1.00 38.28  ?  136  GLU C C   1 
ATOM   8166  O  O   . GLU C  1 105 ? -36.942 46.972  10.618  1.00 44.27  ?  136  GLU C O   1 
ATOM   8167  C  CB  . GLU C  1 105 ? -36.941 47.094  13.409  1.00 37.24  ?  136  GLU C CB  1 
ATOM   8168  C  CG  . GLU C  1 105 ? -36.988 47.421  14.864  1.00 44.41  ?  136  GLU C CG  1 
ATOM   8169  C  CD  . GLU C  1 105 ? -37.311 48.871  15.180  1.00 38.48  ?  136  GLU C CD  1 
ATOM   8170  O  OE1 . GLU C  1 105 ? -37.094 49.788  14.348  1.00 37.53  ?  136  GLU C OE1 1 
ATOM   8171  O  OE2 . GLU C  1 105 ? -37.801 49.078  16.302  1.00 41.69  -1 136  GLU C OE2 1 
ATOM   8172  N  N   . THR C  1 106 ? -38.476 48.602  10.514  1.00 37.54  ?  137  THR C N   1 
ATOM   8173  C  CA  . THR C  1 106 ? -38.278 48.817  9.091   1.00 37.24  ?  137  THR C CA  1 
ATOM   8174  C  C   . THR C  1 106 ? -36.857 49.277  8.786   1.00 36.10  ?  137  THR C C   1 
ATOM   8175  O  O   . THR C  1 106 ? -36.380 50.264  9.353   1.00 37.48  ?  137  THR C O   1 
ATOM   8176  C  CB  . THR C  1 106 ? -39.286 49.843  8.586   1.00 40.48  ?  137  THR C CB  1 
ATOM   8177  O  OG1 . THR C  1 106 ? -40.599 49.445  9.011   1.00 37.25  ?  137  THR C OG1 1 
ATOM   8178  C  CG2 . THR C  1 106 ? -39.228 49.949  7.079   1.00 37.60  ?  137  THR C CG2 1 
ATOM   8179  N  N   . TYR C  1 107 ? -36.203 48.576  7.860   1.00 32.92  ?  138  TYR C N   1 
ATOM   8180  C  CA  . TYR C  1 107 ? -34.855 48.931  7.426   1.00 37.52  ?  138  TYR C CA  1 
ATOM   8181  C  C   . TYR C  1 107 ? -34.871 50.153  6.519   1.00 38.97  ?  138  TYR C C   1 
ATOM   8182  O  O   . TYR C  1 107 ? -35.839 50.412  5.794   1.00 34.59  ?  138  TYR C O   1 
ATOM   8183  C  CB  . TYR C  1 107 ? -34.199 47.788  6.651   1.00 32.82  ?  138  TYR C CB  1 
ATOM   8184  C  CG  . TYR C  1 107 ? -33.808 46.581  7.451   1.00 31.16  ?  138  TYR C CG  1 
ATOM   8185  C  CD1 . TYR C  1 107 ? -34.125 46.469  8.794   1.00 29.92  ?  138  TYR C CD1 1 
ATOM   8186  C  CD2 . TYR C  1 107 ? -33.142 45.526  6.843   1.00 30.34  ?  138  TYR C CD2 1 
ATOM   8187  C  CE1 . TYR C  1 107 ? -33.769 45.342  9.517   1.00 32.09  ?  138  TYR C CE1 1 
ATOM   8188  C  CE2 . TYR C  1 107 ? -32.777 44.409  7.560   1.00 31.46  ?  138  TYR C CE2 1 
ATOM   8189  C  CZ  . TYR C  1 107 ? -33.081 44.325  8.890   1.00 30.51  ?  138  TYR C CZ  1 
ATOM   8190  O  OH  . TYR C  1 107 ? -32.724 43.196  9.593   1.00 32.53  ?  138  TYR C OH  1 
ATOM   8191  N  N   . MET C  1 108 ? -33.751 50.877  6.517   1.00 33.87  ?  139  MET C N   1 
ATOM   8192  C  CA  . MET C  1 108 ? -33.630 52.019  5.620   1.00 36.38  ?  139  MET C CA  1 
ATOM   8193  C  C   . MET C  1 108 ? -33.683 51.599  4.160   1.00 37.65  ?  139  MET C C   1 
ATOM   8194  O  O   . MET C  1 108 ? -34.121 52.384  3.310   1.00 36.57  ?  139  MET C O   1 
ATOM   8195  C  CB  . MET C  1 108 ? -32.345 52.787  5.910   1.00 42.09  ?  139  MET C CB  1 
ATOM   8196  C  CG  . MET C  1 108 ? -31.065 52.046  5.546   1.00 41.01  ?  139  MET C CG  1 
ATOM   8197  S  SD  . MET C  1 108 ? -29.688 53.112  5.992   1.00 38.66  ?  139  MET C SD  1 
ATOM   8198  C  CE  . MET C  1 108 ? -28.281 51.987  6.044   1.00 43.89  ?  139  MET C CE  1 
ATOM   8199  N  N   . SER C  1 109 ? -33.238 50.379  3.848   1.00 32.21  ?  140  SER C N   1 
ATOM   8200  C  CA  . SER C  1 109 ? -33.362 49.868  2.490   1.00 33.14  ?  140  SER C CA  1 
ATOM   8201  C  C   . SER C  1 109 ? -34.819 49.896  2.028   1.00 37.62  ?  140  SER C C   1 
ATOM   8202  O  O   . SER C  1 109 ? -35.115 50.330  0.913   1.00 33.17  ?  140  SER C O   1 
ATOM   8203  C  CB  . SER C  1 109 ? -32.824 48.446  2.430   1.00 30.31  ?  140  SER C CB  1 
ATOM   8204  O  OG  . SER C  1 109 ? -33.340 47.724  3.534   1.00 33.12  ?  140  SER C OG  1 
ATOM   8205  N  N   . LYS C  1 110 ? -35.739 49.409  2.872   1.00 36.69  ?  141  LYS C N   1 
ATOM   8206  C  CA  . LYS C  1 110 ? -37.152 49.404  2.490   1.00 40.53  ?  141  LYS C CA  1 
ATOM   8207  C  C   . LYS C  1 110 ? -37.668 50.824  2.301   1.00 40.12  ?  141  LYS C C   1 
ATOM   8208  O  O   . LYS C  1 110 ? -38.408 51.107  1.351   1.00 44.53  ?  141  LYS C O   1 
ATOM   8209  C  CB  . LYS C  1 110 ? -37.981 48.676  3.545   1.00 38.67  ?  141  LYS C CB  1 
ATOM   8210  C  CG  . LYS C  1 110 ? -39.446 48.436  3.138   1.00 42.15  ?  141  LYS C CG  1 
ATOM   8211  C  CD  . LYS C  1 110 ? -40.076 47.375  4.039   1.00 48.26  ?  141  LYS C CD  1 
ATOM   8212  C  CE  . LYS C  1 110 ? -40.040 45.974  3.407   1.00 47.19  ?  141  LYS C CE  1 
ATOM   8213  N  NZ  . LYS C  1 110 ? -40.343 44.902  4.420   1.00 46.79  ?  141  LYS C NZ  1 
ATOM   8214  N  N   . VAL C  1 111 ? -37.269 51.729  3.194   1.00 39.82  ?  142  VAL C N   1 
ATOM   8215  C  CA  . VAL C  1 111 ? -37.640 53.134  3.077   1.00 40.35  ?  142  VAL C CA  1 
ATOM   8216  C  C   . VAL C  1 111 ? -37.173 53.700  1.741   1.00 40.72  ?  142  VAL C C   1 
ATOM   8217  O  O   . VAL C  1 111 ? -37.925 54.382  1.040   1.00 40.49  ?  142  VAL C O   1 
ATOM   8218  C  CB  . VAL C  1 111 ? -37.071 53.934  4.267   1.00 40.21  ?  142  VAL C CB  1 
ATOM   8219  C  CG1 . VAL C  1 111 ? -37.422 55.404  4.131   1.00 43.23  ?  142  VAL C CG1 1 
ATOM   8220  C  CG2 . VAL C  1 111 ? -37.608 53.383  5.585   1.00 36.37  ?  142  VAL C CG2 1 
ATOM   8221  N  N   . LEU C  1 112 ? -35.926 53.423  1.357   1.00 39.40  ?  143  LEU C N   1 
ATOM   8222  C  CA  . LEU C  1 112 ? -35.425 54.011  0.120   1.00 37.43  ?  143  LEU C CA  1 
ATOM   8223  C  C   . LEU C  1 112 ? -36.078 53.359  -1.090  1.00 39.68  ?  143  LEU C C   1 
ATOM   8224  O  O   . LEU C  1 112 ? -36.361 54.032  -2.084  1.00 42.54  ?  143  LEU C O   1 
ATOM   8225  C  CB  . LEU C  1 112 ? -33.905 53.887  0.046   1.00 36.51  ?  143  LEU C CB  1 
ATOM   8226  C  CG  . LEU C  1 112 ? -33.157 54.555  1.208   1.00 37.65  ?  143  LEU C CG  1 
ATOM   8227  C  CD1 . LEU C  1 112 ? -31.679 54.236  1.125   1.00 39.12  ?  143  LEU C CD1 1 
ATOM   8228  C  CD2 . LEU C  1 112 ? -33.384 56.046  1.206   1.00 37.31  ?  143  LEU C CD2 1 
ATOM   8229  N  N   . GLN C  1 113 ? -36.315 52.046  -1.012  1.00 38.07  ?  144  GLN C N   1 
ATOM   8230  C  CA  . GLN C  1 113 ? -37.016 51.325  -2.068  1.00 37.95  ?  144  GLN C CA  1 
ATOM   8231  C  C   . GLN C  1 113 ? -38.411 51.900  -2.290  1.00 42.01  ?  144  GLN C C   1 
ATOM   8232  O  O   . GLN C  1 113 ? -38.823 52.107  -3.434  1.00 42.77  ?  144  GLN C O   1 
ATOM   8233  C  CB  . GLN C  1 113 ? -37.094 49.841  -1.702  1.00 39.26  ?  144  GLN C CB  1 
ATOM   8234  C  CG  . GLN C  1 113 ? -37.698 48.938  -2.765  1.00 40.64  ?  144  GLN C CG  1 
ATOM   8235  C  CD  . GLN C  1 113 ? -37.870 47.511  -2.272  1.00 39.05  ?  144  GLN C CD  1 
ATOM   8236  O  OE1 . GLN C  1 113 ? -38.476 47.265  -1.213  1.00 40.19  ?  144  GLN C OE1 1 
ATOM   8237  N  NE2 . GLN C  1 113 ? -37.316 46.559  -3.023  1.00 37.06  ?  144  GLN C NE2 1 
ATOM   8238  N  N   . ASN C  1 114 ? -39.143 52.182  -1.203  1.00 43.13  ?  145  ASN C N   1 
ATOM   8239  C  CA  . ASN C  1 114 ? -40.461 52.795  -1.317  1.00 43.19  ?  145  ASN C CA  1 
ATOM   8240  C  C   . ASN C  1 114 ? -40.398 54.218  -1.859  1.00 46.08  ?  145  ASN C C   1 
ATOM   8241  O  O   . ASN C  1 114 ? -41.402 54.713  -2.384  1.00 46.88  ?  145  ASN C O   1 
ATOM   8242  C  CB  . ASN C  1 114 ? -41.179 52.797  0.033   1.00 39.65  ?  145  ASN C CB  1 
ATOM   8243  C  CG  . ASN C  1 114 ? -41.552 51.393  0.515   1.00 48.58  ?  145  ASN C CG  1 
ATOM   8244  O  OD1 . ASN C  1 114 ? -41.391 50.399  -0.201  1.00 51.99  ?  145  ASN C OD1 1 
ATOM   8245  N  ND2 . ASN C  1 114 ? -42.085 51.315  1.732   1.00 52.45  ?  145  ASN C ND2 1 
ATOM   8246  N  N   . ALA C  1 115 ? -39.257 54.886  -1.744  1.00 41.79  ?  146  ALA C N   1 
ATOM   8247  C  CA  . ALA C  1 115 ? -39.051 56.197  -2.339  1.00 41.36  ?  146  ALA C CA  1 
ATOM   8248  C  C   . ALA C  1 115 ? -38.515 56.125  -3.764  1.00 39.91  ?  146  ALA C C   1 
ATOM   8249  O  O   . ALA C  1 115 ? -38.154 57.162  -4.328  1.00 40.38  ?  146  ALA C O   1 
ATOM   8250  C  CB  . ALA C  1 115 ? -38.095 57.024  -1.472  1.00 45.23  ?  146  ALA C CB  1 
ATOM   8251  N  N   . GLY C  1 116 ? -38.429 54.934  -4.349  1.00 36.52  ?  147  GLY C N   1 
ATOM   8252  C  CA  . GLY C  1 116 ? -38.035 54.801  -5.735  1.00 37.85  ?  147  GLY C CA  1 
ATOM   8253  C  C   . GLY C  1 116 ? -36.579 54.501  -6.013  1.00 41.54  ?  147  GLY C C   1 
ATOM   8254  O  O   . GLY C  1 116 ? -36.171 54.531  -7.183  1.00 38.09  ?  147  GLY C O   1 
ATOM   8255  N  N   . TYR C  1 117 ? -35.780 54.198  -4.994  1.00 39.20  ?  148  TYR C N   1 
ATOM   8256  C  CA  . TYR C  1 117 ? -34.407 53.798  -5.246  1.00 40.62  ?  148  TYR C CA  1 
ATOM   8257  C  C   . TYR C  1 117 ? -34.362 52.361  -5.736  1.00 35.78  ?  148  TYR C C   1 
ATOM   8258  O  O   . TYR C  1 117 ? -35.160 51.525  -5.308  1.00 36.07  ?  148  TYR C O   1 
ATOM   8259  C  CB  . TYR C  1 117 ? -33.569 53.941  -3.968  1.00 34.09  ?  148  TYR C CB  1 
ATOM   8260  C  CG  . TYR C  1 117 ? -32.997 55.323  -3.815  1.00 39.86  ?  148  TYR C CG  1 
ATOM   8261  C  CD1 . TYR C  1 117 ? -33.832 56.435  -3.687  1.00 40.46  ?  148  TYR C CD1 1 
ATOM   8262  C  CD2 . TYR C  1 117 ? -31.626 55.531  -3.807  1.00 36.26  ?  148  TYR C CD2 1 
ATOM   8263  C  CE1 . TYR C  1 117 ? -33.304 57.724  -3.555  1.00 40.08  ?  148  TYR C CE1 1 
ATOM   8264  C  CE2 . TYR C  1 117 ? -31.098 56.798  -3.680  1.00 39.71  ?  148  TYR C CE2 1 
ATOM   8265  C  CZ  . TYR C  1 117 ? -31.934 57.894  -3.560  1.00 39.41  ?  148  TYR C CZ  1 
ATOM   8266  O  OH  . TYR C  1 117 ? -31.380 59.149  -3.428  1.00 41.70  ?  148  TYR C OH  1 
ATOM   8267  N  N   . TYR C  1 118 ? -33.431 52.084  -6.648  1.00 36.60  ?  149  TYR C N   1 
ATOM   8268  C  CA  . TYR C  1 118 ? -32.996 50.719  -6.915  1.00 37.10  ?  149  TYR C CA  1 
ATOM   8269  C  C   . TYR C  1 118 ? -32.074 50.263  -5.779  1.00 38.33  ?  149  TYR C C   1 
ATOM   8270  O  O   . TYR C  1 118 ? -31.005 50.851  -5.572  1.00 35.71  ?  149  TYR C O   1 
ATOM   8271  C  CB  . TYR C  1 118 ? -32.264 50.649  -8.252  1.00 35.69  ?  149  TYR C CB  1 
ATOM   8272  C  CG  . TYR C  1 118 ? -31.658 49.287  -8.516  1.00 44.28  ?  149  TYR C CG  1 
ATOM   8273  C  CD1 . TYR C  1 118 ? -32.456 48.153  -8.540  1.00 45.78  ?  149  TYR C CD1 1 
ATOM   8274  C  CD2 . TYR C  1 118 ? -30.296 49.129  -8.727  1.00 36.69  ?  149  TYR C CD2 1 
ATOM   8275  C  CE1 . TYR C  1 118 ? -31.924 46.905  -8.772  1.00 44.99  ?  149  TYR C CE1 1 
ATOM   8276  C  CE2 . TYR C  1 118 ? -29.750 47.864  -8.963  1.00 41.11  ?  149  TYR C CE2 1 
ATOM   8277  C  CZ  . TYR C  1 118 ? -30.575 46.759  -8.974  1.00 40.95  ?  149  TYR C CZ  1 
ATOM   8278  O  OH  . TYR C  1 118 ? -30.087 45.495  -9.208  1.00 41.66  ?  149  TYR C OH  1 
ATOM   8279  N  N   . THR C  1 119 ? -32.479 49.235  -5.034  1.00 36.66  ?  150  THR C N   1 
ATOM   8280  C  CA  . THR C  1 119 ? -31.747 48.810  -3.847  1.00 34.02  ?  150  THR C CA  1 
ATOM   8281  C  C   . THR C  1 119 ? -31.060 47.474  -4.095  1.00 39.66  ?  150  THR C C   1 
ATOM   8282  O  O   . THR C  1 119 ? -31.611 46.590  -4.758  1.00 37.59  ?  150  THR C O   1 
ATOM   8283  C  CB  . THR C  1 119 ? -32.668 48.711  -2.624  1.00 33.98  ?  150  THR C CB  1 
ATOM   8284  O  OG1 . THR C  1 119 ? -33.731 47.774  -2.865  1.00 35.97  ?  150  THR C OG1 1 
ATOM   8285  C  CG2 . THR C  1 119 ? -33.243 50.086  -2.266  1.00 33.33  ?  150  THR C CG2 1 
ATOM   8286  N  N   . SER C  1 120 ? -29.859 47.322  -3.547  1.00 32.98  ?  151  SER C N   1 
ATOM   8287  C  CA  . SER C  1 120 ? -29.088 46.112  -3.763  1.00 32.61  ?  151  SER C CA  1 
ATOM   8288  C  C   . SER C  1 120 ? -28.220 45.877  -2.529  1.00 36.07  ?  151  SER C C   1 
ATOM   8289  O  O   . SER C  1 120 ? -27.778 46.834  -1.891  1.00 33.22  ?  151  SER C O   1 
ATOM   8290  C  CB  . SER C  1 120 ? -28.247 46.247  -5.034  1.00 34.68  ?  151  SER C CB  1 
ATOM   8291  O  OG  . SER C  1 120 ? -27.161 45.341  -5.038  1.00 47.94  ?  151  SER C OG  1 
ATOM   8292  N  N   . ALA C  1 121 ? -28.042 44.608  -2.159  1.00 30.01  ?  152  ALA C N   1 
ATOM   8293  C  CA  . ALA C  1 121 ? -27.200 44.229  -1.037  1.00 30.22  ?  152  ALA C CA  1 
ATOM   8294  C  C   . ALA C  1 121 ? -26.228 43.188  -1.549  1.00 34.71  ?  152  ALA C C   1 
ATOM   8295  O  O   . ALA C  1 121 ? -26.620 42.292  -2.300  1.00 35.05  ?  152  ALA C O   1 
ATOM   8296  C  CB  . ALA C  1 121 ? -28.019 43.671  0.142   1.00 30.90  ?  152  ALA C CB  1 
ATOM   8297  N  N   . ILE C  1 122 ? -24.956 43.315  -1.172  1.00 33.25  ?  153  ILE C N   1 
ATOM   8298  C  CA  . ILE C  1 122 ? -23.923 42.406  -1.645  1.00 32.17  ?  153  ILE C CA  1 
ATOM   8299  C  C   . ILE C  1 122 ? -23.061 41.996  -0.460  1.00 33.95  ?  153  ILE C C   1 
ATOM   8300  O  O   . ILE C  1 122 ? -22.730 42.827  0.398   1.00 31.85  ?  153  ILE C O   1 
ATOM   8301  C  CB  . ILE C  1 122 ? -23.052 43.038  -2.754  1.00 32.13  ?  153  ILE C CB  1 
ATOM   8302  C  CG1 . ILE C  1 122 ? -23.894 43.416  -3.972  1.00 34.40  ?  153  ILE C CG1 1 
ATOM   8303  C  CG2 . ILE C  1 122 ? -21.940 42.088  -3.176  1.00 31.22  ?  153  ILE C CG2 1 
ATOM   8304  C  CD1 . ILE C  1 122 ? -23.299 44.561  -4.764  1.00 32.97  ?  153  ILE C CD1 1 
ATOM   8305  N  N   . GLY C  1 123 ? -22.722 40.715  -0.403  1.00 32.43  ?  154  GLY C N   1 
ATOM   8306  C  CA  . GLY C  1 123 ? -21.781 40.215  0.586   1.00 29.18  ?  154  GLY C CA  1 
ATOM   8307  C  C   . GLY C  1 123 ? -22.497 39.682  1.820   1.00 30.44  ?  154  GLY C C   1 
ATOM   8308  O  O   . GLY C  1 123 ? -23.419 38.865  1.715   1.00 31.27  ?  154  GLY C O   1 
ATOM   8309  N  N   . LYS C  1 124 ? -22.080 40.157  2.983   1.00 30.40  ?  155  LYS C N   1 
ATOM   8310  C  CA  . LYS C  1 124 ? -22.458 39.594  4.270   1.00 31.40  ?  155  LYS C CA  1 
ATOM   8311  C  C   . LYS C  1 124 ? -23.760 40.204  4.752   1.00 28.81  ?  155  LYS C C   1 
ATOM   8312  O  O   . LYS C  1 124 ? -23.976 41.411  4.607   1.00 30.26  ?  155  LYS C O   1 
ATOM   8313  C  CB  . LYS C  1 124 ? -21.355 39.868  5.296   1.00 29.01  ?  155  LYS C CB  1 
ATOM   8314  C  CG  . LYS C  1 124 ? -21.706 39.504  6.738   1.00 32.44  ?  155  LYS C CG  1 
ATOM   8315  C  CD  . LYS C  1 124 ? -20.479 39.621  7.637   1.00 28.44  ?  155  LYS C CD  1 
ATOM   8316  C  CE  . LYS C  1 124 ? -20.880 39.594  9.106   1.00 29.43  ?  155  LYS C CE  1 
ATOM   8317  N  NZ  . LYS C  1 124 ? -19.742 39.137  9.952   1.00 29.19  ?  155  LYS C NZ  1 
ATOM   8318  N  N   . TRP C  1 125 ? -24.606 39.372  5.369   1.00 29.00  ?  156  TRP C N   1 
ATOM   8319  C  CA  . TRP C  1 125 ? -25.884 39.829  5.901   1.00 32.31  ?  156  TRP C CA  1 
ATOM   8320  C  C   . TRP C  1 125 ? -25.866 39.808  7.422   1.00 32.05  ?  156  TRP C C   1 
ATOM   8321  O  O   . TRP C  1 125 ? -25.775 40.867  8.063   1.00 31.94  ?  156  TRP C O   1 
ATOM   8322  C  CB  . TRP C  1 125 ? -27.021 38.956  5.341   1.00 31.45  ?  156  TRP C CB  1 
ATOM   8323  C  CG  . TRP C  1 125 ? -28.434 39.344  5.693   1.00 32.24  ?  156  TRP C CG  1 
ATOM   8324  C  CD1 . TRP C  1 125 ? -29.366 38.572  6.357   1.00 29.11  ?  156  TRP C CD1 1 
ATOM   8325  C  CD2 . TRP C  1 125 ? -29.100 40.573  5.356   1.00 32.37  ?  156  TRP C CD2 1 
ATOM   8326  N  NE1 . TRP C  1 125 ? -30.560 39.265  6.460   1.00 30.05  ?  156  TRP C NE1 1 
ATOM   8327  C  CE2 . TRP C  1 125 ? -30.417 40.488  5.847   1.00 30.84  ?  156  TRP C CE2 1 
ATOM   8328  C  CE3 . TRP C  1 125 ? -28.699 41.744  4.699   1.00 34.69  ?  156  TRP C CE3 1 
ATOM   8329  C  CZ2 . TRP C  1 125 ? -31.332 41.529  5.697   1.00 32.05  ?  156  TRP C CZ2 1 
ATOM   8330  C  CZ3 . TRP C  1 125 ? -29.615 42.764  4.546   1.00 35.78  ?  156  TRP C CZ3 1 
ATOM   8331  C  CH2 . TRP C  1 125 ? -30.912 42.651  5.038   1.00 30.48  ?  156  TRP C CH2 1 
ATOM   8332  N  N   . HIS C  1 126 ? -25.978 38.611  8.009   1.00 31.09  ?  157  HIS C N   1 
ATOM   8333  C  CA  . HIS C  1 126 ? -25.900 38.401  9.456   1.00 25.26  ?  157  HIS C CA  1 
ATOM   8334  C  C   . HIS C  1 126 ? -27.091 39.001  10.204  1.00 29.10  ?  157  HIS C C   1 
ATOM   8335  O  O   . HIS C  1 126 ? -26.995 39.303  11.395  1.00 27.02  ?  157  HIS C O   1 
ATOM   8336  C  CB  . HIS C  1 126 ? -24.577 38.940  10.036  1.00 30.31  ?  157  HIS C CB  1 
ATOM   8337  C  CG  . HIS C  1 126 ? -24.011 38.087  11.125  1.00 30.97  ?  157  HIS C CG  1 
ATOM   8338  N  ND1 . HIS C  1 126 ? -22.895 38.448  11.853  1.00 33.40  ?  157  HIS C ND1 1 
ATOM   8339  C  CD2 . HIS C  1 126 ? -24.411 36.888  11.616  1.00 26.16  ?  157  HIS C CD2 1 
ATOM   8340  C  CE1 . HIS C  1 126 ? -22.640 37.513  12.748  1.00 34.37  ?  157  HIS C CE1 1 
ATOM   8341  N  NE2 . HIS C  1 126 ? -23.542 36.555  12.624  1.00 34.08  ?  157  HIS C NE2 1 
ATOM   8342  N  N   . LEU C  1 127 ? -28.255 39.123  9.549   1.00 27.63  ?  158  LEU C N   1 
ATOM   8343  C  CA  . LEU C  1 127 ? -29.438 39.679  10.203  1.00 32.92  ?  158  LEU C CA  1 
ATOM   8344  C  C   . LEU C  1 127 ? -30.611 38.693  10.255  1.00 31.66  ?  158  LEU C C   1 
ATOM   8345  O  O   . LEU C  1 127 ? -31.750 39.118  10.448  1.00 32.16  ?  158  LEU C O   1 
ATOM   8346  C  CB  . LEU C  1 127 ? -29.871 40.965  9.497   1.00 30.03  ?  158  LEU C CB  1 
ATOM   8347  C  CG  . LEU C  1 127 ? -28.718 41.979  9.426   1.00 34.57  ?  158  LEU C CG  1 
ATOM   8348  C  CD1 . LEU C  1 127 ? -29.115 43.135  8.533   1.00 32.15  ?  158  LEU C CD1 1 
ATOM   8349  C  CD2 . LEU C  1 127 ? -28.300 42.462  10.821  1.00 29.25  ?  158  LEU C CD2 1 
ATOM   8350  N  N   . GLY C  1 128 ? -30.351 37.391  10.116  1.00 32.25  ?  159  GLY C N   1 
ATOM   8351  C  CA  . GLY C  1 128 ? -31.398 36.384  10.087  1.00 29.89  ?  159  GLY C CA  1 
ATOM   8352  C  C   . GLY C  1 128 ? -31.339 35.494  8.856   1.00 30.76  ?  159  GLY C C   1 
ATOM   8353  O  O   . GLY C  1 128 ? -31.281 35.979  7.719   1.00 30.00  ?  159  GLY C O   1 
ATOM   8354  N  N   . ALA C  1 129 ? -31.320 34.180  9.062   1.00 31.16  ?  160  ALA C N   1 
ATOM   8355  C  CA  . ALA C  1 129 ? -31.183 33.254  7.948   1.00 31.17  ?  160  ALA C CA  1 
ATOM   8356  C  C   . ALA C  1 129 ? -32.497 32.547  7.584   1.00 34.07  ?  160  ALA C C   1 
ATOM   8357  O  O   . ALA C  1 129 ? -32.482 31.673  6.717   1.00 39.59  ?  160  ALA C O   1 
ATOM   8358  C  CB  . ALA C  1 129 ? -30.100 32.211  8.241   1.00 33.57  ?  160  ALA C CB  1 
ATOM   8359  N  N   . ALA C  1 130 ? -33.633 32.913  8.215   1.00 33.71  ?  161  ALA C N   1 
ATOM   8360  C  CA  . ALA C  1 130 ? -34.964 32.426  7.850   1.00 32.77  ?  161  ALA C CA  1 
ATOM   8361  C  C   . ALA C  1 130 ? -35.617 33.335  6.809   1.00 35.80  ?  161  ALA C C   1 
ATOM   8362  O  O   . ALA C  1 130 ? -35.286 34.519  6.709   1.00 31.88  ?  161  ALA C O   1 
ATOM   8363  C  CB  . ALA C  1 130 ? -35.840 32.333  9.097   1.00 32.69  ?  161  ALA C CB  1 
ATOM   8364  N  N   . PRO C  1 131 ? -36.565 32.801  6.002   1.00 36.41  ?  162  PRO C N   1 
ATOM   8365  C  CA  . PRO C  1 131 ? -37.146 33.596  4.898   1.00 36.46  ?  162  PRO C CA  1 
ATOM   8366  C  C   . PRO C  1 131 ? -37.642 34.991  5.269   1.00 32.60  ?  162  PRO C C   1 
ATOM   8367  O  O   . PRO C  1 131 ? -37.371 35.935  4.517   1.00 30.16  ?  162  PRO C O   1 
ATOM   8368  C  CB  . PRO C  1 131 ? -38.308 32.708  4.419   1.00 37.59  ?  162  PRO C CB  1 
ATOM   8369  C  CG  . PRO C  1 131 ? -37.828 31.314  4.706   1.00 35.62  ?  162  PRO C CG  1 
ATOM   8370  C  CD  . PRO C  1 131 ? -37.076 31.414  6.004   1.00 37.23  ?  162  PRO C CD  1 
ATOM   8371  N  N   . LYS C  1 132 ? -38.364 35.159  6.381   1.00 31.65  ?  163  LYS C N   1 
ATOM   8372  C  CA  . LYS C  1 132 ? -38.895 36.482  6.717   1.00 35.03  ?  163  LYS C CA  1 
ATOM   8373  C  C   . LYS C  1 132 ? -37.789 37.516  6.943   1.00 36.27  ?  163  LYS C C   1 
ATOM   8374  O  O   . LYS C  1 132 ? -38.049 38.724  6.857   1.00 30.00  ?  163  LYS C O   1 
ATOM   8375  C  CB  . LYS C  1 132 ? -39.787 36.419  7.966   1.00 33.60  ?  163  LYS C CB  1 
ATOM   8376  C  CG  . LYS C  1 132 ? -39.028 36.108  9.251   1.00 41.46  ?  163  LYS C CG  1 
ATOM   8377  C  CD  . LYS C  1 132 ? -39.873 35.488  10.369  1.00 41.98  ?  163  LYS C CD  1 
ATOM   8378  C  CE  . LYS C  1 132 ? -40.591 36.536  11.200  1.00 47.79  ?  163  LYS C CE  1 
ATOM   8379  N  NZ  . LYS C  1 132 ? -41.396 35.904  12.312  1.00 44.43  ?  163  LYS C NZ  1 
ATOM   8380  N  N   . PHE C  1 133 ? -36.564 37.072  7.216   1.00 34.82  ?  164  PHE C N   1 
ATOM   8381  C  CA  . PHE C  1 133 ? -35.448 37.972  7.487   1.00 31.66  ?  164  PHE C CA  1 
ATOM   8382  C  C   . PHE C  1 133 ? -34.598 38.252  6.260   1.00 36.00  ?  164  PHE C C   1 
ATOM   8383  O  O   . PHE C  1 133 ? -33.584 38.960  6.374   1.00 32.13  ?  164  PHE C O   1 
ATOM   8384  C  CB  . PHE C  1 133 ? -34.578 37.371  8.577   1.00 26.86  ?  164  PHE C CB  1 
ATOM   8385  C  CG  . PHE C  1 133 ? -35.308 37.114  9.855   1.00 26.63  ?  164  PHE C CG  1 
ATOM   8386  C  CD1 . PHE C  1 133 ? -35.902 38.157  10.555  1.00 27.85  ?  164  PHE C CD1 1 
ATOM   8387  C  CD2 . PHE C  1 133 ? -35.405 35.831  10.355  1.00 26.16  ?  164  PHE C CD2 1 
ATOM   8388  C  CE1 . PHE C  1 133 ? -36.584 37.928  11.727  1.00 30.02  ?  164  PHE C CE1 1 
ATOM   8389  C  CE2 . PHE C  1 133 ? -36.089 35.580  11.545  1.00 29.90  ?  164  PHE C CE2 1 
ATOM   8390  C  CZ  . PHE C  1 133 ? -36.669 36.637  12.238  1.00 33.26  ?  164  PHE C CZ  1 
ATOM   8391  N  N   . HIS C  1 134 ? -34.988 37.709  5.105   1.00 32.15  ?  165  HIS C N   1 
ATOM   8392  C  CA  . HIS C  1 134 ? -34.168 37.751  3.905   1.00 32.25  ?  165  HIS C CA  1 
ATOM   8393  C  C   . HIS C  1 134 ? -34.067 39.172  3.365   1.00 31.54  ?  165  HIS C C   1 
ATOM   8394  O  O   . HIS C  1 134 ? -35.045 39.917  3.396   1.00 34.64  ?  165  HIS C O   1 
ATOM   8395  C  CB  . HIS C  1 134 ? -34.756 36.831  2.827   1.00 29.92  ?  165  HIS C CB  1 
ATOM   8396  C  CG  . HIS C  1 134 ? -33.850 36.611  1.655   1.00 29.13  ?  165  HIS C CG  1 
ATOM   8397  N  ND1 . HIS C  1 134 ? -33.762 37.501  0.606   1.00 29.82  ?  165  HIS C ND1 1 
ATOM   8398  C  CD2 . HIS C  1 134 ? -33.013 35.592  1.353   1.00 32.83  ?  165  HIS C CD2 1 
ATOM   8399  C  CE1 . HIS C  1 134 ? -32.903 37.044  -0.288  1.00 31.55  ?  165  HIS C CE1 1 
ATOM   8400  N  NE2 . HIS C  1 134 ? -32.438 35.883  0.138   1.00 31.15  ?  165  HIS C NE2 1 
ATOM   8401  N  N   . PRO C  1 135 ? -32.897 39.570  2.849   1.00 31.89  ?  166  PRO C N   1 
ATOM   8402  C  CA  . PRO C  1 135 ? -32.780 40.875  2.173   1.00 28.97  ?  166  PRO C CA  1 
ATOM   8403  C  C   . PRO C  1 135 ? -33.938 41.208  1.218   1.00 34.01  ?  166  PRO C C   1 
ATOM   8404  O  O   . PRO C  1 135 ? -34.438 42.339  1.236   1.00 35.81  ?  166  PRO C O   1 
ATOM   8405  C  CB  . PRO C  1 135 ? -31.462 40.749  1.401   1.00 32.23  ?  166  PRO C CB  1 
ATOM   8406  C  CG  . PRO C  1 135 ? -30.606 39.790  2.265   1.00 34.85  ?  166  PRO C CG  1 
ATOM   8407  C  CD  . PRO C  1 135 ? -31.637 38.794  2.840   1.00 30.83  ?  166  PRO C CD  1 
ATOM   8408  N  N   . ASN C  1 136 ? -34.377 40.250  0.387   1.00 32.57  ?  167  ASN C N   1 
ATOM   8409  C  CA  . ASN C  1 136 ? -35.422 40.548  -0.602  1.00 35.96  ?  167  ASN C CA  1 
ATOM   8410  C  C   . ASN C  1 136 ? -36.748 40.910  0.053   1.00 36.03  ?  167  ASN C C   1 
ATOM   8411  O  O   . ASN C  1 136 ? -37.574 41.603  -0.559  1.00 36.74  ?  167  ASN C O   1 
ATOM   8412  C  CB  . ASN C  1 136 ? -35.644 39.365  -1.549  1.00 32.67  ?  167  ASN C CB  1 
ATOM   8413  C  CG  . ASN C  1 136 ? -34.543 39.214  -2.571  1.00 32.98  ?  167  ASN C CG  1 
ATOM   8414  O  OD1 . ASN C  1 136 ? -34.191 38.100  -2.945  1.00 35.07  ?  167  ASN C OD1 1 
ATOM   8415  N  ND2 . ASN C  1 136 ? -33.991 40.334  -3.031  1.00 36.00  ?  167  ASN C ND2 1 
ATOM   8416  N  N   . LYS C  1 137 ? -36.988 40.426  1.265   1.00 34.38  ?  168  LYS C N   1 
ATOM   8417  C  CA  . LYS C  1 137 ? -38.171 40.795  2.023   1.00 38.05  ?  168  LYS C CA  1 
ATOM   8418  C  C   . LYS C  1 137 ? -37.948 42.038  2.879   1.00 39.37  ?  168  LYS C C   1 
ATOM   8419  O  O   . LYS C  1 137 ? -38.895 42.511  3.520   1.00 35.73  ?  168  LYS C O   1 
ATOM   8420  C  CB  . LYS C  1 137 ? -38.619 39.620  2.907   1.00 38.16  ?  168  LYS C CB  1 
ATOM   8421  N  N   . ARG C  1 138 ? -36.714 42.554  2.882   1.00 36.43  ?  169  ARG C N   1 
ATOM   8422  C  CA  . ARG C  1 138 ? -36.357 43.687  3.777   1.00 35.60  ?  169  ARG C CA  1 
ATOM   8423  C  C   . ARG C  1 138 ? -35.916 44.918  2.971   1.00 38.81  ?  169  ARG C C   1 
ATOM   8424  O  O   . ARG C  1 138 ? -35.062 45.662  3.475   1.00 35.28  ?  169  ARG C O   1 
ATOM   8425  C  CB  . ARG C  1 138 ? -35.303 43.205  4.778   1.00 37.38  ?  169  ARG C CB  1 
ATOM   8426  C  CG  . ARG C  1 138 ? -35.716 42.066  5.697   1.00 39.02  ?  169  ARG C CG  1 
ATOM   8427  C  CD  . ARG C  1 138 ? -36.730 42.511  6.727   1.00 40.38  ?  169  ARG C CD  1 
ATOM   8428  N  NE  . ARG C  1 138 ? -36.142 43.381  7.748   1.00 36.35  ?  169  ARG C NE  1 
ATOM   8429  C  CZ  . ARG C  1 138 ? -36.322 43.234  9.049   1.00 34.12  ?  169  ARG C CZ  1 
ATOM   8430  N  NH1 . ARG C  1 138 ? -35.964 42.112  9.639   1.00 35.38  ?  169  ARG C NH1 1 
ATOM   8431  N  NH2 . ARG C  1 138 ? -36.846 44.216  9.757   1.00 31.79  ?  169  ARG C NH2 1 
ATOM   8432  N  N   . GLY C  1 139 ? -36.435 45.098  1.759   1.00 33.60  ?  170  GLY C N   1 
ATOM   8433  C  CA  . GLY C  1 139 ? -36.212 46.311  0.998   1.00 36.10  ?  170  GLY C CA  1 
ATOM   8434  C  C   . GLY C  1 139 ? -35.142 46.271  -0.069  1.00 36.20  ?  170  GLY C C   1 
ATOM   8435  O  O   . GLY C  1 139 ? -34.883 47.309  -0.690  1.00 36.75  ?  170  GLY C O   1 
ATOM   8436  N  N   . PHE C  1 140 ? -34.526 45.119  -0.328  1.00 32.83  ?  171  PHE C N   1 
ATOM   8437  C  CA  . PHE C  1 140 ? -33.484 45.023  -1.349  1.00 33.83  ?  171  PHE C CA  1 
ATOM   8438  C  C   . PHE C  1 140 ? -34.020 44.359  -2.620  1.00 35.97  ?  171  PHE C C   1 
ATOM   8439  O  O   . PHE C  1 140 ? -34.402 43.188  -2.592  1.00 31.64  ?  171  PHE C O   1 
ATOM   8440  C  CB  . PHE C  1 140 ? -32.283 44.260  -0.800  1.00 34.99  ?  171  PHE C CB  1 
ATOM   8441  C  CG  . PHE C  1 140 ? -31.473 45.065  0.188   1.00 31.29  ?  171  PHE C CG  1 
ATOM   8442  C  CD1 . PHE C  1 140 ? -30.639 46.076  -0.251  1.00 33.53  ?  171  PHE C CD1 1 
ATOM   8443  C  CD2 . PHE C  1 140 ? -31.589 44.840  1.550   1.00 33.48  ?  171  PHE C CD2 1 
ATOM   8444  C  CE1 . PHE C  1 140 ? -29.892 46.848  0.658   1.00 34.11  ?  171  PHE C CE1 1 
ATOM   8445  C  CE2 . PHE C  1 140 ? -30.849 45.592  2.462   1.00 30.83  ?  171  PHE C CE2 1 
ATOM   8446  C  CZ  . PHE C  1 140 ? -29.997 46.602  2.013   1.00 30.64  ?  171  PHE C CZ  1 
ATOM   8447  N  N   . ASP C  1 141 ? -34.014 45.109  -3.734  1.00 35.79  ?  172  ASP C N   1 
ATOM   8448  C  CA  . ASP C  1 141 ? -34.374 44.551  -5.037  1.00 36.77  ?  172  ASP C CA  1 
ATOM   8449  C  C   . ASP C  1 141 ? -33.463 43.391  -5.418  1.00 42.39  ?  172  ASP C C   1 
ATOM   8450  O  O   . ASP C  1 141 ? -33.935 42.363  -5.913  1.00 33.81  ?  172  ASP C O   1 
ATOM   8451  C  CB  . ASP C  1 141 ? -34.288 45.617  -6.126  1.00 36.65  ?  172  ASP C CB  1 
ATOM   8452  C  CG  . ASP C  1 141 ? -35.344 46.707  -5.988  1.00 38.85  ?  172  ASP C CG  1 
ATOM   8453  O  OD1 . ASP C  1 141 ? -36.490 46.420  -5.578  1.00 38.51  ?  172  ASP C OD1 1 
ATOM   8454  O  OD2 . ASP C  1 141 ? -35.014 47.866  -6.316  1.00 38.10  -1 172  ASP C OD2 1 
ATOM   8455  N  N   . ASP C  1 142 ? -32.152 43.548  -5.222  1.00 33.81  ?  173  ASP C N   1 
ATOM   8456  C  CA  . ASP C  1 142 ? -31.170 42.516  -5.521  1.00 38.26  ?  173  ASP C CA  1 
ATOM   8457  C  C   . ASP C  1 142 ? -30.393 42.139  -4.268  1.00 36.68  ?  173  ASP C C   1 
ATOM   8458  O  O   . ASP C  1 142 ? -30.191 42.973  -3.378  1.00 35.76  ?  173  ASP C O   1 
ATOM   8459  C  CB  . ASP C  1 142 ? -30.186 42.976  -6.604  1.00 36.09  ?  173  ASP C CB  1 
ATOM   8460  C  CG  . ASP C  1 142 ? -29.577 41.812  -7.365  1.00 46.62  ?  173  ASP C CG  1 
ATOM   8461  O  OD1 . ASP C  1 142 ? -28.646 41.177  -6.815  1.00 50.21  -1 173  ASP C OD1 1 
ATOM   8462  O  OD2 . ASP C  1 142 ? -30.045 41.496  -8.482  1.00 56.90  ?  173  ASP C OD2 1 
ATOM   8463  N  N   . PHE C  1 143 ? -29.979 40.868  -4.200  1.00 34.94  ?  174  PHE C N   1 
ATOM   8464  C  CA  . PHE C  1 143 ? -29.085 40.391  -3.142  1.00 34.12  ?  174  PHE C CA  1 
ATOM   8465  C  C   . PHE C  1 143 ? -28.145 39.341  -3.709  1.00 37.66  ?  174  PHE C C   1 
ATOM   8466  O  O   . PHE C  1 143 ? -28.598 38.376  -4.336  1.00 33.17  ?  174  PHE C O   1 
ATOM   8467  C  CB  . PHE C  1 143 ? -29.845 39.780  -1.955  1.00 30.86  ?  174  PHE C CB  1 
ATOM   8468  C  CG  . PHE C  1 143 ? -28.928 39.194  -0.903  1.00 34.50  ?  174  PHE C CG  1 
ATOM   8469  C  CD1 . PHE C  1 143 ? -27.918 39.970  -0.353  1.00 31.11  ?  174  PHE C CD1 1 
ATOM   8470  C  CD2 . PHE C  1 143 ? -29.046 37.870  -0.496  1.00 34.17  ?  174  PHE C CD2 1 
ATOM   8471  C  CE1 . PHE C  1 143 ? -27.024 39.439  0.606   1.00 35.63  ?  174  PHE C CE1 1 
ATOM   8472  C  CE2 . PHE C  1 143 ? -28.168 37.335  0.466   1.00 34.12  ?  174  PHE C CE2 1 
ATOM   8473  C  CZ  . PHE C  1 143 ? -27.165 38.127  1.016   1.00 34.52  ?  174  PHE C CZ  1 
ATOM   8474  N  N   . TYR C  1 144 ? -26.845 39.509  -3.462  1.00 30.17  ?  175  TYR C N   1 
ATOM   8475  C  CA  . TYR C  1 144 ? -25.849 38.520  -3.851  1.00 31.16  ?  175  TYR C CA  1 
ATOM   8476  C  C   . TYR C  1 144 ? -24.903 38.345  -2.670  1.00 32.04  ?  175  TYR C C   1 
ATOM   8477  O  O   . TYR C  1 144 ? -24.159 39.275  -2.336  1.00 31.13  ?  175  TYR C O   1 
ATOM   8478  C  CB  . TYR C  1 144 ? -25.090 38.966  -5.094  1.00 31.22  ?  175  TYR C CB  1 
ATOM   8479  C  CG  . TYR C  1 144 ? -24.099 37.957  -5.621  1.00 33.31  ?  175  TYR C CG  1 
ATOM   8480  C  CD1 . TYR C  1 144 ? -22.819 37.830  -5.057  1.00 29.49  ?  175  TYR C CD1 1 
ATOM   8481  C  CD2 . TYR C  1 144 ? -24.434 37.128  -6.687  1.00 33.52  ?  175  TYR C CD2 1 
ATOM   8482  C  CE1 . TYR C  1 144 ? -21.913 36.914  -5.563  1.00 29.58  ?  175  TYR C CE1 1 
ATOM   8483  C  CE2 . TYR C  1 144 ? -23.544 36.203  -7.184  1.00 33.55  ?  175  TYR C CE2 1 
ATOM   8484  C  CZ  . TYR C  1 144 ? -22.282 36.095  -6.618  1.00 31.28  ?  175  TYR C CZ  1 
ATOM   8485  O  OH  . TYR C  1 144 ? -21.401 35.172  -7.133  1.00 32.99  ?  175  TYR C OH  1 
ATOM   8486  N  N   . GLY C  1 145 ? -24.930 37.185  -2.025  1.00 29.09  ?  176  GLY C N   1 
ATOM   8487  C  CA  . GLY C  1 145 ? -23.989 37.005  -0.912  1.00 27.77  ?  176  GLY C CA  1 
ATOM   8488  C  C   . GLY C  1 145 ? -24.422 35.858  -0.016  1.00 26.69  ?  176  GLY C C   1 
ATOM   8489  O  O   . GLY C  1 145 ? -24.959 34.860  -0.487  1.00 34.57  ?  176  GLY C O   1 
ATOM   8490  N  N   . PHE C  1 146 ? -24.138 35.999  1.273   1.00 29.71  ?  177  PHE C N   1 
ATOM   8491  C  CA  . PHE C  1 146 ? -24.426 34.932  2.212   1.00 30.93  ?  177  PHE C CA  1 
ATOM   8492  C  C   . PHE C  1 146 ? -25.154 35.515  3.399   1.00 29.26  ?  177  PHE C C   1 
ATOM   8493  O  O   . PHE C  1 146 ? -24.965 36.681  3.746   1.00 30.16  ?  177  PHE C O   1 
ATOM   8494  C  CB  . PHE C  1 146 ? -23.158 34.193  2.661   1.00 30.41  ?  177  PHE C CB  1 
ATOM   8495  C  CG  . PHE C  1 146 ? -22.105 35.089  3.278   1.00 29.78  ?  177  PHE C CG  1 
ATOM   8496  C  CD1 . PHE C  1 146 ? -22.121 35.356  4.630   1.00 29.40  ?  177  PHE C CD1 1 
ATOM   8497  C  CD2 . PHE C  1 146 ? -21.093 35.639  2.493   1.00 28.43  ?  177  PHE C CD2 1 
ATOM   8498  C  CE1 . PHE C  1 146 ? -21.133 36.174  5.225   1.00 29.60  ?  177  PHE C CE1 1 
ATOM   8499  C  CE2 . PHE C  1 146 ? -20.097 36.456  3.065   1.00 30.21  ?  177  PHE C CE2 1 
ATOM   8500  C  CZ  . PHE C  1 146 ? -20.127 36.724  4.438   1.00 25.65  ?  177  PHE C CZ  1 
ATOM   8501  N  N   . LEU C  1 147 ? -25.992 34.686  4.020   1.00 28.55  ?  178  LEU C N   1 
ATOM   8502  C  CA  . LEU C  1 147 ? -26.889 35.150  5.066   1.00 28.09  ?  178  LEU C CA  1 
ATOM   8503  C  C   . LEU C  1 147 ? -26.263 35.166  6.459   1.00 34.11  ?  178  LEU C C   1 
ATOM   8504  O  O   . LEU C  1 147 ? -26.737 35.926  7.321   1.00 32.50  ?  178  LEU C O   1 
ATOM   8505  C  CB  . LEU C  1 147 ? -28.148 34.275  5.090   1.00 30.29  ?  178  LEU C CB  1 
ATOM   8506  C  CG  . LEU C  1 147 ? -28.981 34.251  3.806   1.00 32.35  ?  178  LEU C CG  1 
ATOM   8507  C  CD1 . LEU C  1 147 ? -30.083 33.180  3.926   1.00 31.62  ?  178  LEU C CD1 1 
ATOM   8508  C  CD2 . LEU C  1 147 ? -29.565 35.636  3.545   1.00 31.56  ?  178  LEU C CD2 1 
ATOM   8509  N  N   . GLY C  1 148 ? -25.219 34.364  6.699   1.00 29.69  ?  179  GLY C N   1 
ATOM   8510  C  CA  . GLY C  1 148 ? -24.621 34.223  8.014   1.00 28.34  ?  179  GLY C CA  1 
ATOM   8511  C  C   . GLY C  1 148 ? -23.507 35.225  8.300   1.00 29.28  ?  179  GLY C C   1 
ATOM   8512  O  O   . GLY C  1 148 ? -23.415 36.295  7.688   1.00 28.77  ?  179  GLY C O   1 
ATOM   8513  N  N   . GLY C  1 149 ? -22.642 34.854  9.254   1.00 28.62  ?  180  GLY C N   1 
ATOM   8514  C  CA  . GLY C  1 149 ? -21.637 35.756  9.789   1.00 32.63  ?  180  GLY C CA  1 
ATOM   8515  C  C   . GLY C  1 149 ? -20.298 35.776  9.081   1.00 34.24  ?  180  GLY C C   1 
ATOM   8516  O  O   . GLY C  1 149 ? -19.467 36.661  9.359   1.00 31.68  ?  180  GLY C O   1 
ATOM   8517  N  N   . GLY C  1 150 ? -20.043 34.822  8.193   1.00 26.99  ?  181  GLY C N   1 
ATOM   8518  C  CA  . GLY C  1 150 ? -18.765 34.821  7.498   1.00 31.64  ?  181  GLY C CA  1 
ATOM   8519  C  C   . GLY C  1 150 ? -18.759 33.756  6.430   1.00 32.87  ?  181  GLY C C   1 
ATOM   8520  O  O   . GLY C  1 150 ? -19.719 32.997  6.279   1.00 32.12  ?  181  GLY C O   1 
ATOM   8521  N  N   . HIS C  1 151 ? -17.662 33.710  5.680   1.00 30.90  ?  182  HIS C N   1 
ATOM   8522  C  CA  . HIS C  1 151 ? -17.575 32.774  4.567   1.00 31.51  ?  182  HIS C CA  1 
ATOM   8523  C  C   . HIS C  1 151 ? -16.127 32.553  4.168   1.00 31.52  ?  182  HIS C C   1 
ATOM   8524  O  O   . HIS C  1 151 ? -15.329 33.492  4.184   1.00 31.33  ?  182  HIS C O   1 
ATOM   8525  C  CB  . HIS C  1 151 ? -18.353 33.271  3.347   1.00 30.16  ?  182  HIS C CB  1 
ATOM   8526  C  CG  . HIS C  1 151 ? -18.835 32.157  2.480   1.00 29.64  ?  182  HIS C CG  1 
ATOM   8527  N  ND1 . HIS C  1 151 ? -18.006 31.492  1.603   1.00 28.71  ?  182  HIS C ND1 1 
ATOM   8528  C  CD2 . HIS C  1 151 ? -20.043 31.544  2.404   1.00 27.93  ?  182  HIS C CD2 1 
ATOM   8529  C  CE1 . HIS C  1 151 ? -18.692 30.530  1.001   1.00 31.40  ?  182  HIS C CE1 1 
ATOM   8530  N  NE2 . HIS C  1 151 ? -19.925 30.533  1.478   1.00 29.72  ?  182  HIS C NE2 1 
ATOM   8531  N  N   . ASP C  1 152 ? -15.803 31.316  3.788   1.00 30.97  ?  183  ASP C N   1 
ATOM   8532  C  CA  . ASP C  1 152 ? -14.515 31.049  3.153   1.00 33.91  ?  183  ASP C CA  1 
ATOM   8533  C  C   . ASP C  1 152 ? -14.430 31.781  1.810   1.00 31.20  ?  183  ASP C C   1 
ATOM   8534  O  O   . ASP C  1 152 ? -15.446 32.036  1.149   1.00 32.36  ?  183  ASP C O   1 
ATOM   8535  C  CB  . ASP C  1 152 ? -14.313 29.540  2.977   1.00 30.29  ?  183  ASP C CB  1 
ATOM   8536  C  CG  . ASP C  1 152 ? -14.005 28.825  4.305   1.00 35.05  ?  183  ASP C CG  1 
ATOM   8537  O  OD1 . ASP C  1 152 ? -14.139 29.447  5.387   1.00 33.68  ?  183  ASP C OD1 1 
ATOM   8538  O  OD2 . ASP C  1 152 ? -13.650 27.626  4.266   1.00 39.41  -1 183  ASP C OD2 1 
ATOM   8539  N  N   . TYR C  1 153 ? -13.205 32.122  1.397   1.00 30.00  ?  184  TYR C N   1 
ATOM   8540  C  CA  . TYR C  1 153 ? -13.019 33.071  0.296   1.00 31.02  ?  184  TYR C CA  1 
ATOM   8541  C  C   . TYR C  1 153 ? -12.768 32.455  -1.078  1.00 31.31  ?  184  TYR C C   1 
ATOM   8542  O  O   . TYR C  1 153 ? -12.853 33.179  -2.072  1.00 35.03  ?  184  TYR C O   1 
ATOM   8543  C  CB  . TYR C  1 153 ? -11.846 34.012  0.576   1.00 28.19  ?  184  TYR C CB  1 
ATOM   8544  C  CG  . TYR C  1 153 ? -12.102 35.059  1.635   1.00 30.86  ?  184  TYR C CG  1 
ATOM   8545  C  CD1 . TYR C  1 153 ? -11.962 34.741  2.992   1.00 30.12  ?  184  TYR C CD1 1 
ATOM   8546  C  CD2 . TYR C  1 153 ? -12.457 36.369  1.294   1.00 28.92  ?  184  TYR C CD2 1 
ATOM   8547  C  CE1 . TYR C  1 153 ? -12.176 35.687  3.977   1.00 30.52  ?  184  TYR C CE1 1 
ATOM   8548  C  CE2 . TYR C  1 153 ? -12.666 37.340  2.294   1.00 27.65  ?  184  TYR C CE2 1 
ATOM   8549  C  CZ  . TYR C  1 153 ? -12.525 36.978  3.629   1.00 31.32  ?  184  TYR C CZ  1 
ATOM   8550  O  OH  . TYR C  1 153 ? -12.730 37.886  4.646   1.00 31.00  ?  184  TYR C OH  1 
ATOM   8551  N  N   . PHE C  1 154 ? -12.419 31.179  -1.184  1.00 31.84  ?  185  PHE C N   1 
ATOM   8552  C  CA  . PHE C  1 154 ? -12.112 30.633  -2.507  1.00 35.26  ?  185  PHE C CA  1 
ATOM   8553  C  C   . PHE C  1 154 ? -13.134 29.583  -2.908  1.00 30.84  ?  185  PHE C C   1 
ATOM   8554  O  O   . PHE C  1 154 ? -13.158 28.486  -2.318  1.00 33.23  ?  185  PHE C O   1 
ATOM   8555  C  CB  . PHE C  1 154 ? -10.702 30.042  -2.546  1.00 34.02  ?  185  PHE C CB  1 
ATOM   8556  C  CG  . PHE C  1 154 ? -9.607  31.083  -2.586  1.00 36.38  ?  185  PHE C CG  1 
ATOM   8557  C  CD1 . PHE C  1 154 ? -9.284  31.734  -3.773  1.00 39.53  ?  185  PHE C CD1 1 
ATOM   8558  C  CD2 . PHE C  1 154 ? -8.896  31.403  -1.430  1.00 35.88  ?  185  PHE C CD2 1 
ATOM   8559  C  CE1 . PHE C  1 154 ? -8.274  32.687  -3.816  1.00 37.37  ?  185  PHE C CE1 1 
ATOM   8560  C  CE2 . PHE C  1 154 ? -7.895  32.354  -1.459  1.00 37.28  ?  185  PHE C CE2 1 
ATOM   8561  C  CZ  . PHE C  1 154 ? -7.572  32.995  -2.654  1.00 36.43  ?  185  PHE C CZ  1 
ATOM   8562  N  N   . PRO C  1 155 ? -13.995 29.870  -3.892  1.00 34.41  ?  186  PRO C N   1 
ATOM   8563  C  CA  . PRO C  1 155 ? -15.022 28.885  -4.266  1.00 30.98  ?  186  PRO C CA  1 
ATOM   8564  C  C   . PRO C  1 155 ? -14.460 27.552  -4.740  1.00 31.27  ?  186  PRO C C   1 
ATOM   8565  O  O   . PRO C  1 155 ? -15.040 26.510  -4.420  1.00 32.98  ?  186  PRO C O   1 
ATOM   8566  C  CB  . PRO C  1 155 ? -15.829 29.616  -5.357  1.00 34.31  ?  186  PRO C CB  1 
ATOM   8567  C  CG  . PRO C  1 155 ? -15.004 30.799  -5.759  1.00 35.69  ?  186  PRO C CG  1 
ATOM   8568  C  CD  . PRO C  1 155 ? -14.232 31.176  -4.534  1.00 34.59  ?  186  PRO C CD  1 
ATOM   8569  N  N   . SER C  1 156 ? -13.335 27.531  -5.458  1.00 33.17  ?  187  SER C N   1 
ATOM   8570  C  CA  . SER C  1 156 ? -12.746 26.234  -5.778  1.00 36.21  ?  187  SER C CA  1 
ATOM   8571  C  C   . SER C  1 156 ? -12.506 25.418  -4.516  1.00 36.50  ?  187  SER C C   1 
ATOM   8572  O  O   . SER C  1 156 ? -12.599 24.189  -4.548  1.00 38.89  ?  187  SER C O   1 
ATOM   8573  C  CB  . SER C  1 156 ? -11.440 26.402  -6.555  1.00 33.77  ?  187  SER C CB  1 
ATOM   8574  O  OG  . SER C  1 156 ? -10.516 27.163  -5.814  1.00 44.53  ?  187  SER C OG  1 
ATOM   8575  N  N   . GLU C  1 157 ? -12.254 26.079  -3.384  1.00 39.29  ?  188  GLU C N   1 
ATOM   8576  C  CA  . GLU C  1 157 ? -12.021 25.345  -2.147  1.00 36.36  ?  188  GLU C CA  1 
ATOM   8577  C  C   . GLU C  1 157 ? -13.331 25.019  -1.430  1.00 36.23  ?  188  GLU C C   1 
ATOM   8578  O  O   . GLU C  1 157 ? -13.601 23.849  -1.124  1.00 33.36  ?  188  GLU C O   1 
ATOM   8579  C  CB  . GLU C  1 157 ? -11.084 26.140  -1.222  1.00 39.56  ?  188  GLU C CB  1 
ATOM   8580  C  CG  . GLU C  1 157 ? -9.602  26.095  -1.644  1.00 38.41  ?  188  GLU C CG  1 
ATOM   8581  C  CD  . GLU C  1 157 ? -8.687  27.021  -0.826  1.00 52.75  ?  188  GLU C CD  1 
ATOM   8582  O  OE1 . GLU C  1 157 ? -9.183  27.781  0.040   1.00 49.32  ?  188  GLU C OE1 1 
ATOM   8583  O  OE2 . GLU C  1 157 ? -7.449  26.948  -1.012  1.00 55.38  -1 188  GLU C OE2 1 
ATOM   8584  N  N   . TYR C  1 158 ? -14.163 26.028  -1.144  1.00 28.65  ?  189  TYR C N   1 
ATOM   8585  C  CA  . TYR C  1 158 ? -15.322 25.739  -0.301  1.00 34.14  ?  189  TYR C CA  1 
ATOM   8586  C  C   . TYR C  1 158 ? -16.387 24.929  -1.038  1.00 32.20  ?  189  TYR C C   1 
ATOM   8587  O  O   . TYR C  1 158 ? -17.041 24.079  -0.413  1.00 33.08  ?  189  TYR C O   1 
ATOM   8588  C  CB  . TYR C  1 158 ? -15.916 27.025  0.312   1.00 32.63  ?  189  TYR C CB  1 
ATOM   8589  C  CG  . TYR C  1 158 ? -16.557 28.050  -0.610  1.00 34.03  ?  189  TYR C CG  1 
ATOM   8590  C  CD1 . TYR C  1 158 ? -17.807 27.819  -1.184  1.00 29.87  ?  189  TYR C CD1 1 
ATOM   8591  C  CD2 . TYR C  1 158 ? -15.947 29.293  -0.841  1.00 28.39  ?  189  TYR C CD2 1 
ATOM   8592  C  CE1 . TYR C  1 158 ? -18.397 28.756  -1.987  1.00 29.84  ?  189  TYR C CE1 1 
ATOM   8593  C  CE2 . TYR C  1 158 ? -16.541 30.248  -1.644  1.00 29.78  ?  189  TYR C CE2 1 
ATOM   8594  C  CZ  . TYR C  1 158 ? -17.770 29.966  -2.224  1.00 32.92  ?  189  TYR C CZ  1 
ATOM   8595  O  OH  . TYR C  1 158 ? -18.400 30.875  -3.053  1.00 33.19  ?  189  TYR C OH  1 
ATOM   8596  N  N   . GLN C  1 159 ? -16.561 25.138  -2.350  1.00 34.13  ?  190  GLN C N   1 
ATOM   8597  C  CA  . GLN C  1 159 ? -17.553 24.342  -3.087  1.00 30.57  ?  190  GLN C CA  1 
ATOM   8598  C  C   . GLN C  1 159 ? -17.174 22.861  -3.106  1.00 34.38  ?  190  GLN C C   1 
ATOM   8599  O  O   . GLN C  1 159 ? -18.050 21.991  -3.040  1.00 30.96  ?  190  GLN C O   1 
ATOM   8600  C  CB  . GLN C  1 159 ? -17.730 24.866  -4.517  1.00 33.75  ?  190  GLN C CB  1 
ATOM   8601  C  CG  . GLN C  1 159 ? -18.434 26.211  -4.599  1.00 33.94  ?  190  GLN C CG  1 
ATOM   8602  C  CD  . GLN C  1 159 ? -18.256 26.913  -5.938  1.00 37.40  ?  190  GLN C CD  1 
ATOM   8603  O  OE1 . GLN C  1 159 ? -17.512 26.445  -6.813  1.00 39.42  ?  190  GLN C OE1 1 
ATOM   8604  N  NE2 . GLN C  1 159 ? -18.930 28.066  -6.100  1.00 34.08  ?  190  GLN C NE2 1 
ATOM   8605  N  N   . LYS C  1 160 ? -15.872 22.553  -3.191  1.00 34.07  ?  191  LYS C N   1 
ATOM   8606  C  CA  . LYS C  1 160 ? -15.458 21.152  -3.165  1.00 36.47  ?  191  LYS C CA  1 
ATOM   8607  C  C   . LYS C  1 160 ? -15.755 20.519  -1.813  1.00 35.92  ?  191  LYS C C   1 
ATOM   8608  O  O   . LYS C  1 160 ? -16.225 19.376  -1.742  1.00 37.33  ?  191  LYS C O   1 
ATOM   8609  C  CB  . LYS C  1 160 ? -13.972 21.019  -3.507  1.00 38.07  ?  191  LYS C CB  1 
ATOM   8610  C  CG  . LYS C  1 160 ? -13.462 19.597  -3.320  1.00 42.07  ?  191  LYS C CG  1 
ATOM   8611  C  CD  . LYS C  1 160 ? -11.945 19.500  -3.429  1.00 48.42  ?  191  LYS C CD  1 
ATOM   8612  C  CE  . LYS C  1 160 ? -11.499 18.082  -3.812  1.00 50.81  ?  191  LYS C CE  1 
ATOM   8613  N  NZ  . LYS C  1 160 ? -10.047 17.847  -3.492  1.00 50.90  ?  191  LYS C NZ  1 
ATOM   8614  N  N   . THR C  1 161 ? -15.515 21.262  -0.731  1.00 35.44  ?  192  THR C N   1 
ATOM   8615  C  CA  . THR C  1 161 ? -15.825 20.764  0.601   1.00 33.23  ?  192  THR C CA  1 
ATOM   8616  C  C   . THR C  1 161 ? -17.321 20.579  0.791   1.00 29.57  ?  192  THR C C   1 
ATOM   8617  O  O   . THR C  1 161 ? -17.769 19.535  1.279   1.00 29.41  ?  192  THR C O   1 
ATOM   8618  C  CB  . THR C  1 161 ? -15.286 21.727  1.645   1.00 32.68  ?  192  THR C CB  1 
ATOM   8619  O  OG1 . THR C  1 161 ? -13.853 21.725  1.578   1.00 33.65  ?  192  THR C OG1 1 
ATOM   8620  C  CG2 . THR C  1 161 ? -15.789 21.323  3.031   1.00 33.40  ?  192  THR C CG2 1 
ATOM   8621  N  N   . TYR C  1 162 ? -18.103 21.603  0.445   1.00 32.14  ?  193  TYR C N   1 
ATOM   8622  C  CA  . TYR C  1 162 ? -19.549 21.520  0.612   1.00 30.99  ?  193  TYR C CA  1 
ATOM   8623  C  C   . TYR C  1 162 ? -20.119 20.294  -0.095  1.00 31.49  ?  193  TYR C C   1 
ATOM   8624  O  O   . TYR C  1 162 ? -20.884 19.513  0.496   1.00 35.54  ?  193  TYR C O   1 
ATOM   8625  C  CB  . TYR C  1 162 ? -20.213 22.793  0.082   1.00 29.63  ?  193  TYR C CB  1 
ATOM   8626  C  CG  . TYR C  1 162 ? -21.725 22.729  0.201   1.00 37.67  ?  193  TYR C CG  1 
ATOM   8627  C  CD1 . TYR C  1 162 ? -22.345 22.909  1.436   1.00 34.77  ?  193  TYR C CD1 1 
ATOM   8628  C  CD2 . TYR C  1 162 ? -22.525 22.445  -0.903  1.00 36.63  ?  193  TYR C CD2 1 
ATOM   8629  C  CE1 . TYR C  1 162 ? -23.710 22.834  1.567   1.00 37.03  ?  193  TYR C CE1 1 
ATOM   8630  C  CE2 . TYR C  1 162 ? -23.914 22.364  -0.781  1.00 34.67  ?  193  TYR C CE2 1 
ATOM   8631  C  CZ  . TYR C  1 162 ? -24.491 22.557  0.456   1.00 36.56  ?  193  TYR C CZ  1 
ATOM   8632  O  OH  . TYR C  1 162 ? -25.842 22.489  0.622   1.00 40.51  ?  193  TYR C OH  1 
ATOM   8633  N  N   . LYS C  1 163 ? -19.777 20.127  -1.376  1.00 34.70  ?  194  LYS C N   1 
ATOM   8634  C  CA  . LYS C  1 163 ? -20.377 19.055  -2.165  1.00 34.69  ?  194  LYS C CA  1 
ATOM   8635  C  C   . LYS C  1 163 ? -20.020 17.696  -1.586  1.00 32.38  ?  194  LYS C C   1 
ATOM   8636  O  O   . LYS C  1 163 ? -20.869 16.797  -1.515  1.00 32.44  ?  194  LYS C O   1 
ATOM   8637  C  CB  . LYS C  1 163 ? -19.926 19.156  -3.624  1.00 39.15  ?  194  LYS C CB  1 
ATOM   8638  N  N   . ALA C  1 164 ? -18.784 17.548  -1.110  1.00 35.11  ?  195  ALA C N   1 
ATOM   8639  C  CA  . ALA C  1 164 ? -18.370 16.264  -0.556  1.00 36.25  ?  195  ALA C CA  1 
ATOM   8640  C  C   . ALA C  1 164 ? -19.077 15.971  0.767   1.00 36.41  ?  195  ALA C C   1 
ATOM   8641  O  O   . ALA C  1 164 ? -19.556 14.852  0.986   1.00 37.11  ?  195  ALA C O   1 
ATOM   8642  C  CB  . ALA C  1 164 ? -16.856 16.234  -0.403  1.00 35.77  ?  195  ALA C CB  1 
ATOM   8643  N  N   . GLN C  1 165 ? -19.186 16.964  1.653   1.00 35.49  ?  196  GLN C N   1 
ATOM   8644  C  CA  . GLN C  1 165 ? -19.870 16.726  2.920   1.00 29.97  ?  196  GLN C CA  1 
ATOM   8645  C  C   . GLN C  1 165 ? -21.361 16.510  2.707   1.00 35.38  ?  196  GLN C C   1 
ATOM   8646  O  O   . GLN C  1 165 ? -21.976 15.659  3.362   1.00 33.36  ?  196  GLN C O   1 
ATOM   8647  C  CB  . GLN C  1 165 ? -19.623 17.896  3.864   1.00 31.13  ?  196  GLN C CB  1 
ATOM   8648  C  CG  . GLN C  1 165 ? -18.168 17.934  4.371   1.00 31.62  ?  196  GLN C CG  1 
ATOM   8649  C  CD  . GLN C  1 165 ? -17.924 19.053  5.327   1.00 41.28  ?  196  GLN C CD  1 
ATOM   8650  O  OE1 . GLN C  1 165 ? -18.335 20.177  5.070   1.00 41.82  ?  196  GLN C OE1 1 
ATOM   8651  N  NE2 . GLN C  1 165 ? -17.161 18.787  6.393   1.00 43.04  ?  196  GLN C NE2 1 
ATOM   8652  N  N   . LYS C  1 166 ? -21.970 17.272  1.801   1.00 32.72  ?  197  LYS C N   1 
ATOM   8653  C  CA  . LYS C  1 166 ? -23.400 17.085  1.586   1.00 33.72  ?  197  LYS C CA  1 
ATOM   8654  C  C   . LYS C  1 166 ? -23.673 15.708  0.987   1.00 40.58  ?  197  LYS C C   1 
ATOM   8655  O  O   . LYS C  1 166 ? -24.651 15.044  1.356   1.00 41.19  ?  197  LYS C O   1 
ATOM   8656  C  CB  . LYS C  1 166 ? -23.946 18.215  0.712   1.00 37.45  ?  197  LYS C CB  1 
ATOM   8657  C  CG  . LYS C  1 166 ? -25.482 18.294  0.618   1.00 45.70  ?  197  LYS C CG  1 
ATOM   8658  C  CD  . LYS C  1 166 ? -25.900 18.768  -0.778  1.00 51.39  ?  197  LYS C CD  1 
ATOM   8659  C  CE  . LYS C  1 166 ? -27.419 18.755  -0.998  1.00 62.64  ?  197  LYS C CE  1 
ATOM   8660  N  NZ  . LYS C  1 166 ? -27.937 17.404  -1.407  1.00 66.61  ?  197  LYS C NZ  1 
ATOM   8661  N  N   . LYS C  1 167 ? -22.787 15.235  0.106   1.00 34.07  ?  198  LYS C N   1 
ATOM   8662  C  CA  . LYS C  1 167 ? -22.967 13.899  -0.454  1.00 43.92  ?  198  LYS C CA  1 
ATOM   8663  C  C   . LYS C  1 167 ? -22.844 12.828  0.629   1.00 43.06  ?  198  LYS C C   1 
ATOM   8664  O  O   . LYS C  1 167 ? -23.637 11.877  0.667   1.00 46.13  ?  198  LYS C O   1 
ATOM   8665  C  CB  . LYS C  1 167 ? -21.960 13.652  -1.579  1.00 42.92  ?  198  LYS C CB  1 
ATOM   8666  N  N   . ALA C  1 168 ? -21.874 12.984  1.537   1.00 42.39  ?  199  ALA C N   1 
ATOM   8667  C  CA  . ALA C  1 168 ? -21.676 12.044  2.634   1.00 41.80  ?  199  ALA C CA  1 
ATOM   8668  C  C   . ALA C  1 168 ? -22.749 12.141  3.719   1.00 38.64  ?  199  ALA C C   1 
ATOM   8669  O  O   . ALA C  1 168 ? -22.751 11.309  4.636   1.00 40.59  ?  199  ALA C O   1 
ATOM   8670  C  CB  . ALA C  1 168 ? -20.292 12.259  3.253   1.00 32.62  ?  199  ALA C CB  1 
ATOM   8671  N  N   . GLY C  1 169 ? -23.645 13.124  3.652   1.00 37.23  ?  200  GLY C N   1 
ATOM   8672  C  CA  . GLY C  1 169 ? -24.676 13.268  4.667   1.00 39.87  ?  200  GLY C CA  1 
ATOM   8673  C  C   . GLY C  1 169 ? -24.191 13.860  5.973   1.00 37.17  ?  200  GLY C C   1 
ATOM   8674  O  O   . GLY C  1 169 ? -24.761 13.570  7.028   1.00 36.26  ?  200  GLY C O   1 
ATOM   8675  N  N   . ASN C  1 170 ? -23.137 14.659  5.933   1.00 39.05  ?  201  ASN C N   1 
ATOM   8676  C  CA  . ASN C  1 170 ? -22.617 15.333  7.120   1.00 36.41  ?  201  ASN C CA  1 
ATOM   8677  C  C   . ASN C  1 170 ? -23.702 16.228  7.707   1.00 41.48  ?  201  ASN C C   1 
ATOM   8678  O  O   . ASN C  1 170 ? -24.215 17.104  6.995   1.00 38.61  ?  201  ASN C O   1 
ATOM   8679  C  CB  . ASN C  1 170 ? -21.396 16.162  6.739   1.00 35.12  ?  201  ASN C CB  1 
ATOM   8680  C  CG  . ASN C  1 170 ? -20.655 16.698  7.941   1.00 38.61  ?  201  ASN C CG  1 
ATOM   8681  O  OD1 . ASN C  1 170 ? -21.255 17.068  8.960   1.00 43.63  ?  201  ASN C OD1 1 
ATOM   8682  N  ND2 . ASN C  1 170 ? -19.336 16.756  7.825   1.00 44.77  ?  201  ASN C ND2 1 
ATOM   8683  N  N   . PRO C  1 171 ? -24.114 16.019  8.956   1.00 41.52  ?  202  PRO C N   1 
ATOM   8684  C  CA  . PRO C  1 171 ? -25.141 16.874  9.566   1.00 46.50  ?  202  PRO C CA  1 
ATOM   8685  C  C   . PRO C  1 171 ? -24.617 18.147  10.217  1.00 46.79  ?  202  PRO C C   1 
ATOM   8686  O  O   . PRO C  1 171 ? -25.401 18.843  10.865  1.00 49.24  ?  202  PRO C O   1 
ATOM   8687  C  CB  . PRO C  1 171 ? -25.736 15.944  10.631  1.00 43.28  ?  202  PRO C CB  1 
ATOM   8688  C  CG  . PRO C  1 171 ? -24.549 15.162  11.098  1.00 41.10  ?  202  PRO C CG  1 
ATOM   8689  C  CD  . PRO C  1 171 ? -23.694 14.935  9.866   1.00 39.87  ?  202  PRO C CD  1 
ATOM   8690  N  N   . ASN C  1 172 ? -23.338 18.474  10.070  1.00 41.65  ?  203  ASN C N   1 
ATOM   8691  C  CA  . ASN C  1 172 ? -22.753 19.592  10.791  1.00 43.61  ?  203  ASN C CA  1 
ATOM   8692  C  C   . ASN C  1 172 ? -21.906 20.447  9.863   1.00 42.17  ?  203  ASN C C   1 
ATOM   8693  O  O   . ASN C  1 172 ? -20.851 20.968  10.254  1.00 44.88  ?  203  ASN C O   1 
ATOM   8694  C  CB  . ASN C  1 172 ? -21.919 19.097  11.973  1.00 45.64  ?  203  ASN C CB  1 
ATOM   8695  C  CG  . ASN C  1 172 ? -22.760 18.439  13.046  1.00 50.86  ?  203  ASN C CG  1 
ATOM   8696  O  OD1 . ASN C  1 172 ? -23.914 18.805  13.262  1.00 60.52  ?  203  ASN C OD1 1 
ATOM   8697  N  ND2 . ASN C  1 172 ? -22.188 17.443  13.716  1.00 58.41  ?  203  ASN C ND2 1 
ATOM   8698  N  N   . ILE C  1 173 ? -22.353 20.604  8.619   1.00 42.00  ?  204  ILE C N   1 
ATOM   8699  C  CA  . ILE C  1 173 ? -21.619 21.400  7.642   1.00 39.79  ?  204  ILE C CA  1 
ATOM   8700  C  C   . ILE C  1 173 ? -21.640 22.866  8.055   1.00 39.02  ?  204  ILE C C   1 
ATOM   8701  O  O   . ILE C  1 173 ? -22.692 23.413  8.414   1.00 37.60  ?  204  ILE C O   1 
ATOM   8702  C  CB  . ILE C  1 173 ? -22.216 21.207  6.240   1.00 32.92  ?  204  ILE C CB  1 
ATOM   8703  C  CG1 . ILE C  1 173 ? -22.081 19.752  5.793   1.00 36.52  ?  204  ILE C CG1 1 
ATOM   8704  C  CG2 . ILE C  1 173 ? -21.571 22.126  5.229   1.00 32.43  ?  204  ILE C CG2 1 
ATOM   8705  C  CD1 . ILE C  1 173 ? -22.799 19.461  4.502   1.00 37.71  ?  204  ILE C CD1 1 
ATOM   8706  N  N   . ARG C  1 174 ? -20.481 23.513  7.993   1.00 35.80  ?  205  ARG C N   1 
ATOM   8707  C  CA  . ARG C  1 174 ? -20.360 24.881  8.478   1.00 39.35  ?  205  ARG C CA  1 
ATOM   8708  C  C   . ARG C  1 174 ? -20.961 25.832  7.460   1.00 32.75  ?  205  ARG C C   1 
ATOM   8709  O  O   . ARG C  1 174 ? -20.754 25.675  6.248   1.00 32.67  ?  205  ARG C O   1 
ATOM   8710  C  CB  . ARG C  1 174 ? -18.892 25.238  8.703   1.00 35.33  ?  205  ARG C CB  1 
ATOM   8711  C  CG  . ARG C  1 174 ? -18.195 24.390  9.726   1.00 45.85  ?  205  ARG C CG  1 
ATOM   8712  C  CD  . ARG C  1 174 ? -16.710 24.668  9.631   1.00 61.22  ?  205  ARG C CD  1 
ATOM   8713  N  NE  . ARG C  1 174 ? -16.414 26.088  9.789   1.00 63.29  ?  205  ARG C NE  1 
ATOM   8714  C  CZ  . ARG C  1 174 ? -15.520 26.750  9.068   1.00 59.02  ?  205  ARG C CZ  1 
ATOM   8715  N  NH1 . ARG C  1 174 ? -14.909 26.183  8.036   1.00 55.35  ?  205  ARG C NH1 1 
ATOM   8716  N  NH2 . ARG C  1 174 ? -15.245 28.019  9.377   1.00 55.01  ?  205  ARG C NH2 1 
ATOM   8717  N  N   . ASP C  1 175 ? -21.683 26.845  7.945   1.00 31.52  ?  206  ASP C N   1 
ATOM   8718  C  CA  . ASP C  1 175 ? -22.255 27.763  6.966   1.00 31.28  ?  206  ASP C CA  1 
ATOM   8719  C  C   . ASP C  1 175 ? -21.180 28.557  6.221   1.00 30.29  ?  206  ASP C C   1 
ATOM   8720  O  O   . ASP C  1 175 ? -21.475 29.145  5.181   1.00 32.66  ?  206  ASP C O   1 
ATOM   8721  C  CB  . ASP C  1 175 ? -23.313 28.693  7.603   1.00 31.71  ?  206  ASP C CB  1 
ATOM   8722  C  CG  . ASP C  1 175 ? -22.833 29.470  8.842   1.00 36.72  ?  206  ASP C CG  1 
ATOM   8723  O  OD1 . ASP C  1 175 ? -21.612 29.541  9.140   1.00 34.09  ?  206  ASP C OD1 1 
ATOM   8724  O  OD2 . ASP C  1 175 ? -23.735 30.035  9.532   1.00 33.71  -1 206  ASP C OD2 1 
ATOM   8725  N  N   . TYR C  1 176 ? -19.930 28.529  6.683   1.00 25.58  ?  207  TYR C N   1 
ATOM   8726  C  CA  . TYR C  1 176 ? -18.858 29.209  5.963   1.00 30.49  ?  207  TYR C CA  1 
ATOM   8727  C  C   . TYR C  1 176 ? -18.557 28.581  4.604   1.00 30.66  ?  207  TYR C C   1 
ATOM   8728  O  O   . TYR C  1 176 ? -17.901 29.218  3.770   1.00 31.06  ?  207  TYR C O   1 
ATOM   8729  C  CB  . TYR C  1 176 ? -17.577 29.203  6.808   1.00 33.75  ?  207  TYR C CB  1 
ATOM   8730  C  CG  . TYR C  1 176 ? -17.437 30.387  7.734   1.00 32.49  ?  207  TYR C CG  1 
ATOM   8731  C  CD1 . TYR C  1 176 ? -18.452 30.731  8.625   1.00 34.88  ?  207  TYR C CD1 1 
ATOM   8732  C  CD2 . TYR C  1 176 ? -16.287 31.167  7.717   1.00 35.38  ?  207  TYR C CD2 1 
ATOM   8733  C  CE1 . TYR C  1 176 ? -18.320 31.823  9.492   1.00 36.25  ?  207  TYR C CE1 1 
ATOM   8734  C  CE2 . TYR C  1 176 ? -16.134 32.255  8.582   1.00 35.20  ?  207  TYR C CE2 1 
ATOM   8735  C  CZ  . TYR C  1 176 ? -17.152 32.581  9.458   1.00 39.19  ?  207  TYR C CZ  1 
ATOM   8736  O  OH  . TYR C  1 176 ? -16.991 33.664  10.296  1.00 36.05  ?  207  TYR C OH  1 
ATOM   8737  N  N   . VAL C  1 177 ? -18.994 27.348  4.353   1.00 27.51  ?  208  VAL C N   1 
ATOM   8738  C  CA  . VAL C  1 177 ? -18.800 26.753  3.037   1.00 29.89  ?  208  VAL C CA  1 
ATOM   8739  C  C   . VAL C  1 177 ? -20.113 26.595  2.264   1.00 32.01  ?  208  VAL C C   1 
ATOM   8740  O  O   . VAL C  1 177 ? -20.085 26.082  1.130   1.00 30.21  ?  208  VAL C O   1 
ATOM   8741  C  CB  . VAL C  1 177 ? -18.042 25.413  3.128   1.00 29.77  ?  208  VAL C CB  1 
ATOM   8742  C  CG1 . VAL C  1 177 ? -16.715 25.599  3.893   1.00 28.87  ?  208  VAL C CG1 1 
ATOM   8743  C  CG2 . VAL C  1 177 ? -18.896 24.295  3.771   1.00 30.91  ?  208  VAL C CG2 1 
ATOM   8744  N  N   . PHE C  1 178 ? -21.255 27.036  2.821   1.00 32.06  ?  209  PHE C N   1 
ATOM   8745  C  CA  . PHE C  1 178 ? -22.524 26.981  2.079   1.00 34.68  ?  209  PHE C CA  1 
ATOM   8746  C  C   . PHE C  1 178 ? -22.394 27.726  0.755   1.00 34.14  ?  209  PHE C C   1 
ATOM   8747  O  O   . PHE C  1 178 ? -21.778 28.797  0.707   1.00 36.16  ?  209  PHE C O   1 
ATOM   8748  C  CB  . PHE C  1 178 ? -23.686 27.626  2.847   1.00 32.58  ?  209  PHE C CB  1 
ATOM   8749  C  CG  . PHE C  1 178 ? -24.200 26.823  4.005   1.00 37.76  ?  209  PHE C CG  1 
ATOM   8750  C  CD1 . PHE C  1 178 ? -23.660 25.584  4.320   1.00 34.51  ?  209  PHE C CD1 1 
ATOM   8751  C  CD2 . PHE C  1 178 ? -25.228 27.333  4.803   1.00 37.39  ?  209  PHE C CD2 1 
ATOM   8752  C  CE1 . PHE C  1 178 ? -24.144 24.857  5.397   1.00 33.32  ?  209  PHE C CE1 1 
ATOM   8753  C  CE2 . PHE C  1 178 ? -25.707 26.622  5.891   1.00 29.49  ?  209  PHE C CE2 1 
ATOM   8754  C  CZ  . PHE C  1 178 ? -25.169 25.373  6.183   1.00 34.58  ?  209  PHE C CZ  1 
ATOM   8755  N  N   . PRO C  1 179 ? -22.991 27.226  -0.323  1.00 33.65  ?  210  PRO C N   1 
ATOM   8756  C  CA  . PRO C  1 179 ? -23.001 28.007  -1.564  1.00 30.90  ?  210  PRO C CA  1 
ATOM   8757  C  C   . PRO C  1 179 ? -23.638 29.369  -1.331  1.00 30.66  ?  210  PRO C C   1 
ATOM   8758  O  O   . PRO C  1 179 ? -24.582 29.513  -0.550  1.00 32.25  ?  210  PRO C O   1 
ATOM   8759  C  CB  . PRO C  1 179 ? -23.822 27.143  -2.526  1.00 33.31  ?  210  PRO C CB  1 
ATOM   8760  C  CG  . PRO C  1 179 ? -24.622 26.244  -1.645  1.00 35.31  ?  210  PRO C CG  1 
ATOM   8761  C  CD  . PRO C  1 179 ? -23.756 25.973  -0.454  1.00 36.41  ?  210  PRO C CD  1 
ATOM   8762  N  N   . MET C  1 180 ? -23.085 30.388  -1.977  1.00 29.11  ?  211  MET C N   1 
ATOM   8763  C  CA  . MET C  1 180 ? -23.689 31.701  -1.839  1.00 26.31  ?  211  MET C CA  1 
ATOM   8764  C  C   . MET C  1 180 ? -24.918 31.764  -2.745  1.00 30.68  ?  211  MET C C   1 
ATOM   8765  O  O   . MET C  1 180 ? -25.224 30.821  -3.487  1.00 31.43  ?  211  MET C O   1 
ATOM   8766  C  CB  . MET C  1 180 ? -22.678 32.802  -2.151  1.00 27.14  ?  211  MET C CB  1 
ATOM   8767  C  CG  . MET C  1 180 ? -21.489 32.865  -1.159  1.00 26.78  ?  211  MET C CG  1 
ATOM   8768  S  SD  . MET C  1 180 ? -20.504 34.359  -1.387  1.00 33.86  ?  211  MET C SD  1 
ATOM   8769  C  CE  . MET C  1 180 ? -20.000 34.294  -3.095  1.00 28.41  ?  211  MET C CE  1 
ATOM   8770  N  N   . GLU C  1 181 ? -25.660 32.863  -2.678  1.00 28.41  ?  212  GLU C N   1 
ATOM   8771  C  CA  . GLU C  1 181 ? -26.943 32.904  -3.381  1.00 30.39  ?  212  GLU C CA  1 
ATOM   8772  C  C   . GLU C  1 181 ? -27.092 34.226  -4.099  1.00 32.99  ?  212  GLU C C   1 
ATOM   8773  O  O   . GLU C  1 181 ? -26.439 35.223  -3.766  1.00 28.00  ?  212  GLU C O   1 
ATOM   8774  C  CB  . GLU C  1 181 ? -28.137 32.731  -2.443  1.00 32.75  ?  212  GLU C CB  1 
ATOM   8775  C  CG  . GLU C  1 181 ? -28.333 33.916  -1.511  1.00 35.85  ?  212  GLU C CG  1 
ATOM   8776  C  CD  . GLU C  1 181 ? -29.717 33.969  -0.917  1.00 36.17  ?  212  GLU C CD  1 
ATOM   8777  O  OE1 . GLU C  1 181 ? -30.596 34.584  -1.561  1.00 32.92  ?  212  GLU C OE1 1 
ATOM   8778  O  OE2 . GLU C  1 181 ? -29.927 33.377  0.174   1.00 35.66  -1 212  GLU C OE2 1 
ATOM   8779  N  N   . HIS C  1 182 ? -27.991 34.219  -5.079  1.00 31.45  ?  213  HIS C N   1 
ATOM   8780  C  CA  . HIS C  1 182 ? -28.393 35.409  -5.812  1.00 34.36  ?  213  HIS C CA  1 
ATOM   8781  C  C   . HIS C  1 182 ? -29.916 35.395  -5.841  1.00 37.51  ?  213  HIS C C   1 
ATOM   8782  O  O   . HIS C  1 182 ? -30.506 34.575  -6.547  1.00 34.26  ?  213  HIS C O   1 
ATOM   8783  C  CB  . HIS C  1 182 ? -27.825 35.408  -7.231  1.00 30.01  ?  213  HIS C CB  1 
ATOM   8784  C  CG  . HIS C  1 182 ? -28.112 36.662  -7.987  1.00 39.87  ?  213  HIS C CG  1 
ATOM   8785  N  ND1 . HIS C  1 182 ? -28.140 36.714  -9.364  1.00 44.79  ?  213  HIS C ND1 1 
ATOM   8786  C  CD2 . HIS C  1 182 ? -28.379 37.918  -7.556  1.00 37.39  ?  213  HIS C CD2 1 
ATOM   8787  C  CE1 . HIS C  1 182 ? -28.416 37.948  -9.750  1.00 46.31  ?  213  HIS C CE1 1 
ATOM   8788  N  NE2 . HIS C  1 182 ? -28.559 38.699  -8.672  1.00 44.24  ?  213  HIS C NE2 1 
ATOM   8789  N  N   . ASN C  1 183 ? -30.538 36.274  -5.054  1.00 35.00  ?  214  ASN C N   1 
ATOM   8790  C  CA  . ASN C  1 183 ? -31.990 36.318  -4.893  1.00 35.88  ?  214  ASN C CA  1 
ATOM   8791  C  C   . ASN C  1 183 ? -32.577 34.922  -4.680  1.00 38.56  ?  214  ASN C C   1 
ATOM   8792  O  O   . ASN C  1 183 ? -33.509 34.509  -5.365  1.00 31.33  ?  214  ASN C O   1 
ATOM   8793  C  CB  . ASN C  1 183 ? -32.651 36.995  -6.098  1.00 34.48  ?  214  ASN C CB  1 
ATOM   8794  C  CG  . ASN C  1 183 ? -32.184 38.413  -6.278  1.00 40.25  ?  214  ASN C CG  1 
ATOM   8795  O  OD1 . ASN C  1 183 ? -32.076 39.171  -5.312  1.00 35.54  ?  214  ASN C OD1 1 
ATOM   8796  N  ND2 . ASN C  1 183 ? -31.880 38.775  -7.512  1.00 41.99  ?  214  ASN C ND2 1 
ATOM   8797  N  N   . GLY C  1 184 ? -32.021 34.185  -3.722  1.00 35.24  ?  215  GLY C N   1 
ATOM   8798  C  CA  . GLY C  1 184 ? -32.527 32.869  -3.389  1.00 32.96  ?  215  GLY C CA  1 
ATOM   8799  C  C   . GLY C  1 184 ? -32.071 31.736  -4.284  1.00 33.81  ?  215  GLY C C   1 
ATOM   8800  O  O   . GLY C  1 184 ? -32.365 30.578  -3.976  1.00 39.64  ?  215  GLY C O   1 
ATOM   8801  N  N   . LYS C  1 185 ? -31.379 32.016  -5.380  1.00 33.48  ?  216  LYS C N   1 
ATOM   8802  C  CA  . LYS C  1 185 ? -30.874 30.980  -6.273  1.00 38.33  ?  216  LYS C CA  1 
ATOM   8803  C  C   . LYS C  1 185 ? -29.370 30.790  -6.086  1.00 38.79  ?  216  LYS C C   1 
ATOM   8804  O  O   . LYS C  1 185 ? -28.695 31.667  -5.542  1.00 37.66  ?  216  LYS C O   1 
ATOM   8805  C  CB  . LYS C  1 185 ? -31.176 31.342  -7.734  1.00 40.04  ?  216  LYS C CB  1 
ATOM   8806  N  N   . PRO C  1 186 ? -28.809 29.655  -6.515  1.00 41.21  ?  217  PRO C N   1 
ATOM   8807  C  CA  . PRO C  1 186 ? -27.355 29.460  -6.388  1.00 37.82  ?  217  PRO C CA  1 
ATOM   8808  C  C   . PRO C  1 186 ? -26.566 30.557  -7.094  1.00 41.03  ?  217  PRO C C   1 
ATOM   8809  O  O   . PRO C  1 186 ? -26.900 30.978  -8.200  1.00 38.23  ?  217  PRO C O   1 
ATOM   8810  C  CB  . PRO C  1 186 ? -27.128 28.095  -7.048  1.00 42.83  ?  217  PRO C CB  1 
ATOM   8811  C  CG  . PRO C  1 186 ? -28.427 27.351  -6.767  1.00 43.26  ?  217  PRO C CG  1 
ATOM   8812  C  CD  . PRO C  1 186 ? -29.496 28.410  -6.922  1.00 40.96  ?  217  PRO C CD  1 
ATOM   8813  N  N   . ALA C  1 187 ? -25.491 31.013  -6.441  1.00 35.45  ?  218  ALA C N   1 
ATOM   8814  C  CA  . ALA C  1 187 ? -24.654 32.058  -7.023  1.00 32.71  ?  218  ALA C CA  1 
ATOM   8815  C  C   . ALA C  1 187 ? -23.676 31.522  -8.063  1.00 36.42  ?  218  ALA C C   1 
ATOM   8816  O  O   . ALA C  1 187 ? -23.346 32.238  -9.013  1.00 33.38  ?  218  ALA C O   1 
ATOM   8817  C  CB  . ALA C  1 187 ? -23.872 32.778  -5.923  1.00 32.98  ?  218  ALA C CB  1 
ATOM   8818  N  N   . ASN C  1 188 ? -23.170 30.303  -7.884  1.00 36.64  ?  219  ASN C N   1 
ATOM   8819  C  CA  . ASN C  1 188 ? -22.157 29.734  -8.780  1.00 37.77  ?  219  ASN C CA  1 
ATOM   8820  C  C   . ASN C  1 188 ? -20.955 30.667  -8.925  1.00 38.20  ?  219  ASN C C   1 
ATOM   8821  O  O   . ASN C  1 188 ? -20.471 30.935  -10.025 1.00 38.32  ?  219  ASN C O   1 
ATOM   8822  C  CB  . ASN C  1 188 ? -22.757 29.404  -10.148 1.00 35.73  ?  219  ASN C CB  1 
ATOM   8823  C  CG  . ASN C  1 188 ? -23.925 28.459  -10.042 1.00 34.32  ?  219  ASN C CG  1 
ATOM   8824  O  OD1 . ASN C  1 188 ? -23.913 27.525  -9.232  1.00 38.57  ?  219  ASN C OD1 1 
ATOM   8825  N  ND2 . ASN C  1 188 ? -24.952 28.698  -10.840 1.00 42.96  ?  219  ASN C ND2 1 
ATOM   8826  N  N   . GLU C  1 189 ? -20.471 31.167  -7.790  1.00 36.06  ?  220  GLU C N   1 
ATOM   8827  C  CA  . GLU C  1 189 ? -19.315 32.059  -7.794  1.00 34.36  ?  220  GLU C CA  1 
ATOM   8828  C  C   . GLU C  1 189 ? -18.111 31.331  -8.373  1.00 33.40  ?  220  GLU C C   1 
ATOM   8829  O  O   . GLU C  1 189 ? -17.930 30.132  -8.152  1.00 33.42  ?  220  GLU C O   1 
ATOM   8830  C  CB  . GLU C  1 189 ? -19.013 32.540  -6.369  1.00 36.30  ?  220  GLU C CB  1 
ATOM   8831  C  CG  . GLU C  1 189 ? -17.830 33.532  -6.221  1.00 31.23  ?  220  GLU C CG  1 
ATOM   8832  C  CD  . GLU C  1 189 ? -17.993 34.733  -7.116  1.00 34.68  ?  220  GLU C CD  1 
ATOM   8833  O  OE1 . GLU C  1 189 ? -18.844 35.595  -6.812  1.00 35.84  ?  220  GLU C OE1 1 
ATOM   8834  O  OE2 . GLU C  1 189 ? -17.296 34.802  -8.148  1.00 37.88  -1 220  GLU C OE2 1 
ATOM   8835  N  N   . THR C  1 190 ? -17.277 32.057  -9.114  1.00 33.92  ?  221  THR C N   1 
ATOM   8836  C  CA  . THR C  1 190 ? -16.041 31.478  -9.624  1.00 37.48  ?  221  THR C CA  1 
ATOM   8837  C  C   . THR C  1 190 ? -14.791 32.233  -9.206  1.00 37.73  ?  221  THR C C   1 
ATOM   8838  O  O   . THR C  1 190 ? -13.692 31.748  -9.469  1.00 37.02  ?  221  THR C O   1 
ATOM   8839  C  CB  . THR C  1 190 ? -16.057 31.409  -11.156 1.00 42.77  ?  221  THR C CB  1 
ATOM   8840  O  OG1 . THR C  1 190 ? -16.290 32.726  -11.671 1.00 40.54  ?  221  THR C OG1 1 
ATOM   8841  C  CG2 . THR C  1 190 ? -17.147 30.451  -11.642 1.00 38.25  ?  221  THR C CG2 1 
ATOM   8842  N  N   . GLU C  1 191 ? -14.918 33.393  -8.580  1.00 36.13  ?  222  GLU C N   1 
ATOM   8843  C  CA  . GLU C  1 191 ? -13.772 34.182  -8.164  1.00 37.11  ?  222  GLU C CA  1 
ATOM   8844  C  C   . GLU C  1 191 ? -13.643 34.200  -6.651  1.00 36.84  ?  222  GLU C C   1 
ATOM   8845  O  O   . GLU C  1 191 ? -14.608 33.961  -5.917  1.00 34.48  ?  222  GLU C O   1 
ATOM   8846  C  CB  . GLU C  1 191 ? -13.884 35.627  -8.661  1.00 35.47  ?  222  GLU C CB  1 
ATOM   8847  C  CG  . GLU C  1 191 ? -14.012 35.771  -10.165 1.00 40.06  ?  222  GLU C CG  1 
ATOM   8848  C  CD  . GLU C  1 191 ? -14.038 37.226  -10.587 1.00 42.98  ?  222  GLU C CD  1 
ATOM   8849  O  OE1 . GLU C  1 191 ? -13.001 37.906  -10.443 1.00 42.98  ?  222  GLU C OE1 1 
ATOM   8850  O  OE2 . GLU C  1 191 ? -15.098 37.702  -11.051 1.00 44.12  -1 222  GLU C OE2 1 
ATOM   8851  N  N   . TYR C  1 192 ? -12.420 34.488  -6.197  1.00 34.42  ?  223  TYR C N   1 
ATOM   8852  C  CA  . TYR C  1 192 ? -12.184 34.994  -4.850  1.00 36.39  ?  223  TYR C CA  1 
ATOM   8853  C  C   . TYR C  1 192 ? -13.301 35.954  -4.477  1.00 33.90  ?  223  TYR C C   1 
ATOM   8854  O  O   . TYR C  1 192 ? -13.501 36.961  -5.157  1.00 36.24  ?  223  TYR C O   1 
ATOM   8855  C  CB  . TYR C  1 192 ? -10.824 35.712  -4.830  1.00 35.24  ?  223  TYR C CB  1 
ATOM   8856  C  CG  . TYR C  1 192 ? -10.336 36.252  -3.506  1.00 37.45  ?  223  TYR C CG  1 
ATOM   8857  C  CD1 . TYR C  1 192 ? -9.881  35.394  -2.512  1.00 34.10  ?  223  TYR C CD1 1 
ATOM   8858  C  CD2 . TYR C  1 192 ? -10.257 37.622  -3.276  1.00 34.39  ?  223  TYR C CD2 1 
ATOM   8859  C  CE1 . TYR C  1 192 ? -9.393  35.882  -1.308  1.00 33.84  ?  223  TYR C CE1 1 
ATOM   8860  C  CE2 . TYR C  1 192 ? -9.769  38.123  -2.069  1.00 35.55  ?  223  TYR C CE2 1 
ATOM   8861  C  CZ  . TYR C  1 192 ? -9.338  37.244  -1.088  1.00 36.79  ?  223  TYR C CZ  1 
ATOM   8862  O  OH  . TYR C  1 192 ? -8.851  37.722  0.117   1.00 34.43  ?  223  TYR C OH  1 
ATOM   8863  N  N   . ILE C  1 193 ? -14.050 35.639  -3.407  1.00 32.64  ?  224  ILE C N   1 
ATOM   8864  C  CA  . ILE C  1 193 ? -15.382 36.242  -3.256  1.00 32.87  ?  224  ILE C CA  1 
ATOM   8865  C  C   . ILE C  1 193 ? -15.316 37.762  -3.135  1.00 32.32  ?  224  ILE C C   1 
ATOM   8866  O  O   . ILE C  1 193 ? -16.258 38.460  -3.536  1.00 31.91  ?  224  ILE C O   1 
ATOM   8867  C  CB  . ILE C  1 193 ? -16.159 35.602  -2.083  1.00 29.84  ?  224  ILE C CB  1 
ATOM   8868  C  CG1 . ILE C  1 193 ? -15.588 36.014  -0.713  1.00 30.32  ?  224  ILE C CG1 1 
ATOM   8869  C  CG2 . ILE C  1 193 ? -16.175 34.087  -2.228  1.00 29.13  ?  224  ILE C CG2 1 
ATOM   8870  C  CD1 . ILE C  1 193 ? -16.397 35.441  0.477   1.00 27.97  ?  224  ILE C CD1 1 
ATOM   8871  N  N   . THR C  1 194 ? -14.210 38.309  -2.627  1.00 32.12  ?  225  THR C N   1 
ATOM   8872  C  CA  . THR C  1 194 ? -14.056 39.765  -2.621  1.00 30.18  ?  225  THR C CA  1 
ATOM   8873  C  C   . THR C  1 194 ? -14.121 40.316  -4.041  1.00 31.64  ?  225  THR C C   1 
ATOM   8874  O  O   . THR C  1 194 ? -14.782 41.329  -4.294  1.00 33.21  ?  225  THR C O   1 
ATOM   8875  C  CB  . THR C  1 194 ? -12.725 40.175  -1.959  1.00 33.80  ?  225  THR C CB  1 
ATOM   8876  O  OG1 . THR C  1 194 ? -12.638 39.643  -0.634  1.00 32.64  ?  225  THR C OG1 1 
ATOM   8877  C  CG2 . THR C  1 194 ? -12.626 41.693  -1.844  1.00 33.10  ?  225  THR C CG2 1 
ATOM   8878  N  N   . ASP C  1 195 ? -13.438 39.660  -4.984  1.00 30.58  ?  226  ASP C N   1 
ATOM   8879  C  CA  . ASP C  1 195 ? -13.527 40.081  -6.379  1.00 32.61  ?  226  ASP C CA  1 
ATOM   8880  C  C   . ASP C  1 195 ? -14.933 39.867  -6.927  1.00 36.27  ?  226  ASP C C   1 
ATOM   8881  O  O   . ASP C  1 195 ? -15.443 40.698  -7.689  1.00 36.19  ?  226  ASP C O   1 
ATOM   8882  C  CB  . ASP C  1 195 ? -12.512 39.316  -7.231  1.00 33.34  ?  226  ASP C CB  1 
ATOM   8883  C  CG  . ASP C  1 195 ? -11.066 39.651  -6.881  1.00 37.69  ?  226  ASP C CG  1 
ATOM   8884  O  OD1 . ASP C  1 195 ? -10.820 40.693  -6.226  1.00 34.37  ?  226  ASP C OD1 1 
ATOM   8885  O  OD2 . ASP C  1 195 ? -10.181 38.856  -7.268  1.00 38.31  -1 226  ASP C OD2 1 
ATOM   8886  N  N   . GLY C  1 196 ? -15.578 38.761  -6.549  1.00 35.65  ?  227  GLY C N   1 
ATOM   8887  C  CA  . GLY C  1 196 ? -16.956 38.545  -6.967  1.00 31.73  ?  227  GLY C CA  1 
ATOM   8888  C  C   . GLY C  1 196 ? -17.911 39.595  -6.427  1.00 34.45  ?  227  GLY C C   1 
ATOM   8889  O  O   . GLY C  1 196 ? -18.829 40.027  -7.129  1.00 35.74  ?  227  GLY C O   1 
ATOM   8890  N  N   . PHE C  1 197 ? -17.734 40.007  -5.162  1.00 32.47  ?  228  PHE C N   1 
ATOM   8891  C  CA  . PHE C  1 197 ? -18.617 41.045  -4.633  1.00 31.63  ?  228  PHE C CA  1 
ATOM   8892  C  C   . PHE C  1 197 ? -18.379 42.362  -5.356  1.00 32.83  ?  228  PHE C C   1 
ATOM   8893  O  O   . PHE C  1 197 ? -19.329 43.094  -5.668  1.00 31.80  ?  228  PHE C O   1 
ATOM   8894  C  CB  . PHE C  1 197 ? -18.422 41.231  -3.125  1.00 32.85  ?  228  PHE C CB  1 
ATOM   8895  C  CG  . PHE C  1 197 ? -18.772 40.025  -2.298  1.00 33.11  ?  228  PHE C CG  1 
ATOM   8896  C  CD1 . PHE C  1 197 ? -19.795 39.170  -2.674  1.00 30.86  ?  228  PHE C CD1 1 
ATOM   8897  C  CD2 . PHE C  1 197 ? -18.064 39.744  -1.131  1.00 33.26  ?  228  PHE C CD2 1 
ATOM   8898  C  CE1 . PHE C  1 197 ? -20.100 38.040  -1.898  1.00 32.41  ?  228  PHE C CE1 1 
ATOM   8899  C  CE2 . PHE C  1 197 ? -18.376 38.614  -0.337  1.00 32.35  ?  228  PHE C CE2 1 
ATOM   8900  C  CZ  . PHE C  1 197 ? -19.379 37.769  -0.731  1.00 33.17  ?  228  PHE C CZ  1 
ATOM   8901  N  N   . SER C  1 198 ? -17.111 42.673  -5.631  1.00 32.23  ?  229  SER C N   1 
ATOM   8902  C  CA  . SER C  1 198 ? -16.777 43.860  -6.407  1.00 30.20  ?  229  SER C CA  1 
ATOM   8903  C  C   . SER C  1 198 ? -17.401 43.786  -7.797  1.00 35.13  ?  229  SER C C   1 
ATOM   8904  O  O   . SER C  1 198 ? -17.954 44.776  -8.293  1.00 31.57  ?  229  SER C O   1 
ATOM   8905  C  CB  . SER C  1 198 ? -15.250 43.999  -6.488  1.00 34.15  ?  229  SER C CB  1 
ATOM   8906  O  OG  . SER C  1 198 ? -14.710 44.308  -5.205  1.00 33.75  ?  229  SER C OG  1 
ATOM   8907  N  N   . ARG C  1 199 ? -17.347 42.606  -8.421  1.00 35.51  ?  230  ARG C N   1 
ATOM   8908  C  CA  . ARG C  1 199 ? -17.931 42.415  -9.745  1.00 38.33  ?  230  ARG C CA  1 
ATOM   8909  C  C   . ARG C  1 199 ? -19.437 42.652  -9.733  1.00 38.29  ?  230  ARG C C   1 
ATOM   8910  O  O   . ARG C  1 199 ? -19.984 43.284  -10.645 1.00 37.14  ?  230  ARG C O   1 
ATOM   8911  C  CB  . ARG C  1 199 ? -17.610 41.005  -10.244 1.00 37.75  ?  230  ARG C CB  1 
ATOM   8912  C  CG  . ARG C  1 199 ? -18.234 40.638  -11.569 1.00 41.18  ?  230  ARG C CG  1 
ATOM   8913  C  CD  . ARG C  1 199 ? -18.298 39.130  -11.719 1.00 44.07  ?  230  ARG C CD  1 
ATOM   8914  N  NE  . ARG C  1 199 ? -19.229 38.524  -10.768 1.00 39.75  ?  230  ARG C NE  1 
ATOM   8915  C  CZ  . ARG C  1 199 ? -18.919 37.496  -9.988  1.00 39.15  ?  230  ARG C CZ  1 
ATOM   8916  N  NH1 . ARG C  1 199 ? -17.728 36.920  -10.043 1.00 35.56  ?  230  ARG C NH1 1 
ATOM   8917  N  NH2 . ARG C  1 199 ? -19.823 37.034  -9.128  1.00 37.63  ?  230  ARG C NH2 1 
ATOM   8918  N  N   . GLU C  1 200 ? -20.123 42.154  -8.704  1.00 35.72  ?  231  GLU C N   1 
ATOM   8919  C  CA  . GLU C  1 200 ? -21.565 42.352  -8.593  1.00 32.06  ?  231  GLU C CA  1 
ATOM   8920  C  C   . GLU C  1 200 ? -21.933 43.801  -8.307  1.00 35.91  ?  231  GLU C C   1 
ATOM   8921  O  O   . GLU C  1 200 ? -23.016 44.257  -8.713  1.00 33.90  ?  231  GLU C O   1 
ATOM   8922  C  CB  . GLU C  1 200 ? -22.118 41.453  -7.489  1.00 34.24  ?  231  GLU C CB  1 
ATOM   8923  C  CG  . GLU C  1 200 ? -22.001 39.967  -7.792  1.00 35.27  ?  231  GLU C CG  1 
ATOM   8924  C  CD  . GLU C  1 200 ? -22.673 39.592  -9.119  1.00 37.23  ?  231  GLU C CD  1 
ATOM   8925  O  OE1 . GLU C  1 200 ? -23.873 39.905  -9.271  1.00 36.08  ?  231  GLU C OE1 1 
ATOM   8926  O  OE2 . GLU C  1 200 ? -22.014 38.982  -9.995  1.00 38.42  -1 231  GLU C OE2 1 
ATOM   8927  N  N   . ALA C  1 201 ? -21.100 44.527  -7.553  1.00 31.22  ?  232  ALA C N   1 
ATOM   8928  C  CA  . ALA C  1 201 ? -21.404 45.935  -7.313  1.00 33.11  ?  232  ALA C CA  1 
ATOM   8929  C  C   . ALA C  1 201 ? -21.319 46.718  -8.610  1.00 36.72  ?  232  ALA C C   1 
ATOM   8930  O  O   . ALA C  1 201 ? -22.141 47.607  -8.874  1.00 36.54  ?  232  ALA C O   1 
ATOM   8931  C  CB  . ALA C  1 201 ? -20.460 46.515  -6.253  1.00 36.57  ?  232  ALA C CB  1 
ATOM   8932  N  N   . ILE C  1 202 ? -20.344 46.369  -9.446  1.00 38.04  ?  233  ILE C N   1 
ATOM   8933  C  CA  . ILE C  1 202 ? -20.224 46.981  -10.763 1.00 36.31  ?  233  ILE C CA  1 
ATOM   8934  C  C   . ILE C  1 202 ? -21.486 46.712  -11.573 1.00 39.89  ?  233  ILE C C   1 
ATOM   8935  O  O   . ILE C  1 202 ? -22.111 47.632  -12.114 1.00 38.32  ?  233  ILE C O   1 
ATOM   8936  C  CB  . ILE C  1 202 ? -18.957 46.453  -11.466 1.00 40.02  ?  233  ILE C CB  1 
ATOM   8937  C  CG1 . ILE C  1 202 ? -17.688 46.974  -10.741 1.00 40.12  ?  233  ILE C CG1 1 
ATOM   8938  C  CG2 . ILE C  1 202 ? -18.940 46.834  -12.932 1.00 37.11  ?  233  ILE C CG2 1 
ATOM   8939  C  CD1 . ILE C  1 202 ? -16.384 46.265  -11.160 1.00 39.18  ?  233  ILE C CD1 1 
ATOM   8940  N  N   . LYS C  1 203 ? -21.909 45.450  -11.619 1.00 36.24  ?  234  LYS C N   1 
ATOM   8941  C  CA  . LYS C  1 203 ? -23.102 45.087  -12.379 1.00 37.61  ?  234  LYS C CA  1 
ATOM   8942  C  C   . LYS C  1 203 ? -24.304 45.915  -11.934 1.00 39.17  ?  234  LYS C C   1 
ATOM   8943  O  O   . LYS C  1 203 ? -25.015 46.507  -12.762 1.00 39.05  ?  234  LYS C O   1 
ATOM   8944  C  CB  . LYS C  1 203 ? -23.375 43.588  -12.218 1.00 34.73  ?  234  LYS C CB  1 
ATOM   8945  C  CG  . LYS C  1 203 ? -24.674 43.086  -12.878 1.00 42.46  ?  234  LYS C CG  1 
ATOM   8946  C  CD  . LYS C  1 203 ? -24.999 41.664  -12.420 1.00 40.81  ?  234  LYS C CD  1 
ATOM   8947  C  CE  . LYS C  1 203 ? -25.630 40.856  -13.551 1.00 48.93  ?  234  LYS C CE  1 
ATOM   8948  N  NZ  . LYS C  1 203 ? -26.748 39.989  -13.069 1.00 49.29  ?  234  LYS C NZ  1 
ATOM   8949  N  N   . ASN C  1 204 ? -24.521 45.999  -10.618 1.00 35.98  ?  235  ASN C N   1 
ATOM   8950  C  CA  . ASN C  1 204 ? -25.676 46.726  -10.101 1.00 38.10  ?  235  ASN C CA  1 
ATOM   8951  C  C   . ASN C  1 204 ? -25.577 48.223  -10.367 1.00 42.95  ?  235  ASN C C   1 
ATOM   8952  O  O   . ASN C  1 204 ? -26.606 48.878  -10.574 1.00 41.29  ?  235  ASN C O   1 
ATOM   8953  C  CB  . ASN C  1 204 ? -25.844 46.432  -8.617  1.00 39.89  ?  235  ASN C CB  1 
ATOM   8954  C  CG  . ASN C  1 204 ? -26.500 45.088  -8.377  1.00 43.60  ?  235  ASN C CG  1 
ATOM   8955  O  OD1 . ASN C  1 204 ? -27.732 44.990  -8.265  1.00 46.25  ?  235  ASN C OD1 1 
ATOM   8956  N  ND2 . ASN C  1 204 ? -25.699 44.036  -8.379  1.00 39.96  ?  235  ASN C ND2 1 
ATOM   8957  N  N   . ILE C  1 205 ? -24.356 48.769  -10.408 1.00 40.43  ?  236  ILE C N   1 
ATOM   8958  C  CA  . ILE C  1 205 ? -24.176 50.161  -10.821 1.00 39.95  ?  236  ILE C CA  1 
ATOM   8959  C  C   . ILE C  1 205 ? -24.600 50.342  -12.278 1.00 42.82  ?  236  ILE C C   1 
ATOM   8960  O  O   . ILE C  1 205 ? -25.265 51.324  -12.633 1.00 39.81  ?  236  ILE C O   1 
ATOM   8961  C  CB  . ILE C  1 205 ? -22.714 50.597  -10.589 1.00 42.01  ?  236  ILE C CB  1 
ATOM   8962  C  CG1 . ILE C  1 205 ? -22.461 50.873  -9.095  1.00 42.68  ?  236  ILE C CG1 1 
ATOM   8963  C  CG2 . ILE C  1 205 ? -22.356 51.824  -11.446 1.00 42.17  ?  236  ILE C CG2 1 
ATOM   8964  C  CD1 . ILE C  1 205 ? -20.975 50.820  -8.686  1.00 37.64  ?  236  ILE C CD1 1 
ATOM   8965  N  N   . LYS C  1 206 ? -24.233 49.394  -13.144 1.00 40.57  ?  237  LYS C N   1 
ATOM   8966  C  CA  . LYS C  1 206 ? -24.594 49.515  -14.550 1.00 41.84  ?  237  LYS C CA  1 
ATOM   8967  C  C   . LYS C  1 206 ? -26.102 49.357  -14.753 1.00 43.79  ?  237  LYS C C   1 
ATOM   8968  O  O   . LYS C  1 206 ? -26.695 50.045  -15.594 1.00 45.25  ?  237  LYS C O   1 
ATOM   8969  C  CB  . LYS C  1 206 ? -23.813 48.492  -15.369 1.00 42.44  ?  237  LYS C CB  1 
ATOM   8970  C  CG  . LYS C  1 206 ? -22.353 48.874  -15.576 1.00 43.15  ?  237  LYS C CG  1 
ATOM   8971  C  CD  . LYS C  1 206 ? -21.576 47.693  -16.121 1.00 44.57  ?  237  LYS C CD  1 
ATOM   8972  C  CE  . LYS C  1 206 ? -20.525 48.139  -17.113 1.00 48.19  ?  237  LYS C CE  1 
ATOM   8973  N  NZ  . LYS C  1 206 ? -19.430 47.139  -17.248 1.00 52.04  ?  237  LYS C NZ  1 
ATOM   8974  N  N   . ILE C  1 207 ? -26.738 48.483  -13.964 1.00 40.69  ?  238  ILE C N   1 
ATOM   8975  C  CA  . ILE C  1 207 ? -28.187 48.293  -14.032 1.00 40.27  ?  238  ILE C CA  1 
ATOM   8976  C  C   . ILE C  1 207 ? -28.920 49.579  -13.658 1.00 43.84  ?  238  ILE C C   1 
ATOM   8977  O  O   . ILE C  1 207 ? -29.865 49.996  -14.341 1.00 40.14  ?  238  ILE C O   1 
ATOM   8978  C  CB  . ILE C  1 207 ? -28.615 47.115  -13.133 1.00 39.20  ?  238  ILE C CB  1 
ATOM   8979  C  CG1 . ILE C  1 207 ? -28.116 45.780  -13.711 1.00 40.96  ?  238  ILE C CG1 1 
ATOM   8980  C  CG2 . ILE C  1 207 ? -30.130 47.090  -12.941 1.00 38.80  ?  238  ILE C CG2 1 
ATOM   8981  C  CD1 . ILE C  1 207 ? -28.147 44.608  -12.699 1.00 39.91  ?  238  ILE C CD1 1 
ATOM   8982  N  N   . ALA C  1 208 ? -28.516 50.220  -12.557 1.00 40.39  ?  239  ALA C N   1 
ATOM   8983  C  CA  . ALA C  1 208 ? -29.168 51.468  -12.165 1.00 39.13  ?  239  ALA C CA  1 
ATOM   8984  C  C   . ALA C  1 208 ? -28.954 52.558  -13.204 1.00 39.92  ?  239  ALA C C   1 
ATOM   8985  O  O   . ALA C  1 208 ? -29.831 53.413  -13.397 1.00 40.55  ?  239  ALA C O   1 
ATOM   8986  C  CB  . ALA C  1 208 ? -28.656 51.940  -10.800 1.00 44.02  ?  239  ALA C CB  1 
ATOM   8987  N  N   . ALA C  1 209 ? -27.803 52.539  -13.884 1.00 38.11  ?  240  ALA C N   1 
ATOM   8988  C  CA  . ALA C  1 209 ? -27.564 53.486  -14.969 1.00 38.56  ?  240  ALA C CA  1 
ATOM   8989  C  C   . ALA C  1 209 ? -28.560 53.276  -16.100 1.00 42.42  ?  240  ALA C C   1 
ATOM   8990  O  O   . ALA C  1 209 ? -29.201 54.228  -16.562 1.00 44.90  ?  240  ALA C O   1 
ATOM   8991  C  CB  . ALA C  1 209 ? -26.138 53.335  -15.494 1.00 40.48  ?  240  ALA C CB  1 
ATOM   8992  N  N   . ALA C  1 210 ? -28.684 52.031  -16.571 1.00 40.34  ?  241  ALA C N   1 
ATOM   8993  C  CA  . ALA C  1 210 ? -29.599 51.732  -17.670 1.00 41.65  ?  241  ALA C CA  1 
ATOM   8994  C  C   . ALA C  1 210 ? -31.042 52.033  -17.285 1.00 40.57  ?  241  ALA C C   1 
ATOM   8995  O  O   . ALA C  1 210 ? -31.835 52.479  -18.126 1.00 43.77  ?  241  ALA C O   1 
ATOM   8996  C  CB  . ALA C  1 210 ? -29.449 50.273  -18.095 1.00 39.23  ?  241  ALA C CB  1 
ATOM   8997  N  N   . LYS C  1 211 ? -31.403 51.809  -16.017 1.00 38.46  ?  242  LYS C N   1 
ATOM   8998  C  CA  . LYS C  1 211 ? -32.746 52.156  -15.566 1.00 42.56  ?  242  LYS C CA  1 
ATOM   8999  C  C   . LYS C  1 211 ? -32.932 53.650  -15.340 1.00 43.01  ?  242  LYS C C   1 
ATOM   9000  O  O   . LYS C  1 211 ? -34.075 54.091  -15.190 1.00 41.09  ?  242  LYS C O   1 
ATOM   9001  C  CB  . LYS C  1 211 ? -33.100 51.395  -14.285 1.00 39.54  ?  242  LYS C CB  1 
ATOM   9002  C  CG  . LYS C  1 211 ? -32.859 49.890  -14.394 1.00 40.02  ?  242  LYS C CG  1 
ATOM   9003  C  CD  . LYS C  1 211 ? -33.424 49.142  -13.219 1.00 40.61  ?  242  LYS C CD  1 
ATOM   9004  C  CE  . LYS C  1 211 ? -34.875 49.538  -12.999 1.00 49.94  ?  242  LYS C CE  1 
ATOM   9005  N  NZ  . LYS C  1 211 ? -35.439 48.965  -11.739 1.00 52.02  ?  242  LYS C NZ  1 
ATOM   9006  N  N   . LYS C  1 212 ? -31.853 54.438  -15.330 1.00 43.11  ?  243  LYS C N   1 
ATOM   9007  C  CA  . LYS C  1 212 ? -31.943 55.864  -15.002 1.00 44.44  ?  243  LYS C CA  1 
ATOM   9008  C  C   . LYS C  1 212 ? -32.654 56.049  -13.668 1.00 46.63  ?  243  LYS C C   1 
ATOM   9009  O  O   . LYS C  1 212 ? -33.560 56.872  -13.519 1.00 42.32  ?  243  LYS C O   1 
ATOM   9010  C  CB  . LYS C  1 212 ? -32.637 56.650  -16.124 1.00 48.98  ?  243  LYS C CB  1 
ATOM   9011  C  CG  . LYS C  1 212 ? -31.680 57.086  -17.229 1.00 47.51  ?  243  LYS C CG  1 
ATOM   9012  C  CD  . LYS C  1 212 ? -31.627 56.111  -18.404 1.00 51.79  ?  243  LYS C CD  1 
ATOM   9013  C  CE  . LYS C  1 212 ? -32.478 56.587  -19.586 1.00 53.90  ?  243  LYS C CE  1 
ATOM   9014  N  NZ  . LYS C  1 212 ? -32.291 55.724  -20.791 1.00 58.19  ?  243  LYS C NZ  1 
ATOM   9015  N  N   . GLN C  1 213 ? -32.229 55.249  -12.685 1.00 43.91  ?  244  GLN C N   1 
ATOM   9016  C  CA  . GLN C  1 213 ? -32.842 55.207  -11.371 1.00 43.00  ?  244  GLN C CA  1 
ATOM   9017  C  C   . GLN C  1 213 ? -31.762 55.398  -10.310 1.00 41.77  ?  244  GLN C C   1 
ATOM   9018  O  O   . GLN C  1 213 ? -30.683 54.789  -10.407 1.00 39.76  ?  244  GLN C O   1 
ATOM   9019  C  CB  . GLN C  1 213 ? -33.569 53.871  -11.179 1.00 40.80  ?  244  GLN C CB  1 
ATOM   9020  C  CG  . GLN C  1 213 ? -34.371 53.746  -9.899  1.00 43.61  ?  244  GLN C CG  1 
ATOM   9021  C  CD  . GLN C  1 213 ? -35.233 52.478  -9.881  1.00 44.59  ?  244  GLN C CD  1 
ATOM   9022  O  OE1 . GLN C  1 213 ? -35.087 51.605  -10.736 1.00 50.52  ?  244  GLN C OE1 1 
ATOM   9023  N  NE2 . GLN C  1 213 ? -36.115 52.370  -8.895  1.00 41.52  ?  244  GLN C NE2 1 
ATOM   9024  N  N   . PRO C  1 214 ? -31.989 56.244  -9.307  1.00 43.58  ?  245  PRO C N   1 
ATOM   9025  C  CA  . PRO C  1 214 ? -30.989 56.387  -8.238  1.00 39.28  ?  245  PRO C CA  1 
ATOM   9026  C  C   . PRO C  1 214 ? -30.847 55.069  -7.487  1.00 43.05  ?  245  PRO C C   1 
ATOM   9027  O  O   . PRO C  1 214 ? -31.822 54.337  -7.298  1.00 43.01  ?  245  PRO C O   1 
ATOM   9028  C  CB  . PRO C  1 214 ? -31.574 57.491  -7.345  1.00 40.98  ?  245  PRO C CB  1 
ATOM   9029  C  CG  . PRO C  1 214 ? -33.057 57.483  -7.653  1.00 47.46  ?  245  PRO C CG  1 
ATOM   9030  C  CD  . PRO C  1 214 ? -33.170 57.103  -9.093  1.00 42.86  ?  245  PRO C CD  1 
ATOM   9031  N  N   . PHE C  1 215 ? -29.624 54.754  -7.062  1.00 40.80  ?  246  PHE C N   1 
ATOM   9032  C  CA  . PHE C  1 215 ? -29.371 53.457  -6.455  1.00 38.09  ?  246  PHE C CA  1 
ATOM   9033  C  C   . PHE C  1 215 ? -28.983 53.600  -4.984  1.00 39.18  ?  246  PHE C C   1 
ATOM   9034  O  O   . PHE C  1 215 ? -28.474 54.642  -4.547  1.00 38.34  ?  246  PHE C O   1 
ATOM   9035  C  CB  . PHE C  1 215 ? -28.296 52.667  -7.262  1.00 36.73  ?  246  PHE C CB  1 
ATOM   9036  C  CG  . PHE C  1 215 ? -26.889 53.244  -7.203  1.00 41.50  ?  246  PHE C CG  1 
ATOM   9037  C  CD1 . PHE C  1 215 ? -26.133 53.192  -6.031  1.00 38.67  ?  246  PHE C CD1 1 
ATOM   9038  C  CD2 . PHE C  1 215 ? -26.295 53.763  -8.346  1.00 42.49  ?  246  PHE C CD2 1 
ATOM   9039  C  CE1 . PHE C  1 215 ? -24.839 53.711  -5.989  1.00 40.26  ?  246  PHE C CE1 1 
ATOM   9040  C  CE2 . PHE C  1 215 ? -24.990 54.263  -8.316  1.00 44.52  ?  246  PHE C CE2 1 
ATOM   9041  C  CZ  . PHE C  1 215 ? -24.261 54.236  -7.135  1.00 36.97  ?  246  PHE C CZ  1 
ATOM   9042  N  N   . PHE C  1 216 ? -29.275 52.549  -4.214  1.00 35.46  ?  247  PHE C N   1 
ATOM   9043  C  CA  . PHE C  1 216 ? -28.719 52.351  -2.880  1.00 34.20  ?  247  PHE C CA  1 
ATOM   9044  C  C   . PHE C  1 216 ? -28.058 50.986  -2.870  1.00 38.59  ?  247  PHE C C   1 
ATOM   9045  O  O   . PHE C  1 216 ? -28.733 49.970  -3.056  1.00 33.85  ?  247  PHE C O   1 
ATOM   9046  C  CB  . PHE C  1 216 ? -29.785 52.450  -1.784  1.00 31.28  ?  247  PHE C CB  1 
ATOM   9047  C  CG  . PHE C  1 216 ? -29.307 52.009  -0.406  1.00 37.28  ?  247  PHE C CG  1 
ATOM   9048  C  CD1 . PHE C  1 216 ? -28.442 52.818  0.339   1.00 39.66  ?  247  PHE C CD1 1 
ATOM   9049  C  CD2 . PHE C  1 216 ? -29.778 50.839  0.178   1.00 29.29  ?  247  PHE C CD2 1 
ATOM   9050  C  CE1 . PHE C  1 216 ? -28.011 52.427  1.621   1.00 36.67  ?  247  PHE C CE1 1 
ATOM   9051  C  CE2 . PHE C  1 216 ? -29.369 50.442  1.449   1.00 34.63  ?  247  PHE C CE2 1 
ATOM   9052  C  CZ  . PHE C  1 216 ? -28.476 51.247  2.177   1.00 37.37  ?  247  PHE C CZ  1 
ATOM   9053  N  N   . ILE C  1 217 ? -26.740 50.957  -2.694  1.00 32.42  ?  248  ILE C N   1 
ATOM   9054  C  CA  . ILE C  1 217 ? -25.999 49.705  -2.725  1.00 30.27  ?  248  ILE C CA  1 
ATOM   9055  C  C   . ILE C  1 217 ? -25.332 49.533  -1.364  1.00 37.07  ?  248  ILE C C   1 
ATOM   9056  O  O   . ILE C  1 217 ? -24.564 50.404  -0.928  1.00 34.58  ?  248  ILE C O   1 
ATOM   9057  C  CB  . ILE C  1 217 ? -24.999 49.671  -3.888  1.00 33.14  ?  248  ILE C CB  1 
ATOM   9058  C  CG1 . ILE C  1 217 ? -25.781 49.667  -5.207  1.00 38.21  ?  248  ILE C CG1 1 
ATOM   9059  C  CG2 . ILE C  1 217 ? -24.082 48.434  -3.803  1.00 33.30  ?  248  ILE C CG2 1 
ATOM   9060  C  CD1 . ILE C  1 217 ? -24.904 49.685  -6.448  1.00 40.31  ?  248  ILE C CD1 1 
ATOM   9061  N  N   . TYR C  1 218 ? -25.715 48.460  -0.658  1.00 31.27  ?  249  TYR C N   1 
ATOM   9062  C  CA  . TYR C  1 218 ? -25.160 48.070  0.641   1.00 31.76  ?  249  TYR C CA  1 
ATOM   9063  C  C   . TYR C  1 218 ? -24.126 46.994  0.353   1.00 33.88  ?  249  TYR C C   1 
ATOM   9064  O  O   . TYR C  1 218 ? -24.454 45.812  0.261   1.00 34.32  ?  249  TYR C O   1 
ATOM   9065  C  CB  . TYR C  1 218 ? -26.262 47.556  1.563   1.00 30.95  ?  249  TYR C CB  1 
ATOM   9066  C  CG  . TYR C  1 218 ? -25.844 47.059  2.950   1.00 34.63  ?  249  TYR C CG  1 
ATOM   9067  C  CD1 . TYR C  1 218 ? -25.507 47.947  3.975   1.00 33.46  ?  249  TYR C CD1 1 
ATOM   9068  C  CD2 . TYR C  1 218 ? -25.824 45.701  3.240   1.00 32.26  ?  249  TYR C CD2 1 
ATOM   9069  C  CE1 . TYR C  1 218 ? -25.173 47.485  5.260   1.00 31.50  ?  249  TYR C CE1 1 
ATOM   9070  C  CE2 . TYR C  1 218 ? -25.487 45.236  4.506   1.00 35.04  ?  249  TYR C CE2 1 
ATOM   9071  C  CZ  . TYR C  1 218 ? -25.160 46.131  5.510   1.00 32.43  ?  249  TYR C CZ  1 
ATOM   9072  O  OH  . TYR C  1 218 ? -24.830 45.655  6.760   1.00 30.90  ?  249  TYR C OH  1 
ATOM   9073  N  N   . LEU C  1 219 ? -22.863 47.405  0.210   1.00 30.53  ?  250  LEU C N   1 
ATOM   9074  C  CA  . LEU C  1 219 ? -21.790 46.504  -0.205  1.00 29.45  ?  250  LEU C CA  1 
ATOM   9075  C  C   . LEU C  1 219 ? -21.007 46.081  1.039   1.00 35.10  ?  250  LEU C C   1 
ATOM   9076  O  O   . LEU C  1 219 ? -20.156 46.824  1.534   1.00 27.90  ?  250  LEU C O   1 
ATOM   9077  C  CB  . LEU C  1 219 ? -20.905 47.188  -1.243  1.00 28.01  ?  250  LEU C CB  1 
ATOM   9078  C  CG  . LEU C  1 219 ? -19.570 46.540  -1.640  1.00 31.58  ?  250  LEU C CG  1 
ATOM   9079  C  CD1 . LEU C  1 219 ? -19.743 45.088  -2.065  1.00 29.41  ?  250  LEU C CD1 1 
ATOM   9080  C  CD2 . LEU C  1 219 ? -18.862 47.365  -2.742  1.00 29.07  ?  250  LEU C CD2 1 
ATOM   9081  N  N   . ALA C  1 220 ? -21.289 44.872  1.528   1.00 31.53  ?  251  ALA C N   1 
ATOM   9082  C  CA  . ALA C  1 220 ? -20.830 44.398  2.831   1.00 32.66  ?  251  ALA C CA  1 
ATOM   9083  C  C   . ALA C  1 220 ? -19.796 43.299  2.610   1.00 31.95  ?  251  ALA C C   1 
ATOM   9084  O  O   . ALA C  1 220 ? -20.079 42.108  2.741   1.00 28.13  ?  251  ALA C O   1 
ATOM   9085  C  CB  . ALA C  1 220 ? -22.018 43.909  3.689   1.00 30.11  ?  251  ALA C CB  1 
ATOM   9086  N  N   . TYR C  1 221 ? -18.581 43.722  2.263   1.00 28.33  ?  252  TYR C N   1 
ATOM   9087  C  CA  . TYR C  1 221 ? -17.440 42.821  2.181   1.00 32.73  ?  252  TYR C CA  1 
ATOM   9088  C  C   . TYR C  1 221 ? -17.261 42.059  3.487   1.00 29.20  ?  252  TYR C C   1 
ATOM   9089  O  O   . TYR C  1 221 ? -17.446 42.609  4.578   1.00 31.36  ?  252  TYR C O   1 
ATOM   9090  C  CB  . TYR C  1 221 ? -16.161 43.612  1.887   1.00 31.28  ?  252  TYR C CB  1 
ATOM   9091  C  CG  . TYR C  1 221 ? -16.057 44.238  0.506   1.00 31.13  ?  252  TYR C CG  1 
ATOM   9092  C  CD1 . TYR C  1 221 ? -15.750 43.460  -0.592  1.00 26.75  ?  252  TYR C CD1 1 
ATOM   9093  C  CD2 . TYR C  1 221 ? -16.181 45.613  0.320   1.00 30.79  ?  252  TYR C CD2 1 
ATOM   9094  C  CE1 . TYR C  1 221 ? -15.614 44.008  -1.857  1.00 31.50  ?  252  TYR C CE1 1 
ATOM   9095  C  CE2 . TYR C  1 221 ? -16.048 46.178  -0.957  1.00 31.68  ?  252  TYR C CE2 1 
ATOM   9096  C  CZ  . TYR C  1 221 ? -15.748 45.365  -2.033  1.00 29.87  ?  252  TYR C CZ  1 
ATOM   9097  O  OH  . TYR C  1 221 ? -15.613 45.867  -3.321  1.00 32.31  ?  252  TYR C OH  1 
ATOM   9098  N  N   . ASN C  1 222 ? -16.889 40.782  3.384   1.00 30.12  ?  253  ASN C N   1 
ATOM   9099  C  CA  . ASN C  1 222 ? -16.516 40.093  4.608   1.00 29.13  ?  253  ASN C CA  1 
ATOM   9100  C  C   . ASN C  1 222 ? -15.049 40.299  4.942   1.00 29.15  ?  253  ASN C C   1 
ATOM   9101  O  O   . ASN C  1 222 ? -14.683 40.158  6.107   1.00 28.71  ?  253  ASN C O   1 
ATOM   9102  C  CB  . ASN C  1 222 ? -16.858 38.590  4.555   1.00 27.02  ?  253  ASN C CB  1 
ATOM   9103  C  CG  . ASN C  1 222 ? -16.129 37.836  3.468   1.00 28.81  ?  253  ASN C CG  1 
ATOM   9104  O  OD1 . ASN C  1 222 ? -16.024 38.291  2.324   1.00 28.99  ?  253  ASN C OD1 1 
ATOM   9105  N  ND2 . ASN C  1 222 ? -15.669 36.632  3.805   1.00 30.79  ?  253  ASN C ND2 1 
ATOM   9106  N  N   . ALA C  1 223 ? -14.232 40.701  3.972   1.00 30.17  ?  254  ALA C N   1 
ATOM   9107  C  CA  . ALA C  1 223 ? -12.847 41.068  4.242   1.00 27.85  ?  254  ALA C CA  1 
ATOM   9108  C  C   . ALA C  1 223 ? -12.783 42.253  5.205   1.00 28.84  ?  254  ALA C C   1 
ATOM   9109  O  O   . ALA C  1 223 ? -13.622 43.155  5.152   1.00 27.39  ?  254  ALA C O   1 
ATOM   9110  C  CB  . ALA C  1 223 ? -12.132 41.422  2.934   1.00 27.10  ?  254  ALA C CB  1 
ATOM   9111  N  N   . PRO C  1 224 ? -11.762 42.304  6.089   1.00 30.40  ?  255  PRO C N   1 
ATOM   9112  C  CA  . PRO C  1 224 ? -10.705 41.320  6.327   1.00 27.29  ?  255  PRO C CA  1 
ATOM   9113  C  C   . PRO C  1 224 ? -11.043 40.356  7.465   1.00 31.78  ?  255  PRO C C   1 
ATOM   9114  O  O   . PRO C  1 224 ? -10.166 39.985  8.246   1.00 28.96  ?  255  PRO C O   1 
ATOM   9115  C  CB  . PRO C  1 224 ? -9.516  42.208  6.703   1.00 33.60  ?  255  PRO C CB  1 
ATOM   9116  C  CG  . PRO C  1 224 ? -10.171 43.297  7.552   1.00 25.50  ?  255  PRO C CG  1 
ATOM   9117  C  CD  . PRO C  1 224 ? -11.508 43.554  6.834   1.00 30.67  ?  255  PRO C CD  1 
ATOM   9118  N  N   . HIS C  1 225 ? -12.309 39.975  7.610   1.00 29.36  ?  256  HIS C N   1 
ATOM   9119  C  CA  . HIS C  1 225 ? -12.716 39.037  8.651   1.00 26.48  ?  256  HIS C CA  1 
ATOM   9120  C  C   . HIS C  1 225 ? -12.119 37.665  8.354   1.00 27.57  ?  256  HIS C C   1 
ATOM   9121  O  O   . HIS C  1 225 ? -11.942 37.285  7.195   1.00 30.12  ?  256  HIS C O   1 
ATOM   9122  C  CB  . HIS C  1 225 ? -14.255 39.001  8.711   1.00 29.40  ?  256  HIS C CB  1 
ATOM   9123  C  CG  . HIS C  1 225 ? -14.844 38.224  9.845   1.00 27.69  ?  256  HIS C CG  1 
ATOM   9124  N  ND1 . HIS C  1 225 ? -14.768 36.848  9.928   1.00 27.85  ?  256  HIS C ND1 1 
ATOM   9125  C  CD2 . HIS C  1 225 ? -15.566 38.629  10.918  1.00 27.78  ?  256  HIS C CD2 1 
ATOM   9126  C  CE1 . HIS C  1 225 ? -15.407 36.442  11.011  1.00 30.33  ?  256  HIS C CE1 1 
ATOM   9127  N  NE2 . HIS C  1 225 ? -15.889 37.504  11.636  1.00 30.72  ?  256  HIS C NE2 1 
ATOM   9128  N  N   . VAL C  1 226 ? -11.796 36.924  9.411   1.00 26.89  ?  257  VAL C N   1 
ATOM   9129  C  CA  . VAL C  1 226 ? -11.285 35.559  9.277   1.00 26.78  ?  257  VAL C CA  1 
ATOM   9130  C  C   . VAL C  1 226 ? -12.263 34.728  8.455   1.00 30.61  ?  257  VAL C C   1 
ATOM   9131  O  O   . VAL C  1 226 ? -13.469 35.025  8.455   1.00 27.45  ?  257  VAL C O   1 
ATOM   9132  C  CB  . VAL C  1 226 ? -11.045 34.919  10.652  1.00 31.38  ?  257  VAL C CB  1 
ATOM   9133  C  CG1 . VAL C  1 226 ? -9.828  35.564  11.305  1.00 31.87  ?  257  VAL C CG1 1 
ATOM   9134  C  CG2 . VAL C  1 226 ? -12.294 35.016  11.523  1.00 33.47  ?  257  VAL C CG2 1 
ATOM   9135  N  N   . PRO C  1 227 ? -11.799 33.668  7.767   1.00 31.01  ?  258  PRO C N   1 
ATOM   9136  C  CA  . PRO C  1 227 ? -10.411 33.144  7.774   1.00 32.10  ?  258  PRO C CA  1 
ATOM   9137  C  C   . PRO C  1 227 ? -9.454  34.024  6.975   1.00 30.72  ?  258  PRO C C   1 
ATOM   9138  O  O   . PRO C  1 227 ? -9.834  34.558  5.928   1.00 30.52  ?  258  PRO C O   1 
ATOM   9139  C  CB  . PRO C  1 227 ? -10.560 31.748  7.145   1.00 33.47  ?  258  PRO C CB  1 
ATOM   9140  C  CG  . PRO C  1 227 ? -11.785 31.868  6.245   1.00 32.69  ?  258  PRO C CG  1 
ATOM   9141  C  CD  . PRO C  1 227 ? -12.704 32.844  6.946   1.00 33.74  ?  258  PRO C CD  1 
ATOM   9142  N  N   . LEU C  1 228 ? -8.214  34.205  7.431   1.00 28.25  ?  259  LEU C N   1 
ATOM   9143  C  CA  . LEU C  1 228 ? -7.229  34.972  6.662   1.00 28.52  ?  259  LEU C CA  1 
ATOM   9144  C  C   . LEU C  1 228 ? -6.908  34.170  5.407   1.00 32.16  ?  259  LEU C C   1 
ATOM   9145  O  O   . LEU C  1 228 ? -6.192  33.170  5.465   1.00 31.38  ?  259  LEU C O   1 
ATOM   9146  C  CB  . LEU C  1 228 ? -5.981  35.242  7.508   1.00 29.28  ?  259  LEU C CB  1 
ATOM   9147  C  CG  . LEU C  1 228 ? -6.249  36.035  8.798   1.00 33.91  ?  259  LEU C CG  1 
ATOM   9148  C  CD1 . LEU C  1 228 ? -4.981  36.483  9.542   1.00 34.46  ?  259  LEU C CD1 1 
ATOM   9149  C  CD2 . LEU C  1 228 ? -7.139  37.234  8.537   1.00 31.58  ?  259  LEU C CD2 1 
ATOM   9150  N  N   . GLN C  1 229 ? -7.511  34.559  4.276   1.00 33.24  ?  260  GLN C N   1 
ATOM   9151  C  CA  . GLN C  1 229 ? -7.341  33.875  2.992   1.00 31.77  ?  260  GLN C CA  1 
ATOM   9152  C  C   . GLN C  1 229 ? -7.205  34.941  1.920   1.00 34.78  ?  260  GLN C C   1 
ATOM   9153  O  O   . GLN C  1 229 ? -8.066  35.817  1.812   1.00 33.66  ?  260  GLN C O   1 
ATOM   9154  C  CB  . GLN C  1 229 ? -8.526  32.945  2.683   1.00 32.57  ?  260  GLN C CB  1 
ATOM   9155  C  CG  . GLN C  1 229 ? -8.599  31.771  3.638   1.00 29.17  ?  260  GLN C CG  1 
ATOM   9156  C  CD  . GLN C  1 229 ? -9.787  30.874  3.434   1.00 34.40  ?  260  GLN C CD  1 
ATOM   9157  O  OE1 . GLN C  1 229 ? -10.721 31.184  2.675   1.00 33.49  ?  260  GLN C OE1 1 
ATOM   9158  N  NE2 . GLN C  1 229 ? -9.767  29.738  4.120   1.00 32.09  ?  260  GLN C NE2 1 
ATOM   9159  N  N   . ALA C  1 230 ? -6.127  34.886  1.140   1.00 35.76  ?  261  ALA C N   1 
ATOM   9160  C  CA  . ALA C  1 230 ? -5.852  35.938  0.172   1.00 36.65  ?  261  ALA C CA  1 
ATOM   9161  C  C   . ALA C  1 230 ? -5.256  35.339  -1.096  1.00 37.59  ?  261  ALA C C   1 
ATOM   9162  O  O   . ALA C  1 230 ? -4.724  34.228  -1.093  1.00 34.31  ?  261  ALA C O   1 
ATOM   9163  C  CB  . ALA C  1 230 ? -4.909  36.999  0.760   1.00 34.12  ?  261  ALA C CB  1 
ATOM   9164  N  N   . LYS C  1 231 ? -5.347  36.094  -2.189  1.00 37.59  ?  262  LYS C N   1 
ATOM   9165  C  CA  . LYS C  1 231 ? -4.812  35.638  -3.470  1.00 42.21  ?  262  LYS C CA  1 
ATOM   9166  C  C   . LYS C  1 231 ? -3.301  35.822  -3.539  1.00 39.78  ?  262  LYS C C   1 
ATOM   9167  O  O   . LYS C  1 231 ? -2.753  36.809  -3.036  1.00 36.05  ?  262  LYS C O   1 
ATOM   9168  C  CB  . LYS C  1 231 ? -5.466  36.386  -4.633  1.00 39.91  ?  262  LYS C CB  1 
ATOM   9169  C  CG  . LYS C  1 231 ? -6.983  36.409  -4.583  1.00 38.45  ?  262  LYS C CG  1 
ATOM   9170  C  CD  . LYS C  1 231 ? -7.527  37.433  -5.568  1.00 43.69  ?  262  LYS C CD  1 
ATOM   9171  C  CE  . LYS C  1 231 ? -7.100  37.116  -6.991  1.00 39.89  ?  262  LYS C CE  1 
ATOM   9172  N  NZ  . LYS C  1 231 ? -7.412  38.287  -7.861  1.00 41.68  ?  262  LYS C NZ  1 
ATOM   9173  N  N   . ALA C  1 232 ? -2.634  34.869  -4.195  1.00 41.57  ?  263  ALA C N   1 
ATOM   9174  C  CA  . ALA C  1 232 ? -1.179  34.930  -4.312  1.00 46.06  ?  263  ALA C CA  1 
ATOM   9175  C  C   . ALA C  1 232 ? -0.740  36.278  -4.850  1.00 43.16  ?  263  ALA C C   1 
ATOM   9176  O  O   . ALA C  1 232 ? 0.236   36.864  -4.366  1.00 43.20  ?  263  ALA C O   1 
ATOM   9177  C  CB  . ALA C  1 232 ? -0.671  33.808  -5.216  1.00 43.29  ?  263  ALA C CB  1 
ATOM   9178  N  N   . GLU C  1 233 ? -1.494  36.810  -5.813  1.00 41.52  ?  264  GLU C N   1 
ATOM   9179  C  CA  . GLU C  1 233 ? -1.092  38.034  -6.492  1.00 43.97  ?  264  GLU C CA  1 
ATOM   9180  C  C   . GLU C  1 233 ? -1.145  39.213  -5.541  1.00 44.66  ?  264  GLU C C   1 
ATOM   9181  O  O   . GLU C  1 233 ? -0.284  40.103  -5.595  1.00 50.19  ?  264  GLU C O   1 
ATOM   9182  C  CB  . GLU C  1 233 ? -1.999  38.280  -7.698  1.00 48.67  ?  264  GLU C CB  1 
ATOM   9183  C  CG  . GLU C  1 233 ? -2.025  37.094  -8.635  1.00 54.57  ?  264  GLU C CG  1 
ATOM   9184  C  CD  . GLU C  1 233 ? -3.322  36.289  -8.492  1.00 58.59  ?  264  GLU C CD  1 
ATOM   9185  O  OE1 . GLU C  1 233 ? -4.312  36.659  -9.168  1.00 64.11  ?  264  GLU C OE1 1 
ATOM   9186  O  OE2 . GLU C  1 233 ? -3.373  35.331  -7.669  1.00 46.28  ?  264  GLU C OE2 1 
ATOM   9187  N  N   . ASP C  1 234 ? -2.143  39.228  -4.651  1.00 38.20  ?  265  ASP C N   1 
ATOM   9188  C  CA  . ASP C  1 234 ? -2.239  40.301  -3.667  1.00 37.57  ?  265  ASP C CA  1 
ATOM   9189  C  C   . ASP C  1 234 ? -1.176  40.144  -2.577  1.00 38.11  ?  265  ASP C C   1 
ATOM   9190  O  O   . ASP C  1 234 ? -0.637  41.137  -2.079  1.00 41.27  ?  265  ASP C O   1 
ATOM   9191  C  CB  . ASP C  1 234 ? -3.641  40.312  -3.058  1.00 39.05  ?  265  ASP C CB  1 
ATOM   9192  C  CG  . ASP C  1 234 ? -4.721  40.677  -4.072  1.00 43.33  ?  265  ASP C CG  1 
ATOM   9193  O  OD1 . ASP C  1 234 ? -4.416  41.400  -5.050  1.00 46.19  ?  265  ASP C OD1 1 
ATOM   9194  O  OD2 . ASP C  1 234 ? -5.873  40.216  -3.898  1.00 41.67  -1 265  ASP C OD2 1 
ATOM   9195  N  N   . VAL C  1 235 ? -0.867  38.904  -2.188  1.00 39.77  ?  266  VAL C N   1 
ATOM   9196  C  CA  . VAL C  1 235 ? 0.140   38.689  -1.148  1.00 42.99  ?  266  VAL C CA  1 
ATOM   9197  C  C   . VAL C  1 235 ? 1.522   39.099  -1.648  1.00 44.69  ?  266  VAL C C   1 
ATOM   9198  O  O   . VAL C  1 235 ? 2.352   39.579  -0.867  1.00 45.44  ?  266  VAL C O   1 
ATOM   9199  C  CB  . VAL C  1 235 ? 0.118   37.220  -0.675  1.00 42.18  ?  266  VAL C CB  1 
ATOM   9200  C  CG1 . VAL C  1 235 ? 1.366   36.883  0.166   1.00 45.52  ?  266  VAL C CG1 1 
ATOM   9201  C  CG2 . VAL C  1 235 ? -1.160  36.914  0.115   1.00 37.98  ?  266  VAL C CG2 1 
ATOM   9202  N  N   . ALA C  1 236 ? 1.784   38.928  -2.952  1.00 43.80  ?  267  ALA C N   1 
ATOM   9203  C  CA  . ALA C  1 236 ? 3.057   39.341  -3.544  1.00 46.59  ?  267  ALA C CA  1 
ATOM   9204  C  C   . ALA C  1 236 ? 3.334   40.827  -3.346  1.00 46.92  ?  267  ALA C C   1 
ATOM   9205  O  O   . ALA C  1 236 ? 4.496   41.225  -3.174  1.00 44.79  ?  267  ALA C O   1 
ATOM   9206  C  CB  . ALA C  1 236 ? 3.078   39.007  -5.035  1.00 47.46  ?  267  ALA C CB  1 
ATOM   9207  N  N   . LYS C  1 237 ? 2.294   41.660  -3.354  1.00 43.69  ?  268  LYS C N   1 
ATOM   9208  C  CA  . LYS C  1 237 ? 2.468   43.093  -3.133  1.00 44.30  ?  268  LYS C CA  1 
ATOM   9209  C  C   . LYS C  1 237 ? 2.857   43.436  -1.699  1.00 44.79  ?  268  LYS C C   1 
ATOM   9210  O  O   . LYS C  1 237 ? 3.099   44.616  -1.411  1.00 46.30  ?  268  LYS C O   1 
ATOM   9211  C  CB  . LYS C  1 237 ? 1.180   43.836  -3.508  1.00 46.03  ?  268  LYS C CB  1 
ATOM   9212  N  N   . PHE C  1 238 ? 2.900   42.457  -0.789  1.00 41.98  ?  269  PHE C N   1 
ATOM   9213  C  CA  . PHE C  1 238 ? 3.207   42.729  0.611   1.00 47.43  ?  269  PHE C CA  1 
ATOM   9214  C  C   . PHE C  1 238 ? 4.306   41.815  1.135   1.00 46.06  ?  269  PHE C C   1 
ATOM   9215  O  O   . PHE C  1 238 ? 4.315   41.450  2.316   1.00 43.23  ?  269  PHE C O   1 
ATOM   9216  C  CB  . PHE C  1 238 ? 1.943   42.621  1.462   1.00 43.45  ?  269  PHE C CB  1 
ATOM   9217  C  CG  . PHE C  1 238 ? 0.945   43.703  1.165   1.00 40.26  ?  269  PHE C CG  1 
ATOM   9218  C  CD1 . PHE C  1 238 ? 1.087   44.963  1.727   1.00 40.83  ?  269  PHE C CD1 1 
ATOM   9219  C  CD2 . PHE C  1 238 ? -0.090  43.478  0.276   1.00 36.47  ?  269  PHE C CD2 1 
ATOM   9220  C  CE1 . PHE C  1 238 ? 0.191   45.976  1.446   1.00 39.73  ?  269  PHE C CE1 1 
ATOM   9221  C  CE2 . PHE C  1 238 ? -0.996  44.482  -0.016  1.00 38.92  ?  269  PHE C CE2 1 
ATOM   9222  C  CZ  . PHE C  1 238 ? -0.861  45.735  0.567   1.00 39.22  ?  269  PHE C CZ  1 
ATOM   9223  N  N   . ALA C  1 239 ? 5.248   41.441  0.269   1.00 50.09  ?  270  ALA C N   1 
ATOM   9224  C  CA  . ALA C  1 239 ? 6.435   40.729  0.734   1.00 52.20  ?  270  ALA C CA  1 
ATOM   9225  C  C   . ALA C  1 239 ? 7.173   41.507  1.817   1.00 49.28  ?  270  ALA C C   1 
ATOM   9226  O  O   . ALA C  1 239 ? 7.851   40.907  2.654   1.00 54.66  ?  270  ALA C O   1 
ATOM   9227  C  CB  . ALA C  1 239 ? 7.365   40.441  -0.443  1.00 55.17  ?  270  ALA C CB  1 
ATOM   9228  N  N   . HIS C  1 240 ? 7.051   42.834  1.832   1.00 54.40  ?  271  HIS C N   1 
ATOM   9229  C  CA  . HIS C  1 240 ? 7.712   43.648  2.850   1.00 52.98  ?  271  HIS C CA  1 
ATOM   9230  C  C   . HIS C  1 240 ? 7.070   43.535  4.234   1.00 58.02  ?  271  HIS C C   1 
ATOM   9231  O  O   . HIS C  1 240 ? 7.494   44.305  5.123   1.00 56.38  ?  271  HIS C O   1 
ATOM   9232  C  CB  . HIS C  1 240 ? 7.717   45.113  2.424   1.00 56.44  ?  271  HIS C CB  1 
ATOM   9233  C  CG  . HIS C  1 240 ? 6.363   45.748  2.451   1.00 54.41  ?  271  HIS C CG  1 
ATOM   9234  N  ND1 . HIS C  1 240 ? 5.463   45.614  1.419   1.00 53.20  ?  271  HIS C ND1 1 
ATOM   9235  C  CD2 . HIS C  1 240 ? 5.756   46.520  3.385   1.00 56.30  ?  271  HIS C CD2 1 
ATOM   9236  C  CE1 . HIS C  1 240 ? 4.356   46.276  1.712   1.00 55.74  ?  271  HIS C CE1 1 
ATOM   9237  N  NE2 . HIS C  1 240 ? 4.508   46.836  2.901   1.00 57.74  ?  271  HIS C NE2 1 
ATOM   9238  N  N   . ILE C  1 241 ? 6.089   42.655  4.441   1.00 50.19  ?  272  ILE C N   1 
ATOM   9239  C  CA  . ILE C  1 241 ? 5.490   42.412  5.753   1.00 46.06  ?  272  ILE C CA  1 
ATOM   9240  C  C   . ILE C  1 241 ? 5.925   41.026  6.203   1.00 46.73  ?  272  ILE C C   1 
ATOM   9241  O  O   . ILE C  1 241 ? 5.607   40.025  5.548   1.00 49.05  ?  272  ILE C O   1 
ATOM   9242  C  CB  . ILE C  1 241 ? 3.959   42.526  5.710   1.00 46.69  ?  272  ILE C CB  1 
ATOM   9243  C  CG1 . ILE C  1 241 ? 3.550   43.892  5.147   1.00 47.20  ?  272  ILE C CG1 1 
ATOM   9244  C  CG2 . ILE C  1 241 ? 3.365   42.269  7.108   1.00 40.58  ?  272  ILE C CG2 1 
ATOM   9245  C  CD1 . ILE C  1 241 ? 2.083   44.236  5.339   1.00 42.55  ?  272  ILE C CD1 1 
ATOM   9246  N  N   . LYS C  1 242 ? 6.664   40.960  7.315   1.00 41.31  ?  273  LYS C N   1 
ATOM   9247  C  CA  . LYS C  1 242 ? 7.271   39.687  7.687   1.00 43.06  ?  273  LYS C CA  1 
ATOM   9248  C  C   . LYS C  1 242 ? 6.288   38.786  8.429   1.00 42.53  ?  273  LYS C C   1 
ATOM   9249  O  O   . LYS C  1 242 ? 6.323   37.563  8.258   1.00 46.75  ?  273  LYS C O   1 
ATOM   9250  C  CB  . LYS C  1 242 ? 8.532   39.923  8.528   1.00 51.71  ?  273  LYS C CB  1 
ATOM   9251  N  N   . ASP C  1 243 ? 5.400   39.358  9.239   1.00 37.72  ?  274  ASP C N   1 
ATOM   9252  C  CA  . ASP C  1 243 ? 4.430   38.534  9.946   1.00 41.19  ?  274  ASP C CA  1 
ATOM   9253  C  C   . ASP C  1 243 ? 3.416   37.969  8.951   1.00 41.96  ?  274  ASP C C   1 
ATOM   9254  O  O   . ASP C  1 243 ? 2.790   38.723  8.195   1.00 39.20  ?  274  ASP C O   1 
ATOM   9255  C  CB  . ASP C  1 243 ? 3.724   39.351  11.027  1.00 37.10  ?  274  ASP C CB  1 
ATOM   9256  C  CG  . ASP C  1 243 ? 2.684   38.539  11.779  1.00 47.96  ?  274  ASP C CG  1 
ATOM   9257  O  OD1 . ASP C  1 243 ? 3.088   37.576  12.468  1.00 48.73  ?  274  ASP C OD1 1 
ATOM   9258  O  OD2 . ASP C  1 243 ? 1.469   38.830  11.659  1.00 43.80  -1 274  ASP C OD2 1 
ATOM   9259  N  N   . LYS C  1 244 ? 3.256   36.636  8.954   1.00 40.80  ?  275  LYS C N   1 
ATOM   9260  C  CA  . LYS C  1 244 ? 2.411   35.976  7.955   1.00 41.73  ?  275  LYS C CA  1 
ATOM   9261  C  C   . LYS C  1 244 ? 0.955   36.413  8.055   1.00 39.86  ?  275  LYS C C   1 
ATOM   9262  O  O   . LYS C  1 244 ? 0.292   36.619  7.028   1.00 35.28  ?  275  LYS C O   1 
ATOM   9263  C  CB  . LYS C  1 244 ? 2.494   34.458  8.095   1.00 45.00  ?  275  LYS C CB  1 
ATOM   9264  C  CG  . LYS C  1 244 ? 1.685   33.717  7.022   1.00 48.94  ?  275  LYS C CG  1 
ATOM   9265  C  CD  . LYS C  1 244 ? 2.028   32.237  6.960   1.00 53.11  ?  275  LYS C CD  1 
ATOM   9266  C  CE  . LYS C  1 244 ? 0.889   31.379  7.495   1.00 61.39  ?  275  LYS C CE  1 
ATOM   9267  N  NZ  . LYS C  1 244 ? 1.369   30.267  8.378   1.00 70.66  ?  275  LYS C NZ  1 
ATOM   9268  N  N   . ASP C  1 245 ? 0.424   36.510  9.276   1.00 38.52  ?  276  ASP C N   1 
ATOM   9269  C  CA  . ASP C  1 245 ? -0.956  36.956  9.454   1.00 42.60  ?  276  ASP C CA  1 
ATOM   9270  C  C   . ASP C  1 245 ? -1.144  38.382  8.955   1.00 38.03  ?  276  ASP C C   1 
ATOM   9271  O  O   . ASP C  1 245 ? -2.085  38.668  8.207   1.00 35.04  ?  276  ASP C O   1 
ATOM   9272  C  CB  . ASP C  1 245 ? -1.361  36.863  10.922  1.00 37.70  ?  276  ASP C CB  1 
ATOM   9273  C  CG  . ASP C  1 245 ? -1.829  35.482  11.313  1.00 45.05  ?  276  ASP C CG  1 
ATOM   9274  O  OD1 . ASP C  1 245 ? -1.867  34.585  10.434  1.00 46.12  ?  276  ASP C OD1 1 
ATOM   9275  O  OD2 . ASP C  1 245 ? -2.153  35.296  12.507  1.00 45.95  -1 276  ASP C OD2 1 
ATOM   9276  N  N   . ARG C  1 246 ? -0.286  39.302  9.404   1.00 32.27  ?  277  ARG C N   1 
ATOM   9277  C  CA  . ARG C  1 246 ? -0.403  40.692  8.973   1.00 36.07  ?  277  ARG C CA  1 
ATOM   9278  C  C   . ARG C  1 246 ? -0.274  40.818  7.465   1.00 37.57  ?  277  ARG C C   1 
ATOM   9279  O  O   . ARG C  1 246 ? -0.917  41.678  6.855   1.00 36.55  ?  277  ARG C O   1 
ATOM   9280  C  CB  . ARG C  1 246 ? 0.657   41.562  9.660   1.00 37.99  ?  277  ARG C CB  1 
ATOM   9281  C  CG  . ARG C  1 246 ? 0.648   43.028  9.222   1.00 37.96  ?  277  ARG C CG  1 
ATOM   9282  C  CD  . ARG C  1 246 ? -0.665  43.688  9.589   1.00 35.35  ?  277  ARG C CD  1 
ATOM   9283  N  NE  . ARG C  1 246 ? -0.608  45.143  9.556   1.00 33.72  ?  277  ARG C NE  1 
ATOM   9284  C  CZ  . ARG C  1 246 ? -1.593  45.934  9.964   1.00 40.48  ?  277  ARG C CZ  1 
ATOM   9285  N  NH1 . ARG C  1 246 ? -2.717  45.433  10.474  1.00 31.40  ?  277  ARG C NH1 1 
ATOM   9286  N  NH2 . ARG C  1 246 ? -1.451  47.257  9.859   1.00 32.02  ?  277  ARG C NH2 1 
ATOM   9287  N  N   . ARG C  1 247 ? 0.556   39.972  6.854   1.00 38.10  ?  278  ARG C N   1 
ATOM   9288  C  CA  . ARG C  1 247 ? 0.747   40.016  5.411   1.00 38.26  ?  278  ARG C CA  1 
ATOM   9289  C  C   . ARG C  1 247 ? -0.506  39.545  4.688   1.00 37.20  ?  278  ARG C C   1 
ATOM   9290  O  O   . ARG C  1 247 ? -0.994  40.213  3.762   1.00 37.76  ?  278  ARG C O   1 
ATOM   9291  C  CB  . ARG C  1 247 ? 1.951   39.150  5.025   1.00 38.95  ?  278  ARG C CB  1 
ATOM   9292  C  CG  . ARG C  1 247 ? 2.299   39.171  3.540   1.00 35.49  ?  278  ARG C CG  1 
ATOM   9293  C  CD  . ARG C  1 247 ? 3.574   38.386  3.242   1.00 43.96  ?  278  ARG C CD  1 
ATOM   9294  N  NE  . ARG C  1 247 ? 3.471   36.969  3.580   1.00 50.88  ?  278  ARG C NE  1 
ATOM   9295  C  CZ  . ARG C  1 247 ? 4.237   36.348  4.471   1.00 46.53  ?  278  ARG C CZ  1 
ATOM   9296  N  NH1 . ARG C  1 247 ? 5.164   36.995  5.154   1.00 44.16  ?  278  ARG C NH1 1 
ATOM   9297  N  NH2 . ARG C  1 247 ? 4.065   35.043  4.680   1.00 41.54  ?  278  ARG C NH2 1 
ATOM   9298  N  N   . THR C  1 248 ? -1.026  38.383  5.089   1.00 31.74  ?  279  THR C N   1 
ATOM   9299  C  CA  . THR C  1 248 ? -2.259  37.865  4.503   1.00 34.68  ?  279  THR C CA  1 
ATOM   9300  C  C   . THR C  1 248 ? -3.395  38.863  4.668   1.00 33.52  ?  279  THR C C   1 
ATOM   9301  O  O   . THR C  1 248 ? -4.153  39.131  3.722   1.00 34.45  ?  279  THR C O   1 
ATOM   9302  C  CB  . THR C  1 248 ? -2.633  36.543  5.164   1.00 34.04  ?  279  THR C CB  1 
ATOM   9303  O  OG1 . THR C  1 248 ? -1.531  35.631  5.084   1.00 34.81  ?  279  THR C OG1 1 
ATOM   9304  C  CG2 . THR C  1 248 ? -3.837  35.945  4.472   1.00 35.88  ?  279  THR C CG2 1 
ATOM   9305  N  N   . TYR C  1 249 ? -3.537  39.406  5.883   1.00 32.38  ?  280  TYR C N   1 
ATOM   9306  C  CA  . TYR C  1 249 ? -4.574  40.403  6.149   1.00 34.44  ?  280  TYR C CA  1 
ATOM   9307  C  C   . TYR C  1 249 ? -4.397  41.631  5.262   1.00 35.14  ?  280  TYR C C   1 
ATOM   9308  O  O   . TYR C  1 249 ? -5.377  42.154  4.720   1.00 33.88  ?  280  TYR C O   1 
ATOM   9309  C  CB  . TYR C  1 249 ? -4.539  40.765  7.634   1.00 30.80  ?  280  TYR C CB  1 
ATOM   9310  C  CG  . TYR C  1 249 ? -5.392  41.921  8.117   1.00 34.26  ?  280  TYR C CG  1 
ATOM   9311  C  CD1 . TYR C  1 249 ? -4.997  43.233  7.915   1.00 31.17  ?  280  TYR C CD1 1 
ATOM   9312  C  CD2 . TYR C  1 249 ? -6.534  41.690  8.888   1.00 30.05  ?  280  TYR C CD2 1 
ATOM   9313  C  CE1 . TYR C  1 249 ? -5.749  44.289  8.396   1.00 31.21  ?  280  TYR C CE1 1 
ATOM   9314  C  CE2 . TYR C  1 249 ? -7.283  42.740  9.382   1.00 30.39  ?  280  TYR C CE2 1 
ATOM   9315  C  CZ  . TYR C  1 249 ? -6.886  44.037  9.129   1.00 31.15  ?  280  TYR C CZ  1 
ATOM   9316  O  OH  . TYR C  1 249 ? -7.626  45.090  9.615   1.00 30.32  ?  280  TYR C OH  1 
ATOM   9317  N  N   . ALA C  1 250 ? -3.150  42.099  5.086   1.00 34.97  ?  281  ALA C N   1 
ATOM   9318  C  CA  . ALA C  1 250 ? -2.916  43.259  4.221   1.00 32.84  ?  281  ALA C CA  1 
ATOM   9319  C  C   . ALA C  1 250 ? -3.408  42.989  2.805   1.00 32.46  ?  281  ALA C C   1 
ATOM   9320  O  O   . ALA C  1 250 ? -4.083  43.829  2.198   1.00 30.38  ?  281  ALA C O   1 
ATOM   9321  C  CB  . ALA C  1 250 ? -1.429  43.636  4.200   1.00 33.02  ?  281  ALA C CB  1 
ATOM   9322  N  N   . ALA C  1 251 ? -3.105  41.798  2.276   1.00 34.33  ?  282  ALA C N   1 
ATOM   9323  C  CA  . ALA C  1 251 ? -3.534  41.439  0.929   1.00 34.03  ?  282  ALA C CA  1 
ATOM   9324  C  C   . ALA C  1 251 ? -5.055  41.365  0.825   1.00 35.32  ?  282  ALA C C   1 
ATOM   9325  O  O   . ALA C  1 251 ? -5.616  41.571  -0.256  1.00 36.97  ?  282  ALA C O   1 
ATOM   9326  C  CB  . ALA C  1 251 ? -2.907  40.105  0.523   1.00 31.65  ?  282  ALA C CB  1 
ATOM   9327  N  N   . MET C  1 252 ? -5.727  41.080  1.936   1.00 33.93  ?  283  MET C N   1 
ATOM   9328  C  CA  . MET C  1 252 ? -7.182  40.983  1.950   1.00 34.35  ?  283  MET C CA  1 
ATOM   9329  C  C   . MET C  1 252 ? -7.813  42.362  1.812   1.00 33.25  ?  283  MET C C   1 
ATOM   9330  O  O   . MET C  1 252 ? -8.796  42.548  1.068   1.00 34.10  ?  283  MET C O   1 
ATOM   9331  C  CB  . MET C  1 252 ? -7.599  40.332  3.261   1.00 32.74  ?  283  MET C CB  1 
ATOM   9332  C  CG  . MET C  1 252 ? -7.480  38.837  3.219   1.00 32.58  ?  283  MET C CG  1 
ATOM   9333  S  SD  . MET C  1 252 ? -7.753  38.125  4.847   1.00 33.07  ?  283  MET C SD  1 
ATOM   9334  C  CE  . MET C  1 252 ? -9.546  37.939  4.765   1.00 28.91  ?  283  MET C CE  1 
ATOM   9335  N  N   . VAL C  1 253 ? -7.283  43.335  2.560   1.00 30.81  ?  284  VAL C N   1 
ATOM   9336  C  CA  . VAL C  1 253 ? -7.733  44.720  2.437   1.00 29.54  ?  284  VAL C CA  1 
ATOM   9337  C  C   . VAL C  1 253 ? -7.392  45.264  1.055   1.00 34.47  ?  284  VAL C C   1 
ATOM   9338  O  O   . VAL C  1 253 ? -8.214  45.931  0.415   1.00 38.19  ?  284  VAL C O   1 
ATOM   9339  C  CB  . VAL C  1 253 ? -7.123  45.603  3.544   1.00 34.09  ?  284  VAL C CB  1 
ATOM   9340  C  CG1 . VAL C  1 253 ? -7.595  47.040  3.386   1.00 33.80  ?  284  VAL C CG1 1 
ATOM   9341  C  CG2 . VAL C  1 253 ? -7.468  45.089  4.947   1.00 34.50  ?  284  VAL C CG2 1 
ATOM   9342  N  N   . TYR C  1 254 ? -6.179  44.984  0.571   1.00 36.09  ?  285  TYR C N   1 
ATOM   9343  C  CA  . TYR C  1 254 ? -5.797  45.419  -0.770  1.00 34.46  ?  285  TYR C CA  1 
ATOM   9344  C  C   . TYR C  1 254 ? -6.807  44.946  -1.806  1.00 36.52  ?  285  TYR C C   1 
ATOM   9345  O  O   . TYR C  1 254 ? -7.176  45.692  -2.722  1.00 36.84  ?  285  TYR C O   1 
ATOM   9346  C  CB  . TYR C  1 254 ? -4.408  44.891  -1.117  1.00 39.87  ?  285  TYR C CB  1 
ATOM   9347  C  CG  . TYR C  1 254 ? -3.909  45.434  -2.424  1.00 39.31  ?  285  TYR C CG  1 
ATOM   9348  C  CD1 . TYR C  1 254 ? -3.685  46.797  -2.583  1.00 38.46  ?  285  TYR C CD1 1 
ATOM   9349  C  CD2 . TYR C  1 254 ? -3.695  44.592  -3.513  1.00 38.25  ?  285  TYR C CD2 1 
ATOM   9350  C  CE1 . TYR C  1 254 ? -3.233  47.310  -3.789  1.00 42.38  ?  285  TYR C CE1 1 
ATOM   9351  C  CE2 . TYR C  1 254 ? -3.259  45.097  -4.728  1.00 43.39  ?  285  TYR C CE2 1 
ATOM   9352  C  CZ  . TYR C  1 254 ? -3.037  46.455  -4.860  1.00 45.84  ?  285  TYR C CZ  1 
ATOM   9353  O  OH  . TYR C  1 254 ? -2.602  46.961  -6.060  1.00 50.08  ?  285  TYR C OH  1 
ATOM   9354  N  N   . ALA C  1 255 ? -7.272  43.704  -1.664  1.00 35.30  ?  286  ALA C N   1 
ATOM   9355  C  CA  . ALA C  1 255 ? -8.270  43.166  -2.586  1.00 36.01  ?  286  ALA C CA  1 
ATOM   9356  C  C   . ALA C  1 255 ? -9.558  43.983  -2.559  1.00 34.32  ?  286  ALA C C   1 
ATOM   9357  O  O   . ALA C  1 255 ? -10.205 44.172  -3.600  1.00 36.85  ?  286  ALA C O   1 
ATOM   9358  C  CB  . ALA C  1 255 ? -8.539  41.701  -2.242  1.00 34.91  ?  286  ALA C CB  1 
ATOM   9359  N  N   . VAL C  1 256 ? -9.954  44.476  -1.382  1.00 32.47  ?  287  VAL C N   1 
ATOM   9360  C  CA  . VAL C  1 256 ? -11.092 45.389  -1.298  1.00 33.37  ?  287  VAL C CA  1 
ATOM   9361  C  C   . VAL C  1 256 ? -10.775 46.687  -2.027  1.00 40.69  ?  287  VAL C C   1 
ATOM   9362  O  O   . VAL C  1 256 ? -11.614 47.236  -2.761  1.00 36.40  ?  287  VAL C O   1 
ATOM   9363  C  CB  . VAL C  1 256 ? -11.457 45.653  0.175   1.00 35.02  ?  287  VAL C CB  1 
ATOM   9364  C  CG1 . VAL C  1 256 ? -12.527 46.747  0.281   1.00 33.94  ?  287  VAL C CG1 1 
ATOM   9365  C  CG2 . VAL C  1 256 ? -11.904 44.372  0.862   1.00 31.22  ?  287  VAL C CG2 1 
ATOM   9366  N  N   . ASP C  1 257 ? -9.556  47.197  -1.829  1.00 30.50  ?  288  ASP C N   1 
ATOM   9367  C  CA  . ASP C  1 257 ? -9.139  48.446  -2.460  1.00 36.81  ?  288  ASP C CA  1 
ATOM   9368  C  C   . ASP C  1 257 ? -9.195  48.333  -3.981  1.00 33.64  ?  288  ASP C C   1 
ATOM   9369  O  O   . ASP C  1 257 ? -9.685  49.238  -4.661  1.00 34.59  ?  288  ASP C O   1 
ATOM   9370  C  CB  . ASP C  1 257 ? -7.711  48.808  -2.033  1.00 36.22  ?  288  ASP C CB  1 
ATOM   9371  C  CG  . ASP C  1 257 ? -7.361  50.267  -2.354  1.00 40.80  ?  288  ASP C CG  1 
ATOM   9372  O  OD1 . ASP C  1 257 ? -8.010  51.180  -1.796  1.00 38.02  ?  288  ASP C OD1 1 
ATOM   9373  O  OD2 . ASP C  1 257 ? -6.524  50.494  -3.259  1.00 41.74  -1 288  ASP C OD2 1 
ATOM   9374  N  N   . ARG C  1 258 ? -8.651  47.239  -4.534  1.00 37.00  ?  289  ARG C N   1 
ATOM   9375  C  CA  . ARG C  1 258 ? -8.744  46.999  -5.972  1.00 36.78  ?  289  ARG C CA  1 
ATOM   9376  C  C   . ARG C  1 258 ? -10.185 47.078  -6.452  1.00 41.28  ?  289  ARG C C   1 
ATOM   9377  O  O   . ARG C  1 258 ? -10.473 47.678  -7.497  1.00 38.47  ?  289  ARG C O   1 
ATOM   9378  C  CB  . ARG C  1 258 ? -8.186  45.628  -6.336  1.00 41.12  ?  289  ARG C CB  1 
ATOM   9379  C  CG  . ARG C  1 258 ? -6.702  45.430  -6.188  1.00 37.77  ?  289  ARG C CG  1 
ATOM   9380  C  CD  . ARG C  1 258 ? -6.300  44.171  -6.940  1.00 44.21  ?  289  ARG C CD  1 
ATOM   9381  N  NE  . ARG C  1 258 ? -6.593  42.934  -6.217  1.00 42.08  ?  289  ARG C NE  1 
ATOM   9382  C  CZ  . ARG C  1 258 ? -7.666  42.170  -6.393  1.00 43.17  ?  289  ARG C CZ  1 
ATOM   9383  N  NH1 . ARG C  1 258 ? -8.624  42.495  -7.258  1.00 38.23  ?  289  ARG C NH1 1 
ATOM   9384  N  NH2 . ARG C  1 258 ? -7.781  41.044  -5.689  1.00 39.37  ?  289  ARG C NH2 1 
ATOM   9385  N  N   . GLY C  1 259 ? -11.100 46.431  -5.718  1.00 37.53  ?  290  GLY C N   1 
ATOM   9386  C  CA  . GLY C  1 259 ? -12.492 46.415  -6.137  1.00 35.05  ?  290  GLY C CA  1 
ATOM   9387  C  C   . GLY C  1 259 ? -13.108 47.798  -6.107  1.00 37.91  ?  290  GLY C C   1 
ATOM   9388  O  O   . GLY C  1 259 ? -13.873 48.171  -7.002  1.00 38.13  ?  290  GLY C O   1 
ATOM   9389  N  N   . VAL C  1 260 ? -12.753 48.593  -5.097  1.00 37.64  ?  291  VAL C N   1 
ATOM   9390  C  CA  . VAL C  1 260 ? -13.246 49.961  -5.008  1.00 37.24  ?  291  VAL C CA  1 
ATOM   9391  C  C   . VAL C  1 260 ? -12.708 50.788  -6.168  1.00 37.37  ?  291  VAL C C   1 
ATOM   9392  O  O   . VAL C  1 260 ? -13.402 51.678  -6.680  1.00 40.88  ?  291  VAL C O   1 
ATOM   9393  C  CB  . VAL C  1 260 ? -12.880 50.567  -3.633  1.00 40.81  ?  291  VAL C CB  1 
ATOM   9394  C  CG1 . VAL C  1 260 ? -13.038 52.091  -3.626  1.00 31.35  ?  291  VAL C CG1 1 
ATOM   9395  C  CG2 . VAL C  1 260 ? -13.739 49.933  -2.528  1.00 34.99  ?  291  VAL C CG2 1 
ATOM   9396  N  N   . GLY C  1 261 ? -11.483 50.497  -6.618  1.00 38.21  ?  292  GLY C N   1 
ATOM   9397  C  CA  . GLY C  1 261 ? -10.969 51.160  -7.809  1.00 40.50  ?  292  GLY C CA  1 
ATOM   9398  C  C   . GLY C  1 261 ? -11.826 50.887  -9.032  1.00 42.75  ?  292  GLY C C   1 
ATOM   9399  O  O   . GLY C  1 261 ? -12.222 51.811  -9.750  1.00 39.38  ?  292  GLY C O   1 
ATOM   9400  N  N   . LYS C  1 262 ? -12.136 49.609  -9.280  1.00 43.20  ?  293  LYS C N   1 
ATOM   9401  C  CA  . LYS C  1 262 ? -12.949 49.257  -10.440 1.00 38.65  ?  293  LYS C CA  1 
ATOM   9402  C  C   . LYS C  1 262 ? -14.354 49.833  -10.310 1.00 42.47  ?  293  LYS C C   1 
ATOM   9403  O  O   . LYS C  1 262 ? -14.956 50.262  -11.303 1.00 43.79  ?  293  LYS C O   1 
ATOM   9404  C  CB  . LYS C  1 262 ? -13.011 47.735  -10.613 1.00 38.78  ?  293  LYS C CB  1 
ATOM   9405  C  CG  . LYS C  1 262 ? -11.663 47.074  -10.930 1.00 46.56  ?  293  LYS C CG  1 
ATOM   9406  C  CD  . LYS C  1 262 ? -11.737 45.542  -10.764 1.00 51.05  ?  293  LYS C CD  1 
ATOM   9407  C  CE  . LYS C  1 262 ? -10.824 44.996  -9.625  1.00 52.22  ?  293  LYS C CE  1 
ATOM   9408  N  NZ  . LYS C  1 262 ? -11.560 44.005  -8.720  1.00 44.33  ?  293  LYS C NZ  1 
ATOM   9409  N  N   . ILE C  1 263 ? -14.891 49.856  -9.092  1.00 37.40  ?  294  ILE C N   1 
ATOM   9410  C  CA  . ILE C  1 263 ? -16.191 50.478  -8.850  1.00 36.61  ?  294  ILE C CA  1 
ATOM   9411  C  C   . ILE C  1 263 ? -16.136 51.958  -9.206  1.00 42.33  ?  294  ILE C C   1 
ATOM   9412  O  O   . ILE C  1 263 ? -17.037 52.495  -9.868  1.00 35.53  ?  294  ILE C O   1 
ATOM   9413  C  CB  . ILE C  1 263 ? -16.620 50.260  -7.384  1.00 35.83  ?  294  ILE C CB  1 
ATOM   9414  C  CG1 . ILE C  1 263 ? -17.187 48.841  -7.210  1.00 35.05  ?  294  ILE C CG1 1 
ATOM   9415  C  CG2 . ILE C  1 263 ? -17.627 51.324  -6.922  1.00 33.01  ?  294  ILE C CG2 1 
ATOM   9416  C  CD1 . ILE C  1 263 ? -17.128 48.325  -5.791  1.00 31.94  ?  294  ILE C CD1 1 
ATOM   9417  N  N   . VAL C  1 264 ? -15.067 52.639  -8.782  1.00 37.09  ?  295  VAL C N   1 
ATOM   9418  C  CA  . VAL C  1 264 ? -14.939 54.067  -9.060  1.00 37.92  ?  295  VAL C CA  1 
ATOM   9419  C  C   . VAL C  1 264 ? -14.850 54.306  -10.565 1.00 38.80  ?  295  VAL C C   1 
ATOM   9420  O  O   . VAL C  1 264 ? -15.476 55.232  -11.101 1.00 40.11  ?  295  VAL C O   1 
ATOM   9421  C  CB  . VAL C  1 264 ? -13.725 54.652  -8.305  1.00 41.70  ?  295  VAL C CB  1 
ATOM   9422  C  CG1 . VAL C  1 264 ? -13.308 55.991  -8.899  1.00 40.41  ?  295  VAL C CG1 1 
ATOM   9423  C  CG2 . VAL C  1 264 ? -14.041 54.804  -6.817  1.00 42.10  ?  295  VAL C CG2 1 
ATOM   9424  N  N   . GLN C  1 265 ? -14.092 53.465  -11.272 1.00 37.53  ?  296  GLN C N   1 
ATOM   9425  C  CA  . GLN C  1 265 ? -14.048 53.555  -12.729 1.00 45.63  ?  296  GLN C CA  1 
ATOM   9426  C  C   . GLN C  1 265 ? -15.442 53.421  -13.332 1.00 46.22  ?  296  GLN C C   1 
ATOM   9427  O  O   . GLN C  1 265 ? -15.779 54.120  -14.296 1.00 44.63  ?  296  GLN C O   1 
ATOM   9428  C  CB  . GLN C  1 265 ? -13.127 52.476  -13.301 1.00 49.61  ?  296  GLN C CB  1 
ATOM   9429  C  CG  . GLN C  1 265 ? -12.306 52.851  -14.557 1.00 55.66  ?  296  GLN C CG  1 
ATOM   9430  C  CD  . GLN C  1 265 ? -11.431 54.103  -14.403 1.00 65.49  ?  296  GLN C CD  1 
ATOM   9431  O  OE1 . GLN C  1 265 ? -11.924 55.234  -14.327 1.00 61.24  ?  296  GLN C OE1 1 
ATOM   9432  N  NE2 . GLN C  1 265 ? -10.116 53.894  -14.370 1.00 66.63  ?  296  GLN C NE2 1 
ATOM   9433  N  N   . THR C  1 266 ? -16.265 52.525  -12.777 1.00 45.10  ?  297  THR C N   1 
ATOM   9434  C  CA  . THR C  1 266 ? -17.591 52.283  -13.342 1.00 41.52  ?  297  THR C CA  1 
ATOM   9435  C  C   . THR C  1 266 ? -18.524 53.449  -13.059 1.00 43.31  ?  297  THR C C   1 
ATOM   9436  O  O   . THR C  1 266 ? -19.312 53.846  -13.927 1.00 45.75  ?  297  THR C O   1 
ATOM   9437  C  CB  . THR C  1 266 ? -18.172 50.973  -12.802 1.00 36.92  ?  297  THR C CB  1 
ATOM   9438  O  OG1 . THR C  1 266 ? -17.248 49.909  -13.064 1.00 41.36  ?  297  THR C OG1 1 
ATOM   9439  C  CG2 . THR C  1 266 ? -19.508 50.630  -13.503 1.00 41.26  ?  297  THR C CG2 1 
ATOM   9440  N  N   . LEU C  1 267 ? -18.445 54.018  -11.859 1.00 40.21  ?  298  LEU C N   1 
ATOM   9441  C  CA  . LEU C  1 267 ? -19.224 55.216  -11.577 1.00 44.06  ?  298  LEU C CA  1 
ATOM   9442  C  C   . LEU C  1 267 ? -18.845 56.354  -12.517 1.00 48.62  ?  298  LEU C C   1 
ATOM   9443  O  O   . LEU C  1 267 ? -19.703 57.167  -12.889 1.00 46.28  ?  298  LEU C O   1 
ATOM   9444  C  CB  . LEU C  1 267 ? -19.031 55.650  -10.128 1.00 41.44  ?  298  LEU C CB  1 
ATOM   9445  C  CG  . LEU C  1 267 ? -19.701 54.826  -9.023  1.00 44.31  ?  298  LEU C CG  1 
ATOM   9446  C  CD1 . LEU C  1 267 ? -19.281 55.337  -7.648  1.00 37.59  ?  298  LEU C CD1 1 
ATOM   9447  C  CD2 . LEU C  1 267 ? -21.225 54.842  -9.169  1.00 34.19  ?  298  LEU C CD2 1 
ATOM   9448  N  N   . LYS C  1 268 ? -17.568 56.431  -12.906 1.00 43.97  ?  299  LYS C N   1 
ATOM   9449  C  CA  . LYS C  1 268 ? -17.142 57.490  -13.812 1.00 47.12  ?  299  LYS C CA  1 
ATOM   9450  C  C   . LYS C  1 268 ? -17.646 57.239  -15.225 1.00 45.95  ?  299  LYS C C   1 
ATOM   9451  O  O   . LYS C  1 268 ? -18.088 58.169  -15.905 1.00 48.52  ?  299  LYS C O   1 
ATOM   9452  C  CB  . LYS C  1 268 ? -15.618 57.613  -13.799 1.00 42.72  ?  299  LYS C CB  1 
ATOM   9453  C  CG  . LYS C  1 268 ? -15.100 58.319  -12.550 1.00 47.43  ?  299  LYS C CG  1 
ATOM   9454  C  CD  . LYS C  1 268 ? -13.591 58.379  -12.518 1.00 46.43  ?  299  LYS C CD  1 
ATOM   9455  C  CE  . LYS C  1 268 ? -13.116 59.473  -11.593 1.00 50.82  ?  299  LYS C CE  1 
ATOM   9456  N  NZ  . LYS C  1 268 ? -11.651 59.328  -11.401 1.00 52.70  ?  299  LYS C NZ  1 
ATOM   9457  N  N   . GLU C  1 269 ? -17.572 55.994  -15.694 1.00 47.69  ?  300  GLU C N   1 
ATOM   9458  C  CA  . GLU C  1 269 ? -17.982 55.711  -17.065 1.00 47.40  ?  300  GLU C CA  1 
ATOM   9459  C  C   . GLU C  1 269 ? -19.475 55.945  -17.252 1.00 51.56  ?  300  GLU C C   1 
ATOM   9460  O  O   . GLU C  1 269 ? -19.907 56.421  -18.309 1.00 52.97  ?  300  GLU C O   1 
ATOM   9461  C  CB  . GLU C  1 269 ? -17.596 54.281  -17.444 1.00 50.32  ?  300  GLU C CB  1 
ATOM   9462  C  CG  . GLU C  1 269 ? -16.089 54.064  -17.481 1.00 51.27  ?  300  GLU C CG  1 
ATOM   9463  C  CD  . GLU C  1 269 ? -15.684 52.627  -17.809 1.00 61.99  ?  300  GLU C CD  1 
ATOM   9464  O  OE1 . GLU C  1 269 ? -16.562 51.734  -17.807 1.00 65.25  ?  300  GLU C OE1 1 
ATOM   9465  O  OE2 . GLU C  1 269 ? -14.474 52.388  -18.043 1.00 62.22  -1 300  GLU C OE2 1 
ATOM   9466  N  N   . THR C  1 270 ? -20.273 55.644  -16.232 1.00 49.51  ?  301  THR C N   1 
ATOM   9467  C  CA  . THR C  1 270 ? -21.717 55.826  -16.281 1.00 47.09  ?  301  THR C CA  1 
ATOM   9468  C  C   . THR C  1 270 ? -22.166 57.223  -15.882 1.00 48.53  ?  301  THR C C   1 
ATOM   9469  O  O   . THR C  1 270 ? -23.376 57.456  -15.793 1.00 48.67  ?  301  THR C O   1 
ATOM   9470  C  CB  . THR C  1 270 ? -22.399 54.821  -15.359 1.00 47.98  ?  301  THR C CB  1 
ATOM   9471  O  OG1 . THR C  1 270 ? -21.988 55.087  -14.009 1.00 48.75  ?  301  THR C OG1 1 
ATOM   9472  C  CG2 . THR C  1 270 ? -22.025 53.401  -15.740 1.00 43.10  ?  301  THR C CG2 1 
ATOM   9473  N  N   . LYS C  1 271 ? -21.238 58.142  -15.606 1.00 42.53  ?  302  LYS C N   1 
ATOM   9474  C  CA  . LYS C  1 271 ? -21.573 59.507  -15.210 1.00 45.76  ?  302  LYS C CA  1 
ATOM   9475  C  C   . LYS C  1 271 ? -22.410 59.554  -13.932 1.00 48.61  ?  302  LYS C C   1 
ATOM   9476  O  O   . LYS C  1 271 ? -23.145 60.521  -13.691 1.00 49.96  ?  302  LYS C O   1 
ATOM   9477  C  CB  . LYS C  1 271 ? -22.298 60.252  -16.341 1.00 49.80  ?  302  LYS C CB  1 
ATOM   9478  N  N   . GLN C  1 272 ? -22.329 58.525  -13.093 1.00 42.47  ?  303  GLN C N   1 
ATOM   9479  C  CA  . GLN C  1 272 ? -22.961 58.593  -11.787 1.00 43.80  ?  303  GLN C CA  1 
ATOM   9480  C  C   . GLN C  1 272 ? -21.995 59.057  -10.704 1.00 45.27  ?  303  GLN C C   1 
ATOM   9481  O  O   . GLN C  1 272 ? -22.419 59.260  -9.563  1.00 45.50  ?  303  GLN C O   1 
ATOM   9482  C  CB  . GLN C  1 272 ? -23.553 57.228  -11.420 1.00 45.11  ?  303  GLN C CB  1 
ATOM   9483  C  CG  . GLN C  1 272 ? -24.719 56.816  -12.328 1.00 47.43  ?  303  GLN C CG  1 
ATOM   9484  C  CD  . GLN C  1 272 ? -25.059 55.339  -12.209 1.00 49.79  ?  303  GLN C CD  1 
ATOM   9485  O  OE1 . GLN C  1 272 ? -26.165 54.972  -11.799 1.00 50.74  ?  303  GLN C OE1 1 
ATOM   9486  N  NE2 . GLN C  1 272 ? -24.101 54.480  -12.556 1.00 47.69  ?  303  GLN C NE2 1 
ATOM   9487  N  N   . PHE C  1 273 ? -20.720 59.256  -11.046 1.00 45.16  ?  304  PHE C N   1 
ATOM   9488  C  CA  . PHE C  1 273 ? -19.698 59.549  -10.042 1.00 43.04  ?  304  PHE C CA  1 
ATOM   9489  C  C   . PHE C  1 273 ? -20.069 60.777  -9.214  1.00 45.85  ?  304  PHE C C   1 
ATOM   9490  O  O   . PHE C  1 273 ? -20.208 60.699  -7.987  1.00 45.14  ?  304  PHE C O   1 
ATOM   9491  C  CB  . PHE C  1 273 ? -18.337 59.732  -10.728 1.00 45.23  ?  304  PHE C CB  1 
ATOM   9492  C  CG  . PHE C  1 273 ? -17.180 59.833  -9.765  1.00 48.21  ?  304  PHE C CG  1 
ATOM   9493  C  CD1 . PHE C  1 273 ? -17.039 58.919  -8.729  1.00 47.17  ?  304  PHE C CD1 1 
ATOM   9494  C  CD2 . PHE C  1 273 ? -16.245 60.858  -9.879  1.00 50.80  ?  304  PHE C CD2 1 
ATOM   9495  C  CE1 . PHE C  1 273 ? -15.970 59.020  -7.825  1.00 51.67  ?  304  PHE C CE1 1 
ATOM   9496  C  CE2 . PHE C  1 273 ? -15.180 60.963  -8.981  1.00 47.49  ?  304  PHE C CE2 1 
ATOM   9497  C  CZ  . PHE C  1 273 ? -15.044 60.046  -7.957  1.00 46.48  ?  304  PHE C CZ  1 
ATOM   9498  N  N   . ASP C  1 274 ? -20.293 61.910  -9.885  1.00 43.90  ?  305  ASP C N   1 
ATOM   9499  C  CA  . ASP C  1 274 ? -20.413 63.195  -9.204  1.00 42.24  ?  305  ASP C CA  1 
ATOM   9500  C  C   . ASP C  1 274 ? -21.549 63.226  -8.188  1.00 46.28  ?  305  ASP C C   1 
ATOM   9501  O  O   . ASP C  1 274 ? -21.427 63.867  -7.134  1.00 43.39  ?  305  ASP C O   1 
ATOM   9502  C  CB  . ASP C  1 274 ? -20.605 64.302  -10.237 1.00 48.44  ?  305  ASP C CB  1 
ATOM   9503  C  CG  . ASP C  1 274 ? -20.088 65.635  -9.757  1.00 52.25  ?  305  ASP C CG  1 
ATOM   9504  O  OD1 . ASP C  1 274 ? -18.859 65.755  -9.543  1.00 57.84  ?  305  ASP C OD1 1 
ATOM   9505  O  OD2 . ASP C  1 274 ? -20.918 66.557  -9.587  1.00 56.78  -1 305  ASP C OD2 1 
ATOM   9506  N  N   . ASN C  1 275 ? -22.679 62.583  -8.497  1.00 44.83  ?  306  ASN C N   1 
ATOM   9507  C  CA  . ASN C  1 275 ? -23.860 62.632  -7.642  1.00 44.49  ?  306  ASN C CA  1 
ATOM   9508  C  C   . ASN C  1 275 ? -24.083 61.321  -6.886  1.00 45.29  ?  306  ASN C C   1 
ATOM   9509  O  O   . ASN C  1 275 ? -25.227 60.926  -6.638  1.00 44.67  ?  306  ASN C O   1 
ATOM   9510  C  CB  . ASN C  1 275 ? -25.113 62.997  -8.447  1.00 41.46  ?  306  ASN C CB  1 
ATOM   9511  C  CG  . ASN C  1 275 ? -26.243 63.496  -7.555  1.00 47.63  ?  306  ASN C CG  1 
ATOM   9512  O  OD1 . ASN C  1 275 ? -26.004 63.881  -6.409  1.00 43.92  ?  306  ASN C OD1 1 
ATOM   9513  N  ND2 . ASN C  1 275 ? -27.482 63.485  -8.067  1.00 47.00  ?  306  ASN C ND2 1 
ATOM   9514  N  N   . THR C  1 276 ? -23.010 60.636  -6.513  1.00 44.11  ?  307  THR C N   1 
ATOM   9515  C  CA  . THR C  1 276 ? -23.094 59.461  -5.655  1.00 40.10  ?  307  THR C CA  1 
ATOM   9516  C  C   . THR C  1 276 ? -22.425 59.787  -4.330  1.00 40.54  ?  307  THR C C   1 
ATOM   9517  O  O   . THR C  1 276 ? -21.254 60.180  -4.308  1.00 41.86  ?  307  THR C O   1 
ATOM   9518  C  CB  . THR C  1 276 ? -22.419 58.250  -6.298  1.00 41.51  ?  307  THR C CB  1 
ATOM   9519  O  OG1 . THR C  1 276 ? -23.116 57.885  -7.495  1.00 43.37  ?  307  THR C OG1 1 
ATOM   9520  C  CG2 . THR C  1 276 ? -22.403 57.067  -5.331  1.00 36.08  ?  307  THR C CG2 1 
ATOM   9521  N  N   . LEU C  1 277 ? -23.156 59.614  -3.231  1.00 38.70  ?  308  LEU C N   1 
ATOM   9522  C  CA  . LEU C  1 277 ? -22.552 59.691  -1.905  1.00 39.40  ?  308  LEU C CA  1 
ATOM   9523  C  C   . LEU C  1 277 ? -21.989 58.311  -1.569  1.00 43.42  ?  308  LEU C C   1 
ATOM   9524  O  O   . LEU C  1 277 ? -22.747 57.336  -1.459  1.00 37.54  ?  308  LEU C O   1 
ATOM   9525  C  CB  . LEU C  1 277 ? -23.568 60.143  -0.849  1.00 31.10  ?  308  LEU C CB  1 
ATOM   9526  C  CG  . LEU C  1 277 ? -23.151 59.899  0.606   1.00 38.60  ?  308  LEU C CG  1 
ATOM   9527  C  CD1 . LEU C  1 277 ? -21.848 60.652  0.914   1.00 33.94  ?  308  LEU C CD1 1 
ATOM   9528  C  CD2 . LEU C  1 277 ? -24.253 60.288  1.592   1.00 37.77  ?  308  LEU C CD2 1 
ATOM   9529  N  N   . ILE C  1 278 ? -20.666 58.218  -1.434  1.00 38.55  ?  309  ILE C N   1 
ATOM   9530  C  CA  . ILE C  1 278 ? -20.005 56.980  -1.033  1.00 38.95  ?  309  ILE C CA  1 
ATOM   9531  C  C   . ILE C  1 278 ? -19.617 57.095  0.431   1.00 40.34  ?  309  ILE C C   1 
ATOM   9532  O  O   . ILE C  1 278 ? -18.891 58.019  0.816   1.00 39.91  ?  309  ILE C O   1 
ATOM   9533  C  CB  . ILE C  1 278 ? -18.765 56.687  -1.888  1.00 39.11  ?  309  ILE C CB  1 
ATOM   9534  C  CG1 . ILE C  1 278 ? -19.123 56.543  -3.368  1.00 35.73  ?  309  ILE C CG1 1 
ATOM   9535  C  CG2 . ILE C  1 278 ? -18.064 55.438  -1.361  1.00 34.85  ?  309  ILE C CG2 1 
ATOM   9536  C  CD1 . ILE C  1 278 ? -17.892 56.426  -4.261  1.00 36.16  ?  309  ILE C CD1 1 
ATOM   9537  N  N   . VAL C  1 279 ? -20.079 56.143  1.239   1.00 34.30  ?  310  VAL C N   1 
ATOM   9538  C  CA  . VAL C  1 279 ? -19.776 56.068  2.665   1.00 32.41  ?  310  VAL C CA  1 
ATOM   9539  C  C   . VAL C  1 279 ? -18.985 54.788  2.910   1.00 36.60  ?  310  VAL C C   1 
ATOM   9540  O  O   . VAL C  1 279 ? -19.437 53.691  2.552   1.00 33.94  ?  310  VAL C O   1 
ATOM   9541  C  CB  . VAL C  1 279 ? -21.066 56.102  3.495   1.00 39.29  ?  310  VAL C CB  1 
ATOM   9542  C  CG1 . VAL C  1 279 ? -20.772 55.897  4.968   1.00 36.52  ?  310  VAL C CG1 1 
ATOM   9543  C  CG2 . VAL C  1 279 ? -21.809 57.415  3.239   1.00 30.42  ?  310  VAL C CG2 1 
ATOM   9544  N  N   . PHE C  1 280 ? -17.787 54.923  3.478   1.00 36.54  ?  311  PHE C N   1 
ATOM   9545  C  CA  . PHE C  1 280 ? -16.925 53.780  3.740   1.00 32.25  ?  311  PHE C CA  1 
ATOM   9546  C  C   . PHE C  1 280 ? -16.692 53.702  5.240   1.00 35.13  ?  311  PHE C C   1 
ATOM   9547  O  O   . PHE C  1 280 ? -16.509 54.734  5.893   1.00 33.39  ?  311  PHE C O   1 
ATOM   9548  C  CB  . PHE C  1 280 ? -15.607 53.886  2.966   1.00 35.08  ?  311  PHE C CB  1 
ATOM   9549  C  CG  . PHE C  1 280 ? -14.547 52.893  3.406   1.00 35.03  ?  311  PHE C CG  1 
ATOM   9550  C  CD1 . PHE C  1 280 ? -14.499 51.615  2.875   1.00 31.22  ?  311  PHE C CD1 1 
ATOM   9551  C  CD2 . PHE C  1 280 ? -13.602 53.250  4.349   1.00 34.54  ?  311  PHE C CD2 1 
ATOM   9552  C  CE1 . PHE C  1 280 ? -13.541 50.715  3.281   1.00 39.59  ?  311  PHE C CE1 1 
ATOM   9553  C  CE2 . PHE C  1 280 ? -12.631 52.354  4.753   1.00 33.08  ?  311  PHE C CE2 1 
ATOM   9554  C  CZ  . PHE C  1 280 ? -12.590 51.092  4.226   1.00 32.46  ?  311  PHE C CZ  1 
ATOM   9555  N  N   . LEU C  1 281 ? -16.759 52.486  5.787   1.00 30.26  ?  312  LEU C N   1 
ATOM   9556  C  CA  . LEU C  1 281 ? -16.541 52.276  7.214   1.00 35.10  ?  312  LEU C CA  1 
ATOM   9557  C  C   . LEU C  1 281 ? -16.352 50.787  7.480   1.00 31.63  ?  312  LEU C C   1 
ATOM   9558  O  O   . LEU C  1 281 ? -16.477 49.943  6.584   1.00 33.50  ?  312  LEU C O   1 
ATOM   9559  C  CB  . LEU C  1 281 ? -17.690 52.845  8.064   1.00 34.60  ?  312  LEU C CB  1 
ATOM   9560  C  CG  . LEU C  1 281 ? -19.026 52.107  8.201   1.00 32.22  ?  312  LEU C CG  1 
ATOM   9561  C  CD1 . LEU C  1 281 ? -19.841 52.692  9.351   1.00 32.93  ?  312  LEU C CD1 1 
ATOM   9562  C  CD2 . LEU C  1 281 ? -19.832 52.181  6.908   1.00 29.67  ?  312  LEU C CD2 1 
ATOM   9563  N  N   . SER C  1 282 ? -16.006 50.488  8.726   1.00 31.22  ?  313  SER C N   1 
ATOM   9564  C  CA  . SER C  1 282 ? -15.952 49.139  9.257   1.00 30.90  ?  313  SER C CA  1 
ATOM   9565  C  C   . SER C  1 282 ? -17.141 48.956  10.193  1.00 28.26  ?  313  SER C C   1 
ATOM   9566  O  O   . SER C  1 282 ? -17.616 49.921  10.795  1.00 27.29  ?  313  SER C O   1 
ATOM   9567  C  CB  . SER C  1 282 ? -14.625 48.908  10.009  1.00 29.20  ?  313  SER C CB  1 
ATOM   9568  O  OG  . SER C  1 282 ? -14.508 47.573  10.469  1.00 32.22  ?  313  SER C OG  1 
ATOM   9569  N  N   . ASP C  1 283 ? -17.613 47.718  10.310  1.00 27.63  ?  314  ASP C N   1 
ATOM   9570  C  CA  . ASP C  1 283 ? -18.747 47.426  11.224  1.00 29.30  ?  314  ASP C CA  1 
ATOM   9571  C  C   . ASP C  1 283 ? -18.287 47.445  12.690  1.00 28.12  ?  314  ASP C C   1 
ATOM   9572  O  O   . ASP C  1 283 ? -19.164 47.544  13.565  1.00 25.83  ?  314  ASP C O   1 
ATOM   9573  C  CB  . ASP C  1 283 ? -19.431 46.118  10.884  1.00 29.32  ?  314  ASP C CB  1 
ATOM   9574  C  CG  . ASP C  1 283 ? -18.625 44.848  11.114  1.00 30.10  ?  314  ASP C CG  1 
ATOM   9575  O  OD1 . ASP C  1 283 ? -17.378 44.924  11.095  1.00 31.84  ?  314  ASP C OD1 1 
ATOM   9576  O  OD2 . ASP C  1 283 ? -19.255 43.787  11.296  1.00 29.84  -1 314  ASP C OD2 1 
ATOM   9577  N  N   . ASN C  1 284 ? -16.979 47.297  12.937  1.00 29.16  ?  315  ASN C N   1 
ATOM   9578  C  CA  . ASN C  1 284 ? -16.457 47.340  14.331  1.00 25.18  ?  315  ASN C CA  1 
ATOM   9579  C  C   . ASN C  1 284 ? -14.930 47.451  14.293  1.00 27.08  ?  315  ASN C C   1 
ATOM   9580  O  O   . ASN C  1 284 ? -14.335 47.365  13.206  1.00 26.87  ?  315  ASN C O   1 
ATOM   9581  C  CB  . ASN C  1 284 ? -16.943 46.176  15.196  1.00 25.07  ?  315  ASN C CB  1 
ATOM   9582  C  CG  . ASN C  1 284 ? -16.750 44.834  14.533  1.00 32.42  ?  315  ASN C CG  1 
ATOM   9583  O  OD1 . ASN C  1 284 ? -17.732 44.169  14.186  1.00 29.60  ?  315  ASN C OD1 1 
ATOM   9584  N  ND2 . ASN C  1 284 ? -15.505 44.419  14.353  1.00 25.84  ?  315  ASN C ND2 1 
ATOM   9585  N  N   . GLY C  1 285 ? -14.323 47.581  15.470  1.00 28.70  ?  316  GLY C N   1 
ATOM   9586  C  CA  . GLY C  1 285 ? -12.865 47.755  15.512  1.00 27.36  ?  316  GLY C CA  1 
ATOM   9587  C  C   . GLY C  1 285 ? -12.168 46.484  15.070  1.00 34.19  ?  316  GLY C C   1 
ATOM   9588  O  O   . GLY C  1 285 ? -12.818 45.419  15.004  1.00 31.65  ?  316  GLY C O   1 
ATOM   9589  N  N   . GLY C  1 286 ? -10.873 46.581  14.815  1.00 29.48  ?  317  GLY C N   1 
ATOM   9590  C  CA  . GLY C  1 286 ? -10.115 45.405  14.379  1.00 29.38  ?  317  GLY C CA  1 
ATOM   9591  C  C   . GLY C  1 286 ? -9.910  44.367  15.471  1.00 28.61  ?  317  GLY C C   1 
ATOM   9592  O  O   . GLY C  1 286 ? -9.942  44.735  16.666  1.00 29.86  ?  317  GLY C O   1 
ATOM   9593  N  N   . ASN C  1 287 ? -9.792  43.101  15.084  1.00 28.55  ?  318  ASN C N   1 
ATOM   9594  C  CA  . ASN C  1 287 ? -9.410  42.043  16.016  1.00 30.09  ?  318  ASN C CA  1 
ATOM   9595  C  C   . ASN C  1 287 ? -7.888  41.930  15.981  1.00 30.22  ?  318  ASN C C   1 
ATOM   9596  O  O   . ASN C  1 287 ? -7.324  41.419  15.003  1.00 28.97  ?  318  ASN C O   1 
ATOM   9597  C  CB  . ASN C  1 287 ? -10.071 40.711  15.642  1.00 26.99  ?  318  ASN C CB  1 
ATOM   9598  C  CG  . ASN C  1 287 ? -9.838  39.618  16.695  1.00 30.24  ?  318  ASN C CG  1 
ATOM   9599  O  OD1 . ASN C  1 287 ? -8.849  39.650  17.419  1.00 32.10  ?  318  ASN C OD1 1 
ATOM   9600  N  ND2 . ASN C  1 287 ? -10.761 38.659  16.789  1.00 27.40  ?  318  ASN C ND2 1 
ATOM   9601  N  N   . PHE C  1 288 ? -7.207  42.392  17.043  1.00 30.76  ?  319  PHE C N   1 
ATOM   9602  C  CA  . PHE C  1 288 ? -5.758  42.365  16.910  1.00 31.60  ?  319  PHE C CA  1 
ATOM   9603  C  C   . PHE C  1 288 ? -5.178  40.971  17.105  1.00 34.80  ?  319  PHE C C   1 
ATOM   9604  O  O   . PHE C  1 288 ? -3.951  40.823  17.062  1.00 32.67  ?  319  PHE C O   1 
ATOM   9605  C  CB  . PHE C  1 288 ? -5.045  43.412  17.825  1.00 32.56  ?  319  PHE C CB  1 
ATOM   9606  C  CG  . PHE C  1 288 ? -5.387  43.364  19.305  1.00 32.30  ?  319  PHE C CG  1 
ATOM   9607  C  CD1 . PHE C  1 288 ? -5.691  42.184  19.959  1.00 31.54  ?  319  PHE C CD1 1 
ATOM   9608  C  CD2 . PHE C  1 288 ? -5.318  44.539  20.058  1.00 28.39  ?  319  PHE C CD2 1 
ATOM   9609  C  CE1 . PHE C  1 288 ? -5.957  42.177  21.333  1.00 33.82  ?  319  PHE C CE1 1 
ATOM   9610  C  CE2 . PHE C  1 288 ? -5.600  44.545  21.416  1.00 31.70  ?  319  PHE C CE2 1 
ATOM   9611  C  CZ  . PHE C  1 288 ? -5.916  43.356  22.063  1.00 33.62  ?  319  PHE C CZ  1 
ATOM   9612  N  N   . ASN C  1 289 ? -6.019  39.947  17.276  1.00 31.51  ?  320  ASN C N   1 
ATOM   9613  C  CA  . ASN C  1 289 ? -5.516  38.582  17.268  1.00 32.92  ?  320  ASN C CA  1 
ATOM   9614  C  C   . ASN C  1 289 ? -5.340  38.030  15.862  1.00 33.86  ?  320  ASN C C   1 
ATOM   9615  O  O   . ASN C  1 289 ? -4.681  36.999  15.700  1.00 32.56  ?  320  ASN C O   1 
ATOM   9616  C  CB  . ASN C  1 289 ? -6.447  37.659  18.056  1.00 31.07  ?  320  ASN C CB  1 
ATOM   9617  C  CG  . ASN C  1 289 ? -6.508  38.009  19.524  1.00 31.06  ?  320  ASN C CG  1 
ATOM   9618  O  OD1 . ASN C  1 289 ? -7.581  38.062  20.117  1.00 34.23  ?  320  ASN C OD1 1 
ATOM   9619  N  ND2 . ASN C  1 289 ? -5.353  38.259  20.122  1.00 31.51  ?  320  ASN C ND2 1 
ATOM   9620  N  N   . HIS C  1 290 ? -5.905  38.688  14.852  1.00 32.38  ?  321  HIS C N   1 
ATOM   9621  C  CA  . HIS C  1 290 ? -5.984  38.147  13.502  1.00 35.75  ?  321  HIS C CA  1 
ATOM   9622  C  C   . HIS C  1 290 ? -5.639  39.216  12.474  1.00 35.77  ?  321  HIS C C   1 
ATOM   9623  O  O   . HIS C  1 290 ? -6.409  39.490  11.552  1.00 32.40  ?  321  HIS C O   1 
ATOM   9624  C  CB  . HIS C  1 290 ? -7.382  37.596  13.231  1.00 36.00  ?  321  HIS C CB  1 
ATOM   9625  C  CG  . HIS C  1 290 ? -7.785  36.495  14.156  1.00 33.61  ?  321  HIS C CG  1 
ATOM   9626  N  ND1 . HIS C  1 290 ? -7.258  35.225  14.075  1.00 38.61  ?  321  HIS C ND1 1 
ATOM   9627  C  CD2 . HIS C  1 290 ? -8.650  36.478  15.198  1.00 36.74  ?  321  HIS C CD2 1 
ATOM   9628  C  CE1 . HIS C  1 290 ? -7.793  34.469  15.018  1.00 38.13  ?  321  HIS C CE1 1 
ATOM   9629  N  NE2 . HIS C  1 290 ? -8.644  35.205  15.711  1.00 33.82  ?  321  HIS C NE2 1 
ATOM   9630  N  N   . GLY C  1 291 ? -4.495  39.871  12.647  1.00 35.58  ?  322  GLY C N   1 
ATOM   9631  C  CA  . GLY C  1 291 ? -3.946  40.709  11.603  1.00 36.27  ?  322  GLY C CA  1 
ATOM   9632  C  C   . GLY C  1 291 ? -4.173  42.200  11.766  1.00 33.75  ?  322  GLY C C   1 
ATOM   9633  O  O   . GLY C  1 291 ? -3.442  42.986  11.156  1.00 36.85  ?  322  GLY C O   1 
ATOM   9634  N  N   . ALA C  1 292 ? -5.129  42.614  12.586  1.00 31.25  ?  323  ALA C N   1 
ATOM   9635  C  CA  . ALA C  1 292 ? -5.546  44.008  12.585  1.00 30.07  ?  323  ALA C CA  1 
ATOM   9636  C  C   . ALA C  1 292 ? -4.684  44.857  13.509  1.00 31.39  ?  323  ALA C C   1 
ATOM   9637  O  O   . ALA C  1 292 ? -3.969  44.352  14.378  1.00 31.97  ?  323  ALA C O   1 
ATOM   9638  C  CB  . ALA C  1 292 ? -7.013  44.150  12.993  1.00 28.30  ?  323  ALA C CB  1 
ATOM   9639  N  N   . ASN C  1 293 ? -4.770  46.171  13.303  1.00 31.62  ?  324  ASN C N   1 
ATOM   9640  C  CA  . ASN C  1 293 ? -4.044  47.146  14.112  1.00 33.74  ?  324  ASN C CA  1 
ATOM   9641  C  C   . ASN C  1 293 ? -4.976  48.325  14.339  1.00 31.53  ?  324  ASN C C   1 
ATOM   9642  O  O   . ASN C  1 293 ? -5.428  48.941  13.375  1.00 33.29  ?  324  ASN C O   1 
ATOM   9643  C  CB  . ASN C  1 293 ? -2.754  47.598  13.415  1.00 31.77  ?  324  ASN C CB  1 
ATOM   9644  C  CG  . ASN C  1 293 ? -1.855  48.416  14.324  1.00 37.85  ?  324  ASN C CG  1 
ATOM   9645  O  OD1 . ASN C  1 293 ? -2.330  49.154  15.188  1.00 32.60  ?  324  ASN C OD1 1 
ATOM   9646  N  ND2 . ASN C  1 293 ? -0.544  48.263  14.152  1.00 39.37  ?  324  ASN C ND2 1 
ATOM   9647  N  N   . ASN C  1 294 ? -5.284  48.627  15.599  1.00 29.52  ?  325  ASN C N   1 
ATOM   9648  C  CA  . ASN C  1 294 ? -6.204  49.705  15.947  1.00 30.32  ?  325  ASN C CA  1 
ATOM   9649  C  C   . ASN C  1 294 ? -5.490  50.973  16.411  1.00 30.70  ?  325  ASN C C   1 
ATOM   9650  O  O   . ASN C  1 294 ? -6.132  51.863  16.982  1.00 27.12  ?  325  ASN C O   1 
ATOM   9651  C  CB  . ASN C  1 294 ? -7.178  49.237  17.033  1.00 30.73  ?  325  ASN C CB  1 
ATOM   9652  C  CG  . ASN C  1 294 ? -8.149  48.188  16.521  1.00 30.83  ?  325  ASN C CG  1 
ATOM   9653  O  OD1 . ASN C  1 294 ? -8.563  48.244  15.372  1.00 29.91  ?  325  ASN C OD1 1 
ATOM   9654  N  ND2 . ASN C  1 294 ? -8.507  47.224  17.368  1.00 30.82  ?  325  ASN C ND2 1 
ATOM   9655  N  N   . TYR C  1 295 ? -4.187  51.069  16.177  1.00 34.19  ?  326  TYR C N   1 
ATOM   9656  C  CA  . TYR C  1 295 ? -3.408  52.200  16.660  1.00 36.48  ?  326  TYR C CA  1 
ATOM   9657  C  C   . TYR C  1 295 ? -4.039  53.516  16.201  1.00 35.06  ?  326  TYR C C   1 
ATOM   9658  O  O   . TYR C  1 295 ? -4.393  53.650  15.023  1.00 36.45  ?  326  TYR C O   1 
ATOM   9659  C  CB  . TYR C  1 295 ? -1.977  52.083  16.132  1.00 39.01  ?  326  TYR C CB  1 
ATOM   9660  C  CG  . TYR C  1 295 ? -1.094  53.247  16.501  1.00 37.54  ?  326  TYR C CG  1 
ATOM   9661  C  CD1 . TYR C  1 295 ? -1.021  54.384  15.688  1.00 39.18  ?  326  TYR C CD1 1 
ATOM   9662  C  CD2 . TYR C  1 295 ? -0.338  53.213  17.661  1.00 38.10  ?  326  TYR C CD2 1 
ATOM   9663  C  CE1 . TYR C  1 295 ? -0.211  55.454  16.036  1.00 41.42  ?  326  TYR C CE1 1 
ATOM   9664  C  CE2 . TYR C  1 295 ? 0.466   54.270  18.019  1.00 40.82  ?  326  TYR C CE2 1 
ATOM   9665  C  CZ  . TYR C  1 295 ? 0.532   55.384  17.210  1.00 44.98  ?  326  TYR C CZ  1 
ATOM   9666  O  OH  . TYR C  1 295 ? 1.354   56.421  17.592  1.00 48.86  ?  326  TYR C OH  1 
ATOM   9667  N  N   . PRO C  1 296 ? -4.143  54.534  17.078  1.00 35.56  ?  327  PRO C N   1 
ATOM   9668  C  CA  . PRO C  1 296 ? -3.597  54.643  18.448  1.00 32.65  ?  327  PRO C CA  1 
ATOM   9669  C  C   . PRO C  1 296 ? -4.605  54.305  19.539  1.00 33.15  ?  327  PRO C C   1 
ATOM   9670  O  O   . PRO C  1 296 ? -4.444  54.709  20.687  1.00 30.37  ?  327  PRO C O   1 
ATOM   9671  C  CB  . PRO C  1 296 ? -3.218  56.123  18.535  1.00 37.58  ?  327  PRO C CB  1 
ATOM   9672  C  CG  . PRO C  1 296 ? -4.344  56.805  17.736  1.00 34.90  ?  327  PRO C CG  1 
ATOM   9673  C  CD  . PRO C  1 296 ? -4.715  55.820  16.631  1.00 31.86  ?  327  PRO C CD  1 
ATOM   9674  N  N   . LEU C  1 297 ? -5.671  53.588  19.205  1.00 28.59  ?  328  LEU C N   1 
ATOM   9675  C  CA  . LEU C  1 297 ? -6.712  53.303  20.176  1.00 28.14  ?  328  LEU C CA  1 
ATOM   9676  C  C   . LEU C  1 297 ? -6.330  52.110  21.024  1.00 24.85  ?  328  LEU C C   1 
ATOM   9677  O  O   . LEU C  1 297 ? -5.620  51.200  20.568  1.00 30.45  ?  328  LEU C O   1 
ATOM   9678  C  CB  . LEU C  1 297 ? -8.041  53.001  19.458  1.00 27.11  ?  328  LEU C CB  1 
ATOM   9679  C  CG  . LEU C  1 297 ? -8.471  54.082  18.483  1.00 28.44  ?  328  LEU C CG  1 
ATOM   9680  C  CD1 . LEU C  1 297 ? -9.776  53.659  17.774  1.00 28.26  ?  328  LEU C CD1 1 
ATOM   9681  C  CD2 . LEU C  1 297 ? -8.649  55.383  19.226  1.00 29.10  ?  328  LEU C CD2 1 
ATOM   9682  N  N   . LYS C  1 298 ? -6.853  52.090  22.247  1.00 24.81  ?  329  LYS C N   1 
ATOM   9683  C  CA  . LYS C  1 298 ? -6.715  50.928  23.110  1.00 30.45  ?  329  LYS C CA  1 
ATOM   9684  C  C   . LYS C  1 298 ? -7.752  49.884  22.726  1.00 29.63  ?  329  LYS C C   1 
ATOM   9685  O  O   . LYS C  1 298 ? -8.887  50.225  22.381  1.00 31.84  ?  329  LYS C O   1 
ATOM   9686  C  CB  . LYS C  1 298 ? -6.900  51.318  24.581  1.00 29.20  ?  329  LYS C CB  1 
ATOM   9687  C  CG  . LYS C  1 298 ? -6.719  50.174  25.604  1.00 32.16  ?  329  LYS C CG  1 
ATOM   9688  C  CD  . LYS C  1 298 ? -7.015  50.653  27.060  1.00 34.89  ?  329  LYS C CD  1 
ATOM   9689  C  CE  . LYS C  1 298 ? -5.825  51.339  27.707  1.00 35.62  ?  329  LYS C CE  1 
ATOM   9690  N  NZ  . LYS C  1 298 ? -6.153  51.797  29.094  1.00 34.85  ?  329  LYS C NZ  1 
ATOM   9691  N  N   . GLY C  1 299 ? -7.355  48.619  22.777  1.00 31.61  ?  330  GLY C N   1 
ATOM   9692  C  CA  . GLY C  1 299 ? -8.312  47.526  22.763  1.00 30.96  ?  330  GLY C CA  1 
ATOM   9693  C  C   . GLY C  1 299 ? -8.555  46.936  21.384  1.00 30.36  ?  330  GLY C C   1 
ATOM   9694  O  O   . GLY C  1 299 ? -7.852  47.200  20.404  1.00 26.61  ?  330  GLY C O   1 
ATOM   9695  N  N   . THR C  1 300 ? -9.606  46.119  21.315  1.00 27.48  ?  331  THR C N   1 
ATOM   9696  C  CA  . THR C  1 300 ? -9.805  45.243  20.170  1.00 27.73  ?  331  THR C CA  1 
ATOM   9697  C  C   . THR C  1 300 ? -11.304 45.063  19.929  1.00 26.32  ?  331  THR C C   1 
ATOM   9698  O  O   . THR C  1 300 ? -12.134 45.533  20.706  1.00 29.41  ?  331  THR C O   1 
ATOM   9699  C  CB  . THR C  1 300 ? -9.112  43.899  20.416  1.00 30.05  ?  331  THR C CB  1 
ATOM   9700  O  OG1 . THR C  1 300 ? -9.202  43.070  19.250  1.00 30.44  ?  331  THR C OG1 1 
ATOM   9701  C  CG2 . THR C  1 300 ? -9.729  43.190  21.630  1.00 28.52  ?  331  THR C CG2 1 
ATOM   9702  N  N   . LYS C  1 301 ? -11.613 44.326  18.862  1.00 27.93  ?  332  LYS C N   1 
ATOM   9703  C  CA  . LYS C  1 301 ? -13.017 44.033  18.504  1.00 28.44  ?  332  LYS C CA  1 
ATOM   9704  C  C   . LYS C  1 301 ? -13.725 43.555  19.777  1.00 27.40  ?  332  LYS C C   1 
ATOM   9705  O  O   . LYS C  1 301 ? -13.157 42.707  20.489  1.00 26.89  ?  332  LYS C O   1 
ATOM   9706  C  CB  . LYS C  1 301 ? -13.064 42.929  17.440  1.00 27.47  ?  332  LYS C CB  1 
ATOM   9707  C  CG  . LYS C  1 301 ? -14.400 42.268  17.139  1.00 26.28  ?  332  LYS C CG  1 
ATOM   9708  C  CD  . LYS C  1 301 ? -14.255 41.076  16.202  1.00 25.75  ?  332  LYS C CD  1 
ATOM   9709  C  CE  . LYS C  1 301 ? -15.539 40.429  15.797  1.00 34.23  ?  332  LYS C CE  1 
ATOM   9710  N  NZ  . LYS C  1 301 ? -15.306 39.268  14.937  1.00 32.79  ?  332  LYS C NZ  1 
ATOM   9711  N  N   . GLY C  1 302 ? -14.915 44.070  20.021  1.00 27.50  ?  333  GLY C N   1 
ATOM   9712  C  CA  . GLY C  1 302 ? -15.704 43.638  21.177  1.00 25.14  ?  333  GLY C CA  1 
ATOM   9713  C  C   . GLY C  1 302 ? -15.547 44.480  22.440  1.00 32.17  ?  333  GLY C C   1 
ATOM   9714  O  O   . GLY C  1 302 ? -16.386 44.368  23.352  1.00 24.56  ?  333  GLY C O   1 
ATOM   9715  N  N   . ASP C  1 303 ? -14.495 45.304  22.536  1.00 28.43  ?  334  ASP C N   1 
ATOM   9716  C  CA  . ASP C  1 303 ? -14.297 46.127  23.724  1.00 29.03  ?  334  ASP C CA  1 
ATOM   9717  C  C   . ASP C  1 303 ? -15.148 47.401  23.684  1.00 30.66  ?  334  ASP C C   1 
ATOM   9718  O  O   . ASP C  1 303 ? -15.611 47.849  22.627  1.00 29.27  ?  334  ASP C O   1 
ATOM   9719  C  CB  . ASP C  1 303 ? -12.824 46.541  23.879  1.00 28.77  ?  334  ASP C CB  1 
ATOM   9720  C  CG  . ASP C  1 303 ? -11.897 45.371  24.133  1.00 31.30  ?  334  ASP C CG  1 
ATOM   9721  O  OD1 . ASP C  1 303 ? -12.350 44.287  24.579  1.00 26.68  ?  334  ASP C OD1 1 
ATOM   9722  O  OD2 . ASP C  1 303 ? -10.681 45.552  23.898  1.00 28.80  -1 334  ASP C OD2 1 
ATOM   9723  N  N   . THR C  1 304 ? -15.307 48.025  24.857  1.00 30.38  ?  335  THR C N   1 
ATOM   9724  C  CA  . THR C  1 304 ? -15.819 49.388  24.910  1.00 30.63  ?  335  THR C CA  1 
ATOM   9725  C  C   . THR C  1 304 ? -14.724 50.419  25.163  1.00 33.76  ?  335  THR C C   1 
ATOM   9726  O  O   . THR C  1 304 ? -15.034 51.603  25.314  1.00 31.76  ?  335  THR C O   1 
ATOM   9727  C  CB  . THR C  1 304 ? -16.936 49.525  25.943  1.00 30.92  ?  335  THR C CB  1 
ATOM   9728  O  OG1 . THR C  1 304 ? -16.457 49.197  27.255  1.00 32.58  ?  335  THR C OG1 1 
ATOM   9729  C  CG2 . THR C  1 304 ? -18.097 48.594  25.561  1.00 30.94  ?  335  THR C CG2 1 
ATOM   9730  N  N   . TRP C  1 305 ? -13.451 50.002  25.171  1.00 31.43  ?  336  TRP C N   1 
ATOM   9731  C  CA  . TRP C  1 305 ? -12.380 50.919  24.785  1.00 33.45  ?  336  TRP C CA  1 
ATOM   9732  C  C   . TRP C  1 305 ? -12.686 51.438  23.390  1.00 33.21  ?  336  TRP C C   1 
ATOM   9733  O  O   . TRP C  1 305 ? -13.441 50.793  22.650  1.00 33.23  ?  336  TRP C O   1 
ATOM   9734  C  CB  . TRP C  1 305 ? -11.003 50.236  24.766  1.00 30.91  ?  336  TRP C CB  1 
ATOM   9735  C  CG  . TRP C  1 305 ? -10.566 49.551  26.042  1.00 27.63  ?  336  TRP C CG  1 
ATOM   9736  C  CD1 . TRP C  1 305 ? -10.320 48.218  26.210  1.00 30.83  ?  336  TRP C CD1 1 
ATOM   9737  C  CD2 . TRP C  1 305 ? -10.284 50.172  27.307  1.00 31.94  ?  336  TRP C CD2 1 
ATOM   9738  N  NE1 . TRP C  1 305 ? -9.909  47.967  27.508  1.00 28.35  ?  336  TRP C NE1 1 
ATOM   9739  C  CE2 . TRP C  1 305 ? -9.882  49.152  28.197  1.00 28.00  ?  336  TRP C CE2 1 
ATOM   9740  C  CE3 . TRP C  1 305 ? -10.327 51.494  27.772  1.00 32.83  ?  336  TRP C CE3 1 
ATOM   9741  C  CZ2 . TRP C  1 305 ? -9.532  49.411  29.522  1.00 32.07  ?  336  TRP C CZ2 1 
ATOM   9742  C  CZ3 . TRP C  1 305 ? -9.989  51.747  29.096  1.00 29.86  ?  336  TRP C CZ3 1 
ATOM   9743  C  CH2 . TRP C  1 305 ? -9.591  50.713  29.950  1.00 32.23  ?  336  TRP C CH2 1 
ATOM   9744  N  N   . GLU C  1 306 ? -12.076 52.563  22.997  1.00 30.06  ?  337  GLU C N   1 
ATOM   9745  C  CA  . GLU C  1 306 ? -12.271 53.089  21.643  1.00 32.81  ?  337  GLU C CA  1 
ATOM   9746  C  C   . GLU C  1 306 ? -12.005 52.040  20.573  1.00 29.52  ?  337  GLU C C   1 
ATOM   9747  O  O   . GLU C  1 306 ? -12.714 51.980  19.559  1.00 32.57  ?  337  GLU C O   1 
ATOM   9748  C  CB  . GLU C  1 306 ? -11.362 54.303  21.405  1.00 32.09  ?  337  GLU C CB  1 
ATOM   9749  C  CG  . GLU C  1 306 ? -11.648 55.466  22.352  1.00 33.06  ?  337  GLU C CG  1 
ATOM   9750  C  CD  . GLU C  1 306 ? -12.957 56.157  22.055  1.00 35.63  ?  337  GLU C CD  1 
ATOM   9751  O  OE1 . GLU C  1 306 ? -12.983 57.033  21.161  1.00 36.70  ?  337  GLU C OE1 1 
ATOM   9752  O  OE2 . GLU C  1 306 ? -13.967 55.830  22.733  1.00 37.70  -1 337  GLU C OE2 1 
ATOM   9753  N  N   . GLY C  1 307 ? -10.972 51.220  20.761  1.00 26.98  ?  338  GLY C N   1 
ATOM   9754  C  CA  . GLY C  1 307 ? -10.568 50.296  19.718  1.00 26.16  ?  338  GLY C CA  1 
ATOM   9755  C  C   . GLY C  1 307 ? -11.657 49.316  19.311  1.00 29.29  ?  338  GLY C C   1 
ATOM   9756  O  O   . GLY C  1 307 ? -11.579 48.728  18.228  1.00 28.83  ?  338  GLY C O   1 
ATOM   9757  N  N   . GLY C  1 308 ? -12.663 49.124  20.164  1.00 29.71  ?  339  GLY C N   1 
ATOM   9758  C  CA  . GLY C  1 308 ? -13.720 48.173  19.869  1.00 29.18  ?  339  GLY C CA  1 
ATOM   9759  C  C   . GLY C  1 308 ? -14.783 48.704  18.936  1.00 28.27  ?  339  GLY C C   1 
ATOM   9760  O  O   . GLY C  1 308 ? -15.393 47.923  18.193  1.00 28.38  ?  339  GLY C O   1 
ATOM   9761  N  N   . TYR C  1 309 ? -15.048 50.026  18.954  1.00 26.20  ?  340  TYR C N   1 
ATOM   9762  C  CA  . TYR C  1 309 ? -16.161 50.514  18.136  1.00 34.09  ?  340  TYR C CA  1 
ATOM   9763  C  C   . TYR C  1 309 ? -15.939 51.884  17.501  1.00 34.88  ?  340  TYR C C   1 
ATOM   9764  O  O   . TYR C  1 309 ? -16.869 52.419  16.879  1.00 34.18  ?  340  TYR C O   1 
ATOM   9765  C  CB  . TYR C  1 309 ? -17.472 50.532  18.945  1.00 29.28  ?  340  TYR C CB  1 
ATOM   9766  C  CG  . TYR C  1 309 ? -17.505 51.439  20.151  1.00 32.48  ?  340  TYR C CG  1 
ATOM   9767  C  CD1 . TYR C  1 309 ? -16.745 51.160  21.273  1.00 32.45  ?  340  TYR C CD1 1 
ATOM   9768  C  CD2 . TYR C  1 309 ? -18.322 52.553  20.180  1.00 34.17  ?  340  TYR C CD2 1 
ATOM   9769  C  CE1 . TYR C  1 309 ? -16.790 51.973  22.373  1.00 33.85  ?  340  TYR C CE1 1 
ATOM   9770  C  CE2 . TYR C  1 309 ? -18.370 53.373  21.276  1.00 32.22  ?  340  TYR C CE2 1 
ATOM   9771  C  CZ  . TYR C  1 309 ? -17.595 53.077  22.369  1.00 36.29  ?  340  TYR C CZ  1 
ATOM   9772  O  OH  . TYR C  1 309 ? -17.630 53.869  23.484  1.00 37.26  ?  340  TYR C OH  1 
ATOM   9773  N  N   . ARG C  1 310 ? -14.745 52.455  17.604  1.00 34.29  ?  341  ARG C N   1 
ATOM   9774  C  CA  . ARG C  1 310 ? -14.392 53.644  16.833  1.00 32.34  ?  341  ARG C CA  1 
ATOM   9775  C  C   . ARG C  1 310 ? -13.762 53.177  15.532  1.00 30.45  ?  341  ARG C C   1 
ATOM   9776  O  O   . ARG C  1 310 ? -12.848 52.354  15.553  1.00 31.48  ?  341  ARG C O   1 
ATOM   9777  C  CB  . ARG C  1 310 ? -13.425 54.528  17.631  1.00 34.79  ?  341  ARG C CB  1 
ATOM   9778  C  CG  . ARG C  1 310 ? -13.156 55.911  17.047  1.00 32.48  ?  341  ARG C CG  1 
ATOM   9779  C  CD  . ARG C  1 310 ? -12.312 56.699  18.067  1.00 34.52  ?  341  ARG C CD  1 
ATOM   9780  N  NE  . ARG C  1 310 ? -11.612 57.845  17.495  1.00 37.62  ?  341  ARG C NE  1 
ATOM   9781  C  CZ  . ARG C  1 310 ? -11.249 58.905  18.207  1.00 34.81  ?  341  ARG C CZ  1 
ATOM   9782  N  NH1 . ARG C  1 310 ? -11.526 58.994  19.500  1.00 31.81  ?  341  ARG C NH1 1 
ATOM   9783  N  NH2 . ARG C  1 310 ? -10.595 59.897  17.611  1.00 30.09  ?  341  ARG C NH2 1 
ATOM   9784  N  N   . VAL C  1 311 ? -14.274 53.658  14.400  1.00 32.31  ?  342  VAL C N   1 
ATOM   9785  C  CA  . VAL C  1 311 ? -13.928 53.032  13.124  1.00 31.63  ?  342  VAL C CA  1 
ATOM   9786  C  C   . VAL C  1 311 ? -13.524 54.115  12.138  1.00 29.32  ?  342  VAL C C   1 
ATOM   9787  O  O   . VAL C  1 311 ? -13.879 55.293  12.310  1.00 32.24  ?  342  VAL C O   1 
ATOM   9788  C  CB  . VAL C  1 311 ? -15.102 52.193  12.563  1.00 33.00  ?  342  VAL C CB  1 
ATOM   9789  C  CG1 . VAL C  1 311 ? -15.428 51.027  13.513  1.00 30.74  ?  342  VAL C CG1 1 
ATOM   9790  C  CG2 . VAL C  1 311 ? -16.350 53.099  12.308  1.00 27.53  ?  342  VAL C CG2 1 
ATOM   9791  N  N   . PRO C  1 312 ? -12.768 53.758  11.099  1.00 26.29  ?  343  PRO C N   1 
ATOM   9792  C  CA  . PRO C  1 312 ? -12.551 54.717  10.015  1.00 26.40  ?  343  PRO C CA  1 
ATOM   9793  C  C   . PRO C  1 312 ? -13.852 54.913  9.268   1.00 35.77  ?  343  PRO C C   1 
ATOM   9794  O  O   . PRO C  1 312 ? -14.641 53.975  9.121   1.00 33.06  ?  343  PRO C O   1 
ATOM   9795  C  CB  . PRO C  1 312 ? -11.494 54.050  9.130   1.00 28.18  ?  343  PRO C CB  1 
ATOM   9796  C  CG  . PRO C  1 312 ? -11.515 52.608  9.508   1.00 35.80  ?  343  PRO C CG  1 
ATOM   9797  C  CD  . PRO C  1 312 ? -12.056 52.487  10.879  1.00 32.74  ?  343  PRO C CD  1 
ATOM   9798  N  N   . MET C  1 313 ? -14.074 56.150  8.827   1.00 34.62  ?  344  MET C N   1 
ATOM   9799  C  CA  . MET C  1 313 ? -15.196 56.521  7.977   1.00 34.46  ?  344  MET C CA  1 
ATOM   9800  C  C   . MET C  1 313 ? -14.771 57.640  7.046   1.00 37.66  ?  344  MET C C   1 
ATOM   9801  O  O   . MET C  1 313 ? -14.010 58.524  7.441   1.00 33.56  ?  344  MET C O   1 
ATOM   9802  C  CB  . MET C  1 313 ? -16.406 57.060  8.742   1.00 34.29  ?  344  MET C CB  1 
ATOM   9803  C  CG  . MET C  1 313 ? -17.676 57.143  7.853   1.00 33.44  ?  344  MET C CG  1 
ATOM   9804  S  SD  . MET C  1 313 ? -19.142 56.755  8.764   1.00 35.36  ?  344  MET C SD  1 
ATOM   9805  C  CE  . MET C  1 313 ? -19.348 58.214  9.773   1.00 37.11  ?  344  MET C CE  1 
ATOM   9806  N  N   . PHE C  1 314 ? -15.317 57.630  5.831   1.00 36.80  ?  345  PHE C N   1 
ATOM   9807  C  CA  . PHE C  1 314 ? -15.327 58.825  5.005   1.00 35.97  ?  345  PHE C CA  1 
ATOM   9808  C  C   . PHE C  1 314 ? -16.646 58.904  4.255   1.00 42.71  ?  345  PHE C C   1 
ATOM   9809  O  O   . PHE C  1 314 ? -17.312 57.888  4.020   1.00 36.91  ?  345  PHE C O   1 
ATOM   9810  C  CB  . PHE C  1 314 ? -14.119 58.914  4.032   1.00 33.56  ?  345  PHE C CB  1 
ATOM   9811  C  CG  . PHE C  1 314 ? -14.099 57.900  2.920   1.00 35.56  ?  345  PHE C CG  1 
ATOM   9812  C  CD1 . PHE C  1 314 ? -15.047 57.923  1.881   1.00 38.20  ?  345  PHE C CD1 1 
ATOM   9813  C  CD2 . PHE C  1 314 ? -13.085 56.957  2.873   1.00 33.96  ?  345  PHE C CD2 1 
ATOM   9814  C  CE1 . PHE C  1 314 ? -14.999 56.995  0.853   1.00 34.29  ?  345  PHE C CE1 1 
ATOM   9815  C  CE2 . PHE C  1 314 ? -13.014 56.021  1.857   1.00 28.75  ?  345  PHE C CE2 1 
ATOM   9816  C  CZ  . PHE C  1 314 ? -13.980 56.037  0.823   1.00 31.39  ?  345  PHE C CZ  1 
ATOM   9817  N  N   . PHE C  1 315 ? -17.033 60.140  3.942   1.00 41.78  ?  346  PHE C N   1 
ATOM   9818  C  CA  . PHE C  1 315 ? -18.072 60.459  2.972   1.00 34.52  ?  346  PHE C CA  1 
ATOM   9819  C  C   . PHE C  1 315 ? -17.384 61.004  1.731   1.00 41.05  ?  346  PHE C C   1 
ATOM   9820  O  O   . PHE C  1 315 ? -16.445 61.800  1.831   1.00 39.32  ?  346  PHE C O   1 
ATOM   9821  C  CB  . PHE C  1 315 ? -19.044 61.529  3.487   1.00 33.45  ?  346  PHE C CB  1 
ATOM   9822  C  CG  . PHE C  1 315 ? -19.998 61.057  4.539   1.00 38.60  ?  346  PHE C CG  1 
ATOM   9823  C  CD1 . PHE C  1 315 ? -19.848 59.821  5.152   1.00 36.33  ?  346  PHE C CD1 1 
ATOM   9824  C  CD2 . PHE C  1 315 ? -21.066 61.864  4.914   1.00 35.63  ?  346  PHE C CD2 1 
ATOM   9825  C  CE1 . PHE C  1 315 ? -20.739 59.407  6.125   1.00 36.60  ?  346  PHE C CE1 1 
ATOM   9826  C  CE2 . PHE C  1 315 ? -21.961 61.460  5.889   1.00 36.59  ?  346  PHE C CE2 1 
ATOM   9827  C  CZ  . PHE C  1 315 ? -21.805 60.227  6.492   1.00 35.28  ?  346  PHE C CZ  1 
ATOM   9828  N  N   . HIS C  1 316 ? -17.849 60.593  0.559   1.00 38.98  ?  347  HIS C N   1 
ATOM   9829  C  CA  . HIS C  1 316 ? -17.295 61.106  -0.682  1.00 38.73  ?  347  HIS C CA  1 
ATOM   9830  C  C   . HIS C  1 316 ? -18.453 61.386  -1.620  1.00 42.88  ?  347  HIS C C   1 
ATOM   9831  O  O   . HIS C  1 316 ? -19.174 60.463  -2.005  1.00 37.04  ?  347  HIS C O   1 
ATOM   9832  C  CB  . HIS C  1 316 ? -16.317 60.119  -1.307  1.00 35.16  ?  347  HIS C CB  1 
ATOM   9833  C  CG  . HIS C  1 316 ? -15.944 60.453  -2.717  1.00 39.00  ?  347  HIS C CG  1 
ATOM   9834  N  ND1 . HIS C  1 316 ? -14.878 61.264  -3.040  1.00 44.94  ?  347  HIS C ND1 1 
ATOM   9835  C  CD2 . HIS C  1 316 ? -16.513 60.097  -3.892  1.00 41.74  ?  347  HIS C CD2 1 
ATOM   9836  C  CE1 . HIS C  1 316 ? -14.789 61.369  -4.354  1.00 46.63  ?  347  HIS C CE1 1 
ATOM   9837  N  NE2 . HIS C  1 316 ? -15.771 60.671  -4.894  1.00 43.00  ?  347  HIS C NE2 1 
ATOM   9838  N  N   . TRP C  1 317 ? -18.630 62.649  -1.972  1.00 38.72  ?  348  TRP C N   1 
ATOM   9839  C  CA  . TRP C  1 317 ? -19.794 63.082  -2.727  1.00 41.32  ?  348  TRP C CA  1 
ATOM   9840  C  C   . TRP C  1 317 ? -19.415 64.356  -3.468  1.00 43.66  ?  348  TRP C C   1 
ATOM   9841  O  O   . TRP C  1 317 ? -19.614 65.459  -2.942  1.00 43.53  ?  348  TRP C O   1 
ATOM   9842  C  CB  . TRP C  1 317 ? -20.989 63.312  -1.797  1.00 40.81  ?  348  TRP C CB  1 
ATOM   9843  C  CG  . TRP C  1 317 ? -22.245 63.691  -2.526  1.00 42.54  ?  348  TRP C CG  1 
ATOM   9844  C  CD1 . TRP C  1 317 ? -22.497 63.558  -3.875  1.00 40.27  ?  348  TRP C CD1 1 
ATOM   9845  C  CD2 . TRP C  1 317 ? -23.423 64.262  -1.953  1.00 41.69  ?  348  TRP C CD2 1 
ATOM   9846  N  NE1 . TRP C  1 317 ? -23.754 64.017  -4.162  1.00 43.40  ?  348  TRP C NE1 1 
ATOM   9847  C  CE2 . TRP C  1 317 ? -24.347 64.451  -3.002  1.00 41.65  ?  348  TRP C CE2 1 
ATOM   9848  C  CE3 . TRP C  1 317 ? -23.786 64.636  -0.653  1.00 41.57  ?  348  TRP C CE3 1 
ATOM   9849  C  CZ2 . TRP C  1 317 ? -25.607 64.993  -2.791  1.00 38.47  ?  348  TRP C CZ2 1 
ATOM   9850  C  CZ3 . TRP C  1 317 ? -25.041 65.175  -0.445  1.00 47.04  ?  348  TRP C CZ3 1 
ATOM   9851  C  CH2 . TRP C  1 317 ? -25.940 65.350  -1.516  1.00 41.67  ?  348  TRP C CH2 1 
ATOM   9852  N  N   . PRO C  1 318 ? -18.858 64.242  -4.676  1.00 40.25  ?  349  PRO C N   1 
ATOM   9853  C  CA  . PRO C  1 318 ? -18.209 65.411  -5.289  1.00 43.93  ?  349  PRO C CA  1 
ATOM   9854  C  C   . PRO C  1 318 ? -19.130 66.605  -5.467  1.00 50.16  ?  349  PRO C C   1 
ATOM   9855  O  O   . PRO C  1 318 ? -18.672 67.746  -5.319  1.00 43.88  ?  349  PRO C O   1 
ATOM   9856  C  CB  . PRO C  1 318 ? -17.709 64.860  -6.630  1.00 43.76  ?  349  PRO C CB  1 
ATOM   9857  C  CG  . PRO C  1 318 ? -17.483 63.389  -6.364  1.00 43.85  ?  349  PRO C CG  1 
ATOM   9858  C  CD  . PRO C  1 318 ? -18.622 63.006  -5.443  1.00 38.86  ?  349  PRO C CD  1 
ATOM   9859  N  N   . LYS C  1 319 ? -20.419 66.385  -5.750  1.00 46.62  ?  350  LYS C N   1 
ATOM   9860  C  CA  . LYS C  1 319 ? -21.325 67.513  -5.943  1.00 49.63  ?  350  LYS C CA  1 
ATOM   9861  C  C   . LYS C  1 319 ? -21.360 68.446  -4.742  1.00 50.74  ?  350  LYS C C   1 
ATOM   9862  O  O   . LYS C  1 319 ? -21.580 69.652  -4.906  1.00 52.05  ?  350  LYS C O   1 
ATOM   9863  C  CB  . LYS C  1 319 ? -22.746 67.023  -6.226  1.00 50.57  ?  350  LYS C CB  1 
ATOM   9864  C  CG  . LYS C  1 319 ? -23.641 68.106  -6.838  1.00 57.56  ?  350  LYS C CG  1 
ATOM   9865  C  CD  . LYS C  1 319 ? -25.076 67.969  -6.353  1.00 55.46  ?  350  LYS C CD  1 
ATOM   9866  C  CE  . LYS C  1 319 ? -25.716 66.766  -6.956  1.00 49.30  ?  350  LYS C CE  1 
ATOM   9867  N  NZ  . LYS C  1 319 ? -27.067 66.480  -6.379  1.00 58.39  ?  350  LYS C NZ  1 
ATOM   9868  N  N   . LYS C  1 320 ? -21.180 67.917  -3.532  1.00 45.23  ?  351  LYS C N   1 
ATOM   9869  C  CA  . LYS C  1 320 ? -21.495 68.722  -2.354  1.00 47.49  ?  351  LYS C CA  1 
ATOM   9870  C  C   . LYS C  1 320 ? -20.392 68.762  -1.306  1.00 48.31  ?  351  LYS C C   1 
ATOM   9871  O  O   . LYS C  1 320 ? -20.255 69.763  -0.599  1.00 50.66  ?  351  LYS C O   1 
ATOM   9872  C  CB  . LYS C  1 320 ? -22.789 68.235  -1.689  1.00 46.89  ?  351  LYS C CB  1 
ATOM   9873  C  CG  . LYS C  1 320 ? -24.030 68.286  -2.588  1.00 49.78  ?  351  LYS C CG  1 
ATOM   9874  C  CD  . LYS C  1 320 ? -24.924 69.449  -2.183  1.00 48.87  ?  351  LYS C CD  1 
ATOM   9875  C  CE  . LYS C  1 320 ? -26.068 69.662  -3.176  1.00 59.07  ?  351  LYS C CE  1 
ATOM   9876  N  NZ  . LYS C  1 320 ? -27.409 69.526  -2.536  1.00 58.90  ?  351  LYS C NZ  1 
ATOM   9877  N  N   . ILE C  1 321 ? -19.623 67.691  -1.166  1.00 48.74  ?  352  ILE C N   1 
ATOM   9878  C  CA  . ILE C  1 321 ? -18.621 67.607  -0.108  1.00 41.61  ?  352  ILE C CA  1 
ATOM   9879  C  C   . ILE C  1 321 ? -17.296 68.103  -0.667  1.00 43.79  ?  352  ILE C C   1 
ATOM   9880  O  O   . ILE C  1 321 ? -16.800 67.569  -1.664  1.00 47.25  ?  352  ILE C O   1 
ATOM   9881  C  CB  . ILE C  1 321 ? -18.492 66.172  0.435   1.00 44.64  ?  352  ILE C CB  1 
ATOM   9882  C  CG1 . ILE C  1 321 ? -19.862 65.629  0.860   1.00 45.23  ?  352  ILE C CG1 1 
ATOM   9883  C  CG2 . ILE C  1 321 ? -17.492 66.117  1.622   1.00 41.90  ?  352  ILE C CG2 1 
ATOM   9884  C  CD1 . ILE C  1 321 ? -20.235 65.833  2.297   1.00 45.98  ?  352  ILE C CD1 1 
ATOM   9885  N  N   . LYS C  1 322 ? -16.719 69.119  -0.020  1.00 47.47  ?  353  LYS C N   1 
ATOM   9886  C  CA  . LYS C  1 322 ? -15.418 69.646  -0.422  1.00 53.44  ?  353  LYS C CA  1 
ATOM   9887  C  C   . LYS C  1 322 ? -14.320 68.598  -0.235  1.00 51.16  ?  353  LYS C C   1 
ATOM   9888  O  O   . LYS C  1 322 ? -14.433 67.672  0.573   1.00 47.00  ?  353  LYS C O   1 
ATOM   9889  C  CB  . LYS C  1 322 ? -15.064 70.899  0.387   1.00 51.18  ?  353  LYS C CB  1 
ATOM   9890  N  N   . LYS C  1 323 ? -13.242 68.762  -0.998  1.00 46.80  ?  354  LYS C N   1 
ATOM   9891  C  CA  . LYS C  1 323 ? -12.105 67.864  -0.912  1.00 47.51  ?  354  LYS C CA  1 
ATOM   9892  C  C   . LYS C  1 323 ? -11.288 68.128  0.356   1.00 51.83  ?  354  LYS C C   1 
ATOM   9893  O  O   . LYS C  1 323 ? -11.415 69.168  1.009   1.00 51.03  ?  354  LYS C O   1 
ATOM   9894  C  CB  . LYS C  1 323 ? -11.203 68.028  -2.132  1.00 51.50  ?  354  LYS C CB  1 
ATOM   9895  C  CG  . LYS C  1 323 ? -11.847 67.654  -3.443  1.00 54.99  ?  354  LYS C CG  1 
ATOM   9896  C  CD  . LYS C  1 323 ? -10.866 67.829  -4.591  1.00 53.87  ?  354  LYS C CD  1 
ATOM   9897  C  CE  . LYS C  1 323 ? -11.596 67.934  -5.917  1.00 53.13  ?  354  LYS C CE  1 
ATOM   9898  N  NZ  . LYS C  1 323 ? -11.844 66.584  -6.504  1.00 54.13  ?  354  LYS C NZ  1 
ATOM   9899  N  N   . ASP C  1 324 ? -10.458 67.137  0.702   1.00 47.60  ?  355  ASP C N   1 
ATOM   9900  C  CA  . ASP C  1 324 ? -9.430  67.227  1.747   1.00 50.92  ?  355  ASP C CA  1 
ATOM   9901  C  C   . ASP C  1 324 ? -9.980  67.783  3.058   1.00 49.83  ?  355  ASP C C   1 
ATOM   9902  O  O   . ASP C  1 324 ? -9.305  68.524  3.782   1.00 50.10  ?  355  ASP C O   1 
ATOM   9903  C  CB  . ASP C  1 324 ? -8.226  68.037  1.255   1.00 52.78  ?  355  ASP C CB  1 
ATOM   9904  C  CG  . ASP C  1 324 ? -6.898  67.350  1.566   1.00 64.23  ?  355  ASP C CG  1 
ATOM   9905  O  OD1 . ASP C  1 324 ? -6.637  67.026  2.749   1.00 60.70  -1 355  ASP C OD1 1 
ATOM   9906  O  OD2 . ASP C  1 324 ? -6.130  67.091  0.612   1.00 69.17  ?  355  ASP C OD2 1 
ATOM   9907  N  N   . GLN C  1 325 ? -11.195 67.377  3.394   1.00 43.22  ?  356  GLN C N   1 
ATOM   9908  C  CA  . GLN C  1 325 ? -11.865 67.824  4.605   1.00 43.35  ?  356  GLN C CA  1 
ATOM   9909  C  C   . GLN C  1 325 ? -11.715 66.772  5.703   1.00 47.83  ?  356  GLN C C   1 
ATOM   9910  O  O   . GLN C  1 325 ? -11.641 65.565  5.427   1.00 39.60  ?  356  GLN C O   1 
ATOM   9911  C  CB  . GLN C  1 325 ? -13.342 68.100  4.320   1.00 47.48  ?  356  GLN C CB  1 
ATOM   9912  C  CG  . GLN C  1 325 ? -14.303 67.684  5.417   1.00 50.08  ?  356  GLN C CG  1 
ATOM   9913  C  CD  . GLN C  1 325 ? -15.715 68.211  5.187   1.00 57.99  ?  356  GLN C CD  1 
ATOM   9914  O  OE1 . GLN C  1 325 ? -16.051 68.652  4.075   1.00 58.76  ?  356  GLN C OE1 1 
ATOM   9915  N  NE2 . GLN C  1 325 ? -16.553 68.169  6.236   1.00 46.93  ?  356  GLN C NE2 1 
ATOM   9916  N  N   . ARG C  1 326 ? -11.633 67.255  6.950   1.00 44.50  ?  357  ARG C N   1 
ATOM   9917  C  CA  . ARG C  1 326 ? -11.569 66.420  8.147   1.00 46.50  ?  357  ARG C CA  1 
ATOM   9918  C  C   . ARG C  1 326 ? -12.668 66.837  9.115   1.00 44.09  ?  357  ARG C C   1 
ATOM   9919  O  O   . ARG C  1 326 ? -12.693 67.983  9.571   1.00 43.56  ?  357  ARG C O   1 
ATOM   9920  C  CB  . ARG C  1 326 ? -10.205 66.538  8.828   1.00 49.81  ?  357  ARG C CB  1 
ATOM   9921  C  CG  . ARG C  1 326 ? -9.238  65.529  8.291   1.00 53.35  ?  357  ARG C CG  1 
ATOM   9922  C  CD  . ARG C  1 326 ? -7.835  65.770  8.753   1.00 56.81  ?  357  ARG C CD  1 
ATOM   9923  N  NE  . ARG C  1 326 ? -7.613  65.007  9.969   1.00 57.04  ?  357  ARG C NE  1 
ATOM   9924  C  CZ  . ARG C  1 326 ? -6.990  63.837  9.992   1.00 63.52  ?  357  ARG C CZ  1 
ATOM   9925  N  NH1 . ARG C  1 326 ? -6.606  63.240  8.874   1.00 61.52  ?  357  ARG C NH1 1 
ATOM   9926  N  NH2 . ARG C  1 326 ? -6.771  63.238  11.161  1.00 63.20  ?  357  ARG C NH2 1 
ATOM   9927  N  N   . PHE C  1 327 ? -13.568 65.909  9.438   1.00 39.79  ?  358  PHE C N   1 
ATOM   9928  C  CA  . PHE C  1 327 ? -14.683 66.177  10.345  1.00 43.10  ?  358  PHE C CA  1 
ATOM   9929  C  C   . PHE C  1 327 ? -14.378 65.506  11.684  1.00 44.31  ?  358  PHE C C   1 
ATOM   9930  O  O   . PHE C  1 327 ? -14.421 64.274  11.792  1.00 40.66  ?  358  PHE C O   1 
ATOM   9931  C  CB  . PHE C  1 327 ? -16.000 65.686  9.736   1.00 41.02  ?  358  PHE C CB  1 
ATOM   9932  C  CG  . PHE C  1 327 ? -17.211 66.124  10.491  1.00 37.62  ?  358  PHE C CG  1 
ATOM   9933  C  CD1 . PHE C  1 327 ? -17.701 65.363  11.539  1.00 38.26  ?  358  PHE C CD1 1 
ATOM   9934  C  CD2 . PHE C  1 327 ? -17.850 67.307  10.169  1.00 36.45  ?  358  PHE C CD2 1 
ATOM   9935  C  CE1 . PHE C  1 327 ? -18.818 65.780  12.263  1.00 37.70  ?  358  PHE C CE1 1 
ATOM   9936  C  CE2 . PHE C  1 327 ? -18.958 67.726  10.881  1.00 40.81  ?  358  PHE C CE2 1 
ATOM   9937  C  CZ  . PHE C  1 327 ? -19.440 66.966  11.929  1.00 42.01  ?  358  PHE C CZ  1 
ATOM   9938  N  N   . ASP C  1 328 ? -14.056 66.322  12.702  1.00 42.26  ?  359  ASP C N   1 
ATOM   9939  C  CA  . ASP C  1 328 ? -13.526 65.838  13.970  1.00 41.17  ?  359  ASP C CA  1 
ATOM   9940  C  C   . ASP C  1 328 ? -14.572 65.682  15.064  1.00 41.59  ?  359  ASP C C   1 
ATOM   9941  O  O   . ASP C  1 328 ? -14.252 65.119  16.116  1.00 42.63  ?  359  ASP C O   1 
ATOM   9942  C  CB  . ASP C  1 328 ? -12.423 66.773  14.498  1.00 42.98  ?  359  ASP C CB  1 
ATOM   9943  C  CG  . ASP C  1 328 ? -11.279 66.969  13.513  1.00 50.04  ?  359  ASP C CG  1 
ATOM   9944  O  OD1 . ASP C  1 328 ? -10.837 65.982  12.870  1.00 41.46  ?  359  ASP C OD1 1 
ATOM   9945  O  OD2 . ASP C  1 328 ? -10.790 68.120  13.418  1.00 54.18  -1 359  ASP C OD2 1 
ATOM   9946  N  N   . PHE C  1 329 ? -15.795 66.170  14.874  1.00 42.58  ?  360  PHE C N   1 
ATOM   9947  C  CA  . PHE C  1 329 ? -16.798 65.963  15.909  1.00 42.98  ?  360  PHE C CA  1 
ATOM   9948  C  C   . PHE C  1 329 ? -17.295 64.516  15.887  1.00 41.43  ?  360  PHE C C   1 
ATOM   9949  O  O   . PHE C  1 329 ? -17.239 63.849  14.852  1.00 40.87  ?  360  PHE C O   1 
ATOM   9950  C  CB  . PHE C  1 329 ? -17.978 66.913  15.726  1.00 46.14  ?  360  PHE C CB  1 
ATOM   9951  C  CG  . PHE C  1 329 ? -17.606 68.371  15.740  1.00 52.38  ?  360  PHE C CG  1 
ATOM   9952  C  CD1 . PHE C  1 329 ? -17.389 69.035  16.944  1.00 49.77  ?  360  PHE C CD1 1 
ATOM   9953  C  CD2 . PHE C  1 329 ? -17.410 69.064  14.548  1.00 50.69  ?  360  PHE C CD2 1 
ATOM   9954  C  CE1 . PHE C  1 329 ? -17.046 70.373  16.958  1.00 51.37  ?  360  PHE C CE1 1 
ATOM   9955  C  CE2 . PHE C  1 329 ? -17.067 70.411  14.558  1.00 54.94  ?  360  PHE C CE2 1 
ATOM   9956  C  CZ  . PHE C  1 329 ? -16.886 71.063  15.759  1.00 52.42  ?  360  PHE C CZ  1 
ATOM   9957  N  N   . PRO C  1 330 ? -17.803 64.019  17.020  1.00 42.70  ?  361  PRO C N   1 
ATOM   9958  C  CA  . PRO C  1 330 ? -18.251 62.616  17.099  1.00 40.20  ?  361  PRO C CA  1 
ATOM   9959  C  C   . PRO C  1 330 ? -19.538 62.379  16.319  1.00 39.22  ?  361  PRO C C   1 
ATOM   9960  O  O   . PRO C  1 330 ? -20.505 63.137  16.449  1.00 37.23  ?  361  PRO C O   1 
ATOM   9961  C  CB  . PRO C  1 330 ? -18.488 62.404  18.600  1.00 37.44  ?  361  PRO C CB  1 
ATOM   9962  C  CG  . PRO C  1 330 ? -17.800 63.514  19.262  1.00 41.60  ?  361  PRO C CG  1 
ATOM   9963  C  CD  . PRO C  1 330 ? -17.856 64.671  18.335  1.00 40.85  ?  361  PRO C CD  1 
ATOM   9964  N  N   . VAL C  1 331 ? -19.563 61.289  15.545  1.00 37.81  ?  362  VAL C N   1 
ATOM   9965  C  CA  . VAL C  1 331 ? -20.764 60.851  14.830  1.00 36.75  ?  362  VAL C CA  1 
ATOM   9966  C  C   . VAL C  1 331 ? -20.953 59.347  15.033  1.00 39.79  ?  362  VAL C C   1 
ATOM   9967  O  O   . VAL C  1 331 ? -20.062 58.639  15.519  1.00 34.41  ?  362  VAL C O   1 
ATOM   9968  C  CB  . VAL C  1 331 ? -20.704 61.183  13.327  1.00 38.50  ?  362  VAL C CB  1 
ATOM   9969  C  CG1 . VAL C  1 331 ? -20.607 62.691  13.107  1.00 39.78  ?  362  VAL C CG1 1 
ATOM   9970  C  CG2 . VAL C  1 331 ? -19.532 60.445  12.651  1.00 35.20  ?  362  VAL C CG2 1 
ATOM   9971  N  N   . SER C  1 332 ? -22.129 58.860  14.621  1.00 37.07  ?  363  SER C N   1 
ATOM   9972  C  CA  . SER C  1 332 ? -22.526 57.474  14.846  1.00 34.73  ?  363  SER C CA  1 
ATOM   9973  C  C   . SER C  1 332 ? -23.011 56.823  13.558  1.00 36.37  ?  363  SER C C   1 
ATOM   9974  O  O   . SER C  1 332 ? -23.634 57.479  12.714  1.00 33.17  ?  363  SER C O   1 
ATOM   9975  C  CB  . SER C  1 332 ? -23.626 57.388  15.898  1.00 34.21  ?  363  SER C CB  1 
ATOM   9976  O  OG  . SER C  1 332 ? -24.092 56.058  16.013  1.00 35.29  ?  363  SER C OG  1 
ATOM   9977  N  N   . SER C  1 333 ? -22.741 55.511  13.412  1.00 30.79  ?  364  SER C N   1 
ATOM   9978  C  CA  . SER C  1 333 ? -23.358 54.777  12.295  1.00 34.00  ?  364  SER C CA  1 
ATOM   9979  C  C   . SER C  1 333 ? -24.875 54.837  12.357  1.00 35.37  ?  364  SER C C   1 
ATOM   9980  O  O   . SER C  1 333 ? -25.544 54.639  11.331  1.00 33.65  ?  364  SER C O   1 
ATOM   9981  C  CB  . SER C  1 333 ? -22.910 53.308  12.262  1.00 31.63  ?  364  SER C CB  1 
ATOM   9982  O  OG  . SER C  1 333 ? -23.310 52.618  13.451  1.00 32.27  ?  364  SER C OG  1 
ATOM   9983  N  N   . LEU C  1 334 ? -25.434 55.102  13.541  1.00 36.29  ?  365  LEU C N   1 
ATOM   9984  C  CA  . LEU C  1 334 ? -26.865 55.356  13.656  1.00 35.62  ?  365  LEU C CA  1 
ATOM   9985  C  C   . LEU C  1 334 ? -27.302 56.572  12.851  1.00 38.93  ?  365  LEU C C   1 
ATOM   9986  O  O   . LEU C  1 334 ? -28.495 56.721  12.575  1.00 42.95  ?  365  LEU C O   1 
ATOM   9987  C  CB  . LEU C  1 334 ? -27.245 55.539  15.129  1.00 37.19  ?  365  LEU C CB  1 
ATOM   9988  C  CG  . LEU C  1 334 ? -27.171 54.278  15.995  1.00 37.83  ?  365  LEU C CG  1 
ATOM   9989  C  CD1 . LEU C  1 334 ? -27.274 54.596  17.472  1.00 33.45  ?  365  LEU C CD1 1 
ATOM   9990  C  CD2 . LEU C  1 334 ? -28.297 53.319  15.573  1.00 37.06  ?  365  LEU C CD2 1 
ATOM   9991  N  N   . ASP C  1 335 ? -26.369 57.441  12.459  1.00 37.87  ?  366  ASP C N   1 
ATOM   9992  C  CA  . ASP C  1 335 ? -26.744 58.611  11.681  1.00 38.22  ?  366  ASP C CA  1 
ATOM   9993  C  C   . ASP C  1 335 ? -27.051 58.277  10.234  1.00 39.27  ?  366  ASP C C   1 
ATOM   9994  O  O   . ASP C  1 335 ? -27.705 59.078  9.562   1.00 36.67  ?  366  ASP C O   1 
ATOM   9995  C  CB  . ASP C  1 335 ? -25.634 59.656  11.717  1.00 36.76  ?  366  ASP C CB  1 
ATOM   9996  C  CG  . ASP C  1 335 ? -25.313 60.098  13.118  1.00 39.19  ?  366  ASP C CG  1 
ATOM   9997  O  OD1 . ASP C  1 335 ? -26.249 60.108  13.959  1.00 36.83  ?  366  ASP C OD1 1 
ATOM   9998  O  OD2 . ASP C  1 335 ? -24.124 60.422  13.378  1.00 41.01  -1 366  ASP C OD2 1 
ATOM   9999  N  N   . LEU C  1 336 ? -26.580 57.133  9.732   1.00 34.02  ?  367  LEU C N   1 
ATOM   10000 C  CA  . LEU C  1 336 ? -26.728 56.857  8.309   1.00 34.93  ?  367  LEU C CA  1 
ATOM   10001 C  C   . LEU C  1 336 ? -28.203 56.755  7.916   1.00 38.62  ?  367  LEU C C   1 
ATOM   10002 O  O   . LEU C  1 336 ? -28.602 57.272  6.872   1.00 36.33  ?  367  LEU C O   1 
ATOM   10003 C  CB  . LEU C  1 336 ? -25.974 55.583  7.930   1.00 33.48  ?  367  LEU C CB  1 
ATOM   10004 C  CG  . LEU C  1 336 ? -24.452 55.670  8.131   1.00 37.00  ?  367  LEU C CG  1 
ATOM   10005 C  CD1 . LEU C  1 336 ? -23.789 54.417  7.612   1.00 33.99  ?  367  LEU C CD1 1 
ATOM   10006 C  CD2 . LEU C  1 336 ? -23.859 56.921  7.444   1.00 35.22  ?  367  LEU C CD2 1 
ATOM   10007 N  N   . TYR C  1 337 ? -29.028 56.108  8.749   1.00 36.17  ?  368  TYR C N   1 
ATOM   10008 C  CA  . TYR C  1 337 ? -30.447 55.952  8.427   1.00 40.46  ?  368  TYR C CA  1 
ATOM   10009 C  C   . TYR C  1 337 ? -31.147 57.298  8.247   1.00 41.57  ?  368  TYR C C   1 
ATOM   10010 O  O   . TYR C  1 337 ? -31.734 57.529  7.174   1.00 42.00  ?  368  TYR C O   1 
ATOM   10011 C  CB  . TYR C  1 337 ? -31.096 55.072  9.504   1.00 35.84  ?  368  TYR C CB  1 
ATOM   10012 C  CG  . TYR C  1 337 ? -32.471 54.493  9.211   1.00 36.44  ?  368  TYR C CG  1 
ATOM   10013 C  CD1 . TYR C  1 337 ? -33.510 55.282  8.693   1.00 41.88  ?  368  TYR C CD1 1 
ATOM   10014 C  CD2 . TYR C  1 337 ? -32.745 53.155  9.489   1.00 36.35  ?  368  TYR C CD2 1 
ATOM   10015 C  CE1 . TYR C  1 337 ? -34.769 54.739  8.454   1.00 41.14  ?  368  TYR C CE1 1 
ATOM   10016 C  CE2 . TYR C  1 337 ? -34.000 52.612  9.273   1.00 35.76  ?  368  TYR C CE2 1 
ATOM   10017 C  CZ  . TYR C  1 337 ? -35.005 53.400  8.752   1.00 42.41  ?  368  TYR C CZ  1 
ATOM   10018 O  OH  . TYR C  1 337 ? -36.242 52.838  8.530   1.00 36.19  ?  368  TYR C OH  1 
ATOM   10019 N  N   . PRO C  1 338 ? -31.128 58.223  9.219   1.00 39.98  ?  369  PRO C N   1 
ATOM   10020 C  CA  . PRO C  1 338 ? -31.772 59.528  8.965   1.00 39.74  ?  369  PRO C CA  1 
ATOM   10021 C  C   . PRO C  1 338 ? -31.079 60.344  7.886   1.00 41.26  ?  369  PRO C C   1 
ATOM   10022 O  O   . PRO C  1 338 ? -31.753 61.035  7.111   1.00 42.98  ?  369  PRO C O   1 
ATOM   10023 C  CB  . PRO C  1 338 ? -31.724 60.223  10.336  1.00 41.25  ?  369  PRO C CB  1 
ATOM   10024 C  CG  . PRO C  1 338 ? -30.608 59.548  11.074  1.00 39.01  ?  369  PRO C CG  1 
ATOM   10025 C  CD  . PRO C  1 338 ? -30.609 58.129  10.597  1.00 41.97  ?  369  PRO C CD  1 
ATOM   10026 N  N   . THR C  1 339 ? -29.750 60.271  7.792   1.00 39.13  ?  370  THR C N   1 
ATOM   10027 C  CA  . THR C  1 339 ? -29.037 60.996  6.744   1.00 39.45  ?  370  THR C CA  1 
ATOM   10028 C  C   . THR C  1 339 ? -29.429 60.502  5.351   1.00 42.49  ?  370  THR C C   1 
ATOM   10029 O  O   . THR C  1 339 ? -29.663 61.310  4.443   1.00 40.75  ?  370  THR C O   1 
ATOM   10030 C  CB  . THR C  1 339 ? -27.528 60.863  6.962   1.00 39.78  ?  370  THR C CB  1 
ATOM   10031 O  OG1 . THR C  1 339 ? -27.194 61.412  8.244   1.00 42.26  ?  370  THR C OG1 1 
ATOM   10032 C  CG2 . THR C  1 339 ? -26.734 61.570  5.862   1.00 40.49  ?  370  THR C CG2 1 
ATOM   10033 N  N   . PHE C  1 340 ? -29.532 59.181  5.167   1.00 40.43  ?  371  PHE C N   1 
ATOM   10034 C  CA  . PHE C  1 340 ? -29.843 58.657  3.839   1.00 39.25  ?  371  PHE C CA  1 
ATOM   10035 C  C   . PHE C  1 340 ? -31.294 58.938  3.455   1.00 40.43  ?  371  PHE C C   1 
ATOM   10036 O  O   . PHE C  1 340 ? -31.578 59.291  2.303   1.00 38.45  ?  371  PHE C O   1 
ATOM   10037 C  CB  . PHE C  1 340 ? -29.546 57.154  3.767   1.00 38.73  ?  371  PHE C CB  1 
ATOM   10038 C  CG  . PHE C  1 340 ? -28.078 56.817  3.817   1.00 41.72  ?  371  PHE C CG  1 
ATOM   10039 C  CD1 . PHE C  1 340 ? -27.114 57.800  3.622   1.00 40.32  ?  371  PHE C CD1 1 
ATOM   10040 C  CD2 . PHE C  1 340 ? -27.662 55.519  4.085   1.00 38.55  ?  371  PHE C CD2 1 
ATOM   10041 C  CE1 . PHE C  1 340 ? -25.754 57.495  3.682   1.00 36.68  ?  371  PHE C CE1 1 
ATOM   10042 C  CE2 . PHE C  1 340 ? -26.302 55.196  4.146   1.00 35.80  ?  371  PHE C CE2 1 
ATOM   10043 C  CZ  . PHE C  1 340 ? -25.350 56.183  3.941   1.00 41.90  ?  371  PHE C CZ  1 
ATOM   10044 N  N   . THR C  1 341 ? -32.228 58.784  4.398   1.00 41.81  ?  372  THR C N   1 
ATOM   10045 C  CA  . THR C  1 341 ? -33.626 59.042  4.071   1.00 42.84  ?  372  THR C CA  1 
ATOM   10046 C  C   . THR C  1 341 ? -33.851 60.519  3.780   1.00 44.85  ?  372  THR C C   1 
ATOM   10047 O  O   . THR C  1 341 ? -34.640 60.866  2.894   1.00 42.73  ?  372  THR C O   1 
ATOM   10048 C  CB  . THR C  1 341 ? -34.543 58.588  5.204   1.00 46.29  ?  372  THR C CB  1 
ATOM   10049 O  OG1 . THR C  1 341 ? -34.092 59.163  6.426   1.00 48.02  ?  372  THR C OG1 1 
ATOM   10050 C  CG2 . THR C  1 341 ? -34.536 57.076  5.342   1.00 47.54  ?  372  THR C CG2 1 
ATOM   10051 N  N   . GLY C  1 342 ? -33.173 61.399  4.524   1.00 44.39  ?  373  GLY C N   1 
ATOM   10052 C  CA  . GLY C  1 342 ? -33.229 62.819  4.216   1.00 40.86  ?  373  GLY C CA  1 
ATOM   10053 C  C   . GLY C  1 342 ? -32.741 63.129  2.813   1.00 42.43  ?  373  GLY C C   1 
ATOM   10054 O  O   . GLY C  1 342 ? -33.376 63.888  2.080   1.00 48.81  ?  373  GLY C O   1 
ATOM   10055 N  N   . LEU C  1 343 ? -31.628 62.523  2.403   1.00 37.50  ?  374  LEU C N   1 
ATOM   10056 C  CA  . LEU C  1 343 ? -31.121 62.785  1.058   1.00 41.73  ?  374  LEU C CA  1 
ATOM   10057 C  C   . LEU C  1 343 ? -32.091 62.284  -0.005  1.00 46.47  ?  374  LEU C C   1 
ATOM   10058 O  O   . LEU C  1 343 ? -32.191 62.863  -1.098  1.00 42.73  ?  374  LEU C O   1 
ATOM   10059 C  CB  . LEU C  1 343 ? -29.766 62.117  0.864   1.00 40.46  ?  374  LEU C CB  1 
ATOM   10060 C  CG  . LEU C  1 343 ? -28.582 62.743  1.602   1.00 43.29  ?  374  LEU C CG  1 
ATOM   10061 C  CD1 . LEU C  1 343 ? -27.352 61.930  1.316   1.00 43.44  ?  374  LEU C CD1 1 
ATOM   10062 C  CD2 . LEU C  1 343 ? -28.358 64.187  1.180   1.00 41.36  ?  374  LEU C CD2 1 
ATOM   10063 N  N   . ALA C  1 344 ? -32.780 61.187  0.284   1.00 42.31  ?  375  ALA C N   1 
ATOM   10064 C  CA  . ALA C  1 344 ? -33.688 60.571  -0.666  1.00 44.86  ?  375  ALA C CA  1 
ATOM   10065 C  C   . ALA C  1 344 ? -35.074 61.180  -0.597  1.00 44.53  ?  375  ALA C C   1 
ATOM   10066 O  O   . ALA C  1 344 ? -35.975 60.720  -1.304  1.00 45.47  ?  375  ALA C O   1 
ATOM   10067 C  CB  . ALA C  1 344 ? -33.765 59.070  -0.407  1.00 39.80  ?  375  ALA C CB  1 
ATOM   10068 N  N   . GLU C  1 345 ? -35.264 62.174  0.266   1.00 45.10  ?  376  GLU C N   1 
ATOM   10069 C  CA  . GLU C  1 345 ? -36.530 62.874  0.393   1.00 46.15  ?  376  GLU C CA  1 
ATOM   10070 C  C   . GLU C  1 345 ? -37.646 61.904  0.760   1.00 49.71  ?  376  GLU C C   1 
ATOM   10071 O  O   . GLU C  1 345 ? -38.807 62.089  0.379   1.00 45.89  ?  376  GLU C O   1 
ATOM   10072 C  CB  . GLU C  1 345 ? -36.844 63.635  -0.898  1.00 48.60  ?  376  GLU C CB  1 
ATOM   10073 C  CG  . GLU C  1 345 ? -36.027 64.909  -1.046  1.00 52.50  ?  376  GLU C CG  1 
ATOM   10074 C  CD  . GLU C  1 345 ? -35.983 65.426  -2.476  1.00 62.70  ?  376  GLU C CD  1 
ATOM   10075 O  OE1 . GLU C  1 345 ? -36.763 64.932  -3.323  1.00 69.33  ?  376  GLU C OE1 1 
ATOM   10076 O  OE2 . GLU C  1 345 ? -35.144 66.308  -2.764  1.00 66.79  -1 376  GLU C OE2 1 
ATOM   10077 N  N   . ALA C  1 346 ? -37.299 60.859  1.505   1.00 42.21  ?  377  ALA C N   1 
ATOM   10078 C  CA  . ALA C  1 346 ? -38.217 59.774  1.810   1.00 45.94  ?  377  ALA C CA  1 
ATOM   10079 C  C   . ALA C  1 346 ? -38.873 59.974  3.171   1.00 53.37  ?  377  ALA C C   1 
ATOM   10080 O  O   . ALA C  1 346 ? -38.214 60.350  4.145   1.00 56.05  ?  377  ALA C O   1 
ATOM   10081 C  CB  . ALA C  1 346 ? -37.485 58.435  1.782   1.00 47.34  ?  377  ALA C CB  1 
ATOM   10082 N  N   . LYS C  1 347 ? -40.168 59.697  3.243   1.00 48.22  ?  378  LYS C N   1 
ATOM   10083 C  CA  . LYS C  1 347 ? -40.893 59.804  4.497   1.00 50.75  ?  378  LYS C CA  1 
ATOM   10084 C  C   . LYS C  1 347 ? -40.756 58.507  5.281   1.00 49.94  ?  378  LYS C C   1 
ATOM   10085 O  O   . LYS C  1 347 ? -40.801 57.415  4.703   1.00 48.57  ?  378  LYS C O   1 
ATOM   10086 C  CB  . LYS C  1 347 ? -42.373 60.112  4.250   1.00 54.93  ?  378  LYS C CB  1 
ATOM   10087 N  N   . LEU C  1 348 ? -40.612 58.642  6.600   1.00 50.59  ?  379  LEU C N   1 
ATOM   10088 C  CA  . LEU C  1 348 ? -40.461 57.497  7.483   1.00 46.72  ?  379  LEU C CA  1 
ATOM   10089 C  C   . LEU C  1 348 ? -41.779 56.749  7.657   1.00 54.99  ?  379  LEU C C   1 
ATOM   10090 O  O   . LEU C  1 348 ? -42.856 57.338  7.548   1.00 52.50  ?  379  LEU C O   1 
ATOM   10091 C  CB  . LEU C  1 348 ? -39.974 57.935  8.858   1.00 51.18  ?  379  LEU C CB  1 
ATOM   10092 C  CG  . LEU C  1 348 ? -38.655 58.679  8.989   1.00 49.29  ?  379  LEU C CG  1 
ATOM   10093 C  CD1 . LEU C  1 348 ? -38.194 58.571  10.428  1.00 56.78  ?  379  LEU C CD1 1 
ATOM   10094 C  CD2 . LEU C  1 348 ? -37.636 58.063  8.042   1.00 49.74  ?  379  LEU C CD2 1 
ATOM   10095 N  N   . PRO C  1 349 ? -41.718 55.448  7.949   1.00 54.83  ?  380  PRO C N   1 
ATOM   10096 C  CA  . PRO C  1 349 ? -42.928 54.734  8.357   1.00 50.45  ?  380  PRO C CA  1 
ATOM   10097 C  C   . PRO C  1 349 ? -43.521 55.366  9.602   1.00 52.96  ?  380  PRO C C   1 
ATOM   10098 O  O   . PRO C  1 349 ? -42.801 55.856  10.475  1.00 50.27  ?  380  PRO C O   1 
ATOM   10099 C  CB  . PRO C  1 349 ? -42.423 53.316  8.636   1.00 52.17  ?  380  PRO C CB  1 
ATOM   10100 C  CG  . PRO C  1 349 ? -41.265 53.168  7.701   1.00 49.11  ?  380  PRO C CG  1 
ATOM   10101 C  CD  . PRO C  1 349 ? -40.592 54.523  7.719   1.00 48.67  ?  380  PRO C CD  1 
ATOM   10102 N  N   . LYS C  1 350 ? -44.848 55.366  9.665   1.00 49.95  ?  381  LYS C N   1 
ATOM   10103 C  CA  . LYS C  1 350 ? -45.554 55.846  10.842  1.00 52.51  ?  381  LYS C CA  1 
ATOM   10104 C  C   . LYS C  1 350 ? -45.060 55.118  12.081  1.00 46.06  ?  381  LYS C C   1 
ATOM   10105 O  O   . LYS C  1 350 ? -45.084 53.888  12.139  1.00 54.58  ?  381  LYS C O   1 
ATOM   10106 C  CB  . LYS C  1 350 ? -47.059 55.628  10.662  1.00 55.87  ?  381  LYS C CB  1 
ATOM   10107 C  CG  . LYS C  1 350 ? -47.916 56.174  11.793  1.00 55.81  ?  381  LYS C CG  1 
ATOM   10108 C  CD  . LYS C  1 350 ? -47.769 57.686  11.895  1.00 58.50  ?  381  LYS C CD  1 
ATOM   10109 C  CE  . LYS C  1 350 ? -49.008 58.333  12.517  1.00 62.21  ?  381  LYS C CE  1 
ATOM   10110 N  NZ  . LYS C  1 350 ? -48.719 59.721  12.989  1.00 62.57  ?  381  LYS C NZ  1 
ATOM   10111 N  N   . GLY C  1 351 ? -44.604 55.879  13.068  1.00 47.53  ?  382  GLY C N   1 
ATOM   10112 C  CA  . GLY C  1 351 ? -44.141 55.311  14.319  1.00 51.40  ?  382  GLY C CA  1 
ATOM   10113 C  C   . GLY C  1 351 ? -42.684 54.885  14.362  1.00 47.26  ?  382  GLY C C   1 
ATOM   10114 O  O   . GLY C  1 351 ? -42.240 54.378  15.397  1.00 49.59  ?  382  GLY C O   1 
ATOM   10115 N  N   . LYS C  1 352 ? -41.928 55.066  13.283  1.00 46.45  ?  383  LYS C N   1 
ATOM   10116 C  CA  . LYS C  1 352 ? -40.550 54.589  13.250  1.00 49.64  ?  383  LYS C CA  1 
ATOM   10117 C  C   . LYS C  1 352 ? -39.687 55.421  14.190  1.00 47.59  ?  383  LYS C C   1 
ATOM   10118 O  O   . LYS C  1 352 ? -39.735 56.653  14.157  1.00 49.03  ?  383  LYS C O   1 
ATOM   10119 C  CB  . LYS C  1 352 ? -40.004 54.646  11.815  1.00 49.48  ?  383  LYS C CB  1 
ATOM   10120 C  CG  . LYS C  1 352 ? -38.493 54.348  11.678  1.00 41.64  ?  383  LYS C CG  1 
ATOM   10121 C  CD  . LYS C  1 352 ? -38.201 52.865  11.799  1.00 39.47  ?  383  LYS C CD  1 
ATOM   10122 C  CE  . LYS C  1 352 ? -36.715 52.631  12.132  1.00 43.03  ?  383  LYS C CE  1 
ATOM   10123 N  NZ  . LYS C  1 352 ? -36.414 51.190  12.374  1.00 40.94  ?  383  LYS C NZ  1 
ATOM   10124 N  N   . GLN C  1 353 ? -38.921 54.742  15.046  1.00 48.42  ?  384  GLN C N   1 
ATOM   10125 C  CA  . GLN C  1 353 ? -38.005 55.382  15.987  1.00 47.10  ?  384  GLN C CA  1 
ATOM   10126 C  C   . GLN C  1 353 ? -36.580 55.335  15.450  1.00 47.39  ?  384  GLN C C   1 
ATOM   10127 O  O   . GLN C  1 353 ? -36.151 54.323  14.888  1.00 40.84  ?  384  GLN C O   1 
ATOM   10128 C  CB  . GLN C  1 353 ? -38.045 54.692  17.348  1.00 46.11  ?  384  GLN C CB  1 
ATOM   10129 C  CG  . GLN C  1 353 ? -39.425 54.433  17.893  1.00 54.97  ?  384  GLN C CG  1 
ATOM   10130 C  CD  . GLN C  1 353 ? -39.715 55.277  19.111  1.00 60.31  ?  384  GLN C CD  1 
ATOM   10131 O  OE1 . GLN C  1 353 ? -39.844 56.499  19.015  1.00 61.88  ?  384  GLN C OE1 1 
ATOM   10132 N  NE2 . GLN C  1 353 ? -39.800 54.634  20.274  1.00 60.98  ?  384  GLN C NE2 1 
ATOM   10133 N  N   . LEU C  1 354 ? -35.844 56.429  15.635  1.00 45.23  ?  385  LEU C N   1 
ATOM   10134 C  CA  . LEU C  1 354 ? -34.464 56.507  15.185  1.00 40.11  ?  385  LEU C CA  1 
ATOM   10135 C  C   . LEU C  1 354 ? -33.602 57.079  16.303  1.00 43.70  ?  385  LEU C C   1 
ATOM   10136 O  O   . LEU C  1 354 ? -34.012 58.000  17.015  1.00 42.25  ?  385  LEU C O   1 
ATOM   10137 C  CB  . LEU C  1 354 ? -34.339 57.356  13.916  1.00 43.35  ?  385  LEU C CB  1 
ATOM   10138 C  CG  . LEU C  1 354 ? -35.009 56.767  12.666  1.00 41.49  ?  385  LEU C CG  1 
ATOM   10139 C  CD1 . LEU C  1 354 ? -34.774 57.659  11.466  1.00 36.58  ?  385  LEU C CD1 1 
ATOM   10140 C  CD2 . LEU C  1 354 ? -34.481 55.365  12.390  1.00 39.69  ?  385  LEU C CD2 1 
ATOM   10141 N  N   . ASP C  1 355 ? -32.400 56.524  16.450  1.00 39.88  ?  386  ASP C N   1 
ATOM   10142 C  CA  . ASP C  1 355 ? -31.495 56.902  17.526  1.00 37.42  ?  386  ASP C CA  1 
ATOM   10143 C  C   . ASP C  1 355 ? -30.400 57.862  17.080  1.00 37.83  ?  386  ASP C C   1 
ATOM   10144 O  O   . ASP C  1 355 ? -29.802 58.534  17.930  1.00 40.47  ?  386  ASP C O   1 
ATOM   10145 C  CB  . ASP C  1 355 ? -30.882 55.637  18.143  1.00 38.27  ?  386  ASP C CB  1 
ATOM   10146 C  CG  . ASP C  1 355 ? -31.829 54.952  19.122  1.00 40.97  ?  386  ASP C CG  1 
ATOM   10147 O  OD1 . ASP C  1 355 ? -32.562 55.670  19.835  1.00 43.82  ?  386  ASP C OD1 1 
ATOM   10148 O  OD2 . ASP C  1 355 ? -31.886 53.701  19.156  1.00 40.28  -1 386  ASP C OD2 1 
ATOM   10149 N  N   . GLY C  1 356 ? -30.143 57.965  15.775  1.00 37.58  ?  387  GLY C N   1 
ATOM   10150 C  CA  . GLY C  1 356 ? -29.162 58.885  15.247  1.00 38.22  ?  387  GLY C CA  1 
ATOM   10151 C  C   . GLY C  1 356 ? -29.789 60.149  14.684  1.00 41.51  ?  387  GLY C C   1 
ATOM   10152 O  O   . GLY C  1 356 ? -30.960 60.462  14.909  1.00 41.27  ?  387  GLY C O   1 
ATOM   10153 N  N   . LYS C  1 357 ? -28.981 60.882  13.919  1.00 40.72  ?  388  LYS C N   1 
ATOM   10154 C  CA  . LYS C  1 357 ? -29.351 62.204  13.432  1.00 40.15  ?  388  LYS C CA  1 
ATOM   10155 C  C   . LYS C  1 357 ? -28.957 62.337  11.970  1.00 41.69  ?  388  LYS C C   1 
ATOM   10156 O  O   . LYS C  1 357 ? -27.978 61.735  11.518  1.00 39.35  ?  388  LYS C O   1 
ATOM   10157 C  CB  . LYS C  1 357 ? -28.667 63.330  14.237  1.00 40.20  ?  388  LYS C CB  1 
ATOM   10158 C  CG  . LYS C  1 357 ? -28.866 63.287  15.754  1.00 43.78  ?  388  LYS C CG  1 
ATOM   10159 C  CD  . LYS C  1 357 ? -27.998 64.364  16.430  1.00 41.76  ?  388  LYS C CD  1 
ATOM   10160 C  CE  . LYS C  1 357 ? -27.998 64.267  17.950  1.00 45.26  ?  388  LYS C CE  1 
ATOM   10161 N  NZ  . LYS C  1 357 ? -29.298 64.690  18.534  1.00 47.92  ?  388  LYS C NZ  1 
ATOM   10162 N  N   . ASN C  1 358 ? -29.736 63.133  11.230  1.00 37.96  ?  389  ASN C N   1 
ATOM   10163 C  CA  . ASN C  1 358 ? -29.352 63.546  9.889   1.00 37.01  ?  389  ASN C CA  1 
ATOM   10164 C  C   . ASN C  1 358 ? -28.214 64.552  10.007  1.00 44.67  ?  389  ASN C C   1 
ATOM   10165 O  O   . ASN C  1 358 ? -28.428 65.682  10.458  1.00 44.03  ?  389  ASN C O   1 
ATOM   10166 C  CB  . ASN C  1 358 ? -30.551 64.163  9.170   1.00 43.93  ?  389  ASN C CB  1 
ATOM   10167 C  CG  . ASN C  1 358 ? -30.239 64.565  7.741   1.00 40.95  ?  389  ASN C CG  1 
ATOM   10168 O  OD1 . ASN C  1 358 ? -29.080 64.656  7.339   1.00 41.62  ?  389  ASN C OD1 1 
ATOM   10169 N  ND2 . ASN C  1 358 ? -31.292 64.816  6.955   1.00 51.52  ?  389  ASN C ND2 1 
ATOM   10170 N  N   . ILE C  1 359 ? -27.012 64.168  9.578   1.00 42.15  ?  390  ILE C N   1 
ATOM   10171 C  CA  . ILE C  1 359 ? -25.819 64.963  9.839   1.00 45.39  ?  390  ILE C CA  1 
ATOM   10172 C  C   . ILE C  1 359 ? -25.274 65.651  8.597   1.00 42.90  ?  390  ILE C C   1 
ATOM   10173 O  O   . ILE C  1 359 ? -24.248 66.341  8.703   1.00 39.88  ?  390  ILE C O   1 
ATOM   10174 C  CB  . ILE C  1 359 ? -24.709 64.119  10.502  1.00 38.73  ?  390  ILE C CB  1 
ATOM   10175 C  CG1 . ILE C  1 359 ? -24.249 62.987  9.573   1.00 37.83  ?  390  ILE C CG1 1 
ATOM   10176 C  CG2 . ILE C  1 359 ? -25.171 63.587  11.857  1.00 42.23  ?  390  ILE C CG2 1 
ATOM   10177 C  CD1 . ILE C  1 359 ? -22.927 62.315  10.020  1.00 39.98  ?  390  ILE C CD1 1 
ATOM   10178 N  N   . MET C  1 360 ? -25.908 65.486  7.425   1.00 42.69  ?  391  MET C N   1 
ATOM   10179 C  CA  . MET C  1 360 ? -25.401 66.128  6.205   1.00 45.46  ?  391  MET C CA  1 
ATOM   10180 C  C   . MET C  1 360 ? -25.107 67.609  6.399   1.00 46.77  ?  391  MET C C   1 
ATOM   10181 O  O   . MET C  1 360 ? -24.038 68.092  6.008   1.00 46.70  ?  391  MET C O   1 
ATOM   10182 C  CB  . MET C  1 360 ? -26.378 65.965  5.044   1.00 41.38  ?  391  MET C CB  1 
ATOM   10183 C  CG  . MET C  1 360 ? -25.699 66.041  3.694   1.00 40.83  ?  391  MET C CG  1 
ATOM   10184 S  SD  . MET C  1 360 ? -24.004 65.478  3.578   1.00 48.28  ?  391  MET C SD  1 
ATOM   10185 C  CE  . MET C  1 360 ? -24.310 63.722  3.276   1.00 45.41  ?  391  MET C CE  1 
ATOM   10186 N  N   . ASP C  1 361 ? -26.061 68.357  6.956   1.00 43.05  ?  392  ASP C N   1 
ATOM   10187 C  CA  . ASP C  1 361 ? -25.850 69.792  7.106   1.00 47.96  ?  392  ASP C CA  1 
ATOM   10188 C  C   . ASP C  1 361 ? -24.626 70.062  7.971   1.00 45.98  ?  392  ASP C C   1 
ATOM   10189 O  O   . ASP C  1 361 ? -23.751 70.855  7.601   1.00 45.16  ?  392  ASP C O   1 
ATOM   10190 C  CB  . ASP C  1 361 ? -27.091 70.458  7.700   1.00 47.14  ?  392  ASP C CB  1 
ATOM   10191 C  CG  . ASP C  1 361 ? -28.146 70.753  6.659   1.00 62.19  ?  392  ASP C CG  1 
ATOM   10192 O  OD1 . ASP C  1 361 ? -27.926 70.424  5.471   1.00 64.97  ?  392  ASP C OD1 1 
ATOM   10193 O  OD2 . ASP C  1 361 ? -29.196 71.322  7.031   1.00 72.00  ?  392  ASP C OD2 1 
ATOM   10194 N  N   . ASP C  1 362 ? -24.533 69.372  9.110   1.00 44.64  ?  393  ASP C N   1 
ATOM   10195 C  CA  . ASP C  1 362 ? -23.379 69.540  9.985   1.00 40.69  ?  393  ASP C CA  1 
ATOM   10196 C  C   . ASP C  1 362 ? -22.085 69.252  9.245   1.00 41.17  ?  393  ASP C C   1 
ATOM   10197 O  O   . ASP C  1 362 ? -21.090 69.960  9.427   1.00 46.25  ?  393  ASP C O   1 
ATOM   10198 C  CB  . ASP C  1 362 ? -23.513 68.643  11.213  1.00 41.76  ?  393  ASP C CB  1 
ATOM   10199 C  CG  . ASP C  1 362 ? -24.713 69.004  12.076  1.00 44.54  ?  393  ASP C CG  1 
ATOM   10200 O  OD1 . ASP C  1 362 ? -24.765 70.138  12.608  1.00 49.62  ?  393  ASP C OD1 1 
ATOM   10201 O  OD2 . ASP C  1 362 ? -25.590 68.143  12.256  1.00 46.56  -1 393  ASP C OD2 1 
ATOM   10202 N  N   . VAL C  1 363 ? -22.081 68.231  8.387   1.00 39.19  ?  394  VAL C N   1 
ATOM   10203 C  CA  . VAL C  1 363 ? -20.871 67.883  7.649   1.00 39.87  ?  394  VAL C CA  1 
ATOM   10204 C  C   . VAL C  1 363 ? -20.526 68.968  6.629   1.00 46.37  ?  394  VAL C C   1 
ATOM   10205 O  O   . VAL C  1 363 ? -19.349 69.291  6.413   1.00 49.14  ?  394  VAL C O   1 
ATOM   10206 C  CB  . VAL C  1 363 ? -21.035 66.499  6.993   1.00 46.80  ?  394  VAL C CB  1 
ATOM   10207 C  CG1 . VAL C  1 363 ? -19.887 66.204  6.021   1.00 39.66  ?  394  VAL C CG1 1 
ATOM   10208 C  CG2 . VAL C  1 363 ? -21.143 65.402  8.075   1.00 42.00  ?  394  VAL C CG2 1 
ATOM   10209 N  N   . LEU C  1 364 ? -21.540 69.564  6.002   1.00 47.77  ?  395  LEU C N   1 
ATOM   10210 C  CA  . LEU C  1 364 ? -21.288 70.614  5.025   1.00 48.32  ?  395  LEU C CA  1 
ATOM   10211 C  C   . LEU C  1 364 ? -20.905 71.931  5.693   1.00 46.22  ?  395  LEU C C   1 
ATOM   10212 O  O   . LEU C  1 364 ? -20.149 72.719  5.111   1.00 47.71  ?  395  LEU C O   1 
ATOM   10213 C  CB  . LEU C  1 364 ? -22.522 70.794  4.143   1.00 46.64  ?  395  LEU C CB  1 
ATOM   10214 C  CG  . LEU C  1 364 ? -22.844 69.552  3.313   1.00 46.26  ?  395  LEU C CG  1 
ATOM   10215 C  CD1 . LEU C  1 364 ? -24.195 69.692  2.607   1.00 47.27  ?  395  LEU C CD1 1 
ATOM   10216 C  CD2 . LEU C  1 364 ? -21.733 69.272  2.315   1.00 42.01  ?  395  LEU C CD2 1 
ATOM   10217 N  N   . LYS C  1 365 ? -21.399 72.173  6.907   1.00 43.93  ?  396  LYS C N   1 
ATOM   10218 C  CA  . LYS C  1 365 ? -21.139 73.401  7.648   1.00 47.37  ?  396  LYS C CA  1 
ATOM   10219 C  C   . LYS C  1 365 ? -20.092 73.232  8.752   1.00 50.01  ?  396  LYS C C   1 
ATOM   10220 O  O   . LYS C  1 365 ? -19.838 74.186  9.494   1.00 49.17  ?  396  LYS C O   1 
ATOM   10221 C  CB  . LYS C  1 365 ? -22.444 73.928  8.254   1.00 49.78  ?  396  LYS C CB  1 
ATOM   10222 N  N   . ASN C  1 366 ? -19.477 72.051  8.869   1.00 46.68  ?  397  ASN C N   1 
ATOM   10223 C  CA  . ASN C  1 366 ? -18.519 71.741  9.938   1.00 45.00  ?  397  ASN C CA  1 
ATOM   10224 C  C   . ASN C  1 366 ? -19.050 72.178  11.302  1.00 48.39  ?  397  ASN C C   1 
ATOM   10225 O  O   . ASN C  1 366 ? -18.406 72.929  12.034  1.00 51.19  ?  397  ASN C O   1 
ATOM   10226 C  CB  . ASN C  1 366 ? -17.148 72.365  9.655   1.00 43.55  ?  397  ASN C CB  1 
ATOM   10227 C  CG  . ASN C  1 366 ? -16.033 71.739  10.486  1.00 56.85  ?  397  ASN C CG  1 
ATOM   10228 O  OD1 . ASN C  1 366 ? -15.733 70.542  10.366  1.00 50.91  ?  397  ASN C OD1 1 
ATOM   10229 N  ND2 . ASN C  1 366 ? -15.408 72.551  11.335  1.00 57.07  ?  397  ASN C ND2 1 
ATOM   10230 N  N   . THR C  1 367 ? -20.248 71.711  11.638  1.00 44.84  ?  398  THR C N   1 
ATOM   10231 C  CA  . THR C  1 367 ? -20.835 71.944  12.950  1.00 45.54  ?  398  THR C CA  1 
ATOM   10232 C  C   . THR C  1 367 ? -20.969 70.615  13.688  1.00 49.76  ?  398  THR C C   1 
ATOM   10233 O  O   . THR C  1 367 ? -20.743 69.540  13.120  1.00 46.98  ?  398  THR C O   1 
ATOM   10234 C  CB  . THR C  1 367 ? -22.198 72.637  12.844  1.00 47.03  ?  398  THR C CB  1 
ATOM   10235 O  OG1 . THR C  1 367 ? -23.036 71.904  11.946  1.00 52.21  ?  398  THR C OG1 1 
ATOM   10236 C  CG2 . THR C  1 367 ? -22.038 74.066  12.302  1.00 50.19  ?  398  THR C CG2 1 
ATOM   10237 N  N   . GLU C  1 368 ? -21.369 70.701  14.969  1.00 47.53  ?  399  GLU C N   1 
ATOM   10238 C  CA  . GLU C  1 368 ? -21.270 69.594  15.915  1.00 50.09  ?  399  GLU C CA  1 
ATOM   10239 C  C   . GLU C  1 368 ? -22.638 68.957  16.113  1.00 45.84  ?  399  GLU C C   1 
ATOM   10240 O  O   . GLU C  1 368 ? -23.447 69.477  16.896  1.00 45.74  ?  399  GLU C O   1 
ATOM   10241 C  CB  . GLU C  1 368 ? -20.702 70.086  17.259  1.00 50.96  ?  399  GLU C CB  1 
ATOM   10242 C  CG  . GLU C  1 368 ? -20.544 69.015  18.368  1.00 49.59  ?  399  GLU C CG  1 
ATOM   10243 C  CD  . GLU C  1 368 ? -19.915 69.580  19.654  1.00 55.68  ?  399  GLU C CD  1 
ATOM   10244 O  OE1 . GLU C  1 368 ? -19.756 70.818  19.734  1.00 55.37  ?  399  GLU C OE1 1 
ATOM   10245 O  OE2 . GLU C  1 368 ? -19.567 68.796  20.578  1.00 48.73  -1 399  GLU C OE2 1 
ATOM   10246 N  N   . PRO C  1 369 ? -22.943 67.826  15.456  1.00 45.10  ?  400  PRO C N   1 
ATOM   10247 C  CA  . PRO C  1 369 ? -24.293 67.254  15.590  1.00 40.03  ?  400  PRO C CA  1 
ATOM   10248 C  C   . PRO C  1 369 ? -24.607 66.753  16.986  1.00 45.34  ?  400  PRO C C   1 
ATOM   10249 O  O   . PRO C  1 369 ? -25.760 66.855  17.420  1.00 38.73  ?  400  PRO C O   1 
ATOM   10250 C  CB  . PRO C  1 369 ? -24.295 66.112  14.561  1.00 39.95  ?  400  PRO C CB  1 
ATOM   10251 C  CG  . PRO C  1 369 ? -22.860 65.762  14.390  1.00 42.89  ?  400  PRO C CG  1 
ATOM   10252 C  CD  . PRO C  1 369 ? -22.119 67.066  14.500  1.00 42.89  ?  400  PRO C CD  1 
ATOM   10253 N  N   . TYR C  1 370 ? -23.628 66.232  17.728  1.00 43.17  ?  401  TYR C N   1 
ATOM   10254 C  CA  . TYR C  1 370 ? -23.908 65.688  19.051  1.00 45.01  ?  401  TYR C CA  1 
ATOM   10255 C  C   . TYR C  1 370 ? -23.484 66.628  20.177  1.00 48.41  ?  401  TYR C C   1 
ATOM   10256 O  O   . TYR C  1 370 ? -23.152 66.171  21.278  1.00 43.13  ?  401  TYR C O   1 
ATOM   10257 C  CB  . TYR C  1 370 ? -23.258 64.313  19.205  1.00 42.21  ?  401  TYR C CB  1 
ATOM   10258 C  CG  . TYR C  1 370 ? -24.026 63.223  18.468  1.00 39.93  ?  401  TYR C CG  1 
ATOM   10259 C  CD1 . TYR C  1 370 ? -23.769 62.940  17.132  1.00 37.81  ?  401  TYR C CD1 1 
ATOM   10260 C  CD2 . TYR C  1 370 ? -25.017 62.486  19.115  1.00 41.10  ?  401  TYR C CD2 1 
ATOM   10261 C  CE1 . TYR C  1 370 ? -24.485 61.949  16.456  1.00 38.48  ?  401  TYR C CE1 1 
ATOM   10262 C  CE2 . TYR C  1 370 ? -25.726 61.490  18.451  1.00 41.73  ?  401  TYR C CE2 1 
ATOM   10263 C  CZ  . TYR C  1 370 ? -25.451 61.230  17.128  1.00 38.17  ?  401  TYR C CZ  1 
ATOM   10264 O  OH  . TYR C  1 370 ? -26.151 60.239  16.482  1.00 40.70  ?  401  TYR C OH  1 
ATOM   10265 N  N   . LYS C  1 371 ? -23.496 67.933  19.919  1.00 48.65  ?  402  LYS C N   1 
ATOM   10266 C  CA  . LYS C  1 371 ? -23.282 68.924  20.967  1.00 50.25  ?  402  LYS C CA  1 
ATOM   10267 C  C   . LYS C  1 371 ? -24.184 68.625  22.147  1.00 46.06  ?  402  LYS C C   1 
ATOM   10268 O  O   . LYS C  1 371 ? -25.403 68.550  21.995  1.00 48.88  ?  402  LYS C O   1 
ATOM   10269 C  CB  . LYS C  1 371 ? -23.567 70.328  20.424  1.00 47.07  ?  402  LYS C CB  1 
ATOM   10270 N  N   . ASP C  1 372 ? -23.574 68.406  23.312  1.00 46.31  ?  403  ASP C N   1 
ATOM   10271 C  CA  . ASP C  1 372 ? -24.280 68.156  24.567  1.00 48.79  ?  403  ASP C CA  1 
ATOM   10272 C  C   . ASP C  1 372 ? -25.036 66.827  24.574  1.00 49.31  ?  403  ASP C C   1 
ATOM   10273 O  O   . ASP C  1 372 ? -25.939 66.634  25.406  1.00 43.80  ?  403  ASP C O   1 
ATOM   10274 C  CB  . ASP C  1 372 ? -25.268 69.285  24.899  1.00 53.88  ?  403  ASP C CB  1 
ATOM   10275 C  CG  . ASP C  1 372 ? -24.579 70.584  25.269  1.00 55.26  ?  403  ASP C CG  1 
ATOM   10276 O  OD1 . ASP C  1 372 ? -23.410 70.561  25.694  1.00 51.58  -1 403  ASP C OD1 1 
ATOM   10277 O  OD2 . ASP C  1 372 ? -25.227 71.640  25.144  1.00 67.51  ?  403  ASP C OD2 1 
ATOM   10278 N  N   . GLU C  1 373 ? -24.685 65.901  23.672  1.00 42.40  ?  404  GLU C N   1 
ATOM   10279 C  CA  . GLU C  1 373 ? -25.378 64.628  23.518  1.00 45.68  ?  404  GLU C CA  1 
ATOM   10280 C  C   . GLU C  1 373 ? -24.399 63.456  23.561  1.00 46.63  ?  404  GLU C C   1 
ATOM   10281 O  O   . GLU C  1 373 ? -23.239 63.577  23.154  1.00 42.24  ?  404  GLU C O   1 
ATOM   10282 C  CB  . GLU C  1 373 ? -26.142 64.577  22.194  1.00 48.13  ?  404  GLU C CB  1 
ATOM   10283 C  CG  . GLU C  1 373 ? -26.956 65.807  21.901  1.00 49.40  ?  404  GLU C CG  1 
ATOM   10284 C  CD  . GLU C  1 373 ? -28.356 65.468  21.424  1.00 58.05  ?  404  GLU C CD  1 
ATOM   10285 O  OE1 . GLU C  1 373 ? -28.854 64.353  21.715  1.00 59.21  ?  404  GLU C OE1 1 
ATOM   10286 O  OE2 . GLU C  1 373 ? -28.935 66.305  20.703  1.00 56.45  -1 404  GLU C OE2 1 
ATOM   10287 N  N   . MET C  1 374 ? -24.910 62.306  24.015  1.00 46.71  ?  405  MET C N   1 
ATOM   10288 C  CA  . MET C  1 374 ? -24.139 61.083  24.243  1.00 40.51  ?  405  MET C CA  1 
ATOM   10289 C  C   . MET C  1 374 ? -24.115 60.193  23.010  1.00 41.68  ?  405  MET C C   1 
ATOM   10290 O  O   . MET C  1 374 ? -25.125 60.049  22.310  1.00 36.60  ?  405  MET C O   1 
ATOM   10291 C  CB  . MET C  1 374 ? -24.752 60.294  25.403  1.00 40.25  ?  405  MET C CB  1 
ATOM   10292 C  CG  . MET C  1 374 ? -24.493 60.802  26.795  1.00 38.22  ?  405  MET C CG  1 
ATOM   10293 S  SD  . MET C  1 374 ? -22.770 60.782  27.319  1.00 45.40  ?  405  MET C SD  1 
ATOM   10294 C  CE  . MET C  1 374 ? -22.980 59.950  28.890  1.00 43.18  ?  405  MET C CE  1 
ATOM   10295 N  N   . ILE C  1 375 ? -22.956 59.587  22.760  1.00 39.31  ?  406  ILE C N   1 
ATOM   10296 C  CA  . ILE C  1 375 ? -22.813 58.444  21.867  1.00 35.98  ?  406  ILE C CA  1 
ATOM   10297 C  C   . ILE C  1 375 ? -22.342 57.276  22.718  1.00 43.69  ?  406  ILE C C   1 
ATOM   10298 O  O   . ILE C  1 375 ? -21.371 57.413  23.475  1.00 38.82  ?  406  ILE C O   1 
ATOM   10299 C  CB  . ILE C  1 375 ? -21.836 58.739  20.720  1.00 38.83  ?  406  ILE C CB  1 
ATOM   10300 C  CG1 . ILE C  1 375 ? -22.545 59.595  19.655  1.00 39.91  ?  406  ILE C CG1 1 
ATOM   10301 C  CG2 . ILE C  1 375 ? -21.282 57.438  20.149  1.00 38.88  ?  406  ILE C CG2 1 
ATOM   10302 C  CD1 . ILE C  1 375 ? -21.629 60.144  18.564  1.00 38.08  ?  406  ILE C CD1 1 
ATOM   10303 N  N   . TYR C  1 376 ? -23.041 56.145  22.621  1.00 34.73  ?  407  TYR C N   1 
ATOM   10304 C  CA  . TYR C  1 376 ? -22.974 55.105  23.644  1.00 40.56  ?  407  TYR C CA  1 
ATOM   10305 C  C   . TYR C  1 376 ? -22.458 53.780  23.108  1.00 37.54  ?  407  TYR C C   1 
ATOM   10306 O  O   . TYR C  1 376 ? -22.520 53.497  21.904  1.00 36.71  ?  407  TYR C O   1 
ATOM   10307 C  CB  . TYR C  1 376 ? -24.349 54.782  24.243  1.00 40.56  ?  407  TYR C CB  1 
ATOM   10308 C  CG  . TYR C  1 376 ? -25.035 55.845  25.046  1.00 42.00  ?  407  TYR C CG  1 
ATOM   10309 C  CD1 . TYR C  1 376 ? -24.556 56.205  26.293  1.00 40.15  ?  407  TYR C CD1 1 
ATOM   10310 C  CD2 . TYR C  1 376 ? -26.229 56.416  24.600  1.00 42.52  ?  407  TYR C CD2 1 
ATOM   10311 C  CE1 . TYR C  1 376 ? -25.203 57.151  27.062  1.00 45.43  ?  407  TYR C CE1 1 
ATOM   10312 C  CE2 . TYR C  1 376 ? -26.891 57.367  25.364  1.00 45.87  ?  407  TYR C CE2 1 
ATOM   10313 C  CZ  . TYR C  1 376 ? -26.375 57.723  26.603  1.00 44.92  ?  407  TYR C CZ  1 
ATOM   10314 O  OH  . TYR C  1 376 ? -27.005 58.673  27.388  1.00 47.64  ?  407  TYR C OH  1 
ATOM   10315 N  N   . SER C  1 377 ? -22.048 52.936  24.056  1.00 38.53  ?  408  SER C N   1 
ATOM   10316 C  CA  . SER C  1 377 ? -21.894 51.508  23.821  1.00 32.59  ?  408  SER C CA  1 
ATOM   10317 C  C   . SER C  1 377 ? -22.017 50.761  25.147  1.00 35.97  ?  408  SER C C   1 
ATOM   10318 O  O   . SER C  1 377 ? -21.493 51.197  26.182  1.00 35.83  ?  408  SER C O   1 
ATOM   10319 C  CB  . SER C  1 377 ? -20.560 51.195  23.130  1.00 36.40  ?  408  SER C CB  1 
ATOM   10320 O  OG  . SER C  1 377 ? -20.425 49.803  22.859  1.00 36.11  ?  408  SER C OG  1 
ATOM   10321 N  N   . LEU C  1 378 ? -22.725 49.638  25.108  1.00 34.99  ?  409  LEU C N   1 
ATOM   10322 C  CA  . LEU C  1 378 ? -22.806 48.726  26.241  1.00 32.33  ?  409  LEU C CA  1 
ATOM   10323 C  C   . LEU C  1 378 ? -22.734 47.310  25.702  1.00 33.41  ?  409  LEU C C   1 
ATOM   10324 O  O   . LEU C  1 378 ? -23.600 46.895  24.922  1.00 30.96  ?  409  LEU C O   1 
ATOM   10325 C  CB  . LEU C  1 378 ? -24.098 48.922  27.036  1.00 31.30  ?  409  LEU C CB  1 
ATOM   10326 C  CG  . LEU C  1 378 ? -24.202 48.079  28.297  1.00 31.00  ?  409  LEU C CG  1 
ATOM   10327 C  CD1 . LEU C  1 378 ? -24.961 48.849  29.375  1.00 34.17  ?  409  LEU C CD1 1 
ATOM   10328 C  CD2 . LEU C  1 378 ? -24.862 46.712  28.027  1.00 28.30  ?  409  LEU C CD2 1 
ATOM   10329 N  N   . ARG C  1 379 ? -21.732 46.564  26.127  1.00 30.72  ?  410  ARG C N   1 
ATOM   10330 C  CA  . ARG C  1 379 ? -21.524 45.218  25.617  1.00 32.31  ?  410  ARG C CA  1 
ATOM   10331 C  C   . ARG C  1 379 ? -21.639 44.241  26.776  1.00 33.35  ?  410  ARG C C   1 
ATOM   10332 O  O   . ARG C  1 379 ? -20.961 44.399  27.803  1.00 30.53  ?  410  ARG C O   1 
ATOM   10333 C  CB  . ARG C  1 379 ? -20.168 45.111  24.911  1.00 29.99  ?  410  ARG C CB  1 
ATOM   10334 C  CG  . ARG C  1 379 ? -19.848 43.735  24.362  1.00 31.07  ?  410  ARG C CG  1 
ATOM   10335 C  CD  . ARG C  1 379 ? -18.991 42.974  25.347  1.00 31.37  ?  410  ARG C CD  1 
ATOM   10336 N  NE  . ARG C  1 379 ? -18.989 41.539  25.089  1.00 29.25  ?  410  ARG C NE  1 
ATOM   10337 C  CZ  . ARG C  1 379 ? -18.323 40.981  24.093  1.00 30.49  ?  410  ARG C CZ  1 
ATOM   10338 N  NH1 . ARG C  1 379 ? -17.611 41.712  23.251  1.00 31.50  ?  410  ARG C NH1 1 
ATOM   10339 N  NH2 . ARG C  1 379 ? -18.370 39.657  23.936  1.00 30.82  ?  410  ARG C NH2 1 
ATOM   10340 N  N   . TYR C  1 380 ? -22.507 43.241  26.608  1.00 30.05  ?  411  TYR C N   1 
ATOM   10341 C  CA  . TYR C  1 380 ? -22.739 42.237  27.640  1.00 29.23  ?  411  TYR C CA  1 
ATOM   10342 C  C   . TYR C  1 380 ? -21.576 41.252  27.721  1.00 28.34  ?  411  TYR C C   1 
ATOM   10343 O  O   . TYR C  1 380 ? -21.135 40.710  26.702  1.00 27.52  ?  411  TYR C O   1 
ATOM   10344 C  CB  . TYR C  1 380 ? -24.033 41.473  27.360  1.00 30.87  ?  411  TYR C CB  1 
ATOM   10345 C  CG  . TYR C  1 380 ? -25.266 42.345  27.296  1.00 29.61  ?  411  TYR C CG  1 
ATOM   10346 C  CD1 . TYR C  1 380 ? -25.792 42.921  28.448  1.00 32.49  ?  411  TYR C CD1 1 
ATOM   10347 C  CD2 . TYR C  1 380 ? -25.925 42.566  26.085  1.00 35.29  ?  411  TYR C CD2 1 
ATOM   10348 C  CE1 . TYR C  1 380 ? -26.955 43.727  28.395  1.00 34.24  ?  411  TYR C CE1 1 
ATOM   10349 C  CE2 . TYR C  1 380 ? -27.086 43.369  26.023  1.00 33.26  ?  411  TYR C CE2 1 
ATOM   10350 C  CZ  . TYR C  1 380 ? -27.582 43.949  27.187  1.00 34.22  ?  411  TYR C CZ  1 
ATOM   10351 O  OH  . TYR C  1 380 ? -28.712 44.746  27.135  1.00 39.17  ?  411  TYR C OH  1 
ATOM   10352 N  N   . ARG C  1 381 ? -21.087 41.027  28.939  1.00 30.32  ?  412  ARG C N   1 
ATOM   10353 C  CA  . ARG C  1 381 ? -20.064 40.034  29.257  1.00 29.63  ?  412  ARG C CA  1 
ATOM   10354 C  C   . ARG C  1 381 ? -20.699 38.922  30.082  1.00 34.37  ?  412  ARG C C   1 
ATOM   10355 O  O   . ARG C  1 381 ? -21.916 38.911  30.306  1.00 31.16  ?  412  ARG C O   1 
ATOM   10356 C  CB  . ARG C  1 381 ? -18.895 40.681  30.000  1.00 29.45  ?  412  ARG C CB  1 
ATOM   10357 C  CG  . ARG C  1 381 ? -18.168 41.704  29.167  1.00 30.75  ?  412  ARG C CG  1 
ATOM   10358 C  CD  . ARG C  1 381 ? -17.239 40.992  28.198  1.00 25.09  ?  412  ARG C CD  1 
ATOM   10359 N  NE  . ARG C  1 381 ? -16.564 41.961  27.345  1.00 28.97  ?  412  ARG C NE  1 
ATOM   10360 C  CZ  . ARG C  1 381 ? -15.759 41.632  26.347  1.00 29.87  ?  412  ARG C CZ  1 
ATOM   10361 N  NH1 . ARG C  1 381 ? -15.582 40.366  25.992  1.00 29.79  ?  412  ARG C NH1 1 
ATOM   10362 N  NH2 . ARG C  1 381 ? -15.124 42.595  25.680  1.00 25.73  ?  412  ARG C NH2 1 
ATOM   10363 N  N   . GLU C  1 382 ? -19.868 37.979  30.539  1.00 29.68  ?  413  GLU C N   1 
ATOM   10364 C  CA  . GLU C  1 382 ? -20.355 36.844  31.327  1.00 34.19  ?  413  GLU C CA  1 
ATOM   10365 C  C   . GLU C  1 382 ? -20.419 37.252  32.797  1.00 29.38  ?  413  GLU C C   1 
ATOM   10366 O  O   . GLU C  1 382 ? -19.551 36.934  33.602  1.00 34.12  ?  413  GLU C O   1 
ATOM   10367 C  CB  . GLU C  1 382 ? -19.478 35.611  31.118  1.00 32.04  ?  413  GLU C CB  1 
ATOM   10368 C  CG  . GLU C  1 382 ? -19.228 35.290  29.662  1.00 27.89  ?  413  GLU C CG  1 
ATOM   10369 C  CD  . GLU C  1 382 ? -20.507 35.256  28.858  1.00 37.47  ?  413  GLU C CD  1 
ATOM   10370 O  OE1 . GLU C  1 382 ? -21.477 34.596  29.300  1.00 38.63  ?  413  GLU C OE1 1 
ATOM   10371 O  OE2 . GLU C  1 382 ? -20.540 35.907  27.795  1.00 36.39  -1 413  GLU C OE2 1 
ATOM   10372 N  N   . GLY C  1 383 ? -21.488 37.966  33.147  1.00 34.71  ?  414  GLY C N   1 
ATOM   10373 C  CA  . GLY C  1 383 ? -21.729 38.360  34.524  1.00 34.76  ?  414  GLY C CA  1 
ATOM   10374 C  C   . GLY C  1 383 ? -21.635 39.845  34.805  1.00 35.87  ?  414  GLY C C   1 
ATOM   10375 O  O   . GLY C  1 383 ? -21.824 40.251  35.962  1.00 36.98  ?  414  GLY C O   1 
ATOM   10376 N  N   . TYR C  1 384 ? -21.343 40.665  33.800  1.00 33.13  ?  415  TYR C N   1 
ATOM   10377 C  CA  . TYR C  1 384 ? -21.128 42.096  33.991  1.00 34.83  ?  415  TYR C CA  1 
ATOM   10378 C  C   . TYR C  1 384 ? -21.202 42.739  32.613  1.00 30.80  ?  415  TYR C C   1 
ATOM   10379 O  O   . TYR C  1 384 ? -21.299 42.047  31.601  1.00 32.85  ?  415  TYR C O   1 
ATOM   10380 C  CB  . TYR C  1 384 ? -19.778 42.381  34.684  1.00 32.19  ?  415  TYR C CB  1 
ATOM   10381 C  CG  . TYR C  1 384 ? -18.583 42.063  33.811  1.00 29.33  ?  415  TYR C CG  1 
ATOM   10382 C  CD1 . TYR C  1 384 ? -18.053 40.779  33.763  1.00 31.81  ?  415  TYR C CD1 1 
ATOM   10383 C  CD2 . TYR C  1 384 ? -18.009 43.038  33.002  1.00 29.90  ?  415  TYR C CD2 1 
ATOM   10384 C  CE1 . TYR C  1 384 ? -16.949 40.478  32.954  1.00 29.96  ?  415  TYR C CE1 1 
ATOM   10385 C  CE2 . TYR C  1 384 ? -16.909 42.745  32.191  1.00 29.62  ?  415  TYR C CE2 1 
ATOM   10386 C  CZ  . TYR C  1 384 ? -16.393 41.468  32.165  1.00 28.76  ?  415  TYR C CZ  1 
ATOM   10387 O  OH  . TYR C  1 384 ? -15.326 41.168  31.339  1.00 26.00  ?  415  TYR C OH  1 
ATOM   10388 N  N   . ASN C  1 385 ? -21.147 44.072  32.573  1.00 33.31  ?  416  ASN C N   1 
ATOM   10389 C  CA  . ASN C  1 385 ? -21.266 44.808  31.316  1.00 28.92  ?  416  ASN C CA  1 
ATOM   10390 C  C   . ASN C  1 385 ? -20.062 45.703  31.077  1.00 27.52  ?  416  ASN C C   1 
ATOM   10391 O  O   . ASN C  1 385 ? -19.548 46.322  32.008  1.00 29.77  ?  416  ASN C O   1 
ATOM   10392 C  CB  . ASN C  1 385 ? -22.527 45.674  31.298  1.00 32.97  ?  416  ASN C CB  1 
ATOM   10393 C  CG  . ASN C  1 385 ? -23.777 44.861  31.484  1.00 31.32  ?  416  ASN C CG  1 
ATOM   10394 O  OD1 . ASN C  1 385 ? -23.964 43.861  30.799  1.00 31.65  ?  416  ASN C OD1 1 
ATOM   10395 N  ND2 . ASN C  1 385 ? -24.641 45.273  32.427  1.00 34.36  ?  416  ASN C ND2 1 
ATOM   10396 N  N   . ASP C  1 386 ? -19.610 45.769  29.824  1.00 28.84  ?  417  ASP C N   1 
ATOM   10397 C  CA  . ASP C  1 386 ? -18.644 46.784  29.416  1.00 29.42  ?  417  ASP C CA  1 
ATOM   10398 C  C   . ASP C  1 386 ? -19.416 47.986  28.877  1.00 30.87  ?  417  ASP C C   1 
ATOM   10399 O  O   . ASP C  1 386 ? -20.415 47.825  28.169  1.00 32.80  ?  417  ASP C O   1 
ATOM   10400 C  CB  . ASP C  1 386 ? -17.680 46.258  28.341  1.00 33.04  ?  417  ASP C CB  1 
ATOM   10401 C  CG  . ASP C  1 386 ? -16.655 45.247  28.879  1.00 28.76  ?  417  ASP C CG  1 
ATOM   10402 O  OD1 . ASP C  1 386 ? -16.363 45.241  30.090  1.00 30.88  ?  417  ASP C OD1 1 
ATOM   10403 O  OD2 . ASP C  1 386 ? -16.131 44.448  28.061  1.00 31.74  -1 417  ASP C OD2 1 
ATOM   10404 N  N   . VAL C  1 387 ? -18.954 49.195  29.208  1.00 30.93  ?  418  VAL C N   1 
ATOM   10405 C  CA  . VAL C  1 387 ? -19.664 50.425  28.857  1.00 28.93  ?  418  VAL C CA  1 
ATOM   10406 C  C   . VAL C  1 387 ? -18.687 51.457  28.322  1.00 31.42  ?  418  VAL C C   1 
ATOM   10407 O  O   . VAL C  1 387 ? -17.552 51.566  28.801  1.00 32.39  ?  418  VAL C O   1 
ATOM   10408 C  CB  . VAL C  1 387 ? -20.436 51.016  30.055  1.00 29.15  ?  418  VAL C CB  1 
ATOM   10409 C  CG1 . VAL C  1 387 ? -21.361 52.158  29.594  1.00 30.09  ?  418  VAL C CG1 1 
ATOM   10410 C  CG2 . VAL C  1 387 ? -21.244 49.934  30.763  1.00 30.55  ?  418  VAL C CG2 1 
ATOM   10411 N  N   . GLY C  1 388 ? -19.131 52.204  27.324  1.00 30.57  ?  419  GLY C N   1 
ATOM   10412 C  CA  . GLY C  1 388 ? -18.484 53.425  26.900  1.00 30.93  ?  419  GLY C CA  1 
ATOM   10413 C  C   . GLY C  1 388 ? -19.530 54.502  26.676  1.00 36.28  ?  419  GLY C C   1 
ATOM   10414 O  O   . GLY C  1 388 ? -20.633 54.208  26.182  1.00 37.00  ?  419  GLY C O   1 
ATOM   10415 N  N   . ALA C  1 389 ? -19.220 55.747  27.037  1.00 32.36  ?  420  ALA C N   1 
ATOM   10416 C  CA  . ALA C  1 389 ? -20.137 56.854  26.769  1.00 34.39  ?  420  ALA C CA  1 
ATOM   10417 C  C   . ALA C  1 389 ? -19.343 58.130  26.536  1.00 37.90  ?  420  ALA C C   1 
ATOM   10418 O  O   . ALA C  1 389 ? -18.524 58.513  27.379  1.00 35.75  ?  420  ALA C O   1 
ATOM   10419 C  CB  . ALA C  1 389 ? -21.130 57.047  27.922  1.00 35.98  ?  420  ALA C CB  1 
ATOM   10420 N  N   . ARG C  1 390 ? -19.584 58.782  25.397  1.00 36.13  ?  421  ARG C N   1 
ATOM   10421 C  CA  . ARG C  1 390 ? -18.842 59.974  25.005  1.00 34.53  ?  421  ARG C CA  1 
ATOM   10422 C  C   . ARG C  1 390 ? -19.755 61.173  24.833  1.00 38.63  ?  421  ARG C C   1 
ATOM   10423 O  O   . ARG C  1 390 ? -20.778 61.092  24.134  1.00 40.19  ?  421  ARG C O   1 
ATOM   10424 C  CB  . ARG C  1 390 ? -18.078 59.767  23.701  1.00 34.53  ?  421  ARG C CB  1 
ATOM   10425 C  CG  . ARG C  1 390 ? -17.181 60.946  23.419  1.00 34.49  ?  421  ARG C CG  1 
ATOM   10426 C  CD  . ARG C  1 390 ? -16.625 60.923  22.049  1.00 36.82  ?  421  ARG C CD  1 
ATOM   10427 N  NE  . ARG C  1 390 ? -15.990 62.194  21.736  1.00 36.80  ?  421  ARG C NE  1 
ATOM   10428 C  CZ  . ARG C  1 390 ? -15.001 62.342  20.864  1.00 35.29  ?  421  ARG C CZ  1 
ATOM   10429 N  NH1 . ARG C  1 390 ? -14.496 61.309  20.206  1.00 34.07  ?  421  ARG C NH1 1 
ATOM   10430 N  NH2 . ARG C  1 390 ? -14.530 63.562  20.621  1.00 36.67  ?  421  ARG C NH2 1 
ATOM   10431 N  N   . MET C  1 391 ? -19.367 62.292  25.441  1.00 35.24  ?  422  MET C N   1 
ATOM   10432 C  CA  . MET C  1 391 ? -19.967 63.591  25.149  1.00 40.03  ?  422  MET C CA  1 
ATOM   10433 C  C   . MET C  1 391 ? -18.867 64.621  24.988  1.00 41.63  ?  422  MET C C   1 
ATOM   10434 O  O   . MET C  1 391 ? -18.056 64.818  25.903  1.00 43.41  ?  422  MET C O   1 
ATOM   10435 C  CB  . MET C  1 391 ? -20.942 64.036  26.231  1.00 45.66  ?  422  MET C CB  1 
ATOM   10436 C  CG  . MET C  1 391 ? -21.859 65.152  25.749  1.00 44.94  ?  422  MET C CG  1 
ATOM   10437 S  SD  . MET C  1 391 ? -22.742 65.889  27.115  1.00 52.95  ?  422  MET C SD  1 
ATOM   10438 C  CE  . MET C  1 391 ? -23.786 64.525  27.621  1.00 48.69  ?  422  MET C CE  1 
ATOM   10439 N  N   . GLY C  1 392 ? -18.860 65.282  23.835  1.00 40.11  ?  423  GLY C N   1 
ATOM   10440 C  CA  . GLY C  1 392 ? -17.835 66.276  23.562  1.00 40.59  ?  423  GLY C CA  1 
ATOM   10441 C  C   . GLY C  1 392 ? -16.455 65.678  23.729  1.00 40.62  ?  423  GLY C C   1 
ATOM   10442 O  O   . GLY C  1 392 ? -16.129 64.641  23.142  1.00 39.17  ?  423  GLY C O   1 
ATOM   10443 N  N   . ASP C  1 393 ? -15.625 66.330  24.546  1.00 39.66  ?  424  ASP C N   1 
ATOM   10444 C  CA  . ASP C  1 393 ? -14.253 65.868  24.731  1.00 39.35  ?  424  ASP C CA  1 
ATOM   10445 C  C   . ASP C  1 393 ? -14.120 64.747  25.749  1.00 39.93  ?  424  ASP C C   1 
ATOM   10446 O  O   . ASP C  1 393 ? -12.999 64.276  25.982  1.00 40.16  ?  424  ASP C O   1 
ATOM   10447 C  CB  . ASP C  1 393 ? -13.351 67.027  25.161  1.00 41.94  ?  424  ASP C CB  1 
ATOM   10448 C  CG  . ASP C  1 393 ? -13.107 68.014  24.043  1.00 46.54  ?  424  ASP C CG  1 
ATOM   10449 O  OD1 . ASP C  1 393 ? -12.816 67.571  22.908  1.00 42.90  ?  424  ASP C OD1 1 
ATOM   10450 O  OD2 . ASP C  1 393 ? -13.205 69.229  24.309  1.00 49.52  -1 424  ASP C OD2 1 
ATOM   10451 N  N   . TRP C  1 394 ? -15.209 64.313  26.362  1.00 37.76  ?  425  TRP C N   1 
ATOM   10452 C  CA  . TRP C  1 394 ? -15.133 63.458  27.532  1.00 41.30  ?  425  TRP C CA  1 
ATOM   10453 C  C   . TRP C  1 394 ? -15.762 62.101  27.255  1.00 41.79  ?  425  TRP C C   1 
ATOM   10454 O  O   . TRP C  1 394 ? -16.793 62.003  26.576  1.00 37.95  ?  425  TRP C O   1 
ATOM   10455 C  CB  . TRP C  1 394 ? -15.805 64.136  28.723  1.00 42.08  ?  425  TRP C CB  1 
ATOM   10456 C  CG  . TRP C  1 394 ? -15.065 65.383  29.109  1.00 47.63  ?  425  TRP C CG  1 
ATOM   10457 C  CD1 . TRP C  1 394 ? -15.341 66.662  28.706  1.00 47.93  ?  425  TRP C CD1 1 
ATOM   10458 C  CD2 . TRP C  1 394 ? -13.886 65.466  29.934  1.00 48.87  ?  425  TRP C CD2 1 
ATOM   10459 N  NE1 . TRP C  1 394 ? -14.424 67.537  29.256  1.00 50.21  ?  425  TRP C NE1 1 
ATOM   10460 C  CE2 . TRP C  1 394 ? -13.520 66.828  30.006  1.00 46.95  ?  425  TRP C CE2 1 
ATOM   10461 C  CE3 . TRP C  1 394 ? -13.118 64.521  30.632  1.00 45.03  ?  425  TRP C CE3 1 
ATOM   10462 C  CZ2 . TRP C  1 394 ? -12.418 67.272  30.752  1.00 49.20  ?  425  TRP C CZ2 1 
ATOM   10463 C  CZ3 . TRP C  1 394 ? -12.026 64.960  31.367  1.00 46.75  ?  425  TRP C CZ3 1 
ATOM   10464 C  CH2 . TRP C  1 394 ? -11.685 66.325  31.420  1.00 48.38  ?  425  TRP C CH2 1 
ATOM   10465 N  N   . LYS C  1 395 ? -15.129 61.053  27.784  1.00 40.27  ?  426  LYS C N   1 
ATOM   10466 C  CA  . LYS C  1 395 ? -15.632 59.692  27.665  1.00 35.43  ?  426  LYS C CA  1 
ATOM   10467 C  C   . LYS C  1 395 ? -15.526 58.996  29.011  1.00 37.51  ?  426  LYS C C   1 
ATOM   10468 O  O   . LYS C  1 395 ? -14.521 59.137  29.720  1.00 33.71  ?  426  LYS C O   1 
ATOM   10469 C  CB  . LYS C  1 395 ? -14.864 58.895  26.579  1.00 35.48  ?  426  LYS C CB  1 
ATOM   10470 C  CG  . LYS C  1 395 ? -15.522 57.565  26.211  1.00 37.41  ?  426  LYS C CG  1 
ATOM   10471 C  CD  . LYS C  1 395 ? -14.518 56.534  25.782  1.00 36.30  ?  426  LYS C CD  1 
ATOM   10472 C  CE  . LYS C  1 395 ? -15.184 55.178  25.576  1.00 37.77  ?  426  LYS C CE  1 
ATOM   10473 N  NZ  . LYS C  1 395 ? -14.281 54.205  24.888  1.00 34.45  ?  426  LYS C NZ  1 
ATOM   10474 N  N   . ILE C  1 396 ? -16.574 58.271  29.377  1.00 35.33  ?  427  ILE C N   1 
ATOM   10475 C  CA  . ILE C  1 396 ? -16.496 57.364  30.514  1.00 33.03  ?  427  ILE C CA  1 
ATOM   10476 C  C   . ILE C  1 396 ? -16.428 55.945  29.973  1.00 35.27  ?  427  ILE C C   1 
ATOM   10477 O  O   . ILE C  1 396 ? -16.991 55.632  28.910  1.00 36.01  ?  427  ILE C O   1 
ATOM   10478 C  CB  . ILE C  1 396 ? -17.659 57.536  31.513  1.00 37.10  ?  427  ILE C CB  1 
ATOM   10479 C  CG1 . ILE C  1 396 ? -19.003 57.326  30.826  1.00 34.96  ?  427  ILE C CG1 1 
ATOM   10480 C  CG2 . ILE C  1 396 ? -17.616 58.929  32.150  1.00 37.93  ?  427  ILE C CG2 1 
ATOM   10481 C  CD1 . ILE C  1 396 ? -20.125 57.119  31.817  1.00 36.86  ?  427  ILE C CD1 1 
ATOM   10482 N  N   . THR C  1 397 ? -15.693 55.095  30.690  1.00 33.60  ?  428  THR C N   1 
ATOM   10483 C  CA  . THR C  1 397 ? -15.437 53.727  30.260  1.00 33.49  ?  428  THR C CA  1 
ATOM   10484 C  C   . THR C  1 397 ? -15.399 52.803  31.466  1.00 36.58  ?  428  THR C C   1 
ATOM   10485 O  O   . THR C  1 397 ? -14.746 53.104  32.471  1.00 33.49  ?  428  THR C O   1 
ATOM   10486 C  CB  . THR C  1 397 ? -14.107 53.641  29.508  1.00 34.93  ?  428  THR C CB  1 
ATOM   10487 O  OG1 . THR C  1 397 ? -14.052 54.687  28.529  1.00 32.28  ?  428  THR C OG1 1 
ATOM   10488 C  CG2 . THR C  1 397 ? -13.939 52.262  28.838  1.00 32.55  ?  428  THR C CG2 1 
ATOM   10489 N  N   . ARG C  1 398 ? -16.065 51.661  31.358  1.00 31.20  ?  429  ARG C N   1 
ATOM   10490 C  CA  . ARG C  1 398 ? -15.864 50.583  32.314  1.00 29.34  ?  429  ARG C CA  1 
ATOM   10491 C  C   . ARG C  1 398 ? -15.560 49.316  31.529  1.00 34.13  ?  429  ARG C C   1 
ATOM   10492 O  O   . ARG C  1 398 ? -16.335 48.926  30.640  1.00 30.25  ?  429  ARG C O   1 
ATOM   10493 C  CB  . ARG C  1 398 ? -17.080 50.409  33.234  1.00 29.36  ?  429  ARG C CB  1 
ATOM   10494 C  CG  . ARG C  1 398 ? -16.864 49.357  34.325  1.00 32.44  ?  429  ARG C CG  1 
ATOM   10495 C  CD  . ARG C  1 398 ? -17.866 49.453  35.481  1.00 30.40  ?  429  ARG C CD  1 
ATOM   10496 N  NE  . ARG C  1 398 ? -17.431 48.662  36.628  1.00 32.53  ?  429  ARG C NE  1 
ATOM   10497 C  CZ  . ARG C  1 398 ? -18.249 48.131  37.531  1.00 32.98  ?  429  ARG C CZ  1 
ATOM   10498 N  NH1 . ARG C  1 398 ? -19.561 48.325  37.481  1.00 34.96  ?  429  ARG C NH1 1 
ATOM   10499 N  NH2 . ARG C  1 398 ? -17.743 47.387  38.504  1.00 34.78  ?  429  ARG C NH2 1 
ATOM   10500 N  N   . MET C  1 399 ? -14.403 48.716  31.807  1.00 30.42  ?  430  MET C N   1 
ATOM   10501 C  CA  . MET C  1 399 ? -14.009 47.470  31.162  1.00 31.11  ?  430  MET C CA  1 
ATOM   10502 C  C   . MET C  1 399 ? -13.577 46.435  32.174  1.00 33.58  ?  430  MET C C   1 
ATOM   10503 O  O   . MET C  1 399 ? -12.890 46.751  33.149  1.00 29.73  ?  430  MET C O   1 
ATOM   10504 C  CB  . MET C  1 399 ? -12.903 47.651  30.115  1.00 29.37  ?  430  MET C CB  1 
ATOM   10505 C  CG  . MET C  1 399 ? -13.495 48.299  28.889  1.00 31.99  ?  430  MET C CG  1 
ATOM   10506 S  SD  . MET C  1 399 ? -14.103 46.967  27.809  1.00 29.42  ?  430  MET C SD  1 
ATOM   10507 C  CE  . MET C  1 399 ? -12.716 45.826  27.742  1.00 32.20  ?  430  MET C CE  1 
ATOM   10508 N  N   . GLY C  1 400 ? -13.960 45.187  31.901  1.00 27.74  ?  431  GLY C N   1 
ATOM   10509 C  CA  . GLY C  1 400 ? -13.655 44.110  32.818  1.00 29.45  ?  431  GLY C CA  1 
ATOM   10510 C  C   . GLY C  1 400 ? -14.301 44.256  34.180  1.00 29.86  ?  431  GLY C C   1 
ATOM   10511 O  O   . GLY C  1 400 ? -13.899 43.564  35.111  1.00 30.14  ?  431  GLY C O   1 
ATOM   10512 N  N   . ASN C  1 401 ? -15.303 45.132  34.315  1.00 29.69  ?  432  ASN C N   1 
ATOM   10513 C  CA  . ASN C  1 401 ? -15.950 45.447  35.592  1.00 30.77  ?  432  ASN C CA  1 
ATOM   10514 C  C   . ASN C  1 401 ? -14.982 46.118  36.571  1.00 32.75  ?  432  ASN C C   1 
ATOM   10515 O  O   . ASN C  1 401 ? -15.190 46.092  37.791  1.00 30.24  ?  432  ASN C O   1 
ATOM   10516 C  CB  . ASN C  1 401 ? -16.595 44.198  36.220  1.00 32.02  ?  432  ASN C CB  1 
ATOM   10517 C  CG  . ASN C  1 401 ? -17.954 44.493  36.864  1.00 31.59  ?  432  ASN C CG  1 
ATOM   10518 O  OD1 . ASN C  1 401 ? -18.726 45.288  36.353  1.00 32.77  ?  432  ASN C OD1 1 
ATOM   10519 N  ND2 . ASN C  1 401 ? -18.236 43.850  37.991  1.00 35.38  ?  432  ASN C ND2 1 
ATOM   10520 N  N   . GLU C  1 402 ? -13.934 46.737  36.041  1.00 30.51  ?  433  GLU C N   1 
ATOM   10521 C  CA  . GLU C  1 402 ? -12.971 47.485  36.836  1.00 32.43  ?  433  GLU C CA  1 
ATOM   10522 C  C   . GLU C  1 402 ? -13.605 48.809  37.278  1.00 31.29  ?  433  GLU C C   1 
ATOM   10523 O  O   . GLU C  1 402 ? -14.719 49.143  36.860  1.00 33.29  ?  433  GLU C O   1 
ATOM   10524 C  CB  . GLU C  1 402 ? -11.705 47.715  36.008  1.00 33.31  ?  433  GLU C CB  1 
ATOM   10525 C  CG  . GLU C  1 402 ? -10.796 46.486  35.943  1.00 33.52  ?  433  GLU C CG  1 
ATOM   10526 C  CD  . GLU C  1 402 ? -10.201 46.144  37.293  1.00 36.30  ?  433  GLU C CD  1 
ATOM   10527 O  OE1 . GLU C  1 402 ? -9.336  46.925  37.744  1.00 37.19  ?  433  GLU C OE1 1 
ATOM   10528 O  OE2 . GLU C  1 402 ? -10.594 45.117  37.919  1.00 35.24  -1 433  GLU C OE2 1 
ATOM   10529 N  N   . PRO C  1 403 ? -12.937 49.565  38.156  1.00 31.39  ?  434  PRO C N   1 
ATOM   10530 C  CA  . PRO C  1 403 ? -13.424 50.908  38.496  1.00 32.47  ?  434  PRO C CA  1 
ATOM   10531 C  C   . PRO C  1 403 ? -13.668 51.774  37.264  1.00 31.74  ?  434  PRO C C   1 
ATOM   10532 O  O   . PRO C  1 403 ? -12.988 51.655  36.244  1.00 34.31  ?  434  PRO C O   1 
ATOM   10533 C  CB  . PRO C  1 403 ? -12.289 51.475  39.357  1.00 32.70  ?  434  PRO C CB  1 
ATOM   10534 C  CG  . PRO C  1 403 ? -11.766 50.249  40.086  1.00 32.08  ?  434  PRO C CG  1 
ATOM   10535 C  CD  . PRO C  1 403 ? -11.806 49.159  39.032  1.00 27.94  ?  434  PRO C CD  1 
ATOM   10536 N  N   . TRP C  1 404 ? -14.650 52.665  37.380  1.00 32.31  ?  435  TRP C N   1 
ATOM   10537 C  CA  . TRP C  1 404 ? -15.025 53.546  36.282  1.00 33.33  ?  435  TRP C CA  1 
ATOM   10538 C  C   . TRP C  1 404 ? -13.872 54.469  35.905  1.00 36.79  ?  435  TRP C C   1 
ATOM   10539 O  O   . TRP C  1 404 ? -13.073 54.884  36.752  1.00 38.99  ?  435  TRP C O   1 
ATOM   10540 C  CB  . TRP C  1 404 ? -16.257 54.368  36.675  1.00 36.55  ?  435  TRP C CB  1 
ATOM   10541 C  CG  . TRP C  1 404 ? -17.555 53.661  36.405  1.00 35.20  ?  435  TRP C CG  1 
ATOM   10542 C  CD1 . TRP C  1 404 ? -18.338 52.992  37.306  1.00 32.83  ?  435  TRP C CD1 1 
ATOM   10543 C  CD2 . TRP C  1 404 ? -18.228 53.570  35.140  1.00 35.34  ?  435  TRP C CD2 1 
ATOM   10544 N  NE1 . TRP C  1 404 ? -19.455 52.473  36.672  1.00 35.81  ?  435  TRP C NE1 1 
ATOM   10545 C  CE2 . TRP C  1 404 ? -19.413 52.820  35.346  1.00 35.33  ?  435  TRP C CE2 1 
ATOM   10546 C  CE3 . TRP C  1 404 ? -17.937 54.038  33.852  1.00 34.43  ?  435  TRP C CE3 1 
ATOM   10547 C  CZ2 . TRP C  1 404 ? -20.310 52.529  34.307  1.00 34.57  ?  435  TRP C CZ2 1 
ATOM   10548 C  CZ3 . TRP C  1 404 ? -18.836 53.756  32.820  1.00 33.66  ?  435  TRP C CZ3 1 
ATOM   10549 C  CH2 . TRP C  1 404 ? -20.004 53.007  33.057  1.00 34.65  ?  435  TRP C CH2 1 
ATOM   10550 N  N   . ARG C  1 405 ? -13.779 54.778  34.611  1.00 35.90  ?  436  ARG C N   1 
ATOM   10551 C  CA  . ARG C  1 405 ? -12.743 55.656  34.089  1.00 34.74  ?  436  ARG C CA  1 
ATOM   10552 C  C   . ARG C  1 405 ? -13.376 56.879  33.444  1.00 38.25  ?  436  ARG C C   1 
ATOM   10553 O  O   . ARG C  1 405 ? -14.416 56.778  32.776  1.00 39.53  ?  436  ARG C O   1 
ATOM   10554 C  CB  . ARG C  1 405 ? -11.870 54.938  33.065  1.00 36.63  ?  436  ARG C CB  1 
ATOM   10555 C  CG  . ARG C  1 405 ? -11.161 53.730  33.619  1.00 35.54  ?  436  ARG C CG  1 
ATOM   10556 C  CD  . ARG C  1 405 ? -10.461 52.945  32.509  1.00 35.77  ?  436  ARG C CD  1 
ATOM   10557 N  NE  . ARG C  1 405 ? -9.215  53.575  32.078  1.00 32.96  ?  436  ARG C NE  1 
ATOM   10558 C  CZ  . ARG C  1 405 ? -8.046  53.427  32.690  1.00 37.39  ?  436  ARG C CZ  1 
ATOM   10559 N  NH1 . ARG C  1 405 ? -7.929  52.713  33.803  1.00 33.29  ?  436  ARG C NH1 1 
ATOM   10560 N  NH2 . ARG C  1 405 ? -6.966  54.006  32.171  1.00 33.50  ?  436  ARG C NH2 1 
ATOM   10561 N  N   . LEU C  1 406 ? -12.751 58.032  33.657  1.00 34.98  ?  437  LEU C N   1 
ATOM   10562 C  CA  . LEU C  1 406 ? -13.077 59.263  32.946  1.00 33.65  ?  437  LEU C CA  1 
ATOM   10563 C  C   . LEU C  1 406 ? -11.860 59.683  32.147  1.00 33.65  ?  437  LEU C C   1 
ATOM   10564 O  O   . LEU C  1 406 ? -10.746 59.736  32.690  1.00 37.91  ?  437  LEU C O   1 
ATOM   10565 C  CB  . LEU C  1 406 ? -13.511 60.382  33.906  1.00 33.00  ?  437  LEU C CB  1 
ATOM   10566 C  CG  . LEU C  1 406 ? -13.780 61.739  33.242  1.00 39.25  ?  437  LEU C CG  1 
ATOM   10567 C  CD1 . LEU C  1 406 ? -15.083 61.707  32.445  1.00 34.77  ?  437  LEU C CD1 1 
ATOM   10568 C  CD2 . LEU C  1 406 ? -13.820 62.868  34.275  1.00 37.33  ?  437  LEU C CD2 1 
ATOM   10569 N  N   . HIS C  1 407 ? -12.059 59.943  30.859  1.00 35.01  ?  438  HIS C N   1 
ATOM   10570 C  CA  . HIS C  1 407 ? -10.971 60.342  29.981  1.00 36.75  ?  438  HIS C CA  1 
ATOM   10571 C  C   . HIS C  1 407 ? -11.358 61.594  29.218  1.00 40.52  ?  438  HIS C C   1 
ATOM   10572 O  O   . HIS C  1 407 ? -12.517 61.758  28.816  1.00 40.18  ?  438  HIS C O   1 
ATOM   10573 C  CB  . HIS C  1 407 ? -10.621 59.226  28.991  1.00 34.44  ?  438  HIS C CB  1 
ATOM   10574 C  CG  . HIS C  1 407 ? -10.096 57.997  29.646  1.00 37.59  ?  438  HIS C CG  1 
ATOM   10575 N  ND1 . HIS C  1 407 ? -8.921  57.993  30.372  1.00 38.67  ?  438  HIS C ND1 1 
ATOM   10576 C  CD2 . HIS C  1 407 ? -10.598 56.741  29.725  1.00 35.92  ?  438  HIS C CD2 1 
ATOM   10577 C  CE1 . HIS C  1 407 ? -8.716  56.781  30.857  1.00 39.75  ?  438  HIS C CE1 1 
ATOM   10578 N  NE2 . HIS C  1 407 ? -9.715  56.001  30.477  1.00 38.30  ?  438  HIS C NE2 1 
ATOM   10579 N  N   . ASN C  1 408 ? -10.394 62.482  29.013  1.00 42.02  ?  439  ASN C N   1 
ATOM   10580 C  CA  . ASN C  1 408 ? -10.587 63.517  28.006  1.00 40.80  ?  439  ASN C CA  1 
ATOM   10581 C  C   . ASN C  1 408 ? -10.078 62.853  26.736  1.00 38.52  ?  439  ASN C C   1 
ATOM   10582 O  O   . ASN C  1 408 ? -8.868  62.792  26.484  1.00 35.64  ?  439  ASN C O   1 
ATOM   10583 C  CB  . ASN C  1 408 ? -9.864  64.812  28.365  1.00 43.52  ?  439  ASN C CB  1 
ATOM   10584 C  CG  . ASN C  1 408 ? -9.776  65.802  27.195  1.00 43.81  ?  439  ASN C CG  1 
ATOM   10585 O  OD1 . ASN C  1 408 ? -9.628  65.442  26.026  1.00 44.10  ?  439  ASN C OD1 1 
ATOM   10586 N  ND2 . ASN C  1 408 ? -9.909  67.076  27.528  1.00 50.96  ?  439  ASN C ND2 1 
ATOM   10587 N  N   . ILE C  1 409 ? -11.011 62.291  25.959  1.00 39.37  ?  440  ILE C N   1 
ATOM   10588 C  CA  . ILE C  1 409 ? -10.623 61.470  24.821  1.00 35.46  ?  440  ILE C CA  1 
ATOM   10589 C  C   . ILE C  1 409 ? -9.917  62.301  23.762  1.00 33.71  ?  440  ILE C C   1 
ATOM   10590 O  O   . ILE C  1 409 ? -9.184  61.756  22.923  1.00 37.14  ?  440  ILE C O   1 
ATOM   10591 C  CB  . ILE C  1 409 ? -11.868 60.741  24.262  1.00 33.07  ?  440  ILE C CB  1 
ATOM   10592 C  CG1 . ILE C  1 409 ? -11.445 59.535  23.419  1.00 30.73  ?  440  ILE C CG1 1 
ATOM   10593 C  CG2 . ILE C  1 409 ? -12.766 61.715  23.489  1.00 34.07  ?  440  ILE C CG2 1 
ATOM   10594 C  CD1 . ILE C  1 409 ? -10.687 58.459  24.213  1.00 34.93  ?  440  ILE C CD1 1 
ATOM   10595 N  N   . THR C  1 410 ? -10.105 63.620  23.788  1.00 35.65  ?  441  THR C N   1 
ATOM   10596 C  CA  . THR C  1 410 ? -9.452  64.472  22.804  1.00 34.87  ?  441  THR C CA  1 
ATOM   10597 C  C   . THR C  1 410 ? -7.964  64.593  23.092  1.00 37.72  ?  441  THR C C   1 
ATOM   10598 O  O   . THR C  1 410 ? -7.141  64.601  22.170  1.00 35.65  ?  441  THR C O   1 
ATOM   10599 C  CB  . THR C  1 410 ? -10.124 65.845  22.793  1.00 39.79  ?  441  THR C CB  1 
ATOM   10600 O  OG1 . THR C  1 410 ? -11.510 65.685  22.454  1.00 39.88  ?  441  THR C OG1 1 
ATOM   10601 C  CG2 . THR C  1 410 ? -9.445  66.766  21.783  1.00 41.77  ?  441  THR C CG2 1 
ATOM   10602 N  N   . GLN C  1 411 ? -7.610  64.664  24.369  1.00 38.42  ?  442  GLN C N   1 
ATOM   10603 C  CA  . GLN C  1 411 ? -6.225  64.807  24.803  1.00 38.52  ?  442  GLN C CA  1 
ATOM   10604 C  C   . GLN C  1 411 ? -5.547  63.464  25.004  1.00 43.75  ?  442  GLN C C   1 
ATOM   10605 O  O   . GLN C  1 411 ? -4.313  63.376  24.927  1.00 40.56  ?  442  GLN C O   1 
ATOM   10606 C  CB  . GLN C  1 411 ? -6.206  65.576  26.130  1.00 43.12  ?  442  GLN C CB  1 
ATOM   10607 C  CG  . GLN C  1 411 ? -6.418  67.087  26.030  1.00 48.53  ?  442  GLN C CG  1 
ATOM   10608 C  CD  . GLN C  1 411 ? -5.735  67.800  24.860  1.00 54.14  ?  442  GLN C CD  1 
ATOM   10609 O  OE1 . GLN C  1 411 ? -6.165  68.893  24.476  1.00 60.96  ?  442  GLN C OE1 1 
ATOM   10610 N  NE2 . GLN C  1 411 ? -4.612  67.266  24.381  1.00 59.35  ?  442  GLN C NE2 1 
ATOM   10611 N  N   . ASP C  1 412 ? -6.334  62.417  25.257  1.00 40.09  ?  443  ASP C N   1 
ATOM   10612 C  CA  . ASP C  1 412 ? -5.851  61.136  25.731  1.00 36.06  ?  443  ASP C CA  1 
ATOM   10613 C  C   . ASP C  1 412 ? -6.645  60.081  24.949  1.00 37.45  ?  443  ASP C C   1 
ATOM   10614 O  O   . ASP C  1 412 ? -7.536  59.431  25.483  1.00 37.42  ?  443  ASP C O   1 
ATOM   10615 C  CB  . ASP C  1 412 ? -6.043  61.029  27.248  1.00 34.14  ?  443  ASP C CB  1 
ATOM   10616 C  CG  . ASP C  1 412 ? -5.801  59.640  27.795  1.00 34.24  ?  443  ASP C CG  1 
ATOM   10617 O  OD1 . ASP C  1 412 ? -4.987  58.903  27.217  1.00 31.66  ?  443  ASP C OD1 1 
ATOM   10618 O  OD2 . ASP C  1 412 ? -6.425  59.309  28.830  1.00 34.17  -1 443  ASP C OD2 1 
ATOM   10619 N  N   . ILE C  1 413 ? -6.323  59.942  23.659  1.00 31.07  ?  444  ILE C N   1 
ATOM   10620 C  CA  . ILE C  1 413 ? -7.097  59.078  22.782  1.00 37.95  ?  444  ILE C CA  1 
ATOM   10621 C  C   . ILE C  1 413 ? -6.880  57.602  23.102  1.00 38.48  ?  444  ILE C C   1 
ATOM   10622 O  O   . ILE C  1 413 ? -7.721  56.768  22.744  1.00 34.02  ?  444  ILE C O   1 
ATOM   10623 C  CB  . ILE C  1 413 ? -6.763  59.378  21.306  1.00 35.60  ?  444  ILE C CB  1 
ATOM   10624 C  CG1 . ILE C  1 413 ? -7.834  58.779  20.382  1.00 33.31  ?  444  ILE C CG1 1 
ATOM   10625 C  CG2 . ILE C  1 413 ? -5.347  58.893  20.950  1.00 36.39  ?  444  ILE C CG2 1 
ATOM   10626 C  CD1 . ILE C  1 413 ? -7.528  58.927  18.899  1.00 32.18  ?  444  ILE C CD1 1 
ATOM   10627 N  N   . GLY C  1 414 ? -5.776  57.262  23.774  1.00 34.97  ?  445  GLY C N   1 
ATOM   10628 C  CA  . GLY C  1 414 ? -5.463  55.908  24.187  1.00 30.75  ?  445  GLY C CA  1 
ATOM   10629 C  C   . GLY C  1 414 ? -6.080  55.474  25.493  1.00 35.36  ?  445  GLY C C   1 
ATOM   10630 O  O   . GLY C  1 414 ? -5.794  54.360  25.945  1.00 35.11  ?  445  GLY C O   1 
ATOM   10631 N  N   . GLU C  1 415 ? -6.895  56.335  26.116  1.00 30.10  ?  446  GLU C N   1 
ATOM   10632 C  CA  . GLU C  1 415 ? -7.555  56.061  27.394  1.00 33.62  ?  446  GLU C CA  1 
ATOM   10633 C  C   . GLU C  1 415 ? -6.555  55.569  28.448  1.00 34.89  ?  446  GLU C C   1 
ATOM   10634 O  O   . GLU C  1 415 ? -6.763  54.563  29.137  1.00 31.64  ?  446  GLU C O   1 
ATOM   10635 C  CB  . GLU C  1 415 ? -8.726  55.080  27.210  1.00 31.37  ?  446  GLU C CB  1 
ATOM   10636 C  CG  . GLU C  1 415 ? -9.780  55.641  26.259  1.00 32.88  ?  446  GLU C CG  1 
ATOM   10637 C  CD  . GLU C  1 415 ? -10.812 54.616  25.830  1.00 31.86  ?  446  GLU C CD  1 
ATOM   10638 O  OE1 . GLU C  1 415 ? -10.518 53.868  24.876  1.00 29.06  ?  446  GLU C OE1 1 
ATOM   10639 O  OE2 . GLU C  1 415 ? -11.901 54.562  26.458  1.00 33.46  -1 446  GLU C OE2 1 
ATOM   10640 N  N   . LYS C  1 416 ? -5.472  56.334  28.607  1.00 34.20  ?  447  LYS C N   1 
ATOM   10641 C  CA  . LYS C  1 416 ? -4.408  55.983  29.549  1.00 29.53  ?  447  LYS C CA  1 
ATOM   10642 C  C   . LYS C  1 416 ? -4.535  56.650  30.908  1.00 35.82  ?  447  LYS C C   1 
ATOM   10643 O  O   . LYS C  1 416 ? -4.044  56.099  31.903  1.00 35.65  ?  447  LYS C O   1 
ATOM   10644 C  CB  . LYS C  1 416 ? -3.040  56.351  28.957  1.00 35.59  ?  447  LYS C CB  1 
ATOM   10645 C  CG  . LYS C  1 416 ? -2.766  55.694  27.608  1.00 33.51  ?  447  LYS C CG  1 
ATOM   10646 C  CD  . LYS C  1 416 ? -1.282  55.604  27.299  1.00 36.15  ?  447  LYS C CD  1 
ATOM   10647 C  CE  . LYS C  1 416 ? -1.078  55.463  25.805  1.00 40.75  ?  447  LYS C CE  1 
ATOM   10648 N  NZ  . LYS C  1 416 ? 0.351   55.480  25.420  1.00 41.40  ?  447  LYS C NZ  1 
ATOM   10649 N  N   . LYS C  1 417 ? -5.165  57.820  30.983  1.00 34.36  ?  448  LYS C N   1 
ATOM   10650 C  CA  . LYS C  1 417 ? -5.090  58.680  32.158  1.00 34.51  ?  448  LYS C CA  1 
ATOM   10651 C  C   . LYS C  1 417 ? -6.471  58.830  32.774  1.00 33.29  ?  448  LYS C C   1 
ATOM   10652 O  O   . LYS C  1 417 ? -7.237  59.718  32.404  1.00 35.04  ?  448  LYS C O   1 
ATOM   10653 C  CB  . LYS C  1 417 ? -4.496  60.031  31.774  1.00 36.96  ?  448  LYS C CB  1 
ATOM   10654 C  CG  . LYS C  1 417 ? -3.261  59.904  30.897  1.00 38.62  ?  448  LYS C CG  1 
ATOM   10655 C  CD  . LYS C  1 417 ? -2.113  59.278  31.699  1.00 43.40  ?  448  LYS C CD  1 
ATOM   10656 C  CE  . LYS C  1 417 ? -0.908  58.982  30.807  1.00 41.52  ?  448  LYS C CE  1 
ATOM   10657 N  NZ  . LYS C  1 417 ? 0.314   58.739  31.616  1.00 48.01  ?  448  LYS C NZ  1 
ATOM   10658 N  N   . ASN C  1 418 ? -6.774  57.986  33.753  1.00 35.86  ?  449  ASN C N   1 
ATOM   10659 C  CA  . ASN C  1 418 ? -8.075  58.033  34.403  1.00 36.27  ?  449  ASN C CA  1 
ATOM   10660 C  C   . ASN C  1 418 ? -8.184  59.304  35.243  1.00 40.47  ?  449  ASN C C   1 
ATOM   10661 O  O   . ASN C  1 418 ? -7.422  59.490  36.199  1.00 33.59  ?  449  ASN C O   1 
ATOM   10662 C  CB  . ASN C  1 418 ? -8.268  56.790  35.270  1.00 34.11  ?  449  ASN C CB  1 
ATOM   10663 C  CG  . ASN C  1 418 ? -9.689  56.659  35.790  1.00 39.32  ?  449  ASN C CG  1 
ATOM   10664 O  OD1 . ASN C  1 418 ? -10.534 57.504  35.519  1.00 36.78  ?  449  ASN C OD1 1 
ATOM   10665 N  ND2 . ASN C  1 418 ? -9.950  55.611  36.562  1.00 38.40  ?  449  ASN C ND2 1 
ATOM   10666 N  N   . LEU C  1 419 ? -9.124  60.174  34.880  1.00 36.97  ?  450  LEU C N   1 
ATOM   10667 C  CA  . LEU C  1 419 ? -9.365  61.444  35.556  1.00 36.34  ?  450  LEU C CA  1 
ATOM   10668 C  C   . LEU C  1 419 ? -10.546 61.376  36.510  1.00 37.27  ?  450  LEU C C   1 
ATOM   10669 O  O   . LEU C  1 419 ? -11.030 62.420  36.957  1.00 41.25  ?  450  LEU C O   1 
ATOM   10670 C  CB  . LEU C  1 419 ? -9.595  62.543  34.518  1.00 36.55  ?  450  LEU C CB  1 
ATOM   10671 C  CG  . LEU C  1 419 ? -8.512  62.719  33.459  1.00 37.25  ?  450  LEU C CG  1 
ATOM   10672 C  CD1 . LEU C  1 419 ? -8.681  64.033  32.732  1.00 41.98  ?  450  LEU C CD1 1 
ATOM   10673 C  CD2 . LEU C  1 419 ? -7.134  62.676  34.118  1.00 49.25  ?  450  LEU C CD2 1 
ATOM   10674 N  N   . ALA C  1 420 ? -11.010 60.169  36.848  1.00 35.60  ?  451  ALA C N   1 
ATOM   10675 C  CA  . ALA C  1 420 ? -12.231 60.025  37.643  1.00 41.90  ?  451  ALA C CA  1 
ATOM   10676 C  C   . ALA C  1 420 ? -12.098 60.653  39.028  1.00 44.42  ?  451  ALA C C   1 
ATOM   10677 O  O   . ALA C  1 420 ? -13.073 61.196  39.559  1.00 47.14  ?  451  ALA C O   1 
ATOM   10678 C  CB  . ALA C  1 420 ? -12.604 58.548  37.773  1.00 38.79  ?  451  ALA C CB  1 
ATOM   10679 N  N   . GLY C  1 421 ? -10.915 60.575  39.640  1.00 48.25  ?  452  GLY C N   1 
ATOM   10680 C  CA  . GLY C  1 421 ? -10.723 61.223  40.929  1.00 45.28  ?  452  GLY C CA  1 
ATOM   10681 C  C   . GLY C  1 421 ? -10.615 62.729  40.837  1.00 43.88  ?  452  GLY C C   1 
ATOM   10682 O  O   . GLY C  1 421 ? -11.007 63.437  41.769  1.00 49.05  ?  452  GLY C O   1 
ATOM   10683 N  N   . ARG C  1 422 ? -10.104 63.242  39.716  1.00 44.54  ?  453  ARG C N   1 
ATOM   10684 C  CA  . ARG C  1 422 ? -9.919  64.676  39.562  1.00 47.62  ?  453  ARG C CA  1 
ATOM   10685 C  C   . ARG C  1 422 ? -11.234 65.397  39.267  1.00 54.20  ?  453  ARG C C   1 
ATOM   10686 O  O   . ARG C  1 422 ? -11.417 66.542  39.695  1.00 56.94  ?  453  ARG C O   1 
ATOM   10687 C  CB  . ARG C  1 422 ? -8.878  64.943  38.465  1.00 49.65  ?  453  ARG C CB  1 
ATOM   10688 C  CG  . ARG C  1 422 ? -8.702  66.408  38.091  1.00 55.70  ?  453  ARG C CG  1 
ATOM   10689 C  CD  . ARG C  1 422 ? -7.234  66.865  38.045  1.00 62.13  ?  453  ARG C CD  1 
ATOM   10690 N  NE  . ARG C  1 422 ? -6.377  66.009  37.234  1.00 62.76  ?  453  ARG C NE  1 
ATOM   10691 C  CZ  . ARG C  1 422 ? -5.107  65.742  37.508  1.00 69.23  ?  453  ARG C CZ  1 
ATOM   10692 N  NH1 . ARG C  1 422 ? -4.516  66.229  38.588  1.00 76.42  ?  453  ARG C NH1 1 
ATOM   10693 N  NH2 . ARG C  1 422 ? -4.413  64.964  36.681  1.00 66.53  ?  453  ARG C NH2 1 
ATOM   10694 N  N   . TYR C  1 423 ? -12.172 64.747  38.580  1.00 48.67  ?  454  TYR C N   1 
ATOM   10695 C  CA  . TYR C  1 423 ? -13.441 65.365  38.188  1.00 47.26  ?  454  TYR C CA  1 
ATOM   10696 C  C   . TYR C  1 423 ? -14.613 64.446  38.521  1.00 47.87  ?  454  TYR C C   1 
ATOM   10697 O  O   . TYR C  1 423 ? -15.352 64.011  37.634  1.00 46.89  ?  454  TYR C O   1 
ATOM   10698 C  CB  . TYR C  1 423 ? -13.401 65.699  36.700  1.00 45.41  ?  454  TYR C CB  1 
ATOM   10699 C  CG  . TYR C  1 423 ? -12.218 66.563  36.313  1.00 49.79  ?  454  TYR C CG  1 
ATOM   10700 C  CD1 . TYR C  1 423 ? -11.937 67.741  36.995  1.00 52.44  ?  454  TYR C CD1 1 
ATOM   10701 C  CD2 . TYR C  1 423 ? -11.425 66.236  35.222  1.00 49.41  ?  454  TYR C CD2 1 
ATOM   10702 C  CE1 . TYR C  1 423 ? -10.862 68.548  36.631  1.00 54.80  ?  454  TYR C CE1 1 
ATOM   10703 C  CE2 . TYR C  1 423 ? -10.346 67.023  34.854  1.00 52.40  ?  454  TYR C CE2 1 
ATOM   10704 C  CZ  . TYR C  1 423 ? -10.073 68.184  35.554  1.00 61.23  ?  454  TYR C CZ  1 
ATOM   10705 O  OH  . TYR C  1 423 ? -9.005  68.972  35.176  1.00 58.90  ?  454  TYR C OH  1 
ATOM   10706 N  N   . PRO C  1 424 ? -14.821 64.138  39.804  1.00 46.99  ?  455  PRO C N   1 
ATOM   10707 C  CA  . PRO C  1 424 ? -15.884 63.183  40.147  1.00 47.55  ?  455  PRO C CA  1 
ATOM   10708 C  C   . PRO C  1 424 ? -17.269 63.650  39.740  1.00 49.66  ?  455  PRO C C   1 
ATOM   10709 O  O   . PRO C  1 424 ? -18.119 62.806  39.432  1.00 47.01  ?  455  PRO C O   1 
ATOM   10710 C  CB  . PRO C  1 424 ? -15.762 63.044  41.669  1.00 48.88  ?  455  PRO C CB  1 
ATOM   10711 C  CG  . PRO C  1 424 ? -15.068 64.261  42.115  1.00 48.48  ?  455  PRO C CG  1 
ATOM   10712 C  CD  . PRO C  1 424 ? -14.139 64.654  41.003  1.00 49.78  ?  455  PRO C CD  1 
ATOM   10713 N  N   . ASP C  1 425 ? -17.523 64.963  39.712  1.00 48.54  ?  456  ASP C N   1 
ATOM   10714 C  CA  . ASP C  1 425 ? -18.860 65.441  39.365  1.00 50.99  ?  456  ASP C CA  1 
ATOM   10715 C  C   . ASP C  1 425 ? -19.179 65.173  37.903  1.00 46.36  ?  456  ASP C C   1 
ATOM   10716 O  O   . ASP C  1 425 ? -20.294 64.756  37.575  1.00 49.59  ?  456  ASP C O   1 
ATOM   10717 C  CB  . ASP C  1 425 ? -18.997 66.932  39.662  1.00 54.12  ?  456  ASP C CB  1 
ATOM   10718 C  CG  . ASP C  1 425 ? -18.828 67.252  41.135  1.00 60.59  ?  456  ASP C CG  1 
ATOM   10719 O  OD1 . ASP C  1 425 ? -19.239 66.422  41.981  1.00 59.93  ?  456  ASP C OD1 1 
ATOM   10720 O  OD2 . ASP C  1 425 ? -18.281 68.336  41.442  1.00 64.48  -1 456  ASP C OD2 1 
ATOM   10721 N  N   . ARG C  1 426 ? -18.225 65.424  37.009  1.00 46.60  ?  457  ARG C N   1 
ATOM   10722 C  CA  . ARG C  1 426 ? -18.456 65.126  35.601  1.00 50.97  ?  457  ARG C CA  1 
ATOM   10723 C  C   . ARG C  1 426 ? -18.684 63.632  35.399  1.00 47.91  ?  457  ARG C C   1 
ATOM   10724 O  O   . ARG C  1 426 ? -19.620 63.222  34.709  1.00 45.07  ?  457  ARG C O   1 
ATOM   10725 C  CB  . ARG C  1 426 ? -17.278 65.612  34.758  1.00 42.61  ?  457  ARG C CB  1 
ATOM   10726 C  CG  . ARG C  1 426 ? -17.433 65.294  33.293  1.00 49.59  ?  457  ARG C CG  1 
ATOM   10727 C  CD  . ARG C  1 426 ? -16.253 65.798  32.504  1.00 47.87  ?  457  ARG C CD  1 
ATOM   10728 N  NE  . ARG C  1 426 ? -16.061 67.237  32.639  1.00 56.54  ?  457  ARG C NE  1 
ATOM   10729 C  CZ  . ARG C  1 426 ? -16.645 68.152  31.877  1.00 55.12  ?  457  ARG C CZ  1 
ATOM   10730 N  NH1 . ARG C  1 426 ? -17.448 67.812  30.885  1.00 50.85  ?  457  ARG C NH1 1 
ATOM   10731 N  NH2 . ARG C  1 426 ? -16.403 69.442  32.107  1.00 54.27  ?  457  ARG C NH2 1 
ATOM   10732 N  N   . LEU C  1 427 ? -17.833 62.799  36.000  1.00 47.78  ?  458  LEU C N   1 
ATOM   10733 C  CA  . LEU C  1 427 ? -18.032 61.357  35.890  1.00 46.43  ?  458  LEU C CA  1 
ATOM   10734 C  C   . LEU C  1 427 ? -19.431 60.964  36.348  1.00 45.10  ?  458  LEU C C   1 
ATOM   10735 O  O   . LEU C  1 427 ? -20.159 60.262  35.634  1.00 42.81  ?  458  LEU C O   1 
ATOM   10736 C  CB  . LEU C  1 427 ? -16.966 60.610  36.697  1.00 42.57  ?  458  LEU C CB  1 
ATOM   10737 C  CG  . LEU C  1 427 ? -17.336 59.153  37.010  1.00 44.44  ?  458  LEU C CG  1 
ATOM   10738 C  CD1 . LEU C  1 427 ? -17.082 58.268  35.799  1.00 42.37  ?  458  LEU C CD1 1 
ATOM   10739 C  CD2 . LEU C  1 427 ? -16.567 58.627  38.215  1.00 47.81  ?  458  LEU C CD2 1 
ATOM   10740 N  N   . LYS C  1 428 ? -19.839 61.431  37.527  1.00 43.24  ?  459  LYS C N   1 
ATOM   10741 C  CA  . LYS C  1 428 ? -21.126 60.990  38.049  1.00 49.10  ?  459  LYS C CA  1 
ATOM   10742 C  C   . LYS C  1 428 ? -22.290 61.503  37.209  1.00 48.00  ?  459  LYS C C   1 
ATOM   10743 O  O   . LYS C  1 428 ? -23.317 60.824  37.110  1.00 47.55  ?  459  LYS C O   1 
ATOM   10744 C  CB  . LYS C  1 428 ? -21.276 61.404  39.510  1.00 50.16  ?  459  LYS C CB  1 
ATOM   10745 C  CG  . LYS C  1 428 ? -20.295 60.675  40.400  1.00 51.49  ?  459  LYS C CG  1 
ATOM   10746 C  CD  . LYS C  1 428 ? -20.846 60.408  41.780  1.00 51.12  ?  459  LYS C CD  1 
ATOM   10747 C  CE  . LYS C  1 428 ? -19.807 59.665  42.622  1.00 48.11  ?  459  LYS C CE  1 
ATOM   10748 N  NZ  . LYS C  1 428 ? -20.309 59.396  43.993  1.00 53.06  ?  459  LYS C NZ  1 
ATOM   10749 N  N   . GLU C  1 429 ? -22.147 62.678  36.585  1.00 48.90  ?  460  GLU C N   1 
ATOM   10750 C  CA  . GLU C  1 429 ? -23.188 63.155  35.675  1.00 49.51  ?  460  GLU C CA  1 
ATOM   10751 C  C   . GLU C  1 429 ? -23.260 62.287  34.430  1.00 43.77  ?  460  GLU C C   1 
ATOM   10752 O  O   . GLU C  1 429 ? -24.351 61.933  33.968  1.00 44.96  ?  460  GLU C O   1 
ATOM   10753 C  CB  . GLU C  1 429 ? -22.936 64.614  35.288  1.00 50.07  ?  460  GLU C CB  1 
ATOM   10754 N  N   . MET C  1 430 ? -22.106 61.932  33.872  1.00 41.27  ?  461  MET C N   1 
ATOM   10755 C  CA  . MET C  1 430 ? -22.094 61.121  32.662  1.00 41.32  ?  461  MET C CA  1 
ATOM   10756 C  C   . MET C  1 430 ? -22.648 59.727  32.932  1.00 41.15  ?  461  MET C C   1 
ATOM   10757 O  O   . MET C  1 430 ? -23.350 59.151  32.088  1.00 41.93  ?  461  MET C O   1 
ATOM   10758 C  CB  . MET C  1 430 ? -20.670 61.081  32.133  1.00 41.81  ?  461  MET C CB  1 
ATOM   10759 C  CG  . MET C  1 430 ? -20.299 62.389  31.473  1.00 41.74  ?  461  MET C CG  1 
ATOM   10760 S  SD  . MET C  1 430 ? -18.683 62.361  30.712  1.00 45.47  ?  461  MET C SD  1 
ATOM   10761 C  CE  . MET C  1 430 ? -19.047 61.526  29.161  1.00 38.42  ?  461  MET C CE  1 
ATOM   10762 N  N   . ILE C  1 431 ? -22.383 59.193  34.122  1.00 39.62  ?  462  ILE C N   1 
ATOM   10763 C  CA  . ILE C  1 431 ? -22.919 57.892  34.502  1.00 41.72  ?  462  ILE C CA  1 
ATOM   10764 C  C   . ILE C  1 431 ? -24.433 57.951  34.675  1.00 44.54  ?  462  ILE C C   1 
ATOM   10765 O  O   . ILE C  1 431 ? -25.148 57.032  34.259  1.00 42.54  ?  462  ILE C O   1 
ATOM   10766 C  CB  . ILE C  1 431 ? -22.203 57.392  35.769  1.00 43.52  ?  462  ILE C CB  1 
ATOM   10767 C  CG1 . ILE C  1 431 ? -20.945 56.630  35.346  1.00 44.71  ?  462  ILE C CG1 1 
ATOM   10768 C  CG2 . ILE C  1 431 ? -23.134 56.544  36.659  1.00 37.41  ?  462  ILE C CG2 1 
ATOM   10769 C  CD1 . ILE C  1 431 ? -20.094 56.199  36.475  1.00 39.99  ?  462  ILE C CD1 1 
ATOM   10770 N  N   . ALA C  1 432 ? -24.945 59.026  35.289  1.00 47.92  ?  463  ALA C N   1 
ATOM   10771 C  CA  . ALA C  1 432 ? -26.390 59.171  35.465  1.00 44.86  ?  463  ALA C CA  1 
ATOM   10772 C  C   . ALA C  1 432 ? -27.112 59.151  34.126  1.00 43.48  ?  463  ALA C C   1 
ATOM   10773 O  O   . ALA C  1 432 ? -28.128 58.464  33.960  1.00 43.71  ?  463  ALA C O   1 
ATOM   10774 C  CB  . ALA C  1 432 ? -26.700 60.465  36.218  1.00 42.79  ?  463  ALA C CB  1 
ATOM   10775 N  N   . LYS C  1 433 ? -26.600 59.908  33.157  1.00 42.14  ?  464  LYS C N   1 
ATOM   10776 C  CA  . LYS C  1 433 ? -27.188 59.927  31.825  1.00 44.08  ?  464  LYS C CA  1 
ATOM   10777 C  C   . LYS C  1 433 ? -27.188 58.531  31.202  1.00 44.12  ?  464  LYS C C   1 
ATOM   10778 O  O   . LYS C  1 433 ? -28.208 58.070  30.668  1.00 41.54  ?  464  LYS C O   1 
ATOM   10779 C  CB  . LYS C  1 433 ? -26.417 60.922  30.953  1.00 41.27  ?  464  LYS C CB  1 
ATOM   10780 C  CG  . LYS C  1 433 ? -27.145 61.357  29.688  1.00 51.07  ?  464  LYS C CG  1 
ATOM   10781 C  CD  . LYS C  1 433 ? -26.882 62.834  29.385  1.00 58.89  ?  464  LYS C CD  1 
ATOM   10782 C  CE  . LYS C  1 433 ? -27.393 63.751  30.500  1.00 60.99  ?  464  LYS C CE  1 
ATOM   10783 N  NZ  . LYS C  1 433 ? -26.796 65.126  30.422  1.00 64.44  ?  464  LYS C NZ  1 
ATOM   10784 N  N   . THR C  1 434 ? -26.051 57.835  31.294  1.00 39.97  ?  465  THR C N   1 
ATOM   10785 C  CA  . THR C  1 434 ? -25.916 56.494  30.732  1.00 38.49  ?  465  THR C CA  1 
ATOM   10786 C  C   . THR C  1 434 ? -26.828 55.493  31.441  1.00 38.95  ?  465  THR C C   1 
ATOM   10787 O  O   . THR C  1 434 ? -27.408 54.604  30.805  1.00 41.99  ?  465  THR C O   1 
ATOM   10788 C  CB  . THR C  1 434 ? -24.448 56.060  30.830  1.00 38.40  ?  465  THR C CB  1 
ATOM   10789 O  OG1 . THR C  1 434 ? -23.625 57.014  30.146  1.00 38.16  ?  465  THR C OG1 1 
ATOM   10790 C  CG2 . THR C  1 434 ? -24.239 54.690  30.198  1.00 40.37  ?  465  THR C CG2 1 
ATOM   10791 N  N   . GLN C  1 435 ? -26.951 55.606  32.766  1.00 39.62  ?  466  GLN C N   1 
ATOM   10792 C  CA  . GLN C  1 435 ? -27.879 54.746  33.493  1.00 40.81  ?  466  GLN C CA  1 
ATOM   10793 C  C   . GLN C  1 435 ? -29.316 54.991  33.037  1.00 44.64  ?  466  GLN C C   1 
ATOM   10794 O  O   . GLN C  1 435 ? -30.096 54.046  32.860  1.00 42.97  ?  466  GLN C O   1 
ATOM   10795 C  CB  . GLN C  1 435 ? -27.744 54.982  34.998  1.00 40.82  ?  466  GLN C CB  1 
ATOM   10796 C  CG  . GLN C  1 435 ? -28.860 54.354  35.803  1.00 43.23  ?  466  GLN C CG  1 
ATOM   10797 C  CD  . GLN C  1 435 ? -28.406 53.846  37.136  1.00 45.89  ?  466  GLN C CD  1 
ATOM   10798 O  OE1 . GLN C  1 435 ? -27.696 54.538  37.869  1.00 49.76  ?  466  GLN C OE1 1 
ATOM   10799 N  NE2 . GLN C  1 435 ? -28.804 52.626  37.469  1.00 47.88  ?  466  GLN C NE2 1 
ATOM   10800 N  N   . GLU C  1 436 ? -29.674 56.258  32.832  1.00 45.11  ?  467  GLU C N   1 
ATOM   10801 C  CA  . GLU C  1 436 ? -31.002 56.583  32.321  1.00 43.31  ?  467  GLU C CA  1 
ATOM   10802 C  C   . GLU C  1 436 ? -31.244 55.909  30.976  1.00 43.71  ?  467  GLU C C   1 
ATOM   10803 O  O   . GLU C  1 436 ? -32.301 55.304  30.751  1.00 43.09  ?  467  GLU C O   1 
ATOM   10804 C  CB  . GLU C  1 436 ? -31.151 58.102  32.210  1.00 46.64  ?  467  GLU C CB  1 
ATOM   10805 C  CG  . GLU C  1 436 ? -32.608 58.592  32.130  1.00 53.77  ?  467  GLU C CG  1 
ATOM   10806 C  CD  . GLU C  1 436 ? -33.444 58.247  33.364  1.00 59.01  ?  467  GLU C CD  1 
ATOM   10807 O  OE1 . GLU C  1 436 ? -32.880 58.088  34.479  1.00 54.89  ?  467  GLU C OE1 1 
ATOM   10808 O  OE2 . GLU C  1 436 ? -34.679 58.111  33.200  1.00 65.19  -1 467  GLU C OE2 1 
ATOM   10809 N  N   . TRP C  1 437 ? -30.261 56.003  30.073  1.00 38.94  ?  468  TRP C N   1 
ATOM   10810 C  CA  . TRP C  1 437 ? -30.335 55.353  28.769  1.00 41.73  ?  468  TRP C CA  1 
ATOM   10811 C  C   . TRP C  1 437 ? -30.706 53.876  28.888  1.00 42.25  ?  468  TRP C C   1 
ATOM   10812 O  O   . TRP C  1 437 ? -31.600 53.391  28.181  1.00 39.48  ?  468  TRP C O   1 
ATOM   10813 C  CB  . TRP C  1 437 ? -29.001 55.531  28.049  1.00 43.21  ?  468  TRP C CB  1 
ATOM   10814 C  CG  . TRP C  1 437 ? -28.874 54.828  26.732  1.00 43.53  ?  468  TRP C CG  1 
ATOM   10815 C  CD1 . TRP C  1 437 ? -29.676 54.980  25.642  1.00 40.50  ?  468  TRP C CD1 1 
ATOM   10816 C  CD2 . TRP C  1 437 ? -27.852 53.887  26.353  1.00 40.14  ?  468  TRP C CD2 1 
ATOM   10817 N  NE1 . TRP C  1 437 ? -29.231 54.183  24.613  1.00 39.59  ?  468  TRP C NE1 1 
ATOM   10818 C  CE2 . TRP C  1 437 ? -28.114 53.501  25.026  1.00 41.47  ?  468  TRP C CE2 1 
ATOM   10819 C  CE3 . TRP C  1 437 ? -26.762 53.315  27.020  1.00 40.09  ?  468  TRP C CE3 1 
ATOM   10820 C  CZ2 . TRP C  1 437 ? -27.315 52.579  24.342  1.00 38.76  ?  468  TRP C CZ2 1 
ATOM   10821 C  CZ3 . TRP C  1 437 ? -25.969 52.399  26.345  1.00 39.56  ?  468  TRP C CZ3 1 
ATOM   10822 C  CH2 . TRP C  1 437 ? -26.248 52.042  25.019  1.00 39.22  ?  468  TRP C CH2 1 
ATOM   10823 N  N   . THR C  1 438 ? -30.044 53.149  29.796  1.00 36.08  ?  469  THR C N   1 
ATOM   10824 C  CA  . THR C  1 438 ? -30.280 51.711  29.898  1.00 40.43  ?  469  THR C CA  1 
ATOM   10825 C  C   . THR C  1 438 ? -31.707 51.397  30.330  1.00 45.32  ?  469  THR C C   1 
ATOM   10826 O  O   . THR C  1 438 ? -32.200 50.294  30.070  1.00 38.38  ?  469  THR C O   1 
ATOM   10827 C  CB  . THR C  1 438 ? -29.301 51.047  30.878  1.00 40.27  ?  469  THR C CB  1 
ATOM   10828 O  OG1 . THR C  1 438 ? -29.598 51.443  32.227  1.00 39.91  ?  469  THR C OG1 1 
ATOM   10829 C  CG2 . THR C  1 438 ? -27.865 51.398  30.539  1.00 37.02  ?  469  THR C CG2 1 
ATOM   10830 N  N   . LYS C  1 439 ? -32.375 52.332  31.012  1.00 42.95  ?  470  LYS C N   1 
ATOM   10831 C  CA  . LYS C  1 439 ? -33.730 52.066  31.483  1.00 40.25  ?  470  LYS C CA  1 
ATOM   10832 C  C   . LYS C  1 439 ? -34.712 51.894  30.337  1.00 42.56  ?  470  LYS C C   1 
ATOM   10833 O  O   . LYS C  1 439 ? -35.823 51.410  30.567  1.00 43.59  ?  470  LYS C O   1 
ATOM   10834 C  CB  . LYS C  1 439 ? -34.196 53.191  32.412  1.00 42.92  ?  470  LYS C CB  1 
ATOM   10835 C  CG  . LYS C  1 439 ? -33.629 53.075  33.822  1.00 52.55  ?  470  LYS C CG  1 
ATOM   10836 C  CD  . LYS C  1 439 ? -34.143 54.167  34.736  1.00 54.81  ?  470  LYS C CD  1 
ATOM   10837 C  CE  . LYS C  1 439 ? -32.995 54.775  35.540  1.00 57.72  ?  470  LYS C CE  1 
ATOM   10838 N  NZ  . LYS C  1 439 ? -33.254 56.193  35.943  1.00 64.35  ?  470  LYS C NZ  1 
ATOM   10839 N  N   . SER C  1 440 ? -34.328 52.269  29.123  1.00 39.33  ?  471  SER C N   1 
ATOM   10840 C  CA  . SER C  1 440 ? -35.163 52.102  27.948  1.00 44.30  ?  471  SER C CA  1 
ATOM   10841 C  C   . SER C  1 440 ? -34.927 50.778  27.232  1.00 44.71  ?  471  SER C C   1 
ATOM   10842 O  O   . SER C  1 440 ? -35.575 50.524  26.219  1.00 44.03  ?  471  SER C O   1 
ATOM   10843 C  CB  . SER C  1 440 ? -34.931 53.264  26.976  1.00 43.64  ?  471  SER C CB  1 
ATOM   10844 O  OG  . SER C  1 440 ? -33.682 53.141  26.317  1.00 47.10  ?  471  SER C OG  1 
ATOM   10845 N  N   . PHE C  1 441 ? -34.028 49.932  27.730  1.00 39.39  ?  472  PHE C N   1 
ATOM   10846 C  CA  . PHE C  1 441 ? -33.648 48.734  26.992  1.00 40.86  ?  472  PHE C CA  1 
ATOM   10847 C  C   . PHE C  1 441 ? -34.730 47.666  27.061  1.00 46.56  ?  472  PHE C C   1 
ATOM   10848 O  O   . PHE C  1 441 ? -35.498 47.583  28.026  1.00 45.59  ?  472  PHE C O   1 
ATOM   10849 C  CB  . PHE C  1 441 ? -32.353 48.132  27.541  1.00 38.22  ?  472  PHE C CB  1 
ATOM   10850 C  CG  . PHE C  1 441 ? -31.120 48.948  27.270  1.00 38.56  ?  472  PHE C CG  1 
ATOM   10851 C  CD1 . PHE C  1 441 ? -31.188 50.152  26.582  1.00 37.63  ?  472  PHE C CD1 1 
ATOM   10852 C  CD2 . PHE C  1 441 ? -29.879 48.487  27.687  1.00 39.38  ?  472  PHE C CD2 1 
ATOM   10853 C  CE1 . PHE C  1 441 ? -30.043 50.895  26.324  1.00 40.38  ?  472  PHE C CE1 1 
ATOM   10854 C  CE2 . PHE C  1 441 ? -28.731 49.220  27.432  1.00 38.28  ?  472  PHE C CE2 1 
ATOM   10855 C  CZ  . PHE C  1 441 ? -28.809 50.426  26.746  1.00 37.76  ?  472  PHE C CZ  1 
ATOM   10856 N  N   . VAL C  1 442 ? -34.750 46.822  26.035  1.00 42.53  ?  473  VAL C N   1 
ATOM   10857 C  CA  . VAL C  1 442 ? -35.544 45.614  26.031  1.00 43.37  ?  473  VAL C CA  1 
ATOM   10858 C  C   . VAL C  1 442 ? -34.658 44.424  26.384  1.00 44.86  ?  473  VAL C C   1 
ATOM   10859 O  O   . VAL C  1 442 ? -33.437 44.535  26.490  1.00 40.12  ?  473  VAL C O   1 
ATOM   10860 C  CB  . VAL C  1 442 ? -36.254 45.410  24.672  1.00 43.52  ?  473  VAL C CB  1 
ATOM   10861 C  CG1 . VAL C  1 442 ? -37.016 46.666  24.304  1.00 38.62  ?  473  VAL C CG1 1 
ATOM   10862 C  CG2 . VAL C  1 442 ? -35.236 45.094  23.579  1.00 37.06  ?  473  VAL C CG2 1 
ATOM   10863 N  N   . LYS C  1 443 ? -35.287 43.256  26.592  1.00 40.41  ?  474  LYS C N   1 
ATOM   10864 C  CA  . LYS C  1 443 ? -34.509 42.044  26.784  1.00 42.83  ?  474  LYS C CA  1 
ATOM   10865 C  C   . LYS C  1 443 ? -34.027 41.514  25.434  1.00 41.81  ?  474  LYS C C   1 
ATOM   10866 O  O   . LYS C  1 443 ? -34.682 41.717  24.408  1.00 41.15  ?  474  LYS C O   1 
ATOM   10867 C  CB  . LYS C  1 443 ? -35.344 40.981  27.492  1.00 42.18  ?  474  LYS C CB  1 
ATOM   10868 N  N   . PRO C  1 444 ? -32.869 40.863  25.392  1.00 42.82  ?  475  PRO C N   1 
ATOM   10869 C  CA  . PRO C  1 444 ? -32.433 40.265  24.125  1.00 37.37  ?  475  PRO C CA  1 
ATOM   10870 C  C   . PRO C  1 444 ? -33.383 39.166  23.674  1.00 39.95  ?  475  PRO C C   1 
ATOM   10871 O  O   . PRO C  1 444 ? -33.839 38.344  24.474  1.00 38.85  ?  475  PRO C O   1 
ATOM   10872 C  CB  . PRO C  1 444 ? -31.035 39.715  24.434  1.00 41.00  ?  475  PRO C CB  1 
ATOM   10873 C  CG  . PRO C  1 444 ? -30.858 39.795  25.907  1.00 42.90  ?  475  PRO C CG  1 
ATOM   10874 C  CD  . PRO C  1 444 ? -31.988 40.542  26.527  1.00 39.39  ?  475  PRO C CD  1 
ATOM   10875 N  N   . LEU C  1 445 ? -33.678 39.173  22.369  1.00 35.69  ?  476  LEU C N   1 
ATOM   10876 C  CA  . LEU C  1 445 ? -34.469 38.107  21.764  1.00 38.44  ?  476  LEU C CA  1 
ATOM   10877 C  C   . LEU C  1 445 ? -33.744 36.773  21.830  1.00 38.77  ?  476  LEU C C   1 
ATOM   10878 O  O   . LEU C  1 445 ? -34.384 35.715  21.903  1.00 33.49  ?  476  LEU C O   1 
ATOM   10879 C  CB  . LEU C  1 445 ? -34.796 38.467  20.312  1.00 34.17  ?  476  LEU C CB  1 
ATOM   10880 C  CG  . LEU C  1 445 ? -35.645 39.730  20.218  1.00 39.05  ?  476  LEU C CG  1 
ATOM   10881 C  CD1 . LEU C  1 445 ? -35.806 40.232  18.794  1.00 36.24  ?  476  LEU C CD1 1 
ATOM   10882 C  CD2 . LEU C  1 445 ? -37.000 39.416  20.849  1.00 44.79  ?  476  LEU C CD2 1 
ATOM   10883 N  N   . TRP C  1 446 ? -32.414 36.802  21.791  1.00 33.36  ?  477  TRP C N   1 
ATOM   10884 C  CA  . TRP C  1 446 ? -31.595 35.614  21.958  1.00 31.78  ?  477  TRP C CA  1 
ATOM   10885 C  C   . TRP C  1 446 ? -30.316 36.054  22.663  1.00 32.91  ?  477  TRP C C   1 
ATOM   10886 O  O   . TRP C  1 446 ? -29.993 37.242  22.694  1.00 32.29  ?  477  TRP C O   1 
ATOM   10887 C  CB  . TRP C  1 446 ? -31.290 34.950  20.613  1.00 30.60  ?  477  TRP C CB  1 
ATOM   10888 C  CG  . TRP C  1 446 ? -30.632 35.911  19.647  1.00 31.12  ?  477  TRP C CG  1 
ATOM   10889 C  CD1 . TRP C  1 446 ? -29.304 36.238  19.601  1.00 27.78  ?  477  TRP C CD1 1 
ATOM   10890 C  CD2 . TRP C  1 446 ? -31.272 36.696  18.634  1.00 33.69  ?  477  TRP C CD2 1 
ATOM   10891 N  NE1 . TRP C  1 446 ? -29.073 37.158  18.614  1.00 31.19  ?  477  TRP C NE1 1 
ATOM   10892 C  CE2 . TRP C  1 446 ? -30.266 37.464  18.005  1.00 29.17  ?  477  TRP C CE2 1 
ATOM   10893 C  CE3 . TRP C  1 446 ? -32.598 36.812  18.179  1.00 32.37  ?  477  TRP C CE3 1 
ATOM   10894 C  CZ2 . TRP C  1 446 ? -30.538 38.343  16.961  1.00 28.05  ?  477  TRP C CZ2 1 
ATOM   10895 C  CZ3 . TRP C  1 446 ? -32.863 37.694  17.135  1.00 34.85  ?  477  TRP C CZ3 1 
ATOM   10896 C  CH2 . TRP C  1 446 ? -31.841 38.446  16.539  1.00 32.00  ?  477  TRP C CH2 1 
ATOM   10897 N  N   . VAL C  1 447 ? -29.611 35.093  23.252  1.00 30.87  ?  478  VAL C N   1 
ATOM   10898 C  CA  . VAL C  1 447 ? -28.270 35.327  23.793  1.00 29.49  ?  478  VAL C CA  1 
ATOM   10899 C  C   . VAL C  1 447 ? -27.294 34.436  23.026  1.00 31.54  ?  478  VAL C C   1 
ATOM   10900 O  O   . VAL C  1 447 ? -27.668 33.803  22.031  1.00 32.80  ?  478  VAL C O   1 
ATOM   10901 C  CB  . VAL C  1 447 ? -28.220 35.085  25.313  1.00 32.85  ?  478  VAL C CB  1 
ATOM   10902 C  CG1 . VAL C  1 447 ? -29.206 35.995  26.032  1.00 35.10  ?  478  VAL C CG1 1 
ATOM   10903 C  CG2 . VAL C  1 447 ? -28.483 33.608  25.672  1.00 34.05  ?  478  VAL C CG2 1 
ATOM   10904 N  N   . TYR C  1 448 ? -26.035 34.383  23.455  1.00 31.18  ?  479  TYR C N   1 
ATOM   10905 C  CA  . TYR C  1 448 ? -25.031 33.689  22.658  1.00 30.18  ?  479  TYR C CA  1 
ATOM   10906 C  C   . TYR C  1 448 ? -24.692 32.305  23.185  1.00 28.85  ?  479  TYR C C   1 
ATOM   10907 O  O   . TYR C  1 448 ? -24.593 31.357  22.402  1.00 30.51  ?  479  TYR C O   1 
ATOM   10908 C  CB  . TYR C  1 448 ? -23.739 34.520  22.558  1.00 32.52  ?  479  TYR C CB  1 
ATOM   10909 C  CG  . TYR C  1 448 ? -22.874 34.043  21.415  1.00 32.76  ?  479  TYR C CG  1 
ATOM   10910 C  CD1 . TYR C  1 448 ? -23.248 34.284  20.101  1.00 31.50  ?  479  TYR C CD1 1 
ATOM   10911 C  CD2 . TYR C  1 448 ? -21.702 33.323  21.647  1.00 34.16  ?  479  TYR C CD2 1 
ATOM   10912 C  CE1 . TYR C  1 448 ? -22.483 33.840  19.041  1.00 32.16  ?  479  TYR C CE1 1 
ATOM   10913 C  CE2 . TYR C  1 448 ? -20.913 32.876  20.582  1.00 34.82  ?  479  TYR C CE2 1 
ATOM   10914 C  CZ  . TYR C  1 448 ? -21.320 33.138  19.280  1.00 36.34  ?  479  TYR C CZ  1 
ATOM   10915 O  OH  . TYR C  1 448 ? -20.574 32.711  18.196  1.00 37.99  ?  479  TYR C OH  1 
ATOM   10916 N  N   . SER C  1 449 ? -24.455 32.180  24.485  1.00 30.42  ?  480  SER C N   1 
ATOM   10917 C  CA  . SER C  1 449 ? -23.984 30.952  25.091  1.00 29.07  ?  480  SER C CA  1 
ATOM   10918 C  C   . SER C  1 449 ? -24.965 30.446  26.140  1.00 29.24  ?  480  SER C C   1 
ATOM   10919 O  O   . SER C  1 449 ? -25.815 31.182  26.647  1.00 32.37  ?  480  SER C O   1 
ATOM   10920 C  CB  . SER C  1 449 ? -22.611 31.163  25.751  1.00 29.19  ?  480  SER C CB  1 
ATOM   10921 O  OG  . SER C  1 449 ? -22.767 32.007  26.882  1.00 29.89  ?  480  SER C OG  1 
ATOM   10922 N  N   . VAL C  1 450 ? -24.790 29.176  26.497  1.00 32.96  ?  481  VAL C N   1 
ATOM   10923 C  CA  . VAL C  1 450 ? -25.545 28.602  27.606  1.00 31.02  ?  481  VAL C CA  1 
ATOM   10924 C  C   . VAL C  1 450 ? -25.271 29.369  28.893  1.00 35.43  ?  481  VAL C C   1 
ATOM   10925 O  O   . VAL C  1 450 ? -26.174 29.573  29.715  1.00 36.95  ?  481  VAL C O   1 
ATOM   10926 C  CB  . VAL C  1 450 ? -25.208 27.108  27.747  1.00 33.07  ?  481  VAL C CB  1 
ATOM   10927 C  CG1 . VAL C  1 450 ? -25.766 26.544  29.052  1.00 37.77  ?  481  VAL C CG1 1 
ATOM   10928 C  CG2 . VAL C  1 450 ? -25.728 26.338  26.522  1.00 31.96  ?  481  VAL C CG2 1 
ATOM   10929 N  N   . LYS C  1 451 ? -24.027 29.825  29.086  1.00 30.97  ?  482  LYS C N   1 
ATOM   10930 C  CA  . LYS C  1 451 ? -23.729 30.646  30.260  1.00 37.00  ?  482  LYS C CA  1 
ATOM   10931 C  C   . LYS C  1 451 ? -24.594 31.903  30.281  1.00 33.57  ?  482  LYS C C   1 
ATOM   10932 O  O   . LYS C  1 451 ? -25.190 32.244  31.313  1.00 34.56  ?  482  LYS C O   1 
ATOM   10933 C  CB  . LYS C  1 451 ? -22.240 31.012  30.296  1.00 31.23  ?  482  LYS C CB  1 
ATOM   10934 C  CG  . LYS C  1 451 ? -21.881 31.876  31.483  1.00 36.15  ?  482  LYS C CG  1 
ATOM   10935 C  CD  . LYS C  1 451 ? -21.978 31.104  32.786  1.00 38.72  ?  482  LYS C CD  1 
ATOM   10936 C  CE  . LYS C  1 451 ? -21.440 31.931  33.961  1.00 38.83  ?  482  LYS C CE  1 
ATOM   10937 N  NZ  . LYS C  1 451 ? -21.524 31.168  35.213  1.00 36.04  ?  482  LYS C NZ  1 
ATOM   10938 N  N   . ASP C  1 452 ? -24.667 32.607  29.143  1.00 31.62  ?  483  ASP C N   1 
ATOM   10939 C  CA  . ASP C  1 452 ? -25.599 33.724  28.997  1.00 35.71  ?  483  ASP C CA  1 
ATOM   10940 C  C   . ASP C  1 452 ? -27.019 33.355  29.444  1.00 39.80  ?  483  ASP C C   1 
ATOM   10941 O  O   . ASP C  1 452 ? -27.676 34.105  30.181  1.00 35.23  ?  483  ASP C O   1 
ATOM   10942 C  CB  . ASP C  1 452 ? -25.659 34.177  27.539  1.00 34.76  ?  483  ASP C CB  1 
ATOM   10943 C  CG  . ASP C  1 452 ? -24.382 34.796  27.044  1.00 33.50  ?  483  ASP C CG  1 
ATOM   10944 O  OD1 . ASP C  1 452 ? -23.542 35.214  27.872  1.00 32.13  ?  483  ASP C OD1 1 
ATOM   10945 O  OD2 . ASP C  1 452 ? -24.251 34.891  25.803  1.00 29.26  -1 483  ASP C OD2 1 
ATOM   10946 N  N   . LYS C  1 453 ? -27.537 32.234  28.946  1.00 38.63  ?  484  LYS C N   1 
ATOM   10947 C  CA  . LYS C  1 453 ? -28.908 31.863  29.273  1.00 37.81  ?  484  LYS C CA  1 
ATOM   10948 C  C   . LYS C  1 453 ? -29.081 31.728  30.779  1.00 40.32  ?  484  LYS C C   1 
ATOM   10949 O  O   . LYS C  1 453 ? -30.009 32.295  31.368  1.00 41.95  ?  484  LYS C O   1 
ATOM   10950 C  CB  . LYS C  1 453 ? -29.275 30.565  28.560  1.00 41.39  ?  484  LYS C CB  1 
ATOM   10951 C  CG  . LYS C  1 453 ? -30.736 30.154  28.692  1.00 44.51  ?  484  LYS C CG  1 
ATOM   10952 C  CD  . LYS C  1 453 ? -31.108 29.133  27.626  1.00 50.99  ?  484  LYS C CD  1 
ATOM   10953 C  CE  . LYS C  1 453 ? -32.608 29.167  27.318  1.00 57.46  ?  484  LYS C CE  1 
ATOM   10954 N  NZ  . LYS C  1 453 ? -33.370 28.496  28.409  1.00 61.69  ?  484  LYS C NZ  1 
ATOM   10955 N  N   . GLU C  1 454 ? -28.157 31.017  31.423  1.00 36.80  ?  485  GLU C N   1 
ATOM   10956 C  CA  . GLU C  1 454 ? -28.215 30.841  32.867  1.00 37.95  ?  485  GLU C CA  1 
ATOM   10957 C  C   . GLU C  1 454 ? -28.169 32.178  33.586  1.00 44.61  ?  485  GLU C C   1 
ATOM   10958 O  O   . GLU C  1 454 ? -28.883 32.383  34.577  1.00 41.42  ?  485  GLU C O   1 
ATOM   10959 C  CB  . GLU C  1 454 ? -27.055 29.957  33.326  1.00 41.91  ?  485  GLU C CB  1 
ATOM   10960 C  CG  . GLU C  1 454 ? -27.063 28.593  32.696  1.00 41.41  ?  485  GLU C CG  1 
ATOM   10961 C  CD  . GLU C  1 454 ? -25.960 27.694  33.202  1.00 43.44  ?  485  GLU C CD  1 
ATOM   10962 O  OE1 . GLU C  1 454 ? -25.010 28.193  33.861  1.00 46.24  ?  485  GLU C OE1 1 
ATOM   10963 O  OE2 . GLU C  1 454 ? -26.049 26.471  32.935  1.00 50.17  -1 485  GLU C OE2 1 
ATOM   10964 N  N   . LEU C  1 455 ? -27.330 33.104  33.107  1.00 41.23  ?  486  LEU C N   1 
ATOM   10965 C  CA  . LEU C  1 455 ? -27.158 34.366  33.816  1.00 40.65  ?  486  LEU C CA  1 
ATOM   10966 C  C   . LEU C  1 455 ? -28.418 35.213  33.715  1.00 40.32  ?  486  LEU C C   1 
ATOM   10967 O  O   . LEU C  1 455 ? -28.882 35.782  34.709  1.00 39.76  ?  486  LEU C O   1 
ATOM   10968 C  CB  . LEU C  1 455 ? -25.944 35.120  33.262  1.00 36.83  ?  486  LEU C CB  1 
ATOM   10969 C  CG  . LEU C  1 455 ? -24.580 34.492  33.589  1.00 39.77  ?  486  LEU C CG  1 
ATOM   10970 C  CD1 . LEU C  1 455 ? -23.447 35.234  32.907  1.00 36.59  ?  486  LEU C CD1 1 
ATOM   10971 C  CD2 . LEU C  1 455 ? -24.358 34.415  35.089  1.00 38.49  ?  486  LEU C CD2 1 
ATOM   10972 N  N   . TRP C  1 456 ? -28.981 35.304  32.514  1.00 40.42  ?  487  TRP C N   1 
ATOM   10973 C  CA  . TRP C  1 456 ? -30.168 36.122  32.297  1.00 42.04  ?  487  TRP C CA  1 
ATOM   10974 C  C   . TRP C  1 456 ? -31.399 35.525  32.969  1.00 44.20  ?  487  TRP C C   1 
ATOM   10975 O  O   . TRP C  1 456 ? -32.274 36.268  33.435  1.00 44.10  ?  487  TRP C O   1 
ATOM   10976 C  CB  . TRP C  1 456 ? -30.415 36.285  30.803  1.00 36.24  ?  487  TRP C CB  1 
ATOM   10977 C  CG  . TRP C  1 456 ? -29.604 37.354  30.165  1.00 37.47  ?  487  TRP C CG  1 
ATOM   10978 C  CD1 . TRP C  1 456 ? -28.361 37.221  29.612  1.00 35.36  ?  487  TRP C CD1 1 
ATOM   10979 C  CD2 . TRP C  1 456 ? -29.988 38.726  29.976  1.00 37.64  ?  487  TRP C CD2 1 
ATOM   10980 N  NE1 . TRP C  1 456 ? -27.940 38.433  29.104  1.00 34.88  ?  487  TRP C NE1 1 
ATOM   10981 C  CE2 . TRP C  1 456 ? -28.913 39.374  29.321  1.00 34.04  ?  487  TRP C CE2 1 
ATOM   10982 C  CE3 . TRP C  1 456 ? -31.131 39.470  30.300  1.00 33.22  ?  487  TRP C CE3 1 
ATOM   10983 C  CZ2 . TRP C  1 456 ? -28.945 40.727  28.989  1.00 34.63  ?  487  TRP C CZ2 1 
ATOM   10984 C  CZ3 . TRP C  1 456 ? -31.159 40.820  29.974  1.00 33.32  ?  487  TRP C CZ3 1 
ATOM   10985 C  CH2 . TRP C  1 456 ? -30.075 41.433  29.316  1.00 37.48  ?  487  TRP C CH2 1 
ATOM   10986 N  N   . GLU C  1 457 ? -31.482 34.193  33.029  1.00 42.86  ?  488  GLU C N   1 
ATOM   10987 C  CA  . GLU C  1 457 ? -32.639 33.552  33.644  1.00 46.25  ?  488  GLU C CA  1 
ATOM   10988 C  C   . GLU C  1 457 ? -32.614 33.675  35.164  1.00 47.74  ?  488  GLU C C   1 
ATOM   10989 O  O   . GLU C  1 457 ? -33.675 33.809  35.785  1.00 50.66  ?  488  GLU C O   1 
ATOM   10990 C  CB  . GLU C  1 457 ? -32.719 32.085  33.209  1.00 43.01  ?  488  GLU C CB  1 
ATOM   10991 C  CG  . GLU C  1 457 ? -33.188 31.932  31.768  1.00 44.16  ?  488  GLU C CG  1 
ATOM   10992 C  CD  . GLU C  1 457 ? -33.414 30.493  31.343  1.00 48.78  ?  488  GLU C CD  1 
ATOM   10993 O  OE1 . GLU C  1 457 ? -32.996 29.561  32.062  1.00 51.49  ?  488  GLU C OE1 1 
ATOM   10994 O  OE2 . GLU C  1 457 ? -33.991 30.297  30.256  1.00 50.73  -1 488  GLU C OE2 1 
ATOM   10995 N  N   . SER C  1 458 ? -31.428 33.655  35.781  1.00 43.36  ?  489  SER C N   1 
ATOM   10996 C  CA  . SER C  1 458 ? -31.349 33.845  37.223  1.00 44.96  ?  489  SER C CA  1 
ATOM   10997 C  C   . SER C  1 458 ? -31.321 35.311  37.628  1.00 46.76  ?  489  SER C C   1 
ATOM   10998 O  O   . SER C  1 458 ? -31.332 35.601  38.829  1.00 49.05  ?  489  SER C O   1 
ATOM   10999 C  CB  . SER C  1 458 ? -30.110 33.153  37.803  1.00 49.94  ?  489  SER C CB  1 
ATOM   11000 O  OG  . SER C  1 458 ? -28.922 33.836  37.438  1.00 43.68  ?  489  SER C OG  1 
ATOM   11001 N  N   . GLY C  1 459 ? -31.275 36.235  36.675  1.00 44.63  ?  490  GLY C N   1 
ATOM   11002 C  CA  . GLY C  1 459 ? -31.239 37.643  37.005  1.00 44.61  ?  490  GLY C CA  1 
ATOM   11003 C  C   . GLY C  1 459 ? -29.867 38.222  37.295  1.00 47.23  ?  490  GLY C C   1 
ATOM   11004 O  O   . GLY C  1 459 ? -29.771 39.438  37.525  1.00 44.79  ?  490  GLY C O   1 
ATOM   11005 N  N   . GLN C  1 460 ? -28.819 37.383  37.293  1.00 47.16  ?  491  GLN C N   1 
ATOM   11006 C  CA  . GLN C  1 460 ? -27.418 37.871  37.451  1.00 45.14  ?  491  GLN C CA  1 
ATOM   11007 C  C   . GLN C  1 460 ? -27.184 38.903  36.349  1.00 38.31  ?  491  GLN C C   1 
ATOM   11008 O  O   . GLN C  1 460 ? -26.532 39.907  36.636  1.00 41.07  ?  491  GLN C O   1 
ATOM   11009 C  CB  . GLN C  1 460 ? -26.465 36.683  37.439  1.00 44.85  ?  491  GLN C CB  1 
ATOM   11010 C  CG  . GLN C  1 460 ? -26.535 35.822  38.691  1.00 52.28  ?  491  GLN C CG  1 
ATOM   11011 C  CD  . GLN C  1 460 ? -25.730 34.549  38.575  1.00 55.48  ?  491  GLN C CD  1 
ATOM   11012 O  OE1 . GLN C  1 460 ? -24.594 34.457  39.051  1.00 60.48  ?  491  GLN C OE1 1 
ATOM   11013 N  NE2 . GLN C  1 460 ? -26.314 33.551  37.933  1.00 52.54  ?  491  GLN C NE2 1 
ATOM   11014 N  N   . MET C  1 461 ? -27.605 38.618  35.122  1.00 41.73  ?  492  MET C N   1 
ATOM   11015 C  CA  . MET C  1 461 ? -27.663 39.616  34.059  1.00 39.48  ?  492  MET C CA  1 
ATOM   11016 C  C   . MET C  1 461 ? -29.087 40.129  33.885  1.00 40.99  ?  492  MET C C   1 
ATOM   11017 O  O   . MET C  1 461 ? -30.057 39.402  34.136  1.00 36.62  ?  492  MET C O   1 
ATOM   11018 C  CB  . MET C  1 461 ? -27.127 39.102  32.709  1.00 38.18  ?  492  MET C CB  1 
ATOM   11019 C  CG  . MET C  1 461 ? -25.688 38.567  32.799  1.00 33.07  ?  492  MET C CG  1 
ATOM   11020 S  SD  . MET C  1 461 ? -24.521 39.958  32.739  1.00 37.84  ?  492  MET C SD  1 
ATOM   11021 C  CE  . MET C  1 461 ? -24.860 40.691  31.129  1.00 32.02  ?  492  MET C CE  1 
ATOM   11022 N  N   . PRO C  1 462 ? -29.240 41.386  33.465  1.00 37.13  ?  493  PRO C N   1 
ATOM   11023 C  CA  . PRO C  1 462 ? -28.172 42.337  33.111  1.00 36.36  ?  493  PRO C CA  1 
ATOM   11024 C  C   . PRO C  1 462 ? -27.574 43.090  34.300  1.00 40.84  ?  493  PRO C C   1 
ATOM   11025 O  O   . PRO C  1 462 ? -26.476 43.618  34.167  1.00 38.83  ?  493  PRO C O   1 
ATOM   11026 C  CB  . PRO C  1 462 ? -28.883 43.292  32.151  1.00 37.47  ?  493  PRO C CB  1 
ATOM   11027 C  CG  . PRO C  1 462 ? -30.307 43.323  32.661  1.00 37.12  ?  493  PRO C CG  1 
ATOM   11028 C  CD  . PRO C  1 462 ? -30.579 41.940  33.209  1.00 34.78  ?  493  PRO C CD  1 
ATOM   11029 N  N   . ASN C  1 463 ? -28.258 43.144  35.444  1.00 40.00  ?  494  ASN C N   1 
ATOM   11030 C  CA  . ASN C  1 463 ? -27.838 43.908  36.627  1.00 39.60  ?  494  ASN C CA  1 
ATOM   11031 C  C   . ASN C  1 463 ? -27.217 45.255  36.242  1.00 41.19  ?  494  ASN C C   1 
ATOM   11032 O  O   . ASN C  1 463 ? -26.042 45.531  36.498  1.00 39.05  ?  494  ASN C O   1 
ATOM   11033 C  CB  . ASN C  1 463 ? -26.883 43.092  37.505  1.00 38.21  ?  494  ASN C CB  1 
ATOM   11034 C  CG  . ASN C  1 463 ? -26.833 43.602  38.944  1.00 42.74  ?  494  ASN C CG  1 
ATOM   11035 O  OD1 . ASN C  1 463 ? -27.359 44.670  39.247  1.00 42.41  ?  494  ASN C OD1 1 
ATOM   11036 N  ND2 . ASN C  1 463 ? -26.188 42.845  39.829  1.00 44.94  ?  494  ASN C ND2 1 
ATOM   11037 N  N   . TYR C  1 464 ? -28.036 46.100  35.602  1.00 39.74  ?  495  TYR C N   1 
ATOM   11038 C  CA  . TYR C  1 464 ? -27.572 47.442  35.247  1.00 42.77  ?  495  TYR C CA  1 
ATOM   11039 C  C   . TYR C  1 464 ? -27.242 48.266  36.489  1.00 44.32  ?  495  TYR C C   1 
ATOM   11040 O  O   . TYR C  1 464 ? -26.348 49.126  36.446  1.00 42.49  ?  495  TYR C O   1 
ATOM   11041 C  CB  . TYR C  1 464 ? -28.618 48.169  34.385  1.00 39.69  ?  495  TYR C CB  1 
ATOM   11042 C  CG  . TYR C  1 464 ? -28.912 47.497  33.056  1.00 39.09  ?  495  TYR C CG  1 
ATOM   11043 C  CD1 . TYR C  1 464 ? -27.891 47.194  32.158  1.00 36.83  ?  495  TYR C CD1 1 
ATOM   11044 C  CD2 . TYR C  1 464 ? -30.209 47.146  32.707  1.00 38.18  ?  495  TYR C CD2 1 
ATOM   11045 C  CE1 . TYR C  1 464 ? -28.150 46.575  30.945  1.00 36.12  ?  495  TYR C CE1 1 
ATOM   11046 C  CE2 . TYR C  1 464 ? -30.485 46.519  31.495  1.00 36.64  ?  495  TYR C CE2 1 
ATOM   11047 C  CZ  . TYR C  1 464 ? -29.457 46.234  30.617  1.00 37.21  ?  495  TYR C CZ  1 
ATOM   11048 O  OH  . TYR C  1 464 ? -29.720 45.603  29.421  1.00 31.61  ?  495  TYR C OH  1 
ATOM   11049 N  N   . GLU C  1 465 ? -27.933 48.015  37.607  1.00 43.57  ?  496  GLU C N   1 
ATOM   11050 C  CA  . GLU C  1 465 ? -27.666 48.783  38.823  1.00 43.81  ?  496  GLU C CA  1 
ATOM   11051 C  C   . GLU C  1 465 ? -26.222 48.616  39.266  1.00 44.36  ?  496  GLU C C   1 
ATOM   11052 O  O   . GLU C  1 465 ? -25.529 49.601  39.564  1.00 41.47  ?  496  GLU C O   1 
ATOM   11053 C  CB  . GLU C  1 465 ? -28.620 48.360  39.943  1.00 45.59  ?  496  GLU C CB  1 
ATOM   11054 N  N   . ALA C  1 466 ? -25.753 47.367  39.334  1.00 42.55  ?  497  ALA C N   1 
ATOM   11055 C  CA  . ALA C  1 466 ? -24.381 47.124  39.759  1.00 41.36  ?  497  ALA C CA  1 
ATOM   11056 C  C   . ALA C  1 466 ? -23.388 47.732  38.777  1.00 41.26  ?  497  ALA C C   1 
ATOM   11057 O  O   . ALA C  1 466 ? -22.332 48.227  39.186  1.00 40.17  ?  497  ALA C O   1 
ATOM   11058 C  CB  . ALA C  1 466 ? -24.135 45.624  39.914  1.00 39.61  ?  497  ALA C CB  1 
ATOM   11059 N  N   . THR C  1 467 ? -23.716 47.711  37.485  1.00 35.57  ?  498  THR C N   1 
ATOM   11060 C  CA  . THR C  1 467 ? -22.846 48.314  36.485  1.00 38.17  ?  498  THR C CA  1 
ATOM   11061 C  C   . THR C  1 467 ? -22.538 49.770  36.813  1.00 40.09  ?  498  THR C C   1 
ATOM   11062 O  O   . THR C  1 467 ? -21.410 50.236  36.607  1.00 38.04  ?  498  THR C O   1 
ATOM   11063 C  CB  . THR C  1 467 ? -23.491 48.180  35.103  1.00 39.06  ?  498  THR C CB  1 
ATOM   11064 O  OG1 . THR C  1 467 ? -23.407 46.808  34.686  1.00 34.69  ?  498  THR C OG1 1 
ATOM   11065 C  CG2 . THR C  1 467 ? -22.794 49.085  34.066  1.00 35.74  ?  498  THR C CG2 1 
ATOM   11066 N  N   . PHE C  1 468 ? -23.511 50.505  37.345  1.00 39.04  ?  499  PHE C N   1 
ATOM   11067 C  CA  . PHE C  1 468 ? -23.319 51.931  37.542  1.00 40.87  ?  499  PHE C CA  1 
ATOM   11068 C  C   . PHE C  1 468 ? -22.941 52.283  38.979  1.00 40.09  ?  499  PHE C C   1 
ATOM   11069 O  O   . PHE C  1 468 ? -22.999 53.457  39.355  1.00 38.15  ?  499  PHE C O   1 
ATOM   11070 C  CB  . PHE C  1 468 ? -24.562 52.688  37.064  1.00 40.25  ?  499  PHE C CB  1 
ATOM   11071 C  CG  . PHE C  1 468 ? -24.816 52.524  35.593  1.00 38.31  ?  499  PHE C CG  1 
ATOM   11072 C  CD1 . PHE C  1 468 ? -23.919 53.030  34.665  1.00 36.34  ?  499  PHE C CD1 1 
ATOM   11073 C  CD2 . PHE C  1 468 ? -25.944 51.846  35.130  1.00 41.09  ?  499  PHE C CD2 1 
ATOM   11074 C  CE1 . PHE C  1 468 ? -24.136 52.873  33.294  1.00 39.37  ?  499  PHE C CE1 1 
ATOM   11075 C  CE2 . PHE C  1 468 ? -26.173 51.682  33.754  1.00 37.74  ?  499  PHE C CE2 1 
ATOM   11076 C  CZ  . PHE C  1 468 ? -25.278 52.201  32.837  1.00 34.05  ?  499  PHE C CZ  1 
ATOM   11077 N  N   . GLU C  1 469 ? -22.541 51.291  39.778  1.00 40.68  ?  500  GLU C N   1 
ATOM   11078 C  CA  . GLU C  1 469 ? -21.828 51.565  41.020  1.00 41.39  ?  500  GLU C CA  1 
ATOM   11079 C  C   . GLU C  1 469 ? -20.546 52.337  40.725  1.00 41.67  ?  500  GLU C C   1 
ATOM   11080 O  O   . GLU C  1 469 ? -19.916 52.161  39.674  1.00 39.69  ?  500  GLU C O   1 
ATOM   11081 C  CB  . GLU C  1 469 ? -21.493 50.261  41.759  1.00 39.71  ?  500  GLU C CB  1 
ATOM   11082 C  CG  . GLU C  1 469 ? -22.689 49.582  42.415  1.00 39.09  ?  500  GLU C CG  1 
ATOM   11083 C  CD  . GLU C  1 469 ? -22.443 48.110  42.749  1.00 46.57  ?  500  GLU C CD  1 
ATOM   11084 O  OE1 . GLU C  1 469 ? -21.444 47.521  42.259  1.00 39.74  ?  500  GLU C OE1 1 
ATOM   11085 O  OE2 . GLU C  1 469 ? -23.286 47.529  43.474  1.00 48.74  -1 500  GLU C OE2 1 
ATOM   11086 N  N   . VAL C  1 470 ? -20.161 53.213  41.661  1.00 40.70  ?  501  VAL C N   1 
ATOM   11087 C  CA  . VAL C  1 470 ? -18.937 53.996  41.502  1.00 40.84  ?  501  VAL C CA  1 
ATOM   11088 C  C   . VAL C  1 470 ? -18.090 53.923  42.767  1.00 41.29  ?  501  VAL C C   1 
ATOM   11089 O  O   . VAL C  1 470 ? -17.004 53.332  42.755  1.00 40.06  ?  501  VAL C O   1 
ATOM   11090 C  CB  . VAL C  1 470 ? -19.238 55.463  41.146  1.00 40.81  ?  501  VAL C CB  1 
ATOM   11091 C  CG1 . VAL C  1 470 ? -17.943 56.264  41.082  1.00 41.62  ?  501  VAL C CG1 1 
ATOM   11092 C  CG2 . VAL C  1 470 ? -19.989 55.548  39.836  1.00 42.17  ?  501  VAL C CG2 1 
ATOM   11093 N  N   . ASP C  1 471 ? -18.587 54.504  43.871  1.00 40.99  ?  502  ASP C N   1 
ATOM   11094 C  CA  . ASP C  1 471 ? -17.738 54.715  45.043  1.00 40.37  ?  502  ASP C CA  1 
ATOM   11095 C  C   . ASP C  1 471 ? -17.222 53.399  45.619  1.00 39.99  ?  502  ASP C C   1 
ATOM   11096 O  O   . ASP C  1 471 ? -16.058 53.315  46.042  1.00 38.85  ?  502  ASP C O   1 
ATOM   11097 C  CB  . ASP C  1 471 ? -18.489 55.498  46.133  1.00 41.74  ?  502  ASP C CB  1 
ATOM   11098 C  CG  . ASP C  1 471 ? -18.858 56.910  45.709  1.00 44.22  ?  502  ASP C CG  1 
ATOM   11099 O  OD1 . ASP C  1 471 ? -18.132 57.525  44.898  1.00 44.63  ?  502  ASP C OD1 1 
ATOM   11100 O  OD2 . ASP C  1 471 ? -19.882 57.419  46.209  1.00 48.08  -1 502  ASP C OD2 1 
ATOM   11101 N  N   . LYS C  1 472 ? -18.070 52.362  45.667  1.00 35.97  ?  503  LYS C N   1 
ATOM   11102 C  CA  . LYS C  1 472 ? -17.624 51.135  46.323  1.00 41.42  ?  503  LYS C CA  1 
ATOM   11103 C  C   . LYS C  1 472 ? -16.489 50.454  45.561  1.00 36.30  ?  503  LYS C C   1 
ATOM   11104 O  O   . LYS C  1 472 ? -15.751 49.657  46.154  1.00 38.16  ?  503  LYS C O   1 
ATOM   11105 C  CB  . LYS C  1 472 ? -18.789 50.157  46.512  1.00 35.83  ?  503  LYS C CB  1 
ATOM   11106 C  CG  . LYS C  1 472 ? -19.371 49.626  45.230  1.00 39.37  ?  503  LYS C CG  1 
ATOM   11107 C  CD  . LYS C  1 472 ? -20.419 48.561  45.511  1.00 39.23  ?  503  LYS C CD  1 
ATOM   11108 C  CE  . LYS C  1 472 ? -21.592 49.124  46.302  1.00 44.66  ?  503  LYS C CE  1 
ATOM   11109 N  NZ  . LYS C  1 472 ? -22.797 48.275  46.134  1.00 37.57  ?  503  LYS C NZ  1 
ATOM   11110 N  N   . LEU C  1 473 ? -16.317 50.778  44.278  1.00 34.27  ?  504  LEU C N   1 
ATOM   11111 C  CA  . LEU C  1 473 ? -15.238 50.208  43.479  1.00 37.06  ?  504  LEU C CA  1 
ATOM   11112 C  C   . LEU C  1 473 ? -13.872 50.774  43.838  1.00 37.10  ?  504  LEU C C   1 
ATOM   11113 O  O   . LEU C  1 473 ? -12.858 50.130  43.542  1.00 33.76  ?  504  LEU C O   1 
ATOM   11114 C  CB  . LEU C  1 473 ? -15.509 50.453  41.991  1.00 38.41  ?  504  LEU C CB  1 
ATOM   11115 C  CG  . LEU C  1 473 ? -16.920 50.041  41.568  1.00 37.67  ?  504  LEU C CG  1 
ATOM   11116 C  CD1 . LEU C  1 473 ? -17.151 50.365  40.126  1.00 34.55  ?  504  LEU C CD1 1 
ATOM   11117 C  CD2 . LEU C  1 473 ? -17.153 48.572  41.861  1.00 29.58  ?  504  LEU C CD2 1 
ATOM   11118 N  N   . VAL C  1 474 ? -13.816 51.972  44.421  1.00 40.25  ?  505  VAL C N   1 
ATOM   11119 C  CA  . VAL C  1 474 ? -12.540 52.597  44.756  1.00 38.46  ?  505  VAL C CA  1 
ATOM   11120 C  C   . VAL C  1 474 ? -12.330 52.797  46.256  1.00 40.16  ?  505  VAL C C   1 
ATOM   11121 O  O   . VAL C  1 474 ? -11.167 52.911  46.691  1.00 38.40  ?  505  VAL C O   1 
ATOM   11122 C  CB  . VAL C  1 474 ? -12.358 53.939  44.007  1.00 41.37  ?  505  VAL C CB  1 
ATOM   11123 C  CG1 . VAL C  1 474 ? -12.446 53.727  42.497  1.00 35.37  ?  505  VAL C CG1 1 
ATOM   11124 C  CG2 . VAL C  1 474 ? -13.367 54.982  44.482  1.00 39.81  ?  505  VAL C CG2 1 
ATOM   11125 N  N   . ASP C  1 475 ? -13.384 52.819  47.071  1.00 38.30  ?  506  ASP C N   1 
ATOM   11126 C  CA  . ASP C  1 475 ? -13.224 53.055  48.500  1.00 37.59  ?  506  ASP C CA  1 
ATOM   11127 C  C   . ASP C  1 475 ? -12.588 51.853  49.181  1.00 37.05  ?  506  ASP C C   1 
ATOM   11128 O  O   . ASP C  1 475 ? -12.915 50.702  48.880  1.00 37.04  ?  506  ASP C O   1 
ATOM   11129 C  CB  . ASP C  1 475 ? -14.578 53.333  49.149  1.00 38.69  ?  506  ASP C CB  1 
ATOM   11130 C  CG  . ASP C  1 475 ? -15.135 54.681  48.770  1.00 40.83  ?  506  ASP C CG  1 
ATOM   11131 O  OD1 . ASP C  1 475 ? -14.345 55.536  48.314  1.00 39.92  ?  506  ASP C OD1 1 
ATOM   11132 O  OD2 . ASP C  1 475 ? -16.364 54.878  48.920  1.00 42.70  -1 506  ASP C OD2 1 
ATOM   11133 N  N   . SER C  1 476 ? -11.696 52.120  50.112  1.00 38.81  ?  507  SER C N   1 
ATOM   11134 C  CA  . SER C  1 476 ? -11.230 51.018  50.936  1.00 35.68  ?  507  SER C CA  1 
ATOM   11135 C  C   . SER C  1 476 ? -12.252 50.736  52.035  1.00 40.28  ?  507  SER C C   1 
ATOM   11136 O  O   . SER C  1 476 ? -12.861 51.668  52.571  1.00 37.56  ?  507  SER C O   1 
ATOM   11137 C  CB  . SER C  1 476 ? -9.873  51.346  51.557  1.00 36.18  ?  507  SER C CB  1 
ATOM   11138 O  OG  . SER C  1 476 ? -9.635  50.523  52.681  1.00 37.40  ?  507  SER C OG  1 
ATOM   11139 N  N   . PRO C  1 477 ? -12.485 49.466  52.373  1.00 37.64  ?  508  PRO C N   1 
ATOM   11140 C  CA  . PRO C  1 477 ? -13.351 49.152  53.516  1.00 37.57  ?  508  PRO C CA  1 
ATOM   11141 C  C   . PRO C  1 477 ? -12.681 49.354  54.871  1.00 45.42  ?  508  PRO C C   1 
ATOM   11142 O  O   . PRO C  1 477 ? -13.299 49.083  55.906  1.00 44.33  ?  508  PRO C O   1 
ATOM   11143 C  CB  . PRO C  1 477 ? -13.689 47.679  53.275  1.00 43.08  ?  508  PRO C CB  1 
ATOM   11144 C  CG  . PRO C  1 477 ? -12.455 47.145  52.607  1.00 41.42  ?  508  PRO C CG  1 
ATOM   11145 C  CD  . PRO C  1 477 ? -12.043 48.248  51.669  1.00 35.57  ?  508  PRO C CD  1 
ATOM   11146 N  N   . TYR C  1 478 ? -11.453 49.837  54.894  1.00 38.85  ?  509  TYR C N   1 
ATOM   11147 C  CA  . TYR C  1 478 ? -10.725 50.041  56.139  1.00 44.46  ?  509  TYR C CA  1 
ATOM   11148 C  C   . TYR C  1 478 ? -10.526 51.534  56.373  1.00 42.72  ?  509  TYR C C   1 
ATOM   11149 O  O   . TYR C  1 478 ? -10.115 51.941  57.454  1.00 50.50  ?  509  TYR C O   1 
ATOM   11150 C  CB  . TYR C  1 478 ? -9.391  49.298  56.074  1.00 39.72  ?  509  TYR C CB  1 
ATOM   11151 C  CG  . TYR C  1 478 ? -9.563  47.879  55.565  1.00 42.27  ?  509  TYR C CG  1 
ATOM   11152 C  CD1 . TYR C  1 478 ? -10.286 46.940  56.297  1.00 42.11  ?  509  TYR C CD1 1 
ATOM   11153 C  CD2 . TYR C  1 478 ? -9.070  47.501  54.320  1.00 42.56  ?  509  TYR C CD2 1 
ATOM   11154 C  CE1 . TYR C  1 478 ? -10.470 45.645  55.824  1.00 46.40  ?  509  TYR C CE1 1 
ATOM   11155 C  CE2 . TYR C  1 478 ? -9.256  46.207  53.828  1.00 39.62  ?  509  TYR C CE2 1 
ATOM   11156 C  CZ  . TYR C  1 478 ? -9.950  45.286  54.580  1.00 43.03  ?  509  TYR C CZ  1 
ATOM   11157 O  OH  . TYR C  1 478 ? -10.124 44.010  54.102  1.00 38.99  ?  509  TYR C OH  1 
ATOM   11158 N  N   . GLU D  1 14  ? 47.923  30.441  -20.339 1.00 61.77  ?  45   GLU D N   1 
ATOM   11159 C  CA  . GLU D  1 14  ? 46.556  30.848  -20.669 1.00 61.92  ?  45   GLU D CA  1 
ATOM   11160 C  C   . GLU D  1 14  ? 46.345  30.989  -22.179 1.00 59.90  ?  45   GLU D C   1 
ATOM   11161 O  O   . GLU D  1 14  ? 46.688  32.005  -22.786 1.00 63.63  ?  45   GLU D O   1 
ATOM   11162 C  CB  . GLU D  1 14  ? 46.196  32.162  -19.970 1.00 55.87  ?  45   GLU D CB  1 
ATOM   11163 C  CG  . GLU D  1 14  ? 44.815  32.685  -20.347 1.00 56.72  ?  45   GLU D CG  1 
ATOM   11164 C  CD  . GLU D  1 14  ? 43.704  31.834  -19.766 1.00 51.67  ?  45   GLU D CD  1 
ATOM   11165 O  OE1 . GLU D  1 14  ? 43.320  30.848  -20.427 1.00 55.80  ?  45   GLU D OE1 1 
ATOM   11166 O  OE2 . GLU D  1 14  ? 43.218  32.138  -18.656 1.00 51.20  ?  45   GLU D OE2 1 
ATOM   11167 N  N   . THR D  1 15  ? 45.767  29.957  -22.779 1.00 58.94  ?  46   THR D N   1 
ATOM   11168 C  CA  . THR D  1 15  ? 45.554  29.917  -24.217 1.00 58.91  ?  46   THR D CA  1 
ATOM   11169 C  C   . THR D  1 15  ? 44.130  30.295  -24.619 1.00 55.22  ?  46   THR D C   1 
ATOM   11170 O  O   . THR D  1 15  ? 43.858  30.408  -25.818 1.00 48.79  ?  46   THR D O   1 
ATOM   11171 C  CB  . THR D  1 15  ? 45.901  28.520  -24.757 1.00 60.05  ?  46   THR D CB  1 
ATOM   11172 O  OG1 . THR D  1 15  ? 44.902  27.574  -24.343 1.00 55.28  ?  46   THR D OG1 1 
ATOM   11173 C  CG2 . THR D  1 15  ? 47.271  28.074  -24.234 1.00 58.41  ?  46   THR D CG2 1 
ATOM   11174 N  N   . ARG D  1 16  ? 43.234  30.517  -23.651 1.00 53.61  ?  47   ARG D N   1 
ATOM   11175 C  CA  . ARG D  1 16  ? 41.817  30.765  -23.953 1.00 46.86  ?  47   ARG D CA  1 
ATOM   11176 C  C   . ARG D  1 16  ? 41.642  32.111  -24.648 1.00 43.82  ?  47   ARG D C   1 
ATOM   11177 O  O   . ARG D  1 16  ? 42.173  33.115  -24.169 1.00 43.68  ?  47   ARG D O   1 
ATOM   11178 C  CB  . ARG D  1 16  ? 40.999  30.742  -22.668 1.00 47.35  ?  47   ARG D CB  1 
ATOM   11179 C  CG  . ARG D  1 16  ? 40.691  29.356  -22.150 1.00 43.96  ?  47   ARG D CG  1 
ATOM   11180 C  CD  . ARG D  1 16  ? 39.914  29.419  -20.843 1.00 45.39  ?  47   ARG D CD  1 
ATOM   11181 N  NE  . ARG D  1 16  ? 40.487  30.368  -19.893 1.00 45.75  ?  47   ARG D NE  1 
ATOM   11182 C  CZ  . ARG D  1 16  ? 39.876  30.796  -18.796 1.00 41.86  ?  47   ARG D CZ  1 
ATOM   11183 N  NH1 . ARG D  1 16  ? 38.646  30.407  -18.485 1.00 39.55  ?  47   ARG D NH1 1 
ATOM   11184 N  NH2 . ARG D  1 16  ? 40.514  31.634  -17.987 1.00 40.47  ?  47   ARG D NH2 1 
ATOM   11185 N  N   . PRO D  1 17  ? 40.880  32.183  -25.747 1.00 40.50  ?  48   PRO D N   1 
ATOM   11186 C  CA  . PRO D  1 17  ? 40.820  33.428  -26.523 1.00 37.70  ?  48   PRO D CA  1 
ATOM   11187 C  C   . PRO D  1 17  ? 40.045  34.539  -25.832 1.00 35.86  ?  48   PRO D C   1 
ATOM   11188 O  O   . PRO D  1 17  ? 39.147  34.308  -25.015 1.00 33.57  ?  48   PRO D O   1 
ATOM   11189 C  CB  . PRO D  1 17  ? 40.117  33.000  -27.816 1.00 40.08  ?  48   PRO D CB  1 
ATOM   11190 C  CG  . PRO D  1 17  ? 39.231  31.886  -27.382 1.00 41.97  ?  48   PRO D CG  1 
ATOM   11191 C  CD  . PRO D  1 17  ? 40.030  31.137  -26.332 1.00 40.52  ?  48   PRO D CD  1 
ATOM   11192 N  N   . ASN D  1 18  ? 40.429  35.765  -26.163 1.00 33.90  ?  49   ASN D N   1 
ATOM   11193 C  CA  . ASN D  1 18  ? 39.555  36.895  -25.925 1.00 35.49  ?  49   ASN D CA  1 
ATOM   11194 C  C   . ASN D  1 18  ? 38.361  36.805  -26.872 1.00 29.98  ?  49   ASN D C   1 
ATOM   11195 O  O   . ASN D  1 18  ? 38.426  36.172  -27.928 1.00 33.51  ?  49   ASN D O   1 
ATOM   11196 C  CB  . ASN D  1 18  ? 40.296  38.208  -26.156 1.00 31.32  ?  49   ASN D CB  1 
ATOM   11197 C  CG  . ASN D  1 18  ? 41.596  38.288  -25.370 1.00 37.06  ?  49   ASN D CG  1 
ATOM   11198 O  OD1 . ASN D  1 18  ? 41.603  38.184  -24.140 1.00 39.67  ?  49   ASN D OD1 1 
ATOM   11199 N  ND2 . ASN D  1 18  ? 42.703  38.461  -26.083 1.00 36.19  ?  49   ASN D ND2 1 
ATOM   11200 N  N   . ILE D  1 19  ? 37.264  37.438  -26.476 1.00 29.56  ?  50   ILE D N   1 
ATOM   11201 C  CA  . ILE D  1 19  ? 36.026  37.438  -27.256 1.00 28.65  ?  50   ILE D CA  1 
ATOM   11202 C  C   . ILE D  1 19  ? 35.502  38.864  -27.307 1.00 29.65  ?  50   ILE D C   1 
ATOM   11203 O  O   . ILE D  1 19  ? 35.197  39.452  -26.261 1.00 32.67  ?  50   ILE D O   1 
ATOM   11204 C  CB  . ILE D  1 19  ? 34.969  36.509  -26.656 1.00 26.84  ?  50   ILE D CB  1 
ATOM   11205 C  CG1 . ILE D  1 19  ? 35.475  35.071  -26.677 1.00 31.48  ?  50   ILE D CG1 1 
ATOM   11206 C  CG2 . ILE D  1 19  ? 33.604  36.642  -27.451 1.00 26.90  ?  50   ILE D CG2 1 
ATOM   11207 C  CD1 . ILE D  1 19  ? 34.578  34.117  -25.911 1.00 36.66  ?  50   ILE D CD1 1 
ATOM   11208 N  N   . LEU D  1 20  ? 35.408  39.417  -28.514 1.00 28.34  ?  51   LEU D N   1 
ATOM   11209 C  CA  . LEU D  1 20  ? 34.856  40.743  -28.753 1.00 28.01  ?  51   LEU D CA  1 
ATOM   11210 C  C   . LEU D  1 20  ? 33.606  40.586  -29.618 1.00 31.32  ?  51   LEU D C   1 
ATOM   11211 O  O   . LEU D  1 20  ? 33.700  40.191  -30.786 1.00 31.74  ?  51   LEU D O   1 
ATOM   11212 C  CB  . LEU D  1 20  ? 35.872  41.644  -29.446 1.00 31.02  ?  51   LEU D CB  1 
ATOM   11213 C  CG  . LEU D  1 20  ? 35.300  42.958  -29.992 1.00 31.39  ?  51   LEU D CG  1 
ATOM   11214 C  CD1 . LEU D  1 20  ? 34.763  43.799  -28.857 1.00 30.95  ?  51   LEU D CD1 1 
ATOM   11215 C  CD2 . LEU D  1 20  ? 36.353  43.736  -30.789 1.00 28.48  ?  51   LEU D CD2 1 
ATOM   11216 N  N   . VAL D  1 21  ? 32.440  40.889  -29.054 1.00 32.11  ?  52   VAL D N   1 
ATOM   11217 C  CA  . VAL D  1 21  ? 31.191  40.917  -29.815 1.00 28.71  ?  52   VAL D CA  1 
ATOM   11218 C  C   . VAL D  1 21  ? 30.923  42.357  -30.218 1.00 30.87  ?  52   VAL D C   1 
ATOM   11219 O  O   . VAL D  1 21  ? 30.703  43.214  -29.348 1.00 31.25  ?  52   VAL D O   1 
ATOM   11220 C  CB  . VAL D  1 21  ? 30.007  40.370  -29.003 1.00 32.96  ?  52   VAL D CB  1 
ATOM   11221 C  CG1 . VAL D  1 21  ? 28.682  40.579  -29.799 1.00 33.06  ?  52   VAL D CG1 1 
ATOM   11222 C  CG2 . VAL D  1 21  ? 30.217  38.909  -28.646 1.00 35.77  ?  52   VAL D CG2 1 
ATOM   11223 N  N   . VAL D  1 22  ? 30.919  42.630  -31.520 1.00 28.80  ?  53   VAL D N   1 
ATOM   11224 C  CA  . VAL D  1 22  ? 30.497  43.930  -32.038 1.00 30.22  ?  53   VAL D CA  1 
ATOM   11225 C  C   . VAL D  1 22  ? 29.077  43.761  -32.571 1.00 30.52  ?  53   VAL D C   1 
ATOM   11226 O  O   . VAL D  1 22  ? 28.867  43.125  -33.603 1.00 28.75  ?  53   VAL D O   1 
ATOM   11227 C  CB  . VAL D  1 22  ? 31.439  44.451  -33.128 1.00 27.78  ?  53   VAL D CB  1 
ATOM   11228 C  CG1 . VAL D  1 22  ? 30.960  45.827  -33.630 1.00 28.39  ?  53   VAL D CG1 1 
ATOM   11229 C  CG2 . VAL D  1 22  ? 32.911  44.515  -32.598 1.00 26.00  ?  53   VAL D CG2 1 
ATOM   11230 N  N   . LEU D  1 23  ? 28.106  44.318  -31.861 1.00 30.54  ?  54   LEU D N   1 
ATOM   11231 C  CA  . LEU D  1 23  ? 26.686  44.145  -32.162 1.00 28.67  ?  54   LEU D CA  1 
ATOM   11232 C  C   . LEU D  1 23  ? 26.149  45.495  -32.610 1.00 30.25  ?  54   LEU D C   1 
ATOM   11233 O  O   . LEU D  1 23  ? 26.116  46.438  -31.814 1.00 27.98  ?  54   LEU D O   1 
ATOM   11234 C  CB  . LEU D  1 23  ? 25.915  43.656  -30.933 1.00 28.90  ?  54   LEU D CB  1 
ATOM   11235 C  CG  . LEU D  1 23  ? 24.405  43.468  -31.149 1.00 29.74  ?  54   LEU D CG  1 
ATOM   11236 C  CD1 . LEU D  1 23  ? 24.183  42.373  -32.188 1.00 26.44  ?  54   LEU D CD1 1 
ATOM   11237 C  CD2 . LEU D  1 23  ? 23.703  43.121  -29.828 1.00 31.89  ?  54   LEU D CD2 1 
ATOM   11238 N  N   . CYS D  1 24  ? 25.734  45.591  -33.873 1.00 32.86  ?  55   CYS D N   1 
ATOM   11239 C  CA  . CYS D  1 24  ? 25.070  46.799  -34.340 1.00 34.10  ?  55   CYS D CA  1 
ATOM   11240 C  C   . CYS D  1 24  ? 23.561  46.676  -34.129 1.00 34.69  ?  55   CYS D C   1 
ATOM   11241 O  O   . CYS D  1 24  ? 23.035  45.600  -33.833 1.00 32.16  ?  55   CYS D O   1 
ATOM   11242 C  CB  . CYS D  1 24  ? 25.399  47.071  -35.814 1.00 34.23  ?  55   CYS D CB  1 
ATOM   11243 S  SG  . CYS D  1 24  ? 27.046  47.865  -36.042 1.00 36.62  ?  55   CYS D SG  1 
ATOM   11244 N  N   . ASP D  1 25  ? 22.900  47.828  -34.294 1.00 29.12  ?  56   ASP D N   1 
ATOM   11245 C  CA  . ASP D  1 25  ? 21.453  47.916  -33.991 1.00 28.81  ?  56   ASP D CA  1 
ATOM   11246 C  C   . ASP D  1 25  ? 20.697  48.335  -35.250 1.00 31.34  ?  56   ASP D C   1 
ATOM   11247 O  O   . ASP D  1 25  ? 20.964  49.440  -35.760 1.00 28.17  ?  56   ASP D O   1 
ATOM   11248 C  CB  . ASP D  1 25  ? 21.232  48.883  -32.846 1.00 29.83  ?  56   ASP D CB  1 
ATOM   11249 C  CG  . ASP D  1 25  ? 19.849  48.892  -32.210 1.00 33.99  ?  56   ASP D CG  1 
ATOM   11250 O  OD1 . ASP D  1 25  ? 19.031  48.019  -32.558 1.00 34.78  -1 56   ASP D OD1 1 
ATOM   11251 O  OD2 . ASP D  1 25  ? 19.610  49.768  -31.358 1.00 32.71  ?  56   ASP D OD2 1 
ATOM   11252 N  N   . ASP D  1 26  ? 19.813  47.461  -35.736 1.00 30.18  ?  57   ASP D N   1 
ATOM   11253 C  CA  . ASP D  1 26  ? 19.028  47.768  -36.969 1.00 30.78  ?  57   ASP D CA  1 
ATOM   11254 C  C   . ASP D  1 26  ? 19.951  48.004  -38.174 1.00 31.01  ?  57   ASP D C   1 
ATOM   11255 O  O   . ASP D  1 26  ? 19.624  48.858  -39.010 1.00 28.86  ?  57   ASP D O   1 
ATOM   11256 C  CB  . ASP D  1 26  ? 18.128  48.973  -36.804 1.00 27.76  ?  57   ASP D CB  1 
ATOM   11257 C  CG  . ASP D  1 26  ? 16.998  48.848  -35.792 1.00 30.23  ?  57   ASP D CG  1 
ATOM   11258 O  OD1 . ASP D  1 26  ? 16.921  47.810  -35.105 1.00 29.56  ?  57   ASP D OD1 1 
ATOM   11259 O  OD2 . ASP D  1 26  ? 16.189  49.790  -35.716 1.00 32.68  -1 57   ASP D OD2 1 
ATOM   11260 N  N   . LEU D  1 27  ? 21.048  47.258  -38.266 1.00 28.79  ?  58   LEU D N   1 
ATOM   11261 C  CA  . LEU D  1 27  ? 21.920  47.333  -39.443 1.00 25.71  ?  58   LEU D CA  1 
ATOM   11262 C  C   . LEU D  1 27  ? 21.363  46.457  -40.568 1.00 31.69  ?  58   LEU D C   1 
ATOM   11263 O  O   . LEU D  1 27  ? 21.171  45.249  -40.379 1.00 32.09  ?  58   LEU D O   1 
ATOM   11264 C  CB  . LEU D  1 27  ? 23.335  46.881  -39.073 1.00 28.70  ?  58   LEU D CB  1 
ATOM   11265 C  CG  . LEU D  1 27  ? 24.347  46.682  -40.213 1.00 34.14  ?  58   LEU D CG  1 
ATOM   11266 C  CD1 . LEU D  1 27  ? 24.716  48.056  -40.774 1.00 31.47  ?  58   LEU D CD1 1 
ATOM   11267 C  CD2 . LEU D  1 27  ? 25.630  45.933  -39.731 1.00 26.95  ?  58   LEU D CD2 1 
ATOM   11268 N  N   . GLY D  1 28  ? 21.136  47.057  -41.747 1.00 30.91  ?  59   GLY D N   1 
ATOM   11269 C  CA  . GLY D  1 28  ? 20.559  46.330  -42.861 1.00 28.63  ?  59   GLY D CA  1 
ATOM   11270 C  C   . GLY D  1 28  ? 21.526  45.352  -43.513 1.00 32.60  ?  59   GLY D C   1 
ATOM   11271 O  O   . GLY D  1 28  ? 22.758  45.452  -43.422 1.00 27.69  ?  59   GLY D O   1 
ATOM   11272 N  N   . TYR D  1 29  ? 20.937  44.397  -44.225 1.00 28.89  ?  60   TYR D N   1 
ATOM   11273 C  CA  . TYR D  1 29  ? 21.685  43.250  -44.735 1.00 28.89  ?  60   TYR D CA  1 
ATOM   11274 C  C   . TYR D  1 29  ? 22.675  43.626  -45.826 1.00 31.40  ?  60   TYR D C   1 
ATOM   11275 O  O   . TYR D  1 29  ? 23.702  42.956  -45.979 1.00 32.24  ?  60   TYR D O   1 
ATOM   11276 C  CB  . TYR D  1 29  ? 20.711  42.210  -45.269 1.00 28.43  ?  60   TYR D CB  1 
ATOM   11277 C  CG  . TYR D  1 29  ? 21.253  40.809  -45.355 1.00 30.41  ?  60   TYR D CG  1 
ATOM   11278 C  CD1 . TYR D  1 29  ? 21.528  40.078  -44.199 1.00 27.22  ?  60   TYR D CD1 1 
ATOM   11279 C  CD2 . TYR D  1 29  ? 21.451  40.193  -46.586 1.00 30.26  ?  60   TYR D CD2 1 
ATOM   11280 C  CE1 . TYR D  1 29  ? 21.985  38.786  -44.269 1.00 25.95  ?  60   TYR D CE1 1 
ATOM   11281 C  CE2 . TYR D  1 29  ? 21.924  38.877  -46.668 1.00 28.53  ?  60   TYR D CE2 1 
ATOM   11282 C  CZ  . TYR D  1 29  ? 22.195  38.190  -45.506 1.00 29.70  ?  60   TYR D CZ  1 
ATOM   11283 O  OH  . TYR D  1 29  ? 22.657  36.892  -45.562 1.00 28.49  ?  60   TYR D OH  1 
ATOM   11284 N  N   . ALA D  1 30  ? 22.367  44.649  -46.621 1.00 27.61  ?  61   ALA D N   1 
ATOM   11285 C  CA  . ALA D  1 30  ? 23.239  45.121  -47.687 1.00 33.54  ?  61   ALA D CA  1 
ATOM   11286 C  C   . ALA D  1 30  ? 24.018  46.367  -47.279 1.00 31.87  ?  61   ALA D C   1 
ATOM   11287 O  O   . ALA D  1 30  ? 24.407  47.164  -48.130 1.00 34.57  ?  61   ALA D O   1 
ATOM   11288 C  CB  . ALA D  1 30  ? 22.422  45.401  -48.954 1.00 31.40  ?  61   ALA D CB  1 
ATOM   11289 N  N   . ASP D  1 31  ? 24.245  46.571  -45.986 1.00 32.63  ?  62   ASP D N   1 
ATOM   11290 C  CA  . ASP D  1 31  ? 24.733  47.862  -45.525 1.00 29.47  ?  62   ASP D CA  1 
ATOM   11291 C  C   . ASP D  1 31  ? 26.153  47.797  -44.983 1.00 32.32  ?  62   ASP D C   1 
ATOM   11292 O  O   . ASP D  1 31  ? 26.594  48.726  -44.300 1.00 28.63  ?  62   ASP D O   1 
ATOM   11293 C  CB  . ASP D  1 31  ? 23.756  48.430  -44.505 1.00 25.41  ?  62   ASP D CB  1 
ATOM   11294 C  CG  . ASP D  1 31  ? 22.428  48.822  -45.165 1.00 32.84  ?  62   ASP D CG  1 
ATOM   11295 O  OD1 . ASP D  1 31  ? 22.421  48.989  -46.400 1.00 34.84  ?  62   ASP D OD1 1 
ATOM   11296 O  OD2 . ASP D  1 31  ? 21.408  48.947  -44.463 1.00 31.57  -1 62   ASP D OD2 1 
ATOM   11297 N  N   . VAL D  1 32  ? 26.879  46.722  -45.288 1.00 33.86  ?  63   VAL D N   1 
ATOM   11298 C  CA  . VAL D  1 32  ? 28.314  46.637  -45.042 1.00 34.72  ?  63   VAL D CA  1 
ATOM   11299 C  C   . VAL D  1 32  ? 28.957  46.059  -46.291 1.00 37.12  ?  63   VAL D C   1 
ATOM   11300 O  O   . VAL D  1 32  ? 28.391  45.155  -46.920 1.00 33.55  ?  63   VAL D O   1 
ATOM   11301 C  CB  . VAL D  1 32  ? 28.677  45.772  -43.815 1.00 30.63  ?  63   VAL D CB  1 
ATOM   11302 C  CG1 . VAL D  1 32  ? 28.353  46.502  -42.527 1.00 29.34  ?  63   VAL D CG1 1 
ATOM   11303 C  CG2 . VAL D  1 32  ? 28.011  44.408  -43.882 1.00 29.73  ?  63   VAL D CG2 1 
ATOM   11304 N  N   . GLY D  1 33  ? 30.143  46.582  -46.633 1.00 31.66  ?  64   GLY D N   1 
ATOM   11305 C  CA  . GLY D  1 33  ? 30.822  46.186  -47.864 1.00 33.58  ?  64   GLY D CA  1 
ATOM   11306 C  C   . GLY D  1 33  ? 30.920  44.685  -48.053 1.00 35.23  ?  64   GLY D C   1 
ATOM   11307 O  O   . GLY D  1 33  ? 30.604  44.162  -49.121 1.00 34.43  ?  64   GLY D O   1 
ATOM   11308 N  N   . PHE D  1 34  ? 31.315  43.964  -47.003 1.00 34.92  ?  65   PHE D N   1 
ATOM   11309 C  CA  . PHE D  1 34  ? 31.515  42.525  -47.139 1.00 36.78  ?  65   PHE D CA  1 
ATOM   11310 C  C   . PHE D  1 34  ? 30.214  41.751  -47.361 1.00 35.40  ?  65   PHE D C   1 
ATOM   11311 O  O   . PHE D  1 34  ? 30.263  40.592  -47.793 1.00 31.86  ?  65   PHE D O   1 
ATOM   11312 C  CB  . PHE D  1 34  ? 32.269  41.983  -45.910 1.00 32.94  ?  65   PHE D CB  1 
ATOM   11313 C  CG  . PHE D  1 34  ? 31.426  41.873  -44.653 1.00 36.19  ?  65   PHE D CG  1 
ATOM   11314 C  CD1 . PHE D  1 34  ? 30.634  40.744  -44.406 1.00 31.72  ?  65   PHE D CD1 1 
ATOM   11315 C  CD2 . PHE D  1 34  ? 31.447  42.881  -43.709 1.00 32.42  ?  65   PHE D CD2 1 
ATOM   11316 C  CE1 . PHE D  1 34  ? 29.876  40.641  -43.243 1.00 29.21  ?  65   PHE D CE1 1 
ATOM   11317 C  CE2 . PHE D  1 34  ? 30.692  42.783  -42.533 1.00 33.27  ?  65   PHE D CE2 1 
ATOM   11318 C  CZ  . PHE D  1 34  ? 29.892  41.664  -42.311 1.00 30.00  ?  65   PHE D CZ  1 
ATOM   11319 N  N   . ASN D  1 35  ? 29.053  42.329  -47.067 1.00 34.58  ?  66   ASN D N   1 
ATOM   11320 C  CA  . ASN D  1 35  ? 27.807  41.606  -47.283 1.00 34.20  ?  66   ASN D CA  1 
ATOM   11321 C  C   . ASN D  1 35  ? 27.022  42.153  -48.470 1.00 35.86  ?  66   ASN D C   1 
ATOM   11322 O  O   . ASN D  1 35  ? 25.823  41.875  -48.596 1.00 37.55  ?  66   ASN D O   1 
ATOM   11323 C  CB  . ASN D  1 35  ? 26.934  41.596  -46.027 1.00 33.22  ?  66   ASN D CB  1 
ATOM   11324 C  CG  . ASN D  1 35  ? 26.140  40.300  -45.895 1.00 35.24  ?  66   ASN D CG  1 
ATOM   11325 O  OD1 . ASN D  1 35  ? 26.703  39.215  -46.014 1.00 34.87  ?  66   ASN D OD1 1 
ATOM   11326 N  ND2 . ASN D  1 35  ? 24.829  40.407  -45.689 1.00 30.79  ?  66   ASN D ND2 1 
ATOM   11327 N  N   . GLY D  1 36  ? 27.681  42.925  -49.335 1.00 37.75  ?  67   GLY D N   1 
ATOM   11328 C  CA  . GLY D  1 36  ? 27.134  43.335  -50.619 1.00 39.24  ?  67   GLY D CA  1 
ATOM   11329 C  C   . GLY D  1 36  ? 26.912  44.827  -50.804 1.00 38.34  ?  67   GLY D C   1 
ATOM   11330 O  O   . GLY D  1 36  ? 26.369  45.214  -51.843 1.00 38.57  ?  67   GLY D O   1 
ATOM   11331 N  N   . SER D  1 37  ? 27.280  45.707  -49.874 1.00 38.09  ?  68   SER D N   1 
ATOM   11332 C  CA  . SER D  1 37  ? 26.980  47.127  -50.045 1.00 38.16  ?  68   SER D CA  1 
ATOM   11333 C  C   . SER D  1 37  ? 27.819  47.742  -51.157 1.00 43.69  ?  68   SER D C   1 
ATOM   11334 O  O   . SER D  1 37  ? 29.034  47.536  -51.224 1.00 41.51  ?  68   SER D O   1 
ATOM   11335 C  CB  . SER D  1 37  ? 27.231  47.900  -48.751 1.00 38.90  ?  68   SER D CB  1 
ATOM   11336 O  OG  . SER D  1 37  ? 26.628  49.188  -48.841 1.00 40.54  ?  68   SER D OG  1 
ATOM   11337 N  N   . THR D  1 38  ? 27.172  48.531  -52.018 1.00 41.34  ?  69   THR D N   1 
ATOM   11338 C  CA  . THR D  1 38  ? 27.888  49.260  -53.054 1.00 42.35  ?  69   THR D CA  1 
ATOM   11339 C  C   . THR D  1 38  ? 27.961  50.763  -52.799 1.00 43.84  ?  69   THR D C   1 
ATOM   11340 O  O   . THR D  1 38  ? 28.653  51.457  -53.546 1.00 47.63  ?  69   THR D O   1 
ATOM   11341 C  CB  . THR D  1 38  ? 27.264  48.999  -54.432 1.00 43.78  ?  69   THR D CB  1 
ATOM   11342 O  OG1 . THR D  1 38  ? 25.889  49.377  -54.412 1.00 44.60  ?  69   THR D OG1 1 
ATOM   11343 C  CG2 . THR D  1 38  ? 27.373  47.505  -54.775 1.00 41.24  ?  69   THR D CG2 1 
ATOM   11344 N  N   . ASP D  1 39  ? 27.291  51.295  -51.764 1.00 41.75  ?  70   ASP D N   1 
ATOM   11345 C  CA  . ASP D  1 39  ? 27.424  52.719  -51.453 1.00 40.93  ?  70   ASP D CA  1 
ATOM   11346 C  C   . ASP D  1 39  ? 27.962  53.020  -50.051 1.00 41.57  ?  70   ASP D C   1 
ATOM   11347 O  O   . ASP D  1 39  ? 28.519  54.102  -49.838 1.00 39.51  ?  70   ASP D O   1 
ATOM   11348 C  CB  . ASP D  1 39  ? 26.078  53.450  -51.637 1.00 37.91  ?  70   ASP D CB  1 
ATOM   11349 C  CG  . ASP D  1 39  ? 24.961  52.854  -50.804 1.00 40.94  ?  70   ASP D CG  1 
ATOM   11350 O  OD1 . ASP D  1 39  ? 25.069  51.686  -50.379 1.00 38.79  ?  70   ASP D OD1 1 
ATOM   11351 O  OD2 . ASP D  1 39  ? 23.961  53.563  -50.568 1.00 45.15  -1 70   ASP D OD2 1 
ATOM   11352 N  N   . ILE D  1 40  ? 27.816  52.117  -49.092 1.00 40.70  ?  71   ILE D N   1 
ATOM   11353 C  CA  . ILE D  1 40  ? 28.323  52.350  -47.746 1.00 35.47  ?  71   ILE D CA  1 
ATOM   11354 C  C   . ILE D  1 40  ? 29.704  51.727  -47.651 1.00 37.61  ?  71   ILE D C   1 
ATOM   11355 O  O   . ILE D  1 40  ? 29.903  50.575  -48.053 1.00 39.74  ?  71   ILE D O   1 
ATOM   11356 C  CB  . ILE D  1 40  ? 27.368  51.773  -46.686 1.00 36.89  ?  71   ILE D CB  1 
ATOM   11357 C  CG1 . ILE D  1 40  ? 25.977  52.401  -46.840 1.00 30.59  ?  71   ILE D CG1 1 
ATOM   11358 C  CG2 . ILE D  1 40  ? 27.905  52.017  -45.280 1.00 33.04  ?  71   ILE D CG2 1 
ATOM   11359 C  CD1 . ILE D  1 40  ? 25.021  52.100  -45.656 1.00 32.67  ?  71   ILE D CD1 1 
ATOM   11360 N  N   . LEU D  1 41  ? 30.662  52.490  -47.135 1.00 35.84  ?  72   LEU D N   1 
ATOM   11361 C  CA  . LEU D  1 41  ? 32.063  52.086  -47.111 1.00 39.07  ?  72   LEU D CA  1 
ATOM   11362 C  C   . LEU D  1 41  ? 32.426  51.623  -45.704 1.00 34.54  ?  72   LEU D C   1 
ATOM   11363 O  O   . LEU D  1 41  ? 32.291  52.388  -44.741 1.00 36.30  ?  72   LEU D O   1 
ATOM   11364 C  CB  . LEU D  1 41  ? 32.962  53.243  -47.558 1.00 36.83  ?  72   LEU D CB  1 
ATOM   11365 C  CG  . LEU D  1 41  ? 32.653  53.770  -48.961 1.00 42.78  ?  72   LEU D CG  1 
ATOM   11366 C  CD1 . LEU D  1 41  ? 33.212  55.177  -49.158 1.00 44.89  ?  72   LEU D CD1 1 
ATOM   11367 C  CD2 . LEU D  1 41  ? 33.174  52.810  -50.023 1.00 37.29  ?  72   LEU D CD2 1 
ATOM   11368 N  N   . THR D  1 42  ? 32.843  50.366  -45.583 1.00 34.49  ?  73   THR D N   1 
ATOM   11369 C  CA  . THR D  1 42  ? 33.202  49.770  -44.292 1.00 31.60  ?  73   THR D CA  1 
ATOM   11370 C  C   . THR D  1 42  ? 34.533  49.043  -44.430 1.00 33.56  ?  73   THR D C   1 
ATOM   11371 O  O   . THR D  1 42  ? 34.622  47.829  -44.220 1.00 33.95  ?  73   THR D O   1 
ATOM   11372 C  CB  . THR D  1 42  ? 32.108  48.816  -43.810 1.00 33.67  ?  73   THR D CB  1 
ATOM   11373 O  OG1 . THR D  1 42  ? 31.933  47.769  -44.777 1.00 35.82  ?  73   THR D OG1 1 
ATOM   11374 C  CG2 . THR D  1 42  ? 30.777  49.554  -43.658 1.00 33.72  ?  73   THR D CG2 1 
ATOM   11375 N  N   . PRO D  1 43  ? 35.604  49.766  -44.788 1.00 36.22  ?  74   PRO D N   1 
ATOM   11376 C  CA  . PRO D  1 43  ? 36.881  49.084  -45.081 1.00 36.34  ?  74   PRO D CA  1 
ATOM   11377 C  C   . PRO D  1 43  ? 37.455  48.290  -43.911 1.00 33.97  ?  74   PRO D C   1 
ATOM   11378 O  O   . PRO D  1 43  ? 38.010  47.203  -44.131 1.00 36.64  ?  74   PRO D O   1 
ATOM   11379 C  CB  . PRO D  1 43  ? 37.805  50.247  -45.488 1.00 39.44  ?  74   PRO D CB  1 
ATOM   11380 C  CG  . PRO D  1 43  ? 37.221  51.455  -44.810 1.00 37.51  ?  74   PRO D CG  1 
ATOM   11381 C  CD  . PRO D  1 43  ? 35.721  51.230  -44.924 1.00 35.63  ?  74   PRO D CD  1 
ATOM   11382 N  N   . GLU D  1 44  ? 37.316  48.787  -42.677 1.00 35.54  ?  75   GLU D N   1 
ATOM   11383 C  CA  . GLU D  1 44  ? 37.857  48.080  -41.517 1.00 35.86  ?  75   GLU D CA  1 
ATOM   11384 C  C   . GLU D  1 44  ? 37.082  46.797  -41.250 1.00 41.60  ?  75   GLU D C   1 
ATOM   11385 O  O   . GLU D  1 44  ? 37.673  45.743  -40.973 1.00 33.97  ?  75   GLU D O   1 
ATOM   11386 C  CB  . GLU D  1 44  ? 37.803  48.962  -40.270 1.00 34.43  ?  75   GLU D CB  1 
ATOM   11387 C  CG  . GLU D  1 44  ? 38.633  50.211  -40.332 1.00 41.82  ?  75   GLU D CG  1 
ATOM   11388 C  CD  . GLU D  1 44  ? 40.140  49.931  -40.353 1.00 42.58  ?  75   GLU D CD  1 
ATOM   11389 O  OE1 . GLU D  1 44  ? 40.579  48.772  -40.147 1.00 39.82  ?  75   GLU D OE1 1 
ATOM   11390 O  OE2 . GLU D  1 44  ? 40.881  50.893  -40.579 1.00 42.74  -1 75   GLU D OE2 1 
ATOM   11391 N  N   . LEU D  1 45  ? 35.746  46.881  -41.279 1.00 35.31  ?  76   LEU D N   1 
ATOM   11392 C  CA  . LEU D  1 45  ? 34.943  45.677  -41.107 1.00 34.50  ?  76   LEU D CA  1 
ATOM   11393 C  C   . LEU D  1 45  ? 35.195  44.695  -42.236 1.00 31.91  ?  76   LEU D C   1 
ATOM   11394 O  O   . LEU D  1 45  ? 35.291  43.487  -41.999 1.00 30.03  ?  76   LEU D O   1 
ATOM   11395 C  CB  . LEU D  1 45  ? 33.463  46.038  -41.018 1.00 31.40  ?  76   LEU D CB  1 
ATOM   11396 C  CG  . LEU D  1 45  ? 33.076  46.692  -39.690 1.00 32.59  ?  76   LEU D CG  1 
ATOM   11397 C  CD1 . LEU D  1 45  ? 31.782  47.541  -39.826 1.00 34.42  ?  76   LEU D CD1 1 
ATOM   11398 C  CD2 . LEU D  1 45  ? 32.957  45.636  -38.583 1.00 30.84  ?  76   LEU D CD2 1 
ATOM   11399 N  N   . ASP D  1 46  ? 35.342  45.197  -43.472 1.00 33.57  ?  77   ASP D N   1 
ATOM   11400 C  CA  . ASP D  1 46  ? 35.570  44.303  -44.601 1.00 34.26  ?  77   ASP D CA  1 
ATOM   11401 C  C   . ASP D  1 46  ? 36.911  43.589  -44.475 1.00 37.01  ?  77   ASP D C   1 
ATOM   11402 O  O   . ASP D  1 46  ? 37.043  42.417  -44.851 1.00 35.74  ?  77   ASP D O   1 
ATOM   11403 C  CB  . ASP D  1 46  ? 35.511  45.076  -45.908 1.00 36.27  ?  77   ASP D CB  1 
ATOM   11404 C  CG  . ASP D  1 46  ? 34.108  45.564  -46.242 1.00 36.82  ?  77   ASP D CG  1 
ATOM   11405 O  OD1 . ASP D  1 46  ? 33.139  45.298  -45.486 1.00 35.26  ?  77   ASP D OD1 1 
ATOM   11406 O  OD2 . ASP D  1 46  ? 33.988  46.227  -47.274 1.00 40.29  -1 77   ASP D OD2 1 
ATOM   11407 N  N   . ASN D  1 47  ? 37.923  44.276  -43.945 1.00 38.14  ?  78   ASN D N   1 
ATOM   11408 C  CA  . ASN D  1 47  ? 39.222  43.621  -43.807 1.00 39.00  ?  78   ASN D CA  1 
ATOM   11409 C  C   . ASN D  1 47  ? 39.156  42.467  -42.809 1.00 36.51  ?  78   ASN D C   1 
ATOM   11410 O  O   . ASN D  1 47  ? 39.689  41.381  -43.074 1.00 39.88  ?  78   ASN D O   1 
ATOM   11411 C  CB  . ASN D  1 47  ? 40.297  44.627  -43.393 1.00 41.82  ?  78   ASN D CB  1 
ATOM   11412 C  CG  . ASN D  1 47  ? 41.695  44.053  -43.530 1.00 44.80  ?  78   ASN D CG  1 
ATOM   11413 O  OD1 . ASN D  1 47  ? 42.181  43.850  -44.640 1.00 50.82  ?  78   ASN D OD1 1 
ATOM   11414 N  ND2 . ASN D  1 47  ? 42.317  43.733  -42.410 1.00 44.28  ?  78   ASN D ND2 1 
ATOM   11415 N  N   . LEU D  1 48  ? 38.484  42.671  -41.670 1.00 33.10  ?  79   LEU D N   1 
ATOM   11416 C  CA  . LEU D  1 48  ? 38.301  41.580  -40.715 1.00 33.13  ?  79   LEU D CA  1 
ATOM   11417 C  C   . LEU D  1 48  ? 37.557  40.422  -41.357 1.00 32.15  ?  79   LEU D C   1 
ATOM   11418 O  O   . LEU D  1 48  ? 37.984  39.264  -41.271 1.00 32.71  ?  79   LEU D O   1 
ATOM   11419 C  CB  . LEU D  1 48  ? 37.549  42.074  -39.473 1.00 27.83  ?  79   LEU D CB  1 
ATOM   11420 C  CG  . LEU D  1 48  ? 38.269  43.079  -38.567 1.00 30.48  ?  79   LEU D CG  1 
ATOM   11421 C  CD1 . LEU D  1 48  ? 37.369  43.594  -37.417 1.00 28.58  ?  79   LEU D CD1 1 
ATOM   11422 C  CD2 . LEU D  1 48  ? 39.545  42.470  -38.006 1.00 32.49  ?  79   LEU D CD2 1 
ATOM   11423 N  N   . ALA D  1 49  ? 36.439  40.727  -42.022 1.00 33.84  ?  80   ALA D N   1 
ATOM   11424 C  CA  . ALA D  1 49  ? 35.632  39.694  -42.666 1.00 33.92  ?  80   ALA D CA  1 
ATOM   11425 C  C   . ALA D  1 49  ? 36.443  38.924  -43.698 1.00 34.11  ?  80   ALA D C   1 
ATOM   11426 O  O   . ALA D  1 49  ? 36.404  37.688  -43.731 1.00 35.38  ?  80   ALA D O   1 
ATOM   11427 C  CB  . ALA D  1 49  ? 34.395  40.328  -43.306 1.00 32.15  ?  80   ALA D CB  1 
ATOM   11428 N  N   . GLN D  1 50  ? 37.190  39.641  -44.551 1.00 34.31  ?  81   GLN D N   1 
ATOM   11429 C  CA  . GLN D  1 50  ? 38.037  38.997  -45.553 1.00 35.35  ?  81   GLN D CA  1 
ATOM   11430 C  C   . GLN D  1 50  ? 39.087  38.092  -44.922 1.00 38.20  ?  81   GLN D C   1 
ATOM   11431 O  O   . GLN D  1 50  ? 39.549  37.138  -45.565 1.00 41.54  ?  81   GLN D O   1 
ATOM   11432 C  CB  . GLN D  1 50  ? 38.726  40.054  -46.427 1.00 36.11  ?  81   GLN D CB  1 
ATOM   11433 C  CG  . GLN D  1 50  ? 37.781  40.766  -47.401 1.00 46.48  ?  81   GLN D CG  1 
ATOM   11434 C  CD  . GLN D  1 50  ? 38.302  42.127  -47.896 1.00 50.43  ?  81   GLN D CD  1 
ATOM   11435 O  OE1 . GLN D  1 50  ? 37.568  42.883  -48.554 1.00 50.80  ?  81   GLN D OE1 1 
ATOM   11436 N  NE2 . GLN D  1 50  ? 39.573  42.427  -47.610 1.00 51.99  ?  81   GLN D NE2 1 
ATOM   11437 N  N   . ASN D  1 51  ? 39.459  38.358  -43.676 1.00 37.76  ?  82   ASN D N   1 
ATOM   11438 C  CA  . ASN D  1 51  ? 40.498  37.604  -42.994 1.00 38.48  ?  82   ASN D CA  1 
ATOM   11439 C  C   . ASN D  1 51  ? 39.929  36.601  -42.010 1.00 41.18  ?  82   ASN D C   1 
ATOM   11440 O  O   . ASN D  1 51  ? 40.668  36.086  -41.163 1.00 36.22  ?  82   ASN D O   1 
ATOM   11441 C  CB  . ASN D  1 51  ? 41.460  38.566  -42.298 1.00 40.86  ?  82   ASN D CB  1 
ATOM   11442 C  CG  . ASN D  1 51  ? 42.488  39.127  -43.260 1.00 50.30  ?  82   ASN D CG  1 
ATOM   11443 O  OD1 . ASN D  1 51  ? 43.342  38.393  -43.752 1.00 53.06  ?  82   ASN D OD1 1 
ATOM   11444 N  ND2 . ASN D  1 51  ? 42.384  40.415  -43.572 1.00 49.21  ?  82   ASN D ND2 1 
ATOM   11445 N  N   . GLY D  1 52  ? 38.628  36.327  -42.092 1.00 37.32  ?  83   GLY D N   1 
ATOM   11446 C  CA  . GLY D  1 52  ? 38.012  35.252  -41.325 1.00 32.90  ?  83   GLY D CA  1 
ATOM   11447 C  C   . GLY D  1 52  ? 36.895  34.613  -42.115 1.00 37.79  ?  83   GLY D C   1 
ATOM   11448 O  O   . GLY D  1 52  ? 37.012  34.420  -43.333 1.00 38.11  ?  83   GLY D O   1 
ATOM   11449 N  N   . SER D  1 53  ? 35.797  34.303  -41.433 1.00 33.42  ?  84   SER D N   1 
ATOM   11450 C  CA  . SER D  1 53  ? 34.705  33.531  -42.001 1.00 34.01  ?  84   SER D CA  1 
ATOM   11451 C  C   . SER D  1 53  ? 33.467  34.415  -42.087 1.00 34.88  ?  84   SER D C   1 
ATOM   11452 O  O   . SER D  1 53  ? 32.991  34.911  -41.061 1.00 33.21  ?  84   SER D O   1 
ATOM   11453 C  CB  . SER D  1 53  ? 34.436  32.294  -41.142 1.00 37.60  ?  84   SER D CB  1 
ATOM   11454 O  OG  . SER D  1 53  ? 33.334  31.560  -41.651 1.00 38.02  ?  84   SER D OG  1 
ATOM   11455 N  N   . ILE D  1 54  ? 32.957  34.619  -43.306 1.00 31.48  ?  85   ILE D N   1 
ATOM   11456 C  CA  . ILE D  1 54  ? 31.691  35.322  -43.529 1.00 34.27  ?  85   ILE D CA  1 
ATOM   11457 C  C   . ILE D  1 54  ? 30.553  34.305  -43.500 1.00 34.83  ?  85   ILE D C   1 
ATOM   11458 O  O   . ILE D  1 54  ? 30.594  33.289  -44.208 1.00 32.57  ?  85   ILE D O   1 
ATOM   11459 C  CB  . ILE D  1 54  ? 31.701  36.079  -44.874 1.00 36.34  ?  85   ILE D CB  1 
ATOM   11460 C  CG1 . ILE D  1 54  ? 32.654  37.276  -44.833 1.00 36.46  ?  85   ILE D CG1 1 
ATOM   11461 C  CG2 . ILE D  1 54  ? 30.292  36.553  -45.225 1.00 33.71  ?  85   ILE D CG2 1 
ATOM   11462 C  CD1 . ILE D  1 54  ? 32.896  37.959  -46.173 1.00 33.93  ?  85   ILE D CD1 1 
ATOM   11463 N  N   . PHE D  1 55  ? 29.517  34.585  -42.706 1.00 35.84  ?  86   PHE D N   1 
ATOM   11464 C  CA  . PHE D  1 55  ? 28.357  33.700  -42.594 1.00 31.27  ?  86   PHE D CA  1 
ATOM   11465 C  C   . PHE D  1 55  ? 27.234  34.212  -43.498 1.00 32.00  ?  86   PHE D C   1 
ATOM   11466 O  O   . PHE D  1 55  ? 26.673  35.290  -43.268 1.00 27.34  ?  86   PHE D O   1 
ATOM   11467 C  CB  . PHE D  1 55  ? 27.909  33.591  -41.137 1.00 31.65  ?  86   PHE D CB  1 
ATOM   11468 C  CG  . PHE D  1 55  ? 28.915  32.907  -40.255 1.00 32.94  ?  86   PHE D CG  1 
ATOM   11469 C  CD1 . PHE D  1 55  ? 30.089  33.540  -39.923 1.00 32.00  ?  86   PHE D CD1 1 
ATOM   11470 C  CD2 . PHE D  1 55  ? 28.684  31.624  -39.768 1.00 30.93  ?  86   PHE D CD2 1 
ATOM   11471 C  CE1 . PHE D  1 55  ? 31.015  32.923  -39.123 1.00 31.20  ?  86   PHE D CE1 1 
ATOM   11472 C  CE2 . PHE D  1 55  ? 29.617  30.990  -38.970 1.00 36.34  ?  86   PHE D CE2 1 
ATOM   11473 C  CZ  . PHE D  1 55  ? 30.781  31.649  -38.636 1.00 32.10  ?  86   PHE D CZ  1 
ATOM   11474 N  N   . THR D  1 56  ? 26.908  33.440  -44.529 1.00 31.58  ?  87   THR D N   1 
ATOM   11475 C  CA  . THR D  1 56  ? 25.954  33.912  -45.519 1.00 31.07  ?  87   THR D CA  1 
ATOM   11476 C  C   . THR D  1 56  ? 24.514  33.593  -45.154 1.00 32.34  ?  87   THR D C   1 
ATOM   11477 O  O   . THR D  1 56  ? 23.607  34.083  -45.833 1.00 31.19  ?  87   THR D O   1 
ATOM   11478 C  CB  . THR D  1 56  ? 26.279  33.336  -46.899 1.00 31.77  ?  87   THR D CB  1 
ATOM   11479 O  OG1 . THR D  1 56  ? 26.196  31.906  -46.872 1.00 30.19  ?  87   THR D OG1 1 
ATOM   11480 C  CG2 . THR D  1 56  ? 27.676  33.749  -47.328 1.00 34.72  ?  87   THR D CG2 1 
ATOM   11481 N  N   . SER D  1 57  ? 24.287  32.798  -44.106 1.00 31.82  ?  88   SER D N   1 
ATOM   11482 C  CA  . SER D  1 57  ? 22.942  32.470  -43.630 1.00 34.53  ?  88   SER D CA  1 
ATOM   11483 C  C   . SER D  1 57  ? 22.922  32.542  -42.097 1.00 29.31  ?  88   SER D C   1 
ATOM   11484 O  O   . SER D  1 57  ? 22.646  31.566  -41.400 1.00 27.99  ?  88   SER D O   1 
ATOM   11485 C  CB  . SER D  1 57  ? 22.489  31.094  -44.123 1.00 30.68  ?  88   SER D CB  1 
ATOM   11486 O  OG  . SER D  1 57  ? 22.015  31.134  -45.463 1.00 33.57  ?  88   SER D OG  1 
ATOM   11487 N  N   . ALA D  1 58  ? 23.204  33.733  -41.561 1.00 29.14  ?  89   ALA D N   1 
ATOM   11488 C  CA  . ALA D  1 58  ? 23.234  33.985  -40.120 1.00 31.14  ?  89   ALA D CA  1 
ATOM   11489 C  C   . ALA D  1 58  ? 21.909  34.580  -39.647 1.00 28.10  ?  89   ALA D C   1 
ATOM   11490 O  O   . ALA D  1 58  ? 21.431  35.563  -40.217 1.00 29.84  ?  89   ALA D O   1 
ATOM   11491 C  CB  . ALA D  1 58  ? 24.369  34.948  -39.768 1.00 30.63  ?  89   ALA D CB  1 
ATOM   11492 N  N   . TYR D  1 59  ? 21.339  34.018  -38.585 1.00 28.18  ?  90   TYR D N   1 
ATOM   11493 C  CA  . TYR D  1 59  ? 20.037  34.474  -38.102 1.00 30.29  ?  90   TYR D CA  1 
ATOM   11494 C  C   . TYR D  1 59  ? 20.092  34.896  -36.640 1.00 31.00  ?  90   TYR D C   1 
ATOM   11495 O  O   . TYR D  1 59  ? 20.842  34.327  -35.837 1.00 31.82  ?  90   TYR D O   1 
ATOM   11496 C  CB  . TYR D  1 59  ? 18.977  33.387  -38.248 1.00 28.24  ?  90   TYR D CB  1 
ATOM   11497 C  CG  . TYR D  1 59  ? 18.733  32.977  -39.669 1.00 31.02  ?  90   TYR D CG  1 
ATOM   11498 C  CD1 . TYR D  1 59  ? 19.484  31.958  -40.268 1.00 31.61  ?  90   TYR D CD1 1 
ATOM   11499 C  CD2 . TYR D  1 59  ? 17.745  33.600  -40.422 1.00 28.76  ?  90   TYR D CD2 1 
ATOM   11500 C  CE1 . TYR D  1 59  ? 19.250  31.579  -41.602 1.00 30.25  ?  90   TYR D CE1 1 
ATOM   11501 C  CE2 . TYR D  1 59  ? 17.512  33.241  -41.724 1.00 28.28  ?  90   TYR D CE2 1 
ATOM   11502 C  CZ  . TYR D  1 59  ? 18.259  32.227  -42.318 1.00 30.07  ?  90   TYR D CZ  1 
ATOM   11503 O  OH  . TYR D  1 59  ? 18.007  31.883  -43.630 1.00 30.59  ?  90   TYR D OH  1 
ATOM   11504 N  N   . VAL D  1 60  ? 19.288  35.906  -36.297 1.00 28.19  ?  91   VAL D N   1 
ATOM   11505 C  CA  . VAL D  1 60  ? 19.032  36.223  -34.893 1.00 29.03  ?  91   VAL D CA  1 
ATOM   11506 C  C   . VAL D  1 60  ? 17.735  35.527  -34.497 1.00 28.26  ?  91   VAL D C   1 
ATOM   11507 O  O   . VAL D  1 60  ? 16.973  35.062  -35.361 1.00 28.20  ?  91   VAL D O   1 
ATOM   11508 C  CB  . VAL D  1 60  ? 18.968  37.744  -34.632 1.00 28.45  ?  91   VAL D CB  1 
ATOM   11509 C  CG1 . VAL D  1 60  ? 20.382  38.359  -34.744 1.00 25.54  ?  91   VAL D CG1 1 
ATOM   11510 C  CG2 . VAL D  1 60  ? 18.007  38.424  -35.590 1.00 25.05  ?  91   VAL D CG2 1 
ATOM   11511 N  N   . ALA D  1 61  ? 17.485  35.437  -33.192 1.00 26.10  ?  92   ALA D N   1 
ATOM   11512 C  CA  . ALA D  1 61  ? 16.374  34.656  -32.662 1.00 30.33  ?  92   ALA D CA  1 
ATOM   11513 C  C   . ALA D  1 61  ? 15.035  35.386  -32.704 1.00 30.97  ?  92   ALA D C   1 
ATOM   11514 O  O   . ALA D  1 61  ? 13.991  34.749  -32.490 1.00 30.41  ?  92   ALA D O   1 
ATOM   11515 C  CB  . ALA D  1 61  ? 16.682  34.228  -31.223 1.00 30.41  ?  92   ALA D CB  1 
ATOM   11516 N  N   . HIS D  1 62  ? 15.031  36.694  -32.954 1.00 27.99  ?  93   HIS D N   1 
ATOM   11517 C  CA  . HIS D  1 62  ? 13.796  37.461  -33.051 1.00 26.46  ?  93   HIS D CA  1 
ATOM   11518 C  C   . HIS D  1 62  ? 14.061  38.655  -33.954 1.00 27.47  ?  93   HIS D C   1 
ATOM   11519 O  O   . HIS D  1 62  ? 15.184  39.176  -33.964 1.00 27.98  ?  93   HIS D O   1 
ATOM   11520 C  CB  . HIS D  1 62  ? 13.307  37.919  -31.666 1.00 27.19  ?  93   HIS D CB  1 
ATOM   11521 C  CG  . HIS D  1 62  ? 11.857  38.313  -31.620 1.00 29.25  ?  93   HIS D CG  1 
ATOM   11522 N  ND1 . HIS D  1 62  ? 10.831  37.391  -31.622 1.00 31.35  ?  93   HIS D ND1 1 
ATOM   11523 C  CD2 . HIS D  1 62  ? 11.266  39.531  -31.522 1.00 30.19  ?  93   HIS D CD2 1 
ATOM   11524 C  CE1 . HIS D  1 62  ? 9.669   38.024  -31.561 1.00 32.08  ?  93   HIS D CE1 1 
ATOM   11525 N  NE2 . HIS D  1 62  ? 9.903   39.325  -31.498 1.00 31.69  ?  93   HIS D NE2 1 
ATOM   11526 N  N   . PRO D  1 63  ? 13.062  39.098  -34.750 1.00 24.53  ?  94   PRO D N   1 
ATOM   11527 C  CA  . PRO D  1 63  ? 13.318  40.181  -35.713 1.00 24.91  ?  94   PRO D CA  1 
ATOM   11528 C  C   . PRO D  1 63  ? 13.249  41.606  -35.156 1.00 27.04  ?  94   PRO D C   1 
ATOM   11529 O  O   . PRO D  1 63  ? 13.101  42.550  -35.937 1.00 27.67  ?  94   PRO D O   1 
ATOM   11530 C  CB  . PRO D  1 63  ? 12.232  39.952  -36.786 1.00 24.94  ?  94   PRO D CB  1 
ATOM   11531 C  CG  . PRO D  1 63  ? 11.086  39.361  -36.009 1.00 24.66  ?  94   PRO D CG  1 
ATOM   11532 C  CD  . PRO D  1 63  ? 11.757  38.441  -34.998 1.00 25.66  ?  94   PRO D CD  1 
ATOM   11533 N  N   . PHE D  1 64  ? 13.459  41.768  -33.843 1.00 27.62  ?  95   PHE D N   1 
ATOM   11534 C  CA  . PHE D  1 64  ? 13.565  43.136  -33.242 1.00 29.22  ?  95   PHE D CA  1 
ATOM   11535 C  C   . PHE D  1 64  ? 14.408  43.108  -31.916 1.00 30.08  ?  95   PHE D C   1 
ATOM   11536 O  O   . PHE D  1 64  ? 14.433  42.047  -31.281 1.00 30.71  ?  95   PHE D O   1 
ATOM   11537 C  CB  . PHE D  1 64  ? 12.242  43.913  -33.177 1.00 26.94  ?  95   PHE D CB  1 
ATOM   11538 C  CG  . PHE D  1 64  ? 11.085  43.360  -32.361 1.00 29.01  ?  95   PHE D CG  1 
ATOM   11539 C  CD1 . PHE D  1 64  ? 11.066  43.478  -30.979 1.00 32.74  ?  95   PHE D CD1 1 
ATOM   11540 C  CD2 . PHE D  1 64  ? 9.990   42.781  -32.987 1.00 31.07  ?  95   PHE D CD2 1 
ATOM   11541 C  CE1 . PHE D  1 64  ? 9.998   42.998  -30.245 1.00 32.14  ?  95   PHE D CE1 1 
ATOM   11542 C  CE2 . PHE D  1 64  ? 8.924   42.305  -32.246 1.00 31.32  ?  95   PHE D CE2 1 
ATOM   11543 C  CZ  . PHE D  1 64  ? 8.932   42.413  -30.879 1.00 28.77  ?  95   PHE D CZ  1 
HETATM 11544 N  N   . OSE D  1 65  ? 15.006  44.238  -31.505 1.00 34.87  ?  96   OSE D N   1 
HETATM 11545 C  CA  . OSE D  1 65  ? 15.958  44.361  -30.352 1.00 31.10  ?  96   OSE D CA  1 
HETATM 11546 C  CB  . OSE D  1 65  ? 16.064  45.797  -29.942 1.00 41.41  ?  96   OSE D CB  1 
HETATM 11547 O  OG  . OSE D  1 65  ? 14.789  46.310  -30.070 1.00 41.77  ?  96   OSE D OG  1 
HETATM 11548 C  C   . OSE D  1 65  ? 15.688  43.561  -29.077 1.00 32.90  ?  96   OSE D C   1 
HETATM 11549 O  O   . OSE D  1 65  ? 16.468  42.630  -28.836 1.00 30.07  ?  96   OSE D O   1 
HETATM 11550 S  S   . OSE D  1 65  ? 14.664  47.312  -31.236 1.00 43.14  ?  96   OSE D S   1 
HETATM 11551 O  O1S . OSE D  1 65  ? 15.526  46.892  -32.307 1.00 44.22  ?  96   OSE D O1S 1 
HETATM 11552 O  O2S . OSE D  1 65  ? 13.261  47.295  -31.559 1.00 42.44  ?  96   OSE D O2S 1 
HETATM 11553 O  O3S . OSE D  1 65  ? 15.146  48.464  -30.517 1.00 45.77  ?  96   OSE D O3S 1 
ATOM   11554 N  N   . GLY D  1 66  ? 14.790  44.049  -28.207 1.00 35.19  ?  97   GLY D N   1 
ATOM   11555 C  CA  . GLY D  1 66  ? 14.575  43.412  -26.887 1.00 32.98  ?  97   GLY D CA  1 
ATOM   11556 C  C   . GLY D  1 66  ? 14.749  41.910  -26.933 1.00 29.08  ?  97   GLY D C   1 
ATOM   11557 O  O   . GLY D  1 66  ? 15.706  41.386  -26.326 1.00 31.92  ?  97   GLY D O   1 
ATOM   11558 N  N   . PRO D  1 67  ? 13.833  41.180  -27.599 1.00 32.28  ?  98   PRO D N   1 
ATOM   11559 C  CA  . PRO D  1 67  ? 13.908  39.714  -27.605 1.00 29.26  ?  98   PRO D CA  1 
ATOM   11560 C  C   . PRO D  1 67  ? 15.173  39.185  -28.249 1.00 30.04  ?  98   PRO D C   1 
ATOM   11561 O  O   . PRO D  1 67  ? 15.704  38.155  -27.812 1.00 29.00  ?  98   PRO D O   1 
ATOM   11562 C  CB  . PRO D  1 67  ? 12.656  39.313  -28.404 1.00 28.42  ?  98   PRO D CB  1 
ATOM   11563 C  CG  . PRO D  1 67  ? 11.742  40.475  -28.252 1.00 31.78  ?  98   PRO D CG  1 
ATOM   11564 C  CD  . PRO D  1 67  ? 12.615  41.666  -28.268 1.00 29.08  ?  98   PRO D CD  1 
ATOM   11565 N  N   . SER D  1 68  ? 15.672  39.846  -29.292 1.00 28.89  ?  99   SER D N   1 
ATOM   11566 C  CA  . SER D  1 68  ? 16.903  39.370  -29.909 1.00 27.05  ?  99   SER D CA  1 
ATOM   11567 C  C   . SER D  1 68  ? 18.073  39.469  -28.933 1.00 27.99  ?  99   SER D C   1 
ATOM   11568 O  O   . SER D  1 68  ? 18.876  38.531  -28.800 1.00 25.93  ?  99   SER D O   1 
ATOM   11569 C  CB  . SER D  1 68  ? 17.188  40.163  -31.180 1.00 27.57  ?  99   SER D CB  1 
ATOM   11570 O  OG  . SER D  1 68  ? 18.473  39.818  -31.700 1.00 28.79  ?  99   SER D OG  1 
ATOM   11571 N  N   . ARG D  1 69  ? 18.164  40.577  -28.204 1.00 27.37  ?  100  ARG D N   1 
ATOM   11572 C  CA  . ARG D  1 69  ? 19.282  40.724  -27.268 1.00 25.79  ?  100  ARG D CA  1 
ATOM   11573 C  C   . ARG D  1 69  ? 19.114  39.810  -26.061 1.00 29.43  ?  100  ARG D C   1 
ATOM   11574 O  O   . ARG D  1 69  ? 20.097  39.275  -25.533 1.00 29.63  ?  100  ARG D O   1 
ATOM   11575 C  CB  . ARG D  1 69  ? 19.398  42.187  -26.865 1.00 27.60  ?  100  ARG D CB  1 
ATOM   11576 C  CG  . ARG D  1 69  ? 19.808  43.057  -28.067 1.00 29.32  ?  100  ARG D CG  1 
ATOM   11577 C  CD  . ARG D  1 69  ? 19.383  44.496  -27.915 1.00 29.05  ?  100  ARG D CD  1 
ATOM   11578 N  NE  . ARG D  1 69  ? 19.669  45.234  -29.136 1.00 30.35  ?  100  ARG D NE  1 
ATOM   11579 C  CZ  . ARG D  1 69  ? 20.846  45.767  -29.435 1.00 30.50  ?  100  ARG D CZ  1 
ATOM   11580 N  NH1 . ARG D  1 69  ? 21.849  45.745  -28.577 1.00 25.14  ?  100  ARG D NH1 1 
ATOM   11581 N  NH2 . ARG D  1 69  ? 21.013  46.350  -30.620 1.00 27.90  ?  100  ARG D NH2 1 
ATOM   11582 N  N   . SER D  1 70  ? 17.873  39.620  -25.616 1.00 25.46  ?  101  SER D N   1 
ATOM   11583 C  CA  . SER D  1 70  ? 17.585  38.625  -24.587 1.00 29.04  ?  101  SER D CA  1 
ATOM   11584 C  C   . SER D  1 70  ? 18.100  37.247  -24.997 1.00 32.49  ?  101  SER D C   1 
ATOM   11585 O  O   . SER D  1 70  ? 18.733  36.539  -24.201 1.00 29.77  ?  101  SER D O   1 
ATOM   11586 C  CB  . SER D  1 70  ? 16.073  38.585  -24.328 1.00 30.24  ?  101  SER D CB  1 
ATOM   11587 O  OG  . SER D  1 70  ? 15.752  37.533  -23.439 1.00 36.46  ?  101  SER D OG  1 
ATOM   11588 N  N   . ALA D  1 71  ? 17.842  36.854  -26.251 1.00 27.94  ?  102  ALA D N   1 
ATOM   11589 C  CA  . ALA D  1 71  ? 18.312  35.557  -26.727 1.00 30.99  ?  102  ALA D CA  1 
ATOM   11590 C  C   . ALA D  1 71  ? 19.835  35.478  -26.799 1.00 29.89  ?  102  ALA D C   1 
ATOM   11591 O  O   . ALA D  1 71  ? 20.414  34.415  -26.559 1.00 30.26  ?  102  ALA D O   1 
ATOM   11592 C  CB  . ALA D  1 71  ? 17.714  35.244  -28.093 1.00 25.27  ?  102  ALA D CB  1 
ATOM   11593 N  N   . ILE D  1 72  ? 20.505  36.554  -27.201 1.00 30.92  ?  103  ILE D N   1 
ATOM   11594 C  CA  . ILE D  1 72  ? 21.961  36.483  -27.288 1.00 31.96  ?  103  ILE D CA  1 
ATOM   11595 C  C   . ILE D  1 72  ? 22.549  36.208  -25.914 1.00 30.27  ?  103  ILE D C   1 
ATOM   11596 O  O   . ILE D  1 72  ? 23.421  35.341  -25.751 1.00 31.78  ?  103  ILE D O   1 
ATOM   11597 C  CB  . ILE D  1 72  ? 22.546  37.766  -27.908 1.00 27.70  ?  103  ILE D CB  1 
ATOM   11598 C  CG1 . ILE D  1 72  ? 22.250  37.812  -29.413 1.00 26.21  ?  103  ILE D CG1 1 
ATOM   11599 C  CG2 . ILE D  1 72  ? 24.072  37.858  -27.648 1.00 30.77  ?  103  ILE D CG2 1 
ATOM   11600 C  CD1 . ILE D  1 72  ? 22.273  39.202  -30.026 1.00 28.44  ?  103  ILE D CD1 1 
ATOM   11601 N  N   . LEU D  1 73  ? 22.077  36.929  -24.897 1.00 31.23  ?  104  LEU D N   1 
ATOM   11602 C  CA  . LEU D  1 73  ? 22.750  36.817  -23.603 1.00 31.53  ?  104  LEU D CA  1 
ATOM   11603 C  C   . LEU D  1 73  ? 22.261  35.611  -22.802 1.00 31.56  ?  104  LEU D C   1 
ATOM   11604 O  O   . LEU D  1 73  ? 23.046  35.022  -22.051 1.00 35.16  ?  104  LEU D O   1 
ATOM   11605 C  CB  . LEU D  1 73  ? 22.581  38.110  -22.804 1.00 32.54  ?  104  LEU D CB  1 
ATOM   11606 C  CG  . LEU D  1 73  ? 23.592  39.160  -23.263 1.00 37.06  ?  104  LEU D CG  1 
ATOM   11607 C  CD1 . LEU D  1 73  ? 23.327  40.487  -22.635 1.00 39.90  ?  104  LEU D CD1 1 
ATOM   11608 C  CD2 . LEU D  1 73  ? 24.973  38.694  -22.845 1.00 33.84  ?  104  LEU D CD2 1 
ATOM   11609 N  N   . THR D  1 74  ? 21.001  35.208  -22.966 1.00 33.12  ?  105  THR D N   1 
ATOM   11610 C  CA  . THR D  1 74  ? 20.496  34.014  -22.290 1.00 33.85  ?  105  THR D CA  1 
ATOM   11611 C  C   . THR D  1 74  ? 20.745  32.719  -23.059 1.00 35.40  ?  105  THR D C   1 
ATOM   11612 O  O   . THR D  1 74  ? 20.734  31.645  -22.448 1.00 32.23  ?  105  THR D O   1 
ATOM   11613 C  CB  . THR D  1 74  ? 18.991  34.116  -22.046 1.00 36.25  ?  105  THR D CB  1 
ATOM   11614 O  OG1 . THR D  1 74  ? 18.303  34.068  -23.307 1.00 31.69  ?  105  THR D OG1 1 
ATOM   11615 C  CG2 . THR D  1 74  ? 18.641  35.388  -21.274 1.00 33.59  ?  105  THR D CG2 1 
ATOM   11616 N  N   . GLY D  1 75  ? 20.944  32.780  -24.377 1.00 33.97  ?  106  GLY D N   1 
ATOM   11617 C  CA  . GLY D  1 75  ? 21.087  31.557  -25.145 1.00 32.18  ?  106  GLY D CA  1 
ATOM   11618 C  C   . GLY D  1 75  ? 19.791  30.810  -25.396 1.00 31.61  ?  106  GLY D C   1 
ATOM   11619 O  O   . GLY D  1 75  ? 19.837  29.648  -25.815 1.00 32.42  ?  106  GLY D O   1 
ATOM   11620 N  N   . ARG D  1 76  ? 18.642  31.434  -25.150 1.00 31.49  ?  107  ARG D N   1 
ATOM   11621 C  CA  . ARG D  1 76  ? 17.343  30.803  -25.331 1.00 31.26  ?  107  ARG D CA  1 
ATOM   11622 C  C   . ARG D  1 76  ? 16.442  31.695  -26.177 1.00 33.14  ?  107  ARG D C   1 
ATOM   11623 O  O   . ARG D  1 76  ? 16.514  32.929  -26.102 1.00 29.74  ?  107  ARG D O   1 
ATOM   11624 C  CB  . ARG D  1 76  ? 16.663  30.520  -23.980 1.00 32.97  ?  107  ARG D CB  1 
ATOM   11625 C  CG  . ARG D  1 76  ? 17.505  29.622  -23.061 1.00 38.60  ?  107  ARG D CG  1 
ATOM   11626 C  CD  . ARG D  1 76  ? 16.752  29.217  -21.826 1.00 38.22  ?  107  ARG D CD  1 
ATOM   11627 N  NE  . ARG D  1 76  ? 15.728  28.218  -22.100 1.00 46.18  ?  107  ARG D NE  1 
ATOM   11628 C  CZ  . ARG D  1 76  ? 14.790  27.863  -21.231 1.00 47.52  ?  107  ARG D CZ  1 
ATOM   11629 N  NH1 . ARG D  1 76  ? 14.734  28.396  -20.015 1.00 45.11  ?  107  ARG D NH1 1 
ATOM   11630 N  NH2 . ARG D  1 76  ? 13.892  26.948  -21.586 1.00 43.80  ?  107  ARG D NH2 1 
ATOM   11631 N  N   . TYR D  1 77  ? 15.560  31.060  -26.951 1.00 33.18  ?  108  TYR D N   1 
ATOM   11632 C  CA  . TYR D  1 77  ? 14.541  31.816  -27.668 1.00 31.07  ?  108  TYR D CA  1 
ATOM   11633 C  C   . TYR D  1 77  ? 13.731  32.633  -26.664 1.00 30.39  ?  108  TYR D C   1 
ATOM   11634 O  O   . TYR D  1 77  ? 13.457  32.158  -25.555 1.00 32.81  ?  108  TYR D O   1 
ATOM   11635 C  CB  . TYR D  1 77  ? 13.598  30.892  -28.458 1.00 28.85  ?  108  TYR D CB  1 
ATOM   11636 C  CG  . TYR D  1 77  ? 14.125  30.430  -29.795 1.00 28.47  ?  108  TYR D CG  1 
ATOM   11637 C  CD1 . TYR D  1 77  ? 14.089  31.264  -30.916 1.00 31.59  ?  108  TYR D CD1 1 
ATOM   11638 C  CD2 . TYR D  1 77  ? 14.615  29.143  -29.948 1.00 31.24  ?  108  TYR D CD2 1 
ATOM   11639 C  CE1 . TYR D  1 77  ? 14.565  30.832  -32.149 1.00 29.32  ?  108  TYR D CE1 1 
ATOM   11640 C  CE2 . TYR D  1 77  ? 15.100  28.705  -31.158 1.00 31.92  ?  108  TYR D CE2 1 
ATOM   11641 C  CZ  . TYR D  1 77  ? 15.070  29.551  -32.255 1.00 30.68  ?  108  TYR D CZ  1 
ATOM   11642 O  OH  . TYR D  1 77  ? 15.560  29.093  -33.439 1.00 31.05  ?  108  TYR D OH  1 
ATOM   11643 N  N   . PRO D  1 78  ? 13.326  33.857  -27.016 1.00 32.17  ?  109  PRO D N   1 
ATOM   11644 C  CA  . PRO D  1 78  ? 12.609  34.692  -26.044 1.00 32.80  ?  109  PRO D CA  1 
ATOM   11645 C  C   . PRO D  1 78  ? 11.246  34.145  -25.681 1.00 33.83  ?  109  PRO D C   1 
ATOM   11646 O  O   . PRO D  1 78  ? 10.700  34.519  -24.636 1.00 34.47  ?  109  PRO D O   1 
ATOM   11647 C  CB  . PRO D  1 78  ? 12.496  36.041  -26.761 1.00 31.81  ?  109  PRO D CB  1 
ATOM   11648 C  CG  . PRO D  1 78  ? 12.534  35.684  -28.191 1.00 33.55  ?  109  PRO D CG  1 
ATOM   11649 C  CD  . PRO D  1 78  ? 13.516  34.558  -28.293 1.00 26.55  ?  109  PRO D CD  1 
ATOM   11650 N  N   . HIS D  1 79  ? 10.676  33.275  -26.512 1.00 31.88  ?  110  HIS D N   1 
ATOM   11651 C  CA  . HIS D  1 79  ? 9.389   32.668  -26.203 1.00 34.07  ?  110  HIS D CA  1 
ATOM   11652 C  C   . HIS D  1 79  ? 9.497   31.669  -25.062 1.00 37.72  ?  110  HIS D C   1 
ATOM   11653 O  O   . HIS D  1 79  ? 8.468   31.247  -24.515 1.00 34.61  ?  110  HIS D O   1 
ATOM   11654 C  CB  . HIS D  1 79  ? 8.831   31.993  -27.459 1.00 35.49  ?  110  HIS D CB  1 
ATOM   11655 C  CG  . HIS D  1 79  ? 9.157   32.724  -28.725 1.00 33.52  ?  110  HIS D CG  1 
ATOM   11656 N  ND1 . HIS D  1 79  ? 10.439  32.806  -29.231 1.00 31.75  ?  110  HIS D ND1 1 
ATOM   11657 C  CD2 . HIS D  1 79  ? 8.367   33.401  -29.588 1.00 31.18  ?  110  HIS D CD2 1 
ATOM   11658 C  CE1 . HIS D  1 79  ? 10.424  33.521  -30.341 1.00 33.65  ?  110  HIS D CE1 1 
ATOM   11659 N  NE2 . HIS D  1 79  ? 9.175   33.882  -30.589 1.00 30.61  ?  110  HIS D NE2 1 
ATOM   11660 N  N   . LEU D  1 80  ? 10.719  31.285  -24.704 1.00 36.46  ?  111  LEU D N   1 
ATOM   11661 C  CA  . LEU D  1 80  ? 10.975  30.370  -23.604 1.00 37.15  ?  111  LEU D CA  1 
ATOM   11662 C  C   . LEU D  1 80  ? 11.294  31.096  -22.303 1.00 39.36  ?  111  LEU D C   1 
ATOM   11663 O  O   . LEU D  1 80  ? 11.199  30.490  -21.232 1.00 39.76  ?  111  LEU D O   1 
ATOM   11664 C  CB  . LEU D  1 80  ? 12.131  29.429  -23.971 1.00 34.50  ?  111  LEU D CB  1 
ATOM   11665 C  CG  . LEU D  1 80  ? 11.745  28.139  -24.720 1.00 42.10  ?  111  LEU D CG  1 
ATOM   11666 C  CD1 . LEU D  1 80  ? 10.810  28.416  -25.877 1.00 43.51  ?  111  LEU D CD1 1 
ATOM   11667 C  CD2 . LEU D  1 80  ? 12.972  27.417  -25.240 1.00 48.60  ?  111  LEU D CD2 1 
ATOM   11668 N  N   . THR D  1 81  ? 11.646  32.380  -22.368 1.00 36.22  ?  112  THR D N   1 
ATOM   11669 C  CA  . THR D  1 81  ? 12.028  33.155  -21.196 1.00 36.33  ?  112  THR D CA  1 
ATOM   11670 C  C   . THR D  1 81  ? 11.030  34.252  -20.879 1.00 36.76  ?  112  THR D C   1 
ATOM   11671 O  O   . THR D  1 81  ? 11.255  35.017  -19.935 1.00 37.60  ?  112  THR D O   1 
ATOM   11672 C  CB  . THR D  1 81  ? 13.410  33.788  -21.393 1.00 37.00  ?  112  THR D CB  1 
ATOM   11673 O  OG1 . THR D  1 81  ? 13.389  34.621  -22.559 1.00 36.34  ?  112  THR D OG1 1 
ATOM   11674 C  CG2 . THR D  1 81  ? 14.483  32.727  -21.543 1.00 36.56  ?  112  THR D CG2 1 
ATOM   11675 N  N   . GLY D  1 82  ? 9.958   34.360  -21.658 1.00 33.64  ?  113  GLY D N   1 
ATOM   11676 C  CA  . GLY D  1 82  ? 8.927   35.354  -21.433 1.00 36.32  ?  113  GLY D CA  1 
ATOM   11677 C  C   . GLY D  1 82  ? 9.238   36.746  -21.933 1.00 37.90  ?  113  GLY D C   1 
ATOM   11678 O  O   . GLY D  1 82  ? 8.555   37.704  -21.541 1.00 33.85  ?  113  GLY D O   1 
ATOM   11679 N  N   . THR D  1 83  ? 10.230  36.895  -22.814 1.00 36.50  ?  114  THR D N   1 
ATOM   11680 C  CA  . THR D  1 83  ? 10.746  38.210  -23.174 1.00 35.06  ?  114  THR D CA  1 
ATOM   11681 C  C   . THR D  1 83  ? 10.613  38.482  -24.671 1.00 34.93  ?  114  THR D C   1 
ATOM   11682 O  O   . THR D  1 83  ? 11.475  39.139  -25.266 1.00 35.06  ?  114  THR D O   1 
ATOM   11683 C  CB  . THR D  1 83  ? 12.201  38.349  -22.727 1.00 33.35  ?  114  THR D CB  1 
ATOM   11684 O  OG1 . THR D  1 83  ? 12.994  37.313  -23.321 1.00 32.81  ?  114  THR D OG1 1 
ATOM   11685 C  CG2 . THR D  1 83  ? 12.307  38.236  -21.203 1.00 37.01  ?  114  THR D CG2 1 
ATOM   11686 N  N   . ALA D  1 84  ? 9.539   37.993  -25.293 1.00 30.57  ?  115  ALA D N   1 
ATOM   11687 C  CA  . ALA D  1 84  ? 9.363   38.131  -26.741 1.00 34.40  ?  115  ALA D CA  1 
ATOM   11688 C  C   . ALA D  1 84  ? 8.774   39.477  -27.158 1.00 31.14  ?  115  ALA D C   1 
ATOM   11689 O  O   . ALA D  1 84  ? 8.600   39.707  -28.361 1.00 31.88  ?  115  ALA D O   1 
ATOM   11690 C  CB  . ALA D  1 84  ? 8.491   36.994  -27.293 1.00 33.92  ?  115  ALA D CB  1 
ATOM   11691 N  N   . TYR D  1 85  ? 8.500   40.378  -26.215 1.00 30.54  ?  116  TYR D N   1 
ATOM   11692 C  CA  . TYR D  1 85  ? 8.089   41.748  -26.501 1.00 30.83  ?  116  TYR D CA  1 
ATOM   11693 C  C   . TYR D  1 85  ? 9.138   42.717  -25.968 1.00 32.23  ?  116  TYR D C   1 
ATOM   11694 O  O   . TYR D  1 85  ? 9.812   42.432  -24.971 1.00 29.75  ?  116  TYR D O   1 
ATOM   11695 C  CB  . TYR D  1 85  ? 6.732   42.096  -25.841 1.00 33.74  ?  116  TYR D CB  1 
ATOM   11696 C  CG  . TYR D  1 85  ? 5.470   41.519  -26.506 1.00 34.79  ?  116  TYR D CG  1 
ATOM   11697 C  CD1 . TYR D  1 85  ? 4.845   42.171  -27.560 1.00 30.96  ?  116  TYR D CD1 1 
ATOM   11698 C  CD2 . TYR D  1 85  ? 4.896   40.342  -26.043 1.00 33.82  ?  116  TYR D CD2 1 
ATOM   11699 C  CE1 . TYR D  1 85  ? 3.679   41.642  -28.157 1.00 32.29  ?  116  TYR D CE1 1 
ATOM   11700 C  CE2 . TYR D  1 85  ? 3.747   39.819  -26.623 1.00 33.82  ?  116  TYR D CE2 1 
ATOM   11701 C  CZ  . TYR D  1 85  ? 3.145   40.461  -27.665 1.00 32.73  ?  116  TYR D CZ  1 
ATOM   11702 O  OH  . TYR D  1 85  ? 2.011   39.908  -28.205 1.00 30.77  ?  116  TYR D OH  1 
ATOM   11703 N  N   . ASN D  1 86  ? 9.232   43.873  -26.626 1.00 29.75  ?  117  ASN D N   1 
ATOM   11704 C  CA  . ASN D  1 86  ? 10.166  44.895  -26.111 1.00 33.67  ?  117  ASN D CA  1 
ATOM   11705 C  C   . ASN D  1 86  ? 9.634   45.574  -24.847 1.00 29.49  ?  117  ASN D C   1 
ATOM   11706 O  O   . ASN D  1 86  ? 8.407   45.670  -24.704 1.00 32.53  ?  117  ASN D O   1 
ATOM   11707 C  CB  . ASN D  1 86  ? 10.333  46.060  -27.069 1.00 29.29  ?  117  ASN D CB  1 
ATOM   11708 C  CG  . ASN D  1 86  ? 11.405  45.885  -28.117 1.00 32.74  ?  117  ASN D CG  1 
ATOM   11709 O  OD1 . ASN D  1 86  ? 12.073  44.850  -28.173 1.00 31.68  ?  117  ASN D OD1 1 
ATOM   11710 N  ND2 . ASN D  1 86  ? 11.578  46.894  -28.957 1.00 32.76  ?  117  ASN D ND2 1 
ATOM   11711 N  N   . LEU D  1 87  ? 10.510  45.876  -23.910 1.00 32.07  ?  118  LEU D N   1 
ATOM   11712 C  CA  . LEU D  1 87  ? 10.169  46.795  -22.833 1.00 32.16  ?  118  LEU D CA  1 
ATOM   11713 C  C   . LEU D  1 87  ? 9.767   48.134  -23.428 1.00 31.64  ?  118  LEU D C   1 
ATOM   11714 O  O   . LEU D  1 87  ? 10.293  48.562  -24.456 1.00 33.25  ?  118  LEU D O   1 
ATOM   11715 C  CB  . LEU D  1 87  ? 11.362  47.003  -21.894 1.00 31.11  ?  118  LEU D CB  1 
ATOM   11716 C  CG  . LEU D  1 87  ? 11.842  45.770  -21.153 1.00 34.37  ?  118  LEU D CG  1 
ATOM   11717 C  CD1 . LEU D  1 87  ? 13.252  46.013  -20.588 1.00 33.00  ?  118  LEU D CD1 1 
ATOM   11718 C  CD2 . LEU D  1 87  ? 10.844  45.430  -20.060 1.00 36.61  ?  118  LEU D CD2 1 
ATOM   11719 N  N   . PHE D  1 88  ? 8.836   48.807  -22.772 1.00 31.65  ?  119  PHE D N   1 
ATOM   11720 C  CA  . PHE D  1 88  ? 8.423   50.102  -23.277 1.00 35.58  ?  119  PHE D CA  1 
ATOM   11721 C  C   . PHE D  1 88  ? 9.459   51.173  -22.918 1.00 35.21  ?  119  PHE D C   1 
ATOM   11722 O  O   . PHE D  1 88  ? 10.306  50.995  -22.033 1.00 32.18  ?  119  PHE D O   1 
ATOM   11723 C  CB  . PHE D  1 88  ? 7.032   50.462  -22.727 1.00 35.62  ?  119  PHE D CB  1 
ATOM   11724 C  CG  . PHE D  1 88  ? 6.264   51.433  -23.586 1.00 36.11  ?  119  PHE D CG  1 
ATOM   11725 C  CD1 . PHE D  1 88  ? 5.617   51.006  -24.737 1.00 36.11  ?  119  PHE D CD1 1 
ATOM   11726 C  CD2 . PHE D  1 88  ? 6.155   52.767  -23.220 1.00 34.96  ?  119  PHE D CD2 1 
ATOM   11727 C  CE1 . PHE D  1 88  ? 4.901   51.902  -25.529 1.00 37.99  ?  119  PHE D CE1 1 
ATOM   11728 C  CE2 . PHE D  1 88  ? 5.443   53.665  -24.004 1.00 37.85  ?  119  PHE D CE2 1 
ATOM   11729 C  CZ  . PHE D  1 88  ? 4.814   53.231  -25.160 1.00 39.94  ?  119  PHE D CZ  1 
ATOM   11730 N  N   . HIS D  1 89  ? 9.391   52.293  -23.639 1.00 34.59  ?  120  HIS D N   1 
ATOM   11731 C  CA  . HIS D  1 89  ? 10.166  53.470  -23.274 1.00 36.22  ?  120  HIS D CA  1 
ATOM   11732 C  C   . HIS D  1 89  ? 10.012  53.742  -21.785 1.00 39.79  ?  120  HIS D C   1 
ATOM   11733 O  O   . HIS D  1 89  ? 8.903   53.665  -21.244 1.00 38.47  ?  120  HIS D O   1 
ATOM   11734 C  CB  . HIS D  1 89  ? 9.691   54.680  -24.088 1.00 40.68  ?  120  HIS D CB  1 
ATOM   11735 C  CG  . HIS D  1 89  ? 9.566   54.409  -25.558 1.00 44.70  ?  120  HIS D CG  1 
ATOM   11736 N  ND1 . HIS D  1 89  ? 10.639  54.481  -26.425 1.00 47.08  ?  120  HIS D ND1 1 
ATOM   11737 C  CD2 . HIS D  1 89  ? 8.494   54.065  -26.316 1.00 46.01  ?  120  HIS D CD2 1 
ATOM   11738 C  CE1 . HIS D  1 89  ? 10.234  54.195  -27.651 1.00 46.40  ?  120  HIS D CE1 1 
ATOM   11739 N  NE2 . HIS D  1 89  ? 8.936   53.942  -27.614 1.00 48.88  ?  120  HIS D NE2 1 
ATOM   11740 N  N   . ASN D  1 90  ? 11.133  54.012  -21.117 1.00 33.06  ?  121  ASN D N   1 
ATOM   11741 C  CA  . ASN D  1 90  ? 11.120  54.413  -19.713 1.00 39.79  ?  121  ASN D CA  1 
ATOM   11742 C  C   . ASN D  1 90  ? 10.463  53.356  -18.832 1.00 41.57  ?  121  ASN D C   1 
ATOM   11743 O  O   . ASN D  1 90  ? 9.700   53.676  -17.918 1.00 41.25  ?  121  ASN D O   1 
ATOM   11744 C  CB  . ASN D  1 90  ? 10.439  55.774  -19.546 1.00 38.33  ?  121  ASN D CB  1 
ATOM   11745 C  CG  . ASN D  1 90  ? 11.239  56.887  -20.182 1.00 42.49  ?  121  ASN D CG  1 
ATOM   11746 O  OD1 . ASN D  1 90  ? 11.374  56.937  -21.398 1.00 43.36  ?  121  ASN D OD1 1 
ATOM   11747 N  ND2 . ASN D  1 90  ? 11.824  57.761  -19.352 1.00 45.06  ?  121  ASN D ND2 1 
ATOM   11748 N  N   . SER D  1 91  ? 10.760  52.085  -19.105 1.00 37.26  ?  122  SER D N   1 
ATOM   11749 C  CA  . SER D  1 91  ? 10.167  51.012  -18.327 1.00 36.97  ?  122  SER D CA  1 
ATOM   11750 C  C   . SER D  1 91  ? 10.663  51.079  -16.879 1.00 39.34  ?  122  SER D C   1 
ATOM   11751 O  O   . SER D  1 91  ? 11.700  51.673  -16.575 1.00 40.71  ?  122  SER D O   1 
ATOM   11752 C  CB  . SER D  1 91  ? 10.487  49.658  -18.958 1.00 33.53  ?  122  SER D CB  1 
ATOM   11753 O  OG  . SER D  1 91  ? 11.870  49.374  -18.858 1.00 36.80  ?  122  SER D OG  1 
ATOM   11754 N  N   . SER D  1 92  ? 9.905   50.453  -15.982 1.00 40.00  ?  123  SER D N   1 
ATOM   11755 C  CA  . SER D  1 92  ? 10.066  50.714  -14.561 1.00 41.42  ?  123  SER D CA  1 
ATOM   11756 C  C   . SER D  1 92  ? 11.466  50.384  -14.070 1.00 43.86  ?  123  SER D C   1 
ATOM   11757 O  O   . SER D  1 92  ? 12.024  49.327  -14.380 1.00 40.60  ?  123  SER D O   1 
ATOM   11758 C  CB  . SER D  1 92  ? 9.065   49.909  -13.745 1.00 44.19  ?  123  SER D CB  1 
ATOM   11759 O  OG  . SER D  1 92  ? 9.537   49.827  -12.405 1.00 48.73  ?  123  SER D OG  1 
ATOM   11760 N  N   . GLU D  1 93  ? 12.014  51.284  -13.259 1.00 40.49  ?  124  GLU D N   1 
ATOM   11761 C  CA  . GLU D  1 93  ? 13.319  51.084  -12.648 1.00 43.05  ?  124  GLU D CA  1 
ATOM   11762 C  C   . GLU D  1 93  ? 13.232  50.512  -11.233 1.00 44.28  ?  124  GLU D C   1 
ATOM   11763 O  O   . GLU D  1 93  ? 14.248  50.470  -10.530 1.00 37.03  ?  124  GLU D O   1 
ATOM   11764 C  CB  . GLU D  1 93  ? 14.098  52.401  -12.666 1.00 42.52  ?  124  GLU D CB  1 
ATOM   11765 C  CG  . GLU D  1 93  ? 13.685  53.283  -13.853 1.00 48.42  ?  124  GLU D CG  1 
ATOM   11766 C  CD  . GLU D  1 93  ? 14.597  54.475  -14.068 1.00 53.45  ?  124  GLU D CD  1 
ATOM   11767 O  OE1 . GLU D  1 93  ? 15.206  54.937  -13.080 1.00 52.80  ?  124  GLU D OE1 1 
ATOM   11768 O  OE2 . GLU D  1 93  ? 14.714  54.942  -15.225 1.00 54.57  -1 124  GLU D OE2 1 
ATOM   11769 N  N   . ASP D  1 94  ? 12.062  50.024  -10.823 1.00 40.05  ?  125  ASP D N   1 
ATOM   11770 C  CA  . ASP D  1 94  ? 11.868  49.428  -9.508  1.00 46.06  ?  125  ASP D CA  1 
ATOM   11771 C  C   . ASP D  1 94  ? 11.919  47.909  -9.625  1.00 45.45  ?  125  ASP D C   1 
ATOM   11772 O  O   . ASP D  1 94  ? 11.162  47.324  -10.407 1.00 44.50  ?  125  ASP D O   1 
ATOM   11773 C  CB  . ASP D  1 94  ? 10.519  49.863  -8.926  1.00 49.21  ?  125  ASP D CB  1 
ATOM   11774 C  CG  . ASP D  1 94  ? 10.513  51.323  -8.473  1.00 59.95  ?  125  ASP D CG  1 
ATOM   11775 O  OD1 . ASP D  1 94  ? 11.607  51.921  -8.314  1.00 60.45  -1 125  ASP D OD1 1 
ATOM   11776 O  OD2 . ASP D  1 94  ? 9.405   51.888  -8.318  1.00 64.60  ?  125  ASP D OD2 1 
ATOM   11777 N  N   . ASP D  1 95  ? 12.797  47.270  -8.836  1.00 45.16  ?  126  ASP D N   1 
ATOM   11778 C  CA  . ASP D  1 95  ? 12.891  45.807  -8.837  1.00 45.00  ?  126  ASP D CA  1 
ATOM   11779 C  C   . ASP D  1 95  ? 11.531  45.142  -8.672  1.00 47.85  ?  126  ASP D C   1 
ATOM   11780 O  O   . ASP D  1 95  ? 11.316  44.036  -9.183  1.00 48.33  ?  126  ASP D O   1 
ATOM   11781 C  CB  . ASP D  1 95  ? 13.830  45.304  -7.721  1.00 41.69  ?  126  ASP D CB  1 
ATOM   11782 C  CG  . ASP D  1 95  ? 15.305  45.457  -8.065  1.00 47.09  ?  126  ASP D CG  1 
ATOM   11783 O  OD1 . ASP D  1 95  ? 15.601  45.864  -9.211  1.00 45.66  -1 126  ASP D OD1 1 
ATOM   11784 O  OD2 . ASP D  1 95  ? 16.178  45.156  -7.197  1.00 44.73  ?  126  ASP D OD2 1 
ATOM   11785 N  N   . LYS D  1 96  ? 10.603  45.791  -7.961  1.00 49.63  ?  127  LYS D N   1 
ATOM   11786 C  CA  . LYS D  1 96  ? 9.316   45.167  -7.659  1.00 51.61  ?  127  LYS D CA  1 
ATOM   11787 C  C   . LYS D  1 96  ? 8.483   44.923  -8.913  1.00 49.37  ?  127  LYS D C   1 
ATOM   11788 O  O   . LYS D  1 96  ? 7.643   44.016  -8.929  1.00 47.06  ?  127  LYS D O   1 
ATOM   11789 C  CB  . LYS D  1 96  ? 8.528   46.032  -6.674  1.00 46.00  ?  127  LYS D CB  1 
ATOM   11790 N  N   . ASP D  1 97  ? 8.682   45.713  -9.964  1.00 47.73  ?  128  ASP D N   1 
ATOM   11791 C  CA  . ASP D  1 97  ? 7.860   45.571  -11.157 1.00 48.46  ?  128  ASP D CA  1 
ATOM   11792 C  C   . ASP D  1 97  ? 8.383   44.518  -12.134 1.00 50.66  ?  128  ASP D C   1 
ATOM   11793 O  O   . ASP D  1 97  ? 7.665   44.169  -13.083 1.00 47.27  ?  128  ASP D O   1 
ATOM   11794 C  CB  . ASP D  1 97  ? 7.717   46.927  -11.857 1.00 47.56  ?  128  ASP D CB  1 
ATOM   11795 C  CG  . ASP D  1 97  ? 6.961   47.941  -11.008 1.00 51.39  ?  128  ASP D CG  1 
ATOM   11796 O  OD1 . ASP D  1 97  ? 5.895   47.590  -10.461 1.00 52.04  ?  128  ASP D OD1 1 
ATOM   11797 O  OD2 . ASP D  1 97  ? 7.428   49.088  -10.882 1.00 50.78  -1 128  ASP D OD2 1 
ATOM   11798 N  N   . ASN D  1 98  ? 9.604   44.006  -11.924 1.00 43.91  ?  129  ASN D N   1 
ATOM   11799 C  CA  . ASN D  1 98  ? 10.139  42.874  -12.696 1.00 45.98  ?  129  ASN D CA  1 
ATOM   11800 C  C   . ASN D  1 98  ? 10.111  43.122  -14.207 1.00 42.87  ?  129  ASN D C   1 
ATOM   11801 O  O   . ASN D  1 98  ? 9.865   42.211  -15.002 1.00 42.37  ?  129  ASN D O   1 
ATOM   11802 C  CB  . ASN D  1 98  ? 9.399   41.581  -12.349 1.00 44.64  ?  129  ASN D CB  1 
ATOM   11803 C  CG  . ASN D  1 98  ? 9.890   40.963  -11.054 1.00 47.41  ?  129  ASN D CG  1 
ATOM   11804 O  OD1 . ASN D  1 98  ? 11.085  40.752  -10.868 1.00 52.64  ?  129  ASN D OD1 1 
ATOM   11805 N  ND2 . ASN D  1 98  ? 8.967   40.685  -10.146 1.00 53.69  ?  129  ASN D ND2 1 
ATOM   11806 N  N   . MET D  1 99  ? 10.402  44.356  -14.618 1.00 41.80  ?  130  MET D N   1 
ATOM   11807 C  CA  . MET D  1 99  ? 10.454  44.700  -16.040 1.00 38.50  ?  130  MET D CA  1 
ATOM   11808 C  C   . MET D  1 99  ? 11.891  44.520  -16.545 1.00 38.29  ?  130  MET D C   1 
ATOM   11809 O  O   . MET D  1 99  ? 12.657  45.472  -16.724 1.00 33.77  ?  130  MET D O   1 
ATOM   11810 C  CB  . MET D  1 99  ? 9.945   46.116  -16.257 1.00 35.69  ?  130  MET D CB  1 
ATOM   11811 C  CG  . MET D  1 99  ? 8.434   46.228  -16.079 1.00 40.38  ?  130  MET D CG  1 
ATOM   11812 S  SD  . MET D  1 99  ? 7.565   45.677  -17.548 1.00 45.14  ?  130  MET D SD  1 
ATOM   11813 C  CE  . MET D  1 99  ? 5.856   45.744  -16.989 1.00 39.95  ?  130  MET D CE  1 
ATOM   11814 N  N   . GLY D  1 100 ? 12.248  43.263  -16.788 1.00 36.14  ?  131  GLY D N   1 
ATOM   11815 C  CA  . GLY D  1 100 ? 13.569  42.916  -17.292 1.00 32.80  ?  131  GLY D CA  1 
ATOM   11816 C  C   . GLY D  1 100 ? 13.661  41.415  -17.461 1.00 36.02  ?  131  GLY D C   1 
ATOM   11817 O  O   . GLY D  1 100 ? 12.760  40.664  -17.067 1.00 36.38  ?  131  GLY D O   1 
ATOM   11818 N  N   . VAL D  1 101 ? 14.761  40.984  -18.074 1.00 29.81  ?  132  VAL D N   1 
ATOM   11819 C  CA  . VAL D  1 101 ? 14.940  39.551  -18.355 1.00 35.35  ?  132  VAL D CA  1 
ATOM   11820 C  C   . VAL D  1 101 ? 15.081  38.787  -17.035 1.00 40.22  ?  132  VAL D C   1 
ATOM   11821 O  O   . VAL D  1 101 ? 15.865  39.207  -16.159 1.00 33.62  ?  132  VAL D O   1 
ATOM   11822 C  CB  . VAL D  1 101 ? 16.172  39.329  -19.261 1.00 33.18  ?  132  VAL D CB  1 
ATOM   11823 C  CG1 . VAL D  1 101 ? 16.389  37.851  -19.529 1.00 37.23  ?  132  VAL D CG1 1 
ATOM   11824 C  CG2 . VAL D  1 101 ? 16.035  40.115  -20.589 1.00 33.70  ?  132  VAL D CG2 1 
ATOM   11825 N  N   . PRO D  1 102 ? 14.367  37.673  -16.848 1.00 39.08  ?  133  PRO D N   1 
ATOM   11826 C  CA  . PRO D  1 102 ? 14.384  36.960  -15.557 1.00 38.32  ?  133  PRO D CA  1 
ATOM   11827 C  C   . PRO D  1 102 ? 15.786  36.744  -14.999 1.00 40.56  ?  133  PRO D C   1 
ATOM   11828 O  O   . PRO D  1 102 ? 16.669  36.237  -15.686 1.00 39.08  ?  133  PRO D O   1 
ATOM   11829 C  CB  . PRO D  1 102 ? 13.724  35.624  -15.895 1.00 37.90  ?  133  PRO D CB  1 
ATOM   11830 C  CG  . PRO D  1 102 ? 12.776  35.930  -17.010 1.00 38.65  ?  133  PRO D CG  1 
ATOM   11831 C  CD  . PRO D  1 102 ? 13.300  37.179  -17.741 1.00 38.77  ?  133  PRO D CD  1 
ATOM   11832 N  N   . VAL D  1 103 ? 15.985  37.121  -13.729 1.00 40.46  ?  134  VAL D N   1 
ATOM   11833 C  CA  . VAL D  1 103 ? 17.328  37.044  -13.143 1.00 40.37  ?  134  VAL D CA  1 
ATOM   11834 C  C   . VAL D  1 103 ? 17.821  35.607  -13.052 1.00 42.31  ?  134  VAL D C   1 
ATOM   11835 O  O   . VAL D  1 103 ? 19.034  35.364  -13.007 1.00 40.60  ?  134  VAL D O   1 
ATOM   11836 C  CB  . VAL D  1 103 ? 17.379  37.724  -11.750 1.00 42.06  ?  134  VAL D CB  1 
ATOM   11837 C  CG1 . VAL D  1 103 ? 17.190  39.211  -11.882 1.00 41.02  ?  134  VAL D CG1 1 
ATOM   11838 C  CG2 . VAL D  1 103 ? 16.351  37.122  -10.795 1.00 42.43  ?  134  VAL D CG2 1 
ATOM   11839 N  N   . GLU D  1 104 ? 16.904  34.642  -13.049 1.00 41.39  ?  135  GLU D N   1 
ATOM   11840 C  CA  . GLU D  1 104 ? 17.274  33.236  -12.951 1.00 42.99  ?  135  GLU D CA  1 
ATOM   11841 C  C   . GLU D  1 104 ? 17.924  32.713  -14.223 1.00 41.75  ?  135  GLU D C   1 
ATOM   11842 O  O   . GLU D  1 104 ? 18.623  31.698  -14.173 1.00 39.97  ?  135  GLU D O   1 
ATOM   11843 C  CB  . GLU D  1 104 ? 16.019  32.431  -12.619 1.00 50.62  ?  135  GLU D CB  1 
ATOM   11844 C  CG  . GLU D  1 104 ? 15.416  32.837  -11.281 1.00 54.15  ?  135  GLU D CG  1 
ATOM   11845 C  CD  . GLU D  1 104 ? 14.278  33.833  -11.440 1.00 58.41  ?  135  GLU D CD  1 
ATOM   11846 O  OE1 . GLU D  1 104 ? 14.226  34.522  -12.487 1.00 58.62  ?  135  GLU D OE1 1 
ATOM   11847 O  OE2 . GLU D  1 104 ? 13.444  33.937  -10.510 1.00 65.43  ?  135  GLU D OE2 1 
ATOM   11848 N  N   . GLU D  1 105 ? 17.690  33.366  -15.362 1.00 40.78  ?  136  GLU D N   1 
ATOM   11849 C  CA  . GLU D  1 105 ? 18.245  32.941  -16.646 1.00 39.26  ?  136  GLU D CA  1 
ATOM   11850 C  C   . GLU D  1 105 ? 19.659  33.495  -16.765 1.00 39.59  ?  136  GLU D C   1 
ATOM   11851 O  O   . GLU D  1 105 ? 19.874  34.617  -17.226 1.00 41.49  ?  136  GLU D O   1 
ATOM   11852 C  CB  . GLU D  1 105 ? 17.352  33.409  -17.791 1.00 37.34  ?  136  GLU D CB  1 
ATOM   11853 C  CG  . GLU D  1 105 ? 17.514  32.597  -19.060 1.00 33.48  ?  136  GLU D CG  1 
ATOM   11854 C  CD  . GLU D  1 105 ? 17.215  31.121  -18.879 1.00 35.96  ?  136  GLU D CD  1 
ATOM   11855 O  OE1 . GLU D  1 105 ? 16.047  30.757  -18.630 1.00 37.10  ?  136  GLU D OE1 1 
ATOM   11856 O  OE2 . GLU D  1 105 ? 18.155  30.319  -19.002 1.00 41.23  -1 136  GLU D OE2 1 
ATOM   11857 N  N   . THR D  1 106 ? 20.634  32.684  -16.356 1.00 39.12  ?  137  THR D N   1 
ATOM   11858 C  CA  . THR D  1 106 ? 22.013  33.150  -16.224 1.00 39.15  ?  137  THR D CA  1 
ATOM   11859 C  C   . THR D  1 106 ? 22.577  33.591  -17.571 1.00 36.98  ?  137  THR D C   1 
ATOM   11860 O  O   . THR D  1 106 ? 22.548  32.836  -18.546 1.00 39.17  ?  137  THR D O   1 
ATOM   11861 C  CB  . THR D  1 106 ? 22.886  32.038  -15.633 1.00 39.69  ?  137  THR D CB  1 
ATOM   11862 O  OG1 . THR D  1 106 ? 22.286  31.535  -14.433 1.00 42.86  ?  137  THR D OG1 1 
ATOM   11863 C  CG2 . THR D  1 106 ? 24.284  32.549  -15.319 1.00 41.90  ?  137  THR D CG2 1 
ATOM   11864 N  N   . TYR D  1 107 ? 23.127  34.803  -17.607 1.00 35.17  ?  138  TYR D N   1 
ATOM   11865 C  CA  . TYR D  1 107 ? 23.756  35.319  -18.817 1.00 35.92  ?  138  TYR D CA  1 
ATOM   11866 C  C   . TYR D  1 107 ? 25.111  34.677  -19.064 1.00 38.65  ?  138  TYR D C   1 
ATOM   11867 O  O   . TYR D  1 107 ? 25.829  34.288  -18.137 1.00 41.10  ?  138  TYR D O   1 
ATOM   11868 C  CB  . TYR D  1 107 ? 23.961  36.833  -18.744 1.00 34.51  ?  138  TYR D CB  1 
ATOM   11869 C  CG  . TYR D  1 107 ? 22.719  37.668  -18.925 1.00 37.14  ?  138  TYR D CG  1 
ATOM   11870 C  CD1 . TYR D  1 107 ? 21.463  37.085  -19.014 1.00 33.71  ?  138  TYR D CD1 1 
ATOM   11871 C  CD2 . TYR D  1 107 ? 22.806  39.056  -19.005 1.00 35.32  ?  138  TYR D CD2 1 
ATOM   11872 C  CE1 . TYR D  1 107 ? 20.328  37.865  -19.164 1.00 34.41  ?  138  TYR D CE1 1 
ATOM   11873 C  CE2 . TYR D  1 107 ? 21.677  39.843  -19.152 1.00 33.22  ?  138  TYR D CE2 1 
ATOM   11874 C  CZ  . TYR D  1 107 ? 20.442  39.242  -19.230 1.00 32.37  ?  138  TYR D CZ  1 
ATOM   11875 O  OH  . TYR D  1 107 ? 19.316  40.026  -19.374 1.00 34.12  ?  138  TYR D OH  1 
ATOM   11876 N  N   . MET D  1 108 ? 25.474  34.623  -20.340 1.00 32.67  ?  139  MET D N   1 
ATOM   11877 C  CA  . MET D  1 108 ? 26.782  34.124  -20.738 1.00 35.33  ?  139  MET D CA  1 
ATOM   11878 C  C   . MET D  1 108 ? 27.920  34.970  -20.168 1.00 37.01  ?  139  MET D C   1 
ATOM   11879 O  O   . MET D  1 108 ? 29.001  34.441  -19.854 1.00 36.29  ?  139  MET D O   1 
ATOM   11880 C  CB  . MET D  1 108 ? 26.780  34.043  -22.262 1.00 36.34  ?  139  MET D CB  1 
ATOM   11881 C  CG  . MET D  1 108 ? 27.159  35.303  -23.020 1.00 35.98  ?  139  MET D CG  1 
ATOM   11882 S  SD  . MET D  1 108 ? 27.425  34.850  -24.741 1.00 36.36  ?  139  MET D SD  1 
ATOM   11883 C  CE  . MET D  1 108 ? 26.669  36.190  -25.666 1.00 29.87  ?  139  MET D CE  1 
ATOM   11884 N  N   . SER D  1 109 ? 27.683  36.270  -19.999 1.00 33.57  ?  140  SER D N   1 
ATOM   11885 C  CA  . SER D  1 109 ? 28.663  37.139  -19.365 1.00 32.68  ?  140  SER D CA  1 
ATOM   11886 C  C   . SER D  1 109 ? 29.003  36.644  -17.963 1.00 32.78  ?  140  SER D C   1 
ATOM   11887 O  O   . SER D  1 109 ? 30.177  36.589  -17.583 1.00 33.58  ?  140  SER D O   1 
ATOM   11888 C  CB  . SER D  1 109 ? 28.128  38.571  -19.324 1.00 32.89  ?  140  SER D CB  1 
ATOM   11889 O  OG  . SER D  1 109 ? 26.749  38.573  -18.958 1.00 33.05  ?  140  SER D OG  1 
ATOM   11890 N  N   . LYS D  1 110 ? 27.986  36.262  -17.179 1.00 38.41  ?  141  LYS D N   1 
ATOM   11891 C  CA  . LYS D  1 110 ? 28.269  35.767  -15.832 1.00 40.40  ?  141  LYS D CA  1 
ATOM   11892 C  C   . LYS D  1 110 ? 29.047  34.460  -15.888 1.00 41.11  ?  141  LYS D C   1 
ATOM   11893 O  O   . LYS D  1 110 ? 29.996  34.256  -15.118 1.00 38.74  ?  141  LYS D O   1 
ATOM   11894 C  CB  . LYS D  1 110 ? 26.976  35.594  -15.035 1.00 36.89  ?  141  LYS D CB  1 
ATOM   11895 C  CG  . LYS D  1 110 ? 27.243  35.209  -13.577 1.00 45.68  ?  141  LYS D CG  1 
ATOM   11896 C  CD  . LYS D  1 110 ? 26.057  35.483  -12.672 1.00 49.05  ?  141  LYS D CD  1 
ATOM   11897 C  CE  . LYS D  1 110 ? 25.750  36.976  -12.571 1.00 47.60  ?  141  LYS D CE  1 
ATOM   11898 N  NZ  . LYS D  1 110 ? 24.488  37.217  -11.810 1.00 48.33  ?  141  LYS D NZ  1 
ATOM   11899 N  N   . VAL D  1 111 ? 28.679  33.577  -16.821 1.00 39.05  ?  142  VAL D N   1 
ATOM   11900 C  CA  . VAL D  1 111 ? 29.399  32.316  -16.979 1.00 38.78  ?  142  VAL D CA  1 
ATOM   11901 C  C   . VAL D  1 111 ? 30.870  32.565  -17.302 1.00 39.42  ?  142  VAL D C   1 
ATOM   11902 O  O   . VAL D  1 111 ? 31.761  31.915  -16.740 1.00 38.44  ?  142  VAL D O   1 
ATOM   11903 C  CB  . VAL D  1 111 ? 28.704  31.452  -18.048 1.00 37.82  ?  142  VAL D CB  1 
ATOM   11904 C  CG1 . VAL D  1 111 ? 29.432  30.128  -18.217 1.00 40.17  ?  142  VAL D CG1 1 
ATOM   11905 C  CG2 . VAL D  1 111 ? 27.272  31.216  -17.644 1.00 36.53  ?  142  VAL D CG2 1 
ATOM   11906 N  N   . LEU D  1 112 ? 31.154  33.522  -18.189 1.00 34.77  ?  143  LEU D N   1 
ATOM   11907 C  CA  . LEU D  1 112 ? 32.546  33.837  -18.507 1.00 36.57  ?  143  LEU D CA  1 
ATOM   11908 C  C   . LEU D  1 112 ? 33.238  34.540  -17.344 1.00 37.99  ?  143  LEU D C   1 
ATOM   11909 O  O   . LEU D  1 112 ? 34.433  34.322  -17.104 1.00 38.73  ?  143  LEU D O   1 
ATOM   11910 C  CB  . LEU D  1 112 ? 32.615  34.697  -19.773 1.00 32.97  ?  143  LEU D CB  1 
ATOM   11911 C  CG  . LEU D  1 112 ? 31.973  34.043  -20.990 1.00 39.83  ?  143  LEU D CG  1 
ATOM   11912 C  CD1 . LEU D  1 112 ? 31.904  35.005  -22.179 1.00 41.71  ?  143  LEU D CD1 1 
ATOM   11913 C  CD2 . LEU D  1 112 ? 32.745  32.812  -21.361 1.00 34.24  ?  143  LEU D CD2 1 
ATOM   11914 N  N   . GLN D  1 113 ? 32.512  35.394  -16.612 1.00 36.18  ?  144  GLN D N   1 
ATOM   11915 C  CA  . GLN D  1 113 ? 33.085  36.015  -15.419 1.00 38.19  ?  144  GLN D CA  1 
ATOM   11916 C  C   . GLN D  1 113 ? 33.556  34.947  -14.429 1.00 40.95  ?  144  GLN D C   1 
ATOM   11917 O  O   . GLN D  1 113 ? 34.708  34.966  -13.970 1.00 35.32  ?  144  GLN D O   1 
ATOM   11918 C  CB  . GLN D  1 113 ? 32.057  36.954  -14.773 1.00 36.20  ?  144  GLN D CB  1 
ATOM   11919 C  CG  . GLN D  1 113 ? 32.623  38.112  -13.933 1.00 40.51  ?  144  GLN D CG  1 
ATOM   11920 C  CD  . GLN D  1 113 ? 31.512  38.899  -13.220 1.00 41.68  ?  144  GLN D CD  1 
ATOM   11921 O  OE1 . GLN D  1 113 ? 30.520  38.320  -12.790 1.00 41.54  ?  144  GLN D OE1 1 
ATOM   11922 N  NE2 . GLN D  1 113 ? 31.677  40.214  -13.100 1.00 40.87  ?  144  GLN D NE2 1 
ATOM   11923 N  N   . ASN D  1 114 ? 32.678  33.986  -14.113 1.00 41.15  ?  145  ASN D N   1 
ATOM   11924 C  CA  . ASN D  1 114 ? 33.027  32.924  -13.172 1.00 42.51  ?  145  ASN D CA  1 
ATOM   11925 C  C   . ASN D  1 114 ? 34.196  32.092  -13.677 1.00 45.21  ?  145  ASN D C   1 
ATOM   11926 O  O   . ASN D  1 114 ? 34.941  31.517  -12.876 1.00 47.22  ?  145  ASN D O   1 
ATOM   11927 C  CB  . ASN D  1 114 ? 31.825  32.016  -12.916 1.00 43.20  ?  145  ASN D CB  1 
ATOM   11928 C  CG  . ASN D  1 114 ? 30.647  32.749  -12.301 1.00 48.63  ?  145  ASN D CG  1 
ATOM   11929 O  OD1 . ASN D  1 114 ? 30.803  33.789  -11.649 1.00 49.62  ?  145  ASN D OD1 1 
ATOM   11930 N  ND2 . ASN D  1 114 ? 29.449  32.198  -12.499 1.00 49.59  ?  145  ASN D ND2 1 
ATOM   11931 N  N   . ALA D  1 115 ? 34.381  32.030  -14.991 1.00 41.75  ?  146  ALA D N   1 
ATOM   11932 C  CA  . ALA D  1 115 ? 35.488  31.319  -15.607 1.00 41.46  ?  146  ALA D CA  1 
ATOM   11933 C  C   . ALA D  1 115 ? 36.744  32.167  -15.745 1.00 39.36  ?  146  ALA D C   1 
ATOM   11934 O  O   . ALA D  1 115 ? 37.729  31.695  -16.321 1.00 35.30  ?  146  ALA D O   1 
ATOM   11935 C  CB  . ALA D  1 115 ? 35.066  30.788  -16.982 1.00 38.58  ?  146  ALA D CB  1 
ATOM   11936 N  N   . GLY D  1 116 ? 36.742  33.398  -15.245 1.00 37.10  ?  147  GLY D N   1 
ATOM   11937 C  CA  . GLY D  1 116 ? 37.970  34.160  -15.136 1.00 36.59  ?  147  GLY D CA  1 
ATOM   11938 C  C   . GLY D  1 116 ? 38.202  35.186  -16.218 1.00 40.11  ?  147  GLY D C   1 
ATOM   11939 O  O   . GLY D  1 116 ? 39.310  35.729  -16.304 1.00 38.02  ?  147  GLY D O   1 
ATOM   11940 N  N   . TYR D  1 117 ? 37.197  35.473  -17.039 1.00 32.41  ?  148  TYR D N   1 
ATOM   11941 C  CA  . TYR D  1 117 ? 37.290  36.530  -18.030 1.00 32.06  ?  148  TYR D CA  1 
ATOM   11942 C  C   . TYR D  1 117 ? 37.052  37.883  -17.367 1.00 31.66  ?  148  TYR D C   1 
ATOM   11943 O  O   . TYR D  1 117 ? 36.230  38.003  -16.460 1.00 37.43  ?  148  TYR D O   1 
ATOM   11944 C  CB  . TYR D  1 117 ? 36.245  36.290  -19.146 1.00 32.96  ?  148  TYR D CB  1 
ATOM   11945 C  CG  . TYR D  1 117 ? 36.739  35.330  -20.211 1.00 31.32  ?  148  TYR D CG  1 
ATOM   11946 C  CD1 . TYR D  1 117 ? 37.046  34.004  -19.895 1.00 37.28  ?  148  TYR D CD1 1 
ATOM   11947 C  CD2 . TYR D  1 117 ? 36.934  35.748  -21.509 1.00 32.81  ?  148  TYR D CD2 1 
ATOM   11948 C  CE1 . TYR D  1 117 ? 37.522  33.118  -20.861 1.00 33.11  ?  148  TYR D CE1 1 
ATOM   11949 C  CE2 . TYR D  1 117 ? 37.383  34.863  -22.492 1.00 37.70  ?  148  TYR D CE2 1 
ATOM   11950 C  CZ  . TYR D  1 117 ? 37.681  33.555  -22.156 1.00 39.34  ?  148  TYR D CZ  1 
ATOM   11951 O  OH  . TYR D  1 117 ? 38.144  32.692  -23.130 1.00 37.93  ?  148  TYR D OH  1 
ATOM   11952 N  N   . TYR D  1 118 ? 37.760  38.908  -17.831 1.00 30.34  ?  149  TYR D N   1 
ATOM   11953 C  CA  . TYR D  1 118 ? 37.370  40.284  -17.537 1.00 32.46  ?  149  TYR D CA  1 
ATOM   11954 C  C   . TYR D  1 118 ? 36.235  40.674  -18.485 1.00 32.17  ?  149  TYR D C   1 
ATOM   11955 O  O   . TYR D  1 118 ? 36.375  40.552  -19.704 1.00 34.63  ?  149  TYR D O   1 
ATOM   11956 C  CB  . TYR D  1 118 ? 38.553  41.232  -17.701 1.00 37.69  ?  149  TYR D CB  1 
ATOM   11957 C  CG  . TYR D  1 118 ? 38.183  42.696  -17.675 1.00 38.90  ?  149  TYR D CG  1 
ATOM   11958 C  CD1 . TYR D  1 118 ? 37.781  43.309  -16.504 1.00 38.57  ?  149  TYR D CD1 1 
ATOM   11959 C  CD2 . TYR D  1 118 ? 38.240  43.461  -18.825 1.00 37.41  ?  149  TYR D CD2 1 
ATOM   11960 C  CE1 . TYR D  1 118 ? 37.444  44.647  -16.487 1.00 41.28  ?  149  TYR D CE1 1 
ATOM   11961 C  CE2 . TYR D  1 118 ? 37.904  44.793  -18.817 1.00 35.13  ?  149  TYR D CE2 1 
ATOM   11962 C  CZ  . TYR D  1 118 ? 37.511  45.384  -17.653 1.00 39.48  ?  149  TYR D CZ  1 
ATOM   11963 O  OH  . TYR D  1 118 ? 37.186  46.731  -17.654 1.00 40.79  ?  149  TYR D OH  1 
ATOM   11964 N  N   . THR D  1 119 ? 35.115  41.122  -17.942 1.00 34.12  ?  150  THR D N   1 
ATOM   11965 C  CA  . THR D  1 119 ? 33.908  41.279  -18.752 1.00 33.14  ?  150  THR D CA  1 
ATOM   11966 C  C   . THR D  1 119 ? 33.451  42.730  -18.756 1.00 35.10  ?  150  THR D C   1 
ATOM   11967 O  O   . THR D  1 119 ? 33.500  43.412  -17.729 1.00 36.73  ?  150  THR D O   1 
ATOM   11968 C  CB  . THR D  1 119 ? 32.777  40.374  -18.259 1.00 35.60  ?  150  THR D CB  1 
ATOM   11969 O  OG1 . THR D  1 119 ? 32.444  40.694  -16.898 1.00 37.49  ?  150  THR D OG1 1 
ATOM   11970 C  CG2 . THR D  1 119 ? 33.180  38.901  -18.380 1.00 32.64  ?  150  THR D CG2 1 
ATOM   11971 N  N   . SER D  1 120 ? 32.977  43.186  -19.916 1.00 35.17  ?  151  SER D N   1 
ATOM   11972 C  CA  . SER D  1 120 ? 32.679  44.594  -20.132 1.00 32.98  ?  151  SER D CA  1 
ATOM   11973 C  C   . SER D  1 120 ? 31.536  44.710  -21.132 1.00 29.33  ?  151  SER D C   1 
ATOM   11974 O  O   . SER D  1 120 ? 31.575  44.063  -22.182 1.00 29.47  ?  151  SER D O   1 
ATOM   11975 C  CB  . SER D  1 120 ? 33.921  45.311  -20.657 1.00 33.40  ?  151  SER D CB  1 
ATOM   11976 O  OG  . SER D  1 120 ? 33.578  46.413  -21.475 1.00 38.95  ?  151  SER D OG  1 
ATOM   11977 N  N   . ALA D  1 121 ? 30.532  45.524  -20.806 1.00 29.80  ?  152  ALA D N   1 
ATOM   11978 C  CA  . ALA D  1 121 ? 29.441  45.839  -21.724 1.00 31.27  ?  152  ALA D CA  1 
ATOM   11979 C  C   . ALA D  1 121 ? 29.463  47.330  -22.024 1.00 29.92  ?  152  ALA D C   1 
ATOM   11980 O  O   . ALA D  1 121 ? 29.728  48.148  -21.140 1.00 34.09  ?  152  ALA D O   1 
ATOM   11981 C  CB  . ALA D  1 121 ? 28.063  45.449  -21.157 1.00 27.13  ?  152  ALA D CB  1 
ATOM   11982 N  N   . ILE D  1 122 ? 29.193  47.680  -23.268 1.00 31.24  ?  153  ILE D N   1 
ATOM   11983 C  CA  . ILE D  1 122 ? 29.313  49.055  -23.732 1.00 29.70  ?  153  ILE D CA  1 
ATOM   11984 C  C   . ILE D  1 122 ? 28.132  49.342  -24.647 1.00 33.28  ?  153  ILE D C   1 
ATOM   11985 O  O   . ILE D  1 122 ? 27.785  48.518  -25.497 1.00 32.12  ?  153  ILE D O   1 
ATOM   11986 C  CB  . ILE D  1 122 ? 30.654  49.283  -24.471 1.00 28.63  ?  153  ILE D CB  1 
ATOM   11987 C  CG1 . ILE D  1 122 ? 31.843  48.971  -23.543 1.00 28.64  ?  153  ILE D CG1 1 
ATOM   11988 C  CG2 . ILE D  1 122 ? 30.744  50.712  -25.039 1.00 27.37  ?  153  ILE D CG2 1 
ATOM   11989 C  CD1 . ILE D  1 122 ? 33.130  48.768  -24.299 1.00 28.08  ?  153  ILE D CD1 1 
ATOM   11990 N  N   . GLY D  1 123 ? 27.510  50.502  -24.461 1.00 31.47  ?  154  GLY D N   1 
ATOM   11991 C  CA  . GLY D  1 123 ? 26.455  50.944  -25.355 1.00 29.98  ?  154  GLY D CA  1 
ATOM   11992 C  C   . GLY D  1 123 ? 25.081  50.581  -24.825 1.00 31.64  ?  154  GLY D C   1 
ATOM   11993 O  O   . GLY D  1 123 ? 24.753  50.864  -23.658 1.00 30.38  ?  154  GLY D O   1 
ATOM   11994 N  N   . LYS D  1 124 ? 24.270  49.968  -25.692 1.00 30.80  ?  155  LYS D N   1 
ATOM   11995 C  CA  . LYS D  1 124 ? 22.869  49.702  -25.418 1.00 23.20  ?  155  LYS D CA  1 
ATOM   11996 C  C   . LYS D  1 124 ? 22.662  48.420  -24.616 1.00 25.99  ?  155  LYS D C   1 
ATOM   11997 O  O   . LYS D  1 124 ? 23.251  47.377  -24.920 1.00 28.25  ?  155  LYS D O   1 
ATOM   11998 C  CB  . LYS D  1 124 ? 22.117  49.587  -26.751 1.00 27.38  ?  155  LYS D CB  1 
ATOM   11999 C  CG  . LYS D  1 124 ? 20.657  49.156  -26.679 1.00 29.88  ?  155  LYS D CG  1 
ATOM   12000 C  CD  . LYS D  1 124 ? 19.999  49.315  -28.062 1.00 28.02  ?  155  LYS D CD  1 
ATOM   12001 C  CE  . LYS D  1 124 ? 18.743  48.451  -28.223 1.00 31.65  ?  155  LYS D CE  1 
ATOM   12002 N  NZ  . LYS D  1 124 ? 17.886  48.963  -29.345 1.00 32.38  ?  155  LYS D NZ  1 
ATOM   12003 N  N   . TRP D  1 125 ? 21.734  48.481  -23.659 1.00 26.76  ?  156  TRP D N   1 
ATOM   12004 C  CA  . TRP D  1 125 ? 21.340  47.323  -22.857 1.00 30.50  ?  156  TRP D CA  1 
ATOM   12005 C  C   . TRP D  1 125 ? 19.988  46.775  -23.324 1.00 31.30  ?  156  TRP D C   1 
ATOM   12006 O  O   . TRP D  1 125 ? 19.950  45.806  -24.093 1.00 28.72  ?  156  TRP D O   1 
ATOM   12007 C  CB  . TRP D  1 125 ? 21.285  47.720  -21.386 1.00 31.67  ?  156  TRP D CB  1 
ATOM   12008 C  CG  . TRP D  1 125 ? 21.147  46.621  -20.386 1.00 29.32  ?  156  TRP D CG  1 
ATOM   12009 C  CD1 . TRP D  1 125 ? 20.210  46.535  -19.411 1.00 32.31  ?  156  TRP D CD1 1 
ATOM   12010 C  CD2 . TRP D  1 125 ? 22.009  45.488  -20.222 1.00 30.21  ?  156  TRP D CD2 1 
ATOM   12011 N  NE1 . TRP D  1 125 ? 20.425  45.411  -18.644 1.00 29.61  ?  156  TRP D NE1 1 
ATOM   12012 C  CE2 . TRP D  1 125 ? 21.517  44.746  -19.134 1.00 30.32  ?  156  TRP D CE2 1 
ATOM   12013 C  CE3 . TRP D  1 125 ? 23.148  45.021  -20.904 1.00 32.00  ?  156  TRP D CE3 1 
ATOM   12014 C  CZ2 . TRP D  1 125 ? 22.130  43.569  -18.687 1.00 33.14  ?  156  TRP D CZ2 1 
ATOM   12015 C  CZ3 . TRP D  1 125 ? 23.748  43.843  -20.475 1.00 30.34  ?  156  TRP D CZ3 1 
ATOM   12016 C  CH2 . TRP D  1 125 ? 23.241  43.134  -19.369 1.00 33.07  ?  156  TRP D CH2 1 
ATOM   12017 N  N   . HIS D  1 126 ? 18.889  47.383  -22.854 1.00 29.84  ?  157  HIS D N   1 
ATOM   12018 C  CA  . HIS D  1 126 ? 17.513  47.047  -23.243 1.00 29.74  ?  157  HIS D CA  1 
ATOM   12019 C  C   . HIS D  1 126 ? 17.053  45.736  -22.635 1.00 31.89  ?  157  HIS D C   1 
ATOM   12020 O  O   . HIS D  1 126 ? 16.165  45.078  -23.177 1.00 33.47  ?  157  HIS D O   1 
ATOM   12021 C  CB  . HIS D  1 126 ? 17.337  46.982  -24.766 1.00 29.19  ?  157  HIS D CB  1 
ATOM   12022 C  CG  . HIS D  1 126 ? 16.002  47.472  -25.245 1.00 32.24  ?  157  HIS D CG  1 
ATOM   12023 N  ND1 . HIS D  1 126 ? 15.603  47.372  -26.560 1.00 34.84  ?  157  HIS D ND1 1 
ATOM   12024 C  CD2 . HIS D  1 126 ? 14.981  48.073  -24.586 1.00 30.69  ?  157  HIS D CD2 1 
ATOM   12025 C  CE1 . HIS D  1 126 ? 14.396  47.894  -26.693 1.00 31.94  ?  157  HIS D CE1 1 
ATOM   12026 N  NE2 . HIS D  1 126 ? 13.997  48.330  -25.511 1.00 30.59  ?  157  HIS D NE2 1 
ATOM   12027 N  N   . LEU D  1 127 ? 17.664  45.325  -21.532 1.00 32.12  ?  158  LEU D N   1 
ATOM   12028 C  CA  . LEU D  1 127 ? 17.311  44.081  -20.863 1.00 31.28  ?  158  LEU D CA  1 
ATOM   12029 C  C   . LEU D  1 127 ? 16.799  44.325  -19.449 1.00 32.96  ?  158  LEU D C   1 
ATOM   12030 O  O   . LEU D  1 127 ? 16.747  43.392  -18.638 1.00 32.54  ?  158  LEU D O   1 
ATOM   12031 C  CB  . LEU D  1 127 ? 18.515  43.143  -20.857 1.00 32.71  ?  158  LEU D CB  1 
ATOM   12032 C  CG  . LEU D  1 127 ? 19.085  42.922  -22.265 1.00 34.03  ?  158  LEU D CG  1 
ATOM   12033 C  CD1 . LEU D  1 127 ? 20.381  42.139  -22.190 1.00 30.37  ?  158  LEU D CD1 1 
ATOM   12034 C  CD2 . LEU D  1 127 ? 18.059  42.218  -23.179 1.00 28.59  ?  158  LEU D CD2 1 
ATOM   12035 N  N   . GLY D  1 128 ? 16.393  45.557  -19.151 1.00 31.67  ?  159  GLY D N   1 
ATOM   12036 C  CA  . GLY D  1 128 ? 15.831  45.886  -17.856 1.00 36.42  ?  159  GLY D CA  1 
ATOM   12037 C  C   . GLY D  1 128 ? 16.529  47.102  -17.272 1.00 35.58  ?  159  GLY D C   1 
ATOM   12038 O  O   . GLY D  1 128 ? 17.756  47.202  -17.344 1.00 33.31  ?  159  GLY D O   1 
ATOM   12039 N  N   . ALA D  1 129 ? 15.764  48.052  -16.738 1.00 35.95  ?  160  ALA D N   1 
ATOM   12040 C  CA  . ALA D  1 129 ? 16.330  49.281  -16.197 1.00 37.86  ?  160  ALA D CA  1 
ATOM   12041 C  C   . ALA D  1 129 ? 16.260  49.341  -14.674 1.00 39.97  ?  160  ALA D C   1 
ATOM   12042 O  O   . ALA D  1 129 ? 16.568  50.383  -14.092 1.00 38.81  ?  160  ALA D O   1 
ATOM   12043 C  CB  . ALA D  1 129 ? 15.635  50.500  -16.807 1.00 34.38  ?  160  ALA D CB  1 
ATOM   12044 N  N   . ALA D  1 130 ? 15.863  48.265  -14.022 1.00 38.99  ?  161  ALA D N   1 
ATOM   12045 C  CA  . ALA D  1 130 ? 15.841  48.203  -12.572 1.00 40.92  ?  161  ALA D CA  1 
ATOM   12046 C  C   . ALA D  1 130 ? 17.138  47.593  -12.055 1.00 40.64  ?  161  ALA D C   1 
ATOM   12047 O  O   . ALA D  1 130 ? 17.847  46.889  -12.789 1.00 38.21  ?  161  ALA D O   1 
ATOM   12048 C  CB  . ALA D  1 130 ? 14.632  47.395  -12.100 1.00 37.88  ?  161  ALA D CB  1 
ATOM   12049 N  N   . PRO D  1 131 ? 17.484  47.859  -10.787 1.00 40.52  ?  162  PRO D N   1 
ATOM   12050 C  CA  . PRO D  1 131 ? 18.812  47.450  -10.283 1.00 36.21  ?  162  PRO D CA  1 
ATOM   12051 C  C   . PRO D  1 131 ? 19.159  45.981  -10.463 1.00 36.24  ?  162  PRO D C   1 
ATOM   12052 O  O   . PRO D  1 131 ? 20.275  45.666  -10.891 1.00 36.86  ?  162  PRO D O   1 
ATOM   12053 C  CB  . PRO D  1 131 ? 18.739  47.848  -8.798  1.00 38.73  ?  162  PRO D CB  1 
ATOM   12054 C  CG  . PRO D  1 131 ? 17.895  49.076  -8.811  1.00 42.69  ?  162  PRO D CG  1 
ATOM   12055 C  CD  . PRO D  1 131 ? 16.810  48.780  -9.851  1.00 38.49  ?  162  PRO D CD  1 
ATOM   12056 N  N   . LYS D  1 132 ? 18.243  45.067  -10.152 1.00 35.22  ?  163  LYS D N   1 
ATOM   12057 C  CA  . LYS D  1 132 ? 18.576  43.659  -10.315 1.00 38.63  ?  163  LYS D CA  1 
ATOM   12058 C  C   . LYS D  1 132 ? 18.753  43.241  -11.780 1.00 38.07  ?  163  LYS D C   1 
ATOM   12059 O  O   . LYS D  1 132 ? 19.311  42.170  -12.028 1.00 37.24  ?  163  LYS D O   1 
ATOM   12060 C  CB  . LYS D  1 132 ? 17.516  42.792  -9.634  1.00 38.37  ?  163  LYS D CB  1 
ATOM   12061 C  CG  . LYS D  1 132 ? 16.173  42.776  -10.351 1.00 44.92  ?  163  LYS D CG  1 
ATOM   12062 C  CD  . LYS D  1 132 ? 15.396  41.519  -9.995  1.00 45.09  ?  163  LYS D CD  1 
ATOM   12063 C  CE  . LYS D  1 132 ? 13.916  41.793  -9.889  1.00 47.81  ?  163  LYS D CE  1 
ATOM   12064 N  NZ  . LYS D  1 132 ? 13.166  40.509  -9.710  1.00 51.42  ?  163  LYS D NZ  1 
ATOM   12065 N  N   . PHE D  1 133 ? 18.351  44.060  -12.752 1.00 37.16  ?  164  PHE D N   1 
ATOM   12066 C  CA  . PHE D  1 133 ? 18.617  43.754  -14.157 1.00 34.22  ?  164  PHE D CA  1 
ATOM   12067 C  C   . PHE D  1 133 ? 19.882  44.431  -14.677 1.00 39.99  ?  164  PHE D C   1 
ATOM   12068 O  O   . PHE D  1 133 ? 20.172  44.353  -15.875 1.00 38.78  ?  164  PHE D O   1 
ATOM   12069 C  CB  . PHE D  1 133 ? 17.418  44.147  -15.037 1.00 33.04  ?  164  PHE D CB  1 
ATOM   12070 C  CG  . PHE D  1 133 ? 16.120  43.515  -14.609 1.00 33.20  ?  164  PHE D CG  1 
ATOM   12071 C  CD1 . PHE D  1 133 ? 15.967  42.139  -14.615 1.00 36.90  ?  164  PHE D CD1 1 
ATOM   12072 C  CD2 . PHE D  1 133 ? 15.057  44.297  -14.186 1.00 35.46  ?  164  PHE D CD2 1 
ATOM   12073 C  CE1 . PHE D  1 133 ? 14.777  41.550  -14.210 1.00 38.29  ?  164  PHE D CE1 1 
ATOM   12074 C  CE2 . PHE D  1 133 ? 13.858  43.712  -13.776 1.00 37.11  ?  164  PHE D CE2 1 
ATOM   12075 C  CZ  . PHE D  1 133 ? 13.721  42.338  -13.792 1.00 36.29  ?  164  PHE D CZ  1 
ATOM   12076 N  N   . HIS D  1 134 ? 20.662  45.049  -13.802 1.00 40.76  ?  165  HIS D N   1 
ATOM   12077 C  CA  . HIS D  1 134 ? 21.767  45.882  -14.248 1.00 36.38  ?  165  HIS D CA  1 
ATOM   12078 C  C   . HIS D  1 134 ? 22.928  45.023  -14.749 1.00 34.23  ?  165  HIS D C   1 
ATOM   12079 O  O   . HIS D  1 134 ? 23.202  43.955  -14.190 1.00 37.64  ?  165  HIS D O   1 
ATOM   12080 C  CB  . HIS D  1 134 ? 22.241  46.778  -13.098 1.00 35.83  ?  165  HIS D CB  1 
ATOM   12081 C  CG  . HIS D  1 134 ? 23.142  47.884  -13.536 1.00 37.24  ?  165  HIS D CG  1 
ATOM   12082 N  ND1 . HIS D  1 134 ? 24.485  47.693  -13.765 1.00 37.32  ?  165  HIS D ND1 1 
ATOM   12083 C  CD2 . HIS D  1 134 ? 22.894  49.190  -13.799 1.00 37.09  ?  165  HIS D CD2 1 
ATOM   12084 C  CE1 . HIS D  1 134 ? 25.033  48.836  -14.142 1.00 39.77  ?  165  HIS D CE1 1 
ATOM   12085 N  NE2 . HIS D  1 134 ? 24.086  49.757  -14.181 1.00 38.11  ?  165  HIS D NE2 1 
ATOM   12086 N  N   . PRO D  1 135 ? 23.647  45.477  -15.778 1.00 35.55  ?  166  PRO D N   1 
ATOM   12087 C  CA  . PRO D  1 135 ? 24.825  44.725  -16.240 1.00 33.53  ?  166  PRO D CA  1 
ATOM   12088 C  C   . PRO D  1 135 ? 25.784  44.314  -15.123 1.00 36.00  ?  166  PRO D C   1 
ATOM   12089 O  O   . PRO D  1 135 ? 26.264  43.170  -15.118 1.00 32.13  ?  166  PRO D O   1 
ATOM   12090 C  CB  . PRO D  1 135 ? 25.485  45.702  -17.223 1.00 31.75  ?  166  PRO D CB  1 
ATOM   12091 C  CG  . PRO D  1 135 ? 24.359  46.507  -17.757 1.00 35.05  ?  166  PRO D CG  1 
ATOM   12092 C  CD  . PRO D  1 135 ? 23.378  46.664  -16.611 1.00 34.64  ?  166  PRO D CD  1 
ATOM   12093 N  N   . ASN D  1 136 ? 26.073  45.208  -14.171 1.00 36.30  ?  167  ASN D N   1 
ATOM   12094 C  CA  . ASN D  1 136 ? 27.033  44.871  -13.115 1.00 34.72  ?  167  ASN D CA  1 
ATOM   12095 C  C   . ASN D  1 136 ? 26.550  43.683  -12.285 1.00 37.87  ?  167  ASN D C   1 
ATOM   12096 O  O   . ASN D  1 136 ? 27.365  42.932  -11.735 1.00 41.47  ?  167  ASN D O   1 
ATOM   12097 C  CB  . ASN D  1 136 ? 27.274  46.083  -12.207 1.00 36.94  ?  167  ASN D CB  1 
ATOM   12098 C  CG  . ASN D  1 136 ? 28.063  47.203  -12.893 1.00 37.83  ?  167  ASN D CG  1 
ATOM   12099 O  OD1 . ASN D  1 136 ? 27.867  48.381  -12.586 1.00 35.77  ?  167  ASN D OD1 1 
ATOM   12100 N  ND2 . ASN D  1 136 ? 28.958  46.842  -13.810 1.00 31.62  ?  167  ASN D ND2 1 
ATOM   12101 N  N   . LYS D  1 137 ? 25.233  43.493  -12.197 1.00 34.87  ?  168  LYS D N   1 
ATOM   12102 C  CA  . LYS D  1 137 ? 24.606  42.349  -11.545 1.00 38.83  ?  168  LYS D CA  1 
ATOM   12103 C  C   . LYS D  1 137 ? 24.458  41.130  -12.452 1.00 42.47  ?  168  LYS D C   1 
ATOM   12104 O  O   . LYS D  1 137 ? 24.055  40.067  -11.961 1.00 35.68  ?  168  LYS D O   1 
ATOM   12105 C  CB  . LYS D  1 137 ? 23.205  42.734  -11.048 1.00 36.56  ?  168  LYS D CB  1 
ATOM   12106 C  CG  . LYS D  1 137 ? 23.149  43.904  -10.087 1.00 43.54  ?  168  LYS D CG  1 
ATOM   12107 C  CD  . LYS D  1 137 ? 23.261  43.423  -8.664  1.00 46.91  ?  168  LYS D CD  1 
ATOM   12108 C  CE  . LYS D  1 137 ? 23.162  44.574  -7.675  1.00 54.40  ?  168  LYS D CE  1 
ATOM   12109 N  NZ  . LYS D  1 137 ? 23.802  44.190  -6.372  1.00 54.60  ?  168  LYS D NZ  1 
ATOM   12110 N  N   . ARG D  1 138 ? 24.722  41.271  -13.758 1.00 39.33  ?  169  ARG D N   1 
ATOM   12111 C  CA  . ARG D  1 138 ? 24.508  40.209  -14.732 1.00 36.16  ?  169  ARG D CA  1 
ATOM   12112 C  C   . ARG D  1 138 ? 25.818  39.730  -15.337 1.00 38.57  ?  169  ARG D C   1 
ATOM   12113 O  O   . ARG D  1 138 ? 25.842  39.294  -16.487 1.00 36.58  ?  169  ARG D O   1 
ATOM   12114 C  CB  . ARG D  1 138 ? 23.578  40.657  -15.859 1.00 39.82  ?  169  ARG D CB  1 
ATOM   12115 C  CG  . ARG D  1 138 ? 22.172  40.950  -15.430 1.00 39.23  ?  169  ARG D CG  1 
ATOM   12116 C  CD  . ARG D  1 138 ? 21.529  39.735  -14.822 1.00 43.70  ?  169  ARG D CD  1 
ATOM   12117 N  NE  . ARG D  1 138 ? 20.103  39.795  -15.049 1.00 47.71  ?  169  ARG D NE  1 
ATOM   12118 C  CZ  . ARG D  1 138 ? 19.397  38.912  -15.736 1.00 37.55  ?  169  ARG D CZ  1 
ATOM   12119 N  NH1 . ARG D  1 138 ? 19.906  37.750  -16.099 1.00 39.67  ?  169  ARG D NH1 1 
ATOM   12120 N  NH2 . ARG D  1 138 ? 18.130  39.182  -16.003 1.00 35.05  ?  169  ARG D NH2 1 
ATOM   12121 N  N   . GLY D  1 139 ? 26.919  39.833  -14.594 1.00 33.51  ?  170  GLY D N   1 
ATOM   12122 C  CA  . GLY D  1 139 ? 28.175  39.274  -15.030 1.00 33.27  ?  170  GLY D CA  1 
ATOM   12123 C  C   . GLY D  1 139 ? 29.147  40.218  -15.700 1.00 36.43  ?  170  GLY D C   1 
ATOM   12124 O  O   . GLY D  1 139 ? 30.165  39.750  -16.228 1.00 36.20  ?  170  GLY D O   1 
ATOM   12125 N  N   . PHE D  1 140 ? 28.886  41.526  -15.698 1.00 33.31  ?  171  PHE D N   1 
ATOM   12126 C  CA  . PHE D  1 140 ? 29.763  42.477  -16.368 1.00 37.34  ?  171  PHE D CA  1 
ATOM   12127 C  C   . PHE D  1 140 ? 30.577  43.247  -15.334 1.00 36.16  ?  171  PHE D C   1 
ATOM   12128 O  O   . PHE D  1 140 ? 30.015  43.966  -14.495 1.00 39.16  ?  171  PHE D O   1 
ATOM   12129 C  CB  . PHE D  1 140 ? 28.956  43.419  -17.258 1.00 34.49  ?  171  PHE D CB  1 
ATOM   12130 C  CG  . PHE D  1 140 ? 28.506  42.770  -18.539 1.00 34.12  ?  171  PHE D CG  1 
ATOM   12131 C  CD1 . PHE D  1 140 ? 29.425  42.461  -19.538 1.00 28.94  ?  171  PHE D CD1 1 
ATOM   12132 C  CD2 . PHE D  1 140 ? 27.172  42.434  -18.725 1.00 31.15  ?  171  PHE D CD2 1 
ATOM   12133 C  CE1 . PHE D  1 140 ? 29.019  41.847  -20.694 1.00 29.78  ?  171  PHE D CE1 1 
ATOM   12134 C  CE2 . PHE D  1 140 ? 26.752  41.823  -19.883 1.00 28.39  ?  171  PHE D CE2 1 
ATOM   12135 C  CZ  . PHE D  1 140 ? 27.669  41.529  -20.877 1.00 29.29  ?  171  PHE D CZ  1 
ATOM   12136 N  N   . ASP D  1 141 ? 31.897  43.083  -15.391 1.00 36.37  ?  172  ASP D N   1 
ATOM   12137 C  CA  . ASP D  1 141 ? 32.778  43.865  -14.528 1.00 37.96  ?  172  ASP D CA  1 
ATOM   12138 C  C   . ASP D  1 141 ? 32.590  45.360  -14.767 1.00 38.98  ?  172  ASP D C   1 
ATOM   12139 O  O   . ASP D  1 141 ? 32.378  46.126  -13.822 1.00 37.87  ?  172  ASP D O   1 
ATOM   12140 C  CB  . ASP D  1 141 ? 34.233  43.455  -14.759 1.00 36.61  ?  172  ASP D CB  1 
ATOM   12141 C  CG  . ASP D  1 141 ? 34.539  42.060  -14.234 1.00 37.58  ?  172  ASP D CG  1 
ATOM   12142 O  OD1 . ASP D  1 141 ? 33.968  41.680  -13.185 1.00 36.76  ?  172  ASP D OD1 1 
ATOM   12143 O  OD2 . ASP D  1 141 ? 35.372  41.356  -14.848 1.00 35.53  -1 172  ASP D OD2 1 
ATOM   12144 N  N   . ASP D  1 142 ? 32.647  45.791  -16.031 1.00 38.12  ?  173  ASP D N   1 
ATOM   12145 C  CA  . ASP D  1 142 ? 32.442  47.184  -16.399 1.00 34.97  ?  173  ASP D CA  1 
ATOM   12146 C  C   . ASP D  1 142 ? 31.219  47.327  -17.301 1.00 37.43  ?  173  ASP D C   1 
ATOM   12147 O  O   . ASP D  1 142 ? 30.977  46.479  -18.167 1.00 33.30  ?  173  ASP D O   1 
ATOM   12148 C  CB  . ASP D  1 142 ? 33.656  47.738  -17.135 1.00 38.29  ?  173  ASP D CB  1 
ATOM   12149 C  CG  . ASP D  1 142 ? 33.637  49.254  -17.207 1.00 47.43  ?  173  ASP D CG  1 
ATOM   12150 O  OD1 . ASP D  1 142 ? 33.943  49.882  -16.166 1.00 47.22  ?  173  ASP D OD1 1 
ATOM   12151 O  OD2 . ASP D  1 142 ? 33.271  49.818  -18.270 1.00 42.44  -1 173  ASP D OD2 1 
ATOM   12152 N  N   . PHE D  1 143 ? 30.457  48.411  -17.113 1.00 35.31  ?  174  PHE D N   1 
ATOM   12153 C  CA  . PHE D  1 143 ? 29.395  48.787  -18.047 1.00 33.39  ?  174  PHE D CA  1 
ATOM   12154 C  C   . PHE D  1 143 ? 29.453  50.280  -18.328 1.00 34.32  ?  174  PHE D C   1 
ATOM   12155 O  O   . PHE D  1 143 ? 29.499  51.080  -17.394 1.00 38.94  ?  174  PHE D O   1 
ATOM   12156 C  CB  . PHE D  1 143 ? 28.019  48.453  -17.497 1.00 31.10  ?  174  PHE D CB  1 
ATOM   12157 C  CG  . PHE D  1 143 ? 26.893  49.035  -18.304 1.00 36.89  ?  174  PHE D CG  1 
ATOM   12158 C  CD1 . PHE D  1 143 ? 26.784  48.763  -19.667 1.00 34.25  ?  174  PHE D CD1 1 
ATOM   12159 C  CD2 . PHE D  1 143 ? 25.946  49.864  -17.707 1.00 35.21  ?  174  PHE D CD2 1 
ATOM   12160 C  CE1 . PHE D  1 143 ? 25.734  49.295  -20.411 1.00 32.20  ?  174  PHE D CE1 1 
ATOM   12161 C  CE2 . PHE D  1 143 ? 24.904  50.400  -18.444 1.00 33.10  ?  174  PHE D CE2 1 
ATOM   12162 C  CZ  . PHE D  1 143 ? 24.794  50.106  -19.792 1.00 34.41  ?  174  PHE D CZ  1 
ATOM   12163 N  N   . TYR D  1 144 ? 29.412  50.654  -19.606 1.00 34.73  ?  175  TYR D N   1 
ATOM   12164 C  CA  . TYR D  1 144 ? 29.356  52.055  -20.025 1.00 35.25  ?  175  TYR D CA  1 
ATOM   12165 C  C   . TYR D  1 144 ? 28.308  52.189  -21.117 1.00 29.85  ?  175  TYR D C   1 
ATOM   12166 O  O   . TYR D  1 144 ? 28.508  51.658  -22.208 1.00 35.04  ?  175  TYR D O   1 
ATOM   12167 C  CB  . TYR D  1 144 ? 30.711  52.537  -20.554 1.00 31.43  ?  175  TYR D CB  1 
ATOM   12168 C  CG  . TYR D  1 144 ? 30.776  54.023  -20.892 1.00 35.59  ?  175  TYR D CG  1 
ATOM   12169 C  CD1 . TYR D  1 144 ? 30.350  54.497  -22.137 1.00 36.53  ?  175  TYR D CD1 1 
ATOM   12170 C  CD2 . TYR D  1 144 ? 31.273  54.951  -19.972 1.00 36.21  ?  175  TYR D CD2 1 
ATOM   12171 C  CE1 . TYR D  1 144 ? 30.416  55.852  -22.467 1.00 33.23  ?  175  TYR D CE1 1 
ATOM   12172 C  CE2 . TYR D  1 144 ? 31.340  56.309  -20.287 1.00 37.60  ?  175  TYR D CE2 1 
ATOM   12173 C  CZ  . TYR D  1 144 ? 30.915  56.754  -21.531 1.00 39.12  ?  175  TYR D CZ  1 
ATOM   12174 O  OH  . TYR D  1 144 ? 30.976  58.102  -21.834 1.00 38.70  ?  175  TYR D OH  1 
ATOM   12175 N  N   . GLY D  1 145 ? 27.231  52.924  -20.854 1.00 33.21  ?  176  GLY D N   1 
ATOM   12176 C  CA  . GLY D  1 145 ? 26.194  53.075  -21.871 1.00 28.62  ?  176  GLY D CA  1 
ATOM   12177 C  C   . GLY D  1 145 ? 24.879  53.496  -21.245 1.00 37.08  ?  176  GLY D C   1 
ATOM   12178 O  O   . GLY D  1 145 ? 24.856  54.267  -20.281 1.00 37.82  ?  176  GLY D O   1 
ATOM   12179 N  N   . PHE D  1 146 ? 23.786  52.983  -21.828 1.00 34.17  ?  177  PHE D N   1 
ATOM   12180 C  CA  . PHE D  1 146 ? 22.433  53.308  -21.391 1.00 32.30  ?  177  PHE D CA  1 
ATOM   12181 C  C   . PHE D  1 146 ? 21.603  52.034  -21.266 1.00 32.00  ?  177  PHE D C   1 
ATOM   12182 O  O   . PHE D  1 146 ? 21.855  51.030  -21.942 1.00 30.70  ?  177  PHE D O   1 
ATOM   12183 C  CB  . PHE D  1 146 ? 21.743  54.287  -22.349 1.00 31.40  ?  177  PHE D CB  1 
ATOM   12184 C  CG  . PHE D  1 146 ? 21.703  53.828  -23.798 1.00 32.06  ?  177  PHE D CG  1 
ATOM   12185 C  CD1 . PHE D  1 146 ? 22.762  54.096  -24.658 1.00 32.35  ?  177  PHE D CD1 1 
ATOM   12186 C  CD2 . PHE D  1 146 ? 20.583  53.184  -24.309 1.00 33.11  ?  177  PHE D CD2 1 
ATOM   12187 C  CE1 . PHE D  1 146 ? 22.724  53.704  -25.993 1.00 32.83  ?  177  PHE D CE1 1 
ATOM   12188 C  CE2 . PHE D  1 146 ? 20.534  52.779  -25.653 1.00 31.50  ?  177  PHE D CE2 1 
ATOM   12189 C  CZ  . PHE D  1 146 ? 21.601  53.049  -26.494 1.00 29.54  ?  177  PHE D CZ  1 
ATOM   12190 N  N   . LEU D  1 147 ? 20.618  52.078  -20.378 1.00 31.04  ?  178  LEU D N   1 
ATOM   12191 C  CA  . LEU D  1 147 ? 19.869  50.881  -20.023 1.00 32.34  ?  178  LEU D CA  1 
ATOM   12192 C  C   . LEU D  1 147 ? 18.709  50.592  -20.972 1.00 33.51  ?  178  LEU D C   1 
ATOM   12193 O  O   . LEU D  1 147 ? 18.269  49.435  -21.052 1.00 32.87  ?  178  LEU D O   1 
ATOM   12194 C  CB  . LEU D  1 147 ? 19.341  51.014  -18.595 1.00 31.78  ?  178  LEU D CB  1 
ATOM   12195 C  CG  . LEU D  1 147 ? 20.440  51.108  -17.518 1.00 33.59  ?  178  LEU D CG  1 
ATOM   12196 C  CD1 . LEU D  1 147 ? 19.825  51.317  -16.157 1.00 29.98  ?  178  LEU D CD1 1 
ATOM   12197 C  CD2 . LEU D  1 147 ? 21.278  49.844  -17.516 1.00 34.57  ?  178  LEU D CD2 1 
ATOM   12198 N  N   . GLY D  1 148 ? 18.219  51.600  -21.696 1.00 32.86  ?  179  GLY D N   1 
ATOM   12199 C  CA  . GLY D  1 148 ? 17.014  51.475  -22.502 1.00 29.64  ?  179  GLY D CA  1 
ATOM   12200 C  C   . GLY D  1 148 ? 17.270  51.069  -23.939 1.00 33.74  ?  179  GLY D C   1 
ATOM   12201 O  O   . GLY D  1 148 ? 18.301  50.479  -24.275 1.00 30.82  ?  179  GLY D O   1 
ATOM   12202 N  N   . GLY D  1 149 ? 16.296  51.401  -24.813 1.00 31.29  ?  180  GLY D N   1 
ATOM   12203 C  CA  . GLY D  1 149 ? 16.286  50.952  -26.200 1.00 33.26  ?  180  GLY D CA  1 
ATOM   12204 C  C   . GLY D  1 149 ? 16.991  51.827  -27.230 1.00 35.03  ?  180  GLY D C   1 
ATOM   12205 O  O   . GLY D  1 149 ? 17.165  51.400  -28.381 1.00 33.55  ?  180  GLY D O   1 
ATOM   12206 N  N   . GLY D  1 150 ? 17.410  53.033  -26.860 1.00 32.64  ?  181  GLY D N   1 
ATOM   12207 C  CA  . GLY D  1 150 ? 17.979  53.952  -27.830 1.00 32.03  ?  181  GLY D CA  1 
ATOM   12208 C  C   . GLY D  1 150 ? 18.527  55.183  -27.143 1.00 33.93  ?  181  GLY D C   1 
ATOM   12209 O  O   . GLY D  1 150 ? 18.319  55.403  -25.947 1.00 31.76  ?  181  GLY D O   1 
ATOM   12210 N  N   . HIS D  1 151 ? 19.245  55.990  -27.920 1.00 30.80  ?  182  HIS D N   1 
ATOM   12211 C  CA  . HIS D  1 151 ? 19.795  57.203  -27.346 1.00 30.60  ?  182  HIS D CA  1 
ATOM   12212 C  C   . HIS D  1 151 ? 20.137  58.177  -28.455 1.00 31.58  ?  182  HIS D C   1 
ATOM   12213 O  O   . HIS D  1 151 ? 20.633  57.784  -29.514 1.00 31.09  ?  182  HIS D O   1 
ATOM   12214 C  CB  . HIS D  1 151 ? 21.064  56.927  -26.520 1.00 32.77  ?  182  HIS D CB  1 
ATOM   12215 C  CG  . HIS D  1 151 ? 21.276  57.918  -25.421 1.00 33.46  ?  182  HIS D CG  1 
ATOM   12216 N  ND1 . HIS D  1 151 ? 21.807  59.168  -25.646 1.00 35.11  ?  182  HIS D ND1 1 
ATOM   12217 C  CD2 . HIS D  1 151 ? 20.992  57.858  -24.099 1.00 37.10  ?  182  HIS D CD2 1 
ATOM   12218 C  CE1 . HIS D  1 151 ? 21.850  59.835  -24.505 1.00 34.60  ?  182  HIS D CE1 1 
ATOM   12219 N  NE2 . HIS D  1 151 ? 21.362  59.062  -23.551 1.00 37.37  ?  182  HIS D NE2 1 
ATOM   12220 N  N   . ASP D  1 152 ? 19.933  59.456  -28.167 1.00 32.94  ?  183  ASP D N   1 
ATOM   12221 C  CA  . ASP D  1 152 ? 20.449  60.512  -29.026 1.00 32.47  ?  183  ASP D CA  1 
ATOM   12222 C  C   . ASP D  1 152 ? 21.974  60.517  -28.995 1.00 35.47  ?  183  ASP D C   1 
ATOM   12223 O  O   . ASP D  1 152 ? 22.597  60.150  -27.989 1.00 34.83  ?  183  ASP D O   1 
ATOM   12224 C  CB  . ASP D  1 152 ? 19.891  61.859  -28.569 1.00 34.52  ?  183  ASP D CB  1 
ATOM   12225 C  CG  . ASP D  1 152 ? 18.457  62.086  -29.067 1.00 41.01  ?  183  ASP D CG  1 
ATOM   12226 O  OD1 . ASP D  1 152 ? 17.748  61.087  -29.326 1.00 36.12  ?  183  ASP D OD1 1 
ATOM   12227 O  OD2 . ASP D  1 152 ? 18.040  63.252  -29.193 1.00 42.32  -1 183  ASP D OD2 1 
ATOM   12228 N  N   . TYR D  1 153 ? 22.577  60.937  -30.114 1.00 32.39  ?  184  TYR D N   1 
ATOM   12229 C  CA  . TYR D  1 153 ? 23.994  60.674  -30.349 1.00 33.36  ?  184  TYR D CA  1 
ATOM   12230 C  C   . TYR D  1 153 ? 24.934  61.804  -29.943 1.00 35.61  ?  184  TYR D C   1 
ATOM   12231 O  O   . TYR D  1 153 ? 26.133  61.551  -29.779 1.00 35.11  ?  184  TYR D O   1 
ATOM   12232 C  CB  . TYR D  1 153 ? 24.249  60.366  -31.827 1.00 34.26  ?  184  TYR D CB  1 
ATOM   12233 C  CG  . TYR D  1 153 ? 23.726  59.027  -32.293 1.00 34.92  ?  184  TYR D CG  1 
ATOM   12234 C  CD1 . TYR D  1 153 ? 22.374  58.854  -32.585 1.00 34.43  ?  184  TYR D CD1 1 
ATOM   12235 C  CD2 . TYR D  1 153 ? 24.584  57.930  -32.444 1.00 32.65  ?  184  TYR D CD2 1 
ATOM   12236 C  CE1 . TYR D  1 153 ? 21.891  57.638  -33.020 1.00 32.03  ?  184  TYR D CE1 1 
ATOM   12237 C  CE2 . TYR D  1 153 ? 24.111  56.704  -32.874 1.00 31.27  ?  184  TYR D CE2 1 
ATOM   12238 C  CZ  . TYR D  1 153 ? 22.750  56.562  -33.158 1.00 31.83  ?  184  TYR D CZ  1 
ATOM   12239 O  OH  . TYR D  1 153 ? 22.238  55.352  -33.594 1.00 32.18  ?  184  TYR D OH  1 
ATOM   12240 N  N   . PHE D  1 154 ? 24.453  63.031  -29.797 1.00 36.90  ?  185  PHE D N   1 
ATOM   12241 C  CA  . PHE D  1 154 ? 25.352  64.155  -29.540 1.00 40.49  ?  185  PHE D CA  1 
ATOM   12242 C  C   . PHE D  1 154 ? 25.185  64.654  -28.117 1.00 39.05  ?  185  PHE D C   1 
ATOM   12243 O  O   . PHE D  1 154 ? 24.117  65.184  -27.773 1.00 37.65  ?  185  PHE D O   1 
ATOM   12244 C  CB  . PHE D  1 154 ? 25.104  65.285  -30.541 1.00 40.69  ?  185  PHE D CB  1 
ATOM   12245 C  CG  . PHE D  1 154 ? 25.725  65.031  -31.875 1.00 37.55  ?  185  PHE D CG  1 
ATOM   12246 C  CD1 . PHE D  1 154 ? 27.104  65.100  -32.031 1.00 37.94  ?  185  PHE D CD1 1 
ATOM   12247 C  CD2 . PHE D  1 154 ? 24.944  64.692  -32.972 1.00 41.47  ?  185  PHE D CD2 1 
ATOM   12248 C  CE1 . PHE D  1 154 ? 27.689  64.850  -33.254 1.00 37.90  ?  185  PHE D CE1 1 
ATOM   12249 C  CE2 . PHE D  1 154 ? 25.527  64.441  -34.203 1.00 38.20  ?  185  PHE D CE2 1 
ATOM   12250 C  CZ  . PHE D  1 154 ? 26.898  64.523  -34.346 1.00 37.05  ?  185  PHE D CZ  1 
ATOM   12251 N  N   . PRO D  1 155 ? 26.199  64.485  -27.252 1.00 39.66  ?  186  PRO D N   1 
ATOM   12252 C  CA  . PRO D  1 155 ? 26.060  64.939  -25.859 1.00 39.59  ?  186  PRO D CA  1 
ATOM   12253 C  C   . PRO D  1 155 ? 25.750  66.423  -25.736 1.00 37.20  ?  186  PRO D C   1 
ATOM   12254 O  O   . PRO D  1 155 ? 24.927  66.808  -24.899 1.00 37.98  ?  186  PRO D O   1 
ATOM   12255 C  CB  . PRO D  1 155 ? 27.431  64.594  -25.251 1.00 37.51  ?  186  PRO D CB  1 
ATOM   12256 C  CG  . PRO D  1 155 ? 27.955  63.520  -26.108 1.00 39.78  ?  186  PRO D CG  1 
ATOM   12257 C  CD  . PRO D  1 155 ? 27.504  63.856  -27.492 1.00 38.36  ?  186  PRO D CD  1 
ATOM   12258 N  N   . SER D  1 156 ? 26.378  67.266  -26.562 1.00 36.81  ?  187  SER D N   1 
ATOM   12259 C  CA  . SER D  1 156 ? 26.127  68.702  -26.471 1.00 39.35  ?  187  SER D CA  1 
ATOM   12260 C  C   . SER D  1 156 ? 24.649  69.022  -26.654 1.00 45.04  ?  187  SER D C   1 
ATOM   12261 O  O   . SER D  1 156 ? 24.143  69.999  -26.089 1.00 44.83  ?  187  SER D O   1 
ATOM   12262 C  CB  . SER D  1 156 ? 26.970  69.452  -27.503 1.00 43.75  ?  187  SER D CB  1 
ATOM   12263 O  OG  . SER D  1 156 ? 26.896  68.859  -28.787 1.00 46.83  ?  187  SER D OG  1 
ATOM   12264 N  N   . GLU D  1 157 ? 23.931  68.185  -27.388 1.00 41.63  ?  188  GLU D N   1 
ATOM   12265 C  CA  . GLU D  1 157 ? 22.510  68.406  -27.598 1.00 37.37  ?  188  GLU D CA  1 
ATOM   12266 C  C   . GLU D  1 157 ? 21.671  67.755  -26.501 1.00 40.79  ?  188  GLU D C   1 
ATOM   12267 O  O   . GLU D  1 157 ? 20.848  68.427  -25.864 1.00 41.36  ?  188  GLU D O   1 
ATOM   12268 C  CB  . GLU D  1 157 ? 22.141  67.873  -28.975 1.00 40.17  ?  188  GLU D CB  1 
ATOM   12269 C  CG  . GLU D  1 157 ? 22.958  68.519  -30.066 1.00 40.89  ?  188  GLU D CG  1 
ATOM   12270 C  CD  . GLU D  1 157 ? 22.501  68.135  -31.453 1.00 51.87  ?  188  GLU D CD  1 
ATOM   12271 O  OE1 . GLU D  1 157 ? 21.793  67.108  -31.590 1.00 50.01  ?  188  GLU D OE1 1 
ATOM   12272 O  OE2 . GLU D  1 157 ? 22.878  68.842  -32.418 1.00 62.38  -1 188  GLU D OE2 1 
ATOM   12273 N  N   . TYR D  1 158 ? 21.885  66.461  -26.228 1.00 39.98  ?  189  TYR D N   1 
ATOM   12274 C  CA  . TYR D  1 158 ? 20.972  65.795  -25.304 1.00 39.70  ?  189  TYR D CA  1 
ATOM   12275 C  C   . TYR D  1 158 ? 21.228  66.199  -23.857 1.00 39.67  ?  189  TYR D C   1 
ATOM   12276 O  O   . TYR D  1 158 ? 20.280  66.249  -23.063 1.00 39.80  ?  189  TYR D O   1 
ATOM   12277 C  CB  . TYR D  1 158 ? 20.999  64.261  -25.486 1.00 39.08  ?  189  TYR D CB  1 
ATOM   12278 C  CG  . TYR D  1 158 ? 22.245  63.480  -25.047 1.00 37.76  ?  189  TYR D CG  1 
ATOM   12279 C  CD1 . TYR D  1 158 ? 22.579  63.329  -23.698 1.00 37.23  ?  189  TYR D CD1 1 
ATOM   12280 C  CD2 . TYR D  1 158 ? 23.044  62.831  -25.993 1.00 37.86  ?  189  TYR D CD2 1 
ATOM   12281 C  CE1 . TYR D  1 158 ? 23.707  62.596  -23.308 1.00 36.17  ?  189  TYR D CE1 1 
ATOM   12282 C  CE2 . TYR D  1 158 ? 24.168  62.093  -25.616 1.00 36.54  ?  189  TYR D CE2 1 
ATOM   12283 C  CZ  . TYR D  1 158 ? 24.493  61.985  -24.274 1.00 35.90  ?  189  TYR D CZ  1 
ATOM   12284 O  OH  . TYR D  1 158 ? 25.600  61.253  -23.899 1.00 35.73  ?  189  TYR D OH  1 
ATOM   12285 N  N   . GLN D  1 159 ? 22.475  66.509  -23.486 1.00 39.24  ?  190  GLN D N   1 
ATOM   12286 C  CA  . GLN D  1 159 ? 22.708  66.998  -22.124 1.00 41.38  ?  190  GLN D CA  1 
ATOM   12287 C  C   . GLN D  1 159 ? 22.052  68.358  -21.903 1.00 38.57  ?  190  GLN D C   1 
ATOM   12288 O  O   . GLN D  1 159 ? 21.465  68.609  -20.840 1.00 38.06  ?  190  GLN D O   1 
ATOM   12289 C  CB  . GLN D  1 159 ? 24.207  67.079  -21.827 1.00 39.99  ?  190  GLN D CB  1 
ATOM   12290 C  CG  . GLN D  1 159 ? 24.870  65.734  -21.581 1.00 41.95  ?  190  GLN D CG  1 
ATOM   12291 C  CD  . GLN D  1 159 ? 26.385  65.797  -21.690 1.00 45.40  ?  190  GLN D CD  1 
ATOM   12292 O  OE1 . GLN D  1 159 ? 26.966  66.857  -21.985 1.00 39.41  ?  190  GLN D OE1 1 
ATOM   12293 N  NE2 . GLN D  1 159 ? 27.036  64.652  -21.483 1.00 39.24  ?  190  GLN D NE2 1 
ATOM   12294 N  N   . LYS D  1 160 ? 22.153  69.247  -22.895 1.00 43.05  ?  191  LYS D N   1 
ATOM   12295 C  CA  . LYS D  1 160 ? 21.425  70.512  -22.855 1.00 44.15  ?  191  LYS D CA  1 
ATOM   12296 C  C   . LYS D  1 160 ? 19.929  70.279  -22.674 1.00 45.67  ?  191  LYS D C   1 
ATOM   12297 O  O   . LYS D  1 160 ? 19.305  70.864  -21.782 1.00 43.33  ?  191  LYS D O   1 
ATOM   12298 C  CB  . LYS D  1 160 ? 21.695  71.298  -24.139 1.00 49.11  ?  191  LYS D CB  1 
ATOM   12299 C  CG  . LYS D  1 160 ? 21.342  72.777  -24.056 1.00 52.62  ?  191  LYS D CG  1 
ATOM   12300 C  CD  . LYS D  1 160 ? 21.942  73.540  -25.230 1.00 56.09  ?  191  LYS D CD  1 
ATOM   12301 C  CE  . LYS D  1 160 ? 20.897  73.789  -26.310 1.00 65.24  ?  191  LYS D CE  1 
ATOM   12302 N  NZ  . LYS D  1 160 ? 21.437  73.542  -27.683 1.00 71.57  ?  191  LYS D NZ  1 
ATOM   12303 N  N   . THR D  1 161 ? 19.338  69.415  -23.515 1.00 42.59  ?  192  THR D N   1 
ATOM   12304 C  CA  . THR D  1 161 ? 17.905  69.141  -23.420 1.00 38.59  ?  192  THR D CA  1 
ATOM   12305 C  C   . THR D  1 161 ? 17.540  68.522  -22.076 1.00 40.79  ?  192  THR D C   1 
ATOM   12306 O  O   . THR D  1 161 ? 16.545  68.917  -21.457 1.00 41.00  ?  192  THR D O   1 
ATOM   12307 C  CB  . THR D  1 161 ? 17.464  68.229  -24.570 1.00 39.62  ?  192  THR D CB  1 
ATOM   12308 O  OG1 . THR D  1 161 ? 17.805  68.846  -25.815 1.00 39.60  ?  192  THR D OG1 1 
ATOM   12309 C  CG2 . THR D  1 161 ? 15.955  67.970  -24.534 1.00 36.89  ?  192  THR D CG2 1 
ATOM   12310 N  N   . TYR D  1 162 ? 18.334  67.559  -21.601 1.00 38.41  ?  193  TYR D N   1 
ATOM   12311 C  CA  . TYR D  1 162 ? 18.021  66.900  -20.334 1.00 40.46  ?  193  TYR D CA  1 
ATOM   12312 C  C   . TYR D  1 162 ? 18.087  67.878  -19.165 1.00 39.45  ?  193  TYR D C   1 
ATOM   12313 O  O   . TYR D  1 162 ? 17.207  67.890  -18.296 1.00 37.36  ?  193  TYR D O   1 
ATOM   12314 C  CB  . TYR D  1 162 ? 18.984  65.737  -20.091 1.00 36.56  ?  193  TYR D CB  1 
ATOM   12315 C  CG  . TYR D  1 162 ? 18.791  65.094  -18.743 1.00 40.09  ?  193  TYR D CG  1 
ATOM   12316 C  CD1 . TYR D  1 162 ? 17.692  64.283  -18.495 1.00 38.88  ?  193  TYR D CD1 1 
ATOM   12317 C  CD2 . TYR D  1 162 ? 19.700  65.320  -17.699 1.00 39.88  ?  193  TYR D CD2 1 
ATOM   12318 C  CE1 . TYR D  1 162 ? 17.500  63.693  -17.265 1.00 36.67  ?  193  TYR D CE1 1 
ATOM   12319 C  CE2 . TYR D  1 162 ? 19.515  64.738  -16.456 1.00 40.39  ?  193  TYR D CE2 1 
ATOM   12320 C  CZ  . TYR D  1 162 ? 18.406  63.928  -16.244 1.00 43.61  ?  193  TYR D CZ  1 
ATOM   12321 O  OH  . TYR D  1 162 ? 18.208  63.329  -15.020 1.00 40.24  ?  193  TYR D OH  1 
ATOM   12322 N  N   . LYS D  1 163 ? 19.145  68.689  -19.107 1.00 40.60  ?  194  LYS D N   1 
ATOM   12323 C  CA  . LYS D  1 163 ? 19.279  69.621  -17.988 1.00 41.02  ?  194  LYS D CA  1 
ATOM   12324 C  C   . LYS D  1 163 ? 18.142  70.638  -17.983 1.00 40.25  ?  194  LYS D C   1 
ATOM   12325 O  O   . LYS D  1 163 ? 17.585  70.950  -16.924 1.00 41.04  ?  194  LYS D O   1 
ATOM   12326 C  CB  . LYS D  1 163 ? 20.639  70.318  -18.042 1.00 44.36  ?  194  LYS D CB  1 
ATOM   12327 C  CG  . LYS D  1 163 ? 21.812  69.427  -17.623 1.00 51.27  ?  194  LYS D CG  1 
ATOM   12328 C  CD  . LYS D  1 163 ? 23.149  70.177  -17.721 1.00 53.46  ?  194  LYS D CD  1 
ATOM   12329 C  CE  . LYS D  1 163 ? 24.326  69.215  -17.755 1.00 55.99  ?  194  LYS D CE  1 
ATOM   12330 N  NZ  . LYS D  1 163 ? 25.547  69.840  -18.353 1.00 57.93  ?  194  LYS D NZ  1 
ATOM   12331 N  N   . ALA D  1 164 ? 17.757  71.133  -19.163 1.00 41.41  ?  195  ALA D N   1 
ATOM   12332 C  CA  . ALA D  1 164 ? 16.661  72.093  -19.237 1.00 40.86  ?  195  ALA D CA  1 
ATOM   12333 C  C   . ALA D  1 164 ? 15.354  71.469  -18.773 1.00 41.55  ?  195  ALA D C   1 
ATOM   12334 O  O   . ALA D  1 164 ? 14.579  72.096  -18.040 1.00 38.56  ?  195  ALA D O   1 
ATOM   12335 C  CB  . ALA D  1 164 ? 16.527  72.627  -20.659 1.00 37.19  ?  195  ALA D CB  1 
ATOM   12336 N  N   . GLN D  1 165 ? 15.091  70.231  -19.189 1.00 42.49  ?  196  GLN D N   1 
ATOM   12337 C  CA  . GLN D  1 165 ? 13.830  69.588  -18.834 1.00 41.39  ?  196  GLN D CA  1 
ATOM   12338 C  C   . GLN D  1 165 ? 13.829  69.153  -17.378 1.00 42.60  ?  196  GLN D C   1 
ATOM   12339 O  O   . GLN D  1 165 ? 12.771  69.149  -16.733 1.00 44.36  ?  196  GLN D O   1 
ATOM   12340 C  CB  . GLN D  1 165 ? 13.562  68.394  -19.767 1.00 40.47  ?  196  GLN D CB  1 
ATOM   12341 C  CG  . GLN D  1 165 ? 13.313  68.782  -21.231 1.00 37.42  ?  196  GLN D CG  1 
ATOM   12342 C  CD  . GLN D  1 165 ? 12.978  67.584  -22.127 1.00 43.28  ?  196  GLN D CD  1 
ATOM   12343 O  OE1 . GLN D  1 165 ? 12.874  66.444  -21.663 1.00 39.58  ?  196  GLN D OE1 1 
ATOM   12344 N  NE2 . GLN D  1 165 ? 12.801  67.847  -23.415 1.00 39.01  ?  196  GLN D NE2 1 
ATOM   12345 N  N   . LYS D  1 166 ? 14.999  68.775  -16.849 1.00 40.99  ?  197  LYS D N   1 
ATOM   12346 C  CA  . LYS D  1 166 ? 15.104  68.505  -15.418 1.00 44.87  ?  197  LYS D CA  1 
ATOM   12347 C  C   . LYS D  1 166 ? 14.882  69.779  -14.607 1.00 44.38  ?  197  LYS D C   1 
ATOM   12348 O  O   . LYS D  1 166 ? 14.153  69.764  -13.610 1.00 45.78  ?  197  LYS D O   1 
ATOM   12349 C  CB  . LYS D  1 166 ? 16.467  67.878  -15.089 1.00 39.11  ?  197  LYS D CB  1 
ATOM   12350 N  N   . LYS D  1 167 ? 15.482  70.897  -15.032 1.00 46.89  ?  198  LYS D N   1 
ATOM   12351 C  CA  . LYS D  1 167 ? 15.268  72.162  -14.330 1.00 47.90  ?  198  LYS D CA  1 
ATOM   12352 C  C   . LYS D  1 167 ? 13.792  72.557  -14.341 1.00 49.46  ?  198  LYS D C   1 
ATOM   12353 O  O   . LYS D  1 167 ? 13.258  73.025  -13.327 1.00 46.41  ?  198  LYS D O   1 
ATOM   12354 C  CB  . LYS D  1 167 ? 16.133  73.255  -14.962 1.00 48.50  ?  198  LYS D CB  1 
ATOM   12355 C  CG  . LYS D  1 167 ? 16.663  74.303  -13.987 1.00 55.78  ?  198  LYS D CG  1 
ATOM   12356 C  CD  . LYS D  1 167 ? 15.633  75.385  -13.700 1.00 57.88  ?  198  LYS D CD  1 
ATOM   12357 C  CE  . LYS D  1 167 ? 16.171  76.440  -12.739 1.00 63.63  ?  198  LYS D CE  1 
ATOM   12358 N  NZ  . LYS D  1 167 ? 15.944  76.060  -11.310 1.00 67.24  ?  198  LYS D NZ  1 
ATOM   12359 N  N   . ALA D  1 168 ? 13.103  72.339  -15.469 1.00 44.55  ?  199  ALA D N   1 
ATOM   12360 C  CA  . ALA D  1 168 ? 11.684  72.665  -15.589 1.00 42.88  ?  199  ALA D CA  1 
ATOM   12361 C  C   . ALA D  1 168 ? 10.773  71.694  -14.850 1.00 42.05  ?  199  ALA D C   1 
ATOM   12362 O  O   . ALA D  1 168 ? 9.568   71.954  -14.755 1.00 41.16  ?  199  ALA D O   1 
ATOM   12363 C  CB  . ALA D  1 168 ? 11.274  72.713  -17.058 1.00 38.66  ?  199  ALA D CB  1 
ATOM   12364 N  N   . GLY D  1 169 ? 11.311  70.604  -14.310 1.00 44.43  ?  200  GLY D N   1 
ATOM   12365 C  CA  . GLY D  1 169 ? 10.473  69.608  -13.674 1.00 38.81  ?  200  GLY D CA  1 
ATOM   12366 C  C   . GLY D  1 169 ? 9.605   68.821  -14.637 1.00 44.85  ?  200  GLY D C   1 
ATOM   12367 O  O   . GLY D  1 169 ? 8.525   68.362  -14.249 1.00 44.80  ?  200  GLY D O   1 
ATOM   12368 N  N   . ASN D  1 170 ? 10.042  68.662  -15.889 1.00 44.88  ?  201  ASN D N   1 
ATOM   12369 C  CA  . ASN D  1 170 ? 9.357   67.812  -16.854 1.00 44.96  ?  201  ASN D CA  1 
ATOM   12370 C  C   . ASN D  1 170 ? 9.191   66.409  -16.270 1.00 48.00  ?  201  ASN D C   1 
ATOM   12371 O  O   . ASN D  1 170 ? 10.194  65.742  -15.980 1.00 47.69  ?  201  ASN D O   1 
ATOM   12372 C  CB  . ASN D  1 170 ? 10.132  67.756  -18.172 1.00 42.42  ?  201  ASN D CB  1 
ATOM   12373 C  CG  . ASN D  1 170 ? 9.382   66.996  -19.277 1.00 44.28  ?  201  ASN D CG  1 
ATOM   12374 O  OD1 . ASN D  1 170 ? 8.503   66.174  -19.010 1.00 43.79  ?  201  ASN D OD1 1 
ATOM   12375 N  ND2 . ASN D  1 170 ? 9.734   67.279  -20.521 1.00 37.61  ?  201  ASN D ND2 1 
ATOM   12376 N  N   . PRO D  1 171 ? 7.957   65.941  -16.066 1.00 46.68  ?  202  PRO D N   1 
ATOM   12377 C  CA  . PRO D  1 171 ? 7.740   64.623  -15.458 1.00 48.35  ?  202  PRO D CA  1 
ATOM   12378 C  C   . PRO D  1 171 ? 7.820   63.452  -16.436 1.00 54.37  ?  202  PRO D C   1 
ATOM   12379 O  O   . PRO D  1 171 ? 7.684   62.297  -16.009 1.00 53.59  ?  202  PRO D O   1 
ATOM   12380 C  CB  . PRO D  1 171 ? 6.322   64.760  -14.882 1.00 49.80  ?  202  PRO D CB  1 
ATOM   12381 C  CG  . PRO D  1 171 ? 5.635   65.653  -15.881 1.00 50.56  ?  202  PRO D CG  1 
ATOM   12382 C  CD  . PRO D  1 171 ? 6.690   66.629  -16.374 1.00 46.30  ?  202  PRO D CD  1 
ATOM   12383 N  N   . ASN D  1 172 ? 8.014   63.693  -17.733 1.00 51.44  ?  203  ASN D N   1 
ATOM   12384 C  CA  . ASN D  1 172 ? 8.145   62.611  -18.706 1.00 47.66  ?  203  ASN D CA  1 
ATOM   12385 C  C   . ASN D  1 172 ? 9.313   62.910  -19.642 1.00 44.93  ?  203  ASN D C   1 
ATOM   12386 O  O   . ASN D  1 172 ? 9.172   63.016  -20.861 1.00 48.42  ?  203  ASN D O   1 
ATOM   12387 C  CB  . ASN D  1 172 ? 6.849   62.401  -19.471 1.00 49.45  ?  203  ASN D CB  1 
ATOM   12388 C  CG  . ASN D  1 172 ? 5.647   62.327  -18.552 1.00 60.37  ?  203  ASN D CG  1 
ATOM   12389 O  OD1 . ASN D  1 172 ? 5.396   61.298  -17.914 1.00 62.44  ?  203  ASN D OD1 1 
ATOM   12390 N  ND2 . ASN D  1 172 ? 4.887   63.415  -18.488 1.00 57.56  ?  203  ASN D ND2 1 
ATOM   12391 N  N   . ILE D  1 173 ? 10.491  63.056  -19.039 1.00 42.11  ?  204  ILE D N   1 
ATOM   12392 C  CA  . ILE D  1 173 ? 11.729  63.147  -19.804 1.00 42.70  ?  204  ILE D CA  1 
ATOM   12393 C  C   . ILE D  1 173 ? 12.005  61.815  -20.494 1.00 43.65  ?  204  ILE D C   1 
ATOM   12394 O  O   . ILE D  1 173 ? 12.008  60.754  -19.845 1.00 42.62  ?  204  ILE D O   1 
ATOM   12395 C  CB  . ILE D  1 173 ? 12.886  63.529  -18.876 1.00 41.10  ?  204  ILE D CB  1 
ATOM   12396 C  CG1 . ILE D  1 173 ? 12.551  64.817  -18.108 1.00 43.13  ?  204  ILE D CG1 1 
ATOM   12397 C  CG2 . ILE D  1 173 ? 14.164  63.660  -19.671 1.00 43.33  ?  204  ILE D CG2 1 
ATOM   12398 C  CD1 . ILE D  1 173 ? 13.718  65.386  -17.308 1.00 39.72  ?  204  ILE D CD1 1 
ATOM   12399 N  N   . ARG D  1 174 ? 12.252  61.866  -21.810 1.00 38.99  ?  205  ARG D N   1 
ATOM   12400 C  CA  . ARG D  1 174 ? 12.499  60.656  -22.588 1.00 40.81  ?  205  ARG D CA  1 
ATOM   12401 C  C   . ARG D  1 174 ? 13.824  60.025  -22.197 1.00 42.83  ?  205  ARG D C   1 
ATOM   12402 O  O   . ARG D  1 174 ? 14.827  60.723  -22.018 1.00 39.02  ?  205  ARG D O   1 
ATOM   12403 C  CB  . ARG D  1 174 ? 12.522  60.960  -24.088 1.00 44.60  ?  205  ARG D CB  1 
ATOM   12404 C  CG  . ARG D  1 174 ? 11.181  61.335  -24.696 1.00 49.61  ?  205  ARG D CG  1 
ATOM   12405 C  CD  . ARG D  1 174 ? 11.379  62.043  -26.027 1.00 56.53  ?  205  ARG D CD  1 
ATOM   12406 N  NE  . ARG D  1 174 ? 11.792  61.112  -27.073 1.00 56.98  ?  205  ARG D NE  1 
ATOM   12407 C  CZ  . ARG D  1 174 ? 12.930  61.198  -27.751 1.00 55.06  ?  205  ARG D CZ  1 
ATOM   12408 N  NH1 . ARG D  1 174 ? 13.770  62.206  -27.570 1.00 50.20  ?  205  ARG D NH1 1 
ATOM   12409 N  NH2 . ARG D  1 174 ? 13.233  60.249  -28.637 1.00 51.70  ?  205  ARG D NH2 1 
ATOM   12410 N  N   . ASP D  1 175 ? 13.846  58.691  -22.098 1.00 40.40  ?  206  ASP D N   1 
ATOM   12411 C  CA  . ASP D  1 175 ? 15.122  58.084  -21.734 1.00 37.77  ?  206  ASP D CA  1 
ATOM   12412 C  C   . ASP D  1 175 ? 16.174  58.244  -22.823 1.00 34.26  ?  206  ASP D C   1 
ATOM   12413 O  O   . ASP D  1 175 ? 17.360  58.077  -22.525 1.00 35.08  ?  206  ASP D O   1 
ATOM   12414 C  CB  . ASP D  1 175 ? 14.971  56.599  -21.323 1.00 38.44  ?  206  ASP D CB  1 
ATOM   12415 C  CG  . ASP D  1 175 ? 14.296  55.713  -22.386 1.00 39.88  ?  206  ASP D CG  1 
ATOM   12416 O  OD1 . ASP D  1 175 ? 14.224  56.086  -23.575 1.00 34.89  ?  206  ASP D OD1 1 
ATOM   12417 O  OD2 . ASP D  1 175 ? 13.861  54.602  -22.008 1.00 39.42  -1 206  ASP D OD2 1 
ATOM   12418 N  N   . TYR D  1 176 ? 15.784  58.625  -24.043 1.00 34.59  ?  207  TYR D N   1 
ATOM   12419 C  CA  . TYR D  1 176 ? 16.750  58.883  -25.118 1.00 33.05  ?  207  TYR D CA  1 
ATOM   12420 C  C   . TYR D  1 176 ? 17.709  60.036  -24.809 1.00 34.87  ?  207  TYR D C   1 
ATOM   12421 O  O   . TYR D  1 176 ? 18.723  60.194  -25.498 1.00 33.16  ?  207  TYR D O   1 
ATOM   12422 C  CB  . TYR D  1 176 ? 16.002  59.184  -26.422 1.00 34.82  ?  207  TYR D CB  1 
ATOM   12423 C  CG  . TYR D  1 176 ? 15.772  57.952  -27.262 1.00 34.92  ?  207  TYR D CG  1 
ATOM   12424 C  CD1 . TYR D  1 176 ? 15.046  56.876  -26.760 1.00 38.34  ?  207  TYR D CD1 1 
ATOM   12425 C  CD2 . TYR D  1 176 ? 16.296  57.849  -28.537 1.00 34.61  ?  207  TYR D CD2 1 
ATOM   12426 C  CE1 . TYR D  1 176 ? 14.833  55.731  -27.518 1.00 34.99  ?  207  TYR D CE1 1 
ATOM   12427 C  CE2 . TYR D  1 176 ? 16.093  56.711  -29.303 1.00 36.70  ?  207  TYR D CE2 1 
ATOM   12428 C  CZ  . TYR D  1 176 ? 15.359  55.657  -28.785 1.00 36.32  ?  207  TYR D CZ  1 
ATOM   12429 O  OH  . TYR D  1 176 ? 15.164  54.522  -29.539 1.00 33.61  ?  207  TYR D OH  1 
ATOM   12430 N  N   . VAL D  1 177 ? 17.397  60.880  -23.831 1.00 36.51  ?  208  VAL D N   1 
ATOM   12431 C  CA  . VAL D  1 177 ? 18.279  61.982  -23.472 1.00 36.48  ?  208  VAL D CA  1 
ATOM   12432 C  C   . VAL D  1 177 ? 18.832  61.848  -22.067 1.00 38.54  ?  208  VAL D C   1 
ATOM   12433 O  O   . VAL D  1 177 ? 19.608  62.708  -21.644 1.00 38.64  ?  208  VAL D O   1 
ATOM   12434 C  CB  . VAL D  1 177 ? 17.590  63.353  -23.646 1.00 37.99  ?  208  VAL D CB  1 
ATOM   12435 C  CG1 . VAL D  1 177 ? 17.163  63.557  -25.114 1.00 35.12  ?  208  VAL D CG1 1 
ATOM   12436 C  CG2 . VAL D  1 177 ? 16.412  63.500  -22.695 1.00 37.68  ?  208  VAL D CG2 1 
ATOM   12437 N  N   . PHE D  1 178 ? 18.459  60.796  -21.333 1.00 37.83  ?  209  PHE D N   1 
ATOM   12438 C  CA  . PHE D  1 178 ? 19.018  60.562  -20.011 1.00 37.61  ?  209  PHE D CA  1 
ATOM   12439 C  C   . PHE D  1 178 ? 20.538  60.588  -20.085 1.00 35.63  ?  209  PHE D C   1 
ATOM   12440 O  O   . PHE D  1 178 ? 21.117  60.133  -21.083 1.00 36.18  ?  209  PHE D O   1 
ATOM   12441 C  CB  . PHE D  1 178 ? 18.597  59.200  -19.445 1.00 39.28  ?  209  PHE D CB  1 
ATOM   12442 C  CG  . PHE D  1 178 ? 17.210  59.151  -18.891 1.00 35.58  ?  209  PHE D CG  1 
ATOM   12443 C  CD1 . PHE D  1 178 ? 16.358  60.239  -18.983 1.00 38.58  ?  209  PHE D CD1 1 
ATOM   12444 C  CD2 . PHE D  1 178 ? 16.753  57.983  -18.277 1.00 33.44  ?  209  PHE D CD2 1 
ATOM   12445 C  CE1 . PHE D  1 178 ? 15.059  60.167  -18.471 1.00 38.27  ?  209  PHE D CE1 1 
ATOM   12446 C  CE2 . PHE D  1 178 ? 15.473  57.903  -17.766 1.00 43.12  ?  209  PHE D CE2 1 
ATOM   12447 C  CZ  . PHE D  1 178 ? 14.616  58.997  -17.867 1.00 40.79  ?  209  PHE D CZ  1 
ATOM   12448 N  N   . PRO D  1 179 ? 21.218  61.093  -19.059 1.00 40.27  ?  210  PRO D N   1 
ATOM   12449 C  CA  . PRO D  1 179 ? 22.673  60.929  -19.012 1.00 36.98  ?  210  PRO D CA  1 
ATOM   12450 C  C   . PRO D  1 179 ? 23.035  59.451  -19.038 1.00 34.77  ?  210  PRO D C   1 
ATOM   12451 O  O   . PRO D  1 179 ? 22.381  58.616  -18.408 1.00 35.56  ?  210  PRO D O   1 
ATOM   12452 C  CB  . PRO D  1 179 ? 23.073  61.592  -17.688 1.00 38.94  ?  210  PRO D CB  1 
ATOM   12453 C  CG  . PRO D  1 179 ? 21.813  61.625  -16.880 1.00 45.24  ?  210  PRO D CG  1 
ATOM   12454 C  CD  . PRO D  1 179 ? 20.703  61.808  -17.885 1.00 37.92  ?  210  PRO D CD  1 
ATOM   12455 N  N   . MET D  1 180 ? 24.075  59.142  -19.802 1.00 33.11  ?  211  MET D N   1 
ATOM   12456 C  CA  . MET D  1 180 ? 24.665  57.819  -19.872 1.00 33.16  ?  211  MET D CA  1 
ATOM   12457 C  C   . MET D  1 180 ? 25.364  57.518  -18.534 1.00 42.87  ?  211  MET D C   1 
ATOM   12458 O  O   . MET D  1 180 ? 25.674  58.428  -17.758 1.00 38.78  ?  211  MET D O   1 
ATOM   12459 C  CB  . MET D  1 180 ? 25.655  57.830  -21.026 1.00 36.62  ?  211  MET D CB  1 
ATOM   12460 C  CG  . MET D  1 180 ? 25.008  58.020  -22.425 1.00 37.18  ?  211  MET D CG  1 
ATOM   12461 S  SD  . MET D  1 180 ? 25.466  56.870  -23.727 1.00 35.31  ?  211  MET D SD  1 
ATOM   12462 C  CE  . MET D  1 180 ? 27.015  57.612  -24.212 1.00 39.59  ?  211  MET D CE  1 
ATOM   12463 N  N   . GLU D  1 181 ? 25.620  56.234  -18.260 1.00 38.31  ?  212  GLU D N   1 
ATOM   12464 C  CA  . GLU D  1 181 ? 26.209  55.843  -16.985 1.00 36.29  ?  212  GLU D CA  1 
ATOM   12465 C  C   . GLU D  1 181 ? 27.460  55.014  -17.205 1.00 39.62  ?  212  GLU D C   1 
ATOM   12466 O  O   . GLU D  1 181 ? 27.664  54.396  -18.254 1.00 35.95  ?  212  GLU D O   1 
ATOM   12467 C  CB  . GLU D  1 181 ? 25.253  55.030  -16.108 1.00 40.11  ?  212  GLU D CB  1 
ATOM   12468 C  CG  . GLU D  1 181 ? 24.923  53.656  -16.664 1.00 41.51  ?  212  GLU D CG  1 
ATOM   12469 C  CD  . GLU D  1 181 ? 24.450  52.678  -15.594 1.00 40.09  ?  212  GLU D CD  1 
ATOM   12470 O  OE1 . GLU D  1 181 ? 23.250  52.682  -15.245 1.00 41.74  ?  212  GLU D OE1 1 
ATOM   12471 O  OE2 . GLU D  1 181 ? 25.282  51.905  -15.091 1.00 43.43  -1 212  GLU D OE2 1 
ATOM   12472 N  N   . HIS D  1 182 ? 28.300  55.009  -16.175 1.00 42.22  ?  213  HIS D N   1 
ATOM   12473 C  CA  . HIS D  1 182 ? 29.489  54.173  -16.115 1.00 38.31  ?  213  HIS D CA  1 
ATOM   12474 C  C   . HIS D  1 182 ? 29.450  53.489  -14.754 1.00 42.43  ?  213  HIS D C   1 
ATOM   12475 O  O   . HIS D  1 182 ? 29.606  54.154  -13.723 1.00 38.47  ?  213  HIS D O   1 
ATOM   12476 C  CB  . HIS D  1 182 ? 30.754  55.009  -16.291 1.00 40.99  ?  213  HIS D CB  1 
ATOM   12477 C  CG  . HIS D  1 182 ? 32.005  54.194  -16.321 1.00 45.08  ?  213  HIS D CG  1 
ATOM   12478 N  ND1 . HIS D  1 182 ? 33.233  54.695  -15.946 1.00 48.40  ?  213  HIS D ND1 1 
ATOM   12479 C  CD2 . HIS D  1 182 ? 32.216  52.910  -16.691 1.00 43.72  ?  213  HIS D CD2 1 
ATOM   12480 C  CE1 . HIS D  1 182 ? 34.147  53.749  -16.076 1.00 49.61  ?  213  HIS D CE1 1 
ATOM   12481 N  NE2 . HIS D  1 182 ? 33.556  52.656  -16.527 1.00 47.45  ?  213  HIS D NE2 1 
ATOM   12482 N  N   . ASN D  1 183 ? 29.186  52.183  -14.747 1.00 39.20  ?  214  ASN D N   1 
ATOM   12483 C  CA  . ASN D  1 183 ? 29.026  51.410  -13.511 1.00 40.28  ?  214  ASN D CA  1 
ATOM   12484 C  C   . ASN D  1 183 ? 28.173  52.158  -12.487 1.00 42.74  ?  214  ASN D C   1 
ATOM   12485 O  O   . ASN D  1 183 ? 28.531  52.286  -11.311 1.00 41.81  ?  214  ASN D O   1 
ATOM   12486 C  CB  . ASN D  1 183 ? 30.377  51.051  -12.889 1.00 40.27  ?  214  ASN D CB  1 
ATOM   12487 C  CG  . ASN D  1 183 ? 31.263  50.237  -13.802 1.00 42.47  ?  214  ASN D CG  1 
ATOM   12488 O  OD1 . ASN D  1 183 ? 30.800  49.371  -14.538 1.00 37.41  ?  214  ASN D OD1 1 
ATOM   12489 N  ND2 . ASN D  1 183 ? 32.572  50.479  -13.712 1.00 44.14  ?  214  ASN D ND2 1 
ATOM   12490 N  N   . GLY D  1 184 ? 27.045  52.688  -12.946 1.00 38.98  ?  215  GLY D N   1 
ATOM   12491 C  CA  . GLY D  1 184 ? 26.099  53.323  -12.057 1.00 41.11  ?  215  GLY D CA  1 
ATOM   12492 C  C   . GLY D  1 184 ? 26.310  54.801  -11.799 1.00 41.08  ?  215  GLY D C   1 
ATOM   12493 O  O   . GLY D  1 184 ? 25.459  55.421  -11.147 1.00 46.15  ?  215  GLY D O   1 
ATOM   12494 N  N   . LYS D  1 185 ? 27.396  55.386  -12.287 1.00 41.02  ?  216  LYS D N   1 
ATOM   12495 C  CA  . LYS D  1 185 ? 27.722  56.791  -12.094 1.00 42.10  ?  216  LYS D CA  1 
ATOM   12496 C  C   . LYS D  1 185 ? 27.592  57.550  -13.411 1.00 42.48  ?  216  LYS D C   1 
ATOM   12497 O  O   . LYS D  1 185 ? 27.570  56.938  -14.481 1.00 41.89  ?  216  LYS D O   1 
ATOM   12498 C  CB  . LYS D  1 185 ? 29.146  56.950  -11.536 1.00 42.00  ?  216  LYS D CB  1 
ATOM   12499 C  CG  . LYS D  1 185 ? 29.392  56.224  -10.204 1.00 44.32  ?  216  LYS D CG  1 
ATOM   12500 C  CD  . LYS D  1 185 ? 30.800  55.611  -10.107 1.00 54.80  ?  216  LYS D CD  1 
ATOM   12501 C  CE  . LYS D  1 185 ? 30.868  54.185  -10.658 1.00 57.49  ?  216  LYS D CE  1 
ATOM   12502 N  NZ  . LYS D  1 185 ? 30.521  53.135  -9.631  1.00 57.60  ?  216  LYS D NZ  1 
ATOM   12503 N  N   . PRO D  1 186 ? 27.490  58.884  -13.375 1.00 45.72  ?  217  PRO D N   1 
ATOM   12504 C  CA  . PRO D  1 186 ? 27.349  59.649  -14.625 1.00 40.44  ?  217  PRO D CA  1 
ATOM   12505 C  C   . PRO D  1 186 ? 28.528  59.435  -15.567 1.00 43.25  ?  217  PRO D C   1 
ATOM   12506 O  O   . PRO D  1 186 ? 29.694  59.459  -15.157 1.00 41.68  ?  217  PRO D O   1 
ATOM   12507 C  CB  . PRO D  1 186 ? 27.273  61.105  -14.144 1.00 42.64  ?  217  PRO D CB  1 
ATOM   12508 C  CG  . PRO D  1 186 ? 27.835  61.091  -12.769 1.00 44.49  ?  217  PRO D CG  1 
ATOM   12509 C  CD  . PRO D  1 186 ? 27.420  59.770  -12.199 1.00 46.68  ?  217  PRO D CD  1 
ATOM   12510 N  N   . ALA D  1 187 ? 28.209  59.219  -16.846 1.00 35.56  ?  218  ALA D N   1 
ATOM   12511 C  CA  . ALA D  1 187 ? 29.247  58.977  -17.841 1.00 39.89  ?  218  ALA D CA  1 
ATOM   12512 C  C   . ALA D  1 187 ? 30.032  60.240  -18.170 1.00 38.18  ?  218  ALA D C   1 
ATOM   12513 O  O   . ALA D  1 187 ? 31.213  60.150  -18.525 1.00 39.82  ?  218  ALA D O   1 
ATOM   12514 C  CB  . ALA D  1 187 ? 28.633  58.407  -19.129 1.00 37.67  ?  218  ALA D CB  1 
ATOM   12515 N  N   . ASN D  1 188 ? 29.387  61.411  -18.098 1.00 37.81  ?  219  ASN D N   1 
ATOM   12516 C  CA  . ASN D  1 188 ? 29.971  62.675  -18.569 1.00 39.25  ?  219  ASN D CA  1 
ATOM   12517 C  C   . ASN D  1 188 ? 30.565  62.526  -19.971 1.00 39.65  ?  219  ASN D C   1 
ATOM   12518 O  O   . ASN D  1 188 ? 31.693  62.940  -20.245 1.00 38.75  ?  219  ASN D O   1 
ATOM   12519 C  CB  . ASN D  1 188 ? 31.026  63.194  -17.581 1.00 41.54  ?  219  ASN D CB  1 
ATOM   12520 C  CG  . ASN D  1 188 ? 30.468  63.383  -16.196 1.00 42.74  ?  219  ASN D CG  1 
ATOM   12521 O  OD1 . ASN D  1 188 ? 29.381  63.923  -16.029 1.00 43.42  ?  219  ASN D OD1 1 
ATOM   12522 N  ND2 . ASN D  1 188 ? 31.192  62.900  -15.190 1.00 51.26  ?  219  ASN D ND2 1 
ATOM   12523 N  N   . GLU D  1 189 ? 29.784  61.926  -20.879 1.00 36.60  ?  220  GLU D N   1 
ATOM   12524 C  CA  . GLU D  1 189 ? 30.252  61.736  -22.244 1.00 32.04  ?  220  GLU D CA  1 
ATOM   12525 C  C   . GLU D  1 189 ? 30.509  63.086  -22.900 1.00 35.61  ?  220  GLU D C   1 
ATOM   12526 O  O   . GLU D  1 189 ? 29.799  64.061  -22.650 1.00 37.94  ?  220  GLU D O   1 
ATOM   12527 C  CB  . GLU D  1 189 ? 29.216  60.943  -23.058 1.00 37.50  ?  220  GLU D CB  1 
ATOM   12528 C  CG  . GLU D  1 189 ? 29.608  60.670  -24.511 1.00 33.16  ?  220  GLU D CG  1 
ATOM   12529 C  CD  . GLU D  1 189 ? 30.963  60.000  -24.635 1.00 38.14  ?  220  GLU D CD  1 
ATOM   12530 O  OE1 . GLU D  1 189 ? 31.111  58.825  -24.224 1.00 39.10  ?  220  GLU D OE1 1 
ATOM   12531 O  OE2 . GLU D  1 189 ? 31.891  60.650  -25.145 1.00 38.09  -1 220  GLU D OE2 1 
ATOM   12532 N  N   . THR D  1 190 ? 31.526  63.141  -23.757 1.00 36.68  ?  221  THR D N   1 
ATOM   12533 C  CA  . THR D  1 190 ? 31.851  64.365  -24.471 1.00 41.69  ?  221  THR D CA  1 
ATOM   12534 C  C   . THR D  1 190 ? 31.867  64.196  -25.974 1.00 39.45  ?  221  THR D C   1 
ATOM   12535 O  O   . THR D  1 190 ? 31.901  65.203  -26.686 1.00 44.91  ?  221  THR D O   1 
ATOM   12536 C  CB  . THR D  1 190 ? 33.226  64.908  -24.046 1.00 40.52  ?  221  THR D CB  1 
ATOM   12537 O  OG1 . THR D  1 190 ? 34.222  63.905  -24.290 1.00 45.85  ?  221  THR D OG1 1 
ATOM   12538 C  CG2 . THR D  1 190 ? 33.224  65.276  -22.582 1.00 41.18  ?  221  THR D CG2 1 
ATOM   12539 N  N   . GLU D  1 191 ? 31.869  62.967  -26.474 1.00 37.78  ?  222  GLU D N   1 
ATOM   12540 C  CA  . GLU D  1 191 ? 31.961  62.690  -27.896 1.00 38.48  ?  222  GLU D CA  1 
ATOM   12541 C  C   . GLU D  1 191 ? 30.633  62.155  -28.417 1.00 37.93  ?  222  GLU D C   1 
ATOM   12542 O  O   . GLU D  1 191 ? 29.820  61.616  -27.661 1.00 37.83  ?  222  GLU D O   1 
ATOM   12543 C  CB  . GLU D  1 191 ? 33.065  61.666  -28.184 1.00 37.37  ?  222  GLU D CB  1 
ATOM   12544 C  CG  . GLU D  1 191 ? 34.458  62.051  -27.686 1.00 40.79  ?  222  GLU D CG  1 
ATOM   12545 C  CD  . GLU D  1 191 ? 35.516  61.103  -28.225 1.00 43.64  ?  222  GLU D CD  1 
ATOM   12546 O  OE1 . GLU D  1 191 ? 35.647  61.026  -29.466 1.00 42.17  ?  222  GLU D OE1 1 
ATOM   12547 O  OE2 . GLU D  1 191 ? 36.213  60.444  -27.413 1.00 45.09  -1 222  GLU D OE2 1 
ATOM   12548 N  N   . TYR D  1 192 ? 30.418  62.335  -29.721 1.00 34.17  ?  223  TYR D N   1 
ATOM   12549 C  CA  . TYR D  1 192 ? 29.437  61.554  -30.470 1.00 36.52  ?  223  TYR D CA  1 
ATOM   12550 C  C   . TYR D  1 192 ? 29.479  60.112  -29.975 1.00 36.35  ?  223  TYR D C   1 
ATOM   12551 O  O   . TYR D  1 192 ? 30.553  59.497  -29.940 1.00 36.34  ?  223  TYR D O   1 
ATOM   12552 C  CB  . TYR D  1 192 ? 29.794  61.630  -31.959 1.00 35.11  ?  223  TYR D CB  1 
ATOM   12553 C  CG  . TYR D  1 192 ? 28.880  60.892  -32.930 1.00 32.85  ?  223  TYR D CG  1 
ATOM   12554 C  CD1 . TYR D  1 192 ? 27.581  61.324  -33.175 1.00 33.59  ?  223  TYR D CD1 1 
ATOM   12555 C  CD2 . TYR D  1 192 ? 29.340  59.770  -33.606 1.00 33.52  ?  223  TYR D CD2 1 
ATOM   12556 C  CE1 . TYR D  1 192 ? 26.758  60.640  -34.078 1.00 34.91  ?  223  TYR D CE1 1 
ATOM   12557 C  CE2 . TYR D  1 192 ? 28.533  59.081  -34.499 1.00 35.32  ?  223  TYR D CE2 1 
ATOM   12558 C  CZ  . TYR D  1 192 ? 27.259  59.520  -34.738 1.00 31.54  ?  223  TYR D CZ  1 
ATOM   12559 O  OH  . TYR D  1 192 ? 26.476  58.805  -35.612 1.00 32.86  ?  223  TYR D OH  1 
ATOM   12560 N  N   . ILE D  1 193 ? 28.335  59.585  -29.513 1.00 36.53  ?  224  ILE D N   1 
ATOM   12561 C  CA  . ILE D  1 193 ? 28.421  58.452  -28.587 1.00 33.40  ?  224  ILE D CA  1 
ATOM   12562 C  C   . ILE D  1 193 ? 29.000  57.221  -29.263 1.00 34.24  ?  224  ILE D C   1 
ATOM   12563 O  O   . ILE D  1 193 ? 29.605  56.376  -28.593 1.00 33.30  ?  224  ILE D O   1 
ATOM   12564 C  CB  . ILE D  1 193 ? 27.069  58.148  -27.909 1.00 34.60  ?  224  ILE D CB  1 
ATOM   12565 C  CG1 . ILE D  1 193 ? 26.022  57.586  -28.897 1.00 34.93  ?  224  ILE D CG1 1 
ATOM   12566 C  CG2 . ILE D  1 193 ? 26.565  59.382  -27.161 1.00 30.73  ?  224  ILE D CG2 1 
ATOM   12567 C  CD1 . ILE D  1 193 ? 24.679  57.309  -28.221 1.00 32.63  ?  224  ILE D CD1 1 
ATOM   12568 N  N   . THR D  1 194 ? 28.873  57.107  -30.585 1.00 31.66  ?  225  THR D N   1 
ATOM   12569 C  CA  . THR D  1 194 ? 29.546  56.008  -31.273 1.00 32.63  ?  225  THR D CA  1 
ATOM   12570 C  C   . THR D  1 194 ? 31.047  56.082  -31.048 1.00 34.95  ?  225  THR D C   1 
ATOM   12571 O  O   . THR D  1 194 ? 31.695  55.057  -30.796 1.00 34.64  ?  225  THR D O   1 
ATOM   12572 C  CB  . THR D  1 194 ? 29.234  56.024  -32.767 1.00 31.06  ?  225  THR D CB  1 
ATOM   12573 O  OG1 . THR D  1 194 ? 27.827  55.810  -32.971 1.00 33.88  ?  225  THR D OG1 1 
ATOM   12574 C  CG2 . THR D  1 194 ? 30.042  54.948  -33.518 1.00 31.10  ?  225  THR D CG2 1 
ATOM   12575 N  N   . ASP D  1 195 ? 31.615  57.293  -31.114 1.00 33.56  ?  226  ASP D N   1 
ATOM   12576 C  CA  . ASP D  1 195 ? 33.046  57.449  -30.865 1.00 32.36  ?  226  ASP D CA  1 
ATOM   12577 C  C   . ASP D  1 195 ? 33.375  57.174  -29.409 1.00 32.64  ?  226  ASP D C   1 
ATOM   12578 O  O   . ASP D  1 195 ? 34.427  56.597  -29.106 1.00 36.45  ?  226  ASP D O   1 
ATOM   12579 C  CB  . ASP D  1 195 ? 33.522  58.856  -31.252 1.00 35.35  ?  226  ASP D CB  1 
ATOM   12580 C  CG  . ASP D  1 195 ? 33.545  59.079  -32.761 1.00 38.52  ?  226  ASP D CG  1 
ATOM   12581 O  OD1 . ASP D  1 195 ? 33.466  58.095  -33.528 1.00 36.45  ?  226  ASP D OD1 1 
ATOM   12582 O  OD2 . ASP D  1 195 ? 33.663  60.246  -33.183 1.00 39.44  -1 226  ASP D OD2 1 
ATOM   12583 N  N   . GLY D  1 196 ? 32.504  57.599  -28.489 1.00 33.55  ?  227  GLY D N   1 
ATOM   12584 C  CA  . GLY D  1 196 ? 32.751  57.318  -27.084 1.00 36.31  ?  227  GLY D CA  1 
ATOM   12585 C  C   . GLY D  1 196 ? 32.724  55.831  -26.786 1.00 38.34  ?  227  GLY D C   1 
ATOM   12586 O  O   . GLY D  1 196 ? 33.543  55.322  -26.011 1.00 31.61  ?  227  GLY D O   1 
ATOM   12587 N  N   . PHE D  1 197 ? 31.776  55.112  -27.392 1.00 28.86  ?  228  PHE D N   1 
ATOM   12588 C  CA  . PHE D  1 197 ? 31.692  53.676  -27.155 1.00 33.37  ?  228  PHE D CA  1 
ATOM   12589 C  C   . PHE D  1 197 ? 32.949  52.983  -27.647 1.00 29.88  ?  228  PHE D C   1 
ATOM   12590 O  O   . PHE D  1 197 ? 33.484  52.096  -26.971 1.00 31.82  ?  228  PHE D O   1 
ATOM   12591 C  CB  . PHE D  1 197 ? 30.445  53.091  -27.840 1.00 30.29  ?  228  PHE D CB  1 
ATOM   12592 C  CG  . PHE D  1 197 ? 29.147  53.584  -27.265 1.00 33.96  ?  228  PHE D CG  1 
ATOM   12593 C  CD1 . PHE D  1 197 ? 29.060  53.950  -25.938 1.00 34.20  ?  228  PHE D CD1 1 
ATOM   12594 C  CD2 . PHE D  1 197 ? 27.993  53.670  -28.066 1.00 32.93  ?  228  PHE D CD2 1 
ATOM   12595 C  CE1 . PHE D  1 197 ? 27.866  54.404  -25.412 1.00 32.58  ?  228  PHE D CE1 1 
ATOM   12596 C  CE2 . PHE D  1 197 ? 26.800  54.117  -27.547 1.00 30.97  ?  228  PHE D CE2 1 
ATOM   12597 C  CZ  . PHE D  1 197 ? 26.731  54.487  -26.220 1.00 31.68  ?  228  PHE D CZ  1 
ATOM   12598 N  N   . SER D  1 198 ? 33.445  53.390  -28.817 1.00 28.97  ?  229  SER D N   1 
ATOM   12599 C  CA  . SER D  1 198 ? 34.703  52.850  -29.331 1.00 31.54  ?  229  SER D CA  1 
ATOM   12600 C  C   . SER D  1 198 ? 35.866  53.186  -28.410 1.00 33.91  ?  229  SER D C   1 
ATOM   12601 O  O   . SER D  1 198 ? 36.757  52.359  -28.191 1.00 34.34  ?  229  SER D O   1 
ATOM   12602 C  CB  . SER D  1 198 ? 34.972  53.408  -30.724 1.00 32.15  ?  229  SER D CB  1 
ATOM   12603 O  OG  . SER D  1 198 ? 33.837  53.217  -31.576 1.00 34.05  ?  229  SER D OG  1 
ATOM   12604 N  N   . ARG D  1 199 ? 35.888  54.412  -27.890 1.00 32.64  ?  230  ARG D N   1 
ATOM   12605 C  CA  . ARG D  1 199 ? 36.922  54.788  -26.931 1.00 37.42  ?  230  ARG D CA  1 
ATOM   12606 C  C   . ARG D  1 199 ? 36.894  53.861  -25.723 1.00 36.65  ?  230  ARG D C   1 
ATOM   12607 O  O   . ARG D  1 199 ? 37.937  53.371  -25.270 1.00 36.01  ?  230  ARG D O   1 
ATOM   12608 C  CB  . ARG D  1 199 ? 36.727  56.243  -26.507 1.00 36.32  ?  230  ARG D CB  1 
ATOM   12609 C  CG  . ARG D  1 199 ? 37.774  56.755  -25.478 1.00 34.25  ?  230  ARG D CG  1 
ATOM   12610 C  CD  . ARG D  1 199 ? 37.229  58.008  -24.784 1.00 35.36  ?  230  ARG D CD  1 
ATOM   12611 N  NE  . ARG D  1 199 ? 36.005  57.716  -24.038 1.00 43.04  ?  230  ARG D NE  1 
ATOM   12612 C  CZ  . ARG D  1 199 ? 34.845  58.352  -24.192 1.00 38.89  ?  230  ARG D CZ  1 
ATOM   12613 N  NH1 . ARG D  1 199 ? 34.699  59.329  -25.072 1.00 36.85  ?  230  ARG D NH1 1 
ATOM   12614 N  NH2 . ARG D  1 199 ? 33.807  58.000  -23.437 1.00 32.52  ?  230  ARG D NH2 1 
ATOM   12615 N  N   . GLU D  1 200 ? 35.698  53.608  -25.189 1.00 33.60  ?  231  GLU D N   1 
ATOM   12616 C  CA  . GLU D  1 200 ? 35.579  52.754  -24.015 1.00 33.61  ?  231  GLU D CA  1 
ATOM   12617 C  C   . GLU D  1 200 ? 35.992  51.320  -24.323 1.00 34.52  ?  231  GLU D C   1 
ATOM   12618 O  O   . GLU D  1 200 ? 36.535  50.632  -23.451 1.00 35.47  ?  231  GLU D O   1 
ATOM   12619 C  CB  . GLU D  1 200 ? 34.152  52.797  -23.464 1.00 32.02  ?  231  GLU D CB  1 
ATOM   12620 C  CG  . GLU D  1 200 ? 33.727  54.159  -22.907 1.00 33.46  ?  231  GLU D CG  1 
ATOM   12621 C  CD  . GLU D  1 200 ? 34.658  54.669  -21.797 1.00 39.72  ?  231  GLU D CD  1 
ATOM   12622 O  OE1 . GLU D  1 200 ? 34.977  53.902  -20.868 1.00 34.82  ?  231  GLU D OE1 1 
ATOM   12623 O  OE2 . GLU D  1 200 ? 35.076  55.846  -21.868 1.00 40.61  -1 231  GLU D OE2 1 
ATOM   12624 N  N   . ALA D  1 201 ? 35.754  50.852  -25.546 1.00 31.65  ?  232  ALA D N   1 
ATOM   12625 C  CA  . ALA D  1 201 ? 36.216  49.520  -25.917 1.00 36.01  ?  232  ALA D CA  1 
ATOM   12626 C  C   . ALA D  1 201 ? 37.736  49.459  -25.897 1.00 37.06  ?  232  ALA D C   1 
ATOM   12627 O  O   . ALA D  1 201 ? 38.327  48.514  -25.361 1.00 31.98  ?  232  ALA D O   1 
ATOM   12628 C  CB  . ALA D  1 201 ? 35.675  49.138  -27.292 1.00 30.67  ?  232  ALA D CB  1 
ATOM   12629 N  N   . ILE D  1 202 ? 38.382  50.477  -26.467 1.00 36.04  ?  233  ILE D N   1 
ATOM   12630 C  CA  . ILE D  1 202 ? 39.839  50.555  -26.440 1.00 33.69  ?  233  ILE D CA  1 
ATOM   12631 C  C   . ILE D  1 202 ? 40.343  50.561  -25.005 1.00 38.89  ?  233  ILE D C   1 
ATOM   12632 O  O   . ILE D  1 202 ? 41.295  49.847  -24.665 1.00 39.01  ?  233  ILE D O   1 
ATOM   12633 C  CB  . ILE D  1 202 ? 40.310  51.801  -27.212 1.00 36.84  ?  233  ILE D CB  1 
ATOM   12634 C  CG1 . ILE D  1 202 ? 40.122  51.579  -28.711 1.00 35.34  ?  233  ILE D CG1 1 
ATOM   12635 C  CG2 . ILE D  1 202 ? 41.761  52.160  -26.866 1.00 40.69  ?  233  ILE D CG2 1 
ATOM   12636 C  CD1 . ILE D  1 202 ? 40.208  52.875  -29.511 1.00 35.25  ?  233  ILE D CD1 1 
ATOM   12637 N  N   . LYS D  1 203 ? 39.696  51.349  -24.140 1.00 37.86  ?  234  LYS D N   1 
ATOM   12638 C  CA  . LYS D  1 203 ? 40.080  51.414  -22.734 1.00 38.92  ?  234  LYS D CA  1 
ATOM   12639 C  C   . LYS D  1 203 ? 39.974  50.048  -22.067 1.00 41.71  ?  234  LYS D C   1 
ATOM   12640 O  O   . LYS D  1 203 ? 40.873  49.629  -21.329 1.00 36.12  ?  234  LYS D O   1 
ATOM   12641 C  CB  . LYS D  1 203 ? 39.196  52.424  -22.000 1.00 45.07  ?  234  LYS D CB  1 
ATOM   12642 C  CG  . LYS D  1 203 ? 39.456  52.483  -20.488 1.00 45.95  ?  234  LYS D CG  1 
ATOM   12643 C  CD  . LYS D  1 203 ? 38.556  53.488  -19.783 1.00 46.92  ?  234  LYS D CD  1 
ATOM   12644 C  CE  . LYS D  1 203 ? 39.137  53.869  -18.419 1.00 43.98  ?  234  LYS D CE  1 
ATOM   12645 N  NZ  . LYS D  1 203 ? 38.205  54.697  -17.586 1.00 43.18  ?  234  LYS D NZ  1 
ATOM   12646 N  N   . ASN D  1 204 ? 38.878  49.338  -22.312 1.00 33.85  ?  235  ASN D N   1 
ATOM   12647 C  CA  . ASN D  1 204 ? 38.665  48.063  -21.632 1.00 35.55  ?  235  ASN D CA  1 
ATOM   12648 C  C   . ASN D  1 204 ? 39.579  46.976  -22.182 1.00 34.33  ?  235  ASN D C   1 
ATOM   12649 O  O   . ASN D  1 204 ? 39.964  46.052  -21.449 1.00 37.21  ?  235  ASN D O   1 
ATOM   12650 C  CB  . ASN D  1 204 ? 37.184  47.667  -21.731 1.00 32.34  ?  235  ASN D CB  1 
ATOM   12651 C  CG  . ASN D  1 204 ? 36.329  48.384  -20.696 1.00 39.88  ?  235  ASN D CG  1 
ATOM   12652 O  OD1 . ASN D  1 204 ? 36.109  47.874  -19.600 1.00 46.40  ?  235  ASN D OD1 1 
ATOM   12653 N  ND2 . ASN D  1 204 ? 35.877  49.579  -21.023 1.00 41.51  ?  235  ASN D ND2 1 
ATOM   12654 N  N   . ILE D  1 205 ? 39.944  47.072  -23.458 1.00 32.06  ?  236  ILE D N   1 
ATOM   12655 C  CA  . ILE D  1 205 ? 40.942  46.171  -24.018 1.00 32.88  ?  236  ILE D CA  1 
ATOM   12656 C  C   . ILE D  1 205 ? 42.282  46.383  -23.323 1.00 38.04  ?  236  ILE D C   1 
ATOM   12657 O  O   . ILE D  1 205 ? 43.030  45.431  -23.065 1.00 37.61  ?  236  ILE D O   1 
ATOM   12658 C  CB  . ILE D  1 205 ? 41.042  46.390  -25.537 1.00 33.59  ?  236  ILE D CB  1 
ATOM   12659 C  CG1 . ILE D  1 205 ? 39.840  45.754  -26.250 1.00 33.51  ?  236  ILE D CG1 1 
ATOM   12660 C  CG2 . ILE D  1 205 ? 42.353  45.834  -26.102 1.00 33.83  ?  236  ILE D CG2 1 
ATOM   12661 C  CD1 . ILE D  1 205 ? 39.643  46.273  -27.657 1.00 31.96  ?  236  ILE D CD1 1 
ATOM   12662 N  N   . LYS D  1 206 ? 42.604  47.636  -23.001 1.00 34.42  ?  237  LYS D N   1 
ATOM   12663 C  CA  . LYS D  1 206 ? 43.888  47.909  -22.359 1.00 37.56  ?  237  LYS D CA  1 
ATOM   12664 C  C   . LYS D  1 206 ? 43.881  47.471  -20.899 1.00 36.07  ?  237  LYS D C   1 
ATOM   12665 O  O   . LYS D  1 206 ? 44.922  47.064  -20.367 1.00 40.81  ?  237  LYS D O   1 
ATOM   12666 C  CB  . LYS D  1 206 ? 44.222  49.395  -22.474 1.00 34.80  ?  237  LYS D CB  1 
ATOM   12667 C  CG  . LYS D  1 206 ? 44.704  49.805  -23.845 1.00 39.58  ?  237  LYS D CG  1 
ATOM   12668 C  CD  . LYS D  1 206 ? 44.570  51.300  -24.017 1.00 44.00  ?  237  LYS D CD  1 
ATOM   12669 C  CE  . LYS D  1 206 ? 45.364  51.803  -25.203 1.00 44.36  ?  237  LYS D CE  1 
ATOM   12670 N  NZ  . LYS D  1 206 ? 45.408  53.301  -25.196 1.00 50.93  ?  237  LYS D NZ  1 
ATOM   12671 N  N   . ILE D  1 207 ? 42.727  47.573  -20.237 1.00 34.12  ?  238  ILE D N   1 
ATOM   12672 C  CA  . ILE D  1 207 ? 42.583  47.088  -18.872 1.00 38.18  ?  238  ILE D CA  1 
ATOM   12673 C  C   . ILE D  1 207 ? 42.806  45.585  -18.831 1.00 42.17  ?  238  ILE D C   1 
ATOM   12674 O  O   . ILE D  1 207 ? 43.519  45.067  -17.963 1.00 40.52  ?  238  ILE D O   1 
ATOM   12675 C  CB  . ILE D  1 207 ? 41.202  47.477  -18.317 1.00 36.85  ?  238  ILE D CB  1 
ATOM   12676 C  CG1 . ILE D  1 207 ? 41.130  48.987  -18.083 1.00 38.26  ?  238  ILE D CG1 1 
ATOM   12677 C  CG2 . ILE D  1 207 ? 40.903  46.744  -17.030 1.00 37.20  ?  238  ILE D CG2 1 
ATOM   12678 C  CD1 . ILE D  1 207 ? 39.736  49.482  -17.775 1.00 39.76  ?  238  ILE D CD1 1 
ATOM   12679 N  N   . ALA D  1 208 ? 42.215  44.863  -19.786 1.00 34.36  ?  239  ALA D N   1 
ATOM   12680 C  CA  . ALA D  1 208 ? 42.409  43.419  -19.832 1.00 37.47  ?  239  ALA D CA  1 
ATOM   12681 C  C   . ALA D  1 208 ? 43.867  43.072  -20.090 1.00 38.69  ?  239  ALA D C   1 
ATOM   12682 O  O   . ALA D  1 208 ? 44.405  42.129  -19.495 1.00 38.50  ?  239  ALA D O   1 
ATOM   12683 C  CB  . ALA D  1 208 ? 41.504  42.791  -20.897 1.00 37.42  ?  239  ALA D CB  1 
ATOM   12684 N  N   . ALA D  1 209 ? 44.532  43.829  -20.965 1.00 36.78  ?  240  ALA D N   1 
ATOM   12685 C  CA  . ALA D  1 209 ? 45.946  43.572  -21.210 1.00 39.15  ?  240  ALA D CA  1 
ATOM   12686 C  C   . ALA D  1 209 ? 46.765  43.801  -19.945 1.00 37.00  ?  240  ALA D C   1 
ATOM   12687 O  O   . ALA D  1 209 ? 47.752  43.100  -19.698 1.00 41.32  ?  240  ALA D O   1 
ATOM   12688 C  CB  . ALA D  1 209 ? 46.458  44.453  -22.351 1.00 36.42  ?  240  ALA D CB  1 
ATOM   12689 N  N   . ALA D  1 210 ? 46.357  44.761  -19.119 1.00 36.55  ?  241  ALA D N   1 
ATOM   12690 C  CA  . ALA D  1 210 ? 47.117  45.055  -17.914 1.00 38.29  ?  241  ALA D CA  1 
ATOM   12691 C  C   . ALA D  1 210 ? 46.869  44.004  -16.838 1.00 43.60  ?  241  ALA D C   1 
ATOM   12692 O  O   . ALA D  1 210 ? 47.787  43.646  -16.087 1.00 38.28  ?  241  ALA D O   1 
ATOM   12693 C  CB  . ALA D  1 210 ? 46.766  46.453  -17.410 1.00 37.86  ?  241  ALA D CB  1 
ATOM   12694 N  N   . LYS D  1 211 ? 45.638  43.497  -16.753 1.00 37.18  ?  242  LYS D N   1 
ATOM   12695 C  CA  . LYS D  1 211 ? 45.317  42.422  -15.824 1.00 35.26  ?  242  LYS D CA  1 
ATOM   12696 C  C   . LYS D  1 211 ? 45.842  41.069  -16.278 1.00 39.13  ?  242  LYS D C   1 
ATOM   12697 O  O   . LYS D  1 211 ? 45.807  40.124  -15.481 1.00 47.43  ?  242  LYS D O   1 
ATOM   12698 C  CB  . LYS D  1 211 ? 43.798  42.310  -15.633 1.00 37.71  ?  242  LYS D CB  1 
ATOM   12699 C  CG  . LYS D  1 211 ? 43.126  43.568  -15.137 1.00 36.66  ?  242  LYS D CG  1 
ATOM   12700 C  CD  . LYS D  1 211 ? 41.624  43.461  -15.309 1.00 45.27  ?  242  LYS D CD  1 
ATOM   12701 C  CE  . LYS D  1 211 ? 40.931  43.324  -13.979 1.00 48.80  ?  242  LYS D CE  1 
ATOM   12702 N  NZ  . LYS D  1 211 ? 40.545  44.662  -13.490 1.00 51.04  ?  242  LYS D NZ  1 
ATOM   12703 N  N   . LYS D  1 212 ? 46.304  40.947  -17.523 1.00 34.44  ?  243  LYS D N   1 
ATOM   12704 C  CA  . LYS D  1 212 ? 46.718  39.667  -18.091 1.00 34.51  ?  243  LYS D CA  1 
ATOM   12705 C  C   . LYS D  1 212 ? 45.617  38.625  -17.918 1.00 41.16  ?  243  LYS D C   1 
ATOM   12706 O  O   . LYS D  1 212 ? 45.831  37.519  -17.414 1.00 35.96  ?  243  LYS D O   1 
ATOM   12707 C  CB  . LYS D  1 212 ? 48.042  39.195  -17.478 1.00 43.34  ?  243  LYS D CB  1 
ATOM   12708 N  N   . GLN D  1 213 ? 44.414  38.994  -18.366 1.00 39.71  ?  244  GLN D N   1 
ATOM   12709 C  CA  . GLN D  1 213 ? 43.209  38.222  -18.134 1.00 40.49  ?  244  GLN D CA  1 
ATOM   12710 C  C   . GLN D  1 213 ? 42.442  38.202  -19.455 1.00 37.80  ?  244  GLN D C   1 
ATOM   12711 O  O   . GLN D  1 213 ? 42.393  39.236  -20.155 1.00 38.57  ?  244  GLN D O   1 
ATOM   12712 C  CB  . GLN D  1 213 ? 42.420  38.891  -17.009 1.00 38.58  ?  244  GLN D CB  1 
ATOM   12713 C  CG  . GLN D  1 213 ? 41.134  38.263  -16.598 1.00 45.89  ?  244  GLN D CG  1 
ATOM   12714 C  CD  . GLN D  1 213 ? 40.533  38.954  -15.379 1.00 44.08  ?  244  GLN D CD  1 
ATOM   12715 O  OE1 . GLN D  1 213 ? 41.010  40.008  -14.949 1.00 45.10  ?  244  GLN D OE1 1 
ATOM   12716 N  NE2 . GLN D  1 213 ? 39.452  38.386  -14.845 1.00 41.66  ?  244  GLN D NE2 1 
ATOM   12717 N  N   . PRO D  1 214 ? 41.912  37.057  -19.879 1.00 37.59  ?  245  PRO D N   1 
ATOM   12718 C  CA  . PRO D  1 214 ? 41.098  37.059  -21.102 1.00 39.69  ?  245  PRO D CA  1 
ATOM   12719 C  C   . PRO D  1 214 ? 39.919  37.993  -20.909 1.00 34.40  ?  245  PRO D C   1 
ATOM   12720 O  O   . PRO D  1 214 ? 39.377  38.108  -19.806 1.00 35.71  ?  245  PRO D O   1 
ATOM   12721 C  CB  . PRO D  1 214 ? 40.646  35.600  -21.260 1.00 39.21  ?  245  PRO D CB  1 
ATOM   12722 C  CG  . PRO D  1 214 ? 41.155  34.858  -20.085 1.00 44.38  ?  245  PRO D CG  1 
ATOM   12723 C  CD  . PRO D  1 214 ? 42.076  35.716  -19.295 1.00 39.02  ?  245  PRO D CD  1 
ATOM   12724 N  N   . PHE D  1 215 ? 39.520  38.673  -21.984 1.00 36.01  ?  246  PHE D N   1 
ATOM   12725 C  CA  . PHE D  1 215 ? 38.400  39.600  -21.904 1.00 34.70  ?  246  PHE D CA  1 
ATOM   12726 C  C   . PHE D  1 215 ? 37.207  39.070  -22.686 1.00 32.08  ?  246  PHE D C   1 
ATOM   12727 O  O   . PHE D  1 215 ? 37.354  38.299  -23.637 1.00 30.29  ?  246  PHE D O   1 
ATOM   12728 C  CB  . PHE D  1 215 ? 38.783  41.020  -22.381 1.00 34.12  ?  246  PHE D CB  1 
ATOM   12729 C  CG  . PHE D  1 215 ? 39.022  41.165  -23.881 1.00 32.02  ?  246  PHE D CG  1 
ATOM   12730 C  CD1 . PHE D  1 215 ? 37.969  41.096  -24.801 1.00 33.43  ?  246  PHE D CD1 1 
ATOM   12731 C  CD2 . PHE D  1 215 ? 40.288  41.453  -24.360 1.00 35.80  ?  246  PHE D CD2 1 
ATOM   12732 C  CE1 . PHE D  1 215 ? 38.195  41.243  -26.143 1.00 32.10  ?  246  PHE D CE1 1 
ATOM   12733 C  CE2 . PHE D  1 215 ? 40.526  41.617  -25.718 1.00 33.93  ?  246  PHE D CE2 1 
ATOM   12734 C  CZ  . PHE D  1 215 ? 39.470  41.509  -26.615 1.00 38.17  ?  246  PHE D CZ  1 
ATOM   12735 N  N   . PHE D  1 216 ? 36.022  39.449  -22.228 1.00 32.36  ?  247  PHE D N   1 
ATOM   12736 C  CA  . PHE D  1 216 ? 34.794  39.330  -23.010 1.00 31.60  ?  247  PHE D CA  1 
ATOM   12737 C  C   . PHE D  1 216 ? 34.187  40.721  -23.049 1.00 33.77  ?  247  PHE D C   1 
ATOM   12738 O  O   . PHE D  1 216 ? 33.851  41.273  -21.998 1.00 34.85  ?  247  PHE D O   1 
ATOM   12739 C  CB  . PHE D  1 216 ? 33.811  38.323  -22.398 1.00 31.59  ?  247  PHE D CB  1 
ATOM   12740 C  CG  . PHE D  1 216 ? 32.431  38.369  -23.015 1.00 35.67  ?  247  PHE D CG  1 
ATOM   12741 C  CD1 . PHE D  1 216 ? 32.197  37.803  -24.248 1.00 31.66  ?  247  PHE D CD1 1 
ATOM   12742 C  CD2 . PHE D  1 216 ? 31.375  38.980  -22.352 1.00 34.65  ?  247  PHE D CD2 1 
ATOM   12743 C  CE1 . PHE D  1 216 ? 30.917  37.843  -24.821 1.00 35.81  ?  247  PHE D CE1 1 
ATOM   12744 C  CE2 . PHE D  1 216 ? 30.102  39.044  -22.920 1.00 35.14  ?  247  PHE D CE2 1 
ATOM   12745 C  CZ  . PHE D  1 216 ? 29.873  38.472  -24.152 1.00 34.22  ?  247  PHE D CZ  1 
ATOM   12746 N  N   . ILE D  1 217 ? 34.095  41.304  -24.243 1.00 32.23  ?  248  ILE D N   1 
ATOM   12747 C  CA  . ILE D  1 217 ? 33.593  42.661  -24.425 1.00 32.05  ?  248  ILE D CA  1 
ATOM   12748 C  C   . ILE D  1 217 ? 32.360  42.584  -25.312 1.00 29.03  ?  248  ILE D C   1 
ATOM   12749 O  O   . ILE D  1 217 ? 32.436  42.099  -26.445 1.00 28.03  ?  248  ILE D O   1 
ATOM   12750 C  CB  . ILE D  1 217 ? 34.640  43.597  -25.047 1.00 34.17  ?  248  ILE D CB  1 
ATOM   12751 C  CG1 . ILE D  1 217 ? 35.833  43.794  -24.106 1.00 31.76  ?  248  ILE D CG1 1 
ATOM   12752 C  CG2 . ILE D  1 217 ? 34.003  44.948  -25.375 1.00 28.83  ?  248  ILE D CG2 1 
ATOM   12753 C  CD1 . ILE D  1 217 ? 36.898  44.737  -24.664 1.00 32.04  ?  248  ILE D CD1 1 
ATOM   12754 N  N   . TYR D  1 218 ? 31.234  43.039  -24.775 1.00 29.13  ?  249  TYR D N   1 
ATOM   12755 C  CA  . TYR D  1 218 ? 29.941  43.094  -25.458 1.00 26.85  ?  249  TYR D CA  1 
ATOM   12756 C  C   . TYR D  1 218 ? 29.750  44.544  -25.884 1.00 24.03  ?  249  TYR D C   1 
ATOM   12757 O  O   . TYR D  1 218 ? 29.292  45.384  -25.113 1.00 28.38  ?  249  TYR D O   1 
ATOM   12758 C  CB  . TYR D  1 218 ? 28.850  42.616  -24.515 1.00 28.73  ?  249  TYR D CB  1 
ATOM   12759 C  CG  . TYR D  1 218 ? 27.434  42.686  -25.040 1.00 29.20  ?  249  TYR D CG  1 
ATOM   12760 C  CD1 . TYR D  1 218 ? 26.954  41.745  -25.938 1.00 27.56  ?  249  TYR D CD1 1 
ATOM   12761 C  CD2 . TYR D  1 218 ? 26.567  43.668  -24.590 1.00 30.41  ?  249  TYR D CD2 1 
ATOM   12762 C  CE1 . TYR D  1 218 ? 25.630  41.786  -26.398 1.00 28.61  ?  249  TYR D CE1 1 
ATOM   12763 C  CE2 . TYR D  1 218 ? 25.262  43.731  -25.035 1.00 30.36  ?  249  TYR D CE2 1 
ATOM   12764 C  CZ  . TYR D  1 218 ? 24.802  42.790  -25.935 1.00 32.93  ?  249  TYR D CZ  1 
ATOM   12765 O  OH  . TYR D  1 218 ? 23.509  42.873  -26.350 1.00 29.74  ?  249  TYR D OH  1 
ATOM   12766 N  N   . LEU D  1 219 ? 30.150  44.843  -27.113 1.00 27.44  ?  250  LEU D N   1 
ATOM   12767 C  CA  . LEU D  1 219 ? 30.158  46.203  -27.648 1.00 25.71  ?  250  LEU D CA  1 
ATOM   12768 C  C   . LEU D  1 219 ? 28.875  46.399  -28.461 1.00 29.14  ?  250  LEU D C   1 
ATOM   12769 O  O   . LEU D  1 219 ? 28.824  46.064  -29.643 1.00 28.91  ?  250  LEU D O   1 
ATOM   12770 C  CB  . LEU D  1 219 ? 31.390  46.415  -28.517 1.00 22.77  ?  250  LEU D CB  1 
ATOM   12771 C  CG  . LEU D  1 219 ? 31.485  47.749  -29.257 1.00 25.36  ?  250  LEU D CG  1 
ATOM   12772 C  CD1 . LEU D  1 219 ? 31.363  48.931  -28.302 1.00 30.67  ?  250  LEU D CD1 1 
ATOM   12773 C  CD2 . LEU D  1 219 ? 32.766  47.815  -30.056 1.00 25.72  ?  250  LEU D CD2 1 
ATOM   12774 N  N   . ALA D  1 220 ? 27.857  46.988  -27.839 1.00 28.33  ?  251  ALA D N   1 
ATOM   12775 C  CA  . ALA D  1 220 ? 26.519  47.093  -28.422 1.00 25.62  ?  251  ALA D CA  1 
ATOM   12776 C  C   . ALA D  1 220 ? 26.272  48.536  -28.879 1.00 26.57  ?  251  ALA D C   1 
ATOM   12777 O  O   . ALA D  1 220 ? 25.644  49.335  -28.180 1.00 30.01  ?  251  ALA D O   1 
ATOM   12778 C  CB  . ALA D  1 220 ? 25.463  46.612  -27.360 1.00 28.09  ?  251  ALA D CB  1 
ATOM   12779 N  N   . TYR D  1 221 ? 26.816  48.883  -30.046 1.00 26.55  ?  252  TYR D N   1 
ATOM   12780 C  CA  . TYR D  1 221 ? 26.540  50.185  -30.647 1.00 31.87  ?  252  TYR D CA  1 
ATOM   12781 C  C   . TYR D  1 221 ? 25.042  50.364  -30.870 1.00 32.72  ?  252  TYR D C   1 
ATOM   12782 O  O   . TYR D  1 221 ? 24.351  49.434  -31.297 1.00 28.43  ?  252  TYR D O   1 
ATOM   12783 C  CB  . TYR D  1 221 ? 27.241  50.320  -32.000 1.00 30.16  ?  252  TYR D CB  1 
ATOM   12784 C  CG  . TYR D  1 221 ? 28.758  50.415  -32.000 1.00 32.77  ?  252  TYR D CG  1 
ATOM   12785 C  CD1 . TYR D  1 221 ? 29.412  51.566  -31.571 1.00 35.02  ?  252  TYR D CD1 1 
ATOM   12786 C  CD2 . TYR D  1 221 ? 29.534  49.379  -32.505 1.00 30.90  ?  252  TYR D CD2 1 
ATOM   12787 C  CE1 . TYR D  1 221 ? 30.817  51.663  -31.602 1.00 29.00  ?  252  TYR D CE1 1 
ATOM   12788 C  CE2 . TYR D  1 221 ? 30.938  49.469  -32.538 1.00 32.47  ?  252  TYR D CE2 1 
ATOM   12789 C  CZ  . TYR D  1 221 ? 31.563  50.614  -32.096 1.00 34.07  ?  252  TYR D CZ  1 
ATOM   12790 O  OH  . TYR D  1 221 ? 32.945  50.696  -32.136 1.00 35.02  ?  252  TYR D OH  1 
ATOM   12791 N  N   . ASN D  1 222 ? 24.530  51.569  -30.597 1.00 30.51  ?  253  ASN D N   1 
ATOM   12792 C  CA  . ASN D  1 222 ? 23.156  51.808  -31.028 1.00 30.16  ?  253  ASN D CA  1 
ATOM   12793 C  C   . ASN D  1 222 ? 23.084  52.221  -32.492 1.00 30.43  ?  253  ASN D C   1 
ATOM   12794 O  O   . ASN D  1 222 ? 22.005  52.151  -33.090 1.00 30.44  ?  253  ASN D O   1 
ATOM   12795 C  CB  . ASN D  1 222 ? 22.460  52.843  -30.120 1.00 28.77  ?  253  ASN D CB  1 
ATOM   12796 C  CG  . ASN D  1 222 ? 23.107  54.232  -30.177 1.00 33.77  ?  253  ASN D CG  1 
ATOM   12797 O  OD1 . ASN D  1 222 ? 24.339  54.367  -30.228 1.00 31.61  ?  253  ASN D OD1 1 
ATOM   12798 N  ND2 . ASN D  1 222 ? 22.269  55.272  -30.149 1.00 29.45  ?  253  ASN D ND2 1 
ATOM   12799 N  N   . ALA D  1 223 ? 24.204  52.586  -33.106 1.00 29.38  ?  254  ALA D N   1 
ATOM   12800 C  CA  . ALA D  1 223 ? 24.197  52.863  -34.528 1.00 31.29  ?  254  ALA D CA  1 
ATOM   12801 C  C   . ALA D  1 223 ? 23.925  51.580  -35.307 1.00 32.29  ?  254  ALA D C   1 
ATOM   12802 O  O   . ALA D  1 223 ? 24.356  50.494  -34.898 1.00 28.89  ?  254  ALA D O   1 
ATOM   12803 C  CB  . ALA D  1 223 ? 25.535  53.448  -34.975 1.00 31.08  ?  254  ALA D CB  1 
ATOM   12804 N  N   . PRO D  1 224 ? 23.224  51.681  -36.447 1.00 31.68  ?  255  PRO D N   1 
ATOM   12805 C  CA  . PRO D  1 224 ? 22.583  52.889  -37.005 1.00 32.03  ?  255  PRO D CA  1 
ATOM   12806 C  C   . PRO D  1 224 ? 21.096  53.002  -36.683 1.00 33.19  ?  255  PRO D C   1 
ATOM   12807 O  O   . PRO D  1 224 ? 20.296  53.404  -37.541 1.00 33.39  ?  255  PRO D O   1 
ATOM   12808 C  CB  . PRO D  1 224 ? 22.803  52.714  -38.505 1.00 31.48  ?  255  PRO D CB  1 
ATOM   12809 C  CG  . PRO D  1 224 ? 22.651  51.201  -38.698 1.00 34.52  ?  255  PRO D CG  1 
ATOM   12810 C  CD  . PRO D  1 224 ? 23.202  50.566  -37.419 1.00 31.13  ?  255  PRO D CD  1 
ATOM   12811 N  N   . HIS D  1 225 ? 20.696  52.640  -35.468 1.00 27.98  ?  256  HIS D N   1 
ATOM   12812 C  CA  . HIS D  1 225 ? 19.323  52.840  -35.025 1.00 32.17  ?  256  HIS D CA  1 
ATOM   12813 C  C   . HIS D  1 225 ? 19.012  54.333  -34.942 1.00 33.25  ?  256  HIS D C   1 
ATOM   12814 O  O   . HIS D  1 225 ? 19.901  55.167  -34.739 1.00 31.54  ?  256  HIS D O   1 
ATOM   12815 C  CB  . HIS D  1 225 ? 19.120  52.142  -33.676 1.00 28.29  ?  256  HIS D CB  1 
ATOM   12816 C  CG  . HIS D  1 225 ? 17.705  52.122  -33.164 1.00 33.29  ?  256  HIS D CG  1 
ATOM   12817 N  ND1 . HIS D  1 225 ? 17.036  53.261  -32.758 1.00 32.18  ?  256  HIS D ND1 1 
ATOM   12818 C  CD2 . HIS D  1 225 ? 16.877  51.086  -32.892 1.00 30.41  ?  256  HIS D CD2 1 
ATOM   12819 C  CE1 . HIS D  1 225 ? 15.843  52.929  -32.295 1.00 34.79  ?  256  HIS D CE1 1 
ATOM   12820 N  NE2 . HIS D  1 225 ? 15.722  51.615  -32.362 1.00 34.24  ?  256  HIS D NE2 1 
ATOM   12821 N  N   . VAL D  1 226 ? 17.745  54.669  -35.172 1.00 31.11  ?  257  VAL D N   1 
ATOM   12822 C  CA  . VAL D  1 226 ? 17.283  56.057  -35.144 1.00 31.65  ?  257  VAL D CA  1 
ATOM   12823 C  C   . VAL D  1 226 ? 17.566  56.624  -33.761 1.00 32.13  ?  257  VAL D C   1 
ATOM   12824 O  O   . VAL D  1 226 ? 17.585  55.862  -32.785 1.00 31.01  ?  257  VAL D O   1 
ATOM   12825 C  CB  . VAL D  1 226 ? 15.788  56.169  -35.487 1.00 35.54  ?  257  VAL D CB  1 
ATOM   12826 C  CG1 . VAL D  1 226 ? 15.564  55.950  -36.983 1.00 32.94  ?  257  VAL D CG1 1 
ATOM   12827 C  CG2 . VAL D  1 226 ? 14.943  55.212  -34.631 1.00 33.56  ?  257  VAL D CG2 1 
ATOM   12828 N  N   . PRO D  1 227 ? 17.722  57.949  -33.611 1.00 34.69  ?  258  PRO D N   1 
ATOM   12829 C  CA  . PRO D  1 227 ? 17.555  58.997  -34.633 1.00 33.76  ?  258  PRO D CA  1 
ATOM   12830 C  C   . PRO D  1 227 ? 18.747  59.037  -35.571 1.00 34.90  ?  258  PRO D C   1 
ATOM   12831 O  O   . PRO D  1 227 ? 19.865  58.757  -35.157 1.00 32.92  ?  258  PRO D O   1 
ATOM   12832 C  CB  . PRO D  1 227 ? 17.413  60.270  -33.787 1.00 35.88  ?  258  PRO D CB  1 
ATOM   12833 C  CG  . PRO D  1 227 ? 18.321  59.995  -32.607 1.00 33.85  ?  258  PRO D CG  1 
ATOM   12834 C  CD  . PRO D  1 227 ? 18.076  58.524  -32.300 1.00 34.89  ?  258  PRO D CD  1 
ATOM   12835 N  N   . LEU D  1 228 ? 18.528  59.357  -36.842 1.00 28.42  ?  259  LEU D N   1 
ATOM   12836 C  CA  . LEU D  1 228 ? 19.587  59.390  -37.845 1.00 33.66  ?  259  LEU D CA  1 
ATOM   12837 C  C   . LEU D  1 228 ? 20.404  60.654  -37.607 1.00 38.87  ?  259  LEU D C   1 
ATOM   12838 O  O   . LEU D  1 228 ? 20.105  61.723  -38.145 1.00 39.13  ?  259  LEU D O   1 
ATOM   12839 C  CB  . LEU D  1 228 ? 18.993  59.348  -39.248 1.00 32.23  ?  259  LEU D CB  1 
ATOM   12840 C  CG  . LEU D  1 228 ? 18.260  58.067  -39.692 1.00 30.16  ?  259  LEU D CG  1 
ATOM   12841 C  CD1 . LEU D  1 228 ? 18.006  58.086  -41.203 1.00 35.81  ?  259  LEU D CD1 1 
ATOM   12842 C  CD2 . LEU D  1 228 ? 19.010  56.795  -39.306 1.00 32.56  ?  259  LEU D CD2 1 
ATOM   12843 N  N   . GLN D  1 229 ? 21.448  60.528  -36.783 1.00 35.57  ?  260  GLN D N   1 
ATOM   12844 C  CA  . GLN D  1 229 ? 22.291  61.646  -36.369 1.00 37.73  ?  260  GLN D CA  1 
ATOM   12845 C  C   . GLN D  1 229 ? 23.746  61.258  -36.584 1.00 37.96  ?  260  GLN D C   1 
ATOM   12846 O  O   . GLN D  1 229 ? 24.185  60.216  -36.086 1.00 34.26  ?  260  GLN D O   1 
ATOM   12847 C  CB  . GLN D  1 229 ? 22.043  62.017  -34.897 1.00 32.64  ?  260  GLN D CB  1 
ATOM   12848 C  CG  . GLN D  1 229 ? 20.689  62.648  -34.638 1.00 35.87  ?  260  GLN D CG  1 
ATOM   12849 C  CD  . GLN D  1 229 ? 20.354  62.788  -33.161 1.00 41.07  ?  260  GLN D CD  1 
ATOM   12850 O  OE1 . GLN D  1 229 ? 21.127  62.378  -32.288 1.00 36.24  ?  260  GLN D OE1 1 
ATOM   12851 N  NE2 . GLN D  1 229 ? 19.170  63.332  -32.873 1.00 38.34  ?  260  GLN D NE2 1 
ATOM   12852 N  N   . ALA D  1 230 ? 24.491  62.089  -37.323 1.00 38.20  ?  261  ALA D N   1 
ATOM   12853 C  CA  . ALA D  1 230 ? 25.829  61.733  -37.791 1.00 39.24  ?  261  ALA D CA  1 
ATOM   12854 C  C   . ALA D  1 230 ? 26.767  62.940  -37.733 1.00 41.80  ?  261  ALA D C   1 
ATOM   12855 O  O   . ALA D  1 230 ? 26.336  64.097  -37.762 1.00 36.04  ?  261  ALA D O   1 
ATOM   12856 C  CB  . ALA D  1 230 ? 25.791  61.178  -39.223 1.00 33.64  ?  261  ALA D CB  1 
ATOM   12857 N  N   . LYS D  1 231 ? 28.067  62.648  -37.658 1.00 41.36  ?  262  LYS D N   1 
ATOM   12858 C  CA  . LYS D  1 231 ? 29.092  63.686  -37.672 1.00 43.15  ?  262  LYS D CA  1 
ATOM   12859 C  C   . LYS D  1 231 ? 29.287  64.232  -39.081 1.00 40.74  ?  262  LYS D C   1 
ATOM   12860 O  O   . LYS D  1 231 ? 29.286  63.482  -40.067 1.00 41.16  ?  262  LYS D O   1 
ATOM   12861 C  CB  . LYS D  1 231 ? 30.421  63.147  -37.131 1.00 39.02  ?  262  LYS D CB  1 
ATOM   12862 C  CG  . LYS D  1 231 ? 30.298  62.465  -35.774 1.00 38.28  ?  262  LYS D CG  1 
ATOM   12863 C  CD  . LYS D  1 231 ? 31.655  62.264  -35.068 1.00 41.35  ?  262  LYS D CD  1 
ATOM   12864 C  CE  . LYS D  1 231 ? 32.853  62.276  -36.017 1.00 47.34  ?  262  LYS D CE  1 
ATOM   12865 N  NZ  . LYS D  1 231 ? 34.150  62.271  -35.271 1.00 41.65  ?  262  LYS D NZ  1 
ATOM   12866 N  N   . ALA D  1 232 ? 29.452  65.555  -39.168 1.00 43.27  ?  263  ALA D N   1 
ATOM   12867 C  CA  . ALA D  1 232 ? 29.606  66.197  -40.472 1.00 45.64  ?  263  ALA D CA  1 
ATOM   12868 C  C   . ALA D  1 232 ? 30.784  65.618  -41.238 1.00 41.62  ?  263  ALA D C   1 
ATOM   12869 O  O   . ALA D  1 232 ? 30.708  65.419  -42.452 1.00 46.56  ?  263  ALA D O   1 
ATOM   12870 C  CB  . ALA D  1 232 ? 29.778  67.702  -40.297 1.00 50.21  ?  263  ALA D CB  1 
ATOM   12871 N  N   . GLU D  1 233 ? 31.884  65.342  -40.544 1.00 44.34  ?  264  GLU D N   1 
ATOM   12872 C  CA  . GLU D  1 233 ? 33.048  64.784  -41.219 1.00 43.68  ?  264  GLU D CA  1 
ATOM   12873 C  C   . GLU D  1 233 ? 32.766  63.403  -41.800 1.00 44.58  ?  264  GLU D C   1 
ATOM   12874 O  O   . GLU D  1 233 ? 33.366  63.021  -42.810 1.00 40.35  ?  264  GLU D O   1 
ATOM   12875 C  CB  . GLU D  1 233 ? 34.227  64.748  -40.252 1.00 45.36  ?  264  GLU D CB  1 
ATOM   12876 C  CG  . GLU D  1 233 ? 34.353  66.009  -39.380 1.00 49.74  ?  264  GLU D CG  1 
ATOM   12877 C  CD  . GLU D  1 233 ? 33.753  65.890  -37.971 1.00 58.41  ?  264  GLU D CD  1 
ATOM   12878 O  OE1 . GLU D  1 233 ? 32.507  65.919  -37.827 1.00 60.72  ?  264  GLU D OE1 1 
ATOM   12879 O  OE2 . GLU D  1 233 ? 34.549  65.844  -36.996 1.00 65.04  -1 264  GLU D OE2 1 
ATOM   12880 N  N   . ASP D  1 234 ? 31.854  62.646  -41.189 1.00 42.64  ?  265  ASP D N   1 
ATOM   12881 C  CA  . ASP D  1 234 ? 31.486  61.346  -41.739 1.00 37.97  ?  265  ASP D CA  1 
ATOM   12882 C  C   . ASP D  1 234 ? 30.536  61.504  -42.923 1.00 39.86  ?  265  ASP D C   1 
ATOM   12883 O  O   . ASP D  1 234 ? 30.707  60.857  -43.961 1.00 39.87  ?  265  ASP D O   1 
ATOM   12884 C  CB  . ASP D  1 234 ? 30.848  60.483  -40.639 1.00 40.32  ?  265  ASP D CB  1 
ATOM   12885 C  CG  . ASP D  1 234 ? 31.862  60.018  -39.601 1.00 41.16  ?  265  ASP D CG  1 
ATOM   12886 O  OD1 . ASP D  1 234 ? 33.009  59.752  -39.990 1.00 36.97  ?  265  ASP D OD1 1 
ATOM   12887 O  OD2 . ASP D  1 234 ? 31.512  59.925  -38.405 1.00 42.71  -1 265  ASP D OD2 1 
ATOM   12888 N  N   . VAL D  1 235 ? 29.534  62.370  -42.780 1.00 38.99  ?  266  VAL D N   1 
ATOM   12889 C  CA  . VAL D  1 235 ? 28.588  62.619  -43.867 1.00 41.06  ?  266  VAL D CA  1 
ATOM   12890 C  C   . VAL D  1 235 ? 29.334  63.035  -45.127 1.00 44.90  ?  266  VAL D C   1 
ATOM   12891 O  O   . VAL D  1 235 ? 29.006  62.602  -46.242 1.00 40.37  ?  266  VAL D O   1 
ATOM   12892 C  CB  . VAL D  1 235 ? 27.565  63.685  -43.439 1.00 42.27  ?  266  VAL D CB  1 
ATOM   12893 C  CG1 . VAL D  1 235 ? 26.674  64.073  -44.620 1.00 43.39  ?  266  VAL D CG1 1 
ATOM   12894 C  CG2 . VAL D  1 235 ? 26.739  63.189  -42.261 1.00 42.82  ?  266  VAL D CG2 1 
ATOM   12895 N  N   . ALA D  1 236 ? 30.385  63.846  -44.953 1.00 44.57  ?  267  ALA D N   1 
ATOM   12896 C  CA  . ALA D  1 236 ? 31.179  64.332  -46.074 1.00 45.09  ?  267  ALA D CA  1 
ATOM   12897 C  C   . ALA D  1 236 ? 31.733  63.195  -46.924 1.00 46.53  ?  267  ALA D C   1 
ATOM   12898 O  O   . ALA D  1 236 ? 31.907  63.361  -48.136 1.00 49.11  ?  267  ALA D O   1 
ATOM   12899 C  CB  . ALA D  1 236 ? 32.320  65.216  -45.555 1.00 49.22  ?  267  ALA D CB  1 
ATOM   12900 N  N   . LYS D  1 237 ? 32.030  62.042  -46.319 1.00 40.52  ?  268  LYS D N   1 
ATOM   12901 C  CA  . LYS D  1 237 ? 32.490  60.903  -47.106 1.00 39.89  ?  268  LYS D CA  1 
ATOM   12902 C  C   . LYS D  1 237 ? 31.405  60.350  -48.016 1.00 42.65  ?  268  LYS D C   1 
ATOM   12903 O  O   . LYS D  1 237 ? 31.715  59.548  -48.904 1.00 45.24  ?  268  LYS D O   1 
ATOM   12904 C  CB  . LYS D  1 237 ? 32.991  59.786  -46.187 1.00 37.64  ?  268  LYS D CB  1 
ATOM   12905 C  CG  . LYS D  1 237 ? 34.106  60.224  -45.220 1.00 50.41  ?  268  LYS D CG  1 
ATOM   12906 C  CD  . LYS D  1 237 ? 35.459  59.623  -45.599 1.00 54.08  ?  268  LYS D CD  1 
ATOM   12907 C  CE  . LYS D  1 237 ? 36.623  60.567  -45.298 1.00 52.98  ?  268  LYS D CE  1 
ATOM   12908 N  NZ  . LYS D  1 237 ? 36.562  61.159  -43.927 1.00 56.53  ?  268  LYS D NZ  1 
ATOM   12909 N  N   . PHE D  1 238 ? 30.149  60.747  -47.817 1.00 41.31  ?  269  PHE D N   1 
ATOM   12910 C  CA  . PHE D  1 238 ? 29.038  60.136  -48.543 1.00 44.16  ?  269  PHE D CA  1 
ATOM   12911 C  C   . PHE D  1 238 ? 28.186  61.175  -49.264 1.00 46.54  ?  269  PHE D C   1 
ATOM   12912 O  O   . PHE D  1 238 ? 26.976  60.992  -49.430 1.00 49.29  ?  269  PHE D O   1 
ATOM   12913 C  CB  . PHE D  1 238 ? 28.190  59.285  -47.599 1.00 36.54  ?  269  PHE D CB  1 
ATOM   12914 C  CG  . PHE D  1 238 ? 28.944  58.138  -47.011 1.00 41.03  ?  269  PHE D CG  1 
ATOM   12915 C  CD1 . PHE D  1 238 ? 29.143  56.979  -47.745 1.00 40.21  ?  269  PHE D CD1 1 
ATOM   12916 C  CD2 . PHE D  1 238 ? 29.530  58.249  -45.758 1.00 37.67  ?  269  PHE D CD2 1 
ATOM   12917 C  CE1 . PHE D  1 238 ? 29.874  55.926  -47.217 1.00 41.26  ?  269  PHE D CE1 1 
ATOM   12918 C  CE2 . PHE D  1 238 ? 30.260  57.201  -45.226 1.00 40.88  ?  269  PHE D CE2 1 
ATOM   12919 C  CZ  . PHE D  1 238 ? 30.435  56.039  -45.958 1.00 39.94  ?  269  PHE D CZ  1 
ATOM   12920 N  N   . ALA D  1 239 ? 28.809  62.265  -49.712 1.00 51.88  ?  270  ALA D N   1 
ATOM   12921 C  CA  . ALA D  1 239 ? 28.116  63.225  -50.566 1.00 54.00  ?  270  ALA D CA  1 
ATOM   12922 C  C   . ALA D  1 239 ? 27.663  62.604  -51.885 1.00 51.36  ?  270  ALA D C   1 
ATOM   12923 O  O   . ALA D  1 239 ? 26.745  63.131  -52.518 1.00 53.21  ?  270  ALA D O   1 
ATOM   12924 C  CB  . ALA D  1 239 ? 29.019  64.436  -50.827 1.00 59.99  ?  270  ALA D CB  1 
ATOM   12925 N  N   . HIS D  1 240 ? 28.270  61.487  -52.315 1.00 52.96  ?  271  HIS D N   1 
ATOM   12926 C  CA  . HIS D  1 240 ? 27.724  60.844  -53.506 1.00 51.63  ?  271  HIS D CA  1 
ATOM   12927 C  C   . HIS D  1 240 ? 26.404  60.136  -53.247 1.00 56.13  ?  271  HIS D C   1 
ATOM   12928 O  O   . HIS D  1 240 ? 25.919  59.452  -54.161 1.00 60.99  ?  271  HIS D O   1 
ATOM   12929 C  CB  . HIS D  1 240 ? 28.696  59.825  -54.095 1.00 47.01  ?  271  HIS D CB  1 
ATOM   12930 C  CG  . HIS D  1 240 ? 29.073  58.731  -53.150 1.00 54.15  ?  271  HIS D CG  1 
ATOM   12931 N  ND1 . HIS D  1 240 ? 29.843  58.947  -52.027 1.00 54.81  ?  271  HIS D ND1 1 
ATOM   12932 C  CD2 . HIS D  1 240 ? 28.762  57.413  -53.145 1.00 52.85  ?  271  HIS D CD2 1 
ATOM   12933 C  CE1 . HIS D  1 240 ? 30.007  57.804  -51.382 1.00 56.10  ?  271  HIS D CE1 1 
ATOM   12934 N  NE2 . HIS D  1 240 ? 29.355  56.858  -52.036 1.00 55.75  ?  271  HIS D NE2 1 
ATOM   12935 N  N   . ILE D  1 241 ? 25.804  60.227  -52.065 1.00 53.08  ?  272  ILE D N   1 
ATOM   12936 C  CA  . ILE D  1 241 ? 24.510  59.613  -51.790 1.00 51.56  ?  272  ILE D CA  1 
ATOM   12937 C  C   . ILE D  1 241 ? 23.479  60.728  -51.760 1.00 47.00  ?  272  ILE D C   1 
ATOM   12938 O  O   . ILE D  1 241 ? 23.534  61.615  -50.898 1.00 48.98  ?  272  ILE D O   1 
ATOM   12939 C  CB  . ILE D  1 241 ? 24.515  58.812  -50.476 1.00 44.49  ?  272  ILE D CB  1 
ATOM   12940 C  CG1 . ILE D  1 241 ? 25.600  57.731  -50.500 1.00 43.62  ?  272  ILE D CG1 1 
ATOM   12941 C  CG2 . ILE D  1 241 ? 23.165  58.151  -50.261 1.00 36.79  ?  272  ILE D CG2 1 
ATOM   12942 C  CD1 . ILE D  1 241 ? 25.506  56.740  -49.320 1.00 42.26  ?  272  ILE D CD1 1 
ATOM   12943 N  N   . LYS D  1 242 ? 22.544  60.685  -52.713 1.00 50.41  ?  273  LYS D N   1 
ATOM   12944 C  CA  . LYS D  1 242 ? 21.585  61.776  -52.867 1.00 48.02  ?  273  LYS D CA  1 
ATOM   12945 C  C   . LYS D  1 242 ? 20.555  61.770  -51.750 1.00 43.85  ?  273  LYS D C   1 
ATOM   12946 O  O   . LYS D  1 242 ? 20.218  62.823  -51.201 1.00 47.28  ?  273  LYS D O   1 
ATOM   12947 C  CB  . LYS D  1 242 ? 20.894  61.677  -54.227 1.00 46.83  ?  273  LYS D CB  1 
ATOM   12948 N  N   . ASP D  1 243 ? 20.040  60.600  -51.400 1.00 43.71  ?  274  ASP D N   1 
ATOM   12949 C  CA  . ASP D  1 243 ? 18.980  60.543  -50.408 1.00 44.40  ?  274  ASP D CA  1 
ATOM   12950 C  C   . ASP D  1 243 ? 19.532  60.891  -49.031 1.00 45.73  ?  274  ASP D C   1 
ATOM   12951 O  O   . ASP D  1 243 ? 20.504  60.285  -48.568 1.00 43.56  ?  274  ASP D O   1 
ATOM   12952 C  CB  . ASP D  1 243 ? 18.332  59.166  -50.403 1.00 45.13  ?  274  ASP D CB  1 
ATOM   12953 C  CG  . ASP D  1 243 ? 17.258  59.052  -49.361 1.00 48.33  ?  274  ASP D CG  1 
ATOM   12954 O  OD1 . ASP D  1 243 ? 16.136  59.543  -49.606 1.00 50.34  ?  274  ASP D OD1 1 
ATOM   12955 O  OD2 . ASP D  1 243 ? 17.544  58.491  -48.284 1.00 44.32  -1 274  ASP D OD2 1 
ATOM   12956 N  N   . LYS D  1 244 ? 18.962  61.913  -48.397 1.00 43.35  ?  275  LYS D N   1 
ATOM   12957 C  CA  . LYS D  1 244 ? 19.511  62.399  -47.109 1.00 42.03  ?  275  LYS D CA  1 
ATOM   12958 C  C   . LYS D  1 244 ? 19.563  61.261  -46.093 1.00 45.14  ?  275  LYS D C   1 
ATOM   12959 O  O   . LYS D  1 244 ? 20.632  61.017  -45.525 1.00 39.38  ?  275  LYS D O   1 
ATOM   12960 C  CB  . LYS D  1 244 ? 18.661  63.516  -46.506 1.00 46.81  ?  275  LYS D CB  1 
ATOM   12961 C  CG  . LYS D  1 244 ? 19.298  64.266  -45.350 1.00 47.21  ?  275  LYS D CG  1 
ATOM   12962 C  CD  . LYS D  1 244 ? 18.313  65.144  -44.588 1.00 55.10  ?  275  LYS D CD  1 
ATOM   12963 C  CE  . LYS D  1 244 ? 18.256  64.809  -43.133 1.00 57.82  ?  275  LYS D CE  1 
ATOM   12964 N  NZ  . LYS D  1 244 ? 18.357  66.010  -42.301 1.00 57.61  ?  275  LYS D NZ  1 
ATOM   12965 N  N   . ASP D  1 245 ? 18.421  60.635  -45.851 1.00 42.35  ?  276  ASP D N   1 
ATOM   12966 C  CA  . ASP D  1 245 ? 18.410  59.583  -44.842 1.00 38.71  ?  276  ASP D CA  1 
ATOM   12967 C  C   . ASP D  1 245 ? 19.478  58.532  -45.126 1.00 40.84  ?  276  ASP D C   1 
ATOM   12968 O  O   . ASP D  1 245 ? 20.254  58.160  -44.233 1.00 36.87  ?  276  ASP D O   1 
ATOM   12969 C  CB  . ASP D  1 245 ? 17.023  58.948  -44.760 1.00 43.59  ?  276  ASP D CB  1 
ATOM   12970 C  CG  . ASP D  1 245 ? 16.036  59.836  -44.050 1.00 45.43  ?  276  ASP D CG  1 
ATOM   12971 O  OD1 . ASP D  1 245 ? 16.458  60.923  -43.599 1.00 48.14  ?  276  ASP D OD1 1 
ATOM   12972 O  OD2 . ASP D  1 245 ? 14.856  59.456  -43.928 1.00 49.75  -1 276  ASP D OD2 1 
ATOM   12973 N  N   . ARG D  1 246 ? 19.545  58.045  -46.363 1.00 37.46  ?  277  ARG D N   1 
ATOM   12974 C  CA  . ARG D  1 246 ? 20.570  57.054  -46.671 1.00 39.84  ?  277  ARG D CA  1 
ATOM   12975 C  C   . ARG D  1 246 ? 21.963  57.603  -46.411 1.00 41.83  ?  277  ARG D C   1 
ATOM   12976 O  O   . ARG D  1 246 ? 22.825  56.896  -45.869 1.00 34.72  ?  277  ARG D O   1 
ATOM   12977 C  CB  . ARG D  1 246 ? 20.459  56.580  -48.113 1.00 40.79  ?  277  ARG D CB  1 
ATOM   12978 C  CG  . ARG D  1 246 ? 21.531  55.555  -48.469 1.00 39.86  ?  277  ARG D CG  1 
ATOM   12979 C  CD  . ARG D  1 246 ? 21.265  54.200  -47.839 1.00 37.83  ?  277  ARG D CD  1 
ATOM   12980 N  NE  . ARG D  1 246 ? 22.077  53.132  -48.417 1.00 37.55  ?  277  ARG D NE  1 
ATOM   12981 C  CZ  . ARG D  1 246 ? 22.112  51.893  -47.941 1.00 36.03  ?  277  ARG D CZ  1 
ATOM   12982 N  NH1 . ARG D  1 246 ? 21.384  51.537  -46.894 1.00 34.80  ?  277  ARG D NH1 1 
ATOM   12983 N  NH2 . ARG D  1 246 ? 22.896  50.992  -48.525 1.00 32.21  ?  277  ARG D NH2 1 
ATOM   12984 N  N   . ARG D  1 247 ? 22.193  58.866  -46.777 1.00 39.68  ?  278  ARG D N   1 
ATOM   12985 C  CA  . ARG D  1 247 ? 23.500  59.480  -46.565 1.00 38.62  ?  278  ARG D CA  1 
ATOM   12986 C  C   . ARG D  1 247 ? 23.858  59.534  -45.083 1.00 36.84  ?  278  ARG D C   1 
ATOM   12987 O  O   . ARG D  1 247 ? 24.969  59.157  -44.694 1.00 35.12  ?  278  ARG D O   1 
ATOM   12988 C  CB  . ARG D  1 247 ? 23.525  60.883  -47.173 1.00 41.45  ?  278  ARG D CB  1 
ATOM   12989 C  CG  . ARG D  1 247 ? 24.871  61.594  -47.001 1.00 42.22  ?  278  ARG D CG  1 
ATOM   12990 C  CD  . ARG D  1 247 ? 24.905  62.922  -47.756 1.00 46.53  ?  278  ARG D CD  1 
ATOM   12991 N  NE  . ARG D  1 247 ? 23.884  63.855  -47.297 1.00 44.60  ?  278  ARG D NE  1 
ATOM   12992 C  CZ  . ARG D  1 247 ? 22.857  64.256  -48.036 1.00 49.23  ?  278  ARG D CZ  1 
ATOM   12993 N  NH1 . ARG D  1 247 ? 22.658  63.784  -49.258 1.00 50.61  ?  278  ARG D NH1 1 
ATOM   12994 N  NH2 . ARG D  1 247 ? 22.009  65.150  -47.538 1.00 46.94  ?  278  ARG D NH2 1 
ATOM   12995 N  N   . THR D  1 248 ? 22.937  60.037  -44.250 1.00 34.71  ?  279  THR D N   1 
ATOM   12996 C  CA  . THR D  1 248 ? 23.171  60.120  -42.812 1.00 36.50  ?  279  THR D CA  1 
ATOM   12997 C  C   . THR D  1 248 ? 23.412  58.737  -42.225 1.00 37.90  ?  279  THR D C   1 
ATOM   12998 O  O   . THR D  1 248 ? 24.381  58.521  -41.488 1.00 33.02  ?  279  THR D O   1 
ATOM   12999 C  CB  . THR D  1 248 ? 21.973  60.786  -42.135 1.00 40.00  ?  279  THR D CB  1 
ATOM   13000 O  OG1 . THR D  1 248 ? 21.776  62.097  -42.683 1.00 39.20  ?  279  THR D OG1 1 
ATOM   13001 C  CG2 . THR D  1 248 ? 22.181  60.899  -40.636 1.00 34.16  ?  279  THR D CG2 1 
ATOM   13002 N  N   . TYR D  1 249 ? 22.534  57.788  -42.561 1.00 34.90  ?  280  TYR D N   1 
ATOM   13003 C  CA  . TYR D  1 249 ? 22.665  56.397  -42.123 1.00 36.11  ?  280  TYR D CA  1 
ATOM   13004 C  C   . TYR D  1 249 ? 24.020  55.826  -42.509 1.00 32.99  ?  280  TYR D C   1 
ATOM   13005 O  O   . TYR D  1 249 ? 24.707  55.215  -41.679 1.00 34.38  ?  280  TYR D O   1 
ATOM   13006 C  CB  . TYR D  1 249 ? 21.511  55.574  -42.745 1.00 30.29  ?  280  TYR D CB  1 
ATOM   13007 C  CG  . TYR D  1 249 ? 21.520  54.060  -42.536 1.00 28.69  ?  280  TYR D CG  1 
ATOM   13008 C  CD1 . TYR D  1 249 ? 22.222  53.227  -43.398 1.00 31.71  ?  280  TYR D CD1 1 
ATOM   13009 C  CD2 . TYR D  1 249 ? 20.791  53.471  -41.518 1.00 27.08  ?  280  TYR D CD2 1 
ATOM   13010 C  CE1 . TYR D  1 249 ? 22.229  51.853  -43.237 1.00 28.01  ?  280  TYR D CE1 1 
ATOM   13011 C  CE2 . TYR D  1 249 ? 20.789  52.069  -41.348 1.00 27.71  ?  280  TYR D CE2 1 
ATOM   13012 C  CZ  . TYR D  1 249 ? 21.513  51.282  -42.207 1.00 27.96  ?  280  TYR D CZ  1 
ATOM   13013 O  OH  . TYR D  1 249 ? 21.526  49.910  -42.068 1.00 29.52  ?  280  TYR D OH  1 
ATOM   13014 N  N   . ALA D  1 250 ? 24.413  56.002  -43.777 1.00 29.49  ?  281  ALA D N   1 
ATOM   13015 C  CA  . ALA D  1 250 ? 25.731  55.554  -44.219 1.00 34.29  ?  281  ALA D CA  1 
ATOM   13016 C  C   . ALA D  1 250 ? 26.821  56.141  -43.339 1.00 34.98  ?  281  ALA D C   1 
ATOM   13017 O  O   . ALA D  1 250 ? 27.754  55.440  -42.923 1.00 33.67  ?  281  ALA D O   1 
ATOM   13018 C  CB  . ALA D  1 250 ? 25.959  55.954  -45.676 1.00 33.23  ?  281  ALA D CB  1 
ATOM   13019 N  N   . ALA D  1 251 ? 26.691  57.423  -43.005 1.00 35.02  ?  282  ALA D N   1 
ATOM   13020 C  CA  . ALA D  1 251 ? 27.681  58.049  -42.145 1.00 37.29  ?  282  ALA D CA  1 
ATOM   13021 C  C   . ALA D  1 251 ? 27.674  57.435  -40.746 1.00 38.13  ?  282  ALA D C   1 
ATOM   13022 O  O   . ALA D  1 251 ? 28.737  57.335  -40.117 1.00 34.16  ?  282  ALA D O   1 
ATOM   13023 C  CB  . ALA D  1 251 ? 27.430  59.559  -42.080 1.00 35.48  ?  282  ALA D CB  1 
ATOM   13024 N  N   . MET D  1 252 ? 26.510  56.999  -40.234 1.00 34.07  ?  283  MET D N   1 
ATOM   13025 C  CA  . MET D  1 252 ? 26.537  56.408  -38.900 1.00 32.92  ?  283  MET D CA  1 
ATOM   13026 C  C   . MET D  1 252 ? 27.248  55.067  -38.919 1.00 31.57  ?  283  MET D C   1 
ATOM   13027 O  O   . MET D  1 252 ? 27.984  54.729  -37.979 1.00 37.07  ?  283  MET D O   1 
ATOM   13028 C  CB  . MET D  1 252 ? 25.156  56.209  -38.272 1.00 34.44  ?  283  MET D CB  1 
ATOM   13029 C  CG  . MET D  1 252 ? 24.447  57.439  -37.811 1.00 37.66  ?  283  MET D CG  1 
ATOM   13030 S  SD  . MET D  1 252 ? 22.687  57.420  -38.214 1.00 34.13  ?  283  MET D SD  1 
ATOM   13031 C  CE  . MET D  1 252 ? 22.225  56.716  -36.630 1.00 32.22  ?  283  MET D CE  1 
ATOM   13032 N  N   . VAL D  1 253 ? 27.039  54.288  -39.978 1.00 32.70  ?  284  VAL D N   1 
ATOM   13033 C  CA  . VAL D  1 253 ? 27.708  52.993  -40.088 1.00 30.50  ?  284  VAL D CA  1 
ATOM   13034 C  C   . VAL D  1 253 ? 29.210  53.200  -40.206 1.00 34.19  ?  284  VAL D C   1 
ATOM   13035 O  O   . VAL D  1 253 ? 30.010  52.451  -39.629 1.00 35.31  ?  284  VAL D O   1 
ATOM   13036 C  CB  . VAL D  1 253 ? 27.141  52.210  -41.289 1.00 32.59  ?  284  VAL D CB  1 
ATOM   13037 C  CG1 . VAL D  1 253 ? 27.975  50.968  -41.574 1.00 35.26  ?  284  VAL D CG1 1 
ATOM   13038 C  CG2 . VAL D  1 253 ? 25.691  51.848  -41.022 1.00 28.42  ?  284  VAL D CG2 1 
ATOM   13039 N  N   . TYR D  1 254 ? 29.612  54.254  -40.914 1.00 33.77  ?  285  TYR D N   1 
ATOM   13040 C  CA  . TYR D  1 254 ? 31.031  54.510  -41.127 1.00 34.69  ?  285  TYR D CA  1 
ATOM   13041 C  C   . TYR D  1 254 ? 31.728  54.871  -39.826 1.00 34.94  ?  285  TYR D C   1 
ATOM   13042 O  O   . TYR D  1 254 ? 32.870  54.461  -39.596 1.00 36.39  ?  285  TYR D O   1 
ATOM   13043 C  CB  . TYR D  1 254 ? 31.200  55.620  -42.162 1.00 38.12  ?  285  TYR D CB  1 
ATOM   13044 C  CG  . TYR D  1 254 ? 32.624  55.939  -42.517 1.00 38.52  ?  285  TYR D CG  1 
ATOM   13045 C  CD1 . TYR D  1 254 ? 33.346  55.116  -43.371 1.00 35.70  ?  285  TYR D CD1 1 
ATOM   13046 C  CD2 . TYR D  1 254 ? 33.234  57.083  -42.036 1.00 38.12  ?  285  TYR D CD2 1 
ATOM   13047 C  CE1 . TYR D  1 254 ? 34.650  55.421  -43.726 1.00 42.56  ?  285  TYR D CE1 1 
ATOM   13048 C  CE2 . TYR D  1 254 ? 34.542  57.393  -42.382 1.00 42.88  ?  285  TYR D CE2 1 
ATOM   13049 C  CZ  . TYR D  1 254 ? 35.245  56.562  -43.228 1.00 46.87  ?  285  TYR D CZ  1 
ATOM   13050 O  OH  . TYR D  1 254 ? 36.551  56.867  -43.566 1.00 54.12  ?  285  TYR D OH  1 
ATOM   13051 N  N   . ALA D  1 255 ? 31.056  55.624  -38.956 1.00 33.87  ?  286  ALA D N   1 
ATOM   13052 C  CA  . ALA D  1 255 ? 31.632  55.902  -37.645 1.00 33.32  ?  286  ALA D CA  1 
ATOM   13053 C  C   . ALA D  1 255 ? 31.897  54.612  -36.880 1.00 34.48  ?  286  ALA D C   1 
ATOM   13054 O  O   . ALA D  1 255 ? 32.924  54.485  -36.199 1.00 33.16  ?  286  ALA D O   1 
ATOM   13055 C  CB  . ALA D  1 255 ? 30.713  56.836  -36.852 1.00 29.69  ?  286  ALA D CB  1 
ATOM   13056 N  N   . VAL D  1 256 ? 30.997  53.632  -36.999 1.00 31.85  ?  287  VAL D N   1 
ATOM   13057 C  CA  . VAL D  1 256 ? 31.236  52.315  -36.405 1.00 34.33  ?  287  VAL D CA  1 
ATOM   13058 C  C   . VAL D  1 256 ? 32.476  51.683  -37.010 1.00 33.84  ?  287  VAL D C   1 
ATOM   13059 O  O   . VAL D  1 256 ? 33.326  51.127  -36.299 1.00 35.07  ?  287  VAL D O   1 
ATOM   13060 C  CB  . VAL D  1 256 ? 30.008  51.400  -36.596 1.00 32.27  ?  287  VAL D CB  1 
ATOM   13061 C  CG1 . VAL D  1 256 ? 30.376  49.966  -36.242 1.00 37.17  ?  287  VAL D CG1 1 
ATOM   13062 C  CG2 . VAL D  1 256 ? 28.859  51.872  -35.743 1.00 34.05  ?  287  VAL D CG2 1 
ATOM   13063 N  N   . ASP D  1 257 ? 32.603  51.759  -38.331 1.00 33.69  ?  288  ASP D N   1 
ATOM   13064 C  CA  . ASP D  1 257 ? 33.772  51.191  -38.992 1.00 33.90  ?  288  ASP D CA  1 
ATOM   13065 C  C   . ASP D  1 257 ? 35.062  51.838  -38.494 1.00 38.52  ?  288  ASP D C   1 
ATOM   13066 O  O   . ASP D  1 257 ? 36.048  51.138  -38.214 1.00 36.06  ?  288  ASP D O   1 
ATOM   13067 C  CB  . ASP D  1 257 ? 33.642  51.352  -40.501 1.00 31.21  ?  288  ASP D CB  1 
ATOM   13068 C  CG  . ASP D  1 257 ? 34.614  50.490  -41.252 1.00 37.10  ?  288  ASP D CG  1 
ATOM   13069 O  OD1 . ASP D  1 257 ? 34.423  49.255  -41.214 1.00 33.79  ?  288  ASP D OD1 1 
ATOM   13070 O  OD2 . ASP D  1 257 ? 35.572  51.037  -41.864 1.00 36.67  -1 288  ASP D OD2 1 
ATOM   13071 N  N   . ARG D  1 258 ? 35.072  53.173  -38.385 1.00 35.49  ?  289  ARG D N   1 
ATOM   13072 C  CA  . ARG D  1 258 ? 36.224  53.885  -37.832 1.00 39.61  ?  289  ARG D CA  1 
ATOM   13073 C  C   . ARG D  1 258 ? 36.607  53.342  -36.461 1.00 38.21  ?  289  ARG D C   1 
ATOM   13074 O  O   . ARG D  1 258 ? 37.781  53.042  -36.200 1.00 39.45  ?  289  ARG D O   1 
ATOM   13075 C  CB  . ARG D  1 258 ? 35.916  55.384  -37.728 1.00 41.03  ?  289  ARG D CB  1 
ATOM   13076 C  CG  . ARG D  1 258 ? 35.839  56.134  -39.047 1.00 39.36  ?  289  ARG D CG  1 
ATOM   13077 C  CD  . ARG D  1 258 ? 35.927  57.644  -38.807 1.00 41.61  ?  289  ARG D CD  1 
ATOM   13078 N  NE  . ARG D  1 258 ? 34.727  58.222  -38.197 1.00 35.86  ?  289  ARG D NE  1 
ATOM   13079 C  CZ  . ARG D  1 258 ? 34.581  58.485  -36.903 1.00 40.21  ?  289  ARG D CZ  1 
ATOM   13080 N  NH1 . ARG D  1 258 ? 35.539  58.208  -36.018 1.00 37.53  ?  289  ARG D NH1 1 
ATOM   13081 N  NH2 . ARG D  1 258 ? 33.444  59.029  -36.478 1.00 38.07  ?  289  ARG D NH2 1 
ATOM   13082 N  N   . GLY D  1 259 ? 35.628  53.248  -35.558 1.00 34.12  ?  290  GLY D N   1 
ATOM   13083 C  CA  . GLY D  1 259 ? 35.901  52.734  -34.230 1.00 35.94  ?  290  GLY D CA  1 
ATOM   13084 C  C   . GLY D  1 259 ? 36.451  51.324  -34.256 1.00 36.73  ?  290  GLY D C   1 
ATOM   13085 O  O   . GLY D  1 259 ? 37.389  50.996  -33.519 1.00 34.27  ?  290  GLY D O   1 
ATOM   13086 N  N   . VAL D  1 260 ? 35.883  50.471  -35.107 1.00 30.96  ?  291  VAL D N   1 
ATOM   13087 C  CA  . VAL D  1 260 ? 36.393  49.112  -35.238 1.00 33.23  ?  291  VAL D CA  1 
ATOM   13088 C  C   . VAL D  1 260 ? 37.860  49.136  -35.652 1.00 37.02  ?  291  VAL D C   1 
ATOM   13089 O  O   . VAL D  1 260 ? 38.670  48.344  -35.153 1.00 35.92  ?  291  VAL D O   1 
ATOM   13090 C  CB  . VAL D  1 260 ? 35.535  48.309  -36.235 1.00 32.85  ?  291  VAL D CB  1 
ATOM   13091 C  CG1 . VAL D  1 260 ? 36.240  47.008  -36.617 1.00 34.73  ?  291  VAL D CG1 1 
ATOM   13092 C  CG2 . VAL D  1 260 ? 34.127  48.034  -35.655 1.00 34.97  ?  291  VAL D CG2 1 
ATOM   13093 N  N   . GLY D  1 261 ? 38.226  50.057  -36.554 1.00 35.84  ?  292  GLY D N   1 
ATOM   13094 C  CA  . GLY D  1 261 ? 39.620  50.171  -36.979 1.00 38.90  ?  292  GLY D CA  1 
ATOM   13095 C  C   . GLY D  1 261 ? 40.575  50.562  -35.860 1.00 38.08  ?  292  GLY D C   1 
ATOM   13096 O  O   . GLY D  1 261 ? 41.693  50.042  -35.774 1.00 40.88  ?  292  GLY D O   1 
ATOM   13097 N  N   . LYS D  1 262 ? 40.165  51.498  -35.001 1.00 36.55  ?  293  LYS D N   1 
ATOM   13098 C  CA  . LYS D  1 262 ? 41.001  51.839  -33.852 1.00 36.94  ?  293  LYS D CA  1 
ATOM   13099 C  C   . LYS D  1 262 ? 41.068  50.686  -32.853 1.00 39.30  ?  293  LYS D C   1 
ATOM   13100 O  O   . LYS D  1 262 ? 42.120  50.435  -32.246 1.00 35.56  ?  293  LYS D O   1 
ATOM   13101 C  CB  . LYS D  1 262 ? 40.481  53.113  -33.180 1.00 39.12  ?  293  LYS D CB  1 
ATOM   13102 C  CG  . LYS D  1 262 ? 40.732  54.391  -33.989 1.00 46.94  ?  293  LYS D CG  1 
ATOM   13103 C  CD  . LYS D  1 262 ? 40.243  55.646  -33.257 1.00 51.57  ?  293  LYS D CD  1 
ATOM   13104 C  CE  . LYS D  1 262 ? 40.256  56.882  -34.171 1.00 56.59  ?  293  LYS D CE  1 
ATOM   13105 N  NZ  . LYS D  1 262 ? 38.927  57.122  -34.870 1.00 59.13  ?  293  LYS D NZ  1 
ATOM   13106 N  N   . ILE D  1 263 ? 39.954  49.987  -32.649 1.00 30.28  ?  294  ILE D N   1 
ATOM   13107 C  CA  . ILE D  1 263 ? 39.978  48.797  -31.804 1.00 35.60  ?  294  ILE D CA  1 
ATOM   13108 C  C   . ILE D  1 263 ? 41.010  47.803  -32.331 1.00 38.66  ?  294  ILE D C   1 
ATOM   13109 O  O   . ILE D  1 263 ? 41.850  47.297  -31.579 1.00 36.08  ?  294  ILE D O   1 
ATOM   13110 C  CB  . ILE D  1 263 ? 38.569  48.168  -31.713 1.00 34.96  ?  294  ILE D CB  1 
ATOM   13111 C  CG1 . ILE D  1 263 ? 37.671  48.967  -30.767 1.00 33.79  ?  294  ILE D CG1 1 
ATOM   13112 C  CG2 . ILE D  1 263 ? 38.633  46.709  -31.222 1.00 32.41  ?  294  ILE D CG2 1 
ATOM   13113 C  CD1 . ILE D  1 263 ? 36.177  48.820  -31.086 1.00 32.51  ?  294  ILE D CD1 1 
ATOM   13114 N  N   . VAL D  1 264 ? 40.985  47.540  -33.640 1.00 34.11  ?  295  VAL D N   1 
ATOM   13115 C  CA  . VAL D  1 264 ? 41.909  46.575  -34.240 1.00 36.88  ?  295  VAL D CA  1 
ATOM   13116 C  C   . VAL D  1 264 ? 43.361  46.998  -34.006 1.00 42.03  ?  295  VAL D C   1 
ATOM   13117 O  O   . VAL D  1 264 ? 44.210  46.182  -33.627 1.00 39.33  ?  295  VAL D O   1 
ATOM   13118 C  CB  . VAL D  1 264 ? 41.607  46.411  -35.742 1.00 41.57  ?  295  VAL D CB  1 
ATOM   13119 C  CG1 . VAL D  1 264 ? 42.717  45.622  -36.440 1.00 40.42  ?  295  VAL D CG1 1 
ATOM   13120 C  CG2 . VAL D  1 264 ? 40.249  45.740  -35.959 1.00 36.43  ?  295  VAL D CG2 1 
ATOM   13121 N  N   . GLN D  1 265 ? 43.666  48.280  -34.224 1.00 39.66  ?  296  GLN D N   1 
ATOM   13122 C  CA  . GLN D  1 265 ? 45.017  48.771  -33.942 1.00 46.30  ?  296  GLN D CA  1 
ATOM   13123 C  C   . GLN D  1 265 ? 45.410  48.528  -32.483 1.00 41.38  ?  296  GLN D C   1 
ATOM   13124 O  O   . GLN D  1 265 ? 46.526  48.069  -32.205 1.00 44.70  ?  296  GLN D O   1 
ATOM   13125 C  CB  . GLN D  1 265 ? 45.116  50.260  -34.288 1.00 47.94  ?  296  GLN D CB  1 
ATOM   13126 C  CG  . GLN D  1 265 ? 46.554  50.828  -34.303 1.00 45.50  ?  296  GLN D CG  1 
ATOM   13127 C  CD  . GLN D  1 265 ? 47.547  49.909  -35.009 1.00 54.29  ?  296  GLN D CD  1 
ATOM   13128 O  OE1 . GLN D  1 265 ? 48.613  49.587  -34.468 1.00 60.67  ?  296  GLN D OE1 1 
ATOM   13129 N  NE2 . GLN D  1 265 ? 47.208  49.491  -36.229 1.00 58.12  ?  296  GLN D NE2 1 
ATOM   13130 N  N   . THR D  1 266 ? 44.501  48.816  -31.538 1.00 37.41  ?  297  THR D N   1 
ATOM   13131 C  CA  . THR D  1 266 ? 44.788  48.611  -30.118 1.00 39.21  ?  297  THR D CA  1 
ATOM   13132 C  C   . THR D  1 266 ? 45.074  47.145  -29.819 1.00 42.09  ?  297  THR D C   1 
ATOM   13133 O  O   . THR D  1 266 ? 45.971  46.817  -29.026 1.00 38.31  ?  297  THR D O   1 
ATOM   13134 C  CB  . THR D  1 266 ? 43.611  49.092  -29.255 1.00 39.98  ?  297  THR D CB  1 
ATOM   13135 O  OG1 . THR D  1 266 ? 43.349  50.482  -29.490 1.00 37.91  ?  297  THR D OG1 1 
ATOM   13136 C  CG2 . THR D  1 266 ? 43.912  48.889  -27.771 1.00 34.21  ?  297  THR D CG2 1 
ATOM   13137 N  N   . LEU D  1 267 ? 44.299  46.251  -30.426 1.00 35.56  ?  298  LEU D N   1 
ATOM   13138 C  CA  . LEU D  1 267 ? 44.511  44.819  -30.239 1.00 40.00  ?  298  LEU D CA  1 
ATOM   13139 C  C   . LEU D  1 267 ? 45.864  44.390  -30.778 1.00 40.23  ?  298  LEU D C   1 
ATOM   13140 O  O   . LEU D  1 267 ? 46.504  43.487  -30.226 1.00 40.02  ?  298  LEU D O   1 
ATOM   13141 C  CB  . LEU D  1 267 ? 43.407  44.026  -30.949 1.00 38.41  ?  298  LEU D CB  1 
ATOM   13142 C  CG  . LEU D  1 267 ? 42.035  43.907  -30.289 1.00 41.23  ?  298  LEU D CG  1 
ATOM   13143 C  CD1 . LEU D  1 267 ? 41.085  43.283  -31.305 1.00 32.16  ?  298  LEU D CD1 1 
ATOM   13144 C  CD2 . LEU D  1 267 ? 42.085  43.097  -28.985 1.00 33.73  ?  298  LEU D CD2 1 
ATOM   13145 N  N   . LYS D  1 268 ? 46.288  44.980  -31.897 1.00 40.64  ?  299  LYS D N   1 
ATOM   13146 C  CA  . LYS D  1 268 ? 47.590  44.628  -32.450 1.00 41.68  ?  299  LYS D CA  1 
ATOM   13147 C  C   . LYS D  1 268 ? 48.708  45.153  -31.562 1.00 41.91  ?  299  LYS D C   1 
ATOM   13148 O  O   . LYS D  1 268 ? 49.724  44.479  -31.363 1.00 45.71  ?  299  LYS D O   1 
ATOM   13149 C  CB  . LYS D  1 268 ? 47.725  45.185  -33.863 1.00 44.84  ?  299  LYS D CB  1 
ATOM   13150 C  CG  . LYS D  1 268 ? 46.968  44.407  -34.914 1.00 39.96  ?  299  LYS D CG  1 
ATOM   13151 C  CD  . LYS D  1 268 ? 47.056  45.136  -36.241 1.00 43.73  ?  299  LYS D CD  1 
ATOM   13152 C  CE  . LYS D  1 268 ? 46.384  44.364  -37.365 1.00 45.55  ?  299  LYS D CE  1 
ATOM   13153 N  NZ  . LYS D  1 268 ? 46.118  45.275  -38.507 1.00 45.41  ?  299  LYS D NZ  1 
ATOM   13154 N  N   . GLU D  1 269 ? 48.527  46.355  -31.014 1.00 43.68  ?  300  GLU D N   1 
ATOM   13155 C  CA  . GLU D  1 269 ? 49.545  46.952  -30.162 1.00 44.90  ?  300  GLU D CA  1 
ATOM   13156 C  C   . GLU D  1 269 ? 49.707  46.157  -28.876 1.00 43.84  ?  300  GLU D C   1 
ATOM   13157 O  O   . GLU D  1 269 ? 50.829  45.858  -28.455 1.00 46.41  ?  300  GLU D O   1 
ATOM   13158 C  CB  . GLU D  1 269 ? 49.186  48.413  -29.875 1.00 40.59  ?  300  GLU D CB  1 
ATOM   13159 C  CG  . GLU D  1 269 ? 49.503  49.316  -31.049 1.00 42.64  ?  300  GLU D CG  1 
ATOM   13160 C  CD  . GLU D  1 269 ? 48.910  50.706  -30.936 1.00 50.67  ?  300  GLU D CD  1 
ATOM   13161 O  OE1 . GLU D  1 269 ? 48.454  51.098  -29.835 1.00 53.08  ?  300  GLU D OE1 1 
ATOM   13162 O  OE2 . GLU D  1 269 ? 48.910  51.412  -31.965 1.00 51.05  -1 300  GLU D OE2 1 
ATOM   13163 N  N   . THR D  1 270 ? 48.596  45.793  -28.245 1.00 40.07  ?  301  THR D N   1 
ATOM   13164 C  CA  . THR D  1 270 ? 48.631  45.036  -27.006 1.00 38.30  ?  301  THR D CA  1 
ATOM   13165 C  C   . THR D  1 270 ? 48.949  43.567  -27.222 1.00 40.95  ?  301  THR D C   1 
ATOM   13166 O  O   . THR D  1 270 ? 48.952  42.812  -26.246 1.00 41.08  ?  301  THR D O   1 
ATOM   13167 C  CB  . THR D  1 270 ? 47.290  45.155  -26.274 1.00 38.97  ?  301  THR D CB  1 
ATOM   13168 O  OG1 . THR D  1 270 ? 46.242  44.732  -27.150 1.00 40.65  ?  301  THR D OG1 1 
ATOM   13169 C  CG2 . THR D  1 270 ? 47.030  46.588  -25.849 1.00 36.43  ?  301  THR D CG2 1 
ATOM   13170 N  N   . LYS D  1 271 ? 49.178  43.140  -28.465 1.00 40.73  ?  302  LYS D N   1 
ATOM   13171 C  CA  . LYS D  1 271 ? 49.480  41.742  -28.786 1.00 42.26  ?  302  LYS D CA  1 
ATOM   13172 C  C   . LYS D  1 271 ? 48.320  40.808  -28.454 1.00 42.38  ?  302  LYS D C   1 
ATOM   13173 O  O   . LYS D  1 271 ? 48.523  39.614  -28.208 1.00 41.34  ?  302  LYS D O   1 
ATOM   13174 C  CB  . LYS D  1 271 ? 50.763  41.267  -28.079 1.00 42.88  ?  302  LYS D CB  1 
ATOM   13175 N  N   . GLN D  1 272 ? 47.092  41.328  -28.441 1.00 41.79  ?  303  GLN D N   1 
ATOM   13176 C  CA  . GLN D  1 272 ? 45.914  40.511  -28.187 1.00 41.15  ?  303  GLN D CA  1 
ATOM   13177 C  C   . GLN D  1 272 ? 45.178  40.125  -29.467 1.00 42.75  ?  303  GLN D C   1 
ATOM   13178 O  O   . GLN D  1 272 ? 44.293  39.269  -29.421 1.00 41.50  ?  303  GLN D O   1 
ATOM   13179 C  CB  . GLN D  1 272 ? 44.940  41.251  -27.254 1.00 42.34  ?  303  GLN D CB  1 
ATOM   13180 C  CG  . GLN D  1 272 ? 45.355  41.311  -25.776 1.00 40.81  ?  303  GLN D CG  1 
ATOM   13181 C  CD  . GLN D  1 272 ? 44.563  42.371  -25.000 1.00 44.08  ?  303  GLN D CD  1 
ATOM   13182 O  OE1 . GLN D  1 272 ? 44.551  43.544  -25.367 1.00 44.73  ?  303  GLN D OE1 1 
ATOM   13183 N  NE2 . GLN D  1 272 ? 43.897  41.955  -23.928 1.00 42.10  ?  303  GLN D NE2 1 
ATOM   13184 N  N   . PHE D  1 273 ? 45.549  40.716  -30.601 1.00 41.07  ?  304  PHE D N   1 
ATOM   13185 C  CA  . PHE D  1 273 ? 44.793  40.576  -31.843 1.00 42.54  ?  304  PHE D CA  1 
ATOM   13186 C  C   . PHE D  1 273 ? 44.700  39.129  -32.313 1.00 43.04  ?  304  PHE D C   1 
ATOM   13187 O  O   . PHE D  1 273 ? 43.639  38.680  -32.761 1.00 44.65  ?  304  PHE D O   1 
ATOM   13188 C  CB  . PHE D  1 273 ? 45.451  41.429  -32.926 1.00 41.88  ?  304  PHE D CB  1 
ATOM   13189 C  CG  . PHE D  1 273 ? 44.686  41.475  -34.226 1.00 44.73  ?  304  PHE D CG  1 
ATOM   13190 C  CD1 . PHE D  1 273 ? 43.387  41.953  -34.275 1.00 41.45  ?  304  PHE D CD1 1 
ATOM   13191 C  CD2 . PHE D  1 273 ? 45.283  41.038  -35.399 1.00 42.49  ?  304  PHE D CD2 1 
ATOM   13192 C  CE1 . PHE D  1 273 ? 42.703  42.008  -35.472 1.00 41.83  ?  304  PHE D CE1 1 
ATOM   13193 C  CE2 . PHE D  1 273 ? 44.608  41.091  -36.601 1.00 48.33  ?  304  PHE D CE2 1 
ATOM   13194 C  CZ  . PHE D  1 273 ? 43.315  41.581  -36.638 1.00 46.16  ?  304  PHE D CZ  1 
ATOM   13195 N  N   . ASP D  1 274 ? 45.804  38.398  -32.256 1.00 40.52  ?  305  ASP D N   1 
ATOM   13196 C  CA  . ASP D  1 274 ? 45.854  37.108  -32.928 1.00 41.28  ?  305  ASP D CA  1 
ATOM   13197 C  C   . ASP D  1 274 ? 45.010  36.065  -32.204 1.00 40.44  ?  305  ASP D C   1 
ATOM   13198 O  O   . ASP D  1 274 ? 44.419  35.185  -32.845 1.00 38.20  ?  305  ASP D O   1 
ATOM   13199 C  CB  . ASP D  1 274 ? 47.311  36.662  -33.052 1.00 47.34  ?  305  ASP D CB  1 
ATOM   13200 C  CG  . ASP D  1 274 ? 47.572  35.891  -34.321 1.00 51.81  ?  305  ASP D CG  1 
ATOM   13201 O  OD1 . ASP D  1 274 ? 47.688  36.536  -35.397 1.00 58.43  ?  305  ASP D OD1 1 
ATOM   13202 O  OD2 . ASP D  1 274 ? 47.665  34.646  -34.243 1.00 52.46  -1 305  ASP D OD2 1 
ATOM   13203 N  N   . ASN D  1 275 ? 44.912  36.158  -30.889 1.00 39.72  ?  306  ASN D N   1 
ATOM   13204 C  CA  . ASN D  1 275 ? 44.102  35.232  -30.108 1.00 39.01  ?  306  ASN D CA  1 
ATOM   13205 C  C   . ASN D  1 275 ? 42.860  35.921  -29.553 1.00 37.97  ?  306  ASN D C   1 
ATOM   13206 O  O   . ASN D  1 275 ? 42.430  35.667  -28.427 1.00 34.25  ?  306  ASN D O   1 
ATOM   13207 C  CB  . ASN D  1 275 ? 44.918  34.587  -28.988 1.00 34.70  ?  306  ASN D CB  1 
ATOM   13208 C  CG  . ASN D  1 275 ? 44.255  33.336  -28.462 1.00 41.94  ?  306  ASN D CG  1 
ATOM   13209 O  OD1 . ASN D  1 275 ? 43.522  32.661  -29.192 1.00 41.53  ?  306  ASN D OD1 1 
ATOM   13210 N  ND2 . ASN D  1 275 ? 44.476  33.030  -27.190 1.00 40.00  ?  306  ASN D ND2 1 
ATOM   13211 N  N   . THR D  1 276 ? 42.258  36.795  -30.355 1.00 38.60  ?  307  THR D N   1 
ATOM   13212 C  CA  . THR D  1 276 ? 40.942  37.348  -30.070 1.00 33.25  ?  307  THR D CA  1 
ATOM   13213 C  C   . THR D  1 276 ? 39.964  36.831  -31.115 1.00 30.27  ?  307  THR D C   1 
ATOM   13214 O  O   . THR D  1 276 ? 40.252  36.884  -32.310 1.00 32.94  ?  307  THR D O   1 
ATOM   13215 C  CB  . THR D  1 276 ? 40.969  38.875  -30.105 1.00 37.07  ?  307  THR D CB  1 
ATOM   13216 O  OG1 . THR D  1 276 ? 41.823  39.350  -29.074 1.00 35.05  ?  307  THR D OG1 1 
ATOM   13217 C  CG2 . THR D  1 276 ? 39.557  39.463  -29.918 1.00 31.24  ?  307  THR D CG2 1 
ATOM   13218 N  N   . LEU D  1 277 ? 38.836  36.300  -30.676 1.00 31.26  ?  308  LEU D N   1 
ATOM   13219 C  CA  . LEU D  1 277 ? 37.749  36.008  -31.608 1.00 31.50  ?  308  LEU D CA  1 
ATOM   13220 C  C   . LEU D  1 277 ? 36.859  37.248  -31.681 1.00 29.57  ?  308  LEU D C   1 
ATOM   13221 O  O   . LEU D  1 277 ? 36.268  37.649  -30.674 1.00 30.44  ?  308  LEU D O   1 
ATOM   13222 C  CB  . LEU D  1 277 ? 36.953  34.776  -31.166 1.00 28.67  ?  308  LEU D CB  1 
ATOM   13223 C  CG  . LEU D  1 277 ? 35.567  34.662  -31.836 1.00 31.53  ?  308  LEU D CG  1 
ATOM   13224 C  CD1 . LEU D  1 277 ? 35.730  34.461  -33.332 1.00 29.48  ?  308  LEU D CD1 1 
ATOM   13225 C  CD2 . LEU D  1 277 ? 34.751  33.530  -31.221 1.00 31.63  ?  308  LEU D CD2 1 
ATOM   13226 N  N   . ILE D  1 278 ? 36.786  37.866  -32.855 1.00 32.54  ?  309  ILE D N   1 
ATOM   13227 C  CA  . ILE D  1 278 ? 35.888  38.991  -33.090 1.00 28.85  ?  309  ILE D CA  1 
ATOM   13228 C  C   . ILE D  1 278 ? 34.639  38.466  -33.801 1.00 29.57  ?  309  ILE D C   1 
ATOM   13229 O  O   . ILE D  1 278 ? 34.731  37.860  -34.873 1.00 31.45  ?  309  ILE D O   1 
ATOM   13230 C  CB  . ILE D  1 278 ? 36.563  40.101  -33.912 1.00 30.54  ?  309  ILE D CB  1 
ATOM   13231 C  CG1 . ILE D  1 278 ? 37.862  40.584  -33.242 1.00 27.45  ?  309  ILE D CG1 1 
ATOM   13232 C  CG2 . ILE D  1 278 ? 35.583  41.283  -34.120 1.00 28.11  ?  309  ILE D CG2 1 
ATOM   13233 C  CD1 . ILE D  1 278 ? 38.611  41.604  -34.081 1.00 31.06  ?  309  ILE D CD1 1 
ATOM   13234 N  N   . VAL D  1 279 ? 33.475  38.694  -33.206 1.00 28.12  ?  310  VAL D N   1 
ATOM   13235 C  CA  . VAL D  1 279 ? 32.193  38.353  -33.821 1.00 28.65  ?  310  VAL D CA  1 
ATOM   13236 C  C   . VAL D  1 279 ? 31.454  39.656  -34.084 1.00 26.46  ?  310  VAL D C   1 
ATOM   13237 O  O   . VAL D  1 279 ? 31.193  40.432  -33.153 1.00 29.79  ?  310  VAL D O   1 
ATOM   13238 C  CB  . VAL D  1 279 ? 31.351  37.421  -32.931 1.00 27.89  ?  310  VAL D CB  1 
ATOM   13239 C  CG1 . VAL D  1 279 ? 29.957  37.198  -33.592 1.00 27.56  ?  310  VAL D CG1 1 
ATOM   13240 C  CG2 . VAL D  1 279 ? 32.058  36.095  -32.686 1.00 28.24  ?  310  VAL D CG2 1 
ATOM   13241 N  N   . PHE D  1 280 ? 31.088  39.895  -35.336 1.00 29.56  ?  311  PHE D N   1 
ATOM   13242 C  CA  . PHE D  1 280 ? 30.332  41.082  -35.706 1.00 29.21  ?  311  PHE D CA  1 
ATOM   13243 C  C   . PHE D  1 280 ? 28.993  40.656  -36.291 1.00 29.15  ?  311  PHE D C   1 
ATOM   13244 O  O   . PHE D  1 280 ? 28.966  39.771  -37.150 1.00 27.51  ?  311  PHE D O   1 
ATOM   13245 C  CB  . PHE D  1 280 ? 31.101  41.925  -36.727 1.00 29.09  ?  311  PHE D CB  1 
ATOM   13246 C  CG  . PHE D  1 280 ? 30.279  43.022  -37.352 1.00 30.08  ?  311  PHE D CG  1 
ATOM   13247 C  CD1 . PHE D  1 280 ? 30.193  44.261  -36.747 1.00 31.93  ?  311  PHE D CD1 1 
ATOM   13248 C  CD2 . PHE D  1 280 ? 29.600  42.816  -38.554 1.00 32.05  ?  311  PHE D CD2 1 
ATOM   13249 C  CE1 . PHE D  1 280 ? 29.424  45.278  -37.317 1.00 33.61  ?  311  PHE D CE1 1 
ATOM   13250 C  CE2 . PHE D  1 280 ? 28.836  43.822  -39.122 1.00 31.25  ?  311  PHE D CE2 1 
ATOM   13251 C  CZ  . PHE D  1 280 ? 28.754  45.056  -38.502 1.00 31.03  ?  311  PHE D CZ  1 
ATOM   13252 N  N   . LEU D  1 281 ? 27.902  41.303  -35.852 1.00 28.13  ?  312  LEU D N   1 
ATOM   13253 C  CA  . LEU D  1 281 ? 26.559  41.045  -36.382 1.00 25.69  ?  312  LEU D CA  1 
ATOM   13254 C  C   . LEU D  1 281 ? 25.622  42.204  -36.029 1.00 28.24  ?  312  LEU D C   1 
ATOM   13255 O  O   . LEU D  1 281 ? 25.973  43.106  -35.268 1.00 29.02  ?  312  LEU D O   1 
ATOM   13256 C  CB  . LEU D  1 281 ? 25.993  39.711  -35.851 1.00 26.71  ?  312  LEU D CB  1 
ATOM   13257 C  CG  . LEU D  1 281 ? 25.495  39.664  -34.387 1.00 29.85  ?  312  LEU D CG  1 
ATOM   13258 C  CD1 . LEU D  1 281 ? 24.790  38.329  -34.056 1.00 25.50  ?  312  LEU D CD1 1 
ATOM   13259 C  CD2 . LEU D  1 281 ? 26.637  39.873  -33.365 1.00 29.97  ?  312  LEU D CD2 1 
ATOM   13260 N  N   . SER D  1 282 ? 24.415  42.172  -36.616 1.00 30.81  ?  313  SER D N   1 
ATOM   13261 C  CA  . SER D  1 282 ? 23.318  43.074  -36.272 1.00 26.93  ?  313  SER D CA  1 
ATOM   13262 C  C   . SER D  1 282 ? 22.336  42.353  -35.353 1.00 25.73  ?  313  SER D C   1 
ATOM   13263 O  O   . SER D  1 282 ? 22.191  41.131  -35.426 1.00 26.37  ?  313  SER D O   1 
ATOM   13264 C  CB  . SER D  1 282 ? 22.577  43.543  -37.531 1.00 25.72  ?  313  SER D CB  1 
ATOM   13265 O  OG  . SER D  1 282 ? 21.561  44.472  -37.187 1.00 27.92  ?  313  SER D OG  1 
ATOM   13266 N  N   . ASP D  1 283 ? 21.617  43.125  -34.522 1.00 25.15  ?  314  ASP D N   1 
ATOM   13267 C  CA  . ASP D  1 283 ? 20.617  42.513  -33.599 1.00 25.36  ?  314  ASP D CA  1 
ATOM   13268 C  C   . ASP D  1 283 ? 19.375  42.054  -34.385 1.00 28.18  ?  314  ASP D C   1 
ATOM   13269 O  O   . ASP D  1 283 ? 18.639  41.208  -33.866 1.00 27.71  ?  314  ASP D O   1 
ATOM   13270 C  CB  . ASP D  1 283 ? 20.245  43.418  -32.432 1.00 27.05  ?  314  ASP D CB  1 
ATOM   13271 C  CG  . ASP D  1 283 ? 19.489  44.693  -32.768 1.00 31.17  ?  314  ASP D CG  1 
ATOM   13272 O  OD1 . ASP D  1 283 ? 19.632  45.177  -33.907 1.00 29.55  -1 314  ASP D OD1 1 
ATOM   13273 O  OD2 . ASP D  1 283 ? 18.774  45.193  -31.873 1.00 28.99  ?  314  ASP D OD2 1 
ATOM   13274 N  N   . ASN D  1 284 ? 19.158  42.610  -35.576 1.00 27.84  ?  315  ASN D N   1 
ATOM   13275 C  CA  . ASN D  1 284 ? 17.973  42.278  -36.415 1.00 26.51  ?  315  ASN D CA  1 
ATOM   13276 C  C   . ASN D  1 284 ? 18.114  42.981  -37.768 1.00 28.71  ?  315  ASN D C   1 
ATOM   13277 O  O   . ASN D  1 284 ? 19.050  43.780  -37.954 1.00 28.76  ?  315  ASN D O   1 
ATOM   13278 C  CB  . ASN D  1 284 ? 16.650  42.652  -35.757 1.00 27.47  ?  315  ASN D CB  1 
ATOM   13279 C  CG  . ASN D  1 284 ? 16.660  44.068  -35.230 1.00 30.47  ?  315  ASN D CG  1 
ATOM   13280 O  OD1 . ASN D  1 284 ? 16.604  44.284  -34.015 1.00 27.50  ?  315  ASN D OD1 1 
ATOM   13281 N  ND2 . ASN D  1 284 ? 16.728  45.046  -36.119 1.00 27.79  ?  315  ASN D ND2 1 
ATOM   13282 N  N   . GLY D  1 285 ? 17.155  42.735  -38.662 1.00 30.77  ?  316  GLY D N   1 
ATOM   13283 C  CA  . GLY D  1 285 ? 17.227  43.327  -40.005 1.00 26.98  ?  316  GLY D CA  1 
ATOM   13284 C  C   . GLY D  1 285 ? 17.095  44.839  -39.969 1.00 30.02  ?  316  GLY D C   1 
ATOM   13285 O  O   . GLY D  1 285 ? 16.590  45.372  -38.965 1.00 29.56  ?  316  GLY D O   1 
ATOM   13286 N  N   . GLY D  1 286 ? 17.498  45.504  -41.051 1.00 24.27  ?  317  GLY D N   1 
ATOM   13287 C  CA  . GLY D  1 286 ? 17.376  46.962  -41.133 1.00 27.62  ?  317  GLY D CA  1 
ATOM   13288 C  C   . GLY D  1 286 ? 15.942  47.440  -41.237 1.00 29.87  ?  317  GLY D C   1 
ATOM   13289 O  O   . GLY D  1 286 ? 15.070  46.681  -41.737 1.00 29.16  ?  317  GLY D O   1 
ATOM   13290 N  N   . ASN D  1 287 ? 15.700  48.665  -40.794 1.00 28.83  ?  318  ASN D N   1 
ATOM   13291 C  CA  . ASN D  1 287 ? 14.356  49.263  -40.937 1.00 30.40  ?  318  ASN D CA  1 
ATOM   13292 C  C   . ASN D  1 287 ? 14.419  50.024  -42.256 1.00 34.02  ?  318  ASN D C   1 
ATOM   13293 O  O   . ASN D  1 287 ? 15.061  51.090  -42.271 1.00 31.25  ?  318  ASN D O   1 
ATOM   13294 C  CB  . ASN D  1 287 ? 14.027  50.160  -39.750 1.00 28.69  ?  318  ASN D CB  1 
ATOM   13295 C  CG  . ASN D  1 287 ? 12.618  50.699  -39.782 1.00 35.14  ?  318  ASN D CG  1 
ATOM   13296 O  OD1 . ASN D  1 287 ? 12.037  50.872  -40.859 1.00 33.49  ?  318  ASN D OD1 1 
ATOM   13297 N  ND2 . ASN D  1 287 ? 12.056  50.974  -38.614 1.00 32.38  ?  318  ASN D ND2 1 
ATOM   13298 N  N   . PHE D  1 288 ? 13.805  49.498  -43.314 1.00 32.67  ?  319  PHE D N   1 
ATOM   13299 C  CA  . PHE D  1 288 ? 13.983  50.203  -44.581 1.00 31.08  ?  319  PHE D CA  1 
ATOM   13300 C  C   . PHE D  1 288 ? 13.175  51.494  -44.655 1.00 30.34  ?  319  PHE D C   1 
ATOM   13301 O  O   . PHE D  1 288 ? 13.199  52.160  -45.688 1.00 33.48  ?  319  PHE D O   1 
ATOM   13302 C  CB  . PHE D  1 288 ? 13.729  49.280  -45.805 1.00 31.55  ?  319  PHE D CB  1 
ATOM   13303 C  CG  . PHE D  1 288 ? 12.334  48.627  -45.899 1.00 29.60  ?  319  PHE D CG  1 
ATOM   13304 C  CD1 . PHE D  1 288 ? 11.216  49.181  -45.318 1.00 27.68  ?  319  PHE D CD1 1 
ATOM   13305 C  CD2 . PHE D  1 288 ? 12.179  47.446  -46.646 1.00 32.12  ?  319  PHE D CD2 1 
ATOM   13306 C  CE1 . PHE D  1 288 ? 9.937   48.567  -45.459 1.00 35.04  ?  319  PHE D CE1 1 
ATOM   13307 C  CE2 . PHE D  1 288 ? 10.917  46.823  -46.797 1.00 33.36  ?  319  PHE D CE2 1 
ATOM   13308 C  CZ  . PHE D  1 288 ? 9.799   47.385  -46.196 1.00 30.36  ?  319  PHE D CZ  1 
ATOM   13309 N  N   . ASN D  1 289 ? 12.499  51.886  -43.580 1.00 28.42  ?  320  ASN D N   1 
ATOM   13310 C  CA  . ASN D  1 289 ? 11.940  53.229  -43.508 1.00 33.55  ?  320  ASN D CA  1 
ATOM   13311 C  C   . ASN D  1 289 ? 12.942  54.263  -43.025 1.00 35.24  ?  320  ASN D C   1 
ATOM   13312 O  O   . ASN D  1 289 ? 12.643  55.460  -43.090 1.00 30.51  ?  320  ASN D O   1 
ATOM   13313 C  CB  . ASN D  1 289 ? 10.741  53.266  -42.567 1.00 30.54  ?  320  ASN D CB  1 
ATOM   13314 C  CG  . ASN D  1 289 ? 9.608   52.436  -43.072 1.00 35.07  ?  320  ASN D CG  1 
ATOM   13315 O  OD1 . ASN D  1 289 ? 9.260   52.524  -44.238 1.00 32.77  ?  320  ASN D OD1 1 
ATOM   13316 N  ND2 . ASN D  1 289 ? 9.036   51.611  -42.206 1.00 37.32  ?  320  ASN D ND2 1 
ATOM   13317 N  N   . HIS D  1 290 ? 14.104  53.842  -42.525 1.00 32.61  ?  321  HIS D N   1 
ATOM   13318 C  CA  . HIS D  1 290 ? 15.023  54.789  -41.900 1.00 32.53  ?  321  HIS D CA  1 
ATOM   13319 C  C   . HIS D  1 290 ? 16.444  54.523  -42.356 1.00 37.00  ?  321  HIS D C   1 
ATOM   13320 O  O   . HIS D  1 290 ? 17.362  54.353  -41.548 1.00 35.93  ?  321  HIS D O   1 
ATOM   13321 C  CB  . HIS D  1 290 ? 14.888  54.728  -40.381 1.00 34.74  ?  321  HIS D CB  1 
ATOM   13322 C  CG  . HIS D  1 290 ? 13.518  55.093  -39.894 1.00 38.28  ?  321  HIS D CG  1 
ATOM   13323 N  ND1 . HIS D  1 290 ? 12.680  54.193  -39.268 1.00 39.45  ?  321  HIS D ND1 1 
ATOM   13324 C  CD2 . HIS D  1 290 ? 12.839  56.265  -39.944 1.00 36.79  ?  321  HIS D CD2 1 
ATOM   13325 C  CE1 . HIS D  1 290 ? 11.543  54.795  -38.955 1.00 35.06  ?  321  HIS D CE1 1 
ATOM   13326 N  NE2 . HIS D  1 290 ? 11.616  56.051  -39.352 1.00 38.18  ?  321  HIS D NE2 1 
ATOM   13327 N  N   . GLY D  1 291 ? 16.637  54.499  -43.672 1.00 28.53  ?  322  GLY D N   1 
ATOM   13328 C  CA  . GLY D  1 291 ? 17.955  54.431  -44.276 1.00 34.29  ?  322  GLY D CA  1 
ATOM   13329 C  C   . GLY D  1 291 ? 18.437  53.047  -44.674 1.00 33.51  ?  322  GLY D C   1 
ATOM   13330 O  O   . GLY D  1 291 ? 19.315  52.941  -45.542 1.00 34.19  ?  322  GLY D O   1 
ATOM   13331 N  N   . ALA D  1 292 ? 17.896  51.982  -44.081 1.00 30.88  ?  323  ALA D N   1 
ATOM   13332 C  CA  . ALA D  1 292 ? 18.527  50.684  -44.281 1.00 29.51  ?  323  ALA D CA  1 
ATOM   13333 C  C   . ALA D  1 292 ? 18.112  50.028  -45.600 1.00 31.62  ?  323  ALA D C   1 
ATOM   13334 O  O   . ALA D  1 292 ? 17.077  50.344  -46.205 1.00 30.66  ?  323  ALA D O   1 
ATOM   13335 C  CB  . ALA D  1 292 ? 18.204  49.759  -43.108 1.00 28.36  ?  323  ALA D CB  1 
ATOM   13336 N  N   . ASN D  1 293 ? 18.926  49.061  -46.018 1.00 32.06  ?  324  ASN D N   1 
ATOM   13337 C  CA  . ASN D  1 293 ? 18.711  48.264  -47.219 1.00 28.69  ?  324  ASN D CA  1 
ATOM   13338 C  C   . ASN D  1 293 ? 18.998  46.803  -46.893 1.00 33.24  ?  324  ASN D C   1 
ATOM   13339 O  O   . ASN D  1 293 ? 20.078  46.492  -46.381 1.00 28.75  ?  324  ASN D O   1 
ATOM   13340 C  CB  . ASN D  1 293 ? 19.640  48.744  -48.344 1.00 34.15  ?  324  ASN D CB  1 
ATOM   13341 C  CG  . ASN D  1 293 ? 19.207  48.270  -49.729 1.00 35.25  ?  324  ASN D CG  1 
ATOM   13342 O  OD1 . ASN D  1 293 ? 18.838  47.109  -49.931 1.00 37.95  ?  324  ASN D OD1 1 
ATOM   13343 N  ND2 . ASN D  1 293 ? 19.271  49.169  -50.695 1.00 45.01  ?  324  ASN D ND2 1 
ATOM   13344 N  N   . ASN D  1 294 ? 18.058  45.906  -47.202 1.00 27.84  ?  325  ASN D N   1 
ATOM   13345 C  CA  . ASN D  1 294 ? 18.201  44.496  -46.848 1.00 29.17  ?  325  ASN D CA  1 
ATOM   13346 C  C   . ASN D  1 294 ? 18.403  43.613  -48.062 1.00 28.31  ?  325  ASN D C   1 
ATOM   13347 O  O   . ASN D  1 294 ? 18.316  42.382  -47.942 1.00 28.89  ?  325  ASN D O   1 
ATOM   13348 C  CB  . ASN D  1 294 ? 16.995  43.989  -46.044 1.00 25.60  ?  325  ASN D CB  1 
ATOM   13349 C  CG  . ASN D  1 294 ? 16.882  44.655  -44.690 1.00 27.72  ?  325  ASN D CG  1 
ATOM   13350 O  OD1 . ASN D  1 294 ? 17.883  44.797  -43.962 1.00 27.21  ?  325  ASN D OD1 1 
ATOM   13351 N  ND2 . ASN D  1 294 ? 15.669  45.082  -44.337 1.00 27.28  ?  325  ASN D ND2 1 
ATOM   13352 N  N   . TYR D  1 295 ? 18.681  44.209  -49.213 1.00 27.16  ?  326  TYR D N   1 
ATOM   13353 C  CA  . TYR D  1 295 ? 18.888  43.456  -50.439 1.00 31.62  ?  326  TYR D CA  1 
ATOM   13354 C  C   . TYR D  1 295 ? 19.858  42.298  -50.208 1.00 30.77  ?  326  TYR D C   1 
ATOM   13355 O  O   . TYR D  1 295 ? 20.870  42.466  -49.514 1.00 31.89  ?  326  TYR D O   1 
ATOM   13356 C  CB  . TYR D  1 295 ? 19.423  44.386  -51.529 1.00 33.43  ?  326  TYR D CB  1 
ATOM   13357 C  CG  . TYR D  1 295 ? 19.626  43.709  -52.851 1.00 32.59  ?  326  TYR D CG  1 
ATOM   13358 C  CD1 . TYR D  1 295 ? 18.598  43.642  -53.776 1.00 35.51  ?  326  TYR D CD1 1 
ATOM   13359 C  CD2 . TYR D  1 295 ? 20.839  43.137  -53.175 1.00 36.58  ?  326  TYR D CD2 1 
ATOM   13360 C  CE1 . TYR D  1 295 ? 18.770  43.017  -54.992 1.00 39.75  ?  326  TYR D CE1 1 
ATOM   13361 C  CE2 . TYR D  1 295 ? 21.024  42.507  -54.405 1.00 37.05  ?  326  TYR D CE2 1 
ATOM   13362 C  CZ  . TYR D  1 295 ? 19.983  42.459  -55.304 1.00 35.82  ?  326  TYR D CZ  1 
ATOM   13363 O  OH  . TYR D  1 295 ? 20.148  41.845  -56.517 1.00 43.86  ?  326  TYR D OH  1 
ATOM   13364 N  N   . PRO D  1 296 ? 19.601  41.118  -50.787 1.00 31.49  ?  327  PRO D N   1 
ATOM   13365 C  CA  . PRO D  1 296 ? 18.478  40.757  -51.672 1.00 31.02  ?  327  PRO D CA  1 
ATOM   13366 C  C   . PRO D  1 296 ? 17.290  40.148  -50.936 1.00 32.68  ?  327  PRO D C   1 
ATOM   13367 O  O   . PRO D  1 296 ? 16.429  39.480  -51.535 1.00 33.99  ?  327  PRO D O   1 
ATOM   13368 C  CB  . PRO D  1 296 ? 19.115  39.730  -52.605 1.00 30.92  ?  327  PRO D CB  1 
ATOM   13369 C  CG  . PRO D  1 296 ? 20.021  38.959  -51.647 1.00 30.43  ?  327  PRO D CG  1 
ATOM   13370 C  CD  . PRO D  1 296 ? 20.580  40.018  -50.696 1.00 31.04  ?  327  PRO D CD  1 
ATOM   13371 N  N   . LEU D  1 297 ? 17.202  40.385  -49.634 1.00 31.28  ?  328  LEU D N   1 
ATOM   13372 C  CA  . LEU D  1 297 ? 16.127  39.822  -48.828 1.00 30.53  ?  328  LEU D CA  1 
ATOM   13373 C  C   . LEU D  1 297 ? 14.841  40.628  -48.966 1.00 30.93  ?  328  LEU D C   1 
ATOM   13374 O  O   . LEU D  1 297 ? 14.850  41.836  -49.225 1.00 30.75  ?  328  LEU D O   1 
ATOM   13375 C  CB  . LEU D  1 297 ? 16.532  39.780  -47.354 1.00 28.59  ?  328  LEU D CB  1 
ATOM   13376 C  CG  . LEU D  1 297 ? 17.944  39.255  -47.068 1.00 28.83  ?  328  LEU D CG  1 
ATOM   13377 C  CD1 . LEU D  1 297 ? 18.151  39.129  -45.587 1.00 24.86  ?  328  LEU D CD1 1 
ATOM   13378 C  CD2 . LEU D  1 297 ? 18.129  37.901  -47.727 1.00 28.13  ?  328  LEU D CD2 1 
ATOM   13379 N  N   . LYS D  1 298 ? 13.725  39.953  -48.753 1.00 28.90  ?  329  LYS D N   1 
ATOM   13380 C  CA  . LYS D  1 298 ? 12.439  40.624  -48.711 1.00 24.95  ?  329  LYS D CA  1 
ATOM   13381 C  C   . LYS D  1 298 ? 12.182  41.162  -47.305 1.00 26.69  ?  329  LYS D C   1 
ATOM   13382 O  O   . LYS D  1 298 ? 12.503  40.510  -46.311 1.00 26.37  ?  329  LYS D O   1 
ATOM   13383 C  CB  . LYS D  1 298 ? 11.320  39.654  -49.115 1.00 25.87  ?  329  LYS D CB  1 
ATOM   13384 C  CG  . LYS D  1 298 ? 9.935   40.263  -49.074 1.00 29.99  ?  329  LYS D CG  1 
ATOM   13385 C  CD  . LYS D  1 298 ? 8.842   39.227  -49.356 1.00 30.21  ?  329  LYS D CD  1 
ATOM   13386 C  CE  . LYS D  1 298 ? 8.621   39.012  -50.837 1.00 28.68  ?  329  LYS D CE  1 
ATOM   13387 N  NZ  . LYS D  1 298 ? 7.640   37.905  -51.021 1.00 32.49  ?  329  LYS D NZ  1 
ATOM   13388 N  N   . GLY D  1 299 ? 11.594  42.345  -47.224 1.00 28.18  ?  330  GLY D N   1 
ATOM   13389 C  CA  . GLY D  1 299 ? 11.035  42.795  -45.963 1.00 27.64  ?  330  GLY D CA  1 
ATOM   13390 C  C   . GLY D  1 299 ? 12.003  43.600  -45.116 1.00 29.82  ?  330  GLY D C   1 
ATOM   13391 O  O   . GLY D  1 299 ? 13.087  43.994  -45.550 1.00 27.15  ?  330  GLY D O   1 
ATOM   13392 N  N   . THR D  1 300 ? 11.522  43.908  -43.898 1.00 27.70  ?  331  THR D N   1 
ATOM   13393 C  CA  . THR D  1 300 ? 12.257  44.832  -43.024 1.00 29.63  ?  331  THR D CA  1 
ATOM   13394 C  C   . THR D  1 300 ? 12.235  44.374  -41.578 1.00 31.51  ?  331  THR D C   1 
ATOM   13395 O  O   . THR D  1 300 ? 11.587  43.347  -41.278 1.00 30.90  ?  331  THR D O   1 
ATOM   13396 C  CB  . THR D  1 300 ? 11.554  46.187  -43.173 1.00 28.82  ?  331  THR D CB  1 
ATOM   13397 O  OG1 . THR D  1 300 ? 12.277  47.209  -42.493 1.00 29.05  ?  331  THR D OG1 1 
ATOM   13398 C  CG2 . THR D  1 300 ? 10.133  46.143  -42.636 1.00 28.21  ?  331  THR D CG2 1 
ATOM   13399 N  N   . LYS D  1 301 ? 12.865  45.132  -40.697 1.00 24.66  ?  332  LYS D N   1 
ATOM   13400 C  CA  . LYS D  1 301 ? 12.917  44.868  -39.239 1.00 26.92  ?  332  LYS D CA  1 
ATOM   13401 C  C   . LYS D  1 301 ? 11.533  44.485  -38.708 1.00 26.86  ?  332  LYS D C   1 
ATOM   13402 O  O   . LYS D  1 301 ? 10.568  45.214  -39.004 1.00 29.33  ?  332  LYS D O   1 
ATOM   13403 C  CB  . LYS D  1 301 ? 13.364  46.131  -38.488 1.00 28.65  ?  332  LYS D CB  1 
ATOM   13404 C  CG  . LYS D  1 301 ? 13.105  46.245  -36.998 1.00 28.68  ?  332  LYS D CG  1 
ATOM   13405 C  CD  . LYS D  1 301 ? 13.537  47.586  -36.420 1.00 32.77  ?  332  LYS D CD  1 
ATOM   13406 C  CE  . LYS D  1 301 ? 13.468  47.657  -34.932 1.00 30.42  ?  332  LYS D CE  1 
ATOM   13407 N  NZ  . LYS D  1 301 ? 13.743  48.996  -34.411 1.00 31.87  ?  332  LYS D NZ  1 
ATOM   13408 N  N   . GLY D  1 302 ? 11.462  43.389  -37.972 1.00 24.38  ?  333  GLY D N   1 
ATOM   13409 C  CA  . GLY D  1 302 ? 10.228  42.948  -37.361 1.00 25.43  ?  333  GLY D CA  1 
ATOM   13410 C  C   . GLY D  1 302 ? 9.438   41.911  -38.150 1.00 28.84  ?  333  GLY D C   1 
ATOM   13411 O  O   . GLY D  1 302 ? 8.522   41.301  -37.574 1.00 26.33  ?  333  GLY D O   1 
ATOM   13412 N  N   . ASP D  1 303 ? 9.794   41.732  -39.421 1.00 29.42  ?  334  ASP D N   1 
ATOM   13413 C  CA  . ASP D  1 303 ? 9.137   40.701  -40.267 1.00 29.15  ?  334  ASP D CA  1 
ATOM   13414 C  C   . ASP D  1 303 ? 9.740   39.301  -40.085 1.00 25.59  ?  334  ASP D C   1 
ATOM   13415 O  O   . ASP D  1 303 ? 10.893  39.209  -39.631 1.00 25.39  ?  334  ASP D O   1 
ATOM   13416 C  CB  . ASP D  1 303 ? 9.318   41.076  -41.717 1.00 30.16  ?  334  ASP D CB  1 
ATOM   13417 C  CG  . ASP D  1 303 ? 8.655   42.362  -42.181 1.00 29.59  ?  334  ASP D CG  1 
ATOM   13418 O  OD1 . ASP D  1 303 ? 7.747   42.839  -41.473 1.00 30.34  ?  334  ASP D OD1 1 
ATOM   13419 O  OD2 . ASP D  1 303 ? 9.045   42.849  -43.258 1.00 29.50  -1 334  ASP D OD2 1 
ATOM   13420 N  N   . THR D  1 304 ? 8.993   38.252  -40.402 1.00 27.13  ?  335  THR D N   1 
ATOM   13421 C  CA  . THR D  1 304 ? 9.554   36.904  -40.466 1.00 28.12  ?  335  THR D CA  1 
ATOM   13422 C  C   . THR D  1 304 ? 9.920   36.500  -41.884 1.00 25.38  ?  335  THR D C   1 
ATOM   13423 O  O   . THR D  1 304 ? 10.334  35.354  -42.093 1.00 27.02  ?  335  THR D O   1 
ATOM   13424 C  CB  . THR D  1 304 ? 8.601   35.852  -39.876 1.00 24.36  ?  335  THR D CB  1 
ATOM   13425 O  OG1 . THR D  1 304 ? 7.317   35.967  -40.503 1.00 24.64  ?  335  THR D OG1 1 
ATOM   13426 C  CG2 . THR D  1 304 ? 8.443   36.061  -38.385 1.00 24.74  ?  335  THR D CG2 1 
ATOM   13427 N  N   . TRP D  1 305 ? 9.776   37.404  -42.859 1.00 27.58  ?  336  TRP D N   1 
ATOM   13428 C  CA  . TRP D  1 305 ? 10.600  37.337  -44.059 1.00 28.04  ?  336  TRP D CA  1 
ATOM   13429 C  C   . TRP D  1 305 ? 12.073  37.330  -43.642 1.00 28.34  ?  336  TRP D C   1 
ATOM   13430 O  O   . TRP D  1 305 ? 12.425  37.765  -42.546 1.00 25.00  ?  336  TRP D O   1 
ATOM   13431 C  CB  . TRP D  1 305 ? 10.368  38.541  -44.970 1.00 24.97  ?  336  TRP D CB  1 
ATOM   13432 C  CG  . TRP D  1 305 ? 8.949   38.804  -45.428 1.00 26.89  ?  336  TRP D CG  1 
ATOM   13433 C  CD1 . TRP D  1 305 ? 8.197   39.911  -45.155 1.00 28.02  ?  336  TRP D CD1 1 
ATOM   13434 C  CD2 . TRP D  1 305 ? 8.144   37.967  -46.273 1.00 27.27  ?  336  TRP D CD2 1 
ATOM   13435 N  NE1 . TRP D  1 305 ? 6.970   39.821  -45.781 1.00 26.14  ?  336  TRP D NE1 1 
ATOM   13436 C  CE2 . TRP D  1 305 ? 6.913   38.637  -46.473 1.00 29.63  ?  336  TRP D CE2 1 
ATOM   13437 C  CE3 . TRP D  1 305 ? 8.347   36.719  -46.884 1.00 27.83  ?  336  TRP D CE3 1 
ATOM   13438 C  CZ2 . TRP D  1 305 ? 5.883   38.100  -47.256 1.00 31.07  ?  336  TRP D CZ2 1 
ATOM   13439 C  CZ3 . TRP D  1 305 ? 7.308   36.181  -47.673 1.00 31.59  ?  336  TRP D CZ3 1 
ATOM   13440 C  CH2 . TRP D  1 305 ? 6.096   36.873  -47.838 1.00 29.89  ?  336  TRP D CH2 1 
ATOM   13441 N  N   . GLU D  1 306 ? 12.943  36.859  -44.539 1.00 29.40  ?  337  GLU D N   1 
ATOM   13442 C  CA  . GLU D  1 306 ? 14.368  36.837  -44.200 1.00 27.69  ?  337  GLU D CA  1 
ATOM   13443 C  C   . GLU D  1 306 ? 14.861  38.224  -43.786 1.00 26.12  ?  337  GLU D C   1 
ATOM   13444 O  O   . GLU D  1 306 ? 15.756  38.338  -42.936 1.00 27.99  ?  337  GLU D O   1 
ATOM   13445 C  CB  . GLU D  1 306 ? 15.192  36.325  -45.386 1.00 28.38  ?  337  GLU D CB  1 
ATOM   13446 C  CG  . GLU D  1 306 ? 14.847  34.916  -45.861 1.00 30.12  ?  337  GLU D CG  1 
ATOM   13447 C  CD  . GLU D  1 306 ? 15.333  33.868  -44.889 1.00 31.90  ?  337  GLU D CD  1 
ATOM   13448 O  OE1 . GLU D  1 306 ? 16.510  33.403  -45.021 1.00 30.36  ?  337  GLU D OE1 1 
ATOM   13449 O  OE2 . GLU D  1 306 ? 14.543  33.544  -43.967 1.00 31.61  -1 337  GLU D OE2 1 
ATOM   13450 N  N   . GLY D  1 307 ? 14.293  39.284  -44.374 1.00 29.75  ?  338  GLY D N   1 
ATOM   13451 C  CA  . GLY D  1 307 ? 14.778  40.632  -44.101 1.00 27.92  ?  338  GLY D CA  1 
ATOM   13452 C  C   . GLY D  1 307 ? 14.686  41.039  -42.644 1.00 30.95  ?  338  GLY D C   1 
ATOM   13453 O  O   . GLY D  1 307 ? 15.430  41.928  -42.207 1.00 27.98  ?  338  GLY D O   1 
ATOM   13454 N  N   . GLY D  1 308 ? 13.800  40.397  -41.872 1.00 26.95  ?  339  GLY D N   1 
ATOM   13455 C  CA  . GLY D  1 308 ? 13.615  40.782  -40.484 1.00 25.85  ?  339  GLY D CA  1 
ATOM   13456 C  C   . GLY D  1 308 ? 14.677  40.251  -39.543 1.00 25.44  ?  339  GLY D C   1 
ATOM   13457 O  O   . GLY D  1 308 ? 14.961  40.875  -38.515 1.00 29.76  ?  339  GLY D O   1 
ATOM   13458 N  N   . TYR D  1 309 ? 15.277  39.090  -39.856 1.00 26.35  ?  340  TYR D N   1 
ATOM   13459 C  CA  . TYR D  1 309 ? 16.131  38.462  -38.853 1.00 27.24  ?  340  TYR D CA  1 
ATOM   13460 C  C   . TYR D  1 309 ? 17.315  37.687  -39.426 1.00 28.90  ?  340  TYR D C   1 
ATOM   13461 O  O   . TYR D  1 309 ? 18.015  37.016  -38.653 1.00 28.04  ?  340  TYR D O   1 
ATOM   13462 C  CB  . TYR D  1 309 ? 15.276  37.555  -37.926 1.00 24.57  ?  340  TYR D CB  1 
ATOM   13463 C  CG  . TYR D  1 309 ? 14.631  36.338  -38.570 1.00 28.09  ?  340  TYR D CG  1 
ATOM   13464 C  CD1 . TYR D  1 309 ? 13.494  36.453  -39.375 1.00 25.12  ?  340  TYR D CD1 1 
ATOM   13465 C  CD2 . TYR D  1 309 ? 15.118  35.069  -38.318 1.00 26.94  ?  340  TYR D CD2 1 
ATOM   13466 C  CE1 . TYR D  1 309 ? 12.900  35.312  -39.953 1.00 28.74  ?  340  TYR D CE1 1 
ATOM   13467 C  CE2 . TYR D  1 309 ? 14.543  33.937  -38.881 1.00 26.17  ?  340  TYR D CE2 1 
ATOM   13468 C  CZ  . TYR D  1 309 ? 13.428  34.058  -39.680 1.00 28.25  ?  340  TYR D CZ  1 
ATOM   13469 O  OH  . TYR D  1 309 ? 12.880  32.914  -40.222 1.00 29.26  ?  340  TYR D OH  1 
ATOM   13470 N  N   . ARG D  1 310 ? 17.579  37.768  -40.732 1.00 25.49  ?  341  ARG D N   1 
ATOM   13471 C  CA  . ARG D  1 310 ? 18.842  37.335  -41.318 1.00 29.18  ?  341  ARG D CA  1 
ATOM   13472 C  C   . ARG D  1 310 ? 19.787  38.532  -41.358 1.00 29.80  ?  341  ARG D C   1 
ATOM   13473 O  O   . ARG D  1 310 ? 19.421  39.593  -41.865 1.00 27.81  ?  341  ARG D O   1 
ATOM   13474 C  CB  . ARG D  1 310 ? 18.620  36.775  -42.724 1.00 26.58  ?  341  ARG D CB  1 
ATOM   13475 C  CG  . ARG D  1 310 ? 19.773  35.987  -43.314 1.00 27.61  ?  341  ARG D CG  1 
ATOM   13476 C  CD  . ARG D  1 310 ? 19.302  35.285  -44.606 1.00 28.52  ?  341  ARG D CD  1 
ATOM   13477 N  NE  . ARG D  1 310 ? 20.389  34.769  -45.439 1.00 29.01  ?  341  ARG D NE  1 
ATOM   13478 C  CZ  . ARG D  1 310 ? 20.217  33.907  -46.437 1.00 31.09  ?  341  ARG D CZ  1 
ATOM   13479 N  NH1 . ARG D  1 310 ? 19.020  33.416  -46.729 1.00 28.30  ?  341  ARG D NH1 1 
ATOM   13480 N  NH2 . ARG D  1 310 ? 21.264  33.546  -47.177 1.00 28.52  ?  341  ARG D NH2 1 
ATOM   13481 N  N   . VAL D  1 311 ? 20.993  38.370  -40.814 1.00 27.01  ?  342  VAL D N   1 
ATOM   13482 C  CA  . VAL D  1 311 ? 21.844  39.529  -40.544 1.00 26.73  ?  342  VAL D CA  1 
ATOM   13483 C  C   . VAL D  1 311 ? 23.236  39.242  -41.085 1.00 30.35  ?  342  VAL D C   1 
ATOM   13484 O  O   . VAL D  1 311 ? 23.635  38.077  -41.224 1.00 31.10  ?  342  VAL D O   1 
ATOM   13485 C  CB  . VAL D  1 311 ? 21.923  39.839  -39.026 1.00 26.51  ?  342  VAL D CB  1 
ATOM   13486 C  CG1 . VAL D  1 311 ? 20.554  40.193  -38.455 1.00 24.45  ?  342  VAL D CG1 1 
ATOM   13487 C  CG2 . VAL D  1 311 ? 22.590  38.671  -38.266 1.00 24.97  ?  342  VAL D CG2 1 
ATOM   13488 N  N   . PRO D  1 312 ? 24.019  40.276  -41.371 1.00 31.81  ?  343  PRO D N   1 
ATOM   13489 C  CA  . PRO D  1 312 ? 25.430  40.022  -41.684 1.00 31.93  ?  343  PRO D CA  1 
ATOM   13490 C  C   . PRO D  1 312 ? 26.142  39.555  -40.421 1.00 31.25  ?  343  PRO D C   1 
ATOM   13491 O  O   . PRO D  1 312 ? 25.734  39.872  -39.302 1.00 28.05  ?  343  PRO D O   1 
ATOM   13492 C  CB  . PRO D  1 312 ? 25.956  41.376  -42.189 1.00 32.39  ?  343  PRO D CB  1 
ATOM   13493 C  CG  . PRO D  1 312 ? 24.908  42.387  -41.839 1.00 32.56  ?  343  PRO D CG  1 
ATOM   13494 C  CD  . PRO D  1 312 ? 23.639  41.696  -41.487 1.00 29.97  ?  343  PRO D CD  1 
ATOM   13495 N  N   . MET D  1 313 ? 27.153  38.707  -40.606 1.00 29.40  ?  344  MET D N   1 
ATOM   13496 C  CA  . MET D  1 313 ? 27.930  38.214  -39.478 1.00 26.49  ?  344  MET D CA  1 
ATOM   13497 C  C   . MET D  1 313 ? 29.251  37.668  -39.998 1.00 28.95  ?  344  MET D C   1 
ATOM   13498 O  O   . MET D  1 313 ? 29.292  37.010  -41.045 1.00 27.82  ?  344  MET D O   1 
ATOM   13499 C  CB  . MET D  1 313 ? 27.203  37.110  -38.700 1.00 26.34  ?  344  MET D CB  1 
ATOM   13500 C  CG  . MET D  1 313 ? 28.068  36.394  -37.649 1.00 31.90  ?  344  MET D CG  1 
ATOM   13501 S  SD  . MET D  1 313 ? 27.147  35.596  -36.320 1.00 32.26  ?  344  MET D SD  1 
ATOM   13502 C  CE  . MET D  1 313 ? 27.242  33.916  -36.935 1.00 32.93  ?  344  MET D CE  1 
ATOM   13503 N  N   . PHE D  1 314 ? 30.323  37.921  -39.250 1.00 30.63  ?  345  PHE D N   1 
ATOM   13504 C  CA  . PHE D  1 314 ? 31.584  37.259  -39.524 1.00 29.10  ?  345  PHE D CA  1 
ATOM   13505 C  C   . PHE D  1 314 ? 32.213  36.875  -38.184 1.00 31.75  ?  345  PHE D C   1 
ATOM   13506 O  O   . PHE D  1 314 ? 31.850  37.416  -37.130 1.00 27.84  ?  345  PHE D O   1 
ATOM   13507 C  CB  . PHE D  1 314 ? 32.510  38.140  -40.395 1.00 32.32  ?  345  PHE D CB  1 
ATOM   13508 C  CG  . PHE D  1 314 ? 33.052  39.373  -39.693 1.00 31.53  ?  345  PHE D CG  1 
ATOM   13509 C  CD1 . PHE D  1 314 ? 33.983  39.265  -38.651 1.00 31.98  ?  345  PHE D CD1 1 
ATOM   13510 C  CD2 . PHE D  1 314 ? 32.670  40.639  -40.107 1.00 31.12  ?  345  PHE D CD2 1 
ATOM   13511 C  CE1 . PHE D  1 314 ? 34.485  40.389  -38.012 1.00 29.76  ?  345  PHE D CE1 1 
ATOM   13512 C  CE2 . PHE D  1 314 ? 33.177  41.779  -39.481 1.00 31.76  ?  345  PHE D CE2 1 
ATOM   13513 C  CZ  . PHE D  1 314 ? 34.082  41.653  -38.423 1.00 30.70  ?  345  PHE D CZ  1 
ATOM   13514 N  N   . PHE D  1 315 ? 33.105  35.878  -38.244 1.00 30.37  ?  346  PHE D N   1 
ATOM   13515 C  CA  . PHE D  1 315 ? 34.009  35.483  -37.166 1.00 27.86  ?  346  PHE D CA  1 
ATOM   13516 C  C   . PHE D  1 315 ? 35.423  35.795  -37.623 1.00 32.76  ?  346  PHE D C   1 
ATOM   13517 O  O   . PHE D  1 315 ? 35.804  35.433  -38.740 1.00 35.80  ?  346  PHE D O   1 
ATOM   13518 C  CB  . PHE D  1 315 ? 33.956  33.976  -36.859 1.00 32.99  ?  346  PHE D CB  1 
ATOM   13519 C  CG  . PHE D  1 315 ? 32.766  33.515  -36.031 1.00 34.78  ?  346  PHE D CG  1 
ATOM   13520 C  CD1 . PHE D  1 315 ? 31.611  34.270  -35.923 1.00 33.15  ?  346  PHE D CD1 1 
ATOM   13521 C  CD2 . PHE D  1 315 ? 32.805  32.280  -35.400 1.00 32.37  ?  346  PHE D CD2 1 
ATOM   13522 C  CE1 . PHE D  1 315 ? 30.520  33.816  -35.174 1.00 31.69  ?  346  PHE D CE1 1 
ATOM   13523 C  CE2 . PHE D  1 315 ? 31.721  31.823  -34.661 1.00 37.43  ?  346  PHE D CE2 1 
ATOM   13524 C  CZ  . PHE D  1 315 ? 30.570  32.602  -34.557 1.00 34.19  ?  346  PHE D CZ  1 
ATOM   13525 N  N   . HIS D  1 316 ? 36.214  36.428  -36.766 1.00 30.40  ?  347  HIS D N   1 
ATOM   13526 C  CA  . HIS D  1 316 ? 37.594  36.729  -37.112 1.00 33.74  ?  347  HIS D CA  1 
ATOM   13527 C  C   . HIS D  1 316 ? 38.461  36.333  -35.925 1.00 31.87  ?  347  HIS D C   1 
ATOM   13528 O  O   . HIS D  1 316 ? 38.243  36.815  -34.807 1.00 32.74  ?  347  HIS D O   1 
ATOM   13529 C  CB  . HIS D  1 316 ? 37.760  38.209  -37.480 1.00 29.70  ?  347  HIS D CB  1 
ATOM   13530 C  CG  . HIS D  1 316 ? 39.190  38.631  -37.648 1.00 36.59  ?  347  HIS D CG  1 
ATOM   13531 N  ND1 . HIS D  1 316 ? 40.030  38.856  -36.579 1.00 33.70  ?  347  HIS D ND1 1 
ATOM   13532 C  CD2 . HIS D  1 316 ? 39.926  38.862  -38.762 1.00 36.73  ?  347  HIS D CD2 1 
ATOM   13533 C  CE1 . HIS D  1 316 ? 41.219  39.218  -37.027 1.00 40.27  ?  347  HIS D CE1 1 
ATOM   13534 N  NE2 . HIS D  1 316 ? 41.184  39.230  -38.348 1.00 39.72  ?  347  HIS D NE2 1 
ATOM   13535 N  N   . TRP D  1 317 ? 39.397  35.410  -36.159 1.00 35.04  ?  348  TRP D N   1 
ATOM   13536 C  CA  . TRP D  1 317 ? 40.220  34.797  -35.110 1.00 35.95  ?  348  TRP D CA  1 
ATOM   13537 C  C   . TRP D  1 317 ? 41.458  34.208  -35.772 1.00 36.34  ?  348  TRP D C   1 
ATOM   13538 O  O   . TRP D  1 317 ? 41.461  33.028  -36.148 1.00 34.85  ?  348  TRP D O   1 
ATOM   13539 C  CB  . TRP D  1 317 ? 39.442  33.709  -34.370 1.00 30.94  ?  348  TRP D CB  1 
ATOM   13540 C  CG  . TRP D  1 317 ? 40.118  33.140  -33.167 1.00 37.12  ?  348  TRP D CG  1 
ATOM   13541 C  CD1 . TRP D  1 317 ? 41.184  33.672  -32.481 1.00 36.46  ?  348  TRP D CD1 1 
ATOM   13542 C  CD2 . TRP D  1 317 ? 39.769  31.929  -32.489 1.00 37.05  ?  348  TRP D CD2 1 
ATOM   13543 N  NE1 . TRP D  1 317 ? 41.504  32.865  -31.416 1.00 41.94  ?  348  TRP D NE1 1 
ATOM   13544 C  CE2 . TRP D  1 317 ? 40.653  31.789  -31.400 1.00 40.39  ?  348  TRP D CE2 1 
ATOM   13545 C  CE3 . TRP D  1 317 ? 38.787  30.952  -32.691 1.00 35.79  ?  348  TRP D CE3 1 
ATOM   13546 C  CZ2 . TRP D  1 317 ? 40.586  30.706  -30.522 1.00 36.09  ?  348  TRP D CZ2 1 
ATOM   13547 C  CZ3 . TRP D  1 317 ? 38.713  29.886  -31.814 1.00 39.17  ?  348  TRP D CZ3 1 
ATOM   13548 C  CH2 . TRP D  1 317 ? 39.617  29.766  -30.747 1.00 40.07  ?  348  TRP D CH2 1 
ATOM   13549 N  N   . PRO D  1 318 ? 42.519  35.000  -35.940 1.00 40.16  ?  349  PRO D N   1 
ATOM   13550 C  CA  . PRO D  1 318 ? 43.654  34.551  -36.770 1.00 38.93  ?  349  PRO D CA  1 
ATOM   13551 C  C   . PRO D  1 318 ? 44.272  33.242  -36.309 1.00 40.26  ?  349  PRO D C   1 
ATOM   13552 O  O   . PRO D  1 318 ? 44.719  32.452  -37.145 1.00 41.26  ?  349  PRO D O   1 
ATOM   13553 C  CB  . PRO D  1 318 ? 44.643  35.721  -36.662 1.00 41.08  ?  349  PRO D CB  1 
ATOM   13554 C  CG  . PRO D  1 318 ? 43.783  36.913  -36.306 1.00 40.12  ?  349  PRO D CG  1 
ATOM   13555 C  CD  . PRO D  1 318 ? 42.709  36.362  -35.411 1.00 39.32  ?  349  PRO D CD  1 
ATOM   13556 N  N   . LYS D  1 319 ? 44.288  32.977  -35.006 1.00 42.41  ?  350  LYS D N   1 
ATOM   13557 C  CA  . LYS D  1 319 ? 44.893  31.747  -34.504 1.00 40.51  ?  350  LYS D CA  1 
ATOM   13558 C  C   . LYS D  1 319 ? 44.313  30.514  -35.179 1.00 46.11  ?  350  LYS D C   1 
ATOM   13559 O  O   . LYS D  1 319 ? 45.049  29.577  -35.508 1.00 46.42  ?  350  LYS D O   1 
ATOM   13560 C  CB  . LYS D  1 319 ? 44.714  31.659  -32.983 1.00 42.76  ?  350  LYS D CB  1 
ATOM   13561 C  CG  . LYS D  1 319 ? 45.903  31.079  -32.221 1.00 48.27  ?  350  LYS D CG  1 
ATOM   13562 C  CD  . LYS D  1 319 ? 45.475  30.618  -30.824 1.00 52.31  ?  350  LYS D CD  1 
ATOM   13563 C  CE  . LYS D  1 319 ? 46.495  29.674  -30.181 1.00 54.88  ?  350  LYS D CE  1 
ATOM   13564 N  NZ  . LYS D  1 319 ? 45.862  28.504  -29.486 1.00 62.66  ?  350  LYS D NZ  1 
ATOM   13565 N  N   . LYS D  1 320 ? 43.001  30.507  -35.432 1.00 42.47  ?  351  LYS D N   1 
ATOM   13566 C  CA  . LYS D  1 320 ? 42.324  29.272  -35.809 1.00 38.99  ?  351  LYS D CA  1 
ATOM   13567 C  C   . LYS D  1 320 ? 41.451  29.360  -37.055 1.00 42.70  ?  351  LYS D C   1 
ATOM   13568 O  O   . LYS D  1 320 ? 41.247  28.344  -37.725 1.00 40.27  ?  351  LYS D O   1 
ATOM   13569 C  CB  . LYS D  1 320 ? 41.460  28.772  -34.653 1.00 40.74  ?  351  LYS D CB  1 
ATOM   13570 C  CG  . LYS D  1 320 ? 42.223  28.549  -33.373 1.00 46.63  ?  351  LYS D CG  1 
ATOM   13571 C  CD  . LYS D  1 320 ? 41.996  27.157  -32.810 1.00 50.96  ?  351  LYS D CD  1 
ATOM   13572 C  CE  . LYS D  1 320 ? 43.273  26.321  -32.912 1.00 62.06  ?  351  LYS D CE  1 
ATOM   13573 N  NZ  . LYS D  1 320 ? 43.110  24.919  -32.398 1.00 60.71  ?  351  LYS D NZ  1 
ATOM   13574 N  N   . ILE D  1 321 ? 40.910  30.533  -37.375 1.00 36.66  ?  352  ILE D N   1 
ATOM   13575 C  CA  . ILE D  1 321 ? 39.969  30.664  -38.488 1.00 37.39  ?  352  ILE D CA  1 
ATOM   13576 C  C   . ILE D  1 321 ? 40.736  31.148  -39.709 1.00 37.17  ?  352  ILE D C   1 
ATOM   13577 O  O   . ILE D  1 321 ? 41.348  32.223  -39.681 1.00 38.68  ?  352  ILE D O   1 
ATOM   13578 C  CB  . ILE D  1 321 ? 38.807  31.611  -38.142 1.00 34.11  ?  352  ILE D CB  1 
ATOM   13579 C  CG1 . ILE D  1 321 ? 37.979  31.019  -36.989 1.00 36.12  ?  352  ILE D CG1 1 
ATOM   13580 C  CG2 . ILE D  1 321 ? 37.928  31.850  -39.380 1.00 38.01  ?  352  ILE D CG2 1 
ATOM   13581 C  CD1 . ILE D  1 321 ? 36.699  31.810  -36.618 1.00 35.09  ?  352  ILE D CD1 1 
ATOM   13582 N  N   . LYS D  1 322 ? 40.688  30.367  -40.786 1.00 39.25  ?  353  LYS D N   1 
ATOM   13583 C  CA  . LYS D  1 322 ? 41.403  30.711  -42.008 1.00 43.23  ?  353  LYS D CA  1 
ATOM   13584 C  C   . LYS D  1 322 ? 40.780  31.938  -42.676 1.00 41.96  ?  353  LYS D C   1 
ATOM   13585 O  O   . LYS D  1 322 ? 39.618  32.285  -42.443 1.00 41.96  ?  353  LYS D O   1 
ATOM   13586 C  CB  . LYS D  1 322 ? 41.400  29.524  -42.973 1.00 42.49  ?  353  LYS D CB  1 
ATOM   13587 N  N   . LYS D  1 323 ? 41.576  32.605  -43.512 1.00 39.69  ?  354  LYS D N   1 
ATOM   13588 C  CA  . LYS D  1 323 ? 41.096  33.763  -44.247 1.00 40.28  ?  354  LYS D CA  1 
ATOM   13589 C  C   . LYS D  1 323 ? 40.206  33.334  -45.411 1.00 39.37  ?  354  LYS D C   1 
ATOM   13590 O  O   . LYS D  1 323 ? 40.170  32.166  -45.804 1.00 36.05  ?  354  LYS D O   1 
ATOM   13591 C  CB  . LYS D  1 323 ? 42.250  34.596  -44.797 1.00 43.90  ?  354  LYS D CB  1 
ATOM   13592 C  CG  . LYS D  1 323 ? 43.382  34.870  -43.825 1.00 47.79  ?  354  LYS D CG  1 
ATOM   13593 C  CD  . LYS D  1 323 ? 44.638  35.264  -44.588 1.00 49.61  ?  354  LYS D CD  1 
ATOM   13594 C  CE  . LYS D  1 323 ? 45.799  35.525  -43.622 1.00 50.19  ?  354  LYS D CE  1 
ATOM   13595 N  NZ  . LYS D  1 323 ? 45.664  36.865  -43.007 1.00 53.03  ?  354  LYS D NZ  1 
ATOM   13596 N  N   . ASP D  1 324 ? 39.501  34.327  -45.970 1.00 41.76  ?  355  ASP D N   1 
ATOM   13597 C  CA  . ASP D  1 324 ? 38.650  34.194  -47.167 1.00 43.16  ?  355  ASP D CA  1 
ATOM   13598 C  C   . ASP D  1 324 ? 37.639  33.061  -47.053 1.00 43.02  ?  355  ASP D C   1 
ATOM   13599 O  O   . ASP D  1 324 ? 37.214  32.499  -48.066 1.00 46.82  ?  355  ASP D O   1 
ATOM   13600 C  CB  . ASP D  1 324 ? 39.464  33.996  -48.454 1.00 46.02  ?  355  ASP D CB  1 
ATOM   13601 C  CG  . ASP D  1 324 ? 40.611  34.970  -48.590 1.00 51.95  ?  355  ASP D CG  1 
ATOM   13602 O  OD1 . ASP D  1 324 ? 40.391  36.191  -48.449 1.00 51.98  ?  355  ASP D OD1 1 
ATOM   13603 O  OD2 . ASP D  1 324 ? 41.736  34.503  -48.890 1.00 59.85  -1 355  ASP D OD2 1 
ATOM   13604 N  N   . GLN D  1 325 ? 37.226  32.721  -45.839 1.00 38.14  ?  356  GLN D N   1 
ATOM   13605 C  CA  . GLN D  1 325 ? 36.299  31.617  -45.664 1.00 39.26  ?  356  GLN D CA  1 
ATOM   13606 C  C   . GLN D  1 325 ? 34.867  32.149  -45.811 1.00 40.65  ?  356  GLN D C   1 
ATOM   13607 O  O   . GLN D  1 325 ? 34.559  33.273  -45.391 1.00 37.08  ?  356  GLN D O   1 
ATOM   13608 C  CB  . GLN D  1 325 ? 36.487  30.992  -44.277 1.00 40.73  ?  356  GLN D CB  1 
ATOM   13609 C  CG  . GLN D  1 325 ? 35.203  30.372  -43.746 1.00 48.82  ?  356  GLN D CG  1 
ATOM   13610 C  CD  . GLN D  1 325 ? 35.406  29.148  -42.851 1.00 53.88  ?  356  GLN D CD  1 
ATOM   13611 O  OE1 . GLN D  1 325 ? 36.459  28.489  -42.875 1.00 59.06  ?  356  GLN D OE1 1 
ATOM   13612 N  NE2 . GLN D  1 325 ? 34.341  28.780  -42.125 1.00 41.00  ?  356  GLN D NE2 1 
ATOM   13613 N  N   . ARG D  1 326 ? 33.994  31.351  -46.422 1.00 36.07  ?  357  ARG D N   1 
ATOM   13614 C  CA  . ARG D  1 326 ? 32.561  31.637  -46.474 1.00 37.32  ?  357  ARG D CA  1 
ATOM   13615 C  C   . ARG D  1 326 ? 31.820  30.441  -45.902 1.00 38.11  ?  357  ARG D C   1 
ATOM   13616 O  O   . ARG D  1 326 ? 31.955  29.326  -46.411 1.00 38.76  ?  357  ARG D O   1 
ATOM   13617 C  CB  . ARG D  1 326 ? 32.089  31.919  -47.903 1.00 39.62  ?  357  ARG D CB  1 
ATOM   13618 C  CG  . ARG D  1 326 ? 32.664  33.209  -48.484 1.00 42.03  ?  357  ARG D CG  1 
ATOM   13619 C  CD  . ARG D  1 326 ? 32.203  33.437  -49.928 1.00 47.85  ?  357  ARG D CD  1 
ATOM   13620 N  NE  . ARG D  1 326 ? 30.882  34.052  -49.983 1.00 49.96  ?  357  ARG D NE  1 
ATOM   13621 C  CZ  . ARG D  1 326 ? 30.650  35.338  -49.749 1.00 47.53  ?  357  ARG D CZ  1 
ATOM   13622 N  NH1 . ARG D  1 326 ? 31.624  36.164  -49.402 1.00 44.24  ?  357  ARG D NH1 1 
ATOM   13623 N  NH2 . ARG D  1 326 ? 29.407  35.799  -49.840 1.00 41.83  ?  357  ARG D NH2 1 
ATOM   13624 N  N   . PHE D  1 327 ? 31.054  30.669  -44.839 1.00 33.89  ?  358  PHE D N   1 
ATOM   13625 C  CA  . PHE D  1 327 ? 30.297  29.619  -44.169 1.00 34.03  ?  358  PHE D CA  1 
ATOM   13626 C  C   . PHE D  1 327 ? 28.846  29.752  -44.598 1.00 31.90  ?  358  PHE D C   1 
ATOM   13627 O  O   . PHE D  1 327 ? 28.186  30.741  -44.268 1.00 35.35  ?  358  PHE D O   1 
ATOM   13628 C  CB  . PHE D  1 327 ? 30.440  29.717  -42.652 1.00 31.50  ?  358  PHE D CB  1 
ATOM   13629 C  CG  . PHE D  1 327 ? 29.995  28.484  -41.935 1.00 32.48  ?  358  PHE D CG  1 
ATOM   13630 C  CD1 . PHE D  1 327 ? 30.829  27.371  -41.847 1.00 36.83  ?  358  PHE D CD1 1 
ATOM   13631 C  CD2 . PHE D  1 327 ? 28.746  28.427  -41.359 1.00 31.27  ?  358  PHE D CD2 1 
ATOM   13632 C  CE1 . PHE D  1 327 ? 30.421  26.230  -41.194 1.00 34.70  ?  358  PHE D CE1 1 
ATOM   13633 C  CE2 . PHE D  1 327 ? 28.328  27.287  -40.703 1.00 32.74  ?  358  PHE D CE2 1 
ATOM   13634 C  CZ  . PHE D  1 327 ? 29.169  26.182  -40.626 1.00 35.34  ?  358  PHE D CZ  1 
ATOM   13635 N  N   . ASP D  1 328 ? 28.354  28.773  -45.355 1.00 32.28  ?  359  ASP D N   1 
ATOM   13636 C  CA  . ASP D  1 328 ? 27.048  28.909  -45.998 1.00 32.59  ?  359  ASP D CA  1 
ATOM   13637 C  C   . ASP D  1 328 ? 25.934  28.140  -45.296 1.00 33.55  ?  359  ASP D C   1 
ATOM   13638 O  O   . ASP D  1 328 ? 24.764  28.317  -45.653 1.00 37.57  ?  359  ASP D O   1 
ATOM   13639 C  CB  . ASP D  1 328 ? 27.118  28.459  -47.470 1.00 36.18  ?  359  ASP D CB  1 
ATOM   13640 C  CG  . ASP D  1 328 ? 27.902  29.427  -48.359 1.00 38.65  ?  359  ASP D CG  1 
ATOM   13641 O  OD1 . ASP D  1 328 ? 27.952  30.646  -48.072 1.00 37.69  ?  359  ASP D OD1 1 
ATOM   13642 O  OD2 . ASP D  1 328 ? 28.435  28.975  -49.385 1.00 38.22  -1 359  ASP D OD2 1 
ATOM   13643 N  N   . PHE D  1 329 ? 26.248  27.283  -44.338 1.00 31.43  ?  360  PHE D N   1 
ATOM   13644 C  CA  . PHE D  1 329 ? 25.186  26.610  -43.602 1.00 35.93  ?  360  PHE D CA  1 
ATOM   13645 C  C   . PHE D  1 329 ? 24.534  27.592  -42.628 1.00 33.61  ?  360  PHE D C   1 
ATOM   13646 O  O   . PHE D  1 329 ? 25.222  28.448  -42.059 1.00 32.48  ?  360  PHE D O   1 
ATOM   13647 C  CB  . PHE D  1 329 ? 25.737  25.410  -42.837 1.00 36.21  ?  360  PHE D CB  1 
ATOM   13648 C  CG  . PHE D  1 329 ? 26.416  24.390  -43.712 1.00 43.15  ?  360  PHE D CG  1 
ATOM   13649 C  CD1 . PHE D  1 329 ? 25.688  23.672  -44.653 1.00 41.62  ?  360  PHE D CD1 1 
ATOM   13650 C  CD2 . PHE D  1 329 ? 27.778  24.147  -43.592 1.00 41.23  ?  360  PHE D CD2 1 
ATOM   13651 C  CE1 . PHE D  1 329 ? 26.309  22.725  -45.461 1.00 46.48  ?  360  PHE D CE1 1 
ATOM   13652 C  CE2 . PHE D  1 329 ? 28.402  23.206  -44.393 1.00 41.20  ?  360  PHE D CE2 1 
ATOM   13653 C  CZ  . PHE D  1 329 ? 27.665  22.492  -45.327 1.00 43.81  ?  360  PHE D CZ  1 
ATOM   13654 N  N   . PRO D  1 330 ? 23.222  27.500  -42.423 1.00 34.23  ?  361  PRO D N   1 
ATOM   13655 C  CA  . PRO D  1 330 ? 22.554  28.400  -41.471 1.00 31.76  ?  361  PRO D CA  1 
ATOM   13656 C  C   . PRO D  1 330 ? 23.052  28.226  -40.040 1.00 33.67  ?  361  PRO D C   1 
ATOM   13657 O  O   . PRO D  1 330 ? 23.329  27.112  -39.582 1.00 31.91  ?  361  PRO D O   1 
ATOM   13658 C  CB  . PRO D  1 330 ? 21.074  28.005  -41.599 1.00 28.89  ?  361  PRO D CB  1 
ATOM   13659 C  CG  . PRO D  1 330 ? 21.102  26.618  -42.159 1.00 33.03  ?  361  PRO D CG  1 
ATOM   13660 C  CD  . PRO D  1 330 ? 22.252  26.646  -43.129 1.00 29.58  ?  361  PRO D CD  1 
ATOM   13661 N  N   . VAL D  1 331 ? 23.178  29.359  -39.338 1.00 29.99  ?  362  VAL D N   1 
ATOM   13662 C  CA  . VAL D  1 331 ? 23.581  29.410  -37.938 1.00 29.98  ?  362  VAL D CA  1 
ATOM   13663 C  C   . VAL D  1 331 ? 22.696  30.440  -37.241 1.00 31.49  ?  362  VAL D C   1 
ATOM   13664 O  O   . VAL D  1 331 ? 22.000  31.221  -37.886 1.00 29.53  ?  362  VAL D O   1 
ATOM   13665 C  CB  . VAL D  1 331 ? 25.078  29.772  -37.771 1.00 32.28  ?  362  VAL D CB  1 
ATOM   13666 C  CG1 . VAL D  1 331 ? 25.961  28.709  -38.422 1.00 28.31  ?  362  VAL D CG1 1 
ATOM   13667 C  CG2 . VAL D  1 331 ? 25.375  31.157  -38.369 1.00 31.69  ?  362  VAL D CG2 1 
ATOM   13668 N  N   . SER D  1 332 ? 22.724  30.437  -35.908 1.00 30.74  ?  363  SER D N   1 
ATOM   13669 C  CA  . SER D  1 332 ? 21.874  31.315  -35.107 1.00 29.36  ?  363  SER D CA  1 
ATOM   13670 C  C   . SER D  1 332 ? 22.717  32.117  -34.130 1.00 31.61  ?  363  SER D C   1 
ATOM   13671 O  O   . SER D  1 332 ? 23.741  31.635  -33.641 1.00 30.29  ?  363  SER D O   1 
ATOM   13672 C  CB  . SER D  1 332 ? 20.843  30.515  -34.306 1.00 27.81  ?  363  SER D CB  1 
ATOM   13673 O  OG  . SER D  1 332 ? 20.116  31.348  -33.417 1.00 30.78  ?  363  SER D OG  1 
ATOM   13674 N  N   . SER D  1 333 ? 22.251  33.328  -33.796 1.00 29.98  ?  364  SER D N   1 
ATOM   13675 C  CA  . SER D  1 333 ? 22.889  34.064  -32.703 1.00 31.20  ?  364  SER D CA  1 
ATOM   13676 C  C   . SER D  1 333 ? 22.777  33.309  -31.388 1.00 31.52  ?  364  SER D C   1 
ATOM   13677 O  O   . SER D  1 333 ? 23.561  33.557  -30.468 1.00 30.34  ?  364  SER D O   1 
ATOM   13678 C  CB  . SER D  1 333 ? 22.265  35.452  -32.565 1.00 27.85  ?  364  SER D CB  1 
ATOM   13679 O  OG  . SER D  1 333 ? 20.913  35.319  -32.178 1.00 29.19  ?  364  SER D OG  1 
ATOM   13680 N  N   . LEU D  1 334 ? 21.828  32.376  -31.286 1.00 30.14  ?  365  LEU D N   1 
ATOM   13681 C  CA  . LEU D  1 334 ? 21.764  31.502  -30.122 1.00 32.47  ?  365  LEU D CA  1 
ATOM   13682 C  C   . LEU D  1 334 ? 23.014  30.651  -29.968 1.00 32.06  ?  365  LEU D C   1 
ATOM   13683 O  O   . LEU D  1 334 ? 23.258  30.122  -28.874 1.00 32.84  ?  365  LEU D O   1 
ATOM   13684 C  CB  . LEU D  1 334 ? 20.530  30.603  -30.216 1.00 29.71  ?  365  LEU D CB  1 
ATOM   13685 C  CG  . LEU D  1 334 ? 19.191  31.335  -30.137 1.00 33.42  ?  365  LEU D CG  1 
ATOM   13686 C  CD1 . LEU D  1 334 ? 18.050  30.471  -30.671 1.00 29.95  ?  365  LEU D CD1 1 
ATOM   13687 C  CD2 . LEU D  1 334 ? 18.910  31.724  -28.694 1.00 29.56  ?  365  LEU D CD2 1 
ATOM   13688 N  N   . ASP D  1 335 ? 23.819  30.510  -31.027 1.00 31.02  ?  366  ASP D N   1 
ATOM   13689 C  CA  . ASP D  1 335 ? 25.013  29.679  -30.936 1.00 31.14  ?  366  ASP D CA  1 
ATOM   13690 C  C   . ASP D  1 335 ? 26.161  30.371  -30.212 1.00 32.74  ?  366  ASP D C   1 
ATOM   13691 O  O   . ASP D  1 335 ? 27.107  29.695  -29.790 1.00 34.41  ?  366  ASP D O   1 
ATOM   13692 C  CB  . ASP D  1 335 ? 25.479  29.250  -32.328 1.00 30.94  ?  366  ASP D CB  1 
ATOM   13693 C  CG  . ASP D  1 335 ? 24.402  28.518  -33.110 1.00 35.12  ?  366  ASP D CG  1 
ATOM   13694 O  OD1 . ASP D  1 335 ? 23.536  27.832  -32.505 1.00 34.28  ?  366  ASP D OD1 1 
ATOM   13695 O  OD2 . ASP D  1 335 ? 24.438  28.625  -34.358 1.00 30.31  -1 366  ASP D OD2 1 
ATOM   13696 N  N   . LEU D  1 336 ? 26.101  31.693  -30.039 1.00 35.15  ?  367  LEU D N   1 
ATOM   13697 C  CA  . LEU D  1 336 ? 27.211  32.403  -29.396 1.00 32.48  ?  367  LEU D CA  1 
ATOM   13698 C  C   . LEU D  1 336 ? 27.440  31.912  -27.968 1.00 35.26  ?  367  LEU D C   1 
ATOM   13699 O  O   . LEU D  1 336 ? 28.575  31.629  -27.578 1.00 33.37  ?  367  LEU D O   1 
ATOM   13700 C  CB  . LEU D  1 336 ? 26.950  33.910  -29.413 1.00 33.54  ?  367  LEU D CB  1 
ATOM   13701 C  CG  . LEU D  1 336 ? 26.734  34.486  -30.820 1.00 35.34  ?  367  LEU D CG  1 
ATOM   13702 C  CD1 . LEU D  1 336 ? 26.687  35.995  -30.761 1.00 29.36  ?  367  LEU D CD1 1 
ATOM   13703 C  CD2 . LEU D  1 336 ? 27.870  34.025  -31.743 1.00 31.20  ?  367  LEU D CD2 1 
ATOM   13704 N  N   . TYR D  1 337 ? 26.373  31.802  -27.175 1.00 32.87  ?  368  TYR D N   1 
ATOM   13705 C  CA  . TYR D  1 337 ? 26.513  31.384  -25.778 1.00 32.70  ?  368  TYR D CA  1 
ATOM   13706 C  C   . TYR D  1 337 ? 27.254  30.054  -25.639 1.00 37.24  ?  368  TYR D C   1 
ATOM   13707 O  O   . TYR D  1 337 ? 28.337  30.033  -25.018 1.00 35.62  ?  368  TYR D O   1 
ATOM   13708 C  CB  . TYR D  1 337 ? 25.117  31.397  -25.133 1.00 32.28  ?  368  TYR D CB  1 
ATOM   13709 C  CG  . TYR D  1 337 ? 24.985  31.275  -23.620 1.00 35.07  ?  368  TYR D CG  1 
ATOM   13710 C  CD1 . TYR D  1 337 ? 25.737  30.354  -22.876 1.00 34.95  ?  368  TYR D CD1 1 
ATOM   13711 C  CD2 . TYR D  1 337 ? 24.049  32.047  -22.940 1.00 33.78  ?  368  TYR D CD2 1 
ATOM   13712 C  CE1 . TYR D  1 337 ? 25.567  30.242  -21.487 1.00 33.47  ?  368  TYR D CE1 1 
ATOM   13713 C  CE2 . TYR D  1 337 ? 23.885  31.955  -21.579 1.00 34.96  ?  368  TYR D CE2 1 
ATOM   13714 C  CZ  . TYR D  1 337 ? 24.632  31.048  -20.853 1.00 36.62  ?  368  TYR D CZ  1 
ATOM   13715 O  OH  . TYR D  1 337 ? 24.432  30.973  -19.490 1.00 40.07  ?  368  TYR D OH  1 
ATOM   13716 N  N   . PRO D  1 338 ? 26.773  28.934  -26.195 1.00 34.55  ?  369  PRO D N   1 
ATOM   13717 C  CA  . PRO D  1 338 ? 27.541  27.683  -26.056 1.00 34.79  ?  369  PRO D CA  1 
ATOM   13718 C  C   . PRO D  1 338 ? 28.871  27.726  -26.772 1.00 35.56  ?  369  PRO D C   1 
ATOM   13719 O  O   . PRO D  1 338 ? 29.825  27.064  -26.337 1.00 37.04  ?  369  PRO D O   1 
ATOM   13720 C  CB  . PRO D  1 338 ? 26.617  26.624  -26.678 1.00 38.22  ?  369  PRO D CB  1 
ATOM   13721 C  CG  . PRO D  1 338 ? 25.705  27.393  -27.564 1.00 34.98  ?  369  PRO D CG  1 
ATOM   13722 C  CD  . PRO D  1 338 ? 25.498  28.706  -26.904 1.00 33.30  ?  369  PRO D CD  1 
ATOM   13723 N  N   . THR D  1 339 ? 28.969  28.470  -27.870 1.00 32.29  ?  370  THR D N   1 
ATOM   13724 C  CA  . THR D  1 339 ? 30.255  28.574  -28.544 1.00 32.47  ?  370  THR D CA  1 
ATOM   13725 C  C   . THR D  1 339 ? 31.264  29.294  -27.663 1.00 37.46  ?  370  THR D C   1 
ATOM   13726 O  O   . THR D  1 339 ? 32.388  28.815  -27.478 1.00 35.52  ?  370  THR D O   1 
ATOM   13727 C  CB  . THR D  1 339 ? 30.104  29.276  -29.886 1.00 35.77  ?  370  THR D CB  1 
ATOM   13728 O  OG1 . THR D  1 339 ? 29.231  28.501  -30.734 1.00 34.20  ?  370  THR D OG1 1 
ATOM   13729 C  CG2 . THR D  1 339 ? 31.467  29.452  -30.552 1.00 33.29  ?  370  THR D CG2 1 
ATOM   13730 N  N   . PHE D  1 340 ? 30.864  30.427  -27.080 1.00 33.28  ?  371  PHE D N   1 
ATOM   13731 C  CA  . PHE D  1 340 ? 31.772  31.210  -26.242 1.00 34.02  ?  371  PHE D CA  1 
ATOM   13732 C  C   . PHE D  1 340 ? 32.167  30.457  -24.973 1.00 35.19  ?  371  PHE D C   1 
ATOM   13733 O  O   . PHE D  1 340 ? 33.356  30.392  -24.621 1.00 38.00  ?  371  PHE D O   1 
ATOM   13734 C  CB  . PHE D  1 340 ? 31.117  32.548  -25.878 1.00 34.27  ?  371  PHE D CB  1 
ATOM   13735 C  CG  . PHE D  1 340 ? 31.000  33.515  -27.034 1.00 32.66  ?  371  PHE D CG  1 
ATOM   13736 C  CD1 . PHE D  1 340 ? 31.644  33.268  -28.243 1.00 32.13  ?  371  PHE D CD1 1 
ATOM   13737 C  CD2 . PHE D  1 340 ? 30.269  34.680  -26.896 1.00 32.48  ?  371  PHE D CD2 1 
ATOM   13738 C  CE1 . PHE D  1 340 ? 31.547  34.162  -29.288 1.00 31.45  ?  371  PHE D CE1 1 
ATOM   13739 C  CE2 . PHE D  1 340 ? 30.166  35.582  -27.945 1.00 31.82  ?  371  PHE D CE2 1 
ATOM   13740 C  CZ  . PHE D  1 340 ? 30.808  35.322  -29.140 1.00 31.08  ?  371  PHE D CZ  1 
ATOM   13741 N  N   . THR D  1 341 ? 31.184  29.912  -24.239 1.00 31.86  ?  372  THR D N   1 
ATOM   13742 C  CA  . THR D  1 341 ? 31.529  29.201  -23.011 1.00 37.12  ?  372  THR D CA  1 
ATOM   13743 C  C   . THR D  1 341 ? 32.378  27.977  -23.313 1.00 41.36  ?  372  THR D C   1 
ATOM   13744 O  O   . THR D  1 341 ? 33.215  27.581  -22.489 1.00 42.83  ?  372  THR D O   1 
ATOM   13745 C  CB  . THR D  1 341 ? 30.274  28.796  -22.234 1.00 39.52  ?  372  THR D CB  1 
ATOM   13746 O  OG1 . THR D  1 341 ? 29.444  27.968  -23.048 1.00 38.40  ?  372  THR D OG1 1 
ATOM   13747 C  CG2 . THR D  1 341 ? 29.486  30.033  -21.794 1.00 38.72  ?  372  THR D CG2 1 
ATOM   13748 N  N   . GLY D  1 342 ? 32.199  27.388  -24.495 1.00 39.76  ?  373  GLY D N   1 
ATOM   13749 C  CA  . GLY D  1 342 ? 33.080  26.339  -24.968 1.00 40.55  ?  373  GLY D CA  1 
ATOM   13750 C  C   . GLY D  1 342 ? 34.510  26.829  -25.081 1.00 45.35  ?  373  GLY D C   1 
ATOM   13751 O  O   . GLY D  1 342 ? 35.424  26.253  -24.480 1.00 46.01  ?  373  GLY D O   1 
ATOM   13752 N  N   . LEU D  1 343 ? 34.709  27.916  -25.834 1.00 40.69  ?  374  LEU D N   1 
ATOM   13753 C  CA  . LEU D  1 343 ? 36.045  28.486  -25.979 1.00 45.20  ?  374  LEU D CA  1 
ATOM   13754 C  C   . LEU D  1 343 ? 36.653  28.834  -24.623 1.00 43.13  ?  374  LEU D C   1 
ATOM   13755 O  O   . LEU D  1 343 ? 37.862  28.691  -24.414 1.00 43.37  ?  374  LEU D O   1 
ATOM   13756 C  CB  . LEU D  1 343 ? 35.972  29.724  -26.864 1.00 39.87  ?  374  LEU D CB  1 
ATOM   13757 C  CG  . LEU D  1 343 ? 35.603  29.399  -28.302 1.00 41.07  ?  374  LEU D CG  1 
ATOM   13758 C  CD1 . LEU D  1 343 ? 35.381  30.678  -29.083 1.00 39.40  ?  374  LEU D CD1 1 
ATOM   13759 C  CD2 . LEU D  1 343 ? 36.661  28.518  -28.948 1.00 39.74  ?  374  LEU D CD2 1 
ATOM   13760 N  N   . ALA D  1 344 ? 35.829  29.293  -23.694 1.00 40.69  ?  375  ALA D N   1 
ATOM   13761 C  CA  . ALA D  1 344 ? 36.286  29.671  -22.372 1.00 43.08  ?  375  ALA D CA  1 
ATOM   13762 C  C   . ALA D  1 344 ? 36.475  28.478  -21.453 1.00 41.27  ?  375  ALA D C   1 
ATOM   13763 O  O   . ALA D  1 344 ? 36.873  28.675  -20.305 1.00 40.02  ?  375  ALA D O   1 
ATOM   13764 C  CB  . ALA D  1 344 ? 35.294  30.641  -21.741 1.00 37.37  ?  375  ALA D CB  1 
ATOM   13765 N  N   . GLU D  1 345 ? 36.191  27.264  -21.931 1.00 43.04  ?  376  GLU D N   1 
ATOM   13766 C  CA  . GLU D  1 345 ? 36.284  26.055  -21.119 1.00 46.64  ?  376  GLU D CA  1 
ATOM   13767 C  C   . GLU D  1 345 ? 35.490  26.215  -19.826 1.00 47.72  ?  376  GLU D C   1 
ATOM   13768 O  O   . GLU D  1 345 ? 35.908  25.770  -18.757 1.00 52.44  ?  376  GLU D O   1 
ATOM   13769 C  CB  . GLU D  1 345 ? 37.749  25.711  -20.830 1.00 46.21  ?  376  GLU D CB  1 
ATOM   13770 C  CG  . GLU D  1 345 ? 38.614  25.609  -22.093 1.00 50.32  ?  376  GLU D CG  1 
ATOM   13771 C  CD  . GLU D  1 345 ? 40.044  25.146  -21.813 1.00 53.98  ?  376  GLU D CD  1 
ATOM   13772 O  OE1 . GLU D  1 345 ? 40.815  25.922  -21.206 1.00 58.81  ?  376  GLU D OE1 1 
ATOM   13773 O  OE2 . GLU D  1 345 ? 40.409  24.022  -22.223 1.00 62.03  -1 376  GLU D OE2 1 
ATOM   13774 N  N   . ALA D  1 346 ? 34.345  26.881  -19.916 1.00 38.25  ?  377  ALA D N   1 
ATOM   13775 C  CA  . ALA D  1 346 ? 33.543  27.212  -18.746 1.00 44.26  ?  377  ALA D CA  1 
ATOM   13776 C  C   . ALA D  1 346 ? 32.448  26.177  -18.523 1.00 48.48  ?  377  ALA D C   1 
ATOM   13777 O  O   . ALA D  1 346 ? 31.818  25.703  -19.471 1.00 53.40  ?  377  ALA D O   1 
ATOM   13778 C  CB  . ALA D  1 346 ? 32.917  28.601  -18.882 1.00 39.61  ?  377  ALA D CB  1 
ATOM   13779 N  N   . LYS D  1 347 ? 32.223  25.831  -17.263 1.00 48.84  ?  378  LYS D N   1 
ATOM   13780 C  CA  . LYS D  1 347 ? 31.126  24.947  -16.917 1.00 47.88  ?  378  LYS D CA  1 
ATOM   13781 C  C   . LYS D  1 347 ? 29.836  25.750  -16.819 1.00 47.31  ?  378  LYS D C   1 
ATOM   13782 O  O   . LYS D  1 347 ? 29.818  26.854  -16.267 1.00 44.80  ?  378  LYS D O   1 
ATOM   13783 C  CB  . LYS D  1 347 ? 31.408  24.237  -15.593 1.00 56.13  ?  378  LYS D CB  1 
ATOM   13784 N  N   . LEU D  1 348 ? 28.758  25.196  -17.369 1.00 46.76  ?  379  LEU D N   1 
ATOM   13785 C  CA  . LEU D  1 348 ? 27.486  25.887  -17.269 1.00 46.51  ?  379  LEU D CA  1 
ATOM   13786 C  C   . LEU D  1 348 ? 26.875  25.657  -15.888 1.00 48.40  ?  379  LEU D C   1 
ATOM   13787 O  O   . LEU D  1 348 ? 27.137  24.632  -15.254 1.00 45.25  ?  379  LEU D O   1 
ATOM   13788 C  CB  . LEU D  1 348 ? 26.525  25.395  -18.343 1.00 46.94  ?  379  LEU D CB  1 
ATOM   13789 C  CG  . LEU D  1 348 ? 27.061  25.514  -19.769 1.00 52.27  ?  379  LEU D CG  1 
ATOM   13790 C  CD1 . LEU D  1 348 ? 26.194  24.720  -20.749 1.00 49.16  ?  379  LEU D CD1 1 
ATOM   13791 C  CD2 . LEU D  1 348 ? 27.206  26.976  -20.175 1.00 45.39  ?  379  LEU D CD2 1 
ATOM   13792 N  N   . PRO D  1 349 ? 26.064  26.595  -15.395 1.00 47.72  ?  380  PRO D N   1 
ATOM   13793 C  CA  . PRO D  1 349 ? 25.339  26.341  -14.144 1.00 48.03  ?  380  PRO D CA  1 
ATOM   13794 C  C   . PRO D  1 349 ? 24.430  25.138  -14.307 1.00 52.02  ?  380  PRO D C   1 
ATOM   13795 O  O   . PRO D  1 349 ? 23.964  24.833  -15.408 1.00 49.74  ?  380  PRO D O   1 
ATOM   13796 C  CB  . PRO D  1 349 ? 24.529  27.622  -13.909 1.00 48.89  ?  380  PRO D CB  1 
ATOM   13797 C  CG  . PRO D  1 349 ? 24.844  28.553  -15.005 1.00 47.50  ?  380  PRO D CG  1 
ATOM   13798 C  CD  . PRO D  1 349 ? 25.756  27.906  -15.995 1.00 48.60  ?  380  PRO D CD  1 
ATOM   13799 N  N   . LYS D  1 350 ? 24.191  24.437  -13.202 1.00 50.32  ?  381  LYS D N   1 
ATOM   13800 C  CA  . LYS D  1 350 ? 23.309  23.282  -13.266 1.00 48.55  ?  381  LYS D CA  1 
ATOM   13801 C  C   . LYS D  1 350 ? 21.902  23.721  -13.653 1.00 43.87  ?  381  LYS D C   1 
ATOM   13802 O  O   . LYS D  1 350 ? 21.403  24.754  -13.195 1.00 49.79  ?  381  LYS D O   1 
ATOM   13803 C  CB  . LYS D  1 350 ? 23.311  22.526  -11.929 1.00 51.69  ?  381  LYS D CB  1 
ATOM   13804 C  CG  . LYS D  1 350 ? 21.993  22.519  -11.162 1.00 55.64  ?  381  LYS D CG  1 
ATOM   13805 C  CD  . LYS D  1 350 ? 22.222  22.083  -9.708  1.00 62.32  ?  381  LYS D CD  1 
ATOM   13806 C  CE  . LYS D  1 350 ? 20.973  22.223  -8.838  1.00 53.56  ?  381  LYS D CE  1 
ATOM   13807 N  NZ  . LYS D  1 350 ? 21.295  21.815  -7.448  1.00 46.76  ?  381  LYS D NZ  1 
ATOM   13808 N  N   . GLY D  1 351 ? 21.280  22.951  -14.539 1.00 40.43  ?  382  GLY D N   1 
ATOM   13809 C  CA  . GLY D  1 351 ? 19.934  23.244  -14.997 1.00 48.61  ?  382  GLY D CA  1 
ATOM   13810 C  C   . GLY D  1 351 ? 19.824  24.281  -16.100 1.00 46.32  ?  382  GLY D C   1 
ATOM   13811 O  O   . GLY D  1 351 ? 18.707  24.546  -16.567 1.00 45.10  ?  382  GLY D O   1 
ATOM   13812 N  N   . LYS D  1 352 ? 20.935  24.879  -16.522 1.00 46.36  ?  383  LYS D N   1 
ATOM   13813 C  CA  . LYS D  1 352 ? 20.902  25.889  -17.573 1.00 44.92  ?  383  LYS D CA  1 
ATOM   13814 C  C   . LYS D  1 352 ? 20.502  25.261  -18.898 1.00 44.22  ?  383  LYS D C   1 
ATOM   13815 O  O   . LYS D  1 352 ? 21.093  24.267  -19.332 1.00 42.73  ?  383  LYS D O   1 
ATOM   13816 C  CB  . LYS D  1 352 ? 22.272  26.549  -17.707 1.00 47.49  ?  383  LYS D CB  1 
ATOM   13817 C  CG  . LYS D  1 352 ? 22.384  27.539  -18.858 1.00 42.39  ?  383  LYS D CG  1 
ATOM   13818 C  CD  . LYS D  1 352 ? 21.330  28.605  -18.780 1.00 39.81  ?  383  LYS D CD  1 
ATOM   13819 C  CE  . LYS D  1 352 ? 21.503  29.599  -19.926 1.00 37.68  ?  383  LYS D CE  1 
ATOM   13820 N  NZ  . LYS D  1 352 ? 20.588  30.767  -19.757 1.00 40.29  ?  383  LYS D NZ  1 
ATOM   13821 N  N   . GLN D  1 353 ? 19.510  25.850  -19.553 1.00 40.21  ?  384  GLN D N   1 
ATOM   13822 C  CA  . GLN D  1 353 ? 19.058  25.385  -20.856 1.00 44.01  ?  384  GLN D CA  1 
ATOM   13823 C  C   . GLN D  1 353 ? 19.549  26.324  -21.949 1.00 43.14  ?  384  GLN D C   1 
ATOM   13824 O  O   . GLN D  1 353 ? 19.602  27.543  -21.754 1.00 39.50  ?  384  GLN D O   1 
ATOM   13825 C  CB  . GLN D  1 353 ? 17.541  25.281  -20.869 1.00 42.22  ?  384  GLN D CB  1 
ATOM   13826 C  CG  . GLN D  1 353 ? 17.072  24.400  -19.734 1.00 45.56  ?  384  GLN D CG  1 
ATOM   13827 C  CD  . GLN D  1 353 ? 15.867  23.602  -20.088 1.00 56.76  ?  384  GLN D CD  1 
ATOM   13828 O  OE1 . GLN D  1 353 ? 14.755  23.954  -19.702 1.00 67.38  ?  384  GLN D OE1 1 
ATOM   13829 N  NE2 . GLN D  1 353 ? 16.063  22.516  -20.836 1.00 61.19  ?  384  GLN D NE2 1 
ATOM   13830 N  N   . LEU D  1 354 ? 19.924  25.743  -23.091 1.00 43.50  ?  385  LEU D N   1 
ATOM   13831 C  CA  . LEU D  1 354 ? 20.461  26.476  -24.231 1.00 38.69  ?  385  LEU D CA  1 
ATOM   13832 C  C   . LEU D  1 354 ? 19.809  25.974  -25.510 1.00 39.56  ?  385  LEU D C   1 
ATOM   13833 O  O   . LEU D  1 354 ? 19.652  24.768  -25.696 1.00 35.82  ?  385  LEU D O   1 
ATOM   13834 C  CB  . LEU D  1 354 ? 21.974  26.305  -24.326 1.00 38.17  ?  385  LEU D CB  1 
ATOM   13835 C  CG  . LEU D  1 354 ? 22.803  26.999  -23.248 1.00 33.99  ?  385  LEU D CG  1 
ATOM   13836 C  CD1 . LEU D  1 354 ? 24.258  26.698  -23.496 1.00 36.06  ?  385  LEU D CD1 1 
ATOM   13837 C  CD2 . LEU D  1 354 ? 22.559  28.507  -23.285 1.00 36.85  ?  385  LEU D CD2 1 
ATOM   13838 N  N   . ASP D  1 355 ? 19.440  26.899  -26.397 1.00 35.57  ?  386  ASP D N   1 
ATOM   13839 C  CA  . ASP D  1 355 ? 18.778  26.539  -27.641 1.00 35.05  ?  386  ASP D CA  1 
ATOM   13840 C  C   . ASP D  1 355 ? 19.727  26.489  -28.832 1.00 39.26  ?  386  ASP D C   1 
ATOM   13841 O  O   . ASP D  1 355 ? 19.343  25.979  -29.889 1.00 38.74  ?  386  ASP D O   1 
ATOM   13842 C  CB  . ASP D  1 355 ? 17.645  27.529  -27.926 1.00 33.84  ?  386  ASP D CB  1 
ATOM   13843 C  CG  . ASP D  1 355 ? 16.396  27.260  -27.095 1.00 39.63  ?  386  ASP D CG  1 
ATOM   13844 O  OD1 . ASP D  1 355 ? 16.030  26.079  -26.935 1.00 41.24  ?  386  ASP D OD1 1 
ATOM   13845 O  OD2 . ASP D  1 355 ? 15.774  28.229  -26.598 1.00 36.13  -1 386  ASP D OD2 1 
ATOM   13846 N  N   . GLY D  1 356 ? 20.945  27.022  -28.702 1.00 38.28  ?  387  GLY D N   1 
ATOM   13847 C  CA  . GLY D  1 356 ? 21.903  27.036  -29.783 1.00 35.39  ?  387  GLY D CA  1 
ATOM   13848 C  C   . GLY D  1 356 ? 22.931  25.932  -29.628 1.00 34.76  ?  387  GLY D C   1 
ATOM   13849 O  O   . GLY D  1 356 ? 22.850  25.094  -28.733 1.00 32.59  ?  387  GLY D O   1 
ATOM   13850 N  N   . LYS D  1 357 ? 23.928  25.954  -30.511 1.00 37.06  ?  388  LYS D N   1 
ATOM   13851 C  CA  . LYS D  1 357 ? 24.958  24.927  -30.546 1.00 36.39  ?  388  LYS D CA  1 
ATOM   13852 C  C   . LYS D  1 357 ? 26.343  25.559  -30.486 1.00 39.28  ?  388  LYS D C   1 
ATOM   13853 O  O   . LYS D  1 357 ? 26.554  26.689  -30.930 1.00 33.46  ?  388  LYS D O   1 
ATOM   13854 C  CB  . LYS D  1 357 ? 24.843  24.068  -31.816 1.00 38.07  ?  388  LYS D CB  1 
ATOM   13855 C  CG  . LYS D  1 357 ? 23.394  23.678  -32.156 1.00 39.68  ?  388  LYS D CG  1 
ATOM   13856 C  CD  . LYS D  1 357 ? 23.310  22.880  -33.444 1.00 42.26  ?  388  LYS D CD  1 
ATOM   13857 C  CE  . LYS D  1 357 ? 22.020  22.082  -33.519 1.00 44.48  ?  388  LYS D CE  1 
ATOM   13858 N  NZ  . LYS D  1 357 ? 21.919  20.987  -32.513 1.00 47.44  ?  388  LYS D NZ  1 
ATOM   13859 N  N   . ASN D  1 358 ? 27.292  24.818  -29.934 1.00 36.33  ?  389  ASN D N   1 
ATOM   13860 C  CA  . ASN D  1 358 ? 28.695  25.183  -30.083 1.00 36.44  ?  389  ASN D CA  1 
ATOM   13861 C  C   . ASN D  1 358 ? 29.125  24.842  -31.507 1.00 37.47  ?  389  ASN D C   1 
ATOM   13862 O  O   . ASN D  1 358 ? 29.250  23.664  -31.858 1.00 40.64  ?  389  ASN D O   1 
ATOM   13863 C  CB  . ASN D  1 358 ? 29.534  24.435  -29.051 1.00 38.53  ?  389  ASN D CB  1 
ATOM   13864 C  CG  . ASN D  1 358 ? 31.002  24.779  -29.123 1.00 37.73  ?  389  ASN D CG  1 
ATOM   13865 O  OD1 . ASN D  1 358 ? 31.472  25.375  -30.084 1.00 37.17  ?  389  ASN D OD1 1 
ATOM   13866 N  ND2 . ASN D  1 358 ? 31.752  24.361  -28.107 1.00 43.45  ?  389  ASN D ND2 1 
ATOM   13867 N  N   . ILE D  1 359 ? 29.374  25.861  -32.329 1.00 34.71  ?  390  ILE D N   1 
ATOM   13868 C  CA  . ILE D  1 359 ? 29.558  25.665  -33.765 1.00 33.93  ?  390  ILE D CA  1 
ATOM   13869 C  C   . ILE D  1 359 ? 31.000  25.840  -34.211 1.00 37.16  ?  390  ILE D C   1 
ATOM   13870 O  O   . ILE D  1 359 ? 31.264  25.777  -35.418 1.00 34.60  ?  390  ILE D O   1 
ATOM   13871 C  CB  . ILE D  1 359 ? 28.641  26.598  -34.590 1.00 36.26  ?  390  ILE D CB  1 
ATOM   13872 C  CG1 . ILE D  1 359 ? 29.004  28.064  -34.328 1.00 33.26  ?  390  ILE D CG1 1 
ATOM   13873 C  CG2 . ILE D  1 359 ? 27.139  26.320  -34.312 1.00 34.16  ?  390  ILE D CG2 1 
ATOM   13874 C  CD1 . ILE D  1 359 ? 28.276  29.062  -35.233 1.00 32.46  ?  390  ILE D CD1 1 
ATOM   13875 N  N   . MET D  1 360 ? 31.941  26.082  -33.291 1.00 38.07  ?  391  MET D N   1 
ATOM   13876 C  CA  . MET D  1 360 ? 33.301  26.410  -33.717 1.00 36.16  ?  391  MET D CA  1 
ATOM   13877 C  C   . MET D  1 360 ? 33.940  25.275  -34.504 1.00 38.23  ?  391  MET D C   1 
ATOM   13878 O  O   . MET D  1 360 ? 34.602  25.513  -35.518 1.00 37.37  ?  391  MET D O   1 
ATOM   13879 C  CB  . MET D  1 360 ? 34.161  26.764  -32.508 1.00 36.34  ?  391  MET D CB  1 
ATOM   13880 C  CG  . MET D  1 360 ? 35.490  27.433  -32.864 1.00 37.32  ?  391  MET D CG  1 
ATOM   13881 S  SD  . MET D  1 360 ? 35.385  28.783  -34.023 1.00 39.93  ?  391  MET D SD  1 
ATOM   13882 C  CE  . MET D  1 360 ? 34.879  30.079  -32.888 1.00 35.82  ?  391  MET D CE  1 
ATOM   13883 N  N   . ASP D  1 361 ? 33.806  24.039  -34.021 1.00 39.50  ?  392  ASP D N   1 
ATOM   13884 C  CA  . ASP D  1 361 ? 34.326  22.914  -34.788 1.00 43.81  ?  392  ASP D CA  1 
ATOM   13885 C  C   . ASP D  1 361 ? 33.696  22.861  -36.167 1.00 43.47  ?  392  ASP D C   1 
ATOM   13886 O  O   . ASP D  1 361 ? 34.393  22.626  -37.161 1.00 45.92  ?  392  ASP D O   1 
ATOM   13887 C  CB  . ASP D  1 361 ? 34.114  21.593  -34.042 1.00 42.34  ?  392  ASP D CB  1 
ATOM   13888 C  CG  . ASP D  1 361 ? 35.348  21.175  -33.235 1.00 59.71  ?  392  ASP D CG  1 
ATOM   13889 O  OD1 . ASP D  1 361 ? 36.424  21.026  -33.857 1.00 65.39  ?  392  ASP D OD1 1 
ATOM   13890 O  OD2 . ASP D  1 361 ? 35.256  20.996  -31.997 1.00 60.49  -1 392  ASP D OD2 1 
ATOM   13891 N  N   . ASP D  1 362 ? 32.384  23.111  -36.254 1.00 41.74  ?  393  ASP D N   1 
ATOM   13892 C  CA  . ASP D  1 362 ? 31.743  23.147  -37.564 1.00 43.11  ?  393  ASP D CA  1 
ATOM   13893 C  C   . ASP D  1 362 ? 32.348  24.238  -38.440 1.00 41.86  ?  393  ASP D C   1 
ATOM   13894 O  O   . ASP D  1 362 ? 32.568  24.028  -39.638 1.00 41.39  ?  393  ASP D O   1 
ATOM   13895 C  CB  . ASP D  1 362 ? 30.234  23.357  -37.423 1.00 40.11  ?  393  ASP D CB  1 
ATOM   13896 C  CG  . ASP D  1 362 ? 29.502  22.083  -37.055 1.00 46.76  ?  393  ASP D CG  1 
ATOM   13897 O  OD1 . ASP D  1 362 ? 29.568  21.099  -37.834 1.00 47.78  ?  393  ASP D OD1 1 
ATOM   13898 O  OD2 . ASP D  1 362 ? 28.850  22.066  -35.984 1.00 45.93  -1 393  ASP D OD2 1 
ATOM   13899 N  N   . VAL D  1 363 ? 32.619  25.414  -37.862 1.00 37.58  ?  394  VAL D N   1 
ATOM   13900 C  CA  . VAL D  1 363 ? 33.193  26.501  -38.652 1.00 34.66  ?  394  VAL D CA  1 
ATOM   13901 C  C   . VAL D  1 363 ? 34.595  26.133  -39.133 1.00 42.83  ?  394  VAL D C   1 
ATOM   13902 O  O   . VAL D  1 363 ? 34.948  26.353  -40.298 1.00 38.78  ?  394  VAL D O   1 
ATOM   13903 C  CB  . VAL D  1 363 ? 33.187  27.813  -37.845 1.00 35.83  ?  394  VAL D CB  1 
ATOM   13904 C  CG1 . VAL D  1 363 ? 33.991  28.891  -38.564 1.00 39.85  ?  394  VAL D CG1 1 
ATOM   13905 C  CG2 . VAL D  1 363 ? 31.744  28.302  -37.625 1.00 34.45  ?  394  VAL D CG2 1 
ATOM   13906 N  N   . LEU D  1 364 ? 35.411  25.549  -38.255 1.00 42.08  ?  395  LEU D N   1 
ATOM   13907 C  CA  . LEU D  1 364 ? 36.780  25.234  -38.647 1.00 42.60  ?  395  LEU D CA  1 
ATOM   13908 C  C   . LEU D  1 364 ? 36.827  24.113  -39.681 1.00 46.93  ?  395  LEU D C   1 
ATOM   13909 O  O   . LEU D  1 364 ? 37.747  24.073  -40.507 1.00 51.22  ?  395  LEU D O   1 
ATOM   13910 C  CB  . LEU D  1 364 ? 37.611  24.887  -37.407 1.00 45.17  ?  395  LEU D CB  1 
ATOM   13911 C  CG  . LEU D  1 364 ? 37.630  26.019  -36.369 1.00 42.03  ?  395  LEU D CG  1 
ATOM   13912 C  CD1 . LEU D  1 364 ? 38.242  25.590  -35.042 1.00 45.00  ?  395  LEU D CD1 1 
ATOM   13913 C  CD2 . LEU D  1 364 ? 38.329  27.255  -36.938 1.00 42.56  ?  395  LEU D CD2 1 
ATOM   13914 N  N   . LYS D  1 365 ? 35.830  23.226  -39.680 1.00 46.17  ?  396  LYS D N   1 
ATOM   13915 C  CA  . LYS D  1 365 ? 35.810  22.071  -40.566 1.00 45.74  ?  396  LYS D CA  1 
ATOM   13916 C  C   . LYS D  1 365 ? 34.798  22.201  -41.699 1.00 48.57  ?  396  LYS D C   1 
ATOM   13917 O  O   . LYS D  1 365 ? 34.695  21.286  -42.524 1.00 48.11  ?  396  LYS D O   1 
ATOM   13918 C  CB  . LYS D  1 365 ? 35.538  20.800  -39.749 1.00 43.30  ?  396  LYS D CB  1 
ATOM   13919 C  CG  . LYS D  1 365 ? 36.529  20.641  -38.609 1.00 49.21  ?  396  LYS D CG  1 
ATOM   13920 C  CD  . LYS D  1 365 ? 36.958  19.204  -38.395 1.00 54.76  ?  396  LYS D CD  1 
ATOM   13921 C  CE  . LYS D  1 365 ? 36.385  18.648  -37.105 1.00 58.16  ?  396  LYS D CE  1 
ATOM   13922 N  NZ  . LYS D  1 365 ? 37.469  18.472  -36.087 1.00 60.02  ?  396  LYS D NZ  1 
ATOM   13923 N  N   . ASN D  1 366 ? 34.075  23.321  -41.774 1.00 44.78  ?  397  ASN D N   1 
ATOM   13924 C  CA  . ASN D  1 366 ? 33.060  23.562  -42.803 1.00 42.48  ?  397  ASN D CA  1 
ATOM   13925 C  C   . ASN D  1 366 ? 32.025  22.434  -42.844 1.00 43.74  ?  397  ASN D C   1 
ATOM   13926 O  O   . ASN D  1 366 ? 31.737  21.849  -43.891 1.00 45.95  ?  397  ASN D O   1 
ATOM   13927 C  CB  . ASN D  1 366 ? 33.696  23.770  -44.181 1.00 42.61  ?  397  ASN D CB  1 
ATOM   13928 C  CG  . ASN D  1 366 ? 32.678  24.244  -45.232 1.00 49.63  ?  397  ASN D CG  1 
ATOM   13929 O  OD1 . ASN D  1 366 ? 32.005  25.260  -45.048 1.00 44.97  ?  397  ASN D OD1 1 
ATOM   13930 N  ND2 . ASN D  1 366 ? 32.556  23.498  -46.324 1.00 45.46  ?  397  ASN D ND2 1 
ATOM   13931 N  N   . THR D  1 367 ? 31.436  22.147  -41.691 1.00 44.63  ?  398  THR D N   1 
ATOM   13932 C  CA  . THR D  1 367 ? 30.385  21.151  -41.587 1.00 42.54  ?  398  THR D CA  1 
ATOM   13933 C  C   . THR D  1 367 ? 29.099  21.817  -41.106 1.00 44.83  ?  398  THR D C   1 
ATOM   13934 O  O   . THR D  1 367 ? 29.103  22.966  -40.659 1.00 40.15  ?  398  THR D O   1 
ATOM   13935 C  CB  . THR D  1 367 ? 30.807  20.021  -40.649 1.00 47.18  ?  398  THR D CB  1 
ATOM   13936 O  OG1 . THR D  1 367 ? 31.217  20.582  -39.399 1.00 49.95  ?  398  THR D OG1 1 
ATOM   13937 C  CG2 . THR D  1 367 ? 31.991  19.268  -41.253 1.00 47.30  ?  398  THR D CG2 1 
ATOM   13938 N  N   . GLU D  1 368 ? 27.984  21.074  -41.197 1.00 40.65  ?  399  GLU D N   1 
ATOM   13939 C  CA  . GLU D  1 368 ? 26.641  21.634  -41.067 1.00 40.25  ?  399  GLU D CA  1 
ATOM   13940 C  C   . GLU D  1 368 ? 26.097  21.470  -39.654 1.00 41.41  ?  399  GLU D C   1 
ATOM   13941 O  O   . GLU D  1 368 ? 25.615  20.383  -39.303 1.00 41.36  ?  399  GLU D O   1 
ATOM   13942 C  CB  . GLU D  1 368 ? 25.698  20.971  -42.080 1.00 40.84  ?  399  GLU D CB  1 
ATOM   13943 C  CG  . GLU D  1 368 ? 24.302  21.577  -42.094 1.00 42.80  ?  399  GLU D CG  1 
ATOM   13944 C  CD  . GLU D  1 368 ? 23.382  20.934  -43.127 1.00 47.74  ?  399  GLU D CD  1 
ATOM   13945 O  OE1 . GLU D  1 368 ? 23.819  19.981  -43.821 1.00 46.65  ?  399  GLU D OE1 1 
ATOM   13946 O  OE2 . GLU D  1 368 ? 22.213  21.375  -43.234 1.00 45.63  -1 399  GLU D OE2 1 
ATOM   13947 N  N   . PRO D  1 369 ? 26.090  22.517  -38.824 1.00 41.02  ?  400  PRO D N   1 
ATOM   13948 C  CA  . PRO D  1 369 ? 25.621  22.339  -37.440 1.00 38.14  ?  400  PRO D CA  1 
ATOM   13949 C  C   . PRO D  1 369 ? 24.137  22.052  -37.312 1.00 39.83  ?  400  PRO D C   1 
ATOM   13950 O  O   . PRO D  1 369 ? 23.741  21.322  -36.392 1.00 39.40  ?  400  PRO D O   1 
ATOM   13951 C  CB  . PRO D  1 369 ? 25.984  23.672  -36.778 1.00 40.76  ?  400  PRO D CB  1 
ATOM   13952 C  CG  . PRO D  1 369 ? 25.953  24.659  -37.909 1.00 35.17  ?  400  PRO D CG  1 
ATOM   13953 C  CD  . PRO D  1 369 ? 26.526  23.900  -39.085 1.00 37.61  ?  400  PRO D CD  1 
ATOM   13954 N  N   . TYR D  1 370 ? 23.296  22.614  -38.181 1.00 40.26  ?  401  TYR D N   1 
ATOM   13955 C  CA  . TYR D  1 370 ? 21.849  22.450  -38.079 1.00 34.24  ?  401  TYR D CA  1 
ATOM   13956 C  C   . TYR D  1 370 ? 21.301  21.443  -39.090 1.00 40.12  ?  401  TYR D C   1 
ATOM   13957 O  O   . TYR D  1 370 ? 20.136  21.539  -39.501 1.00 39.02  ?  401  TYR D O   1 
ATOM   13958 C  CB  . TYR D  1 370 ? 21.158  23.805  -38.229 1.00 35.20  ?  401  TYR D CB  1 
ATOM   13959 C  CG  . TYR D  1 370 ? 21.244  24.613  -36.954 1.00 35.21  ?  401  TYR D CG  1 
ATOM   13960 C  CD1 . TYR D  1 370 ? 22.406  25.324  -36.639 1.00 32.86  ?  401  TYR D CD1 1 
ATOM   13961 C  CD2 . TYR D  1 370 ? 20.196  24.603  -36.022 1.00 33.17  ?  401  TYR D CD2 1 
ATOM   13962 C  CE1 . TYR D  1 370 ? 22.505  26.041  -35.445 1.00 32.89  ?  401  TYR D CE1 1 
ATOM   13963 C  CE2 . TYR D  1 370 ? 20.282  25.317  -34.820 1.00 33.39  ?  401  TYR D CE2 1 
ATOM   13964 C  CZ  . TYR D  1 370 ? 21.438  26.034  -34.546 1.00 35.64  ?  401  TYR D CZ  1 
ATOM   13965 O  OH  . TYR D  1 370 ? 21.527  26.736  -33.388 1.00 38.89  ?  401  TYR D OH  1 
ATOM   13966 N  N   . LYS D  1 371 ? 22.119  20.478  -39.508 1.00 45.81  ?  402  LYS D N   1 
ATOM   13967 C  CA  . LYS D  1 371 ? 21.623  19.456  -40.418 1.00 47.37  ?  402  LYS D CA  1 
ATOM   13968 C  C   . LYS D  1 371 ? 20.394  18.789  -39.819 1.00 43.01  ?  402  LYS D C   1 
ATOM   13969 O  O   . LYS D  1 371 ? 20.427  18.302  -38.688 1.00 45.76  ?  402  LYS D O   1 
ATOM   13970 C  CB  . LYS D  1 371 ? 22.712  18.422  -40.735 1.00 47.72  ?  402  LYS D CB  1 
ATOM   13971 C  CG  . LYS D  1 371 ? 22.167  17.226  -41.555 1.00 51.26  ?  402  LYS D CG  1 
ATOM   13972 C  CD  . LYS D  1 371 ? 23.251  16.266  -42.050 1.00 54.21  ?  402  LYS D CD  1 
ATOM   13973 C  CE  . LYS D  1 371 ? 23.016  15.967  -43.549 1.00 59.97  ?  402  LYS D CE  1 
ATOM   13974 N  NZ  . LYS D  1 371 ? 24.231  15.560  -44.326 1.00 56.73  ?  402  LYS D NZ  1 
ATOM   13975 N  N   . ASP D  1 372 ? 19.291  18.837  -40.560 1.00 46.89  ?  403  ASP D N   1 
ATOM   13976 C  CA  . ASP D  1 372 ? 18.035  18.218  -40.153 1.00 46.79  ?  403  ASP D CA  1 
ATOM   13977 C  C   . ASP D  1 372 ? 17.428  18.858  -38.905 1.00 45.58  ?  403  ASP D C   1 
ATOM   13978 O  O   . ASP D  1 372 ? 16.677  18.206  -38.184 1.00 43.57  ?  403  ASP D O   1 
ATOM   13979 C  CB  . ASP D  1 372 ? 18.202  16.708  -39.939 1.00 53.41  ?  403  ASP D CB  1 
ATOM   13980 C  CG  . ASP D  1 372 ? 18.505  15.966  -41.235 1.00 57.06  ?  403  ASP D CG  1 
ATOM   13981 O  OD1 . ASP D  1 372 ? 17.838  16.251  -42.252 1.00 60.78  ?  403  ASP D OD1 1 
ATOM   13982 O  OD2 . ASP D  1 372 ? 19.411  15.106  -41.239 1.00 59.61  -1 403  ASP D OD2 1 
ATOM   13983 N  N   . GLU D  1 373 ? 17.721  20.131  -38.634 1.00 41.98  ?  404  GLU D N   1 
ATOM   13984 C  CA  . GLU D  1 373 ? 17.159  20.816  -37.472 1.00 43.62  ?  404  GLU D CA  1 
ATOM   13985 C  C   . GLU D  1 373 ? 16.735  22.215  -37.881 1.00 35.94  ?  404  GLU D C   1 
ATOM   13986 O  O   . GLU D  1 373 ? 17.191  22.744  -38.891 1.00 38.12  ?  404  GLU D O   1 
ATOM   13987 C  CB  . GLU D  1 373 ? 18.144  20.895  -36.291 1.00 41.54  ?  404  GLU D CB  1 
ATOM   13988 C  CG  . GLU D  1 373 ? 18.496  19.551  -35.674 1.00 48.16  ?  404  GLU D CG  1 
ATOM   13989 C  CD  . GLU D  1 373 ? 19.279  19.699  -34.378 1.00 56.65  ?  404  GLU D CD  1 
ATOM   13990 O  OE1 . GLU D  1 373 ? 19.042  20.691  -33.650 1.00 59.09  ?  404  GLU D OE1 1 
ATOM   13991 O  OE2 . GLU D  1 373 ? 20.132  18.830  -34.089 1.00 58.11  -1 404  GLU D OE2 1 
ATOM   13992 N  N   . MET D  1 374 ? 15.859  22.814  -37.075 1.00 38.67  ?  405  MET D N   1 
ATOM   13993 C  CA  . MET D  1 374 ? 15.197  24.060  -37.436 1.00 37.75  ?  405  MET D CA  1 
ATOM   13994 C  C   . MET D  1 374 ? 15.870  25.281  -36.805 1.00 33.25  ?  405  MET D C   1 
ATOM   13995 O  O   . MET D  1 374 ? 16.372  25.219  -35.686 1.00 30.33  ?  405  MET D O   1 
ATOM   13996 C  CB  . MET D  1 374 ? 13.728  24.027  -37.022 1.00 41.00  ?  405  MET D CB  1 
ATOM   13997 C  CG  . MET D  1 374 ? 12.894  23.014  -37.787 1.00 39.70  ?  405  MET D CG  1 
ATOM   13998 S  SD  . MET D  1 374 ? 12.355  23.694  -39.355 1.00 43.42  ?  405  MET D SD  1 
ATOM   13999 C  CE  . MET D  1 374 ? 10.605  23.343  -39.308 1.00 38.01  ?  405  MET D CE  1 
ATOM   14000 N  N   . ILE D  1 375 ? 15.881  26.383  -37.556 1.00 35.14  ?  406  ILE D N   1 
ATOM   14001 C  CA  . ILE D  1 375 ? 16.075  27.730  -37.036 1.00 32.44  ?  406  ILE D CA  1 
ATOM   14002 C  C   . ILE D  1 375 ? 14.765  28.472  -37.240 1.00 30.80  ?  406  ILE D C   1 
ATOM   14003 O  O   . ILE D  1 375 ? 14.259  28.523  -38.363 1.00 30.55  ?  406  ILE D O   1 
ATOM   14004 C  CB  . ILE D  1 375 ? 17.229  28.442  -37.753 1.00 31.90  ?  406  ILE D CB  1 
ATOM   14005 C  CG1 . ILE D  1 375 ? 18.569  27.862  -37.272 1.00 34.94  ?  406  ILE D CG1 1 
ATOM   14006 C  CG2 . ILE D  1 375 ? 17.177  29.942  -37.503 1.00 32.07  ?  406  ILE D CG2 1 
ATOM   14007 C  CD1 . ILE D  1 375 ? 19.720  28.235  -38.189 1.00 32.62  ?  406  ILE D CD1 1 
ATOM   14008 N  N   . TYR D  1 376 ? 14.228  29.049  -36.166 1.00 29.51  ?  407  TYR D N   1 
ATOM   14009 C  CA  . TYR D  1 376 ? 12.850  29.519  -36.091 1.00 33.40  ?  407  TYR D CA  1 
ATOM   14010 C  C   . TYR D  1 376 ? 12.768  31.020  -35.875 1.00 32.85  ?  407  TYR D C   1 
ATOM   14011 O  O   . TYR D  1 376 ? 13.660  31.635  -35.290 1.00 28.78  ?  407  TYR D O   1 
ATOM   14012 C  CB  . TYR D  1 376 ? 12.099  28.914  -34.901 1.00 35.05  ?  407  TYR D CB  1 
ATOM   14013 C  CG  . TYR D  1 376 ? 11.881  27.437  -34.897 1.00 34.50  ?  407  TYR D CG  1 
ATOM   14014 C  CD1 . TYR D  1 376 ? 10.998  26.844  -35.804 1.00 34.65  ?  407  TYR D CD1 1 
ATOM   14015 C  CD2 . TYR D  1 376 ? 12.504  26.636  -33.952 1.00 35.52  ?  407  TYR D CD2 1 
ATOM   14016 C  CE1 . TYR D  1 376 ? 10.768  25.484  -35.787 1.00 35.70  ?  407  TYR D CE1 1 
ATOM   14017 C  CE2 . TYR D  1 376 ? 12.284  25.273  -33.923 1.00 37.30  ?  407  TYR D CE2 1 
ATOM   14018 C  CZ  . TYR D  1 376 ? 11.414  24.706  -34.840 1.00 40.69  ?  407  TYR D CZ  1 
ATOM   14019 O  OH  . TYR D  1 376 ? 11.207  23.351  -34.821 1.00 46.75  ?  407  TYR D OH  1 
ATOM   14020 N  N   . SER D  1 377 ? 11.625  31.587  -36.251 1.00 29.68  ?  408  SER D N   1 
ATOM   14021 C  CA  . SER D  1 377 ? 11.231  32.863  -35.679 1.00 28.91  ?  408  SER D CA  1 
ATOM   14022 C  C   . SER D  1 377 ? 9.717   32.876  -35.559 1.00 30.73  ?  408  SER D C   1 
ATOM   14023 O  O   . SER D  1 377 ? 9.028   32.365  -36.439 1.00 32.32  ?  408  SER D O   1 
ATOM   14024 C  CB  . SER D  1 377 ? 11.710  34.043  -36.528 1.00 30.40  ?  408  SER D CB  1 
ATOM   14025 O  OG  . SER D  1 377 ? 11.178  35.266  -36.037 1.00 31.55  ?  408  SER D OG  1 
ATOM   14026 N  N   . LEU D  1 378 ? 9.202   33.429  -34.461 1.00 30.79  ?  409  LEU D N   1 
ATOM   14027 C  CA  . LEU D  1 378 ? 7.772   33.703  -34.336 1.00 32.71  ?  409  LEU D CA  1 
ATOM   14028 C  C   . LEU D  1 378 ? 7.626   35.088  -33.735 1.00 27.72  ?  409  LEU D C   1 
ATOM   14029 O  O   . LEU D  1 378 ? 8.226   35.377  -32.696 1.00 31.13  ?  409  LEU D O   1 
ATOM   14030 C  CB  . LEU D  1 378 ? 7.044   32.661  -33.468 1.00 28.54  ?  409  LEU D CB  1 
ATOM   14031 C  CG  . LEU D  1 378 ? 5.543   32.936  -33.305 1.00 34.06  ?  409  LEU D CG  1 
ATOM   14032 C  CD1 . LEU D  1 378 ? 4.715   31.639  -33.426 1.00 33.96  ?  409  LEU D CD1 1 
ATOM   14033 C  CD2 . LEU D  1 378 ? 5.247   33.675  -31.982 1.00 30.70  ?  409  LEU D CD2 1 
ATOM   14034 N  N   . ARG D  1 379 ? 6.870   35.952  -34.402 1.00 28.32  ?  410  ARG D N   1 
ATOM   14035 C  CA  . ARG D  1 379 ? 6.721   37.331  -33.961 1.00 32.38  ?  410  ARG D CA  1 
ATOM   14036 C  C   . ARG D  1 379 ? 5.243   37.624  -33.760 1.00 30.14  ?  410  ARG D C   1 
ATOM   14037 O  O   . ARG D  1 379 ? 4.443   37.472  -34.691 1.00 27.32  ?  410  ARG D O   1 
ATOM   14038 C  CB  . ARG D  1 379 ? 7.349   38.304  -34.961 1.00 26.62  ?  410  ARG D CB  1 
ATOM   14039 C  CG  . ARG D  1 379 ? 7.235   39.759  -34.548 1.00 26.58  ?  410  ARG D CG  1 
ATOM   14040 C  CD  . ARG D  1 379 ? 6.025   40.396  -35.256 1.00 27.15  ?  410  ARG D CD  1 
ATOM   14041 N  NE  . ARG D  1 379 ? 5.610   41.643  -34.628 1.00 28.30  ?  410  ARG D NE  1 
ATOM   14042 C  CZ  . ARG D  1 379 ? 6.241   42.802  -34.779 1.00 32.89  ?  410  ARG D CZ  1 
ATOM   14043 N  NH1 . ARG D  1 379 ? 7.327   42.907  -35.542 1.00 27.56  ?  410  ARG D NH1 1 
ATOM   14044 N  NH2 . ARG D  1 379 ? 5.772   43.883  -34.153 1.00 32.16  ?  410  ARG D NH2 1 
ATOM   14045 N  N   . TYR D  1 380 ? 4.884   38.036  -32.546 1.00 30.26  ?  411  TYR D N   1 
ATOM   14046 C  CA  . TYR D  1 380 ? 3.488   38.324  -32.243 1.00 31.35  ?  411  TYR D CA  1 
ATOM   14047 C  C   . TYR D  1 380 ? 3.042   39.615  -32.917 1.00 31.56  ?  411  TYR D C   1 
ATOM   14048 O  O   . TYR D  1 380 ? 3.743   40.634  -32.881 1.00 30.44  ?  411  TYR D O   1 
ATOM   14049 C  CB  . TYR D  1 380 ? 3.263   38.423  -30.733 1.00 34.20  ?  411  TYR D CB  1 
ATOM   14050 C  CG  . TYR D  1 380 ? 3.640   37.185  -29.962 1.00 36.41  ?  411  TYR D CG  1 
ATOM   14051 C  CD1 . TYR D  1 380 ? 2.874   36.026  -30.052 1.00 32.89  ?  411  TYR D CD1 1 
ATOM   14052 C  CD2 . TYR D  1 380 ? 4.747   37.178  -29.115 1.00 32.29  ?  411  TYR D CD2 1 
ATOM   14053 C  CE1 . TYR D  1 380 ? 3.219   34.885  -29.330 1.00 31.00  ?  411  TYR D CE1 1 
ATOM   14054 C  CE2 . TYR D  1 380 ? 5.093   36.049  -28.406 1.00 36.37  ?  411  TYR D CE2 1 
ATOM   14055 C  CZ  . TYR D  1 380 ? 4.323   34.905  -28.519 1.00 33.51  ?  411  TYR D CZ  1 
ATOM   14056 O  OH  . TYR D  1 380 ? 4.688   33.781  -27.808 1.00 36.07  ?  411  TYR D OH  1 
ATOM   14057 N  N   . ARG D  1 381 ? 1.848   39.530  -33.516 1.00 29.96  ?  412  ARG D N   1 
ATOM   14058 C  CA  . ARG D  1 381 ? 1.221   40.720  -34.132 1.00 30.56  ?  412  ARG D CA  1 
ATOM   14059 C  C   . ARG D  1 381 ? -0.091  41.008  -33.381 1.00 32.95  ?  412  ARG D C   1 
ATOM   14060 O  O   . ARG D  1 381 ? -0.408  40.291  -32.404 1.00 36.21  ?  412  ARG D O   1 
ATOM   14061 C  CB  . ARG D  1 381 ? 0.997   40.469  -35.629 1.00 29.83  ?  412  ARG D CB  1 
ATOM   14062 C  CG  . ARG D  1 381 ? 2.286   40.378  -36.432 1.00 30.43  ?  412  ARG D CG  1 
ATOM   14063 C  CD  . ARG D  1 381 ? 2.828   41.756  -36.749 1.00 28.38  ?  412  ARG D CD  1 
ATOM   14064 N  NE  . ARG D  1 381 ? 4.001   41.716  -37.627 1.00 29.10  ?  412  ARG D NE  1 
ATOM   14065 C  CZ  . ARG D  1 381 ? 4.766   42.759  -37.924 1.00 30.65  ?  412  ARG D CZ  1 
ATOM   14066 N  NH1 . ARG D  1 381 ? 4.450   43.968  -37.490 1.00 28.66  ?  412  ARG D NH1 1 
ATOM   14067 N  NH2 . ARG D  1 381 ? 5.845   42.588  -38.660 1.00 28.54  ?  412  ARG D NH2 1 
ATOM   14068 N  N   . GLU D  1 382 ? -0.829  41.992  -33.853 1.00 31.72  ?  413  GLU D N   1 
ATOM   14069 C  CA  . GLU D  1 382 ? -2.130  42.345  -33.264 1.00 34.34  ?  413  GLU D CA  1 
ATOM   14070 C  C   . GLU D  1 382 ? -3.213  41.375  -33.754 1.00 32.60  ?  413  GLU D C   1 
ATOM   14071 O  O   . GLU D  1 382 ? -4.024  41.678  -34.638 1.00 32.57  ?  413  GLU D O   1 
ATOM   14072 C  CB  . GLU D  1 382 ? -2.485  43.789  -33.606 1.00 31.89  ?  413  GLU D CB  1 
ATOM   14073 C  CG  . GLU D  1 382 ? -1.467  44.837  -33.117 1.00 39.18  ?  413  GLU D CG  1 
ATOM   14074 C  CD  . GLU D  1 382 ? -0.772  44.447  -31.816 1.00 41.93  ?  413  GLU D CD  1 
ATOM   14075 O  OE1 . GLU D  1 382 ? -1.453  44.445  -30.766 1.00 41.15  ?  413  GLU D OE1 1 
ATOM   14076 O  OE2 . GLU D  1 382 ? 0.453   44.168  -31.826 1.00 42.12  -1 413  GLU D OE2 1 
ATOM   14077 N  N   . GLY D  1 383 ? -3.257  40.192  -33.133 1.00 34.17  ?  414  GLY D N   1 
ATOM   14078 C  CA  . GLY D  1 383 ? -4.327  39.237  -33.388 1.00 30.95  ?  414  GLY D CA  1 
ATOM   14079 C  C   . GLY D  1 383 ? -3.904  37.994  -34.138 1.00 35.95  ?  414  GLY D C   1 
ATOM   14080 O  O   . GLY D  1 383 ? -4.742  37.112  -34.376 1.00 34.33  ?  414  GLY D O   1 
ATOM   14081 N  N   . TYR D  1 384 ? -2.634  37.884  -34.508 1.00 30.18  ?  415  TYR D N   1 
ATOM   14082 C  CA  . TYR D  1 384 ? -2.133  36.733  -35.249 1.00 31.21  ?  415  TYR D CA  1 
ATOM   14083 C  C   . TYR D  1 384 ? -0.628  36.691  -35.028 1.00 33.09  ?  415  TYR D C   1 
ATOM   14084 O  O   . TYR D  1 384 ? -0.078  37.530  -34.311 1.00 31.66  ?  415  TYR D O   1 
ATOM   14085 C  CB  . TYR D  1 384 ? -2.507  36.832  -36.736 1.00 29.93  ?  415  TYR D CB  1 
ATOM   14086 C  CG  . TYR D  1 384 ? -1.849  38.000  -37.467 1.00 32.60  ?  415  TYR D CG  1 
ATOM   14087 C  CD1 . TYR D  1 384 ? -2.426  39.278  -37.451 1.00 30.62  ?  415  TYR D CD1 1 
ATOM   14088 C  CD2 . TYR D  1 384 ? -0.652  37.819  -38.177 1.00 29.00  ?  415  TYR D CD2 1 
ATOM   14089 C  CE1 . TYR D  1 384 ? -1.829  40.351  -38.129 1.00 31.99  ?  415  TYR D CE1 1 
ATOM   14090 C  CE2 . TYR D  1 384 ? -0.050  38.874  -38.855 1.00 29.30  ?  415  TYR D CE2 1 
ATOM   14091 C  CZ  . TYR D  1 384 ? -0.637  40.144  -38.821 1.00 31.92  ?  415  TYR D CZ  1 
ATOM   14092 O  OH  . TYR D  1 384 ? -0.026  41.201  -39.471 1.00 27.38  ?  415  TYR D OH  1 
ATOM   14093 N  N   . ASN D  1 385 ? 0.039   35.710  -35.653 1.00 29.28  ?  416  ASN D N   1 
ATOM   14094 C  CA  . ASN D  1 385 ? 1.483   35.524  -35.516 1.00 31.01  ?  416  ASN D CA  1 
ATOM   14095 C  C   . ASN D  1 385 ? 2.140   35.458  -36.887 1.00 29.08  ?  416  ASN D C   1 
ATOM   14096 O  O   . ASN D  1 385 ? 1.584   34.878  -37.829 1.00 31.50  ?  416  ASN D O   1 
ATOM   14097 C  CB  . ASN D  1 385 ? 1.828   34.238  -34.753 1.00 28.48  ?  416  ASN D CB  1 
ATOM   14098 C  CG  . ASN D  1 385 ? 1.229   34.206  -33.372 1.00 33.64  ?  416  ASN D CG  1 
ATOM   14099 O  OD1 . ASN D  1 385 ? 1.401   35.141  -32.586 1.00 33.73  ?  416  ASN D OD1 1 
ATOM   14100 N  ND2 . ASN D  1 385 ? 0.507   33.134  -33.066 1.00 33.71  ?  416  ASN D ND2 1 
ATOM   14101 N  N   . ASP D  1 386 ? 3.317   36.085  -36.975 1.00 28.01  ?  417  ASP D N   1 
ATOM   14102 C  CA  . ASP D  1 386 ? 4.173   35.929  -38.180 1.00 28.18  ?  417  ASP D CA  1 
ATOM   14103 C  C   . ASP D  1 386 ? 5.150   34.811  -37.808 1.00 29.69  ?  417  ASP D C   1 
ATOM   14104 O  O   . ASP D  1 386 ? 5.567   34.811  -36.628 1.00 30.21  ?  417  ASP D O   1 
ATOM   14105 C  CB  . ASP D  1 386 ? 4.923   37.198  -38.541 1.00 28.07  ?  417  ASP D CB  1 
ATOM   14106 C  CG  . ASP D  1 386 ? 4.076   38.321  -39.117 1.00 32.39  ?  417  ASP D CG  1 
ATOM   14107 O  OD1 . ASP D  1 386 ? 2.988   38.016  -39.647 1.00 27.21  ?  417  ASP D OD1 1 
ATOM   14108 O  OD2 . ASP D  1 386 ? 4.529   39.480  -39.045 1.00 28.95  -1 417  ASP D OD2 1 
ATOM   14109 N  N   . VAL D  1 387 ? 5.514   33.923  -38.735 1.00 30.96  ?  418  VAL D N   1 
ATOM   14110 C  CA  . VAL D  1 387 ? 6.345   32.759  -38.468 1.00 27.95  ?  418  VAL D CA  1 
ATOM   14111 C  C   . VAL D  1 387 ? 7.351   32.597  -39.592 1.00 28.79  ?  418  VAL D C   1 
ATOM   14112 O  O   . VAL D  1 387 ? 7.071   32.905  -40.752 1.00 26.93  ?  418  VAL D O   1 
ATOM   14113 C  CB  . VAL D  1 387 ? 5.515   31.459  -38.317 1.00 33.28  ?  418  VAL D CB  1 
ATOM   14114 C  CG1 . VAL D  1 387 ? 6.432   30.252  -37.974 1.00 30.25  ?  418  VAL D CG1 1 
ATOM   14115 C  CG2 . VAL D  1 387 ? 4.459   31.626  -37.254 1.00 33.36  ?  418  VAL D CG2 1 
ATOM   14116 N  N   . GLY D  1 388 ? 8.535   32.110  -39.232 1.00 26.88  ?  419  GLY D N   1 
ATOM   14117 C  CA  . GLY D  1 388 ? 9.502   31.642  -40.207 1.00 28.77  ?  419  GLY D CA  1 
ATOM   14118 C  C   . GLY D  1 388 ? 10.225  30.434  -39.651 1.00 30.65  ?  419  GLY D C   1 
ATOM   14119 O  O   . GLY D  1 388 ? 10.495  30.373  -38.447 1.00 30.16  ?  419  GLY D O   1 
ATOM   14120 N  N   . ALA D  1 389 ? 10.520  29.450  -40.496 1.00 31.68  ?  420  ALA D N   1 
ATOM   14121 C  CA  . ALA D  1 389 ? 11.232  28.268  -40.023 1.00 29.07  ?  420  ALA D CA  1 
ATOM   14122 C  C   . ALA D  1 389 ? 12.049  27.725  -41.174 1.00 30.16  ?  420  ALA D C   1 
ATOM   14123 O  O   . ALA D  1 389 ? 11.512  27.535  -42.270 1.00 31.30  ?  420  ALA D O   1 
ATOM   14124 C  CB  . ALA D  1 389 ? 10.278  27.194  -39.500 1.00 25.79  ?  420  ALA D CB  1 
ATOM   14125 N  N   . ARG D  1 390 ? 13.332  27.484  -40.926 1.00 27.12  ?  421  ARG D N   1 
ATOM   14126 C  CA  . ARG D  1 390 ? 14.250  27.019  -41.962 1.00 32.62  ?  421  ARG D CA  1 
ATOM   14127 C  C   . ARG D  1 390 ? 14.914  25.705  -41.562 1.00 33.46  ?  421  ARG D C   1 
ATOM   14128 O  O   . ARG D  1 390 ? 15.462  25.585  -40.460 1.00 35.18  ?  421  ARG D O   1 
ATOM   14129 C  CB  . ARG D  1 390 ? 15.333  28.061  -42.263 1.00 31.73  ?  421  ARG D CB  1 
ATOM   14130 C  CG  . ARG D  1 390 ? 16.236  27.607  -43.395 1.00 30.18  ?  421  ARG D CG  1 
ATOM   14131 C  CD  . ARG D  1 390 ? 17.348  28.581  -43.716 1.00 31.39  ?  421  ARG D CD  1 
ATOM   14132 N  NE  . ARG D  1 390 ? 18.303  27.943  -44.610 1.00 28.22  ?  421  ARG D NE  1 
ATOM   14133 C  CZ  . ARG D  1 390 ? 19.266  28.584  -45.252 1.00 30.05  ?  421  ARG D CZ  1 
ATOM   14134 N  NH1 . ARG D  1 390 ? 19.420  29.894  -45.134 1.00 26.10  ?  421  ARG D NH1 1 
ATOM   14135 N  NH2 . ARG D  1 390 ? 20.099  27.893  -46.023 1.00 31.68  ?  421  ARG D NH2 1 
ATOM   14136 N  N   . MET D  1 391 ? 14.896  24.735  -42.481 1.00 33.71  ?  422  MET D N   1 
ATOM   14137 C  CA  . MET D  1 391 ? 15.680  23.499  -42.376 1.00 32.85  ?  422  MET D CA  1 
ATOM   14138 C  C   . MET D  1 391 ? 16.428  23.281  -43.685 1.00 33.31  ?  422  MET D C   1 
ATOM   14139 O  O   . MET D  1 391 ? 15.805  23.099  -44.733 1.00 32.23  ?  422  MET D O   1 
ATOM   14140 C  CB  . MET D  1 391 ? 14.786  22.302  -42.039 1.00 36.09  ?  422  MET D CB  1 
ATOM   14141 C  CG  . MET D  1 391 ? 15.538  21.013  -41.616 1.00 40.63  ?  422  MET D CG  1 
ATOM   14142 S  SD  . MET D  1 391 ? 14.327  19.740  -41.166 1.00 50.23  ?  422  MET D SD  1 
ATOM   14143 C  CE  . MET D  1 391 ? 15.129  18.228  -41.678 1.00 53.54  ?  422  MET D CE  1 
ATOM   14144 N  N   . GLY D  1 392 ? 17.760  23.321  -43.633 1.00 32.16  ?  423  GLY D N   1 
ATOM   14145 C  CA  . GLY D  1 392 ? 18.537  23.146  -44.853 1.00 33.42  ?  423  GLY D CA  1 
ATOM   14146 C  C   . GLY D  1 392 ? 18.183  24.209  -45.883 1.00 37.40  ?  423  GLY D C   1 
ATOM   14147 O  O   . GLY D  1 392 ? 18.196  25.412  -45.598 1.00 36.78  ?  423  GLY D O   1 
ATOM   14148 N  N   . ASP D  1 393 ? 17.854  23.767  -47.102 1.00 33.74  ?  424  ASP D N   1 
ATOM   14149 C  CA  . ASP D  1 393 ? 17.532  24.684  -48.189 1.00 32.44  ?  424  ASP D CA  1 
ATOM   14150 C  C   . ASP D  1 393 ? 16.110  25.220  -48.121 1.00 32.29  ?  424  ASP D C   1 
ATOM   14151 O  O   . ASP D  1 393 ? 15.756  26.064  -48.951 1.00 35.11  ?  424  ASP D O   1 
ATOM   14152 C  CB  . ASP D  1 393 ? 17.703  24.005  -49.556 1.00 33.10  ?  424  ASP D CB  1 
ATOM   14153 C  CG  . ASP D  1 393 ? 19.161  23.689  -49.897 1.00 40.73  ?  424  ASP D CG  1 
ATOM   14154 O  OD1 . ASP D  1 393 ? 20.083  24.426  -49.467 1.00 36.03  ?  424  ASP D OD1 1 
ATOM   14155 O  OD2 . ASP D  1 393 ? 19.368  22.704  -50.639 1.00 38.74  -1 424  ASP D OD2 1 
ATOM   14156 N  N   . TRP D  1 394 ? 15.288  24.745  -47.186 1.00 30.96  ?  425  TRP D N   1 
ATOM   14157 C  CA  . TRP D  1 394 ? 13.853  24.984  -47.207 1.00 31.29  ?  425  TRP D CA  1 
ATOM   14158 C  C   . TRP D  1 394 ? 13.422  25.912  -46.078 1.00 30.74  ?  425  TRP D C   1 
ATOM   14159 O  O   . TRP D  1 394 ? 13.888  25.787  -44.937 1.00 29.60  ?  425  TRP D O   1 
ATOM   14160 C  CB  . TRP D  1 394 ? 13.089  23.657  -47.105 1.00 31.26  ?  425  TRP D CB  1 
ATOM   14161 C  CG  . TRP D  1 394 ? 13.349  22.777  -48.289 1.00 34.19  ?  425  TRP D CG  1 
ATOM   14162 C  CD1 . TRP D  1 394 ? 14.251  21.759  -48.372 1.00 38.90  ?  425  TRP D CD1 1 
ATOM   14163 C  CD2 . TRP D  1 394 ? 12.733  22.876  -49.575 1.00 34.97  ?  425  TRP D CD2 1 
ATOM   14164 N  NE1 . TRP D  1 394 ? 14.218  21.201  -49.627 1.00 38.26  ?  425  TRP D NE1 1 
ATOM   14165 C  CE2 . TRP D  1 394 ? 13.298  21.872  -50.388 1.00 37.64  ?  425  TRP D CE2 1 
ATOM   14166 C  CE3 . TRP D  1 394 ? 11.748  23.713  -50.116 1.00 33.74  ?  425  TRP D CE3 1 
ATOM   14167 C  CZ2 . TRP D  1 394 ? 12.911  21.675  -51.716 1.00 39.18  ?  425  TRP D CZ2 1 
ATOM   14168 C  CZ3 . TRP D  1 394 ? 11.363  23.521  -51.437 1.00 40.35  ?  425  TRP D CZ3 1 
ATOM   14169 C  CH2 . TRP D  1 394 ? 11.943  22.502  -52.224 1.00 37.38  ?  425  TRP D CH2 1 
ATOM   14170 N  N   . LYS D  1 395 ? 12.497  26.809  -46.397 1.00 27.16  ?  426  LYS D N   1 
ATOM   14171 C  CA  . LYS D  1 395 ? 11.906  27.731  -45.435 1.00 28.92  ?  426  LYS D CA  1 
ATOM   14172 C  C   . LYS D  1 395 ? 10.398  27.741  -45.588 1.00 30.82  ?  426  LYS D C   1 
ATOM   14173 O  O   . LYS D  1 395 ? 9.886   27.723  -46.710 1.00 31.29  ?  426  LYS D O   1 
ATOM   14174 C  CB  . LYS D  1 395 ? 12.418  29.163  -45.617 1.00 27.36  ?  426  LYS D CB  1 
ATOM   14175 C  CG  . LYS D  1 395 ? 12.151  30.039  -44.386 1.00 32.57  ?  426  LYS D CG  1 
ATOM   14176 C  CD  . LYS D  1 395 ? 12.105  31.508  -44.719 1.00 31.11  ?  426  LYS D CD  1 
ATOM   14177 C  CE  . LYS D  1 395 ? 11.637  32.335  -43.492 1.00 30.03  ?  426  LYS D CE  1 
ATOM   14178 N  NZ  . LYS D  1 395 ? 11.866  33.800  -43.735 1.00 28.51  ?  426  LYS D NZ  1 
ATOM   14179 N  N   . ILE D  1 396 ? 9.694   27.789  -44.462 1.00 29.08  ?  427  ILE D N   1 
ATOM   14180 C  CA  . ILE D  1 396 ? 8.266   28.087  -44.454 1.00 30.38  ?  427  ILE D CA  1 
ATOM   14181 C  C   . ILE D  1 396 ? 8.092   29.461  -43.826 1.00 30.75  ?  427  ILE D C   1 
ATOM   14182 O  O   . ILE D  1 396 ? 8.837   29.834  -42.915 1.00 29.00  ?  427  ILE D O   1 
ATOM   14183 C  CB  . ILE D  1 396 ? 7.438   27.015  -43.717 1.00 27.17  ?  427  ILE D CB  1 
ATOM   14184 C  CG1 . ILE D  1 396 ? 7.936   26.810  -42.277 1.00 30.36  ?  427  ILE D CG1 1 
ATOM   14185 C  CG2 . ILE D  1 396 ? 7.459   25.709  -44.518 1.00 30.24  ?  427  ILE D CG2 1 
ATOM   14186 C  CD1 . ILE D  1 396 ? 6.893   26.119  -41.368 1.00 30.15  ?  427  ILE D CD1 1 
ATOM   14187 N  N   . THR D  1 397 ? 7.153   30.234  -44.356 1.00 26.53  ?  428  THR D N   1 
ATOM   14188 C  CA  . THR D  1 397 ? 6.926   31.590  -43.891 1.00 29.32  ?  428  THR D CA  1 
ATOM   14189 C  C   . THR D  1 397 ? 5.428   31.826  -43.852 1.00 27.52  ?  428  THR D C   1 
ATOM   14190 O  O   . THR D  1 397 ? 4.711   31.438  -44.774 1.00 26.24  ?  428  THR D O   1 
ATOM   14191 C  CB  . THR D  1 397 ? 7.556   32.647  -44.835 1.00 27.42  ?  428  THR D CB  1 
ATOM   14192 O  OG1 . THR D  1 397 ? 8.905   32.295  -45.164 1.00 31.65  ?  428  THR D OG1 1 
ATOM   14193 C  CG2 . THR D  1 397 ? 7.515   34.046  -44.196 1.00 26.72  ?  428  THR D CG2 1 
ATOM   14194 N  N   . ARG D  1 398 ? 4.966   32.478  -42.797 1.00 27.88  ?  429  ARG D N   1 
ATOM   14195 C  CA  . ARG D  1 398 ? 3.637   33.077  -42.787 1.00 27.90  ?  429  ARG D CA  1 
ATOM   14196 C  C   . ARG D  1 398 ? 3.795   34.514  -42.317 1.00 28.38  ?  429  ARG D C   1 
ATOM   14197 O  O   . ARG D  1 398 ? 4.385   34.770  -41.257 1.00 27.71  ?  429  ARG D O   1 
ATOM   14198 C  CB  . ARG D  1 398 ? 2.657   32.315  -41.886 1.00 29.80  ?  429  ARG D CB  1 
ATOM   14199 C  CG  . ARG D  1 398 ? 1.208   32.776  -42.082 1.00 31.29  ?  429  ARG D CG  1 
ATOM   14200 C  CD  . ARG D  1 398 ? 0.196   31.908  -41.317 1.00 30.49  ?  429  ARG D CD  1 
ATOM   14201 N  NE  . ARG D  1 398 ? -1.160  32.258  -41.732 1.00 29.82  ?  429  ARG D NE  1 
ATOM   14202 C  CZ  . ARG D  1 398 ? -2.270  31.897  -41.098 1.00 32.24  ?  429  ARG D CZ  1 
ATOM   14203 N  NH1 . ARG D  1 398 ? -2.240  31.073  -40.055 1.00 31.06  ?  429  ARG D NH1 1 
ATOM   14204 N  NH2 . ARG D  1 398 ? -3.443  32.347  -41.543 1.00 32.38  ?  429  ARG D NH2 1 
ATOM   14205 N  N   . MET D  1 399 ? 3.286   35.400  -43.164 1.00 29.23  ?  430  MET D N   1 
ATOM   14206 C  CA  . MET D  1 399 ? 3.367   36.845  -42.887 1.00 30.07  ?  430  MET D CA  1 
ATOM   14207 C  C   . MET D  1 399 ? 1.971   37.418  -43.096 1.00 31.53  ?  430  MET D C   1 
ATOM   14208 O  O   . MET D  1 399 ? 1.290   37.024  -44.062 1.00 28.21  ?  430  MET D O   1 
ATOM   14209 C  CB  . MET D  1 399 ? 4.339   37.562  -43.829 1.00 28.01  ?  430  MET D CB  1 
ATOM   14210 C  CG  . MET D  1 399 ? 5.773   37.536  -43.348 1.00 30.24  ?  430  MET D CG  1 
ATOM   14211 S  SD  . MET D  1 399 ? 5.913   38.465  -41.809 1.00 29.83  ?  430  MET D SD  1 
ATOM   14212 C  CE  . MET D  1 399 ? 5.661   40.111  -42.484 1.00 26.46  ?  430  MET D CE  1 
ATOM   14213 N  N   . GLY D  1 400 ? 1.613   38.338  -42.230 1.00 29.43  ?  431  GLY D N   1 
ATOM   14214 C  CA  . GLY D  1 400 ? 0.344   39.044  -42.317 1.00 28.28  ?  431  GLY D CA  1 
ATOM   14215 C  C   . GLY D  1 400 ? -0.896  38.177  -42.192 1.00 26.91  ?  431  GLY D C   1 
ATOM   14216 O  O   . GLY D  1 400 ? -2.013  38.629  -42.497 1.00 33.01  ?  431  GLY D O   1 
ATOM   14217 N  N   . ASN D  1 401 ? -0.700  36.927  -41.766 1.00 25.48  ?  432  ASN D N   1 
ATOM   14218 C  CA  . ASN D  1 401 ? -1.726  35.892  -41.632 1.00 31.71  ?  432  ASN D CA  1 
ATOM   14219 C  C   . ASN D  1 401 ? -2.223  35.370  -42.980 1.00 31.39  ?  432  ASN D C   1 
ATOM   14220 O  O   . ASN D  1 401 ? -3.300  34.763  -43.058 1.00 29.44  ?  432  ASN D O   1 
ATOM   14221 C  CB  . ASN D  1 401 ? -2.910  36.360  -40.772 1.00 29.70  ?  432  ASN D CB  1 
ATOM   14222 C  CG  . ASN D  1 401 ? -3.367  35.284  -39.787 1.00 31.79  ?  432  ASN D CG  1 
ATOM   14223 O  OD1 . ASN D  1 401 ? -2.549  34.539  -39.278 1.00 29.10  ?  432  ASN D OD1 1 
ATOM   14224 N  ND2 . ASN D  1 401 ? -4.689  35.180  -39.556 1.00 32.83  ?  432  ASN D ND2 1 
ATOM   14225 N  N   . GLU D  1 402 ? -1.438  35.580  -44.032 1.00 25.92  ?  433  GLU D N   1 
ATOM   14226 C  CA  . GLU D  1 402 ? -1.745  35.101  -45.364 1.00 31.51  ?  433  GLU D CA  1 
ATOM   14227 C  C   . GLU D  1 402 ? -1.566  33.586  -45.420 1.00 30.15  ?  433  GLU D C   1 
ATOM   14228 O  O   . GLU D  1 402 ? -1.092  32.973  -44.464 1.00 27.54  ?  433  GLU D O   1 
ATOM   14229 C  CB  . GLU D  1 402 ? -0.844  35.815  -46.381 1.00 29.59  ?  433  GLU D CB  1 
ATOM   14230 C  CG  . GLU D  1 402 ? -1.324  37.222  -46.673 1.00 30.41  ?  433  GLU D CG  1 
ATOM   14231 C  CD  . GLU D  1 402 ? -2.629  37.222  -47.462 1.00 32.17  ?  433  GLU D CD  1 
ATOM   14232 O  OE1 . GLU D  1 402 ? -2.636  36.687  -48.598 1.00 30.69  ?  433  GLU D OE1 1 
ATOM   14233 O  OE2 . GLU D  1 402 ? -3.647  37.752  -46.946 1.00 33.11  -1 433  GLU D OE2 1 
ATOM   14234 N  N   . PRO D  1 403 ? -1.927  32.948  -46.533 1.00 28.86  ?  434  PRO D N   1 
ATOM   14235 C  CA  . PRO D  1 403 ? -1.625  31.519  -46.671 1.00 30.34  ?  434  PRO D CA  1 
ATOM   14236 C  C   . PRO D  1 403 ? -0.142  31.241  -46.466 1.00 31.98  ?  434  PRO D C   1 
ATOM   14237 O  O   . PRO D  1 403 ? 0.717   32.068  -46.782 1.00 28.70  ?  434  PRO D O   1 
ATOM   14238 C  CB  . PRO D  1 403 ? -2.063  31.206  -48.110 1.00 33.94  ?  434  PRO D CB  1 
ATOM   14239 C  CG  . PRO D  1 403 ? -3.170  32.189  -48.366 1.00 30.05  ?  434  PRO D CG  1 
ATOM   14240 C  CD  . PRO D  1 403 ? -2.734  33.446  -47.671 1.00 30.21  ?  434  PRO D CD  1 
ATOM   14241 N  N   . TRP D  1 404 ? 0.146   30.052  -45.945 1.00 31.60  ?  435  TRP D N   1 
ATOM   14242 C  CA  . TRP D  1 404 ? 1.520   29.619  -45.708 1.00 29.31  ?  435  TRP D CA  1 
ATOM   14243 C  C   . TRP D  1 404 ? 2.325   29.552  -46.999 1.00 31.89  ?  435  TRP D C   1 
ATOM   14244 O  O   . TRP D  1 404 ? 1.808   29.202  -48.057 1.00 30.20  ?  435  TRP D O   1 
ATOM   14245 C  CB  . TRP D  1 404 ? 1.519   28.243  -45.064 1.00 28.07  ?  435  TRP D CB  1 
ATOM   14246 C  CG  . TRP D  1 404 ? 1.324   28.303  -43.617 1.00 33.29  ?  435  TRP D CG  1 
ATOM   14247 C  CD1 . TRP D  1 404 ? 0.143   28.150  -42.937 1.00 32.56  ?  435  TRP D CD1 1 
ATOM   14248 C  CD2 . TRP D  1 404 ? 2.335   28.531  -42.633 1.00 28.79  ?  435  TRP D CD2 1 
ATOM   14249 N  NE1 . TRP D  1 404 ? 0.362   28.273  -41.590 1.00 31.15  ?  435  TRP D NE1 1 
ATOM   14250 C  CE2 . TRP D  1 404 ? 1.699   28.506  -41.373 1.00 30.70  ?  435  TRP D CE2 1 
ATOM   14251 C  CE3 . TRP D  1 404 ? 3.720   28.748  -42.695 1.00 31.70  ?  435  TRP D CE3 1 
ATOM   14252 C  CZ2 . TRP D  1 404 ? 2.402   28.690  -40.173 1.00 31.38  ?  435  TRP D CZ2 1 
ATOM   14253 C  CZ3 . TRP D  1 404 ? 4.418   28.934  -41.515 1.00 26.63  ?  435  TRP D CZ3 1 
ATOM   14254 C  CH2 . TRP D  1 404 ? 3.755   28.899  -40.261 1.00 30.37  ?  435  TRP D CH2 1 
ATOM   14255 N  N   . ARG D  1 405 ? 3.630   29.809  -46.887 1.00 31.67  ?  436  ARG D N   1 
ATOM   14256 C  CA  . ARG D  1 405 ? 4.533   29.758  -48.033 1.00 29.56  ?  436  ARG D CA  1 
ATOM   14257 C  C   . ARG D  1 405 ? 5.661   28.772  -47.787 1.00 30.89  ?  436  ARG D C   1 
ATOM   14258 O  O   . ARG D  1 405 ? 6.190   28.683  -46.674 1.00 30.90  ?  436  ARG D O   1 
ATOM   14259 C  CB  . ARG D  1 405 ? 5.133   31.132  -48.337 1.00 32.98  ?  436  ARG D CB  1 
ATOM   14260 C  CG  . ARG D  1 405 ? 4.121   32.247  -48.453 1.00 28.57  ?  436  ARG D CG  1 
ATOM   14261 C  CD  . ARG D  1 405 ? 4.768   33.625  -48.500 1.00 29.53  ?  436  ARG D CD  1 
ATOM   14262 N  NE  . ARG D  1 405 ? 5.523   33.863  -49.724 1.00 29.07  ?  436  ARG D NE  1 
ATOM   14263 C  CZ  . ARG D  1 405 ? 4.984   34.222  -50.879 1.00 32.82  ?  436  ARG D CZ  1 
ATOM   14264 N  NH1 . ARG D  1 405 ? 3.674   34.317  -51.027 1.00 32.35  ?  436  ARG D NH1 1 
ATOM   14265 N  NH2 . ARG D  1 405 ? 5.779   34.476  -51.918 1.00 29.49  ?  436  ARG D NH2 1 
ATOM   14266 N  N   . LEU D  1 406 ? 6.041   28.047  -48.835 1.00 30.63  ?  437  LEU D N   1 
ATOM   14267 C  CA  . LEU D  1 406 ? 7.197   27.159  -48.807 1.00 34.44  ?  437  LEU D CA  1 
ATOM   14268 C  C   . LEU D  1 406 ? 8.171   27.668  -49.852 1.00 32.43  ?  437  LEU D C   1 
ATOM   14269 O  O   . LEU D  1 406 ? 7.796   27.833  -51.019 1.00 30.82  ?  437  LEU D O   1 
ATOM   14270 C  CB  . LEU D  1 406 ? 6.802   25.707  -49.104 1.00 35.95  ?  437  LEU D CB  1 
ATOM   14271 C  CG  . LEU D  1 406 ? 7.967   24.720  -49.245 1.00 34.09  ?  437  LEU D CG  1 
ATOM   14272 C  CD1 . LEU D  1 406 ? 8.708   24.576  -47.905 1.00 28.18  ?  437  LEU D CD1 1 
ATOM   14273 C  CD2 . LEU D  1 406 ? 7.493   23.361  -49.755 1.00 31.77  ?  437  LEU D CD2 1 
ATOM   14274 N  N   . HIS D  1 407 ? 9.412   27.932  -49.435 1.00 32.19  ?  438  HIS D N   1 
ATOM   14275 C  CA  . HIS D  1 407 ? 10.436  28.420  -50.344 1.00 33.93  ?  438  HIS D CA  1 
ATOM   14276 C  C   . HIS D  1 407 ? 11.656  27.518  -50.280 1.00 32.84  ?  438  HIS D C   1 
ATOM   14277 O  O   . HIS D  1 407 ? 12.027  27.021  -49.213 1.00 31.82  ?  438  HIS D O   1 
ATOM   14278 C  CB  . HIS D  1 407 ? 10.857  29.859  -50.017 1.00 31.07  ?  438  HIS D CB  1 
ATOM   14279 C  CG  . HIS D  1 407 ? 9.726   30.834  -50.078 1.00 33.01  ?  438  HIS D CG  1 
ATOM   14280 N  ND1 . HIS D  1 407 ? 9.175   31.258  -51.264 1.00 33.26  ?  438  HIS D ND1 1 
ATOM   14281 C  CD2 . HIS D  1 407 ? 9.033   31.456  -49.095 1.00 31.29  ?  438  HIS D CD2 1 
ATOM   14282 C  CE1 . HIS D  1 407 ? 8.184   32.099  -51.012 1.00 32.14  ?  438  HIS D CE1 1 
ATOM   14283 N  NE2 . HIS D  1 407 ? 8.083   32.239  -49.702 1.00 32.12  ?  438  HIS D NE2 1 
ATOM   14284 N  N   . ASN D  1 408 ? 12.261  27.284  -51.435 1.00 32.14  ?  439  ASN D N   1 
ATOM   14285 C  CA  . ASN D  1 408 ? 13.649  26.865  -51.439 1.00 33.06  ?  439  ASN D CA  1 
ATOM   14286 C  C   . ASN D  1 408 ? 14.455  28.147  -51.284 1.00 33.89  ?  439  ASN D C   1 
ATOM   14287 O  O   . ASN D  1 408 ? 14.619  28.915  -52.236 1.00 29.86  ?  439  ASN D O   1 
ATOM   14288 C  CB  . ASN D  1 408 ? 14.010  26.110  -52.708 1.00 36.55  ?  439  ASN D CB  1 
ATOM   14289 C  CG  . ASN D  1 408 ? 15.366  25.443  -52.590 1.00 37.17  ?  439  ASN D CG  1 
ATOM   14290 O  OD1 . ASN D  1 408 ? 16.374  26.121  -52.412 1.00 35.43  ?  439  ASN D OD1 1 
ATOM   14291 N  ND2 . ASN D  1 408 ? 15.389  24.115  -52.642 1.00 34.77  ?  439  ASN D ND2 1 
ATOM   14292 N  N   . ILE D  1 409 ? 14.912  28.410  -50.057 1.00 32.17  ?  440  ILE D N   1 
ATOM   14293 C  CA  . ILE D  1 409 ? 15.545  29.691  -49.782 1.00 33.35  ?  440  ILE D CA  1 
ATOM   14294 C  C   . ILE D  1 409 ? 16.924  29.784  -50.438 1.00 34.92  ?  440  ILE D C   1 
ATOM   14295 O  O   . ILE D  1 409 ? 17.426  30.888  -50.666 1.00 36.20  ?  440  ILE D O   1 
ATOM   14296 C  CB  . ILE D  1 409 ? 15.611  29.916  -48.256 1.00 33.79  ?  440  ILE D CB  1 
ATOM   14297 C  CG1 . ILE D  1 409 ? 15.690  31.410  -47.921 1.00 32.62  ?  440  ILE D CG1 1 
ATOM   14298 C  CG2 . ILE D  1 409 ? 16.801  29.152  -47.635 1.00 31.46  ?  440  ILE D CG2 1 
ATOM   14299 C  CD1 . ILE D  1 409 ? 14.484  32.196  -48.369 1.00 29.93  ?  440  ILE D CD1 1 
ATOM   14300 N  N   . THR D  1 410 ? 17.554  28.652  -50.763 1.00 34.43  ?  441  THR D N   1 
ATOM   14301 C  CA  . THR D  1 410 ? 18.846  28.704  -51.445 1.00 34.17  ?  441  THR D CA  1 
ATOM   14302 C  C   . THR D  1 410 ? 18.678  29.118  -52.898 1.00 35.76  ?  441  THR D C   1 
ATOM   14303 O  O   . THR D  1 410 ? 19.465  29.913  -53.419 1.00 35.36  ?  441  THR D O   1 
ATOM   14304 C  CB  . THR D  1 410 ? 19.551  27.349  -51.332 1.00 35.69  ?  441  THR D CB  1 
ATOM   14305 O  OG1 . THR D  1 410 ? 19.704  27.020  -49.949 1.00 34.83  ?  441  THR D OG1 1 
ATOM   14306 C  CG2 . THR D  1 410 ? 20.933  27.367  -52.002 1.00 37.38  ?  441  THR D CG2 1 
ATOM   14307 N  N   . GLN D  1 411 ? 17.619  28.633  -53.549 1.00 37.45  ?  442  GLN D N   1 
ATOM   14308 C  CA  . GLN D  1 411 ? 17.317  28.995  -54.920 1.00 36.26  ?  442  GLN D CA  1 
ATOM   14309 C  C   . GLN D  1 411 ? 16.569  30.317  -55.036 1.00 36.67  ?  442  GLN D C   1 
ATOM   14310 O  O   . GLN D  1 411 ? 16.617  30.945  -56.103 1.00 36.30  ?  442  GLN D O   1 
ATOM   14311 C  CB  . GLN D  1 411 ? 16.479  27.885  -55.550 1.00 38.94  ?  442  GLN D CB  1 
ATOM   14312 C  CG  . GLN D  1 411 ? 17.294  26.675  -55.936 1.00 47.46  ?  442  GLN D CG  1 
ATOM   14313 C  CD  . GLN D  1 411 ? 16.633  25.859  -57.024 1.00 58.64  ?  442  GLN D CD  1 
ATOM   14314 O  OE1 . GLN D  1 411 ? 16.283  24.692  -56.810 1.00 60.46  ?  442  GLN D OE1 1 
ATOM   14315 N  NE2 . GLN D  1 411 ? 16.458  26.465  -58.205 1.00 63.43  ?  442  GLN D NE2 1 
ATOM   14316 N  N   . ASP D  1 412 ? 15.879  30.750  -53.971 1.00 34.41  ?  443  ASP D N   1 
ATOM   14317 C  CA  . ASP D  1 412 ? 14.881  31.823  -54.031 1.00 32.99  ?  443  ASP D CA  1 
ATOM   14318 C  C   . ASP D  1 412 ? 14.994  32.668  -52.758 1.00 35.59  ?  443  ASP D C   1 
ATOM   14319 O  O   . ASP D  1 412 ? 14.096  32.700  -51.916 1.00 30.53  ?  443  ASP D O   1 
ATOM   14320 C  CB  . ASP D  1 412 ? 13.494  31.187  -54.233 1.00 34.03  ?  443  ASP D CB  1 
ATOM   14321 C  CG  . ASP D  1 412 ? 12.314  32.179  -54.141 1.00 31.91  ?  443  ASP D CG  1 
ATOM   14322 O  OD1 . ASP D  1 412 ? 12.442  33.358  -54.524 1.00 31.25  ?  443  ASP D OD1 1 
ATOM   14323 O  OD2 . ASP D  1 412 ? 11.221  31.744  -53.705 1.00 33.42  -1 443  ASP D OD2 1 
ATOM   14324 N  N   . ILE D  1 413 ? 16.150  33.343  -52.604 1.00 30.84  ?  444  ILE D N   1 
ATOM   14325 C  CA  . ILE D  1 413 ? 16.472  34.048  -51.365 1.00 30.85  ?  444  ILE D CA  1 
ATOM   14326 C  C   . ILE D  1 413 ? 15.468  35.168  -51.089 1.00 31.82  ?  444  ILE D C   1 
ATOM   14327 O  O   . ILE D  1 413 ? 15.221  35.518  -49.925 1.00 33.00  ?  444  ILE D O   1 
ATOM   14328 C  CB  . ILE D  1 413 ? 17.933  34.580  -51.407 1.00 26.17  ?  444  ILE D CB  1 
ATOM   14329 C  CG1 . ILE D  1 413 ? 18.476  34.876  -49.992 1.00 29.53  ?  444  ILE D CG1 1 
ATOM   14330 C  CG2 . ILE D  1 413 ? 18.035  35.825  -52.258 1.00 28.93  ?  444  ILE D CG2 1 
ATOM   14331 C  CD1 . ILE D  1 413 ? 19.972  35.215  -49.983 1.00 30.31  ?  444  ILE D CD1 1 
ATOM   14332 N  N   . GLY D  1 414 ? 14.863  35.737  -52.133 1.00 27.16  ?  445  GLY D N   1 
ATOM   14333 C  CA  . GLY D  1 414 ? 13.872  36.784  -51.964 1.00 29.02  ?  445  GLY D CA  1 
ATOM   14334 C  C   . GLY D  1 414 ? 12.473  36.311  -51.647 1.00 31.48  ?  445  GLY D C   1 
ATOM   14335 O  O   . GLY D  1 414 ? 11.555  37.134  -51.565 1.00 29.41  ?  445  GLY D O   1 
ATOM   14336 N  N   . GLU D  1 415 ? 12.281  35.000  -51.457 1.00 28.97  ?  446  GLU D N   1 
ATOM   14337 C  CA  . GLU D  1 415 ? 10.991  34.444  -51.057 1.00 28.84  ?  446  GLU D CA  1 
ATOM   14338 C  C   . GLU D  1 415 ? 9.873   34.880  -52.006 1.00 26.82  ?  446  GLU D C   1 
ATOM   14339 O  O   . GLU D  1 415 ? 8.807   35.319  -51.576 1.00 26.21  ?  446  GLU D O   1 
ATOM   14340 C  CB  . GLU D  1 415 ? 10.661  34.829  -49.614 1.00 27.05  ?  446  GLU D CB  1 
ATOM   14341 C  CG  . GLU D  1 415 ? 11.589  34.154  -48.572 1.00 29.15  ?  446  GLU D CG  1 
ATOM   14342 C  CD  . GLU D  1 415 ? 11.428  34.741  -47.200 1.00 28.01  ?  446  GLU D CD  1 
ATOM   14343 O  OE1 . GLU D  1 415 ? 11.890  35.877  -47.014 1.00 27.09  ?  446  GLU D OE1 1 
ATOM   14344 O  OE2 . GLU D  1 415 ? 10.827  34.086  -46.311 1.00 29.67  -1 446  GLU D OE2 1 
ATOM   14345 N  N   . LYS D  1 416 ? 10.124  34.754  -53.310 1.00 29.89  ?  447  LYS D N   1 
ATOM   14346 C  CA  . LYS D  1 416 ? 9.125   35.148  -54.313 1.00 28.58  ?  447  LYS D CA  1 
ATOM   14347 C  C   . LYS D  1 416 ? 8.240   34.004  -54.798 1.00 28.72  ?  447  LYS D C   1 
ATOM   14348 O  O   . LYS D  1 416 ? 7.112   34.255  -55.249 1.00 31.90  ?  447  LYS D O   1 
ATOM   14349 C  CB  . LYS D  1 416 ? 9.810   35.784  -55.531 1.00 27.69  ?  447  LYS D CB  1 
ATOM   14350 C  CG  . LYS D  1 416 ? 10.720  36.966  -55.199 1.00 35.30  ?  447  LYS D CG  1 
ATOM   14351 C  CD  . LYS D  1 416 ? 11.491  37.440  -56.430 1.00 36.17  ?  447  LYS D CD  1 
ATOM   14352 C  CE  . LYS D  1 416 ? 12.091  38.813  -56.194 1.00 44.13  ?  447  LYS D CE  1 
ATOM   14353 N  NZ  . LYS D  1 416 ? 13.194  39.084  -57.141 1.00 50.19  ?  447  LYS D NZ  1 
ATOM   14354 N  N   . LYS D  1 417 ? 8.708   32.759  -54.741 1.00 31.36  ?  448  LYS D N   1 
ATOM   14355 C  CA  . LYS D  1 417 ? 8.058   31.645  -55.434 1.00 32.65  ?  448  LYS D CA  1 
ATOM   14356 C  C   . LYS D  1 417 ? 7.518   30.653  -54.416 1.00 33.08  ?  448  LYS D C   1 
ATOM   14357 O  O   . LYS D  1 417 ? 8.260   29.811  -53.898 1.00 32.22  ?  448  LYS D O   1 
ATOM   14358 C  CB  . LYS D  1 417 ? 9.037   30.972  -56.391 1.00 33.01  ?  448  LYS D CB  1 
ATOM   14359 C  CG  . LYS D  1 417 ? 9.759   31.960  -57.284 1.00 34.31  ?  448  LYS D CG  1 
ATOM   14360 C  CD  . LYS D  1 417 ? 8.740   32.667  -58.208 1.00 39.45  ?  448  LYS D CD  1 
ATOM   14361 C  CE  . LYS D  1 417 ? 9.384   33.840  -58.949 1.00 37.61  ?  448  LYS D CE  1 
ATOM   14362 N  NZ  . LYS D  1 417 ? 8.431   34.442  -59.907 1.00 47.08  ?  448  LYS D NZ  1 
ATOM   14363 N  N   . ASN D  1 418 ? 6.216   30.731  -54.153 1.00 31.72  ?  449  ASN D N   1 
ATOM   14364 C  CA  . ASN D  1 418 ? 5.586   29.837  -53.189 1.00 31.75  ?  449  ASN D CA  1 
ATOM   14365 C  C   . ASN D  1 418 ? 5.488   28.433  -53.777 1.00 34.84  ?  449  ASN D C   1 
ATOM   14366 O  O   . ASN D  1 418 ? 4.746   28.212  -54.738 1.00 37.34  ?  449  ASN D O   1 
ATOM   14367 C  CB  . ASN D  1 418 ? 4.201   30.353  -52.806 1.00 34.11  ?  449  ASN D CB  1 
ATOM   14368 C  CG  . ASN D  1 418 ? 3.656   29.662  -51.574 1.00 37.26  ?  449  ASN D CG  1 
ATOM   14369 O  OD1 . ASN D  1 418 ? 4.266   28.714  -51.074 1.00 33.08  ?  449  ASN D OD1 1 
ATOM   14370 N  ND2 . ASN D  1 418 ? 2.515   30.129  -51.073 1.00 33.70  ?  449  ASN D ND2 1 
ATOM   14371 N  N   . LEU D  1 419 ? 6.192   27.474  -53.177 1.00 33.61  ?  450  LEU D N   1 
ATOM   14372 C  CA  . LEU D  1 419 ? 6.165   26.085  -53.628 1.00 34.40  ?  450  LEU D CA  1 
ATOM   14373 C  C   . LEU D  1 419 ? 5.230   25.216  -52.794 1.00 34.08  ?  450  LEU D C   1 
ATOM   14374 O  O   . LEU D  1 419 ? 5.275   23.983  -52.903 1.00 36.20  ?  450  LEU D O   1 
ATOM   14375 C  CB  . LEU D  1 419 ? 7.581   25.504  -53.613 1.00 31.71  ?  450  LEU D CB  1 
ATOM   14376 C  CG  . LEU D  1 419 ? 8.565   26.270  -54.505 1.00 33.05  ?  450  LEU D CG  1 
ATOM   14377 C  CD1 . LEU D  1 419 ? 9.954   25.651  -54.427 1.00 33.87  ?  450  LEU D CD1 1 
ATOM   14378 C  CD2 . LEU D  1 419 ? 8.095   26.284  -55.938 1.00 36.46  ?  450  LEU D CD2 1 
ATOM   14379 N  N   . ALA D  1 420 ? 4.378   25.830  -51.974 1.00 33.62  ?  451  ALA D N   1 
ATOM   14380 C  CA  . ALA D  1 420 ? 3.499   25.057  -51.102 1.00 37.76  ?  451  ALA D CA  1 
ATOM   14381 C  C   . ALA D  1 420 ? 2.607   24.115  -51.905 1.00 35.59  ?  451  ALA D C   1 
ATOM   14382 O  O   . ALA D  1 420 ? 2.434   22.951  -51.534 1.00 39.18  ?  451  ALA D O   1 
ATOM   14383 C  CB  . ALA D  1 420 ? 2.660   26.002  -50.238 1.00 33.57  ?  451  ALA D CB  1 
ATOM   14384 N  N   . GLY D  1 421 ? 2.053   24.589  -53.020 1.00 36.19  ?  452  GLY D N   1 
ATOM   14385 C  CA  . GLY D  1 421 ? 1.229   23.718  -53.851 1.00 37.36  ?  452  GLY D CA  1 
ATOM   14386 C  C   . GLY D  1 421 ? 1.992   22.538  -54.428 1.00 41.58  ?  452  GLY D C   1 
ATOM   14387 O  O   . GLY D  1 421 ? 1.426   21.454  -54.600 1.00 39.46  ?  452  GLY D O   1 
ATOM   14388 N  N   . ARG D  1 422 ? 3.289   22.721  -54.708 1.00 35.29  ?  453  ARG D N   1 
ATOM   14389 C  CA  . ARG D  1 422 ? 4.100   21.689  -55.353 1.00 35.96  ?  453  ARG D CA  1 
ATOM   14390 C  C   . ARG D  1 422 ? 4.626   20.636  -54.371 1.00 40.87  ?  453  ARG D C   1 
ATOM   14391 O  O   . ARG D  1 422 ? 4.776   19.469  -54.755 1.00 40.62  ?  453  ARG D O   1 
ATOM   14392 C  CB  . ARG D  1 422 ? 5.262   22.350  -56.106 1.00 38.00  ?  453  ARG D CB  1 
ATOM   14393 C  CG  . ARG D  1 422 ? 6.386   21.421  -56.503 1.00 40.09  ?  453  ARG D CG  1 
ATOM   14394 C  CD  . ARG D  1 422 ? 6.182   20.831  -57.881 1.00 49.72  ?  453  ARG D CD  1 
ATOM   14395 N  NE  . ARG D  1 422 ? 7.399   20.898  -58.683 1.00 52.17  ?  453  ARG D NE  1 
ATOM   14396 C  CZ  . ARG D  1 422 ? 8.191   19.861  -58.918 1.00 52.71  ?  453  ARG D CZ  1 
ATOM   14397 N  NH1 . ARG D  1 422 ? 7.885   18.641  -58.477 1.00 49.89  ?  453  ARG D NH1 1 
ATOM   14398 N  NH2 . ARG D  1 422 ? 9.323   20.050  -59.600 1.00 45.61  ?  453  ARG D NH2 1 
ATOM   14399 N  N   . TYR D  1 423 ? 4.923   21.008  -53.119 1.00 34.56  ?  454  TYR D N   1 
ATOM   14400 C  CA  . TYR D  1 423 ? 5.461   20.082  -52.118 1.00 33.44  ?  454  TYR D CA  1 
ATOM   14401 C  C   . TYR D  1 423 ? 4.678   20.187  -50.816 1.00 36.26  ?  454  TYR D C   1 
ATOM   14402 O  O   . TYR D  1 423 ? 5.229   20.582  -49.781 1.00 35.57  ?  454  TYR D O   1 
ATOM   14403 C  CB  . TYR D  1 423 ? 6.943   20.355  -51.845 1.00 37.53  ?  454  TYR D CB  1 
ATOM   14404 C  CG  . TYR D  1 423 ? 7.841   20.232  -53.044 1.00 40.32  ?  454  TYR D CG  1 
ATOM   14405 C  CD1 . TYR D  1 423 ? 8.059   19.001  -53.639 1.00 42.20  ?  454  TYR D CD1 1 
ATOM   14406 C  CD2 . TYR D  1 423 ? 8.476   21.347  -53.583 1.00 39.21  ?  454  TYR D CD2 1 
ATOM   14407 C  CE1 . TYR D  1 423 ? 8.881   18.877  -54.741 1.00 44.35  ?  454  TYR D CE1 1 
ATOM   14408 C  CE2 . TYR D  1 423 ? 9.311   21.230  -54.681 1.00 40.88  ?  454  TYR D CE2 1 
ATOM   14409 C  CZ  . TYR D  1 423 ? 9.506   19.989  -55.250 1.00 42.51  ?  454  TYR D CZ  1 
ATOM   14410 O  OH  . TYR D  1 423 ? 10.315  19.850  -56.344 1.00 46.77  ?  454  TYR D OH  1 
ATOM   14411 N  N   . PRO D  1 424 ? 3.391   19.815  -50.826 1.00 35.64  ?  455  PRO D N   1 
ATOM   14412 C  CA  . PRO D  1 424 ? 2.571   19.997  -49.616 1.00 37.25  ?  455  PRO D CA  1 
ATOM   14413 C  C   . PRO D  1 424 ? 3.014   19.133  -48.451 1.00 39.51  ?  455  PRO D C   1 
ATOM   14414 O  O   . PRO D  1 424 ? 2.815   19.529  -47.295 1.00 41.05  ?  455  PRO D O   1 
ATOM   14415 C  CB  . PRO D  1 424 ? 1.157   19.617  -50.089 1.00 41.69  ?  455  PRO D CB  1 
ATOM   14416 C  CG  . PRO D  1 424 ? 1.389   18.697  -51.243 1.00 41.11  ?  455  PRO D CG  1 
ATOM   14417 C  CD  . PRO D  1 424 ? 2.621   19.228  -51.934 1.00 36.43  ?  455  PRO D CD  1 
ATOM   14418 N  N   . ASP D  1 425 ? 3.601   17.959  -48.708 1.00 36.10  ?  456  ASP D N   1 
ATOM   14419 C  CA  . ASP D  1 425 ? 4.062   17.134  -47.595 1.00 40.47  ?  456  ASP D CA  1 
ATOM   14420 C  C   . ASP D  1 425 ? 5.211   17.803  -46.854 1.00 38.54  ?  456  ASP D C   1 
ATOM   14421 O  O   . ASP D  1 425 ? 5.223   17.825  -45.618 1.00 39.11  ?  456  ASP D O   1 
ATOM   14422 C  CB  . ASP D  1 425 ? 4.480   15.749  -48.082 1.00 39.41  ?  456  ASP D CB  1 
ATOM   14423 C  CG  . ASP D  1 425 ? 3.326   14.974  -48.682 1.00 49.31  ?  456  ASP D CG  1 
ATOM   14424 O  OD1 . ASP D  1 425 ? 2.160   15.370  -48.451 1.00 45.22  ?  456  ASP D OD1 1 
ATOM   14425 O  OD2 . ASP D  1 425 ? 3.592   13.972  -49.383 1.00 48.03  -1 456  ASP D OD2 1 
ATOM   14426 N  N   . ARG D  1 426 ? 6.184   18.340  -47.592 1.00 36.96  ?  457  ARG D N   1 
ATOM   14427 C  CA  . ARG D  1 426 ? 7.288   19.054  -46.956 1.00 41.74  ?  457  ARG D CA  1 
ATOM   14428 C  C   . ARG D  1 426 ? 6.769   20.227  -46.135 1.00 37.00  ?  457  ARG D C   1 
ATOM   14429 O  O   . ARG D  1 426 ? 7.190   20.429  -44.994 1.00 37.34  ?  457  ARG D O   1 
ATOM   14430 C  CB  . ARG D  1 426 ? 8.296   19.547  -47.999 1.00 35.58  ?  457  ARG D CB  1 
ATOM   14431 C  CG  . ARG D  1 426 ? 9.456   20.349  -47.352 1.00 42.25  ?  457  ARG D CG  1 
ATOM   14432 C  CD  . ARG D  1 426 ? 10.675  20.522  -48.256 1.00 37.80  ?  457  ARG D CD  1 
ATOM   14433 N  NE  . ARG D  1 426 ? 11.155  19.271  -48.830 1.00 41.81  ?  457  ARG D NE  1 
ATOM   14434 C  CZ  . ARG D  1 426 ? 12.135  18.524  -48.328 1.00 50.17  ?  457  ARG D CZ  1 
ATOM   14435 N  NH1 . ARG D  1 426 ? 12.718  18.822  -47.174 1.00 46.49  ?  457  ARG D NH1 1 
ATOM   14436 N  NH2 . ARG D  1 426 ? 12.535  17.444  -48.997 1.00 51.60  ?  457  ARG D NH2 1 
ATOM   14437 N  N   . LEU D  1 427 ? 5.846   21.006  -46.707 1.00 35.66  ?  458  LEU D N   1 
ATOM   14438 C  CA  . LEU D  1 427 ? 5.248   22.128  -45.986 1.00 37.34  ?  458  LEU D CA  1 
ATOM   14439 C  C   . LEU D  1 427 ? 4.636   21.665  -44.670 1.00 39.40  ?  458  LEU D C   1 
ATOM   14440 O  O   . LEU D  1 427 ? 4.962   22.190  -43.603 1.00 38.70  ?  458  LEU D O   1 
ATOM   14441 C  CB  . LEU D  1 427 ? 4.193   22.809  -46.862 1.00 35.36  ?  458  LEU D CB  1 
ATOM   14442 C  CG  . LEU D  1 427 ? 3.241   23.812  -46.188 1.00 34.74  ?  458  LEU D CG  1 
ATOM   14443 C  CD1 . LEU D  1 427 ? 3.989   25.052  -45.754 1.00 35.50  ?  458  LEU D CD1 1 
ATOM   14444 C  CD2 . LEU D  1 427 ? 2.116   24.220  -47.107 1.00 38.67  ?  458  LEU D CD2 1 
ATOM   14445 N  N   . LYS D  1 428 ? 3.787   20.636  -44.725 1.00 40.72  ?  459  LYS D N   1 
ATOM   14446 C  CA  . LYS D  1 428 ? 3.050   20.212  -43.535 1.00 42.53  ?  459  LYS D CA  1 
ATOM   14447 C  C   . LYS D  1 428 ? 3.970   19.608  -42.479 1.00 38.44  ?  459  LYS D C   1 
ATOM   14448 O  O   . LYS D  1 428 ? 3.737   19.774  -41.279 1.00 38.39  ?  459  LYS D O   1 
ATOM   14449 C  CB  . LYS D  1 428 ? 1.967   19.209  -43.924 1.00 40.97  ?  459  LYS D CB  1 
ATOM   14450 C  CG  . LYS D  1 428 ? 0.869   19.817  -44.806 1.00 44.50  ?  459  LYS D CG  1 
ATOM   14451 C  CD  . LYS D  1 428 ? -0.246  20.441  -43.989 1.00 47.41  ?  459  LYS D CD  1 
ATOM   14452 C  CE  . LYS D  1 428 ? -1.584  20.172  -44.641 1.00 50.71  ?  459  LYS D CE  1 
ATOM   14453 N  NZ  . LYS D  1 428 ? -1.449  20.093  -46.123 1.00 56.30  ?  459  LYS D NZ  1 
ATOM   14454 N  N   . GLU D  1 429 ? 4.993   18.866  -42.889 1.00 38.34  ?  460  GLU D N   1 
ATOM   14455 C  CA  . GLU D  1 429 ? 5.860   18.279  -41.874 1.00 40.00  ?  460  GLU D CA  1 
ATOM   14456 C  C   . GLU D  1 429 ? 6.703   19.352  -41.207 1.00 37.98  ?  460  GLU D C   1 
ATOM   14457 O  O   . GLU D  1 429 ? 7.024   19.249  -40.020 1.00 38.35  ?  460  GLU D O   1 
ATOM   14458 C  CB  . GLU D  1 429 ? 6.705   17.171  -42.502 1.00 45.41  ?  460  GLU D CB  1 
ATOM   14459 C  CG  . GLU D  1 429 ? 7.778   17.627  -43.464 1.00 50.67  ?  460  GLU D CG  1 
ATOM   14460 C  CD  . GLU D  1 429 ? 8.486   16.453  -44.141 1.00 58.13  ?  460  GLU D CD  1 
ATOM   14461 O  OE1 . GLU D  1 429 ? 8.020   15.303  -43.962 1.00 62.36  ?  460  GLU D OE1 1 
ATOM   14462 O  OE2 . GLU D  1 429 ? 9.515   16.679  -44.826 1.00 56.95  -1 460  GLU D OE2 1 
ATOM   14463 N  N   . MET D  1 430 ? 7.016   20.413  -41.950 1.00 36.33  ?  461  MET D N   1 
ATOM   14464 C  CA  . MET D  1 430 ? 7.776   21.540  -41.417 1.00 39.19  ?  461  MET D CA  1 
ATOM   14465 C  C   . MET D  1 430 ? 6.889   22.373  -40.488 1.00 35.70  ?  461  MET D C   1 
ATOM   14466 O  O   . MET D  1 430 ? 7.321   22.804  -39.411 1.00 34.67  ?  461  MET D O   1 
ATOM   14467 C  CB  . MET D  1 430 ? 8.272   22.342  -42.619 1.00 39.14  ?  461  MET D CB  1 
ATOM   14468 C  CG  . MET D  1 430 ? 9.648   21.921  -43.124 1.00 36.68  ?  461  MET D CG  1 
ATOM   14469 S  SD  . MET D  1 430 ? 10.313  22.998  -44.417 1.00 35.24  ?  461  MET D SD  1 
ATOM   14470 C  CE  . MET D  1 430 ? 11.216  24.171  -43.384 1.00 31.62  ?  461  MET D CE  1 
ATOM   14471 N  N   . ILE D  1 431 ? 5.622   22.554  -40.871 1.00 34.97  ?  462  ILE D N   1 
ATOM   14472 C  CA  . ILE D  1 431 ? 4.638   23.184  -39.993 1.00 35.33  ?  462  ILE D CA  1 
ATOM   14473 C  C   . ILE D  1 431 ? 4.432   22.368  -38.723 1.00 39.61  ?  462  ILE D C   1 
ATOM   14474 O  O   . ILE D  1 431 ? 4.216   22.930  -37.638 1.00 38.59  ?  462  ILE D O   1 
ATOM   14475 C  CB  . ILE D  1 431 ? 3.320   23.390  -40.764 1.00 41.00  ?  462  ILE D CB  1 
ATOM   14476 C  CG1 . ILE D  1 431 ? 3.348   24.735  -41.476 1.00 37.36  ?  462  ILE D CG1 1 
ATOM   14477 C  CG2 . ILE D  1 431 ? 2.109   23.324  -39.843 1.00 38.28  ?  462  ILE D CG2 1 
ATOM   14478 C  CD1 . ILE D  1 431 ? 2.384   24.813  -42.574 1.00 39.19  ?  462  ILE D CD1 1 
ATOM   14479 N  N   . ALA D  1 432 ? 4.510   21.040  -38.823 1.00 40.08  ?  463  ALA D N   1 
ATOM   14480 C  CA  . ALA D  1 432 ? 4.309   20.193  -37.649 1.00 39.95  ?  463  ALA D CA  1 
ATOM   14481 C  C   . ALA D  1 432 ? 5.434   20.379  -36.639 1.00 39.41  ?  463  ALA D C   1 
ATOM   14482 O  O   . ALA D  1 432 ? 5.188   20.512  -35.434 1.00 37.63  ?  463  ALA D O   1 
ATOM   14483 C  CB  . ALA D  1 432 ? 4.199   18.723  -38.072 1.00 40.68  ?  463  ALA D CB  1 
ATOM   14484 N  N   . LYS D  1 433 ? 6.681   20.378  -37.108 1.00 39.22  ?  464  LYS D N   1 
ATOM   14485 C  CA  . LYS D  1 433 ? 7.792   20.623  -36.192 1.00 41.06  ?  464  LYS D CA  1 
ATOM   14486 C  C   . LYS D  1 433 ? 7.670   21.996  -35.543 1.00 37.88  ?  464  LYS D C   1 
ATOM   14487 O  O   . LYS D  1 433 ? 7.898   22.145  -34.334 1.00 37.38  ?  464  LYS D O   1 
ATOM   14488 C  CB  . LYS D  1 433 ? 9.130   20.491  -36.920 1.00 40.55  ?  464  LYS D CB  1 
ATOM   14489 C  CG  . LYS D  1 433 ? 9.361   19.129  -37.541 1.00 47.80  ?  464  LYS D CG  1 
ATOM   14490 C  CD  . LYS D  1 433 ? 10.786  18.969  -38.078 1.00 49.51  ?  464  LYS D CD  1 
ATOM   14491 C  CE  . LYS D  1 433 ? 11.816  19.481  -37.099 1.00 55.21  ?  464  LYS D CE  1 
ATOM   14492 N  NZ  . LYS D  1 433 ? 12.056  18.498  -35.991 1.00 57.73  ?  464  LYS D NZ  1 
ATOM   14493 N  N   . THR D  1 434 ? 7.284   23.005  -36.326 1.00 37.79  ?  465  THR D N   1 
ATOM   14494 C  CA  . THR D  1 434 ? 7.194   24.360  -35.800 1.00 36.92  ?  465  THR D CA  1 
ATOM   14495 C  C   . THR D  1 434 ? 6.059   24.483  -34.791 1.00 38.85  ?  465  THR D C   1 
ATOM   14496 O  O   . THR D  1 434 ? 6.182   25.197  -33.792 1.00 39.24  ?  465  THR D O   1 
ATOM   14497 C  CB  . THR D  1 434 ? 7.015   25.350  -36.955 1.00 33.07  ?  465  THR D CB  1 
ATOM   14498 O  OG1 . THR D  1 434 ? 8.042   25.126  -37.938 1.00 34.76  ?  465  THR D OG1 1 
ATOM   14499 C  CG2 . THR D  1 434 ? 7.079   26.807  -36.448 1.00 31.66  ?  465  THR D CG2 1 
ATOM   14500 N  N   . GLN D  1 435 ? 4.936   23.807  -35.040 1.00 37.70  ?  466  GLN D N   1 
ATOM   14501 C  CA  . GLN D  1 435 ? 3.872   23.801  -34.044 1.00 38.11  ?  466  GLN D CA  1 
ATOM   14502 C  C   . GLN D  1 435 ? 4.333   23.147  -32.745 1.00 36.72  ?  466  GLN D C   1 
ATOM   14503 O  O   . GLN D  1 435 ? 3.991   23.609  -31.649 1.00 37.79  ?  466  GLN D O   1 
ATOM   14504 C  CB  . GLN D  1 435 ? 2.642   23.078  -34.586 1.00 37.70  ?  466  GLN D CB  1 
ATOM   14505 C  CG  . GLN D  1 435 ? 1.521   23.032  -33.575 1.00 40.02  ?  466  GLN D CG  1 
ATOM   14506 C  CD  . GLN D  1 435 ? 0.180   22.877  -34.231 1.00 41.56  ?  466  GLN D CD  1 
ATOM   14507 O  OE1 . GLN D  1 435 ? 0.075   22.260  -35.288 1.00 42.34  ?  466  GLN D OE1 1 
ATOM   14508 N  NE2 . GLN D  1 435 ? -0.856  23.448  -33.619 1.00 41.52  ?  466  GLN D NE2 1 
ATOM   14509 N  N   . GLU D  1 436 ? 5.100   22.059  -32.849 1.00 39.21  ?  467  GLU D N   1 
ATOM   14510 C  CA  . GLU D  1 436 ? 5.566   21.375  -31.651 1.00 42.90  ?  467  GLU D CA  1 
ATOM   14511 C  C   . GLU D  1 436 ? 6.543   22.238  -30.859 1.00 40.77  ?  467  GLU D C   1 
ATOM   14512 O  O   . GLU D  1 436 ? 6.579   22.166  -29.625 1.00 44.75  ?  467  GLU D O   1 
ATOM   14513 C  CB  . GLU D  1 436 ? 6.183   20.031  -32.034 1.00 44.15  ?  467  GLU D CB  1 
ATOM   14514 C  CG  . GLU D  1 436 ? 6.865   19.334  -30.872 1.00 50.02  ?  467  GLU D CG  1 
ATOM   14515 C  CD  . GLU D  1 436 ? 5.993   18.288  -30.201 1.00 60.32  ?  467  GLU D CD  1 
ATOM   14516 O  OE1 . GLU D  1 436 ? 4.745   18.330  -30.369 1.00 56.48  ?  467  GLU D OE1 1 
ATOM   14517 O  OE2 . GLU D  1 436 ? 6.564   17.430  -29.490 1.00 67.97  -1 467  GLU D OE2 1 
ATOM   14518 N  N   . TRP D  1 437 ? 7.320   23.070  -31.549 1.00 36.95  ?  468  TRP D N   1 
ATOM   14519 C  CA  . TRP D  1 437 ? 8.199   24.028  -30.880 1.00 36.80  ?  468  TRP D CA  1 
ATOM   14520 C  C   . TRP D  1 437 ? 7.402   25.007  -30.024 1.00 37.28  ?  468  TRP D C   1 
ATOM   14521 O  O   . TRP D  1 437 ? 7.773   25.284  -28.872 1.00 36.43  ?  468  TRP D O   1 
ATOM   14522 C  CB  . TRP D  1 437 ? 9.028   24.761  -31.949 1.00 38.84  ?  468  TRP D CB  1 
ATOM   14523 C  CG  . TRP D  1 437 ? 9.827   25.950  -31.479 1.00 37.94  ?  468  TRP D CG  1 
ATOM   14524 C  CD1 . TRP D  1 437 ? 10.801  25.958  -30.522 1.00 35.16  ?  468  TRP D CD1 1 
ATOM   14525 C  CD2 . TRP D  1 437 ? 9.735   27.296  -31.972 1.00 32.77  ?  468  TRP D CD2 1 
ATOM   14526 N  NE1 . TRP D  1 437 ? 11.313  27.228  -30.381 1.00 35.92  ?  468  TRP D NE1 1 
ATOM   14527 C  CE2 . TRP D  1 437 ? 10.678  28.067  -31.261 1.00 35.57  ?  468  TRP D CE2 1 
ATOM   14528 C  CE3 . TRP D  1 437 ? 8.951   27.923  -32.947 1.00 33.35  ?  468  TRP D CE3 1 
ATOM   14529 C  CZ2 . TRP D  1 437 ? 10.859  29.438  -31.494 1.00 31.82  ?  468  TRP D CZ2 1 
ATOM   14530 C  CZ3 . TRP D  1 437 ? 9.122   29.288  -33.170 1.00 34.46  ?  468  TRP D CZ3 1 
ATOM   14531 C  CH2 . TRP D  1 437 ? 10.075  30.028  -32.442 1.00 33.94  ?  468  TRP D CH2 1 
ATOM   14532 N  N   . THR D  1 438 ? 6.289   25.527  -30.560 1.00 33.56  ?  469  THR D N   1 
ATOM   14533 C  CA  . THR D  1 438 ? 5.477   26.490  -29.819 1.00 34.69  ?  469  THR D CA  1 
ATOM   14534 C  C   . THR D  1 438 ? 4.841   25.869  -28.584 1.00 38.04  ?  469  THR D C   1 
ATOM   14535 O  O   . THR D  1 438 ? 4.428   26.601  -27.677 1.00 39.36  ?  469  THR D O   1 
ATOM   14536 C  CB  . THR D  1 438 ? 4.357   27.100  -30.701 1.00 38.31  ?  469  THR D CB  1 
ATOM   14537 O  OG1 . THR D  1 438 ? 3.366   26.109  -31.003 1.00 34.87  ?  469  THR D OG1 1 
ATOM   14538 C  CG2 . THR D  1 438 ? 4.899   27.713  -32.015 1.00 32.81  ?  469  THR D CG2 1 
ATOM   14539 N  N   . LYS D  1 439 ? 4.755   24.542  -28.522 1.00 39.73  ?  470  LYS D N   1 
ATOM   14540 C  CA  . LYS D  1 439 ? 4.151   23.915  -27.353 1.00 42.43  ?  470  LYS D CA  1 
ATOM   14541 C  C   . LYS D  1 439 ? 4.998   24.109  -26.108 1.00 41.15  ?  470  LYS D C   1 
ATOM   14542 O  O   . LYS D  1 439 ? 4.460   24.063  -25.001 1.00 45.88  ?  470  LYS D O   1 
ATOM   14543 C  CB  . LYS D  1 439 ? 3.891   22.427  -27.636 1.00 42.32  ?  470  LYS D CB  1 
ATOM   14544 C  CG  . LYS D  1 439 ? 2.776   22.242  -28.668 1.00 43.36  ?  470  LYS D CG  1 
ATOM   14545 C  CD  . LYS D  1 439 ? 2.151   20.864  -28.663 1.00 51.18  ?  470  LYS D CD  1 
ATOM   14546 C  CE  . LYS D  1 439 ? 1.037   20.768  -29.721 1.00 52.55  ?  470  LYS D CE  1 
ATOM   14547 N  NZ  . LYS D  1 439 ? 1.397   19.898  -30.887 1.00 58.07  ?  470  LYS D NZ  1 
ATOM   14548 N  N   . SER D  1 440 ? 6.295   24.375  -26.271 1.00 40.06  ?  471  SER D N   1 
ATOM   14549 C  CA  . SER D  1 440 ? 7.202   24.630  -25.164 1.00 35.11  ?  471  SER D CA  1 
ATOM   14550 C  C   . SER D  1 440 ? 7.196   26.081  -24.691 1.00 42.52  ?  471  SER D C   1 
ATOM   14551 O  O   . SER D  1 440 ? 7.995   26.425  -23.809 1.00 47.65  ?  471  SER D O   1 
ATOM   14552 C  CB  . SER D  1 440 ? 8.627   24.239  -25.567 1.00 41.01  ?  471  SER D CB  1 
ATOM   14553 O  OG  . SER D  1 440 ? 9.155   25.132  -26.551 1.00 40.20  ?  471  SER D OG  1 
ATOM   14554 N  N   . PHE D  1 441 ? 6.334   26.933  -25.237 1.00 37.37  ?  472  PHE D N   1 
ATOM   14555 C  CA  . PHE D  1 441 ? 6.431   28.370  -25.012 1.00 40.01  ?  472  PHE D CA  1 
ATOM   14556 C  C   . PHE D  1 441 ? 5.844   28.755  -23.656 1.00 43.87  ?  472  PHE D C   1 
ATOM   14557 O  O   . PHE D  1 441 ? 4.862   28.167  -23.196 1.00 41.25  ?  472  PHE D O   1 
ATOM   14558 C  CB  . PHE D  1 441 ? 5.695   29.142  -26.117 1.00 34.27  ?  472  PHE D CB  1 
ATOM   14559 C  CG  . PHE D  1 441 ? 6.454   29.235  -27.417 1.00 33.99  ?  472  PHE D CG  1 
ATOM   14560 C  CD1 . PHE D  1 441 ? 7.606   28.496  -27.623 1.00 34.21  ?  472  PHE D CD1 1 
ATOM   14561 C  CD2 . PHE D  1 441 ? 6.008   30.074  -28.437 1.00 37.19  ?  472  PHE D CD2 1 
ATOM   14562 C  CE1 . PHE D  1 441 ? 8.304   28.580  -28.816 1.00 32.83  ?  472  PHE D CE1 1 
ATOM   14563 C  CE2 . PHE D  1 441 ? 6.704   30.157  -29.638 1.00 33.97  ?  472  PHE D CE2 1 
ATOM   14564 C  CZ  . PHE D  1 441 ? 7.860   29.407  -29.818 1.00 31.07  ?  472  PHE D CZ  1 
ATOM   14565 N  N   . VAL D  1 442 ? 6.440   29.760  -23.022 1.00 40.64  ?  473  VAL D N   1 
ATOM   14566 C  CA  . VAL D  1 442 ? 5.866   30.351  -21.817 1.00 42.73  ?  473  VAL D CA  1 
ATOM   14567 C  C   . VAL D  1 442 ? 5.031   31.571  -22.193 1.00 43.55  ?  473  VAL D C   1 
ATOM   14568 O  O   . VAL D  1 442 ? 5.022   32.028  -23.336 1.00 40.18  ?  473  VAL D O   1 
ATOM   14569 C  CB  . VAL D  1 442 ? 6.946   30.727  -20.763 1.00 40.70  ?  473  VAL D CB  1 
ATOM   14570 C  CG1 . VAL D  1 442 ? 7.780   29.502  -20.337 1.00 42.25  ?  473  VAL D CG1 1 
ATOM   14571 C  CG2 . VAL D  1 442 ? 7.831   31.866  -21.276 1.00 37.50  ?  473  VAL D CG2 1 
ATOM   14572 N  N   . LYS D  1 443 ? 4.319   32.101  -21.225 1.00 42.23  ?  474  LYS D N   1 
ATOM   14573 C  CA  . LYS D  1 443 ? 3.579   33.321  -21.463 1.00 40.25  ?  474  LYS D CA  1 
ATOM   14574 C  C   . LYS D  1 443 ? 4.527   34.511  -21.366 1.00 42.08  ?  474  LYS D C   1 
ATOM   14575 O  O   . LYS D  1 443 ? 5.517   34.468  -20.636 1.00 39.20  ?  474  LYS D O   1 
ATOM   14576 C  CB  . LYS D  1 443 ? 2.446   33.466  -20.447 1.00 45.71  ?  474  LYS D CB  1 
ATOM   14577 N  N   . PRO D  1 444 ? 4.264   35.575  -22.113 1.00 38.17  ?  475  PRO D N   1 
ATOM   14578 C  CA  . PRO D  1 444 ? 5.103   36.767  -21.991 1.00 38.58  ?  475  PRO D CA  1 
ATOM   14579 C  C   . PRO D  1 444 ? 4.968   37.364  -20.600 1.00 39.75  ?  475  PRO D C   1 
ATOM   14580 O  O   . PRO D  1 444 ? 3.867   37.462  -20.054 1.00 39.20  ?  475  PRO D O   1 
ATOM   14581 C  CB  . PRO D  1 444 ? 4.540   37.705  -23.065 1.00 35.91  ?  475  PRO D CB  1 
ATOM   14582 C  CG  . PRO D  1 444 ? 3.800   36.791  -23.997 1.00 42.40  ?  475  PRO D CG  1 
ATOM   14583 C  CD  . PRO D  1 444 ? 3.216   35.746  -23.123 1.00 35.98  ?  475  PRO D CD  1 
ATOM   14584 N  N   . LEU D  1 445 ? 6.108   37.745  -20.023 1.00 35.32  ?  476  LEU D N   1 
ATOM   14585 C  CA  . LEU D  1 445 ? 6.092   38.462  -18.753 1.00 36.75  ?  476  LEU D CA  1 
ATOM   14586 C  C   . LEU D  1 445 ? 5.457   39.837  -18.892 1.00 39.64  ?  476  LEU D C   1 
ATOM   14587 O  O   . LEU D  1 445 ? 4.820   40.320  -17.949 1.00 42.94  ?  476  LEU D O   1 
ATOM   14588 C  CB  . LEU D  1 445 ? 7.518   38.596  -18.207 1.00 36.84  ?  476  LEU D CB  1 
ATOM   14589 C  CG  . LEU D  1 445 ? 8.140   37.253  -17.850 1.00 34.28  ?  476  LEU D CG  1 
ATOM   14590 C  CD1 . LEU D  1 445 ? 9.603   37.393  -17.585 1.00 35.30  ?  476  LEU D CD1 1 
ATOM   14591 C  CD2 . LEU D  1 445 ? 7.401   36.672  -16.654 1.00 35.60  ?  476  LEU D CD2 1 
ATOM   14592 N  N   . TRP D  1 446 ? 5.656   40.497  -20.033 1.00 34.39  ?  477  TRP D N   1 
ATOM   14593 C  CA  . TRP D  1 446 ? 5.004   41.760  -20.344 1.00 36.98  ?  477  TRP D CA  1 
ATOM   14594 C  C   . TRP D  1 446 ? 4.633   41.740  -21.821 1.00 35.08  ?  477  TRP D C   1 
ATOM   14595 O  O   . TRP D  1 446 ? 5.157   40.934  -22.594 1.00 34.70  ?  477  TRP D O   1 
ATOM   14596 C  CB  . TRP D  1 446 ? 5.903   42.969  -20.038 1.00 37.04  ?  477  TRP D CB  1 
ATOM   14597 C  CG  . TRP D  1 446 ? 7.227   42.868  -20.731 1.00 37.79  ?  477  TRP D CG  1 
ATOM   14598 C  CD1 . TRP D  1 446 ? 7.503   43.220  -22.020 1.00 33.27  ?  477  TRP D CD1 1 
ATOM   14599 C  CD2 . TRP D  1 446 ? 8.451   42.354  -20.184 1.00 36.17  ?  477  TRP D CD2 1 
ATOM   14600 N  NE1 . TRP D  1 446 ? 8.814   42.953  -22.314 1.00 33.55  ?  477  TRP D NE1 1 
ATOM   14601 C  CE2 . TRP D  1 446 ? 9.425   42.429  -21.204 1.00 34.63  ?  477  TRP D CE2 1 
ATOM   14602 C  CE3 . TRP D  1 446 ? 8.819   41.847  -18.930 1.00 36.83  ?  477  TRP D CE3 1 
ATOM   14603 C  CZ2 . TRP D  1 446 ? 10.750  42.014  -21.011 1.00 33.78  ?  477  TRP D CZ2 1 
ATOM   14604 C  CZ3 . TRP D  1 446 ? 10.125  41.427  -18.741 1.00 35.98  ?  477  TRP D CZ3 1 
ATOM   14605 C  CH2 . TRP D  1 446 ? 11.080  41.517  -19.779 1.00 39.27  ?  477  TRP D CH2 1 
ATOM   14606 N  N   . VAL D  1 447 ? 3.722   42.631  -22.205 1.00 34.45  ?  478  VAL D N   1 
ATOM   14607 C  CA  . VAL D  1 447 ? 3.400   42.843  -23.614 1.00 33.87  ?  478  VAL D CA  1 
ATOM   14608 C  C   . VAL D  1 447 ? 3.728   44.295  -23.937 1.00 32.80  ?  478  VAL D C   1 
ATOM   14609 O  O   . VAL D  1 447 ? 4.317   44.998  -23.109 1.00 33.75  ?  478  VAL D O   1 
ATOM   14610 C  CB  . VAL D  1 447 ? 1.939   42.474  -23.932 1.00 35.16  ?  478  VAL D CB  1 
ATOM   14611 C  CG1 . VAL D  1 447 ? 1.693   41.010  -23.561 1.00 37.77  ?  478  VAL D CG1 1 
ATOM   14612 C  CG2 . VAL D  1 447 ? 0.944   43.405  -23.225 1.00 32.77  ?  478  VAL D CG2 1 
ATOM   14613 N  N   . TYR D  1 448 ? 3.397   44.754  -25.139 1.00 31.62  ?  479  TYR D N   1 
ATOM   14614 C  CA  . TYR D  1 448 ? 3.832   46.089  -25.528 1.00 34.02  ?  479  TYR D CA  1 
ATOM   14615 C  C   . TYR D  1 448 ? 2.725   47.130  -25.503 1.00 32.60  ?  479  TYR D C   1 
ATOM   14616 O  O   . TYR D  1 448 ? 2.951   48.239  -25.030 1.00 31.78  ?  479  TYR D O   1 
ATOM   14617 C  CB  . TYR D  1 448 ? 4.479   46.067  -26.917 1.00 33.29  ?  479  TYR D CB  1 
ATOM   14618 C  CG  . TYR D  1 448 ? 5.329   47.298  -27.202 1.00 33.35  ?  479  TYR D CG  1 
ATOM   14619 C  CD1 . TYR D  1 448 ? 6.575   47.476  -26.590 1.00 34.97  ?  479  TYR D CD1 1 
ATOM   14620 C  CD2 . TYR D  1 448 ? 4.891   48.272  -28.092 1.00 33.96  ?  479  TYR D CD2 1 
ATOM   14621 C  CE1 . TYR D  1 448 ? 7.352   48.616  -26.853 1.00 33.99  ?  479  TYR D CE1 1 
ATOM   14622 C  CE2 . TYR D  1 448 ? 5.650   49.396  -28.363 1.00 33.93  ?  479  TYR D CE2 1 
ATOM   14623 C  CZ  . TYR D  1 448 ? 6.877   49.566  -27.748 1.00 38.64  ?  479  TYR D CZ  1 
ATOM   14624 O  OH  . TYR D  1 448 ? 7.613   50.695  -28.044 1.00 37.60  ?  479  TYR D OH  1 
ATOM   14625 N  N   . SER D  1 449 ? 1.543   46.825  -26.024 1.00 34.46  ?  480  SER D N   1 
ATOM   14626 C  CA  . SER D  1 449 ? 0.466   47.794  -26.090 1.00 34.46  ?  480  SER D CA  1 
ATOM   14627 C  C   . SER D  1 449 ? -0.749  47.290  -25.325 1.00 35.59  ?  480  SER D C   1 
ATOM   14628 O  O   . SER D  1 449 ? -0.862  46.109  -24.987 1.00 32.91  ?  480  SER D O   1 
ATOM   14629 C  CB  . SER D  1 449 ? 0.077   48.088  -27.546 1.00 35.18  ?  480  SER D CB  1 
ATOM   14630 O  OG  . SER D  1 449 ? -0.484  46.933  -28.137 1.00 36.92  ?  480  SER D OG  1 
ATOM   14631 N  N   . VAL D  1 450 ? -1.668  48.226  -25.072 1.00 35.94  ?  481  VAL D N   1 
ATOM   14632 C  CA  . VAL D  1 450 ? -2.960  47.892  -24.481 1.00 37.00  ?  481  VAL D CA  1 
ATOM   14633 C  C   . VAL D  1 450 ? -3.693  46.868  -25.341 1.00 36.45  ?  481  VAL D C   1 
ATOM   14634 O  O   . VAL D  1 450 ? -4.309  45.927  -24.819 1.00 36.92  ?  481  VAL D O   1 
ATOM   14635 C  CB  . VAL D  1 450 ? -3.786  49.179  -24.282 1.00 41.57  ?  481  VAL D CB  1 
ATOM   14636 C  CG1 . VAL D  1 450 ? -5.230  48.864  -23.887 1.00 34.12  ?  481  VAL D CG1 1 
ATOM   14637 C  CG2 . VAL D  1 450 ? -3.105  50.072  -23.222 1.00 34.30  ?  481  VAL D CG2 1 
ATOM   14638 N  N   . LYS D  1 451 ? -3.634  47.029  -26.669 1.00 34.59  ?  482  LYS D N   1 
ATOM   14639 C  CA  . LYS D  1 451 ? -4.234  46.046  -27.571 1.00 37.68  ?  482  LYS D CA  1 
ATOM   14640 C  C   . LYS D  1 451 ? -3.701  44.649  -27.289 1.00 39.16  ?  482  LYS D C   1 
ATOM   14641 O  O   . LYS D  1 451 ? -4.476  43.699  -27.121 1.00 38.85  ?  482  LYS D O   1 
ATOM   14642 C  CB  . LYS D  1 451 ? -3.978  46.442  -29.028 1.00 39.39  ?  482  LYS D CB  1 
ATOM   14643 C  CG  . LYS D  1 451 ? -4.607  45.505  -30.046 1.00 38.95  ?  482  LYS D CG  1 
ATOM   14644 C  CD  . LYS D  1 451 ? -6.142  45.452  -29.880 1.00 38.79  ?  482  LYS D CD  1 
ATOM   14645 C  CE  . LYS D  1 451 ? -6.811  44.696  -31.026 1.00 40.75  ?  482  LYS D CE  1 
ATOM   14646 N  NZ  . LYS D  1 451 ? -8.279  44.967  -31.090 1.00 38.89  ?  482  LYS D NZ  1 
ATOM   14647 N  N   . ASP D  1 452 ? -2.371  44.511  -27.213 1.00 35.72  ?  483  ASP D N   1 
ATOM   14648 C  CA  . ASP D  1 452 ? -1.766  43.242  -26.821 1.00 34.44  ?  483  ASP D CA  1 
ATOM   14649 C  C   . ASP D  1 452 ? -2.412  42.684  -25.563 1.00 39.20  ?  483  ASP D C   1 
ATOM   14650 O  O   . ASP D  1 452 ? -2.731  41.491  -25.484 1.00 38.37  ?  483  ASP D O   1 
ATOM   14651 C  CB  . ASP D  1 452 ? -0.265  43.408  -26.547 1.00 34.15  ?  483  ASP D CB  1 
ATOM   14652 C  CG  . ASP D  1 452 ? 0.556   43.720  -27.788 1.00 35.60  ?  483  ASP D CG  1 
ATOM   14653 O  OD1 . ASP D  1 452 ? 0.095   43.417  -28.901 1.00 35.31  ?  483  ASP D OD1 1 
ATOM   14654 O  OD2 . ASP D  1 452 ? 1.701   44.229  -27.616 1.00 34.84  -1 483  ASP D OD2 1 
ATOM   14655 N  N   . LYS D  1 453 ? -2.548  43.529  -24.539 1.00 37.38  ?  484  LYS D N   1 
ATOM   14656 C  CA  . LYS D  1 453 ? -3.035  43.050  -23.251 1.00 41.97  ?  484  LYS D CA  1 
ATOM   14657 C  C   . LYS D  1 453 ? -4.455  42.508  -23.383 1.00 40.25  ?  484  LYS D C   1 
ATOM   14658 O  O   . LYS D  1 453 ? -4.746  41.384  -22.954 1.00 38.55  ?  484  LYS D O   1 
ATOM   14659 C  CB  . LYS D  1 453 ? -2.961  44.176  -22.214 1.00 41.55  ?  484  LYS D CB  1 
ATOM   14660 C  CG  . LYS D  1 453 ? -3.317  43.758  -20.802 1.00 45.57  ?  484  LYS D CG  1 
ATOM   14661 C  CD  . LYS D  1 453 ? -3.729  44.961  -19.965 1.00 52.26  ?  484  LYS D CD  1 
ATOM   14662 C  CE  . LYS D  1 453 ? -3.744  44.624  -18.476 1.00 54.58  ?  484  LYS D CE  1 
ATOM   14663 N  NZ  . LYS D  1 453 ? -5.131  44.614  -17.915 1.00 60.36  ?  484  LYS D NZ  1 
ATOM   14664 N  N   . GLU D  1 454 ? -5.340  43.279  -24.017 1.00 36.88  ?  485  GLU D N   1 
ATOM   14665 C  CA  . GLU D  1 454 ? -6.704  42.800  -24.246 1.00 39.54  ?  485  GLU D CA  1 
ATOM   14666 C  C   . GLU D  1 454 ? -6.720  41.491  -25.026 1.00 43.33  ?  485  GLU D C   1 
ATOM   14667 O  O   . GLU D  1 454 ? -7.514  40.590  -24.723 1.00 44.33  ?  485  GLU D O   1 
ATOM   14668 C  CB  . GLU D  1 454 ? -7.516  43.854  -24.989 1.00 39.77  ?  485  GLU D CB  1 
ATOM   14669 C  CG  . GLU D  1 454 ? -7.619  45.172  -24.253 1.00 42.75  ?  485  GLU D CG  1 
ATOM   14670 C  CD  . GLU D  1 454 ? -8.375  46.210  -25.054 1.00 43.06  ?  485  GLU D CD  1 
ATOM   14671 O  OE1 . GLU D  1 454 ? -8.846  45.887  -26.167 1.00 46.97  ?  485  GLU D OE1 1 
ATOM   14672 O  OE2 . GLU D  1 454 ? -8.498  47.356  -24.577 1.00 45.84  -1 485  GLU D OE2 1 
ATOM   14673 N  N   . LEU D  1 455 ? -5.864  41.370  -26.046 1.00 38.33  ?  486  LEU D N   1 
ATOM   14674 C  CA  . LEU D  1 455 ? -5.855  40.152  -26.849 1.00 36.81  ?  486  LEU D CA  1 
ATOM   14675 C  C   . LEU D  1 455 ? -5.408  38.955  -26.023 1.00 40.88  ?  486  LEU D C   1 
ATOM   14676 O  O   . LEU D  1 455 ? -6.021  37.883  -26.093 1.00 41.30  ?  486  LEU D O   1 
ATOM   14677 C  CB  . LEU D  1 455 ? -4.959  40.331  -28.078 1.00 41.08  ?  486  LEU D CB  1 
ATOM   14678 C  CG  . LEU D  1 455 ? -5.443  41.259  -29.209 1.00 39.60  ?  486  LEU D CG  1 
ATOM   14679 C  CD1 . LEU D  1 455 ? -4.363  41.413  -30.267 1.00 39.12  ?  486  LEU D CD1 1 
ATOM   14680 C  CD2 . LEU D  1 455 ? -6.742  40.780  -29.857 1.00 43.18  ?  486  LEU D CD2 1 
ATOM   14681 N  N   . TRP D  1 456 ? -4.355  39.119  -25.215 1.00 39.83  ?  487  TRP D N   1 
ATOM   14682 C  CA  . TRP D  1 456 ? -3.864  37.990  -24.430 1.00 42.40  ?  487  TRP D CA  1 
ATOM   14683 C  C   . TRP D  1 456 ? -4.844  37.609  -23.313 1.00 43.26  ?  487  TRP D C   1 
ATOM   14684 O  O   . TRP D  1 456 ? -5.009  36.417  -23.017 1.00 42.88  ?  487  TRP D O   1 
ATOM   14685 C  CB  . TRP D  1 456 ? -2.468  38.299  -23.867 1.00 36.19  ?  487  TRP D CB  1 
ATOM   14686 C  CG  . TRP D  1 456 ? -1.335  38.079  -24.881 1.00 35.59  ?  487  TRP D CG  1 
ATOM   14687 C  CD1 . TRP D  1 456 ? -0.884  38.980  -25.814 1.00 34.72  ?  487  TRP D CD1 1 
ATOM   14688 C  CD2 . TRP D  1 456 ? -0.551  36.888  -25.070 1.00 35.30  ?  487  TRP D CD2 1 
ATOM   14689 N  NE1 . TRP D  1 456 ? 0.134   38.431  -26.556 1.00 34.47  ?  487  TRP D NE1 1 
ATOM   14690 C  CE2 . TRP D  1 456 ? 0.360   37.149  -26.125 1.00 35.94  ?  487  TRP D CE2 1 
ATOM   14691 C  CE3 . TRP D  1 456 ? -0.511  35.637  -24.434 1.00 39.59  ?  487  TRP D CE3 1 
ATOM   14692 C  CZ2 . TRP D  1 456 ? 1.280   36.200  -26.577 1.00 33.62  ?  487  TRP D CZ2 1 
ATOM   14693 C  CZ3 . TRP D  1 456 ? 0.414   34.687  -24.878 1.00 35.19  ?  487  TRP D CZ3 1 
ATOM   14694 C  CH2 . TRP D  1 456 ? 1.308   34.982  -25.937 1.00 37.51  ?  487  TRP D CH2 1 
ATOM   14695 N  N   . GLU D  1 457 ? -5.516  38.589  -22.703 1.00 39.66  ?  488  GLU D N   1 
ATOM   14696 C  CA  . GLU D  1 457 ? -6.449  38.279  -21.618 1.00 44.44  ?  488  GLU D CA  1 
ATOM   14697 C  C   . GLU D  1 457 ? -7.695  37.563  -22.131 1.00 46.88  ?  488  GLU D C   1 
ATOM   14698 O  O   . GLU D  1 457 ? -8.174  36.616  -21.500 1.00 53.77  ?  488  GLU D O   1 
ATOM   14699 C  CB  . GLU D  1 457 ? -6.839  39.557  -20.871 1.00 46.14  ?  488  GLU D CB  1 
ATOM   14700 C  CG  . GLU D  1 457 ? -5.835  40.002  -19.803 1.00 50.18  ?  488  GLU D CG  1 
ATOM   14701 C  CD  . GLU D  1 457 ? -6.201  41.346  -19.180 1.00 54.70  ?  488  GLU D CD  1 
ATOM   14702 O  OE1 . GLU D  1 457 ? -7.146  42.006  -19.679 1.00 57.08  ?  488  GLU D OE1 1 
ATOM   14703 O  OE2 . GLU D  1 457 ? -5.538  41.742  -18.201 1.00 52.32  -1 488  GLU D OE2 1 
ATOM   14704 N  N   . SER D  1 458 ? -8.236  38.001  -23.267 1.00 45.92  ?  489  SER D N   1 
ATOM   14705 C  CA  . SER D  1 458 ? -9.398  37.337  -23.858 1.00 48.41  ?  489  SER D CA  1 
ATOM   14706 C  C   . SER D  1 458 ? -9.062  36.015  -24.532 1.00 45.67  ?  489  SER D C   1 
ATOM   14707 O  O   . SER D  1 458 ? -9.981  35.287  -24.921 1.00 44.77  ?  489  SER D O   1 
ATOM   14708 C  CB  . SER D  1 458 ? -10.058 38.244  -24.890 1.00 46.57  ?  489  SER D CB  1 
ATOM   14709 O  OG  . SER D  1 458 ? -9.316  38.224  -26.096 1.00 49.20  ?  489  SER D OG  1 
ATOM   14710 N  N   . GLY D  1 459 ? -7.785  35.693  -24.698 1.00 45.59  ?  490  GLY D N   1 
ATOM   14711 C  CA  . GLY D  1 459 ? -7.390  34.481  -25.380 1.00 39.86  ?  490  GLY D CA  1 
ATOM   14712 C  C   . GLY D  1 459 ? -7.405  34.563  -26.890 1.00 44.65  ?  490  GLY D C   1 
ATOM   14713 O  O   . GLY D  1 459 ? -7.143  33.543  -27.545 1.00 42.80  ?  490  GLY D O   1 
ATOM   14714 N  N   . GLN D  1 460 ? -7.715  35.736  -27.464 1.00 43.08  ?  491  GLN D N   1 
ATOM   14715 C  CA  . GLN D  1 460 ? -7.550  35.935  -28.902 1.00 38.90  ?  491  GLN D CA  1 
ATOM   14716 C  C   . GLN D  1 460 ? -6.113  35.655  -29.329 1.00 42.26  ?  491  GLN D C   1 
ATOM   14717 O  O   . GLN D  1 460 ? -5.870  35.151  -30.430 1.00 40.81  ?  491  GLN D O   1 
ATOM   14718 C  CB  . GLN D  1 460 ? -7.946  37.368  -29.286 1.00 42.01  ?  491  GLN D CB  1 
ATOM   14719 C  CG  . GLN D  1 460 ? -9.433  37.594  -29.563 1.00 49.01  ?  491  GLN D CG  1 
ATOM   14720 C  CD  . GLN D  1 460 ? -9.910  39.025  -29.250 1.00 52.40  ?  491  GLN D CD  1 
ATOM   14721 O  OE1 . GLN D  1 460 ? -9.728  39.530  -28.133 1.00 53.25  ?  491  GLN D OE1 1 
ATOM   14722 N  NE2 . GLN D  1 460 ? -10.538 39.674  -30.237 1.00 57.58  ?  491  GLN D NE2 1 
ATOM   14723 N  N   . MET D  1 461 ? -5.173  36.041  -28.465 1.00 36.72  ?  492  MET D N   1 
ATOM   14724 C  CA  . MET D  1 461 ? -3.725  35.812  -28.702 1.00 41.78  ?  492  MET D CA  1 
ATOM   14725 C  C   . MET D  1 461 ? -3.263  34.847  -27.607 1.00 38.60  ?  492  MET D C   1 
ATOM   14726 O  O   . MET D  1 461 ? -3.806  35.006  -26.481 1.00 41.84  ?  492  MET D O   1 
ATOM   14727 C  CB  . MET D  1 461 ? -2.933  37.117  -28.585 1.00 36.89  ?  492  MET D CB  1 
ATOM   14728 C  CG  . MET D  1 461 ? -2.986  38.007  -29.802 1.00 42.54  ?  492  MET D CG  1 
ATOM   14729 S  SD  . MET D  1 461 ? -2.156  37.305  -31.239 1.00 36.98  ?  492  MET D SD  1 
ATOM   14730 C  CE  . MET D  1 461 ? -0.452  37.417  -30.682 1.00 34.32  ?  492  MET D CE  1 
ATOM   14731 N  N   . PRO D  1 462 ? -2.354  33.863  -27.839 1.00 37.62  ?  493  PRO D N   1 
ATOM   14732 C  CA  . PRO D  1 462 ? -1.543  33.704  -29.047 1.00 38.59  ?  493  PRO D CA  1 
ATOM   14733 C  C   . PRO D  1 462 ? -2.208  32.833  -30.116 1.00 41.08  ?  493  PRO D C   1 
ATOM   14734 O  O   . PRO D  1 462 ? -1.835  32.915  -31.290 1.00 37.95  ?  493  PRO D O   1 
ATOM   14735 C  CB  . PRO D  1 462 ? -0.265  33.059  -28.495 1.00 35.70  ?  493  PRO D CB  1 
ATOM   14736 C  CG  . PRO D  1 462 ? -0.768  32.164  -27.409 1.00 39.31  ?  493  PRO D CG  1 
ATOM   14737 C  CD  . PRO D  1 462 ? -1.996  32.852  -26.825 1.00 38.53  ?  493  PRO D CD  1 
ATOM   14738 N  N   . ASN D  1 463 ? -3.177  31.995  -29.740 1.00 37.38  ?  494  ASN D N   1 
ATOM   14739 C  CA  . ASN D  1 463 ? -3.904  31.129  -30.669 1.00 36.56  ?  494  ASN D CA  1 
ATOM   14740 C  C   . ASN D  1 463 ? -2.953  30.442  -31.659 1.00 37.18  ?  494  ASN D C   1 
ATOM   14741 O  O   . ASN D  1 463 ? -3.067  30.587  -32.875 1.00 33.95  ?  494  ASN D O   1 
ATOM   14742 C  CB  . ASN D  1 463 ? -4.988  31.925  -31.402 1.00 37.37  ?  494  ASN D CB  1 
ATOM   14743 C  CG  . ASN D  1 463 ? -6.000  31.022  -32.095 1.00 40.52  ?  494  ASN D CG  1 
ATOM   14744 O  OD1 . ASN D  1 463 ? -5.815  29.807  -32.148 1.00 42.18  ?  494  ASN D OD1 1 
ATOM   14745 N  ND2 . ASN D  1 463 ? -7.067  31.613  -32.639 1.00 43.29  ?  494  ASN D ND2 1 
ATOM   14746 N  N   . TYR D  1 464 ? -1.980  29.705  -31.108 1.00 35.95  ?  495  TYR D N   1 
ATOM   14747 C  CA  . TYR D  1 464 ? -1.035  28.993  -31.963 1.00 36.26  ?  495  TYR D CA  1 
ATOM   14748 C  C   . TYR D  1 464 ? -1.754  28.008  -32.880 1.00 38.18  ?  495  TYR D C   1 
ATOM   14749 O  O   . TYR D  1 464 ? -1.287  27.734  -33.993 1.00 35.52  ?  495  TYR D O   1 
ATOM   14750 C  CB  . TYR D  1 464 ? 0.021   28.274  -31.113 1.00 34.38  ?  495  TYR D CB  1 
ATOM   14751 C  CG  . TYR D  1 464 ? 0.867   29.194  -30.244 1.00 40.22  ?  495  TYR D CG  1 
ATOM   14752 C  CD1 . TYR D  1 464 ? 1.623   30.224  -30.806 1.00 39.48  ?  495  TYR D CD1 1 
ATOM   14753 C  CD2 . TYR D  1 464 ? 0.909   29.033  -28.868 1.00 40.88  ?  495  TYR D CD2 1 
ATOM   14754 C  CE1 . TYR D  1 464 ? 2.400   31.070  -30.012 1.00 34.79  ?  495  TYR D CE1 1 
ATOM   14755 C  CE2 . TYR D  1 464 ? 1.684   29.872  -28.064 1.00 41.44  ?  495  TYR D CE2 1 
ATOM   14756 C  CZ  . TYR D  1 464 ? 2.425   30.895  -28.645 1.00 36.77  ?  495  TYR D CZ  1 
ATOM   14757 O  OH  . TYR D  1 464 ? 3.190   31.735  -27.846 1.00 35.89  ?  495  TYR D OH  1 
ATOM   14758 N  N   . GLU D  1 465 ? -2.896  27.479  -32.442 1.00 39.05  ?  496  GLU D N   1 
ATOM   14759 C  CA  . GLU D  1 465 ? -3.616  26.522  -33.277 1.00 40.79  ?  496  GLU D CA  1 
ATOM   14760 C  C   . GLU D  1 465 ? -4.052  27.152  -34.601 1.00 36.15  ?  496  GLU D C   1 
ATOM   14761 O  O   . GLU D  1 465 ? -3.920  26.536  -35.667 1.00 35.81  ?  496  GLU D O   1 
ATOM   14762 C  CB  . GLU D  1 465 ? -4.801  25.945  -32.495 1.00 41.50  ?  496  GLU D CB  1 
ATOM   14763 C  CG  . GLU D  1 465 ? -4.353  25.168  -31.230 1.00 51.38  ?  496  GLU D CG  1 
ATOM   14764 C  CD  . GLU D  1 465 ? -4.216  26.033  -29.951 1.00 53.27  ?  496  GLU D CD  1 
ATOM   14765 O  OE1 . GLU D  1 465 ? -4.072  27.280  -30.048 1.00 49.32  ?  496  GLU D OE1 1 
ATOM   14766 O  OE2 . GLU D  1 465 ? -4.275  25.454  -28.836 1.00 59.83  -1 496  GLU D OE2 1 
ATOM   14767 N  N   . ALA D  1 466 ? -4.562  28.382  -34.567 1.00 37.74  ?  497  ALA D N   1 
ATOM   14768 C  CA  . ALA D  1 466 ? -4.947  29.007  -35.827 1.00 34.21  ?  497  ALA D CA  1 
ATOM   14769 C  C   . ALA D  1 466 ? -3.723  29.354  -36.678 1.00 35.02  ?  497  ALA D C   1 
ATOM   14770 O  O   . ALA D  1 466 ? -3.800  29.333  -37.912 1.00 34.24  ?  497  ALA D O   1 
ATOM   14771 C  CB  . ALA D  1 466 ? -5.787  30.255  -35.561 1.00 38.25  ?  497  ALA D CB  1 
ATOM   14772 N  N   . THR D  1 467 ? -2.593  29.676  -36.040 1.00 33.06  ?  498  THR D N   1 
ATOM   14773 C  CA  . THR D  1 467 ? -1.396  30.030  -36.796 1.00 32.24  ?  498  THR D CA  1 
ATOM   14774 C  C   . THR D  1 467 ? -0.992  28.910  -37.747 1.00 32.41  ?  498  THR D C   1 
ATOM   14775 O  O   . THR D  1 467 ? -0.637  29.160  -38.909 1.00 31.95  ?  498  THR D O   1 
ATOM   14776 C  CB  . THR D  1 467 ? -0.258  30.364  -35.828 1.00 32.94  ?  498  THR D CB  1 
ATOM   14777 O  OG1 . THR D  1 467 ? -0.570  31.589  -35.155 1.00 32.31  ?  498  THR D OG1 1 
ATOM   14778 C  CG2 . THR D  1 467 ? 1.049   30.530  -36.583 1.00 32.52  ?  498  THR D CG2 1 
ATOM   14779 N  N   . PHE D  1 468 ? -1.117  27.665  -37.298 1.00 32.11  ?  499  PHE D N   1 
ATOM   14780 C  CA  . PHE D  1 468 ? -0.681  26.518  -38.075 1.00 32.99  ?  499  PHE D CA  1 
ATOM   14781 C  C   . PHE D  1 468 ? -1.813  25.855  -38.874 1.00 33.65  ?  499  PHE D C   1 
ATOM   14782 O  O   . PHE D  1 468 ? -1.656  24.712  -39.315 1.00 35.01  ?  499  PHE D O   1 
ATOM   14783 C  CB  . PHE D  1 468 ? 0.009   25.537  -37.140 1.00 30.92  ?  499  PHE D CB  1 
ATOM   14784 C  CG  . PHE D  1 468 ? 1.192   26.144  -36.442 1.00 36.59  ?  499  PHE D CG  1 
ATOM   14785 C  CD1 . PHE D  1 468 ? 2.317   26.497  -37.164 1.00 34.78  ?  499  PHE D CD1 1 
ATOM   14786 C  CD2 . PHE D  1 468 ? 1.159   26.415  -35.083 1.00 35.87  ?  499  PHE D CD2 1 
ATOM   14787 C  CE1 . PHE D  1 468 ? 3.407   27.090  -36.533 1.00 37.05  ?  499  PHE D CE1 1 
ATOM   14788 C  CE2 . PHE D  1 468 ? 2.248   27.005  -34.443 1.00 36.87  ?  499  PHE D CE2 1 
ATOM   14789 C  CZ  . PHE D  1 468 ? 3.363   27.342  -35.171 1.00 35.08  ?  499  PHE D CZ  1 
ATOM   14790 N  N   . GLU D  1 469 ? -2.940  26.543  -39.070 1.00 37.26  ?  500  GLU D N   1 
ATOM   14791 C  CA  . GLU D  1 469 ? -3.904  26.152  -40.099 1.00 31.21  ?  500  GLU D CA  1 
ATOM   14792 C  C   . GLU D  1 469 ? -3.261  26.245  -41.481 1.00 36.38  ?  500  GLU D C   1 
ATOM   14793 O  O   . GLU D  1 469 ? -2.386  27.078  -41.732 1.00 33.53  ?  500  GLU D O   1 
ATOM   14794 C  CB  . GLU D  1 469 ? -5.137  27.062  -40.013 1.00 36.40  ?  500  GLU D CB  1 
ATOM   14795 C  CG  . GLU D  1 469 ? -5.837  27.003  -38.642 1.00 37.42  ?  500  GLU D CG  1 
ATOM   14796 C  CD  . GLU D  1 469 ? -7.063  27.894  -38.552 1.00 45.11  ?  500  GLU D CD  1 
ATOM   14797 O  OE1 . GLU D  1 469 ? -7.031  28.999  -39.154 1.00 41.09  ?  500  GLU D OE1 1 
ATOM   14798 O  OE2 . GLU D  1 469 ? -8.026  27.542  -37.818 1.00 45.67  -1 500  GLU D OE2 1 
ATOM   14799 N  N   . VAL D  1 470 ? -3.692  25.381  -42.399 1.00 39.39  ?  501  VAL D N   1 
ATOM   14800 C  CA  . VAL D  1 470 ? -3.087  25.386  -43.725 1.00 32.32  ?  501  VAL D CA  1 
ATOM   14801 C  C   . VAL D  1 470 ? -4.159  25.327  -44.809 1.00 38.50  ?  501  VAL D C   1 
ATOM   14802 O  O   . VAL D  1 470 ? -4.347  26.288  -45.568 1.00 31.53  ?  501  VAL D O   1 
ATOM   14803 C  CB  . VAL D  1 470 ? -2.086  24.226  -43.883 1.00 33.92  ?  501  VAL D CB  1 
ATOM   14804 C  CG1 . VAL D  1 470 ? -1.439  24.269  -45.255 1.00 38.04  ?  501  VAL D CG1 1 
ATOM   14805 C  CG2 . VAL D  1 470 ? -1.014  24.272  -42.794 1.00 33.92  ?  501  VAL D CG2 1 
ATOM   14806 N  N   . ASP D  1 471 ? -4.853  24.184  -44.904 1.00 35.76  ?  502  ASP D N   1 
ATOM   14807 C  CA  . ASP D  1 471 ? -5.746  23.956  -46.032 1.00 33.34  ?  502  ASP D CA  1 
ATOM   14808 C  C   . ASP D  1 471 ? -6.831  25.018  -46.125 1.00 31.66  ?  502  ASP D C   1 
ATOM   14809 O  O   . ASP D  1 471 ? -7.119  25.509  -47.220 1.00 35.23  ?  502  ASP D O   1 
ATOM   14810 C  CB  . ASP D  1 471 ? -6.374  22.564  -45.955 1.00 37.17  ?  502  ASP D CB  1 
ATOM   14811 C  CG  . ASP D  1 471 ? -5.350  21.454  -45.986 1.00 41.95  ?  502  ASP D CG  1 
ATOM   14812 O  OD1 . ASP D  1 471 ? -4.243  21.671  -46.522 1.00 43.92  ?  502  ASP D OD1 1 
ATOM   14813 O  OD2 . ASP D  1 471 ? -5.664  20.351  -45.495 1.00 49.17  -1 502  ASP D OD2 1 
ATOM   14814 N  N   . LYS D  1 472 ? -7.449  25.385  -44.999 1.00 31.88  ?  503  LYS D N   1 
ATOM   14815 C  CA  . LYS D  1 472 ? -8.571  26.322  -45.073 1.00 33.07  ?  503  LYS D CA  1 
ATOM   14816 C  C   . LYS D  1 472 ? -8.147  27.695  -45.581 1.00 32.42  ?  503  LYS D C   1 
ATOM   14817 O  O   . LYS D  1 472 ? -8.996  28.456  -46.061 1.00 30.30  ?  503  LYS D O   1 
ATOM   14818 C  CB  . LYS D  1 472 ? -9.262  26.469  -43.708 1.00 34.29  ?  503  LYS D CB  1 
ATOM   14819 C  CG  . LYS D  1 472 ? -8.397  27.123  -42.638 1.00 36.36  ?  503  LYS D CG  1 
ATOM   14820 C  CD  . LYS D  1 472 ? -9.181  27.402  -41.358 1.00 40.69  ?  503  LYS D CD  1 
ATOM   14821 C  CE  . LYS D  1 472 ? -9.551  26.127  -40.607 1.00 40.82  ?  503  LYS D CE  1 
ATOM   14822 N  NZ  . LYS D  1 472 ? -10.407 26.479  -39.436 1.00 42.61  ?  503  LYS D NZ  1 
ATOM   14823 N  N   . LEU D  1 473 ? -6.856  28.031  -45.481 1.00 32.04  ?  504  LEU D N   1 
ATOM   14824 C  CA  . LEU D  1 473 ? -6.373  29.293  -46.031 1.00 33.37  ?  504  LEU D CA  1 
ATOM   14825 C  C   . LEU D  1 473 ? -6.362  29.334  -47.558 1.00 32.41  ?  504  LEU D C   1 
ATOM   14826 O  O   . LEU D  1 473 ? -6.423  30.434  -48.118 1.00 33.86  ?  504  LEU D O   1 
ATOM   14827 C  CB  . LEU D  1 473 ? -4.968  29.598  -45.503 1.00 29.74  ?  504  LEU D CB  1 
ATOM   14828 C  CG  . LEU D  1 473 ? -4.794  29.488  -43.996 1.00 30.11  ?  504  LEU D CG  1 
ATOM   14829 C  CD1 . LEU D  1 473 ? -3.320  29.688  -43.610 1.00 31.03  ?  504  LEU D CD1 1 
ATOM   14830 C  CD2 . LEU D  1 473 ? -5.701  30.499  -43.277 1.00 29.77  ?  504  LEU D CD2 1 
ATOM   14831 N  N   . VAL D  1 474 ? -6.282  28.185  -48.250 1.00 30.88  ?  505  VAL D N   1 
ATOM   14832 C  CA  . VAL D  1 474 ? -6.222  28.166  -49.709 1.00 32.24  ?  505  VAL D CA  1 
ATOM   14833 C  C   . VAL D  1 474 ? -7.469  27.554  -50.360 1.00 33.74  ?  505  VAL D C   1 
ATOM   14834 O  O   . VAL D  1 474 ? -7.768  27.881  -51.513 1.00 34.89  ?  505  VAL D O   1 
ATOM   14835 C  CB  . VAL D  1 474 ? -4.953  27.445  -50.208 1.00 35.81  ?  505  VAL D CB  1 
ATOM   14836 C  CG1 . VAL D  1 474 ? -3.693  28.235  -49.827 1.00 33.78  ?  505  VAL D CG1 1 
ATOM   14837 C  CG2 . VAL D  1 474 ? -4.893  26.029  -49.673 1.00 34.88  ?  505  VAL D CG2 1 
ATOM   14838 N  N   . ASP D  1 475 ? -8.197  26.678  -49.668 1.00 35.43  ?  506  ASP D N   1 
ATOM   14839 C  CA  . ASP D  1 475 ? -9.373  26.038  -50.259 1.00 36.10  ?  506  ASP D CA  1 
ATOM   14840 C  C   . ASP D  1 475 ? -10.495 27.040  -50.507 1.00 33.45  ?  506  ASP D C   1 
ATOM   14841 O  O   . ASP D  1 475 ? -10.757 27.921  -49.685 1.00 35.32  ?  506  ASP D O   1 
ATOM   14842 C  CB  . ASP D  1 475 ? -9.883  24.916  -49.344 1.00 33.08  ?  506  ASP D CB  1 
ATOM   14843 C  CG  . ASP D  1 475 ? -8.926  23.750  -49.269 1.00 34.73  ?  506  ASP D CG  1 
ATOM   14844 O  OD1 . ASP D  1 475 ? -8.123  23.620  -50.203 1.00 36.33  ?  506  ASP D OD1 1 
ATOM   14845 O  OD2 . ASP D  1 475 ? -8.961  22.983  -48.279 1.00 40.97  -1 506  ASP D OD2 1 
ATOM   14846 N  N   . SER D  1 476 ? -11.185 26.877  -51.641 1.00 33.05  ?  507  SER D N   1 
ATOM   14847 C  CA  . SER D  1 476 ? -12.375 27.669  -51.899 1.00 33.42  ?  507  SER D CA  1 
ATOM   14848 C  C   . SER D  1 476 ? -13.571 27.040  -51.188 1.00 38.21  ?  507  SER D C   1 
ATOM   14849 O  O   . SER D  1 476 ? -13.686 25.814  -51.140 1.00 36.76  ?  507  SER D O   1 
ATOM   14850 C  CB  . SER D  1 476 ? -12.657 27.750  -53.401 1.00 33.54  ?  507  SER D CB  1 
ATOM   14851 O  OG  . SER D  1 476 ? -14.018 28.107  -53.655 1.00 33.54  ?  507  SER D OG  1 
ATOM   14852 N  N   . PRO D  1 477 ? -14.471 27.842  -50.611 1.00 37.00  ?  508  PRO D N   1 
ATOM   14853 C  CA  . PRO D  1 477 ? -15.668 27.259  -49.988 1.00 35.34  ?  508  PRO D CA  1 
ATOM   14854 C  C   . PRO D  1 477 ? -16.723 26.814  -50.995 1.00 40.55  ?  508  PRO D C   1 
ATOM   14855 O  O   . PRO D  1 477 ? -17.709 26.174  -50.597 1.00 43.87  ?  508  PRO D O   1 
ATOM   14856 C  CB  . PRO D  1 477 ? -16.200 28.401  -49.113 1.00 35.95  ?  508  PRO D CB  1 
ATOM   14857 C  CG  . PRO D  1 477 ? -15.707 29.641  -49.763 1.00 37.43  ?  508  PRO D CG  1 
ATOM   14858 C  CD  . PRO D  1 477 ? -14.375 29.293  -50.390 1.00 34.86  ?  508  PRO D CD  1 
ATOM   14859 N  N   . TYR D  1 478 ? -16.559 27.139  -52.277 1.00 38.93  ?  509  TYR D N   1 
ATOM   14860 C  CA  . TYR D  1 478 ? -17.520 26.778  -53.311 1.00 43.97  ?  509  TYR D CA  1 
ATOM   14861 C  C   . TYR D  1 478 ? -17.075 25.561  -54.123 1.00 48.04  ?  509  TYR D C   1 
ATOM   14862 O  O   . TYR D  1 478 ? -17.603 25.325  -55.219 1.00 47.02  ?  509  TYR D O   1 
ATOM   14863 C  CB  . TYR D  1 478 ? -17.780 27.994  -54.198 1.00 36.49  ?  509  TYR D CB  1 
ATOM   14864 C  CG  . TYR D  1 478 ? -17.938 29.219  -53.345 1.00 36.96  ?  509  TYR D CG  1 
ATOM   14865 C  CD1 . TYR D  1 478 ? -19.045 29.356  -52.508 1.00 33.78  ?  509  TYR D CD1 1 
ATOM   14866 C  CD2 . TYR D  1 478 ? -16.943 30.195  -53.295 1.00 38.57  ?  509  TYR D CD2 1 
ATOM   14867 C  CE1 . TYR D  1 478 ? -19.193 30.463  -51.694 1.00 36.39  ?  509  TYR D CE1 1 
ATOM   14868 C  CE2 . TYR D  1 478 ? -17.069 31.309  -52.468 1.00 30.82  ?  509  TYR D CE2 1 
ATOM   14869 C  CZ  . TYR D  1 478 ? -18.187 31.431  -51.670 1.00 38.07  ?  509  TYR D CZ  1 
ATOM   14870 O  OH  . TYR D  1 478 ? -18.321 32.520  -50.852 1.00 36.89  ?  509  TYR D OH  1 
ATOM   14871 N  N   . HIS D  1 479 ? -16.127 24.789  -53.588 1.00 51.72  ?  510  HIS D N   1 
ATOM   14872 C  CA  . HIS D  1 479 ? -15.691 23.495  -54.119 1.00 57.47  ?  510  HIS D CA  1 
ATOM   14873 C  C   . HIS D  1 479 ? -14.989 23.633  -55.462 1.00 63.75  ?  510  HIS D C   1 
ATOM   14874 O  O   . HIS D  1 479 ? -13.844 23.206  -55.614 1.00 63.22  ?  510  HIS D O   1 
ATOM   14875 C  CB  . HIS D  1 479 ? -16.877 22.526  -54.235 1.00 60.32  ?  510  HIS D CB  1 
HETATM 14876 C  C1  . G4S E  2 .   ? -9.666  -17.913 7.298   1.00 67.51  ?  1    G4S I C1  1 
HETATM 14877 C  C2  . G4S E  2 .   ? -9.487  -16.849 6.239   1.00 67.94  ?  1    G4S I C2  1 
HETATM 14878 C  C3  . G4S E  2 .   ? -9.606  -15.443 6.780   1.00 63.72  ?  1    G4S I C3  1 
HETATM 14879 C  C4  . G4S E  2 .   ? -10.760 -15.266 7.769   1.00 62.56  ?  1    G4S I C4  1 
HETATM 14880 C  C5  . G4S E  2 .   ? -10.722 -16.405 8.782   1.00 62.10  ?  1    G4S I C5  1 
HETATM 14881 C  C6  . G4S E  2 .   ? -11.846 -16.372 9.787   1.00 59.80  ?  1    G4S I C6  1 
HETATM 14882 O  O1  . G4S E  2 .   ? -9.805  -19.119 6.642   1.00 75.46  ?  1    G4S I O1  1 
HETATM 14883 O  O2  . G4S E  2 .   ? -8.209  -17.001 5.637   1.00 65.56  ?  1    G4S I O2  1 
HETATM 14884 O  O3  . G4S E  2 .   ? -9.738  -14.563 5.668   1.00 63.86  ?  1    G4S I O3  1 
HETATM 14885 O  O4  . G4S E  2 .   ? -12.057 -15.269 7.050   1.00 60.12  ?  1    G4S I O4  1 
HETATM 14886 O  O5  . G4S E  2 .   ? -10.822 -17.636 8.074   1.00 66.42  ?  1    G4S I O5  1 
HETATM 14887 O  O6  . G4S E  2 .   ? -11.610 -17.256 10.871  1.00 58.48  ?  1    G4S I O6  1 
HETATM 14888 S  S   . G4S E  2 .   ? -13.061 -14.034 7.264   1.00 73.54  ?  1    G4S I S   1 
HETATM 14889 O  O7  . G4S E  2 .   ? -12.180 -12.916 7.461   1.00 69.66  ?  1    G4S I O7  1 
HETATM 14890 O  O8  . G4S E  2 .   ? -13.866 -13.917 6.077   1.00 77.82  -1 1    G4S I O8  1 
HETATM 14891 O  O9  . G4S E  2 .   ? -13.848 -14.335 8.427   1.00 74.44  ?  1    G4S I O9  1 
HETATM 14892 C  C2  . 9RN E  2 .   ? -9.604  -12.386 4.844   1.00 53.81  ?  2    9RN I C2  1 
HETATM 14893 C  C4  . 9RN E  2 .   ? -7.324  -11.573 4.270   1.00 41.15  ?  2    9RN I C4  1 
HETATM 14894 C  C5  . 9RN E  2 .   ? -6.854  -12.342 5.494   1.00 44.88  ?  2    9RN I C5  1 
HETATM 14895 C  C6  . 9RN E  2 .   ? -7.236  -11.373 6.585   1.00 39.12  ?  2    9RN I C6  1 
HETATM 14896 O  O4  . 9RN E  2 .   ? -6.493  -10.474 3.971   1.00 34.50  ?  2    9RN I O4  1 
HETATM 14897 O  O5  . 9RN E  2 .   ? -7.572  -13.577 5.570   1.00 53.50  ?  2    9RN I O5  1 
HETATM 14898 O  O3  . 9RN E  2 .   ? -8.428  -10.704 6.113   1.00 44.41  ?  2    9RN I O3  1 
HETATM 14899 C  C3  . 9RN E  2 .   ? -8.700  -11.179 4.783   1.00 43.33  ?  2    9RN I C3  1 
HETATM 14900 O  O2  . 9RN E  2 .   ? -9.796  -12.937 3.548   1.00 48.12  ?  2    9RN I O2  1 
HETATM 14901 C  C1  . 9RN E  2 .   ? -8.974  -13.408 5.774   1.00 53.82  ?  2    9RN I C1  1 
HETATM 14902 C  C1  . GAL E  2 .   ? -5.244  -10.825 3.475   1.00 34.96  ?  3    GAL I C1  1 
HETATM 14903 C  C2  . GAL E  2 .   ? -5.011  -10.204 2.116   1.00 35.76  ?  3    GAL I C2  1 
HETATM 14904 C  C3  . GAL E  2 .   ? -3.646  -10.598 1.613   1.00 34.07  ?  3    GAL I C3  1 
HETATM 14905 C  C4  . GAL E  2 .   ? -2.607  -10.175 2.612   1.00 34.19  ?  3    GAL I C4  1 
HETATM 14906 C  C5  . GAL E  2 .   ? -2.904  -10.856 3.933   1.00 30.02  ?  3    GAL I C5  1 
HETATM 14907 C  C6  . GAL E  2 .   ? -1.932  -10.498 5.027   1.00 33.02  ?  3    GAL I C6  1 
HETATM 14908 O  O2  . GAL E  2 .   ? -6.032  -10.592 1.204   1.00 31.96  ?  3    GAL I O2  1 
HETATM 14909 O  O3  . GAL E  2 .   ? -3.380  -9.998  0.347   1.00 36.82  ?  3    GAL I O3  1 
HETATM 14910 O  O4  . GAL E  2 .   ? -2.803  -8.718  2.752   1.00 30.66  ?  3    GAL I O4  1 
HETATM 14911 O  O5  . GAL E  2 .   ? -4.204  -10.453 4.380   1.00 32.18  ?  3    GAL I O5  1 
HETATM 14912 O  O6  . GAL E  2 .   ? -2.213  -11.236 6.202   1.00 26.94  ?  3    GAL I O6  1 
HETATM 14913 C  C2  . 9RN E  2 .   ? -1.982  -9.989  -1.603  1.00 32.37  ?  4    9RN I C2  1 
HETATM 14914 C  C4  . 9RN E  2 .   ? -2.650  -11.725 -3.301  1.00 32.44  ?  4    9RN I C4  1 
HETATM 14915 C  C5  . 9RN E  2 .   ? -2.909  -12.623 -2.098  1.00 35.70  ?  4    9RN I C5  1 
HETATM 14916 C  C6  . 9RN E  2 .   ? -1.496  -13.087 -1.820  1.00 32.29  ?  4    9RN I C6  1 
HETATM 14917 O  O4  . 9RN E  2 .   ? -2.246  -12.502 -4.409  1.00 34.00  ?  4    9RN I O4  1 
HETATM 14918 O  O5  . 9RN E  2 .   ? -3.484  -11.849 -1.034  1.00 33.87  ?  4    9RN I O5  1 
HETATM 14919 O  O3  . 9RN E  2 .   ? -0.655  -11.953 -2.144  1.00 28.26  ?  4    9RN I O3  1 
HETATM 14920 C  C3  . 9RN E  2 .   ? -1.495  -10.921 -2.699  1.00 32.57  ?  4    9RN I C3  1 
HETATM 14921 O  O2  . 9RN E  2 .   ? -2.875  -9.001  -2.109  1.00 33.53  ?  4    9RN I O2  1 
HETATM 14922 C  C1  . 9RN E  2 .   ? -2.655  -10.814 -0.516  1.00 30.88  ?  4    9RN I C1  1 
HETATM 14923 C  C1  . G4S F  2 .   ? -7.094  4.094   -36.024 1.00 74.49  ?  1    G4S J C1  1 
HETATM 14924 C  C2  . G4S F  2 .   ? -7.370  3.702   -34.604 1.00 73.88  ?  1    G4S J C2  1 
HETATM 14925 C  C3  . G4S F  2 .   ? -8.451  4.577   -34.018 1.00 73.09  ?  1    G4S J C3  1 
HETATM 14926 C  C4  . G4S F  2 .   ? -8.146  6.056   -34.206 1.00 70.64  ?  1    G4S J C4  1 
HETATM 14927 C  C5  . G4S F  2 .   ? -7.678  6.366   -35.627 1.00 70.51  ?  1    G4S J C5  1 
HETATM 14928 C  C6  . G4S F  2 .   ? -7.100  7.754   -35.770 1.00 71.08  ?  1    G4S J C6  1 
HETATM 14929 O  O1  . G4S F  2 .   ? -6.126  3.247   -36.547 1.00 82.66  ?  1    G4S J O1  1 
HETATM 14930 O  O2  . G4S F  2 .   ? -7.736  2.328   -34.539 1.00 73.80  ?  1    G4S J O2  1 
HETATM 14931 O  O3  . G4S F  2 .   ? -8.569  4.266   -32.629 1.00 67.15  ?  1    G4S J O3  1 
HETATM 14932 O  O4  . G4S F  2 .   ? -7.061  6.413   -33.270 1.00 78.93  ?  1    G4S J O4  1 
HETATM 14933 O  O5  . G4S F  2 .   ? -6.652  5.447   -36.027 1.00 74.55  ?  1    G4S J O5  1 
HETATM 14934 O  O6  . G4S F  2 .   ? -7.221  8.226   -37.105 1.00 67.62  ?  1    G4S J O6  1 
HETATM 14935 S  S   . G4S F  2 .   ? -7.374  7.462   -32.136 1.00 92.00  ?  1    G4S J S   1 
HETATM 14936 O  O7  . G4S F  2 .   ? -8.606  8.081   -32.558 1.00 80.47  ?  1    G4S J O7  1 
HETATM 14937 O  O8  . G4S F  2 .   ? -7.513  6.705   -30.916 1.00 86.49  -1 1    G4S J O8  1 
HETATM 14938 O  O9  . G4S F  2 .   ? -6.258  8.377   -32.113 1.00 89.62  ?  1    G4S J O9  1 
HETATM 14939 C  C2  . 9RN F  2 .   ? -9.872  4.226   -30.635 1.00 59.26  ?  2    9RN J C2  1 
HETATM 14940 C  C4  . 9RN F  2 .   ? -11.651 2.483   -30.534 1.00 48.18  ?  2    9RN J C4  1 
HETATM 14941 C  C5  . 9RN F  2 .   ? -11.818 2.722   -32.026 1.00 50.37  ?  2    9RN J C5  1 
HETATM 14942 C  C6  . 9RN F  2 .   ? -12.649 3.982   -32.003 1.00 47.01  ?  2    9RN J C6  1 
HETATM 14943 O  O4  . 9RN F  2 .   ? -12.845 2.031   -29.932 1.00 42.08  ?  2    9RN J O4  1 
HETATM 14944 O  O5  . 9RN F  2 .   ? -10.528 2.913   -32.613 1.00 55.17  ?  2    9RN J O5  1 
HETATM 14945 O  O3  . 9RN F  2 .   ? -12.230 4.707   -30.822 1.00 51.15  ?  2    9RN J O3  1 
HETATM 14946 C  C3  . 9RN F  2 .   ? -11.258 3.898   -30.135 1.00 49.06  ?  2    9RN J C3  1 
HETATM 14947 O  O2  . 9RN F  2 .   ? -8.909  3.367   -30.038 1.00 56.86  ?  2    9RN J O2  1 
HETATM 14948 C  C1  . 9RN F  2 .   ? -9.864  4.087   -32.150 1.00 60.83  ?  2    9RN J C1  1 
HETATM 14949 C  C1  . GAL F  2 .   ? -13.186 0.720   -30.243 1.00 37.80  ?  3    GAL J C1  1 
HETATM 14950 C  C2  . GAL F  2 .   ? -13.336 -0.104  -28.984 1.00 34.62  ?  3    GAL J C2  1 
HETATM 14951 C  C3  . GAL F  2 .   ? -13.708 -1.526  -29.348 1.00 31.23  ?  3    GAL J C3  1 
HETATM 14952 C  C4  . GAL F  2 .   ? -14.948 -1.530  -30.206 1.00 32.32  ?  3    GAL J C4  1 
HETATM 14953 C  C5  . GAL F  2 .   ? -14.694 -0.695  -31.446 1.00 30.14  ?  3    GAL J C5  1 
HETATM 14954 C  C6  . GAL F  2 .   ? -15.895 -0.609  -32.350 1.00 30.33  ?  3    GAL J C6  1 
HETATM 14955 O  O2  . GAL F  2 .   ? -12.140 -0.053  -28.214 1.00 31.44  ?  3    GAL J O2  1 
HETATM 14956 O  O3  . GAL F  2 .   ? -13.910 -2.328  -28.180 1.00 34.60  ?  3    GAL J O3  1 
HETATM 14957 O  O4  . GAL F  2 .   ? -15.999 -0.880  -29.396 1.00 30.73  ?  3    GAL J O4  1 
HETATM 14958 O  O5  . GAL F  2 .   ? -14.364 0.645   -31.049 1.00 33.09  ?  3    GAL J O5  1 
HETATM 14959 O  O6  . GAL F  2 .   ? -15.591 0.099   -33.533 1.00 26.70  ?  3    GAL J O6  1 
HETATM 14960 C  C2  . 9RN F  2 .   ? -14.021 -4.564  -27.243 1.00 32.12  ?  4    9RN J C2  1 
HETATM 14961 C  C4  . 9RN F  2 .   ? -11.757 -5.599  -26.956 1.00 30.07  ?  4    9RN J C4  1 
HETATM 14962 C  C5  . 9RN F  2 .   ? -11.429 -4.944  -28.288 1.00 34.19  ?  4    9RN J C5  1 
HETATM 14963 C  C6  . 9RN F  2 .   ? -12.085 -5.920  -29.235 1.00 30.02  ?  4    9RN J C6  1 
HETATM 14964 O  O4  . 9RN F  2 .   ? -11.010 -6.780  -26.751 1.00 34.58  ?  4    9RN J O4  1 
HETATM 14965 O  O5  . 9RN F  2 .   ? -12.011 -3.636  -28.330 1.00 30.45  ?  4    9RN J O5  1 
HETATM 14966 O  O3  . 9RN F  2 .   ? -13.213 -6.472  -28.515 1.00 31.57  ?  4    9RN J O3  1 
HETATM 14967 C  C3  . 9RN F  2 .   ? -13.233 -5.858  -27.214 1.00 29.59  ?  4    9RN J C3  1 
HETATM 14968 O  O2  . 9RN F  2 .   ? -14.006 -3.953  -25.961 1.00 30.72  ?  4    9RN J O2  1 
HETATM 14969 C  C1  . 9RN F  2 .   ? -13.435 -3.635  -28.296 1.00 31.63  ?  4    9RN J C1  1 
HETATM 14970 C  C1  . G4S G  2 .   ? -15.785 25.315  14.023  1.00 101.70 ?  1    G4S K C1  1 
HETATM 14971 C  C2  . G4S G  2 .   ? -15.172 26.547  14.622  1.00 100.07 ?  1    G4S K C2  1 
HETATM 14972 C  C3  . G4S G  2 .   ? -14.583 27.425  13.545  1.00 94.99  ?  1    G4S K C3  1 
HETATM 14973 C  C4  . G4S G  2 .   ? -13.638 26.646  12.639  1.00 96.20  ?  1    G4S K C4  1 
HETATM 14974 C  C5  . G4S G  2 .   ? -14.266 25.330  12.185  1.00 97.51  ?  1    G4S K C5  1 
HETATM 14975 C  C6  . G4S G  2 .   ? -13.288 24.418  11.482  1.00 98.77  ?  1    G4S K C6  1 
HETATM 14976 O  O1  . G4S G  2 .   ? -16.325 24.546  15.044  1.00 116.02 ?  1    G4S K O1  1 
HETATM 14977 O  O2  . G4S G  2 .   ? -16.147 27.257  15.379  1.00 97.61  ?  1    G4S K O2  1 
HETATM 14978 O  O3  . G4S G  2 .   ? -13.879 28.487  14.175  1.00 95.05  ?  1    G4S K O3  1 
HETATM 14979 O  O4  . G4S G  2 .   ? -12.417 26.344  13.417  1.00 106.57 ?  1    G4S K O4  1 
HETATM 14980 O  O5  . G4S G  2 .   ? -14.768 24.606  13.319  1.00 106.38 ?  1    G4S K O5  1 
HETATM 14981 O  O6  . G4S G  2 .   ? -13.931 23.237  11.013  1.00 93.70  ?  1    G4S K O6  1 
HETATM 14982 S  S   . G4S G  2 .   ? -11.035 26.957  12.942  1.00 116.71 ?  1    G4S K S   1 
HETATM 14983 O  O7  . G4S G  2 .   ? -11.348 27.818  11.827  1.00 100.33 ?  1    G4S K O7  1 
HETATM 14984 O  O8  . G4S G  2 .   ? -10.215 25.832  12.570  1.00 120.05 -1 1    G4S K O8  1 
HETATM 14985 O  O9  . G4S G  2 .   ? -10.521 27.678  14.083  1.00 107.72 ?  1    G4S K O9  1 
HETATM 14986 C  C2  . 9RN G  2 .   ? -12.930 30.667  13.992  1.00 72.04  ?  2    9RN K C2  1 
HETATM 14987 C  C4  . 9RN G  2 .   ? -14.537 32.569  14.179  1.00 54.98  ?  2    9RN K C4  1 
HETATM 14988 C  C5  . 9RN G  2 .   ? -15.518 31.656  13.462  1.00 54.61  ?  2    9RN K C5  1 
HETATM 14989 C  C6  . 9RN G  2 .   ? -15.028 31.789  12.041  1.00 53.66  ?  2    9RN K C6  1 
HETATM 14990 O  O4  . 9RN G  2 .   ? -14.801 33.933  13.934  1.00 47.41  ?  2    9RN K O4  1 
HETATM 14991 O  O5  . 9RN G  2 .   ? -15.366 30.330  13.974  1.00 66.93  ?  2    9RN K O5  1 
HETATM 14992 O  O3  . 9RN G  2 .   ? -13.607 32.048  12.131  1.00 56.04  ?  2    9RN K O3  1 
HETATM 14993 C  C3  . 9RN G  2 .   ? -13.258 32.066  13.526  1.00 59.24  ?  2    9RN K C3  1 
HETATM 14994 O  O2  . 9RN G  2 .   ? -12.671 30.656  15.389  1.00 69.97  ?  2    9RN K O2  1 
HETATM 14995 C  C1  . 9RN G  2 .   ? -14.101 29.759  13.650  1.00 78.81  ?  2    9RN K C1  1 
HETATM 14996 C  C1  . GAL G  2 .   ? -16.018 34.387  14.428  1.00 39.37  ?  3    GAL K C1  1 
HETATM 14997 C  C2  . GAL G  2 .   ? -15.806 35.565  15.356  1.00 39.18  ?  3    GAL K C2  1 
HETATM 14998 C  C3  . GAL G  2 .   ? -17.148 36.061  15.835  1.00 39.29  ?  3    GAL K C3  1 
HETATM 14999 C  C4  . GAL G  2 .   ? -17.994 36.431  14.644  1.00 38.69  ?  3    GAL K C4  1 
HETATM 15000 C  C5  . GAL G  2 .   ? -18.173 35.207  13.770  1.00 39.47  ?  3    GAL K C5  1 
HETATM 15001 C  C6  . GAL G  2 .   ? -18.973 35.485  12.524  1.00 34.74  ?  3    GAL K C6  1 
HETATM 15002 O  O2  . GAL G  2 .   ? -14.958 35.199  16.439  1.00 36.63  ?  3    GAL K O2  1 
HETATM 15003 O  O3  . GAL G  2 .   ? -17.016 37.167  16.739  1.00 40.76  ?  3    GAL K O3  1 
HETATM 15004 O  O4  . GAL G  2 .   ? -17.213 37.431  13.890  1.00 36.80  ?  3    GAL K O4  1 
HETATM 15005 O  O5  . GAL G  2 .   ? -16.882 34.741  13.347  1.00 38.24  ?  3    GAL K O5  1 
HETATM 15006 O  O6  . GAL G  2 .   ? -19.097 34.311  11.743  1.00 31.73  ?  3    GAL K O6  1 
HETATM 15007 C  C2  . 9RN G  2 .   ? -18.030 38.504  18.513  1.00 38.02  ?  4    9RN K C2  1 
HETATM 15008 C  C4  . 9RN G  2 .   ? -18.139 37.275  20.701  1.00 37.15  ?  4    9RN K C4  1 
HETATM 15009 C  C5  . 9RN G  2 .   ? -18.491 36.064  19.853  1.00 39.20  ?  4    9RN K C5  1 
HETATM 15010 C  C6  . 9RN G  2 .   ? -19.951 36.341  19.584  1.00 34.63  ?  4    9RN K C6  1 
HETATM 15011 O  O4  . 9RN G  2 .   ? -18.724 37.197  21.984  1.00 36.65  ?  4    9RN K O4  1 
HETATM 15012 O  O5  . 9RN G  2 .   ? -17.689 36.064  18.666  1.00 41.48  ?  4    9RN K O5  1 
HETATM 15013 O  O3  . 9RN G  2 .   ? -20.088 37.782  19.595  1.00 37.28  ?  4    9RN K O3  1 
HETATM 15014 C  C3  . 9RN G  2 .   ? -18.779 38.333  19.821  1.00 34.68  ?  4    9RN K C3  1 
HETATM 15015 O  O2  . 9RN G  2 .   ? -16.741 39.049  18.762  1.00 39.49  ?  4    9RN K O2  1 
HETATM 15016 C  C1  . 9RN G  2 .   ? -17.929 37.165  17.795  1.00 40.46  ?  4    9RN K C1  1 
HETATM 15017 C  C1  . G4S H  2 .   ? 8.105   59.794  -28.080 1.00 84.84  ?  1    G4S L C1  1 
HETATM 15018 C  C2  . G4S H  2 .   ? 8.539   58.941  -29.230 1.00 81.53  ?  1    G4S L C2  1 
HETATM 15019 C  C3  . G4S H  2 .   ? 9.767   59.490  -29.944 1.00 81.03  ?  1    G4S L C3  1 
HETATM 15020 C  C4  . G4S H  2 .   ? 9.771   61.017  -30.099 1.00 83.27  ?  1    G4S L C4  1 
HETATM 15021 C  C5  . G4S H  2 .   ? 9.112   61.740  -28.915 1.00 84.54  ?  1    G4S L C5  1 
HETATM 15022 C  C6  . G4S H  2 .   ? 8.778   63.185  -29.195 1.00 89.84  ?  1    G4S L C6  1 
HETATM 15023 O  O1  . G4S H  2 .   ? 6.937   59.280  -27.536 1.00 94.02  ?  1    G4S L O1  1 
HETATM 15024 O  O2  . G4S H  2 .   ? 8.794   57.620  -28.762 1.00 80.70  ?  1    G4S L O2  1 
HETATM 15025 O  O3  . G4S H  2 .   ? 9.814   58.894  -31.235 1.00 74.94  ?  1    G4S L O3  1 
HETATM 15026 O  O4  . G4S H  2 .   ? 9.037   61.345  -31.341 1.00 88.20  ?  1    G4S L O4  1 
HETATM 15027 O  O5  . G4S H  2 .   ? 7.885   61.101  -28.575 1.00 90.46  ?  1    G4S L O5  1 
HETATM 15028 O  O6  . G4S H  2 .   ? 7.995   63.743  -28.143 1.00 89.46  ?  1    G4S L O6  1 
HETATM 15029 S  S   . G4S H  2 .   ? 9.837   61.963  -32.564 1.00 92.56  ?  1    G4S L S   1 
HETATM 15030 O  O7  . G4S H  2 .   ? 10.921  61.056  -32.839 1.00 81.97  ?  1    G4S L O7  1 
HETATM 15031 O  O8  . G4S H  2 .   ? 10.296  63.257  -32.126 1.00 93.14  -1 1    G4S L O8  1 
HETATM 15032 O  O9  . G4S H  2 .   ? 8.886   62.046  -33.642 1.00 92.77  ?  1    G4S L O9  1 
HETATM 15033 C  C2  . 9RN H  2 .   ? 10.721  57.502  -32.928 1.00 66.64  ?  2    9RN L C2  1 
HETATM 15034 C  C4  . 9RN H  2 .   ? 11.386  55.186  -32.235 1.00 50.96  ?  2    9RN L C4  1 
HETATM 15035 C  C5  . 9RN H  2 .   ? 11.806  55.829  -30.923 1.00 54.90  ?  2    9RN L C5  1 
HETATM 15036 C  C6  . 9RN H  2 .   ? 13.143  56.401  -31.325 1.00 51.69  ?  2    9RN L C6  1 
HETATM 15037 O  O4  . 9RN H  2 .   ? 12.137  54.028  -32.542 1.00 47.05  ?  2    9RN L O4  1 
HETATM 15038 O  O5  . 9RN H  2 .   ? 10.855  56.839  -30.569 1.00 56.76  ?  2    9RN L O5  1 
HETATM 15039 O  O3  . 9RN H  2 .   ? 13.004  56.774  -32.716 1.00 54.99  ?  2    9RN L O3  1 
HETATM 15040 C  C3  . 9RN H  2 .   ? 11.693  56.366  -33.148 1.00 53.42  ?  2    9RN L C3  1 
HETATM 15041 O  O2  . 9RN H  2 .   ? 9.399   57.101  -33.262 1.00 70.16  ?  2    9RN L O2  1 
HETATM 15042 C  C1  . 9RN H  2 .   ? 10.811  57.942  -31.474 1.00 66.34  ?  2    9RN L C1  1 
HETATM 15043 C  C1  . GAL H  2 .   ? 11.878  52.904  -31.764 1.00 41.40  ?  3    GAL L C1  1 
HETATM 15044 C  C2  . GAL H  2 .   ? 11.525  51.700  -32.620 1.00 43.47  ?  3    GAL L C2  1 
HETATM 15045 C  C3  . GAL H  2 .   ? 11.259  50.496  -31.741 1.00 39.13  ?  3    GAL L C3  1 
HETATM 15046 C  C4  . GAL H  2 .   ? 12.452  50.255  -30.855 1.00 37.57  ?  3    GAL L C4  1 
HETATM 15047 C  C5  . GAL H  2 .   ? 12.704  51.494  -30.015 1.00 35.56  ?  3    GAL L C5  1 
HETATM 15048 C  C6  . GAL H  2 .   ? 13.894  51.359  -29.100 1.00 34.37  ?  3    GAL L C6  1 
HETATM 15049 O  O2  . GAL H  2 .   ? 10.407  51.987  -33.452 1.00 40.81  ?  3    GAL L O2  1 
HETATM 15050 O  O3  . GAL H  2 .   ? 10.976  49.332  -32.526 1.00 41.12  ?  3    GAL L O3  1 
HETATM 15051 O  O4  . GAL H  2 .   ? 13.582  50.067  -31.786 1.00 33.95  ?  3    GAL L O4  1 
HETATM 15052 O  O5  . GAL H  2 .   ? 12.968  52.604  -30.888 1.00 39.99  ?  3    GAL L O5  1 
HETATM 15053 O  O6  . GAL H  2 .   ? 14.068  52.521  -28.301 1.00 33.87  ?  3    GAL L O6  1 
HETATM 15054 C  C2  . 9RN H  2 .   ? 10.010  47.098  -32.598 1.00 35.80  ?  4    9RN L C2  1 
HETATM 15055 C  C4  . 9RN H  2 .   ? 7.495   47.095  -32.651 1.00 39.03  ?  4    9RN L C4  1 
HETATM 15056 C  C5  . 9RN H  2 .   ? 7.612   48.282  -31.708 1.00 40.40  ?  4    9RN L C5  1 
HETATM 15057 C  C6  . 9RN H  2 .   ? 7.896   47.563  -30.412 1.00 39.40  ?  4    9RN L C6  1 
HETATM 15058 O  O4  . 9RN H  2 .   ? 6.316   46.348  -32.432 1.00 33.10  ?  4    9RN L O4  1 
HETATM 15059 O  O5  . 9RN H  2 .   ? 8.695   49.119  -32.129 1.00 42.17  ?  4    9RN L O5  1 
HETATM 15060 O  O3  . 9RN H  2 .   ? 8.597   46.349  -30.775 1.00 39.74  ?  4    9RN L O3  1 
HETATM 15061 C  C3  . 9RN H  2 .   ? 8.747   46.357  -32.205 1.00 37.22  ?  4    9RN L C3  1 
HETATM 15062 O  O2  . 9RN H  2 .   ? 10.138  47.136  -34.012 1.00 35.20  ?  4    9RN L O2  1 
HETATM 15063 C  C1  . 9RN H  2 .   ? 9.973   48.504  -32.018 1.00 41.71  ?  4    9RN L C1  1 
HETATM 15064 CA CA  . CA  I  3 .   ? -0.253  -3.788  2.511   1.00 34.13  ?  601  CA  A CA  1 
HETATM 15065 BR BR  . BR  J  4 .   ? 20.023  -8.022  8.545   0.86 37.85  ?  602  BR  A BR  1 
HETATM 15066 BR BR  . BR  K  4 .   ? -0.977  -9.651  23.027  0.72 34.96  ?  603  BR  A BR  1 
HETATM 15067 BR BR  . BR  L  4 .   ? -10.168 -8.791  -1.725  1.00 66.28  ?  604  BR  A BR  1 
HETATM 15068 CL CL  . CL  M  5 .   ? 15.195  25.480  6.886   1.00 70.02  ?  605  CL  A CL  1 
HETATM 15069 CL CL  . CL  N  5 .   ? -8.435  -19.627 14.751  1.00 32.95  ?  606  CL  A CL  1 
HETATM 15070 CL CL  . CL  O  5 .   ? 7.418   8.336   -30.422 1.00 44.78  ?  607  CL  A CL  1 
HETATM 15071 CL CL  . CL  P  5 .   ? -9.297  -0.323  -18.169 1.00 36.41  ?  608  CL  A CL  1 
HETATM 15072 CL CL  . CL  Q  5 .   ? 5.053   -9.269  -30.970 1.00 42.68  ?  609  CL  A CL  1 
HETATM 15073 CL CL  . CL  R  5 .   ? 12.977  20.035  19.211  1.00 35.16  ?  610  CL  A CL  1 
HETATM 15074 CL CL  . CL  S  5 .   ? -11.053 -6.580  -7.143  1.00 38.51  ?  611  CL  A CL  1 
HETATM 15075 CL CL  . CL  T  5 .   ? 9.379   -22.098 -7.125  1.00 61.56  ?  612  CL  A CL  1 
HETATM 15076 C  C1  . GOL U  6 .   ? -7.712  -7.680  -9.922  1.00 44.76  ?  613  GOL A C1  1 
HETATM 15077 O  O1  . GOL U  6 .   ? -7.264  -6.451  -10.477 1.00 39.94  ?  613  GOL A O1  1 
HETATM 15078 C  C2  . GOL U  6 .   ? -8.259  -8.538  -11.112 1.00 42.88  ?  613  GOL A C2  1 
HETATM 15079 O  O2  . GOL U  6 .   ? -9.079  -9.599  -10.693 1.00 45.58  ?  613  GOL A O2  1 
HETATM 15080 C  C3  . GOL U  6 .   ? -6.992  -9.006  -11.861 1.00 37.55  ?  613  GOL A C3  1 
HETATM 15081 O  O3  . GOL U  6 .   ? -6.721  -8.010  -12.796 1.00 47.11  ?  613  GOL A O3  1 
HETATM 15082 C  C1  . GOL V  6 .   ? -0.422  -16.612 -21.584 1.00 45.11  ?  614  GOL A C1  1 
HETATM 15083 O  O1  . GOL V  6 .   ? 0.556   -17.054 -20.667 1.00 55.68  ?  614  GOL A O1  1 
HETATM 15084 C  C2  . GOL V  6 .   ? 0.348   -16.066 -22.810 1.00 48.17  ?  614  GOL A C2  1 
HETATM 15085 O  O2  . GOL V  6 .   ? 1.076   -14.909 -22.506 1.00 46.76  ?  614  GOL A O2  1 
HETATM 15086 C  C3  . GOL V  6 .   ? 1.264   -17.247 -23.230 1.00 51.45  ?  614  GOL A C3  1 
HETATM 15087 O  O3  . GOL V  6 .   ? 1.855   -16.892 -24.430 1.00 48.48  ?  614  GOL A O3  1 
HETATM 15088 C  C1  . GOL W  6 .   ? -12.223 11.697  -0.502  1.00 38.73  ?  615  GOL A C1  1 
HETATM 15089 O  O1  . GOL W  6 .   ? -11.444 10.682  0.018   1.00 39.86  ?  615  GOL A O1  1 
HETATM 15090 C  C2  . GOL W  6 .   ? -12.525 11.297  -1.953  1.00 43.71  ?  615  GOL A C2  1 
HETATM 15091 O  O2  . GOL W  6 .   ? -13.735 11.792  -2.392  1.00 51.02  ?  615  GOL A O2  1 
HETATM 15092 C  C3  . GOL W  6 .   ? -11.357 11.828  -2.772  1.00 42.57  ?  615  GOL A C3  1 
HETATM 15093 O  O3  . GOL W  6 .   ? -11.885 12.775  -3.646  1.00 48.54  ?  615  GOL A O3  1 
HETATM 15094 CA CA  . CA  X  3 .   ? -20.734 -1.365  -27.096 1.00 35.34  ?  601  CA  B CA  1 
HETATM 15095 BR BR  . BR  Y  4 .   ? -10.006 1.901   -23.604 1.00 73.43  ?  602  BR  B BR  1 
HETATM 15096 BR BR  . BR  Z  4 .   ? -31.786 -13.925 -40.942 0.78 34.41  ?  603  BR  B BR  1 
HETATM 15097 BR BR  . BR  AA 4 .   ? -23.404 9.945   -44.843 0.79 32.87  ?  604  BR  B BR  1 
HETATM 15098 CL CL  . CL  BA 5 .   ? -22.776 -23.813 0.971   1.00 48.92  ?  605  CL  B CL  1 
HETATM 15099 CL CL  . CL  CA 5 .   ? -8.176  -27.591 -8.600  1.00 46.45  ?  606  CL  B CL  1 
HETATM 15100 CL CL  . CL  DA 5 .   ? -51.920 6.149   -28.722 1.00 39.06  ?  607  CL  B CL  1 
HETATM 15101 CL CL  . CL  EA 5 .   ? -9.532  -19.562 -34.939 1.00 74.38  ?  608  CL  B CL  1 
HETATM 15102 C  C1  . GOL FA 6 .   ? -9.589  -4.774  -16.680 1.00 37.71  ?  609  GOL B C1  1 
HETATM 15103 O  O1  . GOL FA 6 .   ? -10.814 -4.598  -17.285 1.00 39.55  ?  609  GOL B O1  1 
HETATM 15104 C  C2  . GOL FA 6 .   ? -8.749  -5.495  -17.751 1.00 44.07  ?  609  GOL B C2  1 
HETATM 15105 O  O2  . GOL FA 6 .   ? -7.354  -5.222  -17.660 1.00 41.94  ?  609  GOL B O2  1 
HETATM 15106 C  C3  . GOL FA 6 .   ? -9.043  -6.922  -17.409 1.00 38.80  ?  609  GOL B C3  1 
HETATM 15107 O  O3  . GOL FA 6 .   ? -7.906  -7.360  -16.760 1.00 40.55  ?  609  GOL B O3  1 
HETATM 15108 C  C1  . GOL GA 6 .   ? -24.086 9.075   -11.451 1.00 38.60  ?  610  GOL B C1  1 
HETATM 15109 O  O1  . GOL GA 6 .   ? -24.248 10.371  -11.938 1.00 39.53  ?  610  GOL B O1  1 
HETATM 15110 C  C2  . GOL GA 6 .   ? -23.262 9.146   -10.135 1.00 46.83  ?  610  GOL B C2  1 
HETATM 15111 O  O2  . GOL GA 6 .   ? -23.599 10.252  -9.353  1.00 49.47  ?  610  GOL B O2  1 
HETATM 15112 C  C3  . GOL GA 6 .   ? -23.598 7.836   -9.392  1.00 40.46  ?  610  GOL B C3  1 
HETATM 15113 O  O3  . GOL GA 6 .   ? -22.579 7.680   -8.452  1.00 52.13  ?  610  GOL B O3  1 
HETATM 15114 CA CA  . CA  HA 3 .   ? -17.191 42.596  12.319  1.00 43.30  ?  601  CA  C CA  1 
HETATM 15115 BR BR  . BR  IA 4 .   ? -37.819 45.931  6.483   0.78 36.28  ?  602  BR  C BR  1 
HETATM 15116 BR BR  . BR  JA 4 .   ? -3.950  52.763  35.343  1.00 81.11  ?  603  BR  C BR  1 
HETATM 15117 BR BR  . BR  KA 4 .   ? -21.074 29.973  -4.523  0.69 35.67  ?  604  BR  C BR  1 
HETATM 15118 CL CL  . CL  LA 5 .   ? -15.941 68.074  37.588  1.00 55.29  ?  605  CL  C CL  1 
HETATM 15119 CL CL  . CL  MA 5 .   ? -6.023  49.359  30.991  1.00 41.75  ?  606  CL  C CL  1 
HETATM 15120 CL CL  . CL  NA 5 .   ? -21.553 52.807  44.917  1.00 48.49  ?  607  CL  C CL  1 
HETATM 15121 CL CL  . CL  OA 5 .   ? -19.808 61.830  -13.140 1.00 45.18  ?  608  CL  C CL  1 
HETATM 15122 CL CL  . CL  PA 5 .   ? -33.119 35.853  27.469  1.00 70.49  ?  609  CL  C CL  1 
HETATM 15123 CA CA  . CA  QA 3 .   ? 17.789  46.586  -33.331 1.00 39.54  ?  601  CA  D CA  1 
HETATM 15124 BR BR  . BR  RA 4 .   ? 23.140  36.620  -14.933 0.81 37.23  ?  602  BR  D BR  1 
HETATM 15125 BR BR  . BR  SA 4 .   ? 2.619   35.733  -55.020 1.00 78.11  ?  603  BR  D BR  1 
HETATM 15126 BR BR  . BR  TA 4 .   ? 26.315  61.368  -20.738 0.69 36.61  ?  604  BR  D BR  1 
HETATM 15127 CL CL  . CL  UA 5 .   ? 4.730   39.160  -50.834 1.00 40.31  ?  605  CL  D CL  1 
HETATM 15128 CL CL  . CL  VA 5 .   ? -6.801  23.821  -41.971 1.00 41.04  ?  606  CL  D CL  1 
HETATM 15129 CL CL  . CL  WA 5 .   ? 48.796  39.908  -31.912 1.00 43.86  ?  607  CL  D CL  1 
HETATM 15130 CL CL  . CL  XA 5 .   ? 0.253   38.833  -20.656 1.00 73.22  ?  608  CL  D CL  1 
HETATM 15131 C  C1  . GOL YA 6 .   ? -8.029  43.509  -34.127 1.00 49.11  ?  609  GOL D C1  1 
HETATM 15132 O  O1  . GOL YA 6 .   ? -8.476  44.319  -35.221 1.00 47.22  ?  609  GOL D O1  1 
HETATM 15133 C  C2  . GOL YA 6 .   ? -8.982  42.274  -33.958 1.00 57.71  ?  609  GOL D C2  1 
HETATM 15134 O  O2  . GOL YA 6 .   ? -8.438  41.107  -34.512 1.00 62.66  ?  609  GOL D O2  1 
HETATM 15135 C  C3  . GOL YA 6 .   ? -9.197  42.141  -32.413 1.00 55.37  ?  609  GOL D C3  1 
HETATM 15136 O  O3  . GOL YA 6 .   ? -10.537 42.453  -32.131 1.00 59.26  ?  609  GOL D O3  1 
HETATM 15137 C  C1  . GOL ZA 6 .   ? -7.141  35.625  -35.880 1.00 52.37  ?  610  GOL D C1  1 
HETATM 15138 O  O1  . GOL ZA 6 .   ? -7.655  36.898  -36.178 1.00 55.68  ?  610  GOL D O1  1 
HETATM 15139 C  C2  . GOL ZA 6 .   ? -7.614  34.676  -37.008 1.00 49.64  ?  610  GOL D C2  1 
HETATM 15140 O  O2  . GOL ZA 6 .   ? -6.678  33.656  -37.264 1.00 52.51  ?  610  GOL D O2  1 
HETATM 15141 C  C3  . GOL ZA 6 .   ? -8.930  34.104  -36.471 1.00 53.92  ?  610  GOL D C3  1 
HETATM 15142 O  O3  . GOL ZA 6 .   ? -8.665  32.777  -36.116 1.00 54.98  ?  610  GOL D O3  1 
HETATM 15143 O  O   . HOH AB 7 .   ? 10.199  -1.697  19.466  1.00 27.06  ?  701  HOH A O   1 
HETATM 15144 O  O   . HOH AB 7 .   ? 1.546   23.856  2.973   1.00 44.01  ?  702  HOH A O   1 
HETATM 15145 O  O   . HOH AB 7 .   ? -9.181  -12.363 11.592  1.00 44.06  ?  703  HOH A O   1 
HETATM 15146 O  O   . HOH AB 7 .   ? 16.287  -0.165  -16.071 1.00 48.28  ?  704  HOH A O   1 
HETATM 15147 O  O   . HOH AB 7 .   ? 13.503  -12.861 31.507  1.00 50.05  ?  705  HOH A O   1 
HETATM 15148 O  O   . HOH AB 7 .   ? -11.319 -11.848 13.345  1.00 51.97  ?  706  HOH A O   1 
HETATM 15149 O  O   . HOH AB 7 .   ? 12.442  -24.276 -12.770 1.00 62.99  ?  707  HOH A O   1 
HETATM 15150 O  O   . HOH AB 7 .   ? 14.316  -11.942 19.938  1.00 37.96  ?  708  HOH A O   1 
HETATM 15151 O  O   . HOH AB 7 .   ? 19.731  -5.013  -6.603  1.00 44.10  ?  709  HOH A O   1 
HETATM 15152 O  O   . HOH AB 7 .   ? -13.418 3.266   -2.643  1.00 40.58  ?  710  HOH A O   1 
HETATM 15153 O  O   . HOH AB 7 .   ? -13.154 1.886   22.397  1.00 46.61  ?  711  HOH A O   1 
HETATM 15154 O  O   . HOH AB 7 .   ? -4.740  -16.091 0.883   1.00 43.87  ?  712  HOH A O   1 
HETATM 15155 O  O   . HOH AB 7 .   ? 0.508   -26.208 -15.373 1.00 47.30  ?  713  HOH A O   1 
HETATM 15156 O  O   . HOH AB 7 .   ? -3.844  -19.138 8.927   1.00 45.84  ?  714  HOH A O   1 
HETATM 15157 O  O   . HOH AB 7 .   ? 17.892  3.771   -11.306 1.00 49.84  ?  715  HOH A O   1 
HETATM 15158 O  O   . HOH AB 7 .   ? 8.022   0.862   -8.253  1.00 27.71  ?  716  HOH A O   1 
HETATM 15159 O  O   . HOH AB 7 .   ? 3.866   18.921  24.445  1.00 41.98  ?  717  HOH A O   1 
HETATM 15160 O  O   . HOH AB 7 .   ? 2.694   -1.177  8.234   1.00 24.14  ?  718  HOH A O   1 
HETATM 15161 O  O   . HOH AB 7 .   ? 17.772  10.690  20.227  1.00 41.19  ?  719  HOH A O   1 
HETATM 15162 O  O   . HOH AB 7 .   ? 0.464   -13.586 4.154   1.00 29.20  ?  720  HOH A O   1 
HETATM 15163 O  O   . HOH AB 7 .   ? -3.910  5.464   -12.647 1.00 22.93  ?  721  HOH A O   1 
HETATM 15164 O  O   . HOH AB 7 .   ? -4.440  -8.561  -13.761 1.00 24.69  ?  722  HOH A O   1 
HETATM 15165 O  O   A HOH AB 7 .   ? 26.242  -3.950  8.747   0.54 24.75  ?  723  HOH A O   1 
HETATM 15166 O  O   B HOH AB 7 .   ? 26.731  -2.824  8.376   0.46 27.11  ?  723  HOH A O   1 
HETATM 15167 O  O   . HOH AB 7 .   ? 19.985  13.699  -4.035  1.00 38.95  ?  724  HOH A O   1 
HETATM 15168 O  O   . HOH AB 7 .   ? 6.097   2.547   -12.720 1.00 35.60  ?  725  HOH A O   1 
HETATM 15169 O  O   . HOH AB 7 .   ? -9.582  15.447  5.407   1.00 32.31  ?  726  HOH A O   1 
HETATM 15170 O  O   . HOH AB 7 .   ? -3.968  -16.048 9.533   1.00 40.50  ?  727  HOH A O   1 
HETATM 15171 O  O   . HOH AB 7 .   ? 6.702   21.661  -6.631  1.00 41.83  ?  728  HOH A O   1 
HETATM 15172 O  O   . HOH AB 7 .   ? 7.186   -2.175  26.365  1.00 41.64  ?  729  HOH A O   1 
HETATM 15173 O  O   . HOH AB 7 .   ? 13.435  -7.053  -1.751  1.00 29.76  ?  730  HOH A O   1 
HETATM 15174 O  O   . HOH AB 7 .   ? -2.433  19.358  4.231   1.00 41.26  ?  731  HOH A O   1 
HETATM 15175 O  O   . HOH AB 7 .   ? -13.795 1.658   -1.115  1.00 39.30  ?  732  HOH A O   1 
HETATM 15176 O  O   . HOH AB 7 .   ? -0.434  -16.210 -6.579  1.00 26.09  ?  733  HOH A O   1 
HETATM 15177 O  O   . HOH AB 7 .   ? 10.802  21.139  21.569  1.00 45.10  ?  734  HOH A O   1 
HETATM 15178 O  O   . HOH AB 7 .   ? -5.949  13.012  15.221  1.00 30.83  ?  735  HOH A O   1 
HETATM 15179 O  O   . HOH AB 7 .   ? 1.742   -16.208 -10.004 1.00 32.93  ?  736  HOH A O   1 
HETATM 15180 O  O   . HOH AB 7 .   ? 26.726  10.521  4.227   1.00 44.22  ?  737  HOH A O   1 
HETATM 15181 O  O   . HOH AB 7 .   ? 1.687   -12.298 -7.239  1.00 27.13  ?  738  HOH A O   1 
HETATM 15182 O  O   . HOH AB 7 .   ? 6.517   -13.304 8.540   1.00 28.68  ?  739  HOH A O   1 
HETATM 15183 O  O   . HOH AB 7 .   ? -11.847 -13.018 17.738  1.00 46.86  ?  740  HOH A O   1 
HETATM 15184 O  O   . HOH AB 7 .   ? -7.216  -0.897  2.035   1.00 23.06  ?  741  HOH A O   1 
HETATM 15185 O  O   . HOH AB 7 .   ? -20.666 11.289  16.617  1.00 33.08  ?  742  HOH A O   1 
HETATM 15186 O  O   . HOH AB 7 .   ? -10.333 3.089   15.923  1.00 24.50  ?  743  HOH A O   1 
HETATM 15187 O  O   . HOH AB 7 .   ? 21.432  13.134  -0.996  1.00 37.86  ?  744  HOH A O   1 
HETATM 15188 O  O   . HOH AB 7 .   ? 8.299   -0.914  -1.138  1.00 24.68  ?  745  HOH A O   1 
HETATM 15189 O  O   . HOH AB 7 .   ? -25.602 10.127  6.682   1.00 42.35  ?  746  HOH A O   1 
HETATM 15190 O  O   . HOH AB 7 .   ? -2.435  22.000  9.611   1.00 42.98  ?  747  HOH A O   1 
HETATM 15191 O  O   . HOH AB 7 .   ? -1.364  -25.650 -13.629 1.00 43.48  ?  748  HOH A O   1 
HETATM 15192 O  O   . HOH AB 7 .   ? 1.749   -9.437  -35.450 1.00 36.79  ?  749  HOH A O   1 
HETATM 15193 O  O   . HOH AB 7 .   ? -6.447  1.572   13.582  1.00 24.61  ?  750  HOH A O   1 
HETATM 15194 O  O   . HOH AB 7 .   ? -6.114  -6.353  -29.815 1.00 32.70  ?  751  HOH A O   1 
HETATM 15195 O  O   . HOH AB 7 .   ? 3.861   -18.659 11.449  1.00 37.41  ?  752  HOH A O   1 
HETATM 15196 O  O   . HOH AB 7 .   ? -5.848  19.149  7.800   1.00 46.85  ?  753  HOH A O   1 
HETATM 15197 O  O   . HOH AB 7 .   ? -10.496 -8.031  17.513  1.00 29.55  ?  754  HOH A O   1 
HETATM 15198 O  O   . HOH AB 7 .   ? -8.387  -3.000  -10.973 1.00 27.38  ?  755  HOH A O   1 
HETATM 15199 O  O   . HOH AB 7 .   ? -3.316  12.797  19.133  1.00 38.31  ?  756  HOH A O   1 
HETATM 15200 O  O   . HOH AB 7 .   ? 12.285  -14.936 -12.323 1.00 32.14  ?  757  HOH A O   1 
HETATM 15201 O  O   . HOH AB 7 .   ? -0.204  -12.568 11.291  1.00 31.10  ?  758  HOH A O   1 
HETATM 15202 O  O   . HOH AB 7 .   ? 10.460  15.921  12.726  1.00 28.54  ?  759  HOH A O   1 
HETATM 15203 O  O   . HOH AB 7 .   ? 12.795  15.837  -16.970 1.00 36.28  ?  760  HOH A O   1 
HETATM 15204 O  O   . HOH AB 7 .   ? -15.131 10.822  19.329  1.00 45.64  ?  761  HOH A O   1 
HETATM 15205 O  O   . HOH AB 7 .   ? -3.483  5.020   24.107  1.00 39.22  ?  762  HOH A O   1 
HETATM 15206 O  O   . HOH AB 7 .   ? 13.235  -11.673 -21.953 1.00 49.73  ?  763  HOH A O   1 
HETATM 15207 O  O   . HOH AB 7 .   ? -0.239  13.970  -4.106  1.00 33.97  ?  764  HOH A O   1 
HETATM 15208 O  O   . HOH AB 7 .   ? -8.591  9.774   -12.831 1.00 37.64  ?  765  HOH A O   1 
HETATM 15209 O  O   . HOH AB 7 .   ? 5.307   20.657  12.236  1.00 42.18  ?  766  HOH A O   1 
HETATM 15210 O  O   . HOH AB 7 .   ? 2.481   10.102  -4.348  1.00 27.69  ?  767  HOH A O   1 
HETATM 15211 O  O   . HOH AB 7 .   ? 17.995  1.097   -2.676  1.00 30.95  ?  768  HOH A O   1 
HETATM 15212 O  O   . HOH AB 7 .   ? 8.200   -17.867 8.117   1.00 32.82  ?  769  HOH A O   1 
HETATM 15213 O  O   . HOH AB 7 .   ? 11.505  23.593  8.044   1.00 41.74  ?  770  HOH A O   1 
HETATM 15214 O  O   . HOH AB 7 .   ? 2.210   -10.695 -19.161 1.00 28.66  ?  771  HOH A O   1 
HETATM 15215 O  O   . HOH AB 7 .   ? 4.643   -15.327 8.644   1.00 30.74  ?  772  HOH A O   1 
HETATM 15216 O  O   . HOH AB 7 .   ? 7.311   13.647  -14.488 1.00 31.90  ?  773  HOH A O   1 
HETATM 15217 O  O   . HOH AB 7 .   ? -3.987  -25.977 20.139  1.00 48.41  ?  774  HOH A O   1 
HETATM 15218 O  O   . HOH AB 7 .   ? -7.475  15.831  7.523   1.00 29.80  ?  775  HOH A O   1 
HETATM 15219 O  O   . HOH AB 7 .   ? -9.658  14.239  -3.665  1.00 38.77  ?  776  HOH A O   1 
HETATM 15220 O  O   . HOH AB 7 .   ? -5.897  12.113  -4.257  1.00 32.76  ?  777  HOH A O   1 
HETATM 15221 O  O   . HOH AB 7 .   ? 19.740  -13.930 11.166  1.00 38.47  ?  778  HOH A O   1 
HETATM 15222 O  O   . HOH AB 7 .   ? 6.838   -4.978  -8.431  1.00 24.44  ?  779  HOH A O   1 
HETATM 15223 O  O   . HOH AB 7 .   ? 14.721  2.583   -7.814  1.00 34.83  ?  780  HOH A O   1 
HETATM 15224 O  O   . HOH AB 7 .   ? 0.965   -11.523 25.007  1.00 41.12  ?  781  HOH A O   1 
HETATM 15225 O  O   . HOH AB 7 .   ? 14.036  1.860   -10.297 1.00 31.29  ?  782  HOH A O   1 
HETATM 15226 O  O   . HOH AB 7 .   ? 6.533   16.926  -15.359 1.00 49.15  ?  783  HOH A O   1 
HETATM 15227 O  O   . HOH AB 7 .   ? 10.071  14.336  -15.178 1.00 38.47  ?  784  HOH A O   1 
HETATM 15228 O  O   . HOH AB 7 .   ? -8.099  17.129  1.536   1.00 37.89  ?  785  HOH A O   1 
HETATM 15229 O  O   . HOH AB 7 .   ? 10.389  1.289   -7.158  1.00 30.64  ?  786  HOH A O   1 
HETATM 15230 O  O   . HOH AB 7 .   ? 9.467   -14.768 18.750  1.00 37.75  ?  787  HOH A O   1 
HETATM 15231 O  O   . HOH AB 7 .   ? -9.868  6.920   -9.165  1.00 26.79  ?  788  HOH A O   1 
HETATM 15232 O  O   A HOH AB 7 .   ? -8.683  -5.097  -4.517  0.39 25.52  ?  789  HOH A O   1 
HETATM 15233 O  O   B HOH AB 7 .   ? -7.072  -5.243  -4.305  0.61 22.06  ?  789  HOH A O   1 
HETATM 15234 O  O   . HOH AB 7 .   ? 3.808   14.318  -9.486  1.00 29.24  ?  790  HOH A O   1 
HETATM 15235 O  O   . HOH AB 7 .   ? 16.989  -1.583  -18.413 1.00 39.89  ?  791  HOH A O   1 
HETATM 15236 O  O   . HOH AB 7 .   ? -10.502 -10.701 17.413  1.00 38.71  ?  792  HOH A O   1 
HETATM 15237 O  O   . HOH AB 7 .   ? 15.540  -17.263 2.983   1.00 33.12  ?  793  HOH A O   1 
HETATM 15238 O  O   . HOH AB 7 .   ? -1.343  4.230   26.483  1.00 37.63  ?  794  HOH A O   1 
HETATM 15239 O  O   . HOH AB 7 .   ? 23.528  0.539   17.972  1.00 40.67  ?  795  HOH A O   1 
HETATM 15240 O  O   . HOH AB 7 .   ? -6.820  -4.603  3.598   1.00 23.20  ?  796  HOH A O   1 
HETATM 15241 O  O   . HOH AB 7 .   ? -6.674  2.539   23.750  1.00 36.25  ?  797  HOH A O   1 
HETATM 15242 O  O   . HOH AB 7 .   ? 9.969   -21.465 -14.412 1.00 44.67  ?  798  HOH A O   1 
HETATM 15243 O  O   . HOH AB 7 .   ? -4.425  -26.750 22.173  1.00 52.08  ?  799  HOH A O   1 
HETATM 15244 O  O   . HOH AB 7 .   ? 9.099   19.202  -8.006  1.00 34.72  ?  800  HOH A O   1 
HETATM 15245 O  O   . HOH AB 7 .   ? -14.508 17.745  3.028   1.00 42.82  ?  801  HOH A O   1 
HETATM 15246 O  O   . HOH AB 7 .   ? -1.683  0.527   28.147  1.00 47.58  ?  802  HOH A O   1 
HETATM 15247 O  O   . HOH AB 7 .   ? -9.044  3.234   -8.006  1.00 23.28  ?  803  HOH A O   1 
HETATM 15248 O  O   . HOH AB 7 .   ? 2.656   -14.649 6.683   1.00 29.12  ?  804  HOH A O   1 
HETATM 15249 O  O   . HOH AB 7 .   ? -17.628 9.239   2.599   1.00 40.16  ?  805  HOH A O   1 
HETATM 15250 O  O   . HOH AB 7 .   ? 16.206  -17.401 -5.828  1.00 44.14  ?  806  HOH A O   1 
HETATM 15251 O  O   . HOH AB 7 .   ? -5.996  -10.447 -21.718 1.00 26.61  ?  807  HOH A O   1 
HETATM 15252 O  O   . HOH AB 7 .   ? 3.974   -14.155 20.111  1.00 44.74  ?  808  HOH A O   1 
HETATM 15253 O  O   . HOH AB 7 .   ? 1.314   16.669  13.746  1.00 29.62  ?  809  HOH A O   1 
HETATM 15254 O  O   . HOH AB 7 .   ? 12.800  11.598  -10.354 1.00 34.37  ?  810  HOH A O   1 
HETATM 15255 O  O   . HOH AB 7 .   ? 18.421  -18.454 14.306  1.00 43.95  ?  811  HOH A O   1 
HETATM 15256 O  O   . HOH AB 7 .   ? 10.254  19.794  7.537   1.00 33.95  ?  812  HOH A O   1 
HETATM 15257 O  O   . HOH AB 7 .   ? 2.771   24.028  -1.427  1.00 42.84  ?  813  HOH A O   1 
HETATM 15258 O  O   . HOH AB 7 .   ? -4.889  -9.369  -28.127 1.00 34.51  ?  814  HOH A O   1 
HETATM 15259 O  O   . HOH AB 7 .   ? 23.834  13.688  8.555   1.00 45.22  ?  815  HOH A O   1 
HETATM 15260 O  O   . HOH AB 7 .   ? 11.815  8.939   -14.170 1.00 30.71  ?  816  HOH A O   1 
HETATM 15261 O  O   . HOH AB 7 .   ? -16.350 12.775  1.065   1.00 42.33  ?  817  HOH A O   1 
HETATM 15262 O  O   . HOH AB 7 .   ? -2.766  3.928   -4.430  1.00 21.98  ?  818  HOH A O   1 
HETATM 15263 O  O   . HOH AB 7 .   ? 25.569  6.194   19.268  1.00 37.37  ?  819  HOH A O   1 
HETATM 15264 O  O   . HOH AB 7 .   ? 0.479   -14.205 8.146   1.00 29.72  ?  820  HOH A O   1 
HETATM 15265 O  O   . HOH AB 7 .   ? 1.708   12.140  -1.173  1.00 25.41  ?  821  HOH A O   1 
HETATM 15266 O  O   . HOH AB 7 .   ? 10.056  20.529  -4.334  1.00 35.47  ?  822  HOH A O   1 
HETATM 15267 O  O   . HOH AB 7 .   ? 7.112   12.712  -5.839  1.00 26.51  ?  823  HOH A O   1 
HETATM 15268 O  O   . HOH AB 7 .   ? -3.814  19.938  10.529  1.00 39.72  ?  824  HOH A O   1 
HETATM 15269 O  O   . HOH AB 7 .   ? 21.593  0.552   20.612  1.00 41.64  ?  825  HOH A O   1 
HETATM 15270 O  O   . HOH AB 7 .   ? 3.847   -16.347 -26.556 1.00 44.92  ?  826  HOH A O   1 
HETATM 15271 O  O   . HOH AB 7 .   ? 4.399   4.503   -12.539 1.00 29.26  ?  827  HOH A O   1 
HETATM 15272 O  O   . HOH AB 7 .   ? -11.505 9.503   18.911  1.00 38.71  ?  828  HOH A O   1 
HETATM 15273 O  O   . HOH AB 7 .   ? -9.029  6.165   -14.157 1.00 29.60  ?  829  HOH A O   1 
HETATM 15274 O  O   . HOH AB 7 .   ? 5.527   -13.987 18.019  1.00 36.49  ?  830  HOH A O   1 
HETATM 15275 O  O   . HOH AB 7 .   ? -0.756  -8.050  -17.592 1.00 28.81  ?  831  HOH A O   1 
HETATM 15276 O  O   . HOH AB 7 .   ? 6.826   -4.732  7.995   1.00 25.05  ?  832  HOH A O   1 
HETATM 15277 O  O   . HOH AB 7 .   ? -15.039 -0.966  0.333   1.00 36.43  ?  833  HOH A O   1 
HETATM 15278 O  O   . HOH AB 7 .   ? 20.556  -7.524  14.832  1.00 37.45  ?  834  HOH A O   1 
HETATM 15279 O  O   . HOH AB 7 .   ? 10.991  -14.280 12.880  1.00 30.02  ?  835  HOH A O   1 
HETATM 15280 O  O   . HOH AB 7 .   ? -0.192  6.060   24.965  1.00 35.35  ?  836  HOH A O   1 
HETATM 15281 O  O   . HOH AB 7 .   ? -0.729  -1.849  -27.574 1.00 33.83  ?  837  HOH A O   1 
HETATM 15282 O  O   . HOH AB 7 .   ? 13.104  11.781  -16.898 1.00 37.29  ?  838  HOH A O   1 
HETATM 15283 O  O   . HOH AB 7 .   ? 9.766   7.670   -22.276 1.00 41.23  ?  839  HOH A O   1 
HETATM 15284 O  O   . HOH AB 7 .   ? 13.704  -11.650 -19.418 1.00 37.40  ?  840  HOH A O   1 
HETATM 15285 O  O   . HOH AB 7 .   ? 3.895   -18.412 0.303   1.00 32.56  ?  841  HOH A O   1 
HETATM 15286 O  O   . HOH AB 7 .   ? -16.495 1.292   1.040   1.00 38.54  ?  842  HOH A O   1 
HETATM 15287 O  O   . HOH AB 7 .   ? 20.663  -10.408 -10.178 1.00 40.85  ?  843  HOH A O   1 
HETATM 15288 O  O   . HOH AB 7 .   ? -3.659  -5.637  -38.209 1.00 41.16  ?  844  HOH A O   1 
HETATM 15289 O  O   . HOH AB 7 .   ? -4.991  -6.495  -7.736  1.00 24.97  ?  845  HOH A O   1 
HETATM 15290 O  O   . HOH AB 7 .   ? 11.890  11.460  -13.050 1.00 30.54  ?  846  HOH A O   1 
HETATM 15291 O  O   . HOH AB 7 .   ? 14.474  -22.844 13.866  1.00 42.34  ?  847  HOH A O   1 
HETATM 15292 O  O   . HOH AB 7 .   ? -19.402 4.868   17.939  1.00 34.22  ?  848  HOH A O   1 
HETATM 15293 O  O   . HOH AB 7 .   ? 10.886  -3.115  -27.557 1.00 44.30  ?  849  HOH A O   1 
HETATM 15294 O  O   . HOH AB 7 .   ? 21.025  11.162  2.776   1.00 42.19  ?  850  HOH A O   1 
HETATM 15295 O  O   . HOH AB 7 .   ? 6.158   25.870  -1.879  1.00 50.98  ?  851  HOH A O   1 
HETATM 15296 O  O   . HOH AB 7 .   ? 23.054  -9.872  7.058   1.00 48.57  ?  852  HOH A O   1 
HETATM 15297 O  O   . HOH AB 7 .   ? 13.453  21.592  1.250   1.00 40.02  ?  853  HOH A O   1 
HETATM 15298 O  O   . HOH AB 7 .   ? 2.999   25.377  6.717   1.00 45.19  ?  854  HOH A O   1 
HETATM 15299 O  O   . HOH AB 7 .   ? 7.564   -3.868  12.494  1.00 32.38  ?  855  HOH A O   1 
HETATM 15300 O  O   . HOH AB 7 .   ? -7.509  -3.505  -22.962 1.00 38.34  ?  856  HOH A O   1 
HETATM 15301 O  O   . HOH AB 7 .   ? 13.074  -7.204  26.100  1.00 44.68  ?  857  HOH A O   1 
HETATM 15302 O  O   . HOH AB 7 .   ? -2.813  -3.438  -20.605 1.00 26.02  ?  858  HOH A O   1 
HETATM 15303 O  O   . HOH AB 7 .   ? 4.083   -10.926 -7.414  1.00 24.63  ?  859  HOH A O   1 
HETATM 15304 O  O   . HOH AB 7 .   ? -2.062  4.448   -1.673  1.00 22.53  ?  860  HOH A O   1 
HETATM 15305 O  O   . HOH AB 7 .   ? -13.445 -19.356 19.578  1.00 39.76  ?  861  HOH A O   1 
HETATM 15306 O  O   . HOH AB 7 .   ? 11.374  -13.267 -8.992  1.00 35.28  ?  862  HOH A O   1 
HETATM 15307 O  O   . HOH AB 7 .   ? 1.666   -13.242 -2.954  1.00 26.39  ?  863  HOH A O   1 
HETATM 15308 O  O   . HOH AB 7 .   ? -2.240  9.193   -21.881 1.00 26.43  ?  864  HOH A O   1 
HETATM 15309 O  O   . HOH AB 7 .   ? 7.564   -11.335 0.392   1.00 30.76  ?  865  HOH A O   1 
HETATM 15310 O  O   . HOH AB 7 .   ? 10.893  -20.811 7.947   1.00 37.67  ?  866  HOH A O   1 
HETATM 15311 O  O   . HOH AB 7 .   ? -6.197  -15.387 8.211   1.00 44.82  ?  867  HOH A O   1 
HETATM 15312 O  O   . HOH AB 7 .   ? 22.056  16.900  4.215   1.00 50.00  ?  868  HOH A O   1 
HETATM 15313 O  O   . HOH AB 7 .   ? -1.762  18.851  0.017   1.00 32.68  ?  869  HOH A O   1 
HETATM 15314 O  O   . HOH AB 7 .   ? -8.871  -9.905  -24.610 1.00 29.96  ?  870  HOH A O   1 
HETATM 15315 O  O   . HOH AB 7 .   ? -8.380  -6.398  -26.067 1.00 33.02  ?  871  HOH A O   1 
HETATM 15316 O  O   . HOH AB 7 .   ? -15.951 13.248  7.673   1.00 37.69  ?  872  HOH A O   1 
HETATM 15317 O  O   . HOH AB 7 .   ? -16.733 13.729  10.142  1.00 33.99  ?  873  HOH A O   1 
HETATM 15318 O  O   . HOH AB 7 .   ? 14.545  1.344   0.946   1.00 24.94  ?  874  HOH A O   1 
HETATM 15319 O  O   . HOH AB 7 .   ? -2.296  -0.394  13.552  1.00 22.26  ?  875  HOH A O   1 
HETATM 15320 O  O   . HOH AB 7 .   ? -3.142  5.413   18.116  1.00 28.41  ?  876  HOH A O   1 
HETATM 15321 O  O   . HOH AB 7 .   ? 1.986   19.490  -7.001  1.00 38.28  ?  877  HOH A O   1 
HETATM 15322 O  O   . HOH AB 7 .   ? 13.475  -11.145 8.081   1.00 29.69  ?  878  HOH A O   1 
HETATM 15323 O  O   . HOH AB 7 .   ? 0.551   -4.442  -27.387 1.00 29.78  ?  879  HOH A O   1 
HETATM 15324 O  O   . HOH AB 7 .   ? -8.570  -2.328  4.148   1.00 24.24  ?  880  HOH A O   1 
HETATM 15325 O  O   . HOH AB 7 .   ? -5.919  -3.226  -32.772 1.00 42.03  ?  881  HOH A O   1 
HETATM 15326 O  O   . HOH AB 7 .   ? 20.725  18.574  -6.883  1.00 45.73  ?  882  HOH A O   1 
HETATM 15327 O  O   . HOH AB 7 .   ? -3.148  -8.604  -5.010  1.00 33.18  ?  883  HOH A O   1 
HETATM 15328 O  O   . HOH AB 7 .   ? 10.433  7.360   -13.106 1.00 33.85  ?  884  HOH A O   1 
HETATM 15329 O  O   . HOH AB 7 .   ? -1.252  -13.678 6.259   1.00 31.56  ?  885  HOH A O   1 
HETATM 15330 O  O   . HOH AB 7 .   ? -14.155 -5.926  5.067   1.00 42.65  ?  886  HOH A O   1 
HETATM 15331 O  O   . HOH AB 7 .   ? 0.856   21.817  -0.649  1.00 38.21  ?  887  HOH A O   1 
HETATM 15332 O  O   A HOH AB 7 .   ? -19.446 -1.018  0.104   0.54 39.64  ?  888  HOH A O   1 
HETATM 15333 O  O   B HOH AB 7 .   ? -19.227 -2.432  1.293   0.46 35.17  ?  888  HOH A O   1 
HETATM 15334 O  O   . HOH AB 7 .   ? 11.175  -16.063 -18.937 1.00 34.10  ?  889  HOH A O   1 
HETATM 15335 O  O   . HOH AB 7 .   ? 3.871   20.443  1.999   1.00 28.79  ?  890  HOH A O   1 
HETATM 15336 O  O   . HOH AB 7 .   ? -2.127  -6.331  8.375   1.00 24.70  ?  891  HOH A O   1 
HETATM 15337 O  O   A HOH AB 7 .   ? -23.094 5.393   12.605  0.50 43.96  ?  892  HOH A O   1 
HETATM 15338 O  O   B HOH AB 7 .   ? -22.279 5.154   13.898  0.50 43.96  ?  892  HOH A O   1 
HETATM 15339 O  O   . HOH AB 7 .   ? -1.677  16.174  -2.594  1.00 38.89  ?  893  HOH A O   1 
HETATM 15340 O  O   . HOH AB 7 .   ? -11.834 -17.835 25.893  1.00 41.52  ?  894  HOH A O   1 
HETATM 15341 O  O   . HOH AB 7 .   ? 8.745   -14.971 -3.472  1.00 32.40  ?  895  HOH A O   1 
HETATM 15342 O  O   . HOH AB 7 .   ? 22.828  -1.820  19.242  1.00 42.04  ?  896  HOH A O   1 
HETATM 15343 O  O   . HOH AB 7 .   ? -24.551 9.215   2.006   1.00 43.40  ?  897  HOH A O   1 
HETATM 15344 O  O   . HOH AB 7 .   ? 0.434   16.938  18.613  1.00 40.92  ?  898  HOH A O   1 
HETATM 15345 O  O   . HOH AB 7 .   ? -3.134  5.400   -29.416 1.00 42.49  ?  899  HOH A O   1 
HETATM 15346 O  O   . HOH AB 7 .   ? 1.230   11.928  -12.531 1.00 27.88  ?  900  HOH A O   1 
HETATM 15347 O  O   . HOH AB 7 .   ? 3.070   -16.000 10.848  1.00 32.90  ?  901  HOH A O   1 
HETATM 15348 O  O   . HOH AB 7 .   ? 1.416   -12.083 -24.288 1.00 30.52  ?  902  HOH A O   1 
HETATM 15349 O  O   . HOH AB 7 .   ? 6.149   -23.602 12.005  1.00 40.22  ?  903  HOH A O   1 
HETATM 15350 O  O   . HOH AB 7 .   ? 23.198  -7.085  -1.791  1.00 37.51  ?  904  HOH A O   1 
HETATM 15351 O  O   . HOH AB 7 .   ? 18.569  -5.047  -11.753 1.00 36.76  ?  905  HOH A O   1 
HETATM 15352 O  O   . HOH AB 7 .   ? 3.476   13.309  -12.926 1.00 27.46  ?  906  HOH A O   1 
HETATM 15353 O  O   . HOH AB 7 .   ? -6.755  10.757  -16.174 1.00 29.78  ?  907  HOH A O   1 
HETATM 15354 O  O   . HOH AB 7 .   ? 20.313  10.870  -9.700  1.00 46.57  ?  908  HOH A O   1 
HETATM 15355 O  O   . HOH AB 7 .   ? 4.582   0.110   27.478  1.00 45.19  ?  909  HOH A O   1 
HETATM 15356 O  O   . HOH AB 7 .   ? -1.698  5.331   22.688  1.00 35.16  ?  910  HOH A O   1 
HETATM 15357 O  O   . HOH AB 7 .   ? 19.645  15.173  17.128  1.00 41.36  ?  911  HOH A O   1 
HETATM 15358 O  O   . HOH AB 7 .   ? 19.755  -6.405  17.657  1.00 38.61  ?  912  HOH A O   1 
HETATM 15359 O  O   . HOH AB 7 .   ? 27.162  0.645   9.459   1.00 40.73  ?  913  HOH A O   1 
HETATM 15360 O  O   . HOH AB 7 .   ? -9.471  -4.726  23.936  1.00 29.10  ?  914  HOH A O   1 
HETATM 15361 O  O   . HOH AB 7 .   ? -4.460  9.250   21.098  1.00 44.96  ?  915  HOH A O   1 
HETATM 15362 O  O   . HOH AB 7 .   ? -0.304  13.091  -27.104 1.00 50.27  ?  916  HOH A O   1 
HETATM 15363 O  O   . HOH AB 7 .   ? 1.324   -3.094  -34.895 1.00 45.72  ?  917  HOH A O   1 
HETATM 15364 O  O   . HOH AB 7 .   ? 9.048   -19.095 -18.838 1.00 39.71  ?  918  HOH A O   1 
HETATM 15365 O  O   . HOH AB 7 .   ? 18.282  -16.905 4.750   1.00 38.82  ?  919  HOH A O   1 
HETATM 15366 O  O   . HOH AB 7 .   ? -15.155 10.779  -0.083  1.00 50.15  ?  920  HOH A O   1 
HETATM 15367 O  O   . HOH AB 7 .   ? 1.494   -12.925 12.940  1.00 31.97  ?  921  HOH A O   1 
HETATM 15368 O  O   . HOH AB 7 .   ? 15.561  -15.179 16.864  1.00 36.34  ?  922  HOH A O   1 
HETATM 15369 O  O   . HOH AB 7 .   ? -13.416 -23.780 23.554  1.00 44.84  ?  923  HOH A O   1 
HETATM 15370 O  O   . HOH AB 7 .   ? 16.853  -3.585  -10.306 1.00 34.85  ?  924  HOH A O   1 
HETATM 15371 O  O   . HOH AB 7 .   ? -14.776 6.362   -0.791  1.00 37.32  ?  925  HOH A O   1 
HETATM 15372 O  O   . HOH AB 7 .   ? -10.180 6.932   20.576  1.00 37.59  ?  926  HOH A O   1 
HETATM 15373 O  O   . HOH AB 7 .   ? 12.150  6.270   -23.884 1.00 47.62  ?  927  HOH A O   1 
HETATM 15374 O  O   . HOH AB 7 .   ? 4.389   -7.983  29.718  1.00 49.21  ?  928  HOH A O   1 
HETATM 15375 O  O   . HOH AB 7 .   ? 4.544   5.125   26.220  1.00 39.44  ?  929  HOH A O   1 
HETATM 15376 O  O   . HOH AB 7 .   ? 13.277  10.182  28.440  1.00 37.31  ?  930  HOH A O   1 
HETATM 15377 O  O   . HOH AB 7 .   ? -3.268  3.226   -28.723 1.00 41.34  ?  931  HOH A O   1 
HETATM 15378 O  O   . HOH AB 7 .   ? -10.429 3.825   -5.680  1.00 24.36  ?  932  HOH A O   1 
HETATM 15379 O  O   . HOH AB 7 .   ? -8.109  -17.426 -37.307 1.00 52.01  ?  933  HOH A O   1 
HETATM 15380 O  O   . HOH AB 7 .   ? -8.001  0.572   23.627  1.00 35.66  ?  934  HOH A O   1 
HETATM 15381 O  O   . HOH AB 7 .   ? -20.501 0.703   13.123  1.00 51.46  ?  935  HOH A O   1 
HETATM 15382 O  O   A HOH AB 7 .   ? 1.556   -12.425 17.000  0.50 38.62  ?  936  HOH A O   1 
HETATM 15383 O  O   B HOH AB 7 .   ? 0.539   -12.914 15.323  0.50 38.62  ?  936  HOH A O   1 
HETATM 15384 O  O   . HOH AB 7 .   ? 1.701   24.503  11.527  1.00 48.98  ?  937  HOH A O   1 
HETATM 15385 O  O   . HOH AB 7 .   ? -19.820 -1.348  3.762   1.00 41.47  ?  938  HOH A O   1 
HETATM 15386 O  O   . HOH AB 7 .   ? 5.542   -11.882 3.010   1.00 28.20  ?  939  HOH A O   1 
HETATM 15387 O  O   . HOH AB 7 .   ? -5.015  -2.135  -23.250 1.00 29.01  ?  940  HOH A O   1 
HETATM 15388 O  O   . HOH AB 7 .   ? 11.600  22.123  15.203  1.00 48.85  ?  941  HOH A O   1 
HETATM 15389 O  O   A HOH AB 7 .   ? -20.891 12.608  12.369  0.50 41.98  ?  942  HOH A O   1 
HETATM 15390 O  O   B HOH AB 7 .   ? -19.846 13.391  12.892  0.50 41.98  ?  942  HOH A O   1 
HETATM 15391 O  O   . HOH AB 7 .   ? 24.352  -1.468  -5.709  1.00 45.76  ?  943  HOH A O   1 
HETATM 15392 O  O   . HOH AB 7 .   ? -6.070  -9.111  -7.393  1.00 39.37  ?  944  HOH A O   1 
HETATM 15393 O  O   . HOH AB 7 .   ? 22.364  7.576   -4.885  1.00 40.44  ?  945  HOH A O   1 
HETATM 15394 O  O   . HOH AB 7 .   ? -23.264 1.385   1.241   1.00 52.66  ?  946  HOH A O   1 
HETATM 15395 O  O   . HOH AB 7 .   ? 6.922   15.353  -12.595 1.00 37.69  ?  947  HOH A O   1 
HETATM 15396 O  O   . HOH AB 7 .   ? -15.417 -2.022  14.549  1.00 29.70  ?  948  HOH A O   1 
HETATM 15397 O  O   . HOH AB 7 .   ? -14.130 -5.778  16.506  1.00 41.09  ?  949  HOH A O   1 
HETATM 15398 O  O   . HOH AB 7 .   ? -4.504  -30.306 18.830  1.00 50.59  ?  950  HOH A O   1 
HETATM 15399 O  O   . HOH AB 7 .   ? -14.682 0.549   21.258  1.00 35.09  ?  951  HOH A O   1 
HETATM 15400 O  O   . HOH AB 7 .   ? 19.937  12.540  16.956  1.00 41.27  ?  952  HOH A O   1 
HETATM 15401 O  O   . HOH AB 7 .   ? -23.181 -0.156  5.022   1.00 40.18  ?  953  HOH A O   1 
HETATM 15402 O  O   . HOH AB 7 .   ? -3.926  -13.857 21.943  1.00 34.86  ?  954  HOH A O   1 
HETATM 15403 O  O   . HOH AB 7 .   ? 16.123  18.039  17.657  1.00 34.20  ?  955  HOH A O   1 
HETATM 15404 O  O   . HOH AB 7 .   ? 9.294   22.536  9.443   1.00 35.88  ?  956  HOH A O   1 
HETATM 15405 O  O   . HOH AB 7 .   ? 5.791   -22.637 5.497   1.00 41.34  ?  957  HOH A O   1 
HETATM 15406 O  O   . HOH AB 7 .   ? -4.165  -6.648  10.051  1.00 26.45  ?  958  HOH A O   1 
HETATM 15407 O  O   . HOH AB 7 .   ? -14.192 -8.444  12.229  1.00 35.76  ?  959  HOH A O   1 
HETATM 15408 O  O   . HOH AB 7 .   ? 11.143  -13.013 -6.178  1.00 37.94  ?  960  HOH A O   1 
HETATM 15409 O  O   . HOH AB 7 .   ? -6.808  -6.737  1.708   1.00 25.30  ?  961  HOH A O   1 
HETATM 15410 O  O   . HOH AB 7 .   ? -1.114  -13.022 2.030   1.00 30.08  ?  962  HOH A O   1 
HETATM 15411 O  O   . HOH AB 7 .   ? 14.095  25.047  12.456  1.00 54.08  ?  963  HOH A O   1 
HETATM 15412 O  O   . HOH AB 7 .   ? -10.375 1.659   -11.176 1.00 30.41  ?  964  HOH A O   1 
HETATM 15413 O  O   . HOH AB 7 .   ? 16.128  18.496  -12.135 1.00 41.85  ?  965  HOH A O   1 
HETATM 15414 O  O   . HOH AB 7 .   ? 9.220   13.088  -19.731 1.00 33.51  ?  966  HOH A O   1 
HETATM 15415 O  O   . HOH AB 7 .   ? -17.908 14.210  5.629   1.00 25.63  ?  967  HOH A O   1 
HETATM 15416 O  O   . HOH AB 7 .   ? 16.674  3.177   -15.730 1.00 42.24  ?  968  HOH A O   1 
HETATM 15417 O  O   . HOH AB 7 .   ? 6.972   23.449  -3.530  1.00 39.76  ?  969  HOH A O   1 
HETATM 15418 O  O   . HOH AB 7 .   ? -10.419 -10.896 -8.310  1.00 28.84  ?  970  HOH A O   1 
HETATM 15419 O  O   . HOH AB 7 .   ? -7.909  -25.902 12.168  1.00 50.73  ?  971  HOH A O   1 
HETATM 15420 O  O   . HOH AB 7 .   ? 19.646  10.754  30.545  1.00 45.92  ?  972  HOH A O   1 
HETATM 15421 O  O   . HOH AB 7 .   ? 3.888   11.852  25.795  1.00 49.72  ?  973  HOH A O   1 
HETATM 15422 O  O   . HOH AB 7 .   ? 20.734  11.869  -7.671  1.00 47.09  ?  974  HOH A O   1 
HETATM 15423 O  O   . HOH AB 7 .   ? 22.582  3.973   -4.188  1.00 48.46  ?  975  HOH A O   1 
HETATM 15424 O  O   . HOH AB 7 .   ? -4.883  16.989  -18.351 1.00 52.81  ?  976  HOH A O   1 
HETATM 15425 O  O   . HOH AB 7 .   ? 4.971   -19.253 2.410   1.00 30.67  ?  977  HOH A O   1 
HETATM 15426 O  O   . HOH AB 7 .   ? 10.540  9.537   -20.776 1.00 39.64  ?  978  HOH A O   1 
HETATM 15427 O  O   . HOH AB 7 .   ? 13.230  24.513  -8.664  1.00 48.36  ?  979  HOH A O   1 
HETATM 15428 O  O   . HOH AB 7 .   ? 2.828   -4.711  -36.758 1.00 53.41  ?  980  HOH A O   1 
HETATM 15429 O  O   . HOH AB 7 .   ? -7.859  -4.025  -13.839 1.00 31.46  ?  981  HOH A O   1 
HETATM 15430 O  O   . HOH AB 7 .   ? 13.295  -20.406 0.680   1.00 46.10  ?  982  HOH A O   1 
HETATM 15431 O  O   . HOH AB 7 .   ? -13.961 11.932  -5.721  1.00 52.87  ?  983  HOH A O   1 
HETATM 15432 O  O   . HOH AB 7 .   ? -0.919  13.183  -6.280  1.00 40.73  ?  984  HOH A O   1 
HETATM 15433 O  O   . HOH AB 7 .   ? 3.823   -14.251 -19.330 1.00 43.36  ?  985  HOH A O   1 
HETATM 15434 O  O   . HOH AB 7 .   ? -3.779  14.021  -14.895 1.00 36.71  ?  986  HOH A O   1 
HETATM 15435 O  O   A HOH AB 7 .   ? -6.419  0.753   -25.595 0.54 34.61  ?  987  HOH A O   1 
HETATM 15436 O  O   B HOH AB 7 .   ? -5.920  -1.168  -25.429 0.46 30.51  ?  987  HOH A O   1 
HETATM 15437 O  O   . HOH AB 7 .   ? -2.123  -24.324 16.694  1.00 47.46  ?  988  HOH A O   1 
HETATM 15438 O  O   . HOH AB 7 .   ? -17.095 14.499  2.819   1.00 41.68  ?  989  HOH A O   1 
HETATM 15439 O  O   . HOH AB 7 .   ? -20.918 6.435   2.597   1.00 37.74  ?  990  HOH A O   1 
HETATM 15440 O  O   . HOH AB 7 .   ? 4.233   21.344  14.404  1.00 50.67  ?  991  HOH A O   1 
HETATM 15441 O  O   . HOH AB 7 .   ? 25.547  5.162   2.897   1.00 49.42  ?  992  HOH A O   1 
HETATM 15442 O  O   . HOH AB 7 .   ? 6.397   -21.718 -21.691 1.00 56.29  ?  993  HOH A O   1 
HETATM 15443 O  O   . HOH AB 7 .   ? -7.833  4.619   -24.851 1.00 36.52  ?  994  HOH A O   1 
HETATM 15444 O  O   A HOH AB 7 .   ? -17.090 -2.718  8.672   0.50 48.18  ?  995  HOH A O   1 
HETATM 15445 O  O   B HOH AB 7 .   ? -16.374 -4.405  9.788   0.50 48.18  ?  995  HOH A O   1 
HETATM 15446 O  O   . HOH AB 7 .   ? -3.340  -0.837  -27.854 1.00 38.93  ?  996  HOH A O   1 
HETATM 15447 O  O   . HOH AB 7 .   ? 18.318  18.501  21.362  1.00 51.76  ?  997  HOH A O   1 
HETATM 15448 O  O   . HOH AB 7 .   ? -13.213 -6.827  7.455   1.00 28.33  ?  998  HOH A O   1 
HETATM 15449 O  O   . HOH AB 7 .   ? 9.577   -10.193 -26.486 1.00 50.70  ?  999  HOH A O   1 
HETATM 15450 O  O   . HOH AB 7 .   ? 5.004   -5.606  27.166  1.00 50.30  ?  1000 HOH A O   1 
HETATM 15451 O  O   . HOH AB 7 .   ? 3.916   -13.197 16.081  1.00 34.84  ?  1001 HOH A O   1 
HETATM 15452 O  O   . HOH AB 7 .   ? 17.878  14.861  18.448  1.00 43.68  ?  1002 HOH A O   1 
HETATM 15453 O  O   . HOH AB 7 .   ? -5.014  14.742  17.831  1.00 48.93  ?  1003 HOH A O   1 
HETATM 15454 O  O   . HOH AB 7 .   ? 13.805  18.105  27.347  1.00 50.98  ?  1004 HOH A O   1 
HETATM 15455 O  O   . HOH AB 7 .   ? 16.547  2.512   -12.841 1.00 45.43  ?  1005 HOH A O   1 
HETATM 15456 O  O   . HOH AB 7 .   ? 10.269  27.032  5.639   1.00 37.68  ?  1006 HOH A O   1 
HETATM 15457 O  O   . HOH AB 7 .   ? 3.865   16.602  -20.150 1.00 51.53  ?  1007 HOH A O   1 
HETATM 15458 O  O   . HOH AB 7 .   ? -5.302  -8.483  -1.033  1.00 38.14  ?  1008 HOH A O   1 
HETATM 15459 O  O   . HOH AB 7 .   ? 17.758  -17.870 -9.318  1.00 44.34  ?  1009 HOH A O   1 
HETATM 15460 O  O   . HOH AB 7 .   ? -11.136 -10.104 2.956   1.00 52.71  ?  1010 HOH A O   1 
HETATM 15461 O  O   . HOH AB 7 .   ? 3.434   -22.751 11.563  1.00 51.10  ?  1011 HOH A O   1 
HETATM 15462 O  O   . HOH AB 7 .   ? 24.389  6.346   0.480   1.00 48.35  ?  1012 HOH A O   1 
HETATM 15463 O  O   A HOH AB 7 .   ? 11.362  -23.051 -0.123  0.53 40.01  ?  1013 HOH A O   1 
HETATM 15464 O  O   B HOH AB 7 .   ? 11.480  -21.591 1.009   0.47 34.58  ?  1013 HOH A O   1 
HETATM 15465 O  O   . HOH AB 7 .   ? 4.100   -14.160 22.730  1.00 46.93  ?  1014 HOH A O   1 
HETATM 15466 O  O   . HOH AB 7 .   ? -0.492  14.763  -12.372 1.00 45.10  ?  1015 HOH A O   1 
HETATM 15467 O  O   . HOH AB 7 .   ? -0.099  17.480  -7.178  1.00 46.24  ?  1016 HOH A O   1 
HETATM 15468 O  O   . HOH AB 7 .   ? -3.208  -9.166  28.270  1.00 51.14  ?  1017 HOH A O   1 
HETATM 15469 O  O   . HOH AB 7 .   ? -3.426  -22.214 -17.044 1.00 51.71  ?  1018 HOH A O   1 
HETATM 15470 O  O   . HOH AB 7 .   ? 8.669   21.297  -9.247  1.00 48.74  ?  1019 HOH A O   1 
HETATM 15471 O  O   . HOH AB 7 .   ? 9.564   -18.859 -21.982 1.00 56.19  ?  1020 HOH A O   1 
HETATM 15472 O  O   . HOH AB 7 .   ? 17.379  -2.162  -23.346 1.00 43.38  ?  1021 HOH A O   1 
HETATM 15473 O  O   . HOH AB 7 .   ? 6.343   11.453  -27.764 1.00 45.85  ?  1022 HOH A O   1 
HETATM 15474 O  O   . HOH AB 7 .   ? -11.668 6.020   -6.939  1.00 35.78  ?  1023 HOH A O   1 
HETATM 15475 O  O   . HOH AB 7 .   ? -14.118 8.974   -5.449  1.00 44.71  ?  1024 HOH A O   1 
HETATM 15476 O  O   . HOH AB 7 .   ? 21.362  -12.742 -1.254  1.00 54.88  ?  1025 HOH A O   1 
HETATM 15477 O  O   . HOH AB 7 .   ? 19.023  -17.421 0.136   1.00 58.66  ?  1026 HOH A O   1 
HETATM 15478 O  O   . HOH AB 7 .   ? 11.634  24.280  26.199  1.00 54.36  ?  1027 HOH A O   1 
HETATM 15479 O  O   . HOH AB 7 .   ? -24.280 0.801   8.769   1.00 42.37  ?  1028 HOH A O   1 
HETATM 15480 O  O   . HOH AB 7 .   ? -15.184 8.498   -0.265  1.00 39.30  ?  1029 HOH A O   1 
HETATM 15481 O  O   . HOH AB 7 .   ? -0.039  -3.050  27.822  1.00 48.67  ?  1030 HOH A O   1 
HETATM 15482 O  O   . HOH AB 7 .   ? 15.598  -11.919 22.992  1.00 49.52  ?  1031 HOH A O   1 
HETATM 15483 O  O   . HOH AB 7 .   ? 26.354  -7.646  -10.166 1.00 58.68  ?  1032 HOH A O   1 
HETATM 15484 O  O   . HOH AB 7 .   ? 29.036  6.055   11.637  1.00 50.40  ?  1033 HOH A O   1 
HETATM 15485 O  O   . HOH AB 7 .   ? -6.655  -7.727  -3.286  1.00 45.85  ?  1034 HOH A O   1 
HETATM 15486 O  O   . HOH AB 7 .   ? 0.280   14.660  -10.035 1.00 43.06  ?  1035 HOH A O   1 
HETATM 15487 O  O   . HOH AB 7 .   ? 12.267  -14.365 19.499  1.00 38.65  ?  1036 HOH A O   1 
HETATM 15488 O  O   . HOH AB 7 .   ? 1.100   13.840  -24.593 1.00 51.96  ?  1037 HOH A O   1 
HETATM 15489 O  O   . HOH AB 7 .   ? -14.375 -4.794  21.967  1.00 52.89  ?  1038 HOH A O   1 
HETATM 15490 O  O   . HOH AB 7 .   ? -3.424  -2.751  -35.743 1.00 50.63  ?  1039 HOH A O   1 
HETATM 15491 O  O   . HOH AB 7 .   ? -2.768  7.177   20.551  1.00 32.97  ?  1040 HOH A O   1 
HETATM 15492 O  O   . HOH AB 7 .   ? 21.958  16.399  9.252   1.00 49.66  ?  1041 HOH A O   1 
HETATM 15493 O  O   . HOH AB 7 .   ? 23.500  12.470  3.025   1.00 44.26  ?  1042 HOH A O   1 
HETATM 15494 O  O   . HOH AB 7 .   ? 2.338   -21.071 12.876  1.00 50.24  ?  1043 HOH A O   1 
HETATM 15495 O  O   . HOH AB 7 .   ? 1.449   -22.612 5.339   1.00 42.01  ?  1044 HOH A O   1 
HETATM 15496 O  O   . HOH AB 7 .   ? 11.143  -15.750 15.541  1.00 41.80  ?  1045 HOH A O   1 
HETATM 15497 O  O   . HOH AB 7 .   ? -18.278 0.112   13.406  1.00 53.74  ?  1046 HOH A O   1 
HETATM 15498 O  O   . HOH AB 7 .   ? 29.175  2.712   10.350  1.00 49.54  ?  1047 HOH A O   1 
HETATM 15499 O  O   . HOH AB 7 .   ? 0.606   1.674   -34.201 1.00 53.87  ?  1048 HOH A O   1 
HETATM 15500 O  O   . HOH AB 7 .   ? -5.515  19.519  3.203   1.00 49.56  ?  1049 HOH A O   1 
HETATM 15501 O  O   . HOH AB 7 .   ? 0.173   -13.795 -5.316  1.00 26.38  ?  1050 HOH A O   1 
HETATM 15502 O  O   . HOH AB 7 .   ? 19.002  12.033  21.598  1.00 40.47  ?  1051 HOH A O   1 
HETATM 15503 O  O   . HOH AB 7 .   ? -8.329  -7.245  -5.182  1.00 49.46  ?  1052 HOH A O   1 
HETATM 15504 O  O   . HOH AB 7 .   ? 19.591  -12.304 -2.864  1.00 56.34  ?  1053 HOH A O   1 
HETATM 15505 O  O   . HOH AB 7 .   ? -5.846  -25.047 26.739  1.00 56.68  ?  1054 HOH A O   1 
HETATM 15506 O  O   A HOH AB 7 .   ? 10.573  9.306   -28.367 0.52 42.44  ?  1055 HOH A O   1 
HETATM 15507 O  O   B HOH AB 7 .   ? 11.732  8.190   -29.110 0.48 45.24  ?  1055 HOH A O   1 
HETATM 15508 O  O   . HOH AB 7 .   ? -8.206  17.765  9.320   1.00 35.31  ?  1056 HOH A O   1 
HETATM 15509 O  O   . HOH AB 7 .   ? 12.577  -2.289  26.684  1.00 52.10  ?  1057 HOH A O   1 
HETATM 15510 O  O   . HOH AB 7 .   ? 5.971   -12.737 -33.466 1.00 55.81  ?  1058 HOH A O   1 
HETATM 15511 O  O   . HOH AB 7 .   ? -15.070 3.378   -0.221  1.00 44.00  ?  1059 HOH A O   1 
HETATM 15512 O  O   A HOH AB 7 .   ? 13.366  19.340  -14.516 0.50 40.77  ?  1060 HOH A O   1 
HETATM 15513 O  O   B HOH AB 7 .   ? 14.713  17.944  -14.315 0.50 40.77  ?  1060 HOH A O   1 
HETATM 15514 O  O   . HOH AB 7 .   ? 3.016   -14.998 13.529  1.00 38.55  ?  1061 HOH A O   1 
HETATM 15515 O  O   . HOH AB 7 .   ? 3.964   6.718   -35.486 1.00 57.42  ?  1062 HOH A O   1 
HETATM 15516 O  O   . HOH AB 7 .   ? -17.150 13.323  -2.868  1.00 53.32  ?  1063 HOH A O   1 
HETATM 15517 O  O   . HOH AB 7 .   ? -25.185 11.039  11.725  1.00 47.35  ?  1064 HOH A O   1 
HETATM 15518 O  O   . HOH AB 7 .   ? -10.569 -4.622  -10.303 1.00 40.78  ?  1065 HOH A O   1 
HETATM 15519 O  O   . HOH AB 7 .   ? -3.213  -16.260 -5.623  1.00 35.34  ?  1066 HOH A O   1 
HETATM 15520 O  O   . HOH AB 7 .   ? 8.270   22.403  11.726  1.00 43.97  ?  1067 HOH A O   1 
HETATM 15521 O  O   . HOH AB 7 .   ? 16.923  -1.043  -11.145 1.00 46.41  ?  1068 HOH A O   1 
HETATM 15522 O  O   . HOH AB 7 .   ? -20.965 6.317   16.313  1.00 35.58  ?  1069 HOH A O   1 
HETATM 15523 O  O   . HOH AB 7 .   ? 20.972  10.688  -16.986 1.00 54.67  ?  1070 HOH A O   1 
HETATM 15524 O  O   . HOH AB 7 .   ? -8.279  -9.066  1.541   1.00 31.88  ?  1071 HOH A O   1 
HETATM 15525 O  O   . HOH AB 7 .   ? -13.719 -27.077 23.838  1.00 38.33  ?  1072 HOH A O   1 
HETATM 15526 O  O   . HOH AB 7 .   ? 16.951  -7.531  23.647  1.00 57.54  ?  1073 HOH A O   1 
HETATM 15527 O  O   . HOH AB 7 .   ? 25.587  0.757   19.259  1.00 49.14  ?  1074 HOH A O   1 
HETATM 15528 O  O   . HOH AB 7 .   ? -21.077 -4.249  6.709   1.00 58.45  ?  1075 HOH A O   1 
HETATM 15529 O  O   . HOH AB 7 .   ? -23.510 12.421  12.958  1.00 46.12  ?  1076 HOH A O   1 
HETATM 15530 O  O   . HOH AB 7 .   ? 4.011   -10.012 -34.681 1.00 43.42  ?  1077 HOH A O   1 
HETATM 15531 O  O   . HOH AB 7 .   ? 27.349  -1.058  18.068  1.00 56.66  ?  1078 HOH A O   1 
HETATM 15532 O  O   . HOH AB 7 .   ? 21.238  12.492  19.764  1.00 52.94  ?  1079 HOH A O   1 
HETATM 15533 O  O   . HOH AB 7 .   ? -9.951  -0.975  -12.024 1.00 27.62  ?  1080 HOH A O   1 
HETATM 15534 O  O   . HOH AB 7 .   ? 17.007  -9.344  22.406  1.00 56.13  ?  1081 HOH A O   1 
HETATM 15535 O  O   . HOH AB 7 .   ? 3.500   15.674  -11.826 1.00 39.06  ?  1082 HOH A O   1 
HETATM 15536 O  O   . HOH AB 7 .   ? -3.725  16.178  -3.817  1.00 50.64  ?  1083 HOH A O   1 
HETATM 15537 O  O   . HOH AB 7 .   ? 0.775   -0.805  -29.878 1.00 40.13  ?  1084 HOH A O   1 
HETATM 15538 O  O   . HOH AB 7 .   ? 24.029  12.482  31.097  1.00 44.61  ?  1085 HOH A O   1 
HETATM 15539 O  O   . HOH AB 7 .   ? -12.014 -9.141  5.244   1.00 50.95  ?  1086 HOH A O   1 
HETATM 15540 O  O   . HOH AB 7 .   ? -0.068  8.067   -35.596 1.00 53.26  ?  1087 HOH A O   1 
HETATM 15541 O  O   . HOH AB 7 .   ? -10.483 15.882  13.757  1.00 47.05  ?  1088 HOH A O   1 
HETATM 15542 O  O   . HOH AB 7 .   ? -1.116  13.730  -23.237 1.00 41.95  ?  1089 HOH A O   1 
HETATM 15543 O  O   A HOH AB 7 .   ? 2.998   -19.772 18.293  0.50 43.24  ?  1090 HOH A O   1 
HETATM 15544 O  O   B HOH AB 7 .   ? 1.111   -19.769 18.839  0.50 33.13  ?  1090 HOH A O   1 
HETATM 15545 O  O   . HOH AB 7 .   ? 17.119  -16.740 18.220  1.00 46.08  ?  1091 HOH A O   1 
HETATM 15546 O  O   . HOH AB 7 .   ? 2.075   6.385   26.135  1.00 45.85  ?  1092 HOH A O   1 
HETATM 15547 O  O   . HOH AB 7 .   ? -7.506  14.106  -4.832  1.00 31.61  ?  1093 HOH A O   1 
HETATM 15548 O  O   . HOH AB 7 .   ? 7.473   -24.641 4.616   1.00 47.19  ?  1094 HOH A O   1 
HETATM 15549 O  O   . HOH AB 7 .   ? -23.058 5.125   0.666   1.00 45.53  ?  1095 HOH A O   1 
HETATM 15550 O  O   . HOH AB 7 .   ? -1.012  20.214  2.233   1.00 36.60  ?  1096 HOH A O   1 
HETATM 15551 O  O   . HOH AB 7 .   ? 21.910  -9.998  -17.581 1.00 55.31  ?  1097 HOH A O   1 
HETATM 15552 O  O   . HOH AB 7 .   ? -3.691  13.531  -5.872  1.00 42.39  ?  1098 HOH A O   1 
HETATM 15553 O  O   . HOH AB 7 .   ? -11.318 7.624   -11.107 1.00 42.50  ?  1099 HOH A O   1 
HETATM 15554 O  O   . HOH AB 7 .   ? -3.061  15.361  -12.139 1.00 48.49  ?  1100 HOH A O   1 
HETATM 15555 O  O   . HOH AB 7 .   ? 18.228  19.446  17.537  1.00 51.88  ?  1101 HOH A O   1 
HETATM 15556 O  O   . HOH AB 7 .   ? -21.983 2.959   14.858  1.00 55.45  ?  1102 HOH A O   1 
HETATM 15557 O  O   . HOH AB 7 .   ? -15.164 0.623   -6.005  1.00 52.07  ?  1103 HOH A O   1 
HETATM 15558 O  O   . HOH AB 7 .   ? -2.807  11.832  -22.459 1.00 36.48  ?  1104 HOH A O   1 
HETATM 15559 O  O   . HOH AB 7 .   ? 13.233  -15.545 17.652  1.00 40.84  ?  1105 HOH A O   1 
HETATM 15560 O  O   . HOH AB 7 .   ? -1.247  -13.879 -38.361 1.00 48.54  ?  1106 HOH A O   1 
HETATM 15561 O  O   . HOH AB 7 .   ? -0.677  15.244  -7.993  1.00 42.15  ?  1107 HOH A O   1 
HETATM 15562 O  O   . HOH AB 7 .   ? 11.260  26.297  7.888   1.00 46.04  ?  1108 HOH A O   1 
HETATM 15563 O  O   . HOH AB 7 .   ? -11.617 2.917   -9.179  1.00 40.56  ?  1109 HOH A O   1 
HETATM 15564 O  O   . HOH AB 7 .   ? 1.427   21.563  1.823   1.00 34.98  ?  1110 HOH A O   1 
HETATM 15565 O  O   . HOH AB 7 .   ? -19.187 2.110   17.071  1.00 38.81  ?  1111 HOH A O   1 
HETATM 15566 O  O   . HOH AB 7 .   ? -8.471  11.975  -13.586 1.00 55.06  ?  1112 HOH A O   1 
HETATM 15567 O  O   . HOH AB 7 .   ? -3.295  -14.828 24.984  1.00 39.08  ?  1113 HOH A O   1 
HETATM 15568 O  O   . HOH AB 7 .   ? -7.285  -13.012 -44.478 1.00 55.08  ?  1114 HOH A O   1 
HETATM 15569 O  O   . HOH AB 7 .   ? -10.614 0.357   23.263  1.00 42.75  ?  1115 HOH A O   1 
HETATM 15570 O  O   . HOH AB 7 .   ? -6.794  14.572  -10.808 1.00 51.79  ?  1116 HOH A O   1 
HETATM 15571 O  O   A HOH AB 7 .   ? -10.764 3.963   -12.678 0.44 31.84  ?  1117 HOH A O   1 
HETATM 15572 O  O   B HOH AB 7 .   ? -12.482 4.511   -13.029 0.56 35.24  ?  1117 HOH A O   1 
HETATM 15573 O  O   . HOH AB 7 .   ? 17.144  -18.345 1.198   1.00 48.56  ?  1118 HOH A O   1 
HETATM 15574 O  O   . HOH AB 7 .   ? -4.291  -31.958 12.220  1.00 56.12  ?  1119 HOH A O   1 
HETATM 15575 O  O   . HOH AB 7 .   ? 24.500  4.605   -1.282  1.00 53.61  ?  1120 HOH A O   1 
HETATM 15576 O  O   . HOH AB 7 .   ? -9.851  17.607  11.880  1.00 38.79  ?  1121 HOH A O   1 
HETATM 15577 O  O   . HOH AB 7 .   ? 13.045  -17.532 -13.783 1.00 52.89  ?  1122 HOH A O   1 
HETATM 15578 O  O   . HOH AB 7 .   ? -18.721 6.518   1.497   1.00 44.00  ?  1123 HOH A O   1 
HETATM 15579 O  O   . HOH AB 7 .   ? 15.425  27.169  12.313  1.00 58.95  ?  1124 HOH A O   1 
HETATM 15580 O  O   . HOH AB 7 .   ? -3.622  14.822  -8.675  1.00 54.25  ?  1125 HOH A O   1 
HETATM 15581 O  O   . HOH BB 7 .   ? -9.112  7.772   -42.638 1.00 25.57  ?  701  HOH B O   1 
HETATM 15582 O  O   . HOH BB 7 .   ? -29.250 18.089  -35.642 1.00 44.80  ?  702  HOH B O   1 
HETATM 15583 O  O   . HOH BB 7 .   ? 7.647   -23.809 -3.887  1.00 48.73  ?  703  HOH B O   1 
HETATM 15584 O  O   . HOH BB 7 .   ? -17.905 17.810  -47.947 1.00 52.25  ?  704  HOH B O   1 
HETATM 15585 O  O   . HOH BB 7 .   ? -47.709 0.519   -36.981 1.00 38.73  ?  705  HOH B O   1 
HETATM 15586 O  O   . HOH BB 7 .   ? 1.200   -19.598 -28.323 1.00 45.50  ?  706  HOH B O   1 
HETATM 15587 O  O   . HOH BB 7 .   ? -23.615 -28.426 -22.018 1.00 49.13  ?  707  HOH B O   1 
HETATM 15588 O  O   . HOH BB 7 .   ? 1.812   -15.853 -35.517 1.00 46.34  ?  708  HOH B O   1 
HETATM 15589 O  O   . HOH BB 7 .   ? -36.996 -21.515 -14.063 1.00 46.48  ?  709  HOH B O   1 
HETATM 15590 O  O   . HOH BB 7 .   ? -48.818 -6.234  -14.087 1.00 48.49  ?  710  HOH B O   1 
HETATM 15591 O  O   . HOH BB 7 .   ? -34.833 8.113   -45.373 1.00 40.66  ?  711  HOH B O   1 
HETATM 15592 O  O   . HOH BB 7 .   ? -12.213 2.248   -38.408 1.00 41.74  ?  712  HOH B O   1 
HETATM 15593 O  O   . HOH BB 7 .   ? -23.789 -13.483 -14.357 1.00 33.44  ?  713  HOH B O   1 
HETATM 15594 O  O   . HOH BB 7 .   ? -43.113 -15.416 -18.874 1.00 42.14  ?  714  HOH B O   1 
HETATM 15595 O  O   . HOH BB 7 .   ? -21.276 7.831   -6.326  1.00 49.09  ?  715  HOH B O   1 
HETATM 15596 O  O   . HOH BB 7 .   ? -36.819 -11.361 -46.036 1.00 48.61  ?  716  HOH B O   1 
HETATM 15597 O  O   . HOH BB 7 .   ? -28.290 -22.928 -28.157 1.00 39.97  ?  717  HOH B O   1 
HETATM 15598 O  O   . HOH BB 7 .   ? -31.744 -0.159  -11.336 1.00 39.01  ?  718  HOH B O   1 
HETATM 15599 O  O   . HOH BB 7 .   ? -29.558 -15.297 -43.124 1.00 44.05  ?  719  HOH B O   1 
HETATM 15600 O  O   . HOH BB 7 .   ? -19.507 -0.787  -5.717  1.00 38.86  ?  720  HOH B O   1 
HETATM 15601 O  O   . HOH BB 7 .   ? -10.922 -26.703 -23.214 1.00 42.60  ?  721  HOH B O   1 
HETATM 15602 O  O   . HOH BB 7 .   ? -7.064  14.906  -50.991 1.00 42.31  ?  722  HOH B O   1 
HETATM 15603 O  O   . HOH BB 7 .   ? -30.202 -23.323 -24.423 1.00 46.68  ?  723  HOH B O   1 
HETATM 15604 O  O   . HOH BB 7 .   ? -44.079 9.532   -14.089 1.00 53.17  ?  724  HOH B O   1 
HETATM 15605 O  O   . HOH BB 7 .   ? -7.872  -24.758 -29.131 1.00 39.90  ?  725  HOH B O   1 
HETATM 15606 O  O   A HOH BB 7 .   ? -15.718 7.786   -16.493 0.44 25.65  ?  726  HOH B O   1 
HETATM 15607 O  O   B HOH BB 7 .   ? -16.193 9.770   -15.903 0.56 30.88  ?  726  HOH B O   1 
HETATM 15608 O  O   . HOH BB 7 .   ? -26.708 7.022   -8.215  1.00 38.84  ?  727  HOH B O   1 
HETATM 15609 O  O   . HOH BB 7 .   ? -27.935 -13.839 -46.221 1.00 43.08  ?  728  HOH B O   1 
HETATM 15610 O  O   . HOH BB 7 .   ? -23.487 14.507  -9.480  1.00 45.43  ?  729  HOH B O   1 
HETATM 15611 O  O   . HOH BB 7 .   ? -25.485 -12.790 -19.488 1.00 28.12  ?  730  HOH B O   1 
HETATM 15612 O  O   . HOH BB 7 .   ? -52.105 5.164   -45.550 1.00 46.26  ?  731  HOH B O   1 
HETATM 15613 O  O   . HOH BB 7 .   ? -22.312 0.600   -46.299 1.00 34.94  ?  732  HOH B O   1 
HETATM 15614 O  O   . HOH BB 7 .   ? -26.462 0.631   -30.574 1.00 21.22  ?  733  HOH B O   1 
HETATM 15615 O  O   . HOH BB 7 .   ? -11.183 -24.346 -2.253  1.00 47.75  ?  734  HOH B O   1 
HETATM 15616 O  O   . HOH BB 7 .   ? -28.715 -18.038 -19.585 1.00 33.51  ?  735  HOH B O   1 
HETATM 15617 O  O   . HOH BB 7 .   ? -19.037 -10.822 -32.817 1.00 30.69  ?  736  HOH B O   1 
HETATM 15618 O  O   . HOH BB 7 .   ? -42.328 -6.111  -10.794 1.00 39.90  ?  737  HOH B O   1 
HETATM 15619 O  O   . HOH BB 7 .   ? -26.870 3.079   -10.666 1.00 33.54  ?  738  HOH B O   1 
HETATM 15620 O  O   . HOH BB 7 .   ? -8.584  -14.340 -26.592 1.00 35.09  ?  739  HOH B O   1 
HETATM 15621 O  O   . HOH BB 7 .   ? -18.792 4.019   -22.452 1.00 21.76  ?  740  HOH B O   1 
HETATM 15622 O  O   . HOH BB 7 .   ? -39.729 -16.788 -7.201  1.00 44.87  ?  741  HOH B O   1 
HETATM 15623 O  O   . HOH BB 7 .   ? -9.113  -9.381  -36.249 1.00 33.15  ?  742  HOH B O   1 
HETATM 15624 O  O   . HOH BB 7 .   ? -17.356 -8.369  -42.548 1.00 27.05  ?  743  HOH B O   1 
HETATM 15625 O  O   . HOH BB 7 .   ? -32.752 12.701  -15.779 1.00 30.93  ?  744  HOH B O   1 
HETATM 15626 O  O   . HOH BB 7 .   ? -45.796 -16.661 -15.808 1.00 51.23  ?  745  HOH B O   1 
HETATM 15627 O  O   . HOH BB 7 .   ? -8.807  5.411   -51.657 1.00 40.49  ?  746  HOH B O   1 
HETATM 15628 O  O   . HOH BB 7 .   ? -41.064 11.788  -15.435 1.00 47.62  ?  747  HOH B O   1 
HETATM 15629 O  O   . HOH BB 7 .   ? -12.065 -3.602  -14.164 1.00 27.56  ?  748  HOH B O   1 
HETATM 15630 O  O   . HOH BB 7 .   ? -20.225 -5.329  -9.366  1.00 22.80  ?  749  HOH B O   1 
HETATM 15631 O  O   . HOH BB 7 .   ? -15.494 -3.307  -43.972 1.00 32.40  ?  750  HOH B O   1 
HETATM 15632 O  O   . HOH BB 7 .   ? -20.509 -13.789 -22.482 1.00 23.83  ?  751  HOH B O   1 
HETATM 15633 O  O   . HOH BB 7 .   ? -20.342 14.981  -12.774 1.00 36.92  ?  752  HOH B O   1 
HETATM 15634 O  O   . HOH BB 7 .   ? -25.708 -24.441 -24.304 1.00 39.45  ?  753  HOH B O   1 
HETATM 15635 O  O   . HOH BB 7 .   ? -7.941  -11.665 -6.472  1.00 39.23  ?  754  HOH B O   1 
HETATM 15636 O  O   . HOH BB 7 .   ? -12.545 9.912   -19.778 1.00 43.51  ?  755  HOH B O   1 
HETATM 15637 O  O   . HOH BB 7 .   ? -26.380 -24.090 -6.363  1.00 48.05  ?  756  HOH B O   1 
HETATM 15638 O  O   . HOH BB 7 .   ? -24.942 -12.188 -50.665 1.00 38.70  ?  757  HOH B O   1 
HETATM 15639 O  O   . HOH BB 7 .   ? -12.691 8.655   -35.013 1.00 40.56  ?  758  HOH B O   1 
HETATM 15640 O  O   . HOH BB 7 .   ? -33.374 -16.694 -26.810 1.00 30.31  ?  759  HOH B O   1 
HETATM 15641 O  O   . HOH BB 7 .   ? -32.125 -6.456  -8.910  1.00 33.57  ?  760  HOH B O   1 
HETATM 15642 O  O   . HOH BB 7 .   ? -34.446 16.356  -38.559 1.00 39.47  ?  761  HOH B O   1 
HETATM 15643 O  O   . HOH BB 7 .   ? -16.932 3.801   -25.854 1.00 27.18  ?  762  HOH B O   1 
HETATM 15644 O  O   . HOH BB 7 .   ? -26.665 -9.220  -25.694 1.00 24.53  ?  763  HOH B O   1 
HETATM 15645 O  O   . HOH BB 7 .   ? -27.096 -24.186 -17.384 1.00 43.33  ?  764  HOH B O   1 
HETATM 15646 O  O   . HOH BB 7 .   ? -9.149  -25.610 -0.830  1.00 50.65  ?  765  HOH B O   1 
HETATM 15647 O  O   . HOH BB 7 .   ? -41.011 2.154   -13.070 1.00 29.24  ?  766  HOH B O   1 
HETATM 15648 O  O   . HOH BB 7 .   ? -26.269 -3.606  -34.020 1.00 24.64  ?  767  HOH B O   1 
HETATM 15649 O  O   . HOH BB 7 .   ? -13.779 8.407   -18.054 1.00 34.12  ?  768  HOH B O   1 
HETATM 15650 O  O   . HOH BB 7 .   ? -14.228 -1.272  -35.342 1.00 29.35  ?  769  HOH B O   1 
HETATM 15651 O  O   A HOH BB 7 .   ? -30.681 -22.243 -34.101 0.74 28.53  ?  770  HOH B O   1 
HETATM 15652 O  O   B HOH BB 7 .   ? -29.974 -24.034 -34.384 0.26 35.84  ?  770  HOH B O   1 
HETATM 15653 O  O   . HOH BB 7 .   ? -14.939 13.118  -38.478 1.00 32.83  ?  771  HOH B O   1 
HETATM 15654 O  O   . HOH BB 7 .   ? -32.916 17.124  -35.683 1.00 40.65  ?  772  HOH B O   1 
HETATM 15655 O  O   . HOH BB 7 .   ? -20.123 2.791   -32.012 1.00 27.04  ?  773  HOH B O   1 
HETATM 15656 O  O   . HOH BB 7 .   ? 1.439   -16.728 -28.485 1.00 38.63  ?  774  HOH B O   1 
HETATM 15657 O  O   . HOH BB 7 .   ? 1.874   -20.479 0.144   1.00 31.15  ?  775  HOH B O   1 
HETATM 15658 O  O   . HOH BB 7 .   ? -43.035 -5.015  -44.592 1.00 44.44  ?  776  HOH B O   1 
HETATM 15659 O  O   . HOH BB 7 .   ? -31.170 9.634   -10.806 1.00 39.98  ?  777  HOH B O   1 
HETATM 15660 O  O   . HOH BB 7 .   ? -43.720 -8.040  -43.435 1.00 38.51  ?  778  HOH B O   1 
HETATM 15661 O  O   . HOH BB 7 .   ? -38.764 13.093  -16.778 1.00 39.26  ?  779  HOH B O   1 
HETATM 15662 O  O   . HOH BB 7 .   ? -7.732  -25.553 -24.798 1.00 40.49  ?  780  HOH B O   1 
HETATM 15663 O  O   . HOH BB 7 .   ? -34.419 1.951   -41.264 1.00 30.05  ?  781  HOH B O   1 
HETATM 15664 O  O   . HOH BB 7 .   ? -24.809 -15.169 -30.937 1.00 29.14  ?  782  HOH B O   1 
HETATM 15665 O  O   . HOH BB 7 .   ? -38.778 -5.755  -48.015 1.00 50.74  ?  783  HOH B O   1 
HETATM 15666 O  O   . HOH BB 7 .   ? -35.326 11.462  -43.692 1.00 38.75  ?  784  HOH B O   1 
HETATM 15667 O  O   . HOH BB 7 .   ? -31.652 -16.846 -11.569 1.00 29.89  ?  785  HOH B O   1 
HETATM 15668 O  O   . HOH BB 7 .   ? -11.809 14.635  -19.190 1.00 35.80  ?  786  HOH B O   1 
HETATM 15669 O  O   . HOH BB 7 .   ? -26.043 7.818   -32.083 1.00 23.97  ?  787  HOH B O   1 
HETATM 15670 O  O   . HOH BB 7 .   ? -34.202 -20.972 -23.049 1.00 48.09  ?  788  HOH B O   1 
HETATM 15671 O  O   . HOH BB 7 .   ? -18.417 -0.892  -45.346 1.00 44.56  ?  789  HOH B O   1 
HETATM 15672 O  O   . HOH BB 7 .   ? -14.842 -23.189 -27.804 1.00 32.22  ?  790  HOH B O   1 
HETATM 15673 O  O   . HOH BB 7 .   ? -37.327 -19.853 -25.143 1.00 38.73  ?  791  HOH B O   1 
HETATM 15674 O  O   . HOH BB 7 .   ? -30.387 12.678  -13.818 1.00 40.02  ?  792  HOH B O   1 
HETATM 15675 O  O   . HOH BB 7 .   ? -29.399 14.748  -47.750 1.00 44.88  ?  793  HOH B O   1 
HETATM 15676 O  O   . HOH BB 7 .   ? -35.211 4.900   -43.144 1.00 37.38  ?  794  HOH B O   1 
HETATM 15677 O  O   . HOH BB 7 .   ? -32.552 -0.505  -15.346 1.00 23.21  ?  795  HOH B O   1 
HETATM 15678 O  O   . HOH BB 7 .   ? -31.520 13.219  -31.389 1.00 30.02  ?  796  HOH B O   1 
HETATM 15679 O  O   . HOH BB 7 .   ? -24.549 -11.590 -12.830 1.00 27.04  ?  797  HOH B O   1 
HETATM 15680 O  O   . HOH BB 7 .   ? -17.430 1.355   -38.662 1.00 29.91  ?  798  HOH B O   1 
HETATM 15681 O  O   . HOH BB 7 .   ? -17.202 13.850  -36.561 1.00 27.71  ?  799  HOH B O   1 
HETATM 15682 O  O   . HOH BB 7 .   ? -42.943 -21.581 -33.208 1.00 51.33  ?  800  HOH B O   1 
HETATM 15683 O  O   . HOH BB 7 .   ? -15.736 -1.491  -37.699 1.00 28.69  ?  801  HOH B O   1 
HETATM 15684 O  O   . HOH BB 7 .   ? -13.162 -30.494 -5.067  1.00 60.95  ?  802  HOH B O   1 
HETATM 15685 O  O   . HOH BB 7 .   ? -3.581  -18.556 -7.225  1.00 31.92  ?  803  HOH B O   1 
HETATM 15686 O  O   . HOH BB 7 .   ? -4.327  -13.726 -5.534  1.00 33.19  ?  804  HOH B O   1 
HETATM 15687 O  O   . HOH BB 7 .   ? -17.409 -4.664  -40.084 1.00 30.93  ?  805  HOH B O   1 
HETATM 15688 O  O   . HOH BB 7 .   ? -22.650 -1.640  -16.469 1.00 21.66  ?  806  HOH B O   1 
HETATM 15689 O  O   . HOH BB 7 .   ? -25.055 11.505  -29.362 1.00 26.11  ?  807  HOH B O   1 
HETATM 15690 O  O   . HOH BB 7 .   ? -8.620  -10.488 -28.169 1.00 28.05  ?  808  HOH B O   1 
HETATM 15691 O  O   . HOH BB 7 .   ? -33.862 -15.563 -11.030 1.00 32.21  ?  809  HOH B O   1 
HETATM 15692 O  O   . HOH BB 7 .   ? -18.956 1.546   -8.961  1.00 29.19  ?  810  HOH B O   1 
HETATM 15693 O  O   . HOH BB 7 .   ? -9.636  -18.701 -16.871 1.00 31.39  ?  811  HOH B O   1 
HETATM 15694 O  O   . HOH BB 7 .   ? -25.471 -10.395 -40.287 1.00 28.70  ?  812  HOH B O   1 
HETATM 15695 O  O   . HOH BB 7 .   ? -45.264 2.778   -25.820 1.00 31.89  ?  813  HOH B O   1 
HETATM 15696 O  O   . HOH BB 7 .   ? -12.471 -4.979  -19.854 1.00 25.01  ?  814  HOH B O   1 
HETATM 15697 O  O   . HOH BB 7 .   ? -12.683 17.102  -48.584 1.00 37.65  ?  815  HOH B O   1 
HETATM 15698 O  O   . HOH BB 7 .   ? -17.347 0.561   -12.232 1.00 24.27  ?  816  HOH B O   1 
HETATM 15699 O  O   . HOH BB 7 .   ? -17.954 18.970  -12.253 1.00 46.37  ?  817  HOH B O   1 
HETATM 15700 O  O   . HOH BB 7 .   ? -12.468 -11.361 -26.131 1.00 25.03  ?  818  HOH B O   1 
HETATM 15701 O  O   . HOH BB 7 .   ? -35.711 4.563   -10.723 1.00 34.10  ?  819  HOH B O   1 
HETATM 15702 O  O   . HOH BB 7 .   ? -26.591 -20.749 -5.929  1.00 39.82  ?  820  HOH B O   1 
HETATM 15703 O  O   . HOH BB 7 .   ? -24.769 16.183  -28.681 1.00 30.61  ?  821  HOH B O   1 
HETATM 15704 O  O   . HOH BB 7 .   ? -49.768 1.484   -18.328 1.00 40.71  ?  822  HOH B O   1 
HETATM 15705 O  O   . HOH BB 7 .   ? -13.730 22.406  -16.987 1.00 52.67  ?  823  HOH B O   1 
HETATM 15706 O  O   . HOH BB 7 .   ? -17.245 -2.434  -6.076  1.00 32.44  ?  824  HOH B O   1 
HETATM 15707 O  O   . HOH BB 7 .   ? -40.090 16.331  -27.391 1.00 47.48  ?  825  HOH B O   1 
HETATM 15708 O  O   . HOH BB 7 .   ? -19.908 -5.568  -39.461 1.00 29.16  ?  826  HOH B O   1 
HETATM 15709 O  O   . HOH BB 7 .   ? -29.305 -3.721  -49.593 1.00 36.09  ?  827  HOH B O   1 
HETATM 15710 O  O   . HOH BB 7 .   ? -38.174 -17.241 -41.040 1.00 40.00  ?  828  HOH B O   1 
HETATM 15711 O  O   . HOH BB 7 .   ? -35.808 -2.277  -6.969  1.00 34.99  ?  829  HOH B O   1 
HETATM 15712 O  O   . HOH BB 7 .   ? -33.837 -10.177 -7.111  1.00 41.37  ?  830  HOH B O   1 
HETATM 15713 O  O   . HOH BB 7 .   ? -39.016 3.456   -9.275  1.00 48.40  ?  831  HOH B O   1 
HETATM 15714 O  O   . HOH BB 7 .   ? -31.713 -7.298  -50.500 1.00 47.73  ?  832  HOH B O   1 
HETATM 15715 O  O   . HOH BB 7 .   ? -40.676 10.477  -23.068 1.00 28.32  ?  833  HOH B O   1 
HETATM 15716 O  O   . HOH BB 7 .   ? -14.900 -16.591 1.903   1.00 43.72  ?  834  HOH B O   1 
HETATM 15717 O  O   . HOH BB 7 .   ? -16.683 -27.057 -25.489 1.00 49.31  ?  835  HOH B O   1 
HETATM 15718 O  O   . HOH BB 7 .   ? -51.588 2.106   -29.879 1.00 33.04  ?  836  HOH B O   1 
HETATM 15719 O  O   . HOH BB 7 .   ? -11.838 -10.172 -35.818 1.00 29.66  ?  837  HOH B O   1 
HETATM 15720 O  O   . HOH BB 7 .   ? -9.285  -9.885  -16.954 1.00 24.97  ?  838  HOH B O   1 
HETATM 15721 O  O   . HOH BB 7 .   ? -41.523 -7.560  -45.844 1.00 44.18  ?  839  HOH B O   1 
HETATM 15722 O  O   . HOH BB 7 .   ? -34.494 15.518  -23.816 1.00 32.97  ?  840  HOH B O   1 
HETATM 15723 O  O   . HOH BB 7 .   ? -30.307 -3.561  -14.684 1.00 23.63  ?  841  HOH B O   1 
HETATM 15724 O  O   . HOH BB 7 .   ? -18.923 0.945   -40.507 1.00 33.87  ?  842  HOH B O   1 
HETATM 15725 O  O   . HOH BB 7 .   ? -56.885 2.639   -45.914 1.00 46.77  ?  843  HOH B O   1 
HETATM 15726 O  O   . HOH BB 7 .   ? -10.492 -14.732 -15.138 1.00 24.76  ?  844  HOH B O   1 
HETATM 15727 O  O   . HOH BB 7 .   ? -16.733 -11.315 -45.211 1.00 32.77  ?  845  HOH B O   1 
HETATM 15728 O  O   . HOH BB 7 .   ? -20.549 -16.624 -41.125 1.00 37.81  ?  846  HOH B O   1 
HETATM 15729 O  O   . HOH BB 7 .   ? -34.392 17.087  -30.883 1.00 40.44  ?  847  HOH B O   1 
HETATM 15730 O  O   . HOH BB 7 .   ? -27.493 -13.759 -20.704 1.00 27.45  ?  848  HOH B O   1 
HETATM 15731 O  O   . HOH BB 7 .   ? -44.207 -12.391 -25.299 1.00 43.15  ?  849  HOH B O   1 
HETATM 15732 O  O   . HOH BB 7 .   ? -19.084 3.077   -41.748 1.00 35.63  ?  850  HOH B O   1 
HETATM 15733 O  O   . HOH BB 7 .   ? -17.912 -22.609 -35.167 1.00 46.73  ?  851  HOH B O   1 
HETATM 15734 O  O   . HOH BB 7 .   ? -43.487 13.787  -35.751 1.00 49.50  ?  852  HOH B O   1 
HETATM 15735 O  O   . HOH BB 7 .   ? -20.817 -11.165 -1.226  1.00 26.86  ?  853  HOH B O   1 
HETATM 15736 O  O   . HOH BB 7 .   ? -55.402 -1.665  -21.331 1.00 41.02  ?  854  HOH B O   1 
HETATM 15737 O  O   . HOH BB 7 .   ? -8.550  -2.899  -31.279 1.00 46.58  ?  855  HOH B O   1 
HETATM 15738 O  O   . HOH BB 7 .   ? -34.345 -7.024  -13.620 1.00 26.52  ?  856  HOH B O   1 
HETATM 15739 O  O   . HOH BB 7 .   ? -17.838 3.197   -13.027 1.00 27.64  ?  857  HOH B O   1 
HETATM 15740 O  O   A HOH BB 7 .   ? -20.475 -17.100 -49.298 0.50 51.83  ?  858  HOH B O   1 
HETATM 15741 O  O   B HOH BB 7 .   ? -19.717 -17.454 -50.819 0.50 51.83  ?  858  HOH B O   1 
HETATM 15742 O  O   . HOH BB 7 .   ? -43.139 -13.463 -7.308  1.00 46.73  ?  859  HOH B O   1 
HETATM 15743 O  O   . HOH BB 7 .   ? -46.089 0.810   -19.750 1.00 30.53  ?  860  HOH B O   1 
HETATM 15744 O  O   . HOH BB 7 .   ? -49.160 -7.439  -41.606 1.00 45.30  ?  861  HOH B O   1 
HETATM 15745 O  O   . HOH BB 7 .   ? -32.976 2.215   -10.821 1.00 41.65  ?  862  HOH B O   1 
HETATM 15746 O  O   . HOH BB 7 .   ? -14.681 -3.593  -34.429 1.00 30.06  ?  863  HOH B O   1 
HETATM 15747 O  O   . HOH BB 7 .   ? -25.302 -26.042 -17.237 1.00 46.62  ?  864  HOH B O   1 
HETATM 15748 O  O   . HOH BB 7 .   ? -41.729 2.175   -8.109  1.00 41.91  ?  865  HOH B O   1 
HETATM 15749 O  O   . HOH BB 7 .   ? -26.147 -25.240 -1.976  1.00 60.60  ?  866  HOH B O   1 
HETATM 15750 O  O   . HOH BB 7 .   ? -23.439 -6.357  -44.665 1.00 30.02  ?  867  HOH B O   1 
HETATM 15751 O  O   . HOH BB 7 .   ? -4.155  -14.068 -11.899 1.00 25.47  ?  868  HOH B O   1 
HETATM 15752 O  O   . HOH BB 7 .   ? -28.562 -19.656 -6.186  1.00 40.72  ?  869  HOH B O   1 
HETATM 15753 O  O   . HOH BB 7 .   ? -13.162 12.274  -53.368 1.00 41.72  ?  870  HOH B O   1 
HETATM 15754 O  O   . HOH BB 7 .   ? -23.275 17.180  -45.099 1.00 44.41  ?  871  HOH B O   1 
HETATM 15755 O  O   . HOH BB 7 .   ? -32.777 -11.761 -27.983 1.00 27.25  ?  872  HOH B O   1 
HETATM 15756 O  O   . HOH BB 7 .   ? -10.397 -13.412 -6.220  1.00 30.04  ?  873  HOH B O   1 
HETATM 15757 O  O   . HOH BB 7 .   ? -17.765 6.002   -24.500 1.00 25.57  ?  874  HOH B O   1 
HETATM 15758 O  O   . HOH BB 7 .   ? -30.076 11.417  -44.977 1.00 34.65  ?  875  HOH B O   1 
HETATM 15759 O  O   . HOH BB 7 .   ? -47.138 -4.683  -15.275 1.00 41.41  ?  876  HOH B O   1 
HETATM 15760 O  O   . HOH BB 7 .   ? -16.617 -19.745 -28.815 1.00 30.96  ?  877  HOH B O   1 
HETATM 15761 O  O   . HOH BB 7 .   ? -35.374 -14.388 -12.952 1.00 30.93  ?  878  HOH B O   1 
HETATM 15762 O  O   A HOH BB 7 .   ? -37.928 4.181   -46.683 0.53 32.21  ?  879  HOH B O   1 
HETATM 15763 O  O   B HOH BB 7 .   ? -37.071 4.525   -45.055 0.47 32.21  ?  879  HOH B O   1 
HETATM 15764 O  O   . HOH BB 7 .   ? -26.927 -7.558  -49.493 1.00 37.56  ?  880  HOH B O   1 
HETATM 15765 O  O   . HOH BB 7 .   ? -13.026 13.602  -31.897 1.00 38.17  ?  881  HOH B O   1 
HETATM 15766 O  O   . HOH BB 7 .   ? -11.710 -19.148 -4.322  1.00 33.73  ?  882  HOH B O   1 
HETATM 15767 O  O   . HOH BB 7 .   ? -19.223 -10.630 -51.851 1.00 46.40  ?  883  HOH B O   1 
HETATM 15768 O  O   . HOH BB 7 .   ? -12.680 13.507  -39.514 1.00 41.66  ?  884  HOH B O   1 
HETATM 15769 O  O   . HOH BB 7 .   ? -13.121 -9.074  -29.636 1.00 27.39  ?  885  HOH B O   1 
HETATM 15770 O  O   A HOH BB 7 .   ? -34.159 -14.618 -6.939  0.50 42.30  ?  886  HOH B O   1 
HETATM 15771 O  O   B HOH BB 7 .   ? -34.344 -15.519 -4.831  0.50 42.30  ?  886  HOH B O   1 
HETATM 15772 O  O   . HOH BB 7 .   ? -34.621 -10.332 -45.451 1.00 37.93  ?  887  HOH B O   1 
HETATM 15773 O  O   . HOH BB 7 .   ? -4.230  -17.582 -3.592  1.00 31.74  ?  888  HOH B O   1 
HETATM 15774 O  O   . HOH BB 7 .   ? -29.994 -21.020 -18.141 1.00 44.55  ?  889  HOH B O   1 
HETATM 15775 O  O   . HOH BB 7 .   ? -23.699 9.257   -48.048 1.00 35.65  ?  890  HOH B O   1 
HETATM 15776 O  O   . HOH BB 7 .   ? -36.415 12.926  -14.928 1.00 43.59  ?  891  HOH B O   1 
HETATM 15777 O  O   . HOH BB 7 .   ? -1.947  -13.581 -8.572  1.00 28.55  ?  892  HOH B O   1 
HETATM 15778 O  O   . HOH BB 7 .   ? -6.403  -21.651 -13.775 1.00 32.82  ?  893  HOH B O   1 
HETATM 15779 O  O   . HOH BB 7 .   ? -39.959 -19.120 -23.192 1.00 42.37  ?  894  HOH B O   1 
HETATM 15780 O  O   . HOH BB 7 .   ? -24.927 -20.820 -35.603 1.00 39.84  ?  895  HOH B O   1 
HETATM 15781 O  O   . HOH BB 7 .   ? -12.999 -5.291  -23.638 1.00 31.90  ?  896  HOH B O   1 
HETATM 15782 O  O   . HOH BB 7 .   ? -33.403 -18.474 -8.052  1.00 38.37  ?  897  HOH B O   1 
HETATM 15783 O  O   . HOH BB 7 .   ? -36.561 -7.401  -4.674  1.00 45.28  ?  898  HOH B O   1 
HETATM 15784 O  O   . HOH BB 7 .   ? -33.263 -20.979 -37.982 1.00 43.95  ?  899  HOH B O   1 
HETATM 15785 O  O   . HOH BB 7 .   ? -47.974 8.361   -41.632 1.00 38.48  ?  900  HOH B O   1 
HETATM 15786 O  O   . HOH BB 7 .   ? -29.451 20.184  -29.862 1.00 40.30  ?  901  HOH B O   1 
HETATM 15787 O  O   . HOH BB 7 .   ? -23.229 -14.675 4.813   1.00 56.49  ?  902  HOH B O   1 
HETATM 15788 O  O   . HOH BB 7 .   ? -13.325 -3.891  -31.879 1.00 29.98  ?  903  HOH B O   1 
HETATM 15789 O  O   . HOH BB 7 .   ? -4.481  12.408  -55.872 1.00 42.98  ?  904  HOH B O   1 
HETATM 15790 O  O   . HOH BB 7 .   ? -16.725 -2.332  -41.540 1.00 32.45  ?  905  HOH B O   1 
HETATM 15791 O  O   A HOH BB 7 .   ? -16.584 -0.090  -48.971 0.54 42.13  ?  906  HOH B O   1 
HETATM 15792 O  O   B HOH BB 7 .   ? -16.380 1.875   -48.740 0.46 38.69  ?  906  HOH B O   1 
HETATM 15793 O  O   . HOH BB 7 .   ? -10.907 -13.088 -2.708  1.00 46.17  ?  907  HOH B O   1 
HETATM 15794 O  O   . HOH BB 7 .   ? -15.296 16.505  -29.273 1.00 44.80  ?  908  HOH B O   1 
HETATM 15795 O  O   . HOH BB 7 .   ? -39.444 -7.957  -8.846  1.00 37.49  ?  909  HOH B O   1 
HETATM 15796 O  O   . HOH BB 7 .   ? -13.325 -10.446 0.083   1.00 36.88  ?  910  HOH B O   1 
HETATM 15797 O  O   . HOH BB 7 .   ? -21.277 -4.010  -2.634  1.00 32.08  ?  911  HOH B O   1 
HETATM 15798 O  O   . HOH BB 7 .   ? -15.836 -15.020 -32.922 1.00 27.79  ?  912  HOH B O   1 
HETATM 15799 O  O   . HOH BB 7 .   ? -37.401 16.007  -27.441 1.00 34.42  ?  913  HOH B O   1 
HETATM 15800 O  O   . HOH BB 7 .   ? -15.328 1.104   -3.330  1.00 45.79  ?  914  HOH B O   1 
HETATM 15801 O  O   . HOH BB 7 .   ? -20.820 3.291   -43.317 1.00 32.75  ?  915  HOH B O   1 
HETATM 15802 O  O   . HOH BB 7 .   ? -11.412 17.937  -17.905 1.00 45.68  ?  916  HOH B O   1 
HETATM 15803 O  O   . HOH BB 7 .   ? -30.512 -16.987 -20.923 1.00 35.32  ?  917  HOH B O   1 
HETATM 15804 O  O   . HOH BB 7 .   ? -9.672  1.272   -39.892 1.00 46.28  ?  918  HOH B O   1 
HETATM 15805 O  O   . HOH BB 7 .   ? -21.283 24.632  -25.922 1.00 41.69  ?  919  HOH B O   1 
HETATM 15806 O  O   . HOH BB 7 .   ? -13.370 -0.917  -20.686 1.00 31.40  ?  920  HOH B O   1 
HETATM 15807 O  O   . HOH BB 7 .   ? -13.431 -5.694  -47.928 1.00 37.51  ?  921  HOH B O   1 
HETATM 15808 O  O   . HOH BB 7 .   ? -14.299 -0.907  -10.608 1.00 27.60  ?  922  HOH B O   1 
HETATM 15809 O  O   . HOH BB 7 .   ? -35.873 -7.440  -46.553 1.00 39.26  ?  923  HOH B O   1 
HETATM 15810 O  O   . HOH BB 7 .   ? -18.452 -7.800  -34.354 1.00 30.81  ?  924  HOH B O   1 
HETATM 15811 O  O   . HOH BB 7 .   ? -29.954 20.717  -34.668 1.00 47.08  ?  925  HOH B O   1 
HETATM 15812 O  O   . HOH BB 7 .   ? -14.744 -12.745 -25.841 1.00 25.45  ?  926  HOH B O   1 
HETATM 15813 O  O   . HOH BB 7 .   ? -28.977 -0.931  -36.869 1.00 34.66  ?  927  HOH B O   1 
HETATM 15814 O  O   . HOH BB 7 .   ? -30.243 -8.677  -6.831  1.00 30.70  ?  928  HOH B O   1 
HETATM 15815 O  O   . HOH BB 7 .   ? -3.576  -24.559 1.944   1.00 31.43  ?  929  HOH B O   1 
HETATM 15816 O  O   . HOH BB 7 .   ? -13.587 14.752  -27.202 1.00 47.17  ?  930  HOH B O   1 
HETATM 15817 O  O   . HOH BB 7 .   ? -6.134  6.363   -42.373 1.00 47.41  ?  931  HOH B O   1 
HETATM 15818 O  O   . HOH BB 7 .   ? -48.150 3.638   -18.879 1.00 40.83  ?  932  HOH B O   1 
HETATM 15819 O  O   . HOH BB 7 .   ? -24.571 -0.351  -18.282 1.00 23.50  ?  933  HOH B O   1 
HETATM 15820 O  O   . HOH BB 7 .   ? -43.463 -18.211 -26.474 1.00 52.09  ?  934  HOH B O   1 
HETATM 15821 O  O   . HOH BB 7 .   ? -10.807 -5.838  -12.971 1.00 35.82  ?  935  HOH B O   1 
HETATM 15822 O  O   . HOH BB 7 .   ? -12.116 -4.377  -46.114 1.00 45.68  ?  936  HOH B O   1 
HETATM 15823 O  O   . HOH BB 7 .   ? -42.212 13.432  -25.825 1.00 40.04  ?  937  HOH B O   1 
HETATM 15824 O  O   . HOH BB 7 .   ? -33.864 14.587  -35.185 1.00 41.28  ?  938  HOH B O   1 
HETATM 15825 O  O   A HOH BB 7 .   ? -25.760 -4.547  -2.637  0.50 35.35  ?  939  HOH B O   1 
HETATM 15826 O  O   B HOH BB 7 .   ? -24.286 -3.527  -1.354  0.50 35.35  ?  939  HOH B O   1 
HETATM 15827 O  O   . HOH BB 7 .   ? -30.053 -15.675 -13.040 1.00 37.96  ?  940  HOH B O   1 
HETATM 15828 O  O   . HOH BB 7 .   ? -21.343 -21.374 -35.934 1.00 50.82  ?  941  HOH B O   1 
HETATM 15829 O  O   . HOH BB 7 .   ? -16.158 -4.281  -37.679 1.00 30.81  ?  942  HOH B O   1 
HETATM 15830 O  O   . HOH BB 7 .   ? -15.614 -27.408 -21.309 1.00 42.16  ?  943  HOH B O   1 
HETATM 15831 O  O   . HOH BB 7 .   ? -11.750 -13.603 -9.637  1.00 27.15  ?  944  HOH B O   1 
HETATM 15832 O  O   . HOH BB 7 .   ? -42.688 -16.019 -38.719 1.00 42.30  ?  945  HOH B O   1 
HETATM 15833 O  O   . HOH BB 7 .   ? -38.565 12.246  -40.020 1.00 35.75  ?  946  HOH B O   1 
HETATM 15834 O  O   . HOH BB 7 .   ? -28.170 -7.132  -7.373  1.00 30.67  ?  947  HOH B O   1 
HETATM 15835 O  O   . HOH BB 7 .   ? -17.015 -25.637 -33.714 1.00 44.90  ?  948  HOH B O   1 
HETATM 15836 O  O   . HOH BB 7 .   ? -10.566 -20.485 -6.536  1.00 31.29  ?  949  HOH B O   1 
HETATM 15837 O  O   . HOH BB 7 .   ? -30.928 -17.430 -4.564  1.00 36.47  ?  950  HOH B O   1 
HETATM 15838 O  O   . HOH BB 7 .   ? -32.441 -12.146 -7.110  1.00 33.80  ?  951  HOH B O   1 
HETATM 15839 O  O   . HOH BB 7 .   ? -27.123 18.360  -36.486 1.00 34.99  ?  952  HOH B O   1 
HETATM 15840 O  O   . HOH BB 7 .   ? -7.923  -21.242 -18.741 1.00 44.15  ?  953  HOH B O   1 
HETATM 15841 O  O   . HOH BB 7 .   ? -36.794 16.125  -25.061 1.00 42.91  ?  954  HOH B O   1 
HETATM 15842 O  O   . HOH BB 7 .   ? -29.652 7.907   -51.969 1.00 48.93  ?  955  HOH B O   1 
HETATM 15843 O  O   . HOH BB 7 .   ? -50.468 1.937   -14.178 1.00 42.45  ?  956  HOH B O   1 
HETATM 15844 O  O   . HOH BB 7 .   ? -37.054 7.707   -13.243 1.00 43.94  ?  957  HOH B O   1 
HETATM 15845 O  O   . HOH BB 7 .   ? -42.798 -2.685  -8.671  1.00 38.05  ?  958  HOH B O   1 
HETATM 15846 O  O   . HOH BB 7 .   ? -45.386 7.340   -13.190 1.00 49.63  ?  959  HOH B O   1 
HETATM 15847 O  O   . HOH BB 7 .   ? -26.303 -21.744 -24.171 1.00 37.73  ?  960  HOH B O   1 
HETATM 15848 O  O   . HOH BB 7 .   ? -10.158 -4.824  -21.095 1.00 40.87  ?  961  HOH B O   1 
HETATM 15849 O  O   . HOH BB 7 .   ? -19.163 5.211   -32.696 1.00 23.80  ?  962  HOH B O   1 
HETATM 15850 O  O   . HOH BB 7 .   ? -18.424 10.089  -45.735 1.00 29.22  ?  963  HOH B O   1 
HETATM 15851 O  O   . HOH BB 7 .   ? -30.327 -20.992 -21.191 1.00 53.04  ?  964  HOH B O   1 
HETATM 15852 O  O   . HOH BB 7 .   ? -24.210 -1.958  -48.828 1.00 38.72  ?  965  HOH B O   1 
HETATM 15853 O  O   . HOH BB 7 .   ? 0.496   -21.372 -32.252 1.00 41.82  ?  966  HOH B O   1 
HETATM 15854 O  O   . HOH BB 7 .   ? -17.525 17.563  -29.107 1.00 30.95  ?  967  HOH B O   1 
HETATM 15855 O  O   . HOH BB 7 .   ? -51.157 -7.897  -27.314 1.00 48.98  ?  968  HOH B O   1 
HETATM 15856 O  O   . HOH BB 7 .   ? -21.075 1.008   -43.711 1.00 31.83  ?  969  HOH B O   1 
HETATM 15857 O  O   . HOH BB 7 .   ? -45.501 7.495   -21.110 1.00 45.51  ?  970  HOH B O   1 
HETATM 15858 O  O   . HOH BB 7 .   ? -41.870 -17.514 -27.959 1.00 45.65  ?  971  HOH B O   1 
HETATM 15859 O  O   . HOH BB 7 .   ? -12.670 -9.834  -38.393 1.00 31.86  ?  972  HOH B O   1 
HETATM 15860 O  O   . HOH BB 7 .   ? -34.779 -23.600 -28.207 1.00 48.15  ?  973  HOH B O   1 
HETATM 15861 O  O   . HOH BB 7 .   ? -9.399  2.992   -48.346 1.00 40.61  ?  974  HOH B O   1 
HETATM 15862 O  O   . HOH BB 7 .   ? -41.722 -15.924 -8.681  1.00 40.38  ?  975  HOH B O   1 
HETATM 15863 O  O   . HOH BB 7 .   ? -49.005 -10.468 -23.399 1.00 50.18  ?  976  HOH B O   1 
HETATM 15864 O  O   . HOH BB 7 .   ? -9.955  9.187   -40.046 1.00 39.79  ?  977  HOH B O   1 
HETATM 15865 O  O   . HOH BB 7 .   ? -17.238 -28.179 -9.250  1.00 46.83  ?  978  HOH B O   1 
HETATM 15866 O  O   . HOH BB 7 .   ? -49.905 -2.593  -34.447 1.00 46.99  ?  979  HOH B O   1 
HETATM 15867 O  O   . HOH BB 7 .   ? -22.362 18.293  -39.426 1.00 25.14  ?  980  HOH B O   1 
HETATM 15868 O  O   . HOH BB 7 .   ? -8.636  17.348  -51.055 1.00 48.14  ?  981  HOH B O   1 
HETATM 15869 O  O   . HOH BB 7 .   ? -16.109 16.618  -33.371 1.00 41.02  ?  982  HOH B O   1 
HETATM 15870 O  O   . HOH BB 7 .   ? -4.583  -27.831 -4.452  1.00 42.55  ?  983  HOH B O   1 
HETATM 15871 O  O   . HOH BB 7 .   ? -35.329 -4.146  -48.823 1.00 48.47  ?  984  HOH B O   1 
HETATM 15872 O  O   . HOH BB 7 .   ? -13.297 -23.328 2.665   1.00 48.35  ?  985  HOH B O   1 
HETATM 15873 O  O   . HOH BB 7 .   ? -22.009 2.901   -47.431 1.00 39.49  ?  986  HOH B O   1 
HETATM 15874 O  O   . HOH BB 7 .   ? -11.645 -9.674  -42.808 1.00 33.22  ?  987  HOH B O   1 
HETATM 15875 O  O   . HOH BB 7 .   ? -16.589 21.122  -24.031 1.00 46.02  ?  988  HOH B O   1 
HETATM 15876 O  O   . HOH BB 7 .   ? -30.067 -1.541  -10.138 1.00 39.06  ?  989  HOH B O   1 
HETATM 15877 O  O   . HOH BB 7 .   ? -44.819 13.324  -25.884 1.00 45.42  ?  990  HOH B O   1 
HETATM 15878 O  O   . HOH BB 7 .   ? -12.862 17.217  -41.128 1.00 42.66  ?  991  HOH B O   1 
HETATM 15879 O  O   . HOH BB 7 .   ? -17.373 -17.884 -30.459 1.00 34.28  ?  992  HOH B O   1 
HETATM 15880 O  O   . HOH BB 7 .   ? -34.913 9.875   -12.594 1.00 47.08  ?  993  HOH B O   1 
HETATM 15881 O  O   . HOH BB 7 .   ? -55.129 5.885   -46.113 1.00 44.42  ?  994  HOH B O   1 
HETATM 15882 O  O   . HOH BB 7 .   ? -12.856 -16.572 0.171   1.00 40.90  ?  995  HOH B O   1 
HETATM 15883 O  O   . HOH BB 7 .   ? -14.697 1.885   -26.028 1.00 26.55  ?  996  HOH B O   1 
HETATM 15884 O  O   . HOH BB 7 .   ? -6.486  -20.802 -16.283 1.00 46.73  ?  997  HOH B O   1 
HETATM 15885 O  O   . HOH BB 7 .   ? -12.891 10.175  -27.880 1.00 31.15  ?  998  HOH B O   1 
HETATM 15886 O  O   . HOH BB 7 .   ? -25.454 -4.305  2.137   1.00 47.56  ?  999  HOH B O   1 
HETATM 15887 O  O   A HOH BB 7 .   ? -30.039 -12.858 0.142   0.50 46.33  ?  1000 HOH B O   1 
HETATM 15888 O  O   B HOH BB 7 .   ? -30.794 -11.481 0.331   0.50 46.33  ?  1000 HOH B O   1 
HETATM 15889 O  O   A HOH BB 7 .   ? -30.406 -4.033  -7.526  0.50 40.27  ?  1001 HOH B O   1 
HETATM 15890 O  O   B HOH BB 7 .   ? -30.678 -2.714  -7.688  0.50 40.27  ?  1001 HOH B O   1 
HETATM 15891 O  O   . HOH BB 7 .   ? -20.571 18.185  -45.994 1.00 52.22  ?  1002 HOH B O   1 
HETATM 15892 O  O   . HOH BB 7 .   ? -29.460 -23.362 -15.378 1.00 36.72  ?  1003 HOH B O   1 
HETATM 15893 O  O   . HOH BB 7 .   ? -10.256 19.333  -47.541 1.00 54.65  ?  1004 HOH B O   1 
HETATM 15894 O  O   . HOH BB 7 .   ? -22.679 -15.854 -51.198 1.00 51.49  ?  1005 HOH B O   1 
HETATM 15895 O  O   . HOH BB 7 .   ? -53.653 2.640   -21.487 1.00 55.49  ?  1006 HOH B O   1 
HETATM 15896 O  O   . HOH BB 7 .   ? -22.499 -17.599 -43.059 1.00 37.75  ?  1007 HOH B O   1 
HETATM 15897 O  O   . HOH BB 7 .   ? -21.873 -11.490 -53.512 1.00 53.25  ?  1008 HOH B O   1 
HETATM 15898 O  O   A HOH BB 7 .   ? -23.429 21.607  -33.379 0.50 38.96  ?  1009 HOH B O   1 
HETATM 15899 O  O   B HOH BB 7 .   ? -21.827 21.939  -32.594 0.50 38.96  ?  1009 HOH B O   1 
HETATM 15900 O  O   . HOH BB 7 .   ? -34.296 2.574   -50.709 1.00 49.00  ?  1010 HOH B O   1 
HETATM 15901 O  O   . HOH BB 7 .   ? -13.087 21.816  -19.230 1.00 55.21  ?  1011 HOH B O   1 
HETATM 15902 O  O   . HOH BB 7 .   ? -44.982 -16.558 -38.686 1.00 49.53  ?  1012 HOH B O   1 
HETATM 15903 O  O   . HOH BB 7 .   ? -22.787 4.709   -49.004 1.00 40.75  ?  1013 HOH B O   1 
HETATM 15904 O  O   . HOH BB 7 .   ? -45.983 9.729   -21.716 1.00 48.83  ?  1014 HOH B O   1 
HETATM 15905 O  O   . HOH BB 7 .   ? -24.604 27.321  -20.629 1.00 57.05  ?  1015 HOH B O   1 
HETATM 15906 O  O   . HOH BB 7 .   ? -19.275 7.436   -8.801  1.00 44.84  ?  1016 HOH B O   1 
HETATM 15907 O  O   . HOH BB 7 .   ? -33.047 -20.402 -20.290 1.00 50.56  ?  1017 HOH B O   1 
HETATM 15908 O  O   . HOH BB 7 .   ? -11.719 3.010   -49.713 1.00 54.99  ?  1018 HOH B O   1 
HETATM 15909 O  O   . HOH BB 7 .   ? -11.187 3.011   -36.144 1.00 50.78  ?  1019 HOH B O   1 
HETATM 15910 O  O   . HOH BB 7 .   ? -25.065 -14.219 2.857   1.00 51.37  ?  1020 HOH B O   1 
HETATM 15911 O  O   . HOH BB 7 .   ? -30.409 14.120  -44.531 1.00 36.41  ?  1021 HOH B O   1 
HETATM 15912 O  O   . HOH BB 7 .   ? -13.243 -1.020  -25.640 1.00 34.62  ?  1022 HOH B O   1 
HETATM 15913 O  O   . HOH BB 7 .   ? -11.250 10.980  -38.637 1.00 51.24  ?  1023 HOH B O   1 
HETATM 15914 O  O   . HOH BB 7 .   ? -46.322 -9.620  -7.328  1.00 49.84  ?  1024 HOH B O   1 
HETATM 15915 O  O   A HOH BB 7 .   ? -3.047  -25.193 -17.641 0.62 42.14  ?  1025 HOH B O   1 
HETATM 15916 O  O   B HOH BB 7 .   ? -4.007  -26.979 -17.776 0.38 32.91  ?  1025 HOH B O   1 
HETATM 15917 O  O   . HOH BB 7 .   ? -30.506 -2.900  -52.077 1.00 52.67  ?  1026 HOH B O   1 
HETATM 15918 O  O   . HOH BB 7 .   ? -40.044 -17.664 -39.870 1.00 49.38  ?  1027 HOH B O   1 
HETATM 15919 O  O   . HOH BB 7 .   ? 6.656   -27.086 3.866   1.00 47.10  ?  1028 HOH B O   1 
HETATM 15920 O  O   . HOH BB 7 .   ? -4.913  10.722  -47.160 1.00 42.13  ?  1029 HOH B O   1 
HETATM 15921 O  O   . HOH BB 7 .   ? -40.652 -6.942  -6.611  1.00 45.63  ?  1030 HOH B O   1 
HETATM 15922 O  O   . HOH BB 7 .   ? -10.506 -17.096 -2.643  1.00 46.19  ?  1031 HOH B O   1 
HETATM 15923 O  O   . HOH BB 7 .   ? -21.138 -30.008 -28.067 1.00 51.79  ?  1032 HOH B O   1 
HETATM 15924 O  O   . HOH BB 7 .   ? -15.126 -26.350 -28.697 1.00 54.69  ?  1033 HOH B O   1 
HETATM 15925 O  O   . HOH BB 7 .   ? -23.499 -22.492 -35.097 1.00 52.04  ?  1034 HOH B O   1 
HETATM 15926 O  O   . HOH BB 7 .   ? -18.368 6.322   -52.092 1.00 49.83  ?  1035 HOH B O   1 
HETATM 15927 O  O   . HOH BB 7 .   ? -39.184 -20.789 -17.709 1.00 55.39  ?  1036 HOH B O   1 
HETATM 15928 O  O   . HOH BB 7 .   ? -21.600 -29.268 -3.729  1.00 50.54  ?  1037 HOH B O   1 
HETATM 15929 O  O   . HOH BB 7 .   ? -11.771 11.091  -34.998 1.00 56.83  ?  1038 HOH B O   1 
HETATM 15930 O  O   . HOH BB 7 .   ? -52.848 -1.574  -17.938 1.00 53.67  ?  1039 HOH B O   1 
HETATM 15931 O  O   . HOH BB 7 .   ? -22.975 2.418   -50.330 1.00 53.83  ?  1040 HOH B O   1 
HETATM 15932 O  O   . HOH BB 7 .   ? -33.127 -1.312  -6.997  1.00 39.35  ?  1041 HOH B O   1 
HETATM 15933 O  O   . HOH BB 7 .   ? -31.316 -22.078 -36.764 1.00 44.77  ?  1042 HOH B O   1 
HETATM 15934 O  O   A HOH BB 7 .   ? -50.973 0.510   -33.202 0.50 47.09  ?  1043 HOH B O   1 
HETATM 15935 O  O   B HOH BB 7 .   ? -51.595 -1.392  -32.956 0.50 47.09  ?  1043 HOH B O   1 
HETATM 15936 O  O   . HOH BB 7 .   ? -9.536  8.245   -56.802 1.00 46.49  ?  1044 HOH B O   1 
HETATM 15937 O  O   . HOH BB 7 .   ? -13.258 14.953  -36.423 1.00 45.41  ?  1045 HOH B O   1 
HETATM 15938 O  O   . HOH BB 7 .   ? -11.481 16.568  -51.211 1.00 43.82  ?  1046 HOH B O   1 
HETATM 15939 O  O   . HOH BB 7 .   ? -33.763 -12.189 -47.564 1.00 51.84  ?  1047 HOH B O   1 
HETATM 15940 O  O   A HOH BB 7 .   ? -18.573 20.843  -35.337 0.48 37.86  ?  1048 HOH B O   1 
HETATM 15941 O  O   B HOH BB 7 .   ? -19.750 20.609  -36.380 0.52 37.68  ?  1048 HOH B O   1 
HETATM 15942 O  O   . HOH BB 7 .   ? -26.473 -3.380  -49.950 1.00 34.51  ?  1049 HOH B O   1 
HETATM 15943 O  O   . HOH BB 7 .   ? -45.952 -1.848  -10.836 1.00 44.57  ?  1050 HOH B O   1 
HETATM 15944 O  O   . HOH BB 7 .   ? -29.240 -6.483  -49.798 1.00 44.27  ?  1051 HOH B O   1 
HETATM 15945 O  O   . HOH BB 7 .   ? -24.451 16.654  -10.096 1.00 53.18  ?  1052 HOH B O   1 
HETATM 15946 O  O   . HOH BB 7 .   ? -7.649  1.405   -41.301 1.00 47.97  ?  1053 HOH B O   1 
HETATM 15947 O  O   . HOH BB 7 .   ? -9.989  -1.107  -30.831 1.00 47.66  ?  1054 HOH B O   1 
HETATM 15948 O  O   . HOH BB 7 .   ? -33.711 14.590  -32.256 1.00 35.36  ?  1055 HOH B O   1 
HETATM 15949 O  O   . HOH BB 7 .   ? -11.266 -15.063 -43.735 1.00 53.71  ?  1056 HOH B O   1 
HETATM 15950 O  O   . HOH BB 7 .   ? -33.467 -3.808  -50.327 1.00 50.36  ?  1057 HOH B O   1 
HETATM 15951 O  O   . HOH BB 7 .   ? -12.003 10.828  -55.477 1.00 43.53  ?  1058 HOH B O   1 
HETATM 15952 O  O   . HOH BB 7 .   ? -23.367 -5.280  -47.608 1.00 33.33  ?  1059 HOH B O   1 
HETATM 15953 O  O   . HOH BB 7 .   ? -27.043 -8.186  -52.191 1.00 48.40  ?  1060 HOH B O   1 
HETATM 15954 O  O   . HOH BB 7 .   ? -12.009 2.485   -26.831 1.00 35.40  ?  1061 HOH B O   1 
HETATM 15955 O  O   . HOH BB 7 .   ? -45.153 -11.352 -45.052 1.00 53.73  ?  1062 HOH B O   1 
HETATM 15956 O  O   . HOH BB 7 .   ? -17.422 9.587   -14.044 1.00 45.27  ?  1063 HOH B O   1 
HETATM 15957 O  O   A HOH BB 7 .   ? -15.266 -22.986 6.430   0.47 45.38  ?  1064 HOH B O   1 
HETATM 15958 O  O   B HOH BB 7 .   ? -16.796 -23.629 5.740   0.53 43.37  ?  1064 HOH B O   1 
HETATM 15959 O  O   . HOH BB 7 .   ? -17.818 3.848   -10.045 1.00 40.23  ?  1065 HOH B O   1 
HETATM 15960 O  O   . HOH BB 7 .   ? -6.070  -2.740  -20.081 1.00 35.75  ?  1066 HOH B O   1 
HETATM 15961 O  O   . HOH BB 7 .   ? -9.801  -1.972  -14.850 1.00 35.97  ?  1067 HOH B O   1 
HETATM 15962 O  O   . HOH BB 7 .   ? -22.240 -10.348 1.274   1.00 37.73  ?  1068 HOH B O   1 
HETATM 15963 O  O   . HOH BB 7 .   ? -9.330  -14.478 -3.519  1.00 48.71  ?  1069 HOH B O   1 
HETATM 15964 O  O   . HOH BB 7 .   ? -20.790 -1.635  -2.786  1.00 46.87  ?  1070 HOH B O   1 
HETATM 15965 O  O   . HOH BB 7 .   ? -22.910 -0.437  -50.210 1.00 54.61  ?  1071 HOH B O   1 
HETATM 15966 O  O   . HOH BB 7 .   ? -11.183 -9.574  -27.826 1.00 24.45  ?  1072 HOH B O   1 
HETATM 15967 O  O   . HOH BB 7 .   ? -6.167  -29.175 -6.178  1.00 49.27  ?  1073 HOH B O   1 
HETATM 15968 O  O   A HOH BB 7 .   ? -12.632 -29.330 -12.811 0.44 39.33  ?  1074 HOH B O   1 
HETATM 15969 O  O   B HOH BB 7 .   ? -11.310 -28.126 -13.792 0.56 34.78  ?  1074 HOH B O   1 
HETATM 15970 O  O   . HOH BB 7 .   ? -50.551 0.800   -37.677 1.00 47.01  ?  1075 HOH B O   1 
HETATM 15971 O  O   . HOH BB 7 .   ? -7.319  -7.966  -27.756 1.00 37.57  ?  1076 HOH B O   1 
HETATM 15972 O  O   . HOH BB 7 .   ? -34.465 15.152  -15.818 1.00 34.80  ?  1077 HOH B O   1 
HETATM 15973 O  O   . HOH BB 7 .   ? -40.835 12.055  -41.256 1.00 41.70  ?  1078 HOH B O   1 
HETATM 15974 O  O   . HOH BB 7 .   ? -15.581 18.274  -49.041 1.00 53.17  ?  1079 HOH B O   1 
HETATM 15975 O  O   . HOH BB 7 .   ? -9.066  -28.216 0.129   1.00 55.38  ?  1080 HOH B O   1 
HETATM 15976 O  O   . HOH BB 7 .   ? -41.464 -19.812 -40.302 1.00 58.21  ?  1081 HOH B O   1 
HETATM 15977 O  O   . HOH BB 7 .   ? -18.410 -0.341  -43.046 1.00 37.20  ?  1082 HOH B O   1 
HETATM 15978 O  O   . HOH BB 7 .   ? -38.274 5.349   -7.785  1.00 54.87  ?  1083 HOH B O   1 
HETATM 15979 O  O   . HOH BB 7 .   ? -12.255 -2.304  -11.595 1.00 29.69  ?  1084 HOH B O   1 
HETATM 15980 O  O   A HOH BB 7 .   ? -12.446 -21.270 -2.366  0.50 40.58  ?  1085 HOH B O   1 
HETATM 15981 O  O   B HOH BB 7 .   ? -13.336 -22.549 -1.325  0.50 40.58  ?  1085 HOH B O   1 
HETATM 15982 O  O   . HOH BB 7 .   ? -22.017 -8.120  2.397   1.00 48.30  ?  1086 HOH B O   1 
HETATM 15983 O  O   . HOH BB 7 .   ? -40.585 14.945  -19.943 1.00 45.53  ?  1087 HOH B O   1 
HETATM 15984 O  O   . HOH BB 7 .   ? -25.795 -2.582  -52.654 1.00 51.69  ?  1088 HOH B O   1 
HETATM 15985 O  O   . HOH BB 7 .   ? -10.997 -12.099 -44.052 1.00 46.85  ?  1089 HOH B O   1 
HETATM 15986 O  O   . HOH BB 7 .   ? -32.397 -7.335  -6.229  1.00 40.32  ?  1090 HOH B O   1 
HETATM 15987 O  O   . HOH BB 7 .   ? -39.224 -8.721  -6.636  1.00 48.96  ?  1091 HOH B O   1 
HETATM 15988 O  O   . HOH BB 7 .   ? -51.945 -1.605  -37.084 1.00 30.00  ?  1092 HOH B O   1 
HETATM 15989 O  O   A HOH BB 7 .   ? -25.934 -19.822 2.320   0.57 39.59  ?  1093 HOH B O   1 
HETATM 15990 O  O   B HOH BB 7 .   ? -25.202 -20.898 0.731   0.43 39.87  ?  1093 HOH B O   1 
HETATM 15991 O  O   . HOH BB 7 .   ? -37.841 6.035   -11.668 1.00 41.41  ?  1094 HOH B O   1 
HETATM 15992 O  O   . HOH BB 7 .   ? -33.201 18.651  -19.177 1.00 48.06  ?  1095 HOH B O   1 
HETATM 15993 O  O   . HOH BB 7 .   ? -5.122  15.031  -52.856 1.00 53.40  ?  1096 HOH B O   1 
HETATM 15994 O  O   . HOH BB 7 .   ? -11.888 7.959   -30.379 1.00 43.34  ?  1097 HOH B O   1 
HETATM 15995 O  O   . HOH BB 7 .   ? -28.808 0.977   -9.187  1.00 41.76  ?  1098 HOH B O   1 
HETATM 15996 O  O   . HOH BB 7 .   ? -51.913 -10.056 -15.244 1.00 56.85  ?  1099 HOH B O   1 
HETATM 15997 O  O   . HOH BB 7 .   ? -40.203 4.154   -11.623 1.00 32.46  ?  1100 HOH B O   1 
HETATM 15998 O  O   . HOH BB 7 .   ? -27.953 -21.727 -21.268 1.00 54.04  ?  1101 HOH B O   1 
HETATM 15999 O  O   . HOH BB 7 .   ? -27.676 -2.818  -3.528  1.00 50.89  ?  1102 HOH B O   1 
HETATM 16000 O  O   . HOH BB 7 .   ? -10.851 7.026   -28.173 1.00 45.89  ?  1103 HOH B O   1 
HETATM 16001 O  O   . HOH BB 7 .   ? -20.308 -0.971  -47.480 1.00 42.35  ?  1104 HOH B O   1 
HETATM 16002 O  O   . HOH BB 7 .   ? -6.313  -13.797 -3.558  1.00 39.00  ?  1105 HOH B O   1 
HETATM 16003 O  O   . HOH BB 7 .   ? -27.164 4.667   -8.018  1.00 38.08  ?  1106 HOH B O   1 
HETATM 16004 O  O   . HOH BB 7 .   ? -20.787 -20.309 -40.609 1.00 55.10  ?  1107 HOH B O   1 
HETATM 16005 O  O   . HOH BB 7 .   ? 3.775   -21.227 4.250   1.00 38.83  ?  1108 HOH B O   1 
HETATM 16006 O  O   . HOH BB 7 .   ? -11.241 -8.740  -40.627 1.00 38.61  ?  1109 HOH B O   1 
HETATM 16007 O  O   . HOH BB 7 .   ? -11.647 -16.767 -41.681 1.00 56.89  ?  1110 HOH B O   1 
HETATM 16008 O  O   . HOH BB 7 .   ? -25.014 -5.516  -49.585 1.00 37.45  ?  1111 HOH B O   1 
HETATM 16009 O  O   . HOH BB 7 .   ? -17.304 19.413  -27.594 1.00 50.68  ?  1112 HOH B O   1 
HETATM 16010 O  O   . HOH BB 7 .   ? -30.020 -18.801 -45.770 1.00 57.09  ?  1113 HOH B O   1 
HETATM 16011 O  O   A HOH BB 7 .   ? -17.340 14.917  -13.418 0.50 32.86  ?  1114 HOH B O   1 
HETATM 16012 O  O   B HOH BB 7 .   ? -16.714 16.614  -13.350 0.50 32.86  ?  1114 HOH B O   1 
HETATM 16013 O  O   . HOH BB 7 .   ? -19.007 11.249  -48.573 1.00 25.81  ?  1115 HOH B O   1 
HETATM 16014 O  O   . HOH BB 7 .   ? -14.630 -27.708 -8.518  1.00 54.86  ?  1116 HOH B O   1 
HETATM 16015 O  O   . HOH BB 7 .   ? -16.523 -31.060 -27.315 1.00 60.13  ?  1117 HOH B O   1 
HETATM 16016 O  O   . HOH BB 7 .   ? -47.371 -12.926 -23.272 1.00 51.08  ?  1118 HOH B O   1 
HETATM 16017 O  O   . HOH BB 7 .   ? -14.854 1.597   -10.765 1.00 39.26  ?  1119 HOH B O   1 
HETATM 16018 O  O   . HOH BB 7 .   ? -46.817 14.832  -27.709 1.00 54.24  ?  1120 HOH B O   1 
HETATM 16019 O  O   . HOH BB 7 .   ? -12.071 -27.293 -25.707 1.00 54.86  ?  1121 HOH B O   1 
HETATM 16020 O  O   . HOH BB 7 .   ? -38.466 14.384  -38.402 1.00 47.68  ?  1122 HOH B O   1 
HETATM 16021 O  O   . HOH BB 7 .   ? -6.110  -16.601 -1.992  1.00 44.78  ?  1123 HOH B O   1 
HETATM 16022 O  O   . HOH BB 7 .   ? -15.227 10.464  -52.880 1.00 53.12  ?  1124 HOH B O   1 
HETATM 16023 O  O   . HOH BB 7 .   ? -10.594 -25.304 -29.837 1.00 54.87  ?  1125 HOH B O   1 
HETATM 16024 O  O   . HOH BB 7 .   ? -42.054 -13.146 -5.203  1.00 53.15  ?  1126 HOH B O   1 
HETATM 16025 O  O   . HOH BB 7 .   ? -50.064 8.974   -43.459 1.00 50.01  ?  1127 HOH B O   1 
HETATM 16026 O  O   . HOH BB 7 .   ? -3.146  -29.916 -3.984  1.00 53.71  ?  1128 HOH B O   1 
HETATM 16027 O  O   . HOH BB 7 .   ? -15.195 -1.093  -7.661  1.00 35.83  ?  1129 HOH B O   1 
HETATM 16028 O  O   . HOH BB 7 .   ? -6.952  -3.761  -29.490 1.00 45.34  ?  1130 HOH B O   1 
HETATM 16029 O  O   . HOH BB 7 .   ? -34.306 17.463  -16.868 1.00 39.52  ?  1131 HOH B O   1 
HETATM 16030 O  O   . HOH BB 7 .   ? -24.813 20.264  -35.426 1.00 47.24  ?  1132 HOH B O   1 
HETATM 16031 O  O   . HOH BB 7 .   ? -12.883 -25.540 -28.546 1.00 51.60  ?  1133 HOH B O   1 
HETATM 16032 O  O   . HOH BB 7 .   ? -25.510 0.111   -3.039  1.00 54.30  ?  1134 HOH B O   1 
HETATM 16033 O  O   A HOH BB 7 .   ? -20.430 -28.729 -32.192 0.52 45.97  ?  1135 HOH B O   1 
HETATM 16034 O  O   B HOH BB 7 .   ? -20.047 -28.803 -30.498 0.48 43.60  ?  1135 HOH B O   1 
HETATM 16035 O  O   . HOH BB 7 .   ? -27.485 3.131   -5.833  1.00 54.07  ?  1136 HOH B O   1 
HETATM 16036 O  O   . HOH BB 7 .   ? -8.533  -18.051 0.449   1.00 51.38  ?  1137 HOH B O   1 
HETATM 16037 O  O   . HOH BB 7 .   ? -30.894 -6.963  -55.637 1.00 61.31  ?  1138 HOH B O   1 
HETATM 16038 O  O   . HOH BB 7 .   ? -20.173 -9.564  3.932   1.00 52.90  ?  1139 HOH B O   1 
HETATM 16039 O  O   . HOH BB 7 .   ? -10.257 -27.701 -27.803 1.00 64.27  ?  1140 HOH B O   1 
HETATM 16040 O  O   . HOH BB 7 .   ? -23.952 -23.782 4.161   1.00 56.19  ?  1141 HOH B O   1 
HETATM 16041 O  O   . HOH BB 7 .   ? -23.655 -5.049  -52.081 1.00 47.87  ?  1142 HOH B O   1 
HETATM 16042 O  O   . HOH BB 7 .   ? -37.616 17.747  -17.392 1.00 56.78  ?  1143 HOH B O   1 
HETATM 16043 O  O   . HOH BB 7 .   ? -33.728 19.545  -14.891 1.00 55.53  ?  1144 HOH B O   1 
HETATM 16044 O  O   . HOH CB 7 .   ? -21.280 26.272  11.736  1.00 44.59  ?  701  HOH C O   1 
HETATM 16045 O  O   . HOH CB 7 .   ? -16.098 67.682  -3.862  1.00 46.06  ?  702  HOH C O   1 
HETATM 16046 O  O   . HOH CB 7 .   ? -31.845 60.796  17.056  1.00 48.15  ?  703  HOH C O   1 
HETATM 16047 O  O   . HOH CB 7 .   ? -31.272 28.445  33.235  1.00 51.11  ?  704  HOH C O   1 
HETATM 16048 O  O   . HOH CB 7 .   ? -10.379 64.497  3.690   1.00 36.67  ?  705  HOH C O   1 
HETATM 16049 O  O   . HOH CB 7 .   ? -2.433  53.715  1.060   1.00 36.26  ?  706  HOH C O   1 
HETATM 16050 O  O   . HOH CB 7 .   ? -8.707  18.125  -1.507  1.00 48.64  ?  707  HOH C O   1 
HETATM 16051 O  O   . HOH CB 7 .   ? -21.026 32.606  12.609  1.00 34.58  ?  708  HOH C O   1 
HETATM 16052 O  O   . HOH CB 7 .   ? -0.747  56.328  6.419   1.00 51.13  ?  709  HOH C O   1 
HETATM 16053 O  O   . HOH CB 7 .   ? -18.001 21.782  6.869   1.00 31.17  ?  710  HOH C O   1 
HETATM 16054 O  O   . HOH CB 7 .   ? -33.372 54.935  24.690  1.00 44.94  ?  711  HOH C O   1 
HETATM 16055 O  O   . HOH CB 7 .   ? -26.492 31.328  36.919  1.00 50.52  ?  712  HOH C O   1 
HETATM 16056 O  O   . HOH CB 7 .   ? -23.742 55.103  18.266  1.00 39.32  ?  713  HOH C O   1 
HETATM 16057 O  O   . HOH CB 7 .   ? -27.370 40.618  16.546  1.00 32.68  ?  714  HOH C O   1 
HETATM 16058 O  O   . HOH CB 7 .   ? -7.412  63.600  13.531  1.00 52.50  ?  715  HOH C O   1 
HETATM 16059 O  O   . HOH CB 7 .   ? -26.303 57.945  20.798  1.00 33.55  ?  716  HOH C O   1 
HETATM 16060 O  O   . HOH CB 7 .   ? -20.066 27.919  10.231  1.00 42.96  ?  717  HOH C O   1 
HETATM 16061 O  O   . HOH CB 7 .   ? -5.806  49.025  -5.140  1.00 43.00  ?  718  HOH C O   1 
HETATM 16062 O  O   . HOH CB 7 .   ? -31.897 44.558  28.771  1.00 35.59  ?  719  HOH C O   1 
HETATM 16063 O  O   . HOH CB 7 .   ? -12.676 57.518  13.030  1.00 31.97  ?  720  HOH C O   1 
HETATM 16064 O  O   . HOH CB 7 .   ? -19.030 59.735  -5.380  1.00 41.23  ?  721  HOH C O   1 
HETATM 16065 O  O   . HOH CB 7 .   ? -25.937 41.048  -8.391  1.00 40.34  ?  722  HOH C O   1 
HETATM 16066 O  O   . HOH CB 7 .   ? -18.780 56.109  23.402  1.00 41.02  ?  723  HOH C O   1 
HETATM 16067 O  O   . HOH CB 7 .   ? -11.954 63.502  16.494  1.00 40.79  ?  724  HOH C O   1 
HETATM 16068 O  O   . HOH CB 7 .   ? -21.086 69.038  -10.066 1.00 54.75  ?  725  HOH C O   1 
HETATM 16069 O  O   . HOH CB 7 .   ? -31.355 32.730  11.643  1.00 30.99  ?  726  HOH C O   1 
HETATM 16070 O  O   . HOH CB 7 .   ? -27.197 33.038  10.669  1.00 30.73  ?  727  HOH C O   1 
HETATM 16071 O  O   . HOH CB 7 .   ? -32.524 38.912  33.725  1.00 38.18  ?  728  HOH C O   1 
HETATM 16072 O  O   . HOH CB 7 .   ? -12.642 19.475  1.621   1.00 49.07  ?  729  HOH C O   1 
HETATM 16073 O  O   . HOH CB 7 .   ? -2.285  37.331  14.051  1.00 47.75  ?  730  HOH C O   1 
HETATM 16074 O  O   . HOH CB 7 .   ? -31.101 50.558  34.098  1.00 45.16  ?  731  HOH C O   1 
HETATM 16075 O  O   . HOH CB 7 .   ? -14.959 40.266  1.070   1.00 30.45  ?  732  HOH C O   1 
HETATM 16076 O  O   . HOH CB 7 .   ? -10.569 58.184  -6.466  1.00 54.17  ?  733  HOH C O   1 
HETATM 16077 O  O   . HOH CB 7 .   ? -21.568 54.053  19.570  1.00 32.67  ?  734  HOH C O   1 
HETATM 16078 O  O   . HOH CB 7 .   ? -40.232 40.051  6.481   1.00 43.50  ?  735  HOH C O   1 
HETATM 16079 O  O   . HOH CB 7 .   ? -37.088 42.013  23.515  1.00 47.45  ?  736  HOH C O   1 
HETATM 16080 O  O   . HOH CB 7 .   ? -27.145 42.765  -5.303  1.00 35.38  ?  737  HOH C O   1 
HETATM 16081 O  O   A HOH CB 7 .   ? -13.308 28.859  7.875   0.57 35.82  ?  738  HOH C O   1 
HETATM 16082 O  O   B HOH CB 7 .   ? -11.989 27.767  7.710   0.43 44.41  ?  738  HOH C O   1 
HETATM 16083 O  O   . HOH CB 7 .   ? -21.815 32.107  7.521   1.00 33.88  ?  739  HOH C O   1 
HETATM 16084 O  O   . HOH CB 7 .   ? -15.773 62.326  13.348  1.00 37.24  ?  740  HOH C O   1 
HETATM 16085 O  O   . HOH CB 7 .   ? -8.567  49.089  36.532  1.00 37.53  ?  741  HOH C O   1 
HETATM 16086 O  O   . HOH CB 7 .   ? -28.121 25.306  31.888  1.00 43.83  ?  742  HOH C O   1 
HETATM 16087 O  O   . HOH CB 7 .   ? -30.743 47.403  16.335  1.00 32.89  ?  743  HOH C O   1 
HETATM 16088 O  O   . HOH CB 7 .   ? -10.340 40.191  0.473   1.00 28.78  ?  744  HOH C O   1 
HETATM 16089 O  O   . HOH CB 7 .   ? -19.335 43.927  5.805   1.00 30.14  ?  745  HOH C O   1 
HETATM 16090 O  O   . HOH CB 7 .   ? -28.445 55.989  -11.010 1.00 48.64  ?  746  HOH C O   1 
HETATM 16091 O  O   . HOH CB 7 .   ? -26.403 30.916  20.572  1.00 33.71  ?  747  HOH C O   1 
HETATM 16092 O  O   . HOH CB 7 .   ? -23.311 50.054  13.950  1.00 28.62  ?  748  HOH C O   1 
HETATM 16093 O  O   . HOH CB 7 .   ? -41.477 34.585  5.325   1.00 42.10  ?  749  HOH C O   1 
HETATM 16094 O  O   . HOH CB 7 .   ? 7.614   43.152  8.377   1.00 56.51  ?  750  HOH C O   1 
HETATM 16095 O  O   . HOH CB 7 .   ? -11.764 42.996  -5.419  1.00 32.79  ?  751  HOH C O   1 
HETATM 16096 O  O   . HOH CB 7 .   ? -24.449 43.068  6.861   1.00 27.81  ?  752  HOH C O   1 
HETATM 16097 O  O   . HOH CB 7 .   ? -8.637  48.759  -9.034  1.00 43.22  ?  753  HOH C O   1 
HETATM 16098 O  O   . HOH CB 7 .   ? -30.937 56.577  13.535  1.00 34.58  ?  754  HOH C O   1 
HETATM 16099 O  O   . HOH CB 7 .   ? -10.239 49.925  43.707  1.00 37.76  ?  755  HOH C O   1 
HETATM 16100 O  O   . HOH CB 7 .   ? -35.198 31.648  12.329  1.00 35.82  ?  756  HOH C O   1 
HETATM 16101 O  O   . HOH CB 7 .   ? -23.466 37.800  28.401  1.00 38.67  ?  757  HOH C O   1 
HETATM 16102 O  O   . HOH CB 7 .   ? -26.743 12.084  7.955   1.00 44.91  ?  758  HOH C O   1 
HETATM 16103 O  O   . HOH CB 7 .   ? -16.989 46.424  32.736  1.00 30.43  ?  759  HOH C O   1 
HETATM 16104 O  O   . HOH CB 7 .   ? -8.519  44.755  25.205  1.00 32.25  ?  760  HOH C O   1 
HETATM 16105 O  O   . HOH CB 7 .   ? -28.101 35.646  9.576   1.00 31.13  ?  761  HOH C O   1 
HETATM 16106 O  O   . HOH CB 7 .   ? -37.915 44.312  -6.327  1.00 46.19  ?  762  HOH C O   1 
HETATM 16107 O  O   . HOH CB 7 .   ? -41.398 52.660  3.917   1.00 42.87  ?  763  HOH C O   1 
HETATM 16108 O  O   . HOH CB 7 .   ? -10.283 55.572  -6.118  1.00 42.27  ?  764  HOH C O   1 
HETATM 16109 O  O   . HOH CB 7 .   ? -27.544 68.074  9.706   1.00 54.16  ?  765  HOH C O   1 
HETATM 16110 O  O   . HOH CB 7 .   ? -13.310 42.166  23.088  1.00 28.43  ?  766  HOH C O   1 
HETATM 16111 O  O   . HOH CB 7 .   ? -23.091 30.860  3.942   1.00 37.20  ?  767  HOH C O   1 
HETATM 16112 O  O   . HOH CB 7 .   ? -17.267 37.698  7.859   1.00 29.85  ?  768  HOH C O   1 
HETATM 16113 O  O   . HOH CB 7 .   ? -30.500 41.903  36.777  1.00 43.41  ?  769  HOH C O   1 
HETATM 16114 O  O   . HOH CB 7 .   ? -21.972 38.706  -12.662 1.00 42.82  ?  770  HOH C O   1 
HETATM 16115 O  O   . HOH CB 7 .   ? -8.423  54.119  23.032  1.00 30.54  ?  771  HOH C O   1 
HETATM 16116 O  O   . HOH CB 7 .   ? -4.061  57.125  -3.500  1.00 41.66  ?  772  HOH C O   1 
HETATM 16117 O  O   . HOH CB 7 .   ? -26.830 15.628  2.814   1.00 46.58  ?  773  HOH C O   1 
HETATM 16118 O  O   . HOH CB 7 .   ? -11.246 29.701  -6.314  1.00 31.56  ?  774  HOH C O   1 
HETATM 16119 O  O   . HOH CB 7 .   ? -23.771 28.494  -5.985  1.00 38.04  ?  775  HOH C O   1 
HETATM 16120 O  O   . HOH CB 7 .   ? -7.670  61.378  30.019  1.00 34.43  ?  776  HOH C O   1 
HETATM 16121 O  O   . HOH CB 7 .   ? -4.768  55.781  13.414  1.00 39.45  ?  777  HOH C O   1 
HETATM 16122 O  O   . HOH CB 7 .   ? -25.951 17.091  4.931   1.00 46.53  ?  778  HOH C O   1 
HETATM 16123 O  O   . HOH CB 7 .   ? -41.137 50.785  11.289  1.00 45.49  ?  779  HOH C O   1 
HETATM 16124 O  O   . HOH CB 7 .   ? -20.789 46.109  34.820  1.00 33.52  ?  780  HOH C O   1 
HETATM 16125 O  O   . HOH CB 7 .   ? -14.267 42.873  29.525  1.00 29.80  ?  781  HOH C O   1 
HETATM 16126 O  O   . HOH CB 7 .   ? -16.356 57.107  22.748  1.00 38.02  ?  782  HOH C O   1 
HETATM 16127 O  O   . HOH CB 7 .   ? -33.223 40.688  8.698   1.00 32.62  ?  783  HOH C O   1 
HETATM 16128 O  O   . HOH CB 7 .   ? -27.114 33.456  19.401  1.00 30.78  ?  784  HOH C O   1 
HETATM 16129 O  O   . HOH CB 7 .   ? -9.170  45.395  27.953  1.00 35.28  ?  785  HOH C O   1 
HETATM 16130 O  O   . HOH CB 7 .   ? -30.726 44.209  25.397  1.00 37.55  ?  786  HOH C O   1 
HETATM 16131 O  O   . HOH CB 7 .   ? -9.632  42.002  12.236  1.00 27.81  ?  787  HOH C O   1 
HETATM 16132 O  O   . HOH CB 7 .   ? -20.013 46.524  40.176  1.00 43.61  ?  788  HOH C O   1 
HETATM 16133 O  O   . HOH CB 7 .   ? -41.046 40.363  15.400  1.00 53.70  ?  789  HOH C O   1 
HETATM 16134 O  O   . HOH CB 7 .   ? -37.349 38.693  15.185  1.00 40.04  ?  790  HOH C O   1 
HETATM 16135 O  O   . HOH CB 7 .   ? -34.844 54.237  19.478  1.00 49.12  ?  791  HOH C O   1 
HETATM 16136 O  O   . HOH CB 7 .   ? -18.279 66.816  44.494  1.00 63.12  ?  792  HOH C O   1 
HETATM 16137 O  O   . HOH CB 7 .   ? -5.316  39.967  -7.421  1.00 44.72  ?  793  HOH C O   1 
HETATM 16138 O  O   . HOH CB 7 .   ? -22.211 34.409  14.272  1.00 32.05  ?  794  HOH C O   1 
HETATM 16139 O  O   . HOH CB 7 .   ? -10.864 50.288  16.100  1.00 31.52  ?  795  HOH C O   1 
HETATM 16140 O  O   . HOH CB 7 .   ? -25.258 24.228  34.283  1.00 52.38  ?  796  HOH C O   1 
HETATM 16141 O  O   . HOH CB 7 .   ? -3.690  52.898  24.987  1.00 41.15  ?  797  HOH C O   1 
HETATM 16142 O  O   . HOH CB 7 .   ? -11.474 29.084  0.776   1.00 32.75  ?  798  HOH C O   1 
HETATM 16143 O  O   . HOH CB 7 .   ? -6.246  38.677  -1.663  1.00 38.23  ?  799  HOH C O   1 
HETATM 16144 O  O   . HOH CB 7 .   ? -5.388  48.389  20.259  1.00 28.66  ?  800  HOH C O   1 
HETATM 16145 O  O   . HOH CB 7 .   ? -21.803 35.992  25.248  1.00 30.08  ?  801  HOH C O   1 
HETATM 16146 O  O   . HOH CB 7 .   ? -16.686 64.582  -1.926  1.00 43.70  ?  802  HOH C O   1 
HETATM 16147 O  O   . HOH CB 7 .   ? -23.064 32.369  10.806  1.00 34.93  ?  803  HOH C O   1 
HETATM 16148 O  O   . HOH CB 7 .   ? -44.234 58.595  13.175  1.00 50.90  ?  804  HOH C O   1 
HETATM 16149 O  O   . HOH CB 7 .   ? -9.774  43.977  40.277  1.00 31.26  ?  805  HOH C O   1 
HETATM 16150 O  O   . HOH CB 7 .   ? -28.250 29.370  4.925   1.00 43.54  ?  806  HOH C O   1 
HETATM 16151 O  O   . HOH CB 7 .   ? -4.321  32.897  1.707   1.00 40.40  ?  807  HOH C O   1 
HETATM 16152 O  O   . HOH CB 7 .   ? -39.916 43.474  7.356   1.00 45.45  ?  808  HOH C O   1 
HETATM 16153 O  O   . HOH CB 7 .   ? -30.611 50.733  36.635  1.00 51.09  ?  809  HOH C O   1 
HETATM 16154 O  O   . HOH CB 7 .   ? -20.922 65.662  17.450  1.00 40.92  ?  810  HOH C O   1 
HETATM 16155 O  O   . HOH CB 7 .   ? -18.050 52.789  49.513  1.00 44.01  ?  811  HOH C O   1 
HETATM 16156 O  O   . HOH CB 7 .   ? -17.127 28.679  11.270  1.00 55.02  ?  812  HOH C O   1 
HETATM 16157 O  O   . HOH CB 7 .   ? -11.176 41.048  19.543  1.00 36.97  ?  813  HOH C O   1 
HETATM 16158 O  O   . HOH CB 7 .   ? -26.925 58.160  18.115  1.00 41.05  ?  814  HOH C O   1 
HETATM 16159 O  O   . HOH CB 7 .   ? -2.742  39.848  14.772  1.00 42.96  ?  815  HOH C O   1 
HETATM 16160 O  O   . HOH CB 7 .   ? -38.641 44.066  0.467   1.00 39.01  ?  816  HOH C O   1 
HETATM 16161 O  O   . HOH CB 7 .   ? -11.557 57.762  9.444   1.00 38.59  ?  817  HOH C O   1 
HETATM 16162 O  O   . HOH CB 7 .   ? -23.150 48.921  22.240  1.00 29.19  ?  818  HOH C O   1 
HETATM 16163 O  O   . HOH CB 7 .   ? -12.891 43.588  37.759  1.00 29.35  ?  819  HOH C O   1 
HETATM 16164 O  O   . HOH CB 7 .   ? -3.517  58.396  24.931  1.00 39.20  ?  820  HOH C O   1 
HETATM 16165 O  O   . HOH CB 7 .   ? -39.707 39.431  13.475  1.00 41.74  ?  821  HOH C O   1 
HETATM 16166 O  O   . HOH CB 7 .   ? -32.940 35.334  5.491   1.00 31.22  ?  822  HOH C O   1 
HETATM 16167 O  O   . HOH CB 7 .   ? -16.294 17.593  -3.857  1.00 44.17  ?  823  HOH C O   1 
HETATM 16168 O  O   . HOH CB 7 .   ? -24.213 30.247  35.537  1.00 43.87  ?  824  HOH C O   1 
HETATM 16169 O  O   . HOH CB 7 .   ? -22.709 8.680   3.760   1.00 36.60  ?  825  HOH C O   1 
HETATM 16170 O  O   . HOH CB 7 .   ? -37.832 51.074  -5.892  1.00 48.69  ?  826  HOH C O   1 
HETATM 16171 O  O   . HOH CB 7 .   ? -19.696 43.135  -13.398 1.00 42.30  ?  827  HOH C O   1 
HETATM 16172 O  O   A HOH CB 7 .   ? -34.230 61.945  -7.698  0.46 46.33  ?  828  HOH C O   1 
HETATM 16173 O  O   B HOH CB 7 .   ? -34.599 60.960  -9.179  0.54 41.00  ?  828  HOH C O   1 
HETATM 16174 O  O   . HOH CB 7 .   ? -20.497 68.622  23.192  1.00 49.55  ?  829  HOH C O   1 
HETATM 16175 O  O   . HOH CB 7 .   ? -38.585 48.180  -6.076  1.00 47.51  ?  830  HOH C O   1 
HETATM 16176 O  O   . HOH CB 7 .   ? -12.912 47.396  43.019  1.00 39.96  ?  831  HOH C O   1 
HETATM 16177 O  O   . HOH CB 7 .   ? -11.840 63.833  19.954  1.00 39.91  ?  832  HOH C O   1 
HETATM 16178 O  O   . HOH CB 7 .   ? -32.444 32.196  0.335   1.00 44.73  ?  833  HOH C O   1 
HETATM 16179 O  O   . HOH CB 7 .   ? -28.105 53.878  10.442  1.00 31.97  ?  834  HOH C O   1 
HETATM 16180 O  O   . HOH CB 7 .   ? -22.713 37.603  20.581  1.00 32.46  ?  835  HOH C O   1 
HETATM 16181 O  O   . HOH CB 7 .   ? -11.619 50.139  13.247  1.00 32.36  ?  836  HOH C O   1 
HETATM 16182 O  O   . HOH CB 7 .   ? -28.302 28.996  8.808   1.00 38.04  ?  837  HOH C O   1 
HETATM 16183 O  O   . HOH CB 7 .   ? -26.099 38.247  14.357  1.00 30.69  ?  838  HOH C O   1 
HETATM 16184 O  O   . HOH CB 7 .   ? -29.984 37.240  40.651  1.00 53.81  ?  839  HOH C O   1 
HETATM 16185 O  O   . HOH CB 7 .   ? 1.617   35.309  11.744  1.00 45.34  ?  840  HOH C O   1 
HETATM 16186 O  O   . HOH CB 7 .   ? -20.096 32.810  27.111  1.00 35.66  ?  841  HOH C O   1 
HETATM 16187 O  O   . HOH CB 7 .   ? -14.357 69.081  12.317  1.00 47.25  ?  842  HOH C O   1 
HETATM 16188 O  O   . HOH CB 7 .   ? -8.739  69.828  23.882  1.00 57.62  ?  843  HOH C O   1 
HETATM 16189 O  O   . HOH CB 7 .   ? -29.764 39.580  21.150  1.00 31.56  ?  844  HOH C O   1 
HETATM 16190 O  O   . HOH CB 7 .   ? -12.781 24.139  2.545   1.00 43.60  ?  845  HOH C O   1 
HETATM 16191 O  O   . HOH CB 7 .   ? 3.270   34.258  2.098   1.00 52.87  ?  846  HOH C O   1 
HETATM 16192 O  O   . HOH CB 7 .   ? -4.596  56.582  34.859  1.00 45.56  ?  847  HOH C O   1 
HETATM 16193 O  O   . HOH CB 7 .   ? -23.949 32.111  5.580   1.00 37.80  ?  848  HOH C O   1 
HETATM 16194 O  O   . HOH CB 7 .   ? -28.376 56.922  -16.658 1.00 51.44  ?  849  HOH C O   1 
HETATM 16195 O  O   . HOH CB 7 .   ? -4.461  61.838  22.568  1.00 45.22  ?  850  HOH C O   1 
HETATM 16196 O  O   . HOH CB 7 .   ? -20.133 66.115  19.890  1.00 42.20  ?  851  HOH C O   1 
HETATM 16197 O  O   . HOH CB 7 .   ? -12.758 26.484  1.840   1.00 37.08  ?  852  HOH C O   1 
HETATM 16198 O  O   . HOH CB 7 .   ? -27.409 29.612  -0.527  1.00 41.37  ?  853  HOH C O   1 
HETATM 16199 O  O   . HOH CB 7 .   ? -21.845 39.975  24.064  1.00 29.86  ?  854  HOH C O   1 
HETATM 16200 O  O   . HOH CB 7 .   ? -20.845 64.626  21.928  1.00 41.63  ?  855  HOH C O   1 
HETATM 16201 O  O   . HOH CB 7 .   ? -28.540 31.174  1.285   1.00 36.16  ?  856  HOH C O   1 
HETATM 16202 O  O   . HOH CB 7 .   ? -13.726 55.217  39.486  1.00 42.84  ?  857  HOH C O   1 
HETATM 16203 O  O   . HOH CB 7 .   ? -36.548 41.469  -5.288  1.00 48.36  ?  858  HOH C O   1 
HETATM 16204 O  O   . HOH CB 7 .   ? -2.881  51.233  19.842  1.00 35.25  ?  859  HOH C O   1 
HETATM 16205 O  O   . HOH CB 7 .   ? -23.164 16.973  -3.168  1.00 46.93  ?  860  HOH C O   1 
HETATM 16206 O  O   . HOH CB 7 .   ? -23.292 42.455  23.689  1.00 29.07  ?  861  HOH C O   1 
HETATM 16207 O  O   . HOH CB 7 .   ? -20.487 25.812  -1.669  1.00 35.04  ?  862  HOH C O   1 
HETATM 16208 O  O   . HOH CB 7 .   ? -21.536 34.358  -9.853  1.00 46.12  ?  863  HOH C O   1 
HETATM 16209 O  O   . HOH CB 7 .   ? -25.344 22.390  8.424   1.00 44.21  ?  864  HOH C O   1 
HETATM 16210 O  O   . HOH CB 7 .   ? -28.680 32.230  17.251  1.00 32.39  ?  865  HOH C O   1 
HETATM 16211 O  O   . HOH CB 7 .   ? -37.508 43.483  -2.694  1.00 43.10  ?  866  HOH C O   1 
HETATM 16212 O  O   . HOH CB 7 .   ? -10.152 51.503  36.014  1.00 37.78  ?  867  HOH C O   1 
HETATM 16213 O  O   . HOH CB 7 .   ? 5.101   35.000  10.396  1.00 46.31  ?  868  HOH C O   1 
HETATM 16214 O  O   . HOH CB 7 .   ? -26.365 30.919  8.809   1.00 35.87  ?  869  HOH C O   1 
HETATM 16215 O  O   . HOH CB 7 .   ? -9.407  39.636  10.990  1.00 30.35  ?  870  HOH C O   1 
HETATM 16216 O  O   . HOH CB 7 .   ? -13.812 42.103  -9.585  1.00 40.84  ?  871  HOH C O   1 
HETATM 16217 O  O   A HOH CB 7 .   ? -4.194  32.691  -5.225  0.50 46.37  ?  872  HOH C O   1 
HETATM 16218 O  O   B HOH CB 7 .   ? -5.577  33.405  -6.787  0.50 46.37  ?  872  HOH C O   1 
HETATM 16219 O  O   . HOH CB 7 .   ? -24.948 33.575  12.108  1.00 30.12  ?  873  HOH C O   1 
HETATM 16220 O  O   . HOH CB 7 .   ? -10.410 34.813  -8.231  1.00 42.57  ?  874  HOH C O   1 
HETATM 16221 O  O   . HOH CB 7 .   ? -7.595  68.098  6.058   1.00 51.41  ?  875  HOH C O   1 
HETATM 16222 O  O   . HOH CB 7 .   ? -37.648 35.275  1.728   1.00 37.51  ?  876  HOH C O   1 
HETATM 16223 O  O   . HOH CB 7 .   ? -31.467 65.398  -2.260  1.00 51.15  ?  877  HOH C O   1 
HETATM 16224 O  O   . HOH CB 7 .   ? -8.697  47.590  40.475  1.00 34.59  ?  878  HOH C O   1 
HETATM 16225 O  O   . HOH CB 7 .   ? -16.448 68.710  25.954  1.00 46.35  ?  879  HOH C O   1 
HETATM 16226 O  O   A HOH CB 7 .   ? -25.313 38.114  -11.017 0.59 36.96  ?  880  HOH C O   1 
HETATM 16227 O  O   B HOH CB 7 .   ? -25.316 36.266  -10.719 0.41 40.80  ?  880  HOH C O   1 
HETATM 16228 O  O   . HOH CB 7 .   ? -29.374 64.185  4.428   1.00 43.14  ?  881  HOH C O   1 
HETATM 16229 O  O   . HOH CB 7 .   ? -11.641 38.643  12.008  1.00 32.36  ?  882  HOH C O   1 
HETATM 16230 O  O   . HOH CB 7 .   ? -23.463 62.128  -11.269 1.00 41.30  ?  883  HOH C O   1 
HETATM 16231 O  O   . HOH CB 7 .   ? -12.775 50.325  33.625  1.00 33.29  ?  884  HOH C O   1 
HETATM 16232 O  O   . HOH CB 7 .   ? -30.203 30.132  35.897  1.00 43.72  ?  885  HOH C O   1 
HETATM 16233 O  O   . HOH CB 7 .   ? -20.463 34.843  16.196  1.00 36.79  ?  886  HOH C O   1 
HETATM 16234 O  O   . HOH CB 7 .   ? -15.671 35.701  6.650   1.00 28.91  ?  887  HOH C O   1 
HETATM 16235 O  O   . HOH CB 7 .   ? -10.381 61.645  20.243  1.00 38.68  ?  888  HOH C O   1 
HETATM 16236 O  O   . HOH CB 7 .   ? 6.040   34.007  6.597   1.00 50.97  ?  889  HOH C O   1 
HETATM 16237 O  O   . HOH CB 7 .   ? -3.902  47.337  17.854  1.00 34.79  ?  890  HOH C O   1 
HETATM 16238 O  O   . HOH CB 7 .   ? -25.106 19.926  7.823   1.00 46.35  ?  891  HOH C O   1 
HETATM 16239 O  O   . HOH CB 7 .   ? -31.229 28.769  15.900  1.00 35.97  ?  892  HOH C O   1 
HETATM 16240 O  O   . HOH CB 7 .   ? -29.763 25.757  10.702  1.00 47.97  ?  893  HOH C O   1 
HETATM 16241 O  O   . HOH CB 7 .   ? -7.515  32.764  9.920   1.00 38.10  ?  894  HOH C O   1 
HETATM 16242 O  O   . HOH CB 7 .   ? -12.720 37.847  14.683  1.00 31.92  ?  895  HOH C O   1 
HETATM 16243 O  O   . HOH CB 7 .   ? -35.079 36.348  36.387  1.00 57.53  ?  896  HOH C O   1 
HETATM 16244 O  O   . HOH CB 7 .   ? -32.237 25.717  10.113  1.00 45.89  ?  897  HOH C O   1 
HETATM 16245 O  O   . HOH CB 7 .   ? -10.981 42.166  26.139  1.00 35.94  ?  898  HOH C O   1 
HETATM 16246 O  O   A HOH CB 7 .   ? -29.840 59.676  28.763  0.54 34.10  ?  899  HOH C O   1 
HETATM 16247 O  O   B HOH CB 7 .   ? -29.520 60.111  26.851  0.46 43.79  ?  899  HOH C O   1 
HETATM 16248 O  O   . HOH CB 7 .   ? -24.030 31.169  1.864   1.00 39.48  ?  900  HOH C O   1 
HETATM 16249 O  O   . HOH CB 7 .   ? -14.749 66.731  20.781  1.00 45.96  ?  901  HOH C O   1 
HETATM 16250 O  O   . HOH CB 7 .   ? -15.467 53.452  40.186  1.00 34.70  ?  902  HOH C O   1 
HETATM 16251 O  O   . HOH CB 7 .   ? 1.489   41.520  -7.553  1.00 47.05  ?  903  HOH C O   1 
HETATM 16252 O  O   . HOH CB 7 .   ? -1.246  42.119  17.194  1.00 48.98  ?  904  HOH C O   1 
HETATM 16253 O  O   . HOH CB 7 .   ? -31.324 54.999  22.609  1.00 41.36  ?  905  HOH C O   1 
HETATM 16254 O  O   . HOH CB 7 .   ? -23.483 44.041  35.934  1.00 48.07  ?  906  HOH C O   1 
HETATM 16255 O  O   . HOH CB 7 .   ? -27.469 28.872  -2.964  1.00 38.92  ?  907  HOH C O   1 
HETATM 16256 O  O   . HOH CB 7 .   ? -31.543 43.572  -11.028 1.00 48.77  ?  908  HOH C O   1 
HETATM 16257 O  O   . HOH CB 7 .   ? -18.041 70.943  22.235  1.00 60.26  ?  909  HOH C O   1 
HETATM 16258 O  O   . HOH CB 7 .   ? -11.097 70.238  7.186   1.00 51.86  ?  910  HOH C O   1 
HETATM 16259 O  O   . HOH CB 7 .   ? -7.658  29.202  6.245   1.00 40.00  ?  911  HOH C O   1 
HETATM 16260 O  O   . HOH CB 7 .   ? -38.324 43.057  26.776  1.00 47.68  ?  912  HOH C O   1 
HETATM 16261 O  O   . HOH CB 7 .   ? -39.606 28.952  7.231   1.00 42.61  ?  913  HOH C O   1 
HETATM 16262 O  O   . HOH CB 7 .   ? -11.356 55.099  50.740  1.00 45.46  ?  914  HOH C O   1 
HETATM 16263 O  O   . HOH CB 7 .   ? -36.555 35.092  19.013  1.00 48.43  ?  915  HOH C O   1 
HETATM 16264 O  O   . HOH CB 7 .   ? 5.503   42.317  10.041  1.00 47.16  ?  916  HOH C O   1 
HETATM 16265 O  O   . HOH CB 7 .   ? -4.589  47.762  23.809  1.00 32.14  ?  917  HOH C O   1 
HETATM 16266 O  O   . HOH CB 7 .   ? -18.923 66.573  28.277  1.00 48.81  ?  918  HOH C O   1 
HETATM 16267 O  O   . HOH CB 7 .   ? -40.615 55.911  2.022   1.00 46.37  ?  919  HOH C O   1 
HETATM 16268 O  O   . HOH CB 7 .   ? -26.444 31.851  2.895   1.00 38.18  ?  920  HOH C O   1 
HETATM 16269 O  O   . HOH CB 7 .   ? -26.263 48.084  42.828  1.00 50.69  ?  921  HOH C O   1 
HETATM 16270 O  O   . HOH CB 7 .   ? -14.315 37.839  17.501  1.00 44.31  ?  922  HOH C O   1 
HETATM 16271 O  O   . HOH CB 7 .   ? -16.839 48.973  -16.006 1.00 55.31  ?  923  HOH C O   1 
HETATM 16272 O  O   . HOH CB 7 .   ? -7.433  53.845  37.063  1.00 44.98  ?  924  HOH C O   1 
HETATM 16273 O  O   . HOH CB 7 .   ? -32.519 37.058  -10.037 1.00 49.07  ?  925  HOH C O   1 
HETATM 16274 O  O   . HOH CB 7 .   ? -39.410 51.695  15.515  1.00 40.09  ?  926  HOH C O   1 
HETATM 16275 O  O   . HOH CB 7 .   ? -12.509 61.696  -6.187  1.00 49.83  ?  927  HOH C O   1 
HETATM 16276 O  O   . HOH CB 7 .   ? -14.130 67.241  18.467  1.00 50.21  ?  928  HOH C O   1 
HETATM 16277 O  O   . HOH CB 7 .   ? -21.537 55.704  43.747  1.00 46.16  ?  929  HOH C O   1 
HETATM 16278 O  O   . HOH CB 7 .   ? -31.095 65.815  3.204   1.00 53.99  ?  930  HOH C O   1 
HETATM 16279 O  O   . HOH CB 7 .   ? -15.996 39.951  21.136  1.00 34.64  ?  931  HOH C O   1 
HETATM 16280 O  O   . HOH CB 7 .   ? -27.705 62.813  25.473  1.00 44.86  ?  932  HOH C O   1 
HETATM 16281 O  O   . HOH CB 7 .   ? -28.812 59.830  -9.398  1.00 50.28  ?  933  HOH C O   1 
HETATM 16282 O  O   . HOH CB 7 .   ? -30.723 43.336  22.960  1.00 36.40  ?  934  HOH C O   1 
HETATM 16283 O  O   . HOH CB 7 .   ? -30.603 46.272  37.939  1.00 46.34  ?  935  HOH C O   1 
HETATM 16284 O  O   . HOH CB 7 .   ? -21.390 23.295  12.408  1.00 54.11  ?  936  HOH C O   1 
HETATM 16285 O  O   . HOH CB 7 .   ? -28.243 60.732  22.745  1.00 53.72  ?  937  HOH C O   1 
HETATM 16286 O  O   . HOH CB 7 .   ? -15.595 23.265  6.755   1.00 47.49  ?  938  HOH C O   1 
HETATM 16287 O  O   . HOH CB 7 .   ? -0.078  50.622  10.494  1.00 46.70  ?  939  HOH C O   1 
HETATM 16288 O  O   . HOH CB 7 .   ? -16.408 69.247  21.404  1.00 52.76  ?  940  HOH C O   1 
HETATM 16289 O  O   . HOH CB 7 .   ? -1.596  48.675  18.368  1.00 44.28  ?  941  HOH C O   1 
HETATM 16290 O  O   . HOH CB 7 .   ? -10.384 54.655  39.693  1.00 43.40  ?  942  HOH C O   1 
HETATM 16291 O  O   . HOH CB 7 .   ? -35.282 68.162  -5.573  1.00 72.25  ?  943  HOH C O   1 
HETATM 16292 O  O   . HOH CB 7 .   ? -41.677 30.191  5.568   1.00 51.86  ?  944  HOH C O   1 
HETATM 16293 O  O   . HOH CB 7 .   ? -22.975 36.982  40.594  1.00 53.08  ?  945  HOH C O   1 
HETATM 16294 O  O   . HOH CB 7 .   ? -30.710 68.903  8.880   1.00 50.92  ?  946  HOH C O   1 
HETATM 16295 O  O   . HOH CB 7 .   ? -41.798 58.607  12.213  1.00 57.07  ?  947  HOH C O   1 
HETATM 16296 O  O   . HOH CB 7 .   ? -34.586 33.403  -0.804  1.00 39.18  ?  948  HOH C O   1 
HETATM 16297 O  O   A HOH CB 7 .   ? -13.636 69.155  34.099  0.62 46.92  ?  949  HOH C O   1 
HETATM 16298 O  O   B HOH CB 7 .   ? -12.320 70.647  33.828  0.38 49.41  ?  949  HOH C O   1 
HETATM 16299 O  O   . HOH CB 7 .   ? -35.942 33.122  19.848  1.00 48.12  ?  950  HOH C O   1 
HETATM 16300 O  O   . HOH CB 7 .   ? -39.337 51.754  -7.785  1.00 52.09  ?  951  HOH C O   1 
HETATM 16301 O  O   A HOH CB 7 .   ? -17.179 32.249  17.640  0.52 42.29  ?  952  HOH C O   1 
HETATM 16302 O  O   B HOH CB 7 .   ? -18.462 31.323  18.874  0.48 34.13  ?  952  HOH C O   1 
HETATM 16303 O  O   . HOH CB 7 .   ? -16.994 23.332  -8.261  1.00 53.04  ?  953  HOH C O   1 
HETATM 16304 O  O   A HOH CB 7 .   ? -0.889  42.804  13.910  0.54 37.41  ?  954  HOH C O   1 
HETATM 16305 O  O   B HOH CB 7 .   ? -2.444  42.302  14.613  0.46 35.37  ?  954  HOH C O   1 
HETATM 16306 O  O   . HOH CB 7 .   ? -25.254 15.584  -2.673  1.00 48.70  ?  955  HOH C O   1 
HETATM 16307 O  O   . HOH CB 7 .   ? -19.581 34.285  24.795  1.00 38.42  ?  956  HOH C O   1 
HETATM 16308 O  O   . HOH CB 7 .   ? -12.189 35.202  15.860  1.00 38.81  ?  957  HOH C O   1 
HETATM 16309 O  O   . HOH CB 7 .   ? -33.750 33.093  3.679   1.00 37.01  ?  958  HOH C O   1 
HETATM 16310 O  O   . HOH CB 7 .   ? -17.199 16.319  10.673  1.00 52.27  ?  959  HOH C O   1 
HETATM 16311 O  O   . HOH CB 7 .   ? -12.133 70.310  27.572  1.00 59.14  ?  960  HOH C O   1 
HETATM 16312 O  O   A HOH CB 7 .   ? -38.267 59.879  14.820  0.50 59.68  ?  961  HOH C O   1 
HETATM 16313 O  O   B HOH CB 7 .   ? -37.620 58.749  16.597  0.50 59.68  ?  961  HOH C O   1 
HETATM 16314 O  O   . HOH CB 7 .   ? -18.173 15.447  -3.978  1.00 42.17  ?  962  HOH C O   1 
HETATM 16315 O  O   . HOH CB 7 .   ? -20.271 10.108  0.029   1.00 44.94  ?  963  HOH C O   1 
HETATM 16316 O  O   . HOH CB 7 .   ? -39.649 61.754  -3.804  1.00 60.03  ?  964  HOH C O   1 
HETATM 16317 O  O   . HOH CB 7 .   ? -21.378 37.655  23.227  1.00 32.19  ?  965  HOH C O   1 
HETATM 16318 O  O   . HOH CB 7 .   ? -13.489 24.095  5.301   1.00 51.73  ?  966  HOH C O   1 
HETATM 16319 O  O   . HOH CB 7 .   ? -37.244 36.689  -0.372  1.00 45.98  ?  967  HOH C O   1 
HETATM 16320 O  O   . HOH CB 7 .   ? -8.912  52.469  38.241  1.00 46.71  ?  968  HOH C O   1 
HETATM 16321 O  O   . HOH CB 7 .   ? -26.249 30.896  5.836   1.00 37.52  ?  969  HOH C O   1 
HETATM 16322 O  O   . HOH CB 7 .   ? 7.340   36.119  11.534  1.00 53.43  ?  970  HOH C O   1 
HETATM 16323 O  O   . HOH CB 7 .   ? -8.128  67.996  31.678  1.00 58.56  ?  971  HOH C O   1 
HETATM 16324 O  O   . HOH CB 7 .   ? -34.245 28.213  17.926  1.00 45.97  ?  972  HOH C O   1 
HETATM 16325 O  O   . HOH CB 7 .   ? -7.943  61.973  15.939  1.00 44.23  ?  973  HOH C O   1 
HETATM 16326 O  O   . HOH CB 7 .   ? 0.948   51.340  12.578  1.00 50.52  ?  974  HOH C O   1 
HETATM 16327 O  O   . HOH CB 7 .   ? -23.264 24.972  14.335  1.00 57.16  ?  975  HOH C O   1 
HETATM 16328 O  O   . HOH CB 7 .   ? 0.603   44.747  13.323  1.00 47.98  ?  976  HOH C O   1 
HETATM 16329 O  O   . HOH CB 7 .   ? -9.487  45.158  32.556  1.00 49.63  ?  977  HOH C O   1 
HETATM 16330 O  O   . HOH CB 7 .   ? -21.285 44.260  -15.572 1.00 48.15  ?  978  HOH C O   1 
HETATM 16331 O  O   . HOH CB 7 .   ? -11.023 31.091  10.492  1.00 53.47  ?  979  HOH C O   1 
HETATM 16332 O  O   . HOH CB 7 .   ? -6.639  46.328  28.709  1.00 43.88  ?  980  HOH C O   1 
HETATM 16333 O  O   . HOH CB 7 .   ? -9.923  49.414  33.475  1.00 36.28  ?  981  HOH C O   1 
HETATM 16334 O  O   . HOH CB 7 .   ? -18.213 71.733  -3.300  1.00 56.22  ?  982  HOH C O   1 
HETATM 16335 O  O   . HOH CB 7 .   ? -1.033  54.112  -1.219  1.00 44.89  ?  983  HOH C O   1 
HETATM 16336 O  O   . HOH CB 7 .   ? -28.730 25.289  3.462   1.00 57.26  ?  984  HOH C O   1 
HETATM 16337 O  O   . HOH CB 7 .   ? -5.894  46.169  25.539  1.00 33.93  ?  985  HOH C O   1 
HETATM 16338 O  O   . HOH CB 7 .   ? -14.046 57.784  41.392  1.00 44.49  ?  986  HOH C O   1 
HETATM 16339 O  O   . HOH CB 7 .   ? -31.398 65.449  14.080  1.00 58.90  ?  987  HOH C O   1 
HETATM 16340 O  O   . HOH CB 7 .   ? -19.098 69.099  35.432  1.00 59.06  ?  988  HOH C O   1 
HETATM 16341 O  O   . HOH CB 7 .   ? -27.635 23.770  30.268  1.00 53.26  ?  989  HOH C O   1 
HETATM 16342 O  O   . HOH CB 7 .   ? -29.838 33.546  -11.368 1.00 58.07  ?  990  HOH C O   1 
HETATM 16343 O  O   . HOH CB 7 .   ? -7.708  50.170  39.798  1.00 42.68  ?  991  HOH C O   1 
HETATM 16344 O  O   . HOH CB 7 .   ? -3.352  47.755  21.964  1.00 43.50  ?  992  HOH C O   1 
HETATM 16345 O  O   . HOH CB 7 .   ? -30.165 29.552  3.015   1.00 42.53  ?  993  HOH C O   1 
HETATM 16346 O  O   . HOH CB 7 .   ? -5.754  28.914  -4.315  1.00 57.33  ?  994  HOH C O   1 
HETATM 16347 O  O   . HOH CB 7 .   ? -5.944  63.334  30.050  1.00 43.33  ?  995  HOH C O   1 
HETATM 16348 O  O   . HOH CB 7 .   ? -5.647  58.478  14.034  1.00 49.67  ?  996  HOH C O   1 
HETATM 16349 O  O   . HOH CB 7 .   ? -43.729 42.804  7.847   1.00 56.95  ?  997  HOH C O   1 
HETATM 16350 O  O   . HOH CB 7 .   ? -27.950 36.024  41.474  1.00 58.63  ?  998  HOH C O   1 
HETATM 16351 O  O   . HOH CB 7 .   ? -21.010 67.485  34.307  1.00 56.59  ?  999  HOH C O   1 
HETATM 16352 O  O   . HOH CB 7 .   ? -35.623 33.239  1.563   1.00 42.48  ?  1000 HOH C O   1 
HETATM 16353 O  O   . HOH CB 7 .   ? -20.740 40.930  -14.293 1.00 48.54  ?  1001 HOH C O   1 
HETATM 16354 O  O   . HOH CB 7 .   ? -21.744 24.175  -4.280  1.00 28.18  ?  1002 HOH C O   1 
HETATM 16355 O  O   . HOH CB 7 .   ? -30.913 58.765  25.224  1.00 50.35  ?  1003 HOH C O   1 
HETATM 16356 O  O   A HOH CB 7 .   ? -15.016 42.215  -12.235 0.50 45.43  ?  1004 HOH C O   1 
HETATM 16357 O  O   B HOH CB 7 .   ? -15.082 40.249  -12.641 0.50 45.43  ?  1004 HOH C O   1 
HETATM 16358 O  O   . HOH CB 7 .   ? -0.191  52.763  -3.143  1.00 44.48  ?  1005 HOH C O   1 
HETATM 16359 O  O   . HOH CB 7 .   ? -16.083 18.797  -6.232  1.00 45.58  ?  1006 HOH C O   1 
HETATM 16360 O  O   . HOH CB 7 .   ? -8.732  51.748  42.485  1.00 42.22  ?  1007 HOH C O   1 
HETATM 16361 O  O   . HOH CB 7 .   ? -38.836 35.755  20.328  1.00 55.57  ?  1008 HOH C O   1 
HETATM 16362 O  O   . HOH CB 7 .   ? -17.276 31.493  21.494  1.00 45.44  ?  1009 HOH C O   1 
HETATM 16363 O  O   . HOH CB 7 .   ? -2.073  43.128  20.984  1.00 50.88  ?  1010 HOH C O   1 
HETATM 16364 O  O   . HOH CB 7 .   ? -17.823 39.507  -15.463 1.00 60.85  ?  1011 HOH C O   1 
HETATM 16365 O  O   A HOH CB 7 .   ? -32.963 45.304  35.038  0.50 43.91  ?  1012 HOH C O   1 
HETATM 16366 O  O   B HOH CB 7 .   ? -31.018 45.435  35.622  0.50 43.91  ?  1012 HOH C O   1 
HETATM 16367 O  O   . HOH CB 7 .   ? -33.736 43.294  31.938  1.00 53.41  ?  1013 HOH C O   1 
HETATM 16368 O  O   . HOH CB 7 .   ? -45.136 40.103  9.774   1.00 68.17  ?  1014 HOH C O   1 
HETATM 16369 O  O   . HOH DB 7 .   ? 45.753  48.221  -37.481 1.00 53.58  ?  701  HOH D O   1 
HETATM 16370 O  O   . HOH DB 7 .   ? 11.610  19.537  -59.236 1.00 44.02  ?  702  HOH D O   1 
HETATM 16371 O  O   . HOH DB 7 .   ? 24.035  47.179  -30.556 1.00 30.85  ?  703  HOH D O   1 
HETATM 16372 O  O   . HOH DB 7 .   ? 1.061   41.172  -30.022 1.00 40.33  ?  704  HOH D O   1 
HETATM 16373 O  O   . HOH DB 7 .   ? 43.347  39.889  -22.781 1.00 43.87  ?  705  HOH D O   1 
HETATM 16374 O  O   . HOH DB 7 .   ? 21.719  23.319  -41.855 1.00 35.34  ?  706  HOH D O   1 
HETATM 16375 O  O   . HOH DB 7 .   ? 19.966  72.991  -20.785 1.00 46.84  ?  707  HOH D O   1 
HETATM 16376 O  O   . HOH DB 7 .   ? 24.042  30.757  -47.193 1.00 36.41  ?  708  HOH D O   1 
HETATM 16377 O  O   . HOH DB 7 .   ? 32.451  48.618  -20.259 1.00 34.36  ?  709  HOH D O   1 
HETATM 16378 O  O   . HOH DB 7 .   ? -4.308  35.884  -50.225 1.00 31.98  ?  710  HOH D O   1 
HETATM 16379 O  O   . HOH DB 7 .   ? 13.705  30.587  -40.076 1.00 37.31  ?  711  HOH D O   1 
HETATM 16380 O  O   . HOH DB 7 .   ? 36.684  53.206  -41.434 1.00 45.66  ?  712  HOH D O   1 
HETATM 16381 O  O   . HOH DB 7 .   ? -3.210  22.930  -48.392 1.00 42.05  ?  713  HOH D O   1 
HETATM 16382 O  O   . HOH DB 7 .   ? 39.534  27.550  -25.859 1.00 48.26  ?  714  HOH D O   1 
HETATM 16383 O  O   . HOH DB 7 .   ? 36.007  55.161  -18.654 1.00 43.23  ?  715  HOH D O   1 
HETATM 16384 O  O   . HOH DB 7 .   ? -4.297  32.936  -37.326 1.00 43.43  ?  716  HOH D O   1 
HETATM 16385 O  O   . HOH DB 7 .   ? 35.857  33.199  -50.035 1.00 49.84  ?  717  HOH D O   1 
HETATM 16386 O  O   . HOH DB 7 .   ? 33.213  61.476  -15.516 1.00 56.22  ?  718  HOH D O   1 
HETATM 16387 O  O   . HOH DB 7 .   ? 33.295  27.381  -44.753 1.00 43.13  ?  719  HOH D O   1 
HETATM 16388 O  O   . HOH DB 7 .   ? 37.238  40.144  -13.701 1.00 45.59  ?  720  HOH D O   1 
HETATM 16389 O  O   . HOH DB 7 .   ? 10.913  18.316  -43.542 1.00 55.80  ?  721  HOH D O   1 
HETATM 16390 O  O   . HOH DB 7 .   ? 33.169  26.766  -28.695 1.00 40.60  ?  722  HOH D O   1 
HETATM 16391 O  O   . HOH DB 7 .   ? 16.774  54.630  -24.115 1.00 37.20  ?  723  HOH D O   1 
HETATM 16392 O  O   . HOH DB 7 .   ? 4.411   48.497  -22.977 1.00 35.45  ?  724  HOH D O   1 
HETATM 16393 O  O   . HOH DB 7 .   ? -10.069 41.952  -27.446 1.00 53.40  ?  725  HOH D O   1 
HETATM 16394 O  O   . HOH DB 7 .   ? 39.739  25.656  -40.640 1.00 57.86  ?  726  HOH D O   1 
HETATM 16395 O  O   . HOH DB 7 .   ? 26.518  53.854  -31.470 1.00 29.71  ?  727  HOH D O   1 
HETATM 16396 O  O   . HOH DB 7 .   ? 26.289  37.042  -47.307 1.00 41.55  ?  728  HOH D O   1 
HETATM 16397 O  O   . HOH DB 7 .   ? 13.733  37.024  -48.479 1.00 25.31  ?  729  HOH D O   1 
HETATM 16398 O  O   . HOH DB 7 .   ? 22.252  52.630  -12.882 1.00 42.60  ?  730  HOH D O   1 
HETATM 16399 O  O   . HOH DB 7 .   ? 39.092  46.692  -46.404 1.00 44.08  ?  731  HOH D O   1 
HETATM 16400 O  O   . HOH DB 7 .   ? 19.635  65.230  -28.790 1.00 40.11  ?  732  HOH D O   1 
HETATM 16401 O  O   . HOH DB 7 .   ? 15.584  43.130  -51.324 1.00 38.32  ?  733  HOH D O   1 
HETATM 16402 O  O   . HOH DB 7 .   ? 2.862   31.624  -25.290 1.00 36.07  ?  734  HOH D O   1 
HETATM 16403 O  O   . HOH DB 7 .   ? -9.557  29.145  -36.497 1.00 54.67  ?  735  HOH D O   1 
HETATM 16404 O  O   . HOH DB 7 .   ? 12.169  20.447  -45.237 1.00 47.31  ?  736  HOH D O   1 
HETATM 16405 O  O   . HOH DB 7 .   ? 33.335  48.710  -47.601 1.00 39.04  ?  737  HOH D O   1 
HETATM 16406 O  O   A HOH DB 7 .   ? 28.068  30.385  -13.732 0.57 33.38  ?  738  HOH D O   1 
HETATM 16407 O  O   B HOH DB 7 .   ? 28.988  29.080  -13.960 0.43 37.82  ?  738  HOH D O   1 
HETATM 16408 O  O   . HOH DB 7 .   ? 12.682  48.111  -16.744 1.00 37.85  ?  739  HOH D O   1 
HETATM 16409 O  O   . HOH DB 7 .   ? 11.672  24.601  -26.877 1.00 41.41  ?  740  HOH D O   1 
HETATM 16410 O  O   . HOH DB 7 .   ? 17.719  30.576  -58.431 1.00 48.57  ?  741  HOH D O   1 
HETATM 16411 O  O   . HOH DB 7 .   ? 16.225  47.954  -20.155 1.00 33.89  ?  742  HOH D O   1 
HETATM 16412 O  O   . HOH DB 7 .   ? 12.351  52.528  -26.218 1.00 37.78  ?  743  HOH D O   1 
HETATM 16413 O  O   . HOH DB 7 .   ? 12.356  64.399  -23.193 1.00 39.01  ?  744  HOH D O   1 
HETATM 16414 O  O   . HOH DB 7 .   ? -0.859  33.592  -37.528 1.00 37.27  ?  745  HOH D O   1 
HETATM 16415 O  O   . HOH DB 7 .   ? 30.370  44.928  -51.608 1.00 44.86  ?  746  HOH D O   1 
HETATM 16416 O  O   . HOH DB 7 .   ? 17.570  31.321  -34.010 1.00 31.38  ?  747  HOH D O   1 
HETATM 16417 O  O   . HOH DB 7 .   ? 22.010  47.140  -9.600  1.00 43.69  ?  748  HOH D O   1 
HETATM 16418 O  O   . HOH DB 7 .   ? 17.662  50.352  -39.888 1.00 27.82  ?  749  HOH D O   1 
HETATM 16419 O  O   . HOH DB 7 .   ? 27.155  56.210  -35.470 1.00 31.29  ?  750  HOH D O   1 
HETATM 16420 O  O   . HOH DB 7 .   ? -2.737  28.747  -28.334 1.00 39.61  ?  751  HOH D O   1 
HETATM 16421 O  O   . HOH DB 7 .   ? 2.700   44.821  -29.969 1.00 33.69  ?  752  HOH D O   1 
HETATM 16422 O  O   . HOH DB 7 .   ? 33.699  55.481  -33.575 1.00 32.04  ?  753  HOH D O   1 
HETATM 16423 O  O   . HOH DB 7 .   ? 34.556  51.548  -19.785 1.00 39.91  ?  754  HOH D O   1 
HETATM 16424 O  O   . HOH DB 7 .   ? 25.760  18.298  -44.371 1.00 49.03  ?  755  HOH D O   1 
HETATM 16425 O  O   . HOH DB 7 .   ? 14.288  35.183  -54.937 1.00 36.86  ?  756  HOH D O   1 
HETATM 16426 O  O   . HOH DB 7 .   ? 19.091  52.107  -30.270 1.00 30.27  ?  757  HOH D O   1 
HETATM 16427 O  O   . HOH DB 7 .   ? 28.827  32.061  -50.111 1.00 41.79  ?  758  HOH D O   1 
HETATM 16428 O  O   . HOH DB 7 .   ? 11.641  50.083  -26.130 1.00 33.02  ?  759  HOH D O   1 
HETATM 16429 O  O   . HOH DB 7 .   ? -0.953  24.149  -31.082 1.00 48.91  ?  760  HOH D O   1 
HETATM 16430 O  O   . HOH DB 7 .   ? 7.259   16.818  -39.029 1.00 45.65  ?  761  HOH D O   1 
HETATM 16431 O  O   . HOH DB 7 .   ? 18.074  25.522  -40.093 1.00 37.45  ?  762  HOH D O   1 
HETATM 16432 O  O   . HOH DB 7 .   ? 16.084  32.546  -35.813 1.00 27.67  ?  763  HOH D O   1 
HETATM 16433 O  O   . HOH DB 7 .   ? 39.731  53.553  -37.908 1.00 41.75  ?  764  HOH D O   1 
HETATM 16434 O  O   . HOH DB 7 .   ? 32.817  23.418  -31.250 1.00 44.02  ?  765  HOH D O   1 
HETATM 16435 O  O   . HOH DB 7 .   ? 18.779  44.639  -7.181  1.00 45.52  ?  766  HOH D O   1 
HETATM 16436 O  O   . HOH DB 7 .   ? 15.053  31.463  -42.391 1.00 33.99  ?  767  HOH D O   1 
HETATM 16437 O  O   . HOH DB 7 .   ? 40.068  46.200  -39.699 1.00 34.81  ?  768  HOH D O   1 
HETATM 16438 O  O   . HOH DB 7 .   ? 22.062  44.965  -25.560 1.00 30.15  ?  769  HOH D O   1 
HETATM 16439 O  O   . HOH DB 7 .   ? 19.157  47.933  -14.862 1.00 36.13  ?  770  HOH D O   1 
HETATM 16440 O  O   . HOH DB 7 .   ? 16.845  26.757  -33.509 1.00 32.42  ?  771  HOH D O   1 
HETATM 16441 O  O   . HOH DB 7 .   ? 22.102  28.692  -26.940 1.00 30.84  ?  772  HOH D O   1 
HETATM 16442 O  O   . HOH DB 7 .   ? 32.914  59.806  -20.555 1.00 41.91  ?  773  HOH D O   1 
HETATM 16443 O  O   . HOH DB 7 .   ? 37.150  59.403  -30.965 1.00 44.64  ?  774  HOH D O   1 
HETATM 16444 O  O   . HOH DB 7 .   ? 23.444  41.378  -49.709 1.00 35.30  ?  775  HOH D O   1 
HETATM 16445 O  O   . HOH DB 7 .   ? 17.890  27.631  -18.389 1.00 43.22  ?  776  HOH D O   1 
HETATM 16446 O  O   . HOH DB 7 .   ? 6.484   46.542  -22.808 1.00 34.69  ?  777  HOH D O   1 
HETATM 16447 O  O   . HOH DB 7 .   ? -6.219  38.117  -47.599 1.00 33.66  ?  778  HOH D O   1 
HETATM 16448 O  O   . HOH DB 7 .   ? 19.200  37.146  -31.227 1.00 26.59  ?  779  HOH D O   1 
HETATM 16449 O  O   . HOH DB 7 .   ? 35.161  23.707  -23.686 1.00 54.12  ?  780  HOH D O   1 
HETATM 16450 O  O   . HOH DB 7 .   ? 28.459  66.684  -28.907 1.00 34.31  ?  781  HOH D O   1 
HETATM 16451 O  O   . HOH DB 7 .   ? 43.788  33.330  -39.867 1.00 42.52  ?  782  HOH D O   1 
HETATM 16452 O  O   A HOH DB 7 .   ? 19.285  56.524  -21.476 0.47 32.53  ?  783  HOH D O   1 
HETATM 16453 O  O   B HOH DB 7 .   ? 18.304  54.366  -21.731 0.53 34.58  ?  783  HOH D O   1 
HETATM 16454 O  O   . HOH DB 7 .   ? 11.098  29.055  -53.648 1.00 29.24  ?  784  HOH D O   1 
HETATM 16455 O  O   . HOH DB 7 .   ? -0.313  27.630  -48.603 1.00 32.44  ?  785  HOH D O   1 
HETATM 16456 O  O   . HOH DB 7 .   ? 7.842   44.497  -39.348 1.00 30.38  ?  786  HOH D O   1 
HETATM 16457 O  O   . HOH DB 7 .   ? 16.151  52.349  -36.570 1.00 30.17  ?  787  HOH D O   1 
HETATM 16458 O  O   . HOH DB 7 .   ? 12.388  57.491  -24.970 1.00 45.69  ?  788  HOH D O   1 
HETATM 16459 O  O   . HOH DB 7 .   ? 21.717  19.121  -36.256 1.00 52.50  ?  789  HOH D O   1 
HETATM 16460 O  O   . HOH DB 7 .   ? 1.404   35.953  -40.376 1.00 29.30  ?  790  HOH D O   1 
HETATM 16461 O  O   . HOH DB 7 .   ? 12.422  41.769  -24.749 1.00 29.67  ?  791  HOH D O   1 
HETATM 16462 O  O   . HOH DB 7 .   ? -9.246  30.826  -34.336 1.00 50.80  ?  792  HOH D O   1 
HETATM 16463 O  O   . HOH DB 7 .   ? 15.518  35.027  -24.439 1.00 32.39  ?  793  HOH D O   1 
HETATM 16464 O  O   . HOH DB 7 .   ? 43.015  49.165  -37.969 1.00 46.92  ?  794  HOH D O   1 
HETATM 16465 O  O   . HOH DB 7 .   ? 19.065  27.383  -32.438 1.00 37.60  ?  795  HOH D O   1 
HETATM 16466 O  O   . HOH DB 7 .   ? 12.804  50.302  -22.855 1.00 31.67  ?  796  HOH D O   1 
HETATM 16467 O  O   . HOH DB 7 .   ? 22.040  64.244  -30.532 1.00 37.11  ?  797  HOH D O   1 
HETATM 16468 O  O   . HOH DB 7 .   ? 13.912  52.641  -23.893 1.00 32.60  ?  798  HOH D O   1 
HETATM 16469 O  O   . HOH DB 7 .   ? 25.992  31.023  -42.514 1.00 31.05  ?  799  HOH D O   1 
HETATM 16470 O  O   . HOH DB 7 .   ? 11.333  34.913  -33.073 1.00 30.55  ?  800  HOH D O   1 
HETATM 16471 O  O   . HOH DB 7 .   ? 23.102  55.093  -52.658 1.00 43.66  ?  801  HOH D O   1 
HETATM 16472 O  O   . HOH DB 7 .   ? 40.407  34.697  -38.826 1.00 36.74  ?  802  HOH D O   1 
HETATM 16473 O  O   . HOH DB 7 .   ? -9.013  44.038  -28.182 1.00 44.70  ?  803  HOH D O   1 
HETATM 16474 O  O   . HOH DB 7 .   ? 27.560  40.198  -11.791 1.00 42.45  ?  804  HOH D O   1 
HETATM 16475 O  O   . HOH DB 7 .   ? 7.559   43.936  -45.290 1.00 34.72  ?  805  HOH D O   1 
HETATM 16476 O  O   . HOH DB 7 .   ? 19.184  23.501  -41.166 1.00 35.77  ?  806  HOH D O   1 
HETATM 16477 O  O   . HOH DB 7 .   ? 22.195  21.396  -29.813 1.00 52.68  ?  807  HOH D O   1 
HETATM 16478 O  O   . HOH DB 7 .   ? 13.937  44.209  -48.191 1.00 26.88  ?  808  HOH D O   1 
HETATM 16479 O  O   . HOH DB 7 .   ? 8.113   21.269  -27.524 1.00 48.44  ?  809  HOH D O   1 
HETATM 16480 O  O   . HOH DB 7 .   ? 21.203  25.274  -47.100 1.00 41.30  ?  810  HOH D O   1 
HETATM 16481 O  O   . HOH DB 7 .   ? 23.944  36.055  -43.275 1.00 27.40  ?  811  HOH D O   1 
HETATM 16482 O  O   . HOH DB 7 .   ? 29.846  26.616  -46.210 1.00 39.24  ?  812  HOH D O   1 
HETATM 16483 O  O   . HOH DB 7 .   ? 46.939  37.114  -29.280 1.00 44.14  ?  813  HOH D O   1 
HETATM 16484 O  O   . HOH DB 7 .   ? 38.753  59.440  -27.846 1.00 47.49  ?  814  HOH D O   1 
HETATM 16485 O  O   . HOH DB 7 .   ? 40.949  39.054  -33.878 1.00 37.15  ?  815  HOH D O   1 
HETATM 16486 O  O   . HOH DB 7 .   ? -0.256  36.178  -49.914 1.00 40.62  ?  816  HOH D O   1 
HETATM 16487 O  O   . HOH DB 7 .   ? -3.867  34.006  -23.771 1.00 44.37  ?  817  HOH D O   1 
HETATM 16488 O  O   . HOH DB 7 .   ? 18.994  42.169  -17.567 1.00 38.34  ?  818  HOH D O   1 
HETATM 16489 O  O   . HOH DB 7 .   ? 5.523   17.775  -57.307 1.00 50.32  ?  819  HOH D O   1 
HETATM 16490 O  O   . HOH DB 7 .   ? 5.752   41.681  -31.279 1.00 32.87  ?  820  HOH D O   1 
HETATM 16491 O  O   . HOH DB 7 .   ? 34.540  62.385  -31.648 1.00 44.44  ?  821  HOH D O   1 
HETATM 16492 O  O   . HOH DB 7 .   ? 26.789  69.603  -21.612 1.00 49.22  ?  822  HOH D O   1 
HETATM 16493 O  O   . HOH DB 7 .   ? 15.345  63.477  -29.824 1.00 46.82  ?  823  HOH D O   1 
HETATM 16494 O  O   . HOH DB 7 .   ? 35.899  35.778  -45.686 1.00 38.13  ?  824  HOH D O   1 
HETATM 16495 O  O   . HOH DB 7 .   ? 13.468  53.576  -17.567 1.00 40.99  ?  825  HOH D O   1 
HETATM 16496 O  O   . HOH DB 7 .   ? 20.780  37.484  -12.565 1.00 45.47  ?  826  HOH D O   1 
HETATM 16497 O  O   . HOH DB 7 .   ? 1.089   19.709  -40.428 1.00 48.97  ?  827  HOH D O   1 
HETATM 16498 O  O   . HOH DB 7 .   ? 19.534  31.544  -48.968 1.00 32.28  ?  828  HOH D O   1 
HETATM 16499 O  O   . HOH DB 7 .   ? -6.455  31.748  -50.574 1.00 33.99  ?  829  HOH D O   1 
HETATM 16500 O  O   . HOH DB 7 .   ? 14.446  74.878  -18.128 1.00 45.90  ?  830  HOH D O   1 
HETATM 16501 O  O   . HOH DB 7 .   ? 14.099  50.264  -20.278 1.00 36.03  ?  831  HOH D O   1 
HETATM 16502 O  O   . HOH DB 7 .   ? 11.261  46.623  -13.107 1.00 39.10  ?  832  HOH D O   1 
HETATM 16503 O  O   . HOH DB 7 .   ? 26.696  61.797  -17.464 1.00 39.55  ?  833  HOH D O   1 
HETATM 16504 O  O   . HOH DB 7 .   ? 17.804  53.048  -38.755 1.00 32.62  ?  834  HOH D O   1 
HETATM 16505 O  O   . HOH DB 7 .   ? 37.449  57.072  -21.045 1.00 46.19  ?  835  HOH D O   1 
HETATM 16506 O  O   . HOH DB 7 .   ? 21.220  56.684  -20.072 1.00 40.01  ?  836  HOH D O   1 
HETATM 16507 O  O   . HOH DB 7 .   ? 6.431   52.783  -29.497 1.00 46.79  ?  837  HOH D O   1 
HETATM 16508 O  O   . HOH DB 7 .   ? 25.876  49.257  -10.811 1.00 41.26  ?  838  HOH D O   1 
HETATM 16509 O  O   . HOH DB 7 .   ? -10.336 23.399  -45.865 1.00 45.43  ?  839  HOH D O   1 
HETATM 16510 O  O   . HOH DB 7 .   ? 31.893  29.430  -15.425 1.00 41.94  ?  840  HOH D O   1 
HETATM 16511 O  O   . HOH DB 7 .   ? 7.610   39.719  -23.264 1.00 32.80  ?  841  HOH D O   1 
HETATM 16512 O  O   . HOH DB 7 .   ? 27.291  38.076  -43.507 1.00 32.97  ?  842  HOH D O   1 
HETATM 16513 O  O   . HOH DB 7 .   ? 32.040  38.948  -49.548 1.00 44.35  ?  843  HOH D O   1 
HETATM 16514 O  O   . HOH DB 7 .   ? 9.167   15.775  -47.476 1.00 53.17  ?  844  HOH D O   1 
HETATM 16515 O  O   . HOH DB 7 .   ? 30.321  42.282  -11.740 1.00 43.08  ?  845  HOH D O   1 
HETATM 16516 O  O   . HOH DB 7 .   ? 20.929  29.098  -48.478 1.00 34.31  ?  846  HOH D O   1 
HETATM 16517 O  O   . HOH DB 7 .   ? 6.737   51.345  -9.093  1.00 54.31  ?  847  HOH D O   1 
HETATM 16518 O  O   . HOH DB 7 .   ? 15.860  61.059  -47.231 1.00 47.63  ?  848  HOH D O   1 
HETATM 16519 O  O   . HOH DB 7 .   ? 19.835  19.885  -43.634 1.00 47.56  ?  849  HOH D O   1 
HETATM 16520 O  O   . HOH DB 7 .   ? 30.873  22.457  -33.845 1.00 47.89  ?  850  HOH D O   1 
HETATM 16521 O  O   . HOH DB 7 .   ? 23.776  33.246  -27.629 1.00 31.57  ?  851  HOH D O   1 
HETATM 16522 O  O   . HOH DB 7 .   ? 18.161  41.859  -43.019 1.00 27.07  ?  852  HOH D O   1 
HETATM 16523 O  O   . HOH DB 7 .   ? -4.262  37.848  -44.050 1.00 28.93  ?  853  HOH D O   1 
HETATM 16524 O  O   . HOH DB 7 .   ? 2.575   40.990  -40.598 1.00 26.62  ?  854  HOH D O   1 
HETATM 16525 O  O   . HOH DB 7 .   ? 7.076   39.504  -30.757 1.00 24.90  ?  855  HOH D O   1 
HETATM 16526 O  O   . HOH DB 7 .   ? 20.306  54.499  -18.909 1.00 40.76  ?  856  HOH D O   1 
HETATM 16527 O  O   . HOH DB 7 .   ? 5.886   34.129  -25.246 1.00 38.34  ?  857  HOH D O   1 
HETATM 16528 O  O   . HOH DB 7 .   ? 34.864  42.057  -48.167 1.00 44.95  ?  858  HOH D O   1 
HETATM 16529 O  O   . HOH DB 7 .   ? 15.253  61.352  -30.700 1.00 48.51  ?  859  HOH D O   1 
HETATM 16530 O  O   . HOH DB 7 .   ? 10.215  49.562  -28.412 1.00 38.33  ?  860  HOH D O   1 
HETATM 16531 O  O   . HOH DB 7 .   ? 23.600  24.414  -40.498 1.00 36.19  ?  861  HOH D O   1 
HETATM 16532 O  O   . HOH DB 7 .   ? 14.891  52.983  -19.884 1.00 39.02  ?  862  HOH D O   1 
HETATM 16533 O  O   . HOH DB 7 .   ? 1.149   33.563  -49.192 1.00 32.72  ?  863  HOH D O   1 
HETATM 16534 O  O   . HOH DB 7 .   ? 30.709  66.522  -35.668 1.00 48.16  ?  864  HOH D O   1 
HETATM 16535 O  O   . HOH DB 7 .   ? 28.674  59.847  -37.951 1.00 37.40  ?  865  HOH D O   1 
HETATM 16536 O  O   . HOH DB 7 .   ? -10.523 24.748  -53.465 1.00 43.47  ?  866  HOH D O   1 
HETATM 16537 O  O   . HOH DB 7 .   ? 37.871  44.327  -12.469 1.00 53.80  ?  867  HOH D O   1 
HETATM 16538 O  O   . HOH DB 7 .   ? 6.214   46.225  -37.909 1.00 46.21  ?  868  HOH D O   1 
HETATM 16539 O  O   . HOH DB 7 .   ? 20.596  42.658  -41.539 1.00 26.80  ?  869  HOH D O   1 
HETATM 16540 O  O   . HOH DB 7 .   ? 10.383  43.824  -49.402 1.00 32.06  ?  870  HOH D O   1 
HETATM 16541 O  O   . HOH DB 7 .   ? 21.689  19.156  -45.605 1.00 48.23  ?  871  HOH D O   1 
HETATM 16542 O  O   . HOH DB 7 .   ? -7.375  37.593  -33.256 1.00 52.42  ?  872  HOH D O   1 
HETATM 16543 O  O   . HOH DB 7 .   ? 19.424  54.929  -30.629 1.00 30.17  ?  873  HOH D O   1 
HETATM 16544 O  O   . HOH DB 7 .   ? -9.653  41.154  -22.838 1.00 52.48  ?  874  HOH D O   1 
HETATM 16545 O  O   . HOH DB 7 .   ? 47.512  48.011  -21.292 1.00 44.93  ?  875  HOH D O   1 
HETATM 16546 O  O   . HOH DB 7 .   ? -5.291  31.314  -39.504 1.00 34.78  ?  876  HOH D O   1 
HETATM 16547 O  O   . HOH DB 7 .   ? 2.471   34.144  -45.671 1.00 27.26  ?  877  HOH D O   1 
HETATM 16548 O  O   . HOH DB 7 .   ? 7.170   49.636  -16.611 1.00 44.62  ?  878  HOH D O   1 
HETATM 16549 O  O   . HOH DB 7 .   ? 5.268   42.200  -45.600 1.00 37.84  ?  879  HOH D O   1 
HETATM 16550 O  O   . HOH DB 7 .   ? 21.359  54.776  -16.039 1.00 39.11  ?  880  HOH D O   1 
HETATM 16551 O  O   . HOH DB 7 .   ? 43.450  35.951  -40.242 1.00 45.56  ?  881  HOH D O   1 
HETATM 16552 O  O   . HOH DB 7 .   ? 26.462  14.774  -46.066 1.00 50.52  ?  882  HOH D O   1 
HETATM 16553 O  O   . HOH DB 7 .   ? 31.382  48.926  -49.981 1.00 49.17  ?  883  HOH D O   1 
HETATM 16554 O  O   . HOH DB 7 .   ? 17.267  64.029  -34.999 1.00 42.87  ?  884  HOH D O   1 
HETATM 16555 O  O   . HOH DB 7 .   ? 10.944  62.901  -16.087 1.00 46.97  ?  885  HOH D O   1 
HETATM 16556 O  O   . HOH DB 7 .   ? 2.719   19.251  -34.453 1.00 42.87  ?  886  HOH D O   1 
HETATM 16557 O  O   . HOH DB 7 .   ? 36.187  63.549  -33.570 1.00 50.67  ?  887  HOH D O   1 
HETATM 16558 O  O   . HOH DB 7 .   ? 14.623  40.154  -53.770 1.00 49.44  ?  888  HOH D O   1 
HETATM 16559 O  O   . HOH DB 7 .   ? 32.510  63.773  -31.227 1.00 42.29  ?  889  HOH D O   1 
HETATM 16560 O  O   . HOH DB 7 .   ? 13.310  45.040  -24.347 1.00 33.53  ?  890  HOH D O   1 
HETATM 16561 O  O   . HOH DB 7 .   ? -5.108  31.403  -27.448 1.00 40.20  ?  891  HOH D O   1 
HETATM 16562 O  O   . HOH DB 7 .   ? 15.458  46.528  -48.470 1.00 32.87  ?  892  HOH D O   1 
HETATM 16563 O  O   . HOH DB 7 .   ? 36.940  56.873  -30.644 1.00 40.02  ?  893  HOH D O   1 
HETATM 16564 O  O   . HOH DB 7 .   ? 13.334  51.613  -36.022 1.00 34.15  ?  894  HOH D O   1 
HETATM 16565 O  O   . HOH DB 7 .   ? 21.918  63.930  -20.243 1.00 42.08  ?  895  HOH D O   1 
HETATM 16566 O  O   . HOH DB 7 .   ? 36.370  37.486  -13.540 1.00 43.86  ?  896  HOH D O   1 
HETATM 16567 O  O   . HOH DB 7 .   ? 33.845  27.350  -15.292 1.00 49.19  ?  897  HOH D O   1 
HETATM 16568 O  O   . HOH DB 7 .   ? 5.477   44.655  -42.099 1.00 42.83  ?  898  HOH D O   1 
HETATM 16569 O  O   . HOH DB 7 .   ? 23.138  64.399  -38.629 1.00 38.19  ?  899  HOH D O   1 
HETATM 16570 O  O   A HOH DB 7 .   ? 22.474  57.358  -15.707 0.51 38.65  ?  900  HOH D O   1 
HETATM 16571 O  O   B HOH DB 7 .   ? 24.217  58.610  -15.044 0.49 38.67  ?  900  HOH D O   1 
HETATM 16572 O  O   . HOH DB 7 .   ? -1.923  27.881  -46.257 1.00 28.41  ?  901  HOH D O   1 
HETATM 16573 O  O   . HOH DB 7 .   ? -4.698  22.206  -42.676 1.00 41.69  ?  902  HOH D O   1 
HETATM 16574 O  O   . HOH DB 7 .   ? 11.036  27.618  -20.440 1.00 44.47  ?  903  HOH D O   1 
HETATM 16575 O  O   . HOH DB 7 .   ? 40.516  54.773  -24.716 1.00 45.22  ?  904  HOH D O   1 
HETATM 16576 O  O   . HOH DB 7 .   ? 11.537  58.108  -27.421 1.00 58.02  ?  905  HOH D O   1 
HETATM 16577 O  O   . HOH DB 7 .   ? 39.287  53.428  -40.430 1.00 49.80  ?  906  HOH D O   1 
HETATM 16578 O  O   . HOH DB 7 .   ? 20.892  28.990  -15.197 1.00 46.23  ?  907  HOH D O   1 
HETATM 16579 O  O   . HOH DB 7 .   ? -3.609  23.576  -36.049 1.00 47.10  ?  908  HOH D O   1 
HETATM 16580 O  O   . HOH DB 7 .   ? 14.656  20.881  -35.119 1.00 48.01  ?  909  HOH D O   1 
HETATM 16581 O  O   . HOH DB 7 .   ? 13.536  38.383  -12.536 1.00 44.85  ?  910  HOH D O   1 
HETATM 16582 O  O   . HOH DB 7 .   ? 10.522  48.041  -40.019 1.00 39.12  ?  911  HOH D O   1 
HETATM 16583 O  O   . HOH DB 7 .   ? 13.561  26.190  -28.645 1.00 42.47  ?  912  HOH D O   1 
HETATM 16584 O  O   . HOH DB 7 .   ? 1.673   27.503  -53.659 1.00 44.21  ?  913  HOH D O   1 
HETATM 16585 O  O   . HOH DB 7 .   ? 7.903   35.588  -24.338 1.00 39.42  ?  914  HOH D O   1 
HETATM 16586 O  O   A HOH DB 7 .   ? 48.356  27.297  -28.302 0.54 47.21  ?  915  HOH D O   1 
HETATM 16587 O  O   B HOH DB 7 .   ? 49.229  26.697  -29.733 0.46 42.43  ?  915  HOH D O   1 
HETATM 16588 O  O   . HOH DB 7 .   ? 14.261  48.847  -6.716  1.00 51.90  ?  916  HOH D O   1 
HETATM 16589 O  O   . HOH DB 7 .   ? 32.273  66.052  -49.464 1.00 47.77  ?  917  HOH D O   1 
HETATM 16590 O  O   . HOH DB 7 .   ? 28.973  67.333  -36.751 1.00 46.79  ?  918  HOH D O   1 
HETATM 16591 O  O   . HOH DB 7 .   ? 11.762  39.255  -14.565 1.00 40.93  ?  919  HOH D O   1 
HETATM 16592 O  O   . HOH DB 7 .   ? 4.322   32.487  -55.764 1.00 40.16  ?  920  HOH D O   1 
HETATM 16593 O  O   . HOH DB 7 .   ? 35.204  28.942  -47.838 1.00 44.62  ?  921  HOH D O   1 
HETATM 16594 O  O   A HOH DB 7 .   ? -7.988  47.410  -21.575 0.48 41.68  ?  922  HOH D O   1 
HETATM 16595 O  O   B HOH DB 7 .   ? -6.438  46.550  -20.706 0.52 45.05  ?  922  HOH D O   1 
HETATM 16596 O  O   . HOH DB 7 .   ? 0.813   25.250  -29.581 1.00 43.64  ?  923  HOH D O   1 
HETATM 16597 O  O   . HOH DB 7 .   ? 8.553   45.694  -35.668 1.00 35.87  ?  924  HOH D O   1 
HETATM 16598 O  O   . HOH DB 7 .   ? 28.212  18.448  -42.733 1.00 48.59  ?  925  HOH D O   1 
HETATM 16599 O  O   . HOH DB 7 .   ? 25.951  66.725  -39.270 1.00 54.83  ?  926  HOH D O   1 
HETATM 16600 O  O   . HOH DB 7 .   ? 22.154  23.096  -45.763 1.00 43.82  ?  927  HOH D O   1 
HETATM 16601 O  O   . HOH DB 7 .   ? 29.019  67.340  -44.132 1.00 47.73  ?  928  HOH D O   1 
HETATM 16602 O  O   . HOH DB 7 .   ? 15.644  60.046  -37.615 1.00 35.41  ?  929  HOH D O   1 
HETATM 16603 O  O   . HOH DB 7 .   ? 19.653  70.576  -27.702 1.00 45.31  ?  930  HOH D O   1 
HETATM 16604 O  O   . HOH DB 7 .   ? 6.848   33.587  -62.397 1.00 45.60  ?  931  HOH D O   1 
HETATM 16605 O  O   . HOH DB 7 .   ? 36.297  51.073  -17.740 1.00 47.43  ?  932  HOH D O   1 
HETATM 16606 O  O   . HOH DB 7 .   ? 21.561  23.370  -52.685 1.00 49.59  ?  933  HOH D O   1 
HETATM 16607 O  O   . HOH DB 7 .   ? 7.375   44.856  -28.873 1.00 32.66  ?  934  HOH D O   1 
HETATM 16608 O  O   . HOH DB 7 .   ? 16.632  22.808  -33.782 1.00 47.12  ?  935  HOH D O   1 
HETATM 16609 O  O   . HOH DB 7 .   ? 19.692  17.135  -44.571 1.00 54.83  ?  936  HOH D O   1 
HETATM 16610 O  O   . HOH DB 7 .   ? 1.641   26.481  -26.272 1.00 51.72  ?  937  HOH D O   1 
HETATM 16611 O  O   . HOH DB 7 .   ? 23.800  48.938  -51.156 1.00 48.28  ?  938  HOH D O   1 
HETATM 16612 O  O   . HOH DB 7 .   ? 23.867  26.474  -48.019 1.00 48.21  ?  939  HOH D O   1 
HETATM 16613 O  O   . HOH DB 7 .   ? 42.964  40.833  -40.374 1.00 50.34  ?  940  HOH D O   1 
HETATM 16614 O  O   . HOH DB 7 .   ? 20.269  22.628  -22.948 1.00 47.85  ?  941  HOH D O   1 
HETATM 16615 O  O   . HOH DB 7 .   ? 18.543  33.137  -54.628 1.00 40.08  ?  942  HOH D O   1 
HETATM 16616 O  O   . HOH DB 7 .   ? 12.062  56.342  -16.168 1.00 52.56  ?  943  HOH D O   1 
HETATM 16617 O  O   . HOH DB 7 .   ? 17.907  20.706  -47.825 1.00 35.30  ?  944  HOH D O   1 
HETATM 16618 O  O   . HOH DB 7 .   ? 10.429  54.963  -15.109 1.00 55.21  ?  945  HOH D O   1 
HETATM 16619 O  O   . HOH DB 7 .   ? 1.312   32.466  -52.854 1.00 49.93  ?  946  HOH D O   1 
HETATM 16620 O  O   . HOH DB 7 .   ? 24.399  23.413  -26.500 1.00 50.30  ?  947  HOH D O   1 
HETATM 16621 O  O   . HOH DB 7 .   ? 16.141  40.310  -56.667 1.00 61.05  ?  948  HOH D O   1 
HETATM 16622 O  O   A HOH DB 7 .   ? -14.786 27.372  -56.704 0.39 36.67  ?  949  HOH D O   1 
HETATM 16623 O  O   B HOH DB 7 .   ? -14.282 26.283  -58.197 0.61 41.72  ?  949  HOH D O   1 
HETATM 16624 O  O   . HOH DB 7 .   ? -0.581  29.180  -50.978 1.00 42.98  ?  950  HOH D O   1 
HETATM 16625 O  O   . HOH DB 7 .   ? 21.747  65.743  -34.537 1.00 46.29  ?  951  HOH D O   1 
HETATM 16626 O  O   . HOH DB 7 .   ? 33.500  57.956  -17.763 1.00 51.57  ?  952  HOH D O   1 
HETATM 16627 O  O   . HOH DB 7 .   ? 27.814  18.654  -36.530 1.00 55.04  ?  953  HOH D O   1 
HETATM 16628 O  O   . HOH DB 7 .   ? 6.630   41.595  -15.333 1.00 51.79  ?  954  HOH D O   1 
HETATM 16629 O  O   . HOH DB 7 .   ? 34.109  61.417  -21.979 1.00 49.98  ?  955  HOH D O   1 
HETATM 16630 O  O   . HOH DB 7 .   ? 36.317  56.032  -33.051 1.00 40.68  ?  956  HOH D O   1 
HETATM 16631 O  O   . HOH DB 7 .   ? 44.693  42.439  -40.399 1.00 48.10  ?  957  HOH D O   1 
HETATM 16632 O  O   . HOH DB 7 .   ? 15.785  46.380  -51.245 1.00 51.70  ?  958  HOH D O   1 
HETATM 16633 O  O   . HOH DB 7 .   ? 33.363  23.442  -21.495 1.00 49.25  ?  959  HOH D O   1 
HETATM 16634 O  O   . HOH DB 7 .   ? 13.179  65.116  -25.882 1.00 43.57  ?  960  HOH D O   1 
HETATM 16635 O  O   . HOH DB 7 .   ? 8.147   67.770  -23.516 1.00 58.47  ?  961  HOH D O   1 
HETATM 16636 O  O   . HOH DB 7 .   ? 10.471  49.444  -35.336 1.00 48.31  ?  962  HOH D O   1 
HETATM 16637 O  O   . HOH DB 7 .   ? 29.520  22.407  -19.230 1.00 53.76  ?  963  HOH D O   1 
HETATM 16638 O  O   . HOH DB 7 .   ? 26.050  39.213  -9.271  1.00 56.64  ?  964  HOH D O   1 
HETATM 16639 O  O   . HOH DB 7 .   ? 6.917   16.881  -50.640 1.00 43.68  ?  965  HOH D O   1 
HETATM 16640 O  O   . HOH DB 7 .   ? 19.788  49.767  -12.908 1.00 39.12  ?  966  HOH D O   1 
HETATM 16641 O  O   . HOH DB 7 .   ? 18.941  24.071  -53.822 1.00 45.92  ?  967  HOH D O   1 
HETATM 16642 O  O   . HOH DB 7 .   ? -7.562  24.507  -53.536 1.00 54.00  ?  968  HOH D O   1 
HETATM 16643 O  O   . HOH DB 7 .   ? 38.246  15.089  -36.572 1.00 38.69  ?  969  HOH D O   1 
HETATM 16644 O  O   . HOH DB 7 .   ? 45.531  28.815  -38.901 1.00 58.46  ?  970  HOH D O   1 
HETATM 16645 O  O   . HOH DB 7 .   ? 46.434  55.345  -22.462 1.00 53.99  ?  971  HOH D O   1 
HETATM 16646 O  O   . HOH DB 7 .   ? 12.590  41.965  -6.491  1.00 52.79  ?  972  HOH D O   1 
HETATM 16647 O  O   . HOH DB 7 .   ? 43.177  21.926  -30.399 1.00 62.80  ?  973  HOH D O   1 
HETATM 16648 O  O   . HOH DB 7 .   ? 11.513  17.277  -52.510 1.00 51.29  ?  974  HOH D O   1 
HETATM 16649 O  O   . HOH DB 7 .   ? 8.979   49.138  -37.811 1.00 50.74  ?  975  HOH D O   1 
HETATM 16650 O  O   . HOH DB 7 .   ? 2.525   47.167  -31.365 1.00 36.25  ?  976  HOH D O   1 
HETATM 16651 O  O   . HOH DB 7 .   ? 18.492  28.391  -15.771 1.00 49.92  ?  977  HOH D O   1 
HETATM 16652 O  O   . HOH DB 7 .   ? 48.005  32.089  -27.606 1.00 52.73  ?  978  HOH D O   1 
HETATM 16653 O  O   . HOH DB 7 .   ? 44.770  45.490  -46.733 1.00 52.28  ?  979  HOH D O   1 
HETATM 16654 O  O   . HOH DB 7 .   ? 5.379   44.400  -30.478 1.00 30.49  ?  980  HOH D O   1 
HETATM 16655 O  O   . HOH DB 7 .   ? 30.612  25.681  -48.650 1.00 54.48  ?  981  HOH D O   1 
HETATM 16656 O  O   . HOH DB 7 .   ? 49.398  39.782  -34.688 1.00 58.60  ?  982  HOH D O   1 
HETATM 16657 O  O   . HOH DB 7 .   ? 26.855  39.391  -51.260 1.00 51.77  ?  983  HOH D O   1 
HETATM 16658 O  O   . HOH DB 7 .   ? 26.559  69.202  -33.238 1.00 56.79  ?  984  HOH D O   1 
HETATM 16659 O  O   . HOH DB 7 .   ? 24.969  47.046  -10.047 1.00 44.87  ?  985  HOH D O   1 
HETATM 16660 O  O   . HOH DB 7 .   ? 17.093  54.073  -19.026 1.00 43.00  ?  986  HOH D O   1 
HETATM 16661 O  O   A HOH DB 7 .   ? 21.757  54.671  -11.647 0.47 44.72  ?  987  HOH D O   1 
HETATM 16662 O  O   B HOH DB 7 .   ? 22.884  55.848  -12.697 0.53 40.44  ?  987  HOH D O   1 
HETATM 16663 O  O   . HOH DB 7 .   ? 23.649  28.788  -49.266 1.00 44.17  ?  988  HOH D O   1 
HETATM 16664 O  O   . HOH DB 7 .   ? 11.199  53.399  -35.796 1.00 41.40  ?  989  HOH D O   1 
HETATM 16665 O  O   A HOH DB 7 .   ? 12.485  31.417  -17.403 0.47 37.10  ?  990  HOH D O   1 
HETATM 16666 O  O   B HOH DB 7 .   ? 13.592  32.031  -18.369 0.53 27.24  ?  990  HOH D O   1 
HETATM 16667 O  O   . HOH DB 7 .   ? 29.371  46.701  -9.455  1.00 52.03  ?  991  HOH D O   1 
HETATM 16668 O  O   . HOH DB 7 .   ? -1.609  25.649  -52.256 1.00 47.71  ?  992  HOH D O   1 
HETATM 16669 O  O   . HOH DB 7 .   ? 25.501  63.851  -16.273 1.00 49.48  ?  993  HOH D O   1 
HETATM 16670 O  O   . HOH DB 7 .   ? 31.808  48.648  -10.350 1.00 54.17  ?  994  HOH D O   1 
HETATM 16671 O  O   . HOH DB 7 .   ? 26.796  42.094  -7.962  1.00 53.97  ?  995  HOH D O   1 
HETATM 16672 O  O   . HOH DB 7 .   ? 24.089  34.401  -49.766 1.00 41.97  ?  996  HOH D O   1 
HETATM 16673 O  O   . HOH DB 7 .   ? 2.357   36.482  -48.027 1.00 32.97  ?  997  HOH D O   1 
HETATM 16674 O  O   . HOH DB 7 .   ? 23.892  38.740  -49.997 1.00 43.80  ?  998  HOH D O   1 
HETATM 16675 O  O   . HOH DB 7 .   ? 5.478   42.262  -48.494 1.00 43.38  ?  999  HOH D O   1 
HETATM 16676 O  O   . HOH DB 7 .   ? 7.998   43.767  -48.042 1.00 35.55  ?  1000 HOH D O   1 
HETATM 16677 O  O   . HOH DB 7 .   ? 26.613  33.059  -50.916 1.00 47.42  ?  1001 HOH D O   1 
HETATM 16678 O  O   . HOH DB 7 .   ? 1.722   39.603  -47.060 1.00 47.33  ?  1002 HOH D O   1 
HETATM 16679 O  O   . HOH DB 7 .   ? 13.202  29.873  -57.859 1.00 47.92  ?  1003 HOH D O   1 
HETATM 16680 O  O   . HOH DB 7 .   ? 20.905  21.165  -47.253 1.00 45.29  ?  1004 HOH D O   1 
HETATM 16681 O  O   . HOH DB 7 .   ? 5.279   48.492  -14.358 1.00 45.93  ?  1005 HOH D O   1 
HETATM 16682 O  O   . HOH DB 7 .   ? 22.705  47.325  -52.982 1.00 56.58  ?  1006 HOH D O   1 
HETATM 16683 O  O   A HOH DB 7 .   ? 13.946  59.085  -34.594 0.53 38.02  ?  1007 HOH D O   1 
HETATM 16684 O  O   B HOH DB 7 .   ? 14.333  58.902  -32.822 0.47 41.91  ?  1007 HOH D O   1 
HETATM 16685 O  O   . HOH DB 7 .   ? 41.801  49.216  -44.165 1.00 52.98  ?  1008 HOH D O   1 
HETATM 16686 O  O   . HOH DB 7 .   ? 21.595  49.580  -10.576 1.00 42.75  ?  1009 HOH D O   1 
HETATM 16687 O  O   . HOH DB 7 .   ? -4.684  48.284  -19.924 1.00 52.64  ?  1010 HOH D O   1 
HETATM 16688 O  O   . HOH DB 7 .   ? 6.912   49.781  -18.870 1.00 45.51  ?  1011 HOH D O   1 
HETATM 16689 O  O   . HOH DB 7 .   ? 33.539  47.718  -51.203 1.00 50.55  ?  1012 HOH D O   1 
HETATM 16690 O  O   . HOH DB 7 .   ? 7.359   20.644  -24.497 1.00 54.39  ?  1013 HOH D O   1 
HETATM 16691 O  O   . HOH DB 7 .   ? -16.100 29.510  -57.125 1.00 38.41  ?  1014 HOH D O   1 
HETATM 16692 O  O   . HOH DB 7 .   ? 34.367  21.895  -19.760 1.00 66.77  ?  1015 HOH D O   1 
HETATM 16693 O  O   . HOH DB 7 .   ? 23.378  65.765  -18.183 1.00 38.73  ?  1016 HOH D O   1 
HETATM 16694 O  O   . HOH DB 7 .   ? 34.761  39.582  -48.868 1.00 46.00  ?  1017 HOH D O   1 
HETATM 16695 O  O   . HOH DB 7 .   ? -0.787  24.895  -49.339 1.00 42.61  ?  1018 HOH D O   1 
HETATM 16696 O  O   . HOH DB 7 .   ? 0.835   41.111  -45.554 1.00 42.30  ?  1019 HOH D O   1 
HETATM 16697 O  O   . HOH DB 7 .   ? 39.149  57.029  -29.204 1.00 41.50  ?  1020 HOH D O   1 
HETATM 16698 O  O   . HOH DB 7 .   ? 35.989  36.971  -48.152 1.00 38.58  ?  1021 HOH D O   1 
HETATM 16699 O  O   . HOH DB 7 .   ? 5.264   15.198  -39.538 1.00 54.02  ?  1022 HOH D O   1 
HETATM 16700 O  O   . HOH DB 7 .   ? 12.569  28.090  -56.121 1.00 43.54  ?  1023 HOH D O   1 
HETATM 16701 O  O   . HOH DB 7 .   ? 12.800  61.775  -15.423 1.00 51.59  ?  1024 HOH D O   1 
HETATM 16702 O  O   . HOH DB 7 .   ? 20.687  34.197  -54.091 1.00 46.68  ?  1025 HOH D O   1 
HETATM 16703 O  O   . HOH DB 7 .   ? 38.995  25.439  -30.510 1.00 56.79  ?  1026 HOH D O   1 
HETATM 16704 O  O   . HOH DB 7 .   ? 41.011  56.043  -27.316 1.00 48.51  ?  1027 HOH D O   1 
HETATM 16705 O  O   . HOH DB 7 .   ? 31.544  65.402  -32.985 1.00 50.32  ?  1028 HOH D O   1 
HETATM 16706 O  O   . HOH DB 7 .   ? 36.927  52.483  -48.377 1.00 41.72  ?  1029 HOH D O   1 
HETATM 16707 O  O   . HOH DB 7 .   ? 0.327   30.755  -24.083 1.00 48.50  ?  1030 HOH D O   1 
HETATM 16708 O  O   . HOH DB 7 .   ? 10.862  45.190  -51.214 1.00 54.93  ?  1031 HOH D O   1 
HETATM 16709 O  O   . HOH DB 7 .   ? -1.528  32.662  -22.583 1.00 56.48  ?  1032 HOH D O   1 
HETATM 16710 O  O   . HOH DB 7 .   ? 10.146  50.312  -49.320 1.00 46.67  ?  1033 HOH D O   1 
HETATM 16711 O  O   . HOH DB 7 .   ? 7.662   50.835  -34.400 1.00 45.11  ?  1034 HOH D O   1 
# 
